data_9EW6
# 
_entry.id   9EW6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9EW6         pdb_00009ew6 10.2210/pdb9ew6/pdb 
WWPDB D_1292137252 ?            ?                   
# 
_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       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EW6 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_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              michelle.arkin@ucsf.edu 
_pdbx_contact_author.name_first         Michelle 
_pdbx_contact_author.name_last          Arkin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9366-6770 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Konstantinidou, M.' 1  ? 
'Vickery, H.'        2  ? 
'Pennings, M.A.M.'   3  ? 
'Virta, J.'          4  ? 
'Visser, E.J.'       5  ? 
'Oetelaar, M.C.M.'   6  ? 
'Overmans, M.'       7  ? 
'Neitz, J.'          8  ? 
'Ottmann, C.'        9  ? 
'Brunsveld, L.'      10 ? 
'Arkin, M.R.'        11 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Small molecule stabilization of the 14-3-3sigma/CRAF complex inhibits the MAPK pathway' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Konstantinidou, M.' 1  ? 
primary 'Vickery, H.'        2  ? 
primary 'Pennings, M.A.M.'   3  ? 
primary 'Virta, J.'          4  ? 
primary 'Visser, E.J.'       5  ? 
primary 'Oetelaar, M.C.M.'   6  ? 
primary 'Overmans, M.'       7  ? 
primary 'Neitz, J.'          8  ? 
primary 'Ottmann, C.'        9  ? 
primary 'Brunsveld, L.'      10 ? 
primary 'Arkin, M.R.'        11 ? 
# 
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 '14-3-3 protein sigma'                  26542.914 1   ?        ? ? ? 
2 polymer     syn 'Serine/threonine-protein kinase B-raf' 1012.935  1   2.7.11.1 ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                          35.453    2   ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                         24.305    1   ?        ? ? ? 
5 water       nat water                                   18.015    186 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Epithelial cell marker protein 1,Stratifin'                              
2 'Proto-oncogene B-Raf,p94,v-Raf murine sarcoma viral oncogene homolog B1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
A ? 
2 'polypeptide(L)' no yes 'DRSS(SEP)APNV' DRSSSAPNV P ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'  CL  
4 'MAGNESIUM ION' MG  
5 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   GLU n 
1 8   ARG n 
1 9   ALA n 
1 10  SER n 
1 11  LEU n 
1 12  ILE n 
1 13  GLN n 
1 14  LYS n 
1 15  ALA n 
1 16  LYS n 
1 17  LEU n 
1 18  ALA n 
1 19  GLU n 
1 20  GLN n 
1 21  ALA n 
1 22  GLU n 
1 23  ARG n 
1 24  TYR n 
1 25  GLU n 
1 26  ASP n 
1 27  MET n 
1 28  ALA n 
1 29  ALA n 
1 30  PHE n 
1 31  MET n 
1 32  LYS n 
1 33  GLY n 
1 34  ALA n 
1 35  VAL n 
1 36  GLU n 
1 37  LYS n 
1 38  GLY n 
1 39  GLU n 
1 40  GLU n 
1 41  LEU n 
1 42  SER n 
1 43  CYS n 
1 44  GLU n 
1 45  GLU n 
1 46  ARG n 
1 47  ASN n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  VAL n 
1 52  ALA n 
1 53  TYR n 
1 54  LYS n 
1 55  ASN n 
1 56  VAL n 
1 57  VAL n 
1 58  GLY n 
1 59  GLY n 
1 60  GLN n 
1 61  ARG n 
1 62  ALA n 
1 63  ALA n 
1 64  TRP n 
1 65  ARG n 
1 66  VAL n 
1 67  LEU n 
1 68  SER n 
1 69  SER n 
1 70  ILE n 
1 71  GLU n 
1 72  GLN n 
1 73  LYS n 
1 74  SER n 
1 75  ASN n 
1 76  GLU n 
1 77  GLU n 
1 78  GLY n 
1 79  SER n 
1 80  GLU n 
1 81  GLU n 
1 82  LYS n 
1 83  GLY n 
1 84  PRO n 
1 85  GLU n 
1 86  VAL n 
1 87  ARG n 
1 88  GLU n 
1 89  TYR n 
1 90  ARG n 
1 91  GLU n 
1 92  LYS n 
1 93  VAL n 
1 94  GLU n 
1 95  THR n 
1 96  GLU n 
1 97  LEU n 
1 98  GLN n 
1 99  GLY n 
1 100 VAL n 
1 101 CYS n 
1 102 ASP n 
1 103 THR n 
1 104 VAL n 
1 105 LEU n 
1 106 GLY n 
1 107 LEU n 
1 108 LEU n 
1 109 ASP n 
1 110 SER n 
1 111 HIS n 
1 112 LEU n 
1 113 ILE n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 GLY n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 SER n 
1 122 ARG n 
1 123 VAL n 
1 124 PHE n 
1 125 TYR n 
1 126 LEU n 
1 127 LYS n 
1 128 MET n 
1 129 LYS n 
1 130 GLY n 
1 131 ASP n 
1 132 TYR n 
1 133 TYR n 
1 134 ARG n 
1 135 TYR n 
1 136 LEU n 
1 137 ALA n 
1 138 GLU n 
1 139 VAL n 
1 140 ALA n 
1 141 THR n 
1 142 GLY n 
1 143 ASP n 
1 144 ASP n 
1 145 LYS n 
1 146 LYS n 
1 147 ARG n 
1 148 ILE n 
1 149 ILE n 
1 150 ASP n 
1 151 SER n 
1 152 ALA n 
1 153 ARG n 
1 154 SER n 
1 155 ALA n 
1 156 TYR n 
1 157 GLN n 
1 158 GLU n 
1 159 ALA n 
1 160 MET n 
1 161 ASP n 
1 162 ILE n 
1 163 SER n 
1 164 LYS n 
1 165 LYS n 
1 166 GLU n 
1 167 MET n 
1 168 PRO n 
1 169 PRO n 
1 170 THR n 
1 171 ASN n 
1 172 PRO n 
1 173 ILE n 
1 174 ARG n 
1 175 LEU n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 LEU n 
1 180 ASN n 
1 181 PHE n 
1 182 SER n 
1 183 VAL n 
1 184 PHE n 
1 185 HIS n 
1 186 TYR n 
1 187 GLU n 
1 188 ILE n 
1 189 ALA n 
1 190 ASN n 
1 191 SER n 
1 192 PRO n 
1 193 GLU n 
1 194 GLU n 
1 195 ALA n 
1 196 ILE n 
1 197 SER n 
1 198 LEU n 
1 199 ALA n 
1 200 LYS n 
1 201 THR n 
1 202 THR n 
1 203 PHE n 
1 204 ASP n 
1 205 GLU n 
1 206 ALA n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 LEU n 
1 211 HIS n 
1 212 THR n 
1 213 LEU n 
1 214 SER n 
1 215 GLU n 
1 216 ASP n 
1 217 SER n 
1 218 TYR n 
1 219 LYS n 
1 220 ASP n 
1 221 SER n 
1 222 THR n 
1 223 LEU n 
1 224 ILE n 
1 225 MET n 
1 226 GLN n 
1 227 LEU n 
1 228 LEU n 
1 229 ARG n 
1 230 ASP n 
1 231 ASN n 
1 232 LEU n 
1 233 THR n 
1 234 LEU n 
1 235 TRP n 
1 236 THR n 
2 1   ASP n 
2 2   ARG n 
2 3   SER n 
2 4   SER n 
2 5   SEP n 
2 6   ALA n 
2 7   PRO n 
2 8   ASN n 
2 9   VAL 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                   236 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SFN, HME1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       9 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
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 
CL  non-polymer         . 'CHLORIDE ION'  ?               'Cl -1'          35.453  
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 
MG  non-polymer         . 'MAGNESIUM ION' ?               'Mg 2'           24.305  
PHE 'L-peptide linking' y PHENYLALANINE   ?               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?               'C5 H9 N O2'     115.130 
