data_9GWU
# 
_entry.id   9GWU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9GWU         pdb_00009gwu 10.2210/pdb9gwu/pdb 
WWPDB D_1292142067 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        9GWU 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_contact_author.id                 2 
_pdbx_contact_author.email              gideon.davies@york.ac.uk 
_pdbx_contact_author.name_first         Gideon 
_pdbx_contact_author.name_last          'Davies J' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7343-776X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sharma, M.'   1 0000-0003-3960-2212 
'Davies, G.J.' 2 0000-0002-7343-776X 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biochem.J. 
_citation.journal_id_ASTM           BIJOAK 
_citation.journal_id_CSD            0043 
_citation.journal_id_ISSN           1470-8728 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            482 
_citation.language                  ? 
_citation.page_first                57 
_citation.page_last                 72 
_citation.title                     
;Structure, kinetics, and mechanism of Pseudomonas putida sulfoquinovose dehydrogenase, the first enzyme in the sulfoglycolytic Entner-Doudoroff pathway.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1042/BCJ20240605 
_citation.pdbx_database_id_PubMed   39840830 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Burchill, L.'         1 ?                   
primary 'Sharma, M.'           2 ?                   
primary 'Soler, N.M.'          3 ?                   
primary 'Goddard-Borger, E.D.' 4 ?                   
primary 'Davies, G.J.'         5 ?                   
primary 'Williams, S.J.'       6 0000-0001-6341-4364 
# 
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 'Sulfoquinovose 1-dehydrogenase' 29323.127 2   1.1.1.390 ? ? ? 
2 water   nat water                            18.015    179 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'SQ dehydrogenase' 
# 
_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       
;MGSSHHHHHHSSGMNRHTDTHYPSLADKVVLISGGASGIGRAFVEAFVAQGSRVAFLDLDAEAGQGLAHALGANSLFLPC
DVRDIERLKACVAEVERTWGAVDVLINNAARDDRHALADVSVEYWDERMQTNLRHAFFAAQAVAPGMARRGSGAIINMGS
ISWMRGRPGMVCYTTAKAALNGMTRTLARELGGQGIRINSLVPGAIRTERQDAMWAADPAGLEAASQAFIDQQMLKFRLD
ASDCARLALFLASDDSRGCTGQNFVVDAGLSIQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGMNRHTDTHYPSLADKVVLISGGASGIGRAFVEAFVAQGSRVAFLDLDAEAGQGLAHALGANSLFLPC
DVRDIERLKACVAEVERTWGAVDVLINNAARDDRHALADVSVEYWDERMQTNLRHAFFAAQAVAPGMARRGSGAIINMGS
ISWMRGRPGMVCYTTAKAALNGMTRTLARELGGQGIRINSLVPGAIRTERQDAMWAADPAGLEAASQAFIDQQMLKFRLD
ASDCARLALFLASDDSRGCTGQNFVVDAGLSIQ
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  MET n 
1 15  ASN n 
1 16  ARG n 
1 17  HIS n 
1 18  THR n 
1 19  ASP n 
1 20  THR n 
1 21  HIS n 
1 22  TYR n 
1 23  PRO n 
1 24  SER n 
1 25  LEU n 
1 26  ALA n 
1 27  ASP n 
1 28  LYS n 
1 29  VAL n 
1 30  VAL n 
1 31  LEU n 
1 32  ILE n 
1 33  SER n 
1 34  GLY n 
1 35  GLY n 
1 36  ALA n 
1 37  SER n 
1 38  GLY n 
1 39  ILE n 
1 40  GLY n 
1 41  ARG n 
1 42  ALA n 
1 43  PHE n 
1 44  VAL n 
1 45  GLU n 
1 46  ALA n 
1 47  PHE n 
1 48  VAL n 
1 49  ALA n 
1 50  GLN n 
1 51  GLY n 
1 52  SER n 
1 53  ARG n 
1 54  VAL n 
1 55  ALA n 
1 56  PHE n 
1 57  LEU n 
1 58  ASP n 
1 59  LEU n 
1 60  ASP n 
1 61  ALA n 
1 62  GLU n 
1 63  ALA n 
1 64  GLY n 
1 65  GLN n 
1 66  GLY n 
1 67  LEU n 
1 68  ALA n 
1 69  HIS n 
1 70  ALA n 
1 71  LEU n 
1 72  GLY n 
1 73  ALA n 
1 74  ASN n 
1 75  SER n 
1 76  LEU n 
1 77  PHE n 
1 78  LEU n 
1 79  PRO n 
1 80  CYS n 
1 81  ASP n 
1 82  VAL n 
1 83  ARG n 
1 84  ASP n 
1 85  ILE n 
1 86  GLU n 
1 87  ARG n 
1 88  LEU n 
1 89  LYS n 
1 90  ALA n 
1 91  CYS n 
1 92  VAL n 
1 93  ALA n 
1 94  GLU n 
1 95  VAL n 
1 96  GLU n 
1 97  ARG n 
1 98  THR n 
1 99  TRP n 
1 100 GLY n 
1 101 ALA n 
1 102 VAL n 
1 103 ASP n 
1 104 VAL n 
1 105 LEU n 
1 106 ILE n 
1 107 ASN n 
1 108 ASN n 
1 109 ALA n 
1 110 ALA n 
1 111 ARG n 
1 112 ASP n 
1 113 ASP n 
1 114 ARG n 
1 115 HIS n 
1 116 ALA n 
1 117 LEU n 
1 118 ALA n 
1 119 ASP n 
1 120 VAL n 
1 121 SER n 
1 122 VAL n 
1 123 GLU n 
1 124 TYR n 
1 125 TRP n 
1 126 ASP n 
1 127 GLU n 
1 128 ARG n 
1 129 MET n 
1 130 GLN n 
1 131 THR n 
1 132 ASN n 
1 133 LEU n 
1 134 ARG n 
1 135 HIS n 
1 136 ALA n 
1 137 PHE n 
1 138 PHE n 
1 139 ALA n 
1 140 ALA n 
1 141 GLN n 
1 142 ALA n 
1 143 VAL n 
1 144 ALA n 
1 145 PRO n 
1 146 GLY n 
1 147 MET n 
1 148 ALA n 
1 149 ARG n 
1 150 ARG n 
1 151 GLY n 
1 152 SER n 
1 153 GLY n 
1 154 ALA n 
1 155 ILE n 
1 156 ILE n 
1 157 ASN n 
1 158 MET n 
1 159 GLY n 
1 160 SER n 
1 161 ILE n 
1 162 SER n 
1 163 TRP n 
1 164 MET n 
1 165 ARG n 
1 166 GLY n 
1 167 ARG n 
1 168 PRO n 
1 169 GLY n 
1 170 MET n 
1 171 VAL n 
1 172 CYS n 
1 173 TYR n 
1 174 THR n 
1 175 THR n 
1 176 ALA n 
1 177 LYS n 
1 178 ALA n 
1 179 ALA n 
1 180 LEU n 
1 181 ASN n 
1 182 GLY n 
1 183 MET n 
1 184 THR n 
1 185 ARG n 
1 186 THR n 
1 187 LEU n 
1 188 ALA n 
1 189 ARG n 
1 190 GLU n 
1 191 LEU n 
1 192 GLY n 
1 193 GLY n 
1 194 GLN n 
1 195 GLY n 
1 196 ILE n 
1 197 ARG n 
1 198 ILE n 
1 199 ASN n 
1 200 SER n 
1 201 LEU n 
1 202 VAL n 
1 203 PRO n 
1 204 GLY n 
1 205 ALA n 
1 206 ILE n 
1 207 ARG n 
1 208 THR n 
1 209 GLU n 
1 210 ARG n 
1 211 GLN n 
1 212 ASP n 
1 213 ALA n 
1 214 MET n 
1 215 TRP n 
1 216 ALA n 
1 217 ALA n 
1 218 ASP n 
1 219 PRO n 
1 220 ALA n 
1 221 GLY n 
1 222 LEU n 
1 223 GLU n 
1 224 ALA n 
1 225 ALA n 
1 226 SER n 
1 227 GLN n 
1 228 ALA n 
1 229 PHE n 
1 230 ILE n 
1 231 ASP n 
1 232 GLN n 
1 233 GLN n 
1 234 MET n 
1 235 LEU n 
1 236 LYS n 
1 237 PHE n 
1 238 ARG n 
1 239 LEU n 
1 240 ASP n 
1 241 ALA n 
1 242 SER n 
1 243 ASP n 
1 244 CYS n 
1 245 ALA n 
1 246 ARG n 
1 247 LEU n 
1 248 ALA n 
1 249 LEU n 
1 250 PHE n 
1 251 LEU n 
1 252 ALA n 
1 253 SER n 
1 254 ASP n 
1 255 ASP n 
1 256 SER n 
1 257 ARG n 
1 258 GLY n 
1 259 CYS n 
1 260 THR n 
1 261 GLY n 
1 262 GLN n 
1 263 ASN n 
1 264 PHE n 
1 265 VAL n 
1 266 VAL n 
1 267 ASP n 
1 268 ALA n 
1 269 GLY n 
1 270 LEU n 
1 271 SER n 
1 272 ILE n 
1 273 GLN 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                   273 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PpSQ1_00405 
_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      'Pseudomonas putida' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     303 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28a 
_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 
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   MET 1   -12 ?   ?   ?   B . n 
A 1 2   GLY 2   -11 ?   ?   ?   B . n 
A 1 3   SER 3   -10 ?   ?   ?   B . n 
A 1 4   SER 4   -9  ?   ?   ?   B . n 
A 1 5   HIS 5   -8  ?   ?   ?   B . n 
A 1 6   HIS 6   -7  ?   ?   ?   B . n 
A 1 7   HIS 7   -6  ?   ?   ?   B . n 
A 1 8   HIS 8   -5  ?   ?   ?   B . n 
A 1 9   HIS 9   -4  ?   ?   ?   B . n 
A 1 10  HIS 10  -3  ?   ?   ?   B . n 
A 1 11  SER 11  -2  ?   ?   ?   B . n 
A 1 12  SER 12  -1  ?   ?   ?   B . n 
A 1 13  GLY 13  0   ?   ?   ?   B . n 
A 1 14  MET 14  1   1   MET MET B . n 
A 1 15  ASN 15  2   2   ASN ASN B . n 
A 1 16  ARG 16  3   3   ARG ARG B . n 
A 1 17  HIS 17  4   4   HIS HIS B . n 
A 1 18  THR 18  5   5   THR THR B . n 
A 1 19  ASP 19  6   6   ASP ASP B . n 
A 1 20  THR 20  7   7   THR THR B . n 
A 1 21  HIS 21  8   8   HIS HIS B . n 
A 1 22  TYR 22  9   9   TYR TYR B . n 
A 1 23  PRO 23  10  10  PRO PRO B . n 
A 1 24  SER 24  11  11  SER SER B . n 
A 1 25  LEU 25  12  12  LEU LEU B . n 
A 1 26  ALA 26  13  13  ALA ALA B . n 
A 1 27  ASP 27  14  14  ASP ASP B . n 
A 1 28  LYS 28  15  15  LYS LYS B . n 
A 1 29  VAL 29  16  16  VAL VAL B . n 
A 1 30  VAL 30  17  17  VAL VAL B . n 
A 1 31  LEU 31  18  18  LEU LEU B . n 
A 1 32  ILE 32  19  19  ILE ILE B . n 
A 1 33  SER 33  20  20  SER SER B . n 
A 1 34  GLY 34  21  21  GLY GLY B . n 
A 1 35  GLY 35  22  22  GLY GLY B . n 
A 1 36  ALA 36  23  23  ALA ALA B . n 
A 1 37  SER 37  24  24  SER SER B . n 
A 1 38  GLY 38  25  25  GLY GLY B . n 
A 1 39  ILE 39  26  26  ILE ILE B . n 
A 1 40  GLY 40  27  27  GLY GLY B . n 
A 1 41  ARG 41  28  28  ARG ARG B . n 
A 1 42  ALA 42  29  29  ALA ALA B . n 
A 1 43  PHE 43  30  30  PHE PHE B . n 
A 1 44  VAL 44  31  31  VAL VAL B . n 
A 1 45  GLU 45  32  32  GLU GLU B . n 
A 1 46  ALA 46  33  33  ALA ALA B . n 
A 1 47  PHE 47  34  34  PHE PHE B . n 
A 1 48  VAL 48  35  35  VAL VAL B . n 
A 1 49  ALA 49  36  36  ALA ALA B . n 
A 1 50  GLN 50  37  37  GLN GLN B . n 
A 1 51  GLY 51  38  38  GLY GLY B . n 
A 1 52  SER 52  39  39  SER SER B . n 
A 1 53  ARG 53  40  40  ARG ARG B . n 
A 1 54  VAL 54  41  41  VAL VAL B . n 
A 1 55  ALA 55  42  42  ALA ALA B . n 
A 1 56  PHE 56  43  43  PHE PHE B . n 
A 1 57  LEU 57  44  44  LEU LEU B . n 
A 1 58  ASP 58  45  45  ASP ASP B . n 
A 1 59  LEU 59  46  46  LEU LEU B . n 
A 1 60  ASP 60  47  47  ASP ASP B . n 
A 1 61  ALA 61  48  48  ALA ALA B . n 
A 1 62  GLU 62  49  49  GLU GLU B . n 
A 1 63  ALA 63  50  50  ALA ALA B . n 
A 1 64  GLY 64  51  51  GLY GLY B . n 
A 1 65  GLN 65  52  52  GLN GLN B . n 
A 1 66  GLY 66  53  53  GLY GLY B . n 
A 1 67  LEU 67  54  54  LEU LEU B . n 
A 1 68  ALA 68  55  55  ALA ALA B . n 
A 1 69  HIS 69  56  56  HIS HIS B . n 
A 1 70  ALA 70  57  57  ALA ALA B . n 
A 1 71  LEU 71  58  58  LEU LEU B . n 
A 1 72  GLY 72  59  59  GLY GLY B . n 
A 1 73  ALA 73  60  60  ALA ALA B . n 
A 1 74  ASN 74  61  61  ASN ASN B . n 
A 1 75  SER 75  62  62  SER SER B . n 
A 1 76  LEU 76  63  63  LEU LEU B . n 
A 1 77  PHE 77  64  64  PHE PHE B . n 
A 1 78  LEU 78  65  65  LEU LEU B . n 
A 1 79  PRO 79  66  66  PRO PRO B . n 
A 1 80  CYS 80  67  67  CYS CYS B . n 
A 1 81  ASP 81  68  68  ASP ASP B . n 
A 1 82  VAL 82  69  69  VAL VAL B . n 
A 1 83  ARG 83  70  70  ARG ARG B . n 
A 1 84  ASP 84  71  71  ASP ASP B . n 
A 1 85  ILE 85  72  72  ILE ILE B . n 
A 1 86  GLU 86  73  73  GLU GLU B . n 
A 1 87  ARG 87  74  74  ARG ARG B . n 
A 1 88  LEU 88  75  75  LEU LEU B . n 
A 1 89  LYS 89  76  76  LYS LYS B . n 
A 1 90  ALA 90  77  77  ALA ALA B . n 
A 1 91  CYS 91  78  78  CYS CYS B . n 
A 1 92  VAL 92  79  79  VAL VAL B . n 
A 1 93  ALA 93  80  80  ALA ALA B . n 
A 1 94  GLU 94  81  81  GLU GLU B . n 
A 1 95  VAL 95  82  82  VAL VAL B . n 
A 1 96  GLU 96  83  83  GLU GLU B . n 
A 1 97  ARG 97  84  84  ARG ARG B . n 
A 1 98  THR 98  85  85  THR THR B . n 
A 1 99  TRP 99  86  86  TRP TRP B . n 
A 1 100 GLY 100 87  87  GLY GLY B . n 
A 1 101 ALA 101 88  88  ALA ALA B . n 
A 1 102 VAL 102 89  89  VAL VAL B . n 
A 1 103 ASP 103 90  90  ASP ASP B . n 
A 1 104 VAL 104 91  91  VAL VAL B . n 
A 1 105 LEU 105 92  92  LEU LEU B . n 
A 1 106 ILE 106 93  93  ILE ILE B . n 
A 1 107 ASN 107 94  94  ASN ASN B . n 
A 1 108 ASN 108 95  95  ASN ASN B . n 
A 1 109 ALA 109 96  96  ALA ALA B . n 
A 1 110 ALA 110 97  97  ALA ALA B . n 
A 1 111 ARG 111 98  98  ARG ARG B . n 
A 1 112 ASP 112 99  99  ASP ASP B . n 
A 1 113 ASP 113 100 100 ASP ASP B . n 
A 1 114 ARG 114 101 101 ARG ARG B . n 
A 1 115 HIS 115 102 102 HIS HIS B . n 
A 1 116 ALA 116 103 103 ALA ALA B . n 
A 1 117 LEU 117 104 104 LEU LEU B . n 
A 1 118 ALA 118 105 105 ALA ALA B . n 
A 1 119 ASP 119 106 106 ASP ASP B . n 
A 1 120 VAL 120 107 107 VAL VAL B . n 
A 1 121 SER 121 108 108 SER SER B . n 
A 1 122 VAL 122 109 109 VAL VAL B . n 
A 1 123 GLU 123 110 110 GLU GLU B . n 
A 1 124 TYR 124 111 111 TYR TYR B . n 
A 1 125 TRP 125 112 112 TRP TRP B . n 
A 1 126 ASP 126 113 113 ASP ASP B . n 
A 1 127 GLU 127 114 114 GLU GLU B . n 
A 1 128 ARG 128 115 115 ARG ARG B . n 
A 1 129 MET 129 116 116 MET MET B . n 
A 1 130 GLN 130 117 117 GLN GLN B . n 
A 1 131 THR 131 118 118 THR THR B . n 
A 1 132 ASN 132 119 119 ASN ASN B . n 
A 1 133 LEU 133 120 120 LEU LEU B . n 
A 1 134 ARG 134 121 121 ARG ARG B . n 
A 1 135 HIS 135 122 122 HIS HIS B . n 
A 1 136 ALA 136 123 123 ALA ALA B . n 
A 1 137 PHE 137 124 124 PHE PHE B . n 
A 1 138 PHE 138 125 125 PHE PHE B . n 
A 1 139 ALA 139 126 126 ALA ALA B . n 
A 1 140 ALA 140 127 127 ALA ALA B . n 
A 1 141 GLN 141 128 128 GLN GLN B . n 
A 1 142 ALA 142 129 129 ALA ALA B . n 
A 1 143 VAL 143 130 130 VAL VAL B . n 
A 1 144 ALA 144 131 131 ALA ALA B . n 
A 1 145 PRO 145 132 132 PRO PRO B . n 
A 1 146 GLY 146 133 133 GLY GLY B . n 
A 1 147 MET 147 134 134 MET MET B . n 
A 1 148 ALA 148 135 135 ALA ALA B . n 
A 1 149 ARG 149 136 136 ARG ARG B . n 
A 1 150 ARG 150 137 137 ARG ARG B . n 
A 1 151 GLY 151 138 138 GLY GLY B . n 
A 1 152 SER 152 139 139 SER SER B . n 
A 1 153 GLY 153 140 140 GLY GLY B . n 
A 1 154 ALA 154 141 141 ALA ALA B . n 
A 1 155 ILE 155 142 142 ILE ILE B . n 
A 1 156 ILE 156 143 143 ILE ILE B . n 
A 1 157 ASN 157 144 144 ASN ASN B . n 
A 1 158 MET 158 145 145 MET MET B . n 
A 1 159 GLY 159 146 146 GLY GLY B . n 
A 1 160 SER 160 147 147 SER SER B . n 
A 1 161 ILE 161 148 148 ILE ILE B . n 
A 1 162 SER 162 149 149 SER SER B . n 
A 1 163 TRP 163 150 150 TRP TRP B . n 
A 1 164 MET 164 151 151 MET MET B . n 
A 1 165 ARG 165 152 152 ARG ARG B . n 
A 1 166 GLY 166 153 153 GLY GLY B . n 
A 1 167 ARG 167 154 154 ARG ARG B . n 
A 1 168 PRO 168 155 155 PRO PRO B . n 
A 1 169 GLY 169 156 156 GLY GLY B . n 
A 1 170 MET 170 157 157 MET MET B . n 
A 1 171 VAL 171 158 158 VAL VAL B . n 
A 1 172 CYS 172 159 159 CYS CYS B . n 
A 1 173 TYR 173 160 160 TYR TYR B . n 
A 1 174 THR 174 161 161 THR THR B . n 
A 1 175 THR 175 162 162 THR THR B . n 
A 1 176 ALA 176 163 163 ALA ALA B . n 
A 1 177 LYS 177 164 164 LYS LYS B . n 
A 1 178 ALA 178 165 165 ALA ALA B . n 
A 1 179 ALA 179 166 166 ALA ALA B . n 
A 1 180 LEU 180 167 167 LEU LEU B . n 
A 1 181 ASN 181 168 168 ASN ASN B . n 
A 1 182 GLY 182 169 169 GLY GLY B . n 
A 1 183 MET 183 170 170 MET MET B . n 
A 1 184 THR 184 171 171 THR THR B . n 
A 1 185 ARG 185 172 172 ARG ARG B . n 
A 1 186 THR 186 173 173 THR THR B . n 
A 1 187 LEU 187 174 174 LEU LEU B . n 
A 1 188 ALA 188 175 175 ALA ALA B . n 
A 1 189 ARG 189 176 176 ARG ARG B . n 
A 1 190 GLU 190 177 177 GLU GLU B . n 
A 1 191 LEU 191 178 178 LEU LEU B . n 
A 1 192 GLY 192 179 179 GLY GLY B . n 
A 1 193 GLY 193 180 180 GLY GLY B . n 
A 1 194 GLN 194 181 181 GLN GLN B . n 
A 1 195 GLY 195 182 182 GLY GLY B . n 
A 1 196 ILE 196 183 183 ILE ILE B . n 
A 1 197 ARG 197 184 184 ARG ARG B . n 
A 1 198 ILE 198 185 185 ILE ILE B . n 
A 1 199 ASN 199 186 186 ASN ASN B . n 
A 1 200 SER 200 187 187 SER SER B . n 
A 1 201 LEU 201 188 188 LEU LEU B . n 
A 1 202 VAL 202 189 189 VAL VAL B . n 
A 1 203 PRO 203 190 190 PRO PRO B . n 
A 1 204 GLY 204 191 191 GLY GLY B . n 
A 1 205 ALA 205 192 192 ALA ALA B . n 
A 1 206 ILE 206 193 193 ILE ILE B . n 
A 1 207 ARG 207 194 194 ARG ARG B . n 
A 1 208 THR 208 195 195 THR THR B . n 
A 1 209 GLU 209 196 196 GLU GLU B . n 
A 1 210 ARG 210 197 197 ARG ARG B . n 
A 1 211 GLN 211 198 198 GLN GLN B . n 
A 1 212 ASP 212 199 199 ASP ASP B . n 
A 1 213 ALA 213 200 200 ALA ALA B . n 
A 1 214 MET 214 201 201 MET MET B . n 
A 1 215 TRP 215 202 202 TRP TRP B . n 
A 1 216 ALA 216 203 203 ALA ALA B . n 
A 1 217 ALA 217 204 204 ALA ALA B . n 
A 1 218 ASP 218 205 205 ASP ASP B . n 
A 1 219 PRO 219 206 206 PRO PRO B . n 
A 1 220 ALA 220 207 207 ALA ALA B . n 
A 1 221 GLY 221 208 208 GLY GLY B . n 
A 1 222 LEU 222 209 209 LEU LEU B . n 
A 1 223 GLU 223 210 210 GLU GLU B . n 
A 1 224 ALA 224 211 211 ALA ALA B . n 
A 1 225 ALA 225 212 212 ALA ALA B . n 
A 1 226 SER 226 213 213 SER SER B . n 
A 1 227 GLN 227 214 214 GLN GLN B . n 
A 1 228 ALA 228 215 215 ALA ALA B . n 
A 1 229 PHE 229 216 216 PHE PHE B . n 
A 1 230 ILE 230 217 217 ILE ILE B . n 
A 1 231 ASP 231 218 218 ASP ASP B . n 
A 1 232 GLN 232 219 219 GLN GLN B . n 
A 1 233 GLN 233 220 220 GLN GLN B . n 
A 1 234 MET 234 221 221 MET MET B . n 
A 1 235 LEU 235 222 222 LEU LEU B . n 
A 1 236 LYS 236 223 223 LYS LYS B . n 
A 1 237 PHE 237 224 224 PHE PHE B . n 
A 1 238 ARG 238 225 225 ARG ARG B . n 
A 1 239 LEU 239 226 226 LEU LEU B . n 
A 1 240 ASP 240 227 227 ASP ASP B . n 
A 1 241 ALA 241 228 228 ALA ALA B . n 
A 1 242 SER 242 229 229 SER SER B . n 
A 1 243 ASP 243 230 230 ASP ASP B . n 
A 1 244 CYS 244 231 231 CYS CYS B . n 
A 1 245 ALA 245 232 232 ALA ALA B . n 
A 1 246 ARG 246 233 233 ARG ARG B . n 
A 1 247 LEU 247 234 234 LEU LEU B . n 
A 1 248 ALA 248 235 235 ALA ALA B . n 
A 1 249 LEU 249 236 236 LEU LEU B . n 
A 1 250 PHE 250 237 237 PHE PHE B . n 
A 1 251 LEU 251 238 238 LEU LEU B . n 
A 1 252 ALA 252 239 239 ALA ALA B . n 
A 1 253 SER 253 240 240 SER SER B . n 
A 1 254 ASP 254 241 241 ASP ASP B . n 
A 1 255 ASP 255 242 242 ASP ASP B . n 
A 1 256 SER 256 243 243 SER SER B . n 
A 1 257 ARG 257 244 244 ARG ARG B . n 
A 1 258 GLY 258 245 245 GLY GLY B . n 
A 1 259 CYS 259 246 246 CYS CYS B . n 
A 1 260 THR 260 247 247 THR THR B . n 
A 1 261 GLY 261 248 248 GLY GLY B . n 
A 1 262 GLN 262 249 249 GLN GLN B . n 
A 1 263 ASN 263 250 250 ASN ASN B . n 
A 1 264 PHE 264 251 251 PHE PHE B . n 
A 1 265 VAL 265 252 252 VAL VAL B . n 
A 1 266 VAL 266 253 253 VAL VAL B . n 
A 1 267 ASP 267 254 254 ASP ASP B . n 
A 1 268 ALA 268 255 255 ALA ALA B . n 
A 1 269 GLY 269 256 256 GLY GLY B . n 
A 1 270 LEU 270 257 257 LEU LEU B . n 
A 1 271 SER 271 258 258 SER SER B . n 
A 1 272 ILE 272 259 259 ILE ILE B . n 
A 1 273 GLN 273 260 260 GLN GLN B . n 
B 1 1   MET 1   -12 ?   ?   ?   A . n 
B 1 2   GLY 2   -11 ?   ?   ?   A . n 
B 1 3   SER 3   -10 ?   ?   ?   A . n 
B 1 4   SER 4   -9  ?   ?   ?   A . n 
B 1 5   HIS 5   -8  ?   ?   ?   A . n 
B 1 6   HIS 6   -7  ?   ?   ?   A . n 
B 1 7   HIS 7   -6  ?   ?   ?   A . n 
B 1 8   HIS 8   -5  ?   ?   ?   A . n 
B 1 9   HIS 9   -4  ?   ?   ?   A . n 
B 1 10  HIS 10  -3  ?   ?   ?   A . n 
B 1 11  SER 11  -2  ?   ?   ?   A . n 
B 1 12  SER 12  -1  ?   ?   ?   A . n 
B 1 13  GLY 13  0   ?   ?   ?   A . n 
B 1 14  MET 14  1   ?   ?   ?   A . n 
B 1 15  ASN 15  2   2   ASN ASN A . n 
B 1 16  ARG 16  3   3   ARG ARG A . n 
B 1 17  HIS 17  4   4   HIS HIS A . n 
B 1 18  THR 18  5   5   THR THR A . n 
B 1 19  ASP 19  6   6   ASP ASP A . n 
B 1 20  THR 20  7   7   THR THR A . n 
B 1 21  HIS 21  8   8   HIS HIS A . n 
B 1 22  TYR 22  9   9   TYR TYR A . n 
B 1 23  PRO 23  10  10  PRO PRO A . n 
B 1 24  SER 24  11  11  SER SER A . n 
B 1 25  LEU 25  12  12  LEU LEU A . n 
B 1 26  ALA 26  13  13  ALA ALA A . n 
B 1 27  ASP 27  14  14  ASP ASP A . n 
B 1 28  LYS 28  15  15  LYS LYS A . n 
B 1 29  VAL 29  16  16  VAL VAL A . n 
B 1 30  VAL 30  17  17  VAL VAL A . n 
B 1 31  LEU 31  18  18  LEU LEU A . n 
B 1 32  ILE 32  19  19  ILE ILE A . n 
B 1 33  SER 33  20  20  SER SER A . n 
B 1 34  GLY 34  21  21  GLY GLY A . n 
B 1 35  GLY 35  22  22  GLY GLY A . n 
B 1 36  ALA 36  23  23  ALA ALA A . n 
B 1 37  SER 37  24  24  SER SER A . n 
B 1 38  GLY 38  25  25  GLY GLY A . n 
B 1 39  ILE 39  26  26  ILE ILE A . n 
B 1 40  GLY 40  27  27  GLY GLY A . n 
B 1 41  ARG 41  28  28  ARG ARG A . n 
B 1 42  ALA 42  29  29  ALA ALA A . n 
B 1 43  PHE 43  30  30  PHE PHE A . n 
B 1 44  VAL 44  31  31  VAL VAL A . n 
B 1 45  GLU 45  32  32  GLU GLU A . n 
B 1 46  ALA 46  33  33  ALA ALA A . n 
B 1 47  PHE 47  34  34  PHE PHE A . n 
B 1 48  VAL 48  35  35  VAL VAL A . n 
B 1 49  ALA 49  36  36  ALA ALA A . n 
B 1 50  GLN 50  37  37  GLN GLN A . n 
B 1 51  GLY 51  38  38  GLY GLY A . n 
B 1 52  SER 52  39  39  SER SER A . n 
B 1 53  ARG 53  40  40  ARG ARG A . n 
B 1 54  VAL 54  41  41  VAL VAL A . n 
B 1 55  ALA 55  42  42  ALA ALA A . n 
B 1 56  PHE 56  43  43  PHE PHE A . n 
B 1 57  LEU 57  44  44  LEU LEU A . n 
B 1 58  ASP 58  45  45  ASP ASP A . n 
B 1 59  LEU 59  46  46  LEU LEU A . n 
B 1 60  ASP 60  47  47  ASP ASP A . n 
B 1 61  ALA 61  48  48  ALA ALA A . n 
B 1 62  GLU 62  49  49  GLU GLU A . n 
B 1 63  ALA 63  50  50  ALA ALA A . n 
B 1 64  GLY 64  51  51  GLY GLY A . n 
B 1 65  GLN 65  52  52  GLN GLN A . n 
B 1 66  GLY 66  53  53  GLY GLY A . n 
B 1 67  LEU 67  54  54  LEU LEU A . n 
B 1 68  ALA 68  55  55  ALA ALA A . n 
B 1 69  HIS 69  56  56  HIS HIS A . n 
B 1 70  ALA 70  57  57  ALA ALA A . n 
B 1 71  LEU 71  58  58  LEU LEU A . n 
B 1 72  GLY 72  59  59  GLY GLY A . n 
B 1 73  ALA 73  60  60  ALA ALA A . n 
B 1 74  ASN 74  61  61  ASN ASN A . n 
B 1 75  SER 75  62  62  SER SER A . n 
B 1 76  LEU 76  63  63  LEU LEU A . n 
B 1 77  PHE 77  64  64  PHE PHE A . n 
B 1 78  LEU 78  65  65  LEU LEU A . n 
B 1 79  PRO 79  66  66  PRO PRO A . n 
B 1 80  CYS 80  67  67  CYS CYS A . n 
B 1 81  ASP 81  68  68  ASP ASP A . n 
B 1 82  VAL 82  69  69  VAL VAL A . n 
B 1 83  ARG 83  70  70  ARG ARG A . n 
B 1 84  ASP 84  71  71  ASP ASP A . n 
B 1 85  ILE 85  72  72  ILE ILE A . n 
B 1 86  GLU 86  73  73  GLU GLU A . n 
B 1 87  ARG 87  74  74  ARG ARG A . n 
B 1 88  LEU 88  75  75  LEU LEU A . n 
B 1 89  LYS 89  76  76  LYS LYS A . n 
B 1 90  ALA 90  77  77  ALA ALA A . n 
B 1 91  CYS 91  78  78  CYS CYS A . n 
B 1 92  VAL 92  79  79  VAL VAL A . n 
B 1 93  ALA 93  80  80  ALA ALA A . n 
B 1 94  GLU 94  81  81  GLU GLU A . n 
B 1 95  VAL 95  82  82  VAL VAL A . n 
B 1 96  GLU 96  83  83  GLU GLU A . n 
B 1 97  ARG 97  84  84  ARG ARG A . n 
B 1 98  THR 98  85  85  THR THR A . n 
B 1 99  TRP 99  86  86  TRP TRP A . n 
B 1 100 GLY 100 87  87  GLY GLY A . n 
B 1 101 ALA 101 88  88  ALA ALA A . n 
B 1 102 VAL 102 89  89  VAL VAL A . n 
B 1 103 ASP 103 90  90  ASP ASP A . n 
B 1 104 VAL 104 91  91  VAL VAL A . n 
B 1 105 LEU 105 92  92  LEU LEU A . n 
B 1 106 ILE 106 93  93  ILE ILE A . n 
B 1 107 ASN 107 94  94  ASN ASN A . n 
B 1 108 ASN 108 95  95  ASN ASN A . n 
B 1 109 ALA 109 96  96  ALA ALA A . n 
B 1 110 ALA 110 97  97  ALA ALA A . n 
B 1 111 ARG 111 98  98  ARG ARG A . n 
B 1 112 ASP 112 99  99  ASP ASP A . n 
B 1 113 ASP 113 100 100 ASP ASP A . n 
B 1 114 ARG 114 101 101 ARG ARG A . n 
B 1 115 HIS 115 102 102 HIS HIS A . n 
B 1 116 ALA 116 103 103 ALA ALA A . n 
B 1 117 LEU 117 104 104 LEU LEU A . n 
B 1 118 ALA 118 105 105 ALA ALA A . n 
B 1 119 ASP 119 106 106 ASP ASP A . n 
B 1 120 VAL 120 107 107 VAL VAL A . n 
B 1 121 SER 121 108 108 SER SER A . n 
B 1 122 VAL 122 109 109 VAL VAL A . n 
B 1 123 GLU 123 110 110 GLU GLU A . n 
B 1 124 TYR 124 111 111 TYR TYR A . n 
B 1 125 TRP 125 112 112 TRP TRP A . n 
B 1 126 ASP 126 113 113 ASP ASP A . n 
B 1 127 GLU 127 114 114 GLU GLU A . n 
B 1 128 ARG 128 115 115 ARG ARG A . n 
B 1 129 MET 129 116 116 MET MET A . n 
B 1 130 GLN 130 117 117 GLN GLN A . n 
B 1 131 THR 131 118 118 THR THR A . n 
B 1 132 ASN 132 119 119 ASN ASN A . n 
B 1 133 LEU 133 120 120 LEU LEU A . n 
B 1 134 ARG 134 121 121 ARG ARG A . n 
B 1 135 HIS 135 122 122 HIS HIS A . n 
B 1 136 ALA 136 123 123 ALA ALA A . n 
B 1 137 PHE 137 124 124 PHE PHE A . n 
B 1 138 PHE 138 125 125 PHE PHE A . n 
B 1 139 ALA 139 126 126 ALA ALA A . n 
B 1 140 ALA 140 127 127 ALA ALA A . n 
B 1 141 GLN 141 128 128 GLN GLN A . n 
B 1 142 ALA 142 129 129 ALA ALA A . n 
B 1 143 VAL 143 130 130 VAL VAL A . n 
B 1 144 ALA 144 131 131 ALA ALA A . n 
B 1 145 PRO 145 132 132 PRO PRO A . n 
B 1 146 GLY 146 133 133 GLY GLY A . n 
B 1 147 MET 147 134 134 MET MET A . n 
B 1 148 ALA 148 135 135 ALA ALA A . n 
B 1 149 ARG 149 136 136 ARG ARG A . n 
B 1 150 ARG 150 137 137 ARG ARG A . n 
B 1 151 GLY 151 138 138 GLY GLY A . n 
B 1 152 SER 152 139 139 SER SER A . n 
B 1 153 GLY 153 140 140 GLY GLY A . n 
B 1 154 ALA 154 141 141 ALA ALA A . n 
B 1 155 ILE 155 142 142 ILE ILE A . n 
B 1 156 ILE 156 143 143 ILE ILE A . n 
B 1 157 ASN 157 144 144 ASN ASN A . n 
B 1 158 MET 158 145 145 MET MET A . n 
B 1 159 GLY 159 146 146 GLY GLY A . n 
B 1 160 SER 160 147 147 SER SER A . n 
B 1 161 ILE 161 148 148 ILE ILE A . n 
B 1 162 SER 162 149 149 SER SER A . n 
B 1 163 TRP 163 150 150 TRP TRP A . n 
B 1 164 MET 164 151 151 MET MET A . n 
B 1 165 ARG 165 152 152 ARG ARG A . n 
B 1 166 GLY 166 153 153 GLY GLY A . n 
B 1 167 ARG 167 154 154 ARG ARG A . n 
B 1 168 PRO 168 155 155 PRO PRO A . n 
B 1 169 GLY 169 156 156 GLY GLY A . n 
B 1 170 MET 170 157 157 MET MET A . n 
B 1 171 VAL 171 158 158 VAL VAL A . n 
B 1 172 CYS 172 159 159 CYS CYS A . n 
B 1 173 TYR 173 160 160 TYR TYR A . n 
B 1 174 THR 174 161 161 THR THR A . n 
B 1 175 THR 175 162 162 THR THR A . n 
B 1 176 ALA 176 163 163 ALA ALA A . n 
B 1 177 LYS 177 164 164 LYS LYS A . n 
B 1 178 ALA 178 165 165 ALA ALA A . n 
B 1 179 ALA 179 166 166 ALA ALA A . n 
B 1 180 LEU 180 167 167 LEU LEU A . n 
B 1 181 ASN 181 168 168 ASN ASN A . n 
B 1 182 GLY 182 169 169 GLY GLY A . n 
B 1 183 MET 183 170 170 MET MET A . n 
B 1 184 THR 184 171 171 THR THR A . n 
B 1 185 ARG 185 172 172 ARG ARG A . n 
B 1 186 THR 186 173 173 THR THR A . n 
B 1 187 LEU 187 174 174 LEU LEU A . n 
B 1 188 ALA 188 175 175 ALA ALA A . n 
B 1 189 ARG 189 176 176 ARG ARG A . n 
B 1 190 GLU 190 177 177 GLU GLU A . n 
B 1 191 LEU 191 178 178 LEU LEU A . n 
B 1 192 GLY 192 179 179 GLY GLY A . n 
B 1 193 GLY 193 180 180 GLY GLY A . n 
B 1 194 GLN 194 181 181 GLN GLN A . n 
B 1 195 GLY 195 182 182 GLY GLY A . n 
B 1 196 ILE 196 183 183 ILE ILE A . n 
B 1 197 ARG 197 184 184 ARG ARG A . n 
B 1 198 ILE 198 185 185 ILE ILE A . n 
B 1 199 ASN 199 186 186 ASN ASN A . n 
B 1 200 SER 200 187 187 SER SER A . n 
B 1 201 LEU 201 188 188 LEU LEU A . n 
B 1 202 VAL 202 189 189 VAL VAL A . n 
B 1 203 PRO 203 190 190 PRO PRO A . n 
B 1 204 GLY 204 191 191 GLY GLY A . n 
B 1 205 ALA 205 192 192 ALA ALA A . n 
B 1 206 ILE 206 193 193 ILE ILE A . n 
B 1 207 ARG 207 194 194 ARG ARG A . n 
B 1 208 THR 208 195 195 THR THR A . n 
B 1 209 GLU 209 196 196 GLU GLU A . n 
B 1 210 ARG 210 197 197 ARG ARG A . n 
B 1 211 GLN 211 198 198 GLN GLN A . n 
B 1 212 ASP 212 199 199 ASP ASP A . n 
B 1 213 ALA 213 200 200 ALA ALA A . n 
B 1 214 MET 214 201 201 MET MET A . n 
B 1 215 TRP 215 202 202 TRP TRP A . n 
B 1 216 ALA 216 203 203 ALA ALA A . n 
B 1 217 ALA 217 204 204 ALA ALA A . n 
B 1 218 ASP 218 205 205 ASP ASP A . n 
B 1 219 PRO 219 206 206 PRO PRO A . n 
B 1 220 ALA 220 207 207 ALA ALA A . n 
B 1 221 GLY 221 208 208 GLY GLY A . n 
B 1 222 LEU 222 209 209 LEU LEU A . n 
B 1 223 GLU 223 210 210 GLU GLU A . n 
B 1 224 ALA 224 211 211 ALA ALA A . n 
B 1 225 ALA 225 212 212 ALA ALA A . n 
B 1 226 SER 226 213 213 SER SER A . n 
B 1 227 GLN 227 214 214 GLN GLN A . n 
B 1 228 ALA 228 215 215 ALA ALA A . n 
B 1 229 PHE 229 216 216 PHE PHE A . n 
B 1 230 ILE 230 217 217 ILE ILE A . n 
B 1 231 ASP 231 218 218 ASP ASP A . n 
B 1 232 GLN 232 219 219 GLN GLN A . n 
B 1 233 GLN 233 220 220 GLN GLN A . n 
B 1 234 MET 234 221 221 MET MET A . n 
B 1 235 LEU 235 222 222 LEU LEU A . n 
B 1 236 LYS 236 223 223 LYS LYS A . n 
B 1 237 PHE 237 224 224 PHE PHE A . n 
B 1 238 ARG 238 225 225 ARG ARG A . n 
B 1 239 LEU 239 226 226 LEU LEU A . n 
B 1 240 ASP 240 227 227 ASP ASP A . n 
B 1 241 ALA 241 228 228 ALA ALA A . n 
B 1 242 SER 242 229 229 SER SER A . n 
B 1 243 ASP 243 230 230 ASP ASP A . n 
B 1 244 CYS 244 231 231 CYS CYS A . n 
B 1 245 ALA 245 232 232 ALA ALA A . n 
B 1 246 ARG 246 233 233 ARG ARG A . n 
B 1 247 LEU 247 234 234 LEU LEU A . n 
B 1 248 ALA 248 235 235 ALA ALA A . n 
B 1 249 LEU 249 236 236 LEU LEU A . n 
B 1 250 PHE 250 237 237 PHE PHE A . n 
B 1 251 LEU 251 238 238 LEU LEU A . n 
B 1 252 ALA 252 239 239 ALA ALA A . n 
B 1 253 SER 253 240 240 SER SER A . n 
B 1 254 ASP 254 241 241 ASP ASP A . n 
B 1 255 ASP 255 242 242 ASP ASP A . n 
B 1 256 SER 256 243 243 SER SER A . n 
B 1 257 ARG 257 244 244 ARG ARG A . n 
B 1 258 GLY 258 245 245 GLY GLY A . n 
B 1 259 CYS 259 246 246 CYS CYS A . n 
B 1 260 THR 260 247 247 THR THR A . n 
B 1 261 GLY 261 248 248 GLY GLY A . n 
B 1 262 GLN 262 249 249 GLN GLN A . n 
B 1 263 ASN 263 250 250 ASN ASN A . n 
B 1 264 PHE 264 251 251 PHE PHE A . n 
B 1 265 VAL 265 252 252 VAL VAL A . n 
B 1 266 VAL 266 253 253 VAL VAL A . n 
B 1 267 ASP 267 254 254 ASP ASP A . n 
B 1 268 ALA 268 255 255 ALA ALA A . n 
B 1 269 GLY 269 256 256 GLY GLY A . n 
B 1 270 LEU 270 257 257 LEU LEU A . n 
B 1 271 SER 271 258 258 SER SER A . n 
B 1 272 ILE 272 259 259 ILE ILE A . n 
B 1 273 GLN 273 260 260 GLN GLN A . 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 HOH 1   301 202 HOH HOH B . 
C 2 HOH 2   302 200 HOH HOH B . 
C 2 HOH 3   303 73  HOH HOH B . 
C 2 HOH 4   304 98  HOH HOH B . 
C 2 HOH 5   305 246 HOH HOH B . 
C 2 HOH 6   306 59  HOH HOH B . 
C 2 HOH 7   307 227 HOH HOH B . 
C 2 HOH 8   308 125 HOH HOH B . 
C 2 HOH 9   309 49  HOH HOH B . 
C 2 HOH 10  310 23  HOH HOH B . 
C 2 HOH 11  311 124 HOH HOH B . 
C 2 HOH 12  312 110 HOH HOH B . 
C 2 HOH 13  313 69  HOH HOH B . 
C 2 HOH 14  314 243 HOH HOH B . 
C 2 HOH 15  315 34  HOH HOH B . 
C 2 HOH 16  316 35  HOH HOH B . 
C 2 HOH 17  317 121 HOH HOH B . 
C 2 HOH 18  318 155 HOH HOH B . 
C 2 HOH 19  319 107 HOH HOH B . 
C 2 HOH 20  320 192 HOH HOH B . 
C 2 HOH 21  321 4   HOH HOH B . 
C 2 HOH 22  322 280 HOH HOH B . 
C 2 HOH 23  323 51  HOH HOH B . 
C 2 HOH 24  324 13  HOH HOH B . 
C 2 HOH 25  325 47  HOH HOH B . 
C 2 HOH 26  326 46  HOH HOH B . 
C 2 HOH 27  327 66  HOH HOH B . 
C 2 HOH 28  328 186 HOH HOH B . 
C 2 HOH 29  329 97  HOH HOH B . 
C 2 HOH 30  330 10  HOH HOH B . 
C 2 HOH 31  331 44  HOH HOH B . 
C 2 HOH 32  332 134 HOH HOH B . 
C 2 HOH 33  333 195 HOH HOH B . 
C 2 HOH 34  334 18  HOH HOH B . 
C 2 HOH 35  335 184 HOH HOH B . 
C 2 HOH 36  336 156 HOH HOH B . 
C 2 HOH 37  337 101 HOH HOH B . 
C 2 HOH 38  338 65  HOH HOH B . 
C 2 HOH 39  339 278 HOH HOH B . 
C 2 HOH 40  340 88  HOH HOH B . 
C 2 HOH 41  341 250 HOH HOH B . 
C 2 HOH 42  342 40  HOH HOH B . 
C 2 HOH 43  343 119 HOH HOH B . 
C 2 HOH 44  344 55  HOH HOH B . 
C 2 HOH 45  345 137 HOH HOH B . 
C 2 HOH 46  346 74  HOH HOH B . 
C 2 HOH 47  347 58  HOH HOH B . 
C 2 HOH 48  348 50  HOH HOH B . 
C 2 HOH 49  349 279 HOH HOH B . 
C 2 HOH 50  350 14  HOH HOH B . 
C 2 HOH 51  351 16  HOH HOH B . 
C 2 HOH 52  352 267 HOH HOH B . 
C 2 HOH 53  353 60  HOH HOH B . 
C 2 HOH 54  354 116 HOH HOH B . 
C 2 HOH 55  355 96  HOH HOH B . 
C 2 HOH 56  356 253 HOH HOH B . 
C 2 HOH 57  357 233 HOH HOH B . 
C 2 HOH 58  358 57  HOH HOH B . 
C 2 HOH 59  359 64  HOH HOH B . 
C 2 HOH 60  360 20  HOH HOH B . 
C 2 HOH 61  361 126 HOH HOH B . 
C 2 HOH 62  362 154 HOH HOH B . 
C 2 HOH 63  363 82  HOH HOH B . 
C 2 HOH 64  364 258 HOH HOH B . 
C 2 HOH 65  365 72  HOH HOH B . 
C 2 HOH 66  366 127 HOH HOH B . 
C 2 HOH 67  367 275 HOH HOH B . 
C 2 HOH 68  368 61  HOH HOH B . 
C 2 HOH 69  369 165 HOH HOH B . 
C 2 HOH 70  370 231 HOH HOH B . 
C 2 HOH 71  371 45  HOH HOH B . 
C 2 HOH 72  372 274 HOH HOH B . 
C 2 HOH 73  373 272 HOH HOH B . 
C 2 HOH 74  374 215 HOH HOH B . 
C 2 HOH 75  375 271 HOH HOH B . 
C 2 HOH 76  376 152 HOH HOH B . 
D 2 HOH 1   301 260 HOH HOH A . 
D 2 HOH 2   302 169 HOH HOH A . 
D 2 HOH 3   303 108 HOH HOH A . 
D 2 HOH 4   304 130 HOH HOH A . 
D 2 HOH 5   305 19  HOH HOH A . 
D 2 HOH 6   306 189 HOH HOH A . 
D 2 HOH 7   307 22  HOH HOH A . 
D 2 HOH 8   308 11  HOH HOH A . 
D 2 HOH 9   309 17  HOH HOH A . 
D 2 HOH 10  310 145 HOH HOH A . 
D 2 HOH 11  311 237 HOH HOH A . 
D 2 HOH 12  312 158 HOH HOH A . 
D 2 HOH 13  313 3   HOH HOH A . 
D 2 HOH 14  314 92  HOH HOH A . 
D 2 HOH 15  315 190 HOH HOH A . 
D 2 HOH 16  316 28  HOH HOH A . 
D 2 HOH 17  317 26  HOH HOH A . 
D 2 HOH 18  318 187 HOH HOH A . 
D 2 HOH 19  319 6   HOH HOH A . 
D 2 HOH 20  320 203 HOH HOH A . 
D 2 HOH 21  321 68  HOH HOH A . 
D 2 HOH 22  322 38  HOH HOH A . 
D 2 HOH 23  323 167 HOH HOH A . 
D 2 HOH 24  324 39  HOH HOH A . 
D 2 HOH 25  325 122 HOH HOH A . 
D 2 HOH 26  326 172 HOH HOH A . 
D 2 HOH 27  327 84  HOH HOH A . 
D 2 HOH 28  328 21  HOH HOH A . 
D 2 HOH 29  329 12  HOH HOH A . 
D 2 HOH 30  330 142 HOH HOH A . 
D 2 HOH 31  331 75  HOH HOH A . 
D 2 HOH 32  332 153 HOH HOH A . 
D 2 HOH 33  333 106 HOH HOH A . 
D 2 HOH 34  334 123 HOH HOH A . 
D 2 HOH 35  335 80  HOH HOH A . 
D 2 HOH 36  336 87  HOH HOH A . 
D 2 HOH 37  337 93  HOH HOH A . 
D 2 HOH 38  338 71  HOH HOH A . 
D 2 HOH 39  339 225 HOH HOH A . 
D 2 HOH 40  340 136 HOH HOH A . 
D 2 HOH 41  341 85  HOH HOH A . 
D 2 HOH 42  342 27  HOH HOH A . 
D 2 HOH 43  343 5   HOH HOH A . 
D 2 HOH 44  344 56  HOH HOH A . 
D 2 HOH 45  345 109 HOH HOH A . 
D 2 HOH 46  346 7   HOH HOH A . 
D 2 HOH 47  347 30  HOH HOH A . 
D 2 HOH 48  348 33  HOH HOH A . 
D 2 HOH 49  349 113 HOH HOH A . 
D 2 HOH 50  350 15  HOH HOH A . 
D 2 HOH 51  351 89  HOH HOH A . 
D 2 HOH 52  352 144 HOH HOH A . 
D 2 HOH 53  353 201 HOH HOH A . 
D 2 HOH 54  354 244 HOH HOH A . 
D 2 HOH 55  355 63  HOH HOH A . 
D 2 HOH 56  356 90  HOH HOH A . 
D 2 HOH 57  357 188 HOH HOH A . 
D 2 HOH 58  358 174 HOH HOH A . 
D 2 HOH 59  359 8   HOH HOH A . 
D 2 HOH 60  360 138 HOH HOH A . 
D 2 HOH 61  361 149 HOH HOH A . 
D 2 HOH 62  362 151 HOH HOH A . 
D 2 HOH 63  363 29  HOH HOH A . 
D 2 HOH 64  364 2   HOH HOH A . 
D 2 HOH 65  365 86  HOH HOH A . 
D 2 HOH 66  366 32  HOH HOH A . 
D 2 HOH 67  367 79  HOH HOH A . 
D 2 HOH 68  368 222 HOH HOH A . 
D 2 HOH 69  369 141 HOH HOH A . 
D 2 HOH 70  370 163 HOH HOH A . 
D 2 HOH 71  371 77  HOH HOH A . 
D 2 HOH 72  372 146 HOH HOH A . 
D 2 HOH 73  373 139 HOH HOH A . 
D 2 HOH 74  374 204 HOH HOH A . 
D 2 HOH 75  375 234 HOH HOH A . 
D 2 HOH 76  376 31  HOH HOH A . 
D 2 HOH 77  377 164 HOH HOH A . 
D 2 HOH 78  378 24  HOH HOH A . 
D 2 HOH 79  379 194 HOH HOH A . 
D 2 HOH 80  380 83  HOH HOH A . 
D 2 HOH 81  381 100 HOH HOH A . 
D 2 HOH 82  382 162 HOH HOH A . 
D 2 HOH 83  383 242 HOH HOH A . 
D 2 HOH 84  384 43  HOH HOH A . 
D 2 HOH 85  385 150 HOH HOH A . 
D 2 HOH 86  386 36  HOH HOH A . 
D 2 HOH 87  387 129 HOH HOH A . 
D 2 HOH 88  388 70  HOH HOH A . 
D 2 HOH 89  389 112 HOH HOH A . 
D 2 HOH 90  390 103 HOH HOH A . 
D 2 HOH 91  391 276 HOH HOH A . 
D 2 HOH 92  392 117 HOH HOH A . 
D 2 HOH 93  393 148 HOH HOH A . 
D 2 HOH 94  394 238 HOH HOH A . 
D 2 HOH 95  395 159 HOH HOH A . 
D 2 HOH 96  396 52  HOH HOH A . 
D 2 HOH 97  397 247 HOH HOH A . 
D 2 HOH 98  398 220 HOH HOH A . 
D 2 HOH 99  399 239 HOH HOH A . 
D 2 HOH 100 400 270 HOH HOH A . 
D 2 HOH 101 401 273 HOH HOH A . 
D 2 HOH 102 402 264 HOH HOH A . 
D 2 HOH 103 403 277 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 B MET 1   ? CG  ? A MET 14  CG  
2   1 Y 1 B MET 1   ? SD  ? A MET 14  SD  
3   1 Y 1 B MET 1   ? CE  ? A MET 14  CE  
4   1 Y 1 B ARG 3   ? NE  ? A ARG 16  NE  
5   1 Y 1 B ARG 3   ? CZ  ? A ARG 16  CZ  
6   1 Y 1 B ARG 3   ? NH1 ? A ARG 16  NH1 
7   1 Y 1 B ARG 3   ? NH2 ? A ARG 16  NH2 
8   1 Y 1 B GLN 52  ? CG  ? A GLN 65  CG  
9   1 Y 1 B GLN 52  ? CD  ? A GLN 65  CD  
10  1 Y 1 B GLN 52  ? OE1 ? A GLN 65  OE1 
11  1 Y 1 B GLN 52  ? NE2 ? A GLN 65  NE2 
12  1 Y 1 B LEU 54  ? CG  ? A LEU 67  CG  
13  1 Y 1 B LEU 54  ? CD1 ? A LEU 67  CD1 
14  1 Y 1 B LEU 54  ? CD2 ? A LEU 67  CD2 
15  1 Y 1 B ASP 68  ? CG  ? A ASP 81  CG  
16  1 Y 1 B ASP 68  ? OD1 ? A ASP 81  OD1 
17  1 Y 1 B ASP 68  ? OD2 ? A ASP 81  OD2 
18  1 Y 1 B GLU 73  ? CG  ? A GLU 86  CG  
19  1 Y 1 B GLU 73  ? CD  ? A GLU 86  CD  
20  1 Y 1 B GLU 73  ? OE1 ? A GLU 86  OE1 
21  1 Y 1 B GLU 73  ? OE2 ? A GLU 86  OE2 
22  1 Y 1 B ARG 74  ? CG  ? A ARG 87  CG  
23  1 Y 1 B ARG 74  ? CD  ? A ARG 87  CD  
24  1 Y 1 B ARG 74  ? NE  ? A ARG 87  NE  
25  1 Y 1 B ARG 74  ? CZ  ? A ARG 87  CZ  
26  1 Y 1 B ARG 74  ? NH1 ? A ARG 87  NH1 
27  1 Y 1 B ARG 74  ? NH2 ? A ARG 87  NH2 
28  1 Y 1 B GLU 83  ? CG  ? A GLU 96  CG  
29  1 Y 1 B GLU 83  ? CD  ? A GLU 96  CD  
30  1 Y 1 B GLU 83  ? OE1 ? A GLU 96  OE1 
31  1 Y 1 B GLU 83  ? OE2 ? A GLU 96  OE2 
32  1 Y 1 B ARG 84  ? CG  ? A ARG 97  CG  
33  1 Y 1 B ARG 84  ? CD  ? A ARG 97  CD  
34  1 Y 1 B ARG 84  ? NE  ? A ARG 97  NE  
35  1 Y 1 B ARG 84  ? CZ  ? A ARG 97  CZ  
36  1 Y 1 B ARG 84  ? NH1 ? A ARG 97  NH1 
37  1 Y 1 B ARG 84  ? NH2 ? A ARG 97  NH2 
38  1 Y 1 B ARG 101 ? CG  ? A ARG 114 CG  
39  1 Y 1 B ARG 101 ? CD  ? A ARG 114 CD  
40  1 Y 1 B ARG 101 ? NE  ? A ARG 114 NE  
41  1 Y 1 B ARG 101 ? CZ  ? A ARG 114 CZ  
42  1 Y 1 B ARG 101 ? NH1 ? A ARG 114 NH1 
43  1 Y 1 B ARG 101 ? NH2 ? A ARG 114 NH2 
44  1 Y 1 B GLU 110 ? CG  ? A GLU 123 CG  
45  1 Y 1 B GLU 110 ? CD  ? A GLU 123 CD  
46  1 Y 1 B GLU 110 ? OE1 ? A GLU 123 OE1 
47  1 Y 1 B GLU 110 ? OE2 ? A GLU 123 OE2 
48  1 Y 1 B GLU 196 ? CG  ? A GLU 209 CG  
49  1 Y 1 B GLU 196 ? CD  ? A GLU 209 CD  
50  1 Y 1 B GLU 196 ? OE1 ? A GLU 209 OE1 
51  1 Y 1 B GLU 196 ? OE2 ? A GLU 209 OE2 
52  1 Y 1 B ARG 197 ? CG  ? A ARG 210 CG  
53  1 Y 1 B ARG 197 ? CD  ? A ARG 210 CD  
54  1 Y 1 B ARG 197 ? NE  ? A ARG 210 NE  
55  1 Y 1 B ARG 197 ? CZ  ? A ARG 210 CZ  
56  1 Y 1 B ARG 197 ? NH1 ? A ARG 210 NH1 
57  1 Y 1 B ARG 197 ? NH2 ? A ARG 210 NH2 
58  1 Y 1 B GLN 198 ? CG  ? A GLN 211 CG  
59  1 Y 1 B GLN 198 ? CD  ? A GLN 211 CD  
60  1 Y 1 B GLN 198 ? OE1 ? A GLN 211 OE1 
61  1 Y 1 B GLN 198 ? NE2 ? A GLN 211 NE2 
62  1 Y 1 B MET 201 ? CG  ? A MET 214 CG  
63  1 Y 1 B MET 201 ? SD  ? A MET 214 SD  
64  1 Y 1 B MET 201 ? CE  ? A MET 214 CE  
65  1 Y 1 A ARG 3   ? CD  ? B ARG 16  CD  
66  1 Y 1 A ARG 3   ? NE  ? B ARG 16  NE  
67  1 Y 1 A ARG 3   ? CZ  ? B ARG 16  CZ  
68  1 Y 1 A ARG 3   ? NH1 ? B ARG 16  NH1 
69  1 Y 1 A ARG 3   ? NH2 ? B ARG 16  NH2 
70  1 Y 1 A GLU 49  ? CG  ? B GLU 62  CG  
71  1 Y 1 A GLU 49  ? CD  ? B GLU 62  CD  
72  1 Y 1 A GLU 49  ? OE1 ? B GLU 62  OE1 
73  1 Y 1 A GLU 49  ? OE2 ? B GLU 62  OE2 
74  1 Y 1 A ARG 98  ? CG  ? B ARG 111 CG  
75  1 Y 1 A ARG 98  ? CD  ? B ARG 111 CD  
76  1 Y 1 A ARG 98  ? NE  ? B ARG 111 NE  
77  1 Y 1 A ARG 98  ? CZ  ? B ARG 111 CZ  
78  1 Y 1 A ARG 98  ? NH1 ? B ARG 111 NH1 
79  1 Y 1 A ARG 98  ? NH2 ? B ARG 111 NH2 
80  1 Y 1 A ARG 101 ? CG  ? B ARG 114 CG  
81  1 Y 1 A ARG 101 ? CD  ? B ARG 114 CD  
82  1 Y 1 A ARG 101 ? NE  ? B ARG 114 NE  
83  1 Y 1 A ARG 101 ? CZ  ? B ARG 114 CZ  
84  1 Y 1 A ARG 101 ? NH1 ? B ARG 114 NH1 
85  1 Y 1 A ARG 101 ? NH2 ? B ARG 114 NH2 
86  1 Y 1 A ARG 136 ? CG  ? B ARG 149 CG  
87  1 Y 1 A ARG 136 ? CD  ? B ARG 149 CD  
88  1 Y 1 A ARG 136 ? NE  ? B ARG 149 NE  
89  1 Y 1 A ARG 136 ? CZ  ? B ARG 149 CZ  
90  1 Y 1 A ARG 136 ? NH1 ? B ARG 149 NH1 
91  1 Y 1 A ARG 136 ? NH2 ? B ARG 149 NH2 
92  1 Y 1 A GLU 196 ? CG  ? B GLU 209 CG  
93  1 Y 1 A GLU 196 ? CD  ? B GLU 209 CD  
94  1 Y 1 A GLU 196 ? OE1 ? B GLU 209 OE1 
95  1 Y 1 A GLU 196 ? OE2 ? B GLU 209 OE2 
96  1 Y 1 A ARG 197 ? CG  ? B ARG 210 CG  
97  1 Y 1 A ARG 197 ? CD  ? B ARG 210 CD  
98  1 Y 1 A ARG 197 ? NE  ? B ARG 210 NE  
99  1 Y 1 A ARG 197 ? CZ  ? B ARG 210 CZ  
100 1 Y 1 A ARG 197 ? NH1 ? B ARG 210 NH1 
101 1 Y 1 A ARG 197 ? NH2 ? B ARG 210 NH2 
102 1 Y 1 A GLN 198 ? CG  ? B GLN 211 CG  
103 1 Y 1 A GLN 198 ? CD  ? B GLN 211 CD  
104 1 Y 1 A GLN 198 ? OE1 ? B GLN 211 OE1 
105 1 Y 1 A GLN 198 ? NE2 ? B GLN 211 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0430 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BALBES  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.40 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GWU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.727 
_cell.length_a_esd                 ? 
_cell.length_b                     57.293 
_cell.length_b_esd                 ? 
_cell.length_c                     91.267 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9GWU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 1 2 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                   9GWU 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;apo-SQDH was grown using a 20 mg/mL protein solution in 50 mM TRIS buffer pH 7.5 containing 300 mM NaCl in a drop with 0.15 uL protein: 0.15 uL mother liquor, the latter comprising 0.1 M MIB (Sodium malonate dibasic monohydrate, Imidazole, Boric acid) buffer pH 7.0 and 25% w/v PEG (polyethylene glycol) 1500.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GWU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               63.07 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     46667 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.89 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.086 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       312595 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.079 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.70 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           16598 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2440 
_reflns_shell.percent_possible_obs                          99.8 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.8 
_reflns_shell.pdbx_chi_squared                              0.86 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.1 
_reflns_shell.pdbx_Rrim_I_all                               0.956 
_reflns_shell.pdbx_Rpim_I_all                               0.362 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.761 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.883 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -1.48 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.07 
_refine.aniso_B[2][2]                            1.57 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.11 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.591 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9GWU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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                            1.70 
_refine.ls_d_res_low                             63.07 
_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                     44228 
_refine.ls_number_reflns_R_free                  2394 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.15 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19677 
_refine.ls_R_factor_R_free                       0.23706 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19460 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.127 
_refine.pdbx_overall_ESU_R_Free                  0.123 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_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                 ? 
_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                             7.641 
_refine.overall_SU_ML                            0.117 
_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                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        63.07 
_refine_hist.number_atoms_solvent             179 
_refine_hist.number_atoms_total               3972 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3793 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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_restraint_function 
'X-RAY DIFFRACTION' ? 0.016  0.012  3863 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.468  1.774  5244 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.367  5.000  521  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.586 5.000  34   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.435 10.000 581  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.166  0.200  596  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  2996 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.229  1.658  2078 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.944  2.977  2595 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.632  1.905  1785 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.022  20.02  5854 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             193 
_refine_ls_shell.number_reflns_R_work             3243 
_refine_ls_shell.percent_reflns_obs               99.25 
_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                  0.285 
_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.pdbx_total_number_of_bins_used   20 
_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                  0.335 
# 
_struct.entry_id                     9GWU 
_struct.title                        
'Crystal structure of sulfoquinovose-1-dehydrogenase from Pseudomonas Putida (sulfo-ED pathway)' 
_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        9GWU 
_struct_keywords.text            
'sulfoquinovose; sulfoglycolysis; short-chain dehydrogenase/reductase; native structure, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SQD_PSEPU 
_struct_ref.pdbx_db_accession          P0DOV5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNRHTDTHYPSLADKVVLISGGASGIGRAFVEAFVAQGSRVAFLDLDAEAGQGLAHALGANSLFLPCDVRDIERLKACVA
EVERTWGAVDVLINNAARDDRHALADVSVEYWDERMQTNLRHAFFAAQAVAPGMARRGSGAIINMGSISWMRGRPGMVCY
TTAKAALNGMTRTLARELGGQGIRINSLVPGAIRTERQDAMWAADPAGLEAASQAFIDQQMLKFRLDASDCARLALFLAS
DDSRGCTGQNFVVDAGLSIQ
;
_struct_ref.pdbx_align_begin           1 
# 
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 9GWU B 14 ? 273 ? P0DOV5 1 ? 260 ? 1 260 
2 1 9GWU A 14 ? 273 ? P0DOV5 1 ? 260 ? 1 260 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GWU MET B 1  ? UNP P0DOV5 ? ? 'initiating methionine' -12 1  
1 9GWU GLY B 2  ? UNP P0DOV5 ? ? 'expression tag'        -11 2  
1 9GWU SER B 3  ? UNP P0DOV5 ? ? 'expression tag'        -10 3  
1 9GWU SER B 4  ? UNP P0DOV5 ? ? 'expression tag'        -9  4  
1 9GWU HIS B 5  ? UNP P0DOV5 ? ? 'expression tag'        -8  5  
1 9GWU HIS B 6  ? UNP P0DOV5 ? ? 'expression tag'        -7  6  
1 9GWU HIS B 7  ? UNP P0DOV5 ? ? 'expression tag'        -6  7  
1 9GWU HIS B 8  ? UNP P0DOV5 ? ? 'expression tag'        -5  8  
1 9GWU HIS B 9  ? UNP P0DOV5 ? ? 'expression tag'        -4  9  
1 9GWU HIS B 10 ? UNP P0DOV5 ? ? 'expression tag'        -3  10 
1 9GWU SER B 11 ? UNP P0DOV5 ? ? 'expression tag'        -2  11 
1 9GWU SER B 12 ? UNP P0DOV5 ? ? 'expression tag'        -1  12 
1 9GWU GLY B 13 ? UNP P0DOV5 ? ? 'expression tag'        0   13 
2 9GWU MET A 1  ? UNP P0DOV5 ? ? 'initiating methionine' -12 14 
2 9GWU GLY A 2  ? UNP P0DOV5 ? ? 'expression tag'        -11 15 
2 9GWU SER A 3  ? UNP P0DOV5 ? ? 'expression tag'        -10 16 
2 9GWU SER A 4  ? UNP P0DOV5 ? ? 'expression tag'        -9  17 
2 9GWU HIS A 5  ? UNP P0DOV5 ? ? 'expression tag'        -8  18 
2 9GWU HIS A 6  ? UNP P0DOV5 ? ? 'expression tag'        -7  19 
2 9GWU HIS A 7  ? UNP P0DOV5 ? ? 'expression tag'        -6  20 
2 9GWU HIS A 8  ? UNP P0DOV5 ? ? 'expression tag'        -5  21 
2 9GWU HIS A 9  ? UNP P0DOV5 ? ? 'expression tag'        -4  22 
2 9GWU HIS A 10 ? UNP P0DOV5 ? ? 'expression tag'        -3  23 
2 9GWU SER A 11 ? UNP P0DOV5 ? ? 'expression tag'        -2  24 
2 9GWU SER A 12 ? UNP P0DOV5 ? ? 'expression tag'        -1  25 
2 9GWU GLY A 13 ? UNP P0DOV5 ? ? 'expression tag'        0   26 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 14060 ? 
1 MORE         -73   ? 
1 'SSA (A^2)'  33670 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'SEC-MALLS confirmed homotetrameric assembly in solution' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_555 -x,y,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 TYR A 22  ? ALA A 26  ? TYR B 9   ALA B 13  5 ? 5  
HELX_P HELX_P2  AA2 SER A 37  ? GLN A 50  ? SER B 24  GLN B 37  1 ? 14 
HELX_P HELX_P3  AA3 ASP A 60  ? GLY A 72  ? ASP B 47  GLY B 59  1 ? 13 
HELX_P HELX_P4  AA4 ASP A 84  ? GLY A 100 ? ASP B 71  GLY B 87  1 ? 17 
HELX_P HELX_P5  AA5 ALA A 116 ? VAL A 120 ? ALA B 103 VAL B 107 5 ? 5  
HELX_P HELX_P6  AA6 SER A 121 ? LEU A 133 ? SER B 108 LEU B 120 1 ? 13 
HELX_P HELX_P7  AA7 LEU A 133 ? GLY A 151 ? LEU B 120 GLY B 138 1 ? 19 
HELX_P HELX_P8  AA8 SER A 160 ? ARG A 165 ? SER B 147 ARG B 152 1 ? 6  
HELX_P HELX_P9  AA9 MET A 170 ? GLY A 193 ? MET B 157 GLY B 180 1 ? 24 
HELX_P HELX_P10 AB1 THR A 208 ? MET A 214 ? THR B 195 MET B 201 1 ? 7  
HELX_P HELX_P11 AB2 ASP A 218 ? GLN A 233 ? ASP B 205 GLN B 220 1 ? 16 
HELX_P HELX_P12 AB3 ALA A 241 ? SER A 253 ? ALA B 228 SER B 240 1 ? 13 
HELX_P HELX_P13 AB4 ASP A 254 ? ARG A 257 ? ASP B 241 ARG B 244 5 ? 4  
HELX_P HELX_P14 AB5 TYR B 22  ? ALA B 26  ? TYR A 9   ALA A 13  5 ? 5  
HELX_P HELX_P15 AB6 SER B 37  ? GLN B 50  ? SER A 24  GLN A 37  1 ? 14 
HELX_P HELX_P16 AB7 ASP B 60  ? GLY B 72  ? ASP A 47  GLY A 59  1 ? 13 
HELX_P HELX_P17 AB8 ASP B 84  ? GLY B 100 ? ASP A 71  GLY A 87  1 ? 17 
HELX_P HELX_P18 AB9 ALA B 116 ? VAL B 120 ? ALA A 103 VAL A 107 5 ? 5  
HELX_P HELX_P19 AC1 SER B 121 ? LEU B 133 ? SER A 108 LEU A 120 1 ? 13 
HELX_P HELX_P20 AC2 LEU B 133 ? GLY B 151 ? LEU A 120 GLY A 138 1 ? 19 
HELX_P HELX_P21 AC3 SER B 160 ? ARG B 165 ? SER A 147 ARG A 152 1 ? 6  
HELX_P HELX_P22 AC4 MET B 170 ? GLY B 193 ? MET A 157 GLY A 180 1 ? 24 
HELX_P HELX_P23 AC5 THR B 208 ? MET B 214 ? THR A 195 MET A 201 1 ? 7  
HELX_P HELX_P24 AC6 ASP B 218 ? GLN B 233 ? ASP A 205 GLN A 220 1 ? 16 
HELX_P HELX_P25 AC7 ALA B 241 ? SER B 253 ? ALA A 228 SER A 240 1 ? 13 
HELX_P HELX_P26 AC8 ASP B 254 ? ARG B 257 ? ASP A 241 ARG A 244 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA2 1 2 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
AA4 1 2 ? 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 SER A 75  ? PRO A 79  ? SER B 62  PRO B 66  
AA1 2 ARG A 53  ? ASP A 58  ? ARG B 40  ASP B 45  
AA1 3 VAL A 29  ? SER A 33  ? VAL B 16  SER B 20  
AA1 4 VAL A 104 ? ASN A 107 ? VAL B 91  ASN B 94  
AA1 5 GLY A 153 ? MET A 158 ? GLY B 140 MET B 145 
AA1 6 ILE A 196 ? PRO A 203 ? ILE B 183 PRO B 190 
AA1 7 ASN A 263 ? VAL A 266 ? ASN B 250 VAL B 253 
AA2 1 ILE A 206 ? ARG A 207 ? ILE B 193 ARG B 194 
AA2 2 LEU A 239 ? ASP A 240 ? LEU B 226 ASP B 227 
AA3 1 SER B 75  ? PRO B 79  ? SER A 62  PRO A 66  
AA3 2 ARG B 53  ? ASP B 58  ? ARG A 40  ASP A 45  
AA3 3 VAL B 29  ? SER B 33  ? VAL A 16  SER A 20  
AA3 4 VAL B 104 ? ASN B 107 ? VAL A 91  ASN A 94  
AA3 5 GLY B 153 ? MET B 158 ? GLY A 140 MET A 145 
AA3 6 ILE B 196 ? PRO B 203 ? ILE A 183 PRO A 190 
AA3 7 ASN B 263 ? VAL B 266 ? ASN A 250 VAL A 253 
AA4 1 ILE B 206 ? ARG B 207 ? ILE A 193 ARG A 194 
AA4 2 LEU B 239 ? ASP B 240 ? LEU A 226 ASP A 227 
# 
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 LEU A 78  ? O LEU B 65  N PHE A 56  ? N PHE B 43  
AA1 2 3 O ALA A 55  ? O ALA B 42  N VAL A 30  ? N VAL B 17  
AA1 3 4 N LEU A 31  ? N LEU B 18  O ILE A 106 ? O ILE B 93  
AA1 4 5 N LEU A 105 ? N LEU B 92  O ILE A 156 ? O ILE B 143 
AA1 5 6 N ASN A 157 ? N ASN B 144 O ASN A 199 ? O ASN B 186 
AA1 6 7 N VAL A 202 ? N VAL B 189 O PHE A 264 ? O PHE B 251 
AA2 1 2 N ARG A 207 ? N ARG B 194 O LEU A 239 ? O LEU B 226 
AA3 1 2 O LEU B 76  ? O LEU A 63  N PHE B 56  ? N PHE A 43  
AA3 2 3 O ALA B 55  ? O ALA A 42  N VAL B 30  ? N VAL A 17  
AA3 3 4 N LEU B 31  ? N LEU A 18  O ILE B 106 ? O ILE A 93  
AA3 4 5 N LEU B 105 ? N LEU A 92  O ILE B 156 ? O ILE A 143 
AA3 5 6 N GLY B 153 ? N GLY A 140 O ARG B 197 ? O ARG A 184 
AA3 6 7 N VAL B 202 ? N VAL A 189 O PHE B 264 ? O PHE A 251 
AA4 1 2 N ARG B 207 ? N ARG A 194 O LEU B 239 ? O LEU A 226 
# 
_pdbx_entry_details.entry_id                   9GWU 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA B ARG 3   ? ? CB B ARG 3   ? ? CG  B ARG 3   ? ? 127.64 113.40 14.24  2.20 N 
2  1 CB B LEU 58  ? ? CG B LEU 58  ? ? CD1 B LEU 58  ? ? 99.81  111.00 -11.19 1.70 N 
3  1 NE B ARG 70  ? ? CZ B ARG 70  ? ? NH1 B ARG 70  ? ? 116.64 120.30 -3.66  0.50 N 
4  1 CB B GLU 73  ? ? CA B GLU 73  ? ? C   B GLU 73  ? ? 129.87 110.40 19.47  2.00 N 
5  1 N  B ARG 74  ? ? CA B ARG 74  ? ? CB  B ARG 74  ? ? 121.71 110.60 11.11  1.80 N 
6  1 CG B ARG 98  ? ? CD B ARG 98  ? ? NE  B ARG 98  ? ? 96.46  111.80 -15.34 2.10 N 
7  1 CD B ARG 137 ? ? NE B ARG 137 ? ? CZ  B ARG 137 ? ? 133.61 123.60 10.01  1.40 N 
8  1 CG B MET 157 ? ? SD B MET 157 ? ? CE  B MET 157 ? ? 111.86 100.20 11.66  1.60 N 
9  1 CG B GLU 177 ? ? CD B GLU 177 ? ? OE1 B GLU 177 ? ? 135.60 118.30 17.30  2.00 N 
10 1 CG B GLU 177 ? ? CD B GLU 177 ? ? OE2 B GLU 177 ? ? 99.12  118.30 -19.18 2.00 N 
11 1 NE B ARG 233 ? ? CZ B ARG 233 ? ? NH1 B ARG 233 ? ? 124.96 120.30 4.66   0.50 N 
12 1 NE B ARG 233 ? ? CZ B ARG 233 ? ? NH2 B ARG 233 ? ? 117.07 120.30 -3.23  0.50 N 
13 1 CB B GLN 260 ? ? CA B GLN 260 ? ? C   B GLN 260 ? ? 96.54  110.40 -13.86 2.00 N 
14 1 NE A ARG 70  ? ? CZ A ARG 70  ? ? NH1 A ARG 70  ? ? 116.27 120.30 -4.03  0.50 N 
15 1 NE A ARG 74  ? ? CZ A ARG 74  ? ? NH2 A ARG 74  ? ? 117.10 120.30 -3.20  0.50 N 
16 1 CB A ARG 101 ? ? CA A ARG 101 ? ? C   A ARG 101 ? ? 123.74 110.40 13.34  2.00 N 
17 1 NE A ARG 152 ? ? CZ A ARG 152 ? ? NH1 A ARG 152 ? ? 116.61 120.30 -3.69  0.50 N 
18 1 NE A ARG 154 ? ? CZ A ARG 154 ? ? NH2 A ARG 154 ? ? 116.73 120.30 -3.57  0.50 N 
19 1 NE A ARG 194 ? ? CZ A ARG 194 ? ? NH1 A ARG 194 ? ? 123.68 120.30 3.38   0.50 N 
20 1 CG A MET 201 ? ? SD A MET 201 ? ? CE  A MET 201 ? ? 115.47 100.20 15.27  1.60 N 
21 1 NE A ARG 233 ? ? CZ A ARG 233 ? ? NH1 A ARG 233 ? ? 116.94 120.30 -3.36  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS B 4   ? ? 68.84   -24.72 
2  1 ASP B 14  ? ? 72.58   -1.70  
3  1 HIS B 102 ? ? -168.73 117.24 
4  1 MET B 157 ? ? -152.58 48.61  
5  1 ALA B 203 ? ? -64.96  2.14   
6  1 LYS B 223 ? ? -99.82  51.17  
7  1 HIS A 4   ? ? 75.09   -25.51 
8  1 ASP A 14  ? ? 73.73   -13.13 
9  1 LEU A 120 ? ? -128.17 -50.73 
10 1 MET A 157 ? ? -157.06 53.30  
11 1 ALA A 203 ? ? -58.64  -1.37  
12 1 LYS A 223 ? ? -103.91 56.84  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG B 115 ? ? 0.113 'SIDE CHAIN' 
2 1 ARG B 136 ? ? 0.084 'SIDE CHAIN' 
3 1 ARG B 233 ? ? 0.083 'SIDE CHAIN' 
4 1 ARG A 40  ? ? 0.082 'SIDE CHAIN' 
5 1 ARG A 137 ? ? 0.089 'SIDE CHAIN' 
6 1 ARG A 233 ? ? 0.085 'SIDE CHAIN' 
7 1 ARG A 244 ? ? 0.109 'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -21.0103 -5.1013 4.0682  0.0346 ? -0.0766 ? 0.0177 ? 0.2436 ? -0.0363 ? 0.0765 ? 1.4399 ? -0.1397 
? -0.3733 ? 0.4483 ? 0.2156 ? 2.6434 ? -0.0059 ? 0.1582  ? -0.1702 ? 0.0147 ? -0.0903 ? 0.1373  ? 0.2654  ? -0.7971 ? 0.0963  ? 
2 'X-RAY DIFFRACTION' ? refined 2.6064   2.8850  21.3546 0.0228 ? -0.0294 ? 0.0064 ? 0.1163 ? 0.0030  ? 0.0354 ? 1.2342 ? -0.2802 
? -0.1773 ? 0.2542 ? 0.0827 ? 2.8483 ? 0.0090  ? -0.2639 ? 0.0689  ? 0.0417 ? -0.0077 ? -0.0443 ? -0.1218 ? 0.3425  ? -0.0013 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? B 1 ? ? ? B 260 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 2 ? ? ? A 260 ? ? ? 
# 
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 B MET -12 ? A MET 1  
2  1 Y 1 B GLY -11 ? A GLY 2  
3  1 Y 1 B SER -10 ? A SER 3  
4  1 Y 1 B SER -9  ? A SER 4  
5  1 Y 1 B HIS -8  ? A HIS 5  
6  1 Y 1 B HIS -7  ? A HIS 6  
7  1 Y 1 B HIS -6  ? A HIS 7  
8  1 Y 1 B HIS -5  ? A HIS 8  
9  1 Y 1 B HIS -4  ? A HIS 9  
10 1 Y 1 B HIS -3  ? A HIS 10 
11 1 Y 1 B SER -2  ? A SER 11 
12 1 Y 1 B SER -1  ? A SER 12 
13 1 Y 1 B GLY 0   ? A GLY 13 
14 1 Y 1 A MET -12 ? B MET 1  
15 1 Y 1 A GLY -11 ? B GLY 2  
16 1 Y 1 A SER -10 ? B SER 3  
17 1 Y 1 A SER -9  ? B SER 4  
18 1 Y 1 A HIS -8  ? B HIS 5  
19 1 Y 1 A HIS -7  ? B HIS 6  
20 1 Y 1 A HIS -6  ? B HIS 7  
21 1 Y 1 A HIS -5  ? B HIS 8  
22 1 Y 1 A HIS -4  ? B HIS 9  
23 1 Y 1 A HIS -3  ? B HIS 10 
24 1 Y 1 A SER -2  ? B SER 11 
25 1 Y 1 A SER -1  ? B SER 12 
26 1 Y 1 A GLY 0   ? B GLY 13 
27 1 Y 1 A MET 1   ? B MET 14 
# 
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 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Biotechnology and Biological Sciences Research Council (BBSRC)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/W003805/1 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-P0DOV5 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GWU 
_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]   0.012088 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000718 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017454 
_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]   0.010976 
_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   . MET A 1 14  ? -32.413 -12.692 20.769  1.00 46.44  ? 1   MET B N   1 
ATOM   2    C CA  . MET A 1 14  ? -31.690 -11.780 19.838  1.00 57.03  ? 1   MET B CA  1 
ATOM   3    C C   . MET A 1 14  ? -30.159 -11.767 20.096  1.00 56.36  ? 1   MET B C   1 
ATOM   4    O O   . MET A 1 14  ? -29.705 -11.508 21.196  1.00 53.77  ? 1   MET B O   1 
ATOM   5    C CB  . MET A 1 14  ? -32.359 -10.393 19.837  1.00 60.45  ? 1   MET B CB  1 
ATOM   6    N N   . ASN A 1 15  ? -29.348 -11.989 19.050  1.00 56.08  ? 2   ASN B N   1 
ATOM   7    C CA  . ASN A 1 15  ? -27.892 -12.186 19.064  1.00 57.79  ? 2   ASN B CA  1 
ATOM   8    C C   . ASN A 1 15  ? -27.146 -10.847 19.040  1.00 49.40  ? 2   ASN B C   1 
ATOM   9    O O   . ASN A 1 15  ? -27.362 -10.019 18.163  1.00 45.81  ? 2   ASN B O   1 
ATOM   10   C CB  . ASN A 1 15  ? -27.384 -12.965 17.844  1.00 63.26  ? 2   ASN B CB  1 
ATOM   11   C CG  . ASN A 1 15  ? -28.099 -14.275 17.594  1.00 76.50  ? 2   ASN B CG  1 
ATOM   12   O OD1 . ASN A 1 15  ? -29.317 -14.386 17.799  1.00 80.85  ? 2   ASN B OD1 1 
ATOM   13   N ND2 . ASN A 1 15  ? -27.356 -15.272 17.126  1.00 88.30  ? 2   ASN B ND2 1 
ATOM   14   N N   . ARG A 1 16  ? -26.248 -10.701 20.009  1.00 44.58  ? 3   ARG B N   1 
ATOM   15   C CA  . ARG A 1 16  ? -25.587 -9.458  20.372  1.00 44.07  ? 3   ARG B CA  1 
ATOM   16   C C   . ARG A 1 16  ? -24.328 -9.346  19.525  1.00 35.56  ? 3   ARG B C   1 
ATOM   17   O O   . ARG A 1 16  ? -23.929 -8.199  19.207  1.00 33.55  ? 3   ARG B O   1 
ATOM   18   C CB  . ARG A 1 16  ? -25.378 -9.473  21.897  1.00 47.55  ? 3   ARG B CB  1 
ATOM   19   C CG  . ARG A 1 16  ? -26.275 -8.860  22.965  1.00 51.86  ? 3   ARG B CG  1 
ATOM   20   C CD  . ARG A 1 16  ? -25.470 -8.781  24.264  1.00 46.66  ? 3   ARG B CD  1 
ATOM   21   N N   . HIS A 1 17  ? -23.704 -10.515 19.170  1.00 31.38  ? 4   HIS B N   1 
ATOM   22   C CA  . HIS A 1 17  ? -22.384 -10.577 18.508  1.00 32.29  ? 4   HIS B CA  1 
ATOM   23   C C   . HIS A 1 17  ? -21.192 -10.137 19.406  1.00 35.75  ? 4   HIS B C   1 
ATOM   24   O O   . HIS A 1 17  ? -20.046 -10.492 19.117  1.00 36.47  ? 4   HIS B O   1 
ATOM   25   C CB  . HIS A 1 17  ? -22.361 -9.841  17.131  1.00 31.28  ? 4   HIS B CB  1 
ATOM   26   C CG  . HIS A 1 17  ? -23.361 -10.521 16.242  1.00 34.06  ? 4   HIS B CG  1 
ATOM   27   N ND1 . HIS A 1 17  ? -23.112 -11.760 15.689  1.00 36.03  ? 4   HIS B ND1 1 
ATOM   28   C CD2 . HIS A 1 17  ? -24.687 -10.275 16.030  1.00 37.83  ? 4   HIS B CD2 1 
ATOM   29   C CE1 . HIS A 1 17  ? -24.213 -12.195 15.045  1.00 34.10  ? 4   HIS B CE1 1 
ATOM   30   N NE2 . HIS A 1 17  ? -25.180 -11.332 15.239  1.00 38.09  ? 4   HIS B NE2 1 
ATOM   31   N N   . THR A 1 18  ? -21.419 -9.295  20.445  1.00 33.34  ? 5   THR B N   1 
ATOM   32   C CA  . THR A 1 18  ? -20.340 -8.840  21.325  1.00 28.18  ? 5   THR B CA  1 
ATOM   33   C C   . THR A 1 18  ? -20.936 -8.571  22.696  1.00 29.22  ? 5   THR B C   1 
ATOM   34   O O   . THR A 1 18  ? -22.138 -8.301  22.778  1.00 31.92  ? 5   THR B O   1 
ATOM   35   C CB  . THR A 1 18  ? -19.640 -7.594  20.761  1.00 26.61  ? 5   THR B CB  1 
ATOM   36   O OG1 . THR A 1 18  ? -18.551 -7.352  21.641  1.00 26.62  ? 5   THR B OG1 1 
ATOM   37   C CG2 . THR A 1 18  ? -20.535 -6.387  20.555  1.00 27.33  ? 5   THR B CG2 1 
ATOM   38   N N   . ASP A 1 19  ? -20.104 -8.609  23.751  1.00 29.73  ? 6   ASP B N   1 
ATOM   39   C CA  . ASP A 1 19  ? -20.544 -8.046  25.039  1.00 32.27  ? 6   ASP B CA  1 
ATOM   40   C C   . ASP A 1 19  ? -20.173 -6.559  25.212  1.00 29.09  ? 6   ASP B C   1 
ATOM   41   O O   . ASP A 1 19  ? -20.563 -5.920  26.209  1.00 26.86  ? 6   ASP B O   1 
ATOM   42   C CB  . ASP A 1 19  ? -20.073 -8.889  26.209  1.00 35.19  ? 6   ASP B CB  1 
ATOM   43   C CG  . ASP A 1 19  ? -18.572 -9.099  26.218  1.00 38.91  ? 6   ASP B CG  1 
ATOM   44   O OD1 . ASP A 1 19  ? -17.909 -8.704  25.224  1.00 38.03  ? 6   ASP B OD1 1 
ATOM   45   O OD2 . ASP A 1 19  ? -18.036 -9.625  27.223  1.00 43.02  ? 6   ASP B OD2 1 
ATOM   46   N N   . THR A 1 20  ? -19.363 -6.002  24.296  1.00 28.83  ? 7   THR B N   1 
ATOM   47   C CA  . THR A 1 20  ? -19.023 -4.581  24.362  1.00 25.69  ? 7   THR B CA  1 
ATOM   48   C C   . THR A 1 20  ? -20.267 -3.692  24.216  1.00 27.05  ? 7   THR B C   1 
ATOM   49   O O   . THR A 1 20  ? -21.174 -4.053  23.477  1.00 28.83  ? 7   THR B O   1 
ATOM   50   C CB  . THR A 1 20  ? -18.065 -4.318  23.199  1.00 24.34  ? 7   THR B CB  1 
ATOM   51   O OG1 . THR A 1 20  ? -16.935 -5.123  23.509  1.00 25.92  ? 7   THR B OG1 1 
ATOM   52   C CG2 . THR A 1 20  ? -17.617 -2.874  23.129  1.00 21.90  ? 7   THR B CG2 1 
ATOM   53   N N   . HIS A 1 21  ? -20.274 -2.524  24.853  1.00 24.78  ? 8   HIS B N   1 
ATOM   54   C CA  . HIS A 1 21  ? -21.361 -1.566  24.838  1.00 25.03  ? 8   HIS B CA  1 
ATOM   55   C C   . HIS A 1 21  ? -20.887 -0.215  24.349  1.00 25.77  ? 8   HIS B C   1 
ATOM   56   O O   . HIS A 1 21  ? -19.967 0.369   24.927  1.00 23.89  ? 8   HIS B O   1 
ATOM   57   C CB  . HIS A 1 21  ? -21.942 -1.403  26.251  1.00 33.20  ? 8   HIS B CB  1 
ATOM   58   C CG  . HIS A 1 21  ? -23.125 -0.484  26.176  1.00 38.49  ? 8   HIS B CG  1 
ATOM   59   N ND1 . HIS A 1 21  ? -23.333 0.509   27.104  1.00 45.24  ? 8   HIS B ND1 1 
ATOM   60   C CD2 . HIS A 1 21  ? -24.129 -0.344  25.235  1.00 40.78  ? 8   HIS B CD2 1 
ATOM   61   C CE1 . HIS A 1 21  ? -24.454 1.186   26.799  1.00 43.53  ? 8   HIS B CE1 1 
ATOM   62   N NE2 . HIS A 1 21  ? -24.921 0.694   25.658  1.00 46.07  ? 8   HIS B NE2 1 
ATOM   63   N N   . TYR A 1 22  ? -21.411 0.214   23.179  1.00 23.57  ? 9   TYR B N   1 
ATOM   64   C CA  . TYR A 1 22  ? -21.076 1.516   22.633  1.00 21.48  ? 9   TYR B CA  1 
ATOM   65   C C   . TYR A 1 22  ? -22.198 2.491   22.851  1.00 25.48  ? 9   TYR B C   1 
ATOM   66   O O   . TYR A 1 22  ? -23.164 2.501   22.072  1.00 26.46  ? 9   TYR B O   1 
ATOM   67   C CB  . TYR A 1 22  ? -20.773 1.471   21.140  1.00 21.30  ? 9   TYR B CB  1 
ATOM   68   C CG  . TYR A 1 22  ? -19.610 0.579   20.737  1.00 20.86  ? 9   TYR B CG  1 
ATOM   69   C CD1 . TYR A 1 22  ? -19.805 -0.796  20.519  1.00 23.80  ? 9   TYR B CD1 1 
ATOM   70   C CD2 . TYR A 1 22  ? -18.351 1.121   20.480  1.00 21.08  ? 9   TYR B CD2 1 
ATOM   71   C CE1 . TYR A 1 22  ? -18.774 -1.585  20.036  1.00 21.61  ? 9   TYR B CE1 1 
ATOM   72   C CE2 . TYR A 1 22  ? -17.334 0.358   19.941  1.00 23.04  ? 9   TYR B CE2 1 
ATOM   73   C CZ  . TYR A 1 22  ? -17.554 -0.991  19.741  1.00 24.20  ? 9   TYR B CZ  1 
ATOM   74   O OH  . TYR A 1 22  ? -16.500 -1.711  19.295  1.00 26.36  ? 9   TYR B OH  1 
ATOM   75   N N   . PRO A 1 23  ? -22.193 3.326   23.901  1.00 26.47  ? 10  PRO B N   1 
ATOM   76   C CA  . PRO A 1 23  ? -23.306 4.270   24.077  1.00 26.38  ? 10  PRO B CA  1 
ATOM   77   C C   . PRO A 1 23  ? -23.488 5.203   22.877  1.00 27.09  ? 10  PRO B C   1 
ATOM   78   O O   . PRO A 1 23  ? -24.644 5.629   22.567  1.00 30.54  ? 10  PRO B O   1 
ATOM   79   C CB  . PRO A 1 23  ? -22.934 5.061   25.345  1.00 26.82  ? 10  PRO B CB  1 
ATOM   80   C CG  . PRO A 1 23  ? -22.100 4.068   26.076  1.00 28.91  ? 10  PRO B CG  1 
ATOM   81   C CD  . PRO A 1 23  ? -21.289 3.273   25.042  1.00 24.83  ? 10  PRO B CD  1 
ATOM   82   N N   . SER A 1 24  ? -22.398 5.438   22.120  1.00 24.04  ? 11  SER B N   1 
ATOM   83   C CA  . SER A 1 24  ? -22.494 6.319   20.959  1.00 24.72  ? 11  SER B CA  1 
ATOM   84   C C   . SER A 1 24  ? -23.387 5.723   19.839  1.00 29.76  ? 11  SER B C   1 
ATOM   85   O O   . SER A 1 24  ? -23.773 6.433   18.919  1.00 29.18  ? 11  SER B O   1 
ATOM   86   C CB  . SER A 1 24  ? -21.124 6.757   20.443  1.00 24.24  ? 11  SER B CB  1 
ATOM   87   O OG  . SER A 1 24  ? -20.391 5.612   20.003  1.00 23.88  ? 11  SER B OG  1 
ATOM   88   N N   . LEU A 1 25  ? -23.701 4.410   19.881  1.00 26.57  ? 12  LEU B N   1 
ATOM   89   C CA  . LEU A 1 25  ? -24.518 3.799   18.828  1.00 27.84  ? 12  LEU B CA  1 
ATOM   90   C C   . LEU A 1 25  ? -26.023 3.937   19.103  1.00 29.73  ? 12  LEU B C   1 
ATOM   91   O O   . LEU A 1 25  ? -26.839 3.749   18.204  1.00 30.89  ? 12  LEU B O   1 
ATOM   92   C CB  . LEU A 1 25  ? -24.144 2.356   18.487  1.00 28.42  ? 12  LEU B CB  1 
ATOM   93   C CG  . LEU A 1 25  ? -22.727 2.231   17.884  1.00 24.21  ? 12  LEU B CG  1 
ATOM   94   C CD1 . LEU A 1 25  ? -22.327 0.767   17.691  1.00 23.14  ? 12  LEU B CD1 1 
ATOM   95   C CD2 . LEU A 1 25  ? -22.656 2.988   16.513  1.00 25.29  ? 12  LEU B CD2 1 
ATOM   96   N N   . ALA A 1 26  ? -26.387 4.293   20.352  1.00 31.11  ? 13  ALA B N   1 
ATOM   97   C CA  . ALA A 1 26  ? -27.801 4.287   20.697  1.00 29.99  ? 13  ALA B CA  1 
ATOM   98   C C   . ALA A 1 26  ? -28.559 5.322   19.850  1.00 32.79  ? 13  ALA B C   1 
ATOM   99   O O   . ALA A 1 26  ? -28.115 6.477   19.725  1.00 31.93  ? 13  ALA B O   1 
ATOM   100  C CB  . ALA A 1 26  ? -27.960 4.647   22.200  1.00 30.42  ? 13  ALA B CB  1 
ATOM   101  N N   . ASP A 1 27  ? -29.736 4.930   19.305  1.00 36.12  ? 14  ASP B N   1 
ATOM   102  C CA  . ASP A 1 27  ? -30.603 5.830   18.560  1.00 39.26  ? 14  ASP B CA  1 
ATOM   103  C C   . ASP A 1 27  ? -30.031 6.171   17.186  1.00 37.07  ? 14  ASP B C   1 
ATOM   104  O O   . ASP A 1 27  ? -30.668 6.895   16.438  1.00 38.33  ? 14  ASP B O   1 
ATOM   105  C CB  . ASP A 1 27  ? -31.008 7.077   19.342  1.00 42.83  ? 14  ASP B CB  1 
ATOM   106  C CG  . ASP A 1 27  ? -31.604 6.795   20.728  1.00 56.09  ? 14  ASP B CG  1 
ATOM   107  O OD1 . ASP A 1 27  ? -32.350 5.802   20.856  1.00 57.74  ? 14  ASP B OD1 1 
ATOM   108  O OD2 . ASP A 1 27  ? -31.302 7.544   21.691  1.00 57.10  ? 14  ASP B OD2 1 
ATOM   109  N N   . LYS A 1 28  ? -28.846 5.674   16.829  1.00 30.90  ? 15  LYS B N   1 
ATOM   110  C CA  . LYS A 1 28  ? -28.303 6.089   15.529  1.00 30.28  ? 15  LYS B CA  1 
ATOM   111  C C   . LYS A 1 28  ? -29.079 5.373   14.446  1.00 31.25  ? 15  LYS B C   1 
ATOM   112  O O   . LYS A 1 28  ? -29.451 4.209   14.642  1.00 31.43  ? 15  LYS B O   1 
ATOM   113  C CB  . LYS A 1 28  ? -26.824 5.699   15.408  1.00 29.39  ? 15  LYS B CB  1 
ATOM   114  C CG  . LYS A 1 28  ? -25.917 6.578   16.292  1.00 35.31  ? 15  LYS B CG  1 
ATOM   115  C CD  . LYS A 1 28  ? -25.733 8.064   15.952  1.00 45.18  ? 15  LYS B CD  1 
ATOM   116  C CE  . LYS A 1 28  ? -24.535 8.638   16.661  1.00 51.66  ? 15  LYS B CE  1 
ATOM   117  N NZ  . LYS A 1 28  ? -24.954 9.976   17.096  1.00 59.60  ? 15  LYS B NZ  1 
ATOM   118  N N   . VAL A 1 29  ? -29.186 6.001   13.272  1.00 31.59  ? 16  VAL B N   1 
ATOM   119  C CA  . VAL A 1 29  ? -29.940 5.370   12.204  1.00 32.72  ? 16  VAL B CA  1 
ATOM   120  C C   . VAL A 1 29  ? -28.944 4.646   11.310  1.00 30.07  ? 16  VAL B C   1 
ATOM   121  O O   . VAL A 1 29  ? -28.040 5.299   10.812  1.00 30.17  ? 16  VAL B O   1 
ATOM   122  C CB  . VAL A 1 29  ? -30.758 6.438   11.425  1.00 33.07  ? 16  VAL B CB  1 
ATOM   123  C CG1 . VAL A 1 29  ? -31.398 5.870   10.131  1.00 32.60  ? 16  VAL B CG1 1 
ATOM   124  C CG2 . VAL A 1 29  ? -31.790 7.169   12.281  1.00 33.74  ? 16  VAL B CG2 1 
ATOM   125  N N   . VAL A 1 30  ? -29.068 3.309   11.177  1.00 30.70  ? 17  VAL B N   1 
ATOM   126  C CA  . VAL A 1 30  ? -28.090 2.503   10.446  1.00 29.47  ? 17  VAL B CA  1 
ATOM   127  C C   . VAL A 1 30  ? -28.814 1.886   9.255   1.00 29.38  ? 17  VAL B C   1 
ATOM   128  O O   . VAL A 1 30  ? -29.958 1.492   9.440   1.00 31.61  ? 17  VAL B O   1 
ATOM   129  C CB  . VAL A 1 30  ? -27.595 1.376   11.365  1.00 31.21  ? 17  VAL B CB  1 
ATOM   130  C CG1 . VAL A 1 30  ? -26.643 0.435   10.611  1.00 31.84  ? 17  VAL B CG1 1 
ATOM   131  C CG2 . VAL A 1 30  ? -26.861 1.948   12.560  1.00 27.37  ? 17  VAL B CG2 1 
ATOM   132  N N   . LEU A 1 31  ? -28.182 1.821   8.057   1.00 28.50  ? 18  LEU B N   1 
ATOM   133  C CA  . LEU A 1 31  ? -28.812 1.287   6.857   1.00 30.37  ? 18  LEU B CA  1 
ATOM   134  C C   . LEU A 1 31  ? -27.839 0.321   6.175   1.00 29.87  ? 18  LEU B C   1 
ATOM   135  O O   . LEU A 1 31  ? -26.707 0.701   5.929   1.00 31.63  ? 18  LEU B O   1 
ATOM   136  C CB  . LEU A 1 31  ? -29.148 2.472   5.955   1.00 31.60  ? 18  LEU B CB  1 
ATOM   137  C CG  . LEU A 1 31  ? -29.668 2.056   4.567   1.00 33.76  ? 18  LEU B CG  1 
ATOM   138  C CD1 . LEU A 1 31  ? -30.919 1.143   4.549   1.00 40.07  ? 18  LEU B CD1 1 
ATOM   139  C CD2 . LEU A 1 31  ? -29.698 3.258   3.630   1.00 29.87  ? 18  LEU B CD2 1 
ATOM   140  N N   . ILE A 1 32  ? -28.245 -0.945  6.042   1.00 32.06  ? 19  ILE B N   1 
ATOM   141  C CA  . ILE A 1 32  ? -27.391 -2.054  5.643   1.00 31.39  ? 19  ILE B CA  1 
ATOM   142  C C   . ILE A 1 32  ? -28.017 -2.719  4.416   1.00 31.40  ? 19  ILE B C   1 
ATOM   143  O O   . ILE A 1 32  ? -29.228 -3.091  4.463   1.00 31.85  ? 19  ILE B O   1 
ATOM   144  C CB  . ILE A 1 32  ? -27.299 -3.066  6.795   1.00 30.32  ? 19  ILE B CB  1 
ATOM   145  C CG1 . ILE A 1 32  ? -26.642 -2.367  8.059   1.00 28.63  ? 19  ILE B CG1 1 
ATOM   146  C CG2 . ILE A 1 32  ? -26.455 -4.270  6.334   1.00 30.61  ? 19  ILE B CG2 1 
ATOM   147  C CD1 . ILE A 1 32  ? -27.009 -3.021  9.392   1.00 28.09  ? 19  ILE B CD1 1 
ATOM   148  N N   . SER A 1 33  ? -27.267 -2.761  3.287   1.00 30.00  ? 20  SER B N   1 
ATOM   149  C CA  . SER A 1 33  ? -27.797 -3.456  2.137   1.00 29.85  ? 20  SER B CA  1 
ATOM   150  C C   . SER A 1 33  ? -27.429 -4.933  2.256   1.00 29.86  ? 20  SER B C   1 
ATOM   151  O O   . SER A 1 33  ? -26.450 -5.283  2.928   1.00 30.98  ? 20  SER B O   1 
ATOM   152  C CB  . SER A 1 33  ? -27.295 -2.808  0.832   1.00 28.27  ? 20  SER B CB  1 
ATOM   153  O OG  . SER A 1 33  ? -25.875 -2.938  0.738   1.00 27.83  ? 20  SER B OG  1 
ATOM   154  N N   . GLY A 1 34  ? -28.242 -5.810  1.633   1.00 30.27  ? 21  GLY B N   1 
ATOM   155  C CA  . GLY A 1 34  ? -28.020 -7.248  1.731   1.00 32.52  ? 21  GLY B CA  1 
ATOM   156  C C   . GLY A 1 34  ? -28.089 -7.700  3.187   1.00 33.42  ? 21  GLY B C   1 
ATOM   157  O O   . GLY A 1 34  ? -27.365 -8.620  3.559   1.00 32.86  ? 21  GLY B O   1 
ATOM   158  N N   . GLY A 1 35  ? -29.076 -7.171  3.922   1.00 36.14  ? 22  GLY B N   1 
ATOM   159  C CA  . GLY A 1 35  ? -29.153 -7.274  5.382   1.00 33.19  ? 22  GLY B CA  1 
ATOM   160  C C   . GLY A 1 35  ? -29.946 -8.493  5.893   1.00 37.48  ? 22  GLY B C   1 
ATOM   161  O O   . GLY A 1 35  ? -29.986 -8.694  7.106   1.00 36.44  ? 22  GLY B O   1 
ATOM   162  N N   . ALA A 1 36  ? -30.558 -9.331  5.050   1.00 37.73  ? 23  ALA B N   1 
ATOM   163  C CA  . ALA A 1 36  ? -31.479 -10.320 5.607   1.00 39.42  ? 23  ALA B CA  1 
ATOM   164  C C   . ALA A 1 36  ? -30.798 -11.676 5.825   1.00 44.07  ? 23  ALA B C   1 
ATOM   165  O O   . ALA A 1 36  ? -31.427 -12.555 6.403   1.00 44.43  ? 23  ALA B O   1 
ATOM   166  C CB  . ALA A 1 36  ? -32.697 -10.514 4.684   1.00 41.53  ? 23  ALA B CB  1 
ATOM   167  N N   . SER A 1 37  ? -29.577 -11.900 5.328   1.00 41.60  ? 24  SER B N   1 
ATOM   168  C CA  . SER A 1 37  ? -28.857 -13.166 5.512   1.00 43.75  ? 24  SER B CA  1 
ATOM   169  C C   . SER A 1 37  ? -27.360 -12.962 5.745   1.00 42.12  ? 24  SER B C   1 
ATOM   170  O O   . SER A 1 37  ? -26.876 -11.858 5.553   1.00 39.27  ? 24  SER B O   1 
ATOM   171  C CB  . SER A 1 37  ? -29.090 -14.116 4.334   1.00 47.21  ? 24  SER B CB  1 
ATOM   172  O OG  . SER A 1 37  ? -28.346 -13.737 3.191   1.00 48.48  ? 24  SER B OG  1 
ATOM   173  N N   . GLY A 1 38  ? -26.657 -14.008 6.222   1.00 42.28  ? 25  GLY B N   1 
ATOM   174  C CA  . GLY A 1 38  ? -25.195 -13.993 6.333   1.00 37.87  ? 25  GLY B CA  1 
ATOM   175  C C   . GLY A 1 38  ? -24.620 -12.791 7.101   1.00 34.63  ? 25  GLY B C   1 
ATOM   176  O O   . GLY A 1 38  ? -25.066 -12.453 8.199   1.00 34.98  ? 25  GLY B O   1 
ATOM   177  N N   . ILE A 1 39  ? -23.669 -12.096 6.463   1.00 34.74  ? 26  ILE B N   1 
ATOM   178  C CA  . ILE A 1 39  ? -22.931 -11.107 7.209   1.00 31.50  ? 26  ILE B CA  1 
ATOM   179  C C   . ILE A 1 39  ? -23.875 -9.940  7.471   1.00 29.60  ? 26  ILE B C   1 
ATOM   180  O O   . ILE A 1 39  ? -23.862 -9.335  8.556   1.00 30.35  ? 26  ILE B O   1 
ATOM   181  C CB  . ILE A 1 39  ? -21.620 -10.711 6.494   1.00 27.64  ? 26  ILE B CB  1 
ATOM   182  C CG1 . ILE A 1 39  ? -20.684 -11.910 6.504   1.00 29.79  ? 26  ILE B CG1 1 
ATOM   183  C CG2 . ILE A 1 39  ? -21.005 -9.484  7.164   1.00 29.25  ? 26  ILE B CG2 1 
ATOM   184  C CD1 . ILE A 1 39  ? -19.563 -11.860 5.463   1.00 31.57  ? 26  ILE B CD1 1 
ATOM   185  N N   . GLY A 1 40  ? -24.636 -9.573  6.447   1.00 31.11  ? 27  GLY B N   1 
ATOM   186  C CA  . GLY A 1 40  ? -25.447 -8.374  6.595   1.00 30.94  ? 27  GLY B CA  1 
ATOM   187  C C   . GLY A 1 40  ? -26.473 -8.571  7.731   1.00 33.56  ? 27  GLY B C   1 
ATOM   188  O O   . GLY A 1 40  ? -26.738 -7.628  8.470   1.00 28.07  ? 27  GLY B O   1 
ATOM   189  N N   . ARG A 1 41  ? -26.914 -9.841  7.915   1.00 32.90  ? 28  ARG B N   1 
ATOM   190  C CA  . ARG A 1 41  ? -27.820 -10.213 8.986   1.00 35.20  ? 28  ARG B CA  1 
ATOM   191  C C   . ARG A 1 41  ? -27.146 -10.007 10.334  1.00 32.69  ? 28  ARG B C   1 
ATOM   192  O O   . ARG A 1 41  ? -27.737 -9.488  11.268  1.00 32.69  ? 28  ARG B O   1 
ATOM   193  C CB  . ARG A 1 41  ? -28.472 -11.608 8.817   1.00 36.08  ? 28  ARG B CB  1 
ATOM   194  C CG  . ARG A 1 41  ? -29.122 -12.121 10.091  1.00 39.58  ? 28  ARG B CG  1 
ATOM   195  C CD  . ARG A 1 41  ? -29.634 -13.517 9.894   1.00 46.16  ? 28  ARG B CD  1 
ATOM   196  N NE  . ARG A 1 41  ? -30.130 -14.006 11.177  1.00 51.79  ? 28  ARG B NE  1 
ATOM   197  C CZ  . ARG A 1 41  ? -31.300 -14.638 11.261  1.00 58.34  ? 28  ARG B CZ  1 
ATOM   198  N NH1 . ARG A 1 41  ? -31.657 -15.225 12.416  1.00 55.29  ? 28  ARG B NH1 1 
ATOM   199  N NH2 . ARG A 1 41  ? -32.072 -14.693 10.164  1.00 56.07  ? 28  ARG B NH2 1 
ATOM   200  N N   . ALA A 1 42  ? -25.879 -10.416 10.423  1.00 33.72  ? 29  ALA B N   1 
ATOM   201  C CA  . ALA A 1 42  ? -25.142 -10.187 11.656  1.00 30.92  ? 29  ALA B CA  1 
ATOM   202  C C   . ALA A 1 42  ? -24.995 -8.688  11.956  1.00 29.89  ? 29  ALA B C   1 
ATOM   203  O O   . ALA A 1 42  ? -25.099 -8.302  13.107  1.00 30.53  ? 29  ALA B O   1 
ATOM   204  C CB  . ALA A 1 42  ? -23.824 -10.929 11.658  1.00 30.88  ? 29  ALA B CB  1 
ATOM   205  N N   . PHE A 1 43  ? -24.819 -7.820  10.947  1.00 29.24  ? 30  PHE B N   1 
ATOM   206  C CA  . PHE A 1 43  ? -24.734 -6.395  11.211  1.00 27.01  ? 30  PHE B CA  1 
ATOM   207  C C   . PHE A 1 43  ? -26.060 -5.889  11.749  1.00 31.40  ? 30  PHE B C   1 
ATOM   208  O O   . PHE A 1 43  ? -26.101 -5.146  12.739  1.00 29.70  ? 30  PHE B O   1 
ATOM   209  C CB  . PHE A 1 43  ? -24.433 -5.598  9.930   1.00 27.62  ? 30  PHE B CB  1 
ATOM   210  C CG  . PHE A 1 43  ? -23.070 -5.850  9.304   1.00 24.48  ? 30  PHE B CG  1 
ATOM   211  C CD1 . PHE A 1 43  ? -21.982 -6.215  10.064  1.00 24.68  ? 30  PHE B CD1 1 
ATOM   212  C CD2 . PHE A 1 43  ? -22.905 -5.734  7.930   1.00 26.42  ? 30  PHE B CD2 1 
ATOM   213  C CE1 . PHE A 1 43  ? -20.724 -6.395  9.470   1.00 27.19  ? 30  PHE B CE1 1 
ATOM   214  C CE2 . PHE A 1 43  ? -21.638 -5.787  7.307   1.00 26.90  ? 30  PHE B CE2 1 
ATOM   215  C CZ  . PHE A 1 43  ? -20.527 -6.145  8.087   1.00 25.15  ? 30  PHE B CZ  1 
ATOM   216  N N   . VAL A 1 44  ? -27.164 -6.327  11.125  1.00 34.05  ? 31  VAL B N   1 
ATOM   217  C CA  . VAL A 1 44  ? -28.485 -5.873  11.501  1.00 30.26  ? 31  VAL B CA  1 
ATOM   218  C C   . VAL A 1 44  ? -28.677 -6.217  12.973  1.00 31.15  ? 31  VAL B C   1 
ATOM   219  O O   . VAL A 1 44  ? -29.025 -5.347  13.761  1.00 30.93  ? 31  VAL B O   1 
ATOM   220  C CB  . VAL A 1 44  ? -29.643 -6.416  10.629  1.00 31.93  ? 31  VAL B CB  1 
ATOM   221  C CG1 . VAL A 1 44  ? -31.023 -6.065  11.188  1.00 33.81  ? 31  VAL B CG1 1 
ATOM   222  C CG2 . VAL A 1 44  ? -29.517 -5.901  9.186   1.00 28.98  ? 31  VAL B CG2 1 
ATOM   223  N N   . GLU A 1 45  ? -28.422 -7.487  13.315  1.00 33.46  ? 32  GLU B N   1 
ATOM   224  C CA  . GLU A 1 45  ? -28.565 -7.946  14.702  1.00 34.17  ? 32  GLU B CA  1 
ATOM   225  C C   . GLU A 1 45  ? -27.696 -7.141  15.680  1.00 35.68  ? 32  GLU B C   1 
ATOM   226  O O   . GLU A 1 45  ? -28.169 -6.773  16.762  1.00 38.34  ? 32  GLU B O   1 
ATOM   227  C CB  . GLU A 1 45  ? -28.218 -9.427  14.807  1.00 34.36  ? 32  GLU B CB  1 
ATOM   228  C CG  . GLU A 1 45  ? -29.296 -10.306 14.154  1.00 35.55  ? 32  GLU B CG  1 
ATOM   229  C CD  . GLU A 1 45  ? -28.875 -11.754 13.936  1.00 39.47  ? 32  GLU B CD  1 
ATOM   230  O OE1 . GLU A 1 45  ? -27.659 -11.976 14.004  1.00 38.75  ? 32  GLU B OE1 1 
ATOM   231  O OE2 . GLU A 1 45  ? -29.711 -12.686 13.729  1.00 39.52  ? 32  GLU B OE2 1 
ATOM   232  N N   . ALA A 1 46  ? -26.422 -6.908  15.312  1.00 33.47  ? 33  ALA B N   1 
ATOM   233  C CA  . ALA A 1 46  ? -25.481 -6.291  16.246  1.00 30.21  ? 33  ALA B CA  1 
ATOM   234  C C   . ALA A 1 46  ? -25.899 -4.843  16.489  1.00 27.96  ? 33  ALA B C   1 
ATOM   235  O O   . ALA A 1 46  ? -25.841 -4.363  17.617  1.00 29.10  ? 33  ALA B O   1 
ATOM   236  C CB  . ALA A 1 46  ? -24.026 -6.439  15.786  1.00 27.44  ? 33  ALA B CB  1 
ATOM   237  N N   . PHE A 1 47  ? -26.297 -4.116  15.442  1.00 30.16  ? 34  PHE B N   1 
ATOM   238  C CA  . PHE A 1 47  ? -26.668 -2.732  15.723  1.00 28.84  ? 34  PHE B CA  1 
ATOM   239  C C   . PHE A 1 47  ? -27.968 -2.619  16.521  1.00 31.43  ? 34  PHE B C   1 
ATOM   240  O O   . PHE A 1 47  ? -28.141 -1.685  17.320  1.00 29.42  ? 34  PHE B O   1 
ATOM   241  C CB  . PHE A 1 47  ? -26.741 -1.907  14.448  1.00 27.46  ? 34  PHE B CB  1 
ATOM   242  C CG  . PHE A 1 47  ? -25.347 -1.518  13.971  1.00 28.43  ? 34  PHE B CG  1 
ATOM   243  C CD1 . PHE A 1 47  ? -24.785 -0.287  14.311  1.00 26.00  ? 34  PHE B CD1 1 
ATOM   244  C CD2 . PHE A 1 47  ? -24.681 -2.300  13.013  1.00 23.93  ? 34  PHE B CD2 1 
ATOM   245  C CE1 . PHE A 1 47  ? -23.510 0.034   13.839  1.00 23.23  ? 34  PHE B CE1 1 
ATOM   246  C CE2 . PHE A 1 47  ? -23.398 -1.956  12.577  1.00 25.36  ? 34  PHE B CE2 1 
ATOM   247  C CZ  . PHE A 1 47  ? -22.842 -0.753  12.939  1.00 23.90  ? 34  PHE B CZ  1 
ATOM   248  N N   . VAL A 1 48  ? -28.919 -3.538  16.262  1.00 31.07  ? 35  VAL B N   1 
ATOM   249  C CA  . VAL A 1 48  ? -30.171 -3.517  16.992  1.00 32.96  ? 35  VAL B CA  1 
ATOM   250  C C   . VAL A 1 48  ? -29.819 -3.693  18.468  1.00 32.12  ? 35  VAL B C   1 
ATOM   251  O O   . VAL A 1 48  ? -30.382 -2.996  19.309  1.00 34.11  ? 35  VAL B O   1 
ATOM   252  C CB  . VAL A 1 48  ? -31.275 -4.481  16.494  1.00 33.24  ? 35  VAL B CB  1 
ATOM   253  C CG1 . VAL A 1 48  ? -32.383 -4.728  17.525  1.00 35.76  ? 35  VAL B CG1 1 
ATOM   254  C CG2 . VAL A 1 48  ? -31.889 -4.003  15.166  1.00 31.48  ? 35  VAL B CG2 1 
ATOM   255  N N   . ALA A 1 49  ? -28.924 -4.638  18.751  1.00 31.30  ? 36  ALA B N   1 
ATOM   256  C CA  . ALA A 1 49  ? -28.525 -4.921  20.143  1.00 32.61  ? 36  ALA B CA  1 
ATOM   257  C C   . ALA A 1 49  ? -27.884 -3.702  20.832  1.00 30.39  ? 36  ALA B C   1 
ATOM   258  O O   . ALA A 1 49  ? -28.022 -3.573  22.021  1.00 34.72  ? 36  ALA B O   1 
ATOM   259  C CB  . ALA A 1 49  ? -27.611 -6.139  20.220  1.00 33.24  ? 36  ALA B CB  1 
ATOM   260  N N   . GLN A 1 50  ? -27.228 -2.805  20.112  1.00 29.72  ? 37  GLN B N   1 
ATOM   261  C CA  . GLN A 1 50  ? -26.637 -1.583  20.635  1.00 29.96  ? 37  GLN B CA  1 
ATOM   262  C C   . GLN A 1 50  ? -27.675 -0.461  20.783  1.00 35.18  ? 37  GLN B C   1 
ATOM   263  O O   . GLN A 1 50  ? -27.348 0.665   21.219  1.00 31.88  ? 37  GLN B O   1 
ATOM   264  C CB  . GLN A 1 50  ? -25.475 -1.100  19.731  1.00 26.94  ? 37  GLN B CB  1 
ATOM   265  C CG  . GLN A 1 50  ? -24.274 -2.060  19.623  1.00 25.70  ? 37  GLN B CG  1 
ATOM   266  C CD  . GLN A 1 50  ? -23.474 -2.157  20.925  1.00 26.00  ? 37  GLN B CD  1 
ATOM   267  O OE1 . GLN A 1 50  ? -23.389 -1.198  21.712  1.00 26.34  ? 37  GLN B OE1 1 
ATOM   268  N NE2 . GLN A 1 50  ? -22.985 -3.368  21.197  1.00 25.72  ? 37  GLN B NE2 1 
ATOM   269  N N   . GLY A 1 51  ? -28.939 -0.753  20.389  1.00 34.66  ? 38  GLY B N   1 
ATOM   270  C CA  . GLY A 1 51  ? -29.981 0.260   20.505  1.00 34.39  ? 38  GLY B CA  1 
ATOM   271  C C   . GLY A 1 51  ? -30.077 1.264   19.343  1.00 33.83  ? 38  GLY B C   1 
ATOM   272  O O   . GLY A 1 51  ? -30.739 2.315   19.461  1.00 34.05  ? 38  GLY B O   1 
ATOM   273  N N   . SER A 1 52  ? -29.461 0.932   18.211  1.00 33.22  ? 39  SER B N   1 
ATOM   274  C CA  . SER A 1 52  ? -29.583 1.704   16.970  1.00 34.32  ? 39  SER B CA  1 
ATOM   275  C C   . SER A 1 52  ? -30.975 1.462   16.362  1.00 34.28  ? 39  SER B C   1 
ATOM   276  O O   . SER A 1 52  ? -31.602 0.429   16.618  1.00 35.93  ? 39  SER B O   1 
ATOM   277  C CB  . SER A 1 52  ? -28.561 1.227   15.938  1.00 30.05  ? 39  SER B CB  1 
ATOM   278  O OG  . SER A 1 52  ? -27.278 1.445   16.501  1.00 28.88  ? 39  SER B OG  1 
ATOM   279  N N   . ARG A 1 53  ? -31.343 2.334   15.408  1.00 34.14  ? 40  ARG B N   1 
ATOM   280  C CA  . ARG A 1 53  ? -32.545 2.180   14.581  1.00 38.25  ? 40  ARG B CA  1 
ATOM   281  C C   . ARG A 1 53  ? -32.068 1.678   13.225  1.00 35.53  ? 40  ARG B C   1 
ATOM   282  O O   . ARG A 1 53  ? -31.298 2.387   12.560  1.00 36.32  ? 40  ARG B O   1 
ATOM   283  C CB  . ARG A 1 53  ? -33.283 3.517   14.509  1.00 38.25  ? 40  ARG B CB  1 
ATOM   284  C CG  . ARG A 1 53  ? -34.063 3.791   15.810  1.00 42.44  ? 40  ARG B CG  1 
ATOM   285  C CD  . ARG A 1 53  ? -34.876 5.114   15.870  1.00 48.38  ? 40  ARG B CD  1 
ATOM   286  N NE  . ARG A 1 53  ? -33.930 6.250   15.929  1.00 50.41  ? 40  ARG B NE  1 
ATOM   287  C CZ  . ARG A 1 53  ? -34.021 7.439   15.259  1.00 44.49  ? 40  ARG B CZ  1 
ATOM   288  N NH1 . ARG A 1 53  ? -35.119 7.783   14.579  1.00 45.30  ? 40  ARG B NH1 1 
ATOM   289  N NH2 . ARG A 1 53  ? -33.009 8.306   15.283  1.00 42.60  ? 40  ARG B NH2 1 
ATOM   290  N N   . VAL A 1 54  ? -32.360 0.402   12.927  1.00 35.63  ? 41  VAL B N   1 
ATOM   291  C CA  . VAL A 1 54  ? -31.647 -0.280  11.832  1.00 34.25  ? 41  VAL B CA  1 
ATOM   292  C C   . VAL A 1 54  ? -32.627 -0.573  10.685  1.00 37.64  ? 41  VAL B C   1 
ATOM   293  O O   . VAL A 1 54  ? -33.543 -1.400  10.847  1.00 37.45  ? 41  VAL B O   1 
ATOM   294  C CB  . VAL A 1 54  ? -30.950 -1.582  12.288  1.00 34.22  ? 41  VAL B CB  1 
ATOM   295  C CG1 . VAL A 1 54  ? -30.183 -2.293  11.170  1.00 32.24  ? 41  VAL B CG1 1 
ATOM   296  C CG2 . VAL A 1 54  ? -30.015 -1.336  13.480  1.00 30.95  ? 41  VAL B CG2 1 
ATOM   297  N N   . ALA A 1 55  ? -32.358 0.031   9.514   1.00 35.94  ? 42  ALA B N   1 
ATOM   298  C CA  . ALA A 1 55  ? -33.112 -0.287  8.314   1.00 36.70  ? 42  ALA B CA  1 
ATOM   299  C C   . ALA A 1 55  ? -32.239 -1.209  7.455   1.00 38.60  ? 42  ALA B C   1 
ATOM   300  O O   . ALA A 1 55  ? -31.007 -1.024  7.415   1.00 35.96  ? 42  ALA B O   1 
ATOM   301  C CB  . ALA A 1 55  ? -33.383 1.030   7.623   1.00 36.33  ? 42  ALA B CB  1 
ATOM   302  N N   . PHE A 1 56  ? -32.819 -2.227  6.806   1.00 38.81  ? 43  PHE B N   1 
ATOM   303  C CA  . PHE A 1 56  ? -31.980 -3.026  5.942   1.00 37.62  ? 43  PHE B CA  1 
ATOM   304  C C   . PHE A 1 56  ? -32.716 -3.394  4.652   1.00 41.12  ? 43  PHE B C   1 
ATOM   305  O O   . PHE A 1 56  ? -33.964 -3.485  4.619   1.00 41.46  ? 43  PHE B O   1 
ATOM   306  C CB  . PHE A 1 56  ? -31.446 -4.231  6.705   1.00 36.19  ? 43  PHE B CB  1 
ATOM   307  C CG  . PHE A 1 56  ? -32.548 -5.171  7.198   1.00 37.78  ? 43  PHE B CG  1 
ATOM   308  C CD1 . PHE A 1 56  ? -33.243 -4.892  8.363   1.00 38.02  ? 43  PHE B CD1 1 
ATOM   309  C CD2 . PHE A 1 56  ? -32.790 -6.389  6.565   1.00 40.07  ? 43  PHE B CD2 1 
ATOM   310  C CE1 . PHE A 1 56  ? -34.225 -5.756  8.864   1.00 45.09  ? 43  PHE B CE1 1 
ATOM   311  C CE2 . PHE A 1 56  ? -33.779 -7.266  7.062   1.00 39.73  ? 43  PHE B CE2 1 
ATOM   312  C CZ  . PHE A 1 56  ? -34.482 -6.949  8.220   1.00 43.56  ? 43  PHE B CZ  1 
ATOM   313  N N   . LEU A 1 57  ? -31.939 -3.577  3.569   1.00 38.84  ? 44  LEU B N   1 
ATOM   314  C CA  . LEU A 1 57  ? -32.492 -3.889  2.243   1.00 37.72  ? 44  LEU B CA  1 
ATOM   315  C C   . LEU A 1 57  ? -32.136 -5.321  1.884   1.00 38.66  ? 44  LEU B C   1 
ATOM   316  O O   . LEU A 1 57  ? -31.021 -5.723  2.189   1.00 42.02  ? 44  LEU B O   1 
ATOM   317  C CB  . LEU A 1 57  ? -31.673 -2.922  1.396   1.00 40.52  ? 44  LEU B CB  1 
ATOM   318  C CG  . LEU A 1 57  ? -32.203 -1.486  1.236   1.00 41.48  ? 44  LEU B CG  1 
ATOM   319  C CD1 . LEU A 1 57  ? -33.132 -0.892  2.243   1.00 41.85  ? 44  LEU B CD1 1 
ATOM   320  C CD2 . LEU A 1 57  ? -31.114 -0.486  0.854   1.00 44.77  ? 44  LEU B CD2 1 
ATOM   321  N N   . ASP A 1 58  ? -33.046 -6.070  1.214   1.00 38.83  ? 45  ASP B N   1 
ATOM   322  C CA  . ASP A 1 58  ? -32.687 -7.365  0.660   1.00 42.52  ? 45  ASP B CA  1 
ATOM   323  C C   . ASP A 1 58  ? -33.666 -7.728  -0.460  1.00 46.53  ? 45  ASP B C   1 
ATOM   324  O O   . ASP A 1 58  ? -34.765 -7.202  -0.510  1.00 47.96  ? 45  ASP B O   1 
ATOM   325  C CB  . ASP A 1 58  ? -32.650 -8.480  1.691   1.00 43.86  ? 45  ASP B CB  1 
ATOM   326  C CG  . ASP A 1 58  ? -31.623 -9.590  1.440   1.00 46.56  ? 45  ASP B CG  1 
ATOM   327  O OD1 . ASP A 1 58  ? -31.947 -10.560 0.699   1.00 44.12  ? 45  ASP B OD1 1 
ATOM   328  O OD2 . ASP A 1 58  ? -30.564 -9.550  2.085   1.00 38.21  ? 45  ASP B OD2 1 
ATOM   329  N N   . LEU A 1 59  ? -33.176 -8.548  -1.400  1.00 46.32  ? 46  LEU B N   1 
ATOM   330  C CA  . LEU A 1 59  ? -33.986 -9.118  -2.453  1.00 51.37  ? 46  LEU B CA  1 
ATOM   331  C C   . LEU A 1 59  ? -34.946 -10.149 -1.841  1.00 54.32  ? 46  LEU B C   1 
ATOM   332  O O   . LEU A 1 59  ? -36.055 -10.282 -2.327  1.00 56.05  ? 46  LEU B O   1 
ATOM   333  C CB  . LEU A 1 59  ? -32.959 -9.787  -3.354  1.00 51.58  ? 46  LEU B CB  1 
ATOM   334  C CG  . LEU A 1 59  ? -33.486 -10.516 -4.606  1.00 55.90  ? 46  LEU B CG  1 
ATOM   335  C CD1 . LEU A 1 59  ? -34.329 -9.615  -5.545  1.00 58.52  ? 46  LEU B CD1 1 
ATOM   336  C CD2 . LEU A 1 59  ? -32.304 -11.179 -5.366  1.00 54.74  ? 46  LEU B CD2 1 
ATOM   337  N N   . ASP A 1 60  ? -34.511 -10.902 -0.808  1.00 54.47  ? 47  ASP B N   1 
ATOM   338  C CA  . ASP A 1 60  ? -35.300 -11.995 -0.243  1.00 55.84  ? 47  ASP B CA  1 
ATOM   339  C C   . ASP A 1 60  ? -36.321 -11.437 0.748   1.00 56.03  ? 47  ASP B C   1 
ATOM   340  O O   . ASP A 1 60  ? -35.979 -11.177 1.886   1.00 56.83  ? 47  ASP B O   1 
ATOM   341  C CB  . ASP A 1 60  ? -34.391 -13.000 0.459   1.00 55.11  ? 47  ASP B CB  1 
ATOM   342  C CG  . ASP A 1 60  ? -35.057 -14.325 0.838   1.00 55.07  ? 47  ASP B CG  1 
ATOM   343  O OD1 . ASP A 1 60  ? -36.249 -14.322 1.119   1.00 55.88  ? 47  ASP B OD1 1 
ATOM   344  O OD2 . ASP A 1 60  ? -34.350 -15.357 0.886   1.00 57.33  ? 47  ASP B OD2 1 
ATOM   345  N N   . ALA A 1 61  ? -37.577 -11.269 0.332   1.00 56.63  ? 48  ALA B N   1 
ATOM   346  C CA  . ALA A 1 61  ? -38.608 -10.617 1.142   1.00 60.48  ? 48  ALA B CA  1 
ATOM   347  C C   . ALA A 1 61  ? -39.011 -11.480 2.335   1.00 62.19  ? 48  ALA B C   1 
ATOM   348  O O   . ALA A 1 61  ? -39.298 -10.945 3.399   1.00 60.49  ? 48  ALA B O   1 
ATOM   349  C CB  . ALA A 1 61  ? -39.825 -10.255 0.308   1.00 65.06  ? 48  ALA B CB  1 
ATOM   350  N N   . GLU A 1 62  ? -39.084 -12.807 2.135   1.00 64.08  ? 49  GLU B N   1 
ATOM   351  C CA  . GLU A 1 62  ? -39.473 -13.726 3.200   1.00 65.72  ? 49  GLU B CA  1 
ATOM   352  C C   . GLU A 1 62  ? -38.400 -13.775 4.296   1.00 62.12  ? 49  GLU B C   1 
ATOM   353  O O   . GLU A 1 62  ? -38.682 -13.724 5.485   1.00 60.72  ? 49  GLU B O   1 
ATOM   354  C CB  . GLU A 1 62  ? -39.787 -15.095 2.605   1.00 69.77  ? 49  GLU B CB  1 
ATOM   355  C CG  . GLU A 1 62  ? -41.011 -15.745 3.220   1.00 71.14  ? 49  GLU B CG  1 
ATOM   356  C CD  . GLU A 1 62  ? -41.366 -16.733 2.131   1.00 73.62  ? 49  GLU B CD  1 
ATOM   357  O OE1 . GLU A 1 62  ? -40.392 -17.081 1.471   1.00 76.63  ? 49  GLU B OE1 1 
ATOM   358  O OE2 . GLU A 1 62  ? -42.520 -17.091 1.867   1.00 75.16  ? 49  GLU B OE2 1 
ATOM   359  N N   . ALA A 1 63  ? -37.140 -13.815 3.892   1.00 56.90  ? 50  ALA B N   1 
ATOM   360  C CA  . ALA A 1 63  ? -36.022 -13.763 4.823   1.00 57.76  ? 50  ALA B CA  1 
ATOM   361  C C   . ALA A 1 63  ? -36.003 -12.419 5.552   1.00 54.99  ? 50  ALA B C   1 
ATOM   362  O O   . ALA A 1 63  ? -35.768 -12.371 6.758   1.00 54.86  ? 50  ALA B O   1 
ATOM   363  C CB  . ALA A 1 63  ? -34.717 -14.041 4.099   1.00 52.74  ? 50  ALA B CB  1 
ATOM   364  N N   . GLY A 1 64  ? -36.307 -11.338 4.820   1.00 50.98  ? 51  GLY B N   1 
ATOM   365  C CA  . GLY A 1 64  ? -36.263 -10.014 5.414   1.00 47.06  ? 51  GLY B CA  1 
ATOM   366  C C   . GLY A 1 64  ? -37.325 -9.820  6.480   1.00 48.48  ? 51  GLY B C   1 
ATOM   367  O O   . GLY A 1 64  ? -37.039 -9.327  7.570   1.00 51.24  ? 51  GLY B O   1 
ATOM   368  N N   . GLN A 1 65  ? -38.564 -10.197 6.103   1.00 50.86  ? 52  GLN B N   1 
ATOM   369  C CA  . GLN A 1 65  ? -39.739 -10.130 6.947   1.00 51.07  ? 52  GLN B CA  1 
ATOM   370  C C   . GLN A 1 65  ? -39.491 -11.016 8.180   1.00 50.40  ? 52  GLN B C   1 
ATOM   371  O O   . GLN A 1 65  ? -39.752 -10.618 9.292   1.00 50.58  ? 52  GLN B O   1 
ATOM   372  C CB  . GLN A 1 65  ? -40.925 -10.404 5.993   1.00 51.28  ? 52  GLN B CB  1 
ATOM   373  N N   . GLY A 1 66  ? -38.931 -12.218 7.998   1.00 53.82  ? 53  GLY B N   1 
ATOM   374  C CA  . GLY A 1 66  ? -38.574 -13.112 9.092   1.00 55.84  ? 53  GLY B CA  1 
ATOM   375  C C   . GLY A 1 66  ? -37.611 -12.465 10.093  1.00 55.73  ? 53  GLY B C   1 
ATOM   376  O O   . GLY A 1 66  ? -37.850 -12.519 11.292  1.00 56.19  ? 53  GLY B O   1 
ATOM   377  N N   . LEU A 1 67  ? -36.536 -11.854 9.594   1.00 50.93  ? 54  LEU B N   1 
ATOM   378  C CA  . LEU A 1 67  ? -35.501 -11.245 10.442  1.00 47.35  ? 54  LEU B CA  1 
ATOM   379  C C   . LEU A 1 67  ? -36.087 -10.049 11.189  1.00 45.06  ? 54  LEU B C   1 
ATOM   380  O O   . LEU A 1 67  ? -35.860 -9.905  12.387  1.00 48.45  ? 54  LEU B O   1 
ATOM   381  C CB  . LEU A 1 67  ? -34.260 -10.871 9.618   1.00 45.57  ? 54  LEU B CB  1 
ATOM   382  N N   . ALA A 1 68  ? -36.833 -9.178  10.503  1.00 44.16  ? 55  ALA B N   1 
ATOM   383  C CA  . ALA A 1 68  ? -37.481 -8.075  11.188  1.00 47.78  ? 55  ALA B CA  1 
ATOM   384  C C   . ALA A 1 68  ? -38.515 -8.590  12.219  1.00 51.03  ? 55  ALA B C   1 
ATOM   385  O O   . ALA A 1 68  ? -38.743 -7.941  13.244  1.00 52.01  ? 55  ALA B O   1 
ATOM   386  C CB  . ALA A 1 68  ? -38.165 -7.182  10.195  1.00 46.64  ? 55  ALA B CB  1 
ATOM   387  N N   . HIS A 1 69  ? -39.134 -9.766  11.995  1.00 54.14  ? 56  HIS B N   1 
ATOM   388  C CA  . HIS A 1 69  ? -40.070 -10.270 13.002  1.00 57.19  ? 56  HIS B CA  1 
ATOM   389  C C   . HIS A 1 69  ? -39.297 -10.587 14.278  1.00 53.05  ? 56  HIS B C   1 
ATOM   390  O O   . HIS A 1 69  ? -39.768 -10.300 15.377  1.00 56.16  ? 56  HIS B O   1 
ATOM   391  C CB  . HIS A 1 69  ? -40.966 -11.435 12.497  1.00 58.40  ? 56  HIS B CB  1 
ATOM   392  C CG  . HIS A 1 69  ? -41.823 -12.073 13.572  1.00 67.70  ? 56  HIS B CG  1 
ATOM   393  N ND1 . HIS A 1 69  ? -41.433 -13.168 14.336  1.00 69.43  ? 56  HIS B ND1 1 
ATOM   394  C CD2 . HIS A 1 69  ? -43.034 -11.719 14.074  1.00 69.06  ? 56  HIS B CD2 1 
ATOM   395  C CE1 . HIS A 1 69  ? -42.368 -13.479 15.226  1.00 68.28  ? 56  HIS B CE1 1 
ATOM   396  N NE2 . HIS A 1 69  ? -43.352 -12.614 15.086  1.00 70.99  ? 56  HIS B NE2 1 
ATOM   397  N N   . ALA A 1 70  ? -38.163 -11.271 14.143  1.00 52.19  ? 57  ALA B N   1 
ATOM   398  C CA  . ALA A 1 70  ? -37.331 -11.588 15.297  1.00 51.56  ? 57  ALA B CA  1 
ATOM   399  C C   . ALA A 1 70  ? -36.909 -10.314 16.060  1.00 52.77  ? 57  ALA B C   1 
ATOM   400  O O   . ALA A 1 70  ? -36.999 -10.264 17.295  1.00 51.17  ? 57  ALA B O   1 
ATOM   401  C CB  . ALA A 1 70  ? -36.124 -12.441 14.883  1.00 51.02  ? 57  ALA B CB  1 
ATOM   402  N N   . LEU A 1 71  ? -36.458 -9.264  15.341  1.00 51.25  ? 58  LEU B N   1 
ATOM   403  C CA  . LEU A 1 71  ? -35.740 -8.157  15.974  1.00 47.56  ? 58  LEU B CA  1 
ATOM   404  C C   . LEU A 1 71  ? -36.662 -7.047  16.464  1.00 51.09  ? 58  LEU B C   1 
ATOM   405  O O   . LEU A 1 71  ? -36.227 -6.218  17.256  1.00 46.37  ? 58  LEU B O   1 
ATOM   406  C CB  . LEU A 1 71  ? -34.714 -7.612  14.983  1.00 43.23  ? 58  LEU B CB  1 
ATOM   407  C CG  . LEU A 1 71  ? -33.649 -8.629  14.606  1.00 46.92  ? 58  LEU B CG  1 
ATOM   408  C CD1 . LEU A 1 71  ? -32.791 -7.782  13.715  1.00 46.45  ? 58  LEU B CD1 1 
ATOM   409  C CD2 . LEU A 1 71  ? -32.892 -9.030  15.857  1.00 48.25  ? 58  LEU B CD2 1 