SEP 'L-peptide linking' n PHOSPHOSERINE   PHOSPHONOSERINE 'C3 H8 N O6 P'   185.072 
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   GLY 1   -4  ?   ?   ?   A . n 
A 1 2   ALA 2   -3  ?   ?   ?   A . n 
A 1 3   MET 3   -2  ?   ?   ?   A . n 
A 1 4   GLY 4   -1  ?   ?   ?   A . n 
A 1 5   SER 5   0   ?   ?   ?   A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   GLU 7   2   2   GLU GLU A . n 
A 1 8   ARG 8   3   3   ARG ARG A . n 
A 1 9   ALA 9   4   4   ALA ALA A . n 
A 1 10  SER 10  5   5   SER SER A . n 
A 1 11  LEU 11  6   6   LEU LEU A . n 
A 1 12  ILE 12  7   7   ILE ILE A . n 
A 1 13  GLN 13  8   8   GLN GLN A . n 
A 1 14  LYS 14  9   9   LYS LYS A . n 
A 1 15  ALA 15  10  10  ALA ALA A . n 
A 1 16  LYS 16  11  11  LYS LYS A . n 
A 1 17  LEU 17  12  12  LEU LEU A . n 
A 1 18  ALA 18  13  13  ALA ALA A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  GLN 20  15  15  GLN GLN A . n 
A 1 21  ALA 21  16  16  ALA ALA A . n 
A 1 22  GLU 22  17  17  GLU GLU A . n 
A 1 23  ARG 23  18  18  ARG ARG A . n 
A 1 24  TYR 24  19  19  TYR TYR A . n 
A 1 25  GLU 25  20  20  GLU GLU A . n 
A 1 26  ASP 26  21  21  ASP ASP A . n 
A 1 27  MET 27  22  22  MET MET A . n 
A 1 28  ALA 28  23  23  ALA ALA A . n 
A 1 29  ALA 29  24  24  ALA ALA A . n 
A 1 30  PHE 30  25  25  PHE PHE A . n 
A 1 31  MET 31  26  26  MET MET A . n 
A 1 32  LYS 32  27  27  LYS LYS A . n 
A 1 33  GLY 33  28  28  GLY GLY A . n 
A 1 34  ALA 34  29  29  ALA ALA A . n 
A 1 35  VAL 35  30  30  VAL VAL A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  LYS 37  32  32  LYS LYS A . n 
A 1 38  GLY 38  33  33  GLY GLY A . n 
A 1 39  GLU 39  34  34  GLU GLU A . n 
A 1 40  GLU 40  35  35  GLU GLU A . n 
A 1 41  LEU 41  36  36  LEU LEU A . n 
A 1 42  SER 42  37  37  SER SER A . n 
A 1 43  CYS 43  38  38  CYS CYS A . n 
A 1 44  GLU 44  39  39  GLU GLU A . n 
A 1 45  GLU 45  40  40  GLU GLU A . n 
A 1 46  ARG 46  41  41  ARG ARG A . n 
A 1 47  ASN 47  42  42  ASN ASN A . n 
A 1 48  LEU 48  43  43  LEU LEU A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  SER 50  45  45  SER SER A . n 
A 1 51  VAL 51  46  46  VAL VAL A . n 
A 1 52  ALA 52  47  47  ALA ALA A . n 
A 1 53  TYR 53  48  48  TYR TYR A . n 
A 1 54  LYS 54  49  49  LYS LYS A . n 
A 1 55  ASN 55  50  50  ASN ASN A . n 
A 1 56  VAL 56  51  51  VAL VAL A . n 
A 1 57  VAL 57  52  52  VAL VAL A . n 
A 1 58  GLY 58  53  53  GLY GLY A . n 
A 1 59  GLY 59  54  54  GLY GLY A . n 
A 1 60  GLN 60  55  55  GLN GLN A . n 
A 1 61  ARG 61  56  56  ARG ARG A . n 
A 1 62  ALA 62  57  57  ALA ALA A . n 
A 1 63  ALA 63  58  58  ALA ALA A . n 
A 1 64  TRP 64  59  59  TRP TRP A . n 
A 1 65  ARG 65  60  60  ARG ARG A . n 
A 1 66  VAL 66  61  61  VAL VAL A . n 
A 1 67  LEU 67  62  62  LEU LEU A . n 
A 1 68  SER 68  63  63  SER SER A . n 
A 1 69  SER 69  64  64  SER SER A . n 
A 1 70  ILE 70  65  65  ILE ILE A . n 
A 1 71  GLU 71  66  66  GLU GLU A . n 
A 1 72  GLN 72  67  67  GLN GLN A . n 
A 1 73  LYS 73  68  68  LYS LYS A . n 
A 1 74  SER 74  69  69  SER SER A . n 
A 1 75  ASN 75  70  70  ASN ASN A . n 
A 1 76  GLU 76  71  71  GLU GLU A . n 
A 1 77  GLU 77  72  72  GLU GLU A . n 
A 1 78  GLY 78  73  73  GLY GLY A . n 
A 1 79  SER 79  74  ?   ?   ?   A . n 
A 1 80  GLU 80  75  ?   ?   ?   A . n 
A 1 81  GLU 81  76  ?   ?   ?   A . n 
A 1 82  LYS 82  77  ?   ?   ?   A . n 
A 1 83  GLY 83  78  78  GLY GLY A . n 
A 1 84  PRO 84  79  79  PRO PRO A . n 
A 1 85  GLU 85  80  80  GLU GLU A . n 
A 1 86  VAL 86  81  81  VAL VAL A . n 
A 1 87  ARG 87  82  82  ARG ARG A . n 
A 1 88  GLU 88  83  83  GLU GLU A . n 
A 1 89  TYR 89  84  84  TYR TYR A . n 
A 1 90  ARG 90  85  85  ARG ARG A . n 
A 1 91  GLU 91  86  86  GLU GLU A . n 
A 1 92  LYS 92  87  87  LYS LYS A . n 
A 1 93  VAL 93  88  88  VAL VAL A . n 
A 1 94  GLU 94  89  89  GLU GLU A . n 
A 1 95  THR 95  90  90  THR THR A . n 
A 1 96  GLU 96  91  91  GLU GLU A . n 
A 1 97  LEU 97  92  92  LEU LEU A . n 
A 1 98  GLN 98  93  93  GLN GLN A . n 
A 1 99  GLY 99  94  94  GLY GLY A . n 
A 1 100 VAL 100 95  95  VAL VAL A . n 
A 1 101 CYS 101 96  96  CYS CYS A . n 
A 1 102 ASP 102 97  97  ASP ASP A . n 
A 1 103 THR 103 98  98  THR THR A . n 
A 1 104 VAL 104 99  99  VAL VAL A . n 
A 1 105 LEU 105 100 100 LEU LEU A . n 
A 1 106 GLY 106 101 101 GLY GLY A . n 
A 1 107 LEU 107 102 102 LEU LEU A . n 
A 1 108 LEU 108 103 103 LEU LEU A . n 
A 1 109 ASP 109 104 104 ASP ASP A . n 
A 1 110 SER 110 105 105 SER SER A . n 
A 1 111 HIS 111 106 106 HIS HIS A . n 
A 1 112 LEU 112 107 107 LEU LEU A . n 
A 1 113 ILE 113 108 108 ILE ILE A . n 
A 1 114 LYS 114 109 109 LYS LYS A . n 
A 1 115 GLU 115 110 110 GLU GLU A . n 
A 1 116 ALA 116 111 111 ALA ALA A . n 
A 1 117 GLY 117 112 112 GLY GLY A . n 
A 1 118 ASP 118 113 113 ASP ASP A . n 
A 1 119 ALA 119 114 114 ALA ALA A . n 
A 1 120 GLU 120 115 115 GLU GLU A . n 
A 1 121 SER 121 116 116 SER SER A . n 
A 1 122 ARG 122 117 117 ARG ARG A . n 
A 1 123 VAL 123 118 118 VAL VAL A . n 
A 1 124 PHE 124 119 119 PHE PHE A . n 
A 1 125 TYR 125 120 120 TYR TYR A . n 
A 1 126 LEU 126 121 121 LEU LEU A . n 
A 1 127 LYS 127 122 122 LYS LYS A . n 
A 1 128 MET 128 123 123 MET MET A . n 
A 1 129 LYS 129 124 124 LYS LYS A . n 
A 1 130 GLY 130 125 125 GLY GLY A . n 
A 1 131 ASP 131 126 126 ASP ASP A . n 
A 1 132 TYR 132 127 127 TYR TYR A . n 
A 1 133 TYR 133 128 128 TYR TYR A . n 
A 1 134 ARG 134 129 129 ARG ARG A . n 
A 1 135 TYR 135 130 130 TYR TYR A . n 
A 1 136 LEU 136 131 131 LEU LEU A . n 
A 1 137 ALA 137 132 132 ALA ALA A . n 
A 1 138 GLU 138 133 133 GLU GLU A . n 
A 1 139 VAL 139 134 134 VAL VAL A . n 
A 1 140 ALA 140 135 135 ALA ALA A . n 
A 1 141 THR 141 136 136 THR THR A . n 
A 1 142 GLY 142 137 137 GLY GLY A . n 
A 1 143 ASP 143 138 138 ASP ASP A . n 
A 1 144 ASP 144 139 139 ASP ASP A . n 
A 1 145 LYS 145 140 140 LYS LYS A . n 
A 1 146 LYS 146 141 141 LYS LYS A . n 
A 1 147 ARG 147 142 142 ARG ARG A . n 
A 1 148 ILE 148 143 143 ILE ILE A . n 
A 1 149 ILE 149 144 144 ILE ILE A . n 
A 1 150 ASP 150 145 145 ASP ASP A . n 
A 1 151 SER 151 146 146 SER SER A . n 
A 1 152 ALA 152 147 147 ALA ALA A . n 
A 1 153 ARG 153 148 148 ARG ARG A . n 
A 1 154 SER 154 149 149 SER SER A . n 
A 1 155 ALA 155 150 150 ALA ALA A . n 
A 1 156 TYR 156 151 151 TYR TYR A . n 
A 1 157 GLN 157 152 152 GLN GLN A . n 
A 1 158 GLU 158 153 153 GLU GLU A . n 
A 1 159 ALA 159 154 154 ALA ALA A . n 
A 1 160 MET 160 155 155 MET MET A . n 
A 1 161 ASP 161 156 156 ASP ASP A . n 
A 1 162 ILE 162 157 157 ILE ILE A . n 
A 1 163 SER 163 158 158 SER SER A . n 
A 1 164 LYS 164 159 159 LYS LYS A . n 
A 1 165 LYS 165 160 160 LYS LYS A . n 
A 1 166 GLU 166 161 161 GLU GLU A . n 
A 1 167 MET 167 162 162 MET MET A . n 
A 1 168 PRO 168 163 163 PRO PRO A . n 
A 1 169 PRO 169 164 164 PRO PRO A . n 
A 1 170 THR 170 165 165 THR THR A . n 
A 1 171 ASN 171 166 166 ASN ASN A . n 
A 1 172 PRO 172 167 167 PRO PRO A . n 
A 1 173 ILE 173 168 168 ILE ILE A . n 
A 1 174 ARG 174 169 169 ARG ARG A . n 
A 1 175 LEU 175 170 170 LEU LEU A . n 
A 1 176 GLY 176 171 171 GLY GLY A . n 
A 1 177 LEU 177 172 172 LEU LEU A . n 
A 1 178 ALA 178 173 173 ALA ALA A . n 
A 1 179 LEU 179 174 174 LEU LEU A . n 
A 1 180 ASN 180 175 175 ASN ASN A . n 
A 1 181 PHE 181 176 176 PHE PHE A . n 
A 1 182 SER 182 177 177 SER SER A . n 
A 1 183 VAL 183 178 178 VAL VAL A . n 
A 1 184 PHE 184 179 179 PHE PHE A . n 
A 1 185 HIS 185 180 180 HIS HIS A . n 
A 1 186 TYR 186 181 181 TYR TYR A . n 
A 1 187 GLU 187 182 182 GLU GLU A . n 
A 1 188 ILE 188 183 183 ILE ILE A . n 
A 1 189 ALA 189 184 184 ALA ALA A . n 
A 1 190 ASN 190 185 185 ASN ASN A . n 
A 1 191 SER 191 186 186 SER SER A . n 
A 1 192 PRO 192 187 187 PRO PRO A . n 
A 1 193 GLU 193 188 188 GLU GLU A . n 
A 1 194 GLU 194 189 189 GLU GLU A . n 
A 1 195 ALA 195 190 190 ALA ALA A . n 
A 1 196 ILE 196 191 191 ILE ILE A . n 
A 1 197 SER 197 192 192 SER SER A . n 
A 1 198 LEU 198 193 193 LEU LEU A . n 
A 1 199 ALA 199 194 194 ALA ALA A . n 
A 1 200 LYS 200 195 195 LYS LYS A . n 
A 1 201 THR 201 196 196 THR THR A . n 
A 1 202 THR 202 197 197 THR THR A . n 
A 1 203 PHE 203 198 198 PHE PHE A . n 
A 1 204 ASP 204 199 199 ASP ASP A . n 
A 1 205 GLU 205 200 200 GLU GLU A . n 
A 1 206 ALA 206 201 201 ALA ALA A . n 
A 1 207 MET 207 202 202 MET MET A . n 
A 1 208 ALA 208 203 203 ALA ALA A . n 
A 1 209 ASP 209 204 204 ASP ASP A . n 
A 1 210 LEU 210 205 205 LEU LEU A . n 
A 1 211 HIS 211 206 206 HIS HIS A . n 
A 1 212 THR 212 207 207 THR THR A . n 
A 1 213 LEU 213 208 208 LEU LEU A . n 
A 1 214 SER 214 209 209 SER SER A . n 
A 1 215 GLU 215 210 210 GLU GLU A . n 
A 1 216 ASP 216 211 211 ASP ASP A . n 
A 1 217 SER 217 212 212 SER SER A . n 
A 1 218 TYR 218 213 213 TYR TYR A . n 
A 1 219 LYS 219 214 214 LYS LYS A . n 
A 1 220 ASP 220 215 215 ASP ASP A . n 
A 1 221 SER 221 216 216 SER SER A . n 
A 1 222 THR 222 217 217 THR THR A . n 
A 1 223 LEU 223 218 218 LEU LEU A . n 
A 1 224 ILE 224 219 219 ILE ILE A . n 
A 1 225 MET 225 220 220 MET MET A . n 
A 1 226 GLN 226 221 221 GLN GLN A . n 
A 1 227 LEU 227 222 222 LEU LEU A . n 
A 1 228 LEU 228 223 223 LEU LEU A . n 
A 1 229 ARG 229 224 224 ARG ARG A . n 
A 1 230 ASP 230 225 225 ASP ASP A . n 
A 1 231 ASN 231 226 226 ASN ASN A . n 
A 1 232 LEU 232 227 227 LEU LEU A . n 
A 1 233 THR 233 228 228 THR THR A . n 
A 1 234 LEU 234 229 229 LEU LEU A . n 
A 1 235 TRP 235 230 230 TRP TRP A . n 
A 1 236 THR 236 231 231 THR THR A . n 
B 2 1   ASP 1   361 361 ASP ASP P . n 
B 2 2   ARG 2   362 362 ARG ARG P . n 
B 2 3   SER 3   363 363 SER SER P . n 
B 2 4   SER 4   364 364 SER SER P . n 
B 2 5   SEP 5   365 365 SEP SEP P . n 
B 2 6   ALA 6   366 366 ALA ALA P . n 
B 2 7   PRO 7   367 367 PRO PRO P . n 
B 2 8   ASN 8   368 368 ASN ASN P . n 
B 2 9   VAL 9   369 369 VAL VAL P . 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 3 CL  1   301 232 CL  CL  A . 
D 4 MG  1   302 233 MG  MG  A . 
E 3 CL  1   303 1   CL  CL  A . 
F 5 HOH 1   401 220 HOH HOH A . 
F 5 HOH 2   402 96  HOH HOH A . 
F 5 HOH 3   403 92  HOH HOH A . 
F 5 HOH 4   404 216 HOH HOH A . 
F 5 HOH 5   405 29  HOH HOH A . 
F 5 HOH 6   406 182 HOH HOH A . 
F 5 HOH 7   407 116 HOH HOH A . 
F 5 HOH 8   408 145 HOH HOH A . 
F 5 HOH 9   409 191 HOH HOH A . 
F 5 HOH 10  410 155 HOH HOH A . 
F 5 HOH 11  411 60  HOH HOH A . 
F 5 HOH 12  412 148 HOH HOH A . 
F 5 HOH 13  413 193 HOH HOH A . 
F 5 HOH 14  414 85  HOH HOH A . 
F 5 HOH 15  415 156 HOH HOH A . 
F 5 HOH 16  416 13  HOH HOH A . 
F 5 HOH 17  417 12  HOH HOH A . 
F 5 HOH 18  418 30  HOH HOH A . 
F 5 HOH 19  419 49  HOH HOH A . 
F 5 HOH 20  420 45  HOH HOH A . 
F 5 HOH 21  421 239 HOH HOH A . 
F 5 HOH 22  422 126 HOH HOH A . 
F 5 HOH 23  423 188 HOH HOH A . 
F 5 HOH 24  424 102 HOH HOH A . 
F 5 HOH 25  425 11  HOH HOH A . 
F 5 HOH 26  426 212 HOH HOH A . 
F 5 HOH 27  427 114 HOH HOH A . 
F 5 HOH 28  428 223 HOH HOH A . 
F 5 HOH 29  429 64  HOH HOH A . 
F 5 HOH 30  430 40  HOH HOH A . 
F 5 HOH 31  431 8   HOH HOH A . 
F 5 HOH 32  432 129 HOH HOH A . 
F 5 HOH 33  433 93  HOH HOH A . 
F 5 HOH 34  434 25  HOH HOH A . 
F 5 HOH 35  435 16  HOH HOH A . 
F 5 HOH 36  436 55  HOH HOH A . 
F 5 HOH 37  437 101 HOH HOH A . 
F 5 HOH 38  438 74  HOH HOH A . 
F 5 HOH 39  439 18  HOH HOH A . 
F 5 HOH 40  440 103 HOH HOH A . 
F 5 HOH 41  441 95  HOH HOH A . 
F 5 HOH 42  442 226 HOH HOH A . 
F 5 HOH 43  443 77  HOH HOH A . 
F 5 HOH 44  444 190 HOH HOH A . 
F 5 HOH 45  445 139 HOH HOH A . 
F 5 HOH 46  446 26  HOH HOH A . 
F 5 HOH 47  447 108 HOH HOH A . 
F 5 HOH 48  448 71  HOH HOH A . 
F 5 HOH 49  449 46  HOH HOH A . 
F 5 HOH 50  450 36  HOH HOH A . 
F 5 HOH 51  451 38  HOH HOH A . 
F 5 HOH 52  452 82  HOH HOH A . 
F 5 HOH 53  453 32  HOH HOH A . 
F 5 HOH 54  454 57  HOH HOH A . 
F 5 HOH 55  455 66  HOH HOH A . 
F 5 HOH 56  456 33  HOH HOH A . 
F 5 HOH 57  457 104 HOH HOH A . 
F 5 HOH 58  458 236 HOH HOH A . 
F 5 HOH 59  459 87  HOH HOH A . 
F 5 HOH 60  460 177 HOH HOH A . 
F 5 HOH 61  461 83  HOH HOH A . 
F 5 HOH 62  462 181 HOH HOH A . 
F 5 HOH 63  463 109 HOH HOH A . 
F 5 HOH 64  464 214 HOH HOH A . 
F 5 HOH 65  465 197 HOH HOH A . 
F 5 HOH 66  466 237 HOH HOH A . 
F 5 HOH 67  467 80  HOH HOH A . 
F 5 HOH 68  468 61  HOH HOH A . 
F 5 HOH 69  469 17  HOH HOH A . 
F 5 HOH 70  470 7   HOH HOH A . 
F 5 HOH 71  471 160 HOH HOH A . 
F 5 HOH 72  472 89  HOH HOH A . 
F 5 HOH 73  473 142 HOH HOH A . 
F 5 HOH 74  474 111 HOH HOH A . 
F 5 HOH 75  475 23  HOH HOH A . 
F 5 HOH 76  476 141 HOH HOH A . 
F 5 HOH 77  477 21  HOH HOH A . 