ATOM   410  N N   . GLY A 1 72  ? -37.912 -7.023  15.978  1.00 52.35  ? 59  GLY B N   1 
ATOM   411  C CA  . GLY A 1 72  ? -38.918 -6.072  16.451  1.00 57.49  ? 59  GLY B CA  1 
ATOM   412  C C   . GLY A 1 72  ? -38.764 -4.645  15.903  1.00 53.46  ? 59  GLY B C   1 
ATOM   413  O O   . GLY A 1 72  ? -38.129 -4.430  14.851  1.00 51.28  ? 59  GLY B O   1 
ATOM   414  N N   . ALA A 1 73  ? -39.348 -3.679  16.647  1.00 50.79  ? 60  ALA B N   1 
ATOM   415  C CA  . ALA A 1 73  ? -39.695 -2.352  16.139  1.00 53.32  ? 60  ALA B CA  1 
ATOM   416  C C   . ALA A 1 73  ? -38.495 -1.418  15.878  1.00 51.19  ? 60  ALA B C   1 
ATOM   417  O O   . ALA A 1 73  ? -38.599 -0.410  15.170  1.00 53.23  ? 60  ALA B O   1 
ATOM   418  C CB  . ALA A 1 73  ? -40.746 -1.720  17.023  1.00 54.79  ? 60  ALA B CB  1 
ATOM   419  N N   . ASN A 1 74  ? -37.331 -1.713  16.440  1.00 47.35  ? 61  ASN B N   1 
ATOM   420  C CA  . ASN A 1 74  ? -36.206 -0.875  16.031  1.00 46.03  ? 61  ASN B CA  1 
ATOM   421  C C   . ASN A 1 74  ? -35.545 -1.415  14.775  1.00 45.24  ? 61  ASN B C   1 
ATOM   422  O O   . ASN A 1 74  ? -34.476 -0.877  14.397  1.00 41.29  ? 61  ASN B O   1 
ATOM   423  C CB  . ASN A 1 74  ? -35.125 -0.734  17.093  1.00 43.55  ? 61  ASN B CB  1 
ATOM   424  C CG  . ASN A 1 74  ? -35.551 0.109   18.270  1.00 49.05  ? 61  ASN B CG  1 
ATOM   425  O OD1 . ASN A 1 74  ? -36.435 0.955   18.157  1.00 50.93  ? 61  ASN B OD1 1 
ATOM   426  N ND2 . ASN A 1 74  ? -34.912 -0.094  19.405  1.00 50.14  ? 61  ASN B ND2 1 
ATOM   427  N N   . SER A 1 75  ? -36.134 -2.473  14.173  1.00 44.50  ? 62  SER B N   1 
ATOM   428  C CA  . SER A 1 75  ? -35.667 -2.885  12.844  1.00 43.62  ? 62  SER B CA  1 
ATOM   429  C C   . SER A 1 75  ? -36.690 -2.523  11.766  1.00 45.88  ? 62  SER B C   1 
ATOM   430  O O   . SER A 1 75  ? -37.872 -2.443  12.069  1.00 48.88  ? 62  SER B O   1 
ATOM   431  C CB  . SER A 1 75  ? -35.294 -4.371  12.809  1.00 45.24  ? 62  SER B CB  1 
ATOM   432  O OG  . SER A 1 75  ? -36.435 -5.249  12.804  1.00 48.78  ? 62  SER B OG  1 
ATOM   433  N N   . LEU A 1 76  ? -36.241 -2.296  10.529  1.00 43.06  ? 63  LEU B N   1 
ATOM   434  C CA  . LEU A 1 76  ? -37.152 -1.969  9.441   1.00 47.96  ? 63  LEU B CA  1 
ATOM   435  C C   . LEU A 1 76  ? -36.639 -2.586  8.127   1.00 45.27  ? 63  LEU B C   1 
ATOM   436  O O   . LEU A 1 76  ? -35.552 -2.212  7.675   1.00 43.18  ? 63  LEU B O   1 
ATOM   437  C CB  . LEU A 1 76  ? -37.263 -0.445  9.341   1.00 46.89  ? 63  LEU B CB  1 
ATOM   438  C CG  . LEU A 1 76  ? -38.092 0.037   8.148   1.00 54.05  ? 63  LEU B CG  1 
ATOM   439  C CD1 . LEU A 1 76  ? -39.656 -0.346  8.325   1.00 54.10  ? 63  LEU B CD1 1 
ATOM   440  C CD2 . LEU A 1 76  ? -37.756 1.535   7.945   1.00 53.94  ? 63  LEU B CD2 1 
ATOM   441  N N   . PHE A 1 77  ? -37.414 -3.553  7.573   1.00 46.76  ? 64  PHE B N   1 
ATOM   442  C CA  . PHE A 1 77  ? -37.044 -4.344  6.405   1.00 44.08  ? 64  PHE B CA  1 
ATOM   443  C C   . PHE A 1 77  ? -37.645 -3.709  5.160   1.00 45.47  ? 64  PHE B C   1 
ATOM   444  O O   . PHE A 1 77  ? -38.865 -3.536  5.095   1.00 47.50  ? 64  PHE B O   1 
ATOM   445  C CB  . PHE A 1 77  ? -37.472 -5.825  6.412   1.00 47.71  ? 64  PHE B CB  1 
ATOM   446  C CG  . PHE A 1 77  ? -37.249 -6.526  5.059   1.00 46.84  ? 64  PHE B CG  1 
ATOM   447  C CD1 . PHE A 1 77  ? -36.011 -6.510  4.413   1.00 46.15  ? 64  PHE B CD1 1 
ATOM   448  C CD2 . PHE A 1 77  ? -38.317 -7.108  4.389   1.00 49.56  ? 64  PHE B CD2 1 
ATOM   449  C CE1 . PHE A 1 77  ? -35.866 -7.098  3.148   1.00 43.96  ? 64  PHE B CE1 1 
ATOM   450  C CE2 . PHE A 1 77  ? -38.153 -7.702  3.152   1.00 48.35  ? 64  PHE B CE2 1 
ATOM   451  C CZ  . PHE A 1 77  ? -36.941 -7.725  2.529   1.00 48.06  ? 64  PHE B CZ  1 
ATOM   452  N N   . LEU A 1 78  ? -36.796 -3.356  4.184   1.00 44.53  ? 65  LEU B N   1 
ATOM   453  C CA  . LEU A 1 78  ? -37.288 -2.827  2.905   1.00 50.63  ? 65  LEU B CA  1 
ATOM   454  C C   . LEU A 1 78  ? -36.922 -3.805  1.799   1.00 49.98  ? 65  LEU B C   1 
ATOM   455  O O   . LEU A 1 78  ? -35.743 -4.031  1.575   1.00 46.11  ? 65  LEU B O   1 
ATOM   456  C CB  . LEU A 1 78  ? -36.913 -1.393  2.524   1.00 48.30  ? 65  LEU B CB  1 
ATOM   457  C CG  . LEU A 1 78  ? -37.288 -0.342  3.573   1.00 48.59  ? 65  LEU B CG  1 
ATOM   458  C CD1 . LEU A 1 78  ? -37.030 1.098   3.135   1.00 46.13  ? 65  LEU B CD1 1 
ATOM   459  C CD2 . LEU A 1 78  ? -38.767 -0.494  4.086   1.00 55.15  ? 65  LEU B CD2 1 
ATOM   460  N N   . PRO A 1 79  ? -37.901 -4.369  1.061   1.00 47.28  ? 66  PRO B N   1 
ATOM   461  C CA  . PRO A 1 79  ? -37.600 -5.108  -0.164  1.00 49.26  ? 66  PRO B CA  1 
ATOM   462  C C   . PRO A 1 79  ? -36.889 -4.216  -1.200  1.00 50.05  ? 66  PRO B C   1 
ATOM   463  O O   . PRO A 1 79  ? -37.318 -3.087  -1.453  1.00 52.42  ? 66  PRO B O   1 
ATOM   464  C CB  . PRO A 1 79  ? -38.975 -5.611  -0.644  1.00 50.35  ? 66  PRO B CB  1 
ATOM   465  C CG  . PRO A 1 79  ? -39.975 -4.840  0.139   1.00 52.11  ? 66  PRO B CG  1 
ATOM   466  C CD  . PRO A 1 79  ? -39.355 -4.249  1.345   1.00 50.20  ? 66  PRO B CD  1 
ATOM   467  N N   . CYS A 1 80  ? -35.693 -4.616  -1.666  1.00 46.27  ? 67  CYS B N   1 
ATOM   468  C CA  . CYS A 1 80  ? -35.030 -3.770  -2.642  1.00 49.23  ? 67  CYS B CA  1 
ATOM   469  C C   . CYS A 1 80  ? -34.112 -4.639  -3.490  1.00 46.27  ? 67  CYS B C   1 
ATOM   470  O O   . CYS A 1 80  ? -33.473 -5.549  -2.964  1.00 46.07  ? 67  CYS B O   1 
ATOM   471  C CB  . CYS A 1 80  ? -34.426 -2.538  -1.985  1.00 50.72  ? 67  CYS B CB  1 
ATOM   472  S SG  . CYS A 1 80  ? -33.404 -1.530  -3.080  1.00 51.69  ? 67  CYS B SG  1 
ATOM   473  N N   . ASP A 1 81  ? -34.215 -4.474  -4.815  1.00 49.49  ? 68  ASP B N   1 
ATOM   474  C CA  . ASP A 1 81  ? -33.226 -4.996  -5.757  1.00 47.04  ? 68  ASP B CA  1 
ATOM   475  C C   . ASP A 1 81  ? -32.266 -3.845  -6.023  1.00 44.22  ? 68  ASP B C   1 
ATOM   476  O O   . ASP A 1 81  ? -32.673 -2.789  -6.544  1.00 43.93  ? 68  ASP B O   1 
ATOM   477  C CB  . ASP A 1 81  ? -33.846 -5.585  -7.039  1.00 47.96  ? 68  ASP B CB  1 
ATOM   478  N N   . VAL A 1 82  ? -30.997 -4.038  -5.578  1.00 40.49  ? 69  VAL B N   1 
ATOM   479  C CA  . VAL A 1 82  ? -30.017 -2.955  -5.596  1.00 39.54  ? 69  VAL B CA  1 
ATOM   480  C C   . VAL A 1 82  ? -29.577 -2.600  -7.013  1.00 39.10  ? 69  VAL B C   1 
ATOM   481  O O   . VAL A 1 82  ? -29.050 -1.497  -7.189  1.00 38.02  ? 69  VAL B O   1 
ATOM   482  C CB  . VAL A 1 82  ? -28.854 -3.237  -4.653  1.00 41.00  ? 69  VAL B CB  1 
ATOM   483  C CG1 . VAL A 1 82  ? -29.412 -3.364  -3.227  1.00 43.94  ? 69  VAL B CG1 1 
ATOM   484  C CG2 . VAL A 1 82  ? -28.074 -4.478  -5.084  1.00 43.15  ? 69  VAL B CG2 1 
ATOM   485  N N   . ARG A 1 83  ? -29.946 -3.446  -7.986  1.00 41.52  ? 70  ARG B N   1 
ATOM   486  C CA  . ARG A 1 83  ? -29.746 -3.149  -9.410  1.00 40.89  ? 70  ARG B CA  1 
ATOM   487  C C   . ARG A 1 83  ? -30.682 -2.025  -9.832  1.00 42.99  ? 70  ARG B C   1 
ATOM   488  O O   . ARG A 1 83  ? -30.372 -1.292  -10.777 1.00 44.24  ? 70  ARG B O   1 
ATOM   489  C CB  . ARG A 1 83  ? -29.926 -4.335  -10.350 1.00 42.87  ? 70  ARG B CB  1 
ATOM   490  C CG  . ARG A 1 83  ? -29.127 -5.552  -9.922  1.00 43.50  ? 70  ARG B CG  1 
ATOM   491  C CD  . ARG A 1 83  ? -29.600 -6.849  -10.583 1.00 50.61  ? 70  ARG B CD  1 
ATOM   492  N NE  . ARG A 1 83  ? -28.975 -7.016  -11.904 1.00 62.84  ? 70  ARG B NE  1 
ATOM   493  C CZ  . ARG A 1 83  ? -29.685 -7.309  -13.000 1.00 62.00  ? 70  ARG B CZ  1 
ATOM   494  N NH1 . ARG A 1 83  ? -30.987 -7.477  -12.836 1.00 62.09  ? 70  ARG B NH1 1 
ATOM   495  N NH2 . ARG A 1 83  ? -29.099 -7.426  -14.196 1.00 58.64  ? 70  ARG B NH2 1 
ATOM   496  N N   . ASP A 1 84  ? -31.827 -1.873  -9.117  1.00 41.34  ? 71  ASP B N   1 
ATOM   497  C CA  . ASP A 1 84  ? -32.738 -0.787  -9.418  1.00 45.85  ? 71  ASP B CA  1 
ATOM   498  C C   . ASP A 1 84  ? -32.322 0.426   -8.607  1.00 43.78  ? 71  ASP B C   1 
ATOM   499  O O   . ASP A 1 84  ? -32.736 0.569   -7.449  1.00 42.94  ? 71  ASP B O   1 
ATOM   500  C CB  . ASP A 1 84  ? -34.210 -1.200  -9.283  1.00 49.42  ? 71  ASP B CB  1 
ATOM   501  C CG  . ASP A 1 84  ? -35.318 -0.168  -9.562  1.00 51.68  ? 71  ASP B CG  1 
ATOM   502  O OD1 . ASP A 1 84  ? -35.007 1.037   -9.710  1.00 49.22  ? 71  ASP B OD1 1 
ATOM   503  O OD2 . ASP A 1 84  ? -36.530 -0.565  -9.624  1.00 53.15  ? 71  ASP B OD2 1 
ATOM   504  N N   . ILE A 1 85  ? -31.635 1.354   -9.248  1.00 42.23  ? 72  ILE B N   1 
ATOM   505  C CA  . ILE A 1 85  ? -31.156 2.529   -8.550  1.00 46.18  ? 72  ILE B CA  1 
ATOM   506  C C   . ILE A 1 85  ? -32.290 3.448   -8.114  1.00 47.67  ? 72  ILE B C   1 
ATOM   507  O O   . ILE A 1 85  ? -32.187 4.101   -7.079  1.00 45.83  ? 72  ILE B O   1 
ATOM   508  C CB  . ILE A 1 85  ? -30.068 3.278   -9.327  1.00 46.27  ? 72  ILE B CB  1 
ATOM   509  C CG1 . ILE A 1 85  ? -28.808 2.395   -9.499  1.00 42.66  ? 72  ILE B CG1 1 
ATOM   510  C CG2 . ILE A 1 85  ? -29.759 4.637   -8.676  1.00 43.49  ? 72  ILE B CG2 1 
ATOM   511  C CD1 . ILE A 1 85  ? -28.248 1.854   -8.185  1.00 36.78  ? 72  ILE B CD1 1 
ATOM   512  N N   . GLU A 1 86  ? -33.278 3.634   -8.996  1.00 58.41  ? 73  GLU B N   1 
ATOM   513  C CA  . GLU A 1 86  ? -34.476 4.352   -8.564  1.00 58.64  ? 73  GLU B CA  1 
ATOM   514  C C   . GLU A 1 86  ? -34.922 3.692   -7.219  1.00 47.69  ? 73  GLU B C   1 
ATOM   515  O O   . GLU A 1 86  ? -35.431 4.426   -6.322  1.00 55.32  ? 73  GLU B O   1 
ATOM   516  C CB  . GLU A 1 86  ? -35.315 4.707   -9.830  1.00 60.57  ? 73  GLU B CB  1 
ATOM   517  N N   . ARG A 1 87  ? -35.008 2.320   -7.108  1.00 43.20  ? 74  ARG B N   1 
ATOM   518  C CA  . ARG A 1 87  ? -35.769 1.757   -5.924  1.00 45.67  ? 74  ARG B CA  1 
ATOM   519  C C   . ARG A 1 87  ? -34.827 1.972   -4.741  1.00 57.69  ? 74  ARG B C   1 
ATOM   520  O O   . ARG A 1 87  ? -35.327 2.359   -3.654  1.00 50.29  ? 74  ARG B O   1 
ATOM   521  C CB  . ARG A 1 87  ? -36.432 0.276   -5.962  1.00 36.43  ? 74  ARG B CB  1 
ATOM   522  N N   . LEU A 1 88  ? -33.474 1.809   -4.974  1.00 49.98  ? 75  LEU B N   1 
ATOM   523  C CA  . LEU A 1 88  ? -32.478 2.080   -3.952  1.00 44.30  ? 75  LEU B CA  1 
ATOM   524  C C   . LEU A 1 88  ? -32.677 3.488   -3.421  1.00 42.10  ? 75  LEU B C   1 
ATOM   525  O O   . LEU A 1 88  ? -32.720 3.670   -2.212  1.00 44.93  ? 75  LEU B O   1 
ATOM   526  C CB  . LEU A 1 88  ? -31.078 2.018   -4.547  1.00 36.23  ? 75  LEU B CB  1 
ATOM   527  C CG  . LEU A 1 88  ? -29.955 2.259   -3.531  1.00 33.35  ? 75  LEU B CG  1 
ATOM   528  C CD1 . LEU A 1 88  ? -30.059 1.097   -2.601  1.00 36.39  ? 75  LEU B CD1 1 
ATOM   529  C CD2 . LEU A 1 88  ? -28.634 2.279   -4.263  1.00 33.85  ? 75  LEU B CD2 1 
ATOM   530  N N   . LYS A 1 89  ? -32.810 4.476   -4.318  1.00 42.99  ? 76  LYS B N   1 
ATOM   531  C CA  . LYS A 1 89  ? -32.983 5.813   -3.784  1.00 45.38  ? 76  LYS B CA  1 
ATOM   532  C C   . LYS A 1 89  ? -34.353 5.910   -3.086  1.00 46.58  ? 76  LYS B C   1 
ATOM   533  O O   . LYS A 1 89  ? -34.476 6.630   -2.118  1.00 47.68  ? 76  LYS B O   1 
ATOM   534  C CB  . LYS A 1 89  ? -32.986 6.853   -4.900  1.00 46.43  ? 76  LYS B CB  1 
ATOM   535  C CG  . LYS A 1 89  ? -31.618 7.167   -5.403  1.00 52.45  ? 76  LYS B CG  1 
ATOM   536  C CD  . LYS A 1 89  ? -31.609 8.444   -6.232  1.00 56.79  ? 76  LYS B CD  1 
ATOM   537  C CE  . LYS A 1 89  ? -31.245 8.158   -7.653  1.00 63.26  ? 76  LYS B CE  1 
ATOM   538  N NZ  . LYS A 1 89  ? -31.707 9.318   -8.421  1.00 75.74  ? 76  LYS B NZ  1 
ATOM   539  N N   . ALA A 1 90  ? -35.353 5.152   -3.545  1.00 45.66  ? 77  ALA B N   1 
ATOM   540  C CA  . ALA A 1 90  ? -36.663 5.290   -2.909  1.00 52.32  ? 77  ALA B CA  1 
ATOM   541  C C   . ALA A 1 90  ? -36.544 4.728   -1.506  1.00 50.49  ? 77  ALA B C   1 
ATOM   542  O O   . ALA A 1 90  ? -37.187 5.293   -0.622  1.00 49.21  ? 77  ALA B O   1 
ATOM   543  C CB  . ALA A 1 90  ? -37.841 4.646   -3.662  1.00 52.88  ? 77  ALA B CB  1 
ATOM   544  N N   . CYS A 1 91  ? -35.771 3.613   -1.345  1.00 45.31  ? 78  CYS B N   1 
ATOM   545  C CA  . CYS A 1 91  ? -35.608 2.966   -0.055  1.00 49.75  ? 78  CYS B CA  1 
ATOM   546  C C   . CYS A 1 91  ? -34.961 3.940   0.944   1.00 50.27  ? 78  CYS B C   1 
ATOM   547  O O   . CYS A 1 91  ? -35.370 4.027   2.118   1.00 49.99  ? 78  CYS B O   1 
ATOM   548  C CB  . CYS A 1 91  ? -34.841 1.647   -0.171  1.00 48.35  ? 78  CYS B CB  1 
ATOM   549  S SG  . CYS A 1 91  ? -35.893 0.259   -0.729  1.00 50.01  ? 78  CYS B SG  1 
ATOM   550  N N   . VAL A 1 92  ? -33.959 4.686   0.473   1.00 47.98  ? 79  VAL B N   1 
ATOM   551  C CA  . VAL A 1 92  ? -33.220 5.646   1.301   1.00 45.41  ? 79  VAL B CA  1 
ATOM   552  C C   . VAL A 1 92  ? -34.145 6.791   1.722   1.00 49.64  ? 79  VAL B C   1 
ATOM   553  O O   . VAL A 1 92  ? -34.170 7.196   2.893   1.00 44.08  ? 79  VAL B O   1 
ATOM   554  C CB  . VAL A 1 92  ? -31.903 6.138   0.643   1.00 46.13  ? 79  VAL B CB  1 
ATOM   555  C CG1 . VAL A 1 92  ? -31.201 7.231   1.436   1.00 44.57  ? 79  VAL B CG1 1 
ATOM   556  C CG2 . VAL A 1 92  ? -30.930 4.992   0.377   1.00 39.03  ? 79  VAL B CG2 1 
ATOM   557  N N   . ALA A 1 93  ? -34.912 7.323   0.769   1.00 45.46  ? 80  ALA B N   1 
ATOM   558  C CA  . ALA A 1 93  ? -35.835 8.438   1.038   1.00 48.41  ? 80  ALA B CA  1 
ATOM   559  C C   . ALA A 1 93  ? -36.869 8.041   2.096   1.00 47.40  ? 80  ALA B C   1 
ATOM   560  O O   . ALA A 1 93  ? -37.249 8.829   2.961   1.00 47.57  ? 80  ALA B O   1 
ATOM   561  C CB  . ALA A 1 93  ? -36.529 8.856   -0.283  1.00 49.14  ? 80  ALA B CB  1 
ATOM   562  N N   . GLU A 1 94  ? -37.276 6.762   2.069   1.00 48.31  ? 81  GLU B N   1 
ATOM   563  C CA  . GLU A 1 94  ? -38.289 6.299   3.003   1.00 50.49  ? 81  GLU B CA  1 
ATOM   564  C C   . GLU A 1 94  ? -37.736 6.188   4.430   1.00 48.29  ? 81  GLU B C   1 
ATOM   565  O O   . GLU A 1 94  ? -38.427 6.502   5.424   1.00 47.53  ? 81  GLU B O   1 
ATOM   566  C CB  . GLU A 1 94  ? -38.943 4.966   2.656   1.00 58.70  ? 81  GLU B CB  1 
ATOM   567  C CG  . GLU A 1 94  ? -40.284 4.824   3.381   1.00 67.10  ? 81  GLU B CG  1 
ATOM   568  C CD  . GLU A 1 94  ? -40.745 3.387   3.550   1.00 75.67  ? 81  GLU B CD  1 
ATOM   569  O OE1 . GLU A 1 94  ? -40.324 2.521   2.732   1.00 73.49  ? 81  GLU B OE1 1 
ATOM   570  O OE2 . GLU A 1 94  ? -41.518 3.144   4.518   1.00 86.74  ? 81  GLU B OE2 1 
ATOM   571  N N   . VAL A 1 95  ? -36.501 5.689   4.517   1.00 44.96  ? 82  VAL B N   1 
ATOM   572  C CA  . VAL A 1 95  ? -35.845 5.650   5.809   1.00 44.49  ? 82  VAL B CA  1 
ATOM   573  C C   . VAL A 1 95  ? -35.772 7.095   6.340   1.00 45.42  ? 82  VAL B C   1 
ATOM   574  O O   . VAL A 1 95  ? -36.011 7.361   7.524   1.00 44.01  ? 82  VAL B O   1 
ATOM   575  C CB  . VAL A 1 95  ? -34.468 4.966   5.725   1.00 41.55  ? 82  VAL B CB  1 
ATOM   576  C CG1 . VAL A 1 95  ? -33.828 4.931   7.108   1.00 39.11  ? 82  VAL B CG1 1 
ATOM   577  C CG2 . VAL A 1 95  ? -34.586 3.549   5.148   1.00 41.36  ? 82  VAL B CG2 1 
ATOM   578  N N   . GLU A 1 96  ? -35.357 8.029   5.472   1.00 42.86  ? 83  GLU B N   1 
ATOM   579  C CA  . GLU A 1 96  ? -35.123 9.407   5.916   1.00 43.02  ? 83  GLU B CA  1 
ATOM   580  C C   . GLU A 1 96  ? -36.386 10.013  6.414   1.00 53.02  ? 83  GLU B C   1 
ATOM   581  O O   . GLU A 1 96  ? -36.344 10.737  7.407   1.00 52.45  ? 83  GLU B O   1 
ATOM   582  C CB  . GLU A 1 96  ? -34.401 10.260  4.859   1.00 47.17  ? 83  GLU B CB  1 
ATOM   583  N N   . ARG A 1 97  ? -37.529 9.723   5.713   1.00 51.23  ? 84  ARG B N   1 
ATOM   584  C CA  . ARG A 1 97  ? -38.786 10.332  6.115   1.00 52.97  ? 84  ARG B CA  1 
ATOM   585  C C   . ARG A 1 97  ? -39.240 9.699   7.438   1.00 51.19  ? 84  ARG B C   1 
ATOM   586  O O   . ARG A 1 97  ? -39.798 10.390  8.284   1.00 56.09  ? 84  ARG B O   1 
ATOM   587  C CB  . ARG A 1 97  ? -39.736 10.197  4.918   1.00 51.76  ? 84  ARG B CB  1 
ATOM   588  N N   . THR A 1 98  ? -39.003 8.395   7.629   1.00 51.97  ? 85  THR B N   1 
ATOM   589  C CA  . THR A 1 98  ? -39.382 7.739   8.878   1.00 52.62  ? 85  THR B CA  1 
ATOM   590  C C   . THR A 1 98  ? -38.520 8.202   10.063  1.00 52.32  ? 85  THR B C   1 
ATOM   591  O O   . THR A 1 98  ? -39.084 8.522   11.111  1.00 52.92  ? 85  THR B O   1 
ATOM   592  C CB  . THR A 1 98  ? -39.363 6.216   8.724   1.00 55.64  ? 85  THR B CB  1 
ATOM   593  O OG1 . THR A 1 98  ? -40.186 5.872   7.617   1.00 55.00  ? 85  THR B OG1 1 
ATOM   594  C CG2 . THR A 1 98  ? -40.005 5.503   9.898   1.00 55.66  ? 85  THR B CG2 1 
ATOM   595  N N   . TRP A 1 99  ? -37.177 8.269   9.917   1.00 49.36  ? 86  TRP B N   1 
ATOM   596  C CA  . TRP A 1 99  ? -36.264 8.300   11.073  1.00 49.06  ? 86  TRP B CA  1 
ATOM   597  C C   . TRP A 1 99  ? -35.298 9.497   11.068  1.00 49.62  ? 86  TRP B C   1 
ATOM   598  O O   . TRP A 1 99  ? -34.539 9.642   12.029  1.00 48.40  ? 86  TRP B O   1 
ATOM   599  C CB  . TRP A 1 99  ? -35.474 6.977   11.223  1.00 43.89  ? 86  TRP B CB  1 
ATOM   600  C CG  . TRP A 1 99  ? -36.237 5.824   11.835  1.00 44.47  ? 86  TRP B CG  1 
ATOM   601  C CD1 . TRP A 1 99  ? -37.350 5.884   12.644  1.00 45.33  ? 86  TRP B CD1 1 
ATOM   602  C CD2 . TRP A 1 99  ? -35.872 4.429   11.764  1.00 41.43  ? 86  TRP B CD2 1 
ATOM   603  N NE1 . TRP A 1 99  ? -37.731 4.622   13.019  1.00 44.03  ? 86  TRP B NE1 1 
ATOM   604  C CE2 . TRP A 1 99  ? -36.832 3.712   12.515  1.00 44.15  ? 86  TRP B CE2 1 
ATOM   605  C CE3 . TRP A 1 99  ? -34.878 3.729   11.072  1.00 40.02  ? 86  TRP B CE3 1 
ATOM   606  C CZ2 . TRP A 1 99  ? -36.801 2.319   12.633  1.00 44.93  ? 86  TRP B CZ2 1 
ATOM   607  C CZ3 . TRP A 1 99  ? -34.847 2.352   11.186  1.00 41.93  ? 86  TRP B CZ3 1 
ATOM   608  C CH2 . TRP A 1 99  ? -35.783 1.656   11.982  1.00 42.45  ? 86  TRP B CH2 1 
ATOM   609  N N   . GLY A 1 100 ? -35.279 10.337  10.010  1.00 45.46  ? 87  GLY B N   1 
ATOM   610  C CA  . GLY A 1 100 ? -34.243 11.374  9.903   1.00 42.27  ? 87  GLY B CA  1 
ATOM   611  C C   . GLY A 1 100 ? -32.998 10.888  9.119   1.00 42.20  ? 87  GLY B C   1 
ATOM   612  O O   . GLY A 1 100 ? -32.970 9.730   8.676   1.00 41.58  ? 87  GLY B O   1 
ATOM   613  N N   . ALA A 1 101 ? -32.007 11.780  8.889   1.00 39.24  ? 88  ALA B N   1 
ATOM   614  C CA  . ALA A 1 101 ? -30.816 11.453  8.098   1.00 43.35  ? 88  ALA B CA  1 
ATOM   615  C C   . ALA A 1 101 ? -30.146 10.147  8.571   1.00 43.47  ? 88  ALA B C   1 
ATOM   616  O O   . ALA A 1 101 ? -30.039 9.900   9.769   1.00 37.70  ? 88  ALA B O   1 
ATOM   617  C CB  . ALA A 1 101 ? -29.830 12.620  8.092   1.00 45.94  ? 88  ALA B CB  1 
ATOM   618  N N   . VAL A 1 102 ? -29.669 9.297   7.635   1.00 36.22  ? 89  VAL B N   1 
ATOM   619  C CA  . VAL A 1 102 ? -28.869 8.134   8.007   1.00 34.84  ? 89  VAL B CA  1 
ATOM   620  C C   . VAL A 1 102 ? -27.585 8.583   8.720   1.00 35.26  ? 89  VAL B C   1 
ATOM   621  O O   . VAL A 1 102 ? -26.959 9.588   8.333   1.00 33.15  ? 89  VAL B O   1 
ATOM   622  C CB  . VAL A 1 102 ? -28.555 7.355   6.729   1.00 34.42  ? 89  VAL B CB  1 
ATOM   623  C CG1 . VAL A 1 102 ? -27.712 6.100   7.006   1.00 34.28  ? 89  VAL B CG1 1 
ATOM   624  C CG2 . VAL A 1 102 ? -29.859 6.938   6.114   1.00 33.68  ? 89  VAL B CG2 1 
ATOM   625  N N   . ASP A 1 103 ? -27.258 7.900   9.852   1.00 31.57  ? 90  ASP B N   1 
ATOM   626  C CA  . ASP A 1 103 ? -25.995 8.148   10.531  1.00 29.20  ? 90  ASP B CA  1 
ATOM   627  C C   . ASP A 1 103 ? -24.910 7.240   9.972   1.00 26.42  ? 90  ASP B C   1 
ATOM   628  O O   . ASP A 1 103 ? -23.744 7.640   9.962   1.00 30.84  ? 90  ASP B O   1 
ATOM   629  C CB  . ASP A 1 103 ? -26.203 7.853   12.011  1.00 27.94  ? 90  ASP B CB  1 
ATOM   630  C CG  . ASP A 1 103 ? -27.103 8.846   12.723  1.00 31.37  ? 90  ASP B CG  1 
ATOM   631  O OD1 . ASP A 1 103 ? -26.604 9.978   12.821  1.00 31.72  ? 90  ASP B OD1 1 
ATOM   632  O OD2 . ASP A 1 103 ? -28.261 8.461   13.184  1.00 29.80  ? 90  ASP B OD2 1 
ATOM   633  N N   . VAL A 1 104 ? -25.302 5.994   9.649   1.00 27.36  ? 91  VAL B N   1 
ATOM   634  C CA  . VAL A 1 104 ? -24.357 4.957   9.314   1.00 28.45  ? 91  VAL B CA  1 
ATOM   635  C C   . VAL A 1 104 ? -24.844 4.193   8.082   1.00 27.91  ? 91  VAL B C   1 
ATOM   636  O O   . VAL A 1 104 ? -25.912 3.581   8.156   1.00 31.06  ? 91  VAL B O   1 
ATOM   637  C CB  . VAL A 1 104 ? -24.092 3.955   10.449  1.00 27.62  ? 91  VAL B CB  1 
ATOM   638  C CG1 . VAL A 1 104 ? -23.120 2.864   9.997   1.00 24.45  ? 91  VAL B CG1 1 
ATOM   639  C CG2 . VAL A 1 104 ? -23.633 4.641   11.735  1.00 25.07  ? 91  VAL B CG2 1 
ATOM   640  N N   . LEU A 1 105 ? -24.052 4.204   6.990   1.00 25.02  ? 92  LEU B N   1 
ATOM   641  C CA  . LEU A 1 105 ? -24.423 3.358   5.838   1.00 24.18  ? 92  LEU B CA  1 
ATOM   642  C C   . LEU A 1 105 ? -23.435 2.206   5.719   1.00 23.13  ? 92  LEU B C   1 
ATOM   643  O O   . LEU A 1 105 ? -22.235 2.426   5.713   1.00 23.96  ? 92  LEU B O   1 
ATOM   644  C CB  . LEU A 1 105 ? -24.474 4.156   4.537   1.00 26.08  ? 92  LEU B CB  1 
ATOM   645  C CG  . LEU A 1 105 ? -24.547 3.390   3.207   1.00 28.88  ? 92  LEU B CG  1 
ATOM   646  C CD1 . LEU A 1 105 ? -25.930 2.724   3.072   1.00 29.01  ? 92  LEU B CD1 1 
ATOM   647  C CD2 . LEU A 1 105 ? -24.301 4.359   2.025   1.00 27.76  ? 92  LEU B CD2 1 
ATOM   648  N N   . ILE A 1 106 ? -23.931 0.991   5.552   1.00 24.36  ? 93  ILE B N   1 
ATOM   649  C CA  . ILE A 1 106 ? -23.055 -0.119  5.276   1.00 24.17  ? 93  ILE B CA  1 
ATOM   650  C C   . ILE A 1 106 ? -23.415 -0.692  3.903   1.00 25.20  ? 93  ILE B C   1 
ATOM   651  O O   . ILE A 1 106 ? -24.422 -1.363  3.750   1.00 27.72  ? 93  ILE B O   1 
ATOM   652  C CB  . ILE A 1 106 ? -23.140 -1.214  6.346   1.00 25.83  ? 93  ILE B CB  1 
ATOM   653  C CG1 . ILE A 1 106 ? -22.988 -0.631  7.755   1.00 26.56  ? 93  ILE B CG1 1 
ATOM   654  C CG2 . ILE A 1 106 ? -22.144 -2.334  5.998   1.00 24.40  ? 93  ILE B CG2 1 
ATOM   655  C CD1 . ILE A 1 106 ? -22.921 -1.643  8.904   1.00 27.89  ? 93  ILE B CD1 1 
ATOM   656  N N   . ASN A 1 107 ? -22.491 -0.527  2.937   1.00 20.99  ? 94  ASN B N   1 
ATOM   657  C CA  . ASN A 1 107 ? -22.687 -1.065  1.614   1.00 24.34  ? 94  ASN B CA  1 
ATOM   658  C C   . ASN A 1 107 ? -22.191 -2.507  1.582   1.00 23.56  ? 94  ASN B C   1 
ATOM   659  O O   . ASN A 1 107 ? -21.007 -2.718  1.528   1.00 21.67  ? 94  ASN B O   1 
ATOM   660  C CB  . ASN A 1 107 ? -21.899 -0.198  0.628   1.00 23.43  ? 94  ASN B CB  1 
ATOM   661  C CG  . ASN A 1 107 ? -22.515 1.168   0.391   1.00 26.60  ? 94  ASN B CG  1 
ATOM   662  O OD1 . ASN A 1 107 ? -23.741 1.264   0.298   1.00 26.89  ? 94  ASN B OD1 1 
ATOM   663  N ND2 . ASN A 1 107 ? -21.713 2.236   0.260   1.00 23.55  ? 94  ASN B ND2 1 
ATOM   664  N N   . ASN A 1 108 ? -23.100 -3.454  1.749   1.00 24.46  ? 95  ASN B N   1 
ATOM   665  C CA  . ASN A 1 108 ? -22.793 -4.865  1.942   1.00 27.33  ? 95  ASN B CA  1 
ATOM   666  C C   . ASN A 1 108 ? -23.306 -5.792  0.825   1.00 29.05  ? 95  ASN B C   1 
ATOM   667  O O   . ASN A 1 108 ? -22.742 -6.874  0.624   1.00 28.57  ? 95  ASN B O   1 
ATOM   668  C CB  . ASN A 1 108 ? -23.333 -5.286  3.304   1.00 26.00  ? 95  ASN B CB  1 
ATOM   669  C CG  . ASN A 1 108 ? -23.192 -6.767  3.569   1.00 28.48  ? 95  ASN B CG  1 
ATOM   670  O OD1 . ASN A 1 108 ? -22.089 -7.277  3.822   1.00 27.12  ? 95  ASN B OD1 1 
ATOM   671  N ND2 . ASN A 1 108 ? -24.293 -7.495  3.517   1.00 26.28  ? 95  ASN B ND2 1 
ATOM   672  N N   . ALA A 1 109 ? -24.348 -5.393  0.059   1.00 29.22  ? 96  ALA B N   1 
ATOM   673  C CA  . ALA A 1 109 ? -24.934 -6.308  -0.939  1.00 29.96  ? 96  ALA B CA  1 
ATOM   674  C C   . ALA A 1 109 ? -23.879 -6.623  -1.998  1.00 28.12  ? 96  ALA B C   1 
ATOM   675  O O   . ALA A 1 109 ? -23.232 -5.717  -2.471  1.00 28.85  ? 96  ALA B O   1 
ATOM   676  C CB  . ALA A 1 109 ? -26.145 -5.663  -1.513  1.00 26.87  ? 96  ALA B CB  1 
ATOM   677  N N   . ALA A 1 110 ? -23.733 -7.885  -2.381  1.00 28.71  ? 97  ALA B N   1 
ATOM   678  C CA  . ALA A 1 110 ? -22.824 -8.314  -3.418  1.00 32.86  ? 97  ALA B CA  1 
ATOM   679  C C   . ALA A 1 110 ? -23.222 -9.723  -3.817  1.00 35.56  ? 97  ALA B C   1 
ATOM   680  O O   . ALA A 1 110 ? -24.093 -10.299 -3.195  1.00 34.19  ? 97  ALA B O   1 
ATOM   681  C CB  . ALA A 1 110 ? -21.407 -8.308  -2.785  1.00 29.95  ? 97  ALA B CB  1 
ATOM   682  N N   . ARG A 1 111 ? -22.685 -10.225 -4.931  1.00 35.85  ? 98  ARG B N   1 
ATOM   683  C CA  . ARG A 1 111 ? -22.900 -11.594 -5.361  1.00 38.15  ? 98  ARG B CA  1 
ATOM   684  C C   . ARG A 1 111 ? -21.544 -12.180 -5.755  1.00 39.87  ? 98  ARG B C   1 
ATOM   685  O O   . ARG A 1 111 ? -20.825 -11.622 -6.611  1.00 35.41  ? 98  ARG B O   1 
ATOM   686  C CB  . ARG A 1 111 ? -23.797 -11.429 -6.587  1.00 44.43  ? 98  ARG B CB  1 
ATOM   687  C CG  . ARG A 1 111 ? -24.519 -12.729 -6.793  1.00 56.29  ? 98  ARG B CG  1 
ATOM   688  C CD  . ARG A 1 111 ? -25.830 -12.399 -7.432  1.00 60.24  ? 98  ARG B CD  1 
ATOM   689  N NE  . ARG A 1 111 ? -26.235 -13.782 -7.701  1.00 63.01  ? 98  ARG B NE  1 
ATOM   690  C CZ  . ARG A 1 111 ? -26.779 -14.154 -8.839  1.00 57.39  ? 98  ARG B CZ  1 
ATOM   691  N NH1 . ARG A 1 111 ? -27.170 -13.197 -9.676  1.00 55.81  ? 98  ARG B NH1 1 
ATOM   692  N NH2 . ARG A 1 111 ? -26.907 -15.445 -9.124  1.00 49.63  ? 98  ARG B NH2 1 
ATOM   693  N N   . ASP A 1 112 ? -21.175 -13.296 -5.108  1.00 40.57  ? 99  ASP B N   1 
ATOM   694  C CA  . ASP A 1 112 ? -19.810 -13.782 -5.185  1.00 41.53  ? 99  ASP B CA  1 
ATOM   695  C C   . ASP A 1 112 ? -19.722 -15.093 -5.957  1.00 46.21  ? 99  ASP B C   1 
ATOM   696  O O   . ASP A 1 112 ? -18.802 -15.887 -5.704  1.00 48.13  ? 99  ASP B O   1 
ATOM   697  C CB  . ASP A 1 112 ? -19.184 -13.891 -3.792  1.00 48.59  ? 99  ASP B CB  1 
ATOM   698  C CG  . ASP A 1 112 ? -19.940 -14.814 -2.854  1.00 51.06  ? 99  ASP B CG  1 
ATOM   699  O OD1 . ASP A 1 112 ? -20.974 -15.400 -3.310  1.00 53.38  ? 99  ASP B OD1 1 
ATOM   700  O OD2 . ASP A 1 112 ? -19.494 -14.906 -1.669  1.00 58.75  ? 99  ASP B OD2 1 
ATOM   701  N N   . ASP A 1 113 ? -20.601 -15.288 -6.961  1.00 39.98  ? 100 ASP B N   1 
ATOM   702  C CA  . ASP A 1 113 ? -20.568 -16.544 -7.690  1.00 43.24  ? 100 ASP B CA  1 
ATOM   703  C C   . ASP A 1 113 ? -19.252 -16.628 -8.488  1.00 41.84  ? 100 ASP B C   1 
ATOM   704  O O   . ASP A 1 113 ? -18.718 -15.581 -8.877  1.00 41.81  ? 100 ASP B O   1 
ATOM   705  C CB  . ASP A 1 113 ? -21.885 -16.747 -8.455  1.00 51.70  ? 100 ASP B CB  1 
ATOM   706  C CG  . ASP A 1 113 ? -22.312 -15.636 -9.421  1.00 46.85  ? 100 ASP B CG  1 
ATOM   707  O OD1 . ASP A 1 113 ? -22.314 -14.435 -9.050  1.00 49.29  ? 100 ASP B OD1 1 
ATOM   708  O OD2 . ASP A 1 113 ? -22.600 -15.970 -10.569 1.00 46.46  ? 100 ASP B OD2 1 
ATOM   709  N N   . ARG A 1 114 ? -18.731 -17.853 -8.692  1.00 40.41  ? 101 ARG B N   1 
ATOM   710  C CA  . ARG A 1 114 ? -17.481 -18.117 -9.420  1.00 39.25  ? 101 ARG B CA  1 
ATOM   711  C C   . ARG A 1 114 ? -17.758 -18.064 -10.920 1.00 40.71  ? 101 ARG B C   1 
ATOM   712  O O   . ARG A 1 114 ? -18.880 -18.252 -11.309 1.00 40.72  ? 101 ARG B O   1 
ATOM   713  C CB  . ARG A 1 114 ? -16.984 -19.550 -9.187  1.00 42.19  ? 101 ARG B CB  1 
ATOM   714  N N   . HIS A 1 115 ? -16.768 -17.694 -11.745 1.00 37.04  ? 102 HIS B N   1 
ATOM   715  C CA  . HIS A 1 115 ? -16.945 -17.601 -13.187 1.00 40.29  ? 102 HIS B CA  1 
ATOM   716  C C   . HIS A 1 115 ? -15.541 -17.436 -13.768 1.00 37.53  ? 102 HIS B C   1 
ATOM   717  O O   . HIS A 1 115 ? -14.834 -16.485 -13.426 1.00 37.62  ? 102 HIS B O   1 
ATOM   718  C CB  . HIS A 1 115 ? -17.867 -16.418 -13.539 1.00 38.93  ? 102 HIS B CB  1 
ATOM   719  C CG  . HIS A 1 115 ? -17.576 -15.124 -12.781 1.00 39.39  ? 102 HIS B CG  1 
ATOM   720  N ND1 . HIS A 1 115 ? -18.115 -14.646 -11.573 1.00 37.65  ? 102 HIS B ND1 1 
ATOM   721  C CD2 . HIS A 1 115 ? -16.680 -14.179 -13.194 1.00 37.16  ? 102 HIS B CD2 1 
ATOM   722  C CE1 . HIS A 1 115 ? -17.587 -13.449 -11.291 1.00 37.60  ? 102 HIS B CE1 1 
ATOM   723  N NE2 . HIS A 1 115 ? -16.714 -13.168 -12.320 1.00 33.18  ? 102 HIS B NE2 1 
ATOM   724  N N   . ALA A 1 116 ? -15.130 -18.411 -14.572 1.00 40.49  ? 103 ALA B N   1 
ATOM   725  C CA  . ALA A 1 116 ? -13.963 -18.404 -15.429 1.00 38.08  ? 103 ALA B CA  1 
ATOM   726  C C   . ALA A 1 116 ? -13.933 -17.180 -16.362 1.00 37.73  ? 103 ALA B C   1 
ATOM   727  O O   . ALA A 1 116 ? -14.913 -16.748 -16.958 1.00 36.88  ? 103 ALA B O   1 
ATOM   728  C CB  . ALA A 1 116 ? -13.932 -19.728 -16.185 1.00 36.44  ? 103 ALA B CB  1 
ATOM   729  N N   . LEU A 1 117 ? -12.742 -16.575 -16.497 1.00 38.91  ? 104 LEU B N   1 
ATOM   730  C CA  . LEU A 1 117 ? -12.574 -15.416 -17.360 1.00 38.32  ? 104 LEU B CA  1 
ATOM   731  C C   . LEU A 1 117 ? -13.123 -15.637 -18.783 1.00 37.39  ? 104 LEU B C   1 
ATOM   732  O O   . LEU A 1 117 ? -13.703 -14.720 -19.372 1.00 35.76  ? 104 LEU B O   1 
ATOM   733  C CB  . LEU A 1 117 ? -11.062 -15.217 -17.302 1.00 42.09  ? 104 LEU B CB  1 
ATOM   734  C CG  . LEU A 1 117 ? -10.407 -14.238 -18.278 1.00 49.72  ? 104 LEU B CG  1 
ATOM   735  C CD1 . LEU A 1 117 ? -9.036  -14.047 -17.649 1.00 50.30  ? 104 LEU B CD1 1 
ATOM   736  C CD2 . LEU A 1 117 ? -10.200 -14.830 -19.610 1.00 44.32  ? 104 LEU B CD2 1 
ATOM   737  N N   . ALA A 1 118 ? -12.930 -16.836 -19.352 1.00 40.21  ? 105 ALA B N   1 
ATOM   738  C CA  . ALA A 1 118 ? -13.248 -17.043 -20.759 1.00 40.81  ? 105 ALA B CA  1 
ATOM   739  C C   . ALA A 1 118 ? -14.763 -17.141 -20.912 1.00 41.93  ? 105 ALA B C   1 
ATOM   740  O O   . ALA A 1 118 ? -15.278 -16.900 -21.972 1.00 42.70  ? 105 ALA B O   1 
ATOM   741  C CB  . ALA A 1 118 ? -12.549 -18.270 -21.320 1.00 44.25  ? 105 ALA B CB  1 
ATOM   742  N N   . ASP A 1 119 ? -15.489 -17.365 -19.816 1.00 41.90  ? 106 ASP B N   1 
ATOM   743  C CA  . ASP A 1 119 ? -16.931 -17.562 -19.822 1.00 48.31  ? 106 ASP B CA  1 
ATOM   744  C C   . ASP A 1 119 ? -17.744 -16.273 -19.735 1.00 47.37  ? 106 ASP B C   1 
ATOM   745  O O   . ASP A 1 119 ? -18.910 -16.297 -20.098 1.00 52.49  ? 106 ASP B O   1 
ATOM   746  C CB  . ASP A 1 119 ? -17.336 -18.471 -18.675 1.00 51.69  ? 106 ASP B CB  1 
ATOM   747  C CG  . ASP A 1 119 ? -16.821 -19.886 -18.851 1.00 55.09  ? 106 ASP B CG  1 
ATOM   748  O OD1 . ASP A 1 119 ? -16.499 -20.244 -20.010 1.00 53.16  ? 106 ASP B OD1 1 
ATOM   749  O OD2 . ASP A 1 119 ? -16.665 -20.570 -17.826 1.00 56.70  ? 106 ASP B OD2 1 
ATOM   750  N N   . VAL A 1 120 ? -17.151 -15.155 -19.354 1.00 38.50  ? 107 VAL B N   1 
ATOM   751  C CA  . VAL A 1 120 ? -17.855 -13.926 -19.036 1.00 37.24  ? 107 VAL B CA  1 
ATOM   752  C C   . VAL A 1 120 ? -18.317 -13.217 -20.311 1.00 38.94  ? 107 VAL B C   1 
ATOM   753  O O   . VAL A 1 120 ? -17.512 -12.861 -21.167 1.00 41.43  ? 107 VAL B O   1 
ATOM   754  C CB  . VAL A 1 120 ? -16.860 -13.036 -18.236 1.00 34.06  ? 107 VAL B CB  1 
ATOM   755  C CG1 . VAL A 1 120 ? -17.434 -11.634 -18.063 1.00 32.67  ? 107 VAL B CG1 1 
ATOM   756  C CG2 . VAL A 1 120 ? -16.490 -13.619 -16.863 1.00 32.97  ? 107 VAL B CG2 1 
ATOM   757  N N   . SER A 1 121 ? -19.624 -12.951 -20.401 1.00 38.64  ? 108 SER B N   1 
ATOM   758  C CA  . SER A 1 121 ? -20.247 -12.224 -21.495 1.00 37.01  ? 108 SER B CA  1 
ATOM   759  C C   . SER A 1 121 ? -20.383 -10.775 -21.007 1.00 34.69  ? 108 SER B C   1 
ATOM   760  O O   . SER A 1 121 ? -20.244 -10.497 -19.798 1.00 32.54  ? 108 SER B O   1 
ATOM   761  C CB  . SER A 1 121 ? -21.612 -12.830 -21.773 1.00 39.18  ? 108 SER B CB  1 
ATOM   762  O OG  . SER A 1 121 ? -22.455 -12.562 -20.677 1.00 39.31  ? 108 SER B OG  1 
ATOM   763  N N   . VAL A 1 122 ? -20.717 -9.870  -21.950 1.00 36.52  ? 109 VAL B N   1 
ATOM   764  C CA  . VAL A 1 122 ? -20.932 -8.469  -21.613 1.00 36.05  ? 109 VAL B CA  1 
ATOM   765  C C   . VAL A 1 122 ? -22.099 -8.339  -20.642 1.00 38.54  ? 109 VAL B C   1 
ATOM   766  O O   . VAL A 1 122 ? -22.018 -7.569  -19.679 1.00 37.15  ? 109 VAL B O   1 
ATOM   767  C CB  . VAL A 1 122 ? -21.183 -7.591  -22.854 1.00 37.34  ? 109 VAL B CB  1 
ATOM   768  C CG1 . VAL A 1 122 ? -21.352 -6.147  -22.396 1.00 37.11  ? 109 VAL B CG1 1 
ATOM   769  C CG2 . VAL A 1 122 ? -19.982 -7.638  -23.824 1.00 37.45  ? 109 VAL B CG2 1 
ATOM   770  N N   . GLU A 1 123 ? -23.206 -9.081  -20.942 1.00 40.76  ? 110 GLU B N   1 
ATOM   771  C CA  . GLU A 1 123 ? -24.415 -9.074  -20.125 1.00 40.87  ? 110 GLU B CA  1 
ATOM   772  C C   . GLU A 1 123 ? -24.065 -9.473  -18.689 1.00 38.83  ? 110 GLU B C   1 
ATOM   773  O O   . GLU A 1 123 ? -24.440 -8.755  -17.744 1.00 38.91  ? 110 GLU B O   1 
ATOM   774  C CB  . GLU A 1 123 ? -25.489 -9.953  -20.773 1.00 40.79  ? 110 GLU B CB  1 
ATOM   775  N N   . TYR A 1 124 ? -23.255 -10.546 -18.526 1.00 37.65  ? 111 TYR B N   1 
ATOM   776  C CA  . TYR A 1 124 ? -22.898 -11.004 -17.186 1.00 37.70  ? 111 TYR B CA  1 
ATOM   777  C C   . TYR A 1 124 ? -22.084 -9.955  -16.418 1.00 34.04  ? 111 TYR B C   1 
ATOM   778  O O   . TYR A 1 124 ? -22.309 -9.632  -15.256 1.00 32.40  ? 111 TYR B O   1 
ATOM   779  C CB  . TYR A 1 124 ? -22.157 -12.343 -17.322 1.00 40.35  ? 111 TYR B CB  1 
ATOM   780  C CG  . TYR A 1 124 ? -21.888 -13.001 -15.968 1.00 39.91  ? 111 TYR B CG  1 
ATOM   781  C CD1 . TYR A 1 124 ? -22.831 -13.822 -15.335 1.00 41.96  ? 111 TYR B CD1 1 
ATOM   782  C CD2 . TYR A 1 124 ? -20.685 -12.771 -15.317 1.00 36.84  ? 111 TYR B CD2 1 
ATOM   783  C CE1 . TYR A 1 124 ? -22.579 -14.361 -14.080 1.00 41.14  ? 111 TYR B CE1 1 
ATOM   784  C CE2 . TYR A 1 124 ? -20.410 -13.342 -14.088 1.00 38.74  ? 111 TYR B CE2 1 
ATOM   785  C CZ  . TYR A 1 124 ? -21.349 -14.170 -13.495 1.00 42.23  ? 111 TYR B CZ  1 
ATOM   786  O OH  . TYR A 1 124 ? -20.960 -14.640 -12.272 1.00 41.46  ? 111 TYR B OH  1 
ATOM   787  N N   . TRP A 1 125 ? -21.038 -9.445  -17.082 1.00 33.55  ? 112 TRP B N   1 
ATOM   788  C CA  . TRP A 1 125 ? -20.165 -8.403  -16.532 1.00 31.85  ? 112 TRP B CA  1 
ATOM   789  C C   . TRP A 1 125 ? -21.006 -7.220  -16.034 1.00 31.25  ? 112 TRP B C   1 
ATOM   790  O O   . TRP A 1 125 ? -20.902 -6.825  -14.862 1.00 30.06  ? 112 TRP B O   1 
ATOM   791  C CB  . TRP A 1 125 ? -19.192 -7.921  -17.634 1.00 28.60  ? 112 TRP B CB  1 
ATOM   792  C CG  . TRP A 1 125 ? -18.435 -6.702  -17.162 1.00 30.17  ? 112 TRP B CG  1 
ATOM   793  C CD1 . TRP A 1 125 ? -18.836 -5.400  -17.196 1.00 30.30  ? 112 TRP B CD1 1 
ATOM   794  C CD2 . TRP A 1 125 ? -17.129 -6.702  -16.561 1.00 28.11  ? 112 TRP B CD2 1 
ATOM   795  N NE1 . TRP A 1 125 ? -17.904 -4.594  -16.638 1.00 30.28  ? 112 TRP B NE1 1 
ATOM   796  C CE2 . TRP A 1 125 ? -16.817 -5.370  -16.259 1.00 27.42  ? 112 TRP B CE2 1 
ATOM   797  C CE3 . TRP A 1 125 ? -16.212 -7.715  -16.260 1.00 27.20  ? 112 TRP B CE3 1 
ATOM   798  C CZ2 . TRP A 1 125 ? -15.596 -5.027  -15.638 1.00 26.47  ? 112 TRP B CZ2 1 
ATOM   799  C CZ3 . TRP A 1 125 ? -15.016 -7.382  -15.664 1.00 27.58  ? 112 TRP B CZ3 1 
ATOM   800  C CH2 . TRP A 1 125 ? -14.710 -6.039  -15.387 1.00 25.93  ? 112 TRP B CH2 1 
ATOM   801  N N   . ASP A 1 126 ? -21.900 -6.692  -16.902 1.00 33.20  ? 113 ASP B N   1 
ATOM   802  C CA  . ASP A 1 126 ? -22.714 -5.522  -16.575 1.00 34.53  ? 113 ASP B CA  1 
ATOM   803  C C   . ASP A 1 126 ? -23.564 -5.853  -15.348 1.00 34.49  ? 113 ASP B C   1 
ATOM   804  O O   . ASP A 1 126 ? -23.646 -5.028  -14.425 1.00 31.49  ? 113 ASP B O   1 
ATOM   805  C CB  . ASP A 1 126 ? -23.629 -5.077  -17.727 1.00 38.48  ? 113 ASP B CB  1 
ATOM   806  C CG  . ASP A 1 126 ? -22.885 -4.423  -18.888 1.00 39.37  ? 113 ASP B CG  1 
ATOM   807  O OD1 . ASP A 1 126 ? -21.702 -4.262  -18.767 1.00 38.11  ? 113 ASP B OD1 1 
ATOM   808  O OD2 . ASP A 1 126 ? -23.514 -4.149  -19.933 1.00 44.78  ? 113 ASP B OD2 1 
ATOM   809  N N   . GLU A 1 127 ? -24.207 -7.032  -15.364 1.00 36.78  ? 114 GLU B N   1 
ATOM   810  C CA  . GLU A 1 127 ? -25.105 -7.395  -14.251 1.00 39.43  ? 114 GLU B CA  1 
ATOM   811  C C   . GLU A 1 127 ? -24.325 -7.495  -12.914 1.00 35.94  ? 114 GLU B C   1 
ATOM   812  O O   . GLU A 1 127 ? -24.737 -6.974  -11.864 1.00 36.04  ? 114 GLU B O   1 
ATOM   813  C CB  . GLU A 1 127 ? -25.927 -8.644  -14.579 1.00 43.29  ? 114 GLU B CB  1 
ATOM   814  C CG  . GLU A 1 127 ? -26.600 -9.246  -13.346 1.00 53.72  ? 114 GLU B CG  1 
ATOM   815  C CD  . GLU A 1 127 ? -27.586 -10.380 -13.552 1.00 67.22  ? 114 GLU B CD  1 
ATOM   816  O OE1 . GLU A 1 127 ? -27.594 -10.996 -14.641 1.00 72.29  ? 114 GLU B OE1 1 
ATOM   817  O OE2 . GLU A 1 127 ? -28.373 -10.634 -12.615 1.00 77.24  ? 114 GLU B OE2 1 
ATOM   818  N N   . ARG A 1 128 ? -23.109 -8.076  -12.950 1.00 33.52  ? 115 ARG B N   1 
ATOM   819  C CA  . ARG A 1 128 ? -22.315 -8.212  -11.732 1.00 33.09  ? 115 ARG B CA  1 
ATOM   820  C C   . ARG A 1 128 ? -21.776 -6.854  -11.250 1.00 33.27  ? 115 ARG B C   1 
ATOM   821  O O   . ARG A 1 128 ? -21.721 -6.625  -10.012 1.00 30.70  ? 115 ARG B O   1 
ATOM   822  C CB  . ARG A 1 128 ? -21.319 -9.385  -11.768 1.00 36.15  ? 115 ARG B CB  1 
ATOM   823  C CG  . ARG A 1 128 ? -21.960 -10.764 -11.919 1.00 34.99  ? 115 ARG B CG  1 
ATOM   824  C CD  . ARG A 1 128 ? -22.580 -10.988 -10.506 1.00 41.44  ? 115 ARG B CD  1 
ATOM   825  N NE  . ARG A 1 128 ? -23.085 -12.358 -10.474 1.00 44.74  ? 115 ARG B NE  1 
ATOM   826  C CZ  . ARG A 1 128 ? -24.169 -12.721 -11.134 1.00 51.84  ? 115 ARG B CZ  1 
ATOM   827  N NH1 . ARG A 1 128 ? -25.051 -11.779 -11.459 1.00 59.19  ? 115 ARG B NH1 1 
ATOM   828  N NH2 . ARG A 1 128 ? -24.379 -14.001 -11.463 1.00 52.06  ? 115 ARG B NH2 1 
ATOM   829  N N   . MET A 1 129 ? -21.421 -5.928  -12.173 1.00 30.35  ? 116 MET B N   1 
ATOM   830  C CA  . MET A 1 129 ? -21.022 -4.579  -11.751 1.00 32.97  ? 116 MET B CA  1 
ATOM   831  C C   . MET A 1 129 ? -22.206 -3.853  -11.105 1.00 31.34  ? 116 MET B C   1 
ATOM   832  O O   . MET A 1 129 ? -22.048 -3.103  -10.117 1.00 32.34  ? 116 MET B O   1 
ATOM   833  C CB  . MET A 1 129 ? -20.389 -3.728  -12.866 1.00 32.80  ? 116 MET B CB  1 
ATOM   834  C CG  . MET A 1 129 ? -19.062 -4.322  -13.429 1.00 30.57  ? 116 MET B CG  1 
ATOM   835  S SD  . MET A 1 129 ? -17.964 -4.087  -12.004 1.00 35.28  ? 116 MET B SD  1 
ATOM   836  C CE  . MET A 1 129 ? -16.855 -5.490  -12.241 1.00 30.11  ? 116 MET B CE  1 
ATOM   837  N N   . GLN A 1 130 ? -23.402 -4.133  -11.603 1.00 35.83  ? 117 GLN B N   1 
ATOM   838  C CA  . GLN A 1 130 ? -24.592 -3.527  -11.027 1.00 37.39  ? 117 GLN B CA  1 
ATOM   839  C C   . GLN A 1 130 ? -24.839 -4.021  -9.576  1.00 34.59  ? 117 GLN B C   1 
ATOM   840  O O   . GLN A 1 130 ? -25.167 -3.203  -8.703  1.00 33.61  ? 117 GLN B O   1 
ATOM   841  C CB  . GLN A 1 130 ? -25.842 -3.635  -11.895 1.00 42.89  ? 117 GLN B CB  1 
ATOM   842  C CG  . GLN A 1 130 ? -25.735 -3.060  -13.304 1.00 46.51  ? 117 GLN B CG  1 
ATOM   843  C CD  . GLN A 1 130 ? -27.005 -3.287  -14.100 1.00 51.96  ? 117 GLN B CD  1 
ATOM   844  O OE1 . GLN A 1 130 ? -27.980 -3.942  -13.696 1.00 50.75  ? 117 GLN B OE1 1 
ATOM   845  N NE2 . GLN A 1 130 ? -27.041 -2.685  -15.267 1.00 60.32  ? 117 GLN B NE2 1 
ATOM   846  N N   . THR A 1 131 ? -24.714 -5.345  -9.349  1.00 34.47  ? 118 THR B N   1 
ATOM   847  C CA  . THR A 1 131 ? -25.008 -6.000  -8.064  1.00 34.54  ? 118 THR B CA  1 
ATOM   848  C C   . THR A 1 131 ? -23.869 -5.783  -7.032  1.00 32.62  ? 118 THR B C   1 
ATOM   849  O O   . THR A 1 131 ? -24.032 -5.734  -5.773  1.00 31.24  ? 118 THR B O   1 
ATOM   850  C CB  . THR A 1 131 ? -25.129 -7.475  -8.486  1.00 37.49  ? 118 THR B CB  1 
ATOM   851  O OG1 . THR A 1 131 ? -26.456 -7.689  -9.000  1.00 45.83  ? 118 THR B OG1 1 
ATOM   852  C CG2 . THR A 1 131 ? -25.121 -8.455  -7.334  1.00 43.95  ? 118 THR B CG2 1 
ATOM   853  N N   . ASN A 1 132 ? -22.646 -5.621  -7.540  1.00 29.19  ? 119 ASN B N   1 
ATOM   854  C CA  . ASN A 1 132 ? -21.463 -5.593  -6.662  1.00 31.48  ? 119 ASN B CA  1 
ATOM   855  C C   . ASN A 1 132 ? -20.917 -4.185  -6.392  1.00 28.41  ? 119 ASN B C   1 
ATOM   856  O O   . ASN A 1 132 ? -20.286 -3.958  -5.364  1.00 27.25  ? 119 ASN B O   1 
ATOM   857  C CB  . ASN A 1 132 ? -20.378 -6.572  -7.111  1.00 35.69  ? 119 ASN B CB  1 
ATOM   858  C CG  . ASN A 1 132 ? -20.740 -8.040  -6.906  1.00 42.82  ? 119 ASN B CG  1 
ATOM   859  O OD1 . ASN A 1 132 ? -20.542 -8.587  -5.824  1.00 49.04  ? 119 ASN B OD1 1 
ATOM   860  N ND2 . ASN A 1 132 ? -21.387 -8.687  -7.846  1.00 55.00  ? 119 ASN B ND2 1 
ATOM   861  N N   . LEU A 1 133 ? -21.099 -3.222  -7.311  1.00 25.43  ? 120 LEU B N   1 
ATOM   862  C CA  . LEU A 1 133 ? -20.348 -1.985  -7.161  1.00 24.44  ? 120 LEU B CA  1 
ATOM   863  C C   . LEU A 1 133 ? -21.284 -0.774  -7.244  1.00 25.68  ? 120 LEU B C   1 
ATOM   864  O O   . LEU A 1 133 ? -21.158 0.137   -6.437  1.00 27.65  ? 120 LEU B O   1 
ATOM   865  C CB  . LEU A 1 133 ? -19.371 -1.920  -8.334  1.00 25.77  ? 120 LEU B CB  1 
ATOM   866  C CG  . LEU A 1 133 ? -18.645 -0.582  -8.434  1.00 21.51  ? 120 LEU B CG  1 
ATOM   867  C CD1 . LEU A 1 133 ? -17.870 -0.431  -7.172  1.00 22.51  ? 120 LEU B CD1 1 
ATOM   868  C CD2 . LEU A 1 133 ? -17.652 -0.629  -9.610  1.00 26.09  ? 120 LEU B CD2 1 
ATOM   869  N N   . ARG A 1 134 ? -22.152 -0.718  -8.290  1.00 27.58  ? 121 ARG B N   1 
ATOM   870  C CA  . ARG A 1 134 ? -22.833 0.523   -8.668  1.00 29.37  ? 121 ARG B CA  1 
ATOM   871  C C   . ARG A 1 134 ? -23.701 1.065   -7.503  1.00 30.51  ? 121 ARG B C   1 
ATOM   872  O O   . ARG A 1 134 ? -23.699 2.272   -7.235  1.00 28.05  ? 121 ARG B O   1 
ATOM   873  C CB  . ARG A 1 134 ? -23.655 0.278   -9.941  1.00 30.99  ? 121 ARG B CB  1 
ATOM   874  C CG  . ARG A 1 134 ? -24.317 1.561   -10.418 1.00 31.54  ? 121 ARG B CG  1 
ATOM   875  C CD  . ARG A 1 134 ? -25.030 1.290   -11.715 1.00 32.20  ? 121 ARG B CD  1 
ATOM   876  N NE  . ARG A 1 134 ? -26.274 0.532   -11.540 1.00 34.56  ? 121 ARG B NE  1 
ATOM   877  C CZ  . ARG A 1 134 ? -27.122 0.269   -12.522 1.00 37.75  ? 121 ARG B CZ  1 
ATOM   878  N NH1 . ARG A 1 134 ? -26.860 0.631   -13.781 1.00 37.59  ? 121 ARG B NH1 1 
ATOM   879  N NH2 . ARG A 1 134 ? -28.229 -0.364  -12.236 1.00 38.63  ? 121 ARG B NH2 1 
ATOM   880  N N   . HIS A 1 135 ? -24.423 0.170   -6.840  1.00 31.05  ? 122 HIS B N   1 
ATOM   881  C CA  . HIS A 1 135 ? -25.334 0.564   -5.744  1.00 32.77  ? 122 HIS B CA  1 
ATOM   882  C C   . HIS A 1 135 ? -24.591 1.237   -4.593  1.00 30.70  ? 122 HIS B C   1 
ATOM   883  O O   . HIS A 1 135 ? -25.136 2.084   -3.853  1.00 28.32  ? 122 HIS B O   1 
ATOM   884  C CB  . HIS A 1 135 ? -26.201 -0.626  -5.281  1.00 32.65  ? 122 HIS B CB  1 
ATOM   885  C CG  . HIS A 1 135 ? -25.364 -1.708  -4.641  1.00 32.46  ? 122 HIS B CG  1 
ATOM   886  N ND1 . HIS A 1 135 ? -24.890 -1.675  -3.327  1.00 28.90  ? 122 HIS B ND1 1 
ATOM   887  C CD2 . HIS A 1 135 ? -24.908 -2.842  -5.194  1.00 31.70  ? 122 HIS B CD2 1 
ATOM   888  C CE1 . HIS A 1 135 ? -24.203 -2.783  -3.082  1.00 29.05  ? 122 HIS B CE1 1 
ATOM   889  N NE2 . HIS A 1 135 ? -24.253 -3.527  -4.221  1.00 32.07  ? 122 HIS B NE2 1 
ATOM   890  N N   . ALA A 1 136 ? -23.321 0.855   -4.414  1.00 28.32  ? 123 ALA B N   1 
ATOM   891  C CA  . ALA A 1 136 ? -22.570 1.339   -3.260  1.00 25.76  ? 123 ALA B CA  1 
ATOM   892  C C   . ALA A 1 136 ? -22.318 2.837   -3.467  1.00 24.56  ? 123 ALA B C   1 
ATOM   893  O O   . ALA A 1 136 ? -22.431 3.624   -2.532  1.00 25.41  ? 123 ALA B O   1 
ATOM   894  C CB  . ALA A 1 136 ? -21.276 0.522   -3.011  1.00 24.03  ? 123 ALA B CB  1 
ATOM   895  N N   . PHE A 1 137 ? -22.065 3.250   -4.724  1.00 24.82  ? 124 PHE B N   1 
ATOM   896  C CA  . PHE A 1 137 ? -21.826 4.651   -5.016  1.00 24.18  ? 124 PHE B CA  1 
ATOM   897  C C   . PHE A 1 137 ? -23.161 5.384   -4.825  1.00 26.54  ? 124 PHE B C   1 
ATOM   898  O O   . PHE A 1 137 ? -23.215 6.465   -4.239  1.00 25.88  ? 124 PHE B O   1 
ATOM   899  C CB  . PHE A 1 137 ? -21.351 4.836   -6.490  1.00 25.38  ? 124 PHE B CB  1 
ATOM   900  C CG  . PHE A 1 137 ? -21.381 6.313   -6.871  1.00 25.38  ? 124 PHE B CG  1 
ATOM   901  C CD1 . PHE A 1 137 ? -20.452 7.188   -6.313  1.00 24.66  ? 124 PHE B CD1 1 
ATOM   902  C CD2 . PHE A 1 137 ? -22.419 6.835   -7.645  1.00 26.54  ? 124 PHE B CD2 1 
ATOM   903  C CE1 . PHE A 1 137 ? -20.544 8.549   -6.522  1.00 28.92  ? 124 PHE B CE1 1 
ATOM   904  C CE2 . PHE A 1 137 ? -22.498 8.204   -7.837  1.00 30.00  ? 124 PHE B CE2 1 
ATOM   905  C CZ  . PHE A 1 137 ? -21.569 9.055   -7.305  1.00 30.19  ? 124 PHE B CZ  1 
ATOM   906  N N   . PHE A 1 138 ? -24.209 4.791   -5.375  1.00 25.71  ? 125 PHE B N   1 
ATOM   907  C CA  . PHE A 1 138 ? -25.502 5.495   -5.419  1.00 28.77  ? 125 PHE B CA  1 
ATOM   908  C C   . PHE A 1 138 ? -26.057 5.644   -3.976  1.00 28.81  ? 125 PHE B C   1 
ATOM   909  O O   . PHE A 1 138 ? -26.704 6.671   -3.650  1.00 29.30  ? 125 PHE B O   1 
ATOM   910  C CB  . PHE A 1 138 ? -26.513 5.050   -6.481  1.00 30.65  ? 125 PHE B CB  1 
ATOM   911  C CG  . PHE A 1 138 ? -26.084 5.563   -7.851  1.00 31.84  ? 125 PHE B CG  1 
ATOM   912  C CD1 . PHE A 1 138 ? -26.185 6.918   -8.158  1.00 30.98  ? 125 PHE B CD1 1 
ATOM   913  C CD2 . PHE A 1 138 ? -25.362 4.752   -8.715  1.00 31.50  ? 125 PHE B CD2 1 
ATOM   914  C CE1 . PHE A 1 138 ? -25.750 7.449   -9.356  1.00 35.19  ? 125 PHE B CE1 1 
ATOM   915  C CE2 . PHE A 1 138 ? -24.911 5.276   -9.929  1.00 32.15  ? 125 PHE B CE2 1 
ATOM   916  C CZ  . PHE A 1 138 ? -25.054 6.615   -10.217 1.00 32.56  ? 125 PHE B CZ  1 
ATOM   917  N N   . ALA A 1 139 ? -25.829 4.627   -3.139  1.00 27.89  ? 126 ALA B N   1 
ATOM   918  C CA  . ALA A 1 139 ? -26.277 4.706   -1.742  1.00 29.40  ? 126 ALA B CA  1 
ATOM   919  C C   . ALA A 1 139 ? -25.517 5.803   -0.991  1.00 32.55  ? 126 ALA B C   1 
ATOM   920  O O   . ALA A 1 139 ? -26.102 6.539   -0.178  1.00 32.02  ? 126 ALA B O   1 
ATOM   921  C CB  . ALA A 1 139 ? -26.123 3.386   -1.037  1.00 27.54  ? 126 ALA B CB  1 
ATOM   922  N N   . ALA A 1 140 ? -24.211 5.915   -1.277  1.00 28.40  ? 127 ALA B N   1 
ATOM   923  C CA  . ALA A 1 140 ? -23.418 6.913   -0.577  1.00 27.17  ? 127 ALA B CA  1 
ATOM   924  C C   . ALA A 1 140 ? -23.903 8.273   -1.059  1.00 28.20  ? 127 ALA B C   1 
ATOM   925  O O   . ALA A 1 140 ? -24.033 9.240   -0.319  1.00 32.11  ? 127 ALA B O   1 
ATOM   926  C CB  . ALA A 1 140 ? -21.920 6.691   -0.920  1.00 23.82  ? 127 ALA B CB  1 
ATOM   927  N N   . GLN A 1 141 ? -24.179 8.349   -2.381  1.00 28.55  ? 128 GLN B N   1 
ATOM   928  C CA  . GLN A 1 141 ? -24.667 9.595   -2.942  1.00 27.82  ? 128 GLN B CA  1 
ATOM   929  C C   . GLN A 1 141 ? -26.003 9.987   -2.290  1.00 31.05  ? 128 GLN B C   1 
ATOM   930  O O   . GLN A 1 141 ? -26.210 11.158  -2.040  1.00 31.29  ? 128 GLN B O   1 
ATOM   931  C CB  . GLN A 1 141 ? -24.756 9.535   -4.477  1.00 29.78  ? 128 GLN B CB  1 
ATOM   932  C CG  . GLN A 1 141 ? -25.367 10.773  -5.137  1.00 31.22  ? 128 GLN B CG  1 
ATOM   933  C CD  . GLN A 1 141 ? -25.684 10.564  -6.586  1.00 34.49  ? 128 GLN B CD  1 
ATOM   934  O OE1 . GLN A 1 141 ? -26.577 9.786   -6.922  1.00 37.11  ? 128 GLN B OE1 1 
ATOM   935  N NE2 . GLN A 1 141 ? -24.927 11.199  -7.478  1.00 41.38  ? 128 GLN B NE2 1 
ATOM   936  N N   . ALA A 1 142 ? -26.858 9.002   -2.013  1.00 32.43  ? 129 ALA B N   1 
ATOM   937  C CA  . ALA A 1 142 ? -28.204 9.275   -1.486  1.00 31.92  ? 129 ALA B CA  1 
ATOM   938  C C   . ALA A 1 142 ? -28.145 9.746   -0.036  1.00 33.87  ? 129 ALA B C   1 
ATOM   939  O O   . ALA A 1 142 ? -28.919 10.658  0.327   1.00 34.49  ? 129 ALA B O   1 
ATOM   940  C CB  . ALA A 1 142 ? -29.086 8.067   -1.589  1.00 32.68  ? 129 ALA B CB  1 
ATOM   941  N N   . VAL A 1 143 ? -27.305 9.098   0.777   1.00 31.37  ? 130 VAL B N   1 
ATOM   942  C CA  . VAL A 1 143 ? -27.264 9.410   2.200   1.00 32.43  ? 130 VAL B CA  1 
ATOM   943  C C   . VAL A 1 143 ? -26.453 10.670  2.454   1.00 31.68  ? 130 VAL B C   1 
ATOM   944  O O   . VAL A 1 143 ? -26.640 11.318  3.478   1.00 31.05  ? 130 VAL B O   1 
ATOM   945  C CB  . VAL A 1 143 ? -26.731 8.238   3.027   1.00 29.84  ? 130 VAL B CB  1 
ATOM   946  C CG1 . VAL A 1 143 ? -27.651 7.005   2.887   1.00 30.68  ? 130 VAL B CG1 1 
ATOM   947  C CG2 . VAL A 1 143 ? -25.220 8.022   2.769   1.00 25.89  ? 130 VAL B CG2 1 
ATOM   948  N N   . ALA A 1 144 ? -25.528 11.022  1.562   1.00 31.21  ? 131 ALA B N   1 
ATOM   949  C CA  . ALA A 1 144 ? -24.576 12.087  1.856   1.00 29.88  ? 131 ALA B CA  1 
ATOM   950  C C   . ALA A 1 144 ? -25.300 13.394  2.190   1.00 32.98  ? 131 ALA B C   1 
ATOM   951  O O   . ALA A 1 144 ? -24.920 14.062  3.129   1.00 32.79  ? 131 ALA B O   1 
ATOM   952  C CB  . ALA A 1 144 ? -23.599 12.305  0.680   1.00 29.24  ? 131 ALA B CB  1 
ATOM   953  N N   . PRO A 1 145 ? -26.229 13.953  1.375   1.00 34.99  ? 132 PRO B N   1 
ATOM   954  C CA  . PRO A 1 145 ? -26.704 15.301  1.678   1.00 36.19  ? 132 PRO B CA  1 
ATOM   955  C C   . PRO A 1 145 ? -27.313 15.416  3.072   1.00 35.45  ? 132 PRO B C   1 
ATOM   956  O O   . PRO A 1 145 ? -27.132 16.441  3.721   1.00 35.97  ? 132 PRO B O   1 
ATOM   957  C CB  . PRO A 1 145 ? -27.680 15.681  0.550   1.00 40.78  ? 132 PRO B CB  1 
ATOM   958  C CG  . PRO A 1 145 ? -27.035 14.824  -0.565  1.00 38.37  ? 132 PRO B CG  1 
ATOM   959  C CD  . PRO A 1 145 ? -26.719 13.473  0.080   1.00 36.91  ? 132 PRO B CD  1 
ATOM   960  N N   . GLY A 1 146 ? -27.978 14.353  3.533   1.00 35.35  ? 133 GLY B N   1 
ATOM   961  C CA  . GLY A 1 146 ? -28.609 14.416  4.871   1.00 36.31  ? 133 GLY B CA  1 
ATOM   962  C C   . GLY A 1 146 ? -27.546 14.386  5.974   1.00 37.80  ? 133 GLY B C   1 
ATOM   963  O O   . GLY A 1 146 ? -27.616 15.091  6.981   1.00 36.01  ? 133 GLY B O   1 
ATOM   964  N N   . MET A 1 147 ? -26.483 13.583  5.733   1.00 35.24  ? 134 MET B N   1 
ATOM   965  C CA  . MET A 1 147 ? -25.356 13.529  6.647   1.00 32.49  ? 134 MET B CA  1 
ATOM   966  C C   . MET A 1 147 ? -24.710 14.907  6.730   1.00 32.20  ? 134 MET B C   1 
ATOM   967  O O   . MET A 1 147 ? -24.353 15.327  7.818   1.00 31.57  ? 134 MET B O   1 
ATOM   968  C CB  . MET A 1 147 ? -24.307 12.512  6.188   1.00 28.87  ? 134 MET B CB  1 
ATOM   969  C CG  . MET A 1 147 ? -24.695 11.141  6.549   1.00 26.42  ? 134 MET B CG  1 
ATOM   970  S SD  . MET A 1 147 ? -23.544 9.989   5.777   1.00 28.28  ? 134 MET B SD  1 
ATOM   971  C CE  . MET A 1 147 ? -24.206 8.473   6.460   1.00 25.80  ? 134 MET B CE  1 
ATOM   972  N N   . ALA A 1 148 ? -24.492 15.565  5.586   1.00 34.15  ? 135 ALA B N   1 
ATOM   973  C CA  . ALA A 1 148 ? -23.841 16.877  5.532   1.00 33.10  ? 135 ALA B CA  1 
ATOM   974  C C   . ALA A 1 148 ? -24.667 17.943  6.210   1.00 36.75  ? 135 ALA B C   1 
ATOM   975  O O   . ALA A 1 148 ? -24.076 18.839  6.797   1.00 39.42  ? 135 ALA B O   1 
ATOM   976  C CB  . ALA A 1 148 ? -23.524 17.316  4.094   1.00 36.90  ? 135 ALA B CB  1 
ATOM   977  N N   . ARG A 1 149 ? -26.002 17.912  6.052   1.00 40.26  ? 136 ARG B N   1 
ATOM   978  C CA  . ARG A 1 149 ? -26.873 18.880  6.731   1.00 43.18  ? 136 ARG B CA  1 
ATOM   979  C C   . ARG A 1 149 ? -26.618 18.775  8.239   1.00 45.14  ? 136 ARG B C   1 
ATOM   980  O O   . ARG A 1 149 ? -26.576 19.794  8.925   1.00 43.42  ? 136 ARG B O   1 
ATOM   981  C CB  . ARG A 1 149 ? -28.370 18.839  6.368   1.00 49.90  ? 136 ARG B CB  1 
ATOM   982  C CG  . ARG A 1 149 ? -28.801 19.656  5.145   1.00 63.64  ? 136 ARG B CG  1 
ATOM   983  C CD  . ARG A 1 149 ? -30.301 19.847  4.807   1.00 59.28  ? 136 ARG B CD  1 
ATOM   984  N NE  . ARG A 1 149 ? -30.993 18.579  5.098   1.00 62.58  ? 136 ARG B NE  1 
ATOM   985  C CZ  . ARG A 1 149 ? -31.011 17.405  4.421   1.00 67.88  ? 136 ARG B CZ  1 
ATOM   986  N NH1 . ARG A 1 149 ? -30.727 17.356  3.109   1.00 59.98  ? 136 ARG B NH1 1 
ATOM   987  N NH2 . ARG A 1 149 ? -31.409 16.297  5.061   1.00 65.93  ? 136 ARG B NH2 1 
ATOM   988  N N   . ARG A 1 150 ? -26.458 17.540  8.746   1.00 41.06  ? 137 ARG B N   1 
ATOM   989  C CA  . ARG A 1 150 ? -26.273 17.346  10.187  1.00 38.73  ? 137 ARG B CA  1 
ATOM   990  C C   . ARG A 1 150 ? -24.848 17.730  10.575  1.00 37.73  ? 137 ARG B C   1 
ATOM   991  O O   . ARG A 1 150 ? -24.604 18.210  11.683  1.00 39.94  ? 137 ARG B O   1 
ATOM   992  C CB  . ARG A 1 150 ? -26.757 15.974  10.662  1.00 39.92  ? 137 ARG B CB  1 
ATOM   993  C CG  . ARG A 1 150 ? -26.225 15.474  12.007  1.00 36.10  ? 137 ARG B CG  1 
ATOM   994  C CD  . ARG A 1 150 ? -26.808 14.167  12.566  1.00 35.63  ? 137 ARG B CD  1 
ATOM   995  N NE  . ARG A 1 150 ? -26.308 13.202  11.594  1.00 37.75  ? 137 ARG B NE  1 
ATOM   996  C CZ  . ARG A 1 150 ? -26.887 12.380  10.762  1.00 35.72  ? 137 ARG B CZ  1 
ATOM   997  N NH1 . ARG A 1 150 ? -26.122 11.718  9.918   1.00 32.82  ? 137 ARG B NH1 1 
ATOM   998  N NH2 . ARG A 1 150 ? -28.216 12.226  10.807  1.00 42.37  ? 137 ARG B NH2 1 
ATOM   999  N N   . GLY A 1 151 ? -23.858 17.440  9.709   1.00 36.17  ? 138 GLY B N   1 
ATOM   1000 C CA  . GLY A 1 151 ? -22.469 17.683  10.071  1.00 31.82  ? 138 GLY B CA  1 
ATOM   1001 C C   . GLY A 1 151 ? -21.730 16.409  10.433  1.00 30.36  ? 138 GLY B C   1 
ATOM   1002 O O   . GLY A 1 151 ? -20.617 16.526  10.936  1.00 30.08  ? 138 GLY B O   1 
ATOM   1003 N N   . SER A 1 152 ? -22.343 15.223  10.227  1.00 28.09  ? 139 SER B N   1 
ATOM   1004 C CA  . SER A 1 152 ? -21.682 14.006  10.690  1.00 28.81  ? 139 SER B CA  1 
ATOM   1005 C C   . SER A 1 152 ? -22.251 12.800  9.960   1.00 27.97  ? 139 SER B C   1 
ATOM   1006 O O   . SER A 1 152 ? -23.441 12.871  9.545   1.00 33.83  ? 139 SER B O   1 
ATOM   1007 C CB  . SER A 1 152 ? -21.922 13.877  12.231  1.00 30.54  ? 139 SER B CB  1 
ATOM   1008 O OG  . SER A 1 152 ? -23.224 13.367  12.499  1.00 30.91  ? 139 SER B OG  1 
ATOM   1009 N N   . GLY A 1 153 ? -21.465 11.707  9.889   1.00 25.73  ? 140 GLY B N   1 
ATOM   1010 C CA  . GLY A 1 153 ? -21.992 10.458  9.386   1.00 27.00  ? 140 GLY B CA  1 
ATOM   1011 C C   . GLY A 1 153 ? -20.844 9.506   9.076   1.00 22.70  ? 140 GLY B C   1 
ATOM   1012 O O   . GLY A 1 153 ? -19.716 9.945   9.024   1.00 22.49  ? 140 GLY B O   1 
ATOM   1013 N N   . ALA A 1 154 ? -21.176 8.236   8.845   1.00 23.02  ? 141 ALA B N   1 
ATOM   1014 C CA  . ALA A 1 154 ? -20.137 7.262   8.582   1.00 22.77  ? 141 ALA B CA  1 
ATOM   1015 C C   . ALA A 1 154 ? -20.606 6.275   7.528   1.00 22.18  ? 141 ALA B C   1 
ATOM   1016 O O   . ALA A 1 154 ? -21.769 5.868   7.572   1.00 23.01  ? 141 ALA B O   1 
ATOM   1017 C CB  . ALA A 1 154 ? -19.862 6.511   9.859   1.00 21.90  ? 141 ALA B CB  1 
ATOM   1018 N N   . ILE A 1 155 ? -19.678 5.846   6.649   1.00 19.71  ? 142 ILE B N   1 
ATOM   1019 C CA  . ILE A 1 155 ? -19.986 4.908   5.578   1.00 22.82  ? 142 ILE B CA  1 
ATOM   1020 C C   . ILE A 1 155 ? -18.984 3.767   5.707   1.00 20.35  ? 142 ILE B C   1 
ATOM   1021 O O   . ILE A 1 155 ? -17.797 4.046   5.901   1.00 21.31  ? 142 ILE B O   1 
ATOM   1022 C CB  . ILE A 1 155 ? -19.930 5.578   4.197   1.00 23.59  ? 142 ILE B CB  1 
ATOM   1023 C CG1 . ILE A 1 155 ? -21.086 6.589   4.063   1.00 23.84  ? 142 ILE B CG1 1 
ATOM   1024 C CG2 . ILE A 1 155 ? -20.029 4.536   3.065   1.00 25.34  ? 142 ILE B CG2 1 
ATOM   1025 C CD1 . ILE A 1 155 ? -20.942 7.497   2.843   1.00 23.89  ? 142 ILE B CD1 1 
ATOM   1026 N N   . ILE A 1 156 ? -19.459 2.529   5.592   1.00 21.91  ? 143 ILE B N   1 
ATOM   1027 C CA  . ILE A 1 156 ? -18.570 1.382   5.620   1.00 19.30  ? 143 ILE B CA  1 
ATOM   1028 C C   . ILE A 1 156 ? -18.777 0.675   4.292   1.00 19.15  ? 143 ILE B C   1 
ATOM   1029 O O   . ILE A 1 156 ? -19.885 0.260   4.077   1.00 18.77  ? 143 ILE B O   1 
ATOM   1030 C CB  . ILE A 1 156 ? -18.903 0.462   6.809   1.00 20.70  ? 143 ILE B CB  1 
ATOM   1031 C CG1 . ILE A 1 156 ? -18.744 1.262   8.124   1.00 20.60  ? 143 ILE B CG1 1 
ATOM   1032 C CG2 . ILE A 1 156 ? -17.971 -0.762  6.807   1.00 18.85  ? 143 ILE B CG2 1 
ATOM   1033 C CD1 . ILE A 1 156 ? -19.378 0.605   9.385   1.00 21.02  ? 143 ILE B CD1 1 
ATOM   1034 N N   . ASN A 1 157 ? -17.735 0.536   3.443   1.00 17.97  ? 144 ASN B N   1 
ATOM   1035 C CA  . ASN A 1 157 ? -17.872 -0.238  2.203   1.00 19.28  ? 144 ASN B CA  1 
ATOM   1036 C C   . ASN A 1 157 ? -17.332 -1.629  2.510   1.00 20.72  ? 144 ASN B C   1 
ATOM   1037 O O   . ASN A 1 157 ? -16.178 -1.730  2.963   1.00 21.79  ? 144 ASN B O   1 
ATOM   1038 C CB  . ASN A 1 157 ? -17.002 0.397   1.116   1.00 23.07  ? 144 ASN B CB  1 
ATOM   1039 C CG  . ASN A 1 157 ? -17.570 1.712   0.643   1.00 24.93  ? 144 ASN B CG  1 
ATOM   1040 O OD1 . ASN A 1 157 ? -18.780 1.816   0.553   1.00 25.57  ? 144 ASN B OD1 1 
ATOM   1041 N ND2 . ASN A 1 157 ? -16.801 2.705   0.270   1.00 20.80  ? 144 ASN B ND2 1 
ATOM   1042 N N   . MET A 1 158 ? -18.108 -2.696  2.340   1.00 20.36  ? 145 MET B N   1 
ATOM   1043 C CA  . MET A 1 158 ? -17.577 -4.028  2.492   1.00 19.64  ? 145 MET B CA  1 
ATOM   1044 C C   . MET A 1 158 ? -16.652 -4.356  1.321   1.00 23.62  ? 145 MET B C   1 
ATOM   1045 O O   . MET A 1 158 ? -17.003 -4.337  0.106   1.00 22.84  ? 145 MET B O   1 
ATOM   1046 C CB  . MET A 1 158 ? -18.715 -5.044  2.590   1.00 21.01  ? 145 MET B CB  1 
ATOM   1047 C CG  . MET A 1 158 ? -19.647 -4.763  3.797   1.00 23.01  ? 145 MET B CG  1 
ATOM   1048 S SD  . MET A 1 158 ? -18.688 -5.154  5.243   1.00 24.84  ? 145 MET B SD  1 
ATOM   1049 C CE  . MET A 1 158 ? -18.432 -6.911  4.980   1.00 25.54  ? 145 MET B CE  1 
ATOM   1050 N N   . GLY A 1 159 ? -15.389 -4.663  1.706   1.00 25.73  ? 146 GLY B N   1 
ATOM   1051 C CA  . GLY A 1 159 ? -14.338 -4.929  0.742   1.00 23.01  ? 146 GLY B CA  1 
ATOM   1052 C C   . GLY A 1 159 ? -14.056 -6.420  0.828   1.00 23.70  ? 146 GLY B C   1 
ATOM   1053 O O   . GLY A 1 159 ? -14.917 -7.205  1.253   1.00 23.21  ? 146 GLY B O   1 
ATOM   1054 N N   . SER A 1 160 ? -12.896 -6.803  0.292   1.00 20.95  ? 147 SER B N   1 
ATOM   1055 C CA  . SER A 1 160 ? -12.593 -8.238  0.228   1.00 24.95  ? 147 SER B CA  1 
ATOM   1056 C C   . SER A 1 160 ? -11.067 -8.403  0.053   1.00 22.72  ? 147 SER B C   1 
ATOM   1057 O O   . SER A 1 160 ? -10.407 -7.564  -0.629  1.00 21.42  ? 147 SER B O   1 
ATOM   1058 C CB  . SER A 1 160 ? -13.339 -8.984  -0.872  1.00 25.26  ? 147 SER B CB  1 
ATOM   1059 O OG  . SER A 1 160 ? -12.836 -10.313 -0.954  1.00 24.59  ? 147 SER B OG  1 
ATOM   1060 N N   . ILE A 1 161 ? -10.506 -9.398  0.766   1.00 21.91  ? 148 ILE B N   1 
ATOM   1061 C CA  . ILE A 1 161 ? -9.070  -9.676  0.589   1.00 22.59  ? 148 ILE B CA  1 
ATOM   1062 C C   . ILE A 1 161 ? -8.804  -10.436 -0.714  1.00 22.86  ? 148 ILE B C   1 
ATOM   1063 O O   . ILE A 1 161 ? -7.625  -10.556 -1.079  1.00 19.59  ? 148 ILE B O   1 
ATOM   1064 C CB  . ILE A 1 161 ? -8.389  -10.429 1.741   1.00 21.92  ? 148 ILE B CB  1 
ATOM   1065 C CG1 . ILE A 1 161 ? -8.983  -11.855 1.864   1.00 21.63  ? 148 ILE B CG1 1 
ATOM   1066 C CG2 . ILE A 1 161 ? -8.388  -9.622  3.053   1.00 22.21  ? 148 ILE B CG2 1 
ATOM   1067 C CD1 . ILE A 1 161 ? -8.184  -12.744 2.799   1.00 22.11  ? 148 ILE B CD1 1 
ATOM   1068 N N   . SER A 1 162 ? -9.868  -10.902 -1.373  1.00 22.05  ? 149 SER B N   1 
ATOM   1069 C CA  . SER A 1 162 ? -9.745  -11.730 -2.571  1.00 20.97  ? 149 SER B CA  1 
ATOM   1070 C C   . SER A 1 162 ? -8.942  -10.985 -3.652  1.00 21.14  ? 149 SER B C   1 
ATOM   1071 O O   . SER A 1 162 ? -8.060  -11.593 -4.269  1.00 19.76  ? 149 SER B O   1 
ATOM   1072 C CB  . SER A 1 162 ? -11.096 -12.223 -3.072  1.00 25.06  ? 149 SER B CB  1 
ATOM   1073 O OG  . SER A 1 162 ? -11.865 -11.083 -3.393  1.00 27.56  ? 149 SER B OG  1 
ATOM   1074 N N   . TRP A 1 163 ? -9.145  -9.657  -3.835  1.00 17.88  ? 150 TRP B N   1 
ATOM   1075 C CA  . TRP A 1 163 ? -8.379  -9.046  -4.913  1.00 18.96  ? 150 TRP B CA  1 
ATOM   1076 C C   . TRP A 1 163 ? -6.968  -8.730  -4.480  1.00 19.25  ? 150 TRP B C   1 
ATOM   1077 O O   . TRP A 1 163 ? -6.018  -8.839  -5.314  1.00 21.45  ? 150 TRP B O   1 
ATOM   1078 C CB  . TRP A 1 163 ? -9.059  -7.791  -5.496  1.00 22.12  ? 150 TRP B CB  1 
ATOM   1079 C CG  . TRP A 1 163 ? -9.076  -6.672  -4.475  1.00 19.64  ? 150 TRP B CG  1 
ATOM   1080 C CD1 . TRP A 1 163 ? -10.096 -6.367  -3.609  1.00 22.63  ? 150 TRP B CD1 1 
ATOM   1081 C CD2 . TRP A 1 163 ? -8.047  -5.696  -4.219  1.00 19.80  ? 150 TRP B CD2 1 
ATOM   1082 N NE1 . TRP A 1 163 ? -9.782  -5.316  -2.773  1.00 19.25  ? 150 TRP B NE1 1 
ATOM   1083 C CE2 . TRP A 1 163 ? -8.526  -4.872  -3.147  1.00 21.06  ? 150 TRP B CE2 1 
ATOM   1084 C CE3 . TRP A 1 163 ? -6.769  -5.458  -4.741  1.00 20.69  ? 150 TRP B CE3 1 
ATOM   1085 C CZ2 . TRP A 1 163 ? -7.780  -3.823  -2.643  1.00 21.24  ? 150 TRP B CZ2 1 
ATOM   1086 C CZ3 . TRP A 1 163 ? -5.995  -4.446  -4.190  1.00 25.36  ? 150 TRP B CZ3 1 
ATOM   1087 C CH2 . TRP A 1 163 ? -6.527  -3.610  -3.199  1.00 19.98  ? 150 TRP B CH2 1 
ATOM   1088 N N   . MET A 1 164 ? -6.794  -8.479  -3.169  1.00 17.72  ? 151 MET B N   1 
ATOM   1089 C CA  . MET A 1 164 ? -5.458  -8.274  -2.644  1.00 18.59  ? 151 MET B CA  1 
ATOM   1090 C C   . MET A 1 164 ? -4.625  -9.533  -2.854  1.00 21.29  ? 151 MET B C   1 
ATOM   1091 O O   . MET A 1 164 ? -3.453  -9.423  -3.135  1.00 21.30  ? 151 MET B O   1 
ATOM   1092 C CB  . MET A 1 164 ? -5.547  -7.994  -1.125  1.00 18.35  ? 151 MET B CB  1 
ATOM   1093 C CG  . MET A 1 164 ? -6.276  -6.647  -0.852  1.00 24.66  ? 151 MET B CG  1 
ATOM   1094 S SD  . MET A 1 164 ? -6.602  -6.493  0.916   1.00 24.61  ? 151 MET B SD  1 
ATOM   1095 C CE  . MET A 1 164 ? -7.428  -4.888  0.911   1.00 24.41  ? 151 MET B CE  1 
ATOM   1096 N N   . ARG A 1 165 ? -5.240  -10.724 -2.660  1.00 20.28  ? 152 ARG B N   1 
ATOM   1097 C CA  . ARG A 1 165 ? -4.539  -11.978 -2.764  1.00 19.20  ? 152 ARG B CA  1 
ATOM   1098 C C   . ARG A 1 165 ? -4.552  -12.457 -4.215  1.00 19.39  ? 152 ARG B C   1 
ATOM   1099 O O   . ARG A 1 165 ? -4.012  -13.555 -4.497  1.00 20.49  ? 152 ARG B O   1 
ATOM   1100 C CB  . ARG A 1 165 ? -5.309  -13.073 -2.020  1.00 19.70  ? 152 ARG B CB  1 
ATOM   1101 C CG  . ARG A 1 165 ? -5.207  -12.918 -0.508  1.00 17.03  ? 152 ARG B CG  1 
ATOM   1102 C CD  . ARG A 1 165 ? -5.912  -14.153 0.180   1.00 18.85  ? 152 ARG B CD  1 
ATOM   1103 N NE  . ARG A 1 165 ? -5.230  -15.384 -0.225  1.00 21.77  ? 152 ARG B NE  1 
ATOM   1104 C CZ  . ARG A 1 165 ? -5.714  -16.613 -0.121  1.00 23.48  ? 152 ARG B CZ  1 
ATOM   1105 N NH1 . ARG A 1 165 ? -6.946  -16.783 0.348   1.00 21.96  ? 152 ARG B NH1 1 
ATOM   1106 N NH2 . ARG A 1 165 ? -4.959  -17.644 -0.513  1.00 27.21  ? 152 ARG B NH2 1 
ATOM   1107 N N   . GLY A 1 166 ? -5.040  -11.615 -5.159  1.00 19.07  ? 153 GLY B N   1 
ATOM   1108 C CA  . GLY A 1 166 ? -5.019  -11.947 -6.589  1.00 19.56  ? 153 GLY B CA  1 
ATOM   1109 C C   . GLY A 1 166 ? -5.791  -13.247 -6.864  1.00 20.91  ? 153 GLY B C   1 
ATOM   1110 O O   . GLY A 1 166 ? -5.371  -14.114 -7.629  1.00 21.73  ? 153 GLY B O   1 
ATOM   1111 N N   . ARG A 1 167 ? -6.904  -13.437 -6.155  1.00 22.42  ? 154 ARG B N   1 
ATOM   1112 C CA  . ARG A 1 167 ? -7.603  -14.732 -6.287  1.00 24.55  ? 154 ARG B CA  1 
ATOM   1113 C C   . ARG A 1 167 ? -8.276  -14.858 -7.646  1.00 23.64  ? 154 ARG B C   1 
ATOM   1114 O O   . ARG A 1 167 ? -8.965  -13.925 -8.058  1.00 21.61  ? 154 ARG B O   1 
ATOM   1115 C CB  . ARG A 1 167 ? -8.763  -14.872 -5.297  1.00 26.49  ? 154 ARG B CB  1 
ATOM   1116 C CG  . ARG A 1 167 ? -8.170  -15.001 -3.889  1.00 34.54  ? 154 ARG B CG  1 
ATOM   1117 C CD  . ARG A 1 167 ? -7.113  -16.084 -3.719  1.00 43.53  ? 154 ARG B CD  1 
ATOM   1118 N NE  . ARG A 1 167 ? -7.751  -17.359 -3.408  1.00 47.30  ? 154 ARG B NE  1 
ATOM   1119 C CZ  . ARG A 1 167 ? -7.190  -18.574 -3.635  1.00 59.89  ? 154 ARG B CZ  1 
ATOM   1120 N NH1 . ARG A 1 167 ? -7.761  -19.682 -3.132  1.00 47.28  ? 154 ARG B NH1 1 
ATOM   1121 N NH2 . ARG A 1 167 ? -6.062  -18.662 -4.353  1.00 45.27  ? 154 ARG B NH2 1 
ATOM   1122 N N   . PRO A 1 168 ? -8.073  -15.983 -8.387  1.00 24.46  ? 155 PRO B N   1 
ATOM   1123 C CA  . PRO A 1 168 ? -8.629  -16.144 -9.715  1.00 25.46  ? 155 PRO B CA  1 
ATOM   1124 C C   . PRO A 1 168 ? -10.054 -16.700 -9.686  1.00 27.17  ? 155 PRO B C   1 
ATOM   1125 O O   . PRO A 1 168 ? -10.510 -17.137 -8.618  1.00 27.44  ? 155 PRO B O   1 
ATOM   1126 C CB  . PRO A 1 168 ? -7.665  -17.130 -10.421 1.00 26.00  ? 155 PRO B CB  1 
ATOM   1127 C CG  . PRO A 1 168 ? -7.292  -18.027 -9.279  1.00 26.71  ? 155 PRO B CG  1 
ATOM   1128 C CD  . PRO A 1 168 ? -7.300  -17.173 -7.984  1.00 25.21  ? 155 PRO B CD  1 
ATOM   1129 N N   . GLY A 1 169 ? -10.720 -16.657 -10.838 1.00 29.40  ? 156 GLY B N   1 
ATOM   1130 C CA  . GLY A 1 169 ? -11.954 -17.406 -11.108 1.00 31.38  ? 156 GLY B CA  1 
ATOM   1131 C C   . GLY A 1 169 ? -13.207 -16.638 -10.655 1.00 31.70  ? 156 GLY B C   1 
ATOM   1132 O O   . GLY A 1 169 ? -14.269 -17.230 -10.619 1.00 34.99  ? 156 GLY B O   1 
ATOM   1133 N N   . MET A 1 170 ? -13.116 -15.337 -10.326 1.00 27.16  ? 157 MET B N   1 
ATOM   1134 C CA  . MET A 1 170 ? -14.314 -14.579 -10.003 1.00 27.86  ? 157 MET B CA  1 
ATOM   1135 C C   . MET A 1 170 ? -14.074 -13.123 -10.334 1.00 25.60  ? 157 MET B C   1 
ATOM   1136 O O   . MET A 1 170 ? -14.389 -12.245 -9.538  1.00 24.19  ? 157 MET B O   1 
ATOM   1137 C CB  . MET A 1 170 ? -14.769 -14.764 -8.535  1.00 28.55  ? 157 MET B CB  1 
ATOM   1138 C CG  . MET A 1 170 ? -13.670 -14.611 -7.521  1.00 31.62  ? 157 MET B CG  1 
ATOM   1139 S SD  . MET A 1 170 ? -14.234 -15.242 -5.931  1.00 46.84  ? 157 MET B SD  1 
ATOM   1140 C CE  . MET A 1 170 ? -14.390 -17.026 -5.939  1.00 43.45  ? 157 MET B CE  1 
ATOM   1141 N N   . VAL A 1 171 ? -13.555 -12.899 -11.556 1.00 25.62  ? 158 VAL B N   1 
ATOM   1142 C CA  . VAL A 1 171 ? -13.040 -11.589 -11.970 1.00 23.41  ? 158 VAL B CA  1 
ATOM   1143 C C   . VAL A 1 171 ? -14.078 -10.483 -11.700 1.00 23.33  ? 158 VAL B C   1 
ATOM   1144 O O   . VAL A 1 171 ? -13.710 -9.403  -11.292 1.00 24.21  ? 158 VAL B O   1 
ATOM   1145 C CB  . VAL A 1 171 ? -12.587 -11.629 -13.455 1.00 23.61  ? 158 VAL B CB  1 
ATOM   1146 C CG1 . VAL A 1 171 ? -13.712 -11.891 -14.439 1.00 24.94  ? 158 VAL B CG1 1 
ATOM   1147 C CG2 . VAL A 1 171 ? -11.913 -10.288 -13.810 1.00 23.63  ? 158 VAL B CG2 1 
ATOM   1148 N N   . CYS A 1 172 ? -15.415 -10.696 -11.922 1.00 25.41  ? 159 CYS B N   1 
ATOM   1149 C CA  . CYS A 1 172 ? -16.304 -9.543  -11.738 1.00 25.19  ? 159 CYS B CA  1 
ATOM   1150 C C   . CYS A 1 172 ? -16.409 -9.092  -10.267 1.00 27.45  ? 159 CYS B C   1 
ATOM   1151 O O   . CYS A 1 172 ? -16.414 -7.882  -9.953  1.00 28.96  ? 159 CYS B O   1 
ATOM   1152 C CB  . CYS A 1 172 ? -17.688 -9.844  -12.328 1.00 28.12  ? 159 CYS B CB  1 
ATOM   1153 S SG  . CYS A 1 172 ? -17.693 -10.262 -14.100 1.00 34.32  ? 159 CYS B SG  1 
ATOM   1154 N N   . TYR A 1 173 ? -16.515 -10.077 -9.360  1.00 27.01  ? 160 TYR B N   1 
ATOM   1155 C CA  . TYR A 1 173 ? -16.541 -9.860  -7.907  1.00 26.14  ? 160 TYR B CA  1 
ATOM   1156 C C   . TYR A 1 173 ? -15.279 -9.189  -7.410  1.00 24.39  ? 160 TYR B C   1 
ATOM   1157 O O   . TYR A 1 173 ? -15.358 -8.150  -6.765  1.00 23.32  ? 160 TYR B O   1 
ATOM   1158 C CB  . TYR A 1 173 ? -16.757 -11.237 -7.249  1.00 29.17  ? 160 TYR B CB  1 
ATOM   1159 C CG  . TYR A 1 173 ? -16.773 -11.109 -5.733  1.00 27.91  ? 160 TYR B CG  1 
ATOM   1160 C CD1 . TYR A 1 173 ? -17.930 -10.739 -5.076  1.00 31.30  ? 160 TYR B CD1 1 
ATOM   1161 C CD2 . TYR A 1 173 ? -15.635 -11.358 -4.980  1.00 26.58  ? 160 TYR B CD2 1 
ATOM   1162 C CE1 . TYR A 1 173 ? -17.949 -10.564 -3.689  1.00 31.27  ? 160 TYR B CE1 1 
ATOM   1163 C CE2 . TYR A 1 173 ? -15.626 -11.194 -3.583  1.00 31.67  ? 160 TYR B CE2 1 
ATOM   1164 C CZ  . TYR A 1 173 ? -16.803 -10.809 -2.953  1.00 33.33  ? 160 TYR B CZ  1 
ATOM   1165 O OH  . TYR A 1 173 ? -16.828 -10.603 -1.607  1.00 36.25  ? 160 TYR B OH  1 
ATOM   1166 N N   . THR A 1 174 ? -14.122 -9.690  -7.835  1.00 24.89  ? 161 THR B N   1 
ATOM   1167 C CA  . THR A 1 174 ? -12.867 -9.206  -7.233  1.00 24.17  ? 161 THR B CA  1 
ATOM   1168 C C   . THR A 1 174 ? -12.571 -7.805  -7.788  1.00 22.66  ? 161 THR B C   1 
ATOM   1169 O O   . THR A 1 174 ? -12.059 -6.990  -7.067  1.00 20.92  ? 161 THR B O   1 
ATOM   1170 C CB  . THR A 1 174 ? -11.700 -10.173 -7.548  1.00 25.94  ? 161 THR B CB  1 
ATOM   1171 O OG1 . THR A 1 174 ? -11.631 -10.521 -8.947  1.00 23.60  ? 161 THR B OG1 1 
ATOM   1172 C CG2 . THR A 1 174 ? -11.810 -11.466 -6.757  1.00 24.00  ? 161 THR B CG2 1 
ATOM   1173 N N   . THR A 1 175 ? -12.972 -7.544  -9.036  1.00 20.70  ? 162 THR B N   1 
ATOM   1174 C CA  . THR A 1 175 ? -12.735 -6.259  -9.668  1.00 20.88  ? 162 THR B CA  1 
ATOM   1175 C C   . THR A 1 175 ? -13.639 -5.204  -9.059  1.00 23.15  ? 162 THR B C   1 
ATOM   1176 O O   . THR A 1 175 ? -13.212 -4.098  -8.778  1.00 20.57  ? 162 THR B O   1 
ATOM   1177 C CB  . THR A 1 175 ? -12.872 -6.341  -11.189 1.00 20.14  ? 162 THR B CB  1 
ATOM   1178 O OG1 . THR A 1 175 ? -11.977 -7.282  -11.743 1.00 21.22  ? 162 THR B OG1 1 
ATOM   1179 C CG2 . THR A 1 175 ? -12.550 -4.993  -11.811 1.00 21.18  ? 162 THR B CG2 1 
ATOM   1180 N N   . ALA A 1 176 ? -14.912 -5.588  -8.792  1.00 23.74  ? 163 ALA B N   1 
ATOM   1181 C CA  . ALA A 1 176 ? -15.834 -4.703  -8.075  1.00 22.61  ? 163 ALA B CA  1 
ATOM   1182 C C   . ALA A 1 176 ? -15.269 -4.409  -6.676  1.00 22.25  ? 163 ALA B C   1 
ATOM   1183 O O   . ALA A 1 176 ? -15.250 -3.270  -6.213  1.00 20.45  ? 163 ALA B O   1 
ATOM   1184 C CB  . ALA A 1 176 ? -17.214 -5.369  -7.904  1.00 21.94  ? 163 ALA B CB  1 
ATOM   1185 N N   . LYS A 1 177 ? -14.796 -5.440  -5.989  1.00 18.32  ? 164 LYS B N   1 
ATOM   1186 C CA  . LYS A 1 177 ? -14.252 -5.177  -4.655  1.00 17.91  ? 164 LYS B CA  1 
ATOM   1187 C C   . LYS A 1 177 ? -13.041 -4.210  -4.744  1.00 19.03  ? 164 LYS B C   1 
ATOM   1188 O O   . LYS A 1 177 ? -12.948 -3.352  -3.905  1.00 19.25  ? 164 LYS B O   1 
ATOM   1189 C CB  . LYS A 1 177 ? -14.023 -6.490  -3.900  1.00 21.31  ? 164 LYS B CB  1 
ATOM   1190 C CG  . LYS A 1 177 ? -15.376 -7.206  -3.562  1.00 23.82  ? 164 LYS B CG  1 
ATOM   1191 C CD  . LYS A 1 177 ? -16.296 -6.391  -2.646  1.00 30.19  ? 164 LYS B CD  1 
ATOM   1192 C CE  . LYS A 1 177 ? -17.411 -7.232  -1.989  1.00 29.42  ? 164 LYS B CE  1 
ATOM   1193 N NZ  . LYS A 1 177 ? -18.295 -6.222  -1.360  1.00 27.19  ? 164 LYS B NZ  1 
ATOM   1194 N N   . ALA A 1 178 ? -12.099 -4.409  -5.682  1.00 18.62  ? 165 ALA B N   1 
ATOM   1195 C CA  . ALA A 1 178 ? -10.980 -3.499  -5.821  1.00 20.82  ? 165 ALA B CA  1 
ATOM   1196 C C   . ALA A 1 178 ? -11.444 -2.066  -6.130  1.00 20.02  ? 165 ALA B C   1 
ATOM   1197 O O   . ALA A 1 178 ? -10.801 -1.091  -5.714  1.00 20.52  ? 165 ALA B O   1 
ATOM   1198 C CB  . ALA A 1 178 ? -10.051 -3.980  -6.921  1.00 18.79  ? 165 ALA B CB  1 
ATOM   1199 N N   . ALA A 1 179 ? -12.513 -1.952  -6.960  1.00 20.99  ? 166 ALA B N   1 
ATOM   1200 C CA  . ALA A 1 179 ? -13.120 -0.664  -7.232  1.00 19.55  ? 166 ALA B CA  1 
ATOM   1201 C C   . ALA A 1 179 ? -13.498 0.051   -5.919  1.00 22.72  ? 166 ALA B C   1 
ATOM   1202 O O   . ALA A 1 179 ? -13.266 1.240   -5.746  1.00 20.45  ? 166 ALA B O   1 
ATOM   1203 C CB  . ALA A 1 179 ? -14.319 -0.867  -8.226  1.00 21.29  ? 166 ALA B CB  1 
ATOM   1204 N N   . LEU A 1 180 ? -14.171 -0.686  -5.023  1.00 21.39  ? 167 LEU B N   1 
ATOM   1205 C CA  . LEU A 1 180 ? -14.665 -0.079  -3.763  1.00 23.40  ? 167 LEU B CA  1 
ATOM   1206 C C   . LEU A 1 180 ? -13.497 0.363   -2.861  1.00 23.72  ? 167 LEU B C   1 
ATOM   1207 O O   . LEU A 1 180 ? -13.592 1.402   -2.181  1.00 22.26  ? 167 LEU B O   1 
ATOM   1208 C CB  . LEU A 1 180 ? -15.546 -1.094  -3.024  1.00 27.85  ? 167 LEU B CB  1 
ATOM   1209 C CG  . LEU A 1 180 ? -17.032 -1.068  -3.328  1.00 28.44  ? 167 LEU B CG  1 
ATOM   1210 C CD1 . LEU A 1 180 ? -17.678 -2.020  -2.269  1.00 25.75  ? 167 LEU B CD1 1 
ATOM   1211 C CD2 . LEU A 1 180 ? -17.608 0.340   -3.208  1.00 29.40  ? 167 LEU B CD2 1 
ATOM   1212 N N   . ASN A 1 181 ? -12.322 -0.312  -2.980  1.00 15.65  ? 168 ASN B N   1 
ATOM   1213 C CA  . ASN A 1 181 ? -11.141 0.086   -2.235  1.00 19.00  ? 168 ASN B CA  1 
ATOM   1214 C C   . ASN A 1 181 ? -10.772 1.511   -2.609  1.00 20.54  ? 168 ASN B C   1 
ATOM   1215 O O   . ASN A 1 181 ? -10.477 2.346   -1.730  1.00 21.26  ? 168 ASN B O   1 
ATOM   1216 C CB  . ASN A 1 181 ? -9.994  -0.852  -2.643  1.00 22.35  ? 168 ASN B CB  1 
ATOM   1217 C CG  . ASN A 1 181 ? -8.689  -0.450  -1.997  1.00 26.72  ? 168 ASN B CG  1 
ATOM   1218 O OD1 . ASN A 1 181 ? -8.674  -0.436  -0.759  1.00 24.83  ? 168 ASN B OD1 1 
ATOM   1219 N ND2 . ASN A 1 181 ? -7.597  -0.232  -2.771  1.00 24.61  ? 168 ASN B ND2 1 
ATOM   1220 N N   . GLY A 1 182 ? -10.827 1.812   -3.927  1.00 16.96  ? 169 GLY B N   1 
ATOM   1221 C CA  . GLY A 1 182 ? -10.472 3.136   -4.388  1.00 20.40  ? 169 GLY B CA  1 
ATOM   1222 C C   . GLY A 1 182 ? -11.578 4.128   -4.035  1.00 19.32  ? 169 GLY B C   1 
ATOM   1223 O O   . GLY A 1 182 ? -11.313 5.281   -3.613  1.00 23.07  ? 169 GLY B O   1 
ATOM   1224 N N   . MET A 1 183 ? -12.842 3.711   -4.275  1.00 17.07  ? 170 MET B N   1 
ATOM   1225 C CA  . MET A 1 183 ? -13.947 4.604   -3.956  1.00 18.59  ? 170 MET B CA  1 
ATOM   1226 C C   . MET A 1 183 ? -13.948 5.055   -2.484  1.00 19.93  ? 170 MET B C   1 
ATOM   1227 O O   . MET A 1 183 ? -14.254 6.224   -2.218  1.00 22.07  ? 170 MET B O   1 
ATOM   1228 C CB  . MET A 1 183 ? -15.270 3.949   -4.361  1.00 19.99  ? 170 MET B CB  1 
ATOM   1229 C CG  . MET A 1 183 ? -16.413 4.939   -4.351  1.00 25.04  ? 170 MET B CG  1 
ATOM   1230 S SD  . MET A 1 183 ? -18.033 4.126   -4.452  1.00 31.16  ? 170 MET B SD  1 
ATOM   1231 C CE  . MET A 1 183 ? -17.862 2.891   -5.736  1.00 31.79  ? 170 MET B CE  1 
ATOM   1232 N N   . THR A 1 184 ? -13.506 4.174   -1.557  1.00 16.48  ? 171 THR B N   1 
ATOM   1233 C CA  . THR A 1 184 ? -13.383 4.611   -0.148  1.00 19.48  ? 171 THR B CA  1 
ATOM   1234 C C   . THR A 1 184 ? -12.465 5.846   -0.040  1.00 20.43  ? 171 THR B C   1 
ATOM   1235 O O   . THR A 1 184 ? -12.804 6.785   0.678   1.00 20.23  ? 171 THR B O   1 
ATOM   1236 C CB  . THR A 1 184 ? -12.786 3.483   0.685   1.00 18.63  ? 171 THR B CB  1 
ATOM   1237 O OG1 . THR A 1 184 ? -13.830 2.490   0.721   1.00 20.96  ? 171 THR B OG1 1 
ATOM   1238 C CG2 . THR A 1 184 ? -12.539 3.859   2.135   1.00 19.52  ? 171 THR B CG2 1 
ATOM   1239 N N   . ARG A 1 185 ? -11.252 5.774   -0.662  1.00 17.90  ? 172 ARG B N   1 
ATOM   1240 C CA  . ARG A 1 185 ? -10.230 6.811   -0.512  1.00 18.22  ? 172 ARG B CA  1 
ATOM   1241 C C   . ARG A 1 185 ? -10.772 8.110   -1.101  1.00 16.95  ? 172 ARG B C   1 
ATOM   1242 O O   . ARG A 1 185 ? -10.611 9.187   -0.448  1.00 19.65  ? 172 ARG B O   1 
ATOM   1243 C CB  . ARG A 1 185 ? -8.860  6.491   -1.133  1.00 16.93  ? 172 ARG B CB  1 
ATOM   1244 C CG  . ARG A 1 185 ? -8.454  5.145   -0.485  1.00 18.03  ? 172 ARG B CG  1 
ATOM   1245 C CD  . ARG A 1 185 ? -7.254  4.498   -1.182  1.00 22.45  ? 172 ARG B CD  1 
ATOM   1246 N NE  . ARG A 1 185 ? -6.008  5.211   -1.004  1.00 23.71  ? 172 ARG B NE  1 
ATOM   1247 C CZ  . ARG A 1 185 ? -5.101  4.891   -0.090  1.00 22.84  ? 172 ARG B CZ  1 
ATOM   1248 N NH1 . ARG A 1 185 ? -5.285  3.888   0.769   1.00 25.11  ? 172 ARG B NH1 1 
ATOM   1249 N NH2 . ARG A 1 185 ? -3.997  5.633   0.031   1.00 22.06  ? 172 ARG B NH2 1 
ATOM   1250 N N   . THR A 1 186 ? -11.360 8.075   -2.333  1.00 16.95  ? 173 THR B N   1 
ATOM   1251 C CA  . THR A 1 186 ? -11.730 9.380   -2.938  1.00 20.43  ? 173 THR B CA  1 
ATOM   1252 C C   . THR A 1 186 ? -13.003 9.974   -2.274  1.00 20.89  ? 173 THR B C   1 
ATOM   1253 O O   . THR A 1 186 ? -13.064 11.172  -2.061  1.00 22.25  ? 173 THR B O   1 
ATOM   1254 C CB  . THR A 1 186 ? -11.900 9.427   -4.472  1.00 22.06  ? 173 THR B CB  1 
ATOM   1255 O OG1 . THR A 1 186 ? -12.959 8.482   -4.712  1.00 23.54  ? 173 THR B OG1 1 
ATOM   1256 C CG2 . THR A 1 186 ? -10.684 8.811   -5.151  1.00 19.17  ? 173 THR B CG2 1 
ATOM   1257 N N   . LEU A 1 187 ? -13.956 9.103   -1.858  1.00 19.24  ? 174 LEU B N   1 
ATOM   1258 C CA  . LEU A 1 187 ? -15.131 9.692   -1.227  1.00 27.11  ? 174 LEU B CA  1 
ATOM   1259 C C   . LEU A 1 187 ? -14.714 10.227  0.153   1.00 22.91  ? 174 LEU B C   1 
ATOM   1260 O O   . LEU A 1 187 ? -15.330 11.217  0.589   1.00 21.03  ? 174 LEU B O   1 
ATOM   1261 C CB  . LEU A 1 187 ? -16.218 8.634   -1.058  1.00 28.52  ? 174 LEU B CB  1 
ATOM   1262 C CG  . LEU A 1 187 ? -17.275 8.625   -2.162  1.00 33.08  ? 174 LEU B CG  1 
ATOM   1263 C CD1 . LEU A 1 187 ? -16.600 8.470   -3.484  1.00 41.34  ? 174 LEU B CD1 1 
ATOM   1264 C CD2 . LEU A 1 187 ? -18.148 7.449   -1.879  1.00 32.59  ? 174 LEU B CD2 1 
ATOM   1265 N N   . ALA A 1 188 ? -13.680 9.599   0.790   1.00 20.66  ? 175 ALA B N   1 
ATOM   1266 C CA  . ALA A 1 188 ? -13.244 10.144  2.079   1.00 19.87  ? 175 ALA B CA  1 
ATOM   1267 C C   . ALA A 1 188 ? -12.798 11.605  1.978   1.00 22.64  ? 175 ALA B C   1 
ATOM   1268 O O   . ALA A 1 188 ? -13.172 12.451  2.829   1.00 23.63  ? 175 ALA B O   1 
ATOM   1269 C CB  . ALA A 1 188 ? -12.212 9.159   2.710   1.00 19.28  ? 175 ALA B CB  1 
ATOM   1270 N N   . ARG A 1 189 ? -12.087 11.967  0.879   1.00 20.84  ? 176 ARG B N   1 
ATOM   1271 C CA  . ARG A 1 189 ? -11.720 13.376  0.618   1.00 22.66  ? 176 ARG B CA  1 
ATOM   1272 C C   . ARG A 1 189 ? -12.960 14.174  0.238   1.00 23.42  ? 176 ARG B C   1 
ATOM   1273 O O   . ARG A 1 189 ? -13.117 15.350  0.672   1.00 26.65  ? 176 ARG B O   1 
ATOM   1274 C CB  . ARG A 1 189 ? -10.572 13.369  -0.431  1.00 22.72  ? 176 ARG B CB  1 
ATOM   1275 C CG  . ARG A 1 189 ? -10.212 14.813  -0.802  1.00 29.48  ? 176 ARG B CG  1 
ATOM   1276 C CD  . ARG A 1 189 ? -9.499  15.643  0.270   1.00 26.90  ? 176 ARG B CD  1 
ATOM   1277 N NE  . ARG A 1 189 ? -8.263  15.003  0.757   1.00 28.02  ? 176 ARG B NE  1 
ATOM   1278 C CZ  . ARG A 1 189 ? -7.525  15.470  1.771   1.00 27.85  ? 176 ARG B CZ  1 
ATOM   1279 N NH1 . ARG A 1 189 ? -7.901  16.616  2.380   1.00 25.52  ? 176 ARG B NH1 1 
ATOM   1280 N NH2 . ARG A 1 189 ? -6.349  14.869  2.059   1.00 23.12  ? 176 ARG B NH2 1 
ATOM   1281 N N   . GLU A 1 190 ? -13.789 13.602  -0.644  1.00 23.27  ? 177 GLU B N   1 
ATOM   1282 C CA  . GLU A 1 190 ? -14.912 14.363  -1.205  1.00 26.43  ? 177 GLU B CA  1 
ATOM   1283 C C   . GLU A 1 190 ? -15.877 14.769  -0.088  1.00 27.67  ? 177 GLU B C   1 
ATOM   1284 O O   . GLU A 1 190 ? -16.407 15.848  -0.168  1.00 27.55  ? 177 GLU B O   1 
ATOM   1285 C CB  . GLU A 1 190 ? -15.795 13.364  -1.965  1.00 30.19  ? 177 GLU B CB  1 
ATOM   1286 C CG  . GLU A 1 190 ? -16.549 13.900  -3.168  1.00 52.68  ? 177 GLU B CG  1 
ATOM   1287 C CD  . GLU A 1 190 ? -15.892 14.033  -4.533  1.00 46.72  ? 177 GLU B CD  1 
ATOM   1288 O OE1 . GLU A 1 190 ? -15.510 13.223  -5.446  1.00 31.38  ? 177 GLU B OE1 1 
ATOM   1289 O OE2 . GLU A 1 190 ? -15.829 15.231  -4.598  1.00 39.00  ? 177 GLU B OE2 1 
ATOM   1290 N N   . LEU A 1 191 ? -16.046 13.914  0.967   1.00 27.48  ? 178 LEU B N   1 
ATOM   1291 C CA  . LEU A 1 191 ? -17.147 14.165  1.916   1.00 25.97  ? 178 LEU B CA  1 
ATOM   1292 C C   . LEU A 1 191 ? -16.615 14.532  3.307   1.00 26.85  ? 178 LEU B C   1 
ATOM   1293 O O   . LEU A 1 191 ? -17.433 14.885  4.167   1.00 25.27  ? 178 LEU B O   1 
ATOM   1294 C CB  . LEU A 1 191 ? -18.006 12.890  1.996   1.00 25.65  ? 178 LEU B CB  1 
ATOM   1295 C CG  . LEU A 1 191 ? -18.731 12.485  0.692   1.00 25.74  ? 178 LEU B CG  1 
ATOM   1296 C CD1 . LEU A 1 191 ? -19.494 11.199  0.948   1.00 27.97  ? 178 LEU B CD1 1 
ATOM   1297 C CD2 . LEU A 1 191 ? -19.589 13.537  -0.003  1.00 28.26  ? 178 LEU B CD2 1 
ATOM   1298 N N   . GLY A 1 192 ? -15.288 14.359  3.544   1.00 24.17  ? 179 GLY B N   1 
ATOM   1299 C CA  . GLY A 1 192 ? -14.736 14.544  4.888   1.00 24.89  ? 179 GLY B CA  1 
ATOM   1300 C C   . GLY A 1 192 ? -15.054 15.949  5.420   1.00 24.55  ? 179 GLY B C   1 
ATOM   1301 O O   . GLY A 1 192 ? -15.286 16.128  6.634   1.00 24.51  ? 179 GLY B O   1 
ATOM   1302 N N   . GLY A 1 193 ? -14.996 16.958  4.531   1.00 24.73  ? 180 GLY B N   1 
ATOM   1303 C CA  . GLY A 1 193 ? -15.196 18.317  5.037   1.00 27.54  ? 180 GLY B CA  1 
ATOM   1304 C C   . GLY A 1 193 ? -16.633 18.503  5.480   1.00 29.12  ? 180 GLY B C   1 
ATOM   1305 O O   . GLY A 1 193 ? -16.959 19.465  6.170   1.00 32.83  ? 180 GLY B O   1 
ATOM   1306 N N   . GLN A 1 194 ? -17.537 17.622  5.052   1.00 32.74  ? 181 GLN B N   1 
ATOM   1307 C CA  . GLN A 1 194 ? -18.908 17.724  5.544   1.00 33.75  ? 181 GLN B CA  1 
ATOM   1308 C C   . GLN A 1 194 ? -19.120 16.888  6.815   1.00 32.89  ? 181 GLN B C   1 
ATOM   1309 O O   . GLN A 1 194 ? -20.270 16.771  7.251   1.00 32.33  ? 181 GLN B O   1 
ATOM   1310 C CB  . GLN A 1 194 ? -19.936 17.286  4.505   1.00 38.54  ? 181 GLN B CB  1 
ATOM   1311 C CG  . GLN A 1 194 ? -19.993 18.123  3.222   1.00 54.69  ? 181 GLN B CG  1 
ATOM   1312 C CD  . GLN A 1 194 ? -20.318 17.306  1.976   1.00 69.67  ? 181 GLN B CD  1 
ATOM   1313 O OE1 . GLN A 1 194 ? -21.465 16.918  1.704   1.00 79.15  ? 181 GLN B OE1 1 
ATOM   1314 N NE2 . GLN A 1 194 ? -19.302 17.048  1.165   1.00 74.38  ? 181 GLN B NE2 1 
ATOM   1315 N N   . GLY A 1 195 ? -18.039 16.317  7.383   1.00 27.78  ? 182 GLY B N   1 
ATOM   1316 C CA  . GLY A 1 195 ? -18.123 15.539  8.614   1.00 28.75  ? 182 GLY B CA  1 
ATOM   1317 C C   . GLY A 1 195 ? -18.404 14.056  8.405   1.00 27.23  ? 182 GLY B C   1 
ATOM   1318 O O   . GLY A 1 195 ? -18.656 13.355  9.395   1.00 24.12  ? 182 GLY B O   1 
ATOM   1319 N N   . ILE A 1 196 ? -18.263 13.537  7.173   1.00 24.90  ? 183 ILE B N   1 
ATOM   1320 C CA  . ILE A 1 196 ? -18.565 12.139  6.918   1.00 24.86  ? 183 ILE B CA  1 
ATOM   1321 C C   . ILE A 1 196 ? -17.239 11.389  6.755   1.00 24.54  ? 183 ILE B C   1 
ATOM   1322 O O   . ILE A 1 196 ? -16.394 11.800  5.983   1.00 23.08  ? 183 ILE B O   1 
ATOM   1323 C CB  . ILE A 1 196 ? -19.426 11.995  5.626   1.00 24.48  ? 183 ILE B CB  1 
ATOM   1324 C CG1 . ILE A 1 196 ? -20.732 12.782  5.728   1.00 24.74  ? 183 ILE B CG1 1 
ATOM   1325 C CG2 . ILE A 1 196 ? -19.700 10.517  5.246   1.00 23.91  ? 183 ILE B CG2 1 
ATOM   1326 C CD1 . ILE A 1 196 ? -21.283 13.108  4.338   1.00 28.45  ? 183 ILE B CD1 1 
ATOM   1327 N N   . ARG A 1 197 ? -17.125 10.247  7.436   1.00 21.46  ? 184 ARG B N   1 
ATOM   1328 C CA  . ARG A 1 197 ? -15.954 9.418   7.352   1.00 22.32  ? 184 ARG B CA  1 
ATOM   1329 C C   . ARG A 1 197 ? -16.376 8.162   6.592   1.00 23.83  ? 184 ARG B C   1 
ATOM   1330 O O   . ARG A 1 197 ? -17.524 7.742   6.641   1.00 21.51  ? 184 ARG B O   1 
ATOM   1331 C CB  . ARG A 1 197 ? -15.374 9.191   8.753   1.00 27.51  ? 184 ARG B CB  1 
ATOM   1332 C CG  . ARG A 1 197 ? -16.101 8.287   9.698   1.00 29.54  ? 184 ARG B CG  1 
ATOM   1333 C CD  . ARG A 1 197 ? -15.566 8.543   11.122  1.00 32.33  ? 184 ARG B CD  1 
ATOM   1334 N NE  . ARG A 1 197 ? -16.028 7.349   11.832  1.00 33.28  ? 184 ARG B NE  1 
ATOM   1335 C CZ  . ARG A 1 197 ? -17.096 7.417   12.599  1.00 30.16  ? 184 ARG B CZ  1 
ATOM   1336 N NH1 . ARG A 1 197 ? -17.814 8.525   12.640  1.00 30.77  ? 184 ARG B NH1 1 
ATOM   1337 N NH2 . ARG A 1 197 ? -17.397 6.427   13.407  1.00 32.30  ? 184 ARG B NH2 1 
ATOM   1338 N N   . ILE A 1 198 ? -15.470 7.666   5.746   1.00 21.84  ? 185 ILE B N   1 
ATOM   1339 C CA  . ILE A 1 198 ? -15.792 6.507   4.920   1.00 20.01  ? 185 ILE B CA  1 
ATOM   1340 C C   . ILE A 1 198 ? -14.600 5.572   5.071   1.00 17.41  ? 185 ILE B C   1 
ATOM   1341 O O   . ILE A 1 198 ? -13.465 6.054   4.869   1.00 18.60  ? 185 ILE B O   1 
ATOM   1342 C CB  . ILE A 1 198 ? -15.969 6.963   3.455   1.00 21.52  ? 185 ILE B CB  1 
ATOM   1343 C CG1 . ILE A 1 198 ? -17.123 7.980   3.384   1.00 30.65  ? 185 ILE B CG1 1 
ATOM   1344 C CG2 . ILE A 1 198 ? -16.305 5.728   2.598   1.00 26.59  ? 185 ILE B CG2 1 
ATOM   1345 C CD1 . ILE A 1 198 ? -16.733 9.455   3.499   1.00 30.44  ? 185 ILE B CD1 1 
ATOM   1346 N N   . ASN A 1 199 ? -14.845 4.276   5.385   1.00 16.00  ? 186 ASN B N   1 
ATOM   1347 C CA  . ASN A 1 199 ? -13.736 3.355   5.507   1.00 15.39  ? 186 ASN B CA  1 
ATOM   1348 C C   . ASN A 1 199 ? -14.196 2.039   4.899   1.00 17.61  ? 186 ASN B C   1 
ATOM   1349 O O   . ASN A 1 199 ? -15.378 1.882   4.642   1.00 18.77  ? 186 ASN B O   1 
ATOM   1350 C CB  . ASN A 1 199 ? -13.398 3.068   7.012   1.00 17.50  ? 186 ASN B CB  1 
ATOM   1351 C CG  . ASN A 1 199 ? -12.806 4.279   7.716   1.00 16.02  ? 186 ASN B CG  1 
ATOM   1352 O OD1 . ASN A 1 199 ? -11.680 4.704   7.405   1.00 16.57  ? 186 ASN B OD1 1 
ATOM   1353 N ND2 . ASN A 1 199 ? -13.625 4.915   8.535   1.00 15.91  ? 186 ASN B ND2 1 
ATOM   1354 N N   . SER A 1 200 ? -13.307 1.136   4.628   1.00 15.62  ? 187 SER B N   1 
ATOM   1355 C CA  A SER A 1 200 ? -13.708 -0.168  4.131   0.50 16.01  ? 187 SER B CA  1 
ATOM   1356 C CA  B SER A 1 200 ? -13.682 -0.167  4.109   0.50 16.23  ? 187 SER B CA  1 
ATOM   1357 C C   . SER A 1 200 ? -13.419 -1.238  5.175   1.00 16.55  ? 187 SER B C   1 
ATOM   1358 O O   . SER A 1 200 ? -12.321 -1.292  5.748   1.00 15.97  ? 187 SER B O   1 
ATOM   1359 C CB  A SER A 1 200 ? -12.932 -0.541  2.871   0.50 17.27  ? 187 SER B CB  1 
ATOM   1360 C CB  B SER A 1 200 ? -12.842 -0.531  2.853   0.50 17.44  ? 187 SER B CB  1 
ATOM   1361 O OG  A SER A 1 200 ? -13.434 -1.747  2.292   0.50 16.36  ? 187 SER B OG  1 
ATOM   1362 O OG  B SER A 1 200 ? -12.822 0.357   1.720   0.50 17.47  ? 187 SER B OG  1 
ATOM   1363 N N   . LEU A 1 201 ? -14.407 -2.125  5.385   1.00 16.10  ? 188 LEU B N   1 
ATOM   1364 C CA  . LEU A 1 201 ? -14.303 -3.266  6.282   1.00 18.65  ? 188 LEU B CA  1 
ATOM   1365 C C   . LEU A 1 201 ? -13.960 -4.439  5.356   1.00 18.61  ? 188 LEU B C   1 
ATOM   1366 O O   . LEU A 1 201 ? -14.720 -4.712  4.426   1.00 19.53  ? 188 LEU B O   1 
ATOM   1367 C CB  . LEU A 1 201 ? -15.640 -3.430  7.006   1.00 16.94  ? 188 LEU B CB  1 
ATOM   1368 C CG  . LEU A 1 201 ? -15.739 -4.428  8.166   1.00 17.68  ? 188 LEU B CG  1 
ATOM   1369 C CD1 . LEU A 1 201 ? -17.063 -4.196  8.971   1.00 17.97  ? 188 LEU B CD1 1 
ATOM   1370 C CD2 . LEU A 1 201 ? -15.521 -5.833  7.594   1.00 20.53  ? 188 LEU B CD2 1 
ATOM   1371 N N   . VAL A 1 202 ? -12.810 -5.094  5.594   1.00 17.17  ? 189 VAL B N   1 
ATOM   1372 C CA  . VAL A 1 202 ? -12.333 -6.032  4.561   1.00 16.68  ? 189 VAL B CA  1 
ATOM   1373 C C   . VAL A 1 202 ? -12.197 -7.413  5.236   1.00 19.09  ? 189 VAL B C   1 
ATOM   1374 O O   . VAL A 1 202 ? -11.245 -7.681  5.982   1.00 19.81  ? 189 VAL B O   1 
ATOM   1375 C CB  . VAL A 1 202 ? -10.965 -5.569  4.026   1.00 17.82  ? 189 VAL B CB  1 
ATOM   1376 C CG1 . VAL A 1 202 ? -10.492 -6.524  2.928   1.00 18.06  ? 189 VAL B CG1 1 
ATOM   1377 C CG2 . VAL A 1 202 ? -10.960 -4.146  3.490   1.00 15.14  ? 189 VAL B CG2 1 
ATOM   1378 N N   . PRO A 1 203 ? -13.175 -8.297  5.081   1.00 19.89  ? 190 PRO B N   1 
ATOM   1379 C CA  . PRO A 1 203 ? -13.149 -9.613  5.699   1.00 22.79  ? 190 PRO B CA  1 
ATOM   1380 C C   . PRO A 1 203 ? -12.264 -10.615 4.982   1.00 23.27  ? 190 PRO B C   1 
ATOM   1381 O O   . PRO A 1 203 ? -12.066 -10.557 3.741   1.00 23.26  ? 190 PRO B O   1 
ATOM   1382 C CB  . PRO A 1 203 ? -14.618 -10.094 5.729   1.00 23.14  ? 190 PRO B CB  1 
ATOM   1383 C CG  . PRO A 1 203 ? -15.381 -8.898  5.163   1.00 24.65  ? 190 PRO B CG  1 
ATOM   1384 C CD  . PRO A 1 203 ? -14.475 -7.949  4.470   1.00 20.59  ? 190 PRO B CD  1 
ATOM   1385 N N   . GLY A 1 204 ? -11.884 -11.639 5.757   1.00 23.22  ? 191 GLY B N   1 
ATOM   1386 C CA  . GLY A 1 204 ? -11.172 -12.785 5.211   1.00 25.03  ? 191 GLY B CA  1 
ATOM   1387 C C   . GLY A 1 204 ? -12.199 -13.833 4.820   1.00 25.64  ? 191 GLY B C   1 
ATOM   1388 O O   . GLY A 1 204 ? -13.243 -13.500 4.284   1.00 24.48  ? 191 GLY B O   1 
ATOM   1389 N N   . ALA A 1 205 ? -11.850 -15.093 5.038   1.00 25.21  ? 192 ALA B N   1 
ATOM   1390 C CA  . ALA A 1 205 ? -12.768 -16.169 4.782   1.00 24.54  ? 192 ALA B CA  1 
ATOM   1391 C C   . ALA A 1 205 ? -13.701 -16.421 5.970   1.00 29.15  ? 192 ALA B C   1 
ATOM   1392 O O   . ALA A 1 205 ? -13.400 -17.172 6.932   1.00 30.16  ? 192 ALA B O   1 
ATOM   1393 C CB  . ALA A 1 205 ? -11.915 -17.362 4.419   1.00 27.13  ? 192 ALA B CB  1 
ATOM   1394 N N   . ILE A 1 206 ? -14.918 -15.877 5.821   1.00 28.65  ? 193 ILE B N   1 
ATOM   1395 C CA  . ILE A 1 206 ? -15.944 -15.898 6.844   1.00 30.22  ? 193 ILE B CA  1 
ATOM   1396 C C   . ILE A 1 206 ? -16.817 -17.142 6.700   1.00 32.51  ? 193 ILE B C   1 
ATOM   1397 O O   . ILE A 1 206 ? -17.437 -17.357 5.650   1.00 31.32  ? 193 ILE B O   1 
ATOM   1398 C CB  . ILE A 1 206 ? -16.728 -14.574 6.840   1.00 26.50  ? 193 ILE B CB  1 
ATOM   1399 C CG1 . ILE A 1 206 ? -15.821 -13.336 6.826   1.00 25.28  ? 193 ILE B CG1 1 
ATOM   1400 C CG2 . ILE A 1 206 ? -17.752 -14.567 7.996   1.00 27.11  ? 193 ILE B CG2 1 
ATOM   1401 C CD1 . ILE A 1 206 ? -14.816 -13.290 8.001   1.00 24.26  ? 193 ILE B CD1 1 
ATOM   1402 N N   . ARG A 1 207 ? -16.886 -17.986 7.739   1.00 32.69  ? 194 ARG B N   1 
ATOM   1403 C CA  . ARG A 1 207 ? -17.817 -19.140 7.727   1.00 38.38  ? 194 ARG B CA  1 
ATOM   1404 C C   . ARG A 1 207 ? -19.252 -18.609 7.853   1.00 38.44  ? 194 ARG B C   1 
ATOM   1405 O O   . ARG A 1 207 ? -19.486 -17.706 8.670   1.00 38.19  ? 194 ARG B O   1 
ATOM   1406 C CB  . ARG A 1 207 ? -17.526 -20.150 8.848   1.00 41.77  ? 194 ARG B CB  1 
ATOM   1407 C CG  . ARG A 1 207 ? -18.444 -21.374 8.962   1.00 44.89  ? 194 ARG B CG  1 
ATOM   1408 C CD  . ARG A 1 207 ? -17.952 -22.476 9.879   1.00 51.04  ? 194 ARG B CD  1 
ATOM   1409 N NE  . ARG A 1 207 ? -17.453 -22.153 11.226  1.00 60.61  ? 194 ARG B NE  1 
ATOM   1410 C CZ  . ARG A 1 207 ? -16.825 -23.017 12.088  1.00 63.87  ? 194 ARG B CZ  1 
ATOM   1411 N NH1 . ARG A 1 207 ? -16.441 -24.236 11.731  1.00 66.93  ? 194 ARG B NH1 1 
ATOM   1412 N NH2 . ARG A 1 207 ? -16.517 -22.641 13.312  1.00 59.67  ? 194 ARG B NH2 1 
ATOM   1413 N N   . THR A 1 208 ? -20.137 -18.981 6.908   1.00 42.21  ? 195 THR B N   1 
ATOM   1414 C CA  . THR A 1 208 ? -21.563 -18.614 6.959   1.00 45.81  ? 195 THR B CA  1 
ATOM   1415 C C   . THR A 1 208 ? -22.428 -19.856 6.658   1.00 52.08  ? 195 THR B C   1 
ATOM   1416 O O   . THR A 1 208 ? -21.951 -20.754 5.962   1.00 49.17  ? 195 THR B O   1 
ATOM   1417 C CB  . THR A 1 208 ? -21.922 -17.484 5.984   1.00 46.00  ? 195 THR B CB  1 
ATOM   1418 O OG1 . THR A 1 208 ? -21.776 -17.975 4.650   1.00 50.20  ? 195 THR B OG1 1 
ATOM   1419 C CG2 . THR A 1 208 ? -21.118 -16.206 6.189   1.00 40.18  ? 195 THR B CG2 1 
ATOM   1420 N N   . GLU A 1 209 ? -23.694 -19.864 7.127   1.00 59.75  ? 196 GLU B N   1 
ATOM   1421 C CA  . GLU A 1 209 ? -24.646 -20.959 6.832   1.00 63.99  ? 196 GLU B CA  1 
ATOM   1422 C C   . GLU A 1 209 ? -24.904 -21.129 5.325   1.00 66.38  ? 196 GLU B C   1 
ATOM   1423 O O   . GLU A 1 209 ? -25.189 -22.253 4.900   1.00 72.98  ? 196 GLU B O   1 
ATOM   1424 C CB  . GLU A 1 209 ? -25.912 -21.010 7.691   1.00 58.36  ? 196 GLU B CB  1 
ATOM   1425 N N   . ARG A 1 210 ? -24.751 -20.045 4.526   1.00 60.36  ? 197 ARG B N   1 
ATOM   1426 C CA  . ARG A 1 210 ? -24.890 -20.019 3.067   1.00 60.28  ? 197 ARG B CA  1 
ATOM   1427 C C   . ARG A 1 210 ? -23.694 -20.663 2.354   1.00 66.31  ? 197 ARG B C   1 
ATOM   1428 O O   . ARG A 1 210 ? -23.911 -21.449 1.433   1.00 71.93  ? 197 ARG B O   1 
ATOM   1429 C CB  . ARG A 1 210 ? -25.103 -18.608 2.495   1.00 55.63  ? 197 ARG B CB  1 
ATOM   1430 N N   . GLN A 1 211 ? -22.442 -20.315 2.745   1.00 70.42  ? 198 GLN B N   1 
ATOM   1431 C CA  . GLN A 1 211 ? -21.226 -20.969 2.247   1.00 74.57  ? 198 GLN B CA  1 
ATOM   1432 C C   . GLN A 1 211 ? -21.238 -22.463 2.604   1.00 85.18  ? 198 GLN B C   1 
ATOM   1433 O O   . GLN A 1 211 ? -20.745 -23.292 1.831   1.00 92.12  ? 198 GLN B O   1 
ATOM   1434 C CB  . GLN A 1 211 ? -19.909 -20.241 2.566   1.00 67.78  ? 198 GLN B CB  1 
ATOM   1435 N N   . ASP A 1 212 ? -21.879 -22.803 3.738   1.00 92.54  ? 199 ASP B N   1 
ATOM   1436 C CA  . ASP A 1 212 ? -21.933 -24.159 4.284   1.00 98.73  ? 199 ASP B CA  1 
ATOM   1437 C C   . ASP A 1 212 ? -23.076 -24.968 3.638   1.00 103.16 ? 199 ASP B C   1 
ATOM   1438 O O   . ASP A 1 212 ? -22.941 -26.183 3.452   1.00 100.06 ? 199 ASP B O   1 