F 5 HOH 78  478 22  HOH HOH A . 
F 5 HOH 79  479 31  HOH HOH A . 
F 5 HOH 80  480 240 HOH HOH A . 
F 5 HOH 81  481 62  HOH HOH A . 
F 5 HOH 82  482 58  HOH HOH A . 
F 5 HOH 83  483 56  HOH HOH A . 
F 5 HOH 84  484 47  HOH HOH A . 
F 5 HOH 85  485 14  HOH HOH A . 
F 5 HOH 86  486 44  HOH HOH A . 
F 5 HOH 87  487 63  HOH HOH A . 
F 5 HOH 88  488 19  HOH HOH A . 
F 5 HOH 89  489 41  HOH HOH A . 
F 5 HOH 90  490 50  HOH HOH A . 
F 5 HOH 91  491 20  HOH HOH A . 
F 5 HOH 92  492 183 HOH HOH A . 
F 5 HOH 93  493 72  HOH HOH A . 
F 5 HOH 94  494 189 HOH HOH A . 
F 5 HOH 95  495 179 HOH HOH A . 
F 5 HOH 96  496 54  HOH HOH A . 
F 5 HOH 97  497 28  HOH HOH A . 
F 5 HOH 98  498 52  HOH HOH A . 
F 5 HOH 99  499 196 HOH HOH A . 
F 5 HOH 100 500 219 HOH HOH A . 
F 5 HOH 101 501 34  HOH HOH A . 
F 5 HOH 102 502 9   HOH HOH A . 
F 5 HOH 103 503 194 HOH HOH A . 
F 5 HOH 104 504 48  HOH HOH A . 
F 5 HOH 105 505 78  HOH HOH A . 
F 5 HOH 106 506 184 HOH HOH A . 
F 5 HOH 107 507 232 HOH HOH A . 
F 5 HOH 108 508 51  HOH HOH A . 
F 5 HOH 109 509 132 HOH HOH A . 
F 5 HOH 110 510 180 HOH HOH A . 
F 5 HOH 111 511 10  HOH HOH A . 
F 5 HOH 112 512 6   HOH HOH A . 
F 5 HOH 113 513 91  HOH HOH A . 
F 5 HOH 114 514 136 HOH HOH A . 
F 5 HOH 115 515 3   HOH HOH A . 
F 5 HOH 116 516 195 HOH HOH A . 
F 5 HOH 117 517 27  HOH HOH A . 
F 5 HOH 118 518 84  HOH HOH A . 
F 5 HOH 119 519 4   HOH HOH A . 
F 5 HOH 120 520 69  HOH HOH A . 
F 5 HOH 121 521 79  HOH HOH A . 
F 5 HOH 122 522 203 HOH HOH A . 
F 5 HOH 123 523 200 HOH HOH A . 
F 5 HOH 124 524 224 HOH HOH A . 
F 5 HOH 125 525 35  HOH HOH A . 
F 5 HOH 126 526 43  HOH HOH A . 
F 5 HOH 127 527 37  HOH HOH A . 
F 5 HOH 128 528 185 HOH HOH A . 
F 5 HOH 129 529 186 HOH HOH A . 
F 5 HOH 130 530 234 HOH HOH A . 
F 5 HOH 131 531 39  HOH HOH A . 
F 5 HOH 132 532 213 HOH HOH A . 
F 5 HOH 133 533 172 HOH HOH A . 
F 5 HOH 134 534 88  HOH HOH A . 
F 5 HOH 135 535 137 HOH HOH A . 
F 5 HOH 136 536 151 HOH HOH A . 
F 5 HOH 137 537 217 HOH HOH A . 
F 5 HOH 138 538 76  HOH HOH A . 
F 5 HOH 139 539 94  HOH HOH A . 
F 5 HOH 140 540 67  HOH HOH A . 
F 5 HOH 141 541 163 HOH HOH A . 
F 5 HOH 142 542 211 HOH HOH A . 
F 5 HOH 143 543 131 HOH HOH A . 
F 5 HOH 144 544 24  HOH HOH A . 
F 5 HOH 145 545 115 HOH HOH A . 
F 5 HOH 146 546 209 HOH HOH A . 
F 5 HOH 147 547 157 HOH HOH A . 
F 5 HOH 148 548 167 HOH HOH A . 
F 5 HOH 149 549 81  HOH HOH A . 
F 5 HOH 150 550 205 HOH HOH A . 
F 5 HOH 151 551 227 HOH HOH A . 
F 5 HOH 152 552 222 HOH HOH A . 
F 5 HOH 153 553 161 HOH HOH A . 
F 5 HOH 154 554 99  HOH HOH A . 
F 5 HOH 155 555 166 HOH HOH A . 
F 5 HOH 156 556 202 HOH HOH A . 
F 5 HOH 157 557 171 HOH HOH A . 
F 5 HOH 158 558 178 HOH HOH A . 
F 5 HOH 159 559 70  HOH HOH A . 
F 5 HOH 160 560 135 HOH HOH A . 
F 5 HOH 161 561 117 HOH HOH A . 
F 5 HOH 162 562 42  HOH HOH A . 
F 5 HOH 163 563 164 HOH HOH A . 
F 5 HOH 164 564 100 HOH HOH A . 
F 5 HOH 165 565 159 HOH HOH A . 
F 5 HOH 166 566 230 HOH HOH A . 
F 5 HOH 167 567 113 HOH HOH A . 
F 5 HOH 168 568 68  HOH HOH A . 
F 5 HOH 169 569 73  HOH HOH A . 
F 5 HOH 170 570 165 HOH HOH A . 
F 5 HOH 171 571 119 HOH HOH A . 
F 5 HOH 172 572 140 HOH HOH A . 
F 5 HOH 173 573 146 HOH HOH A . 
F 5 HOH 174 574 176 HOH HOH A . 
F 5 HOH 175 575 158 HOH HOH A . 
F 5 HOH 176 576 204 HOH HOH A . 
F 5 HOH 177 577 168 HOH HOH A . 
F 5 HOH 178 578 162 HOH HOH A . 
F 5 HOH 179 579 118 HOH HOH A . 
G 5 HOH 1   401 59  HOH HOH P . 
G 5 HOH 2   402 53  HOH HOH P . 
G 5 HOH 3   403 5   HOH HOH P . 
G 5 HOH 4   404 75  HOH HOH P . 
G 5 HOH 5   405 15  HOH HOH P . 
G 5 HOH 6   406 149 HOH HOH P . 
G 5 HOH 7   407 175 HOH HOH P . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PDB-REDO ? ? ? . 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? . 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? . 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? . 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EW6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     81.783 
_cell.length_a_esd                 ? 
_cell.length_b                     96.043 
_cell.length_b_esd                 ? 
_cell.length_c                     80.440 
_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                         9EW6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   9EW6 
_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             2.97 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.52 
_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    
;0.095 M HEPES pH=7.1-7.7
0.19 M CaCl2 
5% glycerol
24-29% PEG400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-19 
_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   0.873128 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.873128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EW6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               80.44 
_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                                     38175 
_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                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.65 
_reflns_shell.d_res_low                                     1.68 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1908 
_reflns_shell.percent_possible_obs                          ? 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.694 
_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                                  ? 
_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]                            -0.40 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -5.69 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            6.10 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.648 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.958 
_refine.details                                  
;HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
U VALUES : REFINED INDIVIDUALLY
;
_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                                 9EW6 
_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                            1.65 
_refine.ls_d_res_low                             62.27 
_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                     36201 
_refine.ls_number_reflns_R_free                  1933 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.18 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18669 
_refine.ls_R_factor_R_free                       0.22100 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18484 
_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                       0.107 
_refine.pdbx_overall_ESU_R_Free                  0.089 
_refine.pdbx_solvent_vdw_probe_radii             1.00 
_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                             6.792 
_refine.overall_SU_ML                            0.094 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.65 
_refine_hist.d_res_low                        62.27 
_refine_hist.number_atoms_solvent             186 
_refine_hist.number_atoms_total               2055 
_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        1866 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         3 
_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' ? 0.013  0.016  1905 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1808 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.295  1.822  2570 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 0.499  1.569  4178 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 6.248  5.277  253  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 13.891 10.000 357  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 0.067  0.200  285  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  2237 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  415  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 6.224  3.534  947  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 6.212  3.534  947  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 9.050  6.350  1180 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 9.049  6.353  1181 ? r_mcangle_other        ? ? 
'X-RAY DIFFRACTION' ? 7.130  3.875  958  ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 7.112  3.876  958  ? r_scbond_other         ? ? 
'X-RAY DIFFRACTION' ? 10.574 6.986  1388 ? r_scangle_other        ? ? 
'X-RAY DIFFRACTION' ? 16.656 35.900 2257 ? r_long_range_B_refined ? ? 
'X-RAY DIFFRACTION' ? 15.646 34.450 2213 ? r_long_range_B_other   ? ? 
'X-RAY DIFFRACTION' ? 4.205  3.000  3713 ? r_rigid_bond_restr     ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.650 
_refine_ls_shell.d_res_low                        1.693 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             139 
_refine_ls_shell.number_reflns_R_work             2650 
_refine_ls_shell.percent_reflns_obs               99.68 
_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                  0.362 
_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                  0.374 
# 
_struct.entry_id                     9EW6 
_struct.title                        'Binary structure of 14-3-3s and BRAF phosphopeptide (pS365)' 
_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        9EW6 
_struct_keywords.text            '14-3-3 protein, protein-protein interaction, PEPTIDE BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'PEPTIDE BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
F N N 5 ? 
G N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP 1433S_HUMAN P31947 ? 1 
;MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPE
VREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKK
EMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
1   
2 UNP BRAF_HUMAN  P15056 ? 2 DRSSSAPNV 361 
# 
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 9EW6 A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 9EW6 P 1 ? 9   ? P15056 361 ? 369 ? 361 369 
# 
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 9EW6 GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 9EW6 ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 9EW6 MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 9EW6 GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 9EW6 SER A 5 ? UNP P31947 ? ? 'expression tag' 0  5 
# 
_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)' 5060  ? 
1 MORE         -71   ? 
1 'SSA (A^2)'  22470 ? 
# 
_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,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
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' 4_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 GLU A 7   ? ALA A 21  ? GLU A 2   ALA A 16  1 ? 15 
HELX_P HELX_P2  AA2 ARG A 23  ? GLU A 36  ? ARG A 18  GLU A 31  1 ? 14 
HELX_P HELX_P3  AA3 SER A 42  ? ASN A 75  ? SER A 37  ASN A 70  1 ? 34 
HELX_P HELX_P4  AA4 PRO A 84  ? HIS A 111 ? PRO A 79  HIS A 106 1 ? 28 
HELX_P HELX_P5  AA5 HIS A 111 ? ALA A 116 ? HIS A 106 ALA A 111 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 118 ? ALA A 140 ? ASP A 113 ALA A 135 1 ? 23 
HELX_P HELX_P7  AA7 THR A 141 ? MET A 167 ? THR A 136 MET A 162 1 ? 27 
HELX_P HELX_P8  AA8 ASN A 171 ? ILE A 188 ? ASN A 166 ILE A 183 1 ? 18 
HELX_P HELX_P9  AA9 SER A 191 ? ALA A 208 ? SER A 186 ALA A 203 1 ? 18 
HELX_P HELX_P10 AB1 ASP A 209 ? LEU A 213 ? ASP A 204 LEU A 208 5 ? 5  
HELX_P HELX_P11 AB2 SER A 214 ? THR A 236 ? SER A 209 THR A 231 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? B SER 4  C   ? ? ? 1_555 B SEP 5 N  ? ? P SER 364 P SEP 365 1_555 ? ? ? ? ? ? ? 1.346 ? ? 
covale2 covale both ? B SEP 5  C   ? ? ? 1_555 B ALA 6 N  ? ? P SEP 365 P ALA 366 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
metalc1 metalc ?    ? A GLU 94 OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.990 ? ? 
metalc2 metalc ?    ? A GLN 98 OE1 ? ? ? 1_555 D MG  . MG ? ? A GLN 93  A MG  302 1_555 ? ? ? ? ? ? ? 2.622 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OE2 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   GLU 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    94 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    GLU 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     89 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   D 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     302 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OE1 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   GLN 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    98 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    GLN 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     93 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 111.3 
_pdbx_struct_conn_angle.value_esd             ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      SEP 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       5 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       SEP 
_pdbx_modification_feature.auth_asym_id                       P 
_pdbx_modification_feature.auth_seq_id                        365 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                SER 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        SEP 
_pdbx_modification_feature.type                               Phosphorylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
_pdbx_entry_details.entry_id                   9EW6 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 18  ? ? -100.21 74.66  
2 1 ASN A 70  ? ? -81.18  39.36  
3 1 GLU A 71  ? ? -122.39 -78.22 
4 1 HIS A 106 ? ? -133.18 -62.02 
5 1 SER A 186 ? ? -118.18 75.08  
# 
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 A 41  ? ? 0.149 'SIDE CHAIN' 
2 1 ARG A 56  ? ? 0.148 'SIDE CHAIN' 
3 1 ARG A 117 ? ? 0.176 'SIDE CHAIN' 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    SEP 
_pdbx_struct_mod_residue.label_seq_id     5 
_pdbx_struct_mod_residue.auth_asym_id     P 
_pdbx_struct_mod_residue.auth_comp_id     SEP 
_pdbx_struct_mod_residue.auth_seq_id      365 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   SER 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -4 ? A GLY 1  
2 1 Y 1 A ALA -3 ? A ALA 2  
3 1 Y 1 A MET -2 ? A MET 3  
4 1 Y 1 A GLY -1 ? A GLY 4  
5 1 Y 1 A SER 0  ? A SER 5  
6 1 Y 1 A SER 74 ? A SER 79 
7 1 Y 1 A GLU 75 ? A GLU 80 
8 1 Y 1 A GLU 76 ? A GLU 81 
9 1 Y 1 A LYS 77 ? A LYS 82 
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MG  MG   MG N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SEP N    N  N N 292 
SEP CA   C  N S 293 
SEP CB   C  N N 294 
SEP OG   O  N N 295 
SEP C    C  N N 296 
SEP O    O  N N 297 
SEP OXT  O  N N 298 
SEP P    P  N N 299 
SEP O1P  O  N N 300 
SEP O2P  O  N N 301 
SEP O3P  O  N N 302 
SEP H    H  N N 303 
SEP H2   H  N N 304 
SEP HA   H  N N 305 
SEP HB2  H  N N 306 
SEP HB3  H  N N 307 
SEP HXT  H  N N 308 
SEP HOP2 H  N N 309 
SEP HOP3 H  N N 310 
SER N    N  N N 311 
SER CA   C  N S 312 
SER C    C  N N 313 
SER O    O  N N 314 
SER CB   C  N N 315 
SER OG   O  N N 316 
SER OXT  O  N N 317 
SER H    H  N N 318 
SER H2   H  N N 319 
SER HA   H  N N 320 
SER HB2  H  N N 321 
SER HB3  H  N N 322 
SER HG   H  N N 323 
SER HXT  H  N N 324 
THR N    N  N N 325 
THR CA   C  N S 326 
THR C    C  N N 327 
THR O    O  N N 328 
THR CB   C  N R 329 
THR OG1  O  N N 330 
THR CG2  C  N N 331 
THR OXT  O  N N 332 
THR H    H  N N 333 
THR H2   H  N N 334 
THR HA   H  N N 335 
THR HB   H  N N 336 
THR HG1  H  N N 337 
THR HG21 H  N N 338 
THR HG22 H  N N 339 
THR HG23 H  N N 340 
THR HXT  H  N N 341 
TRP N    N  N N 342 
TRP CA   C  N S 343 
TRP C    C  N N 344 
TRP O    O  N N 345 
TRP CB   C  N N 346 
TRP CG   C  Y N 347 
TRP CD1  C  Y N 348 
TRP CD2  C  Y N 349 
TRP NE1  N  Y N 350 
TRP CE2  C  Y N 351 
TRP CE3  C  Y N 352 
TRP CZ2  C  Y N 353 
TRP CZ3  C  Y N 354 
TRP CH2  C  Y N 355 
TRP OXT  O  N N 356 
TRP H    H  N N 357 
TRP H2   H  N N 358 
TRP HA   H  N N 359 
TRP HB2  H  N N 360 
TRP HB3  H  N N 361 
TRP HD1  H  N N 362 
TRP HE1  H  N N 363 
TRP HE3  H  N N 364 
TRP HZ2  H  N N 365 
TRP HZ3  H  N N 366 
TRP HH2  H  N N 367 
TRP HXT  H  N N 368 