ATOM   1439 C CB  . ASP A 1 212 ? -21.981 -24.190 5.816   1.00 88.56  ? 199 ASP B CB  1 
ATOM   1440 C CG  . ASP A 1 212 ? -20.758 -23.765 6.643   1.00 81.12  ? 199 ASP B CG  1 
ATOM   1441 O OD1 . ASP A 1 212 ? -19.743 -23.296 6.083   1.00 72.89  ? 199 ASP B OD1 1 
ATOM   1442 O OD2 . ASP A 1 212 ? -20.831 -23.871 7.884   1.00 79.29  ? 199 ASP B OD2 1 
ATOM   1443 N N   . ALA A 1 213 ? -24.199 -24.313 3.286   1.00 99.70  ? 200 ALA B N   1 
ATOM   1444 C CA  . ALA A 1 213 ? -25.297 -24.997 2.609   1.00 92.87  ? 200 ALA B CA  1 
ATOM   1445 C C   . ALA A 1 213 ? -24.830 -25.590 1.273   1.00 98.48  ? 200 ALA B C   1 
ATOM   1446 O O   . ALA A 1 213 ? -25.426 -26.550 0.796   1.00 95.58  ? 200 ALA B O   1 
ATOM   1447 C CB  . ALA A 1 213 ? -26.477 -24.065 2.431   1.00 82.20  ? 200 ALA B CB  1 
ATOM   1448 N N   . MET A 1 214 ? -23.733 -25.039 0.716   1.00 100.57 ? 201 MET B N   1 
ATOM   1449 C CA  . MET A 1 214 ? -23.212 -25.306 -0.622  1.00 96.40  ? 201 MET B CA  1 
ATOM   1450 C C   . MET A 1 214 ? -22.488 -26.659 -0.730  1.00 100.64 ? 201 MET B C   1 
ATOM   1451 O O   . MET A 1 214 ? -22.078 -27.033 -1.836  1.00 90.58  ? 201 MET B O   1 
ATOM   1452 C CB  . MET A 1 214 ? -22.295 -24.163 -1.083  1.00 85.12  ? 201 MET B CB  1 
ATOM   1453 N N   . TRP A 1 215 ? -22.356 -27.398 0.392   1.00 104.35 ? 202 TRP B N   1 
ATOM   1454 C CA  . TRP A 1 215 ? -21.622 -28.664 0.475   1.00 105.83 ? 202 TRP B CA  1 
ATOM   1455 C C   . TRP A 1 215 ? -22.430 -29.753 1.210   1.00 110.47 ? 202 TRP B C   1 
ATOM   1456 O O   . TRP A 1 215 ? -21.822 -30.704 1.709   1.00 108.48 ? 202 TRP B O   1 
ATOM   1457 C CB  . TRP A 1 215 ? -20.278 -28.515 1.224   1.00 107.25 ? 202 TRP B CB  1 
ATOM   1458 C CG  . TRP A 1 215 ? -19.192 -27.591 0.719   1.00 105.06 ? 202 TRP B CG  1 
ATOM   1459 C CD1 . TRP A 1 215 ? -19.098 -26.247 0.957   1.00 100.34 ? 202 TRP B CD1 1 
ATOM   1460 C CD2 . TRP A 1 215 ? -17.966 -27.957 0.024   1.00 106.38 ? 202 TRP B CD2 1 
ATOM   1461 N NE1 . TRP A 1 215 ? -17.947 -25.736 0.411   1.00 93.97  ? 202 TRP B NE1 1 
ATOM   1462 C CE2 . TRP A 1 215 ? -17.224 -26.758 -0.158  1.00 101.51 ? 202 TRP B CE2 1 
ATOM   1463 C CE3 . TRP A 1 215 ? -17.431 -29.159 -0.486  1.00 103.38 ? 202 TRP B CE3 1 
ATOM   1464 C CZ2 . TRP A 1 215 ? -15.988 -26.740 -0.816  1.00 95.92  ? 202 TRP B CZ2 1 
ATOM   1465 C CZ3 . TRP A 1 215 ? -16.211 -29.138 -1.138  1.00 96.23  ? 202 TRP B CZ3 1 
ATOM   1466 C CH2 . TRP A 1 215 ? -15.496 -27.943 -1.289  1.00 94.19  ? 202 TRP B CH2 1 
ATOM   1467 N N   . ALA A 1 216 ? -23.773 -29.633 1.287   1.00 106.09 ? 203 ALA B N   1 
ATOM   1468 C CA  . ALA A 1 216 ? -24.590 -30.389 2.242   1.00 92.98  ? 203 ALA B CA  1 
ATOM   1469 C C   . ALA A 1 216 ? -24.566 -31.894 1.990   1.00 95.60  ? 203 ALA B C   1 
ATOM   1470 O O   . ALA A 1 216 ? -25.229 -32.637 2.717   1.00 95.34  ? 203 ALA B O   1 
ATOM   1471 C CB  . ALA A 1 216 ? -26.014 -29.875 2.315   1.00 86.71  ? 203 ALA B CB  1 
ATOM   1472 N N   . ALA A 1 217 ? -23.787 -32.328 0.984   1.00 95.04  ? 204 ALA B N   1 
ATOM   1473 C CA  . ALA A 1 217 ? -23.667 -33.725 0.598   1.00 93.80  ? 204 ALA B CA  1 
ATOM   1474 C C   . ALA A 1 217 ? -22.198 -34.165 0.541   1.00 88.62  ? 204 ALA B C   1 
ATOM   1475 O O   . ALA A 1 217 ? -21.910 -35.282 0.098   1.00 82.16  ? 204 ALA B O   1 
ATOM   1476 C CB  . ALA A 1 217 ? -24.378 -33.945 -0.722  1.00 94.64  ? 204 ALA B CB  1 
ATOM   1477 N N   . ASP A 1 218 ? -21.294 -33.284 0.991   1.00 80.48  ? 205 ASP B N   1 
ATOM   1478 C CA  . ASP A 1 218 ? -19.858 -33.509 1.007   1.00 79.30  ? 205 ASP B CA  1 
ATOM   1479 C C   . ASP A 1 218 ? -19.273 -32.940 2.311   1.00 73.30  ? 205 ASP B C   1 
ATOM   1480 O O   . ASP A 1 218 ? -18.524 -31.922 2.293   1.00 68.37  ? 205 ASP B O   1 
ATOM   1481 C CB  . ASP A 1 218 ? -19.208 -32.931 -0.242  1.00 83.74  ? 205 ASP B CB  1 
ATOM   1482 C CG  . ASP A 1 218 ? -17.713 -33.170 -0.421  1.00 87.04  ? 205 ASP B CG  1 
ATOM   1483 O OD1 . ASP A 1 218 ? -17.177 -34.113 0.219   1.00 92.73  ? 205 ASP B OD1 1 
ATOM   1484 O OD2 . ASP A 1 218 ? -17.093 -32.401 -1.196  1.00 80.03  ? 205 ASP B OD2 1 
ATOM   1485 N N   . PRO A 1 219 ? -19.507 -33.622 3.473   1.00 68.71  ? 206 PRO B N   1 
ATOM   1486 C CA  . PRO A 1 219 ? -19.086 -33.063 4.762   1.00 63.77  ? 206 PRO B CA  1 
ATOM   1487 C C   . PRO A 1 219 ? -17.566 -33.097 4.875   1.00 61.38  ? 206 PRO B C   1 
ATOM   1488 O O   . PRO A 1 219 ? -16.947 -32.182 5.411   1.00 56.70  ? 206 PRO B O   1 
ATOM   1489 C CB  . PRO A 1 219 ? -19.752 -33.963 5.816   1.00 67.33  ? 206 PRO B CB  1 
ATOM   1490 C CG  . PRO A 1 219 ? -20.102 -35.290 5.063   1.00 72.43  ? 206 PRO B CG  1 
ATOM   1491 C CD  . PRO A 1 219 ? -19.978 -35.027 3.569   1.00 72.11  ? 206 PRO B CD  1 
ATOM   1492 N N   . ALA A 1 220 ? -16.982 -34.162 4.284   1.00 62.73  ? 207 ALA B N   1 
ATOM   1493 C CA  . ALA A 1 220 ? -15.541 -34.323 4.165   1.00 60.92  ? 207 ALA B CA  1 
ATOM   1494 C C   . ALA A 1 220 ? -14.942 -33.101 3.464   1.00 57.90  ? 207 ALA B C   1 
ATOM   1495 O O   . ALA A 1 220 ? -13.945 -32.543 3.950   1.00 54.78  ? 207 ALA B O   1 
ATOM   1496 C CB  . ALA A 1 220 ? -15.219 -35.624 3.465   1.00 63.66  ? 207 ALA B CB  1 
ATOM   1497 N N   . GLY A 1 221 ? -15.597 -32.689 2.362   1.00 57.94  ? 208 GLY B N   1 
ATOM   1498 C CA  . GLY A 1 221 ? -15.087 -31.646 1.484   1.00 54.90  ? 208 GLY B CA  1 
ATOM   1499 C C   . GLY A 1 221 ? -15.147 -30.305 2.199   1.00 52.25  ? 208 GLY B C   1 
ATOM   1500 O O   . GLY A 1 221 ? -14.202 -29.482 2.112   1.00 52.12  ? 208 GLY B O   1 
ATOM   1501 N N   . LEU A 1 222 ? -16.276 -30.087 2.888   1.00 52.63  ? 209 LEU B N   1 
ATOM   1502 C CA  . LEU A 1 222 ? -16.453 -28.861 3.669   1.00 53.83  ? 209 LEU B CA  1 
ATOM   1503 C C   . LEU A 1 222 ? -15.312 -28.707 4.689   1.00 51.32  ? 209 LEU B C   1 
ATOM   1504 O O   . LEU A 1 222 ? -14.678 -27.645 4.750   1.00 49.10  ? 209 LEU B O   1 
ATOM   1505 C CB  . LEU A 1 222 ? -17.831 -28.828 4.333   1.00 59.02  ? 209 LEU B CB  1 
ATOM   1506 C CG  . LEU A 1 222 ? -18.188 -27.521 5.072   1.00 61.78  ? 209 LEU B CG  1 
ATOM   1507 C CD1 . LEU A 1 222 ? -19.682 -27.508 5.377   1.00 64.24  ? 209 LEU B CD1 1 
ATOM   1508 C CD2 . LEU A 1 222 ? -17.458 -27.178 6.375   1.00 64.20  ? 209 LEU B CD2 1 
ATOM   1509 N N   . GLU A 1 223 ? -15.085 -29.801 5.466   1.00 50.98  ? 210 GLU B N   1 
ATOM   1510 C CA  . GLU A 1 223 ? -14.160 -29.831 6.605   1.00 49.41  ? 210 GLU B CA  1 
ATOM   1511 C C   . GLU A 1 223 ? -12.724 -29.607 6.101   1.00 44.18  ? 210 GLU B C   1 
ATOM   1512 O O   . GLU A 1 223 ? -11.917 -28.890 6.716   1.00 41.68  ? 210 GLU B O   1 
ATOM   1513 C CB  . GLU A 1 223 ? -14.503 -31.077 7.462   1.00 51.47  ? 210 GLU B CB  1 
ATOM   1514 C CG  . GLU A 1 223 ? -13.853 -31.193 8.848   1.00 54.18  ? 210 GLU B CG  1 
ATOM   1515 C CD  . GLU A 1 223 ? -13.467 -29.923 9.651   1.00 58.17  ? 210 GLU B CD  1 
ATOM   1516 O OE1 . GLU A 1 223 ? -14.328 -29.020 9.725   1.00 58.85  ? 210 GLU B OE1 1 
ATOM   1517 O OE2 . GLU A 1 223 ? -12.317 -29.744 10.180  1.00 56.27  ? 210 GLU B OE2 1 
ATOM   1518 N N   . ALA A 1 224 ? -12.424 -30.236 4.951   1.00 44.71  ? 211 ALA B N   1 
ATOM   1519 C CA  . ALA A 1 224 ? -11.141 -30.149 4.274   1.00 44.49  ? 211 ALA B CA  1 
ATOM   1520 C C   . ALA A 1 224 ? -10.861 -28.680 3.927   1.00 42.19  ? 211 ALA B C   1 
ATOM   1521 O O   . ALA A 1 224 ? -9.781  -28.160 4.176   1.00 43.66  ? 211 ALA B O   1 
ATOM   1522 C CB  . ALA A 1 224 ? -11.179 -31.032 3.055   1.00 47.12  ? 211 ALA B CB  1 
ATOM   1523 N N   . ALA A 1 225 ? -11.865 -28.016 3.340   1.00 40.67  ? 212 ALA B N   1 
ATOM   1524 C CA  . ALA A 1 225 ? -11.731 -26.648 2.865   1.00 40.53  ? 212 ALA B CA  1 
ATOM   1525 C C   . ALA A 1 225 ? -11.609 -25.741 4.095   1.00 37.21  ? 212 ALA B C   1 
ATOM   1526 O O   . ALA A 1 225 ? -10.815 -24.792 4.119   1.00 35.48  ? 212 ALA B O   1 
ATOM   1527 C CB  . ALA A 1 225 ? -12.912 -26.307 1.972   1.00 39.65  ? 212 ALA B CB  1 
ATOM   1528 N N   . SER A 1 226 ? -12.353 -26.087 5.163   1.00 38.42  ? 213 SER B N   1 
ATOM   1529 C CA  . SER A 1 226 ? -12.287 -25.256 6.369   1.00 37.75  ? 213 SER B CA  1 
ATOM   1530 C C   . SER A 1 226 ? -10.864 -25.265 6.942   1.00 36.06  ? 213 SER B C   1 
ATOM   1531 O O   . SER A 1 226 ? -10.314 -24.224 7.318   1.00 36.50  ? 213 SER B O   1 
ATOM   1532 C CB  . SER A 1 226 ? -13.334 -25.677 7.392   1.00 38.85  ? 213 SER B CB  1 
ATOM   1533 O OG  . SER A 1 226 ? -13.246 -24.828 8.528   1.00 38.41  ? 213 SER B OG  1 
ATOM   1534 N N   . GLN A 1 227 ? -10.286 -26.478 7.019   1.00 38.80  ? 214 GLN B N   1 
ATOM   1535 C CA  . GLN A 1 227 ? -8.980  -26.678 7.607   1.00 38.69  ? 214 GLN B CA  1 
ATOM   1536 C C   . GLN A 1 227 ? -7.905  -26.037 6.756   1.00 38.08  ? 214 GLN B C   1 
ATOM   1537 O O   . GLN A 1 227 ? -6.885  -25.610 7.287   1.00 39.97  ? 214 GLN B O   1 
ATOM   1538 C CB  . GLN A 1 227 ? -8.551  -28.148 7.642   1.00 39.84  ? 214 GLN B CB  1 
ATOM   1539 C CG  . GLN A 1 227 ? -8.871  -28.866 8.936   1.00 42.49  ? 214 GLN B CG  1 
ATOM   1540 C CD  . GLN A 1 227 ? -8.447  -28.131 10.184  1.00 39.67  ? 214 GLN B CD  1 
ATOM   1541 O OE1 . GLN A 1 227 ? -7.339  -27.599 10.305  1.00 39.85  ? 214 GLN B OE1 1 
ATOM   1542 N NE2 . GLN A 1 227 ? -9.360  -28.105 11.131  1.00 41.01  ? 214 GLN B NE2 1 
ATOM   1543 N N   . ALA A 1 228 ? -8.158  -25.937 5.448   1.00 38.72  ? 215 ALA B N   1 
ATOM   1544 C CA  . ALA A 1 228 ? -7.199  -25.336 4.550   1.00 36.43  ? 215 ALA B CA  1 
ATOM   1545 C C   . ALA A 1 228 ? -7.125  -23.848 4.892   1.00 33.69  ? 215 ALA B C   1 
ATOM   1546 O O   . ALA A 1 228 ? -6.034  -23.256 4.912   1.00 39.47  ? 215 ALA B O   1 
ATOM   1547 C CB  . ALA A 1 228 ? -7.605  -25.592 3.113   1.00 38.41  ? 215 ALA B CB  1 
ATOM   1548 N N   . PHE A 1 229 ? -8.277  -23.223 5.172   1.00 31.02  ? 216 PHE B N   1 
ATOM   1549 C CA  . PHE A 1 229 ? -8.233  -21.851 5.635   1.00 31.90  ? 216 PHE B CA  1 
ATOM   1550 C C   . PHE A 1 229 ? -7.426  -21.738 6.921   1.00 30.56  ? 216 PHE B C   1 
ATOM   1551 O O   . PHE A 1 229 ? -6.691  -20.792 7.104   1.00 29.89  ? 216 PHE B O   1 
ATOM   1552 C CB  . PHE A 1 229 ? -9.546  -21.076 5.768   1.00 32.49  ? 216 PHE B CB  1 
ATOM   1553 C CG  . PHE A 1 229 ? -10.338 -20.944 4.473   1.00 35.08  ? 216 PHE B CG  1 
ATOM   1554 C CD1 . PHE A 1 229 ? -9.800  -20.201 3.393   1.00 30.53  ? 216 PHE B CD1 1 
ATOM   1555 C CD2 . PHE A 1 229 ? -11.636 -21.499 4.367   1.00 34.56  ? 216 PHE B CD2 1 
ATOM   1556 C CE1 . PHE A 1 229 ? -10.544 -19.963 2.241   1.00 31.80  ? 216 PHE B CE1 1 
ATOM   1557 C CE2 . PHE A 1 229 ? -12.360 -21.290 3.186   1.00 35.52  ? 216 PHE B CE2 1 
ATOM   1558 C CZ  . PHE A 1 229 ? -11.801 -20.574 2.109   1.00 32.94  ? 216 PHE B CZ  1 
ATOM   1559 N N   . ILE A 1 230 ? -7.636  -22.642 7.873   1.00 31.27  ? 217 ILE B N   1 
ATOM   1560 C CA  . ILE A 1 230 ? -6.968  -22.578 9.167   1.00 31.02  ? 217 ILE B CA  1 
ATOM   1561 C C   . ILE A 1 230 ? -5.454  -22.723 8.985   1.00 30.59  ? 217 ILE B C   1 
ATOM   1562 O O   . ILE A 1 230 ? -4.670  -21.959 9.562   1.00 29.63  ? 217 ILE B O   1 
ATOM   1563 C CB  . ILE A 1 230 ? -7.595  -23.631 10.077  1.00 32.67  ? 217 ILE B CB  1 
ATOM   1564 C CG1 . ILE A 1 230 ? -8.975  -23.221 10.555  1.00 34.47  ? 217 ILE B CG1 1 
ATOM   1565 C CG2 . ILE A 1 230 ? -6.645  -24.039 11.220  1.00 36.36  ? 217 ILE B CG2 1 
ATOM   1566 C CD1 . ILE A 1 230 ? -9.508  -24.140 11.644  1.00 39.16  ? 217 ILE B CD1 1 
ATOM   1567 N N   . ASP A 1 231 ? -5.035  -23.598 8.053   1.00 32.38  ? 218 ASP B N   1 
ATOM   1568 C CA  . ASP A 1 231 ? -3.622  -23.850 7.855   1.00 35.47  ? 218 ASP B CA  1 
ATOM   1569 C C   . ASP A 1 231 ? -2.991  -22.630 7.187   1.00 34.20  ? 218 ASP B C   1 
ATOM   1570 O O   . ASP A 1 231 ? -1.869  -22.269 7.506   1.00 36.93  ? 218 ASP B O   1 
ATOM   1571 C CB  . ASP A 1 231 ? -3.397  -25.156 7.091   1.00 45.32  ? 218 ASP B CB  1 
ATOM   1572 C CG  . ASP A 1 231 ? -1.928  -25.513 6.820   1.00 57.93  ? 218 ASP B CG  1 
ATOM   1573 O OD1 . ASP A 1 231 ? -1.142  -25.595 7.802   1.00 66.09  ? 218 ASP B OD1 1 
ATOM   1574 O OD2 . ASP A 1 231 ? -1.543  -25.682 5.622   1.00 60.24  ? 218 ASP B OD2 1 
ATOM   1575 N N   . GLN A 1 232 ? -3.741  -21.926 6.356   1.00 30.04  ? 219 GLN B N   1 
ATOM   1576 C CA  . GLN A 1 232 ? -3.175  -20.791 5.633   1.00 30.94  ? 219 GLN B CA  1 
ATOM   1577 C C   . GLN A 1 232 ? -3.175  -19.550 6.498   1.00 29.01  ? 219 GLN B C   1 
ATOM   1578 O O   . GLN A 1 232 ? -2.315  -18.673 6.360   1.00 32.53  ? 219 GLN B O   1 
ATOM   1579 C CB  . GLN A 1 232 ? -4.009  -20.475 4.405   1.00 29.06  ? 219 GLN B CB  1 
ATOM   1580 C CG  . GLN A 1 232 ? -3.622  -21.307 3.177   1.00 33.05  ? 219 GLN B CG  1 
ATOM   1581 C CD  . GLN A 1 232 ? -4.694  -21.228 2.108   1.00 34.50  ? 219 GLN B CD  1 
ATOM   1582 O OE1 . GLN A 1 232 ? -5.145  -20.153 1.680   1.00 34.82  ? 219 GLN B OE1 1 
ATOM   1583 N NE2 . GLN A 1 232 ? -5.104  -22.402 1.657   1.00 38.02  ? 219 GLN B NE2 1 
ATOM   1584 N N   . GLN A 1 233 ? -4.167  -19.493 7.387   1.00 27.53  ? 220 GLN B N   1 
ATOM   1585 C CA  . GLN A 1 233 ? -4.263  -18.338 8.279   1.00 25.90  ? 220 GLN B CA  1 
ATOM   1586 C C   . GLN A 1 233 ? -3.121  -18.323 9.292   1.00 25.08  ? 220 GLN B C   1 
ATOM   1587 O O   . GLN A 1 233 ? -2.547  -19.341 9.609   1.00 29.17  ? 220 GLN B O   1 
ATOM   1588 C CB  . GLN A 1 233 ? -5.607  -18.395 9.008   1.00 25.12  ? 220 GLN B CB  1 
ATOM   1589 C CG  . GLN A 1 233 ? -6.799  -17.953 8.168   1.00 25.12  ? 220 GLN B CG  1 
ATOM   1590 C CD  . GLN A 1 233 ? -8.132  -18.217 8.838   1.00 24.54  ? 220 GLN B CD  1 
ATOM   1591 O OE1 . GLN A 1 233 ? -8.184  -18.678 10.021  1.00 26.90  ? 220 GLN B OE1 1 
ATOM   1592 N NE2 . GLN A 1 233 ? -9.179  -17.856 8.113   1.00 22.44  ? 220 GLN B NE2 1 
ATOM   1593 N N   . MET A 1 234 ? -2.890  -17.159 9.930   1.00 24.95  ? 221 MET B N   1 
ATOM   1594 C CA  . MET A 1 234 ? -1.903  -17.024 11.001  1.00 23.10  ? 221 MET B CA  1 
ATOM   1595 C C   . MET A 1 234 ? -2.579  -17.484 12.294  1.00 25.66  ? 221 MET B C   1 
ATOM   1596 O O   . MET A 1 234 ? -1.947  -18.148 13.142  1.00 27.64  ? 221 MET B O   1 
ATOM   1597 C CB  . MET A 1 234 ? -1.449  -15.561 11.166  1.00 21.71  ? 221 MET B CB  1 
ATOM   1598 C CG  . MET A 1 234 ? -0.616  -15.044 10.001  1.00 20.43  ? 221 MET B CG  1 
ATOM   1599 S SD  . MET A 1 234 ? -0.339  -13.268 10.213  1.00 23.53  ? 221 MET B SD  1 
ATOM   1600 C CE  . MET A 1 234 ? 0.493   -13.047 8.644   1.00 26.75  ? 221 MET B CE  1 
ATOM   1601 N N   . LEU A 1 235 ? -3.856  -17.100 12.481  1.00 24.97  ? 222 LEU B N   1 
ATOM   1602 C CA  . LEU A 1 235 ? -4.652  -17.532 13.647  1.00 26.47  ? 222 LEU B CA  1 
ATOM   1603 C C   . LEU A 1 235 ? -5.419  -18.812 13.309  1.00 29.41  ? 222 LEU B C   1 
ATOM   1604 O O   . LEU A 1 235 ? -6.052  -18.922 12.248  1.00 32.94  ? 222 LEU B O   1 
ATOM   1605 C CB  . LEU A 1 235 ? -5.572  -16.398 14.127  1.00 22.86  ? 222 LEU B CB  1 
ATOM   1606 C CG  . LEU A 1 235 ? -4.839  -15.139 14.614  1.00 22.42  ? 222 LEU B CG  1 
ATOM   1607 C CD1 . LEU A 1 235 ? -5.879  -13.956 14.872  1.00 22.52  ? 222 LEU B CD1 1 
ATOM   1608 C CD2 . LEU A 1 235 ? -4.053  -15.363 15.847  1.00 27.09  ? 222 LEU B CD2 1 
ATOM   1609 N N   . LYS A 1 236 ? -5.367  -19.789 14.210  1.00 28.28  ? 223 LYS B N   1 
ATOM   1610 C CA  . LYS A 1 236 ? -5.781  -21.142 13.825  1.00 32.81  ? 223 LYS B CA  1 
ATOM   1611 C C   . LYS A 1 236 ? -7.210  -21.446 14.296  1.00 32.75  ? 223 LYS B C   1 
ATOM   1612 O O   . LYS A 1 236 ? -7.498  -22.506 14.884  1.00 35.03  ? 223 LYS B O   1 
ATOM   1613 C CB  . LYS A 1 236 ? -4.772  -22.197 14.320  1.00 32.99  ? 223 LYS B CB  1 
ATOM   1614 C CG  . LYS A 1 236 ? -3.368  -21.814 13.837  1.00 35.76  ? 223 LYS B CG  1 
ATOM   1615 C CD  . LYS A 1 236 ? -3.181  -22.060 12.335  1.00 32.55  ? 223 LYS B CD  1 
ATOM   1616 C CE  . LYS A 1 236 ? -1.828  -21.606 11.921  1.00 31.53  ? 223 LYS B CE  1 
ATOM   1617 N NZ  . LYS A 1 236 ? -1.630  -21.813 10.478  1.00 32.09  ? 223 LYS B NZ  1 
ATOM   1618 N N   . PHE A 1 237 ? -8.134  -20.528 13.963  1.00 32.24  ? 224 PHE B N   1 
ATOM   1619 C CA  . PHE A 1 237 ? -9.577  -20.804 14.136  1.00 34.30  ? 224 PHE B CA  1 
ATOM   1620 C C   . PHE A 1 237 ? -10.312 -20.161 12.947  1.00 31.25  ? 224 PHE B C   1 
ATOM   1621 O O   . PHE A 1 237 ? -9.741  -19.312 12.276  1.00 29.68  ? 224 PHE B O   1 
ATOM   1622 C CB  . PHE A 1 237 ? -10.094 -20.263 15.471  1.00 29.50  ? 224 PHE B CB  1 
ATOM   1623 C CG  . PHE A 1 237 ? -9.924  -18.754 15.680  1.00 29.76  ? 224 PHE B CG  1 
ATOM   1624 C CD1 . PHE A 1 237 ? -8.725  -18.216 16.190  1.00 29.37  ? 224 PHE B CD1 1 
ATOM   1625 C CD2 . PHE A 1 237 ? -10.961 -17.864 15.346  1.00 26.75  ? 224 PHE B CD2 1 
ATOM   1626 C CE1 . PHE A 1 237 ? -8.579  -16.832 16.391  1.00 26.39  ? 224 PHE B CE1 1 
ATOM   1627 C CE2 . PHE A 1 237 ? -10.767 -16.480 15.465  1.00 28.46  ? 224 PHE B CE2 1 
ATOM   1628 C CZ  . PHE A 1 237 ? -9.604  -15.984 16.039  1.00 25.15  ? 224 PHE B CZ  1 
ATOM   1629 N N   . ARG A 1 238 ? -11.585 -20.510 12.742  1.00 32.08  ? 225 ARG B N   1 
ATOM   1630 C CA  . ARG A 1 238 ? -12.365 -19.990 11.627  1.00 32.18  ? 225 ARG B CA  1 
ATOM   1631 C C   . ARG A 1 238 ? -13.027 -18.700 12.092  1.00 32.73  ? 225 ARG B C   1 
ATOM   1632 O O   . ARG A 1 238 ? -13.561 -18.641 13.201  1.00 30.27  ? 225 ARG B O   1 
ATOM   1633 C CB  . ARG A 1 238 ? -13.507 -20.921 11.194  1.00 33.63  ? 225 ARG B CB  1 
ATOM   1634 C CG  . ARG A 1 238 ? -13.021 -22.208 10.559  1.00 34.24  ? 225 ARG B CG  1 
ATOM   1635 C CD  . ARG A 1 238 ? -12.283 -21.894 9.262   1.00 32.87  ? 225 ARG B CD  1 
ATOM   1636 N NE  . ARG A 1 238 ? -12.702 -20.815 8.360   1.00 31.17  ? 225 ARG B NE  1 
ATOM   1637 C CZ  . ARG A 1 238 ? -13.707 -21.022 7.508   1.00 32.42  ? 225 ARG B CZ  1 
ATOM   1638 N NH1 . ARG A 1 238 ? -14.285 -22.211 7.407   1.00 33.62  ? 225 ARG B NH1 1 
ATOM   1639 N NH2 . ARG A 1 238 ? -14.182 -20.006 6.813   1.00 29.97  ? 225 ARG B NH2 1 
ATOM   1640 N N   . LEU A 1 239 ? -12.984 -17.686 11.221  1.00 29.57  ? 226 LEU B N   1 
ATOM   1641 C CA  . LEU A 1 239 ? -13.737 -16.470 11.470  1.00 26.57  ? 226 LEU B CA  1 
ATOM   1642 C C   . LEU A 1 239 ? -15.202 -16.684 11.114  1.00 30.29  ? 226 LEU B C   1 
ATOM   1643 O O   . LEU A 1 239 ? -15.481 -17.487 10.218  1.00 30.49  ? 226 LEU B O   1 
ATOM   1644 C CB  . LEU A 1 239 ? -13.205 -15.332 10.577  1.00 24.42  ? 226 LEU B CB  1 
ATOM   1645 C CG  . LEU A 1 239 ? -11.773 -14.898 10.838  1.00 23.52  ? 226 LEU B CG  1 
ATOM   1646 C CD1 . LEU A 1 239 ? -11.433 -13.930 9.700   1.00 23.53  ? 226 LEU B CD1 1 
ATOM   1647 C CD2 . LEU A 1 239 ? -11.645 -14.273 12.178  1.00 22.90  ? 226 LEU B CD2 1 
ATOM   1648 N N   . ASP A 1 240 ? -16.101 -15.896 11.754  1.00 28.54  ? 227 ASP B N   1 
ATOM   1649 C CA  . ASP A 1 240 ? -17.525 -15.971 11.435  1.00 33.68  ? 227 ASP B CA  1 
ATOM   1650 C C   . ASP A 1 240 ? -18.104 -14.551 11.339  1.00 30.53  ? 227 ASP B C   1 
ATOM   1651 O O   . ASP A 1 240 ? -17.376 -13.555 11.379  1.00 33.76  ? 227 ASP B O   1 
ATOM   1652 C CB  . ASP A 1 240 ? -18.303 -16.870 12.411  1.00 40.02  ? 227 ASP B CB  1 
ATOM   1653 C CG  . ASP A 1 240 ? -18.380 -16.387 13.866  1.00 44.13  ? 227 ASP B CG  1 
ATOM   1654 O OD1 . ASP A 1 240 ? -18.254 -15.177 14.134  1.00 37.79  ? 227 ASP B OD1 1 
ATOM   1655 O OD2 . ASP A 1 240 ? -18.621 -17.225 14.739  1.00 44.88  ? 227 ASP B OD2 1 
ATOM   1656 N N   . ALA A 1 241 ? -19.420 -14.483 11.086  1.00 33.25  ? 228 ALA B N   1 
ATOM   1657 C CA  . ALA A 1 241 ? -20.063 -13.200 10.878  1.00 29.59  ? 228 ALA B CA  1 
ATOM   1658 C C   . ALA A 1 241 ? -19.907 -12.226 12.054  1.00 30.31  ? 228 ALA B C   1 
ATOM   1659 O O   . ALA A 1 241 ? -19.854 -11.000 11.845  1.00 28.65  ? 228 ALA B O   1 
ATOM   1660 C CB  . ALA A 1 241 ? -21.485 -13.406 10.384  1.00 30.43  ? 228 ALA B CB  1 
ATOM   1661 N N   . SER A 1 242 ? -19.795 -12.772 13.276  1.00 32.62  ? 229 SER B N   1 
ATOM   1662 C CA  . SER A 1 242 ? -19.658 -11.959 14.474  1.00 28.01  ? 229 SER B CA  1 
ATOM   1663 C C   . SER A 1 242 ? -18.331 -11.194 14.385  1.00 25.80  ? 229 SER B C   1 
ATOM   1664 O O   . SER A 1 242 ? -18.219 -10.065 14.866  1.00 30.80  ? 229 SER B O   1 
ATOM   1665 C CB  . SER A 1 242 ? -19.664 -12.840 15.694  1.00 26.02  ? 229 SER B CB  1 
ATOM   1666 O OG  . SER A 1 242 ? -20.954 -13.422 15.855  1.00 28.96  ? 229 SER B OG  1 
ATOM   1667 N N   . ASP A 1 243 ? -17.327 -11.842 13.793  1.00 24.24  ? 230 ASP B N   1 
ATOM   1668 C CA  . ASP A 1 243 ? -16.050 -11.103 13.723  1.00 25.03  ? 230 ASP B CA  1 
ATOM   1669 C C   . ASP A 1 243 ? -16.246 -9.879  12.869  1.00 22.95  ? 230 ASP B C   1 
ATOM   1670 O O   . ASP A 1 243 ? -15.588 -8.838  13.127  1.00 24.16  ? 230 ASP B O   1 
ATOM   1671 C CB  . ASP A 1 243 ? -14.947 -11.932 13.134  1.00 24.73  ? 230 ASP B CB  1 
ATOM   1672 C CG  . ASP A 1 243 ? -14.573 -13.070 14.050  1.00 28.75  ? 230 ASP B CG  1 
ATOM   1673 O OD1 . ASP A 1 243 ? -14.023 -12.696 15.134  1.00 25.47  ? 230 ASP B OD1 1 
ATOM   1674 O OD2 . ASP A 1 243 ? -14.892 -14.272 13.722  1.00 28.57  ? 230 ASP B OD2 1 
ATOM   1675 N N   . CYS A 1 244 ? -17.006 -10.031 11.774  1.00 21.03  ? 231 CYS B N   1 
ATOM   1676 C CA  . CYS A 1 244 ? -17.230 -8.842  10.941  1.00 22.82  ? 231 CYS B CA  1 
ATOM   1677 C C   . CYS A 1 244 ? -18.062 -7.795  11.680  1.00 19.76  ? 231 CYS B C   1 
ATOM   1678 O O   . CYS A 1 244 ? -17.809 -6.570  11.657  1.00 21.51  ? 231 CYS B O   1 
ATOM   1679 C CB  . CYS A 1 244 ? -17.933 -9.138  9.627   1.00 24.08  ? 231 CYS B CB  1 
ATOM   1680 S SG  . CYS A 1 244 ? -17.066 -10.366 8.611   1.00 29.21  ? 231 CYS B SG  1 
ATOM   1681 N N   . ALA A 1 245 ? -19.052 -8.244  12.402  1.00 21.98  ? 232 ALA B N   1 
ATOM   1682 C CA  . ALA A 1 245 ? -19.962 -7.296  13.062  1.00 21.12  ? 232 ALA B CA  1 
ATOM   1683 C C   . ALA A 1 245 ? -19.241 -6.553  14.191  1.00 22.24  ? 232 ALA B C   1 
ATOM   1684 O O   . ALA A 1 245 ? -19.472 -5.339  14.381  1.00 21.95  ? 232 ALA B O   1 
ATOM   1685 C CB  . ALA A 1 245 ? -21.191 -8.040  13.601  1.00 23.79  ? 232 ALA B CB  1 
ATOM   1686 N N   . ARG A 1 246 ? -18.339 -7.244  14.924  1.00 23.06  ? 233 ARG B N   1 
ATOM   1687 C CA  . ARG A 1 246 ? -17.529 -6.557  15.945  1.00 22.83  ? 233 ARG B CA  1 
ATOM   1688 C C   . ARG A 1 246 ? -16.781 -5.356  15.354  1.00 21.49  ? 233 ARG B C   1 
ATOM   1689 O O   . ARG A 1 246 ? -16.708 -4.260  15.940  1.00 20.53  ? 233 ARG B O   1 
ATOM   1690 C CB  . ARG A 1 246 ? -16.637 -7.560  16.680  1.00 24.52  ? 233 ARG B CB  1 
ATOM   1691 C CG  . ARG A 1 246 ? -17.471 -8.490  17.566  1.00 27.79  ? 233 ARG B CG  1 
ATOM   1692 C CD  . ARG A 1 246 ? -16.563 -9.713  17.784  1.00 31.51  ? 233 ARG B CD  1 
ATOM   1693 N NE  . ARG A 1 246 ? -17.287 -10.765 18.513  1.00 37.39  ? 233 ARG B NE  1 
ATOM   1694 C CZ  . ARG A 1 246 ? -16.871 -11.441 19.607  1.00 50.57  ? 233 ARG B CZ  1 
ATOM   1695 N NH1 . ARG A 1 246 ? -15.595 -11.590 19.976  1.00 43.09  ? 233 ARG B NH1 1 
ATOM   1696 N NH2 . ARG A 1 246 ? -17.792 -12.092 20.299  1.00 55.76  ? 233 ARG B NH2 1 
ATOM   1697 N N   . LEU A 1 247 ? -16.253 -5.572  14.156  1.00 21.68  ? 234 LEU B N   1 
ATOM   1698 C CA  . LEU A 1 247 ? -15.453 -4.533  13.528  1.00 19.18  ? 234 LEU B CA  1 
ATOM   1699 C C   . LEU A 1 247 ? -16.387 -3.421  13.046  1.00 18.84  ? 234 LEU B C   1 
ATOM   1700 O O   . LEU A 1 247 ? -16.074 -2.227  13.117  1.00 18.45  ? 234 LEU B O   1 
ATOM   1701 C CB  . LEU A 1 247 ? -14.583 -5.104  12.380  1.00 16.81  ? 234 LEU B CB  1 
ATOM   1702 C CG  . LEU A 1 247 ? -13.793 -4.028  11.597  1.00 18.76  ? 234 LEU B CG  1 
ATOM   1703 C CD1 . LEU A 1 247 ? -12.938 -3.102  12.464  1.00 18.61  ? 234 LEU B CD1 1 
ATOM   1704 C CD2 . LEU A 1 247 ? -12.975 -4.854  10.533  1.00 18.37  ? 234 LEU B CD2 1 
ATOM   1705 N N   . ALA A 1 248 ? -17.574 -3.793  12.520  1.00 20.05  ? 235 ALA B N   1 
ATOM   1706 C CA  . ALA A 1 248 ? -18.483 -2.766  12.022  1.00 20.92  ? 235 ALA B CA  1 
ATOM   1707 C C   . ALA A 1 248 ? -18.966 -1.856  13.146  1.00 22.26  ? 235 ALA B C   1 
ATOM   1708 O O   . ALA A 1 248 ? -19.150 -0.646  12.885  1.00 21.26  ? 235 ALA B O   1 
ATOM   1709 C CB  . ALA A 1 248 ? -19.713 -3.386  11.331  1.00 19.86  ? 235 ALA B CB  1 
ATOM   1710 N N   . LEU A 1 249 ? -19.226 -2.427  14.350  1.00 18.26  ? 236 LEU B N   1 
ATOM   1711 C CA  . LEU A 1 249 ? -19.710 -1.573  15.440  1.00 20.22  ? 236 LEU B CA  1 
ATOM   1712 C C   . LEU A 1 249 ? -18.654 -0.498  15.731  1.00 20.95  ? 236 LEU B C   1 
ATOM   1713 O O   . LEU A 1 249 ? -18.953 0.692   15.882  1.00 22.42  ? 236 LEU B O   1 
ATOM   1714 C CB  . LEU A 1 249 ? -19.928 -2.392  16.715  1.00 18.31  ? 236 LEU B CB  1 
ATOM   1715 C CG  . LEU A 1 249 ? -21.076 -3.393  16.606  1.00 22.50  ? 236 LEU B CG  1 
ATOM   1716 C CD1 . LEU A 1 249 ? -21.147 -4.257  17.858  1.00 21.86  ? 236 LEU B CD1 1 
ATOM   1717 C CD2 . LEU A 1 249 ? -22.410 -2.650  16.335  1.00 23.75  ? 236 LEU B CD2 1 
ATOM   1718 N N   . PHE A 1 250 ? -17.388 -0.919  15.770  1.00 19.24  ? 237 PHE B N   1 
ATOM   1719 C CA  . PHE A 1 250 ? -16.293 -0.006  16.052  1.00 18.80  ? 237 PHE B CA  1 
ATOM   1720 C C   . PHE A 1 250 ? -16.242 1.087   14.977  1.00 18.18  ? 237 PHE B C   1 
ATOM   1721 O O   . PHE A 1 250 ? -16.094 2.246   15.318  1.00 18.87  ? 237 PHE B O   1 
ATOM   1722 C CB  . PHE A 1 250 ? -14.926 -0.734  16.109  1.00 19.15  ? 237 PHE B CB  1 
ATOM   1723 C CG  . PHE A 1 250 ? -13.719 0.184   16.316  1.00 18.71  ? 237 PHE B CG  1 
ATOM   1724 C CD1 . PHE A 1 250 ? -13.470 0.744   17.579  1.00 19.23  ? 237 PHE B CD1 1 
ATOM   1725 C CD2 . PHE A 1 250 ? -12.886 0.563   15.266  1.00 21.80  ? 237 PHE B CD2 1 
ATOM   1726 C CE1 . PHE A 1 250 ? -12.440 1.669   17.757  1.00 21.06  ? 237 PHE B CE1 1 
ATOM   1727 C CE2 . PHE A 1 250 ? -11.846 1.475   15.439  1.00 20.20  ? 237 PHE B CE2 1 
ATOM   1728 C CZ  . PHE A 1 250 ? -11.625 2.044   16.667  1.00 20.78  ? 237 PHE B CZ  1 
ATOM   1729 N N   . LEU A 1 251 ? -16.329 0.706   13.672  1.00 17.62  ? 238 LEU B N   1 
ATOM   1730 C CA  . LEU A 1 251 ? -16.199 1.669   12.551  1.00 18.45  ? 238 LEU B CA  1 
ATOM   1731 C C   . LEU A 1 251 ? -17.369 2.644   12.475  1.00 21.69  ? 238 LEU B C   1 
ATOM   1732 O O   . LEU A 1 251 ? -17.269 3.673   11.781  1.00 21.94  ? 238 LEU B O   1 
ATOM   1733 C CB  . LEU A 1 251 ? -16.101 0.903   11.232  1.00 17.22  ? 238 LEU B CB  1 
ATOM   1734 C CG  . LEU A 1 251 ? -14.726 0.217   11.129  1.00 17.34  ? 238 LEU B CG  1 
ATOM   1735 C CD1 . LEU A 1 251 ? -14.513 -0.546  9.765   1.00 16.37  ? 238 LEU B CD1 1 
ATOM   1736 C CD2 . LEU A 1 251 ? -13.506 1.266   11.237  1.00 16.44  ? 238 LEU B CD2 1 
ATOM   1737 N N   . ALA A 1 252 ? -18.505 2.250   13.111  1.00 21.76  ? 239 ALA B N   1 
ATOM   1738 C CA  . ALA A 1 252 ? -19.650 3.157   13.142  1.00 21.08  ? 239 ALA B CA  1 
ATOM   1739 C C   . ALA A 1 252 ? -19.663 4.055   14.383  1.00 22.16  ? 239 ALA B C   1 
ATOM   1740 O O   . ALA A 1 252 ? -20.389 5.021   14.427  1.00 21.99  ? 239 ALA B O   1 
ATOM   1741 C CB  . ALA A 1 252 ? -20.915 2.282   13.093  1.00 23.63  ? 239 ALA B CB  1 
ATOM   1742 N N   . SER A 1 253 ? -19.001 3.635   15.460  1.00 21.24  ? 240 SER B N   1 
ATOM   1743 C CA  . SER A 1 253 ? -19.145 4.295   16.747  1.00 22.72  ? 240 SER B CA  1 
ATOM   1744 C C   . SER A 1 253 ? -18.275 5.569   16.819  1.00 24.34  ? 240 SER B C   1 
ATOM   1745 O O   . SER A 1 253 ? -17.396 5.777   15.980  1.00 22.79  ? 240 SER B O   1 
ATOM   1746 C CB  . SER A 1 253 ? -18.697 3.327   17.828  1.00 23.43  ? 240 SER B CB  1 
ATOM   1747 O OG  . SER A 1 253 ? -17.267 3.178   17.805  1.00 23.53  ? 240 SER B OG  1 
ATOM   1748 N N   . ASP A 1 254 ? -18.430 6.409   17.880  1.00 23.92  ? 241 ASP B N   1 
ATOM   1749 C CA  . ASP A 1 254 ? -17.530 7.542   18.042  1.00 25.03  ? 241 ASP B CA  1 
ATOM   1750 C C   . ASP A 1 254 ? -16.096 7.088   18.357  1.00 23.84  ? 241 ASP B C   1 
ATOM   1751 O O   . ASP A 1 254 ? -15.202 7.899   18.339  1.00 22.53  ? 241 ASP B O   1 
ATOM   1752 C CB  . ASP A 1 254 ? -18.099 8.554   19.050  1.00 25.98  ? 241 ASP B CB  1 
ATOM   1753 C CG  . ASP A 1 254 ? -19.308 9.299   18.493  1.00 31.07  ? 241 ASP B CG  1 
ATOM   1754 O OD1 . ASP A 1 254 ? -19.517 9.245   17.239  1.00 45.00  ? 241 ASP B OD1 1 
ATOM   1755 O OD2 . ASP A 1 254 ? -20.090 9.892   19.247  1.00 38.49  ? 241 ASP B OD2 1 
ATOM   1756 N N   . ASP A 1 255 ? -15.865 5.806   18.716  1.00 21.21  ? 242 ASP B N   1 
ATOM   1757 C CA  . ASP A 1 255 ? -14.521 5.360   18.984  1.00 21.38  ? 242 ASP B CA  1 
ATOM   1758 C C   . ASP A 1 255 ? -13.643 5.415   17.714  1.00 22.28  ? 242 ASP B C   1 
ATOM   1759 O O   . ASP A 1 255 ? -12.394 5.290   17.844  1.00 23.21  ? 242 ASP B O   1 
ATOM   1760 C CB  . ASP A 1 255 ? -14.480 3.929   19.514  1.00 21.55  ? 242 ASP B CB  1 
ATOM   1761 C CG  . ASP A 1 255 ? -15.131 3.908   20.904  1.00 25.58  ? 242 ASP B CG  1 
ATOM   1762 O OD1 . ASP A 1 255 ? -16.342 3.930   20.945  1.00 26.27  ? 242 ASP B OD1 1 
ATOM   1763 O OD2 . ASP A 1 255 ? -14.443 4.050   21.888  1.00 25.74  ? 242 ASP B OD2 1 
ATOM   1764 N N   . SER A 1 256 ? -14.264 5.586   16.512  1.00 19.03  ? 243 SER B N   1 
ATOM   1765 C CA  . SER A 1 256 ? -13.450 5.624   15.324  1.00 19.53  ? 243 SER B CA  1 
ATOM   1766 C C   . SER A 1 256 ? -13.587 6.969   14.614  1.00 17.80  ? 243 SER B C   1 
ATOM   1767 O O   . SER A 1 256 ? -13.379 7.010   13.411  1.00 18.22  ? 243 SER B O   1 
ATOM   1768 C CB  . SER A 1 256 ? -13.740 4.462   14.365  1.00 20.47  ? 243 SER B CB  1 
ATOM   1769 O OG  . SER A 1 256 ? -15.119 4.625   13.975  1.00 20.89  ? 243 SER B OG  1 
ATOM   1770 N N   . ARG A 1 257 ? -13.970 8.033   15.368  1.00 17.84  ? 244 ARG B N   1 
ATOM   1771 C CA  . ARG A 1 257 ? -14.369 9.293   14.748  1.00 19.59  ? 244 ARG B CA  1 
ATOM   1772 C C   . ARG A 1 257 ? -13.271 9.982   13.942  1.00 21.42  ? 244 ARG B C   1 
ATOM   1773 O O   . ARG A 1 257 ? -13.579 10.716  12.958  1.00 22.16  ? 244 ARG B O   1 
ATOM   1774 C CB  . ARG A 1 257 ? -15.012 10.256  15.766  1.00 19.70  ? 244 ARG B CB  1 
ATOM   1775 C CG  . ARG A 1 257 ? -13.958 10.683  16.776  1.00 21.71  ? 244 ARG B CG  1 
ATOM   1776 C CD  . ARG A 1 257 ? -14.738 11.678  17.728  1.00 34.15  ? 244 ARG B CD  1 
ATOM   1777 N NE  . ARG A 1 257 ? -15.372 12.852  17.098  1.00 32.24  ? 244 ARG B NE  1 
ATOM   1778 C CZ  . ARG A 1 257 ? -14.807 14.112  17.036  1.00 37.09  ? 244 ARG B CZ  1 
ATOM   1779 N NH1 . ARG A 1 257 ? -15.333 15.093  16.305  1.00 35.16  ? 244 ARG B NH1 1 
ATOM   1780 N NH2 . ARG A 1 257 ? -13.623 14.374  17.594  1.00 38.09  ? 244 ARG B NH2 1 
ATOM   1781 N N   . GLY A 1 258 ? -12.000 9.685   14.275  1.00 19.38  ? 245 GLY B N   1 
ATOM   1782 C CA  . GLY A 1 258 ? -10.856 10.224  13.526  1.00 21.07  ? 245 GLY B CA  1 
ATOM   1783 C C   . GLY A 1 258 ? -10.347 9.359   12.384  1.00 18.49  ? 245 GLY B C   1 
ATOM   1784 O O   . GLY A 1 258 ? -9.285  9.666   11.792  1.00 17.97  ? 245 GLY B O   1 
ATOM   1785 N N   . CYS A 1 259 ? -10.994 8.241   12.133  1.00 17.05  ? 246 CYS B N   1 
ATOM   1786 C CA  . CYS A 1 259 ? -10.504 7.265   11.146  1.00 15.25  ? 246 CYS B CA  1 
ATOM   1787 C C   . CYS A 1 259 ? -11.259 7.492   9.812   1.00 15.92  ? 246 CYS B C   1 
ATOM   1788 O O   . CYS A 1 259 ? -12.511 7.377   9.805   1.00 16.50  ? 246 CYS B O   1 
ATOM   1789 C CB  . CYS A 1 259 ? -10.782 5.808   11.587  1.00 15.95  ? 246 CYS B CB  1 
ATOM   1790 S SG  . CYS A 1 259 ? -9.811  5.275   13.034  1.00 18.94  ? 246 CYS B SG  1 
ATOM   1791 N N   . THR A 1 260 ? -10.528 7.735   8.697   1.00 16.57  ? 247 THR B N   1 
ATOM   1792 C CA  . THR A 1 260 ? -11.267 7.743   7.450   1.00 15.68  ? 247 THR B CA  1 
ATOM   1793 C C   . THR A 1 260 ? -10.328 7.449   6.297   1.00 16.99  ? 247 THR B C   1 
ATOM   1794 O O   . THR A 1 260 ? -9.100  7.588   6.447   1.00 15.53  ? 247 THR B O   1 
ATOM   1795 C CB  . THR A 1 260 ? -11.872 9.140   7.230   1.00 17.50  ? 247 THR B CB  1 
ATOM   1796 O OG1 . THR A 1 260 ? -12.903 9.113   6.242   1.00 17.05  ? 247 THR B OG1 1 
ATOM   1797 C CG2 . THR A 1 260 ? -10.781 10.175  6.965   1.00 17.27  ? 247 THR B CG2 1 
ATOM   1798 N N   . GLY A 1 261 ? -10.907 6.929   5.206   1.00 16.83  ? 248 GLY B N   1 
ATOM   1799 C CA  . GLY A 1 261 ? -10.191 6.659   3.948   1.00 15.62  ? 248 GLY B CA  1 
ATOM   1800 C C   . GLY A 1 261 ? -9.424  5.354   4.007   1.00 16.72  ? 248 GLY B C   1 
ATOM   1801 O O   . GLY A 1 261 ? -8.636  5.048   3.091   1.00 15.98  ? 248 GLY B O   1 
ATOM   1802 N N   . GLN A 1 262 ? -9.657  4.551   5.069   1.00 17.55  ? 249 GLN B N   1 
ATOM   1803 C CA  . GLN A 1 262 ? -8.785  3.421   5.414   1.00 15.82  ? 249 GLN B CA  1 
ATOM   1804 C C   . GLN A 1 262 ? -9.420  2.039   5.271   1.00 17.83  ? 249 GLN B C   1 
ATOM   1805 O O   . GLN A 1 262 ? -10.618 1.925   5.288   1.00 17.90  ? 249 GLN B O   1 
ATOM   1806 C CB  . GLN A 1 262 ? -8.375  3.573   6.894   1.00 15.96  ? 249 GLN B CB  1 
ATOM   1807 C CG  . GLN A 1 262 ? -7.243  4.612   7.014   1.00 17.47  ? 249 GLN B CG  1 
ATOM   1808 C CD  . GLN A 1 262 ? -5.977  4.140   6.276   1.00 19.18  ? 249 GLN B CD  1 
ATOM   1809 O OE1 . GLN A 1 262 ? -5.681  2.906   6.140   1.00 23.92  ? 249 GLN B OE1 1 
ATOM   1810 N NE2 . GLN A 1 262 ? -5.371  5.105   5.605   1.00 20.64  ? 249 GLN B NE2 1 
ATOM   1811 N N   . ASN A 1 263 ? -8.596  1.018   5.059   1.00 14.14  ? 250 ASN B N   1 
ATOM   1812 C CA  . ASN A 1 263 ? -9.041  -0.352  5.111   1.00 17.98  ? 250 ASN B CA  1 
ATOM   1813 C C   . ASN A 1 263 ? -8.797  -0.843  6.543   1.00 18.02  ? 250 ASN B C   1 
ATOM   1814 O O   . ASN A 1 263 ? -7.760  -0.585  7.151   1.00 20.63  ? 250 ASN B O   1 
ATOM   1815 C CB  . ASN A 1 263 ? -8.219  -1.263  4.200   1.00 19.17  ? 250 ASN B CB  1 
ATOM   1816 C CG  . ASN A 1 263 ? -8.492  -0.963  2.733   1.00 21.53  ? 250 ASN B CG  1 
ATOM   1817 O OD1 . ASN A 1 263 ? -9.615  -0.644  2.346   1.00 21.26  ? 250 ASN B OD1 1 
ATOM   1818 N ND2 . ASN A 1 263 ? -7.564  -1.293  1.867   1.00 24.88  ? 250 ASN B ND2 1 
ATOM   1819 N N   . PHE A 1 264 ? -9.731  -1.673  7.063   1.00 14.68  ? 251 PHE B N   1 
ATOM   1820 C CA  . PHE A 1 264 ? -9.593  -2.328  8.352   1.00 15.42  ? 251 PHE B CA  1 
ATOM   1821 C C   . PHE A 1 264 ? -9.851  -3.805  7.977   1.00 14.22  ? 251 PHE B C   1 
ATOM   1822 O O   . PHE A 1 264 ? -10.964 -4.189  7.632   1.00 19.30  ? 251 PHE B O   1 
ATOM   1823 C CB  . PHE A 1 264 ? -10.695 -1.853  9.302   1.00 16.90  ? 251 PHE B CB  1 
ATOM   1824 C CG  . PHE A 1 264 ? -10.399 -0.449  9.764   1.00 20.51  ? 251 PHE B CG  1 
ATOM   1825 C CD1 . PHE A 1 264 ? -10.764 0.654   8.959   1.00 20.45  ? 251 PHE B CD1 1 
ATOM   1826 C CD2 . PHE A 1 264 ? -9.921  -0.207  11.037  1.00 30.81  ? 251 PHE B CD2 1 
ATOM   1827 C CE1 . PHE A 1 264 ? -10.392 1.949   9.373   1.00 20.28  ? 251 PHE B CE1 1 
ATOM   1828 C CE2 . PHE A 1 264 ? -9.622  1.105   11.463  1.00 30.94  ? 251 PHE B CE2 1 
ATOM   1829 C CZ  . PHE A 1 264 ? -9.805  2.161   10.593  1.00 22.80  ? 251 PHE B CZ  1 
ATOM   1830 N N   . VAL A 1 265 ? -8.825  -4.652  8.152   1.00 15.41  ? 252 VAL B N   1 
ATOM   1831 C CA  . VAL A 1 265 ? -8.945  -5.988  7.604   1.00 16.23  ? 252 VAL B CA  1 
ATOM   1832 C C   . VAL A 1 265 ? -9.042  -6.999  8.755   1.00 18.00  ? 252 VAL B C   1 
ATOM   1833 O O   . VAL A 1 265 ? -8.224  -6.995  9.657   1.00 18.42  ? 252 VAL B O   1 
ATOM   1834 C CB  . VAL A 1 265 ? -7.613  -6.258  6.893   1.00 15.41  ? 252 VAL B CB  1 
ATOM   1835 C CG1 . VAL A 1 265 ? -7.592  -7.701  6.330   1.00 19.06  ? 252 VAL B CG1 1 
ATOM   1836 C CG2 . VAL A 1 265 ? -7.400  -5.276  5.708   1.00 16.69  ? 252 VAL B CG2 1 
ATOM   1837 N N   . VAL A 1 266 ? -10.063 -7.885  8.686   1.00 16.63  ? 253 VAL B N   1 
ATOM   1838 C CA  . VAL A 1 266 ? -10.336 -8.832  9.726   1.00 16.99  ? 253 VAL B CA  1 
ATOM   1839 C C   . VAL A 1 266 ? -10.260 -10.203 9.034   1.00 17.89  ? 253 VAL B C   1 
ATOM   1840 O O   . VAL A 1 266 ? -11.239 -10.628 8.447   1.00 18.45  ? 253 VAL B O   1 
ATOM   1841 C CB  . VAL A 1 266 ? -11.694 -8.623  10.476  1.00 19.72  ? 253 VAL B CB  1 
ATOM   1842 C CG1 . VAL A 1 266 ? -12.930 -8.429  9.578   1.00 17.45  ? 253 VAL B CG1 1 
ATOM   1843 C CG2 . VAL A 1 266 ? -11.953 -9.793  11.466  1.00 20.89  ? 253 VAL B CG2 1 
ATOM   1844 N N   . ASP A 1 267 ? -9.080  -10.861 9.024   1.00 20.00  ? 254 ASP B N   1 
ATOM   1845 C CA  . ASP A 1 267 ? -8.918  -11.996 8.117   1.00 19.21  ? 254 ASP B CA  1 
ATOM   1846 C C   . ASP A 1 267 ? -8.008  -13.040 8.760   1.00 21.96  ? 254 ASP B C   1 
ATOM   1847 O O   . ASP A 1 267 ? -7.561  -13.937 8.042   1.00 21.67  ? 254 ASP B O   1 
ATOM   1848 C CB  . ASP A 1 267 ? -8.323  -11.506 6.771   1.00 18.93  ? 254 ASP B CB  1 
ATOM   1849 C CG  . ASP A 1 267 ? -6.847  -11.098 6.790   1.00 19.55  ? 254 ASP B CG  1 
ATOM   1850 O OD1 . ASP A 1 267 ? -6.286  -10.789 7.922   1.00 18.51  ? 254 ASP B OD1 1 
ATOM   1851 O OD2 . ASP A 1 267 ? -6.256  -11.071 5.659   1.00 18.31  ? 254 ASP B OD2 1 
ATOM   1852 N N   . ALA A 1 268 ? -7.636  -12.903 10.064  1.00 20.83  ? 255 ALA B N   1 
ATOM   1853 C CA  . ALA A 1 268 ? -6.836  -13.936 10.751  1.00 18.87  ? 255 ALA B CA  1 
ATOM   1854 C C   . ALA A 1 268 ? -5.510  -14.178 10.013  1.00 21.35  ? 255 ALA B C   1 
ATOM   1855 O O   . ALA A 1 268 ? -4.875  -15.253 10.154  1.00 21.06  ? 255 ALA B O   1 
ATOM   1856 C CB  . ALA A 1 268 ? -7.662  -15.232 10.955  1.00 19.56  ? 255 ALA B CB  1 
ATOM   1857 N N   . GLY A 1 269 ? -5.048  -13.147 9.258   1.00 25.63  ? 256 GLY B N   1 
ATOM   1858 C CA  . GLY A 1 269 ? -3.762  -13.242 8.564   1.00 22.54  ? 256 GLY B CA  1 
ATOM   1859 C C   . GLY A 1 269 ? -3.835  -13.909 7.152   1.00 23.19  ? 256 GLY B C   1 
ATOM   1860 O O   . GLY A 1 269 ? -2.751  -14.141 6.580   1.00 22.40  ? 256 GLY B O   1 
ATOM   1861 N N   . LEU A 1 270 ? -5.040  -14.250 6.598   1.00 18.68  ? 257 LEU B N   1 
ATOM   1862 C CA  . LEU A 1 270 ? -5.068  -15.049 5.349   1.00 21.31  ? 257 LEU B CA  1 
ATOM   1863 C C   . LEU A 1 270 ? -4.503  -14.225 4.178   1.00 22.03  ? 257 LEU B C   1 
ATOM   1864 O O   . LEU A 1 270 ? -3.949  -14.825 3.258   1.00 22.82  ? 257 LEU B O   1 
ATOM   1865 C CB  . LEU A 1 270 ? -6.531  -15.421 5.087   1.00 24.13  ? 257 LEU B CB  1 
ATOM   1866 C CG  . LEU A 1 270 ? -6.848  -16.363 3.927   1.00 24.32  ? 257 LEU B CG  1 
ATOM   1867 C CD1 . LEU A 1 270 ? -6.131  -17.669 4.187   1.00 26.19  ? 257 LEU B CD1 1 
ATOM   1868 C CD2 . LEU A 1 270 ? -8.382  -16.610 3.863   1.00 23.67  ? 257 LEU B CD2 1 
ATOM   1869 N N   . SER A 1 271 ? -4.538  -12.883 4.267   1.00 18.67  ? 258 SER B N   1 
ATOM   1870 C CA  . SER A 1 271 ? -4.030  -12.053 3.167   1.00 19.65  ? 258 SER B CA  1 
ATOM   1871 C C   . SER A 1 271 ? -2.501  -11.908 3.145   1.00 21.84  ? 258 SER B C   1 
ATOM   1872 O O   . SER A 1 271 ? -1.958  -11.289 2.226   1.00 21.76  ? 258 SER B O   1 
ATOM   1873 C CB  . SER A 1 271 ? -4.695  -10.671 3.126   1.00 19.11  ? 258 SER B CB  1 
ATOM   1874 O OG  . SER A 1 271 ? -4.334  -9.895  4.266   1.00 21.23  ? 258 SER B OG  1 
ATOM   1875 N N   . ILE A 1 272 ? -1.772  -12.496 4.096   1.00 21.06  ? 259 ILE B N   1 
ATOM   1876 C CA  . ILE A 1 272 ? -0.322  -12.307 4.218   1.00 21.46  ? 259 ILE B CA  1 
ATOM   1877 C C   . ILE A 1 272 ? 0.325   -13.696 4.274   1.00 23.27  ? 259 ILE B C   1 
ATOM   1878 O O   . ILE A 1 272 ? 0.409   -14.291 5.347   1.00 24.71  ? 259 ILE B O   1 
ATOM   1879 C CB  . ILE A 1 272 ? 0.001   -11.461 5.464   1.00 22.57  ? 259 ILE B CB  1 
ATOM   1880 C CG1 . ILE A 1 272 ? -0.658  -10.053 5.272   1.00 22.59  ? 259 ILE B CG1 1 
ATOM   1881 C CG2 . ILE A 1 272 ? 1.523   -11.292 5.513   1.00 21.32  ? 259 ILE B CG2 1 
ATOM   1882 C CD1 . ILE A 1 272 ? -0.510  -9.147  6.481   1.00 28.41  ? 259 ILE B CD1 1 
ATOM   1883 N N   . GLN A 1 273 ? 0.559   -14.259 3.096   1.00 23.86  ? 260 GLN B N   1 
ATOM   1884 C CA  . GLN A 1 273 ? 1.072   -15.622 3.087   1.00 28.16  ? 260 GLN B CA  1 
ATOM   1885 C C   . GLN A 1 273 ? 2.243   -15.763 2.121   1.00 32.79  ? 260 GLN B C   1 
ATOM   1886 O O   . GLN A 1 273 ? 2.826   -16.887 2.198   1.00 32.83  ? 260 GLN B O   1 
ATOM   1887 C CB  . GLN A 1 273 ? 0.119   -16.545 2.340   1.00 33.09  ? 260 GLN B CB  1 
ATOM   1888 C CG  . GLN A 1 273 ? -1.109  -16.913 3.149   1.00 32.18  ? 260 GLN B CG  1 
ATOM   1889 C CD  . GLN A 1 273 ? -1.963  -17.915 2.419   1.00 35.52  ? 260 GLN B CD  1 
ATOM   1890 O OE1 . GLN A 1 273 ? -1.507  -19.018 2.054   1.00 34.60  ? 260 GLN B OE1 1 
ATOM   1891 N NE2 . GLN A 1 273 ? -3.217  -17.528 2.236   1.00 36.40  ? 260 GLN B NE2 1 
ATOM   1892 O OXT . GLN A 1 273 ? 2.471   -14.819 1.257   1.00 29.09  ? 260 GLN B OXT 1 
ATOM   1893 N N   . ASN B 1 15  ? -9.783  10.432  33.498  1.00 50.44  ? 2   ASN A N   1 
ATOM   1894 C CA  . ASN B 1 15  ? -9.906  10.403  32.004  1.00 41.27  ? 2   ASN A CA  1 
ATOM   1895 C C   . ASN B 1 15  ? -10.083 8.964   31.481  1.00 40.10  ? 2   ASN A C   1 
ATOM   1896 O O   . ASN B 1 15  ? -9.141  8.158   31.421  1.00 34.07  ? 2   ASN A O   1 
ATOM   1897 C CB  . ASN B 1 15  ? -8.897  11.207  31.174  1.00 45.27  ? 2   ASN A CB  1 
ATOM   1898 C CG  . ASN B 1 15  ? -9.431  11.613  29.800  1.00 58.86  ? 2   ASN A CG  1 
ATOM   1899 O OD1 . ASN B 1 15  ? -10.491 11.157  29.325  1.00 60.09  ? 2   ASN A OD1 1 
ATOM   1900 N ND2 . ASN B 1 15  ? -8.715  12.470  29.086  1.00 49.54  ? 2   ASN A ND2 1 
ATOM   1901 N N   . ARG B 1 16  ? -11.319 8.712   30.988  1.00 30.02  ? 3   ARG A N   1 
ATOM   1902 C CA  . ARG B 1 16  ? -11.776 7.420   30.514  1.00 31.42  ? 3   ARG A CA  1 
ATOM   1903 C C   . ARG B 1 16  ? -11.368 7.306   29.040  1.00 23.57  ? 3   ARG A C   1 
ATOM   1904 O O   . ARG B 1 16  ? -11.229 6.172   28.552  1.00 25.61  ? 3   ARG A O   1 
ATOM   1905 C CB  . ARG B 1 16  ? -13.265 7.421   30.912  1.00 29.66  ? 3   ARG A CB  1 
ATOM   1906 C CG  . ARG B 1 16  ? -13.554 6.902   32.310  1.00 33.56  ? 3   ARG A CG  1 
ATOM   1907 N N   . HIS B 1 17  ? -11.253 8.493   28.339  1.00 22.16  ? 4   HIS A N   1 
ATOM   1908 C CA  . HIS B 1 17  ? -10.956 8.537   26.891  1.00 22.64  ? 4   HIS A CA  1 
ATOM   1909 C C   . HIS B 1 17  ? -12.153 8.161   26.015  1.00 23.52  ? 4   HIS A C   1 
ATOM   1910 O O   . HIS B 1 17  ? -12.189 8.504   24.841  1.00 24.36  ? 4   HIS A O   1 
ATOM   1911 C CB  . HIS B 1 17  ? -9.660  7.795   26.465  1.00 21.49  ? 4   HIS A CB  1 
ATOM   1912 C CG  . HIS B 1 17  ? -8.530  8.426   27.160  1.00 23.21  ? 4   HIS A CG  1 
ATOM   1913 N ND1 . HIS B 1 17  ? -7.993  9.631   26.719  1.00 23.42  ? 4   HIS A ND1 1 
ATOM   1914 C CD2 . HIS B 1 17  ? -7.932  8.155   28.366  1.00 23.39  ? 4   HIS A CD2 1 
ATOM   1915 C CE1 . HIS B 1 17  ? -7.062  10.044  27.575  1.00 23.82  ? 4   HIS A CE1 1 
ATOM   1916 N NE2 . HIS B 1 17  ? -6.973  9.168   28.567  1.00 24.63  ? 4   HIS A NE2 1 
ATOM   1917 N N   . THR B 1 18  ? -13.106 7.374   26.519  1.00 21.55  ? 5   THR A N   1 
ATOM   1918 C CA  . THR B 1 18  ? -14.300 6.952   25.760  1.00 22.79  ? 5   THR A CA  1 
ATOM   1919 C C   . THR B 1 18  ? -15.420 6.678   26.779  1.00 22.95  ? 5   THR A C   1 
ATOM   1920 O O   . THR B 1 18  ? -15.083 6.398   27.939  1.00 25.00  ? 5   THR A O   1 
ATOM   1921 C CB  . THR B 1 18  ? -13.994 5.700   24.917  1.00 22.30  ? 5   THR A CB  1 
ATOM   1922 O OG1 . THR B 1 18  ? -15.155 5.488   24.127  1.00 23.34  ? 5   THR A OG1 1 
ATOM   1923 C CG2 . THR B 1 18  ? -13.556 4.448   25.677  1.00 20.76  ? 5   THR A CG2 1 
ATOM   1924 N N   . ASP B 1 19  ? -16.695 6.622   26.312  1.00 23.85  ? 6   ASP A N   1 
ATOM   1925 C CA  . ASP B 1 19  ? -17.754 6.047   27.097  1.00 25.56  ? 6   ASP A CA  1 
ATOM   1926 C C   . ASP B 1 19  ? -18.033 4.577   26.762  1.00 24.66  ? 6   ASP A C   1 
ATOM   1927 O O   . ASP B 1 19  ? -18.857 3.956   27.460  1.00 25.82  ? 6   ASP A O   1 
ATOM   1928 C CB  . ASP B 1 19  ? -18.992 6.934   27.052  1.00 31.63  ? 6   ASP A CB  1 
ATOM   1929 C CG  . ASP B 1 19  ? -19.523 7.135   25.632  1.00 34.06  ? 6   ASP A CG  1 
ATOM   1930 O OD1 . ASP B 1 19  ? -18.849 6.695   24.629  1.00 31.88  ? 6   ASP A OD1 1 
ATOM   1931 O OD2 . ASP B 1 19  ? -20.606 7.743   25.517  1.00 41.01  ? 6   ASP A OD2 1 
ATOM   1932 N N   . THR B 1 20  ? -17.351 4.027   25.747  1.00 24.40  ? 7   THR A N   1 
ATOM   1933 C CA  . THR B 1 20  ? -17.541 2.624   25.403  1.00 24.48  ? 7   THR A CA  1 
ATOM   1934 C C   . THR B 1 20  ? -16.971 1.750   26.539  1.00 26.01  ? 7   THR A C   1 
ATOM   1935 O O   . THR B 1 20  ? -16.001 2.155   27.160  1.00 23.32  ? 7   THR A O   1 
ATOM   1936 C CB  . THR B 1 20  ? -16.780 2.346   24.124  1.00 23.08  ? 7   THR A CB  1 
ATOM   1937 O OG1 . THR B 1 20  ? -17.454 3.155   23.180  1.00 22.93  ? 7   THR A OG1 1 
ATOM   1938 C CG2 . THR B 1 20  ? -16.744 0.868   23.746  1.00 19.93  ? 7   THR A CG2 1 
ATOM   1939 N N   . HIS B 1 21  ? -17.608 0.575   26.775  1.00 24.85  ? 8   HIS A N   1 
ATOM   1940 C CA  . HIS B 1 21  ? -17.282 -0.338  27.859  1.00 24.70  ? 8   HIS A CA  1 
ATOM   1941 C C   . HIS B 1 21  ? -16.982 -1.690  27.214  1.00 23.32  ? 8   HIS A C   1 
ATOM   1942 O O   . HIS B 1 21  ? -17.843 -2.255  26.511  1.00 23.83  ? 8   HIS A O   1 
ATOM   1943 C CB  . HIS B 1 21  ? -18.372 -0.465  28.941  1.00 26.22  ? 8   HIS A CB  1 
ATOM   1944 C CG  . HIS B 1 21  ? -17.922 -1.480  29.952  1.00 33.64  ? 8   HIS A CG  1 
ATOM   1945 N ND1 . HIS B 1 21  ? -18.608 -2.612  30.373  1.00 43.87  ? 8   HIS A ND1 1 
ATOM   1946 C CD2 . HIS B 1 21  ? -16.709 -1.544  30.603  1.00 39.36  ? 8   HIS A CD2 1 
ATOM   1947 C CE1 . HIS B 1 21  ? -17.878 -3.300  31.271  1.00 39.64  ? 8   HIS A CE1 1 
ATOM   1948 N NE2 . HIS B 1 21  ? -16.734 -2.665  31.437  1.00 43.51  ? 8   HIS A NE2 1 
ATOM   1949 N N   . TYR B 1 22  ? -15.737 -2.138  27.361  1.00 23.59  ? 9   TYR A N   1 
ATOM   1950 C CA  . TYR B 1 22  ? -15.338 -3.445  26.864  1.00 22.21  ? 9   TYR A CA  1 
ATOM   1951 C C   . TYR B 1 22  ? -15.201 -4.420  28.032  1.00 24.13  ? 9   TYR A C   1 
ATOM   1952 O O   . TYR B 1 22  ? -14.156 -4.546  28.643  1.00 24.61  ? 9   TYR A O   1 
ATOM   1953 C CB  . TYR B 1 22  ? -13.994 -3.445  26.128  1.00 22.77  ? 9   TYR A CB  1 
ATOM   1954 C CG  . TYR B 1 22  ? -13.931 -2.550  24.887  1.00 22.97  ? 9   TYR A CG  1 
ATOM   1955 C CD1 . TYR B 1 22  ? -13.622 -1.195  24.999  1.00 21.04  ? 9   TYR A CD1 1 
ATOM   1956 C CD2 . TYR B 1 22  ? -14.037 -3.110  23.641  1.00 20.46  ? 9   TYR A CD2 1 
ATOM   1957 C CE1 . TYR B 1 22  ? -13.434 -0.430  23.853  1.00 21.23  ? 9   TYR A CE1 1 
ATOM   1958 C CE2 . TYR B 1 22  ? -13.919 -2.350  22.484  1.00 22.05  ? 9   TYR A CE2 1 
ATOM   1959 C CZ  . TYR B 1 22  ? -13.628 -1.003  22.599  1.00 22.32  ? 9   TYR A CZ  1 
ATOM   1960 O OH  . TYR B 1 22  ? -13.527 -0.244  21.448  1.00 22.73  ? 9   TYR A OH  1 
ATOM   1961 N N   . PRO B 1 23  ? -16.209 -5.226  28.358  1.00 23.08  ? 10  PRO A N   1 
ATOM   1962 C CA  . PRO B 1 23  ? -16.052 -6.259  29.401  1.00 24.87  ? 10  PRO A CA  1 
ATOM   1963 C C   . PRO B 1 23  ? -14.826 -7.165  29.180  1.00 22.24  ? 10  PRO A C   1 
ATOM   1964 O O   . PRO B 1 23  ? -14.226 -7.674  30.153  1.00 24.61  ? 10  PRO A O   1 
ATOM   1965 C CB  . PRO B 1 23  ? -17.363 -7.111  29.369  1.00 26.63  ? 10  PRO A CB  1 
ATOM   1966 C CG  . PRO B 1 23  ? -18.319 -6.144  28.729  1.00 25.69  ? 10  PRO A CG  1 
ATOM   1967 C CD  . PRO B 1 23  ? -17.567 -5.187  27.784  1.00 22.43  ? 10  PRO A CD  1 
ATOM   1968 N N   . SER B 1 24  ? -14.468 -7.417  27.917  1.00 24.41  ? 11  SER A N   1 
ATOM   1969 C CA  . SER B 1 24  ? -13.342 -8.343  27.709  1.00 23.94  ? 11  SER A CA  1 
ATOM   1970 C C   . SER B 1 24  ? -11.978 -7.771  28.175  1.00 22.56  ? 11  SER A C   1 
ATOM   1971 O O   . SER B 1 24  ? -10.994 -8.503  28.184  1.00 25.82  ? 11  SER A O   1 
ATOM   1972 C CB  . SER B 1 24  ? -13.247 -8.774  26.242  1.00 23.59  ? 11  SER A CB  1 
ATOM   1973 O OG  . SER B 1 24  ? -12.910 -7.651  25.405  1.00 23.59  ? 11  SER A OG  1 
ATOM   1974 N N   . LEU B 1 25  ? -11.888 -6.479  28.509  1.00 22.94  ? 12  LEU A N   1 
ATOM   1975 C CA  . LEU B 1 25  ? -10.666 -5.867  29.010  1.00 21.31  ? 12  LEU A CA  1 
ATOM   1976 C C   . LEU B 1 25  ? -10.484 -6.013  30.525  1.00 23.34  ? 12  LEU A C   1 
ATOM   1977 O O   . LEU B 1 25  ? -9.381  -5.795  31.053  1.00 23.92  ? 12  LEU A O   1 
ATOM   1978 C CB  . LEU B 1 25  ? -10.483 -4.415  28.529  1.00 22.44  ? 12  LEU A CB  1 
ATOM   1979 C CG  . LEU B 1 25  ? -10.303 -4.264  27.020  1.00 19.91  ? 12  LEU A CG  1 
ATOM   1980 C CD1 . LEU B 1 25  ? -10.226 -2.757  26.656  1.00 18.04  ? 12  LEU A CD1 1 
ATOM   1981 C CD2 . LEU B 1 25  ? -9.030  -5.033  26.551  1.00 19.31  ? 12  LEU A CD2 1 
ATOM   1982 N N   . ALA B 1 26  ? -11.560 -6.342  31.220  1.00 23.32  ? 13  ALA A N   1 
ATOM   1983 C CA  . ALA B 1 26  ? -11.506 -6.343  32.686  1.00 23.96  ? 13  ALA A CA  1 
ATOM   1984 C C   . ALA B 1 26  ? -10.442 -7.344  33.165  1.00 26.61  ? 13  ALA A C   1 
ATOM   1985 O O   . ALA B 1 26  ? -10.422 -8.450  32.647  1.00 27.30  ? 13  ALA A O   1 
ATOM   1986 C CB  . ALA B 1 26  ? -12.901 -6.708  33.270  1.00 26.05  ? 13  ALA A CB  1 
ATOM   1987 N N   . ASP B 1 27  ? -9.578  -6.982  34.143  1.00 27.01  ? 14  ASP A N   1 
ATOM   1988 C CA  . ASP B 1 27  ? -8.626  -7.914  34.689  1.00 30.90  ? 14  ASP A CA  1 
ATOM   1989 C C   . ASP B 1 27  ? -7.452  -8.229  33.763  1.00 28.51  ? 14  ASP A C   1 
ATOM   1990 O O   . ASP B 1 27  ? -6.515  -8.842  34.252  1.00 29.69  ? 14  ASP A O   1 
ATOM   1991 C CB  . ASP B 1 27  ? -9.316  -9.155  35.243  1.00 31.86  ? 14  ASP A CB  1 
ATOM   1992 C CG  . ASP B 1 27  ? -10.342 -8.850  36.342  1.00 42.20  ? 14  ASP A CG  1 
ATOM   1993 O OD1 . ASP B 1 27  ? -10.147 -7.879  37.104  1.00 39.06  ? 14  ASP A OD1 1 
ATOM   1994 O OD2 . ASP B 1 27  ? -11.253 -9.658  36.534  1.00 51.35  ? 14  ASP A OD2 1 
ATOM   1995 N N   . LYS B 1 28  ? -7.497  -7.869  32.462  1.00 25.93  ? 15  LYS A N   1 
ATOM   1996 C CA  . LYS B 1 28  ? -6.394  -8.190  31.558  1.00 25.65  ? 15  LYS A CA  1 
ATOM   1997 C C   . LYS B 1 28  ? -5.141  -7.437  31.990  1.00 23.89  ? 15  LYS A C   1 
ATOM   1998 O O   . LYS B 1 28  ? -5.187  -6.276  32.427  1.00 23.08  ? 15  LYS A O   1 
ATOM   1999 C CB  . LYS B 1 28  ? -6.754  -7.792  30.125  1.00 24.01  ? 15  LYS A CB  1 
ATOM   2000 C CG  . LYS B 1 28  ? -7.858  -8.635  29.504  1.00 28.97  ? 15  LYS A CG  1 
ATOM   2001 C CD  . LYS B 1 28  ? -7.447  -9.992  28.960  1.00 39.29  ? 15  LYS A CD  1 
ATOM   2002 C CE  . LYS B 1 28  ? -8.478  -10.559 27.970  1.00 40.24  ? 15  LYS A CE  1 
ATOM   2003 N NZ  . LYS B 1 28  ? -9.167  -11.459 28.889  1.00 42.46  ? 15  LYS A NZ  1 
ATOM   2004 N N   . VAL B 1 29  ? -3.998  -8.076  31.803  1.00 23.11  ? 16  VAL A N   1 
ATOM   2005 C CA  . VAL B 1 29  ? -2.749  -7.457  32.228  1.00 22.63  ? 16  VAL A CA  1 
ATOM   2006 C C   . VAL B 1 29  ? -2.172  -6.774  31.001  1.00 21.48  ? 16  VAL A C   1 
ATOM   2007 O O   . VAL B 1 29  ? -1.964  -7.423  29.960  1.00 21.82  ? 16  VAL A O   1 
ATOM   2008 C CB  . VAL B 1 29  ? -1.798  -8.583  32.698  1.00 23.46  ? 16  VAL A CB  1 
ATOM   2009 C CG1 . VAL B 1 29  ? -0.355  -8.074  32.977  1.00 22.74  ? 16  VAL A CG1 1 
ATOM   2010 C CG2 . VAL B 1 29  ? -2.315  -9.296  33.955  1.00 25.81  ? 16  VAL A CG2 1 
ATOM   2011 N N   . VAL B 1 30  ? -1.972  -5.434  31.077  1.00 19.62  ? 17  VAL A N   1 
ATOM   2012 C CA  . VAL B 1 30  ? -1.613  -4.662  29.909  1.00 18.75  ? 17  VAL A CA  1 
ATOM   2013 C C   . VAL B 1 30  ? -0.280  -4.035  30.266  1.00 21.09  ? 17  VAL A C   1 
ATOM   2014 O O   . VAL B 1 30  ? -0.175  -3.567  31.392  1.00 24.47  ? 17  VAL A O   1 
ATOM   2015 C CB  . VAL B 1 30  ? -2.634  -3.509  29.742  1.00 20.28  ? 17  VAL A CB  1 
ATOM   2016 C CG1 . VAL B 1 30  ? -2.209  -2.540  28.636  1.00 19.66  ? 17  VAL A CG1 1 
ATOM   2017 C CG2 . VAL B 1 30  ? -4.041  -4.028  29.371  1.00 21.78  ? 17  VAL A CG2 1 
ATOM   2018 N N   . LEU B 1 31  ? 0.733   -4.059  29.357  1.00 21.19  ? 18  LEU A N   1 
ATOM   2019 C CA  . LEU B 1 31  ? 2.072   -3.543  29.595  1.00 22.04  ? 18  LEU A CA  1 
ATOM   2020 C C   . LEU B 1 31  ? 2.387   -2.536  28.477  1.00 19.79  ? 18  LEU A C   1 
ATOM   2021 O O   . LEU B 1 31  ? 2.288   -2.907  27.303  1.00 21.25  ? 18  LEU A O   1 
ATOM   2022 C CB  . LEU B 1 31  ? 3.084   -4.686  29.551  1.00 20.22  ? 18  LEU A CB  1 
ATOM   2023 C CG  . LEU B 1 31  ? 4.553   -4.210  29.612  1.00 24.45  ? 18  LEU A CG  1 
ATOM   2024 C CD1 . LEU B 1 31  ? 4.843   -3.405  30.887  1.00 25.09  ? 18  LEU A CD1 1 
ATOM   2025 C CD2 . LEU B 1 31  ? 5.457   -5.477  29.495  1.00 23.29  ? 18  LEU A CD2 1 
ATOM   2026 N N   . ILE B 1 32  ? 2.646   -1.269  28.881  1.00 20.13  ? 19  ILE A N   1 
ATOM   2027 C CA  . ILE B 1 32  ? 2.787   -0.182  27.906  1.00 18.39  ? 19  ILE A CA  1 
ATOM   2028 C C   . ILE B 1 32  ? 4.166   0.451   28.167  1.00 21.10  ? 19  ILE A C   1 
ATOM   2029 O O   . ILE B 1 32  ? 4.479   0.844   29.297  1.00 22.65  ? 19  ILE A O   1 
ATOM   2030 C CB  . ILE B 1 32  ? 1.657   0.860   28.112  1.00 18.97  ? 19  ILE A CB  1 
ATOM   2031 C CG1 . ILE B 1 32  ? 0.250   0.181   27.933  1.00 16.67  ? 19  ILE A CG1 1 
ATOM   2032 C CG2 . ILE B 1 32  ? 1.916   2.143   27.269  1.00 16.19  ? 19  ILE A CG2 1 
ATOM   2033 C CD1 . ILE B 1 32  ? -0.855  0.958   28.658  1.00 20.41  ? 19  ILE A CD1 1 
ATOM   2034 N N   . SER B 1 33  ? 5.009   0.479   27.119  1.00 20.46  ? 20  SER A N   1 
ATOM   2035 C CA  . SER B 1 33  ? 6.280   1.229   27.236  1.00 20.90  ? 20  SER A CA  1 
ATOM   2036 C C   . SER B 1 33  ? 6.034   2.702   26.921  1.00 21.74  ? 20  SER A C   1 
ATOM   2037 O O   . SER B 1 33  ? 5.095   3.023   26.195  1.00 22.72  ? 20  SER A O   1 
ATOM   2038 C CB  . SER B 1 33  ? 7.374   0.567   26.378  1.00 22.56  ? 20  SER A CB  1 
ATOM   2039 O OG  . SER B 1 33  ? 7.023   0.700   24.982  1.00 20.75  ? 20  SER A OG  1 
ATOM   2040 N N   . GLY B 1 34  ? 6.882   3.587   27.467  1.00 22.84  ? 21  GLY A N   1 
ATOM   2041 C CA  . GLY B 1 34  ? 6.663   5.023   27.340  1.00 21.65  ? 21  GLY A CA  1 
ATOM   2042 C C   . GLY B 1 34  ? 5.300   5.442   27.870  1.00 23.88  ? 21  GLY A C   1 
ATOM   2043 O O   . GLY B 1 34  ? 4.708   6.353   27.326  1.00 23.65  ? 21  GLY A O   1 
ATOM   2044 N N   . GLY B 1 35  ? 4.900   4.910   29.045  1.00 23.46  ? 22  GLY A N   1 
ATOM   2045 C CA  . GLY B 1 35  ? 3.557   5.133   29.532  1.00 22.52  ? 22  GLY A CA  1 
ATOM   2046 C C   . GLY B 1 35  ? 3.333   6.326   30.450  1.00 23.28  ? 22  GLY A C   1 
ATOM   2047 O O   . GLY B 1 35  ? 2.201   6.550   30.819  1.00 23.88  ? 22  GLY A O   1 
ATOM   2048 N N   . ALA B 1 36  ? 4.355   7.149   30.774  1.00 22.88  ? 23  ALA A N   1 
ATOM   2049 C CA  . ALA B 1 36  ? 4.116   8.148   31.819  1.00 22.97  ? 23  ALA A CA  1 
ATOM   2050 C C   . ALA B 1 36  ? 3.615   9.517   31.317  1.00 25.77  ? 23  ALA A C   1 
ATOM   2051 O O   . ALA B 1 36  ? 3.104   10.351  32.084  1.00 26.89  ? 23  ALA A O   1 
ATOM   2052 C CB  . ALA B 1 36  ? 5.361   8.316   32.684  1.00 28.08  ? 23  ALA A CB  1 
ATOM   2053 N N   . SER B 1 37  ? 3.780   9.776   30.006  1.00 27.31  ? 24  SER A N   1 
ATOM   2054 C CA  . SER B 1 37  ? 3.380   11.045  29.413  1.00 27.60  ? 24  SER A CA  1 
ATOM   2055 C C   . SER B 1 37  ? 2.806   10.817  27.992  1.00 24.80  ? 24  SER A C   1 
ATOM   2056 O O   . SER B 1 37  ? 2.824   9.677   27.468  1.00 23.97  ? 24  SER A O   1 
ATOM   2057 C CB  . SER B 1 37  ? 4.579   11.982  29.327  1.00 29.07  ? 24  SER A CB  1 
ATOM   2058 O OG  . SER B 1 37  ? 5.545   11.382  28.455  1.00 29.73  ? 24  SER A OG  1 
ATOM   2059 N N   . GLY B 1 38  ? 2.111   11.835  27.473  1.00 27.30  ? 25  GLY A N   1 
ATOM   2060 C CA  . GLY B 1 38  ? 1.721   11.840  26.055  1.00 28.53  ? 25  GLY A CA  1 
ATOM   2061 C C   . GLY B 1 38  ? 0.747   10.696  25.738  1.00 25.28  ? 25  GLY A C   1 
ATOM   2062 O O   . GLY B 1 38  ? -0.177  10.386  26.522  1.00 25.72  ? 25  GLY A O   1 
ATOM   2063 N N   . ILE B 1 39  ? 0.951   10.039  24.573  1.00 23.32  ? 26  ILE A N   1 
ATOM   2064 C CA  . ILE B 1 39  ? 0.007   9.068   24.116  1.00 19.59  ? 26  ILE A CA  1 
ATOM   2065 C C   . ILE B 1 39  ? 0.031   7.848   25.062  1.00 20.30  ? 26  ILE A C   1 
ATOM   2066 O O   . ILE B 1 39  ? -1.031  7.273   25.381  1.00 17.47  ? 26  ILE A O   1 
ATOM   2067 C CB  . ILE B 1 39  ? 0.302   8.640   22.642  1.00 19.59  ? 26  ILE A CB  1 
ATOM   2068 C CG1 . ILE B 1 39  ? 0.050   9.820   21.740  1.00 20.69  ? 26  ILE A CG1 1 
ATOM   2069 C CG2 . ILE B 1 39  ? -0.699  7.525   22.308  1.00 19.19  ? 26  ILE A CG2 1 
ATOM   2070 C CD1 . ILE B 1 39  ? 0.592   9.632   20.323  1.00 22.60  ? 26  ILE A CD1 1 
ATOM   2071 N N   . GLY B 1 40  ? 1.251   7.491   25.498  1.00 19.19  ? 27  GLY A N   1 
ATOM   2072 C CA  . GLY B 1 40  ? 1.331   6.289   26.311  1.00 20.07  ? 27  GLY A CA  1 
ATOM   2073 C C   . GLY B 1 40  ? 0.547   6.484   27.632  1.00 20.17  ? 27  GLY A C   1 
ATOM   2074 O O   . GLY B 1 40  ? -0.090  5.559   28.127  1.00 19.89  ? 27  GLY A O   1 
ATOM   2075 N N   . ARG B 1 41  ? 0.513   7.746   28.136  1.00 19.58  ? 28  ARG A N   1 
ATOM   2076 C CA  . ARG B 1 41  ? -0.237  8.071   29.344  1.00 19.12  ? 28  ARG A CA  1 
ATOM   2077 C C   . ARG B 1 41  ? -1.731  7.885   29.105  1.00 20.15  ? 28  ARG A C   1 
ATOM   2078 O O   . ARG B 1 41  ? -2.514  7.430   29.932  1.00 21.10  ? 28  ARG A O   1 
ATOM   2079 C CB  . ARG B 1 41  ? 0.099   9.451   29.935  1.00 20.16  ? 28  ARG A CB  1 
ATOM   2080 C CG  . ARG B 1 41  ? -0.902  9.946   30.979  1.00 23.01  ? 28  ARG A CG  1 
ATOM   2081 C CD  . ARG B 1 41  ? -0.533  11.293  31.553  1.00 27.11  ? 28  ARG A CD  1 
ATOM   2082 N NE  . ARG B 1 41  ? -1.659  11.620  32.445  1.00 28.51  ? 28  ARG A NE  1 
ATOM   2083 C CZ  . ARG B 1 41  ? -1.563  12.622  33.320  1.00 29.67  ? 28  ARG A CZ  1 
ATOM   2084 N NH1 . ARG B 1 41  ? -0.423  13.292  33.407  1.00 31.00  ? 28  ARG A NH1 1 
ATOM   2085 N NH2 . ARG B 1 41  ? -2.590  13.000  34.102  1.00 31.33  ? 28  ARG A NH2 1 
ATOM   2086 N N   . ALA B 1 42  ? -2.183  8.271   27.925  1.00 19.15  ? 29  ALA A N   1 
ATOM   2087 C CA  . ALA B 1 42  ? -3.562  8.100   27.630  1.00 19.45  ? 29  ALA A CA  1 
ATOM   2088 C C   . ALA B 1 42  ? -3.914  6.599   27.529  1.00 19.31  ? 29  ALA A C   1 
ATOM   2089 O O   . ALA B 1 42  ? -4.972  6.201   27.960  1.00 20.14  ? 29  ALA A O   1 
ATOM   2090 C CB  . ALA B 1 42  ? -3.896  8.853   26.363  1.00 19.03  ? 29  ALA A CB  1 
ATOM   2091 N N   . PHE B 1 43  ? -3.003  5.746   27.036  1.00 18.57  ? 30  PHE A N   1 
ATOM   2092 C CA  . PHE B 1 43  ? -3.279  4.332   27.030  1.00 18.55  ? 30  PHE A CA  1 
ATOM   2093 C C   . PHE B 1 43  ? -3.431  3.832   28.457  1.00 20.36  ? 30  PHE A C   1 
ATOM   2094 O O   . PHE B 1 43  ? -4.392  3.122   28.786  1.00 19.91  ? 30  PHE A O   1 
ATOM   2095 C CB  . PHE B 1 43  ? -2.157  3.492   26.380  1.00 17.86  ? 30  PHE A CB  1 
ATOM   2096 C CG  . PHE B 1 43  ? -1.979  3.778   24.882  1.00 19.06  ? 30  PHE A CG  1 
ATOM   2097 C CD1 . PHE B 1 43  ? -3.046  4.066   24.055  1.00 18.97  ? 30  PHE A CD1 1 
ATOM   2098 C CD2 . PHE B 1 43  ? -0.707  3.633   24.302  1.00 19.91  ? 30  PHE A CD2 1 
ATOM   2099 C CE1 . PHE B 1 43  ? -2.838  4.287   22.673  1.00 21.53  ? 30  PHE A CE1 1 
ATOM   2100 C CE2 . PHE B 1 43  ? -0.490  3.844   22.938  1.00 18.98  ? 30  PHE A CE2 1 
ATOM   2101 C CZ  . PHE B 1 43  ? -1.600  4.110   22.121  1.00 19.26  ? 30  PHE A CZ  1 
ATOM   2102 N N   . VAL B 1 44  ? -2.508  4.248   29.340  1.00 21.54  ? 31  VAL A N   1 
ATOM   2103 C CA  . VAL B 1 44  ? -2.517  3.775   30.724  1.00 20.45  ? 31  VAL A CA  1 
ATOM   2104 C C   . VAL B 1 44  ? -3.856  4.143   31.339  1.00 22.15  ? 31  VAL A C   1 
ATOM   2105 O O   . VAL B 1 44  ? -4.534  3.297   31.909  1.00 20.71  ? 31  VAL A O   1 
ATOM   2106 C CB  . VAL B 1 44  ? -1.322  4.324   31.547  1.00 20.71  ? 31  VAL A CB  1 
ATOM   2107 C CG1 . VAL B 1 44  ? -1.427  3.930   33.049  1.00 19.63  ? 31  VAL A CG1 1 
ATOM   2108 C CG2 . VAL B 1 44  ? 0.013   3.883   30.952  1.00 21.00  ? 31  VAL A CG2 1 
ATOM   2109 N N   . GLU B 1 45  ? -4.256  5.404   31.214  1.00 19.72  ? 32  GLU A N   1 
ATOM   2110 C CA  . GLU B 1 45  ? -5.510  5.870   31.769  1.00 19.92  ? 32  GLU A CA  1 
ATOM   2111 C C   . GLU B 1 45  ? -6.725  5.086   31.224  1.00 19.51  ? 32  GLU A C   1 
ATOM   2112 O O   . GLU B 1 45  ? -7.615  4.724   32.019  1.00 20.76  ? 32  GLU A O   1 
ATOM   2113 C CB  . GLU B 1 45  ? -5.701  7.349   31.480  1.00 20.28  ? 32  GLU A CB  1 
ATOM   2114 C CG  . GLU B 1 45  ? -4.681  8.241   32.220  1.00 20.53  ? 32  GLU A CG  1 
ATOM   2115 C CD  . GLU B 1 45  ? -4.752  9.711   31.716  1.00 22.67  ? 32  GLU A CD  1 
ATOM   2116 O OE1 . GLU B 1 45  ? -5.171  9.973   30.587  1.00 22.15  ? 32  GLU A OE1 1 
ATOM   2117 O OE2 . GLU B 1 45  ? -4.251  10.641  32.434  1.00 24.45  ? 32  GLU A OE2 1 
ATOM   2118 N N   . ALA B 1 46  ? -6.744  4.864   29.887  1.00 19.07  ? 33  ALA A N   1 
ATOM   2119 C CA  . ALA B 1 46  ? -7.917  4.260   29.247  1.00 19.81  ? 33  ALA A CA  1 
ATOM   2120 C C   . ALA B 1 46  ? -8.014  2.825   29.752  1.00 18.04  ? 33  ALA A C   1 
ATOM   2121 O O   . ALA B 1 46  ? -9.118  2.353   29.948  1.00 19.10  ? 33  ALA A O   1 
ATOM   2122 C CB  . ALA B 1 46  ? -7.910  4.364   27.685  1.00 19.25  ? 33  ALA A CB  1 
ATOM   2123 N N   . PHE B 1 47  ? -6.904  2.089   29.778  1.00 18.28  ? 34  PHE A N   1 
ATOM   2124 C CA  . PHE B 1 47  ? -7.098  0.687   30.172  1.00 19.03  ? 34  PHE A CA  1 
ATOM   2125 C C   . PHE B 1 47  ? -7.399  0.571   31.662  1.00 22.28  ? 34  PHE A C   1 
ATOM   2126 O O   . PHE B 1 47  ? -8.173  -0.339  32.064  1.00 22.79  ? 34  PHE A O   1 
ATOM   2127 C CB  . PHE B 1 47  ? -5.847  -0.146  29.840  1.00 19.16  ? 34  PHE A CB  1 
ATOM   2128 C CG  . PHE B 1 47  ? -5.754  -0.475  28.346  1.00 19.14  ? 34  PHE A CG  1 
ATOM   2129 C CD1 . PHE B 1 47  ? -6.346  -1.621  27.833  1.00 23.39  ? 34  PHE A CD1 1 
ATOM   2130 C CD2 . PHE B 1 47  ? -5.041  0.352   27.479  1.00 18.79  ? 34  PHE A CD2 1 
ATOM   2131 C CE1 . PHE B 1 47  ? -6.242  -1.945  26.489  1.00 19.88  ? 34  PHE A CE1 1 
ATOM   2132 C CE2 . PHE B 1 47  ? -4.956  0.042   26.105  1.00 21.67  ? 34  PHE A CE2 1 
ATOM   2133 C CZ  . PHE B 1 47  ? -5.529  -1.117  25.624  1.00 18.98  ? 34  PHE A CZ  1 
ATOM   2134 N N   . VAL B 1 48  ? -6.868  1.472   32.474  1.00 21.34  ? 35  VAL A N   1 
ATOM   2135 C CA  . VAL B 1 48  ? -7.188  1.391   33.899  1.00 24.70  ? 35  VAL A CA  1 
ATOM   2136 C C   . VAL B 1 48  ? -8.706  1.601   34.039  1.00 23.17  ? 35  VAL A C   1 
ATOM   2137 O O   . VAL B 1 48  ? -9.346  0.898   34.820  1.00 25.12  ? 35  VAL A O   1 
ATOM   2138 C CB  . VAL B 1 48  ? -6.359  2.336   34.798  1.00 23.49  ? 35  VAL A CB  1 
ATOM   2139 C CG1 . VAL B 1 48  ? -6.907  2.451   36.234  1.00 24.32  ? 35  VAL A CG1 1 
ATOM   2140 C CG2 . VAL B 1 48  ? -4.895  1.941   34.931  1.00 22.86  ? 35  VAL A CG2 1 
ATOM   2141 N N   . ALA B 1 49  ? -9.257  2.584   33.327  1.00 23.36  ? 36  ALA A N   1 
ATOM   2142 C CA  . ALA B 1 49  ? -10.702 2.846   33.346  1.00 22.54  ? 36  ALA A CA  1 
ATOM   2143 C C   . ALA B 1 49  ? -11.539 1.611   32.932  1.00 24.21  ? 36  ALA A C   1 
ATOM   2144 O O   . ALA B 1 49  ? -12.669 1.470   33.313  1.00 27.24  ? 36  ALA A O   1 
ATOM   2145 C CB  . ALA B 1 49  ? -10.967 4.048   32.414  1.00 22.86  ? 36  ALA A CB  1 
ATOM   2146 N N   . GLN B 1 50  ? -11.043 0.733   32.057  1.00 22.41  ? 37  GLN A N   1 
ATOM   2147 C CA  . GLN B 1 50  ? -11.786 -0.457  31.602  1.00 22.04  ? 37  GLN A CA  1 
ATOM   2148 C C   . GLN B 1 50  ? -11.602 -1.602  32.620  1.00 24.40  ? 37  GLN A C   1 
ATOM   2149 O O   . GLN B 1 50  ? -12.101 -2.722  32.430  1.00 24.37  ? 37  GLN A O   1 
ATOM   2150 C CB  . GLN B 1 50  ? -11.270 -0.925  30.239  1.00 20.16  ? 37  GLN A CB  1 
ATOM   2151 C CG  . GLN B 1 50  ? -11.485 0.052   29.080  1.00 18.02  ? 37  GLN A CG  1 
ATOM   2152 C CD  . GLN B 1 50  ? -12.923 0.201   28.660  1.00 20.59  ? 37  GLN A CD  1 
ATOM   2153 O OE1 . GLN B 1 50  ? -13.699 -0.771  28.792  1.00 20.91  ? 37  GLN A OE1 1 
ATOM   2154 N NE2 . GLN B 1 50  ? -13.292 1.426   28.237  1.00 20.02  ? 37  GLN A NE2 1 
ATOM   2155 N N   . GLY B 1 51  ? -10.876 -1.339  33.718  1.00 24.81  ? 38  GLY A N   1 
ATOM   2156 C CA  . GLY B 1 51  ? -10.718 -2.390  34.723  1.00 22.82  ? 38  GLY A CA  1 
ATOM   2157 C C   . GLY B 1 51  ? -9.525  -3.343  34.458  1.00 23.10  ? 38  GLY A C   1 
ATOM   2158 O O   . GLY B 1 51  ? -9.380  -4.365  35.158  1.00 25.06  ? 38  GLY A O   1 
ATOM   2159 N N   . SER B 1 52  ? -8.643  -3.011  33.479  1.00 20.10  ? 39  SER A N   1 
ATOM   2160 C CA  . SER B 1 52  ? -7.395  -3.766  33.264  1.00 20.36  ? 39  SER A CA  1 
ATOM   2161 C C   . SER B 1 52  ? -6.394  -3.567  34.422  1.00 22.17  ? 39  SER A C   1 
ATOM   2162 O O   . SER B 1 52  ? -6.402  -2.502  35.119  1.00 23.60  ? 39  SER A O   1 
ATOM   2163 C CB  . SER B 1 52  ? -6.761  -3.288  31.949  1.00 18.32  ? 39  SER A CB  1 
ATOM   2164 O OG  . SER B 1 52  ? -7.693  -3.429  30.894  1.00 19.10  ? 39  SER A OG  1 
ATOM   2165 N N   . ARG B 1 53  ? -5.403  -4.480  34.520  1.00 21.52  ? 40  ARG A N   1 
ATOM   2166 C CA  . ARG B 1 53  ? -4.251  -4.326  35.390  1.00 23.34  ? 40  ARG A CA  1 
ATOM   2167 C C   . ARG B 1 53  ? -3.082  -3.848  34.517  1.00 21.73  ? 40  ARG A C   1 
ATOM   2168 O O   . ARG B 1 53  ? -2.668  -4.555  33.623  1.00 22.90  ? 40  ARG A O   1 
ATOM   2169 C CB  . ARG B 1 53  ? -3.974  -5.688  36.029  1.00 23.32  ? 40  ARG A CB  1 
ATOM   2170 C CG  . ARG B 1 53  ? -4.976  -5.973  37.158  1.00 26.85  ? 40  ARG A CG  1 
ATOM   2171 C CD  . ARG B 1 53  ? -4.797  -7.308  37.837  1.00 30.09  ? 40  ARG A CD  1 
ATOM   2172 N NE  . ARG B 1 53  ? -4.785  -8.342  36.787  1.00 33.45  ? 40  ARG A NE  1 
ATOM   2173 C CZ  . ARG B 1 53  ? -4.453  -9.648  36.927  1.00 38.08  ? 40  ARG A CZ  1 
ATOM   2174 N NH1 . ARG B 1 53  ? -3.737  -10.024 37.996  1.00 35.99  ? 40  ARG A NH1 1 
ATOM   2175 N NH2 . ARG B 1 53  ? -4.795  -10.559 35.980  1.00 33.44  ? 40  ARG A NH2 1 
ATOM   2176 N N   . VAL B 1 54  ? -2.688  -2.600  34.701  1.00 21.40  ? 41  VAL A N   1 
ATOM   2177 C CA  . VAL B 1 54  ? -1.849  -1.902  33.708  1.00 20.85  ? 41  VAL A CA  1 
ATOM   2178 C C   . VAL B 1 54  ? -0.461  -1.621  34.321  1.00 23.78  ? 41  VAL A C   1 
ATOM   2179 O O   . VAL B 1 54  ? -0.326  -0.809  35.254  1.00 23.02  ? 41  VAL A O   1 
ATOM   2180 C CB  . VAL B 1 54  ? -2.514  -0.576  33.260  1.00 23.12  ? 41  VAL A CB  1 
ATOM   2181 C CG1 . VAL B 1 54  ? -1.711  0.179   32.180  1.00 22.33  ? 41  VAL A CG1 1 
ATOM   2182 C CG2 . VAL B 1 54  ? -3.914  -0.800  32.716  1.00 20.69  ? 41  VAL A CG2 1 
ATOM   2183 N N   . ALA B 1 55  ? 0.570   -2.260  33.743  1.00 22.29  ? 42  ALA A N   1 
ATOM   2184 C CA  . ALA B 1 55  ? 1.925   -1.939  34.145  1.00 22.87  ? 42  ALA A CA  1 
ATOM   2185 C C   . ALA B 1 55  ? 2.489   -1.007  33.051  1.00 21.64  ? 42  ALA A C   1 
ATOM   2186 O O   . ALA B 1 55  ? 2.152   -1.202  31.850  1.00 23.21  ? 42  ALA A O   1 
ATOM   2187 C CB  . ALA B 1 55  ? 2.644   -3.282  34.131  1.00 21.35  ? 42  ALA A CB  1 
ATOM   2188 N N   . PHE B 1 56  ? 3.288   -0.007  33.407  1.00 22.58  ? 43  PHE A N   1 
ATOM   2189 C CA  . PHE B 1 56  ? 3.862   0.796   32.338  1.00 22.42  ? 43  PHE A CA  1 
ATOM   2190 C C   . PHE B 1 56  ? 5.303   1.138   32.691  1.00 23.17  ? 43  PHE A C   1 
ATOM   2191 O O   . PHE B 1 56  ? 5.713   1.257   33.863  1.00 25.11  ? 43  PHE A O   1 
ATOM   2192 C CB  . PHE B 1 56  ? 2.964   2.015   32.063  1.00 22.04  ? 43  PHE A CB  1 
ATOM   2193 C CG  . PHE B 1 56  ? 2.841   2.968   33.247  1.00 22.02  ? 43  PHE A CG  1 
ATOM   2194 C CD1 . PHE B 1 56  ? 1.940   2.695   34.275  1.00 22.28  ? 43  PHE A CD1 1 
ATOM   2195 C CD2 . PHE B 1 56  ? 3.546   4.169   33.289  1.00 24.63  ? 43  PHE A CD2 1 
ATOM   2196 C CE1 . PHE B 1 56  ? 1.820   3.554   35.380  1.00 23.45  ? 43  PHE A CE1 1 
ATOM   2197 C CE2 . PHE B 1 56  ? 3.424   5.031   34.413  1.00 24.88  ? 43  PHE A CE2 1 
ATOM   2198 C CZ  . PHE B 1 56  ? 2.578   4.723   35.440  1.00 23.15  ? 43  PHE A CZ  1 
ATOM   2199 N N   . LEU B 1 57  ? 6.098   1.310   31.622  1.00 22.99  ? 44  LEU A N   1 
ATOM   2200 C CA  . LEU B 1 57  ? 7.525   1.634   31.790  1.00 26.47  ? 44  LEU A CA  1 
ATOM   2201 C C   . LEU B 1 57  ? 7.770   3.039   31.277  1.00 27.43  ? 44  LEU A C   1 
ATOM   2202 O O   . LEU B 1 57  ? 7.145   3.414   30.298  1.00 27.70  ? 44  LEU A O   1 
ATOM   2203 C CB  . LEU B 1 57  ? 8.355   0.661   30.958  1.00 26.42  ? 44  LEU A CB  1 
ATOM   2204 C CG  . LEU B 1 57  ? 7.878   -0.788  30.961  1.00 26.59  ? 44  LEU A CG  1 
ATOM   2205 C CD1 . LEU B 1 57  ? 8.851   -1.511  30.072  1.00 25.94  ? 44  LEU A CD1 1 
ATOM   2206 C CD2 . LEU B 1 57  ? 7.861   -1.363  32.344  1.00 27.06  ? 44  LEU A CD2 1 
ATOM   2207 N N   . ASP B 1 58  ? 8.704   3.776   31.908  1.00 26.23  ? 45  ASP A N   1 
ATOM   2208 C CA  . ASP B 1 58  ? 9.109   5.059   31.372  1.00 28.47  ? 45  ASP A CA  1 
ATOM   2209 C C   . ASP B 1 58  ? 10.475  5.409   31.956  1.00 30.79  ? 45  ASP A C   1 
ATOM   2210 O O   . ASP B 1 58  ? 10.851  4.894   32.982  1.00 28.67  ? 45  ASP A O   1 
ATOM   2211 C CB  . ASP B 1 58  ? 8.134   6.175   31.696  1.00 30.75  ? 45  ASP A CB  1 
ATOM   2212 C CG  . ASP B 1 58  ? 8.084   7.323   30.682  1.00 32.51  ? 45  ASP A CG  1 
ATOM   2213 O OD1 . ASP B 1 58  ? 8.879   8.274   30.804  1.00 33.75  ? 45  ASP A OD1 1 
ATOM   2214 O OD2 . ASP B 1 58  ? 7.152   7.312   29.841  1.00 24.72  ? 45  ASP A OD2 1 
ATOM   2215 N N   . LEU B 1 59  ? 11.223  6.256   31.229  1.00 30.10  ? 46  LEU A N   1 
ATOM   2216 C CA  . LEU B 1 59  ? 12.471  6.769   31.733  1.00 33.07  ? 46  LEU A CA  1 
ATOM   2217 C C   . LEU B 1 59  ? 12.187  7.769   32.840  1.00 32.93  ? 46  LEU A C   1 
ATOM   2218 O O   . LEU B 1 59  ? 12.963  7.836   33.757  1.00 37.22  ? 46  LEU A O   1 
ATOM   2219 C CB  . LEU B 1 59  ? 13.069  7.427   30.478  1.00 33.64  ? 46  LEU A CB  1 
ATOM   2220 C CG  . LEU B 1 59  ? 14.395  8.174   30.660  1.00 43.30  ? 46  LEU A CG  1 
ATOM   2221 C CD1 . LEU B 1 59  ? 15.433  7.118   31.020  1.00 45.55  ? 46  LEU A CD1 1 
ATOM   2222 C CD2 . LEU B 1 59  ? 14.774  8.979   29.421  1.00 46.44  ? 46  LEU A CD2 1 
ATOM   2223 N N   . ASP B 1 60  ? 11.093  8.554   32.757  1.00 32.50  ? 47  ASP A N   1 
ATOM   2224 C CA  . ASP B 1 60  ? 10.846  9.627   33.715  1.00 33.78  ? 47  ASP A CA  1 
ATOM   2225 C C   . ASP B 1 60  ? 10.243  9.059   35.001  1.00 35.37  ? 47  ASP A C   1 
ATOM   2226 O O   . ASP B 1 60  ? 9.039   8.829   35.012  1.00 32.44  ? 47  ASP A O   1 
ATOM   2227 C CB  . ASP B 1 60  ? 9.941   10.685  33.113  1.00 32.30  ? 47  ASP A CB  1 
ATOM   2228 C CG  . ASP B 1 60  ? 9.830   11.970  33.943  1.00 34.57  ? 47  ASP A CG  1 
ATOM   2229 O OD1 . ASP B 1 60  ? 10.038  11.926  35.135  1.00 34.93  ? 47  ASP A OD1 1 
ATOM   2230 O OD2 . ASP B 1 60  ? 9.529   13.035  33.400  1.00 37.44  ? 47  ASP A OD2 1 
ATOM   2231 N N   . ALA B 1 61  ? 11.062  8.823   36.060  1.00 34.55  ? 48  ALA A N   1 
ATOM   2232 C CA  . ALA B 1 61  ? 10.599  8.112   37.260  1.00 35.66  ? 48  ALA A CA  1 
ATOM   2233 C C   . ALA B 1 61  ? 9.575   8.964   38.008  1.00 36.79  ? 48  ALA A C   1 
ATOM   2234 O O   . ALA B 1 61  ? 8.639   8.429   38.592  1.00 37.03  ? 48  ALA A O   1 
ATOM   2235 C CB  . ALA B 1 61  ? 11.769  7.788   38.211  1.00 34.56  ? 48  ALA A CB  1 
ATOM   2236 N N   . GLU B 1 62  ? 9.802   10.292  38.067  1.00 37.80  ? 49  GLU A N   1 
ATOM   2237 C CA  . GLU B 1 62  ? 8.943   11.213  38.804  1.00 36.64  ? 49  GLU A CA  1 
ATOM   2238 C C   . GLU B 1 62  ? 7.557   11.272  38.153  1.00 35.24  ? 49  GLU A C   1 
ATOM   2239 O O   . GLU B 1 62  ? 6.521   11.150  38.824  1.00 33.17  ? 49  GLU A O   1 
ATOM   2240 C CB  . GLU B 1 62  ? 9.583   12.586  38.999  1.00 37.29  ? 49  GLU A CB  1 
ATOM   2241 N N   . ALA B 1 63  ? 7.526   11.361  36.811  1.00 33.55  ? 50  ALA A N   1 
ATOM   2242 C CA  . ALA B 1 63  ? 6.264   11.352  36.114  1.00 30.67  ? 50  ALA A CA  1 
ATOM   2243 C C   . ALA B 1 63  ? 5.582   9.983   36.288  1.00 28.69  ? 50  ALA A C   1 
ATOM   2244 O O   . ALA B 1 63  ? 4.364   9.919   36.487  1.00 26.84  ? 50  ALA A O   1 
ATOM   2245 C CB  . ALA B 1 63  ? 6.561   11.630  34.623  1.00 28.54  ? 50  ALA A CB  1 
ATOM   2246 N N   . GLY B 1 64  ? 6.360   8.896   36.236  1.00 26.21  ? 51  GLY A N   1 
ATOM   2247 C CA  . GLY B 1 64  ? 5.770   7.563   36.283  1.00 25.14  ? 51  GLY A CA  1 
ATOM   2248 C C   . GLY B 1 64  ? 5.117   7.295   37.657  1.00 26.30  ? 51  GLY A C   1 
ATOM   2249 O O   . GLY B 1 64  ? 4.003   6.790   37.745  1.00 26.99  ? 51  GLY A O   1 
ATOM   2250 N N   . GLN B 1 65  ? 5.849   7.648   38.677  1.00 28.14  ? 52  GLN A N   1 
ATOM   2251 C CA  . GLN B 1 65  ? 5.448   7.471   40.067  1.00 31.07  ? 52  GLN A CA  1 
ATOM   2252 C C   . GLN B 1 65  ? 4.201   8.318   40.300  1.00 30.13  ? 52  GLN A C   1 
ATOM   2253 O O   . GLN B 1 65  ? 3.257   7.797   40.896  1.00 29.20  ? 52  GLN A O   1 
ATOM   2254 C CB  . GLN B 1 65  ? 6.534   7.852   41.095  1.00 34.53  ? 52  GLN A CB  1 
ATOM   2255 C CG  . GLN B 1 65  ? 7.723   6.896   41.148  1.00 39.73  ? 52  GLN A CG  1 
ATOM   2256 C CD  . GLN B 1 65  ? 8.921   7.465   41.887  1.00 48.04  ? 52  GLN A CD  1 
ATOM   2257 O OE1 . GLN B 1 65  ? 8.799   8.277   42.820  1.00 56.66  ? 52  GLN A OE1 1 
ATOM   2258 N NE2 . GLN B 1 65  ? 10.107  7.032   41.490  1.00 43.04  ? 52  GLN A NE2 1 
ATOM   2259 N N   . GLY B 1 66  ? 4.196   9.583   39.831  1.00 28.39  ? 53  GLY A N   1 
ATOM   2260 C CA  . GLY B 1 66  ? 3.058   10.468  39.948  1.00 28.27  ? 53  GLY A CA  1 
ATOM   2261 C C   . GLY B 1 66  ? 1.815   9.798   39.354  1.00 27.62  ? 53  GLY A C   1 
ATOM   2262 O O   . GLY B 1 66  ? 0.738   9.803   39.992  1.00 28.19  ? 53  GLY A O   1 
ATOM   2263 N N   . LEU B 1 67  ? 1.936   9.300   38.090  1.00 25.29  ? 54  LEU A N   1 
ATOM   2264 C CA  . LEU B 1 67  ? 0.800   8.746   37.392  1.00 26.23  ? 54  LEU A CA  1 
ATOM   2265 C C   . LEU B 1 67  ? 0.296   7.460   38.072  1.00 28.31  ? 54  LEU A C   1 
ATOM   2266 O O   . LEU B 1 67  ? -0.911  7.332   38.296  1.00 26.69  ? 54  LEU A O   1 
ATOM   2267 C CB  . LEU B 1 67  ? 1.163   8.520   35.928  1.00 26.10  ? 54  LEU A CB  1 
ATOM   2268 C CG  . LEU B 1 67  ? 0.010   7.965   35.084  1.00 24.89  ? 54  LEU A CG  1 
ATOM   2269 C CD1 . LEU B 1 67  ? -1.129  8.949   35.019  1.00 26.29  ? 54  LEU A CD1 1 
ATOM   2270 C CD2 . LEU B 1 67  ? 0.507   7.615   33.711  1.00 27.53  ? 54  LEU A CD2 1 
ATOM   2271 N N   . ALA B 1 68  ? 1.196   6.555   38.487  1.00 26.03  ? 55  ALA A N   1 
ATOM   2272 C CA  . ALA B 1 68  ? 0.749   5.353   39.168  1.00 30.35  ? 55  ALA A CA  1 
ATOM   2273 C C   . ALA B 1 68  ? 0.107   5.656   40.530  1.00 30.38  ? 55  ALA A C   1 
ATOM   2274 O O   . ALA B 1 68  ? -0.847  4.974   40.908  1.00 28.64  ? 55  ALA A O   1 
ATOM   2275 C CB  . ALA B 1 68  ? 1.876   4.430   39.451  1.00 29.09  ? 55  ALA A CB  1 
ATOM   2276 N N   . HIS B 1 69  ? 0.634   6.626   41.280  1.00 28.38  ? 56  HIS A N   1 
ATOM   2277 C CA  . HIS B 1 69  ? -0.001  7.036   42.516  1.00 29.04  ? 56  HIS A CA  1 
ATOM   2278 C C   . HIS B 1 69  ? -1.406  7.571   42.248  1.00 29.28  ? 56  HIS A C   1 
ATOM   2279 O O   . HIS B 1 69  ? -2.324  7.350   43.050  1.00 30.99  ? 56  HIS A O   1 
ATOM   2280 C CB  . HIS B 1 69  ? 0.844   8.076   43.264  1.00 30.84  ? 56  HIS A CB  1 
ATOM   2281 C CG  . HIS B 1 69  ? 0.262   8.339   44.636  1.00 34.14  ? 56  HIS A CG  1 
ATOM   2282 N ND1 . HIS B 1 69  ? -0.536  9.445   44.910  1.00 35.36  ? 56  HIS A ND1 1 
ATOM   2283 C CD2 . HIS B 1 69  ? 0.303   7.624   45.793  1.00 36.14  ? 56  HIS A CD2 1 
ATOM   2284 C CE1 . HIS B 1 69  ? -0.955  9.388   46.175  1.00 35.57  ? 56  HIS A CE1 1 
ATOM   2285 N NE2 . HIS B 1 69  ? -0.498  8.267   46.703  1.00 38.25  ? 56  HIS A NE2 1 
ATOM   2286 N N   . ALA B 1 70  ? -1.576  8.374   41.209  1.00 27.34  ? 57  ALA A N   1 
ATOM   2287 C CA  . ALA B 1 70  ? -2.896  8.950   40.911  1.00 29.07  ? 57  ALA A CA  1 
ATOM   2288 C C   . ALA B 1 70  ? -3.909  7.864   40.540  1.00 29.02  ? 57  ALA A C   1 
ATOM   2289 O O   . ALA B 1 70  ? -5.066  7.947   40.952  1.00 31.41  ? 57  ALA A O   1 
ATOM   2290 C CB  . ALA B 1 70  ? -2.798  10.017  39.811  1.00 27.28  ? 57  ALA A CB  1 
ATOM   2291 N N   . LEU B 1 71  ? -3.482  6.854   39.773  1.00 27.33  ? 58  LEU A N   1 
ATOM   2292 C CA  . LEU B 1 71  ? -4.408  5.867   39.222  1.00 27.82  ? 58  LEU A CA  1 
ATOM   2293 C C   . LEU B 1 71  ? -4.701  4.736   40.212  1.00 28.98  ? 58  LEU A C   1 
ATOM   2294 O O   . LEU B 1 71  ? -5.663  4.001   40.011  1.00 28.97  ? 58  LEU A O   1 
ATOM   2295 C CB  . LEU B 1 71  ? -3.929  5.316   37.873  1.00 27.51  ? 58  LEU A CB  1 
ATOM   2296 C CG  . LEU B 1 71  ? -3.792  6.418   36.814  1.00 30.49  ? 58  LEU A CG  1 
ATOM   2297 C CD1 . LEU B 1 71  ? -3.251  5.655   35.581  1.00 29.17  ? 58  LEU A CD1 1 
ATOM   2298 C CD2 . LEU B 1 71  ? -5.164  7.005   36.535  1.00 32.73  ? 58  LEU A CD2 1 
ATOM   2299 N N   . GLY B 1 72  ? -3.811  4.535   41.173  1.00 32.49  ? 59  GLY A N   1 
ATOM   2300 C CA  . GLY B 1 72  ? -4.011  3.578   42.267  1.00 32.52  ? 59  GLY A CA  1 
ATOM   2301 C C   . GLY B 1 72  ? -3.545  2.176   41.873  1.00 32.29  ? 59  GLY A C   1 
ATOM   2302 O O   . GLY B 1 72  ? -2.829  1.997   40.877  1.00 31.05  ? 59  GLY A O   1 
ATOM   2303 N N   . ALA B 1 73  ? -4.095  1.174   42.591  1.00 31.98  ? 60  ALA A N   1 
ATOM   2304 C CA  . ALA B 1 73  ? -3.471  -0.149  42.774  1.00 33.27  ? 60  ALA A CA  1 
ATOM   2305 C C   . ALA B 1 73  ? -3.528  -1.050  41.528  1.00 30.55  ? 60  ALA A C   1 
ATOM   2306 O O   . ALA B 1 73  ? -2.783  -2.041  41.435  1.00 31.07  ? 60  ALA A O   1 
ATOM   2307 C CB  . ALA B 1 73  ? -4.125  -0.838  43.999  1.00 35.18  ? 60  ALA A CB  1 
ATOM   2308 N N   . ASN B 1 74  ? -4.408  -0.749  40.582  1.00 27.91  ? 61  ASN A N   1 
ATOM   2309 C CA  . ASN B 1 74  ? -4.393  -1.547  39.366  1.00 27.66  ? 61  ASN A CA  1 
ATOM   2310 C C   . ASN B 1 74  ? -3.431  -0.932  38.349  1.00 29.61  ? 61  ASN A C   1 
ATOM   2311 O O   . ASN B 1 74  ? -3.450  -1.340  37.164  1.00 28.01  ? 61  ASN A O   1 
ATOM   2312 C CB  . ASN B 1 74  ? -5.761  -1.579  38.705  1.00 30.97  ? 61  ASN A CB  1 
ATOM   2313 C CG  . ASN B 1 74  ? -6.702  -2.499  39.453  1.00 36.07  ? 61  ASN A CG  1 
ATOM   2314 O OD1 . ASN B 1 74  ? -6.249  -3.378  40.187  1.00 39.06  ? 61  ASN A OD1 1 
ATOM   2315 N ND2 . ASN B 1 74  ? -7.995  -2.335  39.256  1.00 38.54  ? 61  ASN A ND2 1 
ATOM   2316 N N   . SER B 1 75  ? -2.645  0.065   38.787  1.00 26.25  ? 62  SER A N   1 
ATOM   2317 C CA  . SER B 1 75  ? -1.541  0.521   37.945  1.00 25.36  ? 62  SER A CA  1 
ATOM   2318 C C   . SER B 1 75  ? -0.196  0.195   38.582  1.00 26.23  ? 62  SER A C   1 
ATOM   2319 O O   . SER B 1 75  ? -0.051  0.083   39.785  1.00 26.77  ? 62  SER A O   1 
ATOM   2320 C CB  . SER B 1 75  ? -1.714  1.977   37.564  1.00 25.26  ? 62  SER A CB  1 
ATOM   2321 O OG  . SER B 1 75  ? -1.382  2.829   38.645  1.00 27.21  ? 62  SER A OG  1 
ATOM   2322 N N   . LEU B 1 76  ? 0.832   0.002   37.774  1.00 24.57  ? 63  LEU A N   1 
ATOM   2323 C CA  . LEU B 1 76  ? 2.139   -0.403  38.275  1.00 26.54  ? 63  LEU A CA  1 
ATOM   2324 C C   . LEU B 1 76  ? 3.215   0.279   37.415  1.00 28.54  ? 63  LEU A C   1 
ATOM   2325 O O   . LEU B 1 76  ? 3.290   -0.036  36.232  1.00 27.34  ? 63  LEU A O   1 
ATOM   2326 C CB  . LEU B 1 76  ? 2.285   -1.924  38.225  1.00 29.87  ? 63  LEU A CB  1 
ATOM   2327 C CG  . LEU B 1 76  ? 3.697   -2.482  38.514  1.00 36.66  ? 63  LEU A CG  1 
ATOM   2328 C CD1 . LEU B 1 76  ? 4.074   -2.237  39.954  1.00 39.71  ? 63  LEU A CD1 1 
ATOM   2329 C CD2 . LEU B 1 76  ? 3.862   -3.983  38.176  1.00 36.57  ? 63  LEU A CD2 1 
ATOM   2330 N N   . PHE B 1 77  ? 4.000   1.209   38.015  1.00 28.53  ? 64  PHE A N   1 
ATOM   2331 C CA  . PHE B 1 77  ? 5.010   1.905   37.221  1.00 27.47  ? 64  PHE A CA  1 
ATOM   2332 C C   . PHE B 1 77  ? 6.368   1.244   37.524  1.00 28.92  ? 64  PHE A C   1 
ATOM   2333 O O   . PHE B 1 77  ? 6.761   1.076   38.699  1.00 28.88  ? 64  PHE A O   1 
ATOM   2334 C CB  . PHE B 1 77  ? 5.177   3.351   37.711  1.00 26.36  ? 64  PHE A CB  1 
ATOM   2335 C CG  . PHE B 1 77  ? 6.378   4.049   37.086  1.00 26.64  ? 64  PHE A CG  1 
ATOM   2336 C CD1 . PHE B 1 77  ? 6.573   4.049   35.703  1.00 25.42  ? 64  PHE A CD1 1 
ATOM   2337 C CD2 . PHE B 1 77  ? 7.387   4.580   37.904  1.00 30.84  ? 64  PHE A CD2 1 
ATOM   2338 C CE1 . PHE B 1 77  ? 7.744   4.632   35.195  1.00 27.61  ? 64  PHE A CE1 1 
ATOM   2339 C CE2 . PHE B 1 77  ? 8.536   5.174   37.385  1.00 30.88  ? 64  PHE A CE2 1 
ATOM   2340 C CZ  . PHE B 1 77  ? 8.664   5.264   36.040  1.00 28.48  ? 64  PHE A CZ  1 
ATOM   2341 N N   . LEU B 1 78  ? 7.110   0.909   36.458  1.00 27.42  ? 65  LEU A N   1 
ATOM   2342 C CA  . LEU B 1 78  ? 8.471   0.414   36.553  1.00 30.66  ? 65  LEU A CA  1 
ATOM   2343 C C   . LEU B 1 78  ? 9.365   1.384   35.814  1.00 30.20  ? 65  LEU A C   1 
ATOM   2344 O O   . LEU B 1 78  ? 9.145   1.527   34.619  1.00 26.28  ? 65  LEU A O   1 
ATOM   2345 C CB  . LEU B 1 78  ? 8.634   -0.981  35.953  1.00 31.51  ? 65  LEU A CB  1 
ATOM   2346 C CG  . LEU B 1 78  ? 7.968   -2.079  36.803  1.00 39.54  ? 65  LEU A CG  1 
ATOM   2347 C CD1 . LEU B 1 78  ? 8.194   -3.509  36.393  1.00 37.49  ? 65  LEU A CD1 1 
ATOM   2348 C CD2 . LEU B 1 78  ? 8.357   -1.916  38.278  1.00 47.31  ? 65  LEU A CD2 1 
ATOM   2349 N N   . PRO B 1 79  ? 10.406  1.952   36.461  1.00 29.97  ? 66  PRO A N   1 
ATOM   2350 C CA  . PRO B 1 79  ? 11.387  2.751   35.739  1.00 31.31  ? 66  PRO A CA  1 
ATOM   2351 C C   . PRO B 1 79  ? 12.190  1.902   34.725  1.00 32.39  ? 66  PRO A C   1 
ATOM   2352 O O   . PRO B 1 79  ? 12.587  0.778   35.045  1.00 33.21  ? 66  PRO A O   1 
ATOM   2353 C CB  . PRO B 1 79  ? 12.203  3.313   36.889  1.00 33.42  ? 66  PRO A CB  1 
ATOM   2354 C CG  . PRO B 1 79  ? 12.200  2.191   37.929  1.00 32.42  ? 66  PRO A CG  1 
ATOM   2355 C CD  . PRO B 1 79  ? 10.736  1.758   37.891  1.00 30.57  ? 66  PRO A CD  1 
ATOM   2356 N N   . CYS B 1 80  ? 12.350  2.386   33.478  1.00 31.39  ? 67  CYS A N   1 
ATOM   2357 C CA  . CYS B 1 80  ? 13.039  1.557   32.512  1.00 31.61  ? 67  CYS A CA  1 
ATOM   2358 C C   . CYS B 1 80  ? 13.570  2.447   31.375  1.00 32.10  ? 67  CYS A C   1 
ATOM   2359 O O   . CYS B 1 80  ? 12.817  3.276   30.838  1.00 33.01  ? 67  CYS A O   1 
ATOM   2360 C CB  . CYS B 1 80  ? 12.116  0.470   31.964  1.00 32.33  ? 67  CYS A CB  1 
ATOM   2361 S SG  . CYS B 1 80  ? 12.955  -0.607  30.753  1.00 34.19  ? 67  CYS A SG  1 
ATOM   2362 N N   . ASP B 1 81  ? 14.878  2.310   31.089  1.00 32.30  ? 68  ASP A N   1 
ATOM   2363 C CA  . ASP B 1 81  ? 15.467  2.824   29.843  1.00 32.41  ? 68  ASP A CA  1 
ATOM   2364 C C   . ASP B 1 81  ? 15.441  1.715   28.807  1.00 31.00  ? 68  ASP A C   1 
ATOM   2365 O O   . ASP B 1 81  ? 16.050  0.668   29.036  1.00 34.05  ? 68  ASP A O   1 
ATOM   2366 C CB  . ASP B 1 81  ? 16.885  3.352   30.067  1.00 36.33  ? 68  ASP A CB  1 
ATOM   2367 C CG  . ASP B 1 81  ? 17.552  3.921   28.815  1.00 40.03  ? 68  ASP A CG  1 
ATOM   2368 O OD1 . ASP B 1 81  ? 17.048  3.696   27.680  1.00 39.51  ? 68  ASP A OD1 1 
ATOM   2369 O OD2 . ASP B 1 81  ? 18.569  4.630   28.992  1.00 44.16  ? 68  ASP A OD2 1 
ATOM   2370 N N   . VAL B 1 82  ? 14.558  1.872   27.794  1.00 29.48  ? 69  VAL A N   1 
ATOM   2371 C CA  . VAL B 1 82  ? 14.291  0.834   26.816  1.00 30.47  ? 69  VAL A CA  1 
ATOM   2372 C C   . VAL B 1 82  ? 15.498  0.482   25.950  1.00 31.20  ? 69  VAL A C   1 
ATOM   2373 O O   . VAL B 1 82  ? 15.480  -0.566  25.305  1.00 30.67  ? 69  VAL A O   1 
ATOM   2374 C CB  . VAL B 1 82  ? 13.063  1.197   25.953  1.00 30.02  ? 69  VAL A CB  1 
ATOM   2375 C CG1 . VAL B 1 82  ? 11.846  1.390   26.826  1.00 29.64  ? 69  VAL A CG1 1 
ATOM   2376 C CG2 . VAL B 1 82  ? 13.305  2.425   25.085  1.00 26.09  ? 69  VAL A CG2 1 
ATOM   2377 N N   . ARG B 1 83  ? 16.563  1.289   26.021  1.00 35.41  ? 70  ARG A N   1 
ATOM   2378 C CA  . ARG B 1 83  ? 17.843  0.910   25.407  1.00 38.34  ? 70  ARG A CA  1 
ATOM   2379 C C   . ARG B 1 83  ? 18.486  -0.256  26.156  1.00 40.14  ? 70  ARG A C   1 
ATOM   2380 O O   . ARG B 1 83  ? 19.262  -1.029  25.591  1.00 37.13  ? 70  ARG A O   1 
ATOM   2381 C CB  . ARG B 1 83  ? 18.890  2.023   25.341  1.00 37.93  ? 70  ARG A CB  1 
ATOM   2382 C CG  . ARG B 1 83  ? 18.251  3.234   24.690  1.00 41.85  ? 70  ARG A CG  1 
ATOM   2383 C CD  . ARG B 1 83  ? 19.076  4.453   24.925  1.00 53.22  ? 70  ARG A CD  1 
ATOM   2384 N NE  . ARG B 1 83  ? 20.095  4.464   23.871  1.00 58.45  ? 70  ARG A NE  1 
ATOM   2385 C CZ  . ARG B 1 83  ? 21.290  4.983   24.128  1.00 69.23  ? 70  ARG A CZ  1 
ATOM   2386 N NH1 . ARG B 1 83  ? 21.434  5.576   25.317  1.00 57.88  ? 70  ARG A NH1 1 
ATOM   2387 N NH2 . ARG B 1 83  ? 22.283  4.914   23.218  1.00 61.99  ? 70  ARG A NH2 1 
ATOM   2388 N N   . ASP B 1 84  ? 18.188  -0.338  27.452  1.00 35.60  ? 71  ASP A N   1 
ATOM   2389 C CA  . ASP B 1 84  ? 18.769  -1.368  28.287  1.00 38.51  ? 71  ASP A CA  1 
ATOM   2390 C C   . ASP B 1 84  ? 17.866  -2.594  28.223  1.00 39.85  ? 71  ASP A C   1 
ATOM   2391 O O   . ASP B 1 84  ? 16.854  -2.695  28.930  1.00 35.41  ? 71  ASP A O   1 
ATOM   2392 C CB  . ASP B 1 84  ? 19.052  -0.840  29.702  1.00 38.30  ? 71  ASP A CB  1 
ATOM   2393 C CG  . ASP B 1 84  ? 19.601  -1.820  30.744  1.00 40.13  ? 71  ASP A CG  1 
ATOM   2394 O OD1 . ASP B 1 84  ? 19.699  -3.035  30.446  1.00 42.49  ? 71  ASP A OD1 1 
ATOM   2395 O OD2 . ASP B 1 84  ? 19.939  -1.344  31.865  1.00 39.01  ? 71  ASP A OD2 1 
ATOM   2396 N N   . ILE B 1 85  ? 18.263  -3.557  27.399  1.00 35.46  ? 72  ILE A N   1 
ATOM   2397 C CA  . ILE B 1 85  ? 17.405  -4.699  27.186  1.00 34.71  ? 72  ILE A CA  1 
ATOM   2398 C C   . ILE B 1 85  ? 17.359  -5.604  28.428  1.00 36.06  ? 72  ILE A C   1 
ATOM   2399 O O   . ILE B 1 85  ? 16.343  -6.273  28.653  1.00 36.25  ? 72  ILE A O   1 
ATOM   2400 C CB  . ILE B 1 85  ? 17.844  -5.472  25.927  1.00 35.77  ? 72  ILE A CB  1 
ATOM   2401 C CG1 . ILE B 1 85  ? 17.677  -4.603  24.666  1.00 33.21  ? 72  ILE A CG1 1 
ATOM   2402 C CG2 . ILE B 1 85  ? 17.086  -6.807  25.846  1.00 34.12  ? 72  ILE A CG2 1 
ATOM   2403 C CD1 . ILE B 1 85  ? 16.264  -3.999  24.509  1.00 32.33  ? 72  ILE A CD1 1 
ATOM   2404 N N   . GLU B 1 86  ? 18.479  -5.750  29.128  1.00 36.72  ? 73  GLU A N   1 
ATOM   2405 C CA  . GLU B 1 86  ? 18.434  -6.421  30.426  1.00 39.07  ? 73  GLU A CA  1 
ATOM   2406 C C   . GLU B 1 86  ? 17.323  -5.795  31.286  1.00 33.74  ? 73  GLU A C   1 
ATOM   2407 O O   . GLU B 1 86  ? 16.623  -6.511  32.029  1.00 34.94  ? 73  GLU A O   1 
ATOM   2408 C CB  . GLU B 1 86  ? 19.796  -6.606  31.124  1.00 43.21  ? 73  GLU A CB  1 
ATOM   2409 C CG  . GLU B 1 86  ? 20.616  -7.693  30.418  1.00 51.98  ? 73  GLU A CG  1 
ATOM   2410 C CD  . GLU B 1 86  ? 19.998  -9.088  30.616  1.00 61.06  ? 73  GLU A CD  1 
ATOM   2411 O OE1 . GLU B 1 86  ? 19.726  -9.484  31.789  1.00 78.62  ? 73  GLU A OE1 1 
ATOM   2412 O OE2 . GLU B 1 86  ? 19.780  -9.813  29.618  1.00 64.90  ? 73  GLU A OE2 1 
ATOM   2413 N N   . ARG B 1 87  ? 17.299  -4.464  31.355  1.00 34.18  ? 74  ARG A N   1 
ATOM   2414 C CA  . ARG B 1 87  ? 16.360  -3.850  32.302  1.00 34.06  ? 74  ARG A CA  1 
ATOM   2415 C C   . ARG B 1 87  ? 14.948  -4.100  31.780  1.00 34.20  ? 74  ARG A C   1 
ATOM   2416 O O   . ARG B 1 87  ? 14.022  -4.363  32.577  1.00 33.67  ? 74  ARG A O   1 
ATOM   2417 C CB  . ARG B 1 87  ? 16.675  -2.389  32.689  1.00 35.35  ? 74  ARG A CB  1 
ATOM   2418 C CG  . ARG B 1 87  ? 15.610  -1.649  33.496  1.00 34.22  ? 74  ARG A CG  1 
ATOM   2419 C CD  . ARG B 1 87  ? 15.674  -2.003  35.000  1.00 34.15  ? 74  ARG A CD  1 
ATOM   2420 N NE  . ARG B 1 87  ? 14.426  -1.487  35.538  1.00 34.11  ? 74  ARG A NE  1 
ATOM   2421 C CZ  . ARG B 1 87  ? 13.730  -2.000  36.591  1.00 36.62  ? 74  ARG A CZ  1 
ATOM   2422 N NH1 . ARG B 1 87  ? 14.033  -3.193  37.108  1.00 37.58  ? 74  ARG A NH1 1 
ATOM   2423 N NH2 . ARG B 1 87  ? 12.650  -1.337  36.982  1.00 35.89  ? 74  ARG A NH2 1 
ATOM   2424 N N   . LEU B 1 88  ? 14.791  -4.002  30.440  1.00 30.39  ? 75  LEU A N   1 
ATOM   2425 C CA  . LEU B 1 88  ? 13.480  -4.265  29.849  1.00 29.16  ? 75  LEU A CA  1 
ATOM   2426 C C   . LEU B 1 88  ? 13.043  -5.673  30.240  1.00 29.98  ? 75  LEU A C   1 
ATOM   2427 O O   . LEU B 1 88  ? 11.927  -5.883  30.617  1.00 30.23  ? 75  LEU A O   1 
ATOM   2428 C CB  . LEU B 1 88  ? 13.569  -4.169  28.330  1.00 28.49  ? 75  LEU A CB  1 
ATOM   2429 C CG  . LEU B 1 88  ? 12.273  -4.465  27.555  1.00 27.20  ? 75  LEU A CG  1 
ATOM   2430 C CD1 . LEU B 1 88  ? 11.223  -3.424  27.976  1.00 28.21  ? 75  LEU A CD1 1 
ATOM   2431 C CD2 . LEU B 1 88  ? 12.571  -4.375  26.032  1.00 26.08  ? 75  LEU A CD2 1 
ATOM   2432 N N   . LYS B 1 89  ? 13.930  -6.686  30.079  1.00 34.09  ? 76  LYS A N   1 
ATOM   2433 C CA  . LYS B 1 89  ? 13.493  -8.026  30.421  1.00 32.59  ? 76  LYS A CA  1 
ATOM   2434 C C   . LYS B 1 89  ? 13.200  -8.103  31.908  1.00 33.27  ? 76  LYS A C   1 
ATOM   2435 O O   . LYS B 1 89  ? 12.290  -8.839  32.303  1.00 34.12  ? 76  LYS A O   1 
ATOM   2436 C CB  . LYS B 1 89  ? 14.614  -9.038  30.155  1.00 34.72  ? 76  LYS A CB  1 
ATOM   2437 C CG  . LYS B 1 89  ? 14.769  -9.314  28.647  1.00 37.64  ? 76  LYS A CG  1 
ATOM   2438 C CD  . LYS B 1 89  ? 16.090  -10.106 28.596  1.00 43.85  ? 76  LYS A CD  1 
ATOM   2439 C CE  . LYS B 1 89  ? 16.294  -10.435 27.163  1.00 41.54  ? 76  LYS A CE  1 
ATOM   2440 N NZ  . LYS B 1 89  ? 17.686  -10.763 26.793  1.00 50.66  ? 76  LYS A NZ  1 
ATOM   2441 N N   . ALA B 1 90  ? 13.979  -7.361  32.709  1.00 32.21  ? 77  ALA A N   1 
ATOM   2442 C CA  . ALA B 1 90  ? 13.725  -7.443  34.150  1.00 34.60  ? 77  ALA A CA  1 
ATOM   2443 C C   . ALA B 1 90  ? 12.303  -6.968  34.432  1.00 32.17  ? 77  ALA A C   1 
ATOM   2444 O O   . ALA B 1 90  ? 11.635  -7.530  35.319  1.00 32.57  ? 77  ALA A O   1 
ATOM   2445 C CB  . ALA B 1 90  ? 14.760  -6.682  34.992  1.00 33.75  ? 77  ALA A CB  1 
ATOM   2446 N N   . CYS B 1 91  ? 11.906  -5.887  33.736  1.00 31.48  ? 78  CYS A N   1 
ATOM   2447 C CA  . CYS B 1 91  ? 10.624  -5.237  33.962  1.00 30.09  ? 78  CYS A CA  1 
ATOM   2448 C C   . CYS B 1 91  ? 9.503   -6.192  33.601  1.00 31.25  ? 78  CYS A C   1 
ATOM   2449 O O   . CYS B 1 91  ? 8.526   -6.281  34.348  1.00 33.26  ? 78  CYS A O   1 
ATOM   2450 C CB  . CYS B 1 91  ? 10.503  -3.955  33.151  1.00 30.82  ? 78  CYS A CB  1 
ATOM   2451 S SG  . CYS B 1 91  ? 11.447  -2.600  33.906  1.00 34.54  ? 78  CYS A SG  1 
ATOM   2452 N N   . VAL B 1 92  ? 9.652   -6.911  32.474  1.00 32.45  ? 79  VAL A N   1 
ATOM   2453 C CA  . VAL B 1 92  ? 8.656   -7.880  32.031  1.00 32.13  ? 79  VAL A CA  1 
ATOM   2454 C C   . VAL B 1 92  ? 8.523   -9.011  33.059  1.00 32.14  ? 79  VAL A C   1 
ATOM   2455 O O   . VAL B 1 92  ? 7.395   -9.411  33.430  1.00 31.24  ? 79  VAL A O   1 
ATOM   2456 C CB  . VAL B 1 92  ? 8.931   -8.433  30.616  1.00 32.77  ? 79  VAL A CB  1 
ATOM   2457 C CG1 . VAL B 1 92  ? 7.957   -9.534  30.200  1.00 34.33  ? 79  VAL A CG1 1 
ATOM   2458 C CG2 . VAL B 1 92  ? 8.948   -7.349  29.540  1.00 28.63  ? 79  VAL A CG2 1 
ATOM   2459 N N   . ALA B 1 93  ? 9.657   -9.565  33.524  1.00 31.94  ? 80  ALA A N   1 
ATOM   2460 C CA  . ALA B 1 93  ? 9.604   -10.663 34.496  1.00 33.18  ? 80  ALA A CA  1 
ATOM   2461 C C   . ALA B 1 93  ? 8.880   -10.217 35.776  1.00 31.78  ? 80  ALA A C   1 
ATOM   2462 O O   . ALA B 1 93  ? 8.151   -10.975 36.424  1.00 32.47  ? 80  ALA A O   1 
ATOM   2463 C CB  . ALA B 1 93  ? 11.004  -11.145 34.871  1.00 38.03  ? 80  ALA A CB  1 
ATOM   2464 N N   . GLU B 1 94  ? 9.063   -8.950  36.149  1.00 31.96  ? 81  GLU A N   1 
ATOM   2465 C CA  . GLU B 1 94  ? 8.486   -8.448  37.390  1.00 30.24  ? 81  GLU A CA  1 
ATOM   2466 C C   . GLU B 1 94  ? 6.970   -8.337  37.243  1.00 31.33  ? 81  GLU A C   1 
ATOM   2467 O O   . GLU B 1 94  ? 6.230   -8.627  38.174  1.00 31.03  ? 81  GLU A O   1 
ATOM   2468 C CB  . GLU B 1 94  ? 9.082   -7.138  37.861  1.00 34.15  ? 81  GLU A CB  1 
ATOM   2469 C CG  . GLU B 1 94  ? 8.244   -6.536  38.982  1.00 37.71  ? 81  GLU A CG  1 
ATOM   2470 C CD  . GLU B 1 94  ? 8.927   -5.334  39.607  1.00 49.87  ? 81  GLU A CD  1 
ATOM   2471 O OE1 . GLU B 1 94  ? 10.074  -5.083  39.157  1.00 56.85  ? 81  GLU A OE1 1 
ATOM   2472 O OE2 . GLU B 1 94  ? 8.310   -4.634  40.462  1.00 60.42  ? 81  GLU A OE2 1 
ATOM   2473 N N   . VAL B 1 95  ? 6.519   -7.847  36.083  1.00 27.85  ? 82  VAL A N   1 
ATOM   2474 C CA  . VAL B 1 95  ? 5.081   -7.816  35.826  1.00 28.32  ? 82  VAL A CA  1 
ATOM   2475 C C   . VAL B 1 95  ? 4.506   -9.236  35.889  1.00 30.93  ? 82  VAL A C   1 
ATOM   2476 O O   . VAL B 1 95  ? 3.465   -9.468  36.516  1.00 32.63  ? 82  VAL A O   1 
ATOM   2477 C CB  . VAL B 1 95  ? 4.799   -7.115  34.488  1.00 26.31  ? 82  VAL A CB  1 
ATOM   2478 C CG1 . VAL B 1 95  ? 3.301   -7.197  34.175  1.00 24.90  ? 82  VAL A CG1 1 
ATOM   2479 C CG2 . VAL B 1 95  ? 5.298   -5.663  34.529  1.00 24.09  ? 82  VAL A CG2 1 
ATOM   2480 N N   . GLU B 1 96  ? 5.202   -10.178 35.247  1.00 31.28  ? 83  GLU A N   1 
ATOM   2481 C CA  . GLU B 1 96  ? 4.763   -11.570 35.239  1.00 33.85  ? 83  GLU A CA  1 
ATOM   2482 C C   . GLU B 1 96  ? 4.660   -12.141 36.644  1.00 36.04  ? 83  GLU A C   1 
ATOM   2483 O O   . GLU B 1 96  ? 3.714   -12.859 36.941  1.00 34.71  ? 83  GLU A O   1 
ATOM   2484 C CB  . GLU B 1 96  ? 5.561   -12.517 34.335  1.00 35.46  ? 83  GLU A CB  1 
ATOM   2485 C CG  . GLU B 1 96  ? 5.360   -12.218 32.849  1.00 42.05  ? 83  GLU A CG  1 
ATOM   2486 C CD  . GLU B 1 96  ? 6.227   -13.136 31.965  1.00 44.33  ? 83  GLU A CD  1 
ATOM   2487 O OE1 . GLU B 1 96  ? 7.396   -13.381 32.326  1.00 54.70  ? 83  GLU A OE1 1 
ATOM   2488 O OE2 . GLU B 1 96  ? 5.757   -13.647 30.935  1.00 44.19  ? 83  GLU A OE2 1 
ATOM   2489 N N   . ARG B 1 97  ? 5.635   -11.831 37.492  1.00 34.32  ? 84  ARG A N   1 
ATOM   2490 C CA  . ARG B 1 97  ? 5.597   -12.375 38.835  1.00 38.53  ? 84  ARG A CA  1 
ATOM   2491 C C   . ARG B 1 97  ? 4.467   -11.713 39.630  1.00 36.55  ? 84  ARG A C   1 
ATOM   2492 O O   . ARG B 1 97  ? 3.943   -12.312 40.561  1.00 35.53  ? 84  ARG A O   1 
ATOM   2493 C CB  . ARG B 1 97  ? 6.896   -12.233 39.637  1.00 46.02  ? 84  ARG A CB  1 
ATOM   2494 C CG  . ARG B 1 97  ? 8.106   -13.063 39.230  1.00 55.02  ? 84  ARG A CG  1 
ATOM   2495 C CD  . ARG B 1 97  ? 9.207   -12.805 40.263  1.00 53.82  ? 84  ARG A CD  1 
ATOM   2496 N NE  . ARG B 1 97  ? 9.787   -11.446 40.249  1.00 46.35  ? 84  ARG A NE  1 
ATOM   2497 C CZ  . ARG B 1 97  ? 10.661  -10.940 39.376  1.00 45.56  ? 84  ARG A CZ  1 
ATOM   2498 N NH1 . ARG B 1 97  ? 11.097  -11.675 38.353  1.00 44.46  ? 84  ARG A NH1 1 
ATOM   2499 N NH2 . ARG B 1 97  ? 11.049  -9.676  39.495  1.00 39.92  ? 84  ARG A NH2 1 
ATOM   2500 N N   . THR B 1 98  ? 4.160   -10.451 39.348  1.00 35.12  ? 85  THR A N   1 
ATOM   2501 C CA  . THR B 1 98  ? 3.132   -9.733  40.108  1.00 33.86  ? 85  THR A CA  1 
ATOM   2502 C C   . THR B 1 98  ? 1.738   -10.245 39.720  1.00 32.50  ? 85  THR A C   1 
ATOM   2503 O O   . THR B 1 98  ? 0.953   -10.584 40.607  1.00 32.91  ? 85  THR A O   1 
ATOM   2504 C CB  . THR B 1 98  ? 3.271   -8.220  39.882  1.00 34.74  ? 85  THR A CB  1 
ATOM   2505 O OG1 . THR B 1 98  ? 4.583   -7.851  40.302  1.00 33.52  ? 85  THR A OG1 1 
ATOM   2506 C CG2 . THR B 1 98  ? 2.385   -7.435  40.841  1.00 38.28  ? 85  THR A CG2 1 
ATOM   2507 N N   . TRP B 1 99  ? 1.443   -10.388 38.424  1.00 31.20  ? 86  TRP A N   1 
ATOM   2508 C CA  . TRP B 1 99  ? 0.100   -10.447 37.858  1.00 32.83  ? 86  TRP A CA  1 
ATOM   2509 C C   . TRP B 1 99  ? -0.105  -11.636 36.918  1.00 35.61  ? 86  TRP A C   1 
ATOM   2510 O O   . TRP B 1 99  ? -1.211  -11.778 36.365  1.00 34.98  ? 86  TRP A O   1 
ATOM   2511 C CB  . TRP B 1 99  ? -0.264  -9.138  37.109  1.00 27.08  ? 86  TRP A CB  1 
ATOM   2512 C CG  . TRP B 1 99  ? -0.646  -8.004  38.018  1.00 30.01  ? 86  TRP A CG  1 
ATOM   2513 C CD1 . TRP B 1 99  ? -1.085  -8.051  39.313  1.00 29.72  ? 86  TRP A CD1 1 
ATOM   2514 C CD2 . TRP B 1 99  ? -0.593  -6.617  37.666  1.00 27.51  ? 86  TRP A CD2 1 
ATOM   2515 N NE1 . TRP B 1 99  ? -1.376  -6.801  39.779  1.00 32.18  ? 86  TRP A NE1 1 
ATOM   2516 C CE2 . TRP B 1 99  ? -1.076  -5.901  38.788  1.00 28.79  ? 86  TRP A CE2 1 
ATOM   2517 C CE3 . TRP B 1 99  ? -0.175  -5.945  36.531  1.00 25.17  ? 86  TRP A CE3 1 
ATOM   2518 C CZ2 . TRP B 1 99  ? -1.142  -4.511  38.791  1.00 29.46  ? 86  TRP A CZ2 1 
ATOM   2519 C CZ3 . TRP B 1 99  ? -0.309  -4.583  36.510  1.00 26.45  ? 86  TRP A CZ3 1 
ATOM   2520 C CH2 . TRP B 1 99  ? -0.760  -3.883  37.627  1.00 25.59  ? 86  TRP A CH2 1 
ATOM   2521 N N   . GLY B 1 100 ? 0.969   -12.384 36.577  1.00 37.74  ? 87  GLY A N   1 
ATOM   2522 C CA  . GLY B 1 100 ? 0.842   -13.452 35.590  1.00 35.92  ? 87  GLY A CA  1 
ATOM   2523 C C   . GLY B 1 100 ? 1.238   -12.996 34.189  1.00 33.68  ? 87  GLY A C   1 
ATOM   2524 O O   . GLY B 1 100 ? 1.553   -11.819 34.018  1.00 35.91  ? 87  GLY A O   1 
ATOM   2525 N N   . ALA B 1 101 ? 1.178   -13.877 33.187  1.00 29.58  ? 88  ALA A N   1 
ATOM   2526 C CA  . ALA B 1 101 ? 1.513   -13.554 31.801  1.00 29.17  ? 88  ALA A CA  1 
ATOM   2527 C C   . ALA B 1 101 ? 0.829   -12.266 31.350  1.00 27.19  ? 88  ALA A C   1 
ATOM   2528 O O   . ALA B 1 101 ? -0.355  -12.062 31.638  1.00 27.15  ? 88  ALA A O   1 
ATOM   2529 C CB  . ALA B 1 101 ? 1.084   -14.708 30.927  1.00 31.12  ? 88  ALA A CB  1 
ATOM   2530 N N   . VAL B 1 102 ? 1.549   -11.437 30.583  1.00 28.12  ? 89  VAL A N   1 
ATOM   2531 C CA  . VAL B 1 102 ? 0.930   -10.271 29.976  1.00 25.84  ? 89  VAL A CA  1 
ATOM   2532 C C   . VAL B 1 102 ? -0.119  -10.695 28.941  1.00 26.10  ? 89  VAL A C   1 
ATOM   2533 O O   . VAL B 1 102 ? 0.090   -11.682 28.217  1.00 27.12  ? 89  VAL A O   1 
ATOM   2534 C CB  . VAL B 1 102 ? 2.052   -9.428  29.368  1.00 24.54  ? 89  VAL A CB  1 
ATOM   2535 C CG1 . VAL B 1 102 ? 1.538   -8.184  28.657  1.00 23.73  ? 89  VAL A CG1 1 
ATOM   2536 C CG2 . VAL B 1 102 ? 3.035   -9.044  30.433  1.00 27.60  ? 89  VAL A CG2 1 
ATOM   2537 N N   . ASP B 1 103 ? -1.268  -9.989  28.919  1.00 23.38  ? 90  ASP A N   1 
ATOM   2538 C CA  . ASP B 1 103 ? -2.316  -10.229 27.944  1.00 23.03  ? 90  ASP A CA  1 
ATOM   2539 C C   . ASP B 1 103 ? -2.103  -9.346  26.719  1.00 21.45  ? 90  ASP A C   1 
ATOM   2540 O O   . ASP B 1 103 ? -2.374  -9.737  25.589  1.00 21.95  ? 90  ASP A O   1 
ATOM   2541 C CB  . ASP B 1 103 ? -3.665  -9.942  28.571  1.00 25.86  ? 90  ASP A CB  1 
ATOM   2542 C CG  . ASP B 1 103 ? -4.087  -10.953 29.641  1.00 25.16  ? 90  ASP A CG  1 
ATOM   2543 O OD1 . ASP B 1 103 ? -4.424  -12.090 29.235  1.00 27.99  ? 90  ASP A OD1 1 
ATOM   2544 O OD2 . ASP B 1 103 ? -4.144  -10.662 30.868  1.00 26.23  ? 90  ASP A OD2 1 
ATOM   2545 N N   . VAL B 1 104 ? -1.712  -8.096  27.001  1.00 19.99  ? 91  VAL A N   1 
ATOM   2546 C CA  . VAL B 1 104 ? -1.636  -7.071  25.953  1.00 21.57  ? 91  VAL A CA  1 
ATOM   2547 C C   . VAL B 1 104 ? -0.320  -6.312  26.113  1.00 20.97  ? 91  VAL A C   1 
ATOM   2548 O O   . VAL B 1 104 ? -0.097  -5.729  27.168  1.00 22.79  ? 91  VAL A O   1 
ATOM   2549 C CB  . VAL B 1 104 ? -2.777  -6.021  25.997  1.00 21.38  ? 91  VAL A CB  1 
ATOM   2550 C CG1 . VAL B 1 104 ? -2.576  -5.087  24.803  1.00 20.28  ? 91  VAL A CG1 1 
ATOM   2551 C CG2 . VAL B 1 104 ? -4.166  -6.715  25.939  1.00 21.19  ? 91  VAL A CG2 1 
ATOM   2552 N N   . LEU B 1 105 ? 0.539   -6.324  25.069  1.00 21.44  ? 92  LEU A N   1 
ATOM   2553 C CA  . LEU B 1 105 ? 1.753   -5.502  25.098  1.00 20.10  ? 92  LEU A CA  1 
ATOM   2554 C C   . LEU B 1 105 ? 1.571   -4.356  24.117  1.00 19.13  ? 92  LEU A C   1 
ATOM   2555 O O   . LEU B 1 105 ? 1.249   -4.600  22.963  1.00 20.84  ? 92  LEU A O   1 
ATOM   2556 C CB  . LEU B 1 105 ? 2.978   -6.317  24.698  1.00 21.62  ? 92  LEU A CB  1 
ATOM   2557 C CG  . LEU B 1 105 ? 4.271   -5.520  24.359  1.00 24.24  ? 92  LEU A CG  1 
ATOM   2558 C CD1 . LEU B 1 105 ? 4.858   -4.798  25.617  1.00 20.54  ? 92  LEU A CD1 1 
ATOM   2559 C CD2 . LEU B 1 105 ? 5.401   -6.516  23.879  1.00 24.17  ? 92  LEU A CD2 1 
ATOM   2560 N N   . ILE B 1 106 ? 1.842   -3.122  24.556  1.00 17.79  ? 93  ILE A N   1 
ATOM   2561 C CA  . ILE B 1 106 ? 1.852   -2.003  23.610  1.00 17.36  ? 93  ILE A CA  1 
ATOM   2562 C C   . ILE B 1 106 ? 3.293   -1.458  23.566  1.00 19.07  ? 93  ILE A C   1 
ATOM   2563 O O   . ILE B 1 106 ? 3.756   -0.799  24.492  1.00 20.04  ? 93  ILE A O   1 
ATOM   2564 C CB  . ILE B 1 106 ? 0.868   -0.918  24.018  1.00 15.26  ? 93  ILE A CB  1 
ATOM   2565 C CG1 . ILE B 1 106 ? -0.533  -1.506  24.293  1.00 15.92  ? 93  ILE A CG1 1 
ATOM   2566 C CG2 . ILE B 1 106 ? 0.818   0.168   22.927  1.00 15.11  ? 93  ILE A CG2 1 
ATOM   2567 C CD1 . ILE B 1 106 ? -1.623  -0.448  24.590  1.00 18.37  ? 93  ILE A CD1 1 
ATOM   2568 N N   . ASN B 1 107 ? 3.907   -1.596  22.386  1.00 21.12  ? 94  ASN A N   1 
ATOM   2569 C CA  . ASN B 1 107 ? 5.243   -1.093  22.177  1.00 21.38  ? 94  ASN A CA  1 
ATOM   2570 C C   . ASN B 1 107 ? 5.088   0.342   21.681  1.00 22.27  ? 94  ASN A C   1 
ATOM   2571 O O   . ASN B 1 107 ? 4.856   0.562   20.490  1.00 19.77  ? 94  ASN A O   1 
ATOM   2572 C CB  . ASN B 1 107 ? 5.983   -1.942  21.137  1.00 22.98  ? 94  ASN A CB  1 
ATOM   2573 C CG  . ASN B 1 107 ? 6.408   -3.306  21.659  1.00 22.29  ? 94  ASN A CG  1 
ATOM   2574 O OD1 . ASN B 1 107 ? 6.875   -3.410  22.795  1.00 21.38  ? 94  ASN A OD1 1 
ATOM   2575 N ND2 . ASN B 1 107 ? 6.245   -4.364  20.851  1.00 21.24  ? 94  ASN A ND2 1 
ATOM   2576 N N   . ASN B 1 108 ? 5.285   1.299   22.595  1.00 21.24  ? 95  ASN A N   1 
ATOM   2577 C CA  . ASN B 1 108 ? 4.963   2.702   22.363  1.00 20.79  ? 95  ASN A CA  1 
ATOM   2578 C C   . ASN B 1 108 ? 6.193   3.629   22.540  1.00 23.11  ? 95  ASN A C   1 
ATOM   2579 O O   . ASN B 1 108 ? 6.197   4.745   21.980  1.00 22.91  ? 95  ASN A O   1 
ATOM   2580 C CB  . ASN B 1 108 ? 3.809   3.097   23.279  1.00 20.18  ? 95  ASN A CB  1 
ATOM   2581 C CG  . ASN B 1 108 ? 3.525   4.585   23.266  1.00 21.31  ? 95  ASN A CG  1 
ATOM   2582 O OD1 . ASN B 1 108 ? 3.014   5.126   22.276  1.00 20.81  ? 95  ASN A OD1 1 
ATOM   2583 N ND2 . ASN B 1 108 ? 3.950   5.298   24.292  1.00 21.12  ? 95  ASN A ND2 1 
ATOM   2584 N N   . ALA B 1 109 ? 7.206   3.209   23.302  1.00 21.01  ? 96  ALA A N   1 
ATOM   2585 C CA  . ALA B 1 109 ? 8.344   4.079   23.622  1.00 22.72  ? 96  ALA A CA  1 
ATOM   2586 C C   . ALA B 1 109 ? 8.990   4.515   22.283  1.00 22.06  ? 96  ALA A C   1 
ATOM   2587 O O   . ALA B 1 109 ? 9.266   3.686   21.436  1.00 20.28  ? 96  ALA A O   1 
ATOM   2588 C CB  . ALA B 1 109 ? 9.309   3.368   24.522  1.00 22.35  ? 96  ALA A CB  1 
ATOM   2589 N N   . ALA B 1 110 ? 9.322   5.803   22.157  1.00 23.16  ? 97  ALA A N   1 
ATOM   2590 C CA  . ALA B 1 110 ? 9.918   6.239   20.912  1.00 25.58  ? 97  ALA A CA  1 
ATOM   2591 C C   . ALA B 1 110 ? 10.535  7.606   21.189  1.00 27.83  ? 97  ALA A C   1 
ATOM   2592 O O   . ALA B 1 110 ? 10.227  8.283   22.182  1.00 29.17  ? 97  ALA A O   1 
ATOM   2593 C CB  . ALA B 1 110 ? 8.787   6.361   19.824  1.00 26.65  ? 97  ALA A CB  1 
ATOM   2594 N N   . ARG B 1 111 ? 11.427  8.011   20.294  1.00 29.59  ? 98  ARG A N   1 
ATOM   2595 C CA  . ARG B 1 111 ? 11.983  9.357   20.383  1.00 27.26  ? 98  ARG A CA  1 
ATOM   2596 C C   . ARG B 1 111 ? 11.936  9.922   18.961  1.00 30.10  ? 98  ARG A C   1 
ATOM   2597 O O   . ARG B 1 111 ? 12.622  9.410   18.089  1.00 30.95  ? 98  ARG A O   1 
ATOM   2598 C CB  . ARG B 1 111 ? 13.305  9.394   21.157  1.00 30.64  ? 98  ARG A CB  1 
ATOM   2599 N N   . ASP B 1 112 ? 11.192  11.015  18.768  1.00 33.99  ? 99  ASP A N   1 
ATOM   2600 C CA  . ASP B 1 112 ? 10.874  11.481  17.425  1.00 35.35  ? 99  ASP A CA  1 
ATOM   2601 C C   . ASP B 1 112 ? 11.588  12.789  17.089  1.00 38.25  ? 99  ASP A C   1 
ATOM   2602 O O   . ASP B 1 112 ? 11.108  13.492  16.204  1.00 42.23  ? 99  ASP A O   1 
ATOM   2603 C CB  . ASP B 1 112 ? 9.365   11.648  17.215  1.00 39.81  ? 99  ASP A CB  1 
ATOM   2604 C CG  . ASP B 1 112 ? 8.720   12.647  18.173  1.00 39.62  ? 99  ASP A CG  1 
ATOM   2605 O OD1 . ASP B 1 112 ? 9.483   13.256  18.974  1.00 41.29  ? 99  ASP A OD1 1 
ATOM   2606 O OD2 . ASP B 1 112 ? 7.444   12.703  18.231  1.00 46.29  ? 99  ASP A OD2 1 
ATOM   2607 N N   . ASP B 1 113 ? 12.703  13.093  17.768  1.00 35.29  ? 100 ASP A N   1 
ATOM   2608 C CA  . ASP B 1 113 ? 13.374  14.377  17.528  1.00 37.97  ? 100 ASP A CA  1 
ATOM   2609 C C   . ASP B 1 113 ? 13.773  14.533  16.045  1.00 39.81  ? 100 ASP A C   1 
ATOM   2610 O O   . ASP B 1 113 ? 14.151  13.541  15.392  1.00 36.03  ? 100 ASP A O   1 
ATOM   2611 C CB  . ASP B 1 113 ? 14.582  14.550  18.454  1.00 41.85  ? 100 ASP A CB  1 
ATOM   2612 C CG  . ASP B 1 113 ? 14.317  14.323  19.944  1.00 47.66  ? 100 ASP A CG  1 
ATOM   2613 O OD1 . ASP B 1 113 ? 13.933  13.202  20.302  1.00 43.87  ? 100 ASP A OD1 1 
ATOM   2614 O OD2 . ASP B 1 113 ? 14.516  15.244  20.754  1.00 55.86  ? 100 ASP A OD2 1 
ATOM   2615 N N   . ARG B 1 114 ? 13.724  15.799  15.554  1.00 38.24  ? 101 ARG A N   1 
ATOM   2616 C CA  . ARG B 1 114 ? 14.018  16.172  14.165  1.00 38.85  ? 101 ARG A CA  1 
ATOM   2617 C C   . ARG B 1 114 ? 15.529  16.059  13.972  1.00 39.76  ? 101 ARG A C   1 
ATOM   2618 O O   . ARG B 1 114 ? 16.247  16.354  14.922  1.00 42.75  ? 101 ARG A O   1 
ATOM   2619 C CB  . ARG B 1 114 ? 13.187  17.392  13.721  1.00 40.02  ? 101 ARG A CB  1 
ATOM   2620 N N   . HIS B 1 115 ? 16.042  15.493  12.847  1.00 38.55  ? 102 HIS A N   1 
ATOM   2621 C CA  . HIS B 1 115 ? 17.480  15.493  12.602  1.00 37.58  ? 102 HIS A CA  1 
ATOM   2622 C C   . HIS B 1 115 ? 17.717  15.502  11.100  1.00 37.38  ? 102 HIS A C   1 
ATOM   2623 O O   . HIS B 1 115 ? 17.078  14.738  10.371  1.00 34.72  ? 102 HIS A O   1 
ATOM   2624 C CB  . HIS B 1 115 ? 18.144  14.265  13.239  1.00 37.85  ? 102 HIS A CB  1 
ATOM   2625 C CG  . HIS B 1 115 ? 17.452  12.916  13.058  1.00 36.48  ? 102 HIS A CG  1 
ATOM   2626 N ND1 . HIS B 1 115 ? 16.500  12.336  13.886  1.00 36.59  ? 102 HIS A ND1 1 
ATOM   2627 C CD2 . HIS B 1 115 ? 17.653  12.027  12.063  1.00 37.03  ? 102 HIS A CD2 1 
ATOM   2628 C CE1 . HIS B 1 115 ? 16.158  11.160  13.421  1.00 32.51  ? 102 HIS A CE1 1 
ATOM   2629 N NE2 . HIS B 1 115 ? 16.833  10.934  12.310  1.00 33.96  ? 102 HIS A NE2 1 
ATOM   2630 N N   . ALA B 1 116 ? 18.671  16.315  10.658  1.00 37.72  ? 103 ALA A N   1 
ATOM   2631 C CA  . ALA B 1 116 ? 19.018  16.439  9.243   1.00 39.67  ? 103 ALA A CA  1 
ATOM   2632 C C   . ALA B 1 116 ? 19.722  15.180  8.740   1.00 38.35  ? 103 ALA A C   1 
ATOM   2633 O O   . ALA B 1 116 ? 20.706  14.729  9.313   1.00 38.86  ? 103 ALA A O   1 
ATOM   2634 C CB  . ALA B 1 116 ? 19.956  17.626  9.042   1.00 41.02  ? 103 ALA A CB  1 
ATOM   2635 N N   . LEU B 1 117 ? 19.298  14.678  7.585   1.00 38.01  ? 104 LEU A N   1 
ATOM   2636 C CA  . LEU B 1 117 ? 19.966  13.522  6.991   1.00 39.78  ? 104 LEU A CA  1 
ATOM   2637 C C   . LEU B 1 117 ? 21.486  13.671  6.890   1.00 41.14  ? 104 LEU A C   1 
ATOM   2638 O O   . LEU B 1 117 ? 22.274  12.736  7.143   1.00 41.45  ? 104 LEU A O   1 
ATOM   2639 C CB  . LEU B 1 117 ? 19.304  13.332  5.629   1.00 40.22  ? 104 LEU A CB  1 
ATOM   2640 C CG  . LEU B 1 117 ? 19.740  12.046  4.931   1.00 42.92  ? 104 LEU A CG  1 
ATOM   2641 C CD1 . LEU B 1 117 ? 18.542  11.539  4.091   1.00 38.29  ? 104 LEU A CD1 1 
ATOM   2642 C CD2 . LEU B 1 117 ? 21.047  12.168  4.129   1.00 38.87  ? 104 LEU A CD2 1 
ATOM   2643 N N   . ALA B 1 118 ? 21.937  14.867  6.484   1.00 43.83  ? 105 ALA A N   1 
ATOM   2644 C CA  . ALA B 1 118 ? 23.329  15.011  6.099   1.00 46.32  ? 105 ALA A CA  1 
ATOM   2645 C C   . ALA B 1 118 ? 24.218  14.872  7.336   1.00 46.47  ? 105 ALA A C   1 
ATOM   2646 O O   . ALA B 1 118 ? 25.398  14.615  7.180   1.00 49.30  ? 105 ALA A O   1 
ATOM   2647 C CB  . ALA B 1 118 ? 23.543  16.325  5.357   1.00 49.25  ? 105 ALA A CB  1 
ATOM   2648 N N   . ASP B 1 119 ? 23.628  14.986  8.546   1.00 44.80  ? 106 ASP A N   1 
ATOM   2649 C CA  . ASP B 1 119 ? 24.365  15.239  9.773   1.00 45.42  ? 106 ASP A CA  1 
ATOM   2650 C C   . ASP B 1 119 ? 24.369  14.069  10.747  1.00 45.52  ? 106 ASP A C   1 
ATOM   2651 O O   . ASP B 1 119 ? 24.984  14.184  11.788  1.00 48.89  ? 106 ASP A O   1 
ATOM   2652 C CB  . ASP B 1 119 ? 23.834  16.470  10.487  1.00 45.50  ? 106 ASP A CB  1 
ATOM   2653 C CG  . ASP B 1 119 ? 23.962  17.737  9.652   1.00 46.43  ? 106 ASP A CG  1 
ATOM   2654 O OD1 . ASP B 1 119 ? 24.800  17.769  8.722   1.00 49.59  ? 106 ASP A OD1 1 
ATOM   2655 O OD2 . ASP B 1 119 ? 23.216  18.685  9.896   1.00 47.94  ? 106 ASP A OD2 1 
ATOM   2656 N N   . VAL B 1 120 ? 23.709  12.951  10.448  1.00 41.81  ? 107 VAL A N   1 
ATOM   2657 C CA  . VAL B 1 120 ? 23.594  11.797  11.330  1.00 38.14  ? 107 VAL A CA  1 
ATOM   2658 C C   . VAL B 1 120 ? 24.896  11.004  11.397  1.00 39.75  ? 107 VAL A C   1 
ATOM   2659 O O   . VAL B 1 120 ? 25.474  10.646  10.354  1.00 40.81  ? 107 VAL A O   1 
ATOM   2660 C CB  . VAL B 1 120 ? 22.480  10.923  10.705  1.00 34.49  ? 107 VAL A CB  1 
ATOM   2661 C CG1 . VAL B 1 120 ? 22.528  9.485   11.199  1.00 34.42  ? 107 VAL A CG1 1 
ATOM   2662 C CG2 . VAL B 1 120 ? 21.102  11.583  10.740  1.00 34.63  ? 107 VAL A CG2 1 
ATOM   2663 N N   . SER B 1 121 ? 25.392  10.770  12.632  1.00 37.98  ? 108 SER A N   1 
ATOM   2664 C CA  . SER B 1 121 ? 26.624  10.015  12.874  1.00 39.66  ? 108 SER A CA  1 
ATOM   2665 C C   . SER B 1 121 ? 26.224  8.550   13.098  1.00 38.93  ? 108 SER A C   1 
ATOM   2666 O O   . SER B 1 121 ? 25.033  8.240   13.264  1.00 36.13  ? 108 SER A O   1 
ATOM   2667 C CB  . SER B 1 121 ? 27.347  10.540  14.119  1.00 41.92  ? 108 SER A CB  1 
ATOM   2668 O OG  . SER B 1 121 ? 26.473  10.286  15.206  1.00 43.69  ? 108 SER A OG  1 
ATOM   2669 N N   . VAL B 1 122 ? 27.245  7.672   13.163  1.00 41.72  ? 109 VAL A N   1 
ATOM   2670 C CA  . VAL B 1 122 ? 26.930  6.260   13.402  1.00 40.79  ? 109 VAL A CA  1 
ATOM   2671 C C   . VAL B 1 122 ? 26.348  6.071   14.801  1.00 41.45  ? 109 VAL A C   1 
ATOM   2672 O O   . VAL B 1 122 ? 25.396  5.300   14.965  1.00 42.26  ? 109 VAL A O   1 
ATOM   2673 C CB  . VAL B 1 122 ? 28.143  5.348   13.182  1.00 42.05  ? 109 VAL A CB  1 
ATOM   2674 C CG1 . VAL B 1 122 ? 27.820  3.896   13.506  1.00 40.84  ? 109 VAL A CG1 1 
ATOM   2675 C CG2 . VAL B 1 122 ? 28.620  5.484   11.731  1.00 44.11  ? 109 VAL A CG2 1 
ATOM   2676 N N   . GLU B 1 123 ? 26.919  6.781   15.789  1.00 42.32  ? 110 GLU A N   1 
ATOM   2677 C CA  . GLU B 1 123 ? 26.463  6.676   17.177  1.00 41.33  ? 110 GLU A CA  1 
ATOM   2678 C C   . GLU B 1 123 ? 25.027  7.170   17.300  1.00 39.52  ? 110 GLU A C   1 
ATOM   2679 O O   . GLU B 1 123 ? 24.227  6.501   17.933  1.00 37.16  ? 110 GLU A O   1 
ATOM   2680 C CB  . GLU B 1 123 ? 27.428  7.288   18.203  1.00 44.06  ? 110 GLU A CB  1 
ATOM   2681 C CG  . GLU B 1 123 ? 28.875  6.815   18.071  1.00 46.49  ? 110 GLU A CG  1 
ATOM   2682 C CD  . GLU B 1 123 ? 29.792  7.589   17.093  1.00 52.26  ? 110 GLU A CD  1 
ATOM   2683 O OE1 . GLU B 1 123 ? 29.399  8.523   16.287  1.00 54.01  ? 110 GLU A OE1 1 
ATOM   2684 O OE2 . GLU B 1 123 ? 30.970  7.230   17.115  1.00 58.95  ? 110 GLU A OE2 1 
ATOM   2685 N N   . TYR B 1 124 ? 24.669  8.267   16.624  1.00 41.17  ? 111 TYR A N   1 
ATOM   2686 C CA  . TYR B 1 124 ? 23.311  8.795   16.605  1.00 41.53  ? 111 TYR A CA  1 
ATOM   2687 C C   . TYR B 1 124 ? 22.317  7.755   16.035  1.00 40.43  ? 111 TYR A C   1 
ATOM   2688 O O   . TYR B 1 124 ? 21.292  7.446   16.663  1.00 38.30  ? 111 TYR A O   1 
ATOM   2689 C CB  . TYR B 1 124 ? 23.190  10.091  15.795  1.00 42.19  ? 111 TYR A CB  1 
ATOM   2690 C CG  . TYR B 1 124 ? 21.855  10.785  16.013  1.00 46.38  ? 111 TYR A CG  1 
ATOM   2691 C CD1 . TYR B 1 124 ? 21.655  11.642  17.108  1.00 48.17  ? 111 TYR A CD1 1 
ATOM   2692 C CD2 . TYR B 1 124 ? 20.774  10.521  15.161  1.00 42.93  ? 111 TYR A CD2 1 
ATOM   2693 C CE1 . TYR B 1 124 ? 20.420  12.233  17.343  1.00 49.92  ? 111 TYR A CE1 1 
ATOM   2694 C CE2 . TYR B 1 124 ? 19.550  11.121  15.371  1.00 42.24  ? 111 TYR A CE2 1 
ATOM   2695 C CZ  . TYR B 1 124 ? 19.385  12.003  16.437  1.00 49.19  ? 111 TYR A CZ  1 
ATOM   2696 O OH  . TYR B 1 124 ? 18.150  12.573  16.557  1.00 45.65  ? 111 TYR A OH  1 
ATOM   2697 N N   . TRP B 1 125 ? 22.655  7.219   14.849  1.00 37.26  ? 112 TRP A N   1 
ATOM   2698 C CA  . TRP B 1 125 ? 21.869  6.201   14.172  1.00 37.82  ? 112 TRP A CA  1 
ATOM   2699 C C   . TRP B 1 125 ? 21.571  5.047   15.143  1.00 35.53  ? 112 TRP A C   1 
ATOM   2700 O O   . TRP B 1 125 ? 20.412  4.684   15.334  1.00 32.13  ? 112 TRP A O   1 
ATOM   2701 C CB  . TRP B 1 125 ? 22.657  5.704   12.942  1.00 35.15  ? 112 TRP A CB  1 
ATOM   2702 C CG  . TRP B 1 125 ? 22.012  4.511   12.305  1.00 36.29  ? 112 TRP A CG  1 
ATOM   2703 C CD1 . TRP B 1 125 ? 22.075  3.193   12.695  1.00 35.38  ? 112 TRP A CD1 1 
ATOM   2704 C CD2 . TRP B 1 125 ? 21.008  4.573   11.262  1.00 30.66  ? 112 TRP A CD2 1 
ATOM   2705 N NE1 . TRP B 1 125 ? 21.242  2.441   11.904  1.00 31.18  ? 112 TRP A NE1 1 
ATOM   2706 C CE2 . TRP B 1 125 ? 20.586  3.248   11.024  1.00 30.83  ? 112 TRP A CE2 1 
ATOM   2707 C CE3 . TRP B 1 125 ? 20.479  5.601   10.470  1.00 33.18  ? 112 TRP A CE3 1 
ATOM   2708 C CZ2 . TRP B 1 125 ? 19.595  2.951   10.069  1.00 33.77  ? 112 TRP A CZ2 1 
ATOM   2709 C CZ3 . TRP B 1 125 ? 19.517  5.306   9.527   1.00 31.58  ? 112 TRP A CZ3 1 
ATOM   2710 C CH2 . TRP B 1 125 ? 19.037  3.995   9.365   1.00 30.09  ? 112 TRP A CH2 1 
ATOM   2711 N N   . ASP B 1 126 ? 22.631  4.492   15.758  1.00 34.15  ? 113 ASP A N   1 
ATOM   2712 C CA  . ASP B 1 126 ? 22.544  3.342   16.644  1.00 35.74  ? 113 ASP A CA  1 
ATOM   2713 C C   . ASP B 1 126 ? 21.582  3.663   17.785  1.00 37.34  ? 113 ASP A C   1 
ATOM   2714 O O   . ASP B 1 126 ? 20.675  2.876   18.105  1.00 36.90  ? 113 ASP A O   1 
ATOM   2715 C CB  . ASP B 1 126 ? 23.892  2.869   17.191  1.00 36.80  ? 113 ASP A CB  1 
ATOM   2716 C CG  . ASP B 1 126 ? 24.789  2.193   16.151  1.00 39.02  ? 113 ASP A CG  1 
ATOM   2717 O OD1 . ASP B 1 126 ? 24.305  1.952   15.028  1.00 40.40  ? 113 ASP A OD1 1 
ATOM   2718 O OD2 . ASP B 1 126 ? 25.930  1.855   16.461  1.00 43.92  ? 113 ASP A OD2 1 
ATOM   2719 N N   . GLU B 1 127 ? 21.791  4.831   18.385  1.00 35.65  ? 114 GLU A N   1 
ATOM   2720 C CA  . GLU B 1 127 ? 20.992  5.212   19.555  1.00 35.70  ? 114 GLU A CA  1 
ATOM   2721 C C   . GLU B 1 127 ? 19.513  5.346   19.172  1.00 34.60  ? 114 GLU A C   1 
ATOM   2722 O O   . GLU B 1 127 ? 18.612  4.831   19.870  1.00 32.95  ? 114 GLU A O   1 
ATOM   2723 C CB  . GLU B 1 127 ? 21.658  6.390   20.269  1.00 40.09  ? 114 GLU A CB  1 
ATOM   2724 C CG  . GLU B 1 127 ? 20.903  6.895   21.495  1.00 47.15  ? 114 GLU A CG  1 
ATOM   2725 C CD  . GLU B 1 127 ? 19.692  7.772   21.266  1.00 52.60  ? 114 GLU A CD  1 
ATOM   2726 O OE1 . GLU B 1 127 ? 18.773  7.743   22.135  1.00 59.06  ? 114 GLU A OE1 1 
ATOM   2727 O OE2 . GLU B 1 127 ? 19.657  8.492   20.243  1.00 55.25  ? 114 GLU A OE2 1 
ATOM   2728 N N   . ARG B 1 128 ? 19.227  6.004   18.043  1.00 32.77  ? 115 ARG A N   1 
ATOM   2729 C CA  . ARG B 1 128 ? 17.846  6.150   17.588  1.00 32.76  ? 115 ARG A CA  1 
ATOM   2730 C C   . ARG B 1 128 ? 17.194  4.807   17.190  1.00 33.37  ? 115 ARG A C   1 
ATOM   2731 O O   . ARG B 1 128 ? 16.020  4.590   17.507  1.00 28.37  ? 115 ARG A O   1 
ATOM   2732 C CB  . ARG B 1 128 ? 17.706  7.068   16.366  1.00 36.84  ? 115 ARG A CB  1 
ATOM   2733 C CG  . ARG B 1 128 ? 18.125  8.515   16.527  1.00 37.94  ? 115 ARG A CG  1 
ATOM   2734 C CD  . ARG B 1 128 ? 17.058  9.399   17.116  1.00 42.27  ? 115 ARG A CD  1 
ATOM   2735 N NE  . ARG B 1 128 ? 16.849  9.279   18.564  1.00 43.94  ? 115 ARG A NE  1 
ATOM   2736 C CZ  . ARG B 1 128 ? 16.810  10.331  19.374  1.00 51.35  ? 115 ARG A CZ  1 
ATOM   2737 N NH1 . ARG B 1 128 ? 16.730  11.557  18.888  1.00 57.16  ? 115 ARG A NH1 1 
ATOM   2738 N NH2 . ARG B 1 128 ? 16.805  10.165  20.688  1.00 51.98  ? 115 ARG A NH2 1 
ATOM   2739 N N   . MET B 1 129 ? 17.937  3.881   16.539  1.00 30.49  ? 116 MET A N   1 
ATOM   2740 C CA  . MET B 1 129 ? 17.373  2.546   16.220  1.00 29.57  ? 116 MET A CA  1 
ATOM   2741 C C   . MET B 1 129 ? 17.050  1.790   17.515  1.00 31.92  ? 116 MET A C   1 
ATOM   2742 O O   . MET B 1 129 ? 16.034  1.064   17.612  1.00 30.08  ? 116 MET A O   1 
ATOM   2743 C CB  . MET B 1 129 ? 18.263  1.706   15.283  1.00 30.21  ? 116 MET A CB  1 
ATOM   2744 C CG  . MET B 1 129 ? 18.404  2.365   13.872  1.00 28.92  ? 116 MET A CG  1 
ATOM   2745 S SD  . MET B 1 129 ? 16.725  2.293   13.130  1.00 41.88  ? 116 MET A SD  1 
ATOM   2746 C CE  . MET B 1 129 ? 16.745  4.038   12.840  1.00 27.22  ? 116 MET A CE  1 
ATOM   2747 N N   . GLN B 1 130 ? 17.869  2.024   18.514  1.00 30.56  ? 117 GLN A N   1 
ATOM   2748 C CA  . GLN B 1 130 ? 17.708  1.332   19.768  1.00 34.96  ? 117 GLN A CA  1 
ATOM   2749 C C   . GLN B 1 130 ? 16.498  1.840   20.574  1.00 33.32  ? 117 GLN A C   1 
ATOM   2750 O O   . GLN B 1 130 ? 15.819  1.010   21.211  1.00 29.87  ? 117 GLN A O   1 
ATOM   2751 C CB  . GLN B 1 130 ? 19.035  1.239   20.516  1.00 36.68  ? 117 GLN A CB  1 
ATOM   2752 C CG  . GLN B 1 130 ? 20.056  0.384   19.761  1.00 41.77  ? 117 GLN A CG  1 
ATOM   2753 C CD  . GLN B 1 130 ? 21.455  0.535   20.304  1.00 42.32  ? 117 GLN A CD  1 
ATOM   2754 O OE1 . GLN B 1 130 ? 21.661  1.220   21.306  1.00 49.21  ? 117 GLN A OE1 1 
ATOM   2755 N NE2 . GLN B 1 130 ? 22.409  -0.109  19.650  1.00 43.49  ? 117 GLN A NE2 1 
ATOM   2756 N N   . THR B 1 131 ? 16.258  3.166   20.560  1.00 31.90  ? 118 THR A N   1 
ATOM   2757 C CA  . THR B 1 131 ? 15.159  3.741   21.353  1.00 30.94  ? 118 THR A CA  1 
ATOM   2758 C C   . THR B 1 131 ? 13.835  3.639   20.579  1.00 29.32  ? 118 THR A C   1 
ATOM   2759 O O   . THR B 1 131 ? 12.728  3.677   21.173  1.00 27.36  ? 118 THR A O   1 
ATOM   2760 C CB  . THR B 1 131 ? 15.462  5.180   21.804  1.00 33.01  ? 118 THR A CB  1 
ATOM   2761 O OG1 . THR B 1 131 ? 15.744  5.839   20.581  1.00 34.93  ? 118 THR A OG1 1 
ATOM   2762 C CG2 . THR B 1 131 ? 16.746  5.434   22.568  1.00 32.06  ? 118 THR A CG2 1 
ATOM   2763 N N   . ASN B 1 132 ? 13.925  3.520   19.219  1.00 27.43  ? 119 ASN A N   1 
ATOM   2764 C CA  . ASN B 1 132 ? 12.728  3.478   18.383  1.00 26.04  ? 119 ASN A CA  1 
ATOM   2765 C C   . ASN B 1 132 ? 12.326  2.059   17.931  1.00 27.71  ? 119 ASN A C   1 
ATOM   2766 O O   . ASN B 1 132 ? 11.157  1.837   17.675  1.00 27.08  ? 119 ASN A O   1 
ATOM   2767 C CB  . ASN B 1 132 ? 12.817  4.431   17.198  1.00 28.98  ? 119 ASN A CB  1 
ATOM   2768 C CG  . ASN B 1 132 ? 12.635  5.900   17.579  1.00 30.91  ? 119 ASN A CG  1 
ATOM   2769 O OD1 . ASN B 1 132 ? 11.565  6.299   18.030  1.00 32.54  ? 119 ASN A OD1 1 
ATOM   2770 N ND2 . ASN B 1 132 ? 13.617  6.753   17.320  1.00 32.78  ? 119 ASN A ND2 1 
ATOM   2771 N N   . LEU B 1 133 ? 13.240  1.089   17.811  1.00 24.38  ? 120 LEU A N   1 
ATOM   2772 C CA  . LEU B 1 133 ? 12.874  -0.147  17.153  1.00 23.52  ? 120 LEU A CA  1 
ATOM   2773 C C   . LEU B 1 133 ? 13.227  -1.348  18.026  1.00 21.61  ? 120 LEU A C   1 
ATOM   2774 O O   . LEU B 1 133 ? 12.408  -2.218  18.233  1.00 21.77  ? 120 LEU A O   1 
ATOM   2775 C CB  . LEU B 1 133 ? 13.584  -0.234  15.779  1.00 22.65  ? 120 LEU A CB  1 
ATOM   2776 C CG  . LEU B 1 133 ? 13.613  -1.650  15.194  1.00 23.41  ? 120 LEU A CG  1 
ATOM   2777 C CD1 . LEU B 1 133 ? 12.146  -2.062  14.867  1.00 23.73  ? 120 LEU A CD1 1 
ATOM   2778 C CD2 . LEU B 1 133 ? 14.472  -1.654  13.941  1.00 23.13  ? 120 LEU A CD2 1 
ATOM   2779 N N   . ARG B 1 134 ? 14.488  -1.417  18.528  1.00 25.71  ? 121 ARG A N   1 
ATOM   2780 C CA  . ARG B 1 134 ? 15.040  -2.651  19.088  1.00 26.35  ? 121 ARG A CA  1 
ATOM   2781 C C   . ARG B 1 134 ? 14.169  -3.138  20.273  1.00 25.57  ? 121 ARG A C   1 
ATOM   2782 O O   . ARG B 1 134 ? 13.962  -4.344  20.430  1.00 24.76  ? 121 ARG A O   1 
ATOM   2783 C CB  . ARG B 1 134 ? 16.500  -2.431  19.532  1.00 28.20  ? 121 ARG A CB  1 
ATOM   2784 C CG  . ARG B 1 134 ? 17.153  -3.678  20.093  1.00 28.01  ? 121 ARG A CG  1 
ATOM   2785 C CD  . ARG B 1 134 ? 18.621  -3.447  20.272  1.00 29.82  ? 121 ARG A CD  1 
ATOM   2786 N NE  . ARG B 1 134 ? 18.852  -2.731  21.544  1.00 31.70  ? 121 ARG A NE  1 
ATOM   2787 C CZ  . ARG B 1 134 ? 20.091  -2.463  21.964  1.00 34.44  ? 121 ARG A CZ  1 
ATOM   2788 N NH1 . ARG B 1 134 ? 21.095  -3.026  21.344  1.00 35.66  ? 121 ARG A NH1 1 
ATOM   2789 N NH2 . ARG B 1 134 ? 20.264  -1.655  23.016  1.00 35.71  ? 121 ARG A NH2 1 
ATOM   2790 N N   . HIS B 1 135 ? 13.767  -2.216  21.152  1.00 26.24  ? 122 HIS A N   1 
ATOM   2791 C CA  . HIS B 1 135 ? 13.038  -2.649  22.367  1.00 26.44  ? 122 HIS A CA  1 
ATOM   2792 C C   . HIS B 1 135 ? 11.719  -3.345  22.017  1.00 24.16  ? 122 HIS A C   1 
ATOM   2793 O O   . HIS B 1 135 ? 11.251  -4.256  22.732  1.00 23.41  ? 122 HIS A O   1 
ATOM   2794 C CB  . HIS B 1 135 ? 12.785  -1.484  23.326  1.00 26.26  ? 122 HIS A CB  1 
ATOM   2795 C CG  . HIS B 1 135 ? 12.005  -0.389  22.703  1.00 26.78  ? 122 HIS A CG  1 
ATOM   2796 N ND1 . HIS B 1 135 ? 10.627  -0.397  22.702  1.00 25.64  ? 122 HIS A ND1 1 
ATOM   2797 C CD2 . HIS B 1 135 ? 12.387  0.752   22.067  1.00 26.61  ? 122 HIS A CD2 1 
ATOM   2798 C CE1 . HIS B 1 135 ? 10.176  0.721   22.119  1.00 25.22  ? 122 HIS A CE1 1 
ATOM   2799 N NE2 . HIS B 1 135 ? 11.237  1.455   21.746  1.00 24.89  ? 122 HIS A NE2 1 
ATOM   2800 N N   . ALA B 1 136 ? 11.148  -2.982  20.853  1.00 23.42  ? 123 ALA A N   1 
ATOM   2801 C CA  . ALA B 1 136 ? 9.810   -3.528  20.507  1.00 21.16  ? 123 ALA A CA  1 
ATOM   2802 C C   . ALA B 1 136 ? 9.982   -5.015  20.181  1.00 23.69  ? 123 ALA A C   1 
ATOM   2803 O O   . ALA B 1 136 ? 9.161   -5.858  20.587  1.00 25.59  ? 123 ALA A O   1 
ATOM   2804 C CB  . ALA B 1 136 ? 9.205   -2.769  19.323  1.00 20.19  ? 123 ALA A CB  1 
ATOM   2805 N N   . PHE B 1 137 ? 11.143  -5.397  19.551  1.00 21.95  ? 124 PHE A N   1 
ATOM   2806 C CA  . PHE B 1 137 ? 11.383  -6.805  19.295  1.00 23.36  ? 124 PHE A CA  1 
ATOM   2807 C C   . PHE B 1 137 ? 11.597  -7.546  20.634  1.00 23.06  ? 124 PHE A C   1 
ATOM   2808 O O   . PHE B 1 137 ? 11.037  -8.605  20.892  1.00 25.09  ? 124 PHE A O   1 
ATOM   2809 C CB  . PHE B 1 137 ? 12.606  -7.051  18.371  1.00 21.98  ? 124 PHE A CB  1 
ATOM   2810 C CG  . PHE B 1 137 ? 12.953  -8.527  18.331  1.00 24.52  ? 124 PHE A CG  1 
ATOM   2811 C CD1 . PHE B 1 137 ? 12.168  -9.430  17.637  1.00 28.09  ? 124 PHE A CD1 1 
ATOM   2812 C CD2 . PHE B 1 137 ? 14.022  -9.025  19.082  1.00 28.35  ? 124 PHE A CD2 1 
ATOM   2813 C CE1 . PHE B 1 137 ? 12.405  -10.794 17.674  1.00 31.29  ? 124 PHE A CE1 1 
ATOM   2814 C CE2 . PHE B 1 137 ? 14.274  -10.411 19.153  1.00 33.40  ? 124 PHE A CE2 1 
ATOM   2815 C CZ  . PHE B 1 137 ? 13.484  -11.285 18.402  1.00 32.02  ? 124 PHE A CZ  1 
ATOM   2816 N N   . PHE B 1 138 ? 12.441  -6.970  21.482  1.00 23.44  ? 125 PHE A N   1 
ATOM   2817 C CA  . PHE B 1 138 ? 12.813  -7.709  22.690  1.00 24.28  ? 125 PHE A CA  1 
ATOM   2818 C C   . PHE B 1 138 ? 11.622  -7.780  23.661  1.00 23.41  ? 125 PHE A C   1 
ATOM   2819 O O   . PHE B 1 138 ? 11.527  -8.795  24.406  1.00 25.28  ? 125 PHE A O   1 
ATOM   2820 C CB  . PHE B 1 138 ? 14.124  -7.329  23.405  1.00 26.87  ? 125 PHE A CB  1 
ATOM   2821 C CG  . PHE B 1 138 ? 15.291  -7.788  22.554  1.00 27.95  ? 125 PHE A CG  1 
ATOM   2822 C CD1 . PHE B 1 138 ? 15.659  -9.124  22.583  1.00 27.71  ? 125 PHE A CD1 1 
ATOM   2823 C CD2 . PHE B 1 138 ? 15.858  -6.916  21.607  1.00 28.12  ? 125 PHE A CD2 1 
ATOM   2824 C CE1 . PHE B 1 138 ? 16.720  -9.560  21.811  1.00 30.80  ? 125 PHE A CE1 1 
ATOM   2825 C CE2 . PHE B 1 138 ? 16.877  -7.374  20.785  1.00 29.86  ? 125 PHE A CE2 1 
ATOM   2826 C CZ  . PHE B 1 138 ? 17.301  -8.702  20.861  1.00 32.25  ? 125 PHE A CZ  1 
ATOM   2827 N N   . ALA B 1 139 ? 10.752  -6.743  23.643  1.00 23.44  ? 126 ALA A N   1 
ATOM   2828 C CA  . ALA B 1 139 ? 9.577   -6.826  24.516  1.00 21.89  ? 126 ALA A CA  1 
ATOM   2829 C C   . ALA B 1 139 ? 8.650   -7.938  24.050  1.00 23.87  ? 126 ALA A C   1 
ATOM   2830 O O   . ALA B 1 139 ? 8.028   -8.614  24.870  1.00 27.03  ? 126 ALA A O   1 
ATOM   2831 C CB  . ALA B 1 139 ? 8.861   -5.498  24.596  1.00 22.02  ? 126 ALA A CB  1 
ATOM   2832 N N   . ALA B 1 140 ? 8.517   -8.073  22.709  1.00 24.41  ? 127 ALA A N   1 
ATOM   2833 C CA  . ALA B 1 140 ? 7.631   -9.107  22.180  1.00 24.53  ? 127 ALA A CA  1 
ATOM   2834 C C   . ALA B 1 140 ? 8.242   -10.437 22.560  1.00 24.59  ? 127 ALA A C   1 
ATOM   2835 O O   . ALA B 1 140 ? 7.572   -11.387 22.928  1.00 27.44  ? 127 ALA A O   1 
ATOM   2836 C CB  . ALA B 1 140 ? 7.512   -8.947  20.652  1.00 21.93  ? 127 ALA A CB  1 
ATOM   2837 N N   . GLN B 1 141 ? 9.577   -10.519 22.474  1.00 24.92  ? 128 GLN A N   1 
ATOM   2838 C CA  . GLN B 1 141 ? 10.211  -11.792 22.719  1.00 25.06  ? 128 GLN A CA  1 
ATOM   2839 C C   . GLN B 1 141 ? 10.017  -12.172 24.208  1.00 29.46  ? 128 GLN A C   1 
ATOM   2840 O O   . GLN B 1 141 ? 9.789   -13.346 24.524  1.00 30.02  ? 128 GLN A O   1 
ATOM   2841 C CB  . GLN B 1 141 ? 11.697  -11.720 22.328  1.00 27.65  ? 128 GLN A CB  1 
ATOM   2842 C CG  . GLN B 1 141 ? 12.478  -12.999 22.663  1.00 31.49  ? 128 GLN A CG  1 
ATOM   2843 C CD  . GLN B 1 141 ? 13.968  -12.754 22.553  1.00 32.42  ? 128 GLN A CD  1 
ATOM   2844 O OE1 . GLN B 1 141 ? 14.575  -12.006 23.340  1.00 33.03  ? 128 GLN A OE1 1 
ATOM   2845 N NE2 . GLN B 1 141 ? 14.571  -13.390 21.576  1.00 32.73  ? 128 GLN A NE2 1 
ATOM   2846 N N   . ALA B 1 142 ? 10.054  -11.161 25.081  1.00 28.09  ? 129 ALA A N   1 
ATOM   2847 C CA  . ALA B 1 142 ? 9.863   -11.380 26.531  1.00 29.13  ? 129 ALA A CA  1 
ATOM   2848 C C   . ALA B 1 142 ? 8.448   -11.812 26.927  1.00 27.95  ? 129 ALA A C   1 
ATOM   2849 O O   . ALA B 1 142 ? 8.259   -12.672 27.819  1.00 30.45  ? 129 ALA A O   1 
ATOM   2850 C CB  . ALA B 1 142 ? 10.297  -10.164 27.283  1.00 29.35  ? 129 ALA A CB  1 
ATOM   2851 N N   . VAL B 1 143 ? 7.438   -11.160 26.342  1.00 27.84  ? 130 VAL A N   1 
ATOM   2852 C CA  . VAL B 1 143 ? 6.063   -11.506 26.674  1.00 25.88  ? 130 VAL A CA  1 
ATOM   2853 C C   . VAL B 1 143 ? 5.605   -12.804 26.010  1.00 27.60  ? 130 VAL A C   1 
ATOM   2854 O O   . VAL B 1 143 ? 4.743   -13.474 26.558  1.00 28.32  ? 130 VAL A O   1 
ATOM   2855 C CB  . VAL B 1 143 ? 5.089   -10.361 26.383  1.00 24.40  ? 130 VAL A CB  1 
ATOM   2856 C CG1 . VAL B 1 143 ? 5.506   -9.138  27.208  1.00 23.72  ? 130 VAL A CG1 1 
ATOM   2857 C CG2 . VAL B 1 143 ? 4.914   -10.188 24.861  1.00 22.82  ? 130 VAL A CG2 1 
ATOM   2858 N N   . ALA B 1 144 ? 6.183   -13.163 24.854  1.00 27.65  ? 131 ALA A N   1 
ATOM   2859 C CA  . ALA B 1 144 ? 5.690   -14.332 24.126  1.00 30.31  ? 131 ALA A CA  1 
ATOM   2860 C C   . ALA B 1 144 ? 5.573   -15.609 24.965  1.00 30.45  ? 131 ALA A C   1 
ATOM   2861 O O   . ALA B 1 144 ? 4.540   -16.257 24.871  1.00 31.61  ? 131 ALA A O   1 
ATOM   2862 C CB  . ALA B 1 144 ? 6.404   -14.620 22.805  1.00 31.95  ? 131 ALA A CB  1 
ATOM   2863 N N   . PRO B 1 145 ? 6.594   -16.153 25.669  1.00 33.11  ? 132 PRO A N   1 
ATOM   2864 C CA  . PRO B 1 145 ? 6.417   -17.474 26.263  1.00 34.71  ? 132 PRO A CA  1 
ATOM   2865 C C   . PRO B 1 145 ? 5.217   -17.554 27.206  1.00 33.76  ? 132 PRO A C   1 
ATOM   2866 O O   . PRO B 1 145 ? 4.505   -18.551 27.165  1.00 36.39  ? 132 PRO A O   1 
ATOM   2867 C CB  . PRO B 1 145 ? 7.770   -17.803 26.915  1.00 35.35  ? 132 PRO A CB  1 
ATOM   2868 C CG  . PRO B 1 145 ? 8.706   -16.860 26.163  1.00 32.65  ? 132 PRO A CG  1 
ATOM   2869 C CD  . PRO B 1 145 ? 7.957   -15.633 25.865  1.00 34.64  ? 132 PRO A CD  1 
ATOM   2870 N N   . GLY B 1 146 ? 4.966   -16.470 27.972  1.00 36.19  ? 133 GLY A N   1 
ATOM   2871 C CA  . GLY B 1 146 ? 3.847   -16.343 28.909  1.00 31.44  ? 133 GLY A CA  1 
ATOM   2872 C C   . GLY B 1 146 ? 2.481   -16.357 28.200  1.00 31.21  ? 133 GLY A C   1 
ATOM   2873 O O   . GLY B 1 146 ? 1.558   -17.145 28.558  1.00 33.72  ? 133 GLY A O   1 
ATOM   2874 N N   . MET B 1 147 ? 2.457   -15.647 27.047  1.00 30.18  ? 134 MET A N   1 
ATOM   2875 C CA  . MET B 1 147 ? 1.300   -15.645 26.164  1.00 28.54  ? 134 MET A CA  1 
ATOM   2876 C C   . MET B 1 147 ? 1.038   -17.055 25.660  1.00 27.76  ? 134 MET A C   1 
ATOM   2877 O O   . MET B 1 147 ? -0.097  -17.465 25.663  1.00 34.75  ? 134 MET A O   1 
ATOM   2878 C CB  . MET B 1 147 ? 1.461   -14.683 24.992  1.00 24.74  ? 134 MET A CB  1 
ATOM   2879 C CG  . MET B 1 147 ? 1.200   -13.291 25.478  1.00 24.89  ? 134 MET A CG  1 
ATOM   2880 S SD  . MET B 1 147 ? 1.560   -12.093 24.188  1.00 25.72  ? 134 MET A SD  1 
ATOM   2881 C CE  . MET B 1 147 ? 1.157   -10.634 25.178  1.00 22.33  ? 134 MET A CE  1 
ATOM   2882 N N   . ALA B 1 148 ? 2.044   -17.727 25.098  1.00 31.16  ? 135 ALA A N   1 
ATOM   2883 C CA  . ALA B 1 148 ? 1.891   -19.052 24.499  1.00 31.40  ? 135 ALA A CA  1 
ATOM   2884 C C   . ALA B 1 148 ? 1.446   -20.102 25.507  1.00 33.84  ? 135 ALA A C   1 
ATOM   2885 O O   . ALA B 1 148 ? 0.677   -20.988 25.102  1.00 35.17  ? 135 ALA A O   1 
ATOM   2886 C CB  . ALA B 1 148 ? 3.166   -19.519 23.817  1.00 33.42  ? 135 ALA A CB  1 
ATOM   2887 N N   . ARG B 1 149 ? 1.988   -20.090 26.742  1.00 34.86  ? 136 ARG A N   1 
ATOM   2888 C CA  . ARG B 1 149 ? 1.581   -20.982 27.833  1.00 37.16  ? 136 ARG A CA  1 
ATOM   2889 C C   . ARG B 1 149 ? 0.067   -20.888 27.991  1.00 38.25  ? 136 ARG A C   1 
ATOM   2890 O O   . ARG B 1 149 ? -0.598  -21.913 28.064  1.00 42.40  ? 136 ARG A O   1 
ATOM   2891 C CB  . ARG B 1 149 ? 2.124   -20.622 29.236  1.00 35.59  ? 136 ARG A CB  1 
ATOM   2892 N N   . ARG B 1 150 ? -0.455  -19.634 27.992  1.00 36.60  ? 137 ARG A N   1 
ATOM   2893 C CA  . ARG B 1 150 ? -1.886  -19.441 28.169  1.00 37.15  ? 137 ARG A CA  1 
ATOM   2894 C C   . ARG B 1 150 ? -2.645  -19.778 26.873  1.00 37.59  ? 137 ARG A C   1 
ATOM   2895 O O   . ARG B 1 150 ? -3.770  -20.268 26.906  1.00 37.44  ? 137 ARG A O   1 
ATOM   2896 C CB  . ARG B 1 150 ? -2.180  -18.047 28.746  1.00 37.24  ? 137 ARG A CB  1 
ATOM   2897 C CG  . ARG B 1 150 ? -3.646  -17.639 28.682  1.00 33.81  ? 137 ARG A CG  1 
ATOM   2898 C CD  . ARG B 1 150 ? -3.947  -16.357 29.446  1.00 30.25  ? 137 ARG A CD  1 
ATOM   2899 N NE  . ARG B 1 150 ? -3.318  -15.328 28.618  1.00 34.33  ? 137 ARG A NE  1 
ATOM   2900 C CZ  . ARG B 1 150 ? -2.360  -14.464 28.918  1.00 35.33  ? 137 ARG A CZ  1 
ATOM   2901 N NH1 . ARG B 1 150 ? -2.199  -14.058 30.193  1.00 32.16  ? 137 ARG A NH1 1 
ATOM   2902 N NH2 . ARG B 1 150 ? -1.696  -13.870 27.900  1.00 28.86  ? 137 ARG A NH2 1 
ATOM   2903 N N   . GLY B 1 151 ? -2.045  -19.520 25.701  1.00 33.57  ? 138 GLY A N   1 
ATOM   2904 C CA  . GLY B 1 151 ? -2.729  -19.772 24.442  1.00 32.22  ? 138 GLY A CA  1 
ATOM   2905 C C   . GLY B 1 151 ? -3.345  -18.505 23.841  1.00 29.59  ? 138 GLY A C   1 
ATOM   2906 O O   . GLY B 1 151 ? -4.175  -18.633 22.942  1.00 31.09  ? 138 GLY A O   1 
ATOM   2907 N N   . SER B 1 152 ? -3.012  -17.325 24.392  1.00 26.58  ? 139 SER A N   1 
ATOM   2908 C CA  . SER B 1 152 ? -3.637  -16.099 23.878  1.00 26.50  ? 139 SER A CA  1 
ATOM   2909 C C   . SER B 1 152 ? -2.775  -14.920 24.262  1.00 24.60  ? 139 SER A C   1 
ATOM   2910 O O   . SER B 1 152 ? -2.046  -14.971 25.284  1.00 27.29  ? 139 SER A O   1 
ATOM   2911 C CB  . SER B 1 152 ? -5.055  -15.925 24.500  1.00 28.41  ? 139 SER A CB  1 
ATOM   2912 O OG  . SER B 1 152 ? -4.974  -15.494 25.876  1.00 29.63  ? 139 SER A OG  1 
ATOM   2913 N N   . GLY B 1 153 ? -2.870  -13.845 23.449  1.00 23.11  ? 140 GLY A N   1 
ATOM   2914 C CA  . GLY B 1 153 ? -2.182  -12.611 23.821  1.00 22.69  ? 140 GLY A CA  1 
ATOM   2915 C C   . GLY B 1 153 ? -2.256  -11.660 22.612  1.00 20.77  ? 140 GLY A C   1 
ATOM   2916 O O   . GLY B 1 153 ? -2.563  -12.084 21.501  1.00 23.03  ? 140 GLY A O   1 
ATOM   2917 N N   . ALA B 1 154 ? -1.926  -10.405 22.845  1.00 21.66  ? 141 ALA A N   1 
ATOM   2918 C CA  . ALA B 1 154 ? -2.049  -9.414  21.768  1.00 19.15  ? 141 ALA A CA  1 
ATOM   2919 C C   . ALA B 1 154 ? -0.924  -8.428  21.931  1.00 20.13  ? 141 ALA A C   1 
ATOM   2920 O O   . ALA B 1 154 ? -0.595  -8.032  23.076  1.00 20.76  ? 141 ALA A O   1 
ATOM   2921 C CB  . ALA B 1 154 ? -3.388  -8.695  21.873  1.00 20.85  ? 141 ALA A CB  1 
ATOM   2922 N N   . ILE B 1 155 ? -0.407  -8.000  20.765  1.00 19.94  ? 142 ILE A N   1 
ATOM   2923 C CA  . ILE B 1 155 ? 0.688   -7.046  20.756  1.00 19.31  ? 142 ILE A CA  1 
ATOM   2924 C C   . ILE B 1 155 ? 0.295   -5.940  19.826  1.00 15.75  ? 142 ILE A C   1 
ATOM   2925 O O   . ILE B 1 155 ? -0.263  -6.219  18.790  1.00 18.01  ? 142 ILE A O   1 
ATOM   2926 C CB  . ILE B 1 155 ? 1.991   -7.731  20.317  1.00 20.01  ? 142 ILE A CB  1 
ATOM   2927 C CG1 . ILE B 1 155 ? 2.375   -8.822  21.324  1.00 23.37  ? 142 ILE A CG1 1 
ATOM   2928 C CG2 . ILE B 1 155 ? 3.112   -6.705  20.106  1.00 21.00  ? 142 ILE A CG2 1 
ATOM   2929 C CD1 . ILE B 1 155 ? 3.594   -9.631  20.892  1.00 24.08  ? 142 ILE A CD1 1 
ATOM   2930 N N   . ILE B 1 156 ? 0.533   -4.706  20.253  1.00 17.13  ? 143 ILE A N   1 
ATOM   2931 C CA  . ILE B 1 156 ? 0.217   -3.549  19.426  1.00 16.01  ? 143 ILE A CA  1 
ATOM   2932 C C   . ILE B 1 156 ? 1.528   -2.780  19.269  1.00 16.04  ? 143 ILE A C   1 
ATOM   2933 O O   . ILE B 1 156 ? 2.054   -2.387  20.290  1.00 16.63  ? 143 ILE A O   1 
ATOM   2934 C CB  . ILE B 1 156 ? -0.816  -2.641  20.139  1.00 16.54  ? 143 ILE A CB  1 
ATOM   2935 C CG1 . ILE B 1 156 ? -2.162  -3.369  20.300  1.00 15.44  ? 143 ILE A CG1 1 
ATOM   2936 C CG2 . ILE B 1 156 ? -1.005  -1.332  19.304  1.00 14.95  ? 143 ILE A CG2 1 
ATOM   2937 C CD1 . ILE B 1 156 ? -3.167  -2.757  21.241  1.00 17.70  ? 143 ILE A CD1 1 
ATOM   2938 N N   . ASN B 1 157 ? 2.044   -2.659  18.041  1.00 15.67  ? 144 ASN A N   1 
ATOM   2939 C CA  . ASN B 1 157 ? 3.237   -1.850  17.780  1.00 16.73  ? 144 ASN A CA  1 
ATOM   2940 C C   . ASN B 1 157 ? 2.766   -0.464  17.347  1.00 17.96  ? 144 ASN A C   1 
ATOM   2941 O O   . ASN B 1 157 ? 2.003   -0.352  16.402  1.00 18.15  ? 144 ASN A O   1 
ATOM   2942 C CB  . ASN B 1 157 ? 3.967   -2.533  16.606  1.00 17.88  ? 144 ASN A CB  1 
ATOM   2943 C CG  . ASN B 1 157 ? 4.692   -3.803  16.990  1.00 22.07  ? 144 ASN A CG  1 
ATOM   2944 O OD1 . ASN B 1 157 ? 5.079   -3.935  18.144  1.00 20.33  ? 144 ASN A OD1 1 
ATOM   2945 N ND2 . ASN B 1 157 ? 4.739   -4.838  16.175  1.00 21.53  ? 144 ASN A ND2 1 
ATOM   2946 N N   . MET B 1 158 ? 3.204   0.611   18.022  1.00 16.67  ? 145 MET A N   1 
ATOM   2947 C CA  . MET B 1 158 ? 2.915   1.962   17.529  1.00 19.04  ? 145 MET A CA  1 
ATOM   2948 C C   . MET B 1 158 ? 3.739   2.261   16.268  1.00 20.19  ? 145 MET A C   1 
ATOM   2949 O O   . MET B 1 158 ? 4.989   2.135   16.216  1.00 22.02  ? 145 MET A O   1 
ATOM   2950 C CB  . MET B 1 158 ? 3.225   2.993   18.612  1.00 17.81  ? 145 MET A CB  1 
ATOM   2951 C CG  . MET B 1 158 ? 2.355   2.745   19.813  1.00 18.85  ? 145 MET A CG  1 
ATOM   2952 S SD  . MET B 1 158 ? 0.621   3.092   19.426  1.00 23.78  ? 145 MET A SD  1 
ATOM   2953 C CE  . MET B 1 158 ? 0.872   4.858   19.136  1.00 19.01  ? 145 MET A CE  1 
ATOM   2954 N N   . GLY B 1 159 ? 3.015   2.554   15.214  1.00 18.02  ? 146 GLY A N   1 
ATOM   2955 C CA  . GLY B 1 159 ? 3.597   2.849   13.933  1.00 17.15  ? 146 GLY A CA  1 
ATOM   2956 C C   . GLY B 1 159 ? 3.480   4.352   13.708  1.00 18.72  ? 146 GLY A C   1 
ATOM   2957 O O   . GLY B 1 159 ? 3.361   5.102   14.657  1.00 22.65  ? 146 GLY A O   1 
ATOM   2958 N N   . SER B 1 160 ? 3.555   4.750   12.453  1.00 18.39  ? 147 SER A N   1 
ATOM   2959 C CA  . SER B 1 160 ? 3.493   6.179   12.141  1.00 17.91  ? 147 SER A CA  1 
ATOM   2960 C C   . SER B 1 160 ? 3.287   6.353   10.635  1.00 18.41  ? 147 SER A C   1 
ATOM   2961 O O   . SER B 1 160 ? 3.793   5.556   9.824   1.00 19.90  ? 147 SER A O   1 
ATOM   2962 C CB  . SER B 1 160 ? 4.795   6.944   12.493  1.00 21.34  ? 147 SER A CB  1 
ATOM   2963 O OG  . SER B 1 160 ? 4.717   8.315   12.047  1.00 22.18  ? 147 SER A OG  1 
ATOM   2964 N N   . ILE B 1 161 ? 2.426   7.307   10.242  1.00 16.26  ? 148 ILE A N   1 
ATOM   2965 C CA  . ILE B 1 161 ? 2.175   7.555   8.821   1.00 16.97  ? 148 ILE A CA  1 
ATOM   2966 C C   . ILE B 1 161 ? 3.328   8.310   8.182   1.00 17.26  ? 148 ILE A C   1 
ATOM   2967 O O   . ILE B 1 161 ? 3.344   8.437   6.929   1.00 18.94  ? 148 ILE A O   1 
ATOM   2968 C CB  . ILE B 1 161 ? 0.873   8.371   8.526   1.00 17.20  ? 148 ILE A CB  1 
ATOM   2969 C CG1 . ILE B 1 161 ? 0.966   9.732   9.113   1.00 22.00  ? 148 ILE A CG1 1 
ATOM   2970 C CG2 . ILE B 1 161 ? -0.397  7.644   8.966   1.00 18.51  ? 148 ILE A CG2 1 
ATOM   2971 C CD1 . ILE B 1 161 ? -0.104  10.652  8.635   1.00 20.42  ? 148 ILE A CD1 1 
ATOM   2972 N N   . SER B 1 162 ? 4.245   8.825   8.993   1.00 19.96  ? 149 SER A N   1 
ATOM   2973 C CA  . SER B 1 162 ? 5.363   9.633   8.489   1.00 21.75  ? 149 SER A CA  1 
ATOM   2974 C C   . SER B 1 162 ? 6.218   8.891   7.440   1.00 21.32  ? 149 SER A C   1 
ATOM   2975 O O   . SER B 1 162 ? 6.530   9.483   6.404   1.00 22.98  ? 149 SER A O   1 
ATOM   2976 C CB  . SER B 1 162 ? 6.246   10.116  9.641   1.00 25.73  ? 149 SER A CB  1 
ATOM   2977 O OG  . SER B 1 162 ? 6.800   8.962   10.289  1.00 28.04  ? 149 SER A OG  1 
ATOM   2978 N N   . TRP B 1 163 ? 6.463   7.577   7.587   1.00 19.46  ? 150 TRP A N   1 
ATOM   2979 C CA  . TRP B 1 163 ? 7.249   6.950   6.523   1.00 20.60  ? 150 TRP A CA  1 
ATOM   2980 C C   . TRP B 1 163 ? 6.398   6.647   5.310   1.00 20.37  ? 150 TRP A C   1 
ATOM   2981 O O   . TRP B 1 163 ? 6.899   6.756   4.170   1.00 20.01  ? 150 TRP A O   1 
ATOM   2982 C CB  . TRP B 1 163 ? 7.974   5.705   7.051   1.00 22.56  ? 150 TRP A CB  1 
ATOM   2983 C CG  . TRP B 1 163 ? 7.021   4.585   7.338   1.00 19.18  ? 150 TRP A CG  1 
ATOM   2984 C CD1 . TRP B 1 163 ? 6.467   4.290   8.561   1.00 18.48  ? 150 TRP A CD1 1 
ATOM   2985 C CD2 . TRP B 1 163 ? 6.476   3.621   6.422   1.00 19.65  ? 150 TRP A CD2 1 
ATOM   2986 N NE1 . TRP B 1 163 ? 5.606   3.219   8.500   1.00 16.42  ? 150 TRP A NE1 1 
ATOM   2987 C CE2 . TRP B 1 163 ? 5.587   2.800   7.195   1.00 19.73  ? 150 TRP A CE2 1 
ATOM   2988 C CE3 . TRP B 1 163 ? 6.599   3.382   5.042   1.00 21.37  ? 150 TRP A CE3 1 
ATOM   2989 C CZ2 . TRP B 1 163 ? 4.852   1.744   6.649   1.00 21.02  ? 150 TRP A CZ2 1 
ATOM   2990 C CZ3 . TRP B 1 163 ? 5.846   2.350   4.485   1.00 20.65  ? 150 TRP A CZ3 1 
ATOM   2991 C CH2 . TRP B 1 163 ? 4.972   1.535   5.274   1.00 21.95  ? 150 TRP A CH2 1 
ATOM   2992 N N   . MET B 1 164 ? 5.093   6.399   5.525   1.00 19.19  ? 151 MET A N   1 
ATOM   2993 C CA  . MET B 1 164 ? 4.181   6.190   4.400   1.00 18.18  ? 151 MET A CA  1 
ATOM   2994 C C   . MET B 1 164 ? 4.166   7.447   3.530   1.00 19.18  ? 151 MET A C   1 
ATOM   2995 O O   . MET B 1 164 ? 4.082   7.391   2.317   1.00 18.54  ? 151 MET A O   1 
ATOM   2996 C CB  . MET B 1 164 ? 2.737   5.915   4.903   1.00 19.05  ? 151 MET A CB  1 
ATOM   2997 C CG  . MET B 1 164 ? 2.722   4.639   5.768   1.00 24.85  ? 151 MET A CG  1 
ATOM   2998 S SD  . MET B 1 164 ? 1.134   4.409   6.629   1.00 23.47  ? 151 MET A SD  1 
ATOM   2999 C CE  . MET B 1 164 ? 1.330   2.722   7.252   1.00 26.27  ? 151 MET A CE  1 
ATOM   3000 N N   . ARG B 1 165 ? 4.141   8.644   4.175   1.00 20.36  ? 152 ARG A N   1 
ATOM   3001 C CA  . ARG B 1 165 ? 4.081   9.896   3.442   1.00 18.37  ? 152 ARG A CA  1 
ATOM   3002 C C   . ARG B 1 165 ? 5.492   10.373  3.055   1.00 19.38  ? 152 ARG A C   1 
ATOM   3003 O O   . ARG B 1 165 ? 5.605   11.443  2.479   1.00 19.51  ? 152 ARG A O   1 
ATOM   3004 C CB  . ARG B 1 165 ? 3.572   10.996  4.406   1.00 17.44  ? 152 ARG A CB  1 
ATOM   3005 C CG  . ARG B 1 165 ? 2.102   10.836  4.776   1.00 17.37  ? 152 ARG A CG  1 
ATOM   3006 C CD  . ARG B 1 165 ? 1.669   12.071  5.678   1.00 18.14  ? 152 ARG A CD  1 
ATOM   3007 N NE  . ARG B 1 165 ? 1.844   13.290  4.879   1.00 21.15  ? 152 ARG A NE  1 
ATOM   3008 C CZ  . ARG B 1 165 ? 1.872   14.545  5.386   1.00 23.44  ? 152 ARG A CZ  1 
ATOM   3009 N NH1 . ARG B 1 165 ? 1.733   14.660  6.725   1.00 23.07  ? 152 ARG A NH1 1 
ATOM   3010 N NH2 . ARG B 1 165 ? 2.062   15.586  4.571   1.00 25.89  ? 152 ARG A NH2 1 
ATOM   3011 N N   . GLY B 1 166 ? 6.543   9.520   3.243   1.00 17.76  ? 153 GLY A N   1 
ATOM   3012 C CA  . GLY B 1 166 ? 7.923   9.853   2.896   1.00 17.86  ? 153 GLY A CA  1 
ATOM   3013 C C   . GLY B 1 166 ? 8.389   11.176  3.538   1.00 20.34  ? 153 GLY A C   1 
ATOM   3014 O O   . GLY B 1 166 ? 9.008   12.027  2.870   1.00 25.45  ? 153 GLY A O   1 
ATOM   3015 N N   . ARG B 1 167 ? 7.983   11.393  4.810   1.00 20.79  ? 154 ARG A N   1 
ATOM   3016 C CA  . ARG B 1 167 ? 8.319   12.714  5.395   1.00 22.07  ? 154 ARG A CA  1 
ATOM   3017 C C   . ARG B 1 167 ? 9.812   12.795  5.676   1.00 24.29  ? 154 ARG A C   1 
ATOM   3018 O O   . ARG B 1 167 ? 10.365  11.868  6.264   1.00 23.59  ? 154 ARG A O   1 
ATOM   3019 C CB  . ARG B 1 167 ? 7.696   12.915  6.779   1.00 25.37  ? 154 ARG A CB  1 
ATOM   3020 C CG  . ARG B 1 167 ? 6.189   12.933  6.613   1.00 25.14  ? 154 ARG A CG  1 
ATOM   3021 C CD  . ARG B 1 167 ? 5.723   14.039  5.667   1.00 33.03  ? 154 ARG A CD  1 
ATOM   3022 N NE  . ARG B 1 167 ? 5.636   15.291  6.428   1.00 34.93  ? 154 ARG A NE  1 
ATOM   3023 C CZ  . ARG B 1 167 ? 5.652   16.485  5.859   1.00 42.85  ? 154 ARG A CZ  1 
ATOM   3024 N NH1 . ARG B 1 167 ? 6.035   16.613  4.572   1.00 37.44  ? 154 ARG A NH1 1 
ATOM   3025 N NH2 . ARG B 1 167 ? 5.314   17.524  6.631   1.00 39.83  ? 154 ARG A NH2 1 
ATOM   3026 N N   . PRO B 1 168 ? 10.495  13.911  5.280   1.00 23.91  ? 155 PRO A N   1 
ATOM   3027 C CA  . PRO B 1 168 ? 11.920  14.060  5.486   1.00 26.01  ? 155 PRO A CA  1 
ATOM   3028 C C   . PRO B 1 168 ? 12.211  14.609  6.906   1.00 27.06  ? 155 PRO A C   1 
ATOM   3029 O O   . PRO B 1 168 ? 11.272  14.959  7.623   1.00 27.02  ? 155 PRO A O   1 
ATOM   3030 C CB  . PRO B 1 168 ? 12.296  15.137  4.443   1.00 27.63  ? 155 PRO A CB  1 
ATOM   3031 C CG  . PRO B 1 168 ? 11.067  16.019  4.380   1.00 26.46  ? 155 PRO A CG  1 
ATOM   3032 C CD  . PRO B 1 168 ? 9.905   15.041  4.526   1.00 25.39  ? 155 PRO A CD  1 
ATOM   3033 N N   . GLY B 1 169 ? 13.493  14.663  7.247   1.00 29.57  ? 156 GLY A N   1 
ATOM   3034 C CA  . GLY B 1 169 ? 14.037  15.403  8.390   1.00 33.05  ? 156 GLY A CA  1 
ATOM   3035 C C   . GLY B 1 169 ? 14.023  14.590  9.694   1.00 33.17  ? 156 GLY A C   1 
ATOM   3036 O O   . GLY B 1 169 ? 14.155  15.178  10.761  1.00 34.39  ? 156 GLY A O   1 
ATOM   3037 N N   . MET B 1 170 ? 13.787  13.262  9.665   1.00 29.94  ? 157 MET A N   1 
ATOM   3038 C CA  . MET B 1 170 ? 13.897  12.473  10.876  1.00 29.75  ? 157 MET A CA  1 
ATOM   3039 C C   . MET B 1 170 ? 14.149  11.028  10.438  1.00 28.01  ? 157 MET A C   1 
ATOM   3040 O O   . MET B 1 170 ? 13.465  10.120  10.917  1.00 28.82  ? 157 MET A O   1 
ATOM   3041 C CB  . MET B 1 170 ? 12.661  12.589  11.812  1.00 28.92  ? 157 MET A CB  1 
ATOM   3042 C CG  . MET B 1 170 ? 11.306  12.263  11.129  1.00 33.60  ? 157 MET A CG  1 
ATOM   3043 S SD  . MET B 1 170 ? 10.021  13.037  12.124  1.00 43.75  ? 157 MET A SD  1 
ATOM   3044 C CE  . MET B 1 170 ? 8.776   12.809  10.849  1.00 40.81  ? 157 MET A CE  1 
ATOM   3045 N N   . VAL B 1 171 ? 15.186  10.840  9.591   1.00 29.78  ? 158 VAL A N   1 
ATOM   3046 C CA  . VAL B 1 171 ? 15.333  9.563   8.895   1.00 27.48  ? 158 VAL A CA  1 
ATOM   3047 C C   . VAL B 1 171 ? 15.392  8.388   9.888   1.00 28.23  ? 158 VAL A C   1 
ATOM   3048 O O   . VAL B 1 171 ? 14.891  7.322   9.591   1.00 24.17  ? 158 VAL A O   1 
ATOM   3049 C CB  . VAL B 1 171 ? 16.541  9.582   7.943   1.00 28.48  ? 158 VAL A CB  1 
ATOM   3050 C CG1 . VAL B 1 171 ? 17.831  9.847   8.695   1.00 30.53  ? 158 VAL A CG1 1 
ATOM   3051 C CG2 . VAL B 1 171 ? 16.643  8.259   7.178   1.00 26.90  ? 158 VAL A CG2 1 
ATOM   3052 N N   . CYS B 1 172 ? 16.041  8.512   11.063  1.00 27.93  ? 159 CYS A N   1 
ATOM   3053 C CA  . CYS B 1 172 ? 16.075  7.327   11.925  1.00 29.06  ? 159 CYS A CA  1 
ATOM   3054 C C   . CYS B 1 172 ? 14.697  6.928   12.453  1.00 27.73  ? 159 CYS A C   1 
ATOM   3055 O O   . CYS B 1 172 ? 14.398  5.722   12.555  1.00 28.66  ? 159 CYS A O   1 
ATOM   3056 C CB  . CYS B 1 172 ? 17.041  7.538   13.113  1.00 32.89  ? 159 CYS A CB  1 
ATOM   3057 S SG  . CYS B 1 172 ? 18.733  7.957   12.617  1.00 36.69  ? 159 CYS A SG  1 
ATOM   3058 N N   . TYR B 1 173 ? 13.861  7.921   12.831  1.00 25.16  ? 160 TYR A N   1 
ATOM   3059 C CA  . TYR B 1 173 ? 12.550  7.684   13.397  1.00 23.36  ? 160 TYR A CA  1 
ATOM   3060 C C   . TYR B 1 173 ? 11.678  7.045   12.328  1.00 22.97  ? 160 TYR A C   1 
ATOM   3061 O O   . TYR B 1 173 ? 11.055  6.012   12.574  1.00 22.22  ? 160 TYR A O   1 
ATOM   3062 C CB  . TYR B 1 173 ? 12.001  9.033   13.868  1.00 26.84  ? 160 TYR A CB  1 
ATOM   3063 C CG  . TYR B 1 173 ? 10.563  8.864   14.352  1.00 23.96  ? 160 TYR A CG  1 
ATOM   3064 C CD1 . TYR B 1 173 ? 10.310  8.472   15.663  1.00 22.49  ? 160 TYR A CD1 1 
ATOM   3065 C CD2 . TYR B 1 173 ? 9.468   9.024   13.474  1.00 22.30  ? 160 TYR A CD2 1 
ATOM   3066 C CE1 . TYR B 1 173 ? 8.992   8.329   16.092  1.00 24.98  ? 160 TYR A CE1 1 
ATOM   3067 C CE2 . TYR B 1 173 ? 8.160   8.904   13.894  1.00 24.73  ? 160 TYR A CE2 1 
ATOM   3068 C CZ  . TYR B 1 173 ? 7.939   8.549   15.217  1.00 27.61  ? 160 TYR A CZ  1 
ATOM   3069 O OH  . TYR B 1 173 ? 6.665   8.279   15.633  1.00 31.19  ? 160 TYR A OH  1 
ATOM   3070 N N   . THR B 1 174 ? 11.729  7.577   11.079  1.00 22.24  ? 161 THR A N   1 
ATOM   3071 C CA  . THR B 1 174 ? 10.789  7.054   10.080  1.00 22.31  ? 161 THR A CA  1 
ATOM   3072 C C   . THR B 1 174 ? 11.229  5.646   9.621   1.00 21.69  ? 161 THR A C   1 
ATOM   3073 O O   . THR B 1 174 ? 10.398  4.761   9.429   1.00 19.19  ? 161 THR A O   1 
ATOM   3074 C CB  . THR B 1 174 ? 10.730  8.026   8.888   1.00 20.28  ? 161 THR A CB  1 
ATOM   3075 O OG1 . THR B 1 174 ? 12.039  8.394   8.431   1.00 20.15  ? 161 THR A OG1 1 
ATOM   3076 C CG2 . THR B 1 174 ? 9.947   9.269   9.237   1.00 21.65  ? 161 THR A CG2 1 
ATOM   3077 N N   . THR B 1 175 ? 12.543  5.410   9.568   1.00 21.58  ? 162 THR A N   1 
ATOM   3078 C CA  . THR B 1 175 ? 13.070  4.103   9.186   1.00 22.82  ? 162 THR A CA  1 
ATOM   3079 C C   . THR B 1 175 ? 12.716  3.053   10.256  1.00 24.49  ? 162 THR A C   1 
ATOM   3080 O O   . THR B 1 175 ? 12.278  1.933   9.937   1.00 21.31  ? 162 THR A O   1 
ATOM   3081 C CB  . THR B 1 175 ? 14.592  4.170   8.967   1.00 23.70  ? 162 THR A CB  1 
ATOM   3082 O OG1 . THR B 1 175 ? 14.870  5.142   7.950   1.00 24.57  ? 162 THR A OG1 1 
ATOM   3083 C CG2 . THR B 1 175 ? 15.097  2.816   8.512   1.00 26.37  ? 162 THR A CG2 1 
ATOM   3084 N N   . ALA B 1 176 ? 12.861  3.440   11.540  1.00 24.34  ? 163 ALA A N   1 
ATOM   3085 C CA  . ALA B 1 176 ? 12.440  2.586   12.639  1.00 23.30  ? 163 ALA A CA  1 
ATOM   3086 C C   . ALA B 1 176 ? 10.948  2.253   12.529  1.00 23.26  ? 163 ALA A C   1 
ATOM   3087 O O   . ALA B 1 176 ? 10.517  1.105   12.703  1.00 21.71  ? 163 ALA A O   1 
ATOM   3088 C CB  . ALA B 1 176 ? 12.630  3.327   13.998  1.00 22.98  ? 163 ALA A CB  1 
ATOM   3089 N N   . LYS B 1 177 ? 10.099  3.284   12.290  1.00 20.40  ? 164 LYS A N   1 
ATOM   3090 C CA  . LYS B 1 177 ? 8.684   2.986   12.214  1.00 19.30  ? 164 LYS A CA  1 
ATOM   3091 C C   . LYS B 1 177 ? 8.373   2.074   11.023  1.00 18.17  ? 164 LYS A C   1 
ATOM   3092 O O   . LYS B 1 177 ? 7.520   1.223   11.138  1.00 18.80  ? 164 LYS A O   1 
ATOM   3093 C CB  . LYS B 1 177 ? 7.933   4.331   12.221  1.00 19.93  ? 164 LYS A CB  1 
ATOM   3094 C CG  . LYS B 1 177 ? 8.077   5.051   13.628  1.00 19.45  ? 164 LYS A CG  1 
ATOM   3095 C CD  . LYS B 1 177 ? 7.425   4.212   14.750  1.00 20.76  ? 164 LYS A CD  1 
ATOM   3096 C CE  . LYS B 1 177 ? 7.167   4.980   16.073  1.00 24.00  ? 164 LYS A CE  1 
ATOM   3097 N NZ  . LYS B 1 177 ? 6.799   4.018   17.162  1.00 21.17  ? 164 LYS A NZ  1 
ATOM   3098 N N   . ALA B 1 178 ? 9.028   2.249   9.871   1.00 18.20  ? 165 ALA A N   1 
ATOM   3099 C CA  . ALA B 1 178 ? 8.820   1.360   8.723   1.00 20.06  ? 165 ALA A CA  1 
ATOM   3100 C C   . ALA B 1 178 ? 9.255   -0.067  9.080   1.00 20.03  ? 165 ALA A C   1 
ATOM   3101 O O   . ALA B 1 178 ? 8.683   -1.031  8.591   1.00 19.81  ? 165 ALA A O   1 
ATOM   3102 C CB  . ALA B 1 178 ? 9.624   1.843   7.544   1.00 17.79  ? 165 ALA A CB  1 
ATOM   3103 N N   . ALA B 1 179 ? 10.350  -0.191  9.854   1.00 21.15  ? 166 ALA A N   1 
ATOM   3104 C CA  . ALA B 1 179 ? 10.820  -1.504  10.307  1.00 21.77  ? 166 ALA A CA  1 
ATOM   3105 C C   . ALA B 1 179 ? 9.673   -2.205  11.068  1.00 21.30  ? 166 ALA A C   1 
ATOM   3106 O O   . ALA B 1 179 ? 9.445   -3.405  10.915  1.00 20.12  ? 166 ALA A O   1 
ATOM   3107 C CB  . ALA B 1 179 ? 12.092  -1.289  11.189  1.00 22.15  ? 166 ALA A CB  1 
ATOM   3108 N N   . LEU B 1 180 ? 9.031   -1.471  11.980  1.00 20.84  ? 167 LEU A N   1 
ATOM   3109 C CA  . LEU B 1 180 ? 7.967   -2.060  12.820  1.00 22.59  ? 167 LEU A CA  1 
ATOM   3110 C C   . LEU B 1 180 ? 6.762   -2.508  11.969  1.00 23.16  ? 167 LEU A C   1 
ATOM   3111 O O   . LEU B 1 180 ? 6.077   -3.499  12.258  1.00 21.30  ? 167 LEU A O   1 
ATOM   3112 C CB  . LEU B 1 180 ? 7.480   -0.953  13.781  1.00 25.05  ? 167 LEU A CB  1 
ATOM   3113 C CG  . LEU B 1 180 ? 8.352   -0.753  15.021  1.00 26.54  ? 167 LEU A CG  1 
ATOM   3114 C CD1 . LEU B 1 180 ? 7.683   0.376   15.820  1.00 28.77  ? 167 LEU A CD1 1 
ATOM   3115 C CD2 . LEU B 1 180 ? 8.274   -2.097  15.823  1.00 28.00  ? 167 LEU A CD2 1 
ATOM   3116 N N   . ASN B 1 181 ? 6.491   -1.808  10.842  1.00 21.02  ? 168 ASN A N   1 
ATOM   3117 C CA  . ASN B 1 181 ? 5.472   -2.200  9.898   1.00 20.28  ? 168 ASN A CA  1 
ATOM   3118 C C   . ASN B 1 181 ? 5.725   -3.636  9.444   1.00 19.44  ? 168 ASN A C   1 
ATOM   3119 O O   . ASN B 1 181 ? 4.770   -4.427  9.450   1.00 19.78  ? 168 ASN A O   1 
ATOM   3120 C CB  . ASN B 1 181 ? 5.509   -1.306  8.667   1.00 24.24  ? 168 ASN A CB  1 
ATOM   3121 C CG  . ASN B 1 181 ? 4.463   -1.690  7.671   1.00 23.79  ? 168 ASN A CG  1 
ATOM   3122 O OD1 . ASN B 1 181 ? 3.313   -1.562  8.075   1.00 24.57  ? 168 ASN A OD1 1 
ATOM   3123 N ND2 . ASN B 1 181 ? 4.802   -1.933  6.409   1.00 21.69  ? 168 ASN A ND2 1 
ATOM   3124 N N   . GLY B 1 182 ? 6.991   -3.945  9.036   1.00 17.85  ? 169 GLY A N   1 
ATOM   3125 C CA  . GLY B 1 182 ? 7.419   -5.299  8.627   1.00 17.03  ? 169 GLY A CA  1 
ATOM   3126 C C   . GLY B 1 182 ? 7.325   -6.290  9.794   1.00 17.65  ? 169 GLY A C   1 
ATOM   3127 O O   . GLY B 1 182 ? 6.785   -7.399  9.658   1.00 21.03  ? 169 GLY A O   1 
ATOM   3128 N N   . MET B 1 183 ? 7.833   -5.871  10.953  1.00 17.63  ? 170 MET A N   1 
ATOM   3129 C CA  . MET B 1 183 ? 7.956   -6.722  12.101  1.00 20.20  ? 170 MET A CA  1 
ATOM   3130 C C   . MET B 1 183 ? 6.576   -7.200  12.556  1.00 18.30  ? 170 MET A C   1 
ATOM   3131 O O   . MET B 1 183 ? 6.431   -8.369  12.935  1.00 22.39  ? 170 MET A O   1 
ATOM   3132 C CB  . MET B 1 183 ? 8.819   -6.089  13.224  1.00 21.35  ? 170 MET A CB  1 
ATOM   3133 C CG  . MET B 1 183 ? 9.158   -7.103  14.269  1.00 24.35  ? 170 MET A CG  1 
ATOM   3134 S SD  . MET B 1 183 ? 10.008  -6.340  15.692  1.00 31.91  ? 170 MET A SD  1 
ATOM   3135 C CE  . MET B 1 183 ? 8.810   -5.458  16.620  1.00 27.84  ? 170 MET A CE  1 
ATOM   3136 N N   . THR B 1 184 ? 5.561   -6.323  12.501  1.00 17.29  ? 171 THR A N   1 
ATOM   3137 C CA  . THR B 1 184 ? 4.184   -6.769  12.795  1.00 18.10  ? 171 THR A CA  1 
ATOM   3138 C C   . THR B 1 184 ? 3.799   -7.989  11.936  1.00 18.08  ? 171 THR A C   1 
ATOM   3139 O O   . THR B 1 184 ? 3.206   -8.925  12.464  1.00 19.04  ? 171 THR A O   1 
ATOM   3140 C CB  . THR B 1 184 ? 3.212   -5.629  12.441  1.00 18.20  ? 171 THR A CB  1 
ATOM   3141 O OG1 . THR B 1 184 ? 3.469   -4.625  13.430  1.00 22.60  ? 171 THR A OG1 1 
ATOM   3142 C CG2 . THR B 1 184 ? 1.732   -6.017  12.553  1.00 18.12  ? 171 THR A CG2 1 
ATOM   3143 N N   . ARG B 1 185 ? 4.008   -7.903  10.612  1.00 15.44  ? 172 ARG A N   1 
ATOM   3144 C CA  . ARG B 1 185 ? 3.530   -8.907  9.641   1.00 17.14  ? 172 ARG A CA  1 
ATOM   3145 C C   . ARG B 1 185 ? 4.233   -10.248 9.924   1.00 18.38  ? 172 ARG A C   1 
ATOM   3146 O O   . ARG B 1 185 ? 3.571   -11.308 9.950   1.00 20.41  ? 172 ARG A O   1 
ATOM   3147 C CB  . ARG B 1 185 ? 3.739   -8.566  8.166   1.00 16.58  ? 172 ARG A CB  1 
ATOM   3148 C CG  . ARG B 1 185 ? 3.013   -7.215  8.003   1.00 16.93  ? 172 ARG A CG  1 
ATOM   3149 C CD  . ARG B 1 185 ? 3.289   -6.591  6.633   1.00 21.86  ? 172 ARG A CD  1 
ATOM   3150 N NE  . ARG B 1 185 ? 2.794   -7.298  5.475   1.00 25.43  ? 172 ARG A NE  1 
ATOM   3151 C CZ  . ARG B 1 185 ? 1.656   -7.026  4.835   1.00 28.74  ? 172 ARG A CZ  1 
ATOM   3152 N NH1 . ARG B 1 185 ? 0.748   -6.210  5.375   1.00 26.17  ? 172 ARG A NH1 1 
ATOM   3153 N NH2 . ARG B 1 185 ? 1.376   -7.699  3.725   1.00 21.11  ? 172 ARG A NH2 1 
ATOM   3154 N N   . THR B 1 186 ? 5.568   -10.215 10.151  1.00 18.58  ? 173 THR A N   1 
ATOM   3155 C CA  . THR B 1 186 ? 6.315   -11.493 10.303  1.00 18.81  ? 173 THR A CA  1 
ATOM   3156 C C   . THR B 1 186 ? 6.114   -12.092 11.695  1.00 20.36  ? 173 THR A C   1 
ATOM   3157 O O   . THR B 1 186 ? 5.995   -13.328 11.843  1.00 23.67  ? 173 THR A O   1 
ATOM   3158 C CB  . THR B 1 186 ? 7.809   -11.374 9.978   1.00 20.57  ? 173 THR A CB  1 
ATOM   3159 O OG1 . THR B 1 186 ? 8.459   -10.612 11.015  1.00 21.79  ? 173 THR A OG1 1 
ATOM   3160 C CG2 . THR B 1 186 ? 8.015   -10.862 8.545   1.00 19.39  ? 173 THR A CG2 1 
ATOM   3161 N N   . LEU B 1 187 ? 5.967   -11.230 12.702  1.00 19.43  ? 174 LEU A N   1 
ATOM   3162 C CA  . LEU B 1 187 ? 5.786   -11.790 14.030  1.00 23.52  ? 174 LEU A CA  1 
ATOM   3163 C C   . LEU B 1 187 ? 4.365   -12.335 14.088  1.00 21.05  ? 174 LEU A C   1 
ATOM   3164 O O   . LEU B 1 187 ? 4.158   -13.324 14.841  1.00 20.73  ? 174 LEU A O   1 
ATOM   3165 C CB  . LEU B 1 187 ? 6.030   -10.832 15.194  1.00 22.25  ? 174 LEU A CB  1 
ATOM   3166 C CG  . LEU B 1 187 ? 7.511   -10.547 15.453  1.00 25.71  ? 174 LEU A CG  1 
ATOM   3167 C CD1 . LEU B 1 187 ? 7.711   -9.734  16.704  1.00 30.17  ? 174 LEU A CD1 1 
ATOM   3168 C CD2 . LEU B 1 187 ? 8.308   -11.826 15.485  1.00 28.04  ? 174 LEU A CD2 1 
ATOM   3169 N N   . ALA B 1 188 ? 3.418   -11.675 13.389  1.00 18.26  ? 175 ALA A N   1 
ATOM   3170 C CA  . ALA B 1 188 ? 2.059   -12.202 13.374  1.00 20.85  ? 175 ALA A CA  1 
ATOM   3171 C C   . ALA B 1 188 ? 2.053   -13.656 12.921  1.00 22.46  ? 175 ALA A C   1 
ATOM   3172 O O   . ALA B 1 188 ? 1.332   -14.491 13.487  1.00 23.87  ? 175 ALA A O   1 
ATOM   3173 C CB  . ALA B 1 188 ? 1.177   -11.221 12.560  1.00 19.03  ? 175 ALA A CB  1 
ATOM   3174 N N   . ARG B 1 189 ? 2.827   -14.006 11.882  1.00 21.70  ? 176 ARG A N   1 
ATOM   3175 C CA  . ARG B 1 189 ? 2.876   -15.400 11.428  1.00 23.72  ? 176 ARG A CA  1 
ATOM   3176 C C   . ARG B 1 189 ? 3.684   -16.252 12.405  1.00 24.22  ? 176 ARG A C   1 
ATOM   3177 O O   . ARG B 1 189 ? 3.316   -17.416 12.686  1.00 24.83  ? 176 ARG A O   1 
ATOM   3178 C CB  . ARG B 1 189 ? 3.466   -15.378 9.997   1.00 26.75  ? 176 ARG A CB  1 
ATOM   3179 C CG  . ARG B 1 189 ? 3.785   -16.758 9.433   1.00 26.26  ? 176 ARG A CG  1 
ATOM   3180 C CD  . ARG B 1 189 ? 2.568   -17.590 9.133   1.00 29.10  ? 176 ARG A CD  1 
ATOM   3181 N NE  . ARG B 1 189 ? 1.748   -17.023 8.043   1.00 27.21  ? 176 ARG A NE  1 
ATOM   3182 C CZ  . ARG B 1 189 ? 0.566   -17.460 7.603   1.00 26.02  ? 176 ARG A CZ  1 
ATOM   3183 N NH1 . ARG B 1 189 ? -0.121  -16.768 6.719   1.00 26.11  ? 176 ARG A NH1 1 
ATOM   3184 N NH2 . ARG B 1 189 ? 0.021   -18.534 8.127   1.00 27.56  ? 176 ARG A NH2 1 
ATOM   3185 N N   . GLU B 1 190 ? 4.799   -15.687 12.914  1.00 24.59  ? 177 GLU A N   1 
ATOM   3186 C CA  . GLU B 1 190 ? 5.666   -16.550 13.717  1.00 29.19  ? 177 GLU A CA  1 
ATOM   3187 C C   . GLU B 1 190 ? 4.996   -16.896 15.040  1.00 28.27  ? 177 GLU A C   1 
ATOM   3188 O O   . GLU B 1 190 ? 5.187   -18.014 15.478  1.00 29.80  ? 177 GLU A O   1 
ATOM   3189 C CB  . GLU B 1 190 ? 7.085   -15.988 13.870  1.00 32.42  ? 177 GLU A CB  1 
ATOM   3190 C CG  . GLU B 1 190 ? 8.141   -16.941 14.461  1.00 34.25  ? 177 GLU A CG  1 
ATOM   3191 C CD  . GLU B 1 190 ? 9.542   -16.378 14.249  1.00 40.76  ? 177 GLU A CD  1 
ATOM   3192 O OE1 . GLU B 1 190 ? 9.687   -15.399 13.385  1.00 33.44  ? 177 GLU A OE1 1 
ATOM   3193 O OE2 . GLU B 1 190 ? 10.506  -16.975 14.847  1.00 40.58  ? 177 GLU A OE2 1 
ATOM   3194 N N   . LEU B 1 191 ? 4.123   -16.003 15.593  1.00 27.08  ? 178 LEU A N   1 
ATOM   3195 C CA  . LEU B 1 191 ? 3.568   -16.289 16.930  1.00 27.50  ? 178 LEU A CA  1 
ATOM   3196 C C   . LEU B 1 191 ? 2.100   -16.681 16.858  1.00 27.34  ? 178 LEU A C   1 
ATOM   3197 O O   . LEU B 1 191 ? 1.542   -17.024 17.890  1.00 27.89  ? 178 LEU A O   1 
ATOM   3198 C CB  . LEU B 1 191 ? 3.750   -15.026 17.772  1.00 28.84  ? 178 LEU A CB  1 
ATOM   3199 C CG  . LEU B 1 191 ? 5.204   -14.731 18.159  1.00 28.67  ? 178 LEU A CG  1 
ATOM   3200 C CD1 . LEU B 1 191 ? 5.253   -13.307 18.775  1.00 31.04  ? 178 LEU A CD1 1 
ATOM   3201 C CD2 . LEU B 1 191 ? 5.851   -15.778 19.010  1.00 29.39  ? 178 LEU A CD2 1 
ATOM   3202 N N   . GLY B 1 192 ? 1.433   -16.489 15.707  1.00 25.41  ? 179 GLY A N   1 
ATOM   3203 C CA  . GLY B 1 192 ? -0.009  -16.648 15.591  1.00 25.08  ? 179 GLY A CA  1 
ATOM   3204 C C   . GLY B 1 192 ? -0.454  -18.047 16.022  1.00 27.15  ? 179 GLY A C   1 
ATOM   3205 O O   . GLY B 1 192 ? -1.529  -18.202 16.578  1.00 25.68  ? 179 GLY A O   1 
ATOM   3206 N N   . GLY B 1 193 ? 0.358   -19.080 15.682  1.00 28.34  ? 180 GLY A N   1 
ATOM   3207 C CA  . GLY B 1 193 ? 0.029   -20.432 16.056  1.00 33.44  ? 180 GLY A CA  1 
ATOM   3208 C C   . GLY B 1 193 ? 0.020   -20.600 17.570  1.00 34.15  ? 180 GLY A C   1 
ATOM   3209 O O   . GLY B 1 193 ? -0.574  -21.558 18.109  1.00 35.71  ? 180 GLY A O   1 
ATOM   3210 N N   . GLN B 1 194 ? 0.681   -19.691 18.271  1.00 32.24  ? 181 GLN A N   1 
ATOM   3211 C CA  . GLN B 1 194 ? 0.593   -19.743 19.730  1.00 34.14  ? 181 GLN A CA  1 
ATOM   3212 C C   . GLN B 1 194 ? -0.633  -18.989 20.278  1.00 30.82  ? 181 GLN A C   1 
ATOM   3213 O O   . GLN B 1 194 ? -0.758  -18.869 21.490  1.00 31.83  ? 181 GLN A O   1 
ATOM   3214 C CB  . GLN B 1 194 ? 1.868   -19.245 20.411  1.00 37.06  ? 181 GLN A CB  1 
ATOM   3215 C CG  . GLN B 1 194 ? 3.111   -20.119 20.196  1.00 47.45  ? 181 GLN A CG  1 
ATOM   3216 C CD  . GLN B 1 194 ? 4.410   -19.328 20.314  1.00 57.38  ? 181 GLN A CD  1 
ATOM   3217 O OE1 . GLN B 1 194 ? 4.675   -18.562 21.265  1.00 47.94  ? 181 GLN A OE1 1 
ATOM   3218 N NE2 . GLN B 1 194 ? 5.242   -19.466 19.294  1.00 57.54  ? 181 GLN A NE2 1 
ATOM   3219 N N   . GLY B 1 195 ? -1.506  -18.466 19.426  1.00 28.84  ? 182 GLY A N   1 
ATOM   3220 C CA  . GLY B 1 195 ? -2.635  -17.636 19.842  1.00 25.58  ? 182 GLY A CA  1 
ATOM   3221 C C   . GLY B 1 195 ? -2.333  -16.156 20.058  1.00 27.08  ? 182 GLY A C   1 
ATOM   3222 O O   . GLY B 1 195 ? -3.203  -15.476 20.588  1.00 22.28  ? 182 GLY A O   1 
ATOM   3223 N N   . ILE B 1 196 ? -1.184  -15.636 19.577  1.00 22.29  ? 183 ILE A N   1 
ATOM   3224 C CA  . ILE B 1 196 ? -0.859  -14.236 19.784  1.00 23.35  ? 183 ILE A CA  1 
ATOM   3225 C C   . ILE B 1 196 ? -1.164  -13.507 18.478  1.00 23.92  ? 183 ILE A C   1 
ATOM   3226 O O   . ILE B 1 196 ? -0.687  -13.897 17.440  1.00 25.14  ? 183 ILE A O   1 
ATOM   3227 C CB  . ILE B 1 196 ? 0.642   -14.094 20.115  1.00 24.59  ? 183 ILE A CB  1 
ATOM   3228 C CG1 . ILE B 1 196 ? 1.004   -14.923 21.368  1.00 26.07  ? 183 ILE A CG1 1 
ATOM   3229 C CG2 . ILE B 1 196 ? 1.026   -12.627 20.315  1.00 25.32  ? 183 ILE A CG2 1 
ATOM   3230 C CD1 . ILE B 1 196 ? 2.500   -15.089 21.575  1.00 26.61  ? 183 ILE A CD1 1 
ATOM   3231 N N   . ARG B 1 197 ? -1.918  -12.402 18.578  1.00 22.95  ? 184 ARG A N   1 
ATOM   3232 C CA  . ARG B 1 197 ? -2.210  -11.527 17.457  1.00 21.85  ? 184 ARG A CA  1 
ATOM   3233 C C   . ARG B 1 197 ? -1.344  -10.284 17.589  1.00 18.99  ? 184 ARG A C   1 
ATOM   3234 O O   . ARG B 1 197 ? -1.036  -9.885  18.699  1.00 19.51  ? 184 ARG A O   1 
ATOM   3235 C CB  . ARG B 1 197 ? -3.724  -11.266 17.371  1.00 22.40  ? 184 ARG A CB  1 
ATOM   3236 C CG  . ARG B 1 197 ? -4.368  -10.488 18.484  1.00 25.84  ? 184 ARG A CG  1 
ATOM   3237 C CD  . ARG B 1 197 ? -5.901  -10.686 18.320  1.00 31.47  ? 184 ARG A CD  1 
ATOM   3238 N NE  . ARG B 1 197 ? -6.414  -9.417  18.875  1.00 33.91  ? 184 ARG A NE  1 
ATOM   3239 C CZ  . ARG B 1 197 ? -6.858  -9.473  20.134  1.00 36.43  ? 184 ARG A CZ  1 
ATOM   3240 N NH1 . ARG B 1 197 ? -7.275  -8.374  20.749  1.00 38.64  ? 184 ARG A NH1 1 
ATOM   3241 N NH2 . ARG B 1 197 ? -6.784  -10.642 20.795  1.00 37.67  ? 184 ARG A NH2 1 
ATOM   3242 N N   . ILE B 1 198 ? -0.881  -9.767  16.452  1.00 17.95  ? 185 ILE A N   1 
ATOM   3243 C CA  . ILE B 1 198 ? 0.041   -8.645  16.467  1.00 19.46  ? 185 ILE A CA  1 
ATOM   3244 C C   . ILE B 1 198 ? -0.438  -7.681  15.398  1.00 16.21  ? 185 ILE A C   1 
ATOM   3245 O O   . ILE B 1 198 ? -0.557  -8.126  14.243  1.00 18.69  ? 185 ILE A O   1 
ATOM   3246 C CB  . ILE B 1 198 ? 1.500   -9.102  16.244  1.00 19.34  ? 185 ILE A CB  1 
ATOM   3247 C CG1 . ILE B 1 198 ? 1.859   -10.201 17.283  1.00 22.24  ? 185 ILE A CG1 1 
ATOM   3248 C CG2 . ILE B 1 198 ? 2.391   -7.847  16.378  1.00 22.93  ? 185 ILE A CG2 1 
ATOM   3249 C CD1 . ILE B 1 198 ? 3.294   -10.700 17.293  1.00 28.47  ? 185 ILE A CD1 1 
ATOM   3250 N N   . ASN B 1 199 ? -0.636  -6.395  15.741  1.00 15.32  ? 186 ASN A N   1 
ATOM   3251 C CA  . ASN B 1 199 ? -1.121  -5.421  14.795  1.00 16.54  ? 186 ASN A CA  1 
ATOM   3252 C C   . ASN B 1 199 ? -0.349  -4.137  15.013  1.00 15.67  ? 186 ASN A C   1 
ATOM   3253 O O   . ASN B 1 199 ? 0.214   -3.967  16.074  1.00 17.66  ? 186 ASN A O   1 
ATOM   3254 C CB  . ASN B 1 199 ? -2.635  -5.152  14.916  1.00 16.28  ? 186 ASN A CB  1 
ATOM   3255 C CG  . ASN B 1 199 ? -3.473  -6.346  14.536  1.00 15.35  ? 186 ASN A CG  1 
ATOM   3256 O OD1 . ASN B 1 199 ? -3.530  -6.768  13.392  1.00 14.55  ? 186 ASN A OD1 1 
ATOM   3257 N ND2 . ASN B 1 199 ? -4.023  -6.974  15.561  1.00 16.65  ? 186 ASN A ND2 1 
ATOM   3258 N N   . SER B 1 200 ? -0.389  -3.224  14.039  1.00 16.00  ? 187 SER A N   1 
ATOM   3259 C CA  A SER B 1 200 ? 0.200   -1.929  14.296  0.50 17.42  ? 187 SER A CA  1 
ATOM   3260 C CA  B SER B 1 200 ? 0.208   -1.922  14.237  0.50 17.73  ? 187 SER A CA  1 
ATOM   3261 C C   . SER B 1 200 ? -0.896  -0.865  14.361  1.00 15.62  ? 187 SER A C   1 
ATOM   3262 O O   . SER B 1 200 ? -1.796  -0.876  13.566  1.00 16.53  ? 187 SER A O   1 
ATOM   3263 C CB  A SER B 1 200 ? 1.160   -1.561  13.200  0.50 16.90  ? 187 SER A CB  1 
ATOM   3264 C CB  B SER B 1 200 ? 1.066   -1.562  13.041  0.50 17.21  ? 187 SER A CB  1 
ATOM   3265 O OG  A SER B 1 200 ? 1.826   -0.354  13.540  0.50 18.70  ? 187 SER A OG  1 
ATOM   3266 O OG  B SER B 1 200 ? 2.260   -2.328  12.923  0.50 19.91  ? 187 SER A OG  1 
ATOM   3267 N N   . LEU B 1 201 ? -0.820  0.033   15.367  1.00 15.55  ? 188 LEU A N   1 
ATOM   3268 C CA  . LEU B 1 201 ? -1.714  1.183   15.519  1.00 14.64  ? 188 LEU A CA  1 
ATOM   3269 C C   . LEU B 1 201 ? -0.915  2.372   14.960  1.00 15.24  ? 188 LEU A C   1 
ATOM   3270 O O   . LEU B 1 201 ? 0.212   2.613   15.401  1.00 16.62  ? 188 LEU A O   1 
ATOM   3271 C CB  . LEU B 1 201 ? -1.961  1.276   17.022  1.00 12.97  ? 188 LEU A CB  1 
ATOM   3272 C CG  . LEU B 1 201 ? -3.028  2.320   17.461  1.00 15.55  ? 188 LEU A CG  1 
ATOM   3273 C CD1 . LEU B 1 201 ? -3.364  2.287   18.998  1.00 14.54  ? 188 LEU A CD1 1 
ATOM   3274 C CD2 . LEU B 1 201 ? -2.682  3.779   17.021  1.00 17.68  ? 188 LEU A CD2 1 
ATOM   3275 N N   . VAL B 1 202 ? -1.392  3.023   13.886  1.00 13.16  ? 189 VAL A N   1 
ATOM   3276 C CA  . VAL B 1 202 ? -0.596  3.972   13.131  1.00 13.77  ? 189 VAL A CA  1 
ATOM   3277 C C   . VAL B 1 202 ? -1.290  5.329   13.202  1.00 14.22  ? 189 VAL A C   1 
ATOM   3278 O O   . VAL B 1 202 ? -2.268  5.624   12.487  1.00 15.29  ? 189 VAL A O   1 
ATOM   3279 C CB  . VAL B 1 202 ? -0.536  3.525   11.663  1.00 13.85  ? 189 VAL A CB  1 
ATOM   3280 C CG1 . VAL B 1 202 ? 0.292   4.534   10.867  1.00 14.90  ? 189 VAL A CG1 1 
ATOM   3281 C CG2 . VAL B 1 202 ? -0.075  2.068   11.528  1.00 13.17  ? 189 VAL A CG2 1 
ATOM   3282 N N   . PRO B 1 203 ? -0.878  6.186   14.136  1.00 17.80  ? 190 PRO A N   1 
ATOM   3283 C CA  . PRO B 1 203 ? -1.476  7.537   14.243  1.00 18.69  ? 190 PRO A CA  1 
ATOM   3284 C C   . PRO B 1 203 ? -1.038  8.501   13.162  1.00 19.51  ? 190 PRO A C   1 
ATOM   3285 O O   . PRO B 1 203 ? 0.060   8.402   12.617  1.00 21.65  ? 190 PRO A O   1 
ATOM   3286 C CB  . PRO B 1 203 ? -1.084  7.981   15.639  1.00 19.48  ? 190 PRO A CB  1 
ATOM   3287 C CG  . PRO B 1 203 ? -0.511  6.782   16.284  1.00 20.15  ? 190 PRO A CG  1 
ATOM   3288 C CD  . PRO B 1 203 ? 0.088   5.878   15.181  1.00 17.29  ? 190 PRO A CD  1 
ATOM   3289 N N   . GLY B 1 204 ? -1.830  9.554   12.974  1.00 19.12  ? 191 GLY A N   1 
ATOM   3290 C CA  . GLY B 1 204 ? -1.487  10.703  12.148  1.00 18.80  ? 191 GLY A CA  1 
ATOM   3291 C C   . GLY B 1 204 ? -0.900  11.766  13.048  1.00 21.70  ? 191 GLY A C   1 
ATOM   3292 O O   . GLY B 1 204 ? -0.147  11.431  13.944  1.00 20.53  ? 191 GLY A O   1 
ATOM   3293 N N   . ALA B 1 205 ? -1.278  13.036  12.837  1.00 19.75  ? 192 ALA A N   1 
ATOM   3294 C CA  . ALA B 1 205 ? -0.610  14.072  13.601  1.00 19.65  ? 192 ALA A CA  1 
ATOM   3295 C C   . ALA B 1 205 ? -1.410  14.351  14.864  1.00 23.13  ? 192 ALA A C   1 
ATOM   3296 O O   . ALA B 1 205 ? -2.471  15.009  14.855  1.00 25.26  ? 192 ALA A O   1 
ATOM   3297 C CB  . ALA B 1 205 ? -0.535  15.330  12.715  1.00 21.37  ? 192 ALA A CB  1 
ATOM   3298 N N   . ILE B 1 206 ? -0.939  13.776  15.979  1.00 24.56  ? 193 ILE A N   1 
ATOM   3299 C CA  . ILE B 1 206 ? -1.648  13.817  17.245  1.00 19.98  ? 193 ILE A CA  1 
ATOM   3300 C C   . ILE B 1 206 ? -1.252  15.060  18.065  1.00 26.42  ? 193 ILE A C   1 
ATOM   3301 O O   . ILE B 1 206 ? -0.044  15.307  18.264  1.00 25.42  ? 193 ILE A O   1 
ATOM   3302 C CB  . ILE B 1 206 ? -1.394  12.522  18.008  1.00 21.65  ? 193 ILE A CB  1 
ATOM   3303 C CG1 . ILE B 1 206 ? -1.632  11.259  17.109  1.00 19.74  ? 193 ILE A CG1 1 
ATOM   3304 C CG2 . ILE B 1 206 ? -2.171  12.474  19.324  1.00 20.72  ? 193 ILE A CG2 1 
ATOM   3305 C CD1 . ILE B 1 206 ? -3.040  11.150  16.506  1.00 16.92  ? 193 ILE A CD1 1 
ATOM   3306 N N   . ARG B 1 207 ? -2.241  15.889  18.483  1.00 22.96  ? 194 ARG A N   1 
ATOM   3307 C CA  . ARG B 1 207 ? -1.927  17.060  19.313  1.00 25.48  ? 194 ARG A CA  1 
ATOM   3308 C C   . ARG B 1 207 ? -1.560  16.547  20.692  1.00 26.54  ? 194 ARG A C   1 
ATOM   3309 O O   . ARG B 1 207 ? -2.232  15.650  21.206  1.00 28.38  ? 194 ARG A O   1 
ATOM   3310 C CB  . ARG B 1 207 ? -3.040  18.112  19.377  1.00 27.92  ? 194 ARG A CB  1 
ATOM   3311 C CG  . ARG B 1 207 ? -2.857  19.301  20.342  1.00 30.85  ? 194 ARG A CG  1 
ATOM   3312 C CD  . ARG B 1 207 ? -3.917  20.398  20.153  1.00 42.58  ? 194 ARG A CD  1 
ATOM   3313 N NE  . ARG B 1 207 ? -5.260  19.889  20.497  1.00 57.49  ? 194 ARG A NE  1 
ATOM   3314 C CZ  . ARG B 1 207 ? -6.516  20.287  20.096  1.00 63.01  ? 194 ARG A CZ  1 
ATOM   3315 N NH1 . ARG B 1 207 ? -6.760  21.433  19.441  1.00 50.37  ? 194 ARG A NH1 1 
ATOM   3316 N NH2 . ARG B 1 207 ? -7.532  19.482  20.366  1.00 52.57  ? 194 ARG A NH2 1 
ATOM   3317 N N   . THR B 1 208 ? -0.374  16.990  21.206  1.00 32.56  ? 195 THR A N   1 
ATOM   3318 C CA  . THR B 1 208 ? 0.067   16.589  22.560  1.00 33.96  ? 195 THR A CA  1 
ATOM   3319 C C   . THR B 1 208 ? 0.652   17.838  23.220  1.00 40.10  ? 195 THR A C   1 
ATOM   3320 O O   . THR B 1 208 ? 1.077   18.739  22.477  1.00 35.89  ? 195 THR A O   1 
ATOM   3321 C CB  . THR B 1 208 ? 1.078   15.431  22.638  1.00 36.47  ? 195 THR A CB  1 
ATOM   3322 O OG1 . THR B 1 208 ? 2.291   15.919  22.047  1.00 38.84  ? 195 THR A OG1 1 
ATOM   3323 C CG2 . THR B 1 208 ? 0.657   14.190  21.855  1.00 34.43  ? 195 THR A CG2 1 
ATOM   3324 N N   . GLU B 1 209 ? 0.656   17.853  24.575  1.00 45.75  ? 196 GLU A N   1 
ATOM   3325 C CA  . GLU B 1 209 ? 1.260   18.899  25.396  1.00 50.83  ? 196 GLU A CA  1 
ATOM   3326 C C   . GLU B 1 209 ? 2.729   19.145  24.999  1.00 51.99  ? 196 GLU A C   1 
ATOM   3327 O O   . GLU B 1 209 ? 3.176   20.290  25.042  1.00 61.50  ? 196 GLU A O   1 
ATOM   3328 C CB  . GLU B 1 209 ? 0.876   18.619  26.860  1.00 43.12  ? 196 GLU A CB  1 
ATOM   3329 N N   . ARG B 1 210 ? 3.468   18.079  24.616  1.00 55.78  ? 197 ARG A N   1 
ATOM   3330 C CA  . ARG B 1 210 ? 4.873   18.097  24.188  1.00 58.59  ? 197 ARG A CA  1 
ATOM   3331 C C   . ARG B 1 210 ? 5.068   18.666  22.771  1.00 64.40  ? 197 ARG A C   1 
ATOM   3332 O O   . ARG B 1 210 ? 5.991   19.459  22.579  1.00 76.70  ? 197 ARG A O   1 
ATOM   3333 C CB  . ARG B 1 210 ? 5.582   16.730  24.239  1.00 49.52  ? 197 ARG A CB  1 
ATOM   3334 N N   . GLN B 1 211 ? 4.243   18.257  21.773  1.00 62.71  ? 198 GLN A N   1 
ATOM   3335 C CA  . GLN B 1 211 ? 4.225   18.853  20.427  1.00 55.34  ? 198 GLN A CA  1 
ATOM   3336 C C   . GLN B 1 211 ? 3.893   20.355  20.529  1.00 64.24  ? 198 GLN A C   1 
ATOM   3337 O O   . GLN B 1 211 ? 4.413   21.173  19.767  1.00 74.25  ? 198 GLN A O   1 
ATOM   3338 C CB  . GLN B 1 211 ? 3.461   18.047  19.366  1.00 59.98  ? 198 GLN A CB  1 
ATOM   3339 N N   . ASP B 1 212 ? 3.107   20.744  21.548  1.00 58.16  ? 199 ASP A N   1 
ATOM   3340 C CA  . ASP B 1 212 ? 2.677   22.123  21.736  1.00 61.56  ? 199 ASP A CA  1 
ATOM   3341 C C   . ASP B 1 212 ? 3.693   22.926  22.572  1.00 70.21  ? 199 ASP A C   1 
ATOM   3342 O O   . ASP B 1 212 ? 3.804   24.148  22.412  1.00 64.18  ? 199 ASP A O   1 
ATOM   3343 C CB  . ASP B 1 212 ? 1.266   22.209  22.327  1.00 59.04  ? 199 ASP A CB  1 
ATOM   3344 C CG  . ASP B 1 212 ? 0.037   21.832  21.498  1.00 50.91  ? 199 ASP A CG  1 
ATOM   3345 O OD1 . ASP B 1 212 ? 0.171   21.259  20.394  1.00 51.98  ? 199 ASP A OD1 1 
ATOM   3346 O OD2 . ASP B 1 212 ? -1.081  22.143  21.964  1.00 45.74  ? 199 ASP A OD2 1 
ATOM   3347 N N   . ALA B 1 213 ? 4.384   22.269  23.518  1.00 70.28  ? 200 ALA A N   1 
ATOM   3348 C CA  . ALA B 1 213 ? 5.349   22.944  24.382  1.00 72.15  ? 200 ALA A CA  1 
ATOM   3349 C C   . ALA B 1 213 ? 6.461   23.598  23.558  1.00 70.37  ? 200 ALA A C   1 
ATOM   3350 O O   . ALA B 1 213 ? 7.076   24.563  24.036  1.00 66.45  ? 200 ALA A O   1 
ATOM   3351 C CB  . ALA B 1 213 ? 5.918   21.972  25.389  1.00 63.56  ? 200 ALA A CB  1 
ATOM   3352 N N   . MET B 1 214 ? 6.655   23.098  22.314  1.00 72.80  ? 201 MET A N   1 
ATOM   3353 C CA  . MET B 1 214 ? 7.761   23.426  21.414  1.00 83.36  ? 201 MET A CA  1 
ATOM   3354 C C   . MET B 1 214 ? 7.670   24.854  20.840  1.00 95.41  ? 201 MET A C   1 
ATOM   3355 O O   . MET B 1 214 ? 8.598   25.296  20.154  1.00 91.80  ? 201 MET A O   1 
ATOM   3356 C CB  . MET B 1 214 ? 7.830   22.427  20.245  1.00 84.06  ? 201 MET A CB  1 
ATOM   3357 C CG  . MET B 1 214 ? 8.304   21.009  20.590  1.00 84.35  ? 201 MET A CG  1 
ATOM   3358 S SD  . MET B 1 214 ? 9.125   20.157  19.214  1.00 99.56  ? 201 MET A SD  1 
ATOM   3359 C CE  . MET B 1 214 ? 8.030   19.251  18.096  1.00 73.02  ? 201 MET A CE  1 
ATOM   3360 N N   . TRP B 1 215 ? 6.547   25.561  21.110  1.00 94.85  ? 202 TRP A N   1 
ATOM   3361 C CA  . TRP B 1 215 ? 6.173   26.833  20.488  1.00 82.01  ? 202 TRP A CA  1 
ATOM   3362 C C   . TRP B 1 215 ? 5.640   27.840  21.516  1.00 77.61  ? 202 TRP A C   1 
ATOM   3363 O O   . TRP B 1 215 ? 4.913   28.764  21.136  1.00 69.82  ? 202 TRP A O   1 
ATOM   3364 C CB  . TRP B 1 215 ? 5.043   26.634  19.462  1.00 75.94  ? 202 TRP A CB  1 
ATOM   3365 C CG  . TRP B 1 215 ? 5.210   25.673  18.315  1.00 68.88  ? 202 TRP A CG  1 
ATOM   3366 C CD1 . TRP B 1 215 ? 4.975   24.326  18.337  1.00 70.07  ? 202 TRP A CD1 1 
ATOM   3367 C CD2 . TRP B 1 215 ? 5.505   26.013  16.942  1.00 68.23  ? 202 TRP A CD2 1 
ATOM   3368 N NE1 . TRP B 1 215 ? 5.154   23.795  17.090  1.00 68.50  ? 202 TRP A NE1 1 
ATOM   3369 C CE2 . TRP B 1 215 ? 5.467   24.802  16.207  1.00 68.23  ? 202 TRP A CE2 1 
ATOM   3370 C CE3 . TRP B 1 215 ? 5.812   27.203  16.265  1.00 76.26  ? 202 TRP A CE3 1 
ATOM   3371 C CZ2 . TRP B 1 215 ? 5.715   24.755  14.832  1.00 67.95  ? 202 TRP A CZ2 1 
ATOM   3372 C CZ3 . TRP B 1 215 ? 6.053   27.161  14.904  1.00 74.58  ? 202 TRP A CZ3 1 
ATOM   3373 C CH2 . TRP B 1 215 ? 5.999   25.951  14.200  1.00 79.16  ? 202 TRP A CH2 1 
ATOM   3374 N N   . ALA B 1 216 ? 6.017   27.683  22.799  1.00 82.90  ? 203 ALA A N   1 
ATOM   3375 C CA  . ALA B 1 216 ? 5.458   28.418  23.932  1.00 75.39  ? 203 ALA A CA  1 
ATOM   3376 C C   . ALA B 1 216 ? 5.609   29.936  23.818  1.00 77.73  ? 203 ALA A C   1 
ATOM   3377 O O   . ALA B 1 216 ? 5.178   30.642  24.731  1.00 78.49  ? 203 ALA A O   1 
ATOM   3378 C CB  . ALA B 1 216 ? 6.025   27.900  25.251  1.00 70.03  ? 203 ALA A CB  1 
ATOM   3379 N N   . ALA B 1 217 ? 6.240   30.448  22.749  1.00 75.69  ? 204 ALA A N   1 
ATOM   3380 C CA  . ALA B 1 217 ? 6.320   31.902  22.586  1.00 72.52  ? 204 ALA A CA  1 
ATOM   3381 C C   . ALA B 1 217 ? 6.000   32.306  21.148  1.00 73.39  ? 204 ALA A C   1 
ATOM   3382 O O   . ALA B 1 217 ? 6.258   33.442  20.745  1.00 80.41  ? 204 ALA A O   1 
ATOM   3383 C CB  . ALA B 1 217 ? 7.651   32.484  23.069  1.00 73.55  ? 204 ALA A CB  1 
ATOM   3384 N N   . ASP B 1 218 ? 5.408   31.365  20.395  1.00 69.01  ? 205 ASP A N   1 
ATOM   3385 C CA  . ASP B 1 218 ? 4.956   31.588  19.030  1.00 64.32  ? 205 ASP A CA  1 
ATOM   3386 C C   . ASP B 1 218 ? 3.568   30.956  18.870  1.00 63.37  ? 205 ASP A C   1 
ATOM   3387 O O   . ASP B 1 218 ? 3.407   29.932  18.162  1.00 56.25  ? 205 ASP A O   1 
ATOM   3388 C CB  . ASP B 1 218 ? 5.988   31.022  18.062  1.00 67.48  ? 205 ASP A CB  1 
ATOM   3389 C CG  . ASP B 1 218 ? 5.721   31.192  16.565  1.00 67.51  ? 205 ASP A CG  1 
ATOM   3390 O OD1 . ASP B 1 218 ? 4.930   32.094  16.193  1.00 64.00  ? 205 ASP A OD1 1 
ATOM   3391 O OD2 . ASP B 1 218 ? 6.284   30.402  15.773  1.00 69.31  ? 205 ASP A OD2 1 
ATOM   3392 N N   . PRO B 1 219 ? 2.488   31.519  19.489  1.00 62.92  ? 206 PRO A N   1 
ATOM   3393 C CA  . PRO B 1 219 ? 1.190   30.833  19.445  1.00 57.80  ? 206 PRO A CA  1 
ATOM   3394 C C   . PRO B 1 219 ? 0.596   30.994  18.049  1.00 53.96  ? 206 PRO A C   1 
ATOM   3395 O O   . PRO B 1 219 ? -0.108  30.108  17.622  1.00 48.25  ? 206 PRO A O   1 
ATOM   3396 C CB  . PRO B 1 219 ? 0.392   31.413  20.623  1.00 62.01  ? 206 PRO A CB  1 
ATOM   3397 C CG  . PRO B 1 219 ? 1.008   32.834  20.783  1.00 67.41  ? 206 PRO A CG  1 
ATOM   3398 C CD  . PRO B 1 219 ? 2.391   32.853  20.122  1.00 71.71  ? 206 PRO A CD  1 
ATOM   3399 N N   . ALA B 1 220 ? 0.985   32.086  17.342  1.00 54.94  ? 207 ALA A N   1 
ATOM   3400 C CA  . ALA B 1 220 ? 0.677   32.235  15.926  1.00 55.26  ? 207 ALA A CA  1 
ATOM   3401 C C   . ALA B 1 220 ? 1.197   31.037  15.139  1.00 52.66  ? 207 ALA A C   1 
ATOM   3402 O O   . ALA B 1 220 ? 0.483   30.477  14.307  1.00 49.24  ? 207 ALA A O   1 
ATOM   3403 C CB  . ALA B 1 220 ? 1.219   33.547  15.383  1.00 57.16  ? 207 ALA A CB  1 
ATOM   3404 N N   . GLY B 1 221 ? 2.441   30.633  15.432  1.00 53.63  ? 208 GLY A N   1 
ATOM   3405 C CA  . GLY B 1 221 ? 3.142   29.601  14.684  1.00 45.46  ? 208 GLY A CA  1 
ATOM   3406 C C   . GLY B 1 221 ? 2.511   28.245  14.992  1.00 45.48  ? 208 GLY A C   1 
ATOM   3407 O O   . GLY B 1 221 ? 2.311   27.427  14.085  1.00 43.17  ? 208 GLY A O   1 
ATOM   3408 N N   . LEU B 1 222 ? 2.182   28.036  16.268  1.00 43.56  ? 209 LEU A N   1 
ATOM   3409 C CA  . LEU B 1 222 ? 1.531   26.790  16.677  1.00 43.37  ? 209 LEU A CA  1 
ATOM   3410 C C   . LEU B 1 222 ? 0.211   26.625  15.917  1.00 41.94  ? 209 LEU A C   1 
ATOM   3411 O O   . LEU B 1 222 ? -0.067  25.543  15.368  1.00 39.76  ? 209 LEU A O   1 
ATOM   3412 C CB  . LEU B 1 222 ? 1.320   26.800  18.191  1.00 45.72  ? 209 LEU A CB  1 
ATOM   3413 C CG  . LEU B 1 222 ? 0.589   25.573  18.774  1.00 42.94  ? 209 LEU A CG  1 
ATOM   3414 C CD1 . LEU B 1 222 ? 1.295   24.266  18.485  1.00 45.83  ? 209 LEU A CD1 1 
ATOM   3415 C CD2 . LEU B 1 222 ? 0.219   25.676  20.264  1.00 46.58  ? 209 LEU A CD2 1 
ATOM   3416 N N   . GLU B 1 223 ? -0.591  27.712  15.912  1.00 43.98  ? 210 GLU A N   1 
ATOM   3417 C CA  . GLU B 1 223 ? -1.953  27.762  15.416  1.00 42.02  ? 210 GLU A CA  1 
ATOM   3418 C C   . GLU B 1 223 ? -1.902  27.535  13.912  1.00 39.19  ? 210 GLU A C   1 
ATOM   3419 O O   . GLU B 1 223 ? -2.717  26.808  13.371  1.00 37.95  ? 210 GLU A O   1 
ATOM   3420 C CB  . GLU B 1 223 ? -2.622  29.038  15.980  1.00 46.23  ? 210 GLU A CB  1 
ATOM   3421 C CG  . GLU B 1 223 ? -4.114  29.256  15.705  1.00 50.55  ? 210 GLU A CG  1 
ATOM   3422 C CD  . GLU B 1 223 ? -5.016  28.008  15.741  1.00 54.51  ? 210 GLU A CD  1 
ATOM   3423 O OE1 . GLU B 1 223 ? -4.865  27.183  16.663  1.00 51.15  ? 210 GLU A OE1 1 
ATOM   3424 O OE2 . GLU B 1 223 ? -5.885  27.839  14.839  1.00 52.36  ? 210 GLU A OE2 1 
ATOM   3425 N N   . ALA B 1 224 ? -0.924  28.171  13.238  1.00 39.27  ? 211 ALA A N   1 
ATOM   3426 C CA  . ALA B 1 224 ? -0.738  28.083  11.798  1.00 38.87  ? 211 ALA A CA  1 
ATOM   3427 C C   . ALA B 1 224 ? -0.412  26.630  11.464  1.00 36.04  ? 211 ALA A C   1 
ATOM   3428 O O   . ALA B 1 224 ? -0.944  26.048  10.513  1.00 34.22  ? 211 ALA A O   1 
ATOM   3429 C CB  . ALA B 1 224 ? 0.322   29.096  11.370  1.00 40.51  ? 211 ALA A CB  1 
ATOM   3430 N N   . ALA B 1 225 ? 0.451   26.009  12.274  1.00 35.96  ? 212 ALA A N   1 
ATOM   3431 C CA  . ALA B 1 225 ? 0.877   24.643  11.983  1.00 34.34  ? 212 ALA A CA  1 
ATOM   3432 C C   . ALA B 1 225 ? -0.304  23.690  12.260  1.00 33.10  ? 212 ALA A C   1 
ATOM   3433 O O   . ALA B 1 225 ? -0.541  22.729  11.502  1.00 32.35  ? 212 ALA A O   1 
ATOM   3434 C CB  . ALA B 1 225 ? 2.101   24.255  12.808  1.00 32.52  ? 212 ALA A CB  1 
ATOM   3435 N N   . SER B 1 226 ? -1.098  24.025  13.292  1.00 32.14  ? 213 SER A N   1 
ATOM   3436 C CA  . SER B 1 226 ? -2.251  23.170  13.588  1.00 30.93  ? 213 SER A CA  1 
ATOM   3437 C C   . SER B 1 226 ? -3.255  23.231  12.434  1.00 30.47  ? 213 SER A C   1 
ATOM   3438 O O   . SER B 1 226 ? -3.800  22.233  12.001  1.00 29.62  ? 213 SER A O   1 
ATOM   3439 C CB  . SER B 1 226 ? -2.863  23.529  14.950  1.00 32.05  ? 213 SER A CB  1 
ATOM   3440 O OG  . SER B 1 226 ? -3.994  22.697  15.230  1.00 28.09  ? 213 SER A OG  1 
ATOM   3441 N N   . GLN B 1 227 ? -3.472  24.428  11.914  1.00 35.00  ? 214 GLN A N   1 
ATOM   3442 C CA  . GLN B 1 227 ? -4.440  24.678  10.845  1.00 35.69  ? 214 GLN A CA  1 
ATOM   3443 C C   . GLN B 1 227 ? -3.985  23.997  9.580   1.00 35.10  ? 214 GLN A C   1 
ATOM   3444 O O   . GLN B 1 227 ? -4.817  23.544  8.814   1.00 34.51  ? 214 GLN A O   1 
ATOM   3445 C CB  . GLN B 1 227 ? -4.622  26.150  10.430  1.00 38.40  ? 214 GLN A CB  1 
ATOM   3446 C CG  . GLN B 1 227 ? -5.751  26.886  11.145  1.00 44.90  ? 214 GLN A CG  1 
ATOM   3447 C CD  . GLN B 1 227 ? -7.055  26.099  11.209  1.00 43.25  ? 214 GLN A CD  1 
ATOM   3448 O OE1 . GLN B 1 227 ? -7.526  25.539  10.188  1.00 45.54  ? 214 GLN A OE1 1 
ATOM   3449 N NE2 . GLN B 1 227 ? -7.620  26.073  12.424  1.00 43.89  ? 214 GLN A NE2 1 
ATOM   3450 N N   . ALA B 1 228 ? -2.659  23.924  9.387   1.00 36.87  ? 215 ALA A N   1 
ATOM   3451 C CA  . ALA B 1 228 ? -2.132  23.270  8.195   1.00 37.92  ? 215 ALA A CA  1 
ATOM   3452 C C   . ALA B 1 228 ? -2.475  21.799  8.248   1.00 33.37  ? 215 ALA A C   1 
ATOM   3453 O O   . ALA B 1 228 ? -2.859  21.213  7.243   1.00 33.79  ? 215 ALA A O   1 
ATOM   3454 C CB  . ALA B 1 228 ? -0.640  23.524  8.073   1.00 45.56  ? 215 ALA A CB  1 
ATOM   3455 N N   . PHE B 1 229 ? -2.371  21.174  9.427   1.00 30.42  ? 216 PHE A N   1 
ATOM   3456 C CA  . PHE B 1 229 ? -2.802  19.783  9.454   1.00 30.32  ? 216 PHE A CA  1 
ATOM   3457 C C   . PHE B 1 229 ? -4.294  19.640  9.156   1.00 27.10  ? 216 PHE A C   1 
ATOM   3458 O O   . PHE B 1 229 ? -4.714  18.687  8.536   1.00 26.46  ? 216 PHE A O   1 
ATOM   3459 C CB  . PHE B 1 229 ? -2.551  19.039  10.775  1.00 29.05  ? 216 PHE A CB  1 
ATOM   3460 C CG  . PHE B 1 229 ? -1.085  18.895  11.172  1.00 31.20  ? 216 PHE A CG  1 
ATOM   3461 C CD1 . PHE B 1 229 ? -0.202  18.138  10.362  1.00 28.51  ? 216 PHE A CD1 1 
ATOM   3462 C CD2 . PHE B 1 229 ? -0.636  19.417  12.386  1.00 32.29  ? 216 PHE A CD2 1 
ATOM   3463 C CE1 . PHE B 1 229 ? 1.102   17.913  10.784  1.00 28.54  ? 216 PHE A CE1 1 
ATOM   3464 C CE2 . PHE B 1 229 ? 0.705   19.236  12.782  1.00 34.58  ? 216 PHE A CE2 1 
ATOM   3465 C CZ  . PHE B 1 229 ? 1.555   18.478  11.965  1.00 28.71  ? 216 PHE A CZ  1 
ATOM   3466 N N   . ILE B 1 230 ? -5.122  20.513  9.703   1.00 28.21  ? 217 ILE A N   1 
ATOM   3467 C CA  . ILE B 1 230 ? -6.543  20.450  9.444   1.00 27.35  ? 217 ILE A CA  1 
ATOM   3468 C C   . ILE B 1 230 ? -6.821  20.611  7.926   1.00 26.58  ? 217 ILE A C   1 
ATOM   3469 O O   . ILE B 1 230 ? -7.574  19.833  7.312   1.00 26.40  ? 217 ILE A O   1 
ATOM   3470 C CB  . ILE B 1 230 ? -7.210  21.565  10.256  1.00 29.02  ? 217 ILE A CB  1 
ATOM   3471 C CG1 . ILE B 1 230 ? -7.253  21.216  11.745  1.00 27.40  ? 217 ILE A CG1 1 
ATOM   3472 C CG2 . ILE B 1 230 ? -8.596  21.865  9.713   1.00 28.54  ? 217 ILE A CG2 1 
ATOM   3473 C CD1 . ILE B 1 230 ? -7.956  22.338  12.522  1.00 31.84  ? 217 ILE A CD1 1 
ATOM   3474 N N   . ASP B 1 231 ? -6.119  21.509  7.266   1.00 28.49  ? 218 ASP A N   1 
ATOM   3475 C CA  . ASP B 1 231 ? -6.324  21.801  5.842   1.00 30.12  ? 218 ASP A CA  1 
ATOM   3476 C C   . ASP B 1 231 ? -5.901  20.576  5.029   1.00 29.32  ? 218 ASP A C   1 
ATOM   3477 O O   . ASP B 1 231 ? -6.556  20.234  4.076   1.00 28.73  ? 218 ASP A O   1 
ATOM   3478 C CB  . ASP B 1 231 ? -5.596  23.058  5.394   1.00 36.28  ? 218 ASP A CB  1 
ATOM   3479 C CG  . ASP B 1 231 ? -5.861  24.395  6.110   1.00 49.12  ? 218 ASP A CG  1 
ATOM   3480 O OD1 . ASP B 1 231 ? -6.759  24.508  7.024   1.00 55.64  ? 218 ASP A OD1 1 
ATOM   3481 O OD2 . ASP B 1 231 ? -5.112  25.392  5.795   1.00 54.35  ? 218 ASP A OD2 1 
ATOM   3482 N N   . GLN B 1 232 ? -4.896  19.833  5.488   1.00 29.06  ? 219 GLN A N   1 
ATOM   3483 C CA  . GLN B 1 232 ? -4.409  18.716  4.667   1.00 27.43  ? 219 GLN A CA  1 
ATOM   3484 C C   . GLN B 1 232 ? -5.240  17.477  4.941   1.00 27.33  ? 219 GLN A C   1 
ATOM   3485 O O   . GLN B 1 232 ? -5.343  16.593  4.073   1.00 24.92  ? 219 GLN A O   1 
ATOM   3486 C CB  . GLN B 1 232 ? -2.971  18.470  5.116   1.00 28.14  ? 219 GLN A CB  1 
ATOM   3487 C CG  . GLN B 1 232 ? -2.003  19.470  4.459   1.00 29.64  ? 219 GLN A CG  1 
ATOM   3488 C CD  . GLN B 1 232 ? -0.642  19.228  5.062   1.00 31.26  ? 219 GLN A CD  1 
ATOM   3489 O OE1 . GLN B 1 232 ? -0.178  18.077  5.239   1.00 31.60  ? 219 GLN A OE1 1 
ATOM   3490 N NE2 . GLN B 1 232 ? 0.001   20.349  5.302   1.00 30.79  ? 219 GLN A NE2 1 
ATOM   3491 N N   . GLN B 1 233 ? -5.768  17.413  6.180   1.00 24.74  ? 220 GLN A N   1 
ATOM   3492 C CA  . GLN B 1 233 ? -6.571  16.252  6.557   1.00 24.14  ? 220 GLN A CA  1 
ATOM   3493 C C   . GLN B 1 233 ? -7.882  16.232  5.782   1.00 22.42  ? 220 GLN A C   1 
ATOM   3494 O O   . GLN B 1 233 ? -8.353  17.288  5.268   1.00 25.29  ? 220 GLN A O   1 