TYR N    N  N N 369 
TYR CA   C  N S 370 
TYR C    C  N N 371 
TYR O    O  N N 372 
TYR CB   C  N N 373 
TYR CG   C  Y N 374 
TYR CD1  C  Y N 375 
TYR CD2  C  Y N 376 
TYR CE1  C  Y N 377 
TYR CE2  C  Y N 378 
TYR CZ   C  Y N 379 
TYR OH   O  N N 380 
TYR OXT  O  N N 381 
TYR H    H  N N 382 
TYR H2   H  N N 383 
TYR HA   H  N N 384 
TYR HB2  H  N N 385 
TYR HB3  H  N N 386 
TYR HD1  H  N N 387 
TYR HD2  H  N N 388 
TYR HE1  H  N N 389 
TYR HE2  H  N N 390 
TYR HH   H  N N 391 
TYR HXT  H  N N 392 
VAL N    N  N N 393 
VAL CA   C  N S 394 
VAL C    C  N N 395 
VAL O    O  N N 396 
VAL CB   C  N N 397 
VAL CG1  C  N N 398 
VAL CG2  C  N N 399 
VAL OXT  O  N N 400 
VAL H    H  N N 401 
VAL H2   H  N N 402 
VAL HA   H  N N 403 
VAL HB   H  N N 404 
VAL HG11 H  N N 405 
VAL HG12 H  N N 406 
VAL HG13 H  N N 407 
VAL HG21 H  N N 408 
VAL HG22 H  N N 409 
VAL HG23 H  N N 410 
VAL HXT  H  N N 411 
# 
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 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
VAL N   CA   sing N N 376 
VAL N   H    sing N N 377 
VAL N   H2   sing N N 378 
VAL CA  C    sing N N 379 
VAL CA  CB   sing N N 380 
VAL CA  HA   sing N N 381 
VAL C   O    doub N N 382 
VAL C   OXT  sing N N 383 
VAL CB  CG1  sing N N 384 
VAL CB  CG2  sing N N 385 
VAL CB  HB   sing N N 386 
VAL CG1 HG11 sing N N 387 
VAL CG1 HG12 sing N N 388 
VAL CG1 HG13 sing N N 389 
VAL CG2 HG21 sing N N 390 
VAL CG2 HG22 sing N N 391 
VAL CG2 HG23 sing N N 392 
VAL OXT HXT  sing N N 393 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM147696 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3IQU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EW6 
_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]   0.012227 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010412 
_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]   0.012432 
_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  
CL 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET A 1 6   ? -29.936 -8.199  -17.722 1.00 69.48  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 6   ? -29.900 -7.890  -19.141 1.00 70.38  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 6   ? -28.997 -8.926  -19.812 1.00 65.20  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 6   ? -28.695 -9.951  -19.212 1.00 67.99  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 6   ? -29.419 -6.440  -19.377 1.00 78.29  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 6   ? -27.943 -6.202  -19.071 1.00 84.08  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 6   ? -27.515 -4.436  -19.122 1.00 98.39  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 6   ? -25.977 -4.452  -18.171 1.00 93.27  ? 1   MET A CE  1 
ATOM   9    N  N   . GLU A 1 7   ? -28.588 -8.666  -21.061 1.00 55.43  ? 2   GLU A N   1 
ATOM   10   C  CA  . GLU A 1 7   ? -27.713 -9.566  -21.792 1.00 46.60  ? 2   GLU A CA  1 
ATOM   11   C  C   . GLU A 1 7   ? -26.435 -9.948  -21.038 1.00 42.73  ? 2   GLU A C   1 
ATOM   12   O  O   . GLU A 1 7   ? -25.830 -9.137  -20.322 1.00 39.25  ? 2   GLU A O   1 
ATOM   13   C  CB  . GLU A 1 7   ? -27.418 -8.930  -23.148 1.00 47.90  ? 2   GLU A CB  1 
ATOM   14   C  CG  . GLU A 1 7   ? -26.135 -9.316  -23.828 1.00 46.67  ? 2   GLU A CG  1 
ATOM   15   C  CD  . GLU A 1 7   ? -26.286 -9.474  -25.333 1.00 51.82  ? 2   GLU A CD  1 
ATOM   16   O  OE1 . GLU A 1 7   ? -26.671 -8.505  -26.034 1.00 59.70  ? 2   GLU A OE1 1 
ATOM   17   O  OE2 . GLU A 1 7   ? -26.041 -10.604 -25.805 1.00 56.90  ? 2   GLU A OE2 1 
ATOM   18   N  N   . ARG A 1 8   ? -26.043 -11.223 -21.184 1.00 39.41  ? 3   ARG A N   1 
ATOM   19   C  CA  . ARG A 1 8   ? -24.911 -11.762 -20.445 1.00 36.34  ? 3   ARG A CA  1 
ATOM   20   C  C   . ARG A 1 8   ? -23.622 -11.026 -20.783 1.00 36.36  ? 3   ARG A C   1 
ATOM   21   O  O   . ARG A 1 8   ? -22.797 -10.722 -19.939 1.00 35.86  ? 3   ARG A O   1 
ATOM   22   C  CB  . ARG A 1 8   ? -24.732 -13.248 -20.745 1.00 37.49  ? 3   ARG A CB  1 
ATOM   23   C  CG  . ARG A 1 8   ? -23.615 -13.928 -19.951 1.00 37.59  ? 3   ARG A CG  1 
ATOM   24   C  CD  . ARG A 1 8   ? -23.462 -15.383 -20.346 1.00 36.52  ? 3   ARG A CD  1 
ATOM   25   N  NE  . ARG A 1 8   ? -22.550 -16.106 -19.465 1.00 35.79  ? 3   ARG A NE  1 
ATOM   26   C  CZ  . ARG A 1 8   ? -21.229 -15.979 -19.464 1.00 34.68  ? 3   ARG A CZ  1 
ATOM   27   N  NH1 . ARG A 1 8   ? -20.609 -15.107 -20.254 1.00 33.45  ? 3   ARG A NH1 1 
ATOM   28   N  NH2 . ARG A 1 8   ? -20.508 -16.753 -18.657 1.00 34.68  ? 3   ARG A NH2 1 
ATOM   29   N  N   . ALA A 1 9   ? -23.405 -10.775 -22.072 1.00 38.03  ? 4   ALA A N   1 
ATOM   30   C  CA  . ALA A 1 9   ? -22.192 -10.079 -22.455 1.00 37.44  ? 4   ALA A CA  1 
ATOM   31   C  C   . ALA A 1 9   ? -22.069 -8.683  -21.846 1.00 36.24  ? 4   ALA A C   1 
ATOM   32   O  O   . ALA A 1 9   ? -20.962 -8.257  -21.502 1.00 36.37  ? 4   ALA A O   1 
ATOM   33   C  CB  . ALA A 1 9   ? -22.137 -10.000 -23.967 1.00 38.84  ? 4   ALA A CB  1 
ATOM   34   N  N   . SER A 1 10  ? -23.205 -7.986  -21.684 1.00 36.05  ? 5   SER A N   1 
ATOM   35   C  CA  . SER A 1 10  ? -23.208 -6.657  -21.089 1.00 35.78  ? 5   SER A CA  1 
ATOM   36   C  C   . SER A 1 10  ? -22.848 -6.730  -19.605 1.00 34.44  ? 5   SER A C   1 
ATOM   37   O  O   . SER A 1 10  ? -22.096 -5.884  -19.106 1.00 33.12  ? 5   SER A O   1 
ATOM   38   C  CB  . SER A 1 10  ? -24.554 -5.964  -21.248 1.00 38.17  ? 5   SER A CB  1 
ATOM   39   O  OG  . SER A 1 10  ? -24.740 -5.559  -22.599 1.00 42.16  ? 5   SER A OG  1 
ATOM   40   N  N   . LEU A 1 11  ? -23.352 -7.767  -18.930 1.00 32.89  ? 6   LEU A N   1 
ATOM   41   C  CA  . LEU A 1 11  ? -23.023 -7.955  -17.515 1.00 33.24  ? 6   LEU A CA  1 
ATOM   42   C  C   . LEU A 1 11  ? -21.527 -8.207  -17.310 1.00 31.84  ? 6   LEU A C   1 
ATOM   43   O  O   . LEU A 1 11  ? -20.919 -7.681  -16.378 1.00 31.08  ? 6   LEU A O   1 
ATOM   44   C  CB  . LEU A 1 11  ? -23.849 -9.128  -16.957 1.00 33.33  ? 6   LEU A CB  1 
ATOM   45   C  CG  . LEU A 1 11  ? -25.347 -8.856  -16.839 1.00 34.66  ? 6   LEU A CG  1 
ATOM   46   C  CD1 . LEU A 1 11  ? -26.098 -10.112 -16.535 1.00 34.66  ? 6   LEU A CD1 1 
ATOM   47   C  CD2 . LEU A 1 11  ? -25.628 -7.799  -15.764 1.00 36.58  ? 6   LEU A CD2 1 
ATOM   48   N  N   . ILE A 1 12  ? -20.927 -9.038  -18.176 1.00 30.37  ? 7   ILE A N   1 
ATOM   49   C  CA  . ILE A 1 12  ? -19.499 -9.320  -18.076 1.00 30.46  ? 7   ILE A CA  1 
ATOM   50   C  C   . ILE A 1 12  ? -18.717 -8.036  -18.321 1.00 31.02  ? 7   ILE A C   1 
ATOM   51   O  O   . ILE A 1 12  ? -17.714 -7.777  -17.673 1.00 32.13  ? 7   ILE A O   1 