ATOM   3495 C CB  . GLN B 1 233 ? -6.883  16.300  8.079   1.00 21.22  ? 220 GLN A CB  1 
ATOM   3496 C CG  . GLN B 1 233 ? -5.728  15.828  8.955   1.00 21.62  ? 220 GLN A CG  1 
ATOM   3497 C CD  . GLN B 1 233 ? -5.886  16.066  10.446  1.00 20.68  ? 220 GLN A CD  1 
ATOM   3498 O OE1 . GLN B 1 233 ? -4.944  15.728  11.192  1.00 20.85  ? 220 GLN A OE1 1 
ATOM   3499 N NE2 . GLN B 1 233 ? -7.070  16.526  10.905  1.00 19.64  ? 220 GLN A NE2 1 
ATOM   3500 N N   . MET B 1 234 ? -8.502  15.036  5.742   1.00 22.69  ? 221 MET A N   1 
ATOM   3501 C CA  . MET B 1 234 ? -9.855  14.896  5.185   1.00 23.00  ? 221 MET A CA  1 
ATOM   3502 C C   . MET B 1 234 ? -10.882 15.333  6.240   1.00 22.93  ? 221 MET A C   1 
ATOM   3503 O O   . MET B 1 234 ? -11.849 16.041  5.903   1.00 29.72  ? 221 MET A O   1 
ATOM   3504 C CB  . MET B 1 234 ? -10.172 13.463  4.785   1.00 21.86  ? 221 MET A CB  1 
ATOM   3505 C CG  . MET B 1 234 ? -9.321  13.008  3.545   1.00 19.55  ? 221 MET A CG  1 
ATOM   3506 S SD  . MET B 1 234 ? -9.570  11.205  3.401   1.00 20.94  ? 221 MET A SD  1 
ATOM   3507 C CE  . MET B 1 234 ? -8.536  11.040  1.936   1.00 27.27  ? 221 MET A CE  1 
ATOM   3508 N N   . LEU B 1 235 ? -10.718 14.899  7.491   1.00 21.11  ? 222 LEU A N   1 
ATOM   3509 C CA  . LEU B 1 235 ? -11.589 15.403  8.583   1.00 22.99  ? 222 LEU A CA  1 
ATOM   3510 C C   . LEU B 1 235 ? -11.004 16.669  9.191   1.00 23.45  ? 222 LEU A C   1 
ATOM   3511 O O   . LEU B 1 235 ? -9.799  16.748  9.475   1.00 25.43  ? 222 LEU A O   1 
ATOM   3512 C CB  . LEU B 1 235 ? -11.855 14.286  9.619   1.00 21.54  ? 222 LEU A CB  1 
ATOM   3513 C CG  . LEU B 1 235 ? -12.448 13.001  8.999   1.00 20.59  ? 222 LEU A CG  1 
ATOM   3514 C CD1 . LEU B 1 235 ? -12.285 11.852  10.083  1.00 21.95  ? 222 LEU A CD1 1 
ATOM   3515 C CD2 . LEU B 1 235 ? -13.926 13.285  8.667   1.00 23.52  ? 222 LEU A CD2 1 
ATOM   3516 N N   . LYS B 1 236 ? -11.845 17.660  9.487   1.00 23.60  ? 223 LYS A N   1 
ATOM   3517 C CA  . LYS B 1 236 ? -11.316 19.000  9.737   1.00 25.39  ? 223 LYS A CA  1 
ATOM   3518 C C   . LYS B 1 236 ? -11.310 19.330  11.234  1.00 25.17  ? 223 LYS A C   1 
ATOM   3519 O O   . LYS B 1 236 ? -11.909 20.332  11.693  1.00 27.35  ? 223 LYS A O   1 
ATOM   3520 C CB  . LYS B 1 236 ? -12.100 20.062  8.959   1.00 27.12  ? 223 LYS A CB  1 
ATOM   3521 C CG  . LYS B 1 236 ? -12.117 19.702  7.475   1.00 27.89  ? 223 LYS A CG  1 
ATOM   3522 C CD  . LYS B 1 236 ? -10.751 19.894  6.810   1.00 29.75  ? 223 LYS A CD  1 
ATOM   3523 C CE  . LYS B 1 236 ? -10.787 19.554  5.375   1.00 31.83  ? 223 LYS A CE  1 
ATOM   3524 N NZ  . LYS B 1 236 ? -9.489  19.847  4.814   1.00 34.08  ? 223 LYS A NZ  1 
ATOM   3525 N N   . PHE B 1 237 ? -10.632 18.475  11.999  1.00 24.46  ? 224 PHE A N   1 
ATOM   3526 C CA  . PHE B 1 237 ? -10.452 18.721  13.430  1.00 25.05  ? 224 PHE A CA  1 
ATOM   3527 C C   . PHE B 1 237 ? -9.133  18.030  13.806  1.00 22.83  ? 224 PHE A C   1 
ATOM   3528 O O   . PHE B 1 237 ? -8.650  17.194  13.046  1.00 22.12  ? 224 PHE A O   1 
ATOM   3529 C CB  . PHE B 1 237 ? -11.609 18.204  14.327  1.00 25.31  ? 224 PHE A CB  1 
ATOM   3530 C CG  . PHE B 1 237 ? -11.954 16.720  14.216  1.00 25.30  ? 224 PHE A CG  1 
ATOM   3531 C CD1 . PHE B 1 237 ? -11.317 15.775  15.011  1.00 27.45  ? 224 PHE A CD1 1 
ATOM   3532 C CD2 . PHE B 1 237 ? -12.867 16.246  13.232  1.00 27.45  ? 224 PHE A CD2 1 
ATOM   3533 C CE1 . PHE B 1 237 ? -11.592 14.385  14.844  1.00 27.70  ? 224 PHE A CE1 1 
ATOM   3534 C CE2 . PHE B 1 237 ? -13.142 14.879  13.063  1.00 26.03  ? 224 PHE A CE2 1 
ATOM   3535 C CZ  . PHE B 1 237 ? -12.511 13.958  13.873  1.00 26.10  ? 224 PHE A CZ  1 
ATOM   3536 N N   . ARG B 1 238 ? -8.544  18.461  14.919  1.00 22.79  ? 225 ARG A N   1 
ATOM   3537 C CA  . ARG B 1 238 ? -7.252  17.913  15.354  1.00 23.66  ? 225 ARG A CA  1 
ATOM   3538 C C   . ARG B 1 238 ? -7.466  16.627  16.130  1.00 21.42  ? 225 ARG A C   1 
ATOM   3539 O O   . ARG B 1 238 ? -8.342  16.573  17.036  1.00 21.00  ? 225 ARG A O   1 
ATOM   3540 C CB  . ARG B 1 238 ? -6.505  18.871  16.298  1.00 24.02  ? 225 ARG A CB  1 
ATOM   3541 C CG  . ARG B 1 238 ? -5.943  20.085  15.600  1.00 26.47  ? 225 ARG A CG  1 
ATOM   3542 C CD  . ARG B 1 238 ? -5.006  19.785  14.440  1.00 25.70  ? 225 ARG A CD  1 
ATOM   3543 N NE  . ARG B 1 238 ? -4.023  18.714  14.628  1.00 24.43  ? 225 ARG A NE  1 
ATOM   3544 C CZ  . ARG B 1 238 ? -2.890  18.900  15.332  1.00 26.38  ? 225 ARG A CZ  1 
ATOM   3545 N NH1 . ARG B 1 238 ? -2.584  20.080  15.796  1.00 28.08  ? 225 ARG A NH1 1 
ATOM   3546 N NH2 . ARG B 1 238 ? -2.107  17.844  15.587  1.00 25.41  ? 225 ARG A NH2 1 
ATOM   3547 N N   . LEU B 1 239 ? -6.638  15.619  15.807  1.00 18.90  ? 226 LEU A N   1 
ATOM   3548 C CA  . LEU B 1 239 ? -6.640  14.358  16.544  1.00 18.41  ? 226 LEU A CA  1 
ATOM   3549 C C   . LEU B 1 239 ? -5.897  14.567  17.855  1.00 22.99  ? 226 LEU A C   1 
ATOM   3550 O O   . LEU B 1 239 ? -4.987  15.398  17.930  1.00 24.41  ? 226 LEU A O   1 
ATOM   3551 C CB  . LEU B 1 239 ? -5.931  13.271  15.771  1.00 17.27  ? 226 LEU A CB  1 
ATOM   3552 C CG  . LEU B 1 239 ? -6.599  12.827  14.484  1.00 19.20  ? 226 LEU A CG  1 
ATOM   3553 C CD1 . LEU B 1 239 ? -5.815  11.771  13.710  1.00 17.46  ? 226 LEU A CD1 1 
ATOM   3554 C CD2 . LEU B 1 239 ? -8.038  12.299  14.692  1.00 17.62  ? 226 LEU A CD2 1 
ATOM   3555 N N   . ASP B 1 240 ? -6.217  13.724  18.852  1.00 21.27  ? 227 ASP A N   1 
ATOM   3556 C CA  . ASP B 1 240 ? -5.491  13.840  20.118  1.00 22.71  ? 227 ASP A CA  1 
ATOM   3557 C C   . ASP B 1 240 ? -5.266  12.416  20.658  1.00 20.93  ? 227 ASP A C   1 
ATOM   3558 O O   . ASP B 1 240 ? -5.526  11.427  19.992  1.00 24.61  ? 227 ASP A O   1 
ATOM   3559 C CB  . ASP B 1 240 ? -6.266  14.772  21.039  1.00 22.42  ? 227 ASP A CB  1 
ATOM   3560 C CG  . ASP B 1 240 ? -7.639  14.282  21.484  1.00 25.14  ? 227 ASP A CG  1 
ATOM   3561 O OD1 . ASP B 1 240 ? -7.875  13.065  21.555  1.00 24.28  ? 227 ASP A OD1 1 
ATOM   3562 O OD2 . ASP B 1 240 ? -8.433  15.127  21.883  1.00 27.78  ? 227 ASP A OD2 1 
ATOM   3563 N N   . ALA B 1 241 ? -4.663  12.341  21.831  1.00 22.69  ? 228 ALA A N   1 
ATOM   3564 C CA  . ALA B 1 241 ? -4.269  11.045  22.399  1.00 18.84  ? 228 ALA A CA  1 
ATOM   3565 C C   . ALA B 1 241 ? -5.470  10.125  22.661  1.00 19.62  ? 228 ALA A C   1 
ATOM   3566 O O   . ALA B 1 241 ? -5.316  8.920   22.569  1.00 18.88  ? 228 ALA A O   1 
ATOM   3567 C CB  . ALA B 1 241 ? -3.433  11.305  23.678  1.00 19.09  ? 228 ALA A CB  1 
ATOM   3568 N N   . SER B 1 242 ? -6.671  10.687  22.853  1.00 20.29  ? 229 SER A N   1 
ATOM   3569 C CA  . SER B 1 242 ? -7.857  9.879   23.078  1.00 19.33  ? 229 SER A CA  1 
ATOM   3570 C C   . SER B 1 242 ? -8.212  9.119   21.805  1.00 18.36  ? 229 SER A C   1 
ATOM   3571 O O   . SER B 1 242 ? -8.708  8.009   21.877  1.00 21.20  ? 229 SER A O   1 
ATOM   3572 C CB  . SER B 1 242 ? -8.989  10.770  23.441  1.00 18.55  ? 229 SER A CB  1 
ATOM   3573 O OG  . SER B 1 242 ? -8.760  11.328  24.751  1.00 21.87  ? 229 SER A OG  1 
ATOM   3574 N N   . ASP B 1 243 ? -7.937  9.762   20.658  1.00 16.93  ? 230 ASP A N   1 
ATOM   3575 C CA  . ASP B 1 243 ? -8.280  9.043   19.455  1.00 17.91  ? 230 ASP A CA  1 
ATOM   3576 C C   . ASP B 1 243 ? -7.396  7.819   19.366  1.00 16.61  ? 230 ASP A C   1 
ATOM   3577 O O   . ASP B 1 243 ? -7.803  6.755   18.854  1.00 18.41  ? 230 ASP A O   1 
ATOM   3578 C CB  . ASP B 1 243 ? -7.994  9.872   18.222  1.00 18.16  ? 230 ASP A CB  1 
ATOM   3579 C CG  . ASP B 1 243 ? -8.941  11.039  18.137  1.00 22.79  ? 230 ASP A CG  1 
ATOM   3580 O OD1 . ASP B 1 243 ? -10.130 10.745  17.943  1.00 21.81  ? 230 ASP A OD1 1 
ATOM   3581 O OD2 . ASP B 1 243 ? -8.499  12.214  18.289  1.00 20.15  ? 230 ASP A OD2 1 
ATOM   3582 N N   . CYS B 1 244 ? -6.112  7.989   19.769  1.00 15.54  ? 231 CYS A N   1 
ATOM   3583 C CA  . CYS B 1 244 ? -5.236  6.808   19.752  1.00 14.73  ? 231 CYS A CA  1 
ATOM   3584 C C   . CYS B 1 244 ? -5.675  5.781   20.788  1.00 16.05  ? 231 CYS A C   1 
ATOM   3585 O O   . CYS B 1 244 ? -5.743  4.548   20.535  1.00 15.97  ? 231 CYS A O   1 
ATOM   3586 C CB  . CYS B 1 244 ? -3.776  7.101   20.074  1.00 16.69  ? 231 CYS A CB  1 
ATOM   3587 S SG  . CYS B 1 244 ? -3.075  8.290   18.879  1.00 20.50  ? 231 CYS A SG  1 
ATOM   3588 N N   . ALA B 1 245 ? -6.075  6.244   21.976  1.00 15.96  ? 232 ALA A N   1 
ATOM   3589 C CA  . ALA B 1 245 ? -6.466  5.263   22.999  1.00 16.73  ? 232 ALA A CA  1 
ATOM   3590 C C   . ALA B 1 245 ? -7.753  4.506   22.660  1.00 18.07  ? 232 ALA A C   1 
ATOM   3591 O O   . ALA B 1 245 ? -7.822  3.294   22.897  1.00 18.08  ? 232 ALA A O   1 
ATOM   3592 C CB  . ALA B 1 245 ? -6.624  5.965   24.360  1.00 17.71  ? 232 ALA A CB  1 
ATOM   3593 N N   . ARG B 1 246 ? -8.713  5.173   21.963  1.00 17.04  ? 233 ARG A N   1 
ATOM   3594 C CA  . ARG B 1 246 ? -9.933  4.496   21.490  1.00 17.92  ? 233 ARG A CA  1 
ATOM   3595 C C   . ARG B 1 246 ? -9.561  3.300   20.620  1.00 18.86  ? 233 ARG A C   1 
ATOM   3596 O O   . ARG B 1 246 ? -10.187 2.231   20.680  1.00 17.55  ? 233 ARG A O   1 
ATOM   3597 C CB  . ARG B 1 246 ? -10.880 5.486   20.808  1.00 20.47  ? 233 ARG A CB  1 
ATOM   3598 C CG  . ARG B 1 246 ? -11.457 6.397   21.906  1.00 21.71  ? 233 ARG A CG  1 
ATOM   3599 C CD  . ARG B 1 246 ? -12.263 7.471   21.164  1.00 25.32  ? 233 ARG A CD  1 
ATOM   3600 N NE  . ARG B 1 246 ? -12.608 8.536   22.098  1.00 30.37  ? 233 ARG A NE  1 
ATOM   3601 C CZ  . ARG B 1 246 ? -13.638 9.381   21.907  1.00 30.45  ? 233 ARG A CZ  1 
ATOM   3602 N NH1 . ARG B 1 246 ? -14.061 10.079  22.978  1.00 35.75  ? 233 ARG A NH1 1 
ATOM   3603 N NH2 . ARG B 1 246 ? -14.187 9.534   20.656  1.00 33.46  ? 233 ARG A NH2 1 
ATOM   3604 N N   . LEU B 1 247 ? -8.566  3.532   19.730  1.00 18.21  ? 234 LEU A N   1 
ATOM   3605 C CA  . LEU B 1 247 ? -8.211  2.475   18.821  1.00 17.94  ? 234 LEU A CA  1 
ATOM   3606 C C   . LEU B 1 247 ? -7.470  1.361   19.569  1.00 19.23  ? 234 LEU A C   1 
ATOM   3607 O O   . LEU B 1 247 ? -7.702  0.176   19.294  1.00 17.38  ? 234 LEU A O   1 
ATOM   3608 C CB  . LEU B 1 247 ? -7.441  3.033   17.593  1.00 15.25  ? 234 LEU A CB  1 
ATOM   3609 C CG  . LEU B 1 247 ? -6.874  1.986   16.607  1.00 15.37  ? 234 LEU A CG  1 
ATOM   3610 C CD1 . LEU B 1 247 ? -7.944  1.045   16.098  1.00 16.81  ? 234 LEU A CD1 1 
ATOM   3611 C CD2 . LEU B 1 247 ? -6.192  2.751   15.469  1.00 13.52  ? 234 LEU A CD2 1 
ATOM   3612 N N   . ALA B 1 248 ? -6.601  1.738   20.536  1.00 15.70  ? 235 ALA A N   1 
ATOM   3613 C CA  . ALA B 1 248 ? -5.875  0.716   21.258  1.00 17.08  ? 235 ALA A CA  1 
ATOM   3614 C C   . ALA B 1 248 ? -6.822  -0.205  22.034  1.00 20.31  ? 235 ALA A C   1 
ATOM   3615 O O   . ALA B 1 248 ? -6.529  -1.413  22.117  1.00 17.39  ? 235 ALA A O   1 
ATOM   3616 C CB  . ALA B 1 248 ? -4.844  1.304   22.227  1.00 17.35  ? 235 ALA A CB  1 
ATOM   3617 N N   . LEU B 1 249 ? -7.863  0.383   22.663  1.00 17.95  ? 236 LEU A N   1 
ATOM   3618 C CA  . LEU B 1 249 ? -8.803  -0.444  23.418  1.00 19.31  ? 236 LEU A CA  1 
ATOM   3619 C C   . LEU B 1 249 ? -9.400  -1.512  22.503  1.00 19.15  ? 236 LEU A C   1 
ATOM   3620 O O   . LEU B 1 249 ? -9.505  -2.716  22.850  1.00 18.04  ? 236 LEU A O   1 
ATOM   3621 C CB  . LEU B 1 249 ? -9.893  0.418   24.026  1.00 17.20  ? 236 LEU A CB  1 
ATOM   3622 C CG  . LEU B 1 249 ? -9.414  1.435   25.067  1.00 19.30  ? 236 LEU A CG  1 
ATOM   3623 C CD1 . LEU B 1 249 ? -10.611 2.266   25.547  1.00 19.90  ? 236 LEU A CD1 1 
ATOM   3624 C CD2 . LEU B 1 249 ? -8.918  0.606   26.293  1.00 21.72  ? 236 LEU A CD2 1 
ATOM   3625 N N   . PHE B 1 250 ? -9.834  -1.080  21.281  1.00 15.98  ? 237 PHE A N   1 
ATOM   3626 C CA  . PHE B 1 250 ? -10.471 -2.036  20.363  1.00 18.52  ? 237 PHE A CA  1 
ATOM   3627 C C   . PHE B 1 250 ? -9.424  -3.124  20.031  1.00 17.88  ? 237 PHE A C   1 
ATOM   3628 O O   . PHE B 1 250 ? -9.813  -4.291  19.953  1.00 16.67  ? 237 PHE A O   1 
ATOM   3629 C CB  . PHE B 1 250 ? -11.018 -1.301  19.096  1.00 19.39  ? 237 PHE A CB  1 
ATOM   3630 C CG  . PHE B 1 250 ? -11.495 -2.286  18.019  1.00 20.57  ? 237 PHE A CG  1 
ATOM   3631 C CD1 . PHE B 1 250 ? -12.742 -2.885  18.147  1.00 19.71  ? 237 PHE A CD1 1 
ATOM   3632 C CD2 . PHE B 1 250 ? -10.707 -2.563  16.897  1.00 22.31  ? 237 PHE A CD2 1 
ATOM   3633 C CE1 . PHE B 1 250 ? -13.189 -3.808  17.209  1.00 21.29  ? 237 PHE A CE1 1 
ATOM   3634 C CE2 . PHE B 1 250 ? -11.115 -3.500  15.964  1.00 21.25  ? 237 PHE A CE2 1 
ATOM   3635 C CZ  . PHE B 1 250 ? -12.378 -4.093  16.095  1.00 20.97  ? 237 PHE A CZ  1 
ATOM   3636 N N   . LEU B 1 251 ? -8.168  -2.740  19.715  1.00 15.76  ? 238 LEU A N   1 
ATOM   3637 C CA  . LEU B 1 251 ? -7.143  -3.708  19.252  1.00 16.28  ? 238 LEU A CA  1 
ATOM   3638 C C   . LEU B 1 251 ? -6.679  -4.673  20.348  1.00 20.01  ? 238 LEU A C   1 
ATOM   3639 O O   . LEU B 1 251 ? -6.083  -5.718  20.081  1.00 21.49  ? 238 LEU A O   1 
ATOM   3640 C CB  . LEU B 1 251 ? -5.925  -2.991  18.681  1.00 16.08  ? 238 LEU A CB  1 
ATOM   3641 C CG  . LEU B 1 251 ? -6.222  -2.239  17.379  1.00 18.59  ? 238 LEU A CG  1 
ATOM   3642 C CD1 . LEU B 1 251 ? -4.946  -1.523  16.907  1.00 19.30  ? 238 LEU A CD1 1 
ATOM   3643 C CD2 . LEU B 1 251 ? -6.572  -3.316  16.338  1.00 19.02  ? 238 LEU A CD2 1 
ATOM   3644 N N   . ALA B 1 252 ? -6.963  -4.301  21.607  1.00 17.55  ? 239 ALA A N   1 
ATOM   3645 C CA  . ALA B 1 252 ? -6.673  -5.184  22.739  1.00 20.05  ? 239 ALA A CA  1 
ATOM   3646 C C   . ALA B 1 252 ? -7.859  -6.083  23.105  1.00 21.72  ? 239 ALA A C   1 
ATOM   3647 O O   . ALA B 1 252 ? -7.673  -7.067  23.843  1.00 21.95  ? 239 ALA A O   1 
ATOM   3648 C CB  . ALA B 1 252 ? -6.298  -4.330  23.930  1.00 18.28  ? 239 ALA A CB  1 
ATOM   3649 N N   . SER B 1 253 ? -9.081  -5.666  22.753  1.00 18.27  ? 240 SER A N   1 
ATOM   3650 C CA  . SER B 1 253 ? -10.289 -6.340  23.262  1.00 21.31  ? 240 SER A CA  1 
ATOM   3651 C C   . SER B 1 253 ? -10.577 -7.587  22.434  1.00 23.05  ? 240 SER A C   1 
ATOM   3652 O O   . SER B 1 253 ? -10.028 -7.778  21.348  1.00 22.45  ? 240 SER A O   1 
ATOM   3653 C CB  . SER B 1 253 ? -11.452 -5.388  23.166  1.00 21.25  ? 240 SER A CB  1 
ATOM   3654 O OG  . SER B 1 253 ? -11.873 -5.227  21.791  1.00 23.84  ? 240 SER A OG  1 
ATOM   3655 N N   . ASP B 1 254 ? -11.483 -8.464  22.913  1.00 22.93  ? 241 ASP A N   1 
ATOM   3656 C CA  . ASP B 1 254 ? -11.940 -9.591  22.104  1.00 25.45  ? 241 ASP A CA  1 
ATOM   3657 C C   . ASP B 1 254 ? -12.685 -9.159  20.844  1.00 26.21  ? 241 ASP A C   1 
ATOM   3658 O O   . ASP B 1 254 ? -12.915 -9.990  19.998  1.00 27.40  ? 241 ASP A O   1 
ATOM   3659 C CB  . ASP B 1 254 ? -12.835 -10.495 22.953  1.00 26.65  ? 241 ASP A CB  1 
ATOM   3660 C CG  . ASP B 1 254 ? -12.146 -11.207 24.088  1.00 30.27  ? 241 ASP A CG  1 
ATOM   3661 O OD1 . ASP B 1 254 ? -10.957 -11.081 24.248  1.00 34.65  ? 241 ASP A OD1 1 
ATOM   3662 O OD2 . ASP B 1 254 ? -12.837 -11.985 24.795  1.00 42.51  ? 241 ASP A OD2 1 
ATOM   3663 N N   . ASP B 1 255 ? -13.119 -7.882  20.715  1.00 21.33  ? 242 ASP A N   1 
ATOM   3664 C CA  . ASP B 1 255 ? -13.765 -7.463  19.487  1.00 22.39  ? 242 ASP A CA  1 
ATOM   3665 C C   . ASP B 1 255 ? -12.802 -7.479  18.303  1.00 22.07  ? 242 ASP A C   1 
ATOM   3666 O O   . ASP B 1 255 ? -13.293 -7.380  17.169  1.00 24.15  ? 242 ASP A O   1 
ATOM   3667 C CB  . ASP B 1 255 ? -14.339 -6.075  19.595  1.00 22.72  ? 242 ASP A CB  1 
ATOM   3668 C CG  . ASP B 1 255 ? -15.443 -6.014  20.650  1.00 27.00  ? 242 ASP A CG  1 
ATOM   3669 O OD1 . ASP B 1 255 ? -15.096 -6.005  21.848  1.00 32.84  ? 242 ASP A OD1 1 
ATOM   3670 O OD2 . ASP B 1 255 ? -16.606 -5.944  20.285  1.00 30.95  ? 242 ASP A OD2 1 
ATOM   3671 N N   . SER B 1 256 ? -11.495 -7.672  18.532  1.00 20.31  ? 243 SER A N   1 
ATOM   3672 C CA  . SER B 1 256 ? -10.583 -7.700  17.384  1.00 20.55  ? 243 SER A CA  1 
ATOM   3673 C C   . SER B 1 256 ? -9.831  -9.045  17.375  1.00 21.62  ? 243 SER A C   1 
ATOM   3674 O O   . SER B 1 256 ? -8.711  -9.100  16.851  1.00 22.39  ? 243 SER A O   1 
ATOM   3675 C CB  . SER B 1 256 ? -9.594  -6.511  17.429  1.00 21.89  ? 243 SER A CB  1 
ATOM   3676 O OG  . SER B 1 256 ? -8.817  -6.650  18.608  1.00 21.69  ? 243 SER A OG  1 
ATOM   3677 N N   . ARG B 1 257 ? -10.441 -10.098 17.984  1.00 21.61  ? 244 ARG A N   1 
ATOM   3678 C CA  . ARG B 1 257 ? -9.747  -11.390 18.202  1.00 24.15  ? 244 ARG A CA  1 
ATOM   3679 C C   . ARG B 1 257 ? -9.242  -12.035 16.901  1.00 22.95  ? 244 ARG A C   1 
ATOM   3680 O O   . ARG B 1 257 ? -8.305  -12.847 16.961  1.00 26.11  ? 244 ARG A O   1 
ATOM   3681 C CB  . ARG B 1 257 ? -10.514 -12.447 19.023  1.00 23.48  ? 244 ARG A CB  1 
ATOM   3682 C CG  . ARG B 1 257 ? -11.786 -12.683 18.216  1.00 33.27  ? 244 ARG A CG  1 
ATOM   3683 C CD  . ARG B 1 257 ? -12.475 -14.055 18.263  1.00 46.71  ? 244 ARG A CD  1 
ATOM   3684 N NE  . ARG B 1 257 ? -13.838 -13.992 17.717  1.00 59.93  ? 244 ARG A NE  1 
ATOM   3685 C CZ  . ARG B 1 257 ? -14.555 -15.020 17.233  1.00 92.12  ? 244 ARG A CZ  1 
ATOM   3686 N NH1 . ARG B 1 257 ? -13.951 -16.095 16.693  1.00 78.97  ? 244 ARG A NH1 1 
ATOM   3687 N NH2 . ARG B 1 257 ? -15.890 -14.891 17.195  1.00 88.05  ? 244 ARG A NH2 1 
ATOM   3688 N N   . GLY B 1 258 ? -9.836  -11.716 15.733  1.00 21.97  ? 245 GLY A N   1 
ATOM   3689 C CA  . GLY B 1 258 ? -9.435  -12.387 14.502  1.00 20.34  ? 245 GLY A CA  1 
ATOM   3690 C C   . GLY B 1 258 ? -8.614  -11.425 13.611  1.00 17.37  ? 245 GLY A C   1 
ATOM   3691 O O   . GLY B 1 258 ? -8.416  -11.714 12.428  1.00 19.69  ? 245 GLY A O   1 
ATOM   3692 N N   . CYS B 1 259 ? -8.272  -10.228 14.123  1.00 18.51  ? 246 CYS A N   1 
ATOM   3693 C CA  . CYS B 1 259 ? -7.433  -9.300  13.369  1.00 16.61  ? 246 CYS A CA  1 
ATOM   3694 C C   . CYS B 1 259 ? -5.933  -9.526  13.703  1.00 21.01  ? 246 CYS A C   1 
ATOM   3695 O O   . CYS B 1 259 ? -5.529  -9.472  14.898  1.00 18.44  ? 246 CYS A O   1 
ATOM   3696 C CB  . CYS B 1 259 ? -7.767  -7.863  13.733  1.00 17.08  ? 246 CYS A CB  1 
ATOM   3697 S SG  . CYS B 1 259 ? -9.480  -7.383  13.310  1.00 20.91  ? 246 CYS A SG  1 
ATOM   3698 N N   . THR B 1 260 ? -5.069  -9.818  12.690  1.00 17.45  ? 247 THR A N   1 
ATOM   3699 C CA  . THR B 1 260 ? -3.661  -9.858  13.034  1.00 18.22  ? 247 THR A CA  1 
ATOM   3700 C C   . THR B 1 260 ? -2.879  -9.551  11.761  1.00 16.49  ? 247 THR A C   1 
ATOM   3701 O O   . THR B 1 260 ? -3.422  -9.688  10.666  1.00 16.42  ? 247 THR A O   1 
ATOM   3702 C CB  . THR B 1 260 ? -3.287  -11.266 13.515  1.00 19.86  ? 247 THR A CB  1 
ATOM   3703 O OG1 . THR B 1 260 ? -1.989  -11.296 14.094  1.00 18.42  ? 247 THR A OG1 1 
ATOM   3704 C CG2 . THR B 1 260 ? -3.404  -12.259 12.354  1.00 19.17  ? 247 THR A CG2 1 
ATOM   3705 N N   . GLY B 1 261 ? -1.621  -9.084  11.958  1.00 16.80  ? 248 GLY A N   1 
ATOM   3706 C CA  . GLY B 1 261 ? -0.756  -8.804  10.838  1.00 17.11  ? 248 GLY A CA  1 
ATOM   3707 C C   . GLY B 1 261 ? -1.011  -7.470  10.167  1.00 19.00  ? 248 GLY A C   1 
ATOM   3708 O O   . GLY B 1 261 ? -0.364  -7.209  9.132   1.00 18.75  ? 248 GLY A O   1 
ATOM   3709 N N   . GLN B 1 262 ? -1.908  -6.646  10.753  1.00 16.88  ? 249 GLN A N   1 
ATOM   3710 C CA  . GLN B 1 262 ? -2.513  -5.529  9.988   1.00 16.72  ? 249 GLN A CA  1 
ATOM   3711 C C   . GLN B 1 262 ? -2.151  -4.178  10.569  1.00 18.16  ? 249 GLN A C   1 
ATOM   3712 O O   . GLN B 1 262 ? -1.850  -4.073  11.730  1.00 19.81  ? 249 GLN A O   1 
ATOM   3713 C CB  . GLN B 1 262 ? -4.061  -5.641  10.040  1.00 15.96  ? 249 GLN A CB  1 
ATOM   3714 C CG  . GLN B 1 262 ? -4.490  -6.691  9.022   1.00 16.60  ? 249 GLN A CG  1 
ATOM   3715 C CD  . GLN B 1 262 ? -4.158  -6.275  7.600   1.00 18.20  ? 249 GLN A CD  1 
ATOM   3716 O OE1 . GLN B 1 262 ? -4.130  -5.054  7.255   1.00 21.80  ? 249 GLN A OE1 1 
ATOM   3717 N NE2 . GLN B 1 262 ? -3.794  -7.248  6.803   1.00 21.68  ? 249 GLN A NE2 1 
ATOM   3718 N N   . ASN B 1 263 ? -2.242  -3.122  9.754   1.00 16.31  ? 250 ASN A N   1 
ATOM   3719 C CA  . ASN B 1 263 ? -2.135  -1.764  10.189  1.00 16.67  ? 250 ASN A CA  1 
ATOM   3720 C C   . ASN B 1 263 ? -3.556  -1.263  10.436  1.00 16.45  ? 250 ASN A C   1 
ATOM   3721 O O   . ASN B 1 263 ? -4.432  -1.553  9.657   1.00 18.47  ? 250 ASN A O   1 
ATOM   3722 C CB  . ASN B 1 263 ? -1.543  -0.905  9.063   1.00 15.43  ? 250 ASN A CB  1 
ATOM   3723 C CG  . ASN B 1 263 ? -0.048  -1.101  8.963   1.00 17.16  ? 250 ASN A CG  1 
ATOM   3724 O OD1 . ASN B 1 263 ? 0.640   -1.428  9.940   1.00 18.71  ? 250 ASN A OD1 1 
ATOM   3725 N ND2 . ASN B 1 263 ? 0.464   -0.850  7.786   1.00 24.85  ? 250 ASN A ND2 1 
ATOM   3726 N N   . PHE B 1 264 ? -3.773  -0.464  11.493  1.00 16.92  ? 251 PHE A N   1 
ATOM   3727 C CA  . PHE B 1 264 ? -5.073  0.250   11.697  1.00 15.60  ? 251 PHE A CA  1 
ATOM   3728 C C   . PHE B 1 264 ? -4.620  1.716   11.834  1.00 15.88  ? 251 PHE A C   1 
ATOM   3729 O O   . PHE B 1 264 ? -3.938  2.069   12.803  1.00 15.98  ? 251 PHE A O   1 
ATOM   3730 C CB  . PHE B 1 264 ? -5.601  -0.246  13.072  1.00 16.13  ? 251 PHE A CB  1 
ATOM   3731 C CG  . PHE B 1 264 ? -6.146  -1.662  12.872  1.00 21.42  ? 251 PHE A CG  1 
ATOM   3732 C CD1 . PHE B 1 264 ? -7.456  -1.906  12.478  1.00 27.47  ? 251 PHE A CD1 1 
ATOM   3733 C CD2 . PHE B 1 264 ? -5.293  -2.752  12.975  1.00 19.22  ? 251 PHE A CD2 1 
ATOM   3734 C CE1 . PHE B 1 264 ? -7.930  -3.232  12.273  1.00 28.05  ? 251 PHE A CE1 1 
ATOM   3735 C CE2 . PHE B 1 264 ? -5.745  -4.072  12.736  1.00 20.24  ? 251 PHE A CE2 1 
ATOM   3736 C CZ  . PHE B 1 264 ? -7.036  -4.311  12.384  1.00 23.12  ? 251 PHE A CZ  1 
ATOM   3737 N N   . VAL B 1 265 ? -5.029  2.571   10.901  1.00 13.76  ? 252 VAL A N   1 
ATOM   3738 C CA  . VAL B 1 265 ? -4.546  3.947   10.803  1.00 12.82  ? 252 VAL A CA  1 
ATOM   3739 C C   . VAL B 1 265 ? -5.621  4.891   11.287  1.00 14.37  ? 252 VAL A C   1 
ATOM   3740 O O   . VAL B 1 265 ? -6.768  4.881   10.763  1.00 17.40  ? 252 VAL A O   1 
ATOM   3741 C CB  . VAL B 1 265 ? -4.316  4.247   9.296   1.00 13.46  ? 252 VAL A CB  1 
ATOM   3742 C CG1 . VAL B 1 265 ? -3.741  5.688   9.170   1.00 15.03  ? 252 VAL A CG1 1 
ATOM   3743 C CG2 . VAL B 1 265 ? -3.290  3.218   8.701   1.00 13.58  ? 252 VAL A CG2 1 
ATOM   3744 N N   . VAL B 1 266 ? -5.240  5.747   12.231  1.00 13.43  ? 253 VAL A N   1 
ATOM   3745 C CA  . VAL B 1 266 ? -6.127  6.718   12.803  1.00 13.45  ? 253 VAL A CA  1 
ATOM   3746 C C   . VAL B 1 266 ? -5.473  8.071   12.484  1.00 16.06  ? 253 VAL A C   1 
ATOM   3747 O O   . VAL B 1 266 ? -4.602  8.509   13.246  1.00 16.32  ? 253 VAL A O   1 
ATOM   3748 C CB  . VAL B 1 266 ? -6.445  6.520   14.321  1.00 13.14  ? 253 VAL A CB  1 
ATOM   3749 C CG1 . VAL B 1 266 ? -5.210  6.312   15.203  1.00 16.55  ? 253 VAL A CG1 1 
ATOM   3750 C CG2 . VAL B 1 266 ? -7.357  7.699   14.831  1.00 16.29  ? 253 VAL A CG2 1 
ATOM   3751 N N   . ASP B 1 267 ? -5.782  8.689   11.312  1.00 17.37  ? 254 ASP A N   1 
ATOM   3752 C CA  . ASP B 1 267 ? -4.992  9.825   10.892  1.00 17.15  ? 254 ASP A CA  1 
ATOM   3753 C C   . ASP B 1 267 ? -5.843  10.895  10.234  1.00 19.83  ? 254 ASP A C   1 
ATOM   3754 O O   . ASP B 1 267 ? -5.303  11.850  9.658   1.00 18.34  ? 254 ASP A O   1 
ATOM   3755 C CB  . ASP B 1 267 ? -3.883  9.419   9.915   1.00 17.78  ? 254 ASP A CB  1 
ATOM   3756 C CG  . ASP B 1 267 ? -4.336  9.024   8.522   1.00 17.79  ? 254 ASP A CG  1 
ATOM   3757 O OD1 . ASP B 1 267 ? -5.579  8.760   8.329   1.00 17.91  ? 254 ASP A OD1 1 
ATOM   3758 O OD2 . ASP B 1 267 ? -3.478  8.997   7.599   1.00 17.91  ? 254 ASP A OD2 1 
ATOM   3759 N N   . ALA B 1 268 ? -7.192  10.770  10.296  1.00 16.95  ? 255 ALA A N   1 
ATOM   3760 C CA  . ALA B 1 268 ? -8.069  11.813  9.739   1.00 16.75  ? 255 ALA A CA  1 
ATOM   3761 C C   . ALA B 1 268 ? -7.789  12.086  8.274   1.00 18.26  ? 255 ALA A C   1 
ATOM   3762 O O   . ALA B 1 268 ? -8.125  13.152  7.749   1.00 18.31  ? 255 ALA A O   1 
ATOM   3763 C CB  . ALA B 1 268 ? -8.092  13.078  10.610  1.00 16.88  ? 255 ALA A CB  1 
ATOM   3764 N N   . GLY B 1 269 ? -7.245  11.067  7.575   1.00 17.87  ? 256 GLY A N   1 
ATOM   3765 C CA  . GLY B 1 269 ? -6.973  11.239  6.145   1.00 18.11  ? 256 GLY A CA  1 
ATOM   3766 C C   . GLY B 1 269 ? -5.620  11.920  5.816   1.00 18.20  ? 256 GLY A C   1 
ATOM   3767 O O   . GLY B 1 269 ? -5.400  12.092  4.612   1.00 17.87  ? 256 GLY A O   1 
ATOM   3768 N N   . LEU B 1 270 ? -4.732  12.212  6.790   1.00 16.83  ? 257 LEU A N   1 
ATOM   3769 C CA  . LEU B 1 270 ? -3.508  12.990  6.476   1.00 17.52  ? 257 LEU A CA  1 
ATOM   3770 C C   . LEU B 1 270 ? -2.584  12.200  5.539   1.00 19.36  ? 257 LEU A C   1 
ATOM   3771 O O   . LEU B 1 270 ? -1.847  12.820  4.748   1.00 19.81  ? 257 LEU A O   1 
ATOM   3772 C CB  . LEU B 1 270 ? -2.834  13.288  7.812   1.00 17.42  ? 257 LEU A CB  1 
ATOM   3773 C CG  . LEU B 1 270 ? -1.648  14.256  7.774   1.00 17.06  ? 257 LEU A CG  1 
ATOM   3774 C CD1 . LEU B 1 270 ? -2.117  15.615  7.224   1.00 19.64  ? 257 LEU A CD1 1 
ATOM   3775 C CD2 . LEU B 1 270 ? -1.016  14.408  9.157   1.00 18.27  ? 257 LEU A CD2 1 
ATOM   3776 N N   . SER B 1 271 ? -2.674  10.832  5.654   1.00 17.69  ? 258 SER A N   1 
ATOM   3777 C CA  . SER B 1 271 ? -1.770  10.034  4.779   1.00 17.27  ? 258 SER A CA  1 
ATOM   3778 C C   . SER B 1 271 ? -2.199  9.907   3.316   1.00 18.43  ? 258 SER A C   1 
ATOM   3779 O O   . SER B 1 271 ? -1.496  9.253   2.510   1.00 20.33  ? 258 SER A O   1 
ATOM   3780 C CB  . SER B 1 271 ? -1.557  8.681   5.407   1.00 16.46  ? 258 SER A CB  1 
ATOM   3781 O OG  . SER B 1 271 ? -2.703  7.842   5.354   1.00 17.85  ? 258 SER A OG  1 
ATOM   3782 N N   . ILE B 1 272 ? -3.409  10.437  2.964   1.00 18.16  ? 259 ILE A N   1 
ATOM   3783 C CA  . ILE B 1 272 ? -3.935  10.260  1.607   1.00 18.52  ? 259 ILE A CA  1 
ATOM   3784 C C   . ILE B 1 272 ? -4.175  11.638  1.018   1.00 20.20  ? 259 ILE A C   1 
ATOM   3785 O O   . ILE B 1 272 ? -5.274  12.198  1.127   1.00 24.64  ? 259 ILE A O   1 
ATOM   3786 C CB  . ILE B 1 272 ? -5.205  9.401   1.629   1.00 17.36  ? 259 ILE A CB  1 
ATOM   3787 C CG1 . ILE B 1 272 ? -4.904  8.038   2.220   1.00 19.03  ? 259 ILE A CG1 1 
ATOM   3788 C CG2 . ILE B 1 272 ? -5.781  9.265   0.197   1.00 18.81  ? 259 ILE A CG2 1 
ATOM   3789 C CD1 . ILE B 1 272 ? -6.204  7.234   2.412   1.00 21.21  ? 259 ILE A CD1 1 
ATOM   3790 N N   . GLN B 1 273 ? -3.126  12.163  0.471   1.00 20.71  ? 260 GLN A N   1 
ATOM   3791 C CA  . GLN B 1 273 ? -3.285  13.522  -0.062  1.00 26.31  ? 260 GLN A CA  1 
ATOM   3792 C C   . GLN B 1 273 ? -2.808  13.631  -1.519  1.00 26.52  ? 260 GLN A C   1 
ATOM   3793 O O   . GLN B 1 273 ? -3.177  14.661  -2.074  1.00 26.11  ? 260 GLN A O   1 
ATOM   3794 C CB  . GLN B 1 273 ? -2.334  14.527  0.565   1.00 28.43  ? 260 GLN A CB  1 
ATOM   3795 C CG  . GLN B 1 273 ? -2.565  14.729  2.058   1.00 33.45  ? 260 GLN A CG  1 
ATOM   3796 C CD  . GLN B 1 273 ? -1.569  15.695  2.660   1.00 29.36  ? 260 GLN A CD  1 
ATOM   3797 O OE1 . GLN B 1 273 ? -1.290  16.773  2.128   1.00 31.63  ? 260 GLN A OE1 1 
ATOM   3798 N NE2 . GLN B 1 273 ? -1.100  15.372  3.854   1.00 31.53  ? 260 GLN A NE2 1 
ATOM   3799 O OXT . GLN B 1 273 ? -2.025  12.722  -1.981  1.00 27.03  ? 260 GLN A OXT 1 
HETATM 3800 O O   . HOH C 2 .   ? -41.308 -9.064  9.394   1.00 42.92  ? 301 HOH B O   1 
HETATM 3801 O O   . HOH C 2 .   ? -15.984 -10.239 28.018  1.00 38.21  ? 302 HOH B O   1 
HETATM 3802 O O   . HOH C 2 .   ? -36.425 -4.082  18.144  1.00 36.27  ? 303 HOH B O   1 
HETATM 3803 O O   . HOH C 2 .   ? -32.426 -0.709  18.570  1.00 33.61  ? 304 HOH B O   1 
HETATM 3804 O O   . HOH C 2 .   ? -12.807 -11.661 1.732   1.00 44.93  ? 305 HOH B O   1 
HETATM 3805 O O   . HOH C 2 .   ? -39.348 -5.649  12.488  1.00 38.95  ? 306 HOH B O   1 
HETATM 3806 O O   . HOH C 2 .   ? 0.532   -20.590 10.150  1.00 39.92  ? 307 HOH B O   1 
HETATM 3807 O O   . HOH C 2 .   ? -3.848  -7.449  3.867   1.00 28.15  ? 308 HOH B O   1 
HETATM 3808 O O   . HOH C 2 .   ? -19.129 18.489  10.345  1.00 38.51  ? 309 HOH B O   1 
HETATM 3809 O O   . HOH C 2 .   ? -10.206 -8.662  -9.964  1.00 20.03  ? 310 HOH B O   1 
HETATM 3810 O O   . HOH C 2 .   ? -25.772 19.679  13.441  1.00 34.60  ? 311 HOH B O   1 
HETATM 3811 O O   . HOH C 2 .   ? -15.476 17.666  2.093   1.00 39.12  ? 312 HOH B O   1 
HETATM 3812 O O   . HOH C 2 .   ? -17.298 16.404  -6.376  1.00 35.68  ? 313 HOH B O   1 
HETATM 3813 O O   . HOH C 2 .   ? -15.569 12.315  12.486  1.00 36.66  ? 314 HOH B O   1 
HETATM 3814 O O   . HOH C 2 .   ? -7.586  2.964   1.925   1.00 18.10  ? 315 HOH B O   1 
HETATM 3815 O O   . HOH C 2 .   ? -14.355 10.904  -5.909  1.00 25.96  ? 316 HOH B O   1 
HETATM 3816 O O   . HOH C 2 .   ? -11.704 -18.149 8.827   1.00 27.31  ? 317 HOH B O   1 
HETATM 3817 O O   . HOH C 2 .   ? -1.195  -24.579 10.253  1.00 36.36  ? 318 HOH B O   1 
HETATM 3818 O O   . HOH C 2 .   ? -24.636 13.138  -2.847  1.00 36.52  ? 319 HOH B O   1 
HETATM 3819 O O   . HOH C 2 .   ? -28.355 8.134   -5.131  1.00 37.56  ? 320 HOH B O   1 
HETATM 3820 O O   . HOH C 2 .   ? -13.722 11.463  5.291   1.00 18.91  ? 321 HOH B O   1 
HETATM 3821 O O   . HOH C 2 .   ? -12.437 -10.559 15.278  1.00 24.25  ? 322 HOH B O   1 
HETATM 3822 O O   . HOH C 2 .   ? -25.789 2.041   22.894  1.00 28.01  ? 323 HOH B O   1 
HETATM 3823 O O   . HOH C 2 .   ? -12.665 -14.930 -13.304 1.00 26.91  ? 324 HOH B O   1 
HETATM 3824 O O   . HOH C 2 .   ? -24.237 -5.588  19.720  1.00 27.67  ? 325 HOH B O   1 
HETATM 3825 O O   . HOH C 2 .   ? -9.885  1.656   0.963   1.00 21.60  ? 326 HOH B O   1 
HETATM 3826 O O   . HOH C 2 .   ? -9.925  18.402  2.461   1.00 33.08  ? 327 HOH B O   1 
HETATM 3827 O O   . HOH C 2 .   ? -17.664 11.371  10.936  1.00 36.06  ? 328 HOH B O   1 
HETATM 3828 O O   . HOH C 2 .   ? -26.081 7.692   21.037  1.00 29.80  ? 329 HOH B O   1 
HETATM 3829 O O   . HOH C 2 .   ? -6.819  -9.359  10.161  1.00 17.08  ? 330 HOH B O   1 
HETATM 3830 O O   . HOH C 2 .   ? -25.252 -0.769  -0.794  1.00 27.20  ? 331 HOH B O   1 
HETATM 3831 O O   . HOH C 2 .   ? -22.444 8.450   12.204  1.00 29.47  ? 332 HOH B O   1 
HETATM 3832 O O   . HOH C 2 .   ? -23.335 -2.512  -15.404 1.00 32.34  ? 333 HOH B O   1 
HETATM 3833 O O   . HOH C 2 .   ? -9.738  -15.513 6.815   1.00 22.86  ? 334 HOH B O   1 
HETATM 3834 O O   . HOH C 2 .   ? -23.959 10.644  12.595  1.00 35.07  ? 335 HOH B O   1 
HETATM 3835 O O   . HOH C 2 .   ? -20.743 -4.604  -2.738  1.00 30.05  ? 336 HOH B O   1 
HETATM 3836 O O   . HOH C 2 .   ? -14.724 17.402  9.000   1.00 29.41  ? 337 HOH B O   1 
HETATM 3837 O O   . HOH C 2 .   ? -10.905 8.444   16.471  1.00 26.87  ? 338 HOH B O   1 
HETATM 3838 O O   . HOH C 2 .   ? -19.588 -12.592 -8.874  1.00 34.38  ? 339 HOH B O   1 
HETATM 3839 O O   . HOH C 2 .   ? -7.237  13.164  -1.021  1.00 36.67  ? 340 HOH B O   1 
HETATM 3840 O O   . HOH C 2 .   ? -20.052 -7.476  0.568   1.00 29.06  ? 341 HOH B O   1 
HETATM 3841 O O   . HOH C 2 .   ? -9.848  5.991   17.042  1.00 20.80  ? 342 HOH B O   1 
HETATM 3842 O O   . HOH C 2 .   ? -16.265 -8.904  21.695  1.00 47.48  ? 343 HOH B O   1 
HETATM 3843 O O   . HOH C 2 .   ? -6.202  1.194   8.588   1.00 20.67  ? 344 HOH B O   1 
HETATM 3844 O O   . HOH C 2 .   ? -2.642  -10.209 -0.233  1.00 35.84  ? 345 HOH B O   1 
HETATM 3845 O O   . HOH C 2 .   ? -26.864 -1.096  -9.307  1.00 34.19  ? 346 HOH B O   1 
HETATM 3846 O O   . HOH C 2 .   ? -12.135 16.567  2.978   1.00 25.54  ? 347 HOH B O   1 
HETATM 3847 O O   . HOH C 2 .   ? -6.358  -3.386  8.471   1.00 19.93  ? 348 HOH B O   1 
HETATM 3848 O O   . HOH C 2 .   ? -14.963 17.622  -3.425  1.00 33.84  ? 349 HOH B O   1 
HETATM 3849 O O   . HOH C 2 .   ? -11.154 -13.295 -9.696  1.00 21.19  ? 350 HOH B O   1 
HETATM 3850 O O   . HOH C 2 .   ? -15.749 -6.841  25.396  1.00 24.07  ? 351 HOH B O   1 
HETATM 3851 O O   . HOH C 2 .   ? -11.430 -2.003  0.331   1.00 30.52  ? 352 HOH B O   1 
HETATM 3852 O O   . HOH C 2 .   ? -28.954 10.483  5.176   1.00 31.92  ? 353 HOH B O   1 
HETATM 3853 O O   . HOH C 2 .   ? -7.309  -29.527 4.239   1.00 48.57  ? 354 HOH B O   1 
HETATM 3854 O O   . HOH C 2 .   ? -23.467 -5.653  23.923  1.00 36.21  ? 355 HOH B O   1 
HETATM 3855 O O   . HOH C 2 .   ? -21.188 -15.136 -18.820 1.00 41.29  ? 356 HOH B O   1 
HETATM 3856 O O   . HOH C 2 .   ? -24.086 -13.350 19.274  1.00 44.66  ? 357 HOH B O   1 
HETATM 3857 O O   . HOH C 2 .   ? -25.485 -12.603 22.017  1.00 47.52  ? 358 HOH B O   1 
HETATM 3858 O O   . HOH C 2 .   ? 1.298   -12.265 0.664   1.00 26.80  ? 359 HOH B O   1 
HETATM 3859 O O   . HOH C 2 .   ? -11.674 -4.358  -0.820  1.00 26.75  ? 360 HOH B O   1 
HETATM 3860 O O   . HOH C 2 .   ? -30.239 -9.565  17.763  1.00 48.93  ? 361 HOH B O   1 
HETATM 3861 O O   . HOH C 2 .   ? -22.803 -12.895 3.824   1.00 31.84  ? 362 HOH B O   1 
HETATM 3862 O O   . HOH C 2 .   ? -16.391 4.095   8.856   1.00 22.37  ? 363 HOH B O   1 
HETATM 3863 O O   . HOH C 2 .   ? -1.880  7.592   -0.348  1.00 34.38  ? 364 HOH B O   1 
HETATM 3864 O O   . HOH C 2 .   ? -6.011  1.479   3.615   1.00 26.72  ? 365 HOH B O   1 
HETATM 3865 O O   . HOH C 2 .   ? -30.730 -6.531  -3.614  1.00 42.26  ? 366 HOH B O   1 
HETATM 3866 O O   . HOH C 2 .   ? -18.249 -1.578  -16.478 1.00 20.65  ? 367 HOH B O   1 
HETATM 3867 O O   . HOH C 2 .   ? -24.146 -10.703 3.648   1.00 28.55  ? 368 HOH B O   1 
HETATM 3868 O O   . HOH C 2 .   ? -12.097 -33.826 6.034   1.00 42.17  ? 369 HOH B O   1 
HETATM 3869 O O   . HOH C 2 .   ? -9.877  -26.975 14.032  1.00 45.97  ? 370 HOH B O   1 
HETATM 3870 O O   . HOH C 2 .   ? -4.443  -27.412 6.387   1.00 46.95  ? 371 HOH B O   1 
HETATM 3871 O O   . HOH C 2 .   ? -0.808  5.718   -1.400  1.00 32.95  ? 372 HOH B O   1 
HETATM 3872 O O   . HOH C 2 .   ? -8.766  -21.915 0.067   1.00 33.94  ? 373 HOH B O   1 
HETATM 3873 O O   . HOH C 2 .   ? -16.357 -11.465 30.426  1.00 41.00  ? 374 HOH B O   1 
HETATM 3874 O O   . HOH C 2 .   ? -11.929 -25.787 13.392  1.00 44.89  ? 375 HOH B O   1 
HETATM 3875 O O   . HOH C 2 .   ? -35.704 8.726   -6.666  1.00 40.35  ? 376 HOH B O   1 
HETATM 3876 O O   . HOH D 2 .   ? 3.986   -0.872  13.851  1.00 36.79  ? 301 HOH A O   1 
HETATM 3877 O O   . HOH D 2 .   ? -4.504  -11.965 32.778  1.00 32.75  ? 302 HOH A O   1 
HETATM 3878 O O   . HOH D 2 .   ? 6.854   -14.488 28.997  1.00 32.63  ? 303 HOH A O   1 
HETATM 3879 O O   . HOH D 2 .   ? 6.591   9.045   28.143  1.00 40.99  ? 304 HOH A O   1 
HETATM 3880 O O   . HOH D 2 .   ? -17.420 -4.170  18.696  1.00 27.37  ? 305 HOH A O   1 
HETATM 3881 O O   . HOH D 2 .   ? -8.722  -10.181 23.497  1.00 35.36  ? 306 HOH A O   1 
HETATM 3882 O O   . HOH D 2 .   ? -3.657  13.550  11.264  1.00 20.19  ? 307 HOH A O   1 
HETATM 3883 O O   . HOH D 2 .   ? -12.642 2.072   22.049  1.00 23.06  ? 308 HOH A O   1 
HETATM 3884 O O   . HOH D 2 .   ? 12.779  6.683   6.677   1.00 21.69  ? 309 HOH A O   1 
HETATM 3885 O O   . HOH D 2 .   ? 0.086   11.750  41.524  1.00 36.35  ? 310 HOH A O   1 
HETATM 3886 O O   . HOH D 2 .   ? 22.193  20.230  8.124   1.00 39.13  ? 311 HOH A O   1 
HETATM 3887 O O   . HOH D 2 .   ? -5.082  -12.998 26.510  1.00 30.11  ? 312 HOH A O   1 
HETATM 3888 O O   . HOH D 2 .   ? -0.968  -13.600 14.701  1.00 19.00  ? 313 HOH A O   1 
HETATM 3889 O O   . HOH D 2 .   ? -4.715  16.105  13.752  1.00 19.15  ? 314 HOH A O   1 
HETATM 3890 O O   . HOH D 2 .   ? 2.678   -14.933 6.777   1.00 40.85  ? 315 HOH A O   1 
HETATM 3891 O O   . HOH D 2 .   ? 8.360   -1.314  23.973  1.00 22.52  ? 316 HOH A O   1 
HETATM 3892 O O   . HOH D 2 .   ? 1.993   -3.687  9.837   1.00 22.33  ? 317 HOH A O   1 
HETATM 3893 O O   . HOH D 2 .   ? -1.751  12.143  27.701  1.00 33.33  ? 318 HOH A O   1 
HETATM 3894 O O   . HOH D 2 .   ? -11.549 3.593   29.017  1.00 21.68  ? 319 HOH A O   1 
HETATM 3895 O O   . HOH D 2 .   ? 6.642   -18.077 22.960  1.00 34.69  ? 320 HOH A O   1 
HETATM 3896 O O   . HOH D 2 .   ? -2.581  5.236   4.850   1.00 27.43  ? 321 HOH A O   1 
HETATM 3897 O O   . HOH D 2 .   ? -14.069 -4.181  31.395  1.00 29.99  ? 322 HOH A O   1 
HETATM 3898 O O   . HOH D 2 .   ? 5.923   -20.717 26.521  1.00 36.65  ? 323 HOH A O   1 
HETATM 3899 O O   . HOH D 2 .   ? 0.505   -5.058  7.813   1.00 18.61  ? 324 HOH A O   1 
HETATM 3900 O O   . HOH D 2 .   ? -1.894  -12.701 33.726  1.00 30.70  ? 325 HOH A O   1 
HETATM 3901 O O   . HOH D 2 .   ? 2.439   9.621   12.714  1.00 35.52  ? 326 HOH A O   1 
HETATM 3902 O O   . HOH D 2 .   ? -1.191  10.339  -1.040  1.00 28.26  ? 327 HOH A O   1 
HETATM 3903 O O   . HOH D 2 .   ? -3.756  -9.756  7.813   1.00 26.56  ? 328 HOH A O   1 
HETATM 3904 O O   . HOH D 2 .   ? 12.424  11.181  7.886   1.00 18.54  ? 329 HOH A O   1 
HETATM 3905 O O   . HOH D 2 .   ? 25.269  5.403   20.182  1.00 40.92  ? 330 HOH A O   1 
HETATM 3906 O O   . HOH D 2 .   ? 5.490   5.480   19.467  1.00 24.57  ? 331 HOH A O   1 
HETATM 3907 O O   . HOH D 2 .   ? -8.364  6.384   34.032  1.00 30.25  ? 332 HOH A O   1 
HETATM 3908 O O   . HOH D 2 .   ? -1.852  31.834  13.995  1.00 39.25  ? 333 HOH A O   1 
HETATM 3909 O O   . HOH D 2 .   ? 3.636   7.501   21.083  1.00 29.35  ? 334 HOH A O   1 
HETATM 3910 O O   . HOH D 2 .   ? -6.384  19.509  1.437   1.00 29.09  ? 335 HOH A O   1 
HETATM 3911 O O   . HOH D 2 .   ? -16.096 6.831   21.928  1.00 33.55  ? 336 HOH A O   1 
HETATM 3912 O O   . HOH D 2 .   ? -22.287 8.477   23.477  1.00 36.69  ? 337 HOH A O   1 
HETATM 3913 O O   . HOH D 2 .   ? -8.267  -1.056  36.524  1.00 25.96  ? 338 HOH A O   1 
HETATM 3914 O O   . HOH D 2 .   ? -9.576  22.514  4.157   1.00 30.48  ? 339 HOH A O   1 
HETATM 3915 O O   . HOH D 2 .   ? -3.567  14.608  23.371  1.00 25.35  ? 340 HOH A O   1 
HETATM 3916 O O   . HOH D 2 .   ? 13.578  -10.302 25.454  1.00 32.14  ? 341 HOH A O   1 
HETATM 3917 O O   . HOH D 2 .   ? 3.796   -12.727 29.233  1.00 28.96  ? 342 HOH A O   1 
HETATM 3918 O O   . HOH D 2 .   ? -7.588  7.304   9.532   1.00 15.19  ? 343 HOH A O   1 
HETATM 3919 O O   . HOH D 2 .   ? -13.196 -8.083  14.504  1.00 25.48  ? 344 HOH A O   1 
HETATM 3920 O O   . HOH D 2 .   ? 14.196  10.886  16.141  1.00 30.63  ? 345 HOH A O   1 
HETATM 3921 O O   . HOH D 2 .   ? 9.710   -12.954 12.095  1.00 25.82  ? 346 HOH A O   1 
HETATM 3922 O O   . HOH D 2 .   ? -19.629 4.765   22.592  1.00 23.94  ? 347 HOH A O   1 
HETATM 3923 O O   . HOH D 2 .   ? 12.809  4.282   28.256  1.00 33.75  ? 348 HOH A O   1 
HETATM 3924 O O   . HOH D 2 .   ? -7.190  -9.095  25.670  1.00 35.94  ? 349 HOH A O   1 
HETATM 3925 O O   . HOH D 2 .   ? -6.318  7.764   5.846   1.00 29.79  ? 350 HOH A O   1 
HETATM 3926 O O   . HOH D 2 .   ? -6.333  1.349   40.489  1.00 35.11  ? 351 HOH A O   1 
HETATM 3927 O O   . HOH D 2 .   ? -3.997  -19.477 16.677  1.00 30.50  ? 352 HOH A O   1 
HETATM 3928 O O   . HOH D 2 .   ? -7.199  -14.550 18.864  1.00 34.00  ? 353 HOH A O   1 
HETATM 3929 O O   . HOH D 2 .   ? 8.761   2.760   18.749  1.00 32.87  ? 354 HOH A O   1 
HETATM 3930 O O   . HOH D 2 .   ? 3.042   -0.220  11.033  1.00 27.02  ? 355 HOH A O   1 
HETATM 3931 O O   . HOH D 2 .   ? -10.147 14.466  18.156  1.00 30.63  ? 356 HOH A O   1 
HETATM 3932 O O   . HOH D 2 .   ? 10.358  -15.624 23.010  1.00 39.73  ? 357 HOH A O   1 
HETATM 3933 O O   . HOH D 2 .   ? 16.515  -4.474  37.188  1.00 35.74  ? 358 HOH A O   1 
HETATM 3934 O O   . HOH D 2 .   ? 16.757  -1.087  22.808  1.00 25.68  ? 359 HOH A O   1 
HETATM 3935 O O   . HOH D 2 .   ? 0.012   2.153   41.674  1.00 45.68  ? 360 HOH A O   1 
HETATM 3936 O O   . HOH D 2 .   ? 16.554  1.602   33.225  1.00 36.26  ? 361 HOH A O   1 
HETATM 3937 O O   . HOH D 2 .   ? 24.522  12.559  14.612  1.00 38.90  ? 362 HOH A O   1 
HETATM 3938 O O   . HOH D 2 .   ? -12.388 -9.712  31.083  1.00 24.46  ? 363 HOH A O   1 
HETATM 3939 O O   . HOH D 2 .   ? 16.531  12.917  8.221   1.00 25.14  ? 364 HOH A O   1 
HETATM 3940 O O   . HOH D 2 .   ? 0.815   -18.700 12.336  1.00 29.49  ? 365 HOH A O   1 
HETATM 3941 O O   . HOH D 2 .   ? 3.203   10.698  22.970  1.00 26.92  ? 366 HOH A O   1 
HETATM 3942 O O   . HOH D 2 .   ? 1.826   21.648  10.355  1.00 27.45  ? 367 HOH A O   1 
HETATM 3943 O O   . HOH D 2 .   ? 12.053  13.552  32.163  1.00 39.92  ? 368 HOH A O   1 
HETATM 3944 O O   . HOH D 2 .   ? 22.049  -9.343  33.463  1.00 34.89  ? 369 HOH A O   1 
HETATM 3945 O O   . HOH D 2 .   ? 1.878   17.464  7.311   1.00 30.04  ? 370 HOH A O   1 
HETATM 3946 O O   . HOH D 2 .   ? -6.723  13.358  24.857  1.00 27.36  ? 371 HOH A O   1 
HETATM 3947 O O   . HOH D 2 .   ? 2.677   12.195  35.954  1.00 34.18  ? 372 HOH A O   1 
HETATM 3948 O O   . HOH D 2 .   ? -12.887 11.155  30.934  1.00 46.11  ? 373 HOH A O   1 
HETATM 3949 O O   . HOH D 2 .   ? 17.269  -12.356 24.360  1.00 34.65  ? 374 HOH A O   1 
HETATM 3950 O O   . HOH D 2 .   ? -9.636  20.821  16.240  1.00 32.33  ? 375 HOH A O   1 
HETATM 3951 O O   . HOH D 2 .   ? 3.944   8.208   24.602  1.00 25.08  ? 376 HOH A O   1 
HETATM 3952 O O   . HOH D 2 .   ? 3.805   1.823   40.881  1.00 30.50  ? 377 HOH A O   1 
HETATM 3953 O O   . HOH D 2 .   ? 4.439   2.082   10.954  1.00 24.43  ? 378 HOH A O   1 
HETATM 3954 O O   . HOH D 2 .   ? -5.675  1.841   45.001  1.00 36.42  ? 379 HOH A O   1 
HETATM 3955 O O   . HOH D 2 .   ? -3.607  -6.213  18.395  1.00 24.60  ? 380 HOH A O   1 
HETATM 3956 O O   . HOH D 2 .   ? -5.066  -10.764 24.868  1.00 30.51  ? 381 HOH A O   1 
HETATM 3957 O O   . HOH D 2 .   ? 9.537   -7.834  41.275  1.00 54.40  ? 382 HOH A O   1 
HETATM 3958 O O   . HOH D 2 .   ? -10.118 24.709  13.311  1.00 48.04  ? 383 HOH A O   1 
HETATM 3959 O O   . HOH D 2 .   ? -4.647  -0.821  6.766   1.00 37.05  ? 384 HOH A O   1 
HETATM 3960 O O   . HOH D 2 .   ? 8.295   -9.539  42.031  1.00 45.70  ? 385 HOH A O   1 
HETATM 3961 O O   . HOH D 2 .   ? 7.735   -1.077  5.711   1.00 28.72  ? 386 HOH A O   1 
HETATM 3962 O O   . HOH D 2 .   ? 13.783  10.140  36.337  1.00 36.85  ? 387 HOH A O   1 
HETATM 3963 O O   . HOH D 2 .   ? -1.566  -3.514  6.727   1.00 23.89  ? 388 HOH A O   1 
HETATM 3964 O O   . HOH D 2 .   ? -16.473 11.534  20.804  1.00 38.49  ? 389 HOH A O   1 
HETATM 3965 O O   . HOH D 2 .   ? 1.897   12.641  15.855  1.00 30.90  ? 390 HOH A O   1 
HETATM 3966 O O   . HOH D 2 .   ? 20.917  -0.605  12.279  1.00 29.16  ? 391 HOH A O   1 
HETATM 3967 O O   . HOH D 2 .   ? -10.605 24.878  10.007  1.00 35.07  ? 392 HOH A O   1 
HETATM 3968 O O   . HOH D 2 .   ? 1.525   12.389  11.233  1.00 34.43  ? 393 HOH A O   1 
HETATM 3969 O O   . HOH D 2 .   ? -0.814  -1.890  4.926   1.00 33.83  ? 394 HOH A O   1 
HETATM 3970 O O   . HOH D 2 .   ? 19.805  17.215  5.462   1.00 29.10  ? 395 HOH A O   1 
HETATM 3971 O O   . HOH D 2 .   ? 10.322  5.748   27.902  1.00 31.04  ? 396 HOH A O   1 
HETATM 3972 O O   . HOH D 2 .   ? 2.945   15.393  9.936   1.00 37.80  ? 397 HOH A O   1 
HETATM 3973 O O   . HOH D 2 .   ? -2.561  -24.222 16.515  1.00 50.29  ? 398 HOH A O   1 
HETATM 3974 O O   . HOH D 2 .   ? 18.269  -4.888  35.063  1.00 35.82  ? 399 HOH A O   1 
HETATM 3975 O O   . HOH D 2 .   ? -9.808  5.176   36.280  1.00 34.21  ? 400 HOH A O   1 
HETATM 3976 O O   . HOH D 2 .   ? 5.493   3.779   41.436  1.00 32.79  ? 401 HOH A O   1 
HETATM 3977 O O   . HOH D 2 .   ? 13.214  -12.298 27.597  1.00 43.08  ? 402 HOH A O   1 
HETATM 3978 O O   . HOH D 2 .   ? 18.326  -1.023  13.410  1.00 27.82  ? 403 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 14  ? 0.4382 0.8759 0.4502 -0.3155 0.1178  0.0005  1   MET B N   
2    C CA  . MET A 14  ? 0.5729 1.0009 0.5932 -0.2881 0.1074  -0.0049 1   MET B CA  
3    C C   . MET A 14  ? 0.5892 0.9562 0.5959 -0.2709 0.1039  0.0038  1   MET B C   
4    O O   . MET A 14  ? 0.5625 0.9189 0.5616 -0.2609 0.1057  0.0117  1   MET B O   
5    C CB  . MET A 14  ? 0.5912 1.0764 0.6294 -0.2660 0.1029  -0.0121 1   MET B CB  
6    N N   . ASN A 15  ? 0.5988 0.9292 0.6029 -0.2662 0.0986  0.0015  2   ASN B N   
7    C CA  . ASN A 15  ? 0.6440 0.9166 0.6352 -0.2535 0.0955  0.0086  2   ASN B CA  
8    C C   . ASN A 15  ? 0.5343 0.8097 0.5330 -0.2221 0.0877  0.0075  2   ASN B C   
9    O O   . ASN A 15  ? 0.4767 0.7753 0.4885 -0.2099 0.0818  -0.0007 2   ASN B O   
10   C CB  . ASN A 15  ? 0.7270 0.9634 0.7133 -0.2615 0.0933  0.0050  2   ASN B CB  
11   C CG  . ASN A 15  ? 0.8995 1.1290 0.8782 -0.2937 0.1005  0.0033  2   ASN B CG  
12   O OD1 . ASN A 15  ? 0.9382 1.2099 0.9239 -0.3115 0.1051  -0.0007 2   ASN B OD1 
13   N ND2 . ASN A 15  ? 1.0713 1.2482 1.0355 -0.3017 0.1017  0.0055  2   ASN B ND2 
14   N N   . ARG A 16  ? 0.4852 0.7348 0.4738 -0.2104 0.0879  0.0161  3   ARG B N   
15   C CA  . ARG A 16  ? 0.4761 0.7292 0.4691 -0.1840 0.0824  0.0159  3   ARG B CA  
16   C C   . ARG A 16  ? 0.3818 0.5968 0.3725 -0.1708 0.0759  0.0157  3   ARG B C   
17   O O   . ARG A 16  ? 0.3513 0.5736 0.3501 -0.1506 0.0699  0.0115  3   ARG B O   
18   C CB  . ARG A 16  ? 0.5244 0.7749 0.5072 -0.1820 0.0867  0.0244  3   ARG B CB  
19   C CG  . ARG A 16  ? 0.5633 0.8567 0.5505 -0.1803 0.0905  0.0236  3   ARG B CG  
20   C CD  . ARG A 16  ? 0.5077 0.7829 0.4821 -0.1715 0.0919  0.0323  3   ARG B CD  
21   N N   . HIS A 17  ? 0.3466 0.5203 0.3252 -0.1820 0.0775  0.0203  4   HIS B N   
22   C CA  . HIS A 17  ? 0.3727 0.5075 0.3466 -0.1699 0.0724  0.0215  4   HIS B CA  
23   C C   . HIS A 17  ? 0.4257 0.5404 0.3924 -0.1522 0.0701  0.0286  4   HIS B C   
24   O O   . HIS A 17  ? 0.4489 0.5287 0.4080 -0.1453 0.0675  0.0321  4   HIS B O   
25   C CB  . HIS A 17  ? 0.3516 0.4982 0.3387 -0.1600 0.0658  0.0121  4   HIS B CB  
26   C CG  . HIS A 17  ? 0.3807 0.5418 0.3718 -0.1791 0.0680  0.0056  4   HIS B CG  
27   N ND1 . HIS A 17  ? 0.4199 0.5484 0.4007 -0.1944 0.0705  0.0061  4   HIS B ND1 
28   C CD2 . HIS A 17  ? 0.4099 0.6155 0.4121 -0.1883 0.0694  -0.0011 4   HIS B CD2 
29   C CE1 . HIS A 17  ? 0.3858 0.5378 0.3720 -0.2129 0.0728  -0.0013 4   HIS B CE1 
30   N NE2 . HIS A 17  ? 0.4156 0.6162 0.4153 -0.2098 0.0721  -0.0055 4   HIS B NE2 
31   N N   . THR A 18  ? 0.3860 0.5251 0.3556 -0.1435 0.0705  0.0296  5   THR B N   
32   C CA  . THR A 18  ? 0.3277 0.4524 0.2907 -0.1281 0.0681  0.0349  5   THR B CA  
33   C C   . THR A 18  ? 0.3336 0.4829 0.2937 -0.1295 0.0724  0.0380  5   THR B C   
34   O O   . THR A 18  ? 0.3536 0.5373 0.3217 -0.1365 0.0753  0.0334  5   THR B O   
35   C CB  . THR A 18  ? 0.3036 0.4311 0.2763 -0.1086 0.0609  0.0284  5   THR B CB  
36   O OG1 . THR A 18  ? 0.3114 0.4238 0.2762 -0.0974 0.0592  0.0334  5   THR B OG1 
37   C CG2 . THR A 18  ? 0.2959 0.4603 0.2823 -0.1016 0.0593  0.0197  5   THR B CG2 
38   N N   . ASP A 19  ? 0.3484 0.4837 0.2976 -0.1221 0.0726  0.0452  6   ASP B N   
39   C CA  . ASP A 19  ? 0.3720 0.5343 0.3197 -0.1188 0.0753  0.0462  6   ASP B CA  
40   C C   . ASP A 19  ? 0.3235 0.5020 0.2798 -0.0994 0.0698  0.0381  6   ASP B C   
41   O O   . ASP A 19  ? 0.2872 0.4901 0.2433 -0.0946 0.0716  0.0362  6   ASP B O   
42   C CB  . ASP A 19  ? 0.4207 0.5658 0.3507 -0.1229 0.0794  0.0583  6   ASP B CB  
43   C CG  . ASP A 19  ? 0.4820 0.5933 0.4031 -0.1112 0.0748  0.0636  6   ASP B CG  
44   O OD1 . ASP A 19  ? 0.4724 0.5715 0.4011 -0.1025 0.0690  0.0580  6   ASP B OD1 
45   O OD2 . ASP A 19  ? 0.5430 0.6421 0.4493 -0.1098 0.0770  0.0736  6   ASP B OD2 
46   N N   . THR A 20  ? 0.3233 0.4864 0.2856 -0.0884 0.0636  0.0332  7   THR B N   
47   C CA  . THR A 20  ? 0.2776 0.4516 0.2470 -0.0719 0.0590  0.0252  7   THR B CA  
48   C C   . THR A 20  ? 0.2796 0.4880 0.2601 -0.0690 0.0603  0.0166  7   THR B C   
49   O O   . THR A 20  ? 0.2957 0.5168 0.2828 -0.0777 0.0620  0.0149  7   THR B O   
50   C CB  . THR A 20  ? 0.2668 0.4175 0.2405 -0.0645 0.0533  0.0225  7   THR B CB  
51   O OG1 . THR A 20  ? 0.2994 0.4230 0.2624 -0.0652 0.0525  0.0304  7   THR B OG1 
52   C CG2 . THR A 20  ? 0.2323 0.3878 0.2120 -0.0491 0.0489  0.0145  7   THR B CG2 
53   N N   . HIS A 21  ? 0.2455 0.4685 0.2276 -0.0562 0.0592  0.0105  8   HIS B N   
54   C CA  . HIS A 21  ? 0.2353 0.4898 0.2261 -0.0491 0.0604  0.0022  8   HIS B CA  
55   C C   . HIS A 21  ? 0.2456 0.4927 0.2410 -0.0320 0.0557  -0.0058 8   HIS B C   
56   O O   . HIS A 21  ? 0.2284 0.4614 0.2181 -0.0240 0.0536  -0.0075 8   HIS B O   
57   C CB  . HIS A 21  ? 0.3320 0.6117 0.3177 -0.0491 0.0651  0.0020  8   HIS B CB  
58   C CG  . HIS A 21  ? 0.3845 0.6985 0.3792 -0.0407 0.0668  -0.0067 8   HIS B CG  
59   N ND1 . HIS A 21  ? 0.4652 0.7959 0.4577 -0.0283 0.0680  -0.0132 8   HIS B ND1 
60   C CD2 . HIS A 21  ? 0.4028 0.7381 0.4084 -0.0408 0.0670  -0.0108 8   HIS B CD2 
61   C CE1 . HIS A 21  ? 0.4306 0.7913 0.4318 -0.0205 0.0695  -0.0203 8   HIS B CE1 
62   N NE2 . HIS A 21  ? 0.4588 0.8233 0.4683 -0.0275 0.0686  -0.0186 8   HIS B NE2 
63   N N   . TYR A 22  ? 0.2125 0.4659 0.2172 -0.0274 0.0539  -0.0102 9   TYR B N   
64   C CA  . TYR A 22  ? 0.1879 0.4327 0.1956 -0.0112 0.0503  -0.0169 9   TYR B CA  
65   C C   . TYR A 22  ? 0.2273 0.5013 0.2394 0.0005  0.0524  -0.0241 9   TYR B C   
66   O O   . TYR A 22  ? 0.2301 0.5250 0.2501 0.0016  0.0528  -0.0257 9   TYR B O   
67   C CB  . TYR A 22  ? 0.1890 0.4182 0.2021 -0.0105 0.0465  -0.0162 9   TYR B CB  
68   C CG  . TYR A 22  ? 0.1947 0.3941 0.2039 -0.0194 0.0441  -0.0101 9   TYR B CG  
69   C CD1 . TYR A 22  ? 0.2327 0.4306 0.2409 -0.0347 0.0458  -0.0042 9   TYR B CD1 
70   C CD2 . TYR A 22  ? 0.2073 0.3802 0.2136 -0.0125 0.0404  -0.0107 9   TYR B CD2 
71   C CE1 . TYR A 22  ? 0.2158 0.3853 0.2198 -0.0403 0.0438  0.0007  9   TYR B CE1 
72   C CE2 . TYR A 22  ? 0.2408 0.3899 0.2447 -0.0184 0.0381  -0.0058 9   TYR B CE2 
73   C CZ  . TYR A 22  ? 0.2565 0.4038 0.2590 -0.0312 0.0397  -0.0001 9   TYR B CZ  
74   O OH  . TYR A 22  ? 0.2933 0.4159 0.2921 -0.0347 0.0377  0.0043  9   TYR B OH  
75   N N   . PRO A 23  ? 0.2397 0.5194 0.2467 0.0102  0.0540  -0.0292 10  PRO B N   
76   C CA  . PRO A 23  ? 0.2281 0.5357 0.2385 0.0237  0.0564  -0.0367 10  PRO B CA  
77   C C   . PRO A 23  ? 0.2376 0.5387 0.2529 0.0381  0.0535  -0.0406 10  PRO B C   
78   O O   . PRO A 23  ? 0.2697 0.5997 0.2909 0.0476  0.0551  -0.0442 10  PRO B O   
79   C CB  . PRO A 23  ? 0.2378 0.5417 0.2394 0.0323  0.0579  -0.0424 10  PRO B CB  
80   C CG  . PRO A 23  ? 0.2704 0.5625 0.2656 0.0177  0.0579  -0.0356 10  PRO B CG  
81   C CD  . PRO A 23  ? 0.2267 0.4927 0.2241 0.0080  0.0542  -0.0283 10  PRO B CD  
82   N N   . SER A 24  ? 0.2114 0.4776 0.2245 0.0394  0.0495  -0.0390 11  SER B N   
83   C CA  . SER A 24  ? 0.2223 0.4790 0.2380 0.0528  0.0471  -0.0412 11  SER B CA  
84   C C   . SER A 24  ? 0.2753 0.5548 0.3006 0.0492  0.0463  -0.0380 11  SER B C   
85   O O   . SER A 24  ? 0.2664 0.5483 0.2942 0.0621  0.0447  -0.0396 11  SER B O   
86   C CB  . SER A 24  ? 0.2314 0.4474 0.2421 0.0540  0.0437  -0.0402 11  SER B CB  
87   O OG  . SER A 24  ? 0.2302 0.4343 0.2429 0.0386  0.0415  -0.0335 11  SER B OG  
88   N N   . LEU A 25  ? 0.2283 0.5234 0.2579 0.0313  0.0473  -0.0336 12  LEU B N   
89   C CA  . LEU A 25  ? 0.2340 0.5514 0.2722 0.0253  0.0465  -0.0320 12  LEU B CA  
90   C C   . LEU A 25  ? 0.2399 0.6049 0.2848 0.0295  0.0497  -0.0359 12  LEU B C   
91   O O   . LEU A 25  ? 0.2436 0.6337 0.2963 0.0291  0.0487  -0.0366 12  LEU B O   
92   C CB  . LEU A 25  ? 0.2442 0.5523 0.2833 0.0039  0.0461  -0.0263 12  LEU B CB  
93   C CG  . LEU A 25  ? 0.2066 0.4726 0.2409 0.0023  0.0424  -0.0228 12  LEU B CG  
94   C CD1 . LEU A 25  ? 0.1975 0.4514 0.2303 -0.0172 0.0427  -0.0175 12  LEU B CD1 
95   C CD2 . LEU A 25  ? 0.2212 0.4807 0.2589 0.0145  0.0386  -0.0243 12  LEU B CD2 
96   N N   . ALA A 26  ? 0.2535 0.6333 0.2952 0.0340  0.0535  -0.0390 13  ALA B N   
97   C CA  . ALA A 26  ? 0.2206 0.6497 0.2691 0.0360  0.0571  -0.0426 13  ALA B CA  
98   C C   . ALA A 26  ? 0.2479 0.6965 0.3015 0.0576  0.0553  -0.0471 13  ALA B C   
99   O O   . ALA A 26  ? 0.2469 0.6717 0.2945 0.0773  0.0537  -0.0497 13  ALA B O   
100  C CB  . ALA A 26  ? 0.2246 0.6641 0.2672 0.0403  0.0616  -0.0458 13  ALA B CB  
101  N N   . ASP A 27  ? 0.2719 0.7649 0.3356 0.0544  0.0559  -0.0482 14  ASP B N   
102  C CA  . ASP A 27  ? 0.3009 0.8211 0.3697 0.0759  0.0543  -0.0520 14  ASP B CA  
103  C C   . ASP A 27  ? 0.2825 0.7755 0.3503 0.0838  0.0490  -0.0492 14  ASP B C   
104  O O   . ASP A 27  ? 0.2912 0.8032 0.3617 0.1024  0.0472  -0.0508 14  ASP B O   
105  C CB  . ASP A 27  ? 0.3448 0.8738 0.4088 0.1008  0.0569  -0.0577 14  ASP B CB  
106  C CG  . ASP A 27  ? 0.5023 1.0619 0.5668 0.0945  0.0626  -0.0609 14  ASP B CG  
107  O OD1 . ASP A 27  ? 0.5077 1.1056 0.5806 0.0761  0.0650  -0.0598 14  ASP B OD1 
108  O OD2 . ASP A 27  ? 0.5230 1.0676 0.5789 0.1065  0.0649  -0.0647 14  ASP B OD2 
109  N N   . LYS A 28  ? 0.2201 0.6704 0.2833 0.0709  0.0465  -0.0447 15  LYS B N   
110  C CA  . LYS A 28  ? 0.2210 0.6469 0.2825 0.0797  0.0419  -0.0420 15  LYS B CA  
111  C C   . LYS A 28  ? 0.2188 0.6785 0.2899 0.0713  0.0397  -0.0416 15  LYS B C   
112  O O   . LYS A 28  ? 0.2124 0.6927 0.2892 0.0493  0.0413  -0.0418 15  LYS B O   
113  C CB  . LYS A 28  ? 0.2288 0.6044 0.2837 0.0678  0.0400  -0.0377 15  LYS B CB  
114  C CG  . LYS A 28  ? 0.3190 0.6588 0.3638 0.0775  0.0413  -0.0389 15  LYS B CG  
115  C CD  . LYS A 28  ? 0.4532 0.7727 0.4909 0.1018  0.0405  -0.0407 15  LYS B CD  
116  C CE  . LYS A 28  ? 0.5528 0.8297 0.5803 0.1028  0.0412  -0.0418 15  LYS B CE  
117  N NZ  . LYS A 28  ? 0.6564 0.9310 0.6770 0.1251  0.0436  -0.0470 15  LYS B NZ  
118  N N   . VAL A 29  ? 0.2229 0.6831 0.2942 0.0866  0.0360  -0.0406 16  VAL B N   
119  C CA  . VAL A 29  ? 0.2223 0.7182 0.3025 0.0794  0.0334  -0.0412 16  VAL B CA  
120  C C   . VAL A 29  ? 0.2007 0.6633 0.2787 0.0643  0.0302  -0.0376 16  VAL B C   
121  O O   . VAL A 29  ? 0.2168 0.6419 0.2874 0.0753  0.0281  -0.0341 16  VAL B O   
122  C CB  . VAL A 29  ? 0.2172 0.7404 0.2988 0.1065  0.0312  -0.0420 16  VAL B CB  
123  C CG1 . VAL A 29  ? 0.1968 0.7553 0.2865 0.1006  0.0273  -0.0425 16  VAL B CG1 
124  C CG2 . VAL A 29  ? 0.2131 0.7720 0.2967 0.1242  0.0345  -0.0462 16  VAL B CG2 
125  N N   . VAL A 30  ? 0.2033 0.6769 0.2863 0.0388  0.0306  -0.0386 17  VAL B N   
126  C CA  . VAL A 30  ? 0.1999 0.6400 0.2796 0.0236  0.0284  -0.0359 17  VAL B CA  
127  C C   . VAL A 30  ? 0.1856 0.6585 0.2723 0.0151  0.0256  -0.0390 17  VAL B C   
128  O O   . VAL A 30  ? 0.1960 0.7145 0.2906 0.0073  0.0272  -0.0433 17  VAL B O   
129  C CB  . VAL A 30  ? 0.2294 0.6501 0.3065 0.0004  0.0318  -0.0349 17  VAL B CB  
130  C CG1 . VAL A 30  ? 0.2495 0.6372 0.3228 -0.0149 0.0299  -0.0328 17  VAL B CG1 
131  C CG2 . VAL A 30  ? 0.1927 0.5845 0.2627 0.0081  0.0341  -0.0324 17  VAL B CG2 
132  N N   . LEU A 31  ? 0.1818 0.6352 0.2658 0.0163  0.0216  -0.0373 18  LEU B N   
133  C CA  . LEU A 31  ? 0.1933 0.6777 0.2828 0.0091  0.0185  -0.0410 18  LEU B CA  
134  C C   . LEU A 31  ? 0.2000 0.6500 0.2849 -0.0081 0.0172  -0.0406 18  LEU B C   
135  O O   . LEU A 31  ? 0.2383 0.6474 0.3160 -0.0001 0.0159  -0.0360 18  LEU B O   
136  C CB  . LEU A 31  ? 0.2035 0.7043 0.2927 0.0354  0.0147  -0.0392 18  LEU B CB  
137  C CG  . LEU A 31  ? 0.2191 0.7510 0.3127 0.0314  0.0105  -0.0425 18  LEU B CG  
138  C CD1 . LEU A 31  ? 0.2773 0.8639 0.3814 0.0129  0.0111  -0.0504 18  LEU B CD1 
139  C CD2 . LEU A 31  ? 0.1698 0.7056 0.2594 0.0593  0.0068  -0.0381 18  LEU B CD2 
140  N N   . ILE A 32  ? 0.2219 0.6860 0.3101 -0.0327 0.0184  -0.0455 19  ILE B N   
141  C CA  . ILE A 32  ? 0.2268 0.6565 0.3094 -0.0515 0.0186  -0.0461 19  ILE B CA  
142  C C   . ILE A 32  ? 0.2160 0.6744 0.3025 -0.0632 0.0159  -0.0531 19  ILE B C   
143  O O   . ILE A 32  ? 0.2038 0.7082 0.2980 -0.0742 0.0169  -0.0591 19  ILE B O   
144  C CB  . ILE A 32  ? 0.2193 0.6333 0.2993 -0.0725 0.0239  -0.0459 19  ILE B CB  
145  C CG1 . ILE A 32  ? 0.2082 0.5958 0.2837 -0.0601 0.0263  -0.0394 19  ILE B CG1 
146  C CG2 . ILE A 32  ? 0.2379 0.6147 0.3104 -0.0907 0.0244  -0.0467 19  ILE B CG2 
147  C CD1 . ILE A 32  ? 0.2005 0.5917 0.2752 -0.0754 0.0318  -0.0387 19  ILE B CD1 
148  N N   . SER A 33  ? 0.2068 0.6445 0.2887 -0.0595 0.0123  -0.0529 20  SER B N   
149  C CA  . SER A 33  ? 0.1955 0.6588 0.2798 -0.0719 0.0098  -0.0605 20  SER B CA  
150  C C   . SER A 33  ? 0.2062 0.6431 0.2854 -0.0995 0.0130  -0.0651 20  SER B C   
151  O O   . SER A 33  ? 0.2380 0.6291 0.3099 -0.1030 0.0159  -0.0603 20  SER B O   
152  C CB  . SER A 33  ? 0.1780 0.6371 0.2592 -0.0548 0.0046  -0.0586 20  SER B CB  
153  O OG  . SER A 33  ? 0.1931 0.5990 0.2654 -0.0533 0.0050  -0.0540 20  SER B OG  
154  N N   . GLY A 34  ? 0.2006 0.6667 0.2829 -0.1193 0.0129  -0.0746 21  GLY B N   
155  C CA  . GLY A 34  ? 0.2399 0.6801 0.3157 -0.1468 0.0168  -0.0798 21  GLY B CA  
156  C C   . GLY A 34  ? 0.2573 0.6814 0.3311 -0.1589 0.0230  -0.0758 21  GLY B C   
157  O O   . GLY A 34  ? 0.2682 0.6480 0.3322 -0.1722 0.0267  -0.0743 21  GLY B O   
158  N N   . GLY A 35  ? 0.2754 0.7398 0.3579 -0.1559 0.0245  -0.0751 22  GLY B N   
159  C CA  . GLY A 35  ? 0.2417 0.6965 0.3229 -0.1610 0.0301  -0.0696 22  GLY B CA  
160  C C   . GLY A 35  ? 0.2923 0.7590 0.3728 -0.1925 0.0362  -0.0746 22  GLY B C   
161  O O   . GLY A 35  ? 0.2833 0.7400 0.3610 -0.1987 0.0414  -0.0695 22  GLY B O   
162  N N   . ALA A 36  ? 0.2886 0.7747 0.3703 -0.2137 0.0362  -0.0845 23  ALA B N   
163  C CA  . ALA A 36  ? 0.3035 0.8084 0.3857 -0.2440 0.0426  -0.0894 23  ALA B CA  
164  C C   . ALA A 36  ? 0.3867 0.8343 0.4535 -0.2675 0.0481  -0.0889 23  ALA B C   
165  O O   . ALA A 36  ? 0.3907 0.8429 0.4546 -0.2939 0.0547  -0.0912 23  ALA B O   
166  C CB  . ALA A 36  ? 0.3069 0.8716 0.3993 -0.2579 0.0404  -0.1019 23  ALA B CB  
167  N N   . SER A 37  ? 0.3762 0.7718 0.4326 -0.2593 0.0459  -0.0865 24  SER B N   
168  C CA  . SER A 37  ? 0.4282 0.7659 0.4683 -0.2775 0.0511  -0.0855 24  SER B CA  
169  C C   . SER A 37  ? 0.4293 0.7115 0.4597 -0.2571 0.0497  -0.0758 24  SER B C   
170  O O   . SER A 37  ? 0.3888 0.6778 0.4253 -0.2312 0.0442  -0.0717 24  SER B O   
171  C CB  . SER A 37  ? 0.4744 0.8094 0.5099 -0.2983 0.0509  -0.0982 24  SER B CB  
172  O OG  . SER A 37  ? 0.4942 0.8186 0.5293 -0.2808 0.0443  -0.1010 24  SER B OG  
173  N N   . GLY A 38  ? 0.4544 0.6829 0.4691 -0.2687 0.0550  -0.0718 25  GLY B N   
174  C CA  . GLY A 38  ? 0.4192 0.5958 0.4237 -0.2511 0.0536  -0.0639 25  GLY B CA  
175  C C   . GLY A 38  ? 0.3752 0.5552 0.3854 -0.2248 0.0506  -0.0536 25  GLY B C   
176  O O   . GLY A 38  ? 0.3733 0.5691 0.3867 -0.2246 0.0534  -0.0480 25  GLY B O   
177  N N   . ILE A 39  ? 0.3800 0.5481 0.3918 -0.2030 0.0449  -0.0521 26  ILE B N   
178  C CA  . ILE A 39  ? 0.3407 0.5016 0.3547 -0.1808 0.0429  -0.0428 26  ILE B CA  
179  C C   . ILE A 39  ? 0.2956 0.5058 0.3233 -0.1716 0.0408  -0.0434 26  ILE B C   
180  O O   . ILE A 39  ? 0.3029 0.5178 0.3324 -0.1628 0.0421  -0.0370 26  ILE B O   
181  C CB  . ILE A 39  ? 0.3018 0.4357 0.3129 -0.1621 0.0382  -0.0410 26  ILE B CB  
182  C CG1 . ILE A 39  ? 0.3504 0.4350 0.3466 -0.1694 0.0413  -0.0393 26  ILE B CG1 
183  C CG2 . ILE A 39  ? 0.3202 0.4554 0.3358 -0.1401 0.0357  -0.0332 26  ILE B CG2 
184  C CD1 . ILE A 39  ? 0.3814 0.4438 0.3743 -0.1568 0.0374  -0.0411 26  ILE B CD1 
185  N N   . GLY A 40  ? 0.2994 0.5463 0.3363 -0.1712 0.0373  -0.0511 27  GLY B N   
186  C CA  . GLY A 40  ? 0.2780 0.5704 0.3270 -0.1576 0.0348  -0.0511 27  GLY B CA  
187  C C   . GLY A 40  ? 0.3012 0.6201 0.3536 -0.1701 0.0399  -0.0505 27  GLY B C   
188  O O   . GLY A 40  ? 0.2234 0.5617 0.2813 -0.1560 0.0398  -0.0467 27  GLY B O   
189  N N   . ARG A 41  ? 0.2966 0.6096 0.3436 -0.1968 0.0451  -0.0537 28  ARG B N   
190  C CA  . ARG A 41  ? 0.3184 0.6525 0.3665 -0.2128 0.0512  -0.0525 28  ARG B CA  
191  C C   . ARG A 41  ? 0.2981 0.6045 0.3394 -0.2041 0.0543  -0.0420 28  ARG B C   
192  O O   . ARG A 41  ? 0.2874 0.6210 0.3337 -0.2005 0.0566  -0.0394 28  ARG B O   
193  C CB  . ARG A 41  ? 0.3317 0.6648 0.3744 -0.2456 0.0567  -0.0586 28  ARG B CB  
194  C CG  . ARG A 41  ? 0.3745 0.7154 0.4141 -0.2634 0.0645  -0.0544 28  ARG B CG  
195  C CD  . ARG A 41  ? 0.4638 0.7949 0.4954 -0.2969 0.0706  -0.0598 28  ARG B CD  
196  N NE  . ARG A 41  ? 0.5362 0.8688 0.5625 -0.3135 0.0788  -0.0537 28  ARG B NE  
197  C CZ  . ARG A 41  ? 0.6073 0.9727 0.6365 -0.3414 0.0844  -0.0597 28  ARG B CZ  
198  N NH1 . ARG A 41  ? 0.5732 0.9328 0.5947 -0.3591 0.0929  -0.0530 28  ARG B NH1 
199  N NH2 . ARG A 41  ? 0.5624 0.9662 0.6016 -0.3519 0.0814  -0.0723 28  ARG B NH2 
200  N N   . ALA A 42  ? 0.3325 0.5865 0.3620 -0.1997 0.0542  -0.0363 29  ALA B N   
201  C CA  . ALA A 42  ? 0.3076 0.5368 0.3303 -0.1898 0.0562  -0.0265 29  ALA B CA  
202  C C   . ALA A 42  ? 0.2849 0.5343 0.3164 -0.1643 0.0519  -0.0247 29  ALA B C   
203  O O   . ALA A 42  ? 0.2909 0.5471 0.3218 -0.1595 0.0544  -0.0199 29  ALA B O   
204  C CB  . ALA A 42  ? 0.3306 0.5038 0.3390 -0.1890 0.0567  -0.0211 29  ALA B CB  
205  N N   . PHE A 43  ? 0.2707 0.5306 0.3096 -0.1481 0.0459  -0.0286 30  PHE B N   
206  C CA  . PHE A 43  ? 0.2352 0.5107 0.2805 -0.1247 0.0426  -0.0271 30  PHE B CA  
207  C C   . PHE A 43  ? 0.2715 0.5956 0.3258 -0.1248 0.0447  -0.0299 30  PHE B C   
208  O O   . PHE A 43  ? 0.2474 0.5788 0.3024 -0.1134 0.0459  -0.0269 30  PHE B O   
209  C CB  . PHE A 43  ? 0.2401 0.5190 0.2903 -0.1089 0.0365  -0.0302 30  PHE B CB  
210  C CG  . PHE A 43  ? 0.2171 0.4531 0.2599 -0.1046 0.0339  -0.0278 30  PHE B CG  
211  C CD1 . PHE A 43  ? 0.2353 0.4333 0.2691 -0.1044 0.0356  -0.0217 30  PHE B CD1 
212  C CD2 . PHE A 43  ? 0.2404 0.4780 0.2854 -0.1004 0.0298  -0.0317 30  PHE B CD2 
213  C CE1 . PHE A 43  ? 0.2806 0.4440 0.3086 -0.0988 0.0331  -0.0199 30  PHE B CE1 
214  C CE2 . PHE A 43  ? 0.2600 0.4630 0.2992 -0.0936 0.0273  -0.0296 30  PHE B CE2 
215  C CZ  . PHE A 43  ? 0.2530 0.4187 0.2839 -0.0931 0.0291  -0.0239 30  PHE B CZ  
216  N N   . VAL A 44  ? 0.2910 0.6506 0.3521 -0.1384 0.0453  -0.0365 31  VAL B N   
217  C CA  . VAL A 44  ? 0.2219 0.6347 0.2929 -0.1382 0.0471  -0.0401 31  VAL B CA  
218  C C   . VAL A 44  ? 0.2351 0.6468 0.3017 -0.1476 0.0534  -0.0355 31  VAL B C   
219  O O   . VAL A 44  ? 0.2238 0.6572 0.2942 -0.1338 0.0542  -0.0344 31  VAL B O   
220  C CB  . VAL A 44  ? 0.2263 0.6813 0.3054 -0.1546 0.0470  -0.0486 31  VAL B CB  
221  C CG1 . VAL A 44  ? 0.2271 0.7410 0.3165 -0.1564 0.0498  -0.0521 31  VAL B CG1 
222  C CG2 . VAL A 44  ? 0.1849 0.6476 0.2684 -0.1414 0.0402  -0.0529 31  VAL B CG2 
223  N N   . GLU A 45  ? 0.2766 0.6609 0.3338 -0.1703 0.0581  -0.0326 32  GLU B N   
224  C CA  . GLU A 45  ? 0.2892 0.6692 0.3397 -0.1811 0.0648  -0.0267 32  GLU B CA  
225  C C   . GLU A 45  ? 0.3172 0.6759 0.3626 -0.1607 0.0638  -0.0200 32  GLU B C   
226  O O   . GLU A 45  ? 0.3434 0.7237 0.3898 -0.1580 0.0673  -0.0181 32  GLU B O   
227  C CB  . GLU A 45  ? 0.3084 0.6510 0.3461 -0.2059 0.0697  -0.0231 32  GLU B CB  
228  C CG  . GLU A 45  ? 0.3136 0.6823 0.3550 -0.2321 0.0728  -0.0305 32  GLU B CG  
229  C CD  . GLU A 45  ? 0.3829 0.7068 0.4101 -0.2557 0.0771  -0.0289 32  GLU B CD  
230  O OE1 . GLU A 45  ? 0.3943 0.6680 0.4102 -0.2468 0.0758  -0.0228 32  GLU B OE1 
231  O OE2 . GLU A 45  ? 0.3797 0.7163 0.4056 -0.2830 0.0821  -0.0337 32  GLU B OE2 
232  N N   . ALA A 46  ? 0.3048 0.6224 0.3445 -0.1475 0.0594  -0.0171 33  ALA B N   
233  C CA  . ALA A 46  ? 0.2733 0.5677 0.3070 -0.1317 0.0587  -0.0112 33  ALA B CA  
234  C C   . ALA A 46  ? 0.2317 0.5566 0.2740 -0.1107 0.0563  -0.0149 33  ALA B C   
235  O O   . ALA A 46  ? 0.2458 0.5745 0.2853 -0.1034 0.0584  -0.0125 33  ALA B O   
236  C CB  . ALA A 46  ? 0.2564 0.5035 0.2825 -0.1244 0.0549  -0.0077 33  ALA B CB  
237  N N   . PHE A 47  ? 0.2498 0.5950 0.3013 -0.0996 0.0520  -0.0206 34  PHE B N   
238  C CA  . PHE A 47  ? 0.2232 0.5922 0.2804 -0.0779 0.0504  -0.0235 34  PHE B CA  
239  C C   . PHE A 47  ? 0.2385 0.6542 0.3014 -0.0813 0.0550  -0.0262 34  PHE B C   
240  O O   . PHE A 47  ? 0.2089 0.6370 0.2721 -0.0659 0.0559  -0.0271 34  PHE B O   
241  C CB  . PHE A 47  ? 0.2010 0.5780 0.2645 -0.0623 0.0450  -0.0274 34  PHE B CB  
242  C CG  . PHE A 47  ? 0.2301 0.5626 0.2875 -0.0516 0.0409  -0.0243 34  PHE B CG  
243  C CD1 . PHE A 47  ? 0.2047 0.5237 0.2595 -0.0312 0.0392  -0.0237 34  PHE B CD1 
244  C CD2 . PHE A 47  ? 0.1824 0.4900 0.2370 -0.0611 0.0387  -0.0233 34  PHE B CD2 
245  C CE1 . PHE A 47  ? 0.1840 0.4649 0.2336 -0.0240 0.0359  -0.0212 34  PHE B CE1 
246  C CE2 . PHE A 47  ? 0.2144 0.4851 0.2640 -0.0517 0.0353  -0.0205 34  PHE B CE2 
247  C CZ  . PHE A 47  ? 0.2003 0.4596 0.2480 -0.0333 0.0339  -0.0195 34  PHE B CZ  
248  N N   . VAL A 48  ? 0.2230 0.6669 0.2906 -0.1016 0.0580  -0.0285 35  VAL B N   
249  C CA  . VAL A 48  ? 0.2288 0.7211 0.3024 -0.1073 0.0628  -0.0312 35  VAL B CA  
250  C C   . VAL A 48  ? 0.2260 0.7036 0.2906 -0.1108 0.0678  -0.0255 35  VAL B C   
251  O O   . VAL A 48  ? 0.2408 0.7471 0.3080 -0.1004 0.0702  -0.0273 35  VAL B O   
252  C CB  . VAL A 48  ? 0.2179 0.7465 0.2984 -0.1313 0.0657  -0.0353 35  VAL B CB  
253  C CG1 . VAL A 48  ? 0.2342 0.8064 0.3181 -0.1434 0.0726  -0.0360 35  VAL B CG1 
254  C CG2 . VAL A 48  ? 0.1813 0.7419 0.2728 -0.1225 0.0604  -0.0424 35  VAL B CG2 
255  N N   . ALA A 49  ? 0.2336 0.6683 0.2871 -0.1247 0.0694  -0.0189 36  ALA B N   
256  C CA  . ALA A 49  ? 0.2589 0.6781 0.3019 -0.1287 0.0741  -0.0122 36  ALA B CA  
257  C C   . ALA A 49  ? 0.2345 0.6448 0.2751 -0.1042 0.0714  -0.0124 36  ALA B C   
258  O O   . ALA A 49  ? 0.2878 0.7077 0.3237 -0.1033 0.0754  -0.0103 36  ALA B O   
259  C CB  . ALA A 49  ? 0.2869 0.6591 0.3171 -0.1449 0.0758  -0.0044 36  ALA B CB  
260  N N   . GLN A 50  ? 0.2310 0.6243 0.2740 -0.0853 0.0653  -0.0154 37  GLN B N   
261  C CA  . GLN A 50  ? 0.2383 0.6213 0.2786 -0.0632 0.0629  -0.0171 37  GLN B CA  
262  C C   . GLN A 50  ? 0.2880 0.7123 0.3363 -0.0469 0.0635  -0.0242 37  GLN B C   
263  O O   . GLN A 50  ? 0.2492 0.6671 0.2948 -0.0274 0.0621  -0.0273 37  GLN B O   
264  C CB  . GLN A 50  ? 0.2132 0.5585 0.2518 -0.0516 0.0568  -0.0171 37  GLN B CB  
265  C CG  . GLN A 50  ? 0.2144 0.5174 0.2445 -0.0627 0.0557  -0.0105 37  GLN B CG  
266  C CD  . GLN A 50  ? 0.2282 0.5121 0.2478 -0.0623 0.0575  -0.0057 37  GLN B CD  
267  O OE1 . GLN A 50  ? 0.2307 0.5214 0.2489 -0.0491 0.0575  -0.0086 37  GLN B OE1 
268  N NE2 . GLN A 50  ? 0.2345 0.4967 0.2458 -0.0772 0.0596  0.0015  37  GLN B NE2 
269  N N   . GLY A 51  ? 0.2641 0.7312 0.3217 -0.0543 0.0656  -0.0275 38  GLY B N   
270  C CA  . GLY A 51  ? 0.2437 0.7541 0.3090 -0.0372 0.0663  -0.0341 38  GLY B CA  
271  C C   . GLY A 51  ? 0.2336 0.7470 0.3047 -0.0163 0.0608  -0.0385 38  GLY B C   
272  O O   . GLY A 51  ? 0.2264 0.7664 0.3010 0.0042  0.0609  -0.0435 38  GLY B O   
273  N N   . SER A 52  ? 0.2345 0.7218 0.3057 -0.0206 0.0565  -0.0364 39  SER B N   
274  C CA  . SER A 52  ? 0.2455 0.7368 0.3215 -0.0038 0.0515  -0.0391 39  SER B CA  
275  C C   . SER A 52  ? 0.2229 0.7694 0.3102 -0.0077 0.0519  -0.0434 39  SER B C   
276  O O   . SER A 52  ? 0.2341 0.8055 0.3255 -0.0299 0.0554  -0.0437 39  SER B O   
277  C CB  . SER A 52  ? 0.2057 0.6575 0.2785 -0.0110 0.0472  -0.0356 39  SER B CB  
278  O OG  . SER A 52  ? 0.2095 0.6153 0.2726 -0.0076 0.0468  -0.0320 39  SER B OG  
279  N N   . ARG A 53  ? 0.2146 0.7763 0.3063 0.0123  0.0479  -0.0460 40  ARG B N   
280  C CA  . ARG A 53  ? 0.2455 0.8598 0.3481 0.0115  0.0467  -0.0501 40  ARG B CA  
281  C C   . ARG A 53  ? 0.2170 0.8131 0.3199 0.0032  0.0418  -0.0488 40  ARG B C   
282  O O   . ARG A 53  ? 0.2396 0.8033 0.3372 0.0196  0.0378  -0.0463 40  ARG B O   
283  C CB  . ARG A 53  ? 0.2345 0.8789 0.3398 0.0422  0.0456  -0.0533 40  ARG B CB  
284  C CG  . ARG A 53  ? 0.2758 0.9536 0.3832 0.0468  0.0512  -0.0567 40  ARG B CG  
285  C CD  . ARG A 53  ? 0.3399 1.0495 0.4489 0.0794  0.0511  -0.0606 40  ARG B CD  
286  N NE  . ARG A 53  ? 0.3867 1.0448 0.4838 0.1027  0.0494  -0.0586 40  ARG B NE  
287  C CZ  . ARG A 53  ? 0.3150 0.9675 0.4081 0.1323  0.0465  -0.0587 40  ARG B CZ  
288  N NH1 . ARG A 53  ? 0.3064 1.0079 0.4069 0.1478  0.0449  -0.0610 40  ARG B NH1 
289  N NH2 . ARG A 53  ? 0.3134 0.9111 0.3943 0.1468  0.0456  -0.0564 40  ARG B NH2 
290  N N   . VAL A 54  ? 0.2126 0.8215 0.3196 -0.0242 0.0430  -0.0502 41  VAL B N   
291  C CA  . VAL A 54  ? 0.2059 0.7854 0.3101 -0.0360 0.0394  -0.0491 41  VAL B CA  
292  C C   . VAL A 54  ? 0.2301 0.8562 0.3438 -0.0414 0.0365  -0.0547 41  VAL B C   
293  O O   . VAL A 54  ? 0.2128 0.8772 0.3331 -0.0622 0.0396  -0.0592 41  VAL B O   
294  C CB  . VAL A 54  ? 0.2196 0.7633 0.3171 -0.0634 0.0427  -0.0463 41  VAL B CB  
295  C CG1 . VAL A 54  ? 0.2065 0.7183 0.3002 -0.0741 0.0393  -0.0459 41  VAL B CG1 
296  C CG2 . VAL A 54  ? 0.1947 0.6983 0.2830 -0.0583 0.0453  -0.0407 41  VAL B CG2 
297  N N   . ALA A 55  ? 0.2106 0.8311 0.3238 -0.0248 0.0309  -0.0544 42  ALA B N   
298  C CA  . ALA A 55  ? 0.2045 0.8649 0.3250 -0.0299 0.0273  -0.0596 42  ALA B CA  
299  C C   . ALA A 55  ? 0.2429 0.8658 0.3580 -0.0478 0.0252  -0.0595 42  ALA B C   
300  O O   . ALA A 55  ? 0.2303 0.7997 0.3364 -0.0415 0.0242  -0.0542 42  ALA B O   
301  C CB  . ALA A 55  ? 0.1935 0.8718 0.3151 0.0024  0.0228  -0.0582 42  ALA B CB  
302  N N   . PHE A 56  ? 0.2351 0.8844 0.3549 -0.0707 0.0249  -0.0661 43  PHE B N   
303  C CA  . PHE A 56  ? 0.2345 0.8469 0.3478 -0.0846 0.0229  -0.0669 43  PHE B CA  
304  C C   . PHE A 56  ? 0.2631 0.9168 0.3826 -0.0924 0.0189  -0.0749 43  PHE B C   
305  O O   . PHE A 56  ? 0.2444 0.9570 0.3737 -0.0986 0.0193  -0.0811 43  PHE B O   
306  C CB  . PHE A 56  ? 0.2313 0.8060 0.3379 -0.1111 0.0283  -0.0660 43  PHE B CB  
307  C CG  . PHE A 56  ? 0.2370 0.8493 0.3492 -0.1382 0.0333  -0.0720 43  PHE B CG  
308  C CD1 . PHE A 56  ? 0.2293 0.8689 0.3462 -0.1374 0.0377  -0.0705 43  PHE B CD1 
309  C CD2 . PHE A 56  ? 0.2654 0.8803 0.3766 -0.1662 0.0343  -0.0790 43  PHE B CD2 
310  C CE1 . PHE A 56  ? 0.3059 0.9799 0.4273 -0.1638 0.0431  -0.0753 43  PHE B CE1 
311  C CE2 . PHE A 56  ? 0.2492 0.8960 0.3644 -0.1939 0.0398  -0.0844 43  PHE B CE2 
312  C CZ  . PHE A 56  ? 0.2860 0.9625 0.4065 -0.1929 0.0444  -0.0820 43  PHE B CZ  
313  N N   . LEU A 57  ? 0.2454 0.8712 0.3590 -0.0914 0.0150  -0.0750 44  LEU B N   
314  C CA  . LEU A 57  ? 0.2181 0.8793 0.3356 -0.0972 0.0106  -0.0828 44  LEU B CA  
315  C C   . LEU A 57  ? 0.2401 0.8764 0.3522 -0.1282 0.0125  -0.0893 44  LEU B C   
316  O O   . LEU A 57  ? 0.3050 0.8840 0.4075 -0.1326 0.0147  -0.0848 44  LEU B O   
317  C CB  . LEU A 57  ? 0.2634 0.9010 0.3751 -0.0702 0.0055  -0.0764 44  LEU B CB  
318  C CG  . LEU A 57  ? 0.2636 0.9332 0.3790 -0.0378 0.0022  -0.0717 44  LEU B CG  
319  C CD1 . LEU A 57  ? 0.2540 0.9594 0.3767 -0.0279 0.0049  -0.0710 44  LEU B CD1 
320  C CD2 . LEU A 57  ? 0.3230 0.9489 0.4291 -0.0126 -0.0001 -0.0623 44  LEU B CD2 
321  N N   . ASP A 58  ? 0.2265 0.9051 0.3440 -0.1487 0.0117  -0.1002 45  ASP B N   
322  C CA  . ASP A 58  ? 0.2841 0.9368 0.3946 -0.1762 0.0131  -0.1077 45  ASP B CA  
323  C C   . ASP A 58  ? 0.3142 1.0225 0.4313 -0.1886 0.0094  -0.1202 45  ASP B C   
324  O O   . ASP A 58  ? 0.3078 1.0784 0.4361 -0.1821 0.0074  -0.1231 45  ASP B O   
325  C CB  . ASP A 58  ? 0.3120 0.9368 0.4176 -0.2045 0.0207  -0.1087 45  ASP B CB  
326  C CG  . ASP A 58  ? 0.3714 0.9344 0.4633 -0.2219 0.0232  -0.1102 45  ASP B CG  
327  O OD1 . ASP A 58  ? 0.3391 0.9087 0.4284 -0.2455 0.0236  -0.1213 45  ASP B OD1 
328  O OD2 . ASP A 58  ? 0.2862 0.7960 0.3696 -0.2136 0.0254  -0.1011 45  ASP B OD2 
329  N N   . LEU A 59  ? 0.3220 1.0068 0.4313 -0.2031 0.0081  -0.1273 46  LEU B N   
330  C CA  . LEU A 59  ? 0.3694 1.0997 0.4827 -0.2205 0.0051  -0.1411 46  LEU B CA  
331  C C   . LEU A 59  ? 0.3973 1.1520 0.5146 -0.2558 0.0111  -0.1505 46  LEU B C   
332  O O   . LEU A 59  ? 0.3952 1.2127 0.5218 -0.2674 0.0091  -0.1610 46  LEU B O   
333  C CB  . LEU A 59  ? 0.3925 1.0740 0.4932 -0.2270 0.0039  -0.1450 46  LEU B CB  
334  C CG  . LEU A 59  ? 0.4367 1.1502 0.5370 -0.2463 0.0007  -0.1608 46  LEU B CG  
335  C CD1 . LEU A 59  ? 0.4426 1.2276 0.5533 -0.2279 -0.0070 -0.1637 46  LEU B CD1 
336  C CD2 . LEU A 59  ? 0.4463 1.1017 0.5320 -0.2506 0.0005  -0.1638 46  LEU B CD2 
337  N N   . ASP A 60  ? 0.4180 1.1239 0.5275 -0.2736 0.0186  -0.1469 47  ASP B N   
338  C CA  . ASP A 60  ? 0.4311 1.1496 0.5410 -0.3102 0.0255  -0.1550 47  ASP B CA  
339  C C   . ASP A 60  ? 0.4120 1.1824 0.5347 -0.3074 0.0280  -0.1513 47  ASP B C   
340  O O   . ASP A 60  ? 0.4317 1.1754 0.5522 -0.2996 0.0323  -0.1406 47  ASP B O   
341  C CB  . ASP A 60  ? 0.4524 1.0949 0.5466 -0.3278 0.0328  -0.1508 47  ASP B CB  
342  C CG  . ASP A 60  ? 0.4538 1.0954 0.5433 -0.3695 0.0407  -0.1598 47  ASP B CG  
343  O OD1 . ASP A 60  ? 0.4407 1.1411 0.5414 -0.3840 0.0426  -0.1652 47  ASP B OD1 
344  O OD2 . ASP A 60  ? 0.5082 1.0881 0.5819 -0.3870 0.0455  -0.1609 47  ASP B OD2 
345  N N   . ALA A 61  ? 0.3896 1.2366 0.5256 -0.3139 0.0256  -0.1608 48  ALA B N   
346  C CA  . ALA A 61  ? 0.4139 1.3203 0.5636 -0.3067 0.0271  -0.1582 48  ALA B CA  
347  C C   . ALA A 61  ? 0.4387 1.3375 0.5867 -0.3377 0.0369  -0.1582 48  ALA B C   
348  O O   . ALA A 61  ? 0.4108 1.3237 0.5640 -0.3273 0.0402  -0.1503 48  ALA B O   
349  C CB  . ALA A 61  ? 0.4379 1.4319 0.6023 -0.3049 0.0216  -0.1688 48  ALA B CB  
350  N N   . GLU A 62  ? 0.4721 1.3505 0.6122 -0.3760 0.0419  -0.1675 49  GLU B N   
351  C CA  . GLU A 62  ? 0.4979 1.3654 0.6338 -0.4088 0.0521  -0.1673 49  GLU B CA  
352  C C   . GLU A 62  ? 0.4815 1.2744 0.6041 -0.3996 0.0572  -0.1522 49  GLU B C   
353  O O   . GLU A 62  ? 0.4621 1.2593 0.5858 -0.4033 0.0634  -0.1449 49  GLU B O   
354  C CB  . GLU A 62  ? 0.5542 1.4142 0.6828 -0.4513 0.0561  -0.1815 49  GLU B CB  
355  C CG  . GLU A 62  ? 0.5532 1.4613 0.6883 -0.4873 0.0639  -0.1885 49  GLU B CG  
356  C CD  . GLU A 62  ? 0.5829 1.5000 0.7143 -0.5203 0.0636  -0.2062 49  GLU B CD  
357  O OE1 . GLU A 62  ? 0.6455 1.5029 0.7634 -0.5161 0.0611  -0.2071 49  GLU B OE1 
358  O OE2 . GLU A 62  ? 0.5774 1.5595 0.7189 -0.5471 0.0650  -0.2193 49  GLU B OE2 
359  N N   . ALA A 63  ? 0.4414 1.1687 0.5516 -0.3854 0.0543  -0.1473 50  ALA B N   
360  C CA  . ALA A 63  ? 0.4789 1.1386 0.5770 -0.3724 0.0577  -0.1331 50  ALA B CA  
361  C C   . ALA A 63  ? 0.4335 1.1150 0.5409 -0.3385 0.0549  -0.1225 50  ALA B C   
362  O O   . ALA A 63  ? 0.4407 1.1001 0.5437 -0.3365 0.0602  -0.1127 50  ALA B O   
363  C CB  . ALA A 63  ? 0.4417 1.0358 0.5263 -0.3631 0.0544  -0.1317 50  ALA B CB  
364  N N   . GLY A 64  ? 0.3639 1.0902 0.4831 -0.3123 0.0470  -0.1248 51  GLY B N   
365  C CA  . GLY A 64  ? 0.3064 1.0490 0.4325 -0.2784 0.0443  -0.1156 51  GLY B CA  
366  C C   . GLY A 64  ? 0.3046 1.0970 0.4403 -0.2844 0.0495  -0.1149 51  GLY B C   
367  O O   . GLY A 64  ? 0.3457 1.1219 0.4793 -0.2708 0.0525  -0.1055 51  GLY B O   
368  N N   . GLN A 65  ? 0.3098 1.1667 0.4561 -0.3048 0.0503  -0.1258 52  GLN B N   
369  C CA  . GLN A 65  ? 0.2890 1.2055 0.4461 -0.3149 0.0554  -0.1277 52  GLN B CA  
370  C C   . GLN A 65  ? 0.2979 1.1730 0.4442 -0.3400 0.0654  -0.1216 52  GLN B C   
371  O O   . GLN A 65  ? 0.2949 1.1832 0.4437 -0.3331 0.0697  -0.1151 52  GLN B O   
372  C CB  . GLN A 65  ? 0.2629 1.2530 0.4326 -0.3317 0.0526  -0.1420 52  GLN B CB  
373  N N   . GLY A 66  ? 0.3640 1.1847 0.4964 -0.3679 0.0693  -0.1230 53  GLY B N   
374  C CA  . GLY A 66  ? 0.4102 1.1823 0.5289 -0.3902 0.0788  -0.1156 53  GLY B CA  
375  C C   . GLY A 66  ? 0.4265 1.1534 0.5377 -0.3632 0.0792  -0.1011 53  GLY B C   
376  O O   . GLY A 66  ? 0.4318 1.1621 0.5411 -0.3687 0.0859  -0.0943 53  GLY B O   
377  N N   . LEU A 67  ? 0.3803 1.0675 0.4874 -0.3351 0.0723  -0.0968 54  LEU B N   
378  C CA  . LEU A 67  ? 0.3526 0.9942 0.4520 -0.3101 0.0720  -0.0843 54  LEU B CA  
379  C C   . LEU A 67  ? 0.3039 0.9932 0.4148 -0.2867 0.0713  -0.0813 54  LEU B C   
380  O O   . LEU A 67  ? 0.3536 1.0276 0.4595 -0.2825 0.0759  -0.0730 54  LEU B O   
381  C CB  . LEU A 67  ? 0.3482 0.9418 0.4414 -0.2878 0.0649  -0.0820 54  LEU B CB  
382  N N   . ALA A 68  ? 0.2686 1.0154 0.3940 -0.2699 0.0656  -0.0879 55  ALA B N   
383  C CA  . ALA A 68  ? 0.2953 1.0893 0.4309 -0.2473 0.0654  -0.0861 55  ALA B CA  
384  C C   . ALA A 68  ? 0.3212 1.1566 0.4610 -0.2707 0.0740  -0.0873 55  ALA B C   
385  O O   . ALA A 68  ? 0.3272 1.1796 0.4694 -0.2564 0.0768  -0.0827 55  ALA B O   
386  C CB  . ALA A 68  ? 0.2579 1.1072 0.4068 -0.2266 0.0582  -0.0930 55  ALA B CB  
387  N N   . HIS A 69  ? 0.3556 1.2062 0.4954 -0.3077 0.0789  -0.0935 56  HIS B N   
388  C CA  . HIS A 69  ? 0.3808 1.2686 0.5236 -0.3318 0.0879  -0.0937 56  HIS B CA  
389  C C   . HIS A 69  ? 0.3519 1.1840 0.4796 -0.3349 0.0945  -0.0815 56  HIS B C   
390  O O   . HIS A 69  ? 0.3817 1.2404 0.5117 -0.3328 0.0998  -0.0775 56  HIS B O   
391  C CB  . HIS A 69  ? 0.3845 1.3038 0.5304 -0.3733 0.0924  -0.1037 56  HIS B CB  
392  C CG  . HIS A 69  ? 0.4923 1.4416 0.6385 -0.4024 0.1031  -0.1026 56  HIS B CG  
393  N ND1 . HIS A 69  ? 0.5371 1.4344 0.6667 -0.4310 0.1123  -0.0955 56  HIS B ND1 
394  C CD2 . HIS A 69  ? 0.4788 1.5056 0.6394 -0.4054 0.1066  -0.1066 56  HIS B CD2 
395  C CE1 . HIS A 69  ? 0.5070 1.4472 0.6402 -0.4523 0.1211  -0.0950 56  HIS B CE1 
396  N NE2 . HIS A 69  ? 0.5079 1.5287 0.6606 -0.4375 0.1178  -0.1022 56  HIS B NE2 
397  N N   . ALA A 70  ? 0.3712 1.1289 0.4828 -0.3419 0.0947  -0.0760 57  ALA B N   
398  C CA  . ALA A 70  ? 0.3868 1.0895 0.4828 -0.3426 0.1002  -0.0638 57  ALA B CA  
399  C C   . ALA A 70  ? 0.4008 1.1050 0.4992 -0.3064 0.0970  -0.0574 57  ALA B C   
400  O O   . ALA A 70  ? 0.3814 1.0878 0.4753 -0.3071 0.1029  -0.0506 57  ALA B O   
401  C CB  . ALA A 70  ? 0.4117 1.0362 0.4906 -0.3507 0.0997  -0.0595 57  ALA B CB  
402  N N   . LEU A 71  ? 0.3799 1.0829 0.4844 -0.2751 0.0880  -0.0596 58  LEU B N   
403  C CA  . LEU A 71  ? 0.3403 1.0243 0.4425 -0.2424 0.0849  -0.0533 58  LEU B CA  
404  C C   . LEU A 71  ? 0.3605 1.1055 0.4752 -0.2224 0.0848  -0.0566 58  LEU B C   
405  O O   . LEU A 71  ? 0.3059 1.0388 0.4172 -0.1998 0.0845  -0.0519 58  LEU B O   
406  C CB  . LEU A 71  ? 0.2989 0.9446 0.3990 -0.2204 0.0764  -0.0533 58  LEU B CB  
407  C CG  . LEU A 71  ? 0.3717 0.9531 0.4581 -0.2354 0.0766  -0.0495 58  LEU B CG  
408  C CD1 . LEU A 71  ? 0.3730 0.9316 0.4604 -0.2086 0.0681  -0.0499 58  LEU B CD1 
409  C CD2 . LEU A 71  ? 0.4079 0.9452 0.4802 -0.2392 0.0819  -0.0391 58  LEU B CD2 
410  N N   . GLY A 72  ? 0.3499 1.1606 0.4784 -0.2299 0.0850  -0.0651 59  GLY B N   
411  C CA  . GLY A 72  ? 0.3894 1.2647 0.5300 -0.2119 0.0857  -0.0689 59  GLY B CA  
412  C C   . GLY A 72  ? 0.3334 1.2180 0.4797 -0.1718 0.0777  -0.0709 59  GLY B C   
413  O O   . GLY A 72  ? 0.3159 1.1721 0.4606 -0.1612 0.0709  -0.0714 59  GLY B O   
414  N N   . ALA A 73  ? 0.2849 1.2082 0.4367 -0.1497 0.0792  -0.0719 60  ALA B N   
415  C CA  . ALA A 73  ? 0.3043 1.2579 0.4637 -0.1137 0.0734  -0.0758 60  ALA B CA  
416  C C   . ALA A 73  ? 0.3002 1.1947 0.4501 -0.0844 0.0675  -0.0710 60  ALA B C   
417  O O   . ALA A 73  ? 0.3211 1.2270 0.4744 -0.0562 0.0620  -0.0731 60  ALA B O   
418  C CB  . ALA A 73  ? 0.3001 1.3141 0.4674 -0.1010 0.0777  -0.0791 60  ALA B CB  
419  N N   . ASN A 74  ? 0.2771 1.1079 0.4142 -0.0902 0.0689  -0.0644 61  ASN B N   
420  C CA  . ASN A 74  ? 0.2802 1.0591 0.4095 -0.0657 0.0632  -0.0609 61  ASN B CA  
421  C C   . ASN A 74  ? 0.2817 1.0282 0.4089 -0.0751 0.0581  -0.0601 61  ASN B C   
422  O O   . ASN A 74  ? 0.2503 0.9487 0.3700 -0.0592 0.0538  -0.0565 61  ASN B O   
423  C CB  . ASN A 74  ? 0.2708 0.9964 0.3875 -0.0621 0.0655  -0.0547 61  ASN B CB  
424  C CG  . ASN A 74  ? 0.3330 1.0812 0.4493 -0.0447 0.0693  -0.0560 61  ASN B CG  
425  O OD1 . ASN A 74  ? 0.3394 1.1324 0.4633 -0.0248 0.0687  -0.0612 61  ASN B OD1 
426  N ND2 . ASN A 74  ? 0.3603 1.0780 0.4668 -0.0506 0.0732  -0.0516 61  ASN B ND2 
427  N N   . SER A 75  ? 0.2623 1.0336 0.3951 -0.1017 0.0590  -0.0639 62  SER B N   
428  C CA  . SER A 75  ? 0.2584 1.0084 0.3903 -0.1078 0.0537  -0.0653 62  SER B CA  
429  C C   . SER A 75  ? 0.2636 1.0720 0.4075 -0.0998 0.0493  -0.0725 62  SER B C   
430  O O   . SER A 75  ? 0.2780 1.1472 0.4319 -0.1020 0.0518  -0.0773 62  SER B O   
431  C CB  . SER A 75  ? 0.2911 1.0110 0.4166 -0.1427 0.0571  -0.0645 62  SER B CB  
432  O OG  . SER A 75  ? 0.3175 1.0854 0.4505 -0.1702 0.0614  -0.0706 62  SER B OG  
433  N N   . LEU A 76  ? 0.2335 1.0263 0.3762 -0.0900 0.0428  -0.0731 63  LEU B N   
434  C CA  . LEU A 76  ? 0.2739 1.1217 0.4268 -0.0814 0.0380  -0.0793 63  LEU B CA  
435  C C   . LEU A 76  ? 0.2480 1.0742 0.3979 -0.0929 0.0333  -0.0816 63  LEU B C   
436  O O   . LEU A 76  ? 0.2414 1.0169 0.3826 -0.0793 0.0298  -0.0764 63  LEU B O   
437  C CB  . LEU A 76  ? 0.2560 1.1159 0.4097 -0.0411 0.0343  -0.0766 63  LEU B CB  
438  C CG  . LEU A 76  ? 0.3263 1.2391 0.4882 -0.0258 0.0285  -0.0810 63  LEU B CG  
439  C CD1 . LEU A 76  ? 0.2937 1.2916 0.4704 -0.0384 0.0309  -0.0895 63  LEU B CD1 
440  C CD2 . LEU A 76  ? 0.3322 1.2287 0.4885 0.0154  0.0249  -0.0753 63  LEU B CD2 
441  N N   . PHE A 77  ? 0.2518 1.1165 0.4084 -0.1196 0.0337  -0.0898 64  PHE B N   
442  C CA  . PHE A 77  ? 0.2245 1.0724 0.3780 -0.1364 0.0303  -0.0942 64  PHE B CA  
443  C C   . PHE A 77  ? 0.2236 1.1194 0.3845 -0.1185 0.0232  -0.0988 64  PHE B C   
444  O O   . PHE A 77  ? 0.2223 1.1875 0.3948 -0.1179 0.0228  -0.1048 64  PHE B O   
445  C CB  . PHE A 77  ? 0.2673 1.1239 0.4214 -0.1781 0.0350  -0.1017 64  PHE B CB  
446  C CG  . PHE A 77  ? 0.2598 1.1085 0.4112 -0.1926 0.0308  -0.1088 64  PHE B CG  
447  C CD1 . PHE A 77  ? 0.2744 1.0640 0.4150 -0.1834 0.0272  -0.1048 64  PHE B CD1 
448  C CD2 . PHE A 77  ? 0.2721 1.1787 0.4324 -0.2134 0.0300  -0.1204 64  PHE B CD2 
449  C CE1 . PHE A 77  ? 0.2481 1.0356 0.3864 -0.1950 0.0233  -0.1122 64  PHE B CE1 
450  C CE2 . PHE A 77  ? 0.2589 1.1616 0.4164 -0.2259 0.0260  -0.1281 64  PHE B CE2 
451  C CZ  . PHE A 77  ? 0.2789 1.1218 0.4252 -0.2170 0.0228  -0.1242 64  PHE B CZ  
452  N N   . LEU A 78  ? 0.2255 1.0870 0.3794 -0.1036 0.0177  -0.0958 65  LEU B N   
453  C CA  . LEU A 78  ? 0.2871 1.1906 0.4458 -0.0872 0.0107  -0.0993 65  LEU B CA  
454  C C   . LEU A 78  ? 0.2849 1.1743 0.4397 -0.1094 0.0080  -0.1058 65  LEU B C   
455  O O   . LEU A 78  ? 0.2601 1.0877 0.4041 -0.1106 0.0078  -0.1016 65  LEU B O   
456  C CB  . LEU A 78  ? 0.2624 1.1556 0.4171 -0.0465 0.0060  -0.0909 65  LEU B CB  
457  C CG  . LEU A 78  ? 0.2612 1.1669 0.4182 -0.0218 0.0087  -0.0855 65  LEU B CG  
458  C CD1 . LEU A 78  ? 0.2349 1.1313 0.3863 0.0185  0.0045  -0.0778 65  LEU B CD1 
459  C CD2 . LEU A 78  ? 0.3142 1.2966 0.4849 -0.0289 0.0111  -0.0928 65  LEU B CD2 
460  N N   . PRO A 79  ? 0.2288 1.1759 0.3918 -0.1263 0.0059  -0.1168 66  PRO B N   
461  C CA  . PRO A 79  ? 0.2580 1.1970 0.4167 -0.1420 0.0022  -0.1240 66  PRO B CA  
462  C C   . PRO A 79  ? 0.2766 1.1965 0.4287 -0.1115 -0.0045 -0.1177 66  PRO B C   
463  O O   . PRO A 79  ? 0.2939 1.2477 0.4499 -0.0810 -0.0085 -0.1129 66  PRO B O   
464  C CB  . PRO A 79  ? 0.2412 1.2597 0.4120 -0.1611 0.0009  -0.1371 66  PRO B CB  
465  C CG  . PRO A 79  ? 0.2413 1.3151 0.4234 -0.1454 0.0022  -0.1348 66  PRO B CG  
466  C CD  . PRO A 79  ? 0.2343 1.2618 0.4114 -0.1292 0.0067  -0.1232 66  PRO B CD  
467  N N   . CYS A 80  ? 0.2528 1.1116 0.3936 -0.1164 -0.0050 -0.1155 67  CYS B N   
468  C CA  . CYS A 80  ? 0.2979 1.1404 0.4321 -0.0890 -0.0107 -0.1091 67  CYS B CA  
469  C C   . CYS A 80  ? 0.2775 1.0783 0.4022 -0.1055 -0.0117 -0.1134 67  CYS B C   
470  O O   . CYS A 80  ? 0.2924 1.0466 0.4114 -0.1272 -0.0069 -0.1150 67  CYS B O   
471  C CB  . CYS A 80  ? 0.3291 1.1388 0.4592 -0.0578 -0.0099 -0.0955 67  CYS B CB  
472  S SG  . CYS A 80  ? 0.3564 1.1321 0.4755 -0.0272 -0.0151 -0.0857 67  CYS B SG  
473  N N   . ASP A 81  ? 0.3104 1.1361 0.4337 -0.0976 -0.0176 -0.1170 68  ASP B N   
474  C CA  . ASP A 81  ? 0.2964 1.0819 0.4091 -0.1041 -0.0194 -0.1193 68  ASP B CA  
475  C C   . ASP A 81  ? 0.2749 1.0253 0.3801 -0.0717 -0.0216 -0.1055 68  ASP B C   
476  O O   . ASP A 81  ? 0.2598 1.0429 0.3664 -0.0454 -0.0259 -0.0998 68  ASP B O   
477  C CB  . ASP A 81  ? 0.2921 1.1237 0.4064 -0.1174 -0.0241 -0.1324 68  ASP B CB  
478  N N   . VAL A 82  ? 0.2530 0.9360 0.3495 -0.0738 -0.0181 -0.0995 69  VAL B N   
479  C CA  . VAL A 82  ? 0.2560 0.9007 0.3454 -0.0466 -0.0188 -0.0862 69  VAL B CA  
480  C C   . VAL A 82  ? 0.2522 0.8987 0.3347 -0.0333 -0.0236 -0.0845 69  VAL B C   
481  O O   . VAL A 82  ? 0.2461 0.8752 0.3232 -0.0078 -0.0247 -0.0730 69  VAL B O   
482  C CB  . VAL A 82  ? 0.2980 0.8783 0.3815 -0.0528 -0.0138 -0.0808 69  VAL B CB  
483  C CG1 . VAL A 82  ? 0.3312 0.9169 0.4213 -0.0611 -0.0092 -0.0806 69  VAL B CG1 
484  C CG2 . VAL A 82  ? 0.3391 0.8847 0.4157 -0.0751 -0.0124 -0.0878 69  VAL B CG2 
485  N N   . ARG A 83  ? 0.2738 0.9473 0.3564 -0.0497 -0.0264 -0.0960 70  ARG B N   
486  C CA  . ARG A 83  ? 0.2630 0.9511 0.3395 -0.0378 -0.0315 -0.0959 70  ARG B CA  
487  C C   . ARG A 83  ? 0.2704 1.0120 0.3508 -0.0122 -0.0361 -0.0903 70  ARG B C   
488  O O   . ARG A 83  ? 0.2880 1.0320 0.3611 0.0086  -0.0396 -0.0832 70  ARG B O   
489  C CB  . ARG A 83  ? 0.2830 0.9883 0.3577 -0.0619 -0.0334 -0.1111 70  ARG B CB  
490  C CG  . ARG A 83  ? 0.3097 0.9635 0.3795 -0.0877 -0.0285 -0.1179 70  ARG B CG  
491  C CD  . ARG A 83  ? 0.3933 1.0673 0.4623 -0.1167 -0.0291 -0.1358 70  ARG B CD  
492  N NE  . ARG A 83  ? 0.5536 1.2210 0.6132 -0.1131 -0.0324 -0.1397 70  ARG B NE  
493  C CZ  . ARG A 83  ? 0.5264 1.2426 0.5866 -0.1199 -0.0371 -0.1513 70  ARG B CZ  
494  N NH1 . ARG A 83  ? 0.5056 1.2777 0.5758 -0.1313 -0.0386 -0.1596 70  ARG B NH1 
495  N NH2 . ARG A 83  ? 0.4887 1.1997 0.5396 -0.1155 -0.0400 -0.1547 70  ARG B NH2 
496  N N   . ASP A 84  ? 0.2317 1.0163 0.3228 -0.0126 -0.0357 -0.0929 71  ASP B N   
497  C CA  . ASP A 84  ? 0.2706 1.1062 0.3651 0.0145  -0.0397 -0.0871 71  ASP B CA  
498  C C   . ASP A 84  ? 0.2569 1.0587 0.3477 0.0411  -0.0369 -0.0722 71  ASP B C   
499  O O   . ASP A 84  ? 0.2432 1.0475 0.3407 0.0404  -0.0334 -0.0716 71  ASP B O   
500  C CB  . ASP A 84  ? 0.2873 1.1954 0.3950 0.0028  -0.0414 -0.0984 71  ASP B CB  
501  C CG  . ASP A 84  ? 0.2930 1.2649 0.4057 0.0310  -0.0458 -0.0940 71  ASP B CG  
502  O OD1 . ASP A 84  ? 0.2697 1.2256 0.3747 0.0638  -0.0468 -0.0801 71  ASP B OD1 
503  O OD2 . ASP A 84  ? 0.2852 1.3249 0.4092 0.0205  -0.0479 -0.1046 71  ASP B OD2 
504  N N   . ILE A 85  ? 0.2494 1.0260 0.3293 0.0655  -0.0385 -0.0606 72  ILE B N   
505  C CA  . ILE A 85  ? 0.3140 1.0527 0.3881 0.0896  -0.0354 -0.0469 72  ILE B CA  
506  C C   . ILE A 85  ? 0.3168 1.0984 0.3959 0.1129  -0.0362 -0.0432 72  ILE B C   
507  O O   . ILE A 85  ? 0.3018 1.0591 0.3804 0.1240  -0.0324 -0.0372 72  ILE B O   
508  C CB  . ILE A 85  ? 0.3341 1.0301 0.3939 0.1073  -0.0358 -0.0351 72  ILE B CB  
509  C CG1 . ILE A 85  ? 0.3060 0.9533 0.3614 0.0850  -0.0338 -0.0385 72  ILE B CG1 
510  C CG2 . ILE A 85  ? 0.3123 0.9753 0.3650 0.1341  -0.0328 -0.0214 72  ILE B CG2 
511  C CD1 . ILE A 85  ? 0.2439 0.8503 0.3034 0.0671  -0.0285 -0.0412 72  ILE B CD1 
512  N N   . GLU A 86  ? 0.4316 1.2745 0.5132 0.1244  -0.0415 -0.0454 73  GLU B N   
513  C CA  . GLU A 86  ? 0.4158 1.3085 0.5038 0.1452  -0.0424 -0.0439 73  GLU B CA  
514  C C   . GLU A 86  ? 0.2702 1.1706 0.3710 0.1235  -0.0380 -0.0528 73  GLU B C   
515  O O   . GLU A 86  ? 0.3630 1.2722 0.4667 0.1408  -0.0355 -0.0488 73  GLU B O   
516  C CB  . GLU A 86  ? 0.4201 1.3747 0.5067 0.1638  -0.0491 -0.0432 73  GLU B CB  
517  N N   . ARG A 87  ? 0.2072 1.1177 0.3164 0.0870  -0.0372 -0.0659 74  ARG B N   
518  C CA  . ARG A 87  ? 0.2259 1.1616 0.3477 0.0684  -0.0332 -0.0741 74  ARG B CA  
519  C C   . ARG A 87  ? 0.4022 1.2707 0.5190 0.0679  -0.0272 -0.0672 74  ARG B C   
520  O O   . ARG A 87  ? 0.3033 1.1822 0.4254 0.0746  -0.0238 -0.0660 74  ARG B O   
521  C CB  . ARG A 87  ? 0.0921 1.0672 0.2249 0.0289  -0.0330 -0.0906 74  ARG B CB  
522  N N   . LEU A 88  ? 0.3298 1.1330 0.4361 0.0625  -0.0261 -0.0625 75  LEU B N   
523  C CA  . LEU A 88  ? 0.2808 1.0210 0.3814 0.0637  -0.0211 -0.0556 75  LEU B CA  
524  C C   . LEU A 88  ? 0.2552 0.9921 0.3523 0.0960  -0.0200 -0.0459 75  LEU B C   
525  O O   . LEU A 88  ? 0.2945 1.0184 0.3941 0.0959  -0.0157 -0.0452 75  LEU B O   
526  C CB  . LEU A 88  ? 0.2018 0.8838 0.2910 0.0621  -0.0213 -0.0503 75  LEU B CB  
527  C CG  . LEU A 88  ? 0.1885 0.8067 0.2718 0.0619  -0.0164 -0.0438 75  LEU B CG  
528  C CD1 . LEU A 88  ? 0.2258 0.8409 0.3159 0.0333  -0.0128 -0.0519 75  LEU B CD1 
529  C CD2 . LEU A 88  ? 0.2144 0.7845 0.2873 0.0625  -0.0171 -0.0387 75  LEU B CD2 
530  N N   . LYS A 89  ? 0.2650 1.0131 0.3552 0.1240  -0.0236 -0.0385 76  LYS B N   
531  C CA  . LYS A 89  ? 0.3003 1.0391 0.3850 0.1551  -0.0218 -0.0294 76  LYS B CA  
532  C C   . LYS A 89  ? 0.2918 1.0898 0.3880 0.1611  -0.0212 -0.0351 76  LYS B C   
533  O O   . LYS A 89  ? 0.3103 1.0961 0.4050 0.1759  -0.0176 -0.0318 76  LYS B O   
534  C CB  . LYS A 89  ? 0.3161 1.0582 0.3897 0.1854  -0.0253 -0.0196 76  LYS B CB  
535  C CG  . LYS A 89  ? 0.4180 1.0970 0.4779 0.1873  -0.0244 -0.0110 76  LYS B CG  
536  C CD  . LYS A 89  ? 0.4796 1.1524 0.5256 0.2211  -0.0260 0.0015  76  LYS B CD  
537  C CE  . LYS A 89  ? 0.5616 1.2401 0.6018 0.2184  -0.0301 0.0038  76  LYS B CE  
538  N NZ  . LYS A 89  ? 0.7182 1.4124 0.7470 0.2530  -0.0323 0.0149  76  LYS B NZ  
539  N N   . ALA A 90  ? 0.2551 1.1171 0.3626 0.1478  -0.0245 -0.0445 77  ALA B N   
540  C CA  . ALA A 90  ? 0.3152 1.2384 0.4341 0.1542  -0.0238 -0.0498 77  ALA B CA  
541  C C   . ALA A 90  ? 0.2964 1.2006 0.4213 0.1326  -0.0178 -0.0545 77  ALA B C   
542  O O   . ALA A 90  ? 0.2720 1.1969 0.4008 0.1468  -0.0150 -0.0541 77  ALA B O   
543  C CB  . ALA A 90  ? 0.2917 1.2952 0.4224 0.1442  -0.0285 -0.0596 77  ALA B CB  
544  N N   . CYS A 91  ? 0.2428 1.1110 0.3679 0.0997  -0.0158 -0.0588 78  CYS B N   
545  C CA  . CYS A 91  ? 0.3042 1.1526 0.4335 0.0774  -0.0100 -0.0624 78  CYS B CA  
546  C C   . CYS A 91  ? 0.3297 1.1295 0.4509 0.0972  -0.0061 -0.0540 78  CYS B C   
547  O O   . CYS A 91  ? 0.3216 1.1306 0.4473 0.0963  -0.0018 -0.0557 78  CYS B O   
548  C CB  . CYS A 91  ? 0.2982 1.1125 0.4263 0.0425  -0.0087 -0.0672 78  CYS B CB  
549  S SG  . CYS A 91  ? 0.2945 1.1712 0.4344 0.0089  -0.0102 -0.0815 78  CYS B SG  
550  N N   . VAL A 92  ? 0.3215 1.0709 0.4305 0.1146  -0.0074 -0.0453 79  VAL B N   
551  C CA  . VAL A 92  ? 0.3093 1.0074 0.4088 0.1320  -0.0038 -0.0379 79  VAL B CA  
552  C C   . VAL A 92  ? 0.3526 1.0814 0.4522 0.1627  -0.0030 -0.0359 79  VAL B C   
553  O O   . VAL A 92  ? 0.2867 1.0026 0.3855 0.1683  0.0014  -0.0360 79  VAL B O   
554  C CB  . VAL A 92  ? 0.3430 0.9807 0.4290 0.1403  -0.0049 -0.0295 79  VAL B CB  
555  C CG1 . VAL A 92  ? 0.3433 0.9311 0.4189 0.1586  -0.0013 -0.0227 79  VAL B CG1 
556  C CG2 . VAL A 92  ? 0.2638 0.8694 0.3496 0.1112  -0.0050 -0.0320 79  VAL B CG2 
557  N N   . ALA A 93  ? 0.2856 1.0561 0.3854 0.1839  -0.0071 -0.0341 80  ALA B N   
558  C CA  . ALA A 93  ? 0.3128 1.1150 0.4115 0.2172  -0.0067 -0.0317 80  ALA B CA  
559  C C   . ALA A 93  ? 0.2790 1.1312 0.3910 0.2087  -0.0036 -0.0403 80  ALA B C   
560  O O   . ALA A 93  ? 0.2807 1.1358 0.3908 0.2288  -0.0003 -0.0396 80  ALA B O   
561  C CB  . ALA A 93  ? 0.3077 1.1543 0.4051 0.2387  -0.0124 -0.0287 80  ALA B CB  
562  N N   . GLU A 94  ? 0.2739 1.1627 0.3987 0.1764  -0.0042 -0.0489 81  GLU B N   
563  C CA  . GLU A 94  ? 0.2800 1.2205 0.4178 0.1648  -0.0009 -0.0569 81  GLU B CA  
564  C C   . GLU A 94  ? 0.2670 1.1656 0.4023 0.1536  0.0054  -0.0570 81  GLU B C   
565  O O   . GLU A 94  ? 0.2466 1.1726 0.3865 0.1616  0.0093  -0.0598 81  GLU B O   
566  C CB  . GLU A 94  ? 0.3624 1.3540 0.5137 0.1312  -0.0023 -0.0665 81  GLU B CB  
567  C CG  . GLU A 94  ? 0.4404 1.5038 0.6054 0.1289  0.0004  -0.0739 81  GLU B CG  
568  C CD  . GLU A 94  ? 0.5337 1.6310 0.7106 0.0869  0.0023  -0.0837 81  GLU B CD  
569  O OE1 . GLU A 94  ? 0.5108 1.5945 0.6869 0.0634  -0.0003 -0.0865 81  GLU B OE1 
570  O OE2 . GLU A 94  ? 0.6580 1.7936 0.8440 0.0776  0.0070  -0.0886 81  GLU B OE2 
571  N N   . VAL A 95  ? 0.2480 1.0838 0.3763 0.1347  0.0065  -0.0542 82  VAL B N   
572  C CA  . VAL A 95  ? 0.2580 1.0505 0.3820 0.1264  0.0119  -0.0532 82  VAL B CA  
573  C C   . VAL A 95  ? 0.2795 1.0518 0.3944 0.1612  0.0136  -0.0485 82  VAL B C   
574  O O   . VAL A 95  ? 0.2607 1.0353 0.3761 0.1650  0.0182  -0.0507 82  VAL B O   
575  C CB  . VAL A 95  ? 0.2443 0.9732 0.3612 0.1046  0.0121  -0.0503 82  VAL B CB  
576  C CG1 . VAL A 95  ? 0.2280 0.9175 0.3405 0.0970  0.0174  -0.0492 82  VAL B CG1 
577  C CG2 . VAL A 95  ? 0.2335 0.9803 0.3575 0.0719  0.0107  -0.0557 82  VAL B CG2 
578  N N   . GLU A 96  ? 0.2590 1.0057 0.3636 0.1859  0.0105  -0.0419 83  GLU B N   
579  C CA  . GLU A 96  ? 0.2759 0.9904 0.3684 0.2174  0.0127  -0.0372 83  GLU B CA  
580  C C   . GLU A 96  ? 0.3834 1.1506 0.4807 0.2400  0.0144  -0.0408 83  GLU B C   
581  O O   . GLU A 96  ? 0.3845 1.1327 0.4757 0.2545  0.0187  -0.0414 83  GLU B O   
582  C CB  . GLU A 96  ? 0.3469 1.0198 0.4257 0.2375  0.0099  -0.0284 83  GLU B CB  
583  N N   . ARG A 97  ? 0.3338 1.1705 0.4421 0.2434  0.0110  -0.0439 84  ARG B N   
584  C CA  . ARG A 97  ? 0.3350 1.2290 0.4484 0.2679  0.0123  -0.0474 84  ARG B CA  
585  C C   . ARG A 97  ? 0.3003 1.2205 0.4241 0.2479  0.0175  -0.0552 84  ARG B C   
586  O O   . ARG A 97  ? 0.3571 1.2939 0.4800 0.2682  0.0212  -0.0576 84  ARG B O   
587  C CB  . ARG A 97  ? 0.2954 1.2542 0.4168 0.2764  0.0066  -0.0480 84  ARG B CB  
588  N N   . THR A 98  ? 0.3065 1.2292 0.4390 0.2090  0.0182  -0.0591 85  THR B N   
589  C CA  . THR A 98  ? 0.3048 1.2489 0.4455 0.1880  0.0237  -0.0651 85  THR B CA  
590  C C   . THR A 98  ? 0.3244 1.2095 0.4541 0.1917  0.0286  -0.0630 85  THR B C   
591  O O   . THR A 98  ? 0.3237 1.2316 0.4554 0.1999  0.0331  -0.0668 85  THR B O   
592  C CB  . THR A 98  ? 0.3350 1.2935 0.4855 0.1455  0.0237  -0.0690 85  THR B CB  
593  O OG1 . THR A 98  ? 0.3048 1.3202 0.4649 0.1431  0.0190  -0.0723 85  THR B OG1 
594  C CG2 . THR A 98  ? 0.3205 1.3143 0.4801 0.1237  0.0296  -0.0748 85  THR B CG2 
595  N N   . TRP A 99  ? 0.3147 1.1277 0.4330 0.1863  0.0277  -0.0575 86  TRP B N   
596  C CA  . TRP A 99  ? 0.3310 1.0919 0.4412 0.1779  0.0321  -0.0568 86  TRP B CA  
597  C C   . TRP A 99  ? 0.3645 1.0623 0.4586 0.2018  0.0319  -0.0520 86  TRP B C   
598  O O   . TRP A 99  ? 0.3652 1.0216 0.4520 0.1970  0.0353  -0.0523 86  TRP B O   
599  C CB  . TRP A 99  ? 0.2736 1.0080 0.3859 0.1401  0.0326  -0.0562 86  TRP B CB  
600  C CG  . TRP A 99  ? 0.2619 1.0420 0.3858 0.1125  0.0359  -0.0612 86  TRP B CG  
601  C CD1 . TRP A 99  ? 0.2522 1.0864 0.3838 0.1157  0.0399  -0.0662 86  TRP B CD1 
602  C CD2 . TRP A 99  ? 0.2254 0.9960 0.3527 0.0766  0.0364  -0.0612 86  TRP B CD2 
603  N NE1 . TRP A 99  ? 0.2240 1.0849 0.3640 0.0827  0.0429  -0.0690 86  TRP B NE1 
604  C CE2 . TRP A 99  ? 0.2403 1.0601 0.3769 0.0584  0.0410  -0.0660 86  TRP B CE2 
605  C CE3 . TRP A 99  ? 0.2235 0.9508 0.3464 0.0590  0.0337  -0.0580 86  TRP B CE3 
606  C CZ2 . TRP A 99  ? 0.2485 1.0701 0.3886 0.0222  0.0433  -0.0670 86  TRP B CZ2 
607  C CZ3 . TRP A 99  ? 0.2457 0.9751 0.3722 0.0252  0.0357  -0.0596 86  TRP B CZ3 
608  C CH2 . TRP A 99  ? 0.2352 1.0084 0.3694 0.0066  0.0407  -0.0637 86  TRP B CH2 
609  N N   . GLY A 100 ? 0.3170 1.0056 0.4045 0.2262  0.0283  -0.0474 87  GLY B N   
610  C CA  . GLY A 100 ? 0.3042 0.9266 0.3752 0.2437  0.0287  -0.0422 87  GLY B CA  
611  C C   . GLY A 100 ? 0.3207 0.8953 0.3873 0.2252  0.0256  -0.0367 87  GLY B C   
612  O O   . GLY A 100 ? 0.3039 0.8961 0.3799 0.1999  0.0233  -0.0375 87  GLY B O   
613  N N   . ALA A 101 ? 0.3077 0.8235 0.3597 0.2380  0.0259  -0.0315 88  ALA B N   
614  C CA  . ALA A 101 ? 0.3758 0.8481 0.4231 0.2236  0.0234  -0.0260 88  ALA B CA  
615  C C   . ALA A 101 ? 0.3780 0.8410 0.4326 0.1891  0.0236  -0.0286 88  ALA B C   
616  O O   . ALA A 101 ? 0.3059 0.7645 0.3620 0.1792  0.0270  -0.0326 88  ALA B O   
617  C CB  . ALA A 101 ? 0.4350 0.8453 0.4654 0.2393  0.0252  -0.0212 88  ALA B CB  
618  N N   . VAL A 102 ? 0.2864 0.7452 0.3445 0.1714  0.0202  -0.0261 89  VAL B N   
619  C CA  . VAL A 102 ? 0.2741 0.7138 0.3357 0.1418  0.0206  -0.0274 89  VAL B CA  
620  C C   . VAL A 102 ? 0.3019 0.6845 0.3534 0.1406  0.0230  -0.0253 89  VAL B C   
621  O O   . VAL A 102 ? 0.2903 0.6379 0.3314 0.1563  0.0228  -0.0212 89  VAL B O   
622  C CB  . VAL A 102 ? 0.2675 0.7085 0.3319 0.1287  0.0166  -0.0253 89  VAL B CB  
623  C CG1 . VAL A 102 ? 0.2722 0.6913 0.3389 0.0997  0.0171  -0.0265 89  VAL B CG1 
624  C CG2 . VAL A 102 ? 0.2347 0.7358 0.3091 0.1289  0.0143  -0.0289 89  VAL B CG2 
625  N N   . ASP A 103 ? 0.2567 0.6321 0.3105 0.1227  0.0256  -0.0283 90  ASP B N   
626  C CA  . ASP A 103 ? 0.2457 0.5724 0.2912 0.1182  0.0272  -0.0271 90  ASP B CA  
627  C C   . ASP A 103 ? 0.2192 0.5199 0.2648 0.0988  0.0250  -0.0239 90  ASP B C   
628  O O   . ASP A 103 ? 0.2914 0.5509 0.3294 0.0993  0.0250  -0.0213 90  ASP B O   
629  C CB  . ASP A 103 ? 0.2263 0.5617 0.2735 0.1103  0.0309  -0.0314 90  ASP B CB  
630  C CG  . ASP A 103 ? 0.2638 0.6190 0.3090 0.1309  0.0337  -0.0354 90  ASP B CG  
631  O OD1 . ASP A 103 ? 0.2824 0.6053 0.3173 0.1474  0.0346  -0.0352 90  ASP B OD1 
632  O OD2 . ASP A 103 ? 0.2257 0.6276 0.2790 0.1294  0.0354  -0.0391 90  ASP B OD2 
633  N N   . VAL A 104 ? 0.2201 0.5455 0.2739 0.0807  0.0239  -0.0250 91  VAL B N   
634  C CA  . VAL A 104 ? 0.2416 0.5441 0.2951 0.0612  0.0226  -0.0232 91  VAL B CA  
635  C C   . VAL A 104 ? 0.2251 0.5512 0.2842 0.0532  0.0197  -0.0238 91  VAL B C   
636  O O   . VAL A 104 ? 0.2495 0.6145 0.3161 0.0451  0.0202  -0.0276 91  VAL B O   
637  C CB  . VAL A 104 ? 0.2327 0.5298 0.2871 0.0421  0.0253  -0.0243 91  VAL B CB  
638  C CG1 . VAL A 104 ? 0.2013 0.4735 0.2541 0.0246  0.0240  -0.0221 91  VAL B CG1 
639  C CG2 . VAL A 104 ? 0.2085 0.4866 0.2572 0.0488  0.0280  -0.0246 91  VAL B CG2 
640  N N   . LEU A 105 ? 0.1970 0.5011 0.2525 0.0540  0.0169  -0.0208 92  LEU B N   
641  C CA  . LEU A 105 ? 0.1779 0.5029 0.2379 0.0440  0.0141  -0.0226 92  LEU B CA  
642  C C   . LEU A 105 ? 0.1744 0.4719 0.2323 0.0242  0.0142  -0.0226 92  LEU B C   
643  O O   . LEU A 105 ? 0.1994 0.4598 0.2512 0.0260  0.0141  -0.0190 92  LEU B O   
644  C CB  . LEU A 105 ? 0.2015 0.5308 0.2586 0.0607  0.0109  -0.0196 92  LEU B CB  
645  C CG  . LEU A 105 ? 0.2316 0.5749 0.2908 0.0517  0.0075  -0.0213 92  LEU B CG  
646  C CD1 . LEU A 105 ? 0.2129 0.6079 0.2814 0.0432  0.0067  -0.0277 92  LEU B CD1 
647  C CD2 . LEU A 105 ? 0.2214 0.5589 0.2745 0.0707  0.0048  -0.0159 92  LEU B CD2 
648  N N   . ILE A 106 ? 0.1825 0.4981 0.2448 0.0056  0.0144  -0.0269 93  ILE B N   
649  C CA  . ILE A 106 ? 0.1902 0.4790 0.2490 -0.0111 0.0144  -0.0273 93  ILE B CA  
650  C C   . ILE A 106 ? 0.1967 0.5035 0.2575 -0.0175 0.0115  -0.0313 93  ILE B C   
651  O O   . ILE A 106 ? 0.2161 0.5548 0.2821 -0.0294 0.0118  -0.0369 93  ILE B O   
652  C CB  . ILE A 106 ? 0.2131 0.4967 0.2718 -0.0301 0.0182  -0.0288 93  ILE B CB  
653  C CG1 . ILE A 106 ? 0.2257 0.5006 0.2828 -0.0236 0.0210  -0.0256 93  ILE B CG1 
654  C CG2 . ILE A 106 ? 0.2078 0.4585 0.2606 -0.0442 0.0184  -0.0286 93  ILE B CG2 
655  C CD1 . ILE A 106 ? 0.2466 0.5121 0.3012 -0.0406 0.0251  -0.0250 93  ILE B CD1 
656  N N   . ASN A 107 ? 0.1524 0.4368 0.2084 -0.0119 0.0091  -0.0290 94  ASN B N   
657  C CA  . ASN A 107 ? 0.1900 0.4885 0.2464 -0.0175 0.0063  -0.0332 94  ASN B CA  
658  C C   . ASN A 107 ? 0.1879 0.4662 0.2411 -0.0386 0.0078  -0.0374 94  ASN B C   
659  O O   . ASN A 107 ? 0.1777 0.4206 0.2251 -0.0387 0.0082  -0.0346 94  ASN B O   
660  C CB  . ASN A 107 ? 0.1852 0.4685 0.2366 -0.0013 0.0037  -0.0282 94  ASN B CB  
661  C CG  . ASN A 107 ? 0.2184 0.5220 0.2704 0.0203  0.0021  -0.0240 94  ASN B CG  
662  O OD1 . ASN A 107 ? 0.2068 0.5503 0.2644 0.0229  0.0011  -0.0272 94  ASN B OD1 
663  N ND2 . ASN A 107 ? 0.1903 0.4682 0.2362 0.0360  0.0023  -0.0169 94  ASN B ND2 
664  N N   . ASN A 108 ? 0.1909 0.4908 0.2475 -0.0562 0.0093  -0.0439 95  ASN B N   
665  C CA  . ASN A 108 ? 0.2360 0.5143 0.2880 -0.0776 0.0121  -0.0479 95  ASN B CA  
666  C C   . ASN A 108 ? 0.2523 0.5474 0.3041 -0.0926 0.0108  -0.0571 95  ASN B C   
667  O O   . ASN A 108 ? 0.2578 0.5250 0.3026 -0.1064 0.0125  -0.0605 95  ASN B O   
668  C CB  . ASN A 108 ? 0.2177 0.4991 0.2712 -0.0890 0.0166  -0.0472 95  ASN B CB  
669  C CG  . ASN A 108 ? 0.2586 0.5179 0.3057 -0.1121 0.0204  -0.0506 95  ASN B CG  
670  O OD1 . ASN A 108 ? 0.2580 0.4757 0.2967 -0.1134 0.0219  -0.0471 95  ASN B OD1 
671  N ND2 . ASN A 108 ? 0.2207 0.5070 0.2709 -0.1306 0.0223  -0.0575 95  ASN B ND2 
672  N N   . ALA A 109 ? 0.2371 0.5774 0.2956 -0.0895 0.0076  -0.0618 96  ALA B N   
673  C CA  . ALA A 109 ? 0.2394 0.6007 0.2980 -0.1063 0.0064  -0.0723 96  ALA B CA  
674  C C   . ALA A 109 ? 0.2285 0.5609 0.2790 -0.1039 0.0044  -0.0737 96  ALA B C   
675  O O   . ALA A 109 ? 0.2406 0.5656 0.2898 -0.0846 0.0017  -0.0675 96  ALA B O   
676  C CB  . ALA A 109 ? 0.1786 0.5962 0.2460 -0.0994 0.0028  -0.0758 96  ALA B CB  
677  N N   . ALA A 110 ? 0.2433 0.5599 0.2878 -0.1236 0.0061  -0.0820 97  ALA B N   
678  C CA  . ALA A 110 ? 0.3066 0.5990 0.3430 -0.1228 0.0046  -0.0853 97  ALA B CA  
679  C C   . ALA A 110 ? 0.3434 0.6330 0.3746 -0.1481 0.0068  -0.0979 97  ALA B C   
680  O O   . ALA A 110 ? 0.3211 0.6234 0.3547 -0.1659 0.0098  -0.1022 97  ALA B O   
681  C CB  . ALA A 110 ? 0.2891 0.5303 0.3186 -0.1143 0.0070  -0.0767 97  ALA B CB  
682  N N   . ARG A 111 ? 0.3535 0.6310 0.3775 -0.1501 0.0052  -0.1047 98  ARG B N   
683  C CA  . ARG A 111 ? 0.3890 0.6552 0.4052 -0.1736 0.0077  -0.1176 98  ARG B CA  
684  C C   . ARG A 111 ? 0.4314 0.6483 0.4353 -0.1695 0.0092  -0.1179 98  ARG B C   
685  O O   . ARG A 111 ? 0.3753 0.5921 0.3779 -0.1529 0.0057  -0.1158 98  ARG B O   
686  C CB  . ARG A 111 ? 0.4504 0.7665 0.4713 -0.1769 0.0029  -0.1279 98  ARG B CB  
687  C CG  . ARG A 111 ? 0.6008 0.9206 0.6172 -0.2064 0.0058  -0.1429 98  ARG B CG  
688  C CD  . ARG A 111 ? 0.6261 1.0104 0.6524 -0.2121 0.0016  -0.1510 98  ARG B CD  
689  N NE  . ARG A 111 ? 0.6667 1.0422 0.6853 -0.2424 0.0051  -0.1666 98  ARG B NE  
690  C CZ  . ARG A 111 ? 0.5853 0.9923 0.6029 -0.2536 0.0020  -0.1810 98  ARG B CZ  
691  N NH1 . ARG A 111 ? 0.5459 1.0029 0.5716 -0.2367 -0.0048 -0.1801 98  ARG B NH1 
692  N NH2 . ARG A 111 ? 0.4972 0.8841 0.5046 -0.2805 0.0058  -0.1956 98  ARG B NH2 
693  N N   . ASP A 112 ? 0.4576 0.6323 0.4517 -0.1838 0.0147  -0.1199 99  ASP B N   
694  C CA  . ASP A 112 ? 0.4900 0.6154 0.4726 -0.1760 0.0167  -0.1175 99  ASP B CA  
695  C C   . ASP A 112 ? 0.5612 0.6638 0.5308 -0.1924 0.0192  -0.1315 99  ASP B C   
696  O O   . ASP A 112 ? 0.6056 0.6603 0.5629 -0.1921 0.0231  -0.1308 99  ASP B O   
697  C CB  . ASP A 112 ? 0.5926 0.6817 0.5719 -0.1720 0.0208  -0.1061 99  ASP B CB  
698  C CG  . ASP A 112 ? 0.6292 0.7068 0.6042 -0.1942 0.0263  -0.1083 99  ASP B CG  
699  O OD1 . ASP A 112 ? 0.6518 0.7498 0.6267 -0.2148 0.0272  -0.1198 99  ASP B OD1 
700  O OD2 . ASP A 112 ? 0.7367 0.7871 0.7084 -0.1911 0.0298  -0.0982 99  ASP B OD2 
701  N N   . ASP A 113 ? 0.4703 0.6071 0.4418 -0.2047 0.0167  -0.1445 100 ASP B N   
702  C CA  . ASP A 113 ? 0.5234 0.6380 0.4815 -0.2221 0.0193  -0.1596 100 ASP B CA  
703  C C   . ASP A 113 ? 0.5182 0.6044 0.4672 -0.2052 0.0183  -0.1601 100 ASP B C   
704  O O   . ASP A 113 ? 0.5096 0.6133 0.4656 -0.1836 0.0139  -0.1521 100 ASP B O   
705  C CB  . ASP A 113 ? 0.6133 0.7748 0.5761 -0.2416 0.0171  -0.1742 100 ASP B CB  
706  C CG  . ASP A 113 ? 0.5289 0.7476 0.5035 -0.2276 0.0095  -0.1745 100 ASP B CG  
707  O OD1 . ASP A 113 ? 0.5486 0.7898 0.5344 -0.2084 0.0064  -0.1612 100 ASP B OD1 
708  O OD2 . ASP A 113 ? 0.5186 0.7572 0.4896 -0.2349 0.0070  -0.1879 100 ASP B OD2 
709  N N   . ARG A 114 ? 0.5203 0.5619 0.4531 -0.2147 0.0229  -0.1692 101 ARG B N   
710  C CA  . ARG A 114 ? 0.5188 0.5312 0.4413 -0.1998 0.0229  -0.1714 101 ARG B CA  
711  C C   . ARG A 114 ? 0.5268 0.5712 0.4488 -0.2015 0.0188  -0.1851 101 ARG B C   
712  O O   . ARG A 114 ? 0.5156 0.5912 0.4405 -0.2195 0.0174  -0.1958 101 ARG B O   
713  C CB  . ARG A 114 ? 0.5818 0.5360 0.4851 -0.2103 0.0297  -0.1786 101 ARG B CB  
714  N N   . HIS A 115 ? 0.4816 0.5245 0.4012 -0.1822 0.0164  -0.1838 102 HIS B N   
715  C CA  . HIS A 115 ? 0.5130 0.5870 0.4310 -0.1817 0.0124  -0.1957 102 HIS B CA  
716  C C   . HIS A 115 ? 0.4865 0.5410 0.3983 -0.1601 0.0124  -0.1922 102 HIS B C   
717  O O   . HIS A 115 ? 0.4841 0.5417 0.4036 -0.1406 0.0109  -0.1768 102 HIS B O   
718  C CB  . HIS A 115 ? 0.4702 0.6053 0.4037 -0.1779 0.0062  -0.1913 102 HIS B CB  
719  C CG  . HIS A 115 ? 0.4684 0.6140 0.4144 -0.1585 0.0042  -0.1713 102 HIS B CG  
720  N ND1 . HIS A 115 ? 0.4412 0.5922 0.3970 -0.1602 0.0049  -0.1607 102 HIS B ND1 
721  C CD2 . HIS A 115 ? 0.4374 0.5883 0.3861 -0.1357 0.0017  -0.1609 102 HIS B CD2 
722  C CE1 . HIS A 115 ? 0.4354 0.5940 0.3992 -0.1392 0.0027  -0.1453 102 HIS B CE1 
723  N NE2 . HIS A 115 ? 0.3809 0.5395 0.3402 -0.1251 0.0008  -0.1455 102 HIS B NE2 
724  N N   . ALA A 116 ? 0.5363 0.5687 0.4336 -0.1646 0.0147  -0.2068 103 ALA B N   
725  C CA  . ALA A 116 ? 0.5114 0.5339 0.4014 -0.1471 0.0146  -0.2085 103 ALA B CA  
726  C C   . ALA A 116 ? 0.4873 0.5592 0.3870 -0.1327 0.0087  -0.2029 103 ALA B C   
727  O O   . ALA A 116 ? 0.4600 0.5756 0.3658 -0.1396 0.0043  -0.2074 103 ALA B O   
728  C CB  . ALA A 116 ? 0.5050 0.5021 0.3772 -0.1597 0.0179  -0.2291 103 ALA B CB  
729  N N   . LEU A 117 ? 0.5039 0.5697 0.4047 -0.1112 0.0087  -0.1921 104 LEU B N   
730  C CA  . LEU A 117 ? 0.4807 0.5870 0.3885 -0.0968 0.0042  -0.1850 104 LEU B CA  
731  C C   . LEU A 117 ? 0.4600 0.5989 0.3618 -0.1030 0.0012  -0.2001 104 LEU B C   
732  O O   . LEU A 117 ? 0.4222 0.6053 0.3311 -0.0989 -0.0035 -0.1958 104 LEU B O   
733  C CB  . LEU A 117 ? 0.5372 0.6199 0.4422 -0.0778 0.0068  -0.1761 104 LEU B CB  
734  C CG  . LEU A 117 ? 0.6235 0.7348 0.5308 -0.0611 0.0045  -0.1692 104 LEU B CG  
735  C CD1 . LEU A 117 ? 0.6397 0.7235 0.5478 -0.0464 0.0078  -0.1579 104 LEU B CD1 
736  C CD2 . LEU A 117 ? 0.5560 0.6763 0.4518 -0.0614 0.0045  -0.1841 104 LEU B CD2 
737  N N   . ALA A 118 ? 0.5076 0.6248 0.3953 -0.1119 0.0040  -0.2180 105 ALA B N   
738  C CA  . ALA A 118 ? 0.5077 0.6549 0.3882 -0.1156 0.0013  -0.2330 105 ALA B CA  
739  C C   . ALA A 118 ? 0.5089 0.6905 0.3937 -0.1356 -0.0023 -0.2427 105 ALA B C   
740  O O   . ALA A 118 ? 0.5051 0.7281 0.3891 -0.1372 -0.0065 -0.2504 105 ALA B O   
741  C CB  . ALA A 118 ? 0.5686 0.6811 0.4317 -0.1181 0.0057  -0.2500 105 ALA B CB  
742  N N   . ASP A 119 ? 0.5104 0.6806 0.4012 -0.1496 -0.0009 -0.2403 106 ASP B N   
743  C CA  . ASP A 119 ? 0.5794 0.7813 0.4747 -0.1708 -0.0034 -0.2501 106 ASP B CA  
744  C C   . ASP A 119 ? 0.5446 0.7993 0.4560 -0.1636 -0.0092 -0.2371 106 ASP B C   
745  O O   . ASP A 119 ? 0.5944 0.8901 0.5098 -0.1773 -0.0127 -0.2463 106 ASP B O   
746  C CB  . ASP A 119 ? 0.6356 0.7998 0.5285 -0.1905 0.0016  -0.2539 106 ASP B CB  
747  C CG  . ASP A 119 ? 0.7020 0.8152 0.5761 -0.2017 0.0075  -0.2702 106 ASP B CG  
748  O OD1 . ASP A 119 ? 0.6791 0.7976 0.5430 -0.1998 0.0067  -0.2838 106 ASP B OD1 
749  O OD2 . ASP A 119 ? 0.7394 0.8064 0.6084 -0.2096 0.0131  -0.2680 106 ASP B OD2 
750  N N   . VAL A 120 ? 0.4289 0.6854 0.3485 -0.1422 -0.0102 -0.2171 107 VAL B N   
751  C CA  . VAL A 120 ? 0.3952 0.6908 0.3288 -0.1335 -0.0145 -0.2028 107 VAL B CA  
752  C C   . VAL A 120 ? 0.3986 0.7480 0.3329 -0.1250 -0.0204 -0.2043 107 VAL B C   
753  O O   . VAL A 120 ? 0.4315 0.7829 0.3598 -0.1102 -0.0211 -0.2011 107 VAL B O   
754  C CB  . VAL A 120 ? 0.3617 0.6319 0.3005 -0.1134 -0.0126 -0.1820 107 VAL B CB  
755  C CG1 . VAL A 120 ? 0.3278 0.6352 0.2784 -0.1003 -0.0166 -0.1667 107 VAL B CG1 
756  C CG2 . VAL A 120 ? 0.3636 0.5864 0.3027 -0.1201 -0.0074 -0.1784 107 VAL B CG2 
757  N N   . SER A 121 ? 0.3769 0.7726 0.3188 -0.1331 -0.0246 -0.2078 108 SER B N   
758  C CA  . SER A 121 ? 0.3367 0.7893 0.2801 -0.1242 -0.0307 -0.2079 108 SER B CA  
759  C C   . SER A 121 ? 0.2982 0.7680 0.2519 -0.1032 -0.0329 -0.1858 108 SER B C   
760  O O   . SER A 121 ? 0.2773 0.7209 0.2380 -0.1012 -0.0300 -0.1749 108 SER B O   
761  C CB  . SER A 121 ? 0.3496 0.8434 0.2955 -0.1458 -0.0338 -0.2252 108 SER B CB  
762  O OG  . SER A 121 ? 0.3440 0.8476 0.3021 -0.1518 -0.0337 -0.2190 108 SER B OG  
763  N N   . VAL A 122 ? 0.3066 0.8211 0.2600 -0.0879 -0.0380 -0.1797 109 VAL B N   
764  C CA  . VAL A 122 ? 0.2925 0.8240 0.2531 -0.0669 -0.0400 -0.1594 109 VAL B CA  
765  C C   . VAL A 122 ? 0.3132 0.8652 0.2859 -0.0744 -0.0411 -0.1589 109 VAL B C   
766  O O   . VAL A 122 ? 0.2984 0.8353 0.2779 -0.0637 -0.0395 -0.1440 109 VAL B O   
767  C CB  . VAL A 122 ? 0.2953 0.8723 0.2511 -0.0492 -0.0451 -0.1534 109 VAL B CB  
768  C CG1 . VAL A 122 ? 0.2879 0.8729 0.2492 -0.0267 -0.0461 -0.1315 109 VAL B CG1 
769  C CG2 . VAL A 122 ? 0.3070 0.8656 0.2504 -0.0407 -0.0434 -0.1524 109 VAL B CG2 
770  N N   . GLU A 123 ? 0.3279 0.9177 0.3031 -0.0934 -0.0440 -0.1760 110 GLU B N   
771  C CA  . GLU A 123 ? 0.3161 0.9337 0.3031 -0.1035 -0.0450 -0.1782 110 GLU B CA  
772  C C   . GLU A 123 ? 0.3052 0.8735 0.2966 -0.1135 -0.0390 -0.1746 110 GLU B C   
773  O O   . GLU A 123 ? 0.3018 0.8739 0.3025 -0.1051 -0.0385 -0.1627 110 GLU B O   
774  C CB  . GLU A 123 ? 0.2997 0.9630 0.2872 -0.1258 -0.0483 -0.1995 110 GLU B CB  
775  N N   . TYR A 124 ? 0.3093 0.8287 0.2927 -0.1282 -0.0342 -0.1836 111 TYR B N   
776  C CA  . TYR A 124 ? 0.3249 0.7969 0.3106 -0.1375 -0.0284 -0.1801 111 TYR B CA  
777  C C   . TYR A 124 ? 0.2866 0.7309 0.2757 -0.1151 -0.0267 -0.1593 111 TYR B C   
778  O O   . TYR A 124 ? 0.2666 0.7012 0.2633 -0.1143 -0.0247 -0.1507 111 TYR B O   
779  C CB  . TYR A 124 ? 0.3779 0.8037 0.3516 -0.1543 -0.0238 -0.1936 111 TYR B CB  
780  C CG  . TYR A 124 ? 0.3883 0.7659 0.3622 -0.1663 -0.0176 -0.1915 111 TYR B CG  
781  C CD1 . TYR A 124 ? 0.4122 0.7936 0.3885 -0.1914 -0.0151 -0.2017 111 TYR B CD1 
782  C CD2 . TYR A 124 ? 0.3661 0.6963 0.3373 -0.1525 -0.0141 -0.1787 111 TYR B CD2 
783  C CE1 . TYR A 124 ? 0.4168 0.7542 0.3920 -0.2008 -0.0092 -0.1976 111 TYR B CE1 
784  C CE2 . TYR A 124 ? 0.4046 0.6925 0.3749 -0.1614 -0.0088 -0.1757 111 TYR B CE2 
785  C CZ  . TYR A 124 ? 0.4478 0.7375 0.4191 -0.1855 -0.0062 -0.1851 111 TYR B CZ  
786  O OH  . TYR A 124 ? 0.4536 0.6991 0.4226 -0.1910 -0.0007 -0.1793 111 TYR B OH  
787  N N   . TRP A 125 ? 0.2877 0.7169 0.2702 -0.0974 -0.0271 -0.1515 112 TRP B N   
788  C CA  . TRP A 125 ? 0.2739 0.6780 0.2581 -0.0768 -0.0255 -0.1327 112 TRP B CA  
789  C C   . TRP A 125 ? 0.2530 0.6876 0.2469 -0.0640 -0.0280 -0.1205 112 TRP B C   
790  O O   . TRP A 125 ? 0.2428 0.6568 0.2424 -0.0606 -0.0254 -0.1111 112 TRP B O   
791  C CB  . TRP A 125 ? 0.2366 0.6375 0.2124 -0.0608 -0.0264 -0.1274 112 TRP B CB  
792  C CG  . TRP A 125 ? 0.2622 0.6443 0.2399 -0.0406 -0.0250 -0.1079 112 TRP B CG  
793  C CD1 . TRP A 125 ? 0.2552 0.6599 0.2362 -0.0233 -0.0273 -0.0943 112 TRP B CD1 
794  C CD2 . TRP A 125 ? 0.2525 0.5879 0.2278 -0.0364 -0.0205 -0.1007 112 TRP B CD2 
795  N NE1 . TRP A 125 ? 0.2655 0.6388 0.2462 -0.0107 -0.0243 -0.0798 112 TRP B NE1 
796  C CE2 . TRP A 125 ? 0.2437 0.5765 0.2216 -0.0187 -0.0203 -0.0836 112 TRP B CE2 
797  C CE3 . TRP A 125 ? 0.2553 0.5520 0.2261 -0.0455 -0.0166 -0.1075 112 TRP B CE3 
798  C CZ2 . TRP A 125 ? 0.2448 0.5392 0.2219 -0.0120 -0.0164 -0.0738 112 TRP B CZ2 
799  C CZ3 . TRP A 125 ? 0.2721 0.5336 0.2423 -0.0368 -0.0131 -0.0972 112 TRP B CZ3 
800  C CH2 . TRP A 125 ? 0.2496 0.5121 0.2234 -0.0210 -0.0132 -0.0809 112 TRP B CH2 
801  N N   . ASP A 126 ? 0.2602 0.7458 0.2555 -0.0569 -0.0331 -0.1215 113 ASP B N   
802  C CA  . ASP A 126 ? 0.2641 0.7812 0.2667 -0.0410 -0.0357 -0.1099 113 ASP B CA  
803  C C   . ASP A 126 ? 0.2585 0.7806 0.2713 -0.0541 -0.0341 -0.1135 113 ASP B C   
804  O O   . ASP A 126 ? 0.2212 0.7356 0.2395 -0.0425 -0.0327 -0.1015 113 ASP B O   
805  C CB  . ASP A 126 ? 0.2949 0.8705 0.2966 -0.0322 -0.0417 -0.1121 113 ASP B CB  
806  C CG  . ASP A 126 ? 0.3097 0.8851 0.3008 -0.0139 -0.0433 -0.1038 113 ASP B CG  
807  O OD1 . ASP A 126 ? 0.3101 0.8423 0.2958 -0.0086 -0.0397 -0.0963 113 ASP B OD1 
808  O OD2 . ASP A 126 ? 0.3641 0.9854 0.3521 -0.0066 -0.0482 -0.1058 113 ASP B OD2 
809  N N   . GLU A 127 ? 0.2824 0.8181 0.2971 -0.0787 -0.0339 -0.1302 114 GLU B N   
810  C CA  . GLU A 127 ? 0.3096 0.8550 0.3337 -0.0936 -0.0319 -0.1342 114 GLU B CA  
811  C C   . GLU A 127 ? 0.2833 0.7743 0.3079 -0.0952 -0.0261 -0.1260 114 GLU B C   
812  O O   . GLU A 127 ? 0.2811 0.7750 0.3132 -0.0907 -0.0247 -0.1183 114 GLU B O   
813  C CB  . GLU A 127 ? 0.3503 0.9197 0.3749 -0.1219 -0.0322 -0.1539 114 GLU B CB  
814  C CG  . GLU A 127 ? 0.4812 1.0469 0.5130 -0.1420 -0.0281 -0.1582 114 GLU B CG  
815  C CD  . GLU A 127 ? 0.6422 1.2363 0.6756 -0.1722 -0.0278 -0.1772 114 GLU B CD  
816  O OE1 . GLU A 127 ? 0.7048 1.3105 0.7314 -0.1823 -0.0300 -0.1905 114 GLU B OE1 
817  O OE2 . GLU A 127 ? 0.7624 1.3688 0.8035 -0.1865 -0.0251 -0.1790 114 GLU B OE2 
818  N N   . ARG A 128 ? 0.2722 0.7135 0.2880 -0.0987 -0.0229 -0.1266 115 ARG B N   
819  C CA  . ARG A 128 ? 0.2833 0.6753 0.2986 -0.0995 -0.0178 -0.1191 115 ARG B CA  
820  C C   . ARG A 128 ? 0.2881 0.6697 0.3062 -0.0753 -0.0180 -0.1016 115 ARG B C   
821  O O   . ARG A 128 ? 0.2602 0.6234 0.2827 -0.0745 -0.0151 -0.0946 115 ARG B O   
822  C CB  . ARG A 128 ? 0.3412 0.6858 0.3465 -0.1120 -0.0139 -0.1263 115 ARG B CB  
823  C CG  . ARG A 128 ? 0.3270 0.6739 0.3286 -0.1389 -0.0122 -0.1435 115 ARG B CG  
824  C CD  . ARG A 128 ? 0.4086 0.7493 0.4165 -0.1509 -0.0086 -0.1408 115 ARG B CD  
825  N NE  . ARG A 128 ? 0.4547 0.7877 0.4575 -0.1788 -0.0053 -0.1559 115 ARG B NE  
826  C CZ  . ARG A 128 ? 0.5297 0.9049 0.5349 -0.1944 -0.0077 -0.1690 115 ARG B CZ  
827  N NH1 . ARG A 128 ? 0.6006 1.0318 0.6165 -0.1844 -0.0127 -0.1663 115 ARG B NH1 
828  N NH2 . ARG A 128 ? 0.5397 0.9019 0.5363 -0.2193 -0.0049 -0.1850 115 ARG B NH2 
829  N N   . MET A 129 ? 0.2483 0.6416 0.2633 -0.0562 -0.0210 -0.0944 116 MET B N   
830  C CA  . MET A 129 ? 0.2841 0.6681 0.3006 -0.0344 -0.0208 -0.0783 116 MET B CA  
831  C C   . MET A 129 ? 0.2497 0.6662 0.2748 -0.0280 -0.0222 -0.0742 116 MET B C   
832  O O   . MET A 129 ? 0.2669 0.6669 0.2950 -0.0182 -0.0201 -0.0643 116 MET B O   
833  C CB  . MET A 129 ? 0.2834 0.6699 0.2927 -0.0162 -0.0228 -0.0703 116 MET B CB  
834  C CG  . MET A 129 ? 0.2691 0.6222 0.2701 -0.0198 -0.0207 -0.0728 116 MET B CG  
835  S SD  . MET A 129 ? 0.3453 0.6473 0.3479 -0.0175 -0.0157 -0.0630 116 MET B SD  
836  C CE  . MET A 129 ? 0.2935 0.5612 0.2892 -0.0312 -0.0129 -0.0731 116 MET B CE  
837  N N   . GLN A 130 ? 0.2894 0.7531 0.3187 -0.0346 -0.0255 -0.0830 117 GLN B N   
838  C CA  . GLN A 130 ? 0.2939 0.7946 0.3321 -0.0285 -0.0268 -0.0805 117 GLN B CA  
839  C C   . GLN A 130 ? 0.2615 0.7464 0.3062 -0.0428 -0.0226 -0.0826 117 GLN B C   
840  O O   . GLN A 130 ? 0.2463 0.7348 0.2959 -0.0311 -0.0216 -0.0744 117 GLN B O   
841  C CB  . GLN A 130 ? 0.3419 0.9037 0.3839 -0.0308 -0.0317 -0.0891 117 GLN B CB  
842  C CG  . GLN A 130 ? 0.3827 0.9667 0.4178 -0.0144 -0.0362 -0.0860 117 GLN B CG  
843  C CD  . GLN A 130 ? 0.4287 1.0774 0.4680 -0.0186 -0.0414 -0.0961 117 GLN B CD  
844  O OE1 . GLN A 130 ? 0.4002 1.0799 0.4481 -0.0362 -0.0416 -0.1071 117 GLN B OE1 
845  N NE2 . GLN A 130 ? 0.5283 1.2021 0.5615 -0.0018 -0.0457 -0.0919 117 GLN B NE2 
846  N N   . THR A 131 ? 0.2662 0.7340 0.3097 -0.0675 -0.0200 -0.0934 118 THR B N   
847  C CA  . THR A 131 ? 0.2701 0.7244 0.3180 -0.0844 -0.0155 -0.0962 118 THR B CA  
848  C C   . THR A 131 ? 0.2648 0.6656 0.3091 -0.0781 -0.0114 -0.0859 118 THR B C   
849  O O   . THR A 131 ? 0.2495 0.6400 0.2977 -0.0810 -0.0082 -0.0819 118 THR B O   
850  C CB  . THR A 131 ? 0.3104 0.7602 0.3540 -0.1113 -0.0142 -0.1111 118 THR B CB  
851  O OG1 . THR A 131 ? 0.3951 0.9012 0.4451 -0.1218 -0.0171 -0.1214 118 THR B OG1 
852  C CG2 . THR A 131 ? 0.4021 0.8227 0.4450 -0.1323 -0.0085 -0.1143 118 THR B CG2 
853  N N   . ASN A 132 ? 0.2350 0.6025 0.2717 -0.0687 -0.0116 -0.0813 119 ASN B N   
854  C CA  . ASN A 132 ? 0.2816 0.6000 0.3145 -0.0653 -0.0079 -0.0736 119 ASN B CA  
855  C C   . ASN A 132 ? 0.2457 0.5546 0.2790 -0.0424 -0.0084 -0.0603 119 ASN B C   
856  O O   . ASN A 132 ? 0.2409 0.5205 0.2740 -0.0395 -0.0056 -0.0539 119 ASN B O   
857  C CB  . ASN A 132 ? 0.3499 0.6321 0.3739 -0.0739 -0.0062 -0.0783 119 ASN B CB  
858  C CG  . ASN A 132 ? 0.4441 0.7176 0.4651 -0.0981 -0.0035 -0.0901 119 ASN B CG  
859  O OD1 . ASN A 132 ? 0.5323 0.7791 0.5520 -0.1071 0.0005  -0.0885 119 ASN B OD1 
860  N ND2 . ASN A 132 ? 0.5909 0.8883 0.6104 -0.1103 -0.0053 -0.1019 119 ASN B ND2 
861  N N   . LEU A 133 ? 0.2008 0.5320 0.2334 -0.0259 -0.0118 -0.0558 120 LEU B N   
862  C CA  . LEU A 133 ? 0.1958 0.5074 0.2255 -0.0064 -0.0112 -0.0435 120 LEU B CA  
863  C C   . LEU A 133 ? 0.2001 0.5430 0.2327 0.0112  -0.0134 -0.0374 120 LEU B C   
864  O O   . LEU A 133 ? 0.2294 0.5588 0.2624 0.0228  -0.0116 -0.0294 120 LEU B O   
865  C CB  . LEU A 133 ? 0.2196 0.5179 0.2414 -0.0009 -0.0122 -0.0416 120 LEU B CB  
866  C CG  . LEU A 133 ? 0.1727 0.4543 0.1901 0.0182  -0.0115 -0.0288 120 LEU B CG  
867  C CD1 . LEU A 133 ? 0.1968 0.4431 0.2154 0.0167  -0.0079 -0.0244 120 LEU B CD1 
868  C CD2 . LEU A 133 ? 0.2370 0.5076 0.2466 0.0212  -0.0118 -0.0273 120 LEU B CD2 
869  N N   . ARG A 134 ? 0.2104 0.5941 0.2434 0.0149  -0.0172 -0.0410 121 ARG B N   
870  C CA  . ARG A 134 ? 0.2243 0.6350 0.2566 0.0368  -0.0196 -0.0332 121 ARG B CA  
871  C C   . ARG A 134 ? 0.2319 0.6561 0.2711 0.0430  -0.0183 -0.0310 121 ARG B C   
872  O O   . ARG A 134 ? 0.2043 0.6212 0.2403 0.0631  -0.0176 -0.0212 121 ARG B O   
873  C CB  . ARG A 134 ? 0.2294 0.6865 0.2614 0.0375  -0.0243 -0.0390 121 ARG B CB  
874  C CG  . ARG A 134 ? 0.2280 0.7129 0.2574 0.0629  -0.0269 -0.0296 121 ARG B CG  
875  C CD  . ARG A 134 ? 0.2211 0.7529 0.2493 0.0639  -0.0319 -0.0352 121 ARG B CD  
876  N NE  . ARG A 134 ? 0.2317 0.8110 0.2704 0.0500  -0.0342 -0.0476 121 ARG B NE  
877  C CZ  . ARG A 134 ? 0.2546 0.8849 0.2946 0.0492  -0.0390 -0.0546 121 ARG B CZ  
878  N NH1 . ARG A 134 ? 0.2523 0.8926 0.2833 0.0614  -0.0422 -0.0505 121 ARG B NH1 
879  N NH2 . ARG A 134 ? 0.2482 0.9211 0.2983 0.0353  -0.0405 -0.0658 121 ARG B NH2 
880  N N   . HIS A 135 ? 0.2300 0.6725 0.2774 0.0256  -0.0177 -0.0403 122 HIS B N   
881  C CA  . HIS A 135 ? 0.2429 0.7046 0.2977 0.0296  -0.0162 -0.0398 122 HIS B CA  
882  C C   . HIS A 135 ? 0.2314 0.6515 0.2836 0.0375  -0.0123 -0.0317 122 HIS B C   
883  O O   . HIS A 135 ? 0.1975 0.6267 0.2519 0.0511  -0.0112 -0.0276 122 HIS B O   
884  C CB  . HIS A 135 ? 0.2294 0.7183 0.2928 0.0058  -0.0155 -0.0515 122 HIS B CB  
885  C CG  . HIS A 135 ? 0.2414 0.6892 0.3028 -0.0157 -0.0117 -0.0552 122 HIS B CG  
886  N ND1 . HIS A 135 ? 0.2070 0.6227 0.2685 -0.0182 -0.0075 -0.0510 122 HIS B ND1 
887  C CD2 . HIS A 135 ? 0.2377 0.6714 0.2955 -0.0340 -0.0116 -0.0626 122 HIS B CD2 
888  C CE1 . HIS A 135 ? 0.2202 0.6050 0.2784 -0.0371 -0.0051 -0.0551 122 HIS B CE1 
889  N NE2 . HIS A 135 ? 0.2558 0.6512 0.3117 -0.0472 -0.0073 -0.0627 122 HIS B NE2 
890  N N   . ALA A 136 ? 0.2180 0.5930 0.2652 0.0293  -0.0101 -0.0300 123 ALA B N   
891  C CA  . ALA A 136 ? 0.1987 0.5362 0.2440 0.0331  -0.0065 -0.0242 123 ALA B CA  
892  C C   . ALA A 136 ? 0.1892 0.5158 0.2283 0.0571  -0.0065 -0.0141 123 ALA B C   
893  O O   . ALA A 136 ? 0.2031 0.5203 0.2420 0.0670  -0.0043 -0.0103 123 ALA B O   
894  C CB  . ALA A 136 ? 0.1917 0.4879 0.2335 0.0188  -0.0043 -0.0251 123 ALA B CB  
895  N N   . PHE A 137 ? 0.1935 0.5229 0.2264 0.0670  -0.0088 -0.0101 124 PHE B N   
896  C CA  . PHE A 137 ? 0.1928 0.5086 0.2173 0.0892  -0.0082 0.0004  124 PHE B CA  
897  C C   . PHE A 137 ? 0.2101 0.5610 0.2371 0.1058  -0.0094 0.0016  124 PHE B C   
898  O O   . PHE A 137 ? 0.2082 0.5444 0.2308 0.1220  -0.0072 0.0077  124 PHE B O   
899  C CB  . PHE A 137 ? 0.2108 0.5263 0.2273 0.0953  -0.0103 0.0049  124 PHE B CB  
900  C CG  . PHE A 137 ? 0.2170 0.5239 0.2234 0.1196  -0.0095 0.0166  124 PHE B CG  
901  C CD1 . PHE A 137 ? 0.2248 0.4879 0.2240 0.1255  -0.0054 0.0240  124 PHE B CD1 
902  C CD2 . PHE A 137 ? 0.2205 0.5636 0.2243 0.1366  -0.0125 0.0197  124 PHE B CD2 
903  C CE1 . PHE A 137 ? 0.2867 0.5370 0.2751 0.1469  -0.0037 0.0343  124 PHE B CE1 
904  C CE2 . PHE A 137 ? 0.2721 0.6029 0.2650 0.1603  -0.0111 0.0311  124 PHE B CE2 
905  C CZ  . PHE A 137 ? 0.2933 0.5759 0.2778 0.1651  -0.0064 0.0384  124 PHE B CZ  
906  N N   . PHE A 138 ? 0.1819 0.5795 0.2153 0.1020  -0.0129 -0.0048 125 PHE B N   
907  C CA  . PHE A 138 ? 0.2062 0.6452 0.2418 0.1204  -0.0147 -0.0035 125 PHE B CA  
908  C C   . PHE A 138 ? 0.2033 0.6457 0.2456 0.1203  -0.0118 -0.0063 125 PHE B C   
909  O O   . PHE A 138 ? 0.2065 0.6601 0.2466 0.1419  -0.0111 -0.0018 125 PHE B O   
910  C CB  . PHE A 138 ? 0.2103 0.7042 0.2500 0.1204  -0.0196 -0.0087 125 PHE B CB  
911  C CG  . PHE A 138 ? 0.2302 0.7203 0.2591 0.1339  -0.0221 -0.0011 125 PHE B CG  
912  C CD1 . PHE A 138 ? 0.2249 0.7086 0.2436 0.1620  -0.0218 0.0108  125 PHE B CD1 
913  C CD2 . PHE A 138 ? 0.2298 0.7108 0.2563 0.1186  -0.0234 -0.0047 125 PHE B CD2 
914  C CE1 . PHE A 138 ? 0.2847 0.7609 0.2914 0.1747  -0.0232 0.0195  125 PHE B CE1 
915  C CE2 . PHE A 138 ? 0.2432 0.7194 0.2588 0.1314  -0.0251 0.0031  125 PHE B CE2 
916  C CZ  . PHE A 138 ? 0.2533 0.7250 0.2588 0.1584  -0.0247 0.0157  125 PHE B CZ  
917  N N   . ALA A 139 ? 0.1923 0.6259 0.2415 0.0973  -0.0098 -0.0135 126 ALA B N   
918  C CA  . ALA A 139 ? 0.2088 0.6448 0.2636 0.0955  -0.0066 -0.0159 126 ALA B CA  
919  C C   . ALA A 139 ? 0.2659 0.6582 0.3126 0.1101  -0.0032 -0.0084 126 ALA B C   
920  O O   . ALA A 139 ? 0.2565 0.6563 0.3036 0.1236  -0.0013 -0.0076 126 ALA B O   
921  C CB  . ALA A 139 ? 0.1844 0.6163 0.2459 0.0680  -0.0048 -0.0236 126 ALA B CB  
922  N N   . ALA A 140 ? 0.2308 0.5785 0.2697 0.1072  -0.0023 -0.0037 127 ALA B N   
923  C CA  . ALA A 140 ? 0.2319 0.5374 0.2628 0.1176  0.0011  0.0021  127 ALA B CA  
924  C C   . ALA A 140 ? 0.2465 0.5558 0.2690 0.1447  0.0010  0.0093  127 ALA B C   
925  O O   . ALA A 140 ? 0.3025 0.5973 0.3201 0.1592  0.0038  0.0118  127 ALA B O   
926  C CB  . ALA A 140 ? 0.2055 0.4687 0.2307 0.1073  0.0019  0.0053  127 ALA B CB  
927  N N   . GLN A 141 ? 0.2455 0.5744 0.2649 0.1527  -0.0023 0.0127  128 GLN B N   
928  C CA  . GLN A 141 ? 0.2380 0.5713 0.2477 0.1800  -0.0025 0.0209  128 GLN B CA  
929  C C   . GLN A 141 ? 0.2652 0.6348 0.2799 0.1949  -0.0025 0.0179  128 GLN B C   
930  O O   . GLN A 141 ? 0.2760 0.6315 0.2814 0.2176  -0.0002 0.0236  128 GLN B O   
931  C CB  . GLN A 141 ? 0.2580 0.6101 0.2633 0.1859  -0.0062 0.0253  128 GLN B CB  
932  C CG  . GLN A 141 ? 0.2773 0.6380 0.2711 0.2162  -0.0067 0.0350  128 GLN B CG  
933  C CD  . GLN A 141 ? 0.3090 0.7012 0.3002 0.2214  -0.0112 0.0381  128 GLN B CD  
934  O OE1 . GLN A 141 ? 0.3216 0.7651 0.3233 0.2154  -0.0154 0.0306  128 GLN B OE1 
935  N NE2 . GLN A 141 ? 0.4108 0.7737 0.3879 0.2305  -0.0102 0.0485  128 GLN B NE2 
936  N N   . ALA A 142 ? 0.2631 0.6776 0.2915 0.1816  -0.0046 0.0088  129 ALA B N   
937  C CA  . ALA A 142 ? 0.2397 0.6987 0.2745 0.1946  -0.0048 0.0052  129 ALA B CA  
938  C C   . ALA A 142 ? 0.2718 0.7089 0.3062 0.1978  -0.0001 0.0034  129 ALA B C   
939  O O   . ALA A 142 ? 0.2760 0.7272 0.3074 0.2211  0.0011  0.0050  129 ALA B O   
940  C CB  . ALA A 142 ? 0.2265 0.7394 0.2759 0.1760  -0.0076 -0.0045 129 ALA B CB  
941  N N   . VAL A 143 ? 0.2493 0.6562 0.2865 0.1758  0.0023  -0.0002 130 VAL B N   
942  C CA  . VAL A 143 ? 0.2680 0.6588 0.3054 0.1762  0.0065  -0.0030 130 VAL B CA  
943  C C   . VAL A 143 ? 0.2805 0.6198 0.3036 0.1927  0.0096  0.0033  130 VAL B C   
944  O O   . VAL A 143 ? 0.2768 0.6062 0.2969 0.2024  0.0130  0.0015  130 VAL B O   
945  C CB  . VAL A 143 ? 0.2359 0.6168 0.2809 0.1475  0.0079  -0.0088 130 VAL B CB  
946  C CG1 . VAL A 143 ? 0.2257 0.6566 0.2836 0.1298  0.0059  -0.0158 130 VAL B CG1 
947  C CG2 . VAL A 143 ? 0.2048 0.5354 0.2433 0.1353  0.0082  -0.0053 130 VAL B CG2 
948  N N   . ALA A 144 ? 0.2889 0.5944 0.3025 0.1948  0.0090  0.0102  131 ALA B N   
949  C CA  . ALA A 144 ? 0.2947 0.5461 0.2945 0.2037  0.0127  0.0155  131 ALA B CA  
950  C C   . ALA A 144 ? 0.3380 0.5868 0.3283 0.2321  0.0153  0.0179  131 ALA B C   
951  O O   . ALA A 144 ? 0.3487 0.5650 0.3321 0.2359  0.0193  0.0163  131 ALA B O   
952  C CB  . ALA A 144 ? 0.2995 0.5214 0.2901 0.2026  0.0120  0.0234  131 ALA B CB  
953  N N   . PRO A 145 ? 0.3561 0.6313 0.3422 0.2554  0.0136  0.0227  132 PRO B N   
954  C CA  . PRO A 145 ? 0.3806 0.6408 0.3536 0.2846  0.0169  0.0263  132 PRO B CA  
955  C C   . PRO A 145 ? 0.3654 0.6379 0.3435 0.2880  0.0197  0.0177  132 PRO B C   
956  O O   . PRO A 145 ? 0.3880 0.6250 0.3538 0.3025  0.0241  0.0179  132 PRO B O   
957  C CB  . PRO A 145 ? 0.4281 0.7239 0.3975 0.3088  0.0138  0.0328  132 PRO B CB  
958  C CG  . PRO A 145 ? 0.3949 0.6944 0.3685 0.2894  0.0100  0.0359  132 PRO B CG  
959  C CD  . PRO A 145 ? 0.3665 0.6792 0.3566 0.2572  0.0088  0.0260  132 PRO B CD  
960  N N   . GLY A 146 ? 0.3426 0.6628 0.3378 0.2732  0.0175  0.0098  133 GLY B N   
961  C CA  . GLY A 146 ? 0.3474 0.6844 0.3478 0.2758  0.0205  0.0017  133 GLY B CA  
962  C C   . GLY A 146 ? 0.3824 0.6740 0.3796 0.2591  0.0241  -0.0022 133 GLY B C   
963  O O   . GLY A 146 ? 0.3674 0.6425 0.3583 0.2693  0.0281  -0.0061 133 GLY B O   
964  N N   . MET A 147 ? 0.3561 0.6263 0.3566 0.2339  0.0226  -0.0012 134 MET B N   
965  C CA  . MET A 147 ? 0.3363 0.5647 0.3335 0.2180  0.0254  -0.0040 134 MET B CA  
966  C C   . MET A 147 ? 0.3557 0.5325 0.3353 0.2339  0.0291  -0.0006 134 MET B C   
967  O O   . MET A 147 ? 0.3572 0.5103 0.3320 0.2327  0.0325  -0.0057 134 MET B O   
968  C CB  . MET A 147 ? 0.2932 0.5080 0.2955 0.1923  0.0230  -0.0023 134 MET B CB  
969  C CG  . MET A 147 ? 0.2454 0.4961 0.2622 0.1719  0.0212  -0.0075 134 MET B CG  
970  S SD  . MET A 147 ? 0.2733 0.5074 0.2938 0.1468  0.0184  -0.0050 134 MET B SD  
971  C CE  . MET A 147 ? 0.2240 0.4974 0.2588 0.1249  0.0178  -0.0118 134 MET B CE  
972  N N   . ALA A 148 ? 0.3902 0.5479 0.3595 0.2467  0.0286  0.0078  135 ALA B N   
973  C CA  . ALA A 148 ? 0.4011 0.5051 0.3516 0.2602  0.0327  0.0121  135 ALA B CA  
974  C C   . ALA A 148 ? 0.4517 0.5522 0.3925 0.2858  0.0365  0.0092  135 ALA B C   
975  O O   . ALA A 148 ? 0.5052 0.5599 0.4325 0.2897  0.0410  0.0074  135 ALA B O   
976  C CB  . ALA A 148 ? 0.4582 0.5452 0.3986 0.2689  0.0318  0.0232  135 ALA B CB  
977  N N   . ARG A 149 ? 0.4785 0.6262 0.4248 0.3044  0.0347  0.0087  136 ARG B N   
978  C CA  . ARG A 149 ? 0.5177 0.6675 0.4554 0.3312  0.0384  0.0051  136 ARG B CA  
979  C C   . ARG A 149 ? 0.5446 0.6850 0.4853 0.3192  0.0415  -0.0058 136 ARG B C   
980  O O   . ARG A 149 ? 0.5384 0.6463 0.4652 0.3339  0.0463  -0.0094 136 ARG B O   
981  C CB  . ARG A 149 ? 0.5810 0.7897 0.5254 0.3537  0.0359  0.0057  136 ARG B CB  
982  C CG  . ARG A 149 ? 0.7602 0.9661 0.6917 0.3819  0.0351  0.0165  136 ARG B CG  
983  C CD  . ARG A 149 ? 0.6845 0.9480 0.6197 0.4105  0.0330  0.0174  136 ARG B CD  
984  N NE  . ARG A 149 ? 0.6963 1.0261 0.6552 0.3920  0.0291  0.0097  136 ARG B NE  
985  C CZ  . ARG A 149 ? 0.7460 1.1126 0.7203 0.3698  0.0239  0.0100  136 ARG B CZ  
986  N NH1 . ARG A 149 ? 0.6487 1.0114 0.6188 0.3711  0.0205  0.0189  136 ARG B NH1 
987  N NH2 . ARG A 149 ? 0.7008 1.1105 0.6938 0.3476  0.0225  0.0012  136 ARG B NH2 
988  N N   . ARG A 150 ? 0.4782 0.6462 0.4357 0.2928  0.0391  -0.0109 137 ARG B N   
989  C CA  . ARG A 150 ? 0.4486 0.6137 0.4092 0.2813  0.0417  -0.0205 137 ARG B CA  
990  C C   . ARG A 150 ? 0.4589 0.5657 0.4090 0.2675  0.0441  -0.0215 137 ARG B C   
991  O O   . ARG A 150 ? 0.4959 0.5823 0.4394 0.2678  0.0477  -0.0290 137 ARG B O   
992  C CB  . ARG A 150 ? 0.4403 0.6564 0.4201 0.2614  0.0392  -0.0250 137 ARG B CB  
993  C CG  . ARG A 150 ? 0.3931 0.6020 0.3766 0.2416  0.0411  -0.0324 137 ARG B CG  
994  C CD  . ARG A 150 ? 0.3653 0.6231 0.3654 0.2233  0.0398  -0.0360 137 ARG B CD  
995  N NE  . ARG A 150 ? 0.3892 0.6487 0.3966 0.2046  0.0357  -0.0302 137 ARG B NE  
996  C CZ  . ARG A 150 ? 0.3478 0.6436 0.3657 0.1983  0.0324  -0.0275 137 ARG B CZ  
997  N NH1 . ARG A 150 ? 0.3152 0.5966 0.3353 0.1826  0.0294  -0.0230 137 ARG B NH1 
998  N NH2 . ARG A 150 ? 0.4121 0.7595 0.4382 0.2072  0.0324  -0.0303 137 ARG B NH2 
999  N N   . GLY A 151 ? 0.4473 0.5304 0.3966 0.2530  0.0421  -0.0149 138 GLY B N   
1000 C CA  . GLY A 151 ? 0.4107 0.4457 0.3525 0.2370  0.0440  -0.0163 138 GLY B CA  
1001 C C   . GLY A 151 ? 0.3838 0.4307 0.3390 0.2083  0.0411  -0.0185 138 GLY B C   
1002 O O   . GLY A 151 ? 0.3924 0.4072 0.3431 0.1944  0.0425  -0.0211 138 GLY B O   
1003 N N   . SER A 152 ? 0.3349 0.4269 0.3054 0.1996  0.0375  -0.0178 139 SER B N   
1004 C CA  . SER A 152 ? 0.3378 0.4378 0.3189 0.1739  0.0355  -0.0199 139 SER B CA  
1005 C C   . SER A 152 ? 0.3095 0.4492 0.3038 0.1649  0.0317  -0.0169 139 SER B C   
1006 O O   . SER A 152 ? 0.3712 0.5450 0.3693 0.1785  0.0309  -0.0164 139 SER B O   
1007 C CB  . SER A 152 ? 0.3557 0.4661 0.3387 0.1699  0.0379  -0.0283 139 SER B CB  
1008 O OG  . SER A 152 ? 0.3413 0.4991 0.3338 0.1747  0.0375  -0.0306 139 SER B OG  
1009 N N   . GLY A 153 ? 0.2798 0.4172 0.2808 0.1429  0.0296  -0.0160 140 GLY B N   
1010 C CA  . GLY A 153 ? 0.2803 0.4527 0.2930 0.1313  0.0266  -0.0151 140 GLY B CA  
1011 C C   . GLY A 153 ? 0.2307 0.3858 0.2460 0.1109  0.0248  -0.0130 140 GLY B C   
1012 O O   . GLY A 153 ? 0.2419 0.3621 0.2504 0.1087  0.0254  -0.0111 140 GLY B O   
1013 N N   . ALA A 154 ? 0.2234 0.4036 0.2478 0.0966  0.0229  -0.0135 141 ALA B N   
1014 C CA  . ALA A 154 ? 0.2251 0.3890 0.2511 0.0789  0.0214  -0.0118 141 ALA B CA  
1015 C C   . ALA A 154 ? 0.2077 0.3950 0.2402 0.0709  0.0187  -0.0112 141 ALA B C   
1016 O O   . ALA A 154 ? 0.2044 0.4267 0.2432 0.0700  0.0186  -0.0139 141 ALA B O   
1017 C CB  . ALA A 154 ? 0.2137 0.3763 0.2419 0.0652  0.0230  -0.0147 141 ALA B CB  
1018 N N   . ILE A 155 ? 0.1829 0.3521 0.2139 0.0636  0.0169  -0.0084 142 ILE B N   
1019 C CA  . ILE A 155 ? 0.2148 0.4021 0.2502 0.0554  0.0144  -0.0088 142 ILE B CA  
1020 C C   . ILE A 155 ? 0.1898 0.3581 0.2254 0.0380  0.0143  -0.0092 142 ILE B C   
1021 O O   . ILE A 155 ? 0.2133 0.3521 0.2442 0.0378  0.0149  -0.0068 142 ILE B O   
1022 C CB  . ILE A 155 ? 0.2261 0.4125 0.2578 0.0674  0.0123  -0.0049 142 ILE B CB  
1023 C CG1 . ILE A 155 ? 0.2218 0.4312 0.2527 0.0864  0.0123  -0.0042 142 ILE B CG1 
1024 C CG2 . ILE A 155 ? 0.2419 0.4438 0.2772 0.0570  0.0096  -0.0063 142 ILE B CG2 
1025 C CD1 . ILE A 155 ? 0.2273 0.4292 0.2511 0.1019  0.0110  0.0017  142 ILE B CD1 
1026 N N   . ILE A 156 ? 0.2023 0.3875 0.2426 0.0239  0.0139  -0.0124 143 ILE B N   
1027 C CA  . ILE A 156 ? 0.1763 0.3420 0.2150 0.0091  0.0141  -0.0126 143 ILE B CA  
1028 C C   . ILE A 156 ? 0.1704 0.3469 0.2104 0.0033  0.0119  -0.0148 143 ILE B C   
1029 O O   . ILE A 156 ? 0.1544 0.3597 0.1989 -0.0016 0.0115  -0.0186 143 ILE B O   
1030 C CB  . ILE A 156 ? 0.1922 0.3618 0.2323 -0.0039 0.0166  -0.0145 143 ILE B CB  
1031 C CG1 . ILE A 156 ? 0.1939 0.3564 0.2323 0.0032  0.0187  -0.0130 143 ILE B CG1 
1032 C CG2 . ILE A 156 ? 0.1779 0.3241 0.2143 -0.0173 0.0171  -0.0140 143 ILE B CG2 
1033 C CD1 . ILE A 156 ? 0.1948 0.3696 0.2344 -0.0066 0.0217  -0.0144 143 ILE B CD1 
1034 N N   . ASN A 157 ? 0.1636 0.3197 0.1997 0.0034  0.0105  -0.0131 144 ASN B N   
1035 C CA  . ASN A 157 ? 0.1769 0.3424 0.2132 -0.0031 0.0086  -0.0163 144 ASN B CA  
1036 C C   . ASN A 157 ? 0.2017 0.3499 0.2358 -0.0189 0.0100  -0.0191 144 ASN B C   
1037 O O   . ASN A 157 ? 0.2257 0.3464 0.2559 -0.0186 0.0110  -0.0161 144 ASN B O   
1038 C CB  . ASN A 157 ? 0.2306 0.3833 0.2628 0.0065  0.0070  -0.0128 144 ASN B CB  
1039 C CG  . ASN A 157 ? 0.2494 0.4165 0.2812 0.0227  0.0059  -0.0092 144 ASN B CG  
1040 O OD1 . ASN A 157 ? 0.2465 0.4430 0.2821 0.0255  0.0049  -0.0115 144 ASN B OD1 
1041 N ND2 . ASN A 157 ? 0.2048 0.3540 0.2315 0.0336  0.0061  -0.0035 144 ASN B ND2 
1042 N N   . MET A 158 ? 0.1920 0.3543 0.2275 -0.0325 0.0105  -0.0247 145 MET B N   
1043 C CA  . MET A 158 ? 0.1915 0.3323 0.2223 -0.0464 0.0123  -0.0271 145 MET B CA  
1044 C C   . MET A 158 ? 0.2486 0.3740 0.2749 -0.0448 0.0106  -0.0284 145 MET B C   
1045 O O   . MET A 158 ? 0.2331 0.3748 0.2601 -0.0440 0.0084  -0.0323 145 MET B O   
1046 C CB  . MET A 158 ? 0.2025 0.3612 0.2348 -0.0632 0.0139  -0.0332 145 MET B CB  
1047 C CG  . MET A 158 ? 0.2200 0.3972 0.2569 -0.0655 0.0162  -0.0319 145 MET B CG  
1048 S SD  . MET A 158 ? 0.2570 0.3992 0.2876 -0.0679 0.0196  -0.0258 145 MET B SD  
1049 C CE  . MET A 158 ? 0.2767 0.3950 0.2987 -0.0870 0.0222  -0.0295 145 MET B CE  
1050 N N   . GLY A 159 ? 0.2872 0.3820 0.3084 -0.0434 0.0118  -0.0251 146 GLY B N   
1051 C CA  . GLY A 159 ? 0.2595 0.3385 0.2762 -0.0402 0.0108  -0.0258 146 GLY B CA  
1052 C C   . GLY A 159 ? 0.2771 0.3361 0.2872 -0.0520 0.0130  -0.0300 146 GLY B C   
1053 O O   . GLY A 159 ? 0.2700 0.3326 0.2792 -0.0646 0.0149  -0.0335 146 GLY B O   
1054 N N   . SER A 160 ? 0.2507 0.2898 0.2556 -0.0481 0.0129  -0.0301 147 SER B N   
1055 C CA  . SER A 160 ? 0.3116 0.3284 0.3081 -0.0572 0.0152  -0.0345 147 SER B CA  
1056 C C   . SER A 160 ? 0.2925 0.2868 0.2840 -0.0475 0.0154  -0.0318 147 SER B C   
1057 O O   . SER A 160 ? 0.2723 0.2743 0.2670 -0.0374 0.0134  -0.0299 147 SER B O   
1058 C CB  . SER A 160 ? 0.3133 0.3392 0.3072 -0.0674 0.0149  -0.0440 147 SER B CB  
1059 O OG  . SER A 160 ? 0.3178 0.3150 0.3013 -0.0741 0.0176  -0.0483 147 SER B OG  
1060 N N   . ILE A 161 ? 0.2936 0.2617 0.2774 -0.0499 0.0180  -0.0306 148 ILE B N   
1061 C CA  . ILE A 161 ? 0.3100 0.2596 0.2888 -0.0398 0.0182  -0.0287 148 ILE B CA  
1062 C C   . ILE A 161 ? 0.3176 0.2605 0.2904 -0.0405 0.0185  -0.0366 148 ILE B C   
1063 O O   . ILE A 161 ? 0.2805 0.2139 0.2501 -0.0307 0.0184  -0.0359 148 ILE B O   
1064 C CB  . ILE A 161 ? 0.3123 0.2368 0.2837 -0.0377 0.0207  -0.0238 148 ILE B CB  
1065 C CG1 . ILE A 161 ? 0.3198 0.2220 0.2801 -0.0494 0.0242  -0.0280 148 ILE B CG1 
1066 C CG2 . ILE A 161 ? 0.3117 0.2436 0.2885 -0.0349 0.0202  -0.0161 148 ILE B CG2 
1067 C CD1 . ILE A 161 ? 0.3394 0.2119 0.2888 -0.0448 0.0270  -0.0226 148 ILE B CD1 
1068 N N   . SER A 162 ? 0.3054 0.2557 0.2766 -0.0519 0.0187  -0.0443 149 SER B N   
1069 C CA  . SER A 162 ? 0.2965 0.2397 0.2604 -0.0547 0.0191  -0.0536 149 SER B CA  
1070 C C   . SER A 162 ? 0.2927 0.2502 0.2602 -0.0427 0.0166  -0.0536 149 SER B C   
1071 O O   . SER A 162 ? 0.2822 0.2258 0.2427 -0.0372 0.0177  -0.0574 149 SER B O   
1072 C CB  . SER A 162 ? 0.3448 0.2994 0.3077 -0.0706 0.0194  -0.0626 149 SER B CB  
1073 O OG  . SER A 162 ? 0.3612 0.3510 0.3351 -0.0696 0.0160  -0.0611 149 SER B OG  
1074 N N   . TRP A 163 ? 0.2397 0.2230 0.2168 -0.0374 0.0139  -0.0486 150 TRP B N   
1075 C CA  . TRP A 163 ? 0.2492 0.2436 0.2275 -0.0276 0.0124  -0.0483 150 TRP B CA  
1076 C C   . TRP A 163 ? 0.2564 0.2397 0.2352 -0.0167 0.0133  -0.0416 150 TRP B C   
1077 O O   . TRP A 163 ? 0.2855 0.2683 0.2613 -0.0096 0.0136  -0.0434 150 TRP B O   
1078 C CB  . TRP A 163 ? 0.2772 0.3007 0.2628 -0.0252 0.0097  -0.0454 150 TRP B CB  
1079 C CG  . TRP A 163 ? 0.2421 0.2694 0.2347 -0.0206 0.0094  -0.0359 150 TRP B CG  
1080 C CD1 . TRP A 163 ? 0.2761 0.3107 0.2731 -0.0253 0.0090  -0.0340 150 TRP B CD1 
1081 C CD2 . TRP A 163 ? 0.2440 0.2688 0.2395 -0.0111 0.0096  -0.0281 150 TRP B CD2 
1082 N NE1 . TRP A 163 ? 0.2318 0.2660 0.2335 -0.0187 0.0091  -0.0260 150 TRP B NE1 
1083 C CE2 . TRP A 163 ? 0.2572 0.2850 0.2579 -0.0107 0.0093  -0.0224 150 TRP B CE2 
1084 C CE3 . TRP A 163 ? 0.2569 0.2781 0.2509 -0.0038 0.0102  -0.0258 150 TRP B CE3 
1085 C CZ2 . TRP A 163 ? 0.2594 0.2846 0.2631 -0.0042 0.0097  -0.0155 150 TRP B CZ2 
1086 C CZ3 . TRP A 163 ? 0.3153 0.3353 0.3131 0.0017  0.0107  -0.0184 150 TRP B CZ3 
1087 C CH2 . TRP A 163 ? 0.2451 0.2665 0.2473 0.0012  0.0104  -0.0136 150 TRP B CH2 
1088 N N   . MET A 164 ? 0.2388 0.2139 0.2205 -0.0157 0.0139  -0.0350 151 MET B N   
1089 C CA  . MET A 164 ? 0.2525 0.2193 0.2346 -0.0064 0.0145  -0.0295 151 MET B CA  
1090 C C   . MET A 164 ? 0.2964 0.2433 0.2693 -0.0025 0.0164  -0.0337 151 MET B C   
1091 O O   . MET A 164 ? 0.2961 0.2442 0.2690 0.0067  0.0167  -0.0323 151 MET B O   
1092 C CB  . MET A 164 ? 0.2505 0.2115 0.2354 -0.0073 0.0148  -0.0231 151 MET B CB  
1093 C CG  . MET A 164 ? 0.3216 0.3007 0.3148 -0.0088 0.0132  -0.0191 151 MET B CG  
1094 S SD  . MET A 164 ? 0.3223 0.2954 0.3173 -0.0114 0.0138  -0.0139 151 MET B SD  
1095 C CE  . MET A 164 ? 0.3101 0.3039 0.3132 -0.0107 0.0123  -0.0112 151 MET B CE  
1096 N N   . ARG A 165 ? 0.2925 0.2206 0.2572 -0.0098 0.0182  -0.0388 152 ARG B N   
1097 C CA  . ARG A 165 ? 0.2909 0.1942 0.2444 -0.0054 0.0207  -0.0427 152 ARG B CA  
1098 C C   . ARG A 165 ? 0.2944 0.1996 0.2427 -0.0059 0.0210  -0.0526 152 ARG B C   
1099 O O   . ARG A 165 ? 0.3194 0.2025 0.2567 -0.0018 0.0234  -0.0579 152 ARG B O   
1100 C CB  . ARG A 165 ? 0.3087 0.1869 0.2529 -0.0152 0.0233  -0.0444 152 ARG B CB  
1101 C CG  . ARG A 165 ? 0.2768 0.1478 0.2224 -0.0138 0.0238  -0.0350 152 ARG B CG  
1102 C CD  . ARG A 165 ? 0.3136 0.1555 0.2470 -0.0240 0.0275  -0.0360 152 ARG B CD  
1103 N NE  . ARG A 165 ? 0.3653 0.1773 0.2843 -0.0182 0.0304  -0.0404 152 ARG B NE  
1104 C CZ  . ARG A 165 ? 0.4021 0.1829 0.3069 -0.0268 0.0345  -0.0445 152 ARG B CZ  
1105 N NH1 . ARG A 165 ? 0.3835 0.1628 0.2879 -0.0439 0.0360  -0.0449 152 ARG B NH1 
1106 N NH2 . ARG A 165 ? 0.4639 0.2156 0.3545 -0.0183 0.0372  -0.0484 152 ARG B NH2 
1107 N N   . GLY A 166 ? 0.2794 0.2107 0.2345 -0.0087 0.0187  -0.0547 153 GLY B N   
1108 C CA  . GLY A 166 ? 0.2848 0.2231 0.2353 -0.0085 0.0186  -0.0639 153 GLY B CA  
1109 C C   . GLY A 166 ? 0.3119 0.2310 0.2515 -0.0194 0.0204  -0.0748 153 GLY B C   
1110 O O   . GLY A 166 ? 0.3299 0.2359 0.2596 -0.0169 0.0222  -0.0835 153 GLY B O   
1111 N N   . ARG A 167 ? 0.3321 0.2473 0.2725 -0.0321 0.0207  -0.0747 154 ARG B N   
1112 C CA  . ARG A 167 ? 0.3703 0.2635 0.2992 -0.0451 0.0234  -0.0849 154 ARG B CA  
1113 C C   . ARG A 167 ? 0.3531 0.2646 0.2805 -0.0530 0.0219  -0.0969 154 ARG B C   
1114 O O   . ARG A 167 ? 0.3130 0.2577 0.2502 -0.0556 0.0185  -0.0956 154 ARG B O   
1115 C CB  . ARG A 167 ? 0.3950 0.2855 0.3258 -0.0598 0.0243  -0.0827 154 ARG B CB  
1116 C CG  . ARG A 167 ? 0.5051 0.3732 0.4340 -0.0537 0.0264  -0.0720 154 ARG B CG  
1117 C CD  . ARG A 167 ? 0.6360 0.4669 0.5509 -0.0448 0.0299  -0.0727 154 ARG B CD  
1118 N NE  . ARG A 167 ? 0.6992 0.4978 0.6001 -0.0583 0.0343  -0.0782 154 ARG B NE  
1119 C CZ  . ARG A 167 ? 0.8769 0.6380 0.7609 -0.0550 0.0382  -0.0837 154 ARG B CZ  
1120 N NH1 . ARG A 167 ? 0.7333 0.4600 0.6032 -0.0679 0.0431  -0.0864 154 ARG B NH1 
1121 N NH2 . ARG A 167 ? 0.6938 0.4517 0.5744 -0.0386 0.0378  -0.0864 154 ARG B NH2 
1122 N N   . PRO A 168 ? 0.3748 0.2656 0.2889 -0.0557 0.0244  -0.1088 155 PRO B N   
1123 C CA  . PRO A 168 ? 0.3822 0.2914 0.2937 -0.0628 0.0229  -0.1214 155 PRO B CA  
1124 C C   . PRO A 168 ? 0.4037 0.3156 0.3130 -0.0846 0.0233  -0.1305 155 PRO B C   
1125 O O   . PRO A 168 ? 0.4142 0.3066 0.3215 -0.0942 0.0259  -0.1272 155 PRO B O   
1126 C CB  . PRO A 168 ? 0.4026 0.2855 0.2997 -0.0550 0.0259  -0.1308 155 PRO B CB  
1127 C CG  . PRO A 168 ? 0.4291 0.2691 0.3168 -0.0544 0.0303  -0.1270 155 PRO B CG  
1128 C CD  . PRO A 168 ? 0.4034 0.2513 0.3030 -0.0512 0.0289  -0.1111 155 PRO B CD  
1129 N N   . GLY A 169 ? 0.4231 0.3613 0.3326 -0.0921 0.0209  -0.1414 156 GLY B N   
1130 C CA  . GLY A 169 ? 0.4486 0.3902 0.3533 -0.1141 0.0217  -0.1546 156 GLY B CA  
1131 C C   . GLY A 169 ? 0.4363 0.4137 0.3546 -0.1244 0.0187  -0.1499 156 GLY B C   
1132 O O   . GLY A 169 ? 0.4772 0.4590 0.3932 -0.1442 0.0197  -0.1591 156 GLY B O   
1133 N N   . MET A 170 ? 0.3656 0.3689 0.2973 -0.1115 0.0153  -0.1363 157 MET B N   
1134 C CA  . MET A 170 ? 0.3585 0.3980 0.3023 -0.1185 0.0124  -0.1327 157 MET B CA  
1135 C C   . MET A 170 ? 0.3158 0.3865 0.2703 -0.1009 0.0081  -0.1219 157 MET B C   
1136 O O   . MET A 170 ? 0.2906 0.3737 0.2547 -0.0962 0.0070  -0.1112 157 MET B O   
1137 C CB  . MET A 170 ? 0.3713 0.3954 0.3179 -0.1272 0.0153  -0.1259 157 MET B CB  
1138 C CG  . MET A 170 ? 0.4210 0.4139 0.3665 -0.1140 0.0176  -0.1134 157 MET B CG  
1139 S SD  . MET A 170 ? 0.6224 0.5916 0.5656 -0.1279 0.0222  -0.1087 157 MET B SD  
1140 C CE  . MET A 170 ? 0.5999 0.5262 0.5247 -0.1471 0.0282  -0.1208 157 MET B CE  
1141 N N   . VAL A 171 ? 0.3132 0.3959 0.2645 -0.0918 0.0061  -0.1255 158 VAL B N   
1142 C CA  . VAL A 171 ? 0.2761 0.3795 0.2338 -0.0739 0.0032  -0.1144 158 VAL B CA  
1143 C C   . VAL A 171 ? 0.2598 0.3980 0.2286 -0.0723 -0.0001 -0.1069 158 VAL B C   
1144 O O   . VAL A 171 ? 0.2679 0.4092 0.2427 -0.0595 -0.0008 -0.0942 158 VAL B O   
1145 C CB  . VAL A 171 ? 0.2763 0.3932 0.2276 -0.0679 0.0017  -0.1212 158 VAL B CB  
1146 C CG1 . VAL A 171 ? 0.2827 0.4325 0.2324 -0.0786 -0.0013 -0.1335 158 VAL B CG1 
1147 C CG2 . VAL A 171 ? 0.2698 0.4022 0.2259 -0.0499 0.0000  -0.1079 158 VAL B CG2 
1148 N N   . CYS A 172 ? 0.2757 0.4423 0.2474 -0.0849 -0.0022 -0.1150 159 CYS B N   
1149 C CA  . CYS A 172 ? 0.2577 0.4598 0.2395 -0.0787 -0.0054 -0.1069 159 CYS B CA  
1150 C C   . CYS A 172 ? 0.2882 0.4775 0.2771 -0.0770 -0.0036 -0.0965 159 CYS B C   
1151 O O   . CYS A 172 ? 0.3016 0.5022 0.2967 -0.0633 -0.0050 -0.0850 159 CYS B O   
1152 C CB  . CYS A 172 ? 0.2810 0.5223 0.2650 -0.0913 -0.0084 -0.1180 159 CYS B CB  
1153 S SG  . CYS A 172 ? 0.3547 0.6189 0.3303 -0.0930 -0.0114 -0.1310 159 CYS B SG  
1154 N N   . TYR A 173 ? 0.2916 0.4563 0.2782 -0.0911 0.0000  -0.1008 160 TYR B N   
1155 C CA  . TYR A 173 ? 0.2842 0.4335 0.2755 -0.0912 0.0024  -0.0921 160 TYR B CA  
1156 C C   . TYR A 173 ? 0.2702 0.3951 0.2614 -0.0751 0.0033  -0.0803 160 TYR B C   
1157 O O   . TYR A 173 ? 0.2517 0.3847 0.2497 -0.0657 0.0026  -0.0705 160 TYR B O   
1158 C CB  . TYR A 173 ? 0.3333 0.4565 0.3183 -0.1101 0.0066  -0.0996 160 TYR B CB  
1159 C CG  . TYR A 173 ? 0.3216 0.4289 0.3099 -0.1109 0.0094  -0.0905 160 TYR B CG  
1160 C CD1 . TYR A 173 ? 0.3530 0.4869 0.3495 -0.1174 0.0092  -0.0891 160 TYR B CD1 
1161 C CD2 . TYR A 173 ? 0.3193 0.3882 0.3022 -0.1044 0.0123  -0.0838 160 TYR B CD2 
1162 C CE1 . TYR A 173 ? 0.3556 0.4775 0.3549 -0.1173 0.0118  -0.0807 160 TYR B CE1 
1163 C CE2 . TYR A 173 ? 0.3870 0.4438 0.3724 -0.1042 0.0145  -0.0752 160 TYR B CE2 
1164 C CZ  . TYR A 173 ? 0.3967 0.4796 0.3900 -0.1112 0.0144  -0.0740 160 TYR B CZ  
1165 O OH  . TYR A 173 ? 0.4360 0.5100 0.4315 -0.1106 0.0167  -0.0659 160 TYR B OH  
1166 N N   . THR A 174 ? 0.2876 0.3869 0.2712 -0.0711 0.0048  -0.0819 161 THR B N   
1167 C CA  . THR A 174 ? 0.2861 0.3623 0.2698 -0.0583 0.0061  -0.0717 161 THR B CA  
1168 C C   . THR A 174 ? 0.2587 0.3548 0.2474 -0.0435 0.0036  -0.0634 161 THR B C   
1169 O O   . THR A 174 ? 0.2378 0.3267 0.2303 -0.0350 0.0041  -0.0538 161 THR B O   
1170 C CB  . THR A 174 ? 0.3218 0.3679 0.2959 -0.0569 0.0086  -0.0760 161 THR B CB  
1171 O OG1 . THR A 174 ? 0.2906 0.3468 0.2592 -0.0572 0.0074  -0.0851 161 THR B OG1 
1172 C CG2 . THR A 174 ? 0.3094 0.3261 0.2764 -0.0688 0.0122  -0.0809 161 THR B CG2 
1173 N N   . THR A 175 ? 0.2259 0.3471 0.2136 -0.0414 0.0010  -0.0674 162 THR B N   
1174 C CA  . THR A 175 ? 0.2217 0.3600 0.2115 -0.0276 -0.0009 -0.0589 162 THR B CA  
1175 C C   . THR A 175 ? 0.2422 0.3983 0.2391 -0.0231 -0.0024 -0.0515 162 THR B C   
1176 O O   . THR A 175 ? 0.2101 0.3625 0.2089 -0.0119 -0.0020 -0.0413 162 THR B O   
1177 C CB  . THR A 175 ? 0.2069 0.3667 0.1917 -0.0259 -0.0031 -0.0648 162 THR B CB  
1178 O OG1 . THR A 175 ? 0.2288 0.3711 0.2063 -0.0286 -0.0014 -0.0720 162 THR B OG1 
1179 C CG2 . THR A 175 ? 0.2154 0.3889 0.2005 -0.0111 -0.0043 -0.0539 162 THR B CG2 
1180 N N   . ALA A 176 ? 0.2421 0.4172 0.2427 -0.0326 -0.0036 -0.0575 163 ALA B N   
1181 C CA  . ALA A 176 ? 0.2194 0.4124 0.2271 -0.0281 -0.0045 -0.0516 163 ALA B CA  
1182 C C   . ALA A 176 ? 0.2229 0.3895 0.2330 -0.0260 -0.0017 -0.0443 163 ALA B C   
1183 O O   . ALA A 176 ? 0.1987 0.3665 0.2117 -0.0150 -0.0017 -0.0356 163 ALA B O   
1184 C CB  . ALA A 176 ? 0.2013 0.4194 0.2130 -0.0415 -0.0055 -0.0605 163 ALA B CB  
1185 N N   . LYS A 177 ? 0.1823 0.3237 0.1901 -0.0362 0.0009  -0.0480 164 LYS B N   
1186 C CA  . LYS A 177 ? 0.1838 0.3031 0.1934 -0.0338 0.0032  -0.0411 164 LYS B CA  
1187 C C   . LYS A 177 ? 0.2030 0.3087 0.2115 -0.0204 0.0034  -0.0326 164 LYS B C   
1188 O O   . LYS A 177 ? 0.2060 0.3077 0.2176 -0.0144 0.0040  -0.0259 164 LYS B O   
1189 C CB  . LYS A 177 ? 0.2361 0.3317 0.2419 -0.0462 0.0060  -0.0456 164 LYS B CB  
1190 C CG  . LYS A 177 ? 0.2622 0.3729 0.2699 -0.0611 0.0066  -0.0524 164 LYS B CG  
1191 C CD  . LYS A 177 ? 0.3337 0.4642 0.3491 -0.0590 0.0064  -0.0477 164 LYS B CD  
1192 C CE  . LYS A 177 ? 0.3202 0.4605 0.3370 -0.0758 0.0085  -0.0532 164 LYS B CE  
1193 N NZ  . LYS A 177 ? 0.2803 0.4474 0.3053 -0.0695 0.0077  -0.0489 164 LYS B NZ  
1194 N N   . ALA A 178 ? 0.2020 0.2999 0.2058 -0.0171 0.0034  -0.0336 165 ALA B N   
1195 C CA  . ALA A 178 ? 0.2333 0.3216 0.2363 -0.0067 0.0041  -0.0258 165 ALA B CA  
1196 C C   . ALA A 178 ? 0.2173 0.3213 0.2220 0.0032  0.0030  -0.0186 165 ALA B C   
1197 O O   . ALA A 178 ? 0.2271 0.3203 0.2320 0.0099  0.0043  -0.0111 165 ALA B O   
1198 C CB  . ALA A 178 ? 0.2108 0.2948 0.2084 -0.0053 0.0045  -0.0289 165 ALA B CB  
1199 N N   . ALA A 179 ? 0.2212 0.3505 0.2258 0.0043  0.0006  -0.0213 166 ALA B N   
1200 C CA  . ALA A 179 ? 0.1977 0.3424 0.2025 0.0154  -0.0005 -0.0142 166 ALA B CA  
1201 C C   . ALA A 179 ? 0.2386 0.3770 0.2477 0.0186  0.0006  -0.0096 166 ALA B C   
1202 O O   . ALA A 179 ? 0.2129 0.3440 0.2201 0.0286  0.0017  -0.0017 166 ALA B O   
1203 C CB  . ALA A 179 ? 0.2088 0.3867 0.2134 0.0156  -0.0037 -0.0192 166 ALA B CB  
1204 N N   . LEU A 180 ? 0.2190 0.3610 0.2327 0.0096  0.0007  -0.0151 167 LEU B N   
1205 C CA  . LEU A 180 ? 0.2436 0.3840 0.2612 0.0124  0.0017  -0.0119 167 LEU B CA  
1206 C C   . LEU A 180 ? 0.2578 0.3693 0.2741 0.0143  0.0042  -0.0069 167 LEU B C   
1207 O O   . LEU A 180 ? 0.2407 0.3475 0.2574 0.0219  0.0052  -0.0020 167 LEU B O   
1208 C CB  . LEU A 180 ? 0.2952 0.4458 0.3173 0.0001  0.0019  -0.0188 167 LEU B CB  
1209 C CG  . LEU A 180 ? 0.2895 0.4754 0.3157 -0.0003 -0.0001 -0.0227 167 LEU B CG  
1210 C CD1 . LEU A 180 ? 0.2530 0.4422 0.2833 -0.0147 0.0016  -0.0282 167 LEU B CD1 
1211 C CD2 . LEU A 180 ? 0.2968 0.4961 0.3241 0.0158  -0.0007 -0.0163 167 LEU B CD2 
1212 N N   . ASN A 181 ? 0.1625 0.2557 0.1765 0.0091  0.0052  -0.0080 168 ASN B N   
1213 C CA  . ASN A 181 ? 0.2126 0.2835 0.2258 0.0107  0.0071  -0.0038 168 ASN B CA  
1214 C C   . ASN A 181 ? 0.2344 0.3014 0.2447 0.0206  0.0079  0.0032  168 ASN B C   
1215 O O   . ASN A 181 ? 0.2474 0.3026 0.2578 0.0235  0.0094  0.0067  168 ASN B O   
1216 C CB  . ASN A 181 ? 0.2600 0.3186 0.2707 0.0061  0.0076  -0.0063 168 ASN B CB  
1217 C CG  . ASN A 181 ? 0.3213 0.3624 0.3316 0.0079  0.0093  -0.0023 168 ASN B CG  
1218 O OD1 . ASN A 181 ? 0.2991 0.3328 0.3114 0.0059  0.0100  -0.0017 168 ASN B OD1 
1219 N ND2 . ASN A 181 ? 0.2968 0.3336 0.3048 0.0105  0.0101  -0.0002 168 ASN B ND2 
1220 N N   . GLY A 182 ? 0.1870 0.2635 0.1938 0.0255  0.0071  0.0051  169 GLY B N   
1221 C CA  . GLY A 182 ? 0.2343 0.3045 0.2362 0.0345  0.0086  0.0128  169 GLY B CA  
1222 C C   . GLY A 182 ? 0.2188 0.2955 0.2199 0.0436  0.0084  0.0162  169 GLY B C   
1223 O O   . GLY A 182 ? 0.2727 0.3338 0.2700 0.0497  0.0107  0.0217  169 GLY B O   
1224 N N   . MET A 183 ? 0.1813 0.2821 0.1852 0.0450  0.0059  0.0124  170 MET B N   
1225 C CA  . MET A 183 ? 0.1972 0.3086 0.2007 0.0557  0.0056  0.0152  170 MET B CA  
1226 C C   . MET A 183 ? 0.2183 0.3152 0.2239 0.0557  0.0076  0.0150  170 MET B C   
1227 O O   . MET A 183 ? 0.2490 0.3393 0.2504 0.0669  0.0091  0.0196  170 MET B O   
1228 C CB  . MET A 183 ? 0.2021 0.3472 0.2101 0.0550  0.0024  0.0098  170 MET B CB  
1229 C CG  . MET A 183 ? 0.2609 0.4231 0.2675 0.0697  0.0018  0.0135  170 MET B CG  
1230 S SD  . MET A 183 ? 0.3206 0.5281 0.3354 0.0664  -0.0017 0.0054  170 MET B SD  
1231 C CE  . MET A 183 ? 0.3233 0.5462 0.3383 0.0544  -0.0044 -0.0009 170 MET B CE  
1232 N N   . THR A 184 ? 0.1754 0.2647 0.1860 0.0440  0.0081  0.0101  171 THR B N   
1233 C CA  . THR A 184 ? 0.2175 0.2933 0.2292 0.0437  0.0100  0.0099  171 THR B CA  
1234 C C   . THR A 184 ? 0.2400 0.2910 0.2452 0.0496  0.0126  0.0153  171 THR B C   
1235 O O   . THR A 184 ? 0.2408 0.2844 0.2434 0.0565  0.0142  0.0165  171 THR B O   
1236 C CB  . THR A 184 ? 0.2078 0.2764 0.2234 0.0311  0.0102  0.0056  171 THR B CB  
1237 O OG1 . THR A 184 ? 0.2289 0.3183 0.2490 0.0251  0.0088  0.0007  171 THR B OG1 
1238 C CG2 . THR A 184 ? 0.2231 0.2794 0.2392 0.0301  0.0120  0.0052  171 THR B CG2 
1239 N N   . ARG A 185 ? 0.2133 0.2511 0.2159 0.0452  0.0134  0.0177  172 ARG B N   
1240 C CA  . ARG A 185 ? 0.2269 0.2413 0.2239 0.0463  0.0163  0.0219  172 ARG B CA  
1241 C C   . ARG A 185 ? 0.2156 0.2243 0.2042 0.0588  0.0180  0.0281  172 ARG B C   
1242 O O   . ARG A 185 ? 0.2582 0.2472 0.2414 0.0625  0.0208  0.0299  172 ARG B O   
1243 C CB  . ARG A 185 ? 0.2136 0.2199 0.2097 0.0391  0.0172  0.0233  172 ARG B CB  
1244 C CG  . ARG A 185 ? 0.2235 0.2351 0.2266 0.0297  0.0155  0.0173  172 ARG B CG  
1245 C CD  . ARG A 185 ? 0.2797 0.2901 0.2832 0.0243  0.0156  0.0172  172 ARG B CD  
1246 N NE  . ARG A 185 ? 0.3008 0.2977 0.3022 0.0213  0.0182  0.0198  172 ARG B NE  
1247 C CZ  . ARG A 185 ? 0.2903 0.2825 0.2950 0.0154  0.0184  0.0171  172 ARG B CZ  
1248 N NH1 . ARG A 185 ? 0.3162 0.3125 0.3251 0.0128  0.0165  0.0128  172 ARG B NH1 
1249 N NH2 . ARG A 185 ? 0.2839 0.2672 0.2869 0.0116  0.0208  0.0189  172 ARG B NH2 
1250 N N   . THR A 186 ? 0.2114 0.2351 0.1974 0.0658  0.0165  0.0316  173 THR B N   
1251 C CA  . THR A 186 ? 0.2622 0.2766 0.2376 0.0793  0.0185  0.0394  173 THR B CA  
1252 C C   . THR A 186 ? 0.2660 0.2869 0.2406 0.0916  0.0183  0.0387  173 THR B C   
1253 O O   . THR A 186 ? 0.2932 0.2937 0.2586 0.1013  0.0214  0.0433  173 THR B O   
1254 C CB  . THR A 186 ? 0.2805 0.3071 0.2504 0.0859  0.0176  0.0454  173 THR B CB  
1255 O OG1 . THR A 186 ? 0.2861 0.3451 0.2634 0.0868  0.0132  0.0400  173 THR B OG1 
1256 C CG2 . THR A 186 ? 0.2448 0.2682 0.2155 0.0747  0.0180  0.0453  173 THR B CG2 
1257 N N   . LEU A 187 ? 0.2332 0.2809 0.2170 0.0901  0.0151  0.0323  174 LEU B N   
1258 C CA  . LEU A 187 ? 0.3298 0.3870 0.3132 0.1023  0.0153  0.0315  174 LEU B CA  
1259 C C   . LEU A 187 ? 0.2850 0.3183 0.2672 0.0997  0.0183  0.0287  174 LEU B C   
1260 O O   . LEU A 187 ? 0.2655 0.2919 0.2418 0.1129  0.0203  0.0300  174 LEU B O   
1261 C CB  . LEU A 187 ? 0.3320 0.4256 0.3260 0.0988  0.0118  0.0249  174 LEU B CB  
1262 C CG  . LEU A 187 ? 0.3796 0.5042 0.3731 0.1094  0.0089  0.0270  174 LEU B CG  
1263 C CD1 . LEU A 187 ? 0.4870 0.6082 0.4757 0.1075  0.0080  0.0314  174 LEU B CD1 
1264 C CD2 . LEU A 187 ? 0.3584 0.5167 0.3631 0.1000  0.0061  0.0189  174 LEU B CD2 
1265 N N   . ALA A 188 ? 0.2588 0.2805 0.2456 0.0843  0.0187  0.0248  175 ALA B N   
1266 C CA  . ALA A 188 ? 0.2562 0.2575 0.2412 0.0817  0.0213  0.0217  175 ALA B CA  
1267 C C   . ALA A 188 ? 0.3058 0.2761 0.2783 0.0895  0.0253  0.0264  175 ALA B C   
1268 O O   . ALA A 188 ? 0.3242 0.2820 0.2916 0.0969  0.0277  0.0243  175 ALA B O   
1269 C CB  . ALA A 188 ? 0.2475 0.2459 0.2392 0.0650  0.0206  0.0174  175 ALA B CB  
1270 N N   . ARG A 189 ? 0.2895 0.2466 0.2555 0.0890  0.0266  0.0330  176 ARG B N   
1271 C CA  . ARG A 189 ? 0.3281 0.2531 0.2799 0.0960  0.0313  0.0389  176 ARG B CA  
1272 C C   . ARG A 189 ? 0.3397 0.2671 0.2832 0.1166  0.0318  0.0436  176 ARG B C   
1273 O O   . ARG A 189 ? 0.3932 0.2942 0.3252 0.1261  0.0358  0.0450  176 ARG B O   
1274 C CB  . ARG A 189 ? 0.3335 0.2480 0.2817 0.0874  0.0327  0.0447  176 ARG B CB  
1275 C CG  . ARG A 189 ? 0.4363 0.3158 0.3680 0.0931  0.0382  0.0521  176 ARG B CG  
1276 C CD  . ARG A 189 ? 0.4160 0.2641 0.3420 0.0854  0.0426  0.0478  176 ARG B CD  
1277 N NE  . ARG A 189 ? 0.4263 0.2772 0.3612 0.0659  0.0420  0.0421  176 ARG B NE  
1278 C CZ  . ARG A 189 ? 0.4309 0.2632 0.3641 0.0557  0.0446  0.0362  176 ARG B CZ  
1279 N NH1 . ARG A 189 ? 0.4143 0.2195 0.3360 0.0624  0.0484  0.0347  176 ARG B NH1 
1280 N NH2 . ARG A 189 ? 0.3659 0.2053 0.3072 0.0392  0.0438  0.0321  176 ARG B NH2 
1281 N N   . GLU A 190 ? 0.3263 0.2838 0.2740 0.1240  0.0282  0.0462  177 GLU B N   
1282 C CA  . GLU A 190 ? 0.3671 0.3311 0.3062 0.1454  0.0284  0.0521  177 GLU B CA  
1283 C C   . GLU A 190 ? 0.3811 0.3493 0.3210 0.1564  0.0290  0.0467  177 GLU B C   
1284 O O   . GLU A 190 ? 0.3885 0.3421 0.3163 0.1743  0.0317  0.0514  177 GLU B O   
1285 C CB  . GLU A 190 ? 0.3968 0.4048 0.3455 0.1480  0.0231  0.0512  177 GLU B CB  
1286 C CG  . GLU A 190 ? 0.6805 0.7008 0.6203 0.1666  0.0222  0.0599  177 GLU B CG  
1287 C CD  . GLU A 190 ? 0.6103 0.6231 0.5417 0.1661  0.0227  0.0689  177 GLU B CD  
1288 O OE1 . GLU A 190 ? 0.4090 0.4387 0.3447 0.1569  0.0201  0.0692  177 GLU B OE1 
1289 O OE2 . GLU A 190 ? 0.5272 0.5108 0.4440 0.1785  0.0269  0.0764  177 GLU B OE2 
1290 N N   . LEU A 191 ? 0.3684 0.3545 0.3211 0.1456  0.0270  0.0373  178 LEU B N   
1291 C CA  . LEU A 191 ? 0.3439 0.3441 0.2987 0.1570  0.0272  0.0322  178 LEU B CA  
1292 C C   . LEU A 191 ? 0.3637 0.3395 0.3168 0.1501  0.0303  0.0256  178 LEU B C   
1293 O O   . LEU A 191 ? 0.3414 0.3245 0.2942 0.1601  0.0313  0.0210  178 LEU B O   
1294 C CB  . LEU A 191 ? 0.3194 0.3657 0.2895 0.1512  0.0226  0.0269  178 LEU B CB  
1295 C CG  . LEU A 191 ? 0.3091 0.3871 0.2817 0.1581  0.0190  0.0311  178 LEU B CG  
1296 C CD1 . LEU A 191 ? 0.3185 0.4382 0.3059 0.1478  0.0154  0.0239  178 LEU B CD1 
1297 C CD2 . LEU A 191 ? 0.3431 0.4255 0.3052 0.1829  0.0196  0.0381  178 LEU B CD2 
1298 N N   . GLY A 192 ? 0.3375 0.2903 0.2907 0.1327  0.0315  0.0243  179 GLY B N   
1299 C CA  . GLY A 192 ? 0.3522 0.2882 0.3054 0.1239  0.0336  0.0169  179 GLY B CA  
1300 C C   . GLY A 192 ? 0.3618 0.2698 0.3010 0.1383  0.0382  0.0158  179 GLY B C   
1301 O O   . GLY A 192 ? 0.3615 0.2685 0.3011 0.1387  0.0394  0.0081  179 GLY B O   
1302 N N   . GLY A 193 ? 0.3772 0.2598 0.3025 0.1497  0.0411  0.0235  180 GLY B N   
1303 C CA  . GLY A 193 ? 0.4295 0.2780 0.3389 0.1629  0.0463  0.0223  180 GLY B CA  
1304 C C   . GLY A 193 ? 0.4420 0.3125 0.3519 0.1835  0.0457  0.0194  180 GLY B C   
1305 O O   . GLY A 193 ? 0.5000 0.3485 0.3987 0.1956  0.0497  0.0156  180 GLY B O   
1306 N N   . GLN A 194 ? 0.4689 0.3838 0.3911 0.1884  0.0411  0.0210  181 GLN B N   
1307 C CA  . GLN A 194 ? 0.4715 0.4145 0.3963 0.2064  0.0405  0.0173  181 GLN B CA  
1308 C C   . GLN A 194 ? 0.4477 0.4162 0.3859 0.1944  0.0390  0.0071  181 GLN B C   
1309 O O   . GLN A 194 ? 0.4285 0.4283 0.3717 0.2061  0.0383  0.0034  181 GLN B O   
1310 C CB  . GLN A 194 ? 0.5169 0.4997 0.4476 0.2188  0.0366  0.0232  181 GLN B CB  
1311 C CG  . GLN A 194 ? 0.7322 0.6971 0.6486 0.2357  0.0378  0.0345  181 GLN B CG  
1312 C CD  . GLN A 194 ? 0.9071 0.9081 0.8319 0.2344  0.0328  0.0404  181 GLN B CD  
1313 O OE1 . GLN A 194 ? 1.0100 1.0548 0.9423 0.2454  0.0294  0.0399  181 GLN B OE1 
1314 N NE2 . GLN A 194 ? 0.9729 0.9574 0.8959 0.2206  0.0325  0.0457  181 GLN B NE2 
1315 N N   . GLY A 195 ? 0.3849 0.3423 0.3284 0.1721  0.0386  0.0030  182 GLY B N   
1316 C CA  . GLY A 195 ? 0.3870 0.3647 0.3409 0.1603  0.0376  -0.0054 182 GLY B CA  
1317 C C   . GLY A 195 ? 0.3492 0.3662 0.3191 0.1475  0.0332  -0.0051 182 GLY B C   
1318 O O   . GLY A 195 ? 0.3006 0.3374 0.2784 0.1391  0.0326  -0.0108 182 GLY B O   
1319 N N   . ILE A 196 ? 0.3157 0.3411 0.2892 0.1440  0.0304  0.0013  183 ILE B N   
1320 C CA  . ILE A 196 ? 0.2994 0.3589 0.2863 0.1317  0.0267  0.0007  183 ILE B CA  
1321 C C   . ILE A 196 ? 0.2997 0.3432 0.2894 0.1122  0.0255  0.0016  183 ILE B C   
1322 O O   . ILE A 196 ? 0.2911 0.3112 0.2747 0.1114  0.0260  0.0062  183 ILE B O   
1323 C CB  . ILE A 196 ? 0.2852 0.3706 0.2743 0.1417  0.0241  0.0057  183 ILE B CB  
1324 C CG1 . ILE A 196 ? 0.2832 0.3875 0.2691 0.1638  0.0251  0.0053  183 ILE B CG1 
1325 C CG2 . ILE A 196 ? 0.2628 0.3811 0.2646 0.1266  0.0204  0.0040  183 ILE B CG2 
1326 C CD1 . ILE A 196 ? 0.3271 0.4445 0.3093 0.1785  0.0231  0.0123  183 ILE B CD1 
1327 N N   . ARG A 197 ? 0.2527 0.3112 0.2513 0.0974  0.0241  -0.0023 184 ARG B N   
1328 C CA  . ARG A 197 ? 0.2665 0.3137 0.2680 0.0810  0.0229  -0.0016 184 ARG B CA  
1329 C C   . ARG A 197 ? 0.2744 0.3468 0.2841 0.0734  0.0199  -0.0007 184 ARG B C   
1330 O O   . ARG A 197 ? 0.2338 0.3346 0.2488 0.0755  0.0191  -0.0026 184 ARG B O   
1331 C CB  . ARG A 197 ? 0.3348 0.3736 0.3369 0.0717  0.0240  -0.0063 184 ARG B CB  
1332 C CG  . ARG A 197 ? 0.3501 0.4134 0.3589 0.0658  0.0237  -0.0099 184 ARG B CG  
1333 C CD  . ARG A 197 ? 0.3903 0.4420 0.3958 0.0620  0.0256  -0.0142 184 ARG B CD  
1334 N NE  . ARG A 197 ? 0.3929 0.4667 0.4047 0.0524  0.0251  -0.0154 184 ARG B NE  
1335 C CZ  . ARG A 197 ? 0.3461 0.4404 0.3594 0.0568  0.0267  -0.0185 184 ARG B CZ  
1336 N NH1 . ARG A 197 ? 0.3541 0.4512 0.3639 0.0718  0.0284  -0.0208 184 ARG B NH1 
1337 N NH2 . ARG A 197 ? 0.3665 0.4771 0.3835 0.0469  0.0272  -0.0192 184 ARG B NH2 
1338 N N   . ILE A 198 ? 0.2526 0.3148 0.2624 0.0656  0.0185  0.0021  185 ILE B N   
1339 C CA  . ILE A 198 ? 0.2208 0.3030 0.2366 0.0583  0.0160  0.0021  185 ILE B CA  
1340 C C   . ILE A 198 ? 0.1921 0.2602 0.2092 0.0443  0.0155  0.0016  185 ILE B C   
1341 O O   . ILE A 198 ? 0.2160 0.2620 0.2288 0.0440  0.0162  0.0040  185 ILE B O   
1342 C CB  . ILE A 198 ? 0.2398 0.3257 0.2522 0.0672  0.0147  0.0064  185 ILE B CB  
1343 C CG1 . ILE A 198 ? 0.3521 0.4510 0.3616 0.0843  0.0153  0.0077  185 ILE B CG1 
1344 C CG2 . ILE A 198 ? 0.2948 0.4025 0.3129 0.0585  0.0119  0.0046  185 ILE B CG2 
1345 C CD1 . ILE A 198 ? 0.3622 0.4330 0.3612 0.0972  0.0181  0.0116  185 ILE B CD1 
1346 N N   . ASN A 199 ? 0.1686 0.2488 0.1907 0.0332  0.0147  -0.0013 186 ASN B N   
1347 C CA  . ASN A 199 ? 0.1656 0.2315 0.1876 0.0225  0.0144  -0.0012 186 ASN B CA  
1348 C C   . ASN A 199 ? 0.1883 0.2675 0.2133 0.0137  0.0132  -0.0033 186 ASN B C   
1349 O O   . ASN A 199 ? 0.1946 0.2958 0.2227 0.0139  0.0127  -0.0054 186 ASN B O   
1350 C CB  . ASN A 199 ? 0.1948 0.2537 0.2166 0.0170  0.0158  -0.0026 186 ASN B CB  
1351 C CG  . ASN A 199 ? 0.1821 0.2264 0.2002 0.0232  0.0171  -0.0023 186 ASN B CG  
1352 O OD1 . ASN A 199 ? 0.1956 0.2231 0.2109 0.0233  0.0171  -0.0007 186 ASN B OD1 
1353 N ND2 . ASN A 199 ? 0.1783 0.2303 0.1960 0.0288  0.0185  -0.0043 186 ASN B ND2 
1354 N N   . SER A 200 ? 0.1675 0.2346 0.1913 0.0063  0.0128  -0.0034 187 SER B N   
1355 C CA  A SER A 200 ? 0.1697 0.2443 0.1944 -0.0032 0.0122  -0.0065 187 SER B CA  
1356 C CA  B SER A 200 ? 0.1726 0.2469 0.1973 -0.0032 0.0122  -0.0064 187 SER B CA  
1357 C C   . SER A 200 ? 0.1805 0.2446 0.2036 -0.0128 0.0138  -0.0070 187 SER B C   
1358 O O   . SER A 200 ? 0.1800 0.2265 0.2003 -0.0121 0.0142  -0.0046 187 SER B O   
1359 C CB  A SER A 200 ? 0.1888 0.2559 0.2113 -0.0036 0.0109  -0.0066 187 SER B CB  
1360 C CB  B SER A 200 ? 0.1915 0.2572 0.2137 -0.0034 0.0109  -0.0065 187 SER B CB  
1361 O OG  A SER A 200 ? 0.1749 0.2492 0.1973 -0.0127 0.0105  -0.0111 187 SER B OG  
1362 O OG  B SER A 200 ? 0.1901 0.2617 0.2118 0.0052  0.0097  -0.0046 187 SER B OG  
1363 N N   . LEU A 201 ? 0.1706 0.2465 0.1947 -0.0221 0.0148  -0.0099 188 LEU B N   
1364 C CA  . LEU A 201 ? 0.2077 0.2726 0.2282 -0.0324 0.0170  -0.0096 188 LEU B CA  
1365 C C   . LEU A 201 ? 0.2123 0.2659 0.2289 -0.0398 0.0169  -0.0122 188 LEU B C   
1366 O O   . LEU A 201 ? 0.2186 0.2863 0.2370 -0.0444 0.0161  -0.0167 188 LEU B O   
1367 C CB  . LEU A 201 ? 0.1783 0.2635 0.2017 -0.0391 0.0189  -0.0112 188 LEU B CB  
1368 C CG  . LEU A 201 ? 0.1923 0.2685 0.2110 -0.0499 0.0222  -0.0095 188 LEU B CG  
1369 C CD1 . LEU A 201 ? 0.1859 0.2880 0.2088 -0.0540 0.0243  -0.0106 188 LEU B CD1 
1370 C CD2 . LEU A 201 ? 0.2358 0.2957 0.2487 -0.0612 0.0233  -0.0112 188 LEU B CD2 
1371 N N   . VAL A 202 ? 0.2041 0.2335 0.2148 -0.0398 0.0175  -0.0100 189 VAL B N   
1372 C CA  . VAL A 202 ? 0.2035 0.2204 0.2097 -0.0432 0.0173  -0.0132 189 VAL B CA  
1373 C C   . VAL A 202 ? 0.2438 0.2398 0.2416 -0.0522 0.0203  -0.0126 189 VAL B C   
1374 O O   . VAL A 202 ? 0.2606 0.2386 0.2535 -0.0478 0.0211  -0.0080 189 VAL B O   
1375 C CB  . VAL A 202 ? 0.2216 0.2281 0.2272 -0.0327 0.0156  -0.0111 189 VAL B CB  
1376 C CG1 . VAL A 202 ? 0.2302 0.2256 0.2306 -0.0348 0.0156  -0.0151 189 VAL B CG1 
1377 C CG2 . VAL A 202 ? 0.1810 0.2020 0.1923 -0.0239 0.0136  -0.0099 189 VAL B CG2 
1378 N N   . PRO A 203 ? 0.2541 0.2523 0.2493 -0.0651 0.0224  -0.0167 190 PRO B N   
1379 C CA  . PRO A 203 ? 0.3021 0.2769 0.2871 -0.0750 0.0262  -0.0157 190 PRO B CA  
1380 C C   . PRO A 203 ? 0.3203 0.2679 0.2959 -0.0741 0.0269  -0.0180 190 PRO B C   
1381 O O   . PRO A 203 ? 0.3183 0.2700 0.2955 -0.0716 0.0248  -0.0236 190 PRO B O   
1382 C CB  . PRO A 203 ? 0.3011 0.2910 0.2872 -0.0914 0.0286  -0.0202 190 PRO B CB  
1383 C CG  . PRO A 203 ? 0.3042 0.3300 0.3025 -0.0868 0.0252  -0.0233 190 PRO B CG  
1384 C CD  . PRO A 203 ? 0.2512 0.2779 0.2532 -0.0712 0.0214  -0.0220 190 PRO B CD  
1385 N N   . GLY A 204 ? 0.3326 0.2525 0.2970 -0.0773 0.0304  -0.0141 191 GLY B N   
1386 C CA  . GLY A 204 ? 0.3698 0.2592 0.3222 -0.0769 0.0322  -0.0165 191 GLY B CA  
1387 C C   . GLY A 204 ? 0.3828 0.2632 0.3283 -0.0952 0.0358  -0.0232 191 GLY B C   
1388 O O   . GLY A 204 ? 0.3570 0.2627 0.3102 -0.1049 0.0348  -0.0294 191 GLY B O   
1389 N N   . ALA A 205 ? 0.3947 0.2386 0.3247 -0.0991 0.0400  -0.0224 192 ALA B N   
1390 C CA  . ALA A 205 ? 0.3941 0.2234 0.3148 -0.1186 0.0445  -0.0288 192 ALA B CA  
1391 C C   . ALA A 205 ? 0.4529 0.2834 0.3711 -0.1328 0.0487  -0.0234 192 ALA B C   
1392 O O   . ALA A 205 ? 0.4802 0.2805 0.3850 -0.1338 0.0532  -0.0155 192 ALA B O   
1393 C CB  . ALA A 205 ? 0.4472 0.2332 0.3506 -0.1150 0.0476  -0.0305 192 ALA B CB  
1394 N N   . ILE A 206 ? 0.4308 0.2971 0.3608 -0.1450 0.0478  -0.0282 193 ILE B N   
1395 C CA  . ILE A 206 ? 0.4457 0.3254 0.3772 -0.1587 0.0513  -0.0243 193 ILE B CA  
1396 C C   . ILE A 206 ? 0.4840 0.3467 0.4043 -0.1832 0.0574  -0.0301 193 ILE B C   
1397 O O   . ILE A 206 ? 0.4637 0.3391 0.3870 -0.1949 0.0567  -0.0414 193 ILE B O   
1398 C CB  . ILE A 206 ? 0.3757 0.3052 0.3259 -0.1558 0.0472  -0.0259 193 ILE B CB  
1399 C CG1 . ILE A 206 ? 0.3532 0.2946 0.3126 -0.1329 0.0416  -0.0215 193 ILE B CG1 
1400 C CG2 . ILE A 206 ? 0.3774 0.3234 0.3292 -0.1684 0.0511  -0.0216 193 ILE B CG2 
1401 C CD1 . ILE A 206 ? 0.3496 0.2695 0.3025 -0.1208 0.0425  -0.0107 193 ILE B CD1 
1402 N N   . ARG A 207 ? 0.5005 0.3346 0.4068 -0.1924 0.0637  -0.0225 194 ARG B N   
1403 C CA  . ARG A 207 ? 0.5820 0.3995 0.4768 -0.2192 0.0707  -0.0273 194 ARG B CA  
1404 C C   . ARG A 207 ? 0.5614 0.4282 0.4708 -0.2359 0.0708  -0.0320 194 ARG B C   
1405 O O   . ARG A 207 ? 0.5448 0.4412 0.4651 -0.2282 0.0691  -0.0253 194 ARG B O   
1406 C CB  . ARG A 207 ? 0.6468 0.4192 0.5211 -0.2243 0.0782  -0.0163 194 ARG B CB  
1407 C CG  . ARG A 207 ? 0.6991 0.4481 0.5586 -0.2537 0.0868  -0.0196 194 ARG B CG  
1408 C CD  . ARG A 207 ? 0.8038 0.4971 0.6385 -0.2558 0.0945  -0.0081 194 ARG B CD  
1409 N NE  . ARG A 207 ? 0.9271 0.6172 0.7585 -0.2413 0.0951  0.0080  194 ARG B NE  
1410 C CZ  . ARG A 207 ? 0.9920 0.6340 0.8008 -0.2366 0.1009  0.0206  194 ARG B CZ  
1411 N NH1 . ARG A 207 ? 1.0566 0.6434 0.8429 -0.2410 0.1064  0.0199  194 ARG B NH1 
1412 N NH2 . ARG A 207 ? 0.9371 0.5853 0.7448 -0.2251 0.1010  0.0343  194 ARG B NH2 
1413 N N   . THR A 208 ? 0.6030 0.4853 0.5153 -0.2550 0.0715  -0.0448 195 THR B N   
1414 C CA  . THR A 208 ? 0.6276 0.5596 0.5532 -0.2727 0.0720  -0.0505 195 THR B CA  
1415 C C   . THR A 208 ? 0.7151 0.6338 0.6298 -0.3047 0.0788  -0.0596 195 THR B C   
1416 O O   . THR A 208 ? 0.6963 0.5752 0.5968 -0.3099 0.0807  -0.0656 195 THR B O   
1417 C CB  . THR A 208 ? 0.6066 0.5894 0.5519 -0.2622 0.0640  -0.0586 195 THR B CB  
1418 O OG1 . THR A 208 ? 0.6641 0.6377 0.6057 -0.2672 0.0621  -0.0705 195 THR B OG1 
1419 C CG2 . THR A 208 ? 0.5252 0.5204 0.4808 -0.2328 0.0577  -0.0508 195 THR B CG2 
1420 N N   . GLU A 209 ? 0.7983 0.7521 0.7197 -0.3258 0.0824  -0.0615 196 GLU B N   
1421 C CA  . GLU A 209 ? 0.8565 0.8054 0.7694 -0.3599 0.0891  -0.0715 196 GLU B CA  
1422 C C   . GLU A 209 ? 0.8807 0.8440 0.7976 -0.3676 0.0851  -0.0886 196 GLU B C   
1423 O O   . GLU A 209 ? 0.9779 0.9140 0.8811 -0.3921 0.0906  -0.0977 196 GLU B O   
1424 C CB  . GLU A 209 ? 0.7717 0.7557 0.6901 -0.3828 0.0948  -0.0698 196 GLU B CB  
1425 N N   . ARG A 210 ? 0.7859 0.7879 0.7196 -0.3468 0.0760  -0.0926 197 ARG B N   
1426 C CA  . ARG A 210 ? 0.7769 0.7978 0.7156 -0.3486 0.0708  -0.1074 197 ARG B CA  
1427 C C   . ARG A 210 ? 0.8769 0.8430 0.7997 -0.3392 0.0705  -0.1102 197 ARG B C   
1428 O O   . ARG A 210 ? 0.9544 0.9096 0.8691 -0.3558 0.0719  -0.1239 197 ARG B O   
1429 C CB  . ARG A 210 ? 0.6917 0.7705 0.6517 -0.3275 0.0616  -0.1086 197 ARG B CB  
1430 N N   . GLN A 211 ? 0.9407 0.8755 0.8593 -0.3125 0.0686  -0.0984 198 GLN B N   
1431 C CA  . GLN A 211 ? 1.0165 0.8977 0.9190 -0.3015 0.0692  -0.0993 198 GLN B CA  
1432 C C   . GLN A 211 ? 1.1776 1.0023 1.0565 -0.3229 0.0786  -0.1010 198 GLN B C   
1433 O O   . GLN A 211 ? 1.2830 1.0699 1.1473 -0.3257 0.0804  -0.1096 198 GLN B O   
1434 C CB  . GLN A 211 ? 0.9347 0.8015 0.8391 -0.2690 0.0650  -0.0871 198 GLN B CB  
1435 N N   . ASP A 212 ? 1.2737 1.0941 1.1484 -0.3394 0.0850  -0.0934 199 ASP B N   
1436 C CA  . ASP A 212 ? 1.3786 1.1431 1.2294 -0.3600 0.0951  -0.0915 199 ASP B CA  
1437 C C   . ASP A 212 ? 1.4337 1.2057 1.2802 -0.3958 0.0997  -0.1079 199 ASP B C   
1438 O O   . ASP A 212 ? 1.4198 1.1382 1.2439 -0.4120 0.1068  -0.1133 199 ASP B O   
1439 C CB  . ASP A 212 ? 1.2558 1.0079 1.1013 -0.3603 0.1005  -0.0744 199 ASP B CB  
1440 C CG  . ASP A 212 ? 1.1704 0.8993 1.0124 -0.3292 0.0983  -0.0578 199 ASP B CG  
1441 O OD1 . ASP A 212 ? 1.0664 0.7911 0.9122 -0.3037 0.0920  -0.0579 199 ASP B OD1 
1442 O OD2 . ASP A 212 ? 1.1528 0.8713 0.9886 -0.3310 0.1030  -0.0445 199 ASP B OD2 
1443 N N   . ALA A 213 ? 1.3610 1.1992 1.2279 -0.4083 0.0959  -0.1164 200 ALA B N   
1444 C CA  . ALA A 213 ? 1.2695 1.1242 1.1348 -0.4425 0.0993  -0.1335 200 ALA B CA  
1445 C C   . ALA A 213 ? 1.3529 1.1812 1.2076 -0.4437 0.0975  -0.1491 200 ALA B C   
1446 O O   . ALA A 213 ? 1.3248 1.1387 1.1680 -0.4734 0.1028  -0.1631 200 ALA B O   
1447 C CB  . ALA A 213 ? 1.0986 1.0353 0.9893 -0.4496 0.0941  -0.1391 200 ALA B CB  
1448 N N   . MET A 214 ? 1.3810 1.2014 1.2386 -0.4118 0.0906  -0.1465 201 MET B N   
1449 C CA  . MET A 214 ? 1.3342 1.1422 1.1861 -0.4059 0.0869  -0.1606 201 MET B CA  
1450 C C   . MET A 214 ? 1.4240 1.1530 1.2469 -0.4122 0.0946  -0.1643 201 MET B C   
1451 O O   . MET A 214 ? 1.3042 1.0179 1.1194 -0.4096 0.0928  -0.1777 201 MET B O   
1452 C CB  . MET A 214 ? 1.1793 1.0097 1.0450 -0.3694 0.0775  -0.1547 201 MET B CB  
1453 N N   . TRP A 215 ? 1.4934 1.1726 1.2990 -0.4201 0.1033  -0.1529 202 TRP B N   
1454 C CA  . TRP A 215 ? 1.5491 1.1472 1.3245 -0.4224 0.1114  -0.1529 202 TRP B CA  
1455 C C   . TRP A 215 ? 1.6261 1.1883 1.3829 -0.4574 0.1230  -0.1527 202 TRP B C   
1456 O O   . TRP A 215 ? 1.6332 1.1246 1.3638 -0.4563 0.1310  -0.1456 202 TRP B O   
1457 C CB  . TRP A 215 ? 1.5830 1.1416 1.3503 -0.3883 0.1111  -0.1342 202 TRP B CB  
1458 C CG  . TRP A 215 ? 1.5448 1.1223 1.3248 -0.3516 0.1017  -0.1308 202 TRP B CG  
1459 C CD1 . TRP A 215 ? 1.4587 1.0905 1.2632 -0.3322 0.0936  -0.1220 202 TRP B CD1 
1460 C CD2 . TRP A 215 ? 1.5789 1.1170 1.3460 -0.3291 0.1005  -0.1342 202 TRP B CD2 
1461 N NE1 . TRP A 215 ? 1.3771 1.0078 1.1855 -0.3019 0.0875  -0.1202 202 TRP B NE1 
1462 C CE2 . TRP A 215 ? 1.4981 1.0743 1.2846 -0.2988 0.0914  -0.1274 202 TRP B CE2 
1463 C CE3 . TRP A 215 ? 1.5706 1.0459 1.3115 -0.3313 0.1065  -0.1430 202 TRP B CE3 
1464 C CZ2 . TRP A 215 ? 1.4353 0.9923 1.2168 -0.2722 0.0882  -0.1288 202 TRP B CZ2 
1465 C CZ3 . TRP A 215 ? 1.4879 0.9444 1.2238 -0.3029 0.1031  -0.1447 202 TRP B CZ3 
1466 C CH2 . TRP A 215 ? 1.4411 0.9398 1.1977 -0.2741 0.0940  -0.1374 202 TRP B CH2 
1467 N N   . ALA A 216 ? 1.5507 1.1606 1.3198 -0.4880 0.1244  -0.1598 203 ALA B N   
1468 C CA  . ALA A 216 ? 1.3957 0.9850 1.1522 -0.5198 0.1351  -0.1549 203 ALA B CA  
1469 C C   . ALA A 216 ? 1.4645 0.9791 1.1888 -0.5451 0.1459  -0.1644 203 ALA B C   
1470 O O   . ALA A 216 ? 1.4741 0.9641 1.1843 -0.5745 0.1561  -0.1610 203 ALA B O   
1471 C CB  . ALA A 216 ? 1.2840 0.9479 1.0627 -0.5458 0.1338  -0.1614 203 ALA B CB  
1472 N N   . ALA A 217 ? 1.4738 0.9516 1.1855 -0.5331 0.1441  -0.1760 204 ALA B N   
1473 C CA  . ALA A 217 ? 1.4936 0.8970 1.1733 -0.5534 0.1538  -0.1874 204 ALA B CA  
1474 C C   . ALA A 217 ? 1.4586 0.7918 1.1166 -0.5198 0.1547  -0.1801 204 ALA B C   
1475 O O   . ALA A 217 ? 1.4083 0.6752 1.0383 -0.5293 0.1620  -0.1902 204 ALA B O   
1476 C CB  . ALA A 217 ? 1.4931 0.9254 1.1775 -0.5783 0.1514  -0.2142 204 ALA B CB  
1477 N N   . ASP A 218 ? 1.3459 0.6952 1.0167 -0.4812 0.1477  -0.1632 205 ASP B N   
1478 C CA  . ASP A 218 ? 1.3537 0.6506 1.0089 -0.4453 0.1471  -0.1544 205 ASP B CA  
1479 C C   . ASP A 218 ? 1.2755 0.5739 0.9356 -0.4199 0.1460  -0.1288 205 ASP B C   
1480 O O   . ASP A 218 ? 1.1949 0.5289 0.8739 -0.3874 0.1366  -0.1211 205 ASP B O   
1481 C CB  . ASP A 218 ? 1.3959 0.7215 1.0643 -0.4220 0.1372  -0.1669 205 ASP B CB  
1482 C CG  . ASP A 218 ? 1.4585 0.7364 1.1121 -0.3851 0.1363  -0.1612 205 ASP B CG  
1483 O OD1 . ASP A 218 ? 1.5636 0.7703 1.1893 -0.3802 0.1449  -0.1520 205 ASP B OD1 
1484 O OD2 . ASP A 218 ? 1.3524 0.6661 1.0223 -0.3608 0.1272  -0.1656 205 ASP B OD2 
1485 N N   . PRO A 219 ? 1.2381 0.4936 0.8789 -0.4329 0.1558  -0.1146 206 PRO B N   
1486 C CA  . PRO A 219 ? 1.1712 0.4347 0.8172 -0.4120 0.1547  -0.0909 206 PRO B CA  
1487 C C   . PRO A 219 ? 1.1574 0.3826 0.7923 -0.3708 0.1520  -0.0800 206 PRO B C   
1488 O O   . PRO A 219 ? 1.0823 0.3390 0.7330 -0.3433 0.1451  -0.0667 206 PRO B O   
1489 C CB  . PRO A 219 ? 1.2377 0.4591 0.8614 -0.4396 0.1672  -0.0807 206 PRO B CB  
1490 C CG  . PRO A 219 ? 1.3314 0.4928 0.9277 -0.4682 0.1767  -0.0976 206 PRO B CG  
1491 C CD  . PRO A 219 ? 1.3144 0.5021 0.9232 -0.4642 0.1688  -0.1201 206 PRO B CD  
1492 N N   . ALA A 220 ? 1.2056 0.3644 0.8133 -0.3674 0.1575  -0.0878 207 ALA B N   
1493 C CA  . ALA A 220 ? 1.1991 0.3209 0.7947 -0.3288 0.1553  -0.0815 207 ALA B CA  
1494 C C   . ALA A 220 ? 1.1301 0.3144 0.7554 -0.3024 0.1424  -0.0860 207 ALA B C   
1495 O O   . ALA A 220 ? 1.0857 0.2786 0.7172 -0.2697 0.1374  -0.0720 207 ALA B O   
1496 C CB  . ALA A 220 ? 1.2694 0.3167 0.8327 -0.3334 0.1632  -0.0936 207 ALA B CB  
1497 N N   . GLY A 221 ? 1.1098 0.3386 0.7529 -0.3183 0.1374  -0.1051 208 GLY B N   
1498 C CA  . GLY A 221 ? 1.0453 0.3276 0.7131 -0.2965 0.1263  -0.1119 208 GLY B CA  
1499 C C   . GLY A 221 ? 0.9816 0.3261 0.6775 -0.2842 0.1187  -0.0980 208 GLY B C   
1500 O O   . GLY A 221 ? 0.9676 0.3361 0.6768 -0.2538 0.1112  -0.0918 208 GLY B O   
1501 N N   . LEU A 222 ? 0.9747 0.3459 0.6792 -0.3089 0.1209  -0.0941 209 LEU B N   
1502 C CA  . LEU A 222 ? 0.9629 0.3904 0.6920 -0.2994 0.1149  -0.0814 209 LEU B CA  
1503 C C   . LEU A 222 ? 0.9410 0.3454 0.6635 -0.2693 0.1145  -0.0617 209 LEU B C   
1504 O O   . LEU A 222 ? 0.8941 0.3361 0.6353 -0.2448 0.1064  -0.0557 209 LEU B O   
1505 C CB  . LEU A 222 ? 1.0179 0.4713 0.7533 -0.3308 0.1190  -0.0800 209 LEU B CB  
1506 C CG  . LEU A 222 ? 1.0232 0.5395 0.7848 -0.3231 0.1129  -0.0696 209 LEU B CG  
1507 C CD1 . LEU A 222 ? 1.0400 0.5908 0.8100 -0.3566 0.1166  -0.0739 209 LEU B CD1 
1508 C CD2 . LEU A 222 ? 1.0579 0.5641 0.8172 -0.3009 0.1130  -0.0488 209 LEU B CD2 
1509 N N   . GLU A 223 ? 0.9668 0.3087 0.6614 -0.2724 0.1237  -0.0519 210 GLU B N   
1510 C CA  . GLU A 223 ? 0.9588 0.2757 0.6430 -0.2476 0.1248  -0.0318 210 GLU B CA  
1511 C C   . GLU A 223 ? 0.8949 0.2043 0.5793 -0.2116 0.1189  -0.0312 210 GLU B C   
1512 O O   . GLU A 223 ? 0.8533 0.1831 0.5473 -0.1861 0.1137  -0.0187 210 GLU B O   
1513 C CB  . GLU A 223 ? 1.0159 0.2704 0.6693 -0.2647 0.1368  -0.0226 210 GLU B CB  
1514 C CG  . GLU A 223 ? 1.0625 0.2932 0.7030 -0.2457 0.1396  0.0003  210 GLU B CG  
1515 C CD  . GLU A 223 ? 1.0868 0.3727 0.7506 -0.2245 0.1313  0.0128  210 GLU B CD  
1516 O OE1 . GLU A 223 ? 1.0683 0.4114 0.7564 -0.2388 0.1273  0.0092  210 GLU B OE1 
1517 O OE2 . GLU A 223 ? 1.0669 0.3443 0.7267 -0.1934 0.1282  0.0253  210 GLU B OE2 
1518 N N   . ALA A 224 ? 0.9145 0.1961 0.5883 -0.2109 0.1200  -0.0460 211 ALA B N   
1519 C CA  . ALA A 224 ? 0.9145 0.1886 0.5873 -0.1798 0.1154  -0.0488 211 ALA B CA  
1520 C C   . ALA A 224 ? 0.8512 0.1956 0.5564 -0.1651 0.1043  -0.0497 211 ALA B C   
1521 O O   . ALA A 224 ? 0.8640 0.2196 0.5753 -0.1366 0.0996  -0.0409 211 ALA B O   
1522 C CB  . ALA A 224 ? 0.9646 0.2038 0.6220 -0.1886 0.1189  -0.0674 211 ALA B CB  
1523 N N   . ALA A 225 ? 0.8092 0.2012 0.5347 -0.1855 0.1006  -0.0607 212 ALA B N   
1524 C CA  . ALA A 225 ? 0.7769 0.2321 0.5310 -0.1742 0.0909  -0.0630 212 ALA B CA  
1525 C C   . ALA A 225 ? 0.7207 0.2049 0.4883 -0.1639 0.0878  -0.0461 212 ALA B C   
1526 O O   . ALA A 225 ? 0.6839 0.1980 0.4663 -0.1415 0.0812  -0.0409 212 ALA B O   
1527 C CB  . ALA A 225 ? 0.7480 0.2419 0.5164 -0.1987 0.0887  -0.0783 212 ALA B CB  
1528 N N   . SER A 226 ? 0.7425 0.2148 0.5027 -0.1804 0.0933  -0.0374 213 SER B N   
1529 C CA  . SER A 226 ? 0.7209 0.2209 0.4925 -0.1715 0.0908  -0.0222 213 SER B CA  
1530 C C   . SER A 226 ? 0.7090 0.1886 0.4726 -0.1407 0.0892  -0.0097 213 SER B C   
1531 O O   . SER A 226 ? 0.6973 0.2125 0.4772 -0.1233 0.0829  -0.0031 213 SER B O   
1532 C CB  . SER A 226 ? 0.7403 0.2317 0.5041 -0.1950 0.0976  -0.0152 213 SER B CB  
1533 O OG  . SER A 226 ? 0.7212 0.2420 0.4963 -0.1851 0.0948  -0.0017 213 SER B OG  
1534 N N   . GLN A 227 ? 0.7721 0.1930 0.5092 -0.1344 0.0954  -0.0068 214 GLN B N   
1535 C CA  . GLN A 227 ? 0.7820 0.1801 0.5079 -0.1052 0.0949  0.0055  214 GLN B CA  
1536 C C   . GLN A 227 ? 0.7617 0.1841 0.5009 -0.0811 0.0875  -0.0004 214 GLN B C   
1537 O O   . GLN A 227 ? 0.7809 0.2143 0.5236 -0.0570 0.0838  0.0095  214 GLN B O   
1538 C CB  . GLN A 227 ? 0.8309 0.1586 0.5241 -0.1007 0.1031  0.0079  214 GLN B CB  
1539 C CG  . GLN A 227 ? 0.8836 0.1746 0.5559 -0.1078 0.1107  0.0234  214 GLN B CG  
1540 C CD  . GLN A 227 ? 0.8356 0.1551 0.5165 -0.0921 0.1070  0.0402  214 GLN B CD  
1541 O OE1 . GLN A 227 ? 0.8292 0.1674 0.5176 -0.0645 0.1009  0.0452  214 GLN B OE1 
1542 N NE2 . GLN A 227 ? 0.8513 0.1760 0.5308 -0.1112 0.1109  0.0484  214 GLN B NE2 
1543 N N   . ALA A 228 ? 0.7633 0.1976 0.5102 -0.0888 0.0854  -0.0164 215 ALA B N   
1544 C CA  . ALA A 228 ? 0.7223 0.1808 0.4813 -0.0682 0.0791  -0.0225 215 ALA B CA  
1545 C C   . ALA A 228 ? 0.6590 0.1761 0.4448 -0.0621 0.0715  -0.0172 215 ALA B C   
1546 O O   . ALA A 228 ? 0.7235 0.2588 0.5174 -0.0394 0.0668  -0.0128 215 ALA B O   
1547 C CB  . ALA A 228 ? 0.7471 0.2055 0.5067 -0.0800 0.0791  -0.0407 215 ALA B CB  
1548 N N   . PHE A 229 ? 0.6106 0.1578 0.4100 -0.0822 0.0705  -0.0178 216 PHE B N   
1549 C CA  . PHE A 229 ? 0.5980 0.1943 0.4196 -0.0760 0.0643  -0.0120 216 PHE B CA  
1550 C C   . PHE A 229 ? 0.5845 0.1750 0.4017 -0.0590 0.0641  0.0032  216 PHE B C   
1551 O O   . PHE A 229 ? 0.5617 0.1818 0.3923 -0.0434 0.0586  0.0071  216 PHE B O   
1552 C CB  . PHE A 229 ? 0.5875 0.2214 0.4253 -0.0962 0.0628  -0.0148 216 PHE B CB  
1553 C CG  . PHE A 229 ? 0.6114 0.2640 0.4575 -0.1110 0.0613  -0.0297 216 PHE B CG  
1554 C CD1 . PHE A 229 ? 0.5409 0.2195 0.3996 -0.0990 0.0555  -0.0366 216 PHE B CD1 
1555 C CD2 . PHE A 229 ? 0.6074 0.2561 0.4494 -0.1372 0.0655  -0.0364 216 PHE B CD2 
1556 C CE1 . PHE A 229 ? 0.5465 0.2482 0.4136 -0.1111 0.0535  -0.0493 216 PHE B CE1 
1557 C CE2 . PHE A 229 ? 0.6084 0.2817 0.4595 -0.1497 0.0633  -0.0504 216 PHE B CE2 
1558 C CZ  . PHE A 229 ? 0.5638 0.2616 0.4262 -0.1360 0.0573  -0.0568 216 PHE B CZ  
1559 N N   . ILE A 230 ? 0.6116 0.1664 0.4100 -0.0638 0.0701  0.0122  217 ILE B N   
1560 C CA  . ILE A 230 ? 0.6116 0.1625 0.4043 -0.0486 0.0701  0.0273  217 ILE B CA  
1561 C C   . ILE A 230 ? 0.6111 0.1525 0.3985 -0.0203 0.0675  0.0303  217 ILE B C   
1562 O O   . ILE A 230 ? 0.5867 0.1552 0.3839 -0.0040 0.0626  0.0373  217 ILE B O   
1563 C CB  . ILE A 230 ? 0.6532 0.1640 0.4241 -0.0614 0.0781  0.0359  217 ILE B CB  
1564 C CG1 . ILE A 230 ? 0.6650 0.1994 0.4453 -0.0866 0.0798  0.0356  217 ILE B CG1 
1565 C CG2 . ILE A 230 ? 0.7125 0.2016 0.4676 -0.0406 0.0796  0.0518  217 ILE B CG2 
1566 C CD1 . ILE A 230 ? 0.7429 0.2426 0.5022 -0.0984 0.0879  0.0468  217 ILE B CD1 
1567 N N   . ASP A 231 ? 0.6492 0.1579 0.4234 -0.0146 0.0701  0.0229  218 ASP B N   
1568 C CA  . ASP A 231 ? 0.6936 0.1927 0.4613 0.0131  0.0683  0.0254  218 ASP B CA  
1569 C C   . ASP A 231 ? 0.6528 0.2018 0.4448 0.0231  0.0607  0.0194  218 ASP B C   
1570 O O   . ASP A 231 ? 0.6807 0.2458 0.4767 0.0444  0.0571  0.0252  218 ASP B O   
1571 C CB  . ASP A 231 ? 0.8431 0.2908 0.5880 0.0168  0.0740  0.0188  218 ASP B CB  
1572 C CG  . ASP A 231 ? 1.0092 0.4461 0.7457 0.0476  0.0728  0.0204  218 ASP B CG  
1573 O OD1 . ASP A 231 ? 1.1155 0.5500 0.8455 0.0669  0.0722  0.0337  218 ASP B OD1 
1574 O OD2 . ASP A 231 ? 1.0389 0.4737 0.7761 0.0534  0.0722  0.0083  218 ASP B OD2 
1575 N N   . GLN A 232 ? 0.5854 0.1620 0.3939 0.0072  0.0581  0.0089  219 GLN B N   
1576 C CA  . GLN A 232 ? 0.5755 0.1952 0.4047 0.0155  0.0517  0.0036  219 GLN B CA  
1577 C C   . GLN A 232 ? 0.5321 0.1914 0.3787 0.0161  0.0471  0.0111  219 GLN B C   
1578 O O   . GLN A 232 ? 0.5622 0.2518 0.4220 0.0287  0.0423  0.0116  219 GLN B O   
1579 C CB  . GLN A 232 ? 0.5434 0.1781 0.3825 -0.0007 0.0507  -0.0096 219 GLN B CB  
1580 C CG  . GLN A 232 ? 0.6056 0.2166 0.4335 0.0041  0.0529  -0.0206 219 GLN B CG  
1581 C CD  . GLN A 232 ? 0.6190 0.2394 0.4523 -0.0161 0.0529  -0.0336 219 GLN B CD  
1582 O OE1 . GLN A 232 ? 0.6034 0.2640 0.4554 -0.0230 0.0485  -0.0368 219 GLN B OE1 
1583 N NE2 . GLN A 232 ? 0.6824 0.2643 0.4978 -0.0254 0.0581  -0.0414 219 GLN B NE2 
1584 N N   . GLN A 233 ? 0.5138 0.1723 0.3598 0.0011  0.0490  0.0162  220 GLN B N   
1585 C CA  . GLN A 233 ? 0.4764 0.1702 0.3373 0.0009  0.0452  0.0224  220 GLN B CA  
1586 C C   . GLN A 233 ? 0.4674 0.1620 0.3236 0.0203  0.0437  0.0332  220 GLN B C   
1587 O O   . GLN A 233 ? 0.5355 0.1988 0.3740 0.0314  0.0468  0.0387  220 GLN B O   
1588 C CB  . GLN A 233 ? 0.4676 0.1599 0.3272 -0.0190 0.0483  0.0251  220 GLN B CB  
1589 C CG  . GLN A 233 ? 0.4575 0.1683 0.3287 -0.0380 0.0479  0.0148  220 GLN B CG  
1590 C CD  . GLN A 233 ? 0.4521 0.1601 0.3201 -0.0583 0.0520  0.0167  220 GLN B CD  
1591 O OE1 . GLN A 233 ? 0.4911 0.1830 0.3479 -0.0589 0.0554  0.0269  220 GLN B OE1 
1592 N NE2 . GLN A 233 ? 0.4154 0.1434 0.2938 -0.0739 0.0513  0.0076  220 GLN B NE2 
1593 N N   . MET A 234 ? 0.4489 0.1793 0.3198 0.0234  0.0393  0.0366  221 MET B N   
1594 C CA  . MET A 234 ? 0.4237 0.1621 0.2918 0.0395  0.0373  0.0461  221 MET B CA  
1595 C C   . MET A 234 ? 0.4651 0.1886 0.3214 0.0326  0.0408  0.0558  221 MET B C   
1596 O O   . MET A 234 ? 0.5005 0.2077 0.3422 0.0455  0.0423  0.0657  221 MET B O   
1597 C CB  . MET A 234 ? 0.3850 0.1671 0.2728 0.0425  0.0315  0.0444  221 MET B CB  
1598 C CG  . MET A 234 ? 0.3593 0.1587 0.2581 0.0503  0.0283  0.0367  221 MET B CG  
1599 S SD  . MET A 234 ? 0.3762 0.2214 0.2965 0.0481  0.0230  0.0345  221 MET B SD  
1600 C CE  . MET A 234 ? 0.4112 0.2661 0.3391 0.0548  0.0214  0.0262  221 MET B CE  
1601 N N   . LEU A 235 ? 0.4515 0.1833 0.3140 0.0133  0.0423  0.0536  222 LEU B N   
1602 C CA  . LEU A 235 ? 0.4782 0.1978 0.3298 0.0036  0.0465  0.0622  222 LEU B CA  
1603 C C   . LEU A 235 ? 0.5347 0.2134 0.3693 -0.0091 0.0533  0.0618  222 LEU B C   
1604 O O   . LEU A 235 ? 0.5791 0.2541 0.4181 -0.0214 0.0544  0.0517  222 LEU B O   
1605 C CB  . LEU A 235 ? 0.4156 0.1698 0.2830 -0.0092 0.0447  0.0601  222 LEU B CB  
1606 C CG  . LEU A 235 ? 0.3933 0.1836 0.2748 0.0018  0.0387  0.0604  222 LEU B CG  
1607 C CD1 . LEU A 235 ? 0.3789 0.2007 0.2759 -0.0111 0.0374  0.0558  222 LEU B CD1 
1608 C CD2 . LEU A 235 ? 0.4561 0.2454 0.3276 0.0148  0.0383  0.0710  222 LEU B CD2 
1609 N N   . LYS A 236 ? 0.5377 0.1851 0.3518 -0.0066 0.0583  0.0728  223 LYS B N   
1610 C CA  . LYS A 236 ? 0.6179 0.2172 0.4114 -0.0152 0.0654  0.0729  223 LYS B CA  
1611 C C   . LYS A 236 ? 0.6212 0.2131 0.4100 -0.0407 0.0712  0.0743  223 LYS B C   
1612 O O   . LYS A 236 ? 0.6702 0.2236 0.4371 -0.0467 0.0782  0.0829  223 LYS B O   
1613 C CB  . LYS A 236 ? 0.6410 0.2015 0.4108 0.0046  0.0683  0.0839  223 LYS B CB  
1614 C CG  . LYS A 236 ? 0.6683 0.2449 0.4456 0.0296  0.0622  0.0814  223 LYS B CG  
1615 C CD  . LYS A 236 ? 0.6302 0.1962 0.4105 0.0299  0.0619  0.0682  223 LYS B CD  
1616 C CE  . LYS A 236 ? 0.6071 0.1949 0.3962 0.0533  0.0562  0.0662  223 LYS B CE  
1617 N NZ  . LYS A 236 ? 0.6157 0.1961 0.4075 0.0542  0.0560  0.0536  223 LYS B NZ  
1618 N N   . PHE A 237 ? 0.5959 0.2243 0.4048 -0.0563 0.0687  0.0656  224 PHE B N   
1619 C CA  . PHE A 237 ? 0.6229 0.2503 0.4302 -0.0825 0.0741  0.0637  224 PHE B CA  
1620 C C   . PHE A 237 ? 0.5685 0.2241 0.3949 -0.0951 0.0710  0.0487  224 PHE B C   
1621 O O   . PHE A 237 ? 0.5354 0.2154 0.3770 -0.0830 0.0646  0.0426  224 PHE B O   
1622 C CB  . PHE A 237 ? 0.5527 0.2044 0.3635 -0.0871 0.0749  0.0728  224 PHE B CB  
1623 C CG  . PHE A 237 ? 0.5317 0.2337 0.3654 -0.0781 0.0674  0.0698  224 PHE B CG  
1624 C CD1 . PHE A 237 ? 0.5223 0.2352 0.3584 -0.0561 0.0624  0.0753  224 PHE B CD1 
1625 C CD2 . PHE A 237 ? 0.4751 0.2137 0.3275 -0.0917 0.0656  0.0609  224 PHE B CD2 
1626 C CE1 . PHE A 237 ? 0.4639 0.2193 0.3194 -0.0499 0.0563  0.0717  224 PHE B CE1 
1627 C CE2 . PHE A 237 ? 0.4771 0.2559 0.3484 -0.0824 0.0593  0.0578  224 PHE B CE2 
1628 C CZ  . PHE A 237 ? 0.4328 0.2180 0.3048 -0.0629 0.0551  0.0632  224 PHE B CZ  
1629 N N   . ARG A 238 ? 0.5790 0.2348 0.4050 -0.1193 0.0755  0.0434  225 ARG B N   
1630 C CA  . ARG A 238 ? 0.5655 0.2494 0.4080 -0.1316 0.0728  0.0295  225 ARG B CA  
1631 C C   . ARG A 238 ? 0.5487 0.2833 0.4116 -0.1338 0.0689  0.0293  225 ARG B C   
1632 O O   . ARG A 238 ? 0.5156 0.2583 0.3763 -0.1406 0.0720  0.0369  225 ARG B O   
1633 C CB  . ARG A 238 ? 0.5923 0.2594 0.4260 -0.1583 0.0792  0.0226  225 ARG B CB  
1634 C CG  . ARG A 238 ? 0.6245 0.2392 0.4373 -0.1592 0.0836  0.0196  225 ARG B CG  
1635 C CD  . ARG A 238 ? 0.6025 0.2230 0.4235 -0.1454 0.0778  0.0092  225 ARG B CD  
1636 N NE  . ARG A 238 ? 0.5574 0.2254 0.4015 -0.1471 0.0714  -0.0015 225 ARG B NE  
1637 C CZ  . ARG A 238 ? 0.5685 0.2470 0.4163 -0.1673 0.0725  -0.0136 225 ARG B CZ  
1638 N NH1 . ARG A 238 ? 0.6004 0.2453 0.4315 -0.1873 0.0796  -0.0175 225 ARG B NH1 
1639 N NH2 . ARG A 238 ? 0.5155 0.2397 0.3836 -0.1682 0.0669  -0.0214 225 ARG B NH2 
1640 N N   . LEU A 239 ? 0.4918 0.2587 0.3730 -0.1275 0.0626  0.0206  226 LEU B N   
1641 C CA  . LEU A 239 ? 0.4323 0.2452 0.3321 -0.1299 0.0593  0.0185  226 LEU B CA  
1642 C C   . LEU A 239 ? 0.4722 0.3025 0.3763 -0.1529 0.0625  0.0110  226 LEU B C   
1643 O O   . LEU A 239 ? 0.4823 0.2959 0.3803 -0.1647 0.0646  0.0035  226 LEU B O   
1644 C CB  . LEU A 239 ? 0.3913 0.2295 0.3071 -0.1153 0.0521  0.0123  226 LEU B CB  
1645 C CG  . LEU A 239 ? 0.3824 0.2135 0.2978 -0.0936 0.0483  0.0179  226 LEU B CG  
1646 C CD1 . LEU A 239 ? 0.3704 0.2236 0.3000 -0.0847 0.0425  0.0103  226 LEU B CD1 