ATOM   52   C  CB  . ILE A 1 12  ? -19.071 -10.442 -19.062 1.00 29.36  ? 7   ILE A CB  1 
ATOM   53   C  CG1 . ILE A 1 12  ? -19.758 -11.796 -18.761 1.00 30.40  ? 7   ILE A CG1 1 
ATOM   54   C  CG2 . ILE A 1 12  ? -17.525 -10.594 -19.130 1.00 29.40  ? 7   ILE A CG2 1 
ATOM   55   C  CD1 . ILE A 1 12  ? -19.425 -12.334 -17.355 1.00 31.09  ? 7   ILE A CD1 1 
ATOM   56   N  N   . GLN A 1 13  ? -19.113 -7.282  -19.373 1.00 34.35  ? 8   GLN A N   1 
ATOM   57   C  CA  . GLN A 1 13  ? -18.441 -6.031  -19.658 1.00 35.46  ? 8   GLN A CA  1 
ATOM   58   C  C   . GLN A 1 13  ? -18.452 -5.126  -18.410 1.00 34.02  ? 8   GLN A C   1 
ATOM   59   O  O   . GLN A 1 13  ? -17.450 -4.510  -18.073 1.00 35.89  ? 8   GLN A O   1 
ATOM   60   C  CB  . GLN A 1 13  ? -19.087 -5.370  -20.914 1.00 36.03  ? 8   GLN A CB  1 
ATOM   61   C  CG  . GLN A 1 13  ? -18.406 -4.107  -21.322 1.00 40.10  ? 8   GLN A CG  1 
ATOM   62   C  CD  . GLN A 1 13  ? -19.147 -3.350  -22.401 1.00 45.15  ? 8   GLN A CD  1 
ATOM   63   O  OE1 . GLN A 1 13  ? -20.134 -3.816  -23.014 1.00 48.81  ? 8   GLN A OE1 1 
ATOM   64   N  NE2 . GLN A 1 13  ? -18.689 -2.145  -22.650 1.00 48.34  ? 8   GLN A NE2 1 
ATOM   65   N  N   . LYS A 1 14  ? -19.619 -5.007  -17.792 1.00 33.53  ? 9   LYS A N   1 
ATOM   66   C  CA  . LYS A 1 14  ? -19.785 -4.159  -16.610 1.00 32.72  ? 9   LYS A CA  1 
ATOM   67   C  C   . LYS A 1 14  ? -19.018 -4.669  -15.394 1.00 29.60  ? 9   LYS A C   1 
ATOM   68   O  O   . LYS A 1 14  ? -18.476 -3.852  -14.649 1.00 30.73  ? 9   LYS A O   1 
ATOM   69   C  CB  . LYS A 1 14  ? -21.267 -3.955  -16.335 1.00 34.78  ? 9   LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 14  ? -21.910 -2.985  -17.340 1.00 35.17  ? 9   LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 14  ? -23.276 -2.543  -16.975 1.00 40.72  ? 9   LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 14  ? -23.793 -1.476  -17.929 1.00 43.86  ? 9   LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 14  ? -24.886 -0.665  -17.311 1.00 46.32  ? 9   LYS A NZ  1 
ATOM   74   N  N   . ALA A 1 15  ? -18.904 -5.994  -15.259 1.00 28.04  ? 10  ALA A N   1 
ATOM   75   C  CA  . ALA A 1 15  ? -18.058 -6.558  -14.216 1.00 28.22  ? 10  ALA A CA  1 
ATOM   76   C  C   . ALA A 1 15  ? -16.602 -6.148  -14.407 1.00 29.59  ? 10  ALA A C   1 
ATOM   77   O  O   . ALA A 1 15  ? -15.924 -5.765  -13.472 1.00 30.58  ? 10  ALA A O   1 
ATOM   78   C  CB  . ALA A 1 15  ? -18.175 -8.057  -14.148 1.00 28.33  ? 10  ALA A CB  1 
ATOM   79   N  N   . LYS A 1 16  ? -16.103 -6.163  -15.657 1.00 31.14  ? 11  LYS A N   1 
ATOM   80   C  CA  . LYS A 1 16  ? -14.723 -5.766  -15.893 1.00 31.74  ? 11  LYS A CA  1 
ATOM   81   C  C   . LYS A 1 16  ? -14.485 -4.269  -15.705 1.00 33.32  ? 11  LYS A C   1 
ATOM   82   O  O   . LYS A 1 16  ? -13.415 -3.866  -15.243 1.00 32.48  ? 11  LYS A O   1 
ATOM   83   C  CB  . LYS A 1 16  ? -14.306 -6.129  -17.332 1.00 31.40  ? 11  LYS A CB  1 
ATOM   84   C  CG  . LYS A 1 16  ? -14.109 -7.617  -17.512 1.00 32.04  ? 11  LYS A CG  1 
ATOM   85   C  CD  . LYS A 1 16  ? -13.827 -7.984  -18.950 1.00 34.44  ? 11  LYS A CD  1 
ATOM   86   C  CE  . LYS A 1 16  ? -14.026 -9.455  -19.183 1.00 35.92  ? 11  LYS A CE  1 
ATOM   87   N  NZ  . LYS A 1 16  ? -13.935 -9.771  -20.614 1.00 39.20  ? 11  LYS A NZ  1 
ATOM   88   N  N   . LEU A 1 17  ? -15.485 -3.445  -16.042 1.00 34.78  ? 12  LEU A N   1 
ATOM   89   C  CA  . LEU A 1 17  ? -15.427 -2.022  -15.761 1.00 34.64  ? 12  LEU A CA  1 
ATOM   90   C  C   . LEU A 1 17  ? -15.395 -1.807  -14.236 1.00 33.24  ? 12  LEU A C   1 
ATOM   91   O  O   . LEU A 1 17  ? -14.622 -1.010  -13.756 1.00 33.58  ? 12  LEU A O   1 
ATOM   92   C  CB  . LEU A 1 17  ? -16.638 -1.314  -16.300 1.00 35.01  ? 12  LEU A CB  1 
ATOM   93   C  CG  . LEU A 1 17  ? -16.701 -1.241  -17.882 1.00 36.06  ? 12  LEU A CG  1 
ATOM   94   C  CD1 . LEU A 1 17  ? -18.004 -0.679  -18.282 1.00 37.01  ? 12  LEU A CD1 1 
ATOM   95   C  CD2 . LEU A 1 17  ? -15.535 -0.442  -18.401 1.00 36.14  ? 12  LEU A CD2 1 
ATOM   96   N  N   . ALA A 1 18  ? -16.282 -2.495  -13.538 1.00 31.99  ? 13  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 18  ? -16.319 -2.415  -12.070 1.00 31.23  ? 13  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 18  ? -14.956 -2.732  -11.461 1.00 30.45  ? 13  ALA A C   1 
ATOM   99   O  O   . ALA A 1 18  ? -14.540 -2.124  -10.436 1.00 29.19  ? 13  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 18  ? -17.392 -3.353  -11.553 1.00 32.00  ? 13  ALA A CB  1 
ATOM   101  N  N   . GLU A 1 19  ? -14.324 -3.788  -11.980 1.00 30.69  ? 14  GLU A N   1 
ATOM   102  C  CA  . GLU A 1 19  ? -13.007 -4.172  -11.504 1.00 30.29  ? 14  GLU A CA  1 
ATOM   103  C  C   . GLU A 1 19  ? -11.977 -3.056  -11.685 1.00 30.15  ? 14  GLU A C   1 
ATOM   104  O  O   . GLU A 1 19  ? -11.261 -2.710  -10.747 1.00 30.53  ? 14  GLU A O   1 
ATOM   105  C  CB  . GLU A 1 19  ? -12.522 -5.471  -12.135 1.00 30.51  ? 14  GLU A CB  1 
ATOM   106  C  CG  . GLU A 1 19  ? -11.220 -5.979  -11.529 1.00 34.06  ? 14  GLU A CG  1 
ATOM   107  C  CD  . GLU A 1 19  ? -10.712 -7.255  -12.150 1.00 37.18  ? 14  GLU A CD  1 
ATOM   108  O  OE1 . GLU A 1 19  ? -10.867 -7.394  -13.376 1.00 37.01  ? 14  GLU A OE1 1 
ATOM   109  O  OE2 . GLU A 1 19  ? -10.126 -8.094  -11.427 1.00 40.85  ? 14  GLU A OE2 1 
ATOM   110  N  N   . GLN A 1 20  ? -11.941 -2.455  -12.875 1.00 30.27  ? 15  GLN A N   1 
ATOM   111  C  CA  . GLN A 1 20  ? -11.027 -1.363  -13.142 1.00 31.39  ? 15  GLN A CA  1 
ATOM   112  C  C   . GLN A 1 20  ? -11.307 -0.168  -12.240 1.00 31.02  ? 15  GLN A C   1 
ATOM   113  O  O   . GLN A 1 20  ? -10.371 0.532   -11.858 1.00 32.68  ? 15  GLN A O   1 
ATOM   114  C  CB  . GLN A 1 20  ? -11.126 -0.956  -14.597 1.00 34.51  ? 15  GLN A CB  1 
ATOM   115  C  CG  . GLN A 1 20  ? -10.595 -2.010  -15.497 1.00 38.65  ? 15  GLN A CG  1 
ATOM   116  C  CD  . GLN A 1 20  ? -10.950 -1.674  -16.915 1.00 42.82  ? 15  GLN A CD  1 
ATOM   117  O  OE1 . GLN A 1 20  ? -10.432 -0.711  -17.498 1.00 47.45  ? 15  GLN A OE1 1 
ATOM   118  N  NE2 . GLN A 1 20  ? -11.867 -2.444  -17.507 1.00 47.98  ? 15  GLN A NE2 1 
ATOM   119  N  N   . ALA A 1 21  ? -12.591 0.036   -11.906 1.00 30.11  ? 16  ALA A N   1 
ATOM   120  C  CA  . ALA A 1 21  ? -13.006 1.113   -11.024 1.00 28.79  ? 16  ALA A CA  1 
ATOM   121  C  C   . ALA A 1 21  ? -12.866 0.819   -9.531  1.00 29.02  ? 16  ALA A C   1 
ATOM   122  O  O   . ALA A 1 21  ? -13.156 1.712   -8.741  1.00 31.47  ? 16  ALA A O   1 
ATOM   123  C  CB  . ALA A 1 21  ? -14.428 1.471   -11.296 1.00 29.06  ? 16  ALA A CB  1 