1647 C CD2 . LEU A 239 ? 0.3692 0.2140 0.2867 -0.0873 0.0478  0.0264  226 LEU B CD2 
1648 N N   . ASP A 240 ? 0.4339 0.3010 0.3496 -0.1582 0.0622  0.0119  227 ASP B N   
1649 C CA  . ASP A 240 ? 0.4880 0.3813 0.4105 -0.1789 0.0647  0.0044  227 ASP B CA  
1650 C C   . ASP A 240 ? 0.4246 0.3680 0.3673 -0.1717 0.0596  0.0005  227 ASP B C   
1651 O O   . ASP A 240 ? 0.4600 0.4126 0.4102 -0.1523 0.0545  0.0025  227 ASP B O   
1652 C CB  . ASP A 240 ? 0.5760 0.4579 0.4866 -0.1988 0.0727  0.0100  227 ASP B CB  
1653 C CG  . ASP A 240 ? 0.6235 0.5190 0.5343 -0.1936 0.0743  0.0205  227 ASP B CG  
1654 O OD1 . ASP A 240 ? 0.5284 0.4546 0.4527 -0.1788 0.0693  0.0207  227 ASP B OD1 
1655 O OD2 . ASP A 240 ? 0.6445 0.5197 0.5410 -0.2053 0.0811  0.0283  227 ASP B OD2 
1656 N N   . ALA A 241 ? 0.4456 0.4210 0.3965 -0.1877 0.0611  -0.0063 228 ALA B N   
1657 C CA  . ALA A 241 ? 0.3777 0.4003 0.3465 -0.1800 0.0566  -0.0106 228 ALA B CA  
1658 C C   . ALA A 241 ? 0.3801 0.4181 0.3536 -0.1662 0.0557  -0.0033 228 ALA B C   
1659 O O   . ALA A 241 ? 0.3469 0.4095 0.3322 -0.1509 0.0508  -0.0053 228 ALA B O   
1660 C CB  . ALA A 241 ? 0.3746 0.4309 0.3507 -0.1993 0.0585  -0.0194 228 ALA B CB  
1661 N N   . SER A 242 ? 0.4184 0.4397 0.3813 -0.1713 0.0607  0.0053  229 SER B N   
1662 C CA  . SER A 242 ? 0.3546 0.3897 0.3199 -0.1599 0.0604  0.0117  229 SER B CA  
1663 C C   . SER A 242 ? 0.3306 0.3524 0.2973 -0.1375 0.0546  0.0140  229 SER B C   
1664 O O   . SER A 242 ? 0.3847 0.4264 0.3591 -0.1244 0.0518  0.0144  229 SER B O   
1665 C CB  . SER A 242 ? 0.3407 0.3562 0.2916 -0.1697 0.0668  0.0211  229 SER B CB  
1666 O OG  . SER A 242 ? 0.3723 0.4050 0.3230 -0.1919 0.0727  0.0190  229 SER B OG  
1667 N N   . ASP A 243 ? 0.3250 0.3128 0.2834 -0.1338 0.0535  0.0151  230 ASP B N   
1668 C CA  . ASP A 243 ? 0.3371 0.3165 0.2976 -0.1136 0.0483  0.0171  230 ASP B CA  
1669 C C   . ASP A 243 ? 0.2967 0.3031 0.2721 -0.1048 0.0432  0.0099  230 ASP B C   
1670 O O   . ASP A 243 ? 0.3083 0.3211 0.2887 -0.0899 0.0397  0.0111  230 ASP B O   
1671 C CB  . ASP A 243 ? 0.3485 0.2920 0.2990 -0.1094 0.0478  0.0186  230 ASP B CB  
1672 C CG  . ASP A 243 ? 0.4156 0.3279 0.3490 -0.1135 0.0526  0.0276  230 ASP B CG  
1673 O OD1 . ASP A 243 ? 0.3743 0.2882 0.3051 -0.1036 0.0520  0.0347  230 ASP B OD1 
1674 O OD2 . ASP A 243 ? 0.4251 0.3130 0.3474 -0.1269 0.0572  0.0272  230 ASP B OD2 
1675 N N   . CYS A 244 ? 0.2665 0.2852 0.2474 -0.1132 0.0428  0.0026  231 CYS B N   
1676 C CA  . CYS A 244 ? 0.2763 0.3210 0.2699 -0.1032 0.0381  -0.0031 231 CYS B CA  
1677 C C   . CYS A 244 ? 0.2238 0.3009 0.2259 -0.0989 0.0381  -0.0032 231 CYS B C   
1678 O O   . CYS A 244 ? 0.2401 0.3286 0.2487 -0.0843 0.0348  -0.0037 231 CYS B O   
1679 C CB  . CYS A 244 ? 0.2866 0.3438 0.2846 -0.1117 0.0371  -0.0110 231 CYS B CB  
1680 S SG  . CYS A 244 ? 0.3674 0.3878 0.3548 -0.1167 0.0373  -0.0134 231 CYS B SG  
1681 N N   . ALA A 245 ? 0.2475 0.3390 0.2488 -0.1115 0.0424  -0.0026 232 ALA B N   
1682 C CA  . ALA A 245 ? 0.2222 0.3484 0.2317 -0.1073 0.0428  -0.0038 232 ALA B CA  
1683 C C   . ALA A 245 ? 0.2397 0.3588 0.2466 -0.0942 0.0423  0.0013  232 ALA B C   
1684 O O   . ALA A 245 ? 0.2270 0.3660 0.2409 -0.0818 0.0403  -0.0010 232 ALA B O   
1685 C CB  . ALA A 245 ? 0.2498 0.3955 0.2587 -0.1258 0.0483  -0.0044 232 ALA B CB  
1686 N N   . ARG A 246 ? 0.2632 0.3537 0.2592 -0.0958 0.0440  0.0079  233 ARG B N   
1687 C CA  . ARG A 246 ? 0.2631 0.3479 0.2563 -0.0834 0.0428  0.0119  233 ARG B CA  
1688 C C   . ARG A 246 ? 0.2442 0.3284 0.2438 -0.0674 0.0376  0.0085  233 ARG B C   
1689 O O   . ARG A 246 ? 0.2273 0.3226 0.2300 -0.0571 0.0364  0.0071  233 ARG B O   
1690 C CB  . ARG A 246 ? 0.2988 0.3543 0.2788 -0.0865 0.0449  0.0198  233 ARG B CB  
1691 C CG  . ARG A 246 ? 0.3417 0.4001 0.3141 -0.1014 0.0511  0.0245  233 ARG B CG  
1692 C CD  . ARG A 246 ? 0.4063 0.4273 0.3637 -0.1046 0.0531  0.0324  233 ARG B CD  
1693 N NE  . ARG A 246 ? 0.4860 0.5016 0.4329 -0.1207 0.0598  0.0382  233 ARG B NE  
1694 C CZ  . ARG A 246 ? 0.6638 0.6612 0.5963 -0.1216 0.0634  0.0481  233 ARG B CZ  
1695 N NH1 . ARG A 246 ? 0.5798 0.5542 0.5035 -0.1087 0.0611  0.0543  233 ARG B NH1 
1696 N NH2 . ARG A 246 ? 0.7302 0.7325 0.6558 -0.1372 0.0700  0.0525  233 ARG B NH2 
1697 N N   . LEU A 247 ? 0.2508 0.3213 0.2515 -0.0661 0.0350  0.0067  234 LEU B N   
1698 C CA  . LEU A 247 ? 0.2189 0.2857 0.2240 -0.0527 0.0307  0.0045  234 LEU B CA  
1699 C C   . LEU A 247 ? 0.2030 0.2955 0.2172 -0.0468 0.0295  -0.0006 234 LEU B C   
1700 O O   . LEU A 247 ? 0.1964 0.2913 0.2133 -0.0350 0.0276  -0.0019 234 LEU B O   
1701 C CB  . LEU A 247 ? 0.1964 0.2427 0.1995 -0.0526 0.0287  0.0043  234 LEU B CB  
1702 C CG  . LEU A 247 ? 0.2203 0.2646 0.2280 -0.0405 0.0248  0.0024  234 LEU B CG  
1703 C CD1 . LEU A 247 ? 0.2199 0.2603 0.2268 -0.0312 0.0237  0.0041  234 LEU B CD1 
1704 C CD2 . LEU A 247 ? 0.2228 0.2481 0.2272 -0.0420 0.0237  0.0024  234 LEU B CD2 
1705 N N   . ALA A 248 ? 0.2103 0.3226 0.2288 -0.0548 0.0308  -0.0038 235 ALA B N   
1706 C CA  . ALA A 248 ? 0.2096 0.3488 0.2363 -0.0469 0.0294  -0.0081 235 ALA B CA  
1707 C C   . ALA A 248 ? 0.2208 0.3761 0.2490 -0.0393 0.0310  -0.0085 235 ALA B C   
1708 O O   . ALA A 248 ? 0.2039 0.3684 0.2356 -0.0257 0.0293  -0.0109 235 ALA B O   
1709 C CB  . ALA A 248 ? 0.1865 0.3502 0.2179 -0.0577 0.0304  -0.0120 235 ALA B CB  
1710 N N   . LEU A 249 ? 0.1703 0.3289 0.1947 -0.0475 0.0345  -0.0062 236 LEU B N   
1711 C CA  . LEU A 249 ? 0.1891 0.3650 0.2143 -0.0400 0.0363  -0.0074 236 LEU B CA  
1712 C C   . LEU A 249 ? 0.2053 0.3629 0.2277 -0.0260 0.0339  -0.0076 236 LEU B C   
1713 O O   . LEU A 249 ? 0.2201 0.3873 0.2446 -0.0137 0.0335  -0.0112 236 LEU B O   
1714 C CB  . LEU A 249 ? 0.1659 0.3445 0.1855 -0.0510 0.0406  -0.0038 236 LEU B CB  
1715 C CG  . LEU A 249 ? 0.2115 0.4103 0.2332 -0.0673 0.0442  -0.0039 236 LEU B CG  
1716 C CD1 . LEU A 249 ? 0.2072 0.4026 0.2208 -0.0790 0.0491  0.0015  236 LEU B CD1 
1717 C CD2 . LEU A 249 ? 0.2107 0.4495 0.2423 -0.0624 0.0446  -0.0099 236 LEU B CD2 
1718 N N   . PHE A 250 ? 0.1947 0.3249 0.2115 -0.0280 0.0324  -0.0041 237 PHE B N   
1719 C CA  . PHE A 250 ? 0.1954 0.3093 0.2095 -0.0180 0.0303  -0.0047 237 PHE B CA  
1720 C C   . PHE A 250 ? 0.1868 0.2988 0.2051 -0.0074 0.0279  -0.0080 237 PHE B C   
1721 O O   . PHE A 250 ? 0.1966 0.3066 0.2137 0.0024  0.0277  -0.0109 237 PHE B O   
1722 C CB  . PHE A 250 ? 0.2099 0.2993 0.2185 -0.0218 0.0289  -0.0003 237 PHE B CB  
1723 C CG  . PHE A 250 ? 0.2095 0.2852 0.2161 -0.0135 0.0265  -0.0017 237 PHE B CG  
1724 C CD1 . PHE A 250 ? 0.2164 0.2951 0.2191 -0.0102 0.0272  -0.0032 237 PHE B CD1 
1725 C CD2 . PHE A 250 ? 0.2526 0.3147 0.2611 -0.0096 0.0239  -0.0022 237 PHE B CD2 
1726 C CE1 . PHE A 250 ? 0.2436 0.3120 0.2447 -0.0044 0.0253  -0.0061 237 PHE B CE1 
1727 C CE2 . PHE A 250 ? 0.2362 0.2880 0.2432 -0.0041 0.0223  -0.0041 237 PHE B CE2 
1728 C CZ  . PHE A 250 ? 0.2439 0.2984 0.2473 -0.0020 0.0230  -0.0065 237 PHE B CZ  
1729 N N   . LEU A 251 ? 0.1792 0.2897 0.2007 -0.0096 0.0262  -0.0074 238 LEU B N   
1730 C CA  . LEU A 251 ? 0.1901 0.2971 0.2140 0.0004  0.0240  -0.0089 238 LEU B CA  
1731 C C   . LEU A 251 ? 0.2231 0.3511 0.2501 0.0106  0.0248  -0.0120 238 LEU B C   
1732 O O   . LEU A 251 ? 0.2283 0.3507 0.2548 0.0218  0.0236  -0.0125 238 LEU B O   
1733 C CB  . LEU A 251 ? 0.1746 0.2790 0.2005 -0.0050 0.0223  -0.0078 238 LEU B CB  
1734 C CG  . LEU A 251 ? 0.1857 0.2656 0.2075 -0.0100 0.0213  -0.0049 238 LEU B CG  
1735 C CD1 . LEU A 251 ? 0.1748 0.2498 0.1975 -0.0145 0.0197  -0.0047 238 LEU B CD1 
1736 C CD2 . LEU A 251 ? 0.1810 0.2434 0.2003 -0.0017 0.0200  -0.0044 238 LEU B CD2 
1737 N N   . ALA A 252 ? 0.2146 0.3676 0.2445 0.0066  0.0270  -0.0136 239 ALA B N   
1738 C CA  . ALA A 252 ? 0.1970 0.3740 0.2300 0.0180  0.0280  -0.0169 239 ALA B CA  
1739 C C   . ALA A 252 ? 0.2124 0.3881 0.2414 0.0266  0.0301  -0.0195 239 ALA B C   
1740 O O   . ALA A 252 ? 0.2059 0.3943 0.2353 0.0399  0.0310  -0.0226 239 ALA B O   
1741 C CB  . ALA A 252 ? 0.2163 0.4262 0.2554 0.0087  0.0294  -0.0181 239 ALA B CB  
1742 N N   . SER A 253 ? 0.2058 0.3704 0.2307 0.0191  0.0314  -0.0187 240 SER B N   
1743 C CA  . SER A 253 ? 0.2244 0.3934 0.2454 0.0248  0.0337  -0.0221 240 SER B CA  
1744 C C   . SER A 253 ? 0.2552 0.3992 0.2704 0.0360  0.0328  -0.0250 240 SER B C   
1745 O O   . SER A 253 ? 0.2432 0.3654 0.2572 0.0364  0.0305  -0.0231 240 SER B O   
1746 C CB  . SER A 253 ? 0.2354 0.4018 0.2529 0.0124  0.0351  -0.0194 240 SER B CB  
1747 O OG  . SER A 253 ? 0.2475 0.3859 0.2606 0.0092  0.0328  -0.0170 240 SER B OG  
1748 N N   . ASP A 254 ? 0.2509 0.3967 0.2614 0.0436  0.0350  -0.0302 241 ASP B N   
1749 C CA  . ASP A 254 ? 0.2761 0.3953 0.2795 0.0508  0.0346  -0.0339 241 ASP B CA  
1750 C C   . ASP A 254 ? 0.2686 0.3679 0.2691 0.0400  0.0327  -0.0320 241 ASP B C   
1751 O O   . ASP A 254 ? 0.2610 0.3385 0.2566 0.0424  0.0322  -0.0348 241 ASP B O   
1752 C CB  . ASP A 254 ? 0.2879 0.4133 0.2860 0.0620  0.0376  -0.0413 241 ASP B CB  
1753 C CG  . ASP A 254 ? 0.3473 0.4863 0.3468 0.0775  0.0391  -0.0433 241 ASP B CG  
1754 O OD1 . ASP A 254 ? 0.5225 0.6612 0.5261 0.0805  0.0374  -0.0390 241 ASP B OD1 
1755 O OD2 . ASP A 254 ? 0.4375 0.5906 0.4344 0.0877  0.0419  -0.0489 241 ASP B OD2 
1756 N N   . ASP A 255 ? 0.2321 0.3391 0.2346 0.0281  0.0321  -0.0273 242 ASP B N   
1757 C CA  . ASP A 255 ? 0.2406 0.3315 0.2401 0.0205  0.0301  -0.0250 242 ASP B CA  
1758 C C   . ASP A 255 ? 0.2578 0.3295 0.2593 0.0196  0.0276  -0.0223 242 ASP B C   
1759 O O   . ASP A 255 ? 0.2747 0.3331 0.2739 0.0151  0.0258  -0.0215 242 ASP B O   
1760 C CB  . ASP A 255 ? 0.2399 0.3396 0.2393 0.0100  0.0303  -0.0192 242 ASP B CB  
1761 C CG  . ASP A 255 ? 0.2861 0.4039 0.2819 0.0099  0.0332  -0.0213 242 ASP B CG  
1762 O OD1 . ASP A 255 ? 0.2875 0.4243 0.2862 0.0118  0.0356  -0.0225 242 ASP B OD1 
1763 O OD2 . ASP A 255 ? 0.2911 0.4059 0.2812 0.0092  0.0329  -0.0229 242 ASP B OD2 
1764 N N   . SER A 256 ? 0.2147 0.2880 0.2203 0.0240  0.0273  -0.0209 243 SER B N   
1765 C CA  . SER A 256 ? 0.2261 0.2831 0.2328 0.0230  0.0252  -0.0182 243 SER B CA  
1766 C C   . SER A 256 ? 0.2086 0.2545 0.2130 0.0334  0.0259  -0.0204 243 SER B C   
1767 O O   . SER A 256 ? 0.2159 0.2547 0.2217 0.0346  0.0247  -0.0173 243 SER B O   
1768 C CB  . SER A 256 ? 0.2340 0.2981 0.2457 0.0172  0.0240  -0.0134 243 SER B CB  
1769 O OG  . SER A 256 ? 0.2319 0.3147 0.2471 0.0223  0.0250  -0.0144 243 SER B OG  
1770 N N   . ARG A 257 ? 0.2115 0.2552 0.2110 0.0414  0.0280  -0.0258 244 ARG B N   
1771 C CA  . ARG A 257 ? 0.2388 0.2713 0.2340 0.0538  0.0295  -0.0274 244 ARG B CA  
1772 C C   . ARG A 257 ? 0.2725 0.2778 0.2634 0.0528  0.0292  -0.0259 244 ARG B C   
1773 O O   . ARG A 257 ? 0.2863 0.2818 0.2741 0.0619  0.0300  -0.0235 244 ARG B O   
1774 C CB  . ARG A 257 ? 0.2418 0.2756 0.2312 0.0635  0.0324  -0.0342 244 ARG B CB  
1775 C CG  . ARG A 257 ? 0.2748 0.2920 0.2581 0.0573  0.0330  -0.0397 244 ARG B CG  
1776 C CD  . ARG A 257 ? 0.4342 0.4526 0.4106 0.0685  0.0363  -0.0477 244 ARG B CD  
1777 N NE  . ARG A 257 ? 0.4167 0.4214 0.3870 0.0841  0.0387  -0.0490 244 ARG B NE  
1778 C CZ  . ARG A 257 ? 0.4928 0.4645 0.4521 0.0885  0.0411  -0.0533 244 ARG B CZ  
1779 N NH1 . ARG A 257 ? 0.4762 0.4315 0.4284 0.1032  0.0434  -0.0522 244 ARG B NH1 
1780 N NH2 . ARG A 257 ? 0.5130 0.4664 0.4676 0.0772  0.0412  -0.0580 244 ARG B NH2 
1781 N N   . GLY A 258 ? 0.2502 0.2454 0.2407 0.0419  0.0281  -0.0264 245 GLY B N   
1782 C CA  . GLY A 258 ? 0.2800 0.2532 0.2674 0.0381  0.0280  -0.0249 245 GLY B CA  
1783 C C   . GLY A 258 ? 0.2445 0.2207 0.2375 0.0327  0.0258  -0.0185 245 GLY B C   
1784 O O   . GLY A 258 ? 0.2433 0.2050 0.2346 0.0279  0.0258  -0.0170 245 GLY B O   
1785 N N   . CYS A 259 ? 0.2179 0.2128 0.2171 0.0318  0.0240  -0.0153 246 CYS B N   
1786 C CA  . CYS A 259 ? 0.1926 0.1904 0.1964 0.0262  0.0219  -0.0105 246 CYS B CA  
1787 C C   . CYS A 259 ? 0.1999 0.2007 0.2043 0.0333  0.0219  -0.0070 246 CYS B C   
1788 O O   . CYS A 259 ? 0.2013 0.2180 0.2077 0.0390  0.0220  -0.0074 246 CYS B O   
1789 C CB  . CYS A 259 ? 0.1945 0.2084 0.2030 0.0198  0.0205  -0.0093 246 CYS B CB  
1790 S SG  . CYS A 259 ? 0.2332 0.2463 0.2401 0.0123  0.0200  -0.0111 246 CYS B SG  
1791 N N   . THR A 260 ? 0.2124 0.2018 0.2153 0.0327  0.0216  -0.0036 247 THR B N   
1792 C CA  . THR A 260 ? 0.1985 0.1953 0.2020 0.0392  0.0210  0.0000  247 THR B CA  
1793 C C   . THR A 260 ? 0.2172 0.2075 0.2207 0.0349  0.0202  0.0037  247 THR B C   
1794 O O   . THR A 260 ? 0.2034 0.1809 0.2056 0.0286  0.0208  0.0036  247 THR B O   
1795 C CB  . THR A 260 ? 0.2272 0.2142 0.2237 0.0516  0.0233  0.0009  247 THR B CB  
1796 O OG1 . THR A 260 ? 0.2162 0.2179 0.2135 0.0606  0.0223  0.0041  247 THR B OG1 
1797 C CG2 . THR A 260 ? 0.2358 0.1957 0.2247 0.0505  0.0256  0.0025  247 THR B CG2 
1798 N N   . GLY A 261 ? 0.2102 0.2132 0.2159 0.0373  0.0186  0.0062  248 GLY B N   
1799 C CA  . GLY A 261 ? 0.1961 0.1961 0.2012 0.0350  0.0180  0.0096  248 GLY B CA  
1800 C C   . GLY A 261 ? 0.2073 0.2110 0.2169 0.0251  0.0164  0.0078  248 GLY B C   
1801 O O   . GLY A 261 ? 0.1989 0.2002 0.2082 0.0226  0.0161  0.0097  248 GLY B O   
1802 N N   . GLN A 262 ? 0.2148 0.2243 0.2278 0.0203  0.0158  0.0047  249 GLN B N   
1803 C CA  . GLN A 262 ? 0.1929 0.2003 0.2078 0.0126  0.0149  0.0037  249 GLN B CA  
1804 C C   . GLN A 262 ? 0.2144 0.2317 0.2315 0.0080  0.0138  0.0021  249 GLN B C   
1805 O O   . GLN A 262 ? 0.2107 0.2400 0.2293 0.0087  0.0137  0.0009  249 GLN B O   
1806 C CB  . GLN A 262 ? 0.1965 0.1990 0.2110 0.0101  0.0156  0.0020  249 GLN B CB  
1807 C CG  . GLN A 262 ? 0.2204 0.2109 0.2324 0.0101  0.0166  0.0022  249 GLN B CG  
1808 C CD  . GLN A 262 ? 0.2426 0.2306 0.2555 0.0066  0.0161  0.0037  249 GLN B CD  
1809 O OE1 . GLN A 262 ? 0.3005 0.2930 0.3151 0.0043  0.0147  0.0039  249 GLN B OE1 
1810 N NE2 . GLN A 262 ? 0.2644 0.2449 0.2750 0.0070  0.0175  0.0053  249 GLN B NE2 
1811 N N   . ASN A 263 ? 0.1695 0.1817 0.1862 0.0036  0.0133  0.0020  250 ASN B N   
1812 C CA  . ASN A 263 ? 0.2173 0.2320 0.2337 -0.0021 0.0130  0.0003  250 ASN B CA  
1813 C C   . ASN A 263 ? 0.2202 0.2295 0.2351 -0.0052 0.0138  0.0010  250 ASN B C   
1814 O O   . ASN A 263 ? 0.2557 0.2583 0.2697 -0.0036 0.0137  0.0023  250 ASN B O   
1815 C CB  . ASN A 263 ? 0.2353 0.2435 0.2497 -0.0036 0.0125  -0.0003 250 ASN B CB  
1816 C CG  . ASN A 263 ? 0.2626 0.2781 0.2775 -0.0011 0.0118  -0.0011 250 ASN B CG  
1817 O OD1 . ASN A 263 ? 0.2546 0.2822 0.2709 -0.0004 0.0113  -0.0021 250 ASN B OD1 
1818 N ND2 . ASN A 263 ? 0.3070 0.3180 0.3202 -0.0001 0.0116  -0.0013 250 ASN B ND2 
1819 N N   . PHE A 264 ? 0.1766 0.1902 0.1908 -0.0107 0.0147  0.0001  251 PHE B N   
1820 C CA  . PHE A 264 ? 0.1889 0.1971 0.1999 -0.0143 0.0158  0.0018  251 PHE B CA  
1821 C C   . PHE A 264 ? 0.1774 0.1785 0.1844 -0.0213 0.0168  0.0013  251 PHE B C   
1822 O O   . PHE A 264 ? 0.2386 0.2480 0.2465 -0.0274 0.0177  -0.0011 251 PHE B O   
1823 C CB  . PHE A 264 ? 0.2030 0.2234 0.2155 -0.0155 0.0171  0.0013  251 PHE B CB  
1824 C CG  . PHE A 264 ? 0.2473 0.2701 0.2616 -0.0085 0.0166  0.0008  251 PHE B CG  
1825 C CD1 . PHE A 264 ? 0.2441 0.2720 0.2611 -0.0026 0.0161  -0.0006 251 PHE B CD1 
1826 C CD2 . PHE A 264 ? 0.3795 0.3997 0.3914 -0.0078 0.0171  0.0015  251 PHE B CD2 
1827 C CE1 . PHE A 264 ? 0.2434 0.2673 0.2598 0.0033  0.0164  -0.0012 251 PHE B CE1 
1828 C CE2 . PHE A 264 ? 0.3811 0.4012 0.3934 -0.0026 0.0170  -0.0004 251 PHE B CE2 
1829 C CZ  . PHE A 264 ? 0.2775 0.2970 0.2917 0.0025  0.0168  -0.0018 251 PHE B CZ  
1830 N N   . VAL A 265 ? 0.1994 0.1849 0.2010 -0.0205 0.0171  0.0035  252 VAL B N   
1831 C CA  . VAL A 265 ? 0.2157 0.1891 0.2116 -0.0259 0.0183  0.0023  252 VAL B CA  
1832 C C   . VAL A 265 ? 0.2451 0.2059 0.2331 -0.0305 0.0209  0.0060  252 VAL B C   
1833 O O   . VAL A 265 ? 0.2533 0.2084 0.2381 -0.0252 0.0207  0.0103  252 VAL B O   
1834 C CB  . VAL A 265 ? 0.2099 0.1724 0.2034 -0.0191 0.0172  0.0023  252 VAL B CB  
1835 C CG1 . VAL A 265 ? 0.2646 0.2097 0.2500 -0.0229 0.0189  0.0004  252 VAL B CG1 
1836 C CG2 . VAL A 265 ? 0.2202 0.1940 0.2201 -0.0148 0.0152  -0.0003 252 VAL B CG2 
1837 N N   . VAL A 266 ? 0.2301 0.1874 0.2142 -0.0412 0.0234  0.0045  253 VAL B N   
1838 C CA  . VAL A 266 ? 0.2419 0.1863 0.2172 -0.0476 0.0268  0.0087  253 VAL B CA  
1839 C C   . VAL A 266 ? 0.2644 0.1854 0.2301 -0.0534 0.0291  0.0069  253 VAL B C   
1840 O O   . VAL A 266 ? 0.2704 0.1945 0.2363 -0.0648 0.0306  0.0019  253 VAL B O   
1841 C CB  . VAL A 266 ? 0.2699 0.2313 0.2481 -0.0572 0.0290  0.0087  253 VAL B CB  
1842 C CG1 . VAL A 266 ? 0.2324 0.2131 0.2177 -0.0656 0.0289  0.0021  253 VAL B CG1 
1843 C CG2 . VAL A 266 ? 0.2942 0.2386 0.2608 -0.0659 0.0335  0.0140  253 VAL B CG2 
1844 N N   . ASP A 267 ? 0.3012 0.2000 0.2585 -0.0452 0.0292  0.0098  254 ASP B N   
1845 C CA  . ASP A 267 ? 0.3017 0.1778 0.2502 -0.0482 0.0310  0.0061  254 ASP B CA  
1846 C C   . ASP A 267 ? 0.3513 0.1977 0.2853 -0.0414 0.0334  0.0124  254 ASP B C   
1847 O O   . ASP A 267 ? 0.3580 0.1821 0.2832 -0.0392 0.0348  0.0097  254 ASP B O   
1848 C CB  . ASP A 267 ? 0.2931 0.1778 0.2483 -0.0409 0.0277  0.0002  254 ASP B CB  
1849 C CG  . ASP A 267 ? 0.3006 0.1850 0.2571 -0.0253 0.0252  0.0033  254 ASP B CG  
1850 O OD1 . ASP A 267 ? 0.2869 0.1733 0.2431 -0.0189 0.0247  0.0099  254 ASP B OD1 
1851 O OD2 . ASP A 267 ? 0.2842 0.1692 0.2422 -0.0200 0.0238  -0.0011 254 ASP B OD2 
1852 N N   . ALA A 268 ? 0.3380 0.1844 0.2690 -0.0358 0.0337  0.0207  255 ALA B N   
1853 C CA  . ALA A 268 ? 0.3276 0.1462 0.2431 -0.0280 0.0361  0.0282  255 ALA B CA  
1854 C C   . ALA A 268 ? 0.3629 0.1723 0.2760 -0.0128 0.0340  0.0267  255 ALA B C   
1855 O O   . ALA A 268 ? 0.3735 0.1548 0.2718 -0.0051 0.0364  0.0307  255 ALA B O   
1856 C CB  . ALA A 268 ? 0.3513 0.1404 0.2516 -0.0409 0.0420  0.0300  255 ALA B CB  
1857 N N   . GLY A 269 ? 0.4044 0.2379 0.3313 -0.0074 0.0298  0.0215  256 GLY B N   
1858 C CA  . GLY A 269 ? 0.3660 0.1977 0.2927 0.0066  0.0278  0.0199  256 GLY B CA  
1859 C C   . GLY A 269 ? 0.3803 0.1976 0.3031 0.0047  0.0292  0.0120  256 GLY B C   
1860 O O   . GLY A 269 ? 0.3721 0.1861 0.2928 0.0173  0.0283  0.0105  256 GLY B O   
1861 N N   . LEU A 270 ? 0.3259 0.1366 0.2473 -0.0104 0.0314  0.0063  257 LEU B N   
1862 C CA  . LEU A 270 ? 0.3670 0.1610 0.2818 -0.0124 0.0330  -0.0020 257 LEU B CA  
1863 C C   . LEU A 270 ? 0.3645 0.1817 0.2907 -0.0057 0.0294  -0.0078 257 LEU B C   
1864 O O   . LEU A 270 ? 0.3804 0.1859 0.3005 0.0002  0.0301  -0.0131 257 LEU B O   
1865 C CB  . LEU A 270 ? 0.4047 0.1944 0.3177 -0.0320 0.0356  -0.0074 257 LEU B CB  
1866 C CG  . LEU A 270 ? 0.4164 0.1870 0.3206 -0.0393 0.0380  -0.0173 257 LEU B CG  
1867 C CD1 . LEU A 270 ? 0.4603 0.1895 0.3453 -0.0318 0.0421  -0.0149 257 LEU B CD1 
1868 C CD2 . LEU A 270 ? 0.4071 0.1809 0.3115 -0.0613 0.0403  -0.0224 257 LEU B CD2 
1869 N N   . SER A 271 ? 0.3070 0.1547 0.2477 -0.0052 0.0259  -0.0063 258 SER B N   
1870 C CA  . SER A 271 ? 0.3094 0.1778 0.2595 0.0001  0.0231  -0.0105 258 SER B CA  
1871 C C   . SER A 271 ? 0.3356 0.2079 0.2864 0.0155  0.0219  -0.0078 258 SER B C   
1872 O O   . SER A 271 ? 0.3269 0.2156 0.2844 0.0198  0.0203  -0.0107 258 SER B O   
1873 C CB  . SER A 271 ? 0.2889 0.1848 0.2523 -0.0055 0.0206  -0.0101 258 SER B CB  
1874 O OG  . SER A 271 ? 0.3109 0.2164 0.2795 -0.0016 0.0194  -0.0035 258 SER B OG  
1875 N N   . ILE A 272 ? 0.3325 0.1917 0.2760 0.0243  0.0228  -0.0020 259 ILE B N   
1876 C CA  . ILE A 272 ? 0.3337 0.2028 0.2790 0.0392  0.0213  0.0008  259 ILE B CA  
1877 C C   . ILE A 272 ? 0.3705 0.2128 0.3007 0.0505  0.0239  0.0016  259 ILE B C   
1878 O O   . ILE A 272 ? 0.3970 0.2238 0.3182 0.0546  0.0251  0.0081  259 ILE B O   
1879 C CB  . ILE A 272 ? 0.3398 0.2259 0.2918 0.0409  0.0192  0.0076  259 ILE B CB  
1880 C CG1 . ILE A 272 ? 0.3282 0.2368 0.2934 0.0306  0.0173  0.0057  259 ILE B CG1 
1881 C CG2 . ILE A 272 ? 0.3182 0.2190 0.2727 0.0551  0.0175  0.0093  259 ILE B CG2 
1882 C CD1 . ILE A 272 ? 0.3949 0.3185 0.3661 0.0300  0.0155  0.0105  259 ILE B CD1 
1883 N N   . GLN A 273 ? 0.3824 0.2161 0.3080 0.0541  0.0252  -0.0053 260 GLN B N   
1884 C CA  . GLN A 273 ? 0.4525 0.2558 0.3616 0.0653  0.0283  -0.0056 260 GLN B CA  
1885 C C   . GLN A 273 ? 0.5080 0.3205 0.4173 0.0802  0.0280  -0.0103 260 GLN B C   
1886 O O   . GLN A 273 ? 0.5218 0.3092 0.4164 0.0936  0.0306  -0.0099 260 GLN B O   
1887 C CB  . GLN A 273 ? 0.5282 0.3030 0.4262 0.0548  0.0317  -0.0132 260 GLN B CB  
1888 C CG  . GLN A 273 ? 0.5251 0.2806 0.4170 0.0395  0.0339  -0.0101 260 GLN B CG  
1889 C CD  . GLN A 273 ? 0.5811 0.3077 0.4609 0.0280  0.0377  -0.0186 260 GLN B CD  
1890 O OE1 . GLN A 273 ? 0.5849 0.2807 0.4490 0.0361  0.0411  -0.0219 260 GLN B OE1 
1891 N NE2 . GLN A 273 ? 0.5865 0.3235 0.4730 0.0091  0.0374  -0.0224 260 GLN B NE2 
1892 O OXT . GLN A 273 ? 0.4472 0.2887 0.3694 0.0778  0.0259  -0.0144 260 GLN B OXT 
1893 N N   . ASN B 15  ? 0.6232 0.7469 0.5462 0.0332  0.0119  -0.0682 2   ASN A N   
1894 C CA  . ASN B 15  ? 0.5119 0.6168 0.4393 0.0327  0.0128  -0.0634 2   ASN A CA  
1895 C C   . ASN B 15  ? 0.4861 0.6081 0.4293 0.0274  0.0137  -0.0507 2   ASN A C   
1896 O O   . ASN B 15  ? 0.4062 0.5307 0.3575 0.0176  0.0127  -0.0447 2   ASN A O   
1897 C CB  . ASN B 15  ? 0.5754 0.6476 0.4970 0.0265  0.0118  -0.0677 2   ASN A CB  
1898 C CG  . ASN B 15  ? 0.7550 0.8067 0.6746 0.0322  0.0133  -0.0657 2   ASN A CG  
1899 O OD1 . ASN B 15  ? 0.7647 0.8288 0.6897 0.0399  0.0147  -0.0605 2   ASN A OD1 
1900 N ND2 . ASN B 15  ? 0.6499 0.6709 0.5613 0.0281  0.0131  -0.0695 2   ASN A ND2 
1901 N N   . ARG B 16  ? 0.3541 0.4859 0.3005 0.0345  0.0155  -0.0471 3   ARG A N   
1902 C CA  . ARG B 16  ? 0.3623 0.5101 0.3213 0.0296  0.0167  -0.0366 3   ARG A CA  
1903 C C   . ARG B 16  ? 0.2681 0.3955 0.2318 0.0257  0.0164  -0.0334 3   ARG A C   
1904 O O   . ARG B 16  ? 0.2890 0.4216 0.2626 0.0183  0.0166  -0.0251 3   ARG A O   
1905 C CB  . ARG B 16  ? 0.3322 0.5046 0.2902 0.0385  0.0187  -0.0370 3   ARG A CB  
1906 C CG  . ARG B 16  ? 0.3723 0.5721 0.3307 0.0375  0.0196  -0.0350 3   ARG A CG  
1907 N N   . HIS B 17  ? 0.2611 0.3647 0.2161 0.0315  0.0160  -0.0399 4   HIS A N   
1908 C CA  . HIS B 17  ? 0.2726 0.3574 0.2304 0.0296  0.0160  -0.0371 4   HIS A CA  
1909 C C   . HIS B 17  ? 0.2783 0.3742 0.2410 0.0354  0.0173  -0.0332 4   HIS A C   
1910 O O   . HIS B 17  ? 0.2942 0.3756 0.2557 0.0382  0.0174  -0.0327 4   HIS A O   
1911 C CB  . HIS B 17  ? 0.2576 0.3352 0.2235 0.0174  0.0148  -0.0318 4   HIS A CB  
1912 C CG  . HIS B 17  ? 0.2850 0.3524 0.2446 0.0125  0.0134  -0.0371 4   HIS A CG  
1913 N ND1 . HIS B 17  ? 0.2994 0.3413 0.2490 0.0123  0.0132  -0.0434 4   HIS A ND1 
1914 C CD2 . HIS B 17  ? 0.2828 0.3631 0.2427 0.0080  0.0123  -0.0383 4   HIS A CD2 
1915 C CE1 . HIS B 17  ? 0.3068 0.3465 0.2516 0.0060  0.0118  -0.0488 4   HIS A CE1 
1916 N NE2 . HIS B 17  ? 0.3068 0.3708 0.2582 0.0038  0.0110  -0.0459 4   HIS A NE2 
1917 N N   . THR B 18  ? 0.2421 0.3658 0.2108 0.0358  0.0183  -0.0298 5   THR A N   
1918 C CA  . THR B 18  ? 0.2504 0.3909 0.2246 0.0394  0.0194  -0.0268 5   THR A CA  
1919 C C   . THR B 18  ? 0.2414 0.4141 0.2164 0.0429  0.0209  -0.0269 5   THR A C   
1920 O O   . THR B 18  ? 0.2650 0.4455 0.2395 0.0387  0.0210  -0.0264 5   THR A O   
1921 C CB  . THR B 18  ? 0.2403 0.3811 0.2258 0.0276  0.0192  -0.0193 5   THR A CB  
1922 O OG1 . THR B 18  ? 0.2469 0.4037 0.2362 0.0311  0.0201  -0.0183 5   THR A OG1 
1923 C CG2 . THR B 18  ? 0.2155 0.3656 0.2076 0.0157  0.0194  -0.0130 5   THR A CG2 
1924 N N   . ASP B 19  ? 0.2448 0.4392 0.2221 0.0491  0.0221  -0.0266 6   ASP A N   
1925 C CA  . ASP B 19  ? 0.2532 0.4835 0.2346 0.0480  0.0238  -0.0246 6   ASP A CA  
1926 C C   . ASP B 19  ? 0.2325 0.4783 0.2260 0.0322  0.0247  -0.0164 6   ASP A C   
1927 O O   . ASP B 19  ? 0.2361 0.5118 0.2332 0.0275  0.0266  -0.0133 6   ASP A O   
1928 C CB  . ASP B 19  ? 0.3254 0.5757 0.3006 0.0649  0.0247  -0.0301 6   ASP A CB  
1929 C CG  . ASP B 19  ? 0.3560 0.6054 0.3328 0.0708  0.0244  -0.0302 6   ASP A CG  
1930 O OD1 . ASP B 19  ? 0.3333 0.5626 0.3153 0.0619  0.0233  -0.0268 6   ASP A OD1 
1931 O OD2 . ASP B 19  ? 0.4385 0.7089 0.4107 0.0855  0.0252  -0.0338 6   ASP A OD2 
1932 N N   . THR B 20  ? 0.2345 0.4596 0.2328 0.0238  0.0236  -0.0130 7   THR A N   
1933 C CA  . THR B 20  ? 0.2299 0.4632 0.2369 0.0086  0.0244  -0.0061 7   THR A CA  
1934 C C   . THR B 20  ? 0.2494 0.4821 0.2567 -0.0018 0.0254  -0.0002 7   THR A C   
1935 O O   . THR B 20  ? 0.2220 0.4393 0.2247 0.0014  0.0244  -0.0013 7   THR A O   
1936 C CB  . THR B 20  ? 0.2198 0.4275 0.2294 0.0045  0.0229  -0.0049 7   THR A CB  
1937 O OG1 . THR B 20  ? 0.2166 0.4295 0.2250 0.0151  0.0223  -0.0096 7   THR A OG1 
1938 C CG2 . THR B 20  ? 0.1780 0.3851 0.1939 -0.0112 0.0235  0.0015  7   THR A CG2 
1939 N N   . HIS B 21  ? 0.2275 0.4774 0.2393 -0.0143 0.0275  0.0061  8   HIS A N   
1940 C CA  . HIS B 21  ? 0.2255 0.4771 0.2359 -0.0239 0.0293  0.0133  8   HIS A CA  
1941 C C   . HIS B 21  ? 0.2125 0.4480 0.2254 -0.0384 0.0299  0.0202  8   HIS A C   
1942 O O   . HIS B 21  ? 0.2142 0.4602 0.2311 -0.0469 0.0309  0.0209  8   HIS A O   
1943 C CB  . HIS B 21  ? 0.2332 0.5198 0.2433 -0.0257 0.0321  0.0152  8   HIS A CB  
1944 C CG  . HIS B 21  ? 0.3291 0.6126 0.3364 -0.0361 0.0341  0.0242  8   HIS A CG  
1945 N ND1 . HIS B 21  ? 0.4535 0.7520 0.4614 -0.0505 0.0375  0.0324  8   HIS A ND1 
1946 C CD2 . HIS B 21  ? 0.4096 0.6736 0.4122 -0.0338 0.0331  0.0268  8   HIS A CD2 
1947 C CE1 . HIS B 21  ? 0.4055 0.6925 0.4080 -0.0551 0.0388  0.0403  8   HIS A CE1 
1948 N NE2 . HIS B 21  ? 0.4617 0.7301 0.4614 -0.0444 0.0360  0.0367  8   HIS A NE2 
1949 N N   . TYR B 22  ? 0.2257 0.4352 0.2355 -0.0402 0.0290  0.0242  9   TYR A N   
1950 C CA  . TYR B 22  ? 0.2149 0.4048 0.2240 -0.0516 0.0298  0.0308  9   TYR A CA  
1951 C C   . TYR B 22  ? 0.2411 0.4313 0.2445 -0.0593 0.0324  0.0401  9   TYR A C   
1952 O O   . TYR B 22  ? 0.2531 0.4302 0.2519 -0.0552 0.0319  0.0436  9   TYR A O   
1953 C CB  . TYR B 22  ? 0.2324 0.3924 0.2404 -0.0473 0.0272  0.0301  9   TYR A CB  
1954 C CG  . TYR B 22  ? 0.2355 0.3899 0.2474 -0.0402 0.0248  0.0224  9   TYR A CG  
1955 C CD1 . TYR B 22  ? 0.2106 0.3666 0.2221 -0.0286 0.0231  0.0160  9   TYR A CD1 
1956 C CD2 . TYR B 22  ? 0.2064 0.3501 0.2207 -0.0452 0.0243  0.0220  9   TYR A CD2 
1957 C CE1 . TYR B 22  ? 0.2159 0.3619 0.2288 -0.0224 0.0213  0.0107  9   TYR A CE1 
1958 C CE2 . TYR B 22  ? 0.2276 0.3657 0.2447 -0.0384 0.0222  0.0162  9   TYR A CE2 
1959 C CZ  . TYR B 22  ? 0.2309 0.3701 0.2471 -0.0269 0.0210  0.0111  9   TYR A CZ  
1960 O OH  . TYR B 22  ? 0.2382 0.3700 0.2554 -0.0203 0.0195  0.0064  9   TYR A OH  
1961 N N   . PRO B 23  ? 0.2231 0.4281 0.2258 -0.0715 0.0357  0.0453  10  PRO A N   
1962 C CA  . PRO B 23  ? 0.2497 0.4503 0.2449 -0.0798 0.0389  0.0558  10  PRO A CA  
1963 C C   . PRO B 23  ? 0.2310 0.3951 0.2189 -0.0805 0.0384  0.0620  10  PRO A C   
1964 O O   . PRO B 23  ? 0.2661 0.4230 0.2461 -0.0794 0.0399  0.0700  10  PRO A O   
1965 C CB  . PRO B 23  ? 0.2666 0.4832 0.2619 -0.0970 0.0426  0.0601  10  PRO A CB  
1966 C CG  . PRO B 23  ? 0.2424 0.4867 0.2471 -0.0927 0.0411  0.0504  10  PRO A CG  
1967 C CD  . PRO B 23  ? 0.2050 0.4337 0.2134 -0.0784 0.0368  0.0417  10  PRO A CD  
1968 N N   . SER B 24  ? 0.2653 0.4076 0.2547 -0.0816 0.0365  0.0588  11  SER A N   
1969 C CA  . SER B 24  ? 0.2733 0.3820 0.2543 -0.0809 0.0364  0.0647  11  SER A CA  
1970 C C   . SER B 24  ? 0.2582 0.3610 0.2379 -0.0662 0.0338  0.0643  11  SER A C   
1971 O O   . SER B 24  ? 0.3096 0.3898 0.2817 -0.0630 0.0337  0.0699  11  SER A O   
1972 C CB  . SER B 24  ? 0.2756 0.3631 0.2576 -0.0847 0.0350  0.0608  11  SER A CB  
1973 O OG  . SER B 24  ? 0.2709 0.3637 0.2617 -0.0744 0.0313  0.0514  11  SER A OG  
1974 N N   . LEU B 25  ? 0.2544 0.3768 0.2404 -0.0571 0.0317  0.0573  12  LEU A N   
1975 C CA  . LEU B 25  ? 0.2345 0.3555 0.2195 -0.0459 0.0293  0.0558  12  LEU A CA  
1976 C C   . LEU B 25  ? 0.2580 0.3920 0.2370 -0.0436 0.0307  0.0618  12  LEU A C   
1977 O O   . LEU B 25  ? 0.2666 0.3995 0.2429 -0.0355 0.0290  0.0623  12  LEU A O   
1978 C CB  . LEU B 25  ? 0.2440 0.3727 0.2361 -0.0381 0.0261  0.0448  12  LEU A CB  
1979 C CG  . LEU B 25  ? 0.2155 0.3289 0.2121 -0.0379 0.0244  0.0400  12  LEU A CG  
1980 C CD1 . LEU B 25  ? 0.1880 0.3080 0.1892 -0.0305 0.0220  0.0302  12  LEU A CD1 
1981 C CD2 . LEU B 25  ? 0.2166 0.3075 0.2095 -0.0358 0.0234  0.0442  12  LEU A CD2 
1982 N N   . ALA B 26  ? 0.2531 0.4026 0.2304 -0.0507 0.0339  0.0661  13  ALA A N   
1983 C CA  . ALA B 26  ? 0.2572 0.4239 0.2291 -0.0480 0.0355  0.0712  13  ALA A CA  
1984 C C   . ALA B 26  ? 0.3003 0.4488 0.2621 -0.0452 0.0362  0.0815  13  ALA A C   
1985 O O   . ALA B 26  ? 0.3188 0.4439 0.2746 -0.0513 0.0381  0.0886  13  ALA A O   
1986 C CB  . ALA B 26  ? 0.2774 0.4642 0.2484 -0.0580 0.0396  0.0758  13  ALA A CB  
1987 N N   . ASP B 27  ? 0.3029 0.4619 0.2614 -0.0357 0.0348  0.0822  14  ASP A N   
1988 C CA  . ASP B 27  ? 0.3599 0.5064 0.3077 -0.0309 0.0356  0.0927  14  ASP A CA  
1989 C C   . ASP B 27  ? 0.3379 0.4608 0.2847 -0.0248 0.0331  0.0921  14  ASP A C   
1990 O O   . ASP B 27  ? 0.3579 0.4745 0.2959 -0.0171 0.0331  0.0995  14  ASP A O   
1991 C CB  . ASP B 27  ? 0.3782 0.5170 0.3153 -0.0394 0.0408  0.1061  14  ASP A CB  
1992 C CG  . ASP B 27  ? 0.4993 0.6674 0.4367 -0.0442 0.0435  0.1078  14  ASP A CG  
1993 O OD1 . ASP B 27  ? 0.4499 0.6432 0.3910 -0.0364 0.0414  0.1016  14  ASP A OD1 
1994 O OD2 . ASP B 27  ? 0.6179 0.7834 0.5499 -0.0556 0.0480  0.1163  14  ASP A OD2 
1995 N N   . LYS B 28  ? 0.3064 0.4179 0.2611 -0.0270 0.0311  0.0841  15  LYS A N   
1996 C CA  . LYS B 28  ? 0.3098 0.4013 0.2633 -0.0209 0.0290  0.0837  15  LYS A CA  
1997 C C   . LYS B 28  ? 0.2819 0.3881 0.2377 -0.0102 0.0255  0.0794  15  LYS A C   
1998 O O   . LYS B 28  ? 0.2625 0.3897 0.2248 -0.0095 0.0236  0.0711  15  LYS A O   
1999 C CB  . LYS B 28  ? 0.2895 0.3711 0.2517 -0.0254 0.0276  0.0752  15  LYS A CB  
2000 C CG  . LYS B 28  ? 0.3581 0.4245 0.3179 -0.0367 0.0305  0.0784  15  LYS A CG  
2001 C CD  . LYS B 28  ? 0.5030 0.5379 0.4517 -0.0373 0.0321  0.0859  15  LYS A CD  
2002 C CE  . LYS B 28  ? 0.5200 0.5399 0.4689 -0.0500 0.0338  0.0843  15  LYS A CE  
2003 N NZ  . LYS B 28  ? 0.5530 0.5689 0.4915 -0.0589 0.0381  0.0943  15  LYS A NZ  
2004 N N   . VAL B 29  ? 0.2777 0.3728 0.2275 -0.0020 0.0246  0.0841  16  VAL A N   
2005 C CA  . VAL B 29  ? 0.2649 0.3781 0.2168 0.0073  0.0214  0.0805  16  VAL A CA  
2006 C C   . VAL B 29  ? 0.2487 0.3579 0.2096 0.0074  0.0184  0.0713  16  VAL A C   
2007 O O   . VAL B 29  ? 0.2604 0.3491 0.2196 0.0086  0.0188  0.0733  16  VAL A O   
2008 C CB  . VAL B 29  ? 0.2817 0.3885 0.2211 0.0181  0.0222  0.0917  16  VAL A CB  
2009 C CG1 . VAL B 29  ? 0.2647 0.3931 0.2063 0.0284  0.0185  0.0880  16  VAL A CG1 
2010 C CG2 . VAL B 29  ? 0.3143 0.4237 0.2426 0.0184  0.0255  0.1026  16  VAL A CG2 
2011 N N   . VAL B 30  ? 0.2163 0.3433 0.1857 0.0055  0.0158  0.0608  17  VAL A N   
2012 C CA  . VAL B 30  ? 0.2043 0.3265 0.1817 0.0034  0.0137  0.0522  17  VAL A CA  
2013 C C   . VAL B 30  ? 0.2270 0.3680 0.2062 0.0076  0.0107  0.0479  17  VAL A C   
2014 O O   . VAL B 30  ? 0.2641 0.4240 0.2418 0.0080  0.0099  0.0459  17  VAL A O   
2015 C CB  . VAL B 30  ? 0.2207 0.3457 0.2043 -0.0038 0.0136  0.0432  17  VAL A CB  
2016 C CG1 . VAL B 30  ? 0.2122 0.3323 0.2024 -0.0058 0.0117  0.0346  17  VAL A CG1 
2017 C CG2 . VAL B 30  ? 0.2437 0.3568 0.2271 -0.0090 0.0164  0.0463  17  VAL A CG2 
2018 N N   . LEU B 31  ? 0.2282 0.3668 0.2101 0.0105  0.0092  0.0465  18  LEU A N   
2019 C CA  . LEU B 31  ? 0.2311 0.3910 0.2151 0.0133  0.0065  0.0428  18  LEU A CA  
2020 C C   . LEU B 31  ? 0.2011 0.3578 0.1928 0.0067  0.0051  0.0340  18  LEU A C   
2021 O O   . LEU B 31  ? 0.2246 0.3646 0.2181 0.0074  0.0060  0.0355  18  LEU A O   
2022 C CB  . LEU B 31  ? 0.2091 0.3719 0.1874 0.0248  0.0064  0.0513  18  LEU A CB  
2023 C CG  . LEU B 31  ? 0.2526 0.4423 0.2342 0.0278  0.0035  0.0473  18  LEU A CG  
2024 C CD1 . LEU B 31  ? 0.2512 0.4685 0.2334 0.0244  0.0016  0.0421  18  LEU A CD1 
2025 C CD2 . LEU B 31  ? 0.2397 0.4312 0.2139 0.0427  0.0038  0.0568  18  LEU A CD2 
2026 N N   . ILE B 32  ? 0.1999 0.3703 0.1948 -0.0002 0.0034  0.0248  19  ILE A N   
2027 C CA  . ILE B 32  ? 0.1784 0.3417 0.1784 -0.0081 0.0028  0.0168  19  ILE A CA  
2028 C C   . ILE B 32  ? 0.2045 0.3910 0.2063 -0.0118 0.0004  0.0117  19  ILE A C   
2029 O O   . ILE B 32  ? 0.2187 0.4239 0.2182 -0.0136 -0.0011 0.0080  19  ILE A O   
2030 C CB  . ILE B 32  ? 0.1897 0.3423 0.1888 -0.0145 0.0035  0.0097  19  ILE A CB  
2031 C CG1 . ILE B 32  ? 0.1662 0.3029 0.1643 -0.0114 0.0058  0.0148  19  ILE A CG1 
2032 C CG2 . ILE B 32  ? 0.1567 0.3007 0.1579 -0.0226 0.0030  0.0012  19  ILE A CG2 
2033 C CD1 . ILE B 32  ? 0.2145 0.3511 0.2100 -0.0138 0.0065  0.0095  19  ILE A CD1 
2034 N N   . SER B 33  ? 0.1947 0.3825 0.2003 -0.0129 0.0001  0.0116  20  SER A N   
2035 C CA  . SER B 33  ? 0.1915 0.4031 0.1997 -0.0197 -0.0019 0.0058  20  SER A CA  
2036 C C   . SER B 33  ? 0.2059 0.4058 0.2144 -0.0335 -0.0018 -0.0040 20  SER A C   
2037 O O   . SER B 33  ? 0.2271 0.4010 0.2350 -0.0350 -0.0001 -0.0046 20  SER A O   
2038 C CB  . SER B 33  ? 0.2072 0.4311 0.2188 -0.0142 -0.0022 0.0105  20  SER A CB  
2039 O OG  . SER B 33  ? 0.1908 0.3925 0.2050 -0.0165 -0.0005 0.0108  20  SER A OG  
2040 N N   . GLY B 34  ? 0.2138 0.4324 0.2218 -0.0435 -0.0036 -0.0116 21  GLY A N   
2041 C CA  . GLY B 34  ? 0.2048 0.4084 0.2093 -0.0571 -0.0033 -0.0213 21  GLY A CA  
2042 C C   . GLY B 34  ? 0.2424 0.4238 0.2410 -0.0551 -0.0024 -0.0246 21  GLY A C   
2043 O O   . GLY B 34  ? 0.2490 0.4057 0.2437 -0.0604 -0.0010 -0.0293 21  GLY A O   
2044 N N   . GLY B 35  ? 0.2338 0.4271 0.2304 -0.0480 -0.0032 -0.0231 22  GLY A N   
2045 C CA  . GLY B 35  ? 0.2290 0.4059 0.2207 -0.0442 -0.0020 -0.0248 22  GLY A CA  
2046 C C   . GLY B 35  ? 0.2418 0.4171 0.2257 -0.0508 -0.0030 -0.0362 22  GLY A C   
2047 O O   . GLY B 35  ? 0.2550 0.4180 0.2344 -0.0463 -0.0019 -0.0379 22  GLY A O   
2048 N N   . ALA B 36  ? 0.2337 0.4203 0.2152 -0.0620 -0.0049 -0.0447 23  ALA A N   
2049 C CA  . ALA B 36  ? 0.2383 0.4238 0.2105 -0.0673 -0.0061 -0.0562 23  ALA A CA  
2050 C C   . ALA B 36  ? 0.2883 0.4397 0.2509 -0.0748 -0.0047 -0.0655 23  ALA A C   
2051 O O   . ALA B 36  ? 0.3092 0.4509 0.2615 -0.0758 -0.0051 -0.0750 23  ALA A O   
2052 C CB  . ALA B 36  ? 0.2925 0.5096 0.2646 -0.0756 -0.0091 -0.0621 23  ALA A CB  
2053 N N   . SER B 37  ? 0.3138 0.4456 0.2782 -0.0792 -0.0030 -0.0628 24  SER A N   
2054 C CA  . SER B 37  ? 0.3327 0.4294 0.2864 -0.0855 -0.0013 -0.0698 24  SER A CA  
2055 C C   . SER B 37  ? 0.3034 0.3785 0.2606 -0.0796 0.0014  -0.0615 24  SER A C   
2056 O O   . SER B 37  ? 0.2848 0.3729 0.2531 -0.0726 0.0016  -0.0514 24  SER A O   
2057 C CB  . SER B 37  ? 0.3533 0.4494 0.3019 -0.1040 -0.0020 -0.0779 24  SER A CB  
2058 O OG  . SER B 37  ? 0.3524 0.4652 0.3120 -0.1086 -0.0019 -0.0704 24  SER A OG  
2059 N N   . GLY B 38  ? 0.3499 0.3912 0.2960 -0.0796 0.0034  -0.0657 25  GLY A N   
2060 C CA  . GLY B 38  ? 0.3719 0.3926 0.3194 -0.0761 0.0059  -0.0591 25  GLY A CA  
2061 C C   . GLY B 38  ? 0.3249 0.3536 0.2818 -0.0613 0.0064  -0.0499 25  GLY A C   
2062 O O   . GLY B 38  ? 0.3288 0.3635 0.2849 -0.0519 0.0061  -0.0505 25  GLY A O   
2063 N N   . ILE B 39  ? 0.2968 0.3267 0.2623 -0.0598 0.0073  -0.0416 26  ILE A N   
2064 C CA  . ILE B 39  ? 0.2464 0.2790 0.2188 -0.0482 0.0080  -0.0342 26  ILE A CA  
2065 C C   . ILE B 39  ? 0.2442 0.3029 0.2243 -0.0437 0.0065  -0.0302 26  ILE A C   
2066 O O   . ILE B 39  ? 0.2069 0.2684 0.1883 -0.0352 0.0070  -0.0273 26  ILE A O   
2067 C CB  . ILE B 39  ? 0.2459 0.2738 0.2245 -0.0481 0.0092  -0.0273 26  ILE A CB  
2068 C CG1 . ILE B 39  ? 0.2722 0.2727 0.2414 -0.0503 0.0112  -0.0298 26  ILE A CG1 
2069 C CG2 . ILE B 39  ? 0.2371 0.2697 0.2224 -0.0374 0.0096  -0.0207 26  ILE A CG2 
2070 C CD1 . ILE B 39  ? 0.2960 0.2930 0.2697 -0.0529 0.0124  -0.0240 26  ILE A CD1 
2071 N N   . GLY B 40  ? 0.2221 0.3006 0.2063 -0.0496 0.0048  -0.0297 27  GLY A N   
2072 C CA  . GLY B 40  ? 0.2240 0.3251 0.2137 -0.0437 0.0037  -0.0244 27  GLY A CA  
2073 C C   . GLY B 40  ? 0.2253 0.3315 0.2096 -0.0401 0.0033  -0.0284 27  GLY A C   
2074 O O   . GLY B 40  ? 0.2179 0.3331 0.2047 -0.0329 0.0037  -0.0228 27  GLY A O   
2075 N N   . ARG B 41  ? 0.2236 0.3211 0.1991 -0.0454 0.0029  -0.0385 28  ARG A N   
2076 C CA  . ARG B 41  ? 0.2186 0.3204 0.1876 -0.0413 0.0025  -0.0438 28  ARG A CA  
2077 C C   . ARG B 41  ? 0.2353 0.3267 0.2034 -0.0313 0.0046  -0.0408 28  ARG A C   
2078 O O   . ARG B 41  ? 0.2434 0.3469 0.2114 -0.0249 0.0049  -0.0391 28  ARG A O   
2079 C CB  . ARG B 41  ? 0.2385 0.3313 0.1962 -0.0489 0.0016  -0.0564 28  ARG A CB  
2080 C CG  . ARG B 41  ? 0.2782 0.3693 0.2268 -0.0421 0.0017  -0.0631 28  ARG A CG  
2081 C CD  . ARG B 41  ? 0.3389 0.4173 0.2740 -0.0496 0.0006  -0.0767 28  ARG A CD  
2082 N NE  . ARG B 41  ? 0.3597 0.4372 0.2863 -0.0394 0.0011  -0.0819 28  ARG A NE  
2083 C CZ  . ARG B 41  ? 0.3810 0.4521 0.2943 -0.0424 0.0000  -0.0945 28  ARG A CZ  
2084 N NH1 . ARG B 41  ? 0.4011 0.4674 0.3094 -0.0566 -0.0017 -0.1023 28  ARG A NH1 
2085 N NH2 . ARG B 41  ? 0.4056 0.4753 0.3096 -0.0317 0.0005  -0.1002 28  ARG A NH2 
2086 N N   . ALA B 42  ? 0.2300 0.3004 0.1972 -0.0300 0.0061  -0.0400 29  ALA A N   
2087 C CA  . ALA B 42  ? 0.2358 0.3007 0.2027 -0.0208 0.0079  -0.0375 29  ALA A CA  
2088 C C   . ALA B 42  ? 0.2252 0.3060 0.2025 -0.0176 0.0084  -0.0272 29  ALA A C   
2089 O O   . ALA B 42  ? 0.2328 0.3219 0.2104 -0.0120 0.0094  -0.0251 29  ALA A O   
2090 C CB  . ALA B 42  ? 0.2399 0.2804 0.2028 -0.0194 0.0093  -0.0387 29  ALA A CB  
2091 N N   . PHE B 43  ? 0.2119 0.2974 0.1962 -0.0213 0.0077  -0.0210 30  PHE A N   
2092 C CA  . PHE B 43  ? 0.2062 0.3019 0.1969 -0.0184 0.0084  -0.0118 30  PHE A CA  
2093 C C   . PHE B 43  ? 0.2235 0.3375 0.2125 -0.0165 0.0081  -0.0100 30  PHE A C   
2094 O O   . PHE B 43  ? 0.2156 0.3355 0.2054 -0.0134 0.0097  -0.0052 30  PHE A O   
2095 C CB  . PHE B 43  ? 0.1951 0.2925 0.1911 -0.0205 0.0077  -0.0059 30  PHE A CB  
2096 C CG  . PHE B 43  ? 0.2146 0.2965 0.2130 -0.0220 0.0081  -0.0060 30  PHE A CG  
2097 C CD1 . PHE B 43  ? 0.2179 0.2869 0.2158 -0.0194 0.0095  -0.0067 30  PHE A CD1 
2098 C CD2 . PHE B 43  ? 0.2236 0.3079 0.2250 -0.0252 0.0072  -0.0045 30  PHE A CD2 
2099 C CE1 . PHE B 43  ? 0.2539 0.3105 0.2536 -0.0201 0.0099  -0.0061 30  PHE A CE1 
2100 C CE2 . PHE B 43  ? 0.2151 0.2876 0.2185 -0.0265 0.0078  -0.0039 30  PHE A CE2 
2101 C CZ  . PHE B 43  ? 0.2238 0.2817 0.2262 -0.0236 0.0092  -0.0043 30  PHE A CZ  
2102 N N   . VAL B 44  ? 0.2358 0.3606 0.2219 -0.0192 0.0064  -0.0143 31  VAL A N   
2103 C CA  . VAL B 44  ? 0.2162 0.3609 0.2000 -0.0168 0.0060  -0.0124 31  VAL A CA  
2104 C C   . VAL B 44  ? 0.2384 0.3850 0.2181 -0.0129 0.0074  -0.0153 31  VAL A C   
2105 O O   . VAL B 44  ? 0.2163 0.3740 0.1967 -0.0099 0.0089  -0.0087 31  VAL A O   
2106 C CB  . VAL B 44  ? 0.2159 0.3744 0.1968 -0.0207 0.0035  -0.0185 31  VAL A CB  
2107 C CG1 . VAL B 44  ? 0.1957 0.3768 0.1731 -0.0170 0.0031  -0.0171 31  VAL A CG1 
2108 C CG2 . VAL B 44  ? 0.2163 0.3793 0.2020 -0.0237 0.0022  -0.0149 31  VAL A CG2 
2109 N N   . GLU B 45  ? 0.2132 0.3487 0.1874 -0.0125 0.0073  -0.0250 32  GLU A N   
2110 C CA  . GLU B 45  ? 0.2163 0.3551 0.1854 -0.0066 0.0086  -0.0290 32  GLU A CA  
2111 C C   . GLU B 45  ? 0.2088 0.3496 0.1830 -0.0030 0.0110  -0.0214 32  GLU A C   
2112 O O   . GLU B 45  ? 0.2195 0.3766 0.1928 0.0004  0.0124  -0.0191 32  GLU A O   
2113 C CB  . GLU B 45  ? 0.2300 0.3501 0.1903 -0.0050 0.0082  -0.0402 32  GLU A CB  
2114 C CG  . GLU B 45  ? 0.2363 0.3550 0.1890 -0.0103 0.0060  -0.0499 32  GLU A CG  
2115 C CD  . GLU B 45  ? 0.2763 0.3672 0.2178 -0.0106 0.0061  -0.0605 32  GLU A CD  
2116 O OE1 . GLU B 45  ? 0.2761 0.3480 0.2174 -0.0082 0.0075  -0.0586 32  GLU A OE1 
2117 O OE2 . GLU B 45  ? 0.3040 0.3898 0.2353 -0.0144 0.0047  -0.0709 32  GLU A OE2 
2118 N N   . ALA B 46  ? 0.2065 0.3324 0.1855 -0.0045 0.0115  -0.0182 33  ALA A N   
2119 C CA  . ALA B 46  ? 0.2139 0.3416 0.1971 -0.0024 0.0135  -0.0130 33  ALA A CA  
2120 C C   . ALA B 46  ? 0.1856 0.3267 0.1730 -0.0057 0.0146  -0.0031 33  ALA A C   
2121 O O   . ALA B 46  ? 0.1950 0.3472 0.1835 -0.0052 0.0166  0.0003  33  ALA A O   
2122 C CB  . ALA B 46  ? 0.2116 0.3215 0.1982 -0.0030 0.0135  -0.0124 33  ALA A CB  
2123 N N   . PHE B 47  ? 0.1889 0.3275 0.1781 -0.0091 0.0137  0.0021  34  PHE A N   
2124 C CA  . PHE B 47  ? 0.1956 0.3413 0.1860 -0.0112 0.0154  0.0125  34  PHE A CA  
2125 C C   . PHE B 47  ? 0.2317 0.3970 0.2177 -0.0097 0.0162  0.0141  34  PHE A C   
2126 O O   . PHE B 47  ? 0.2357 0.4089 0.2212 -0.0118 0.0187  0.0218  34  PHE A O   
2127 C CB  . PHE B 47  ? 0.1997 0.3373 0.1909 -0.0123 0.0144  0.0184  34  PHE A CB  
2128 C CG  . PHE B 47  ? 0.2039 0.3239 0.1993 -0.0140 0.0144  0.0197  34  PHE A CG  
2129 C CD1 . PHE B 47  ? 0.2600 0.3726 0.2561 -0.0166 0.0162  0.0267  34  PHE A CD1 
2130 C CD2 . PHE B 47  ? 0.2018 0.3127 0.1993 -0.0138 0.0126  0.0138  34  PHE A CD2 
2131 C CE1 . PHE B 47  ? 0.2196 0.3171 0.2186 -0.0179 0.0160  0.0270  34  PHE A CE1 
2132 C CE2 . PHE B 47  ? 0.2419 0.3387 0.2428 -0.0146 0.0127  0.0151  34  PHE A CE2 
2133 C CZ  . PHE B 47  ? 0.2095 0.3002 0.2112 -0.0161 0.0142  0.0214  34  PHE A CZ  
2134 N N   . VAL B 48  ? 0.2183 0.3917 0.2006 -0.0069 0.0144  0.0070  35  VAL A N   
2135 C CA  . VAL B 48  ? 0.2556 0.4497 0.2332 -0.0047 0.0152  0.0080  35  VAL A CA  
2136 C C   . VAL B 48  ? 0.2332 0.4366 0.2105 -0.0030 0.0176  0.0068  35  VAL A C   
2137 O O   . VAL B 48  ? 0.2530 0.4724 0.2290 -0.0038 0.0199  0.0135  35  VAL A O   
2138 C CB  . VAL B 48  ? 0.2389 0.4419 0.2117 -0.0025 0.0126  -0.0009 35  VAL A CB  
2139 C CG1 . VAL B 48  ? 0.2437 0.4695 0.2108 0.0012  0.0134  -0.0019 35  VAL A CG1 
2140 C CG2 . VAL B 48  ? 0.2302 0.4348 0.2034 -0.0041 0.0104  0.0019  35  VAL A CG2 
2141 N N   . ALA B 49  ? 0.2383 0.4334 0.2159 -0.0001 0.0171  -0.0016 36  ALA A N   
2142 C CA  . ALA B 49  ? 0.2241 0.4310 0.2014 0.0034  0.0192  -0.0034 36  ALA A CA  
2143 C C   . ALA B 49  ? 0.2412 0.4546 0.2241 -0.0026 0.0220  0.0069  36  ALA A C   
2144 O O   . ALA B 49  ? 0.2731 0.5056 0.2562 -0.0022 0.0243  0.0083  36  ALA A O   
2145 C CB  . ALA B 49  ? 0.2338 0.4255 0.2092 0.0089  0.0182  -0.0130 36  ALA A CB  
2146 N N   . GLN B 50  ? 0.2224 0.4198 0.2094 -0.0088 0.0220  0.0134  37  GLN A N   
2147 C CA  . GLN B 50  ? 0.2160 0.4148 0.2064 -0.0165 0.0245  0.0221  37  GLN A CA  
2148 C C   . GLN B 50  ? 0.2449 0.4507 0.2316 -0.0215 0.0267  0.0327  37  GLN A C   
2149 O O   . GLN B 50  ? 0.2451 0.4488 0.2319 -0.0297 0.0293  0.0412  37  GLN A O   
2150 C CB  . GLN B 50  ? 0.1986 0.3744 0.1929 -0.0202 0.0235  0.0239  37  GLN A CB  
2151 C CG  . GLN B 50  ? 0.1733 0.3406 0.1706 -0.0159 0.0219  0.0155  37  GLN A CG  
2152 C CD  . GLN B 50  ? 0.2003 0.3819 0.2003 -0.0159 0.0235  0.0136  37  GLN A CD  
2153 O OE1 . GLN B 50  ? 0.1999 0.3928 0.2017 -0.0237 0.0258  0.0197  37  GLN A OE1 
2154 N NE2 . GLN B 50  ? 0.1932 0.3755 0.1922 -0.0072 0.0224  0.0052  37  GLN A NE2 
2155 N N   . GLY B 51  ? 0.2490 0.4625 0.2311 -0.0169 0.0257  0.0323  38  GLY A N   
2156 C CA  . GLY B 51  ? 0.2231 0.4439 0.2000 -0.0199 0.0279  0.0432  38  GLY A CA  
2157 C C   . GLY B 51  ? 0.2343 0.4349 0.2084 -0.0207 0.0273  0.0510  38  GLY A C   
2158 O O   . GLY B 51  ? 0.2611 0.4622 0.2288 -0.0225 0.0296  0.0619  38  GLY A O   
2159 N N   . SER B 52  ? 0.2009 0.3843 0.1784 -0.0184 0.0244  0.0461  39  SER A N   
2160 C CA  . SER B 52  ? 0.2103 0.3787 0.1847 -0.0162 0.0234  0.0520  39  SER A CA  
2161 C C   . SER B 52  ? 0.2299 0.4128 0.1997 -0.0097 0.0217  0.0526  39  SER A C   
2162 O O   . SER B 52  ? 0.2420 0.4421 0.2125 -0.0071 0.0201  0.0441  39  SER A O   
2163 C CB  . SER B 52  ? 0.1879 0.3404 0.1679 -0.0153 0.0207  0.0454  39  SER A CB  
2164 O OG  . SER B 52  ? 0.1999 0.3420 0.1839 -0.0204 0.0220  0.0443  39  SER A OG  
2165 N N   . ARG B 53  ? 0.2259 0.4012 0.1906 -0.0060 0.0216  0.0609  40  ARG A N   
2166 C CA  . ARG B 53  ? 0.2453 0.4353 0.2063 0.0011  0.0194  0.0610  40  ARG A CA  
2167 C C   . ARG B 53  ? 0.2251 0.4093 0.1911 0.0035  0.0160  0.0544  40  ARG A C   
2168 O O   . ARG B 53  ? 0.2458 0.4125 0.2115 0.0048  0.0162  0.0590  40  ARG A O   
2169 C CB  . ARG B 53  ? 0.2497 0.4361 0.2004 0.0053  0.0219  0.0755  40  ARG A CB  
2170 C CG  . ARG B 53  ? 0.2919 0.4913 0.2370 0.0026  0.0253  0.0817  40  ARG A CG  
2171 C CD  . ARG B 53  ? 0.3393 0.5323 0.2718 0.0062  0.0286  0.0974  40  ARG A CD  
2172 N NE  . ARG B 53  ? 0.3938 0.5545 0.3225 0.0037  0.0304  0.1044  40  ARG A NE  
2173 C CZ  . ARG B 53  ? 0.4636 0.6045 0.3789 0.0077  0.0332  0.1180  40  ARG A CZ  
2174 N NH1 . ARG B 53  ? 0.4366 0.5890 0.3419 0.0179  0.0335  0.1261  40  ARG A NH1 
2175 N NH2 . ARG B 53  ? 0.4171 0.5257 0.3277 0.0022  0.0355  0.1229  40  ARG A NH2 
2176 N N   . VAL B 54  ? 0.2154 0.4125 0.1853 0.0029  0.0131  0.0429  41  VAL A N   
2177 C CA  . VAL B 54  ? 0.2087 0.3991 0.1843 0.0014  0.0103  0.0350  41  VAL A CA  
2178 C C   . VAL B 54  ? 0.2397 0.4497 0.2141 0.0048  0.0073  0.0322  41  VAL A C   
2179 O O   . VAL B 54  ? 0.2244 0.4527 0.1973 0.0037  0.0057  0.0250  41  VAL A O   
2180 C CB  . VAL B 54  ? 0.2377 0.4231 0.2176 -0.0039 0.0097  0.0231  41  VAL A CB  
2181 C CG1 . VAL B 54  ? 0.2295 0.4052 0.2139 -0.0069 0.0075  0.0159  41  VAL A CG1 
2182 C CG2 . VAL B 54  ? 0.2106 0.3835 0.1920 -0.0063 0.0124  0.0253  41  VAL A CG2 
2183 N N   . ALA B 55  ? 0.2215 0.4291 0.1964 0.0089  0.0065  0.0370  42  ALA A N   
2184 C CA  . ALA B 55  ? 0.2212 0.4512 0.1964 0.0114  0.0035  0.0335  42  ALA A CA  
2185 C C   . ALA B 55  ? 0.2051 0.4298 0.1874 0.0044  0.0016  0.0241  42  ALA A C   
2186 O O   . ALA B 55  ? 0.2311 0.4339 0.2167 0.0029  0.0029  0.0256  42  ALA A O   
2187 C CB  . ALA B 55  ? 0.2033 0.4344 0.1734 0.0220  0.0042  0.0457  42  ALA A CB  
2188 N N   . PHE B 56  ? 0.2103 0.4534 0.1943 -0.0009 -0.0012 0.0144  43  PHE A N   
2189 C CA  . PHE B 56  ? 0.2086 0.4451 0.1980 -0.0086 -0.0023 0.0071  43  PHE A CA  
2190 C C   . PHE B 56  ? 0.2080 0.4734 0.1988 -0.0111 -0.0052 0.0026  43  PHE A C   
2191 O O   . PHE B 56  ? 0.2253 0.5158 0.2129 -0.0101 -0.0071 0.0002  43  PHE A O   
2192 C CB  . PHE B 56  ? 0.2099 0.4281 0.1993 -0.0174 -0.0017 -0.0026 43  PHE A CB  
2193 C CG  . PHE B 56  ? 0.2071 0.4379 0.1916 -0.0218 -0.0032 -0.0123 43  PHE A CG  
2194 C CD1 . PHE B 56  ? 0.2102 0.4459 0.1903 -0.0166 -0.0022 -0.0101 43  PHE A CD1 
2195 C CD2 . PHE B 56  ? 0.2389 0.4746 0.2224 -0.0320 -0.0053 -0.0240 43  PHE A CD2 
2196 C CE1 . PHE B 56  ? 0.2227 0.4709 0.1974 -0.0194 -0.0037 -0.0196 43  PHE A CE1 
2197 C CE2 . PHE B 56  ? 0.2409 0.4864 0.2180 -0.0360 -0.0068 -0.0340 43  PHE A CE2 
2198 C CZ  . PHE B 56  ? 0.2182 0.4704 0.1911 -0.0289 -0.0061 -0.0321 43  PHE A CZ  
2199 N N   . LEU B 57  ? 0.2045 0.4690 0.2002 -0.0149 -0.0057 0.0013  44  LEU A N   
2200 C CA  . LEU B 57  ? 0.2372 0.5328 0.2355 -0.0188 -0.0084 -0.0030 44  LEU A CA  
2201 C C   . LEU B 57  ? 0.2506 0.5403 0.2511 -0.0353 -0.0091 -0.0147 44  LEU A C   
2202 O O   . LEU B 57  ? 0.2633 0.5244 0.2648 -0.0393 -0.0072 -0.0156 44  LEU A O   
2203 C CB  . LEU B 57  ? 0.2331 0.5361 0.2345 -0.0096 -0.0081 0.0055  44  LEU A CB  
2204 C CG  . LEU B 57  ? 0.2411 0.5314 0.2379 0.0064  -0.0062 0.0183  44  LEU A CG  
2205 C CD1 . LEU B 57  ? 0.2296 0.5278 0.2283 0.0148  -0.0062 0.0237  44  LEU A CD1 
2206 C CD2 . LEU B 57  ? 0.2433 0.5512 0.2336 0.0153  -0.0067 0.0231  44  LEU A CD2 
2207 N N   . ASP B 58  ? 0.2266 0.5433 0.2268 -0.0449 -0.0116 -0.0234 45  ASP A N   
2208 C CA  . ASP B 58  ? 0.2569 0.5672 0.2576 -0.0624 -0.0120 -0.0339 45  ASP A CA  
2209 C C   . ASP B 58  ? 0.2721 0.6233 0.2745 -0.0713 -0.0149 -0.0403 45  ASP A C   
2210 O O   . ASP B 58  ? 0.2355 0.6166 0.2370 -0.0640 -0.0170 -0.0389 45  ASP A O   
2211 C CB  . ASP B 58  ? 0.2974 0.5801 0.2909 -0.0709 -0.0113 -0.0434 45  ASP A CB  
2212 C CG  . ASP B 58  ? 0.3296 0.5846 0.3210 -0.0849 -0.0098 -0.0500 45  ASP A CG  
2213 O OD1 . ASP B 58  ? 0.3433 0.6068 0.3321 -0.1007 -0.0110 -0.0595 45  ASP A OD1 
2214 O OD2 . ASP B 58  ? 0.2418 0.4651 0.2325 -0.0804 -0.0073 -0.0461 45  ASP A OD2 
2215 N N   . LEU B 59  ? 0.2619 0.6152 0.2664 -0.0873 -0.0150 -0.0466 46  LEU A N   
2216 C CA  . LEU B 59  ? 0.2862 0.6783 0.2921 -0.1003 -0.0177 -0.0547 46  LEU A CA  
2217 C C   . LEU B 59  ? 0.2881 0.6774 0.2857 -0.1119 -0.0194 -0.0675 46  LEU A C   
2218 O O   . LEU B 59  ? 0.3298 0.7569 0.3273 -0.1161 -0.0224 -0.0731 46  LEU A O   
2219 C CB  . LEU B 59  ? 0.2949 0.6792 0.3040 -0.1154 -0.0161 -0.0568 46  LEU A CB  
2220 C CG  . LEU B 59  ? 0.4046 0.8252 0.4155 -0.1354 -0.0180 -0.0659 46  LEU A CG  
2221 C CD1 . LEU B 59  ? 0.4126 0.8870 0.4312 -0.1230 -0.0204 -0.0597 46  LEU A CD1 
2222 C CD2 . LEU B 59  ? 0.4495 0.8538 0.4611 -0.1530 -0.0155 -0.0680 46  LEU A CD2 
2223 N N   . ASP B 60  ? 0.2996 0.6460 0.2894 -0.1164 -0.0176 -0.0728 47  ASP A N   
2224 C CA  . ASP B 60  ? 0.3214 0.6609 0.3010 -0.1279 -0.0191 -0.0867 47  ASP A CA  
2225 C C   . ASP B 60  ? 0.3381 0.6911 0.3148 -0.1135 -0.0206 -0.0856 47  ASP A C   
2226 O O   . ASP B 60  ? 0.3111 0.6367 0.2848 -0.1020 -0.0186 -0.0812 47  ASP A O   
2227 C CB  . ASP B 60  ? 0.3229 0.6112 0.2932 -0.1357 -0.0164 -0.0925 47  ASP A CB  
2228 C CG  . ASP B 60  ? 0.3604 0.6359 0.3172 -0.1500 -0.0176 -0.1088 47  ASP A CG  
2229 O OD1 . ASP B 60  ? 0.3569 0.6588 0.3113 -0.1495 -0.0205 -0.1150 47  ASP A OD1 
2230 O OD2 . ASP B 60  ? 0.4128 0.6500 0.3598 -0.1614 -0.0157 -0.1155 47  ASP A OD2 
2231 N N   . ALA B 61  ? 0.3126 0.7098 0.2902 -0.1139 -0.0240 -0.0890 48  ALA A N   
2232 C CA  . ALA B 61  ? 0.3214 0.7368 0.2968 -0.0982 -0.0252 -0.0853 48  ALA A CA  
2233 C C   . ALA B 61  ? 0.3476 0.7383 0.3119 -0.1010 -0.0250 -0.0957 48  ALA A C   
2234 O O   . ALA B 61  ? 0.3532 0.7387 0.3150 -0.0866 -0.0240 -0.0901 48  ALA A O   
2235 C CB  . ALA B 61  ? 0.2883 0.7589 0.2659 -0.0984 -0.0290 -0.0876 48  ALA A CB  
2236 N N   . GLU B 62  ? 0.3674 0.7450 0.3238 -0.1199 -0.0260 -0.1114 49  GLU A N   
2237 C CA  . GLU B 62  ? 0.3649 0.7190 0.3083 -0.1226 -0.0261 -0.1235 49  GLU A CA  
2238 C C   . GLU B 62  ? 0.3637 0.6716 0.3036 -0.1124 -0.0223 -0.1182 49  GLU A C   
2239 O O   . GLU B 62  ? 0.3417 0.6421 0.2764 -0.1003 -0.0216 -0.1179 49  GLU A O   
2240 C CB  . GLU B 62  ? 0.3786 0.7265 0.3119 -0.1457 -0.0279 -0.1418 49  GLU A CB  
2241 N N   . ALA B 63  ? 0.3500 0.6310 0.2938 -0.1160 -0.0197 -0.1127 50  ALA A N   
2242 C CA  . ALA B 63  ? 0.3272 0.5695 0.2688 -0.1058 -0.0163 -0.1069 50  ALA A CA  
2243 C C   . ALA B 63  ? 0.2950 0.5504 0.2449 -0.0864 -0.0153 -0.0923 50  ALA A C   
2244 O O   . ALA B 63  ? 0.2785 0.5168 0.2244 -0.0759 -0.0135 -0.0904 50  ALA A O   
2245 C CB  . ALA B 63  ? 0.3073 0.5251 0.2522 -0.1139 -0.0141 -0.1031 50  ALA A CB  
2246 N N   . GLY B 64  ? 0.2500 0.5358 0.2101 -0.0818 -0.0162 -0.0821 51  GLY A N   
2247 C CA  . GLY B 64  ? 0.2325 0.5245 0.1984 -0.0649 -0.0146 -0.0675 51  GLY A CA  
2248 C C   . GLY B 64  ? 0.2438 0.5510 0.2043 -0.0556 -0.0152 -0.0679 51  GLY A C   
2249 O O   . GLY B 64  ? 0.2569 0.5520 0.2165 -0.0452 -0.0128 -0.0609 51  GLY A O   
2250 N N   . GLN B 65  ? 0.2589 0.5945 0.2157 -0.0607 -0.0183 -0.0763 52  GLN A N   
2251 C CA  . GLN B 65  ? 0.2910 0.6475 0.2419 -0.0530 -0.0193 -0.0780 52  GLN A CA  
2252 C C   . GLN B 65  ? 0.2914 0.6201 0.2334 -0.0525 -0.0177 -0.0864 52  GLN A C   
2253 O O   . GLN B 65  ? 0.2793 0.6109 0.2193 -0.0409 -0.0161 -0.0804 52  GLN A O   
2254 C CB  . GLN B 65  ? 0.3234 0.7175 0.2713 -0.0602 -0.0234 -0.0881 52  GLN A CB  
2255 C CG  . GLN B 65  ? 0.3741 0.8059 0.3296 -0.0561 -0.0251 -0.0789 52  GLN A CG  
2256 C CD  . GLN B 65  ? 0.4672 0.9370 0.4210 -0.0671 -0.0294 -0.0910 52  GLN A CD  
2257 O OE1 . GLN B 65  ? 0.5768 1.0537 0.5223 -0.0736 -0.0315 -0.1046 52  GLN A OE1 
2258 N NE2 . GLN B 65  ? 0.3923 0.8895 0.3535 -0.0691 -0.0310 -0.0868 52  GLN A NE2 
2259 N N   . GLY B 66  ? 0.2804 0.5824 0.2160 -0.0643 -0.0180 -0.0995 53  GLY A N   
2260 C CA  . GLY B 66  ? 0.2923 0.5647 0.2171 -0.0620 -0.0164 -0.1081 53  GLY A CA  
2261 C C   . GLY B 66  ? 0.2885 0.5433 0.2177 -0.0490 -0.0128 -0.0958 53  GLY A C   
2262 O O   . GLY B 66  ? 0.2976 0.5519 0.2215 -0.0392 -0.0114 -0.0964 53  GLY A O   
2263 N N   . LEU B 67  ? 0.2607 0.5013 0.1988 -0.0497 -0.0111 -0.0859 54  LEU A N   
2264 C CA  . LEU B 67  ? 0.2773 0.5001 0.2192 -0.0399 -0.0078 -0.0758 54  LEU A CA  
2265 C C   . LEU B 67  ? 0.2943 0.5401 0.2411 -0.0288 -0.0067 -0.0634 54  LEU A C   
2266 O O   . LEU B 67  ? 0.2763 0.5169 0.2207 -0.0210 -0.0045 -0.0609 54  LEU A O   
2267 C CB  . LEU B 67  ? 0.2791 0.4839 0.2286 -0.0441 -0.0067 -0.0693 54  LEU A CB  
2268 C CG  . LEU B 67  ? 0.2684 0.4551 0.2221 -0.0354 -0.0035 -0.0598 54  LEU A CG  
2269 C CD1 . LEU B 67  ? 0.2969 0.4606 0.2415 -0.0319 -0.0020 -0.0677 54  LEU A CD1 
2270 C CD2 . LEU B 67  ? 0.3034 0.4777 0.2648 -0.0390 -0.0028 -0.0532 54  LEU A CD2 
2271 N N   . ALA B 68  ? 0.2551 0.5272 0.2068 -0.0278 -0.0080 -0.0560 55  ALA A N   
2272 C CA  . ALA B 68  ? 0.3032 0.5933 0.2566 -0.0176 -0.0065 -0.0435 55  ALA A CA  
2273 C C   . ALA B 68  ? 0.3008 0.6074 0.2462 -0.0129 -0.0067 -0.0488 55  ALA A C   
2274 O O   . ALA B 68  ? 0.2775 0.5880 0.2225 -0.0053 -0.0040 -0.0400 55  ALA A O   
2275 C CB  . ALA B 68  ? 0.2778 0.5925 0.2348 -0.0153 -0.0080 -0.0353 55  ALA A CB  
2276 N N   . HIS B 69  ? 0.2739 0.5918 0.2127 -0.0181 -0.0096 -0.0628 56  HIS A N   
2277 C CA  . HIS B 69  ? 0.2804 0.6124 0.2105 -0.0134 -0.0099 -0.0697 56  HIS A CA  
2278 C C   . HIS B 69  ? 0.2927 0.6015 0.2183 -0.0088 -0.0071 -0.0732 56  HIS A C   
2279 O O   . HIS B 69  ? 0.3113 0.6328 0.2332 -0.0006 -0.0054 -0.0709 56  HIS A O   
2280 C CB  . HIS B 69  ? 0.3016 0.6461 0.2240 -0.0213 -0.0138 -0.0865 56  HIS A CB  
2281 C CG  . HIS B 69  ? 0.3399 0.7041 0.2530 -0.0147 -0.0142 -0.0929 56  HIS A CG  
2282 N ND1 . HIS B 69  ? 0.3647 0.7121 0.2669 -0.0138 -0.0140 -0.1068 56  HIS A ND1 
2283 C CD2 . HIS B 69  ? 0.3542 0.7528 0.2660 -0.0072 -0.0145 -0.0867 56  HIS A CD2 
2284 C CE1 . HIS B 69  ? 0.3611 0.7338 0.2567 -0.0062 -0.0142 -0.1094 56  HIS A CE1 
2285 N NE2 . HIS B 69  ? 0.3827 0.7862 0.2844 -0.0024 -0.0144 -0.0965 56  HIS A NE2 
2286 N N   . ALA B 70  ? 0.2789 0.5563 0.2035 -0.0135 -0.0067 -0.0797 57  ALA A N   
2287 C CA  . ALA B 70  ? 0.3096 0.5661 0.2289 -0.0072 -0.0043 -0.0834 57  ALA A CA  
2288 C C   . ALA B 70  ? 0.3052 0.5650 0.2324 0.0003  -0.0007 -0.0683 57  ALA A C   
2289 O O   . ALA B 70  ? 0.3352 0.5997 0.2586 0.0083  0.0013  -0.0686 57  ALA A O   
2290 C CB  . ALA B 70  ? 0.3003 0.5208 0.2154 -0.0130 -0.0044 -0.0923 57  ALA A CB  
2291 N N   . LEU B 71  ? 0.2809 0.5390 0.2184 -0.0024 0.0000  -0.0556 58  LEU A N   
2292 C CA  . LEU B 71  ? 0.2860 0.5410 0.2300 0.0018  0.0034  -0.0424 58  LEU A CA  
2293 C C   . LEU B 71  ? 0.2918 0.5727 0.2365 0.0063  0.0050  -0.0310 58  LEU A C   
2294 O O   . LEU B 71  ? 0.2906 0.5718 0.2384 0.0088  0.0082  -0.0214 58  LEU A O   
2295 C CB  . LEU B 71  ? 0.2853 0.5222 0.2378 -0.0027 0.0037  -0.0349 58  LEU A CB  
2296 C CG  . LEU B 71  ? 0.3324 0.5424 0.2835 -0.0069 0.0029  -0.0445 58  LEU A CG  
2297 C CD1 . LEU B 71  ? 0.3165 0.5151 0.2766 -0.0105 0.0033  -0.0352 58  LEU A CD1 
2298 C CD2 . LEU B 71  ? 0.3663 0.5640 0.3133 -0.0009 0.0050  -0.0483 58  LEU A CD2 
2299 N N   . GLY B 72  ? 0.3301 0.6321 0.2721 0.0063  0.0030  -0.0310 59  GLY A N   
2300 C CA  . GLY B 72  ? 0.3227 0.6503 0.2626 0.0115  0.0046  -0.0206 59  GLY A CA  
2301 C C   . GLY B 72  ? 0.3188 0.6446 0.2634 0.0117  0.0061  -0.0040 59  GLY A C   
2302 O O   . GLY B 72  ? 0.3066 0.6167 0.2563 0.0084  0.0050  -0.0024 59  GLY A O   
2303 N N   . ALA B 73  ? 0.3114 0.6507 0.2531 0.0158  0.0092  0.0087  60  ALA A N   
2304 C CA  . ALA B 73  ? 0.3267 0.6703 0.2670 0.0188  0.0103  0.0242  60  ALA A CA  
2305 C C   . ALA B 73  ? 0.2997 0.6165 0.2447 0.0162  0.0124  0.0344  60  ALA A C   
2306 O O   . ALA B 73  ? 0.3080 0.6217 0.2508 0.0196  0.0128  0.0452  60  ALA A O   
2307 C CB  . ALA B 73  ? 0.3465 0.7107 0.2796 0.0233  0.0135  0.0344  60  ALA A CB  
2308 N N   . ASN B 74  ? 0.2709 0.5686 0.2209 0.0114  0.0138  0.0310  61  ASN A N   
2309 C CA  . ASN B 74  ? 0.2746 0.5476 0.2286 0.0086  0.0152  0.0388  61  ASN A CA  
2310 C C   . ASN B 74  ? 0.3018 0.5620 0.2613 0.0069  0.0119  0.0305  61  ASN A C   
2311 O O   . ASN B 74  ? 0.2872 0.5261 0.2509 0.0044  0.0126  0.0338  61  ASN A O   
2312 C CB  . ASN B 74  ? 0.3195 0.5803 0.2769 0.0038  0.0182  0.0395  61  ASN A CB  
2313 C CG  . ASN B 74  ? 0.3825 0.6527 0.3351 0.0028  0.0224  0.0511  61  ASN A CG  
2314 O OD1 . ASN B 74  ? 0.4206 0.6969 0.3665 0.0057  0.0237  0.0618  61  ASN A OD1 
2315 N ND2 . ASN B 74  ? 0.4124 0.6846 0.3674 -0.0013 0.0249  0.0499  61  ASN A ND2 
2316 N N   . SER B 75  ? 0.2550 0.5283 0.2140 0.0070  0.0084  0.0193  62  SER A N   
2317 C CA  . SER B 75  ? 0.2448 0.5103 0.2082 0.0041  0.0054  0.0131  62  SER A CA  
2318 C C   . SER B 75  ? 0.2495 0.5362 0.2107 0.0077  0.0029  0.0153  62  SER A C   
2319 O O   . SER B 75  ? 0.2506 0.5600 0.2065 0.0117  0.0024  0.0165  62  SER A O   
2320 C CB  . SER B 75  ? 0.2460 0.5031 0.2106 -0.0015 0.0037  -0.0019 62  SER A CB  
2321 O OG  . SER B 75  ? 0.2663 0.5420 0.2257 -0.0020 0.0014  -0.0121 62  SER A OG  
2322 N N   . LEU B 76  ? 0.2288 0.5112 0.1938 0.0072  0.0014  0.0163  63  LEU A N   
2323 C CA  . LEU B 76  ? 0.2464 0.5522 0.2097 0.0122  -0.0009 0.0193  63  LEU A CA  
2324 C C   . LEU B 76  ? 0.2694 0.5762 0.2387 0.0061  -0.0038 0.0108  63  LEU A C   
2325 O O   . LEU B 76  ? 0.2592 0.5467 0.2328 0.0055  -0.0028 0.0142  63  LEU A O   
2326 C CB  . LEU B 76  ? 0.2915 0.5928 0.2507 0.0223  0.0014  0.0357  63  LEU A CB  
2327 C CG  . LEU B 76  ? 0.3709 0.6947 0.3275 0.0310  -0.0008 0.0405  63  LEU A CG  
2328 C CD1 . LEU B 76  ? 0.3999 0.7575 0.3515 0.0345  -0.0027 0.0383  63  LEU A CD1 
2329 C CD2 . LEU B 76  ? 0.3764 0.6860 0.3269 0.0425  0.0018  0.0566  63  LEU A CD2 
2330 N N   . PHE B 77  ? 0.2617 0.5915 0.2308 0.0006  -0.0071 -0.0005 64  PHE A N   
2331 C CA  . PHE B 77  ? 0.2458 0.5780 0.2201 -0.0080 -0.0094 -0.0087 64  PHE A CA  
2332 C C   . PHE B 77  ? 0.2532 0.6173 0.2282 -0.0017 -0.0116 -0.0037 64  PHE A C   
2333 O O   . PHE B 77  ? 0.2443 0.6379 0.2150 0.0032  -0.0132 -0.0034 64  PHE A O   
2334 C CB  . PHE B 77  ? 0.2300 0.5695 0.2022 -0.0200 -0.0119 -0.0252 64  PHE A CB  
2335 C CG  . PHE B 77  ? 0.2293 0.5773 0.2056 -0.0312 -0.0142 -0.0334 64  PHE A CG  
2336 C CD1 . PHE B 77  ? 0.2186 0.5468 0.2005 -0.0349 -0.0130 -0.0309 64  PHE A CD1 
2337 C CD2 . PHE B 77  ? 0.2721 0.6529 0.2467 -0.0377 -0.0177 -0.0425 64  PHE A CD2 
2338 C CE1 . PHE B 77  ? 0.2407 0.5819 0.2263 -0.0458 -0.0149 -0.0374 64  PHE A CE1 
2339 C CE2 . PHE B 77  ? 0.2670 0.6608 0.2456 -0.0498 -0.0197 -0.0497 64  PHE A CE2 
2340 C CZ  . PHE B 77  ? 0.2419 0.6143 0.2257 -0.0545 -0.0181 -0.0474 64  PHE A CZ  
2341 N N   . LEU B 78  ? 0.2335 0.5945 0.2136 -0.0011 -0.0116 -0.0002 65  LEU A N   
2342 C CA  . LEU B 78  ? 0.2634 0.6567 0.2449 0.0050  -0.0138 0.0032  65  LEU A CA  
2343 C C   . LEU B 78  ? 0.2523 0.6547 0.2404 -0.0087 -0.0158 -0.0075 65  LEU A C   
2344 O O   . LEU B 78  ? 0.2098 0.5866 0.2020 -0.0132 -0.0141 -0.0072 65  LEU A O   
2345 C CB  . LEU B 78  ? 0.2778 0.6618 0.2577 0.0203  -0.0117 0.0180  65  LEU A CB  
2346 C CG  . LEU B 78  ? 0.3844 0.7628 0.3552 0.0340  -0.0095 0.0304  65  LEU A CG  
2347 C CD1 . LEU B 78  ? 0.3640 0.7315 0.3289 0.0502  -0.0074 0.0451  65  LEU A CD1 
2348 C CD2 . LEU B 78  ? 0.4723 0.8869 0.4383 0.0374  -0.0117 0.0283  65  LEU A CD2 
2349 N N   . PRO B 79  ? 0.2366 0.6766 0.2256 -0.0153 -0.0192 -0.0159 66  PRO A N   
2350 C CA  . PRO B 79  ? 0.2473 0.7001 0.2424 -0.0295 -0.0208 -0.0246 66  PRO A CA  
2351 C C   . PRO B 79  ? 0.2563 0.7177 0.2566 -0.0204 -0.0200 -0.0153 66  PRO A C   
2352 O O   . PRO B 79  ? 0.2614 0.7412 0.2593 -0.0028 -0.0202 -0.0048 66  PRO A O   
2353 C CB  . PRO B 79  ? 0.2604 0.7556 0.2538 -0.0365 -0.0245 -0.0343 66  PRO A CB  
2354 C CG  . PRO B 79  ? 0.2419 0.7596 0.2303 -0.0166 -0.0250 -0.0238 66  PRO A CG  
2355 C CD  . PRO B 79  ? 0.2341 0.7093 0.2181 -0.0091 -0.0215 -0.0164 66  PRO A CD  
2356 N N   . CYS B 80  ? 0.2474 0.6921 0.2530 -0.0306 -0.0189 -0.0181 67  CYS A N   
2357 C CA  . CYS B 80  ? 0.2463 0.6986 0.2560 -0.0205 -0.0180 -0.0095 67  CYS A CA  
2358 C C   . CYS B 80  ? 0.2512 0.7012 0.2674 -0.0373 -0.0176 -0.0163 67  CYS A C   
2359 O O   . CYS B 80  ? 0.2744 0.6897 0.2902 -0.0498 -0.0160 -0.0215 67  CYS A O   
2360 C CB  . CYS B 80  ? 0.2686 0.6849 0.2750 -0.0048 -0.0150 0.0024  67  CYS A CB  
2361 S SG  . CYS B 80  ? 0.2891 0.7117 0.2981 0.0098  -0.0140 0.0123  67  CYS A SG  
2362 N N   . ASP B 81  ? 0.2388 0.7283 0.2599 -0.0374 -0.0191 -0.0162 68  ASP A N   
2363 C CA  . ASP B 81  ? 0.2380 0.7281 0.2653 -0.0493 -0.0179 -0.0187 68  ASP A CA  
2364 C C   . ASP B 81  ? 0.2238 0.7017 0.2523 -0.0312 -0.0159 -0.0073 68  ASP A C   
2365 O O   . ASP B 81  ? 0.2542 0.7579 0.2815 -0.0126 -0.0167 0.0001  68  ASP A O   
2366 C CB  . ASP B 81  ? 0.2684 0.8112 0.3007 -0.0615 -0.0204 -0.0256 68  ASP A CB  
2367 C CG  . ASP B 81  ? 0.3117 0.8593 0.3501 -0.0759 -0.0189 -0.0279 68  ASP A CG  
2368 O OD1 . ASP B 81  ? 0.3159 0.8301 0.3550 -0.0715 -0.0160 -0.0223 68  ASP A OD1 
2369 O OD2 . ASP B 81  ? 0.3499 0.9358 0.3920 -0.0929 -0.0205 -0.0358 68  ASP A OD2 
2370 N N   . VAL B 82  ? 0.2192 0.6532 0.2476 -0.0343 -0.0131 -0.0058 69  VAL A N   
2371 C CA  . VAL B 82  ? 0.2384 0.6528 0.2664 -0.0180 -0.0110 0.0038  69  VAL A CA  
2372 C C   . VAL B 82  ? 0.2359 0.6808 0.2687 -0.0130 -0.0111 0.0066  69  VAL A C   
2373 O O   . VAL B 82  ? 0.2331 0.6687 0.2636 0.0046  -0.0099 0.0146  69  VAL A O   
2374 C CB  . VAL B 82  ? 0.2496 0.6144 0.2768 -0.0242 -0.0084 0.0034  69  VAL A CB  
2375 C CG1 . VAL B 82  ? 0.2551 0.5940 0.2772 -0.0255 -0.0082 0.0017  69  VAL A CG1 
2376 C CG2 . VAL B 82  ? 0.2000 0.5598 0.2313 -0.0440 -0.0074 -0.0035 69  VAL A CG2 
2377 N N   . ARG B 83  ? 0.2746 0.7579 0.3129 -0.0277 -0.0125 -0.0001 70  ARG A N   
2378 C CA  . ARG B 83  ? 0.2963 0.8210 0.3394 -0.0217 -0.0128 0.0025  70  ARG A CA  
2379 C C   . ARG B 83  ? 0.3090 0.8675 0.3485 0.0022  -0.0147 0.0090  70  ARG A C   
2380 O O   . ARG B 83  ? 0.2631 0.8448 0.3031 0.0181  -0.0145 0.0146  70  ARG A O   
2381 C CB  . ARG B 83  ? 0.2758 0.8396 0.3257 -0.0447 -0.0137 -0.0062 70  ARG A CB  
2382 C CG  . ARG B 83  ? 0.3379 0.8641 0.3882 -0.0683 -0.0115 -0.0122 70  ARG A CG  
2383 C CD  . ARG B 83  ? 0.4712 1.0262 0.5246 -0.0950 -0.0123 -0.0220 70  ARG A CD  
2384 N NE  . ARG B 83  ? 0.5252 1.1106 0.5851 -0.0993 -0.0109 -0.0198 70  ARG A NE  
2385 C CZ  . ARG B 83  ? 0.6430 1.2797 0.7077 -0.1148 -0.0122 -0.0254 70  ARG A CZ  
2386 N NH1 . ARG B 83  ? 0.4946 1.1471 0.5574 -0.1280 -0.0149 -0.0341 70  ARG A NH1 
2387 N NH2 . ARG B 83  ? 0.5373 1.2094 0.6085 -0.1176 -0.0109 -0.0228 70  ARG A NH2 
2388 N N   . ASP B 84  ? 0.2516 0.8144 0.2866 0.0051  -0.0166 0.0082  71  ASP A N   
2389 C CA  . ASP B 84  ? 0.2796 0.8741 0.3093 0.0278  -0.0184 0.0147  71  ASP A CA  
2390 C C   . ASP B 84  ? 0.3141 0.8661 0.3338 0.0501  -0.0164 0.0256  71  ASP A C   
2391 O O   . ASP B 84  ? 0.2698 0.7919 0.2839 0.0503  -0.0159 0.0271  71  ASP A O   
2392 C CB  . ASP B 84  ? 0.2661 0.8935 0.2955 0.0197  -0.0214 0.0085  71  ASP A CB  
2393 C CG  . ASP B 84  ? 0.2800 0.9422 0.3026 0.0432  -0.0234 0.0153  71  ASP A CG  
2394 O OD1 . ASP B 84  ? 0.3144 0.9698 0.3301 0.0687  -0.0222 0.0264  71  ASP A OD1 
2395 O OD2 . ASP B 84  ? 0.2544 0.9502 0.2775 0.0360  -0.0263 0.0094  71  ASP A OD2 
2396 N N   . ILE B 85  ? 0.2601 0.8109 0.2765 0.0692  -0.0151 0.0330  72  ILE A N   
2397 C CA  . ILE B 85  ? 0.2693 0.7746 0.2749 0.0876  -0.0128 0.0424  72  ILE A CA  
2398 C C   . ILE B 85  ? 0.2887 0.7990 0.2826 0.1067  -0.0135 0.0502  72  ILE A C   
2399 O O   . ILE B 85  ? 0.3084 0.7760 0.2929 0.1138  -0.0115 0.0566  72  ILE A O   
2400 C CB  . ILE B 85  ? 0.2855 0.7849 0.2888 0.1029  -0.0113 0.0472  72  ILE A CB  
2401 C CG1 . ILE B 85  ? 0.2537 0.7407 0.2672 0.0838  -0.0100 0.0407  72  ILE A CG1 
2402 C CG2 . ILE B 85  ? 0.2846 0.7386 0.2733 0.1239  -0.0091 0.0570  72  ILE A CG2 
2403 C CD1 . ILE B 85  ? 0.2585 0.6963 0.2736 0.0665  -0.0085 0.0373  72  ILE A CD1 
2404 N N   . GLU B 86  ? 0.2800 0.8421 0.2731 0.1170  -0.0159 0.0510  73  GLU A N   
2405 C CA  . GLU B 86  ? 0.3105 0.8812 0.2926 0.1329  -0.0167 0.0579  73  GLU A CA  
2406 C C   . GLU B 86  ? 0.2508 0.7976 0.2336 0.1159  -0.0166 0.0541  73  GLU A C   
2407 O O   . GLU B 86  ? 0.2777 0.8005 0.2492 0.1270  -0.0153 0.0621  73  GLU A O   
2408 C CB  . GLU B 86  ? 0.3418 0.9771 0.3229 0.1469  -0.0197 0.0588  73  GLU A CB  
2409 C CG  . GLU B 86  ? 0.4520 1.0978 0.4252 0.1745  -0.0188 0.0671  73  GLU A CG  
2410 C CD  . GLU B 86  ? 0.5891 1.1887 0.5423 0.2005  -0.0160 0.0806  73  GLU A CD  
2411 O OE1 . GLU B 86  ? 0.8152 1.4137 0.7583 0.2096  -0.0162 0.0867  73  GLU A OE1 
2412 O OE2 . GLU B 86  ? 0.6520 1.2154 0.5983 0.2118  -0.0135 0.0852  73  GLU A OE2 
2413 N N   . ARG B 87  ? 0.2479 0.8084 0.2425 0.0903  -0.0182 0.0420  74  ARG A N   
2414 C CA  . ARG B 87  ? 0.2519 0.7965 0.2458 0.0768  -0.0185 0.0375  74  ARG A CA  
2415 C C   . ARG B 87  ? 0.2749 0.7590 0.2653 0.0743  -0.0151 0.0413  74  ARG A C   
2416 O O   . ARG B 87  ? 0.2776 0.7403 0.2612 0.0765  -0.0141 0.0450  74  ARG A O   
2417 C CB  . ARG B 87  ? 0.2558 0.8280 0.2593 0.0515  -0.0211 0.0231  74  ARG A CB  
2418 C CG  . ARG B 87  ? 0.2495 0.7991 0.2516 0.0372  -0.0211 0.0169  74  ARG A CG  
2419 C CD  . ARG B 87  ? 0.2425 0.8178 0.2372 0.0475  -0.0229 0.0196  74  ARG A CD  
2420 N NE  . ARG B 87  ? 0.2535 0.7966 0.2457 0.0370  -0.0219 0.0157  74  ARG A NE  
2421 C CZ  . ARG B 87  ? 0.2907 0.8267 0.2742 0.0469  -0.0212 0.0218  74  ARG A CZ  
2422 N NH1 . ARG B 87  ? 0.3018 0.8499 0.2764 0.0692  -0.0207 0.0345  74  ARG A NH1 
2423 N NH2 . ARG B 87  ? 0.2899 0.8012 0.2726 0.0351  -0.0203 0.0160  74  ARG A NH2 
2424 N N   . LEU B 88  ? 0.2332 0.6932 0.2284 0.0692  -0.0135 0.0401  75  LEU A N   
2425 C CA  . LEU B 88  ? 0.2364 0.6429 0.2287 0.0670  -0.0105 0.0431  75  LEU A CA  
2426 C C   . LEU B 88  ? 0.2586 0.6429 0.2375 0.0876  -0.0085 0.0557  75  LEU A C   
2427 O O   . LEU B 88  ? 0.2737 0.6272 0.2476 0.0853  -0.0067 0.0587  75  LEU A O   
2428 C CB  . LEU B 88  ? 0.2316 0.6216 0.2293 0.0632  -0.0092 0.0415  75  LEU A CB  
2429 C CG  . LEU B 88  ? 0.2333 0.5716 0.2287 0.0611  -0.0063 0.0440  75  LEU A CG  
2430 C CD1 . LEU B 88  ? 0.2502 0.5720 0.2495 0.0427  -0.0062 0.0370  75  LEU A CD1 
2431 C CD2 . LEU B 88  ? 0.2201 0.5501 0.2207 0.0591  -0.0054 0.0421  75  LEU A CD2 
2432 N N   . LYS B 89  ? 0.3086 0.7068 0.2799 0.1087  -0.0086 0.0635  76  LYS A N   
2433 C CA  . LYS B 89  ? 0.3043 0.6744 0.2597 0.1279  -0.0062 0.0758  76  LYS A CA  
2434 C C   . LYS B 89  ? 0.3115 0.6923 0.2603 0.1302  -0.0066 0.0796  76  LYS A C   
2435 O O   . LYS B 89  ? 0.3373 0.6842 0.2751 0.1352  -0.0039 0.0879  76  LYS A O   
2436 C CB  . LYS B 89  ? 0.3288 0.7158 0.2746 0.1529  -0.0064 0.0832  76  LYS A CB  
2437 C CG  . LYS B 89  ? 0.3717 0.7392 0.3193 0.1558  -0.0052 0.0820  76  LYS A CG  
2438 C CD  . LYS B 89  ? 0.4427 0.8415 0.3819 0.1815  -0.0061 0.0876  76  LYS A CD  
2439 C CE  . LYS B 89  ? 0.4189 0.8011 0.3584 0.1867  -0.0050 0.0863  76  LYS A CE  
2440 N NZ  . LYS B 89  ? 0.5211 0.9447 0.4591 0.2057  -0.0063 0.0873  76  LYS A NZ  
2441 N N   . ALA B 90  ? 0.2799 0.7087 0.2351 0.1260  -0.0098 0.0736  77  ALA A N   
2442 C CA  . ALA B 90  ? 0.3081 0.7500 0.2564 0.1293  -0.0103 0.0771  77  ALA A CA  
2443 C C   . ALA B 90  ? 0.2879 0.6963 0.2381 0.1127  -0.0085 0.0742  77  ALA A C   
2444 O O   . ALA B 90  ? 0.3008 0.6960 0.2408 0.1188  -0.0067 0.0822  77  ALA A O   
2445 C CB  . ALA B 90  ? 0.2756 0.7765 0.2304 0.1260  -0.0143 0.0695  77  ALA A CB  
2446 N N   . CYS B 91  ? 0.2781 0.6771 0.2408 0.0923  -0.0090 0.0628  78  CYS A N   
2447 C CA  . CYS B 91  ? 0.2681 0.6415 0.2337 0.0766  -0.0078 0.0579  78  CYS A CA  
2448 C C   . CYS B 91  ? 0.3008 0.6284 0.2582 0.0819  -0.0039 0.0676  78  CYS A C   
2449 O O   . CYS B 91  ? 0.3323 0.6465 0.2851 0.0789  -0.0022 0.0705  78  CYS A O   
2450 C CB  . CYS B 91  ? 0.2745 0.6441 0.2525 0.0567  -0.0088 0.0450  78  CYS A CB  
2451 S SG  . CYS B 91  ? 0.3032 0.7204 0.2886 0.0430  -0.0130 0.0312  78  CYS A SG  
2452 N N   . VAL B 92  ? 0.3242 0.6295 0.2794 0.0892  -0.0024 0.0723  79  VAL A N   
2453 C CA  . VAL B 92  ? 0.3378 0.5986 0.2842 0.0930  0.0013  0.0807  79  VAL A CA  
2454 C C   . VAL B 92  ? 0.3455 0.6001 0.2757 0.1077  0.0033  0.0938  79  VAL A C   
2455 O O   . VAL B 92  ? 0.3452 0.5729 0.2689 0.1034  0.0063  0.0992  79  VAL A O   
2456 C CB  . VAL B 92  ? 0.3533 0.5926 0.2991 0.0987  0.0022  0.0820  79  VAL A CB  
2457 C CG1 . VAL B 92  ? 0.3924 0.5853 0.3268 0.1023  0.0058  0.0903  79  VAL A CG1 
2458 C CG2 . VAL B 92  ? 0.2952 0.5370 0.2557 0.0837  0.0008  0.0706  79  VAL A CG2 
2459 N N   . ALA B 93  ? 0.3372 0.6168 0.2595 0.1256  0.0021  0.0997  80  ALA A N   
2460 C CA  . ALA B 93  ? 0.3613 0.6338 0.2656 0.1418  0.0044  0.1134  80  ALA A CA  
2461 C C   . ALA B 93  ? 0.3397 0.6234 0.2442 0.1329  0.0047  0.1135  80  ALA A C   
2462 O O   . ALA B 93  ? 0.3601 0.6220 0.2517 0.1367  0.0081  0.1241  80  ALA A O   
2463 C CB  . ALA B 93  ? 0.4141 0.7202 0.3108 0.1636  0.0024  0.1185  80  ALA A CB  
2464 N N   . GLU B 94  ? 0.3262 0.6435 0.2447 0.1201  0.0014  0.1012  81  GLU A N   
2465 C CA  . GLU B 94  ? 0.2993 0.6320 0.2176 0.1131  0.0012  0.0996  81  GLU A CA  
2466 C C   . GLU B 94  ? 0.3243 0.6221 0.2439 0.0992  0.0044  0.0994  81  GLU A C   
2467 O O   . GLU B 94  ? 0.3244 0.6183 0.2364 0.0991  0.0067  0.1057  81  GLU A O   
2468 C CB  . GLU B 94  ? 0.3305 0.7059 0.2610 0.1031  -0.0032 0.0856  81  GLU A CB  
2469 C CG  . GLU B 94  ? 0.3731 0.7565 0.3034 0.0939  -0.0030 0.0819  81  GLU A CG  
2470 C CD  . GLU B 94  ? 0.5101 0.9361 0.4487 0.0855  -0.0075 0.0680  81  GLU A CD  
2471 O OE1 . GLU B 94  ? 0.5887 1.0386 0.5329 0.0868  -0.0104 0.0629  81  GLU A OE1 
2472 O OE2 . GLU B 94  ? 0.6406 1.0751 0.5799 0.0767  -0.0080 0.0615  81  GLU A OE2 
2473 N N   . VAL B 95  ? 0.2840 0.5605 0.2136 0.0871  0.0045  0.0916  82  VAL A N   
2474 C CA  . VAL B 95  ? 0.3000 0.5454 0.2307 0.0752  0.0075  0.0916  82  VAL A CA  
2475 C C   . VAL B 95  ? 0.3487 0.5621 0.2644 0.0830  0.0119  0.1066  82  VAL A C   
2476 O O   . VAL B 95  ? 0.3755 0.5782 0.2861 0.0774  0.0148  0.1116  82  VAL A O   
2477 C CB  . VAL B 95  ? 0.2758 0.5053 0.2186 0.0634  0.0067  0.0815  82  VAL A CB  
2478 C CG1 . VAL B 95  ? 0.2676 0.4675 0.2109 0.0529  0.0099  0.0823  82  VAL A CG1 
2479 C CG2 . VAL B 95  ? 0.2344 0.4915 0.1893 0.0539  0.0030  0.0672  82  VAL A CG2 
2480 N N   . GLU B 96  ? 0.3611 0.5591 0.2683 0.0957  0.0125  0.1136  83  GLU A N   
2481 C CA  . GLU B 96  ? 0.4115 0.5733 0.3011 0.1035  0.0169  0.1276  83  GLU A CA  
2482 C C   . GLU B 96  ? 0.4413 0.6111 0.3169 0.1115  0.0190  0.1393  83  GLU A C   
2483 O O   . GLU B 96  ? 0.4371 0.5797 0.3019 0.1074  0.0233  0.1486  83  GLU A O   
2484 C CB  . GLU B 96  ? 0.4421 0.5832 0.3219 0.1182  0.0173  0.1328  83  GLU A CB  
2485 C CG  . GLU B 96  ? 0.5283 0.6509 0.4186 0.1092  0.0165  0.1237  83  GLU A CG  
2486 C CD  . GLU B 96  ? 0.5664 0.6715 0.4463 0.1257  0.0167  0.1279  83  GLU A CD  
2487 O OE1 . GLU B 96  ? 0.6921 0.8201 0.5663 0.1433  0.0150  0.1315  83  GLU A OE1 
2488 O OE2 . GLU B 96  ? 0.5775 0.6474 0.4540 0.1223  0.0184  0.1275  83  GLU A OE2 
2489 N N   . ARG B 97  ? 0.4066 0.6152 0.2821 0.1224  0.0162  0.1390  84  ARG A N   
2490 C CA  . ARG B 97  ? 0.4612 0.6801 0.3225 0.1318  0.0182  0.1507  84  ARG A CA  
2491 C C   . ARG B 97  ? 0.4313 0.6589 0.2986 0.1159  0.0193  0.1473  84  ARG A C   
2492 O O   . ARG B 97  ? 0.4243 0.6467 0.2789 0.1185  0.0228  0.1587  84  ARG A O   
2493 C CB  . ARG B 97  ? 0.5423 0.8052 0.4010 0.1482  0.0147  0.1514  84  ARG A CB  
2494 C CG  . ARG B 97  ? 0.6600 0.9229 0.5077 0.1703  0.0140  0.1584  84  ARG A CG  
2495 C CD  . ARG B 97  ? 0.6278 0.9430 0.4740 0.1844  0.0106  0.1587  84  ARG A CD  
2496 N NE  . ARG B 97  ? 0.5110 0.8720 0.3778 0.1733  0.0052  0.1416  84  ARG A NE  
2497 C CZ  . ARG B 97  ? 0.4911 0.8701 0.3698 0.1723  0.0017  0.1316  84  ARG A CZ  
2498 N NH1 . ARG B 97  ? 0.4864 0.8432 0.3597 0.1835  0.0028  0.1362  84  ARG A NH1 
2499 N NH2 . ARG B 97  ? 0.4015 0.8184 0.2968 0.1587  -0.0025 0.1165  84  ARG A NH2 
2500 N N   . THR B 98  ? 0.4017 0.6455 0.2872 0.1010  0.0164  0.1319  85  THR A N   
2501 C CA  . THR B 98  ? 0.3802 0.6353 0.2710 0.0882  0.0172  0.1271  85  THR A CA  
2502 C C   . THR B 98  ? 0.3760 0.5953 0.2637 0.0771  0.0219  0.1327  85  THR A C   
2503 O O   . THR B 98  ? 0.3837 0.6032 0.2637 0.0745  0.0253  0.1407  85  THR A O   
2504 C CB  . THR B 98  ? 0.3775 0.6567 0.2859 0.0773  0.0127  0.1087  85  THR A CB  
2505 O OG1 . THR B 98  ? 0.3499 0.6640 0.2598 0.0860  0.0086  0.1042  85  THR A OG1 
2506 C CG2 . THR B 98  ? 0.4155 0.7118 0.3270 0.0682  0.0130  0.1029  85  THR A CG2 
2507 N N   . TRP B 99  ? 0.3675 0.5577 0.2601 0.0706  0.0225  0.1295  86  TRP A N   
2508 C CA  . TRP B 99  ? 0.3954 0.5607 0.2914 0.0559  0.0255  0.1286  86  TRP A CA  
2509 C C   . TRP B 99  ? 0.4478 0.5712 0.3339 0.0563  0.0287  0.1371  86  TRP A C   
2510 O O   . TRP B 99  ? 0.4460 0.5487 0.3343 0.0431  0.0312  0.1363  86  TRP A O   
2511 C CB  . TRP B 99  ? 0.3137 0.4876 0.2278 0.0443  0.0225  0.1121  86  TRP A CB  
2512 C CG  . TRP B 99  ? 0.3382 0.5425 0.2595 0.0391  0.0210  0.1034  86  TRP A CG  
2513 C CD1 . TRP B 99  ? 0.3305 0.5530 0.2458 0.0400  0.0227  0.1084  86  TRP A CD1 
2514 C CD2 . TRP B 99  ? 0.2973 0.5160 0.2319 0.0328  0.0174  0.0876  86  TRP A CD2 
2515 N NE1 . TRP B 99  ? 0.3506 0.5974 0.2745 0.0349  0.0203  0.0959  86  TRP A NE1 
2516 C CE2 . TRP B 99  ? 0.3053 0.5482 0.2404 0.0304  0.0171  0.0831  86  TRP A CE2 
2517 C CE3 . TRP B 99  ? 0.2667 0.4787 0.2111 0.0294  0.0147  0.0776  86  TRP A CE3 
2518 C CZ2 . TRP B 99  ? 0.3060 0.5634 0.2500 0.0249  0.0141  0.0679  86  TRP A CZ2 
2519 C CZ3 . TRP B 99  ? 0.2755 0.5005 0.2288 0.0227  0.0121  0.0638  86  TRP A CZ3 
2520 C CH2 . TRP B 99  ? 0.2579 0.5039 0.2103 0.0209  0.0118  0.0588  86  TRP A CH2 
2521 N N   . GLY B 100 ? 0.4820 0.5937 0.3583 0.0709  0.0281  0.1430  87  GLY A N   
2522 C CA  . GLY B 100 ? 0.4765 0.5459 0.3423 0.0721  0.0307  0.1489  87  GLY A CA  
2523 C C   . GLY B 100 ? 0.4459 0.5100 0.3239 0.0704  0.0276  0.1375  87  GLY A C   
2524 O O   . GLY B 100 ? 0.4593 0.5514 0.3536 0.0670  0.0238  0.1257  87  GLY A O   
2525 N N   . ALA B 101 ? 0.4091 0.4365 0.2784 0.0718  0.0293  0.1405  88  ALA A N   
2526 C CA  . ALA B 101 ? 0.4029 0.4235 0.2821 0.0708  0.0268  0.1306  88  ALA A CA  
2527 C C   . ALA B 101 ? 0.3651 0.4031 0.2649 0.0549  0.0247  0.1175  88  ALA A C   
2528 O O   . ALA B 101 ? 0.3642 0.3999 0.2673 0.0414  0.0266  0.1169  88  ALA A O   
2529 C CB  . ALA B 101 ? 0.4472 0.4223 0.3130 0.0695  0.0299  0.1354  88  ALA A CB  
2530 N N   . VAL B 102 ? 0.3672 0.4213 0.2798 0.0568  0.0210  0.1075  89  VAL A N   
2531 C CA  . VAL B 102 ? 0.3297 0.3931 0.2588 0.0432  0.0193  0.0957  89  VAL A CA  
2532 C C   . VAL B 102 ? 0.3431 0.3767 0.2720 0.0332  0.0214  0.0944  89  VAL A C   
2533 O O   . VAL B 102 ? 0.3680 0.3752 0.2874 0.0382  0.0226  0.0985  89  VAL A O   
2534 C CB  . VAL B 102 ? 0.3030 0.3868 0.2425 0.0478  0.0156  0.0871  89  VAL A CB  
2535 C CG1 . VAL B 102 ? 0.2857 0.3758 0.2401 0.0353  0.0140  0.0755  89  VAL A CG1 
2536 C CG2 . VAL B 102 ? 0.3311 0.4471 0.2704 0.0557  0.0135  0.0878  89  VAL A CG2 
2537 N N   . ASP B 103 ? 0.3038 0.3426 0.2420 0.0197  0.0219  0.0888  90  ASP A N   
2538 C CA  . ASP B 103 ? 0.3054 0.3238 0.2456 0.0091  0.0234  0.0861  90  ASP A CA  
2539 C C   . ASP B 103 ? 0.2799 0.3027 0.2324 0.0075  0.0206  0.0755  90  ASP A C   
2540 O O   . ASP B 103 ? 0.2926 0.2967 0.2448 0.0047  0.0209  0.0734  90  ASP A O   
2541 C CB  . ASP B 103 ? 0.3377 0.3640 0.2809 -0.0030 0.0254  0.0860  90  ASP A CB  
2542 C CG  . ASP B 103 ? 0.3360 0.3541 0.2658 -0.0046 0.0292  0.0978  90  ASP A CG  
2543 O OD1 . ASP B 103 ? 0.3852 0.3744 0.3039 -0.0083 0.0319  0.1039  90  ASP A OD1 
2544 O OD2 . ASP B 103 ? 0.3433 0.3814 0.2720 -0.0031 0.0298  0.1011  90  ASP A OD2 
2545 N N   . VAL B 104 ? 0.2497 0.2974 0.2123 0.0081  0.0181  0.0687  91  VAL A N   
2546 C CA  . VAL B 104 ? 0.2646 0.3168 0.2382 0.0049  0.0160  0.0590  91  VAL A CA  
2547 C C   . VAL B 104 ? 0.2490 0.3207 0.2269 0.0110  0.0133  0.0553  91  VAL A C   
2548 O O   . VAL B 104 ? 0.2654 0.3561 0.2442 0.0111  0.0124  0.0541  91  VAL A O   
2549 C CB  . VAL B 104 ? 0.2565 0.3175 0.2382 -0.0043 0.0161  0.0522  91  VAL A CB  
2550 C CG1 . VAL B 104 ? 0.2401 0.3007 0.2299 -0.0056 0.0143  0.0440  91  VAL A CG1 
2551 C CG2 . VAL B 104 ? 0.2590 0.3084 0.2376 -0.0120 0.0189  0.0555  91  VAL A CG2 
2552 N N   . LEU B 105 ? 0.2553 0.3238 0.2354 0.0152  0.0120  0.0531  92  LEU A N   
2553 C CA  . LEU B 105 ? 0.2296 0.3194 0.2149 0.0180  0.0096  0.0487  92  LEU A CA  
2554 C C   . LEU B 105 ? 0.2143 0.3040 0.2086 0.0104  0.0087  0.0403  92  LEU A C   
2555 O O   . LEU B 105 ? 0.2406 0.3151 0.2361 0.0097  0.0093  0.0395  92  LEU A O   
2556 C CB  . LEU B 105 ? 0.2498 0.3414 0.2305 0.0294  0.0089  0.0531  92  LEU A CB  
2557 C CG  . LEU B 105 ? 0.2727 0.3882 0.2601 0.0308  0.0066  0.0481  92  LEU A CG  
2558 C CD1 . LEU B 105 ? 0.2157 0.3598 0.2051 0.0290  0.0049  0.0458  92  LEU A CD1 
2559 C CD2 . LEU B 105 ? 0.2730 0.3910 0.2545 0.0449  0.0064  0.0531  92  LEU A CD2 
2560 N N   . ILE B 106 ? 0.1903 0.2961 0.1895 0.0050  0.0073  0.0339  93  ILE A N   
2561 C CA  . ILE B 106 ? 0.1837 0.2870 0.1889 -0.0015 0.0068  0.0268  93  ILE A CA  
2562 C C   . ILE B 106 ? 0.1980 0.3205 0.2059 -0.0020 0.0051  0.0241  93  ILE A C   
2563 O O   . ILE B 106 ? 0.2047 0.3441 0.2126 -0.0055 0.0038  0.0206  93  ILE A O   
2564 C CB  . ILE B 106 ? 0.1577 0.2584 0.1639 -0.0085 0.0071  0.0209  93  ILE A CB  
2565 C CG1 . ILE B 106 ? 0.1703 0.2605 0.1742 -0.0081 0.0089  0.0240  93  ILE A CG1 
2566 C CG2 . ILE B 106 ? 0.1573 0.2498 0.1669 -0.0137 0.0071  0.0149  93  ILE A CG2 
2567 C CD1 . ILE B 106 ? 0.2014 0.2906 0.2058 -0.0126 0.0093  0.0180  93  ILE A CD1 
2568 N N   . ASN B 107 ? 0.2239 0.3443 0.2342 -0.0003 0.0051  0.0244  94  ASN A N   
2569 C CA  . ASN B 107 ? 0.2193 0.3602 0.2329 -0.0021 0.0039  0.0221  94  ASN A CA  
2570 C C   . ASN B 107 ? 0.2310 0.3673 0.2478 -0.0140 0.0041  0.0150  94  ASN A C   
2571 O O   . ASN B 107 ? 0.2031 0.3265 0.2216 -0.0156 0.0052  0.0146  94  ASN A O   
2572 C CB  . ASN B 107 ? 0.2390 0.3813 0.2527 0.0064  0.0041  0.0261  94  ASN A CB  
2573 C CG  . ASN B 107 ? 0.2308 0.3778 0.2384 0.0200  0.0039  0.0331  94  ASN A CG  
2574 O OD1 . ASN B 107 ? 0.2141 0.3788 0.2195 0.0228  0.0028  0.0346  94  ASN A OD1 
2575 N ND2 . ASN B 107 ? 0.2246 0.3545 0.2278 0.0290  0.0049  0.0373  94  ASN A ND2 
2576 N N   . ASN B 108 ? 0.2147 0.3614 0.2309 -0.0220 0.0032  0.0096  95  ASN A N   
2577 C CA  . ASN B 108 ? 0.2130 0.3486 0.2284 -0.0331 0.0037  0.0027  95  ASN A CA  
2578 C C   . ASN B 108 ? 0.2360 0.3900 0.2522 -0.0440 0.0027  -0.0026 95  ASN A C   
2579 O O   . ASN B 108 ? 0.2381 0.3801 0.2524 -0.0541 0.0037  -0.0072 95  ASN A O   
2580 C CB  . ASN B 108 ? 0.2103 0.3348 0.2214 -0.0337 0.0039  -0.0005 95  ASN A CB  
2581 C CG  . ASN B 108 ? 0.2304 0.3422 0.2373 -0.0433 0.0044  -0.0085 95  ASN A CG  
2582 O OD1 . ASN B 108 ? 0.2311 0.3232 0.2365 -0.0448 0.0059  -0.0092 95  ASN A OD1 
2583 N ND2 . ASN B 108 ? 0.2257 0.3477 0.2292 -0.0499 0.0031  -0.0147 95  ASN A ND2 
2584 N N   . ALA B 109 ? 0.1992 0.3819 0.2171 -0.0425 0.0009  -0.0019 96  ALA A N   
2585 C CA  . ALA B 109 ? 0.2132 0.4182 0.2319 -0.0547 -0.0003 -0.0079 96  ALA A CA  
2586 C C   . ALA B 109 ? 0.2041 0.4083 0.2258 -0.0619 0.0012  -0.0076 96  ALA A C   
2587 O O   . ALA B 109 ? 0.1790 0.3873 0.2043 -0.0530 0.0018  -0.0015 96  ALA A O   
2588 C CB  . ALA B 109 ? 0.1961 0.4364 0.2167 -0.0490 -0.0025 -0.0060 96  ALA A CB  
2589 N N   . ALA B 110 ? 0.2202 0.4204 0.2393 -0.0783 0.0018  -0.0142 97  ALA A N   
2590 C CA  . ALA B 110 ? 0.2505 0.4500 0.2715 -0.0862 0.0036  -0.0129 97  ALA A CA  
2591 C C   . ALA B 110 ? 0.2796 0.4816 0.2962 -0.1069 0.0039  -0.0208 97  ALA A C   
2592 O O   . ALA B 110 ? 0.3012 0.4955 0.3117 -0.1138 0.0029  -0.0279 97  ALA A O   
2593 C CB  . ALA B 110 ? 0.2772 0.4400 0.2953 -0.0813 0.0061  -0.0098 97  ALA A CB  
2594 N N   . ARG B 111 ? 0.2976 0.5103 0.3163 -0.1176 0.0055  -0.0199 98  ARG A N   
2595 C CA  . ARG B 111 ? 0.2712 0.4807 0.2839 -0.1402 0.0065  -0.0269 98  ARG A CA  
2596 C C   . ARG B 111 ? 0.3155 0.5031 0.3253 -0.1468 0.0102  -0.0230 98  ARG A C   
2597 O O   . ARG B 111 ? 0.3168 0.5256 0.3336 -0.1442 0.0111  -0.0173 98  ARG A O   
2598 C CB  . ARG B 111 ? 0.2975 0.5520 0.3148 -0.1514 0.0043  -0.0315 98  ARG A CB  
2599 N N   . ASP B 112 ? 0.3822 0.5289 0.3803 -0.1549 0.0125  -0.0262 99  ASP A N   
2600 C CA  . ASP B 112 ? 0.4099 0.5298 0.4033 -0.1566 0.0162  -0.0210 99  ASP A CA  
2601 C C   . ASP B 112 ? 0.4532 0.5629 0.4372 -0.1808 0.0191  -0.0242 99  ASP A C   
2602 O O   . ASP B 112 ? 0.5182 0.5938 0.4926 -0.1835 0.0225  -0.0211 99  ASP A O   
2603 C CB  . ASP B 112 ? 0.4829 0.5611 0.4685 -0.1436 0.0172  -0.0199 99  ASP A CB  
2604 C CG  . ASP B 112 ? 0.4944 0.5439 0.4669 -0.1496 0.0170  -0.0283 99  ASP A CG  
2605 O OD1 . ASP B 112 ? 0.5135 0.5730 0.4822 -0.1658 0.0161  -0.0355 99  ASP A OD1 
2606 O OD2 . ASP B 112 ? 0.5902 0.6119 0.5568 -0.1366 0.0173  -0.0283 99  ASP A OD2 
2607 N N   . ASP B 113 ? 0.4053 0.5444 0.3912 -0.1981 0.0178  -0.0298 100 ASP A N   
2608 C CA  . ASP B 113 ? 0.4466 0.5740 0.4220 -0.2247 0.0208  -0.0337 100 ASP A CA  
2609 C C   . ASP B 113 ? 0.4703 0.5960 0.4462 -0.2299 0.0249  -0.0249 100 ASP A C   
2610 O O   . ASP B 113 ? 0.4077 0.5647 0.3966 -0.2179 0.0245  -0.0179 100 ASP A O   
2611 C CB  . ASP B 113 ? 0.4809 0.6489 0.4603 -0.2433 0.0185  -0.0414 100 ASP A CB  
2612 C CG  . ASP B 113 ? 0.5512 0.7286 0.5310 -0.2379 0.0141  -0.0499 100 ASP A CG  
2613 O OD1 . ASP B 113 ? 0.4943 0.6887 0.4838 -0.2159 0.0114  -0.0464 100 ASP A OD1 
2614 O OD2 . ASP B 113 ? 0.6616 0.8298 0.6312 -0.2559 0.0136  -0.0600 100 ASP A OD2 
2615 N N   . ARG B 114 ? 0.4681 0.5565 0.4282 -0.2478 0.0291  -0.0255 101 ARG A N   
2616 C CA  . ARG B 114 ? 0.4801 0.5593 0.4366 -0.2551 0.0339  -0.0168 101 ARG A CA  
2617 C C   . ARG B 114 ? 0.4714 0.6015 0.4379 -0.2737 0.0344  -0.0160 101 ARG A C   
2618 O O   . ARG B 114 ? 0.5017 0.6537 0.4688 -0.2905 0.0325  -0.0243 101 ARG A O   
2619 C CB  . ARG B 114 ? 0.5231 0.5398 0.4576 -0.2607 0.0381  -0.0160 101 ARG A CB  
2620 N N   . HIS B 115 ? 0.4438 0.6009 0.4200 -0.2688 0.0363  -0.0069 102 HIS A N   
2621 C CA  . HIS B 115 ? 0.4121 0.6192 0.3966 -0.2874 0.0374  -0.0060 102 HIS A CA  
2622 C C   . HIS B 115 ? 0.4087 0.6178 0.3936 -0.2873 0.0420  0.0047  102 HIS A C   
2623 O O   . HIS B 115 ? 0.3756 0.5786 0.3651 -0.2634 0.0418  0.0112  102 HIS A O   
2624 C CB  . HIS B 115 ? 0.3896 0.6560 0.3924 -0.2741 0.0325  -0.0081 102 HIS A CB  
2625 C CG  . HIS B 115 ? 0.3676 0.6385 0.3801 -0.2405 0.0296  -0.0034 102 HIS A CG  
2626 N ND1 . HIS B 115 ? 0.3746 0.6280 0.3877 -0.2212 0.0260  -0.0066 102 HIS A ND1 
2627 C CD2 . HIS B 115 ? 0.3643 0.6570 0.3857 -0.2243 0.0303  0.0045  102 HIS A CD2 
2628 C CE1 . HIS B 115 ? 0.3171 0.5797 0.3384 -0.1965 0.0246  -0.0009 102 HIS A CE1 
2629 N NE2 . HIS B 115 ? 0.3262 0.6116 0.3524 -0.1968 0.0270  0.0055  102 HIS A NE2 
2630 N N   . ALA B 116 ? 0.4105 0.6318 0.3907 -0.3147 0.0461  0.0063  103 ALA A N   
2631 C CA  . ALA B 116 ? 0.4338 0.6603 0.4132 -0.3184 0.0512  0.0169  103 ALA A CA  
2632 C C   . ALA B 116 ? 0.3903 0.6776 0.3891 -0.3017 0.0493  0.0215  103 ALA A C   
2633 O O   . ALA B 116 ? 0.3749 0.7161 0.3856 -0.3066 0.0467  0.0174  103 ALA A O   
2634 C CB  . ALA B 116 ? 0.4536 0.6820 0.4229 -0.3554 0.0561  0.0169  103 ALA A CB  
2635 N N   . LEU B 117 ? 0.3876 0.6684 0.3882 -0.2830 0.0511  0.0301  104 LEU A N   
2636 C CA  . LEU B 117 ? 0.3869 0.7215 0.4031 -0.2664 0.0499  0.0344  104 LEU A CA  
2637 C C   . LEU B 117 ? 0.3815 0.7761 0.4055 -0.2871 0.0517  0.0348  104 LEU A C   
2638 O O   . LEU B 117 ? 0.3619 0.8129 0.4000 -0.2763 0.0486  0.0332  104 LEU A O   
2639 C CB  . LEU B 117 ? 0.4016 0.7127 0.4138 -0.2508 0.0529  0.0434  104 LEU A CB  
2640 C CG  . LEU B 117 ? 0.4162 0.7726 0.4420 -0.2280 0.0514  0.0472  104 LEU A CG  
2641 C CD1 . LEU B 117 ? 0.3708 0.6912 0.3929 -0.2031 0.0513  0.0515  104 LEU A CD1 
2642 C CD2 . LEU B 117 ? 0.3461 0.7535 0.3773 -0.2417 0.0552  0.0524  104 LEU A CD2 
2643 N N   . ALA B 118 ? 0.4226 0.8066 0.4363 -0.3175 0.0570  0.0375  105 ALA A N   
2644 C CA  . ALA B 118 ? 0.4322 0.8746 0.4531 -0.3376 0.0598  0.0400  105 ALA A CA  
2645 C C   . ALA B 118 ? 0.4151 0.9053 0.4454 -0.3495 0.0557  0.0304  105 ALA A C   
2646 O O   . ALA B 118 ? 0.4260 0.9801 0.4670 -0.3578 0.0562  0.0311  105 ALA A O   
2647 C CB  . ALA B 118 ? 0.4832 0.8988 0.4891 -0.3687 0.0671  0.0459  105 ALA A CB  
2648 N N   . ASP B 119 ? 0.4045 0.8669 0.4309 -0.3478 0.0516  0.0214  106 ASP A N   
2649 C CA  . ASP B 119 ? 0.4001 0.8953 0.4302 -0.3666 0.0485  0.0113  106 ASP A CA  
2650 C C   . ASP B 119 ? 0.3859 0.9148 0.4289 -0.3405 0.0417  0.0059  106 ASP A C   
2651 O O   . ASP B 119 ? 0.4165 0.9778 0.4634 -0.3529 0.0386  -0.0024 106 ASP A O   
2652 C CB  . ASP B 119 ? 0.4257 0.8646 0.4385 -0.3906 0.0495  0.0041  106 ASP A CB  
2653 C CG  . ASP B 119 ? 0.4543 0.8586 0.4511 -0.4206 0.0567  0.0091  106 ASP A CG  
2654 O OD1 . ASP B 119 ? 0.4807 0.9213 0.4823 -0.4318 0.0607  0.0165  106 ASP A OD1 
2655 O OD2 . ASP B 119 ? 0.5010 0.8413 0.4793 -0.4319 0.0585  0.0063  106 ASP A OD2 
2656 N N   . VAL B 120 ? 0.3393 0.8613 0.3880 -0.3053 0.0393  0.0103  107 VAL A N   
2657 C CA  . VAL B 120 ? 0.2822 0.8270 0.3400 -0.2786 0.0334  0.0067  107 VAL A CA  
2658 C C   . VAL B 120 ? 0.2716 0.8952 0.3433 -0.2722 0.0315  0.0071  107 VAL A C   
2659 O O   . VAL B 120 ? 0.2729 0.9276 0.3500 -0.2666 0.0341  0.0139  107 VAL A O   
2660 C CB  . VAL B 120 ? 0.2487 0.7563 0.3056 -0.2463 0.0328  0.0127  107 VAL A CB  
2661 C CG1 . VAL B 120 ? 0.2348 0.7718 0.3012 -0.2150 0.0280  0.0124  107 VAL A CG1 
2662 C CG2 . VAL B 120 ? 0.2792 0.7134 0.3231 -0.2476 0.0339  0.0119  107 VAL A CG2 
2663 N N   . SER B 121 ? 0.2357 0.8947 0.3125 -0.2731 0.0271  -0.0002 108 SER A N   
2664 C CA  . SER B 121 ? 0.2268 0.9641 0.3159 -0.2649 0.0248  -0.0006 108 SER A CA  
2665 C C   . SER B 121 ? 0.2151 0.9558 0.3083 -0.2238 0.0208  0.0024  108 SER A C   
2666 O O   . SER B 121 ? 0.2000 0.8854 0.2872 -0.2076 0.0196  0.0032  108 SER A O   
2667 C CB  . SER B 121 ? 0.2424 1.0168 0.3337 -0.2871 0.0219  -0.0103 108 SER A CB  
2668 O OG  . SER B 121 ? 0.2778 1.0174 0.3647 -0.2739 0.0178  -0.0153 108 SER A OG  
2669 N N   . VAL B 122 ? 0.2251 1.0324 0.3276 -0.2076 0.0189  0.0039  109 VAL A N   
2670 C CA  . VAL B 122 ? 0.2126 1.0210 0.3161 -0.1683 0.0154  0.0070  109 VAL A CA  
2671 C C   . VAL B 122 ? 0.2289 1.0171 0.3290 -0.1618 0.0111  0.0017  109 VAL A C   
2672 O O   . VAL B 122 ? 0.2543 1.0016 0.3497 -0.1375 0.0095  0.0043  109 VAL A O   
2673 C CB  . VAL B 122 ? 0.2015 1.0833 0.3129 -0.1491 0.0144  0.0099  109 VAL A CB  
2674 C CG1 . VAL B 122 ? 0.1886 1.0656 0.2976 -0.1082 0.0110  0.0131  109 VAL A CG1 
2675 C CG2 . VAL B 122 ? 0.2208 1.1202 0.3349 -0.1532 0.0190  0.0156  109 VAL A CG2 
2676 N N   . GLU B 123 ? 0.2295 1.0472 0.3315 -0.1845 0.0093  -0.0058 110 GLU A N   
2677 C CA  . GLU B 123 ? 0.2221 1.0273 0.3209 -0.1802 0.0051  -0.0115 110 GLU A CA  
2678 C C   . GLU B 123 ? 0.2286 0.9549 0.3179 -0.1848 0.0059  -0.0129 110 GLU A C   
2679 O O   . GLU B 123 ? 0.2089 0.9081 0.2948 -0.1640 0.0034  -0.0121 110 GLU A O   
2680 C CB  . GLU B 123 ? 0.2376 1.0962 0.3403 -0.2028 0.0026  -0.0202 110 GLU A CB  
2681 C CG  . GLU B 123 ? 0.2366 1.1805 0.3492 -0.1979 0.0018  -0.0189 110 GLU A CG  
2682 C CD  . GLU B 123 ? 0.2961 1.2755 0.4140 -0.2253 0.0059  -0.0186 110 GLU A CD  
2683 O OE1 . GLU B 123 ? 0.3338 1.2712 0.4471 -0.2494 0.0103  -0.0178 110 GLU A OE1 
2684 O OE2 . GLU B 123 ? 0.3531 1.4075 0.4794 -0.2219 0.0048  -0.0184 110 GLU A OE2 
2685 N N   . TYR B 124 ? 0.2636 0.9526 0.3479 -0.2095 0.0098  -0.0138 111 TYR A N   
2686 C CA  . TYR B 124 ? 0.2960 0.9114 0.3703 -0.2126 0.0111  -0.0146 111 TYR A CA  
2687 C C   . TYR B 124 ? 0.2946 0.8740 0.3676 -0.1810 0.0111  -0.0071 111 TYR A C   
2688 O O   . TYR B 124 ? 0.2816 0.8236 0.3500 -0.1682 0.0091  -0.0081 111 TYR A O   
2689 C CB  . TYR B 124 ? 0.3175 0.9007 0.3849 -0.2414 0.0158  -0.0150 111 TYR A CB  
2690 C CG  . TYR B 124 ? 0.3986 0.9099 0.4538 -0.2458 0.0167  -0.0177 111 TYR A CG  
2691 C CD1 . TYR B 124 ? 0.4295 0.9236 0.4771 -0.2642 0.0152  -0.0273 111 TYR A CD1 
2692 C CD2 . TYR B 124 ? 0.3725 0.8354 0.4232 -0.2293 0.0187  -0.0111 111 TYR A CD2 
2693 C CE1 . TYR B 124 ? 0.4770 0.9073 0.5125 -0.2649 0.0159  -0.0300 111 TYR A CE1 
2694 C CE2 . TYR B 124 ? 0.3877 0.7898 0.4274 -0.2308 0.0194  -0.0134 111 TYR A CE2 
2695 C CZ  . TYR B 124 ? 0.4840 0.8694 0.5157 -0.2485 0.0182  -0.0227 111 TYR A CZ  
2696 O OH  . TYR B 124 ? 0.4630 0.7886 0.4828 -0.2471 0.0191  -0.0245 111 TYR A OH  
2697 N N   . TRP B 125 ? 0.2482 0.8421 0.3252 -0.1696 0.0133  0.0000  112 TRP A N   
2698 C CA  . TRP B 125 ? 0.2652 0.8308 0.3409 -0.1413 0.0135  0.0065  112 TRP A CA  
2699 C C   . TRP B 125 ? 0.2351 0.8041 0.3109 -0.1154 0.0094  0.0065  112 TRP A C   
2700 O O   . TRP B 125 ? 0.2090 0.7321 0.2796 -0.1031 0.0086  0.0075  112 TRP A O   
2701 C CB  . TRP B 125 ? 0.2183 0.8179 0.2991 -0.1324 0.0158  0.0125  112 TRP A CB  
2702 C CG  . TRP B 125 ? 0.2407 0.8183 0.3196 -0.1018 0.0154  0.0179  112 TRP A CG  
2703 C CD1 . TRP B 125 ? 0.2249 0.8155 0.3039 -0.0730 0.0124  0.0197  112 TRP A CD1 
2704 C CD2 . TRP B 125 ? 0.1873 0.7162 0.2613 -0.0977 0.0179  0.0215  112 TRP A CD2 
2705 N NE1 . TRP B 125 ? 0.1854 0.7392 0.2600 -0.0535 0.0132  0.0237  112 TRP A NE1 
2706 C CE2 . TRP B 125 ? 0.1934 0.7121 0.2657 -0.0678 0.0163  0.0245  112 TRP A CE2 
2707 C CE3 . TRP B 125 ? 0.2321 0.7269 0.3018 -0.1158 0.0215  0.0226  112 TRP A CE3 
2708 C CZ2 . TRP B 125 ? 0.2462 0.7227 0.3140 -0.0575 0.0177  0.0275  112 TRP A CZ2 
2709 C CZ3 . TRP B 125 ? 0.2263 0.6817 0.2917 -0.1035 0.0230  0.0264  112 TRP A CZ3 
2710 C CH2 . TRP B 125 ? 0.2106 0.6569 0.2756 -0.0753 0.0208  0.0282  112 TRP A CH2 
2711 N N   . ASP B 126 ? 0.1971 0.8222 0.2781 -0.1076 0.0069  0.0057  113 ASP A N   
2712 C CA  . ASP B 126 ? 0.2146 0.8490 0.2944 -0.0814 0.0033  0.0071  113 ASP A CA  
2713 C C   . ASP B 126 ? 0.2488 0.8464 0.3235 -0.0867 0.0014  0.0028  113 ASP A C   
2714 O O   . ASP B 126 ? 0.2560 0.8204 0.3257 -0.0673 0.0003  0.0058  113 ASP A O   
2715 C CB  . ASP B 126 ? 0.2029 0.9073 0.2881 -0.0738 0.0010  0.0066  113 ASP A CB  
2716 C CG  . ASP B 126 ? 0.2166 0.9602 0.3057 -0.0584 0.0024  0.0119  113 ASP A CG  
2717 O OD1 . ASP B 126 ? 0.2450 0.9580 0.3318 -0.0509 0.0050  0.0161  113 ASP A OD1 
2718 O OD2 . ASP B 126 ? 0.2568 1.0617 0.3503 -0.0517 0.0009  0.0117  113 ASP A OD2 
2719 N N   . GLU B 127 ? 0.2253 0.8290 0.3002 -0.1137 0.0011  -0.0045 114 GLU A N   
2720 C CA  . GLU B 127 ? 0.2371 0.8124 0.3068 -0.1194 -0.0009 -0.0099 114 GLU A CA  
2721 C C   . GLU B 127 ? 0.2478 0.7560 0.3108 -0.1158 0.0009  -0.0081 114 GLU A C   
2722 O O   . GLU B 127 ? 0.2370 0.7190 0.2959 -0.1019 -0.0007 -0.0074 114 GLU A O   
2723 C CB  . GLU B 127 ? 0.2843 0.8845 0.3546 -0.1487 -0.0017 -0.0192 114 GLU A CB  
2724 C CG  . GLU B 127 ? 0.3848 0.9580 0.4486 -0.1560 -0.0038 -0.0264 114 GLU A CG  
2725 C CD  . GLU B 127 ? 0.4783 0.9869 0.5334 -0.1674 -0.0015 -0.0290 114 GLU A CD  
2726 O OE1 . GLU B 127 ? 0.5714 1.0517 0.6211 -0.1610 -0.0031 -0.0318 114 GLU A OE1 
2727 O OE2 . GLU B 127 ? 0.5195 1.0073 0.5726 -0.1819 0.0020  -0.0281 114 GLU A OE2 
2728 N N   . ARG B 128 ? 0.2341 0.7155 0.2955 -0.1273 0.0044  -0.0067 115 ARG A N   
2729 C CA  . ARG B 128 ? 0.2558 0.6781 0.3109 -0.1230 0.0061  -0.0048 115 ARG A CA  
2730 C C   . ARG B 128 ? 0.2684 0.6755 0.3238 -0.0947 0.0057  0.0021  115 ARG A C   
2731 O O   . ARG B 128 ? 0.2194 0.5883 0.2701 -0.0865 0.0052  0.0024  115 ARG A O   
2732 C CB  . ARG B 128 ? 0.3163 0.7148 0.3686 -0.1385 0.0102  -0.0034 115 ARG A CB  
2733 C CG  . ARG B 128 ? 0.3323 0.7289 0.3803 -0.1689 0.0119  -0.0096 115 ARG A CG  
2734 C CD  . ARG B 128 ? 0.4070 0.7545 0.4447 -0.1780 0.0121  -0.0150 115 ARG A CD  
2735 N NE  . ARG B 128 ? 0.4269 0.7795 0.4633 -0.1755 0.0085  -0.0214 115 ARG A NE  
2736 C CZ  . ARG B 128 ? 0.5271 0.8678 0.5562 -0.1949 0.0080  -0.0302 115 ARG A CZ  
2737 N NH1 . ARG B 128 ? 0.6137 0.9248 0.6335 -0.2160 0.0113  -0.0330 115 ARG A NH1 
2738 N NH2 . ARG B 128 ? 0.5303 0.8853 0.5593 -0.1926 0.0045  -0.0362 115 ARG A NH2 
2739 N N   . MET B 129 ? 0.2206 0.6576 0.2803 -0.0794 0.0057  0.0073  116 MET A N   
2740 C CA  . MET B 129 ? 0.2152 0.6357 0.2727 -0.0527 0.0052  0.0130  116 MET A CA  
2741 C C   . MET B 129 ? 0.2463 0.6659 0.3007 -0.0391 0.0023  0.0130  116 MET A C   
2742 O O   . MET B 129 ? 0.2360 0.6213 0.2855 -0.0252 0.0021  0.0159  116 MET A O   
2743 C CB  . MET B 129 ? 0.2120 0.6632 0.2725 -0.0375 0.0059  0.0177  116 MET A CB  
2744 C CG  . MET B 129 ? 0.1965 0.6434 0.2589 -0.0490 0.0092  0.0190  116 MET A CG  
2745 S SD  . MET B 129 ? 0.3844 0.7660 0.4407 -0.0437 0.0108  0.0207  116 MET A SD  
2746 C CE  . MET B 129 ? 0.2020 0.5740 0.2581 -0.0743 0.0136  0.0176  116 MET A CE  
2747 N N   . GLN B 130 ? 0.2158 0.6727 0.2726 -0.0450 0.0002  0.0097  117 GLN A N   
2748 C CA  . GLN B 130 ? 0.2708 0.7333 0.3243 -0.0319 -0.0024 0.0104  117 GLN A CA  
2749 C C   . GLN B 130 ? 0.2645 0.6880 0.3135 -0.0401 -0.0028 0.0069  117 GLN A C   
2750 O O   . GLN B 130 ? 0.2281 0.6347 0.2723 -0.0248 -0.0037 0.0103  117 GLN A O   
2751 C CB  . GLN B 130 ? 0.2718 0.7928 0.3290 -0.0312 -0.0048 0.0088  117 GLN A CB  
2752 C CG  . GLN B 130 ? 0.3235 0.8806 0.3830 -0.0139 -0.0044 0.0140  117 GLN A CG  
2753 C CD  . GLN B 130 ? 0.3068 0.9293 0.3717 -0.0172 -0.0064 0.0114  117 GLN A CD  
2754 O OE1 . GLN B 130 ? 0.3876 1.0281 0.4541 -0.0325 -0.0083 0.0055  117 GLN A OE1 
2755 N NE2 . GLN B 130 ? 0.3086 0.9682 0.3756 -0.0026 -0.0060 0.0154  117 GLN A NE2 
2756 N N   . THR B 131 ? 0.2510 0.6610 0.3003 -0.0634 -0.0019 0.0003  118 THR A N   
2757 C CA  . THR B 131 ? 0.2519 0.6279 0.2960 -0.0706 -0.0022 -0.0041 118 THR A CA  
2758 C C   . THR B 131 ? 0.2489 0.5755 0.2894 -0.0651 -0.0001 -0.0009 118 THR A C   
2759 O O   . THR B 131 ? 0.2353 0.5331 0.2712 -0.0626 -0.0003 -0.0021 118 THR A O   
2760 C CB  . THR B 131 ? 0.2770 0.6575 0.3198 -0.0961 -0.0024 -0.0133 118 THR A CB  
2761 O OG1 . THR B 131 ? 0.3033 0.6765 0.3474 -0.1085 0.0004  -0.0129 118 THR A OG1 
2762 C CG2 . THR B 131 ? 0.2468 0.6782 0.2932 -0.1060 -0.0047 -0.0182 118 THR A CG2 
2763 N N   . ASN B 132 ? 0.2269 0.5459 0.2694 -0.0630 0.0021  0.0029  119 ASN A N   
2764 C CA  . ASN B 132 ? 0.2243 0.5011 0.2638 -0.0587 0.0041  0.0053  119 ASN A CA  
2765 C C   . ASN B 132 ? 0.2487 0.5167 0.2876 -0.0372 0.0040  0.0118  119 ASN A C   
2766 O O   . ASN B 132 ? 0.2527 0.4876 0.2885 -0.0323 0.0048  0.0131  119 ASN A O   
2767 C CB  . ASN B 132 ? 0.2654 0.5308 0.3049 -0.0721 0.0068  0.0046  119 ASN A CB  
2768 C CG  . ASN B 132 ? 0.2965 0.5467 0.3313 -0.0930 0.0077  -0.0019 119 ASN A CG  
2769 O OD1 . ASN B 132 ? 0.3293 0.5486 0.3585 -0.0936 0.0078  -0.0046 119 ASN A OD1 
2770 N ND2 . ASN B 132 ? 0.3137 0.5826 0.3493 -0.1106 0.0089  -0.0044 119 ASN A ND2 
2771 N N   . LEU B 133 ? 0.1965 0.4925 0.2372 -0.0239 0.0032  0.0157  120 LEU A N   
2772 C CA  . LEU B 133 ? 0.1916 0.4729 0.2293 -0.0052 0.0036  0.0211  120 LEU A CA  
2773 C C   . LEU B 133 ? 0.1640 0.4592 0.1978 0.0126  0.0019  0.0250  120 LEU A C   
2774 O O   . LEU B 133 ? 0.1766 0.4460 0.2045 0.0238  0.0019  0.0283  120 LEU A O   
2775 C CB  . LEU B 133 ? 0.1752 0.4697 0.2158 -0.0026 0.0051  0.0228  120 LEU A CB  
2776 C CG  . LEU B 133 ? 0.1881 0.4773 0.2242 0.0194  0.0051  0.0275  120 LEU A CG  
2777 C CD1 . LEU B 133 ? 0.2090 0.4525 0.2402 0.0230  0.0058  0.0281  120 LEU A CD1 
2778 C CD2 . LEU B 133 ? 0.1766 0.4866 0.2157 0.0220  0.0064  0.0284  120 LEU A CD2 
2779 N N   . ARG B 134 ? 0.2010 0.5387 0.2371 0.0154  0.0005  0.0251  121 ARG A N   
2780 C CA  . ARG B 134 ? 0.2052 0.5599 0.2359 0.0367  -0.0008 0.0301  121 ARG A CA  
2781 C C   . ARG B 134 ? 0.2049 0.5377 0.2289 0.0422  -0.0016 0.0324  121 ARG A C   
2782 O O   . ARG B 134 ? 0.2022 0.5210 0.2175 0.0606  -0.0014 0.0383  121 ARG A O   
2783 C CB  . ARG B 134 ? 0.2089 0.6186 0.2440 0.0366  -0.0024 0.0289  121 ARG A CB  
2784 C CG  . ARG B 134 ? 0.2017 0.6324 0.2299 0.0613  -0.0037 0.0347  121 ARG A CG  
2785 C CD  . ARG B 134 ? 0.2032 0.6932 0.2368 0.0620  -0.0052 0.0332  121 ARG A CD  
2786 N NE  . ARG B 134 ? 0.2174 0.7324 0.2545 0.0488  -0.0073 0.0289  121 ARG A NE  
2787 C CZ  . ARG B 134 ? 0.2316 0.8032 0.2737 0.0468  -0.0091 0.0265  121 ARG A CZ  
2788 N NH1 . ARG B 134 ? 0.2354 0.8413 0.2782 0.0614  -0.0089 0.0296  121 ARG A NH1 
2789 N NH2 . ARG B 134 ? 0.2393 0.8324 0.2849 0.0306  -0.0111 0.0207  121 ARG A NH2 
2790 N N   . HIS B 135 ? 0.2126 0.5450 0.2393 0.0267  -0.0024 0.0277  122 HIS A N   
2791 C CA  . HIS B 135 ? 0.2218 0.5404 0.2424 0.0319  -0.0031 0.0300  122 HIS A CA  
2792 C C   . HIS B 135 ? 0.2101 0.4831 0.2247 0.0379  -0.0013 0.0339  122 HIS A C   
2793 O O   . HIS B 135 ? 0.2076 0.4674 0.2142 0.0490  -0.0011 0.0394  122 HIS A O   
2794 C CB  . HIS B 135 ? 0.2162 0.5415 0.2400 0.0144  -0.0042 0.0232  122 HIS A CB  
2795 C CG  . HIS B 135 ? 0.2304 0.5297 0.2575 -0.0028 -0.0028 0.0175  122 HIS A CG  
2796 N ND1 . HIS B 135 ? 0.2295 0.4913 0.2534 -0.0037 -0.0016 0.0179  122 HIS A ND1 
2797 C CD2 . HIS B 135 ? 0.2247 0.5296 0.2568 -0.0193 -0.0023 0.0118  122 HIS A CD2 
2798 C CE1 . HIS B 135 ? 0.2287 0.4742 0.2551 -0.0183 -0.0005 0.0125  122 HIS A CE1 
2799 N NE2 . HIS B 135 ? 0.2153 0.4843 0.2459 -0.0285 -0.0008 0.0088  122 HIS A NE2 
2800 N N   . ALA B 136 ? 0.2074 0.4573 0.2250 0.0309  0.0002  0.0317  123 ALA A N   
2801 C CA  . ALA B 136 ? 0.1938 0.4033 0.2067 0.0335  0.0018  0.0340  123 ALA A CA  
2802 C C   . ALA B 136 ? 0.2322 0.4314 0.2364 0.0524  0.0023  0.0407  123 ALA A C   
2803 O O   . ALA B 136 ? 0.2674 0.4414 0.2636 0.0584  0.0032  0.0449  123 ALA A O   
2804 C CB  . ALA B 136 ? 0.1861 0.3772 0.2038 0.0227  0.0030  0.0300  123 ALA A CB  
2805 N N   . PHE B 137 ? 0.2031 0.4236 0.2071 0.0629  0.0020  0.0420  124 PHE A N   
2806 C CA  . PHE B 137 ? 0.2285 0.4378 0.2214 0.0831  0.0025  0.0478  124 PHE A CA  
2807 C C   . PHE B 137 ? 0.2257 0.4410 0.2096 0.0949  0.0019  0.0537  124 PHE A C   
2808 O O   . PHE B 137 ? 0.2650 0.4516 0.2368 0.1052  0.0031  0.0592  124 PHE A O   
2809 C CB  . PHE B 137 ? 0.2024 0.4366 0.1961 0.0942  0.0023  0.0477  124 PHE A CB  
2810 C CG  . PHE B 137 ? 0.2431 0.4664 0.2223 0.1183  0.0027  0.0538  124 PHE A CG  
2811 C CD1 . PHE B 137 ? 0.3054 0.4871 0.2746 0.1249  0.0042  0.0552  124 PHE A CD1 
2812 C CD2 . PHE B 137 ? 0.2835 0.5366 0.2571 0.1345  0.0017  0.0580  124 PHE A CD2 
2813 C CE1 . PHE B 137 ? 0.3575 0.5214 0.3099 0.1464  0.0049  0.0605  124 PHE A CE1 
2814 C CE2 . PHE B 137 ? 0.3583 0.5956 0.3149 0.1587  0.0024  0.0644  124 PHE A CE2 
2815 C CZ  . PHE B 137 ? 0.3602 0.5508 0.3056 0.1644  0.0041  0.0654  124 PHE A CZ  
2816 N N   . PHE B 138 ? 0.2160 0.4697 0.2049 0.0927  0.0002  0.0525  125 PHE A N   
2817 C CA  . PHE B 138 ? 0.2259 0.4912 0.2055 0.1069  -0.0004 0.0587  125 PHE A CA  
2818 C C   . PHE B 138 ? 0.2252 0.4641 0.2003 0.1002  0.0004  0.0610  125 PHE A C   
2819 O O   . PHE B 138 ? 0.2567 0.4848 0.2190 0.1143  0.0012  0.0688  125 PHE A O   
2820 C CB  . PHE B 138 ? 0.2398 0.5577 0.2236 0.1107  -0.0027 0.0578  125 PHE A CB  
2821 C CG  . PHE B 138 ? 0.2458 0.5878 0.2285 0.1257  -0.0030 0.0589  125 PHE A CG  
2822 C CD1 . PHE B 138 ? 0.2502 0.5845 0.2180 0.1516  -0.0023 0.0667  125 PHE A CD1 
2823 C CD2 . PHE B 138 ? 0.2363 0.6011 0.2311 0.1138  -0.0033 0.0526  125 PHE A CD2 
2824 C CE1 . PHE B 138 ? 0.2823 0.6399 0.2480 0.1677  -0.0025 0.0674  125 PHE A CE1 
2825 C CE2 . PHE B 138 ? 0.2509 0.6391 0.2446 0.1283  -0.0032 0.0538  125 PHE A CE2 
2826 C CZ  . PHE B 138 ? 0.2869 0.6720 0.2662 0.1560  -0.0029 0.0609  125 PHE A CZ  
2827 N N   . ALA B 139 ? 0.2257 0.4549 0.2100 0.0803  0.0005  0.0548  126 ALA A N   
2828 C CA  . ALA B 139 ? 0.2149 0.4217 0.1951 0.0747  0.0015  0.0568  126 ALA A CA  
2829 C C   . ALA B 139 ? 0.2573 0.4224 0.2273 0.0810  0.0039  0.0625  126 ALA A C   
2830 O O   . ALA B 139 ? 0.3057 0.4547 0.2664 0.0846  0.0053  0.0686  126 ALA A O   
2831 C CB  . ALA B 139 ? 0.2134 0.4194 0.2038 0.0548  0.0011  0.0488  126 ALA A CB  
2832 N N   . ALA B 140 ? 0.2692 0.4173 0.2409 0.0805  0.0046  0.0600  127 ALA A N   
2833 C CA  . ALA B 140 ? 0.2874 0.3956 0.2491 0.0843  0.0068  0.0638  127 ALA A CA  
2834 C C   . ALA B 140 ? 0.2960 0.3968 0.2416 0.1042  0.0076  0.0723  127 ALA A C   
2835 O O   . ALA B 140 ? 0.3464 0.4172 0.2790 0.1080  0.0096  0.0784  127 ALA A O   
2836 C CB  . ALA B 140 ? 0.2567 0.3533 0.2232 0.0809  0.0069  0.0586  127 ALA A CB  
2837 N N   . GLN B 141 ? 0.2908 0.4200 0.2359 0.1177  0.0061  0.0730  128 GLN A N   
2838 C CA  . GLN B 141 ? 0.3010 0.4223 0.2288 0.1401  0.0069  0.0811  128 GLN A CA  
2839 C C   . GLN B 141 ? 0.3597 0.4814 0.2783 0.1444  0.0076  0.0888  128 GLN A C   
2840 O O   . GLN B 141 ? 0.3827 0.4747 0.2830 0.1568  0.0098  0.0972  128 GLN A O   
2841 C CB  . GLN B 141 ? 0.3205 0.4795 0.2507 0.1545  0.0052  0.0798  128 GLN A CB  
2842 C CG  . GLN B 141 ? 0.3766 0.5323 0.2874 0.1818  0.0058  0.0884  128 GLN A CG  
2843 C CD  . GLN B 141 ? 0.3701 0.5759 0.2857 0.1952  0.0037  0.0871  128 GLN A CD  
2844 O OE1 . GLN B 141 ? 0.3600 0.6094 0.2855 0.1907  0.0017  0.0857  128 GLN A OE1 
2845 N NE2 . GLN B 141 ? 0.3778 0.5798 0.2860 0.2116  0.0041  0.0871  128 GLN A NE2 
2846 N N   . ALA B 142 ? 0.3282 0.4808 0.2585 0.1331  0.0060  0.0856  129 ALA A N   
2847 C CA  . ALA B 142 ? 0.3417 0.5002 0.2648 0.1360  0.0064  0.0921  129 ALA A CA  
2848 C C   . ALA B 142 ? 0.3421 0.4620 0.2580 0.1268  0.0092  0.0965  129 ALA A C   
2849 O O   . ALA B 142 ? 0.3832 0.4897 0.2840 0.1359  0.0111  0.1062  129 ALA A O   
2850 C CB  . ALA B 142 ? 0.3253 0.5273 0.2623 0.1259  0.0037  0.0860  129 ALA A CB  
2851 N N   . VAL B 143 ? 0.3420 0.4473 0.2685 0.1082  0.0096  0.0896  130 VAL A N   
2852 C CA  . VAL B 143 ? 0.3291 0.4037 0.2505 0.0979  0.0123  0.0929  130 VAL A CA  
2853 C C   . VAL B 143 ? 0.3708 0.4015 0.2765 0.1036  0.0151  0.0986  130 VAL A C   
2854 O O   . VAL B 143 ? 0.3917 0.3974 0.2867 0.0998  0.0179  0.1052  130 VAL A O   
2855 C CB  . VAL B 143 ? 0.3044 0.3815 0.2412 0.0776  0.0117  0.0839  130 VAL A CB  
2856 C CG1 . VAL B 143 ? 0.2793 0.3944 0.2275 0.0720  0.0093  0.0784  130 VAL A CG1 
2857 C CG2 . VAL B 143 ? 0.2872 0.3496 0.2303 0.0727  0.0115  0.0773  130 VAL A CG2 
2858 N N   . ALA B 144 ? 0.3752 0.3967 0.2787 0.1121  0.0145  0.0960  131 ALA A N   
2859 C CA  . ALA B 144 ? 0.4289 0.4058 0.3169 0.1156  0.0170  0.0992  131 ALA A CA  
2860 C C   . ALA B 144 ? 0.4479 0.3961 0.3128 0.1264  0.0201  0.1111  131 ALA A C   
2861 O O   . ALA B 144 ? 0.4780 0.3896 0.3333 0.1168  0.0230  0.1138  131 ALA A O   
2862 C CB  . ALA B 144 ? 0.4522 0.4233 0.3385 0.1261  0.0160  0.0946  131 ALA A CB  
2863 N N   . PRO B 145 ? 0.4825 0.4407 0.3346 0.1470  0.0201  0.1191  132 PRO A N   
2864 C CA  . PRO B 145 ? 0.5240 0.4448 0.3501 0.1580  0.0237  0.1311  132 PRO A CA  
2865 C C   . PRO B 145 ? 0.5177 0.4240 0.3409 0.1416  0.0266  0.1368  132 PRO A C   
2866 O O   . PRO B 145 ? 0.5719 0.4337 0.3770 0.1382  0.0303  0.1430  132 PRO A O   
2867 C CB  . PRO B 145 ? 0.5275 0.4722 0.3434 0.1839  0.0227  0.1381  132 PRO A CB  
2868 C CG  . PRO B 145 ? 0.4727 0.4597 0.3083 0.1866  0.0186  0.1276  132 PRO A CG  
2869 C CD  . PRO B 145 ? 0.4846 0.4876 0.3440 0.1614  0.0170  0.1175  132 PRO A CD  
2870 N N   . GLY B 146 ? 0.5302 0.4736 0.3711 0.1300  0.0249  0.1336  133 GLY A N   
2871 C CA  . GLY B 146 ? 0.4710 0.4110 0.3126 0.1143  0.0273  0.1377  133 GLY A CA  
2872 C C   . GLY B 146 ? 0.4756 0.3885 0.3217 0.0929  0.0292  0.1329  133 GLY A C   
2873 O O   . GLY B 146 ? 0.5222 0.4044 0.3547 0.0843  0.0331  0.1402  133 GLY A O   
2874 N N   . MET B 147 ? 0.4545 0.3755 0.3166 0.0861  0.0265  0.1211  134 MET A N   
2875 C CA  . MET B 147 ? 0.4394 0.3387 0.3064 0.0683  0.0276  0.1151  134 MET A CA  
2876 C C   . MET B 147 ? 0.4531 0.3037 0.2981 0.0708  0.0308  0.1206  134 MET A C   
2877 O O   . MET B 147 ? 0.5507 0.3787 0.3909 0.0550  0.0336  0.1221  134 MET A O   
2878 C CB  . MET B 147 ? 0.3794 0.2957 0.2649 0.0640  0.0243  0.1027  134 MET A CB  
2879 C CG  . MET B 147 ? 0.3625 0.3157 0.2675 0.0542  0.0222  0.0967  134 MET A CG  
2880 S SD  . MET B 147 ? 0.3601 0.3330 0.2843 0.0508  0.0187  0.0838  134 MET A SD  
2881 C CE  . MET B 147 ? 0.3004 0.3081 0.2401 0.0402  0.0173  0.0793  134 MET A CE  
2882 N N   . ALA B 148 ? 0.5055 0.3406 0.3379 0.0891  0.0302  0.1219  135 ALA A N   
2883 C CA  . ALA B 148 ? 0.5331 0.3178 0.3424 0.0932  0.0331  0.1255  135 ALA A CA  
2884 C C   . ALA B 148 ? 0.5826 0.3347 0.3686 0.0926  0.0377  0.1386  135 ALA A C   
2885 O O   . ALA B 148 ? 0.6190 0.3277 0.3896 0.0822  0.0408  0.1399  135 ALA A O   
2886 C CB  . ALA B 148 ? 0.5640 0.3425 0.3631 0.1170  0.0315  0.1246  135 ALA A CB  
2887 N N   . ARG B 149 ? 0.5913 0.3613 0.3720 0.1044  0.0383  0.1483  136 ARG A N   
2888 C CA  . ARG B 149 ? 0.6365 0.3802 0.3953 0.1041  0.0430  0.1624  136 ARG A CA  
2889 C C   . ARG B 149 ? 0.6515 0.3858 0.4160 0.0756  0.0457  0.1616  136 ARG A C   
2890 O O   . ARG B 149 ? 0.7255 0.4162 0.4693 0.0670  0.0502  0.1687  136 ARG A O   
2891 C CB  . ARG B 149 ? 0.6047 0.3831 0.3646 0.1152  0.0427  0.1711  136 ARG A CB  
2892 N N   . ARG B 150 ? 0.6076 0.3833 0.3996 0.0613  0.0430  0.1524  137 ARG A N   
2893 C CA  . ARG B 150 ? 0.6123 0.3877 0.4116 0.0360  0.0452  0.1510  137 ARG A CA  
2894 C C   . ARG B 150 ? 0.6270 0.3748 0.4265 0.0210  0.0456  0.1426  137 ARG A C   
2895 O O   . ARG B 150 ? 0.6337 0.3616 0.4271 0.0015  0.0490  0.1446  137 ARG A O   
2896 C CB  . ARG B 150 ? 0.5878 0.4148 0.4123 0.0289  0.0426  0.1452  137 ARG A CB  
2897 C CG  . ARG B 150 ? 0.5379 0.3727 0.3742 0.0046  0.0440  0.1406  137 ARG A CG  
2898 C CD  . ARG B 150 ? 0.4705 0.3523 0.3267 0.0004  0.0421  0.1364  137 ARG A CD  
2899 N NE  . ARG B 150 ? 0.5090 0.4125 0.3828 0.0069  0.0371  0.1242  137 ARG A NE  
2900 C CZ  . ARG B 150 ? 0.5085 0.4417 0.3920 0.0189  0.0336  0.1205  137 ARG A CZ  
2901 N NH1 . ARG B 150 ? 0.4595 0.4183 0.3440 0.0225  0.0337  0.1248  137 ARG A NH1 
2902 N NH2 . ARG B 150 ? 0.4206 0.3614 0.3148 0.0243  0.0300  0.1111  137 ARG A NH2 
2903 N N   . GLY B 151 ? 0.5734 0.3220 0.3802 0.0291  0.0421  0.1326  138 GLY A N   
2904 C CA  . GLY B 151 ? 0.5632 0.2900 0.3711 0.0157  0.0419  0.1235  138 GLY A CA  
2905 C C   . GLY B 151 ? 0.5082 0.2721 0.3438 0.0029  0.0386  0.1114  138 GLY A C   
2906 O O   . GLY B 151 ? 0.5302 0.2824 0.3686 -0.0117 0.0387  0.1042  138 GLY A O   
2907 N N   . SER B 152 ? 0.4498 0.2564 0.3038 0.0076  0.0360  0.1094  139 SER A N   
2908 C CA  . SER B 152 ? 0.4304 0.2685 0.3079 -0.0035 0.0334  0.0987  139 SER A CA  
2909 C C   . SER B 152 ? 0.3888 0.2645 0.2812 0.0076  0.0301  0.0958  139 SER A C   
2910 O O   . SER B 152 ? 0.4215 0.3070 0.3085 0.0186  0.0303  0.1029  139 SER A O   
2911 C CB  . SER B 152 ? 0.4498 0.2974 0.3321 -0.0232 0.0359  0.1001  139 SER A CB  
2912 O OG  . SER B 152 ? 0.4567 0.3277 0.3413 -0.0203 0.0367  0.1066  139 SER A OG  
2913 N N   . GLY B 153 ? 0.3570 0.2539 0.2672 0.0041  0.0271  0.0854  140 GLY A N   
2914 C CA  . GLY B 153 ? 0.3355 0.2670 0.2597 0.0106  0.0243  0.0817  140 GLY A CA  
2915 C C   . GLY B 153 ? 0.3024 0.2452 0.2414 0.0071  0.0216  0.0709  140 GLY A C   
2916 O O   . GLY B 153 ? 0.3377 0.2627 0.2747 0.0040  0.0217  0.0672  140 GLY A O   
2917 N N   . ALA B 154 ? 0.3000 0.2709 0.2518 0.0080  0.0195  0.0662  141 ALA A N   
2918 C CA  . ALA B 154 ? 0.2609 0.2414 0.2252 0.0044  0.0175  0.0571  141 ALA A CA  
2919 C C   . ALA B 154 ? 0.2633 0.2664 0.2349 0.0112  0.0152  0.0542  141 ALA A C   
2920 O O   . ALA B 154 ? 0.2655 0.2854 0.2378 0.0129  0.0148  0.0563  141 ALA A O   
2921 C CB  . ALA B 154 ? 0.2768 0.2662 0.2492 -0.0076 0.0181  0.0529  141 ALA A CB  
2922 N N   . ILE B 155 ? 0.2585 0.2634 0.2357 0.0135  0.0137  0.0490  142 ILE A N   
2923 C CA  . ILE B 155 ? 0.2411 0.2674 0.2253 0.0174  0.0117  0.0458  142 ILE A CA  
2924 C C   . ILE B 155 ? 0.1914 0.2218 0.1850 0.0105  0.0110  0.0386  142 ILE A C   
2925 O O   . ILE B 155 ? 0.2245 0.2416 0.2182 0.0087  0.0114  0.0367  142 ILE A O   
2926 C CB  . ILE B 155 ? 0.2516 0.2783 0.2305 0.0295  0.0110  0.0485  142 ILE A CB  
2927 C CG1 . ILE B 155 ? 0.2998 0.3213 0.2668 0.0387  0.0120  0.0567  142 ILE A CG1 
2928 C CG2 . ILE B 155 ? 0.2528 0.3049 0.2402 0.0309  0.0092  0.0445  142 ILE A CG2 
2929 C CD1 . ILE B 155 ? 0.3119 0.3320 0.2710 0.0538  0.0115  0.0598  142 ILE A CD1 
2930 N N   . ILE B 156 ? 0.2012 0.2484 0.2013 0.0067  0.0100  0.0348  143 ILE A N   
2931 C CA  . ILE B 156 ? 0.1844 0.2330 0.1910 0.0011  0.0097  0.0287  143 ILE A CA  
2932 C C   . ILE B 156 ? 0.1785 0.2423 0.1886 0.0018  0.0085  0.0265  143 ILE A C   
2933 O O   . ILE B 156 ? 0.1812 0.2591 0.1913 0.0008  0.0078  0.0262  143 ILE A O   
2934 C CB  . ILE B 156 ? 0.1895 0.2410 0.1981 -0.0053 0.0101  0.0253  143 ILE A CB  
2935 C CG1 . ILE B 156 ? 0.1795 0.2214 0.1857 -0.0076 0.0115  0.0275  143 ILE A CG1 
2936 C CG2 . ILE B 156 ? 0.1682 0.2189 0.1809 -0.0091 0.0099  0.0195  143 ILE A CG2 
2937 C CD1 . ILE B 156 ? 0.2056 0.2546 0.2123 -0.0117 0.0121  0.0256  143 ILE A CD1 
2938 N N   . ASN B 157 ? 0.1735 0.2362 0.1858 0.0032  0.0084  0.0252  144 ASN A N   
2939 C CA  . ASN B 157 ? 0.1803 0.2591 0.1962 0.0013  0.0077  0.0232  144 ASN A CA  
2940 C C   . ASN B 157 ? 0.1965 0.2707 0.2152 -0.0075 0.0083  0.0183  144 ASN A C   
2941 O O   . ASN B 157 ? 0.2031 0.2644 0.2220 -0.0077 0.0091  0.0174  144 ASN A O   
2942 C CB  . ASN B 157 ? 0.1948 0.2743 0.2104 0.0082  0.0078  0.0251  144 ASN A CB  
2943 C CG  . ASN B 157 ? 0.2480 0.3322 0.2585 0.0193  0.0074  0.0297  144 ASN A CG  
2944 O OD1 . ASN B 157 ? 0.2227 0.3182 0.2314 0.0212  0.0067  0.0318  144 ASN A OD1 
2945 N ND2 . ASN B 157 ? 0.2464 0.3191 0.2523 0.0279  0.0077  0.0317  144 ASN A ND2 
2946 N N   . MET B 158 ? 0.1768 0.2606 0.1961 -0.0145 0.0079  0.0149  145 MET A N   
2947 C CA  . MET B 158 ? 0.2097 0.2849 0.2286 -0.0222 0.0088  0.0107  145 MET A CA  
2948 C C   . MET B 158 ? 0.2227 0.3009 0.2435 -0.0241 0.0096  0.0114  145 MET A C   
2949 O O   . MET B 158 ? 0.2390 0.3355 0.2621 -0.0252 0.0091  0.0125  145 MET A O   
2950 C CB  . MET B 158 ? 0.1928 0.2744 0.2096 -0.0300 0.0083  0.0061  145 MET A CB  
2951 C CG  . MET B 158 ? 0.2073 0.2872 0.2218 -0.0274 0.0077  0.0054  145 MET A CG  
2952 S SD  . MET B 158 ? 0.2777 0.3365 0.2895 -0.0251 0.0091  0.0039  145 MET A SD  
2953 C CE  . MET B 158 ? 0.2225 0.2706 0.2291 -0.0332 0.0099  -0.0022 145 MET A CE  
2954 N N   . GLY B 159 ? 0.2005 0.2637 0.2203 -0.0234 0.0108  0.0114  146 GLY A N   
2955 C CA  . GLY B 159 ? 0.1888 0.2532 0.2096 -0.0246 0.0120  0.0127  146 GLY A CA  
2956 C C   . GLY B 159 ? 0.2139 0.2672 0.2303 -0.0335 0.0136  0.0102  146 GLY A C   
2957 O O   . GLY B 159 ? 0.2660 0.3155 0.2791 -0.0393 0.0134  0.0068  146 GLY A O   
2958 N N   . SER B 160 ? 0.2120 0.2595 0.2272 -0.0341 0.0152  0.0121  147 SER A N   
2959 C CA  . SER B 160 ? 0.2131 0.2459 0.2215 -0.0422 0.0174  0.0109  147 SER A CA  
2960 C C   . SER B 160 ? 0.2225 0.2479 0.2291 -0.0389 0.0193  0.0144  147 SER A C   
2961 O O   . SER B 160 ? 0.2353 0.2738 0.2468 -0.0346 0.0191  0.0172  147 SER A O   
2962 C CB  . SER B 160 ? 0.2535 0.2966 0.2607 -0.0553 0.0181  0.0098  147 SER A CB  
2963 O OG  . SER B 160 ? 0.2739 0.2968 0.2718 -0.0640 0.0208  0.0094  147 SER A OG  
2964 N N   . ILE B 161 ? 0.2051 0.2091 0.2036 -0.0383 0.0210  0.0143  148 ILE A N   
2965 C CA  . ILE B 161 ? 0.2175 0.2145 0.2128 -0.0343 0.0230  0.0182  148 ILE A CA  
2966 C C   . ILE B 161 ? 0.2215 0.2205 0.2136 -0.0445 0.0256  0.0214  148 ILE A C   
2967 O O   . ILE B 161 ? 0.2441 0.2416 0.2340 -0.0417 0.0274  0.0256  148 ILE A O   
2968 C CB  . ILE B 161 ? 0.2310 0.2054 0.2169 -0.0281 0.0242  0.0180  148 ILE A CB  
2969 C CG1 . ILE B 161 ? 0.3024 0.2565 0.2770 -0.0357 0.0261  0.0163  148 ILE A CG1 
2970 C CG2 . ILE B 161 ? 0.2459 0.2222 0.2353 -0.0183 0.0220  0.0152  148 ILE A CG2 
2971 C CD1 . ILE B 161 ? 0.2943 0.2248 0.2567 -0.0281 0.0281  0.0174  148 ILE A CD1 
2972 N N   . SER B 162 ? 0.2546 0.2580 0.2458 -0.0568 0.0258  0.0194  149 SER A N   
2973 C CA  . SER B 162 ? 0.2777 0.2839 0.2649 -0.0701 0.0286  0.0222  149 SER A CA  
2974 C C   . SER B 162 ? 0.2612 0.2926 0.2562 -0.0680 0.0291  0.0267  149 SER A C   
2975 O O   . SER B 162 ? 0.2852 0.3126 0.2754 -0.0724 0.0323  0.0313  149 SER A O   
2976 C CB  . SER B 162 ? 0.3257 0.3393 0.3125 -0.0846 0.0281  0.0179  149 SER A CB  
2977 O OG  . SER B 162 ? 0.3411 0.3845 0.3397 -0.0806 0.0250  0.0162  149 SER A OG  
2978 N N   . TRP B 163 ? 0.2265 0.2808 0.2319 -0.0590 0.0264  0.0258  150 TRP A N   
2979 C CA  . TRP B 163 ? 0.2320 0.3083 0.2425 -0.0554 0.0271  0.0296  150 TRP A CA  
2980 C C   . TRP B 163 ? 0.2332 0.2990 0.2417 -0.0440 0.0277  0.0321  150 TRP A C   
2981 O O   . TRP B 163 ? 0.2258 0.3007 0.2336 -0.0442 0.0299  0.0363  150 TRP A O   
2982 C CB  . TRP B 163 ? 0.2447 0.3482 0.2642 -0.0490 0.0243  0.0280  150 TRP A CB  
2983 C CG  . TRP B 163 ? 0.2038 0.2993 0.2254 -0.0349 0.0215  0.0259  150 TRP A CG  
2984 C CD1 . TRP B 163 ? 0.1973 0.2855 0.2194 -0.0333 0.0193  0.0226  150 TRP A CD1 
2985 C CD2 . TRP B 163 ? 0.2104 0.3034 0.2328 -0.0220 0.0208  0.0265  150 TRP A CD2 
2986 N NE1 . TRP B 163 ? 0.1733 0.2542 0.1964 -0.0216 0.0176  0.0219  150 TRP A NE1 
2987 C CE2 . TRP B 163 ? 0.2145 0.2973 0.2377 -0.0149 0.0183  0.0237  150 TRP A CE2 
2988 C CE3 . TRP B 163 ? 0.2306 0.3287 0.2526 -0.0164 0.0220  0.0289  150 TRP A CE3 
2989 C CZ2 . TRP B 163 ? 0.2331 0.3093 0.2561 -0.0042 0.0171  0.0227  150 TRP A CZ2 
2990 C CZ3 . TRP B 163 ? 0.2236 0.3156 0.2455 -0.0043 0.0204  0.0272  150 TRP A CZ3 
2991 C CH2 . TRP B 163 ? 0.2438 0.3240 0.2660 0.0010  0.0180  0.0239  150 TRP A CH2 
2992 N N   . MET B 164 ? 0.2249 0.2728 0.2315 -0.0353 0.0261  0.0298  151 MET A N   
2993 C CA  . MET B 164 ? 0.2156 0.2551 0.2198 -0.0252 0.0265  0.0313  151 MET A CA  
2994 C C   . MET B 164 ? 0.2358 0.2621 0.2308 -0.0302 0.0303  0.0361  151 MET A C   
2995 O O   . MET B 164 ? 0.2273 0.2567 0.2205 -0.0249 0.0316  0.0395  151 MET A O   
2996 C CB  . MET B 164 ? 0.2320 0.2567 0.2352 -0.0176 0.0245  0.0277  151 MET A CB  
2997 C CG  . MET B 164 ? 0.2996 0.3345 0.3102 -0.0136 0.0213  0.0241  151 MET A CG  
2998 S SD  . MET B 164 ? 0.2871 0.3081 0.2967 -0.0089 0.0194  0.0202  151 MET A SD  
2999 C CE  . MET B 164 ? 0.3164 0.3488 0.3327 -0.0045 0.0166  0.0181  151 MET A CE  
3000 N N   . ARG B 165 ? 0.2597 0.2673 0.2465 -0.0399 0.0321  0.0362  152 ARG A N   
3001 C CA  . ARG B 165 ? 0.2450 0.2332 0.2196 -0.0447 0.0361  0.0413  152 ARG A CA  
3002 C C   . ARG B 165 ? 0.2541 0.2543 0.2279 -0.0591 0.0392  0.0455  152 ARG A C   
3003 O O   . ARG B 165 ? 0.2654 0.2483 0.2276 -0.0660 0.0431  0.0506  152 ARG A O   
3004 C CB  . ARG B 165 ? 0.2464 0.2062 0.2100 -0.0503 0.0370  0.0388  152 ARG A CB  
3005 C CG  . ARG B 165 ? 0.2505 0.1973 0.2121 -0.0368 0.0349  0.0353  152 ARG A CG  
3006 C CD  . ARG B 165 ? 0.2749 0.1918 0.2227 -0.0412 0.0363  0.0328  152 ARG A CD  
3007 N NE  . ARG B 165 ? 0.3263 0.2189 0.2582 -0.0456 0.0409  0.0386  152 ARG A NE  
3008 C CZ  . ARG B 165 ? 0.3711 0.2329 0.2868 -0.0534 0.0435  0.0379  152 ARG A CZ  
3009 N NH1 . ARG B 165 ? 0.3681 0.2246 0.2838 -0.0569 0.0414  0.0305  152 ARG A NH1 
3010 N NH2 . ARG B 165 ? 0.4155 0.2530 0.3152 -0.0575 0.0481  0.0443  152 ARG A NH2 
3011 N N   . GLY B 166 ? 0.2194 0.2506 0.2047 -0.0622 0.0375  0.0441  153 GLY A N   
3012 C CA  . GLY B 166 ? 0.2136 0.2649 0.2002 -0.0756 0.0402  0.0477  153 GLY A CA  
3013 C C   . GLY B 166 ? 0.2536 0.2884 0.2307 -0.0952 0.0430  0.0478  153 GLY A C   
3014 O O   . GLY B 166 ? 0.3220 0.3535 0.2916 -0.1078 0.0472  0.0533  153 GLY A O   
3015 N N   . ARG B 167 ? 0.2646 0.2852 0.2400 -0.0979 0.0408  0.0416  154 ARG A N   
3016 C CA  . ARG B 167 ? 0.2920 0.2910 0.2555 -0.1165 0.0434  0.0405  154 ARG A CA  
3017 C C   . ARG B 167 ? 0.3082 0.3373 0.2774 -0.1349 0.0442  0.0399  154 ARG A C   
3018 O O   . ARG B 167 ? 0.2841 0.3458 0.2664 -0.1319 0.0408  0.0363  154 ARG A O   
3019 C CB  . ARG B 167 ? 0.3405 0.3223 0.3010 -0.1161 0.0407  0.0328  154 ARG A CB  
3020 C CG  . ARG B 167 ? 0.3488 0.3033 0.3030 -0.0988 0.0401  0.0328  154 ARG A CG  
3021 C CD  . ARG B 167 ? 0.4654 0.3870 0.4027 -0.0991 0.0446  0.0387  154 ARG A CD  
3022 N NE  . ARG B 167 ? 0.5061 0.3940 0.4270 -0.1104 0.0465  0.0354  154 ARG A NE  
3023 C CZ  . ARG B 167 ? 0.6234 0.4788 0.5257 -0.1179 0.0513  0.0401  154 ARG A CZ  
3024 N NH1 . ARG B 167 ? 0.5546 0.4135 0.4544 -0.1197 0.0548  0.0490  154 ARG A NH1 
3025 N NH2 . ARG B 167 ? 0.6029 0.4223 0.4883 -0.1237 0.0525  0.0357  154 ARG A NH2 
3026 N N   . PRO B 168 ? 0.3101 0.3294 0.2689 -0.1545 0.0488  0.0436  155 PRO A N   
3027 C CA  . PRO B 168 ? 0.3243 0.3757 0.2884 -0.1744 0.0498  0.0431  155 PRO A CA  
3028 C C   . PRO B 168 ? 0.3404 0.3864 0.3013 -0.1900 0.0481  0.0346  155 PRO A C   
3029 O O   . PRO B 168 ? 0.3537 0.3667 0.3064 -0.1848 0.0467  0.0298  155 PRO A O   
3030 C CB  . PRO B 168 ? 0.3549 0.3894 0.3056 -0.1899 0.0561  0.0511  155 PRO A CB  
3031 C CG  . PRO B 168 ? 0.3647 0.3435 0.2969 -0.1844 0.0580  0.0521  155 PRO A CG  
3032 C CD  . PRO B 168 ? 0.3489 0.3264 0.2892 -0.1576 0.0535  0.0493  155 PRO A CD  
3033 N N   . GLY B 169 ? 0.3584 0.4395 0.3256 -0.2080 0.0483  0.0326  156 GLY A N   
3034 C CA  . GLY B 169 ? 0.4045 0.4843 0.3668 -0.2296 0.0477  0.0249  156 GLY A CA  
3035 C C   . GLY B 169 ? 0.3945 0.4978 0.3682 -0.2206 0.0419  0.0166  156 GLY A C   
3036 O O   . GLY B 169 ? 0.4144 0.5098 0.3825 -0.2340 0.0407  0.0088  156 GLY A O   
3037 N N   . MET B 170 ? 0.3406 0.4686 0.3282 -0.1976 0.0384  0.0179  157 MET A N   
3038 C CA  . MET B 170 ? 0.3270 0.4793 0.3242 -0.1898 0.0334  0.0115  157 MET A CA  
3039 C C   . MET B 170 ? 0.2884 0.4761 0.2997 -0.1692 0.0312  0.0157  157 MET A C   
3040 O O   . MET B 170 ? 0.2981 0.4830 0.3138 -0.1504 0.0279  0.0143  157 MET A O   
3041 C CB  . MET B 170 ? 0.3305 0.4471 0.3210 -0.1803 0.0311  0.0061  157 MET A CB  
3042 C CG  . MET B 170 ? 0.4016 0.4861 0.3888 -0.1599 0.0315  0.0104  157 MET A CG  
3043 S SD  . MET B 170 ? 0.5498 0.5888 0.5237 -0.1579 0.0307  0.0038  157 MET A SD  
3044 C CE  . MET B 170 ? 0.5228 0.5346 0.4930 -0.1385 0.0326  0.0111  157 MET A CE  
3045 N N   . VAL B 171 ? 0.2975 0.5194 0.3148 -0.1740 0.0332  0.0203  158 VAL A N   
3046 C CA  . VAL B 171 ? 0.2565 0.5040 0.2835 -0.1528 0.0319  0.0248  158 VAL A CA  
3047 C C   . VAL B 171 ? 0.2559 0.5257 0.2912 -0.1363 0.0271  0.0212  158 VAL A C   
3048 O O   . VAL B 171 ? 0.2043 0.4714 0.2427 -0.1149 0.0254  0.0233  158 VAL A O   
3049 C CB  . VAL B 171 ? 0.2548 0.5409 0.2865 -0.1607 0.0347  0.0296  158 VAL A CB  
3050 C CG1 . VAL B 171 ? 0.2646 0.5939 0.3016 -0.1781 0.0341  0.0259  158 VAL A CG1 
3051 C CG2 . VAL B 171 ? 0.2245 0.5335 0.2639 -0.1365 0.0335  0.0335  158 VAL A CG2 
3052 N N   . CYS B 172 ? 0.2432 0.5365 0.2813 -0.1455 0.0249  0.0159  159 CYS A N   
3053 C CA  . CYS B 172 ? 0.2487 0.5622 0.2932 -0.1271 0.0207  0.0142  159 CYS A CA  
3054 C C   . CYS B 172 ? 0.2462 0.5208 0.2866 -0.1131 0.0187  0.0128  159 CYS A C   
3055 O O   . CYS B 172 ? 0.2557 0.5341 0.2993 -0.0926 0.0166  0.0148  159 CYS A O   
3056 C CB  . CYS B 172 ? 0.2839 0.6338 0.3320 -0.1389 0.0185  0.0088  159 CYS A CB  
3057 S SG  . CYS B 172 ? 0.3115 0.7171 0.3656 -0.1571 0.0205  0.0097  159 CYS A SG  
3058 N N   . TYR B 173 ? 0.2287 0.4663 0.2610 -0.1240 0.0196  0.0094  160 TYR A N   
3059 C CA  . TYR B 173 ? 0.2182 0.4227 0.2465 -0.1129 0.0180  0.0076  160 TYR A CA  
3060 C C   . TYR B 173 ? 0.2202 0.4044 0.2483 -0.0968 0.0190  0.0127  160 TYR A C   
3061 O O   . TYR B 173 ? 0.2112 0.3914 0.2418 -0.0803 0.0169  0.0135  160 TYR A O   
3062 C CB  . TYR B 173 ? 0.2765 0.4487 0.2946 -0.1286 0.0193  0.0027  160 TYR A CB  
3063 C CG  . TYR B 173 ? 0.2525 0.3919 0.2661 -0.1163 0.0181  0.0011  160 TYR A CG  
3064 C CD1 . TYR B 173 ? 0.2314 0.3768 0.2463 -0.1115 0.0151  -0.0031 160 TYR A CD1 
3065 C CD2 . TYR B 173 ? 0.2440 0.3507 0.2524 -0.1084 0.0200  0.0043  160 TYR A CD2 
3066 C CE1 . TYR B 173 ? 0.2732 0.3919 0.2841 -0.1011 0.0143  -0.0043 160 TYR A CE1 
3067 C CE2 . TYR B 173 ? 0.2845 0.3661 0.2891 -0.0979 0.0191  0.0027  160 TYR A CE2 
3068 C CZ  . TYR B 173 ? 0.3181 0.4065 0.3243 -0.0948 0.0163  -0.0016 160 TYR A CZ  
3069 O OH  . TYR B 173 ? 0.3705 0.4400 0.3744 -0.0838 0.0154  -0.0025 160 TYR A OH  
3070 N N   . THR B 174 ? 0.2149 0.3898 0.2401 -0.1018 0.0222  0.0165  161 THR A N   
3071 C CA  . THR B 174 ? 0.2228 0.3776 0.2470 -0.0870 0.0229  0.0203  161 THR A CA  
3072 C C   . THR B 174 ? 0.2041 0.3843 0.2357 -0.0706 0.0213  0.0230  161 THR A C   
3073 O O   . THR B 174 ? 0.1767 0.3438 0.2085 -0.0554 0.0200  0.0236  161 THR A O   
3074 C CB  . THR B 174 ? 0.2048 0.3434 0.2225 -0.0959 0.0268  0.0240  161 THR A CB  
3075 O OG1 . THR B 174 ? 0.1929 0.3595 0.2130 -0.1087 0.0290  0.0263  161 THR A OG1 
3076 C CG2 . THR B 174 ? 0.2381 0.3399 0.2447 -0.1059 0.0285  0.0218  161 THR A CG2 
3077 N N   . THR B 175 ? 0.1884 0.4060 0.2254 -0.0735 0.0213  0.0240  162 THR A N   
3078 C CA  . THR B 175 ? 0.1943 0.4367 0.2362 -0.0562 0.0199  0.0262  162 THR A CA  
3079 C C   . THR B 175 ? 0.2158 0.4565 0.2584 -0.0424 0.0166  0.0243  162 THR A C   
3080 O O   . THR B 175 ? 0.1785 0.4111 0.2201 -0.0252 0.0155  0.0257  162 THR A O   
3081 C CB  . THR B 175 ? 0.1887 0.4761 0.2357 -0.0621 0.0208  0.0275  162 THR A CB  
3082 O OG1 . THR B 175 ? 0.2004 0.4874 0.2457 -0.0763 0.0245  0.0302  162 THR A OG1 
3083 C CG2 . THR B 175 ? 0.2137 0.5246 0.2636 -0.0411 0.0196  0.0296  162 THR A CG2 
3084 N N   . ALA B 176 ? 0.2119 0.4581 0.2548 -0.0506 0.0151  0.0211  163 ALA A N   
3085 C CA  . ALA B 176 ? 0.2003 0.4424 0.2425 -0.0393 0.0123  0.0200  163 ALA A CA  
3086 C C   . ALA B 176 ? 0.2142 0.4173 0.2523 -0.0317 0.0122  0.0202  163 ALA A C   
3087 O O   . ALA B 176 ? 0.1975 0.3933 0.2341 -0.0170 0.0108  0.0217  163 ALA A O   
3088 C CB  . ALA B 176 ? 0.1938 0.4433 0.2359 -0.0521 0.0110  0.0157  163 ALA A CB  
3089 N N   . LYS B 177 ? 0.1879 0.3646 0.2228 -0.0422 0.0137  0.0185  164 LYS A N   
3090 C CA  . LYS B 177 ? 0.1854 0.3311 0.2169 -0.0350 0.0135  0.0183  164 LYS A CA  
3091 C C   . LYS B 177 ? 0.1730 0.3129 0.2046 -0.0226 0.0139  0.0212  164 LYS A C   
3092 O O   . LYS B 177 ? 0.1864 0.3116 0.2164 -0.0132 0.0128  0.0212  164 LYS A O   
3093 C CB  . LYS B 177 ? 0.2028 0.3248 0.2296 -0.0468 0.0151  0.0159  164 LYS A CB  
3094 C CG  . LYS B 177 ? 0.1967 0.3208 0.2215 -0.0571 0.0140  0.0114  164 LYS A CG  
3095 C CD  . LYS B 177 ? 0.2138 0.3358 0.2392 -0.0478 0.0117  0.0105  164 LYS A CD  
3096 C CE  . LYS B 177 ? 0.2575 0.3751 0.2793 -0.0560 0.0108  0.0054  164 LYS A CE  
3097 N NZ  . LYS B 177 ? 0.2193 0.3428 0.2423 -0.0467 0.0088  0.0059  164 LYS A NZ  
3098 N N   . ALA B 178 ? 0.1692 0.3203 0.2021 -0.0234 0.0155  0.0232  165 ALA A N   
3099 C CA  . ALA B 178 ? 0.1940 0.3418 0.2262 -0.0110 0.0157  0.0249  165 ALA A CA  
3100 C C   . ALA B 178 ? 0.1899 0.3490 0.2220 0.0035  0.0137  0.0254  165 ALA A C   
3101 O O   . ALA B 178 ? 0.1928 0.3381 0.2218 0.0147  0.0131  0.0253  165 ALA A O   
3102 C CB  . ALA B 178 ? 0.1596 0.3233 0.1930 -0.0147 0.0179  0.0272  165 ALA A CB  
3103 N N   . ALA B 179 ? 0.1946 0.3800 0.2291 0.0037  0.0129  0.0259  166 ALA A N   
3104 C CA  . ALA B 179 ? 0.1998 0.3954 0.2319 0.0194  0.0112  0.0272  166 ALA A CA  
3105 C C   . ALA B 179 ? 0.2049 0.3720 0.2322 0.0245  0.0100  0.0268  166 ALA A C   
3106 O O   . ALA B 179 ? 0.1958 0.3512 0.2174 0.0380  0.0094  0.0278  166 ALA A O   
3107 C CB  . ALA B 179 ? 0.1915 0.4229 0.2270 0.0168  0.0104  0.0277  166 ALA A CB  
3108 N N   . LEU B 180 ? 0.2020 0.3592 0.2305 0.0137  0.0097  0.0253  167 LEU A N   
3109 C CA  . LEU B 180 ? 0.2329 0.3679 0.2575 0.0170  0.0088  0.0254  167 LEU A CA  
3110 C C   . LEU B 180 ? 0.2503 0.3580 0.2718 0.0200  0.0094  0.0247  167 LEU A C   
3111 O O   . LEU B 180 ? 0.2339 0.3248 0.2505 0.0264  0.0089  0.0255  167 LEU A O   
3112 C CB  . LEU B 180 ? 0.2645 0.3963 0.2911 0.0040  0.0087  0.0230  167 LEU A CB  
3113 C CG  . LEU B 180 ? 0.2751 0.4300 0.3031 0.0013  0.0075  0.0228  167 LEU A CG  
3114 C CD1 . LEU B 180 ? 0.3064 0.4521 0.3346 -0.0114 0.0076  0.0190  167 LEU A CD1 
3115 C CD2 . LEU B 180 ? 0.2959 0.4489 0.3190 0.0147  0.0064  0.0263  167 LEU A CD2 
3116 N N   . ASN B 181 ? 0.2238 0.3272 0.2475 0.0150  0.0106  0.0232  168 ASN A N   
3117 C CA  . ASN B 181 ? 0.2218 0.3056 0.2431 0.0181  0.0109  0.0220  168 ASN A CA  
3118 C C   . ASN B 181 ? 0.2142 0.2940 0.2302 0.0310  0.0102  0.0225  168 ASN A C   
3119 O O   . ASN B 181 ? 0.2268 0.2865 0.2384 0.0336  0.0098  0.0214  168 ASN A O   
3120 C CB  . ASN B 181 ? 0.2704 0.3568 0.2938 0.0136  0.0123  0.0215  168 ASN A CB  
3121 C CG  . ASN B 181 ? 0.2710 0.3411 0.2920 0.0173  0.0124  0.0197  168 ASN A CG  
3122 O OD1 . ASN B 181 ? 0.2859 0.3416 0.3062 0.0139  0.0120  0.0183  168 ASN A OD1 
3123 N ND2 . ASN B 181 ? 0.2430 0.3181 0.2631 0.0226  0.0129  0.0196  168 ASN A ND2 
3124 N N   . GLY B 182 ? 0.1877 0.2870 0.2035 0.0387  0.0103  0.0239  169 GLY A N   
3125 C CA  . GLY B 182 ? 0.1809 0.2769 0.1894 0.0538  0.0098  0.0242  169 GLY A CA  
3126 C C   . GLY B 182 ? 0.1947 0.2795 0.1962 0.0606  0.0089  0.0262  169 GLY A C   
3127 O O   . GLY B 182 ? 0.2484 0.3098 0.2409 0.0678  0.0087  0.0257  169 GLY A O   
3128 N N   . MET B 183 ? 0.1881 0.2888 0.1929 0.0575  0.0085  0.0286  170 MET A N   
3129 C CA  . MET B 183 ? 0.2246 0.3205 0.2225 0.0652  0.0079  0.0318  170 MET A CA  
3130 C C   . MET B 183 ? 0.2125 0.2773 0.2055 0.0606  0.0081  0.0319  170 MET A C   
3131 O O   . MET B 183 ? 0.2737 0.3208 0.2561 0.0696  0.0083  0.0345  170 MET A O   
3132 C CB  . MET B 183 ? 0.2280 0.3524 0.2310 0.0622  0.0072  0.0337  170 MET A CB  
3133 C CG  . MET B 183 ? 0.2692 0.3927 0.2634 0.0745  0.0066  0.0381  170 MET A CG  
3134 S SD  . MET B 183 ? 0.3512 0.5099 0.3514 0.0697  0.0054  0.0394  170 MET A SD  
3135 C CE  . MET B 183 ? 0.3027 0.4476 0.3074 0.0526  0.0054  0.0373  170 MET A CE  
3136 N N   . THR B 184 ? 0.1999 0.2579 0.1993 0.0471  0.0084  0.0292  171 THR A N   
3137 C CA  . THR B 184 ? 0.2197 0.2526 0.2153 0.0421  0.0088  0.0288  171 THR A CA  
3138 C C   . THR B 184 ? 0.2302 0.2402 0.2165 0.0488  0.0091  0.0277  171 THR A C   
3139 O O   . THR B 184 ? 0.2521 0.2416 0.2298 0.0496  0.0096  0.0295  171 THR A O   
3140 C CB  . THR B 184 ? 0.2186 0.2508 0.2220 0.0298  0.0091  0.0252  171 THR A CB  
3141 O OG1 . THR B 184 ? 0.2677 0.3146 0.2763 0.0235  0.0089  0.0258  171 THR A OG1 
3142 C CG2 . THR B 184 ? 0.2250 0.2375 0.2259 0.0240  0.0095  0.0239  171 THR A CG2 
3143 N N   . ARG B 185 ? 0.1957 0.2079 0.1833 0.0515  0.0090  0.0242  172 ARG A N   
3144 C CA  . ARG B 185 ? 0.2271 0.2178 0.2061 0.0559  0.0090  0.0211  172 ARG A CA  
3145 C C   . ARG B 185 ? 0.2519 0.2292 0.2171 0.0701  0.0091  0.0237  172 ARG A C   
3146 O O   . ARG B 185 ? 0.2911 0.2398 0.2447 0.0706  0.0096  0.0230  172 ARG A O   
3147 C CB  . ARG B 185 ? 0.2164 0.2151 0.1986 0.0580  0.0088  0.0169  172 ARG A CB  
3148 C CG  . ARG B 185 ? 0.2136 0.2224 0.2071 0.0453  0.0090  0.0156  172 ARG A CG  
3149 C CD  . ARG B 185 ? 0.2707 0.2916 0.2683 0.0464  0.0092  0.0132  172 ARG A CD  
3150 N NE  . ARG B 185 ? 0.3217 0.3307 0.3138 0.0500  0.0087  0.0086  172 ARG A NE  
3151 C CZ  . ARG B 185 ? 0.3650 0.3681 0.3590 0.0433  0.0085  0.0050  172 ARG A CZ  
3152 N NH1 . ARG B 185 ? 0.3301 0.3341 0.3299 0.0336  0.0087  0.0057  172 ARG A NH1 
3153 N NH2 . ARG B 185 ? 0.2727 0.2683 0.2611 0.0473  0.0078  0.0001  172 ARG A NH2 
3154 N N   . THR B 186 ? 0.2478 0.2455 0.2128 0.0815  0.0089  0.0267  173 THR A N   
3155 C CA  . THR B 186 ? 0.2597 0.2455 0.2095 0.0989  0.0091  0.0292  173 THR A CA  
3156 C C   . THR B 186 ? 0.2867 0.2585 0.2282 0.1003  0.0097  0.0350  173 THR A C   
3157 O O   . THR B 186 ? 0.3441 0.2864 0.2687 0.1093  0.0106  0.0370  173 THR A O   
3158 C CB  . THR B 186 ? 0.2716 0.2872 0.2228 0.1132  0.0087  0.0303  173 THR A CB  
3159 O OG1 . THR B 186 ? 0.2744 0.3191 0.2343 0.1104  0.0084  0.0344  173 THR A OG1 
3160 C CG2 . THR B 186 ? 0.2499 0.2789 0.2077 0.1122  0.0086  0.0253  173 THR A CG2 
3161 N N   . LEU B 187 ? 0.2659 0.2548 0.2176 0.0905  0.0095  0.0376  174 LEU A N   
3162 C CA  . LEU B 187 ? 0.3241 0.3021 0.2676 0.0923  0.0102  0.0436  174 LEU A CA  
3163 C C   . LEU B 187 ? 0.3060 0.2505 0.2433 0.0814  0.0114  0.0429  174 LEU A C   
3164 O O   . LEU B 187 ? 0.3143 0.2358 0.2375 0.0855  0.0128  0.0481  174 LEU A O   
3165 C CB  . LEU B 187 ? 0.2954 0.3006 0.2493 0.0860  0.0096  0.0463  174 LEU A CB  
3166 C CG  . LEU B 187 ? 0.3271 0.3661 0.2838 0.0973  0.0086  0.0481  174 LEU A CG  
3167 C CD1 . LEU B 187 ? 0.3728 0.4362 0.3374 0.0905  0.0079  0.0501  174 LEU A CD1 
3168 C CD2 . LEU B 187 ? 0.3649 0.3951 0.3055 0.1183  0.0090  0.0526  174 LEU A CD2 
3169 N N   . ALA B 188 ? 0.2676 0.2116 0.2146 0.0674  0.0111  0.0373  175 ALA A N   
3170 C CA  . ALA B 188 ? 0.3110 0.2285 0.2529 0.0561  0.0122  0.0359  175 ALA A CA  
3171 C C   . ALA B 188 ? 0.3489 0.2323 0.2721 0.0638  0.0131  0.0359  175 ALA A C   
3172 O O   . ALA B 188 ? 0.3794 0.2364 0.2911 0.0584  0.0147  0.0389  175 ALA A O   
3173 C CB  . ALA B 188 ? 0.2799 0.2079 0.2351 0.0432  0.0114  0.0295  175 ALA A CB  
3174 N N   . ARG B 189 ? 0.3416 0.2232 0.2597 0.0760  0.0124  0.0324  176 ARG A N   
3175 C CA  . ARG B 189 ? 0.3860 0.2317 0.2836 0.0850  0.0133  0.0314  176 ARG A CA  
3176 C C   . ARG B 189 ? 0.4018 0.2349 0.2834 0.1005  0.0145  0.0396  176 ARG A C   
3177 O O   . ARG B 189 ? 0.4290 0.2235 0.2908 0.1022  0.0163  0.0421  176 ARG A O   
3178 C CB  . ARG B 189 ? 0.4219 0.2744 0.3199 0.0944  0.0120  0.0246  176 ARG A CB  
3179 C CG  . ARG B 189 ? 0.4349 0.2526 0.3101 0.1082  0.0126  0.0223  176 ARG A CG  
3180 C CD  . ARG B 189 ? 0.4880 0.2667 0.3511 0.0952  0.0135  0.0178  176 ARG A CD  
3181 N NE  . ARG B 189 ? 0.4567 0.2455 0.3318 0.0816  0.0121  0.0091  176 ARG A NE  
3182 C CZ  . ARG B 189 ? 0.4504 0.2174 0.3208 0.0662  0.0123  0.0031  176 ARG A CZ  
3183 N NH1 . ARG B 189 ? 0.4411 0.2261 0.3248 0.0554  0.0108  -0.0038 176 ARG A NH1 
3184 N NH2 . ARG B 189 ? 0.4885 0.2175 0.3410 0.0604  0.0140  0.0047  176 ARG A NH2 
3185 N N   . GLU B 190 ? 0.3934 0.2586 0.2822 0.1119  0.0137  0.0437  177 GLU A N   
3186 C CA  . GLU B 190 ? 0.4603 0.3165 0.3324 0.1304  0.0147  0.0512  177 GLU A CA  
3187 C C   . GLU B 190 ? 0.4566 0.2958 0.3218 0.1229  0.0165  0.0587  177 GLU A C   
3188 O O   . GLU B 190 ? 0.4931 0.3024 0.3369 0.1345  0.0183  0.0645  177 GLU A O   
3189 C CB  . GLU B 190 ? 0.4847 0.3825 0.3647 0.1457  0.0132  0.0533  177 GLU A CB  
3190 C CG  . GLU B 190 ? 0.5157 0.4086 0.3770 0.1703  0.0139  0.0603  177 GLU A CG  
3191 C CD  . GLU B 190 ? 0.5795 0.5191 0.4501 0.1846  0.0122  0.0598  177 GLU A CD  
3192 O OE1 . GLU B 190 ? 0.4714 0.4391 0.3601 0.1756  0.0109  0.0534  177 GLU A OE1 
3193 O OE2 . GLU B 190 ? 0.5787 0.5261 0.4370 0.2059  0.0125  0.0659  177 GLU A OE2 
3194 N N   . LEU B 191 ? 0.4312 0.2854 0.3122 0.1035  0.0163  0.0584  178 LEU A N   
3195 C CA  . LEU B 191 ? 0.4421 0.2858 0.3170 0.0974  0.0182  0.0662  178 LEU A CA  
3196 C C   . LEU B 191 ? 0.4511 0.2656 0.3219 0.0783  0.0200  0.0647  178 LEU A C   
3197 O O   . LEU B 191 ? 0.4642 0.2673 0.3283 0.0719  0.0221  0.0713  178 LEU A O   
3198 C CB  . LEU B 191 ? 0.4390 0.3239 0.3327 0.0915  0.0168  0.0672  178 LEU A CB  
3199 C CG  . LEU B 191 ? 0.4257 0.3420 0.3217 0.1086  0.0153  0.0701  178 LEU A CG  
3200 C CD1 . LEU B 191 ? 0.4358 0.3917 0.3520 0.0978  0.0136  0.0680  178 LEU A CD1 
3201 C CD2 . LEU B 191 ? 0.4455 0.3489 0.3220 0.1264  0.0167  0.0794  178 LEU A CD2 
3202 N N   . GLY B 192 ? 0.4263 0.2355 0.3035 0.0678  0.0192  0.0559  179 GLY A N   
3203 C CA  . GLY B 192 ? 0.4275 0.2202 0.3053 0.0474  0.0204  0.0531  179 GLY A CA  
3204 C C   . GLY B 192 ? 0.4764 0.2248 0.3303 0.0450  0.0235  0.0584  179 GLY A C   
3205 O O   . GLY B 192 ? 0.4610 0.2007 0.3140 0.0282  0.0254  0.0607  179 GLY A O   
3206 N N   . GLY B 193 ? 0.5081 0.2271 0.3414 0.0618  0.0242  0.0600  180 GLY A N   
3207 C CA  . GLY B 193 ? 0.5976 0.2684 0.4045 0.0609  0.0275  0.0655  180 GLY A CA  
3208 C C   . GLY B 193 ? 0.6089 0.2791 0.4095 0.0615  0.0300  0.0777  180 GLY A C   
3209 O O   . GLY B 193 ? 0.6476 0.2804 0.4286 0.0538  0.0335  0.0840  180 GLY A O   
3210 N N   . GLN B 194 ? 0.5662 0.2767 0.3819 0.0700  0.0284  0.0814  181 GLN A N   
3211 C CA  . GLN B 194 ? 0.5901 0.3054 0.4018 0.0694  0.0305  0.0923  181 GLN A CA  
3212 C C   . GLN B 194 ? 0.5359 0.2711 0.3642 0.0460  0.0311  0.0915  181 GLN A C   
3213 O O   . GLN B 194 ? 0.5452 0.2910 0.3731 0.0444  0.0326  0.0996  181 GLN A O   
3214 C CB  . GLN B 194 ? 0.6144 0.3627 0.4311 0.0895  0.0288  0.0972  181 GLN A CB  
3215 C CG  . GLN B 194 ? 0.7584 0.4895 0.5550 0.1161  0.0289  0.1011  181 GLN A CG  
3216 C CD  . GLN B 194 ? 0.8643 0.6417 0.6741 0.1334  0.0258  0.1003  181 GLN A CD  
3217 O OE1 . GLN B 194 ? 0.7287 0.5421 0.5509 0.1328  0.0247  0.1037  181 GLN A OE1 
3218 N NE2 . GLN B 194 ? 0.8662 0.6459 0.6740 0.1480  0.0241  0.0949  181 GLN A NE2 
3219 N N   . GLY B 195 ? 0.5034 0.2467 0.3458 0.0296  0.0298  0.0819  182 GLY A N   
3220 C CA  . GLY B 195 ? 0.4482 0.2161 0.3076 0.0102  0.0299  0.0799  182 GLY A CA  
3221 C C   . GLY B 195 ? 0.4440 0.2583 0.3268 0.0126  0.0270  0.0762  182 GLY A C   
3222 O O   . GLY B 195 ? 0.3726 0.2069 0.2669 -0.0002 0.0273  0.0756  182 GLY A O   
3223 N N   . ILE B 196 ? 0.3754 0.2067 0.2648 0.0276  0.0242  0.0729  183 ILE A N   
3224 C CA  . ILE B 196 ? 0.3688 0.2402 0.2780 0.0282  0.0217  0.0693  183 ILE A CA  
3225 C C   . ILE B 196 ? 0.3685 0.2495 0.2910 0.0222  0.0197  0.0592  183 ILE A C   
3226 O O   . ILE B 196 ? 0.3892 0.2587 0.3073 0.0292  0.0188  0.0556  183 ILE A O   
3227 C CB  . ILE B 196 ? 0.3795 0.2671 0.2874 0.0467  0.0202  0.0725  183 ILE A CB  
3228 C CG1 . ILE B 196 ? 0.4071 0.2843 0.2992 0.0557  0.0223  0.0833  183 ILE A CG1 
3229 C CG2 . ILE B 196 ? 0.3692 0.2964 0.2963 0.0450  0.0177  0.0679  183 ILE A CG2 
3230 C CD1 . ILE B 196 ? 0.4116 0.3014 0.2981 0.0767  0.0210  0.0869  183 ILE A CD1 
3231 N N   . ARG B 197 ? 0.3435 0.2471 0.2814 0.0111  0.0189  0.0550  184 ARG A N   
3232 C CA  . ARG B 197 ? 0.3211 0.2374 0.2717 0.0066  0.0171  0.0465  184 ARG A CA  
3233 C C   . ARG B 197 ? 0.2715 0.2160 0.2340 0.0126  0.0151  0.0446  184 ARG A C   
3234 O O   . ARG B 197 ? 0.2729 0.2314 0.2372 0.0141  0.0152  0.0482  184 ARG A O   
3235 C CB  . ARG B 197 ? 0.3255 0.2439 0.2818 -0.0090 0.0179  0.0431  184 ARG A CB  
3236 C CG  . ARG B 197 ? 0.3599 0.2982 0.3236 -0.0156 0.0185  0.0449  184 ARG A CG  
3237 C CD  . ARG B 197 ? 0.4314 0.3680 0.3965 -0.0303 0.0199  0.0425  184 ARG A CD  
3238 N NE  . ARG B 197 ? 0.4493 0.4131 0.4262 -0.0328 0.0193  0.0402  184 ARG A NE  
3239 C CZ  . ARG B 197 ? 0.4794 0.4505 0.4544 -0.0370 0.0211  0.0451  184 ARG A CZ  
3240 N NH1 . ARG B 197 ? 0.4968 0.4911 0.4803 -0.0377 0.0207  0.0429  184 ARG A NH1 
3241 N NH2 . ARG B 197 ? 0.5051 0.4583 0.4679 -0.0389 0.0233  0.0526  184 ARG A NH2 
3242 N N   . ILE B 198 ? 0.2539 0.2053 0.2226 0.0159  0.0136  0.0393  185 ILE A N   
3243 C CA  . ILE B 198 ? 0.2619 0.2375 0.2401 0.0200  0.0122  0.0377  185 ILE A CA  
3244 C C   . ILE B 198 ? 0.2151 0.1978 0.2029 0.0141  0.0114  0.0313  185 ILE A C   
3245 O O   . ILE B 198 ? 0.2508 0.2231 0.2363 0.0156  0.0113  0.0284  185 ILE A O   
3246 C CB  . ILE B 198 ? 0.2607 0.2402 0.2339 0.0336  0.0115  0.0400  185 ILE A CB  
3247 C CG1 . ILE B 198 ? 0.3054 0.2739 0.2658 0.0417  0.0125  0.0473  185 ILE A CG1 
3248 C CG2 . ILE B 198 ? 0.2931 0.3013 0.2769 0.0339  0.0101  0.0381  185 ILE A CG2 
3249 C CD1 . ILE B 198 ? 0.3841 0.3598 0.3380 0.0580  0.0119  0.0505  185 ILE A CD1 
3250 N N   . ASN B 199 ? 0.1955 0.1945 0.1922 0.0088  0.0110  0.0291  186 ASN A N   
3251 C CA  . ASN B 199 ? 0.2070 0.2108 0.2105 0.0045  0.0107  0.0241  186 ASN A CA  
3252 C C   . ASN B 199 ? 0.1887 0.2086 0.1981 0.0042  0.0102  0.0230  186 ASN A C   
3253 O O   . ASN B 199 ? 0.2110 0.2398 0.2200 0.0047  0.0099  0.0249  186 ASN A O   
3254 C CB  . ASN B 199 ? 0.2038 0.2052 0.2094 -0.0033 0.0113  0.0219  186 ASN A CB  
3255 C CG  . ASN B 199 ? 0.1987 0.1856 0.1990 -0.0064 0.0119  0.0219  186 ASN A CG  
3256 O OD1 . ASN B 199 ? 0.1916 0.1709 0.1903 -0.0053 0.0115  0.0191  186 ASN A OD1 
3257 N ND2 . ASN B 199 ? 0.2182 0.2003 0.2142 -0.0107 0.0130  0.0252  186 ASN A ND2 
3258 N N   . SER B 200 ? 0.1906 0.2135 0.2040 0.0024  0.0101  0.0197  187 SER A N   
3259 C CA  A SER B 200 ? 0.2037 0.2374 0.2206 -0.0007 0.0101  0.0184  187 SER A CA  
3260 C CA  B SER B 200 ? 0.2076 0.2413 0.2246 -0.0006 0.0101  0.0183  187 SER A CA  
3261 C C   . SER B 200 ? 0.1817 0.2120 0.1997 -0.0056 0.0107  0.0153  187 SER A C   
3262 O O   . SER B 200 ? 0.1952 0.2194 0.2134 -0.0052 0.0110  0.0139  187 SER A O   
3263 C CB  A SER B 200 ? 0.1947 0.2341 0.2133 0.0010  0.0102  0.0181  187 SER A CB  
3264 C CB  B SER B 200 ? 0.1990 0.2373 0.2176 0.0011  0.0103  0.0179  187 SER A CB  
3265 O OG  A SER B 200 ? 0.2137 0.2626 0.2343 -0.0043 0.0104  0.0170  187 SER A OG  
3266 O OG  B SER B 200 ? 0.2309 0.2773 0.2485 0.0071  0.0098  0.0202  187 SER A OG  
3267 N N   . LEU B 201 ? 0.1793 0.2144 0.1972 -0.0092 0.0107  0.0140  188 LEU A N   
3268 C CA  . LEU B 201 ? 0.1696 0.2005 0.1863 -0.0117 0.0113  0.0106  188 LEU A CA  
3269 C C   . LEU B 201 ? 0.1781 0.2074 0.1936 -0.0147 0.0119  0.0091  188 LEU A C   
3270 O O   . LEU B 201 ? 0.1929 0.2299 0.2088 -0.0183 0.0115  0.0091  188 LEU A O   
3271 C CB  . LEU B 201 ? 0.1471 0.1832 0.1624 -0.0135 0.0110  0.0099  188 LEU A CB  
3272 C CG  . LEU B 201 ? 0.1819 0.2145 0.1943 -0.0140 0.0116  0.0060  188 LEU A CG  
3273 C CD1 . LEU B 201 ? 0.1671 0.2074 0.1778 -0.0148 0.0114  0.0051  188 LEU A CD1 
3274 C CD2 . LEU B 201 ? 0.2130 0.2373 0.2214 -0.0158 0.0123  0.0026  188 LEU A CD2 
3275 N N   . VAL B 202 ? 0.1552 0.1760 0.1689 -0.0135 0.0129  0.0084  189 VAL A N   
3276 C CA  . VAL B 202 ? 0.1649 0.1821 0.1764 -0.0168 0.0140  0.0086  189 VAL A CA  
3277 C C   . VAL B 202 ? 0.1775 0.1810 0.1818 -0.0176 0.0153  0.0060  189 VAL A C   
3278 O O   . VAL B 202 ? 0.1945 0.1903 0.1960 -0.0122 0.0161  0.0061  189 VAL A O   
3279 C CB  . VAL B 202 ? 0.1652 0.1825 0.1785 -0.0129 0.0145  0.0109  189 VAL A CB  
3280 C CG1 . VAL B 202 ? 0.1805 0.1948 0.1908 -0.0171 0.0161  0.0123  189 VAL A CG1 
3281 C CG2 . VAL B 202 ? 0.1521 0.1785 0.1698 -0.0094 0.0132  0.0127  189 VAL A CG2 
3282 N N   . PRO B 203 ? 0.2255 0.2254 0.2255 -0.0233 0.0155  0.0032  190 PRO A N   
3283 C CA  . PRO B 203 ? 0.2461 0.2281 0.2359 -0.0232 0.0170  0.0002  190 PRO A CA  
3284 C C   . PRO B 203 ? 0.2636 0.2312 0.2466 -0.0261 0.0192  0.0021  190 PRO A C   
3285 O O   . PRO B 203 ? 0.2876 0.2614 0.2736 -0.0326 0.0197  0.0046  190 PRO A O   
3286 C CB  . PRO B 203 ? 0.2566 0.2399 0.2435 -0.0292 0.0162  -0.0042 190 PRO A CB  
3287 C CG  . PRO B 203 ? 0.2551 0.2591 0.2513 -0.0304 0.0143  -0.0027 190 PRO A CG  
3288 C CD  . PRO B 203 ? 0.2137 0.2264 0.2168 -0.0290 0.0142  0.0022  190 PRO A CD  
3289 N N   . GLY B 204 ? 0.2689 0.2167 0.2409 -0.0218 0.0209  0.0008  191 GLY A N   
3290 C CA  . GLY B 204 ? 0.2755 0.2027 0.2363 -0.0249 0.0236  0.0027  191 GLY A CA  
3291 C C   . GLY B 204 ? 0.3207 0.2324 0.2714 -0.0350 0.0245  -0.0017 191 GLY A C   
3292 O O   . GLY B 204 ? 0.2994 0.2248 0.2559 -0.0435 0.0228  -0.0046 191 GLY A O   
3293 N N   . ALA B 205 ? 0.3114 0.1938 0.2454 -0.0335 0.0270  -0.0025 192 ALA A N   
3294 C CA  . ALA B 205 ? 0.3201 0.1841 0.2424 -0.0456 0.0281  -0.0074 192 ALA A CA  
3295 C C   . ALA B 205 ? 0.3682 0.2261 0.2845 -0.0393 0.0267  -0.0146 192 ALA A C   
3296 O O   . ALA B 205 ? 0.4061 0.2440 0.3098 -0.0271 0.0279  -0.0161 192 ALA A O   
3297 C CB  . ALA B 205 ? 0.3593 0.1893 0.2633 -0.0479 0.0321  -0.0043 192 ALA A CB  
3298 N N   . ILE B 206 ? 0.3763 0.2551 0.3019 -0.0458 0.0240  -0.0189 193 ILE A N   
3299 C CA  . ILE B 206 ? 0.3184 0.1994 0.2413 -0.0399 0.0224  -0.0254 193 ILE A CA  
3300 C C   . ILE B 206 ? 0.4135 0.2705 0.3198 -0.0489 0.0232  -0.0334 193 ILE A C   
3301 O O   . ILE B 206 ? 0.4002 0.2592 0.3066 -0.0655 0.0231  -0.0355 193 ILE A O   
3302 C CB  . ILE B 206 ? 0.3225 0.2377 0.2625 -0.0411 0.0194  -0.0252 193 ILE A CB  
3303 C CG1 . ILE B 206 ? 0.2870 0.2216 0.2414 -0.0345 0.0188  -0.0176 193 ILE A CG1 
3304 C CG2 . ILE B 206 ? 0.3094 0.2306 0.2473 -0.0346 0.0179  -0.0309 193 ILE A CG2 
3305 C CD1 . ILE B 206 ? 0.2535 0.1831 0.2062 -0.0201 0.0196  -0.0154 193 ILE A CD1 
3306 N N   . ARG B 207 ? 0.3827 0.2164 0.2733 -0.0383 0.0241  -0.0383 194 ARG A N   
3307 C CA  . ARG B 207 ? 0.4294 0.2369 0.3018 -0.0460 0.0248  -0.0473 194 ARG A CA  
3308 C C   . ARG B 207 ? 0.4312 0.2648 0.3124 -0.0521 0.0216  -0.0538 194 ARG A C   
3309 O O   . ARG B 207 ? 0.4421 0.3012 0.3349 -0.0417 0.0197  -0.0528 194 ARG A O   
3310 C CB  . ARG B 207 ? 0.4790 0.2523 0.3296 -0.0310 0.0268  -0.0512 194 ARG A CB  
3311 C CG  . ARG B 207 ? 0.5335 0.2762 0.3624 -0.0367 0.0274  -0.0621 194 ARG A CG  
3312 C CD  . ARG B 207 ? 0.7038 0.4065 0.5075 -0.0193 0.0301  -0.0646 194 ARG A CD  
3313 N NE  . ARG B 207 ? 0.8839 0.6074 0.6931 0.0030  0.0288  -0.0646 194 ARG A NE  
3314 C CZ  . ARG B 207 ? 0.9620 0.6728 0.7594 0.0256  0.0305  -0.0629 194 ARG A CZ  
3315 N NH1 . ARG B 207 ? 0.8249 0.4915 0.5974 0.0336  0.0339  -0.0622 194 ARG A NH1 
3316 N NH2 . ARG B 207 ? 0.8140 0.5588 0.6246 0.0404  0.0288  -0.0616 194 ARG A NH2 
3317 N N   . THR B 208 ? 0.5093 0.3410 0.3870 -0.0708 0.0210  -0.0593 195 THR A N   
3318 C CA  . THR B 208 ? 0.5160 0.3738 0.4005 -0.0770 0.0179  -0.0661 195 THR A CA  
3319 C C   . THR B 208 ? 0.6085 0.4409 0.4742 -0.0911 0.0183  -0.0770 195 THR A C   
3320 O O   . THR B 208 ? 0.5699 0.3714 0.4224 -0.1011 0.0211  -0.0768 195 THR A O   
3321 C CB  . THR B 208 ? 0.5274 0.4257 0.4327 -0.0857 0.0156  -0.0614 195 THR A CB  
3322 O OG1 . THR B 208 ? 0.5599 0.4528 0.4630 -0.1038 0.0168  -0.0611 195 THR A OG1 
3323 C CG2 . THR B 208 ? 0.4892 0.4079 0.4111 -0.0742 0.0154  -0.0508 195 THR A CG2 
3324 N N   . GLU B 209 ? 0.6763 0.5216 0.5403 -0.0922 0.0158  -0.0861 196 GLU A N   
3325 C CA  . GLU B 209 ? 0.7522 0.5795 0.5996 -0.1070 0.0153  -0.0985 196 GLU A CA  
3326 C C   . GLU B 209 ? 0.7646 0.5964 0.6144 -0.1317 0.0156  -0.0987 196 GLU A C   
3327 O O   . GLU B 209 ? 0.9020 0.7019 0.7329 -0.1466 0.0172  -0.1064 196 GLU A O   
3328 C CB  . GLU B 209 ? 0.6470 0.4958 0.4957 -0.1001 0.0123  -0.1066 196 GLU A CB  
3329 N N   . ARG B 210 ? 0.7923 0.6632 0.6639 -0.1361 0.0143  -0.0904 197 ARG A N   
3330 C CA  . ARG B 210 ? 0.8205 0.7074 0.6984 -0.1574 0.0145  -0.0890 197 ARG A CA  
3331 C C   . ARG B 210 ? 0.9060 0.7641 0.7768 -0.1641 0.0186  -0.0821 197 ARG A C   
3332 O O   . ARG B 210 ? 1.0687 0.9152 0.9303 -0.1856 0.0202  -0.0857 197 ARG A O   
3333 C CB  . ARG B 210 ? 0.6799 0.6193 0.5821 -0.1563 0.0118  -0.0821 197 ARG A CB  
3334 N N   . GLN B 211 ? 0.8864 0.7351 0.7611 -0.1471 0.0204  -0.0720 198 GLN A N   
3335 C CA  . GLN B 211 ? 0.8064 0.6245 0.6717 -0.1497 0.0246  -0.0650 198 GLN A CA  
3336 C C   . GLN B 211 ? 0.9467 0.7109 0.7833 -0.1551 0.0276  -0.0721 198 GLN A C   
3337 O O   . GLN B 211 ? 1.0870 0.8236 0.9107 -0.1691 0.0312  -0.0698 198 GLN A O   
3338 C CB  . GLN B 211 ? 0.8594 0.6839 0.7356 -0.1306 0.0255  -0.0536 198 GLN A CB  
3339 N N   . ASP B 212 ? 0.8787 0.6275 0.7037 -0.1452 0.0262  -0.0812 199 ASP A N   
3340 C CA  . ASP B 212 ? 0.9496 0.6444 0.7448 -0.1463 0.0289  -0.0889 199 ASP A CA  
3341 C C   . ASP B 212 ? 1.0665 0.7516 0.8494 -0.1719 0.0283  -0.1012 199 ASP A C   
3342 O O   . ASP B 212 ? 1.0152 0.6514 0.7720 -0.1826 0.0316  -0.1060 199 ASP A O   
3343 C CB  . ASP B 212 ? 0.9251 0.6066 0.7115 -0.1209 0.0281  -0.0929 199 ASP A CB  
3344 C CG  . ASP B 212 ? 0.8224 0.5001 0.6116 -0.0952 0.0295  -0.0833 199 ASP A CG  
3345 O OD1 . ASP B 212 ? 0.8274 0.5181 0.6295 -0.0939 0.0306  -0.0721 199 ASP A OD1 
3346 O OD2 . ASP B 212 ? 0.7658 0.4286 0.5434 -0.0759 0.0295  -0.0876 199 ASP A OD2 
3347 N N   . ALA B 213 ? 1.0470 0.7768 0.8465 -0.1814 0.0242  -0.1067 200 ALA A N   
3348 C CA  . ALA B 213 ? 1.0743 0.8029 0.8641 -0.2061 0.0229  -0.1194 200 ALA A CA  
3349 C C   . ALA B 213 ? 1.0590 0.7730 0.8418 -0.2332 0.0262  -0.1172 200 ALA A C   
3350 O O   . ALA B 213 ? 1.0228 0.7143 0.7877 -0.2556 0.0269  -0.1282 200 ALA A O   
3351 C CB  . ALA B 213 ? 0.9389 0.7257 0.7506 -0.2090 0.0180  -0.1232 200 ALA A CB  
3352 N N   . MET B 214 ? 1.0819 0.8067 0.8773 -0.2310 0.0285  -0.1033 201 MET A N   
3353 C CA  . MET B 214 ? 1.2155 0.9408 1.0108 -0.2551 0.0316  -0.0980 201 MET A CA  
3354 C C   . MET B 214 ? 1.4007 1.0600 1.1643 -0.2673 0.0371  -0.0992 201 MET A C   
3355 O O   . MET B 214 ? 1.3580 1.0123 1.1175 -0.2909 0.0403  -0.0955 201 MET A O   
3356 C CB  . MET B 214 ? 1.2073 0.9625 1.0240 -0.2445 0.0325  -0.0826 201 MET A CB  
3357 C CG  . MET B 214 ? 1.1790 0.9999 1.0259 -0.2386 0.0280  -0.0797 201 MET A CG  
3358 S SD  . MET B 214 ? 1.3526 1.2100 1.2201 -0.2416 0.0296  -0.0653 201 MET A SD  
3359 C CE  . MET B 214 ? 1.0139 0.8691 0.8916 -0.2115 0.0305  -0.0518 201 MET A CE  
3360 N N   . TRP B 215 ? 1.4180 1.0273 1.1585 -0.2505 0.0384  -0.1038 202 TRP A N   
3361 C CA  . TRP B 215 ? 1.2895 0.8294 0.9970 -0.2529 0.0439  -0.1027 202 TRP A CA  
3362 C C   . TRP B 215 ? 1.2591 0.7520 0.9377 -0.2510 0.0437  -0.1177 202 TRP A C   
3363 O O   . TRP B 215 ? 1.1902 0.6228 0.8399 -0.2405 0.0477  -0.1169 202 TRP A O   
3364 C CB  . TRP B 215 ? 1.2195 0.7406 0.9252 -0.2236 0.0465  -0.0898 202 TRP A CB  
3365 C CG  . TRP B 215 ? 1.1098 0.6677 0.8398 -0.2174 0.0470  -0.0747 202 TRP A CG  
3366 C CD1 . TRP B 215 ? 1.0968 0.7088 0.8569 -0.2017 0.0430  -0.0698 202 TRP A CD1 
3367 C CD2 . TRP B 215 ? 1.1104 0.6485 0.8336 -0.2239 0.0521  -0.0623 202 TRP A CD2 
3368 N NE1 . TRP B 215 ? 1.0673 0.6953 0.8401 -0.1987 0.0450  -0.0565 202 TRP A NE1 
3369 C CE2 . TRP B 215 ? 1.0851 0.6707 0.8365 -0.2114 0.0505  -0.0514 202 TRP A CE2 
3370 C CE3 . TRP B 215 ? 1.2393 0.7239 0.9344 -0.2393 0.0581  -0.0591 202 TRP A CE3 
3371 C CZ2 . TRP B 215 ? 1.0816 0.6654 0.8347 -0.2130 0.0544  -0.0381 202 TRP A CZ2 
3372 C CZ3 . TRP B 215 ? 1.2181 0.7006 0.9148 -0.2411 0.0622  -0.0447 202 TRP A CZ3 
3373 C CH2 . TRP B 215 ? 1.2495 0.7827 0.9755 -0.2277 0.0603  -0.0347 202 TRP A CH2 
3374 N N   . ALA B 216 ? 1.3152 0.8348 0.9997 -0.2603 0.0391  -0.1313 203 ALA A N   
3375 C CA  . ALA B 216 ? 1.2388 0.7253 0.9002 -0.2548 0.0378  -0.1469 203 ALA A CA  
3376 C C   . ALA B 216 ? 1.3066 0.7190 0.9279 -0.2716 0.0425  -0.1545 203 ALA A C   
3377 O O   . ALA B 216 ? 1.3351 0.7138 0.9331 -0.2676 0.0416  -0.1686 203 ALA A O   
3378 C CB  . ALA B 216 ? 1.1490 0.6853 0.8265 -0.2652 0.0320  -0.1592 203 ALA A CB  
3379 N N   . ALA B 217 ? 1.2928 0.6787 0.9044 -0.2910 0.0475  -0.1459 204 ALA A N   
3380 C CA  . ALA B 217 ? 1.2924 0.6006 0.8624 -0.3063 0.0527  -0.1517 204 ALA A CA  
3381 C C   . ALA B 217 ? 1.3222 0.5882 0.8780 -0.2988 0.0592  -0.1352 204 ALA A C   
3382 O O   . ALA B 217 ? 1.4432 0.6460 0.9658 -0.3155 0.0647  -0.1358 204 ALA A O   
3383 C CB  . ALA B 217 ? 1.3082 0.6158 0.8704 -0.3494 0.0528  -0.1634 204 ALA A CB  
3384 N N   . ASP B 218 ? 1.2474 0.5476 0.8271 -0.2731 0.0586  -0.1207 205 ASP A N   
3385 C CA  . ASP B 218 ? 1.2016 0.4708 0.7713 -0.2599 0.0639  -0.1044 205 ASP A CA  
3386 C C   . ASP B 218 ? 1.1824 0.4640 0.7615 -0.2177 0.0620  -0.0983 205 ASP A C   
3387 O O   . ASP B 218 ? 1.0675 0.3950 0.6749 -0.2052 0.0607  -0.0862 205 ASP A O   
3388 C CB  . ASP B 218 ? 1.2207 0.5298 0.8136 -0.2808 0.0654  -0.0919 205 ASP A CB  
3389 C CG  . ASP B 218 ? 1.2316 0.5164 0.8169 -0.2715 0.0711  -0.0741 205 ASP A CG  
3390 O OD1 . ASP B 218 ? 1.2195 0.4400 0.7720 -0.2563 0.0755  -0.0712 205 ASP A OD1 
3391 O OD2 . ASP B 218 ? 1.2303 0.5616 0.8417 -0.2775 0.0711  -0.0629 205 ASP A OD2 
3392 N N   . PRO B 219 ? 1.1974 0.4403 0.7529 -0.1937 0.0618  -0.1064 206 PRO A N   
3393 C CA  . PRO B 219 ? 1.1209 0.3866 0.6888 -0.1553 0.0594  -0.1017 206 PRO A CA  
3394 C C   . PRO B 219 ? 1.0832 0.3248 0.6422 -0.1371 0.0641  -0.0854 206 PRO A C   
3395 O O   . PRO B 219 ? 0.9908 0.2707 0.5717 -0.1143 0.0622  -0.0771 206 PRO A O   
3396 C CB  . PRO B 219 ? 1.1909 0.4284 0.7367 -0.1390 0.0577  -0.1168 206 PRO A CB  
3397 C CG  . PRO B 219 ? 1.2965 0.4625 0.8022 -0.1624 0.0620  -0.1256 206 PRO A CG  
3398 C CD  . PRO B 219 ? 1.3457 0.5191 0.8597 -0.2000 0.0643  -0.1194 206 PRO A CD  
3399 N N   . ALA B 220 ? 1.1263 0.3072 0.6540 -0.1504 0.0703  -0.0809 207 ALA A N   
3400 C CA  . ALA B 220 ? 1.1395 0.3007 0.6595 -0.1387 0.0751  -0.0639 207 ALA A CA  
3401 C C   . ALA B 220 ? 1.0717 0.2982 0.6310 -0.1455 0.0733  -0.0522 207 ALA A C   
3402 O O   . ALA B 220 ? 1.0180 0.2641 0.5889 -0.1219 0.0734  -0.0410 207 ALA A O   
3403 C CB  . ALA B 220 ? 1.2007 0.2892 0.6818 -0.1580 0.0822  -0.0608 207 ALA A CB  
3404 N N   . GLY B 221 ? 1.0655 0.3274 0.6448 -0.1774 0.0715  -0.0558 208 GLY A N   
3405 C CA  . GLY B 221 ? 0.9317 0.2511 0.5445 -0.1874 0.0703  -0.0455 208 GLY A CA  
3406 C C   . GLY B 221 ? 0.9000 0.2812 0.5469 -0.1647 0.0643  -0.0454 208 GLY A C   
3407 O O   . GLY B 221 ? 0.8531 0.2669 0.5200 -0.1529 0.0640  -0.0341 208 GLY A O   
3408 N N   . LEU B 222 ? 0.8695 0.2644 0.5211 -0.1590 0.0598  -0.0583 209 LEU A N   
3409 C CA  . LEU B 222 ? 0.8392 0.2885 0.5201 -0.1383 0.0544  -0.0586 209 LEU A CA  
3410 C C   . LEU B 222 ? 0.8248 0.2663 0.5025 -0.1055 0.0556  -0.0497 209 LEU A C   
3411 O O   . LEU B 222 ? 0.7740 0.2591 0.4775 -0.0941 0.0536  -0.0418 209 LEU A O   
3412 C CB  . LEU B 222 ? 0.8668 0.3235 0.5469 -0.1370 0.0503  -0.0738 209 LEU A CB  
3413 C CG  . LEU B 222 ? 0.8050 0.3144 0.5122 -0.1164 0.0452  -0.0747 209 LEU A CG  
3414 C CD1 . LEU B 222 ? 0.8100 0.3793 0.5521 -0.1252 0.0423  -0.0680 209 LEU A CD1 
3415 C CD2 . LEU B 222 ? 0.8513 0.3645 0.5540 -0.1116 0.0417  -0.0890 209 LEU A CD2 
3416 N N   . GLU B 223 ? 0.8803 0.2658 0.5250 -0.0903 0.0589  -0.0518 210 GLU A N   
3417 C CA  . GLU B 223 ? 0.8621 0.2363 0.4980 -0.0566 0.0598  -0.0461 210 GLU A CA  
3418 C C   . GLU B 223 ? 0.8231 0.2015 0.4643 -0.0531 0.0629  -0.0305 210 GLU A C   
3419 O O   . GLU B 223 ? 0.7924 0.2007 0.4487 -0.0315 0.0614  -0.0239 210 GLU A O   
3420 C CB  . GLU B 223 ? 0.9489 0.2618 0.5460 -0.0437 0.0624  -0.0545 210 GLU A CB  
3421 C CG  . GLU B 223 ? 1.0129 0.3120 0.5959 -0.0056 0.0632  -0.0512 210 GLU A CG  
3422 C CD  . GLU B 223 ? 1.0317 0.3934 0.6461 0.0158  0.0588  -0.0486 210 GLU A CD  
3423 O OE1 . GLU B 223 ? 0.9666 0.3719 0.6051 0.0090  0.0541  -0.0559 210 GLU A OE1 
3424 O OE2 . GLU B 223 ? 1.0023 0.3703 0.6168 0.0390  0.0600  -0.0390 210 GLU A OE2 
3425 N N   . ALA B 224 ? 0.8382 0.1875 0.4663 -0.0758 0.0673  -0.0249 211 ALA A N   
3426 C CA  . ALA B 224 ? 0.8325 0.1822 0.4624 -0.0755 0.0710  -0.0099 211 ALA A CA  
3427 C C   . ALA B 224 ? 0.7600 0.1790 0.4303 -0.0781 0.0669  -0.0054 211 ALA A C   
3428 O O   . ALA B 224 ? 0.7261 0.1666 0.4075 -0.0613 0.0669  0.0042  211 ALA A O   
3429 C CB  . ALA B 224 ? 0.8759 0.1807 0.4826 -0.1032 0.0766  -0.0064 211 ALA A CB  
3430 N N   . ALA B 225 ? 0.7398 0.1950 0.4315 -0.0983 0.0632  -0.0130 212 ALA A N   
3431 C CA  . ALA B 225 ? 0.6867 0.2039 0.4140 -0.1015 0.0596  -0.0089 212 ALA A CA  
3432 C C   . ALA B 225 ? 0.6545 0.2041 0.3990 -0.0745 0.0552  -0.0103 212 ALA A C   
3433 O O   . ALA B 225 ? 0.6267 0.2112 0.3912 -0.0647 0.0538  -0.0029 212 ALA A O   
3434 C CB  . ALA B 225 ? 0.6482 0.1956 0.3918 -0.1280 0.0568  -0.0164 212 ALA A CB  
3435 N N   . SER B 226 ? 0.6508 0.1858 0.3846 -0.0621 0.0535  -0.0197 213 SER A N   
3436 C CA  . SER B 226 ? 0.6199 0.1864 0.3688 -0.0380 0.0498  -0.0209 213 SER A CA  
3437 C C   . SER B 226 ? 0.6189 0.1776 0.3613 -0.0146 0.0520  -0.0113 213 SER A C   
3438 O O   . SER B 226 ? 0.5889 0.1852 0.3515 -0.0024 0.0497  -0.0070 213 SER A O   
3439 C CB  . SER B 226 ? 0.6408 0.1970 0.3798 -0.0299 0.0478  -0.0330 213 SER A CB  
3440 O OG  . SER B 226 ? 0.5746 0.1641 0.3283 -0.0078 0.0446  -0.0335 213 SER A OG  
3441 N N   . GLN B 227 ? 0.7033 0.2112 0.4155 -0.0089 0.0567  -0.0079 214 GLN A N   
3442 C CA  . GLN B 227 ? 0.7199 0.2154 0.4206 0.0152  0.0591  0.0013  214 GLN A CA  
3443 C C   . GLN B 227 ? 0.6981 0.2199 0.4158 0.0098  0.0599  0.0124  214 GLN A C   
3444 O O   . GLN B 227 ? 0.6819 0.2230 0.4061 0.0293  0.0593  0.0184  214 GLN A O   
3445 C CB  . GLN B 227 ? 0.7890 0.2195 0.4505 0.0219  0.0648  0.0047  214 GLN A CB  
3446 C CG  . GLN B 227 ? 0.8890 0.2902 0.5267 0.0462  0.0650  -0.0023 214 GLN A CG  
3447 C CD  . GLN B 227 ? 0.8487 0.2922 0.5023 0.0739  0.0614  -0.0029 214 GLN A CD  
3448 O OE1 . GLN B 227 ? 0.8650 0.3349 0.5303 0.0863  0.0612  0.0062  214 GLN A OE1 
3449 N NE2 . GLN B 227 ? 0.8544 0.3052 0.5080 0.0823  0.0586  -0.0140 214 GLN A NE2 
3450 N N   . ALA B 228 ? 0.7170 0.2421 0.4418 -0.0170 0.0610  0.0144  215 ALA A N   
3451 C CA  . ALA B 228 ? 0.7160 0.2680 0.4567 -0.0227 0.0617  0.0246  215 ALA A CA  
3452 C C   . ALA B 228 ? 0.6288 0.2374 0.4015 -0.0148 0.0565  0.0231  215 ALA A C   
3453 O O   . ALA B 228 ? 0.6238 0.2538 0.4062 -0.0034 0.0563  0.0302  215 ALA A O   
3454 C CB  . ALA B 228 ? 0.8143 0.3613 0.5555 -0.0530 0.0641  0.0263  215 ALA A CB  
3455 N N   . PHE B 229 ? 0.5781 0.2110 0.3665 -0.0203 0.0523  0.0138  216 PHE A N   
3456 C CA  . PHE B 229 ? 0.5517 0.2331 0.3672 -0.0116 0.0479  0.0132  216 PHE A CA  
3457 C C   . PHE B 229 ? 0.5103 0.1963 0.3230 0.0148  0.0470  0.0144  216 PHE A C   
3458 O O   . PHE B 229 ? 0.4859 0.2041 0.3153 0.0231  0.0451  0.0178  216 PHE A O   
3459 C CB  . PHE B 229 ? 0.5210 0.2294 0.3534 -0.0195 0.0436  0.0041  216 PHE A CB  
3460 C CG  . PHE B 229 ? 0.5420 0.2606 0.3828 -0.0444 0.0432  0.0020  216 PHE A CG  
3461 C CD1 . PHE B 229 ? 0.4934 0.2391 0.3506 -0.0541 0.0431  0.0082  216 PHE A CD1 
3462 C CD2 . PHE B 229 ? 0.5622 0.2688 0.3959 -0.0566 0.0425  -0.0068 216 PHE A CD2 
3463 C CE1 . PHE B 229 ? 0.4850 0.2477 0.3515 -0.0749 0.0423  0.0058  216 PHE A CE1 
3464 C CE2 . PHE B 229 ? 0.5829 0.3054 0.4256 -0.0794 0.0417  -0.0093 216 PHE A CE2 
3465 C CZ  . PHE B 229 ? 0.4932 0.2450 0.3525 -0.0878 0.0417  -0.0026 216 PHE A CZ  
3466 N N   . ILE B 230 ? 0.5404 0.1983 0.3332 0.0282  0.0481  0.0103  217 ILE A N   
3467 C CA  . ILE B 230 ? 0.5282 0.1937 0.3173 0.0541  0.0474  0.0113  217 ILE A CA  
3468 C C   . ILE B 230 ? 0.5220 0.1833 0.3047 0.0650  0.0501  0.0219  217 ILE A C   
3469 O O   . ILE B 230 ? 0.5045 0.1983 0.3005 0.0780  0.0481  0.0246  217 ILE A O   
3470 C CB  . ILE B 230 ? 0.5698 0.1993 0.3334 0.0666  0.0490  0.0053  217 ILE A CB  
3471 C CG1 . ILE B 230 ? 0.5411 0.1860 0.3140 0.0613  0.0456  -0.0055 217 ILE A CG1 
3472 C CG2 . ILE B 230 ? 0.5681 0.1964 0.3199 0.0956  0.0498  0.0086  217 ILE A CG2 
3473 C CD1 . ILE B 230 ? 0.6182 0.2274 0.3642 0.0759  0.0471  -0.0123 217 ILE A CD1 
3474 N N   . ASP B 231 ? 0.5643 0.1895 0.3285 0.0571  0.0545  0.0282  218 ASP A N   
3475 C CA  . ASP B 231 ? 0.5911 0.2078 0.3455 0.0674  0.0577  0.0391  218 ASP A CA  
3476 C C   . ASP B 231 ? 0.5572 0.2183 0.3385 0.0601  0.0554  0.0432  218 ASP A C   
3477 O O   . ASP B 231 ? 0.5426 0.2216 0.3273 0.0749  0.0551  0.0485  218 ASP A O   
3478 C CB  . ASP B 231 ? 0.6956 0.2607 0.4224 0.0581  0.0635  0.0455  218 ASP A CB  
3479 C CG  . ASP B 231 ? 0.8872 0.3973 0.5816 0.0632  0.0666  0.0416  218 ASP A CG  
3480 O OD1 . ASP B 231 ? 0.9717 0.4808 0.6615 0.0787  0.0644  0.0333  218 ASP A OD1 
3481 O OD2 . ASP B 231 ? 0.9764 0.4410 0.6476 0.0503  0.0716  0.0465  218 ASP A OD2 
3482 N N   . GLN B 232 ? 0.5401 0.2228 0.3412 0.0392  0.0532  0.0395  219 GLN A N   
3483 C CA  . GLN B 232 ? 0.4994 0.2200 0.3229 0.0330  0.0515  0.0434  219 GLN A CA  
3484 C C   . GLN B 232 ? 0.4774 0.2387 0.3224 0.0433  0.0465  0.0383  219 GLN A C   
3485 O O   . GLN B 232 ? 0.4326 0.2226 0.2916 0.0468  0.0450  0.0414  219 GLN A O   
3486 C CB  . GLN B 232 ? 0.5029 0.2295 0.3367 0.0079  0.0513  0.0414  219 GLN A CB  
3487 C CG  . GLN B 232 ? 0.5379 0.2340 0.3544 -0.0061 0.0566  0.0487  219 GLN A CG  
3488 C CD  . GLN B 232 ? 0.5508 0.2586 0.3783 -0.0310 0.0560  0.0451  219 GLN A CD  
3489 O OE1 . GLN B 232 ? 0.5341 0.2813 0.3852 -0.0364 0.0524  0.0424  219 GLN A OE1 
3490 N NE2 . GLN B 232 ? 0.5632 0.2353 0.3715 -0.0459 0.0598  0.0457  219 GLN A NE2 
3491 N N   . GLN B 233 ? 0.4433 0.2063 0.2902 0.0463  0.0441  0.0302  220 GLN A N   
3492 C CA  . GLN B 233 ? 0.4170 0.2173 0.2830 0.0537  0.0398  0.0255  220 GLN A CA  
3493 C C   . GLN B 233 ? 0.3928 0.2038 0.2550 0.0751  0.0397  0.0280  220 GLN A C   
3494 O O   . GLN B 233 ? 0.4448 0.2301 0.2859 0.0884  0.0427  0.0323  220 GLN A O   
3495 C CB  . GLN B 233 ? 0.3801 0.1794 0.2467 0.0527  0.0379  0.0169  220 GLN A CB  
3496 C CG  . GLN B 233 ? 0.3788 0.1853 0.2572 0.0325  0.0364  0.0129  220 GLN A CG  
3497 C CD  . GLN B 233 ? 0.3696 0.1710 0.2452 0.0304  0.0350  0.0048  220 GLN A CD  
3498 O OE1 . GLN B 233 ? 0.3664 0.1751 0.2505 0.0147  0.0337  0.0015  220 GLN A OE1 
3499 N NE2 . GLN B 233 ? 0.3620 0.1569 0.2272 0.0467  0.0350  0.0014  220 GLN A NE2 
3500 N N   . MET B 234 ? 0.3773 0.2262 0.2585 0.0786  0.0361  0.0252  221 MET A N   
3501 C CA  . MET B 234 ? 0.3754 0.2430 0.2556 0.0977  0.0351  0.0257  221 MET A CA  
3502 C C   . MET B 234 ? 0.3774 0.2436 0.2501 0.1097  0.0345  0.0201  221 MET A C   
3503 O O   . MET B 234 ? 0.4699 0.3311 0.3282 0.1291  0.0358  0.0217  221 MET A O   
3504 C CB  . MET B 234 ? 0.3403 0.2481 0.2421 0.0948  0.0316  0.0238  221 MET A CB  
3505 C CG  . MET B 234 ? 0.3074 0.2202 0.2152 0.0875  0.0321  0.0290  221 MET A CG  
3506 S SD  . MET B 234 ? 0.3031 0.2573 0.2353 0.0809  0.0276  0.0241  221 MET A SD  
3507 C CE  . MET B 234 ? 0.3835 0.3364 0.3162 0.0762  0.0291  0.0304  221 MET A CE  
3508 N N   . LEU B 235 ? 0.3488 0.2221 0.2309 0.1001  0.0326  0.0138  222 LEU A N   
3509 C CA  . LEU B 235 ? 0.3764 0.2470 0.2500 0.1109  0.0324  0.0082  222 LEU A CA  
3510 C C   . LEU B 235 ? 0.4036 0.2309 0.2564 0.1093  0.0352  0.0070  222 LEU A C   
3511 O O   . LEU B 235 ? 0.4339 0.2445 0.2878 0.0914  0.0358  0.0068  222 LEU A O   
3512 C CB  . LEU B 235 ? 0.3410 0.2435 0.2340 0.1029  0.0292  0.0024  222 LEU A CB  
3513 C CG  . LEU B 235 ? 0.3096 0.2515 0.2213 0.1023  0.0267  0.0032  222 LEU A CG  
3514 C CD1 . LEU B 235 ? 0.3137 0.2772 0.2430 0.0883  0.0242  -0.0011 222 LEU A CD1 
3515 C CD2 . LEU B 235 ? 0.3424 0.3030 0.2482 0.1226  0.0266  0.0026  222 LEU A CD2 
3516 N N   . LYS B 236 ? 0.4182 0.2276 0.2510 0.1275  0.0368  0.0051  223 LYS A N   
3517 C CA  . LYS B 236 ? 0.4659 0.2255 0.2732 0.1276  0.0402  0.0050  223 LYS A CA  
3518 C C   . LYS B 236 ? 0.4683 0.2178 0.2703 0.1246  0.0394  -0.0041 223 LYS A C   
3519 O O   . LYS B 236 ? 0.5118 0.2359 0.2914 0.1403  0.0411  -0.0076 223 LYS A O   
3520 C CB  . LYS B 236 ? 0.5044 0.2394 0.2865 0.1511  0.0434  0.0098  223 LYS A CB  
3521 C CG  . LYS B 236 ? 0.5077 0.2565 0.2954 0.1544  0.0440  0.0188  223 LYS A CG  
3522 C CD  . LYS B 236 ? 0.5402 0.2644 0.3259 0.1349  0.0464  0.0248  223 LYS A CD  
3523 C CE  . LYS B 236 ? 0.5601 0.2991 0.3504 0.1393  0.0470  0.0333  223 LYS A CE  
3524 N NZ  . LYS B 236 ? 0.5979 0.3128 0.3840 0.1212  0.0499  0.0392  223 LYS A NZ  
3525 N N   . PHE B 237 ? 0.4461 0.2158 0.2677 0.1058  0.0368  -0.0081 224 PHE A N   
3526 C CA  . PHE B 237 ? 0.4570 0.2196 0.2751 0.1001  0.0359  -0.0167 224 PHE A CA  
3527 C C   . PHE B 237 ? 0.4204 0.1920 0.2552 0.0747  0.0343  -0.0175 224 PHE A C   
3528 O O   . PHE B 237 ? 0.3995 0.1902 0.2507 0.0658  0.0335  -0.0120 224 PHE A O   
3529 C CB  . PHE B 237 ? 0.4465 0.2422 0.2729 0.1127  0.0336  -0.0221 224 PHE A CB  
3530 C CG  . PHE B 237 ? 0.4210 0.2655 0.2749 0.1080  0.0306  -0.0200 224 PHE A CG  
3531 C CD1 . PHE B 237 ? 0.4355 0.3000 0.3074 0.0908  0.0283  -0.0223 224 PHE A CD1 
3532 C CD2 . PHE B 237 ? 0.4376 0.3069 0.2983 0.1200  0.0303  -0.0153 224 PHE A CD2 
3533 C CE1 . PHE B 237 ? 0.4181 0.3215 0.3126 0.0856  0.0261  -0.0197 224 PHE A CE1 
3534 C CE2 . PHE B 237 ? 0.3983 0.3082 0.2823 0.1132  0.0278  -0.0139 224 PHE A CE2 
3535 C CZ  . PHE B 237 ? 0.3891 0.3134 0.2891 0.0960  0.0259  -0.0159 224 PHE A CZ  
3536 N N   . ARG B 238 ? 0.4271 0.1835 0.2554 0.0645  0.0340  -0.0245 225 ARG A N   
3537 C CA  . ARG B 238 ? 0.4302 0.1963 0.2723 0.0414  0.0325  -0.0257 225 ARG A CA  
3538 C C   . ARG B 238 ? 0.3802 0.1887 0.2450 0.0390  0.0290  -0.0277 225 ARG A C   
3539 O O   . ARG B 238 ? 0.3713 0.1913 0.2351 0.0493  0.0279  -0.0328 225 ARG A O   
3540 C CB  . ARG B 238 ? 0.4501 0.1864 0.2763 0.0299  0.0333  -0.0334 225 ARG A CB  
3541 C CG  . ARG B 238 ? 0.5039 0.1944 0.3074 0.0246  0.0371  -0.0312 225 ARG A CG  
3542 C CD  . ARG B 238 ? 0.4902 0.1837 0.3024 0.0111  0.0384  -0.0225 225 ARG A CD  
3543 N NE  . ARG B 238 ? 0.4545 0.1830 0.2908 -0.0062 0.0358  -0.0218 225 ARG A NE  
3544 C CZ  . ARG B 238 ? 0.4797 0.2059 0.3165 -0.0262 0.0352  -0.0267 225 ARG A CZ  
3545 N NH1 . ARG B 238 ? 0.5207 0.2103 0.3358 -0.0336 0.0372  -0.0325 225 ARG A NH1 
3546 N NH2 . ARG B 238 ? 0.4481 0.2106 0.3069 -0.0378 0.0325  -0.0261 225 ARG A NH2 
3547 N N   . LEU B 239 ? 0.3346 0.1651 0.2183 0.0256  0.0276  -0.0236 226 LEU A N   
3548 C CA  . LEU B 239 ? 0.3102 0.1760 0.2135 0.0212  0.0246  -0.0246 226 LEU A CA  
3549 C C   . LEU B 239 ? 0.3693 0.2335 0.2708 0.0100  0.0234  -0.0312 226 LEU A C   
3550 O O   . LEU B 239 ? 0.3985 0.2398 0.2894 -0.0007 0.0245  -0.0338 226 LEU A O   
3551 C CB  . LEU B 239 ? 0.2836 0.1687 0.2040 0.0122  0.0236  -0.0184 226 LEU A CB  
3552 C CG  . LEU B 239 ? 0.3038 0.1969 0.2290 0.0214  0.0242  -0.0125 226 LEU A CG  
3553 C CD1 . LEU B 239 ? 0.2711 0.1808 0.2113 0.0128  0.0232  -0.0074 226 LEU A CD1 
3554 C CD2 . LEU B 239 ? 0.2753 0.1890 0.2052 0.0348  0.0231  -0.0135 226 LEU A CD2 
3555 N N   . ASP B 240 ? 0.3349 0.2259 0.2475 0.0108  0.0212  -0.0334 227 ASP A N   
3556 C CA  . ASP B 240 ? 0.3523 0.2465 0.2641 0.0007  0.0198  -0.0395 227 ASP A CA  
3557 C C   . ASP B 240 ? 0.3119 0.2407 0.2427 -0.0038 0.0175  -0.0364 227 ASP A C   
3558 O O   . ASP B 240 ? 0.3492 0.2939 0.2921 -0.0015 0.0172  -0.0301 227 ASP A O   
3559 C CB  . ASP B 240 ? 0.3586 0.2389 0.2544 0.0103  0.0203  -0.0475 227 ASP A CB  
3560 C CG  . ASP B 240 ? 0.3845 0.2864 0.2844 0.0254  0.0199  -0.0476 227 ASP A CG  
3561 O OD1 . ASP B 240 ? 0.3581 0.2898 0.2748 0.0244  0.0186  -0.0429 227 ASP A OD1 
3562 O OD2 . ASP B 240 ? 0.4271 0.3161 0.3122 0.0375  0.0208  -0.0530 227 ASP A OD2 
3563 N N   . ALA B 241 ? 0.3307 0.2689 0.2624 -0.0113 0.0160  -0.0410 228 ALA A N   
3564 C CA  . ALA B 241 ? 0.2669 0.2349 0.2140 -0.0158 0.0141  -0.0374 228 ALA A CA  
3565 C C   . ALA B 241 ? 0.2679 0.2552 0.2223 -0.0058 0.0139  -0.0340 228 ALA A C   
3566 O O   . ALA B 241 ? 0.2486 0.2538 0.2150 -0.0080 0.0132  -0.0281 228 ALA A O   
3567 C CB  . ALA B 241 ? 0.2689 0.2436 0.2130 -0.0244 0.0125  -0.0436 228 ALA A CB  
3568 N N   . SER B 242 ? 0.2806 0.2633 0.2271 0.0052  0.0149  -0.0373 229 SER A N   
3569 C CA  . SER B 242 ? 0.2590 0.2632 0.2123 0.0131  0.0151  -0.0343 229 SER A CA  
3570 C C   . SER B 242 ? 0.2422 0.2508 0.2044 0.0144  0.0156  -0.0274 229 SER A C   
3571 O O   . SER B 242 ? 0.2684 0.2968 0.2405 0.0139  0.0154  -0.0231 229 SER A O   
3572 C CB  . SER B 242 ? 0.2545 0.2542 0.1962 0.0257  0.0162  -0.0397 229 SER A CB  
3573 O OG  . SER B 242 ? 0.2994 0.2985 0.2330 0.0250  0.0155  -0.0468 229 SER A OG  
3574 N N   . ASP B 243 ? 0.2323 0.2212 0.1896 0.0155  0.0164  -0.0267 230 ASP A N   
3575 C CA  . ASP B 243 ? 0.2401 0.2351 0.2054 0.0171  0.0167  -0.0210 230 ASP A CA  
3576 C C   . ASP B 243 ? 0.2158 0.2219 0.1933 0.0071  0.0155  -0.0163 230 ASP A C   
3577 O O   . ASP B 243 ? 0.2317 0.2501 0.2178 0.0070  0.0152  -0.0121 230 ASP A O   
3578 C CB  . ASP B 243 ? 0.2529 0.2262 0.2109 0.0194  0.0179  -0.0200 230 ASP A CB  
3579 C CG  . ASP B 243 ? 0.3208 0.2804 0.2646 0.0322  0.0193  -0.0236 230 ASP A CG  
3580 O OD1 . ASP B 243 ? 0.3024 0.2777 0.2486 0.0420  0.0195  -0.0228 230 ASP A OD1 
3581 O OD2 . ASP B 243 ? 0.3007 0.2345 0.2303 0.0324  0.0204  -0.0272 230 ASP A OD2 
3582 N N   . CYS B 244 ? 0.2044 0.2049 0.1813 -0.0013 0.0148  -0.0172 231 CYS A N   
3583 C CA  . CYS B 244 ? 0.1867 0.1991 0.1737 -0.0082 0.0137  -0.0126 231 CYS A CA  
3584 C C   . CYS B 244 ? 0.1957 0.2262 0.1879 -0.0079 0.0130  -0.0108 231 CYS A C   
3585 O O   . CYS B 244 ? 0.1894 0.2286 0.1887 -0.0090 0.0128  -0.0057 231 CYS A O   
3586 C CB  . CYS B 244 ? 0.2125 0.2228 0.1987 -0.0167 0.0129  -0.0138 231 CYS A CB  
3587 S SG  . CYS B 244 ? 0.2703 0.2591 0.2495 -0.0207 0.0143  -0.0149 231 CYS A SG  
3588 N N   . ALA B 245 ? 0.1945 0.2300 0.1820 -0.0061 0.0130  -0.0148 232 ALA A N   
3589 C CA  . ALA B 245 ? 0.1968 0.2504 0.1885 -0.0065 0.0128  -0.0120 232 ALA A CA  
3590 C C   . ALA B 245 ? 0.2093 0.2721 0.2050 -0.0032 0.0138  -0.0086 232 ALA A C   
3591 O O   . ALA B 245 ? 0.2046 0.2769 0.2056 -0.0067 0.0140  -0.0033 232 ALA A O   
3592 C CB  . ALA B 245 ? 0.2095 0.2687 0.1946 -0.0049 0.0125  -0.0176 232 ALA A CB  
3593 N N   . ARG B 246 ? 0.1984 0.2576 0.1913 0.0030  0.0146  -0.0113 233 ARG A N   
3594 C CA  . ARG B 246 ? 0.2038 0.2756 0.2013 0.0050  0.0155  -0.0088 233 ARG A CA  
3595 C C   . ARG B 246 ? 0.2140 0.2839 0.2185 -0.0012 0.0151  -0.0035 233 ARG A C   
3596 O O   . ARG B 246 ? 0.1924 0.2733 0.2013 -0.0052 0.0157  -0.0001 233 ARG A O   
3597 C CB  . ARG B 246 ? 0.2385 0.3082 0.2309 0.0146  0.0162  -0.0126 233 ARG A CB  
3598 C CG  . ARG B 246 ? 0.2551 0.3301 0.2395 0.0219  0.0167  -0.0178 233 ARG A CG  
3599 C CD  . ARG B 246 ? 0.3057 0.3743 0.2821 0.0341  0.0175  -0.0214 233 ARG A CD  
3600 N NE  . ARG B 246 ? 0.3743 0.4399 0.3395 0.0430  0.0180  -0.0274 233 ARG A NE  
3601 C CZ  . ARG B 246 ? 0.3776 0.4452 0.3341 0.0573  0.0190  -0.0309 233 ARG A CZ  
3602 N NH1 . ARG B 246 ? 0.4468 0.5176 0.3939 0.0655  0.0194  -0.0366 233 ARG A NH1 
3603 N NH2 . ARG B 246 ? 0.4162 0.4828 0.3723 0.0642  0.0194  -0.0290 233 ARG A NH2 
3604 N N   . LEU B 247 ? 0.2108 0.2660 0.2152 -0.0021 0.0144  -0.0032 234 LEU A N   
3605 C CA  . LEU B 247 ? 0.2064 0.2590 0.2160 -0.0059 0.0141  0.0008  234 LEU A CA  
3606 C C   . LEU B 247 ? 0.2214 0.2762 0.2330 -0.0111 0.0137  0.0051  234 LEU A C   
3607 O O   . LEU B 247 ? 0.1969 0.2524 0.2109 -0.0144 0.0140  0.0087  234 LEU A O   
3608 C CB  . LEU B 247 ? 0.1772 0.2166 0.1858 -0.0044 0.0137  0.0002  234 LEU A CB  
3609 C CG  . LEU B 247 ? 0.1782 0.2144 0.1912 -0.0071 0.0132  0.0036  234 LEU A CG  
3610 C CD1 . LEU B 247 ? 0.1934 0.2361 0.2093 -0.0081 0.0134  0.0044  234 LEU A CD1 
3611 C CD2 . LEU B 247 ? 0.1586 0.1850 0.1700 -0.0050 0.0133  0.0030  234 LEU A CD2 
3612 N N   . ALA B 248 ? 0.1773 0.2327 0.1867 -0.0117 0.0132  0.0045  235 ALA A N   
3613 C CA  . ALA B 248 ? 0.1934 0.2524 0.2034 -0.0144 0.0129  0.0092  235 ALA A CA  
3614 C C   . ALA B 248 ? 0.2315 0.2989 0.2412 -0.0164 0.0141  0.0129  235 ALA A C   
3615 O O   . ALA B 248 ? 0.1958 0.2599 0.2049 -0.0186 0.0145  0.0185  235 ALA A O   
3616 C CB  . ALA B 248 ? 0.1961 0.2595 0.2038 -0.0146 0.0119  0.0074  235 ALA A CB  
3617 N N   . LEU B 249 ? 0.1986 0.2762 0.2073 -0.0153 0.0149  0.0100  236 LEU A N   
3618 C CA  . LEU B 249 ? 0.2120 0.3010 0.2205 -0.0187 0.0165  0.0138  236 LEU A CA  
3619 C C   . LEU B 249 ? 0.2108 0.2953 0.2216 -0.0237 0.0174  0.0171  236 LEU A C   
3620 O O   . LEU B 249 ? 0.1980 0.2805 0.2070 -0.0293 0.0186  0.0230  236 LEU A O   
3621 C CB  . LEU B 249 ? 0.1808 0.2845 0.1882 -0.0155 0.0173  0.0095  236 LEU A CB  
3622 C CG  . LEU B 249 ? 0.2076 0.3150 0.2107 -0.0111 0.0165  0.0051  236 LEU A CG  
3623 C CD1 . LEU B 249 ? 0.2116 0.3326 0.2120 -0.0057 0.0174  0.0002  236 LEU A CD1 
3624 C CD2 . LEU B 249 ? 0.2362 0.3512 0.2377 -0.0143 0.0169  0.0106  236 LEU A CD2 
3625 N N   . PHE B 250 ? 0.1707 0.2525 0.1841 -0.0221 0.0168  0.0132  237 PHE A N   
3626 C CA  . PHE B 250 ? 0.2029 0.2826 0.2183 -0.0276 0.0173  0.0147  237 PHE A CA  
3627 C C   . PHE B 250 ? 0.2014 0.2633 0.2145 -0.0302 0.0170  0.0190  237 PHE A C   
3628 O O   . PHE B 250 ? 0.1886 0.2453 0.1994 -0.0370 0.0181  0.0224  237 PHE A O   
3629 C CB  . PHE B 250 ? 0.2122 0.2943 0.2303 -0.0236 0.0165  0.0095  237 PHE A CB  
3630 C CG  . PHE B 250 ? 0.2273 0.3069 0.2472 -0.0296 0.0165  0.0098  237 PHE A CG  
3631 C CD1 . PHE B 250 ? 0.2110 0.3055 0.2323 -0.0371 0.0177  0.0098  237 PHE A CD1 
3632 C CD2 . PHE B 250 ? 0.2545 0.3190 0.2743 -0.0283 0.0153  0.0094  237 PHE A CD2 
3633 C CE1 . PHE B 250 ? 0.2316 0.3238 0.2536 -0.0447 0.0176  0.0090  237 PHE A CE1 
3634 C CE2 . PHE B 250 ? 0.2421 0.3033 0.2621 -0.0341 0.0152  0.0086  237 PHE A CE2 
3635 C CZ  . PHE B 250 ? 0.2338 0.3082 0.2548 -0.0427 0.0162  0.0080  237 PHE A CZ  
3636 N N   . LEU B 251 ? 0.1779 0.2302 0.1906 -0.0248 0.0156  0.0185  238 LEU A N   
3637 C CA  . LEU B 251 ? 0.1903 0.2279 0.2003 -0.0243 0.0152  0.0220  238 LEU A CA  
3638 C C   . LEU B 251 ? 0.2406 0.2744 0.2451 -0.0252 0.0161  0.0284  238 LEU A C   
3639 O O   . LEU B 251 ? 0.2657 0.2855 0.2652 -0.0242 0.0163  0.0322  238 LEU A O   
3640 C CB  . LEU B 251 ? 0.1884 0.2227 0.2000 -0.0185 0.0137  0.0199  238 LEU A CB  
3641 C CG  . LEU B 251 ? 0.2194 0.2527 0.2342 -0.0170 0.0131  0.0153  238 LEU A CG  
3642 C CD1 . LEU B 251 ? 0.2290 0.2596 0.2446 -0.0131 0.0122  0.0143  238 LEU A CD1 
3643 C CD2 . LEU B 251 ? 0.2279 0.2529 0.2420 -0.0191 0.0132  0.0157  238 LEU A CD2 
3644 N N   . ALA B 252 ? 0.2056 0.2515 0.2096 -0.0258 0.0168  0.0296  239 ALA A N   
3645 C CA  . ALA B 252 ? 0.2399 0.2843 0.2377 -0.0264 0.0180  0.0366  239 ALA A CA  
3646 C C   . ALA B 252 ? 0.2625 0.3059 0.2568 -0.0349 0.0206  0.0407  239 ALA A C   
3647 O O   . ALA B 252 ? 0.2706 0.3064 0.2572 -0.0363 0.0222  0.0480  239 ALA A O   
3648 C CB  . ALA B 252 ? 0.2120 0.2719 0.2105 -0.0229 0.0174  0.0356  239 ALA A CB  
3649 N N   . SER B 253 ? 0.2135 0.2678 0.2127 -0.0402 0.0211  0.0365  240 SER A N   
3650 C CA  . SER B 253 ? 0.2504 0.3117 0.2475 -0.0500 0.0237  0.0399  240 SER A CA  
3651 C C   . SER B 253 ? 0.2802 0.3229 0.2727 -0.0586 0.0248  0.0421  240 SER A C   
3652 O O   . SER B 253 ? 0.2778 0.3054 0.2700 -0.0557 0.0232  0.0394  240 SER A O   
3653 C CB  . SER B 253 ? 0.2398 0.3240 0.2438 -0.0511 0.0237  0.0339  240 SER A CB  
3654 O OG  . SER B 253 ? 0.2717 0.3540 0.2800 -0.0522 0.0225  0.0285  240 SER A OG  
3655 N N   . ASP B 254 ? 0.2800 0.3234 0.2678 -0.0702 0.0276  0.0467  241 ASP A N   
3656 C CA  . ASP B 254 ? 0.3196 0.3451 0.3020 -0.0813 0.0288  0.0473  241 ASP A CA  
3657 C C   . ASP B 254 ? 0.3231 0.3593 0.3136 -0.0847 0.0271  0.0386  241 ASP A C   
3658 O O   . ASP B 254 ? 0.3445 0.3655 0.3308 -0.0927 0.0273  0.0370  241 ASP A O   
3659 C CB  . ASP B 254 ? 0.3367 0.3635 0.3123 -0.0956 0.0326  0.0540  241 ASP A CB  
3660 C CG  . ASP B 254 ? 0.3918 0.4025 0.3558 -0.0933 0.0349  0.0642  241 ASP A CG  
3661 O OD1 . ASP B 254 ? 0.4519 0.4517 0.4131 -0.0804 0.0334  0.0660  241 ASP A OD1 
3662 O OD2 . ASP B 254 ? 0.5498 0.5589 0.5064 -0.1055 0.0386  0.0710  241 ASP A OD2 
3663 N N   . ASP B 255 ? 0.2493 0.3112 0.2498 -0.0784 0.0256  0.0328  242 ASP A N   
3664 C CA  . ASP B 255 ? 0.2572 0.3294 0.2640 -0.0792 0.0240  0.0253  242 ASP A CA  
3665 C C   . ASP B 255 ? 0.2602 0.3122 0.2663 -0.0721 0.0216  0.0222  242 ASP A C   
3666 O O   . ASP B 255 ? 0.2836 0.3407 0.2931 -0.0738 0.0204  0.0165  242 ASP A O   
3667 C CB  . ASP B 255 ? 0.2496 0.3493 0.2643 -0.0709 0.0230  0.0206  242 ASP A CB  
3668 C CG  . ASP B 255 ? 0.2946 0.4205 0.3108 -0.0770 0.0253  0.0225  242 ASP A CG  
3669 O OD1 . ASP B 255 ? 0.3697 0.4955 0.3827 -0.0753 0.0266  0.0274  242 ASP A OD1 
3670 O OD2 . ASP B 255 ? 0.3356 0.4844 0.3560 -0.0826 0.0257  0.0190  242 ASP A OD2 
3671 N N   . SER B 256 ? 0.2462 0.2781 0.2475 -0.0646 0.0211  0.0258  243 SER A N   
3672 C CA  . SER B 256 ? 0.2547 0.2709 0.2553 -0.0577 0.0191  0.0229  243 SER A CA  
3673 C C   . SER B 256 ? 0.2813 0.2692 0.2710 -0.0592 0.0200  0.0274  243 SER A C   
3674 O O   . SER B 256 ? 0.2961 0.2711 0.2835 -0.0500 0.0186  0.0272  243 SER A O   
3675 C CB  . SER B 256 ? 0.2685 0.2898 0.2736 -0.0451 0.0175  0.0217  243 SER A CB  
3676 O OG  . SER B 256 ? 0.2685 0.2860 0.2698 -0.0418 0.0181  0.0272  243 SER A OG  
3677 N N   . ARG B 257 ? 0.2869 0.2652 0.2687 -0.0704 0.0224  0.0317  244 ARG A N   
3678 C CA  . ARG B 257 ? 0.3343 0.2814 0.3020 -0.0705 0.0239  0.0375  244 ARG A CA  
3679 C C   . ARG B 257 ? 0.3287 0.2530 0.2904 -0.0677 0.0225  0.0332  244 ARG A C   
3680 O O   . ARG B 257 ? 0.3810 0.2798 0.3310 -0.0607 0.0230  0.0372  244 ARG A O   
3681 C CB  . ARG B 257 ? 0.3329 0.2688 0.2904 -0.0844 0.0274  0.0437  244 ARG A CB  
3682 C CG  . ARG B 257 ? 0.4535 0.3965 0.4140 -0.0999 0.0276  0.0373  244 ARG A CG  
3683 C CD  . ARG B 257 ? 0.6359 0.5560 0.5830 -0.1177 0.0306  0.0399  244 ARG A CD  
3684 N NE  . ARG B 257 ? 0.7939 0.7353 0.7478 -0.1340 0.0307  0.0333  244 ARG A NE  
3685 C CZ  . ARG B 257 ? 1.2096 1.1359 1.1548 -0.1521 0.0322  0.0307  244 ARG A CZ  
3686 N NH1 . ARG B 257 ? 1.0621 0.9468 0.9915 -0.1531 0.0325  0.0304  244 ARG A NH1 
3687 N NH2 . ARG B 257 ? 1.1459 1.1014 1.0984 -0.1685 0.0330  0.0271  244 ARG A NH2 
3688 N N   . GLY B 258 ? 0.3109 0.2445 0.2792 -0.0717 0.0209  0.0251  245 GLY A N   
3689 C CA  . GLY B 258 ? 0.2994 0.2124 0.2611 -0.0697 0.0197  0.0203  245 GLY A CA  
3690 C C   . GLY B 258 ? 0.2550 0.1796 0.2254 -0.0558 0.0169  0.0160  245 GLY A C   
3691 O O   . GLY B 258 ? 0.2881 0.2041 0.2561 -0.0535 0.0156  0.0106  245 GLY A O   
3692 N N   . CYS B 259 ? 0.2592 0.2047 0.2394 -0.0483 0.0163  0.0178  246 CYS A N   
3693 C CA  . CYS B 259 ? 0.2299 0.1845 0.2168 -0.0369 0.0143  0.0150  246 CYS A CA  
3694 C C   . CYS B 259 ? 0.2909 0.2347 0.2726 -0.0253 0.0142  0.0196  246 CYS A C   
3695 O O   . CYS B 259 ? 0.2582 0.2040 0.2384 -0.0230 0.0150  0.0252  246 CYS A O   
3696 C CB  . CYS B 259 ? 0.2240 0.2032 0.2217 -0.0351 0.0139  0.0142  246 CYS A CB  
3697 S SG  . CYS B 259 ? 0.2636 0.2631 0.2680 -0.0442 0.0138  0.0089  246 CYS A SG  
3698 N N   . THR B 260 ? 0.2499 0.1847 0.2283 -0.0171 0.0131  0.0173  247 THR A N   
3699 C CA  . THR B 260 ? 0.2613 0.1943 0.2366 -0.0053 0.0128  0.0214  247 THR A CA  
3700 C C   . THR B 260 ? 0.2370 0.1745 0.2149 0.0029  0.0114  0.0174  247 THR A C   
3701 O O   . THR B 260 ? 0.2372 0.1714 0.2152 0.0000  0.0108  0.0121  247 THR A O   
3702 C CB  . THR B 260 ? 0.2955 0.2032 0.2558 -0.0020 0.0141  0.0259  247 THR A CB  
3703 O OG1 . THR B 260 ? 0.2772 0.1881 0.2344 0.0105  0.0140  0.0309  247 THR A OG1 
3704 C CG2 . THR B 260 ? 0.2975 0.1829 0.2480 -0.0016 0.0139  0.0212  247 THR A CG2 
3705 N N   . GLY B 261 ? 0.2366 0.1850 0.2168 0.0124  0.0110  0.0201  248 GLY A N   
3706 C CA  . GLY B 261 ? 0.2374 0.1931 0.2197 0.0202  0.0100  0.0175  248 GLY A CA  
3707 C C   . GLY B 261 ? 0.2518 0.2252 0.2450 0.0164  0.0096  0.0144  248 GLY A C   
3708 O O   . GLY B 261 ? 0.2458 0.2259 0.2406 0.0218  0.0091  0.0125  248 GLY A O   
3709 N N   . GLN B 262 ? 0.2206 0.2011 0.2199 0.0082  0.0099  0.0142  249 GLN A N   
3710 C CA  . GLN B 262 ? 0.2127 0.2036 0.2189 0.0050  0.0097  0.0109  249 GLN A CA  
3711 C C   . GLN B 262 ? 0.2250 0.2284 0.2367 0.0040  0.0100  0.0126  249 GLN A C   
3712 O O   . GLN B 262 ? 0.2450 0.2510 0.2567 0.0029  0.0102  0.0151  249 GLN A O   
3713 C CB  . GLN B 262 ? 0.2035 0.1925 0.2104 -0.0027 0.0098  0.0082  249 GLN A CB  
3714 C CG  . GLN B 262 ? 0.2168 0.1954 0.2186 -0.0037 0.0092  0.0043  249 GLN A CG  
3715 C CD  . GLN B 262 ? 0.2344 0.2190 0.2380 0.0016  0.0085  0.0012  249 GLN A CD  
3716 O OE1 . GLN B 262 ? 0.2739 0.2712 0.2831 0.0034  0.0086  0.0015  249 GLN A OE1 
3717 N NE2 . GLN B 262 ? 0.2840 0.2583 0.2813 0.0052  0.0079  -0.0015 249 GLN A NE2 
3718 N N   . ASN B 263 ? 0.1982 0.2082 0.2134 0.0040  0.0102  0.0109  250 ASN A N   
3719 C CA  . ASN B 263 ? 0.1997 0.2160 0.2176 0.0017  0.0109  0.0115  250 ASN A CA  
3720 C C   . ASN B 263 ? 0.1969 0.2128 0.2154 -0.0011 0.0111  0.0094  250 ASN A C   
3721 O O   . ASN B 263 ? 0.2225 0.2383 0.2410 -0.0007 0.0108  0.0072  250 ASN A O   
3722 C CB  . ASN B 263 ? 0.1825 0.2026 0.2011 0.0036  0.0115  0.0116  250 ASN A CB  
3723 C CG  . ASN B 263 ? 0.2020 0.2288 0.2210 0.0057  0.0116  0.0138  250 ASN A CG  
3724 O OD1 . ASN B 263 ? 0.2204 0.2511 0.2395 0.0055  0.0112  0.0154  250 ASN A OD1 
3725 N ND2 . ASN B 263 ? 0.2980 0.3290 0.3171 0.0082  0.0122  0.0142  250 ASN A ND2 
3726 N N   . PHE B 264 ? 0.2021 0.2201 0.2208 -0.0034 0.0115  0.0096  251 PHE A N   
3727 C CA  . PHE B 264 ? 0.1848 0.2050 0.2031 -0.0036 0.0120  0.0074  251 PHE A CA  
3728 C C   . PHE B 264 ? 0.1900 0.2074 0.2058 -0.0028 0.0128  0.0072  251 PHE A C   
3729 O O   . PHE B 264 ? 0.1917 0.2089 0.2067 -0.0055 0.0129  0.0075  251 PHE A O   
3730 C CB  . PHE B 264 ? 0.1903 0.2138 0.2088 -0.0070 0.0119  0.0078  251 PHE A CB  
3731 C CG  . PHE B 264 ? 0.2575 0.2799 0.2763 -0.0098 0.0116  0.0082  251 PHE A CG  
3732 C CD1 . PHE B 264 ? 0.3320 0.3600 0.3516 -0.0120 0.0117  0.0058  251 PHE A CD1 
3733 C CD2 . PHE B 264 ? 0.2328 0.2479 0.2495 -0.0100 0.0113  0.0108  251 PHE A CD2 
3734 C CE1 . PHE B 264 ? 0.3408 0.3655 0.3593 -0.0173 0.0115  0.0056  251 PHE A CE1 
3735 C CE2 . PHE B 264 ? 0.2491 0.2570 0.2630 -0.0131 0.0113  0.0109  251 PHE A CE2 
3736 C CZ  . PHE B 264 ? 0.2841 0.2957 0.2987 -0.0179 0.0114  0.0081  251 PHE A CZ  
3737 N N   . VAL B 265 ? 0.1651 0.1795 0.1783 0.0008  0.0136  0.0065  252 VAL A N   
3738 C CA  . VAL B 265 ? 0.1578 0.1637 0.1657 0.0011  0.0149  0.0069  252 VAL A CA  
3739 C C   . VAL B 265 ? 0.1806 0.1825 0.1830 0.0051  0.0157  0.0046  252 VAL A C   
3740 O O   . VAL B 265 ? 0.2175 0.2242 0.2192 0.0111  0.0156  0.0038  252 VAL A O   
3741 C CB  . VAL B 265 ? 0.1674 0.1704 0.1734 0.0042  0.0158  0.0088  252 VAL A CB  
3742 C CG1 . VAL B 265 ? 0.1941 0.1844 0.1924 0.0028  0.0179  0.0102  252 VAL A CG1 
3743 C CG2 . VAL B 265 ? 0.1652 0.1744 0.1762 0.0023  0.0151  0.0105  252 VAL A CG2 
3744 N N   . VAL B 266 ? 0.1728 0.1671 0.1703 0.0026  0.0163  0.0033  253 VAL A N   
3745 C CA  . VAL B 266 ? 0.1777 0.1658 0.1677 0.0076  0.0170  0.0005  253 VAL A CA  
3746 C C   . VAL B 266 ? 0.2207 0.1890 0.2004 0.0067  0.0189  0.0007  253 VAL A C   
3747 O O   . VAL B 266 ? 0.2270 0.1888 0.2040 -0.0006 0.0190  -0.0009 253 VAL A O   
3748 C CB  . VAL B 266 ? 0.1709 0.1661 0.1621 0.0059  0.0162  -0.0024 253 VAL A CB  
3749 C CG1 . VAL B 266 ? 0.2131 0.2091 0.2066 -0.0027 0.0155  -0.0025 253 VAL A CG1 
3750 C CG2 . VAL B 266 ? 0.2168 0.2042 0.1978 0.0135  0.0173  -0.0061 253 VAL A CG2 
3751 N N   . ASP B 267 ? 0.2426 0.2014 0.2160 0.0128  0.0204  0.0030  254 ASP A N   
3752 C CA  . ASP B 267 ? 0.2503 0.1882 0.2132 0.0093  0.0226  0.0047  254 ASP A CA  
3753 C C   . ASP B 267 ? 0.2943 0.2153 0.2436 0.0203  0.0247  0.0058  254 ASP A C   
3754 O O   . ASP B 267 ? 0.2861 0.1863 0.2243 0.0184  0.0272  0.0087  254 ASP A O   
3755 C CB  . ASP B 267 ? 0.2551 0.1973 0.2233 0.0025  0.0230  0.0089  254 ASP A CB  
3756 C CG  . ASP B 267 ? 0.2522 0.2010 0.2226 0.0099  0.0233  0.0125  254 ASP A CG  
3757 O OD1 . ASP B 267 ? 0.2511 0.2072 0.2221 0.0197  0.0224  0.0113  254 ASP A OD1 
3758 O OD2 . ASP B 267 ? 0.2534 0.2025 0.2246 0.0060  0.0243  0.0162  254 ASP A OD2 
3759 N N   . ALA B 268 ? 0.2550 0.1852 0.2038 0.0324  0.0240  0.0042  255 ALA A N   
3760 C CA  . ALA B 268 ? 0.2621 0.1780 0.1962 0.0462  0.0259  0.0053  255 ALA A CA  
3761 C C   . ALA B 268 ? 0.2852 0.1938 0.2148 0.0490  0.0276  0.0113  255 ALA A C   
3762 O O   . ALA B 268 ? 0.2978 0.1863 0.2116 0.0586  0.0301  0.0140  255 ALA A O   
3763 C CB  . ALA B 268 ? 0.2781 0.1675 0.1956 0.0488  0.0276  0.0021  255 ALA A CB  
3764 N N   . GLY B 269 ? 0.2701 0.1960 0.2129 0.0423  0.0264  0.0135  256 GLY A N   
3765 C CA  . GLY B 269 ? 0.2753 0.1982 0.2146 0.0451  0.0279  0.0191  256 GLY A CA  
3766 C C   . GLY B 269 ? 0.2854 0.1883 0.2178 0.0345  0.0306  0.0233  256 GLY A C   
3767 O O   . GLY B 269 ? 0.2830 0.1842 0.2118 0.0370  0.0323  0.0287  256 GLY A O   
3768 N N   . LEU B 270 ? 0.2718 0.1642 0.2034 0.0222  0.0310  0.0210  257 LEU A N   
3769 C CA  . LEU B 270 ? 0.2893 0.1635 0.2129 0.0104  0.0339  0.0248  257 LEU A CA  
3770 C C   . LEU B 270 ? 0.3025 0.1959 0.2373 0.0038  0.0338  0.0288  257 LEU A C   
3771 O O   . LEU B 270 ? 0.3142 0.1970 0.2415 -0.0018 0.0368  0.0343  257 LEU A O   
3772 C CB  . LEU B 270 ? 0.2909 0.1574 0.2136 -0.0019 0.0334  0.0197  257 LEU A CB  
3773 C CG  . LEU B 270 ? 0.2966 0.1426 0.2089 -0.0169 0.0365  0.0217  257 LEU A CG  
3774 C CD1 . LEU B 270 ? 0.3490 0.1588 0.2386 -0.0108 0.0405  0.0254  257 LEU A CD1 
3775 C CD2 . LEU B 270 ? 0.3119 0.1568 0.2254 -0.0294 0.0352  0.0152  257 LEU A CD2 
3776 N N   . SER B 271 ? 0.2669 0.1873 0.2180 0.0051  0.0304  0.0261  258 SER A N   
3777 C CA  . SER B 271 ? 0.2524 0.1908 0.2129 0.0008  0.0302  0.0291  258 SER A CA  
3778 C C   . SER B 271 ? 0.2659 0.2096 0.2246 0.0101  0.0310  0.0333  258 SER A C   
3779 O O   . SER B 271 ? 0.2827 0.2417 0.2480 0.0081  0.0309  0.0354  258 SER A O   
3780 C CB  . SER B 271 ? 0.2303 0.1900 0.2052 -0.0013 0.0268  0.0250  258 SER A CB  
3781 O OG  . SER B 271 ? 0.2428 0.2123 0.2231 0.0080  0.0244  0.0221  258 SER A OG  
3782 N N   . ILE B 272 ? 0.2684 0.2031 0.2183 0.0221  0.0316  0.0340  259 ILE A N   
3783 C CA  . ILE B 272 ? 0.2705 0.2143 0.2189 0.0324  0.0319  0.0373  259 ILE A CA  
3784 C C   . ILE B 272 ? 0.3057 0.2259 0.2359 0.0385  0.0358  0.0436  259 ILE A C   
3785 O O   . ILE B 272 ? 0.3680 0.2792 0.2890 0.0503  0.0360  0.0431  259 ILE A O   
3786 C CB  . ILE B 272 ? 0.2474 0.2092 0.2031 0.0422  0.0286  0.0322  259 ILE A CB  
3787 C CG1 . ILE B 272 ? 0.2577 0.2368 0.2284 0.0351  0.0253  0.0269  259 ILE A CG1 
3788 C CG2 . ILE B 272 ? 0.2625 0.2362 0.2159 0.0528  0.0286  0.0348  259 ILE A CG2 
3789 C CD1 . ILE B 272 ? 0.2782 0.2729 0.2549 0.0413  0.0224  0.0216  259 ILE A CD1 
3790 N N   . GLN B 273 ? 0.3172 0.2279 0.2418 0.0302  0.0390  0.0494  260 GLN A N   
3791 C CA  . GLN B 273 ? 0.4042 0.2869 0.3085 0.0347  0.0434  0.0565  260 GLN A CA  
3792 C C   . GLN B 273 ? 0.4065 0.2945 0.3068 0.0360  0.0461  0.0646  260 GLN A C   
3793 O O   . GLN B 273 ? 0.4146 0.2805 0.2970 0.0435  0.0497  0.0713  260 GLN A O   
3794 C CB  . GLN B 273 ? 0.4438 0.2990 0.3373 0.0200  0.0467  0.0585  260 GLN A CB  
3795 C CG  . GLN B 273 ? 0.5114 0.3549 0.4045 0.0162  0.0450  0.0511  260 GLN A CG  
3796 C CD  . GLN B 273 ? 0.4720 0.2895 0.3540 -0.0006 0.0481  0.0518  260 GLN A CD  
3797 O OE1 . GLN B 273 ? 0.5161 0.3057 0.3800 -0.0038 0.0526  0.0582  260 GLN A OE1 
3798 N NE2 . GLN B 273 ? 0.4942 0.3186 0.3852 -0.0114 0.0458  0.0449  260 GLN A NE2 
3799 O OXT . GLN B 273 ? 0.4002 0.3128 0.3140 0.0295  0.0449  0.0642  260 GLN A OXT 
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