ATOM   124  N  N   . GLU A 1 22  ? -12.470 -0.415  -9.179  1.00 29.00  ? 17  GLU A N   1 
ATOM   125  C  CA  . GLU A 1 22  ? -12.375 -0.884  -7.789  1.00 29.80  ? 17  GLU A CA  1 
ATOM   126  C  C   . GLU A 1 22  ? -13.710 -0.795  -7.058  1.00 28.56  ? 17  GLU A C   1 
ATOM   127  O  O   . GLU A 1 22  ? -13.787 -0.531  -5.838  1.00 31.25  ? 17  GLU A O   1 
ATOM   128  C  CB  . GLU A 1 22  ? -11.267 -0.144  -7.051  1.00 32.08  ? 17  GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 22  ? -9.913  -0.391  -7.694  1.00 37.77  ? 17  GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 22  ? -8.716  0.078   -6.900  1.00 42.37  ? 17  GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 22  ? -8.914  0.738   -5.865  1.00 45.93  ? 17  GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 22  ? -7.574  -0.226  -7.304  1.00 49.02  ? 17  GLU A OE2 1 
ATOM   133  N  N   . ARG A 1 23  ? -14.767 -1.051  -7.837  1.00 27.72  ? 18  ARG A N   1 
ATOM   134  C  CA  . ARG A 1 23  ? -16.132 -1.102  -7.345  1.00 27.76  ? 18  ARG A CA  1 
ATOM   135  C  C   . ARG A 1 23  ? -16.553 -2.556  -7.148  1.00 27.35  ? 18  ARG A C   1 
ATOM   136  O  O   . ARG A 1 23  ? -17.352 -3.117  -7.883  1.00 30.17  ? 18  ARG A O   1 
ATOM   137  C  CB  . ARG A 1 23  ? -17.052 -0.385  -8.327  1.00 28.98  ? 18  ARG A CB  1 
ATOM   138  C  CG  . ARG A 1 23  ? -16.774 1.136   -8.472  1.00 31.06  ? 18  ARG A CG  1 
ATOM   139  C  CD  . ARG A 1 23  ? -17.520 1.924   -7.417  1.00 32.12  ? 18  ARG A CD  1 
ATOM   140  N  NE  . ARG A 1 23  ? -18.963 1.914   -7.672  1.00 32.70  ? 18  ARG A NE  1 
ATOM   141  C  CZ  . ARG A 1 23  ? -19.851 2.719   -7.100  1.00 30.92  ? 18  ARG A CZ  1 
ATOM   142  N  NH1 . ARG A 1 23  ? -19.487 3.697   -6.279  1.00 35.12  ? 18  ARG A NH1 1 
ATOM   143  N  NH2 . ARG A 1 23  ? -21.141 2.539   -7.360  1.00 31.86  ? 18  ARG A NH2 1 
ATOM   144  N  N   . TYR A 1 24  ? -16.046 -3.189  -6.088  1.00 29.65  ? 19  TYR A N   1 
ATOM   145  C  CA  . TYR A 1 24  ? -16.212 -4.619  -5.944  1.00 28.96  ? 19  TYR A CA  1 
ATOM   146  C  C   . TYR A 1 24  ? -17.634 -5.098  -5.637  1.00 28.77  ? 19  TYR A C   1 
ATOM   147  O  O   . TYR A 1 24  ? -17.996 -6.198  -6.046  1.00 29.91  ? 19  TYR A O   1 
ATOM   148  C  CB  . TYR A 1 24  ? -15.171 -5.181  -4.947  1.00 28.73  ? 19  TYR A CB  1 
ATOM   149  C  CG  . TYR A 1 24  ? -13.749 -4.870  -5.388  1.00 28.95  ? 19  TYR A CG  1 
ATOM   150  C  CD1 . TYR A 1 24  ? -13.228 -5.411  -6.550  1.00 29.45  ? 19  TYR A CD1 1 
ATOM   151  C  CD2 . TYR A 1 24  ? -12.968 -3.960  -4.701  1.00 30.58  ? 19  TYR A CD2 1 
ATOM   152  C  CE1 . TYR A 1 24  ? -11.945 -5.109  -6.980  1.00 30.93  ? 19  TYR A CE1 1 
ATOM   153  C  CE2 . TYR A 1 24  ? -11.677 -3.653  -5.120  1.00 32.87  ? 19  TYR A CE2 1 
ATOM   154  C  CZ  . TYR A 1 24  ? -11.182 -4.208  -6.280  1.00 32.62  ? 19  TYR A CZ  1 
ATOM   155  O  OH  . TYR A 1 24  ? -9.917  -3.913  -6.719  1.00 37.55  ? 19  TYR A OH  1 
ATOM   156  N  N   . GLU A 1 25  ? -18.432 -4.335  -4.869  1.00 29.25  ? 20  GLU A N   1 
ATOM   157  C  CA  . GLU A 1 25  ? -19.831 -4.709  -4.669  1.00 30.30  ? 20  GLU A CA  1 
ATOM   158  C  C   . GLU A 1 25  ? -20.570 -4.765  -6.011  1.00 29.28  ? 20  GLU A C   1 
ATOM   159  O  O   . GLU A 1 25  ? -21.318 -5.702  -6.255  1.00 28.93  ? 20  GLU A O   1 
ATOM   160  C  CB  . GLU A 1 25  ? -20.585 -3.756  -3.675  1.00 31.51  ? 20  GLU A CB  1 
ATOM   161  C  CG  . GLU A 1 25  ? -19.984 -3.806  -2.312  1.00 37.04  ? 20  GLU A CG  1 
ATOM   162  C  CD  . GLU A 1 25  ? -18.774 -2.907  -2.069  1.00 43.80  ? 20  GLU A CD  1 
ATOM   163  O  OE1 . GLU A 1 25  ? -18.237 -2.338  -3.053  1.00 44.58  ? 20  GLU A OE1 1 
ATOM   164  O  OE2 . GLU A 1 25  ? -18.364 -2.772  -0.890  1.00 47.66  ? 20  GLU A OE2 1 
ATOM   165  N  N   . ASP A 1 26  ? -20.347 -3.748  -6.840  1.00 28.95  ? 21  ASP A N   1 
ATOM   166  C  CA  . ASP A 1 26  ? -20.975 -3.701  -8.161  1.00 28.14  ? 21  ASP A CA  1 
ATOM   167  C  C   . ASP A 1 26  ? -20.482 -4.872  -8.991  1.00 26.94  ? 21  ASP A C   1 
ATOM   168  O  O   . ASP A 1 26  ? -21.286 -5.563  -9.613  1.00 26.00  ? 21  ASP A O   1 
ATOM   169  C  CB  . ASP A 1 26  ? -20.668 -2.406  -8.868  1.00 28.87  ? 21  ASP A CB  1 
ATOM   170  C  CG  . ASP A 1 26  ? -21.364 -1.181  -8.362  1.00 29.14  ? 21  ASP A CG  1 
ATOM   171  O  OD1 . ASP A 1 26  ? -22.269 -1.318  -7.487  1.00 31.44  ? 21  ASP A OD1 1 
ATOM   172  O  OD2 . ASP A 1 26  ? -20.990 -0.070  -8.785  1.00 31.52  ? 21  ASP A OD2 1 
ATOM   173  N  N   . MET A 1 27  ? -19.166 -5.073  -8.993  1.00 27.21  ? 22  MET A N   1 
ATOM   174  C  CA  . MET A 1 27  ? -18.546 -6.169  -9.720  1.00 27.37  ? 22  MET A CA  1 
ATOM   175  C  C   . MET A 1 27  ? -19.167 -7.517  -9.371  1.00 27.73  ? 22  MET A C   1 
ATOM   176  O  O   . MET A 1 27  ? -19.473 -8.348  -10.206 1.00 28.67  ? 22  MET A O   1 
ATOM   177  C  CB  . MET A 1 27  ? -17.053 -6.118  -9.486  1.00 26.76  ? 22  MET A CB  1 
ATOM   178  C  CG  . MET A 1 27  ? -16.275 -7.217  -10.172 1.00 25.50  ? 22  MET A CG  1 
ATOM   179  S  SD  . MET A 1 27  ? -14.559 -7.172  -9.698  1.00 26.51  ? 22  MET A SD  1 
ATOM   180  C  CE  . MET A 1 27  ? -13.942 -8.531  -10.647 1.00 27.36  ? 22  MET A CE  1 
ATOM   181  N  N   . ALA A 1 28  ? -19.354 -7.763  -8.055  1.00 28.22  ? 23  ALA A N   1 
ATOM   182  C  CA  . ALA A 1 28  ? -19.995 -8.982  -7.633  1.00 28.23  ? 23  ALA A CA  1 
ATOM   183  C  C   . ALA A 1 28  ? -21.433 -9.107  -8.107  1.00 27.98  ? 23  ALA A C   1 
ATOM   184  O  O   . ALA A 1 28  ? -21.835 -10.188 -8.529  1.00 25.91  ? 23  ALA A O   1 
ATOM   185  C  CB  . ALA A 1 28  ? -19.980 -9.043  -6.061  1.00 28.88  ? 23  ALA A CB  1 
ATOM   186  N  N   . ALA A 1 29  ? -22.198 -8.012  -8.040  1.00 27.52  ? 24  ALA A N   1 
ATOM   187  C  CA  . ALA A 1 29  ? -23.587 -8.034  -8.481  1.00 28.48  ? 24  ALA A CA  1 
ATOM   188  C  C   . ALA A 1 29  ? -23.692 -8.321  -9.984  1.00 28.95  ? 24  ALA A C   1 
ATOM   189  O  O   . ALA A 1 29  ? -24.594 -9.048  -10.368 1.00 30.05  ? 24  ALA A O   1 
ATOM   190  C  CB  . ALA A 1 29  ? -24.293 -6.734  -8.185  1.00 28.73  ? 24  ALA A CB  1 
ATOM   191  N  N   . PHE A 1 30  ? -22.755 -7.775  -10.758 1.00 27.54  ? 25  PHE A N   1 
ATOM   192  C  CA  . PHE A 1 30  ? -22.766 -8.016  -12.208 1.00 27.93  ? 25  PHE A CA  1 
ATOM   193  C  C   . PHE A 1 30  ? -22.473 -9.492  -12.467 1.00 27.50  ? 25  PHE A C   1 
ATOM   194  O  O   . PHE A 1 30  ? -23.120 -10.128 -13.303 1.00 27.21  ? 25  PHE A O   1 
ATOM   195  C  CB  . PHE A 1 30  ? -21.759 -7.101  -12.919 1.00 28.94  ? 25  PHE A CB  1 
ATOM   196  C  CG  . PHE A 1 30  ? -22.108 -5.649  -12.927 1.00 30.23  ? 25  PHE A CG  1 
ATOM   197  C  CD1 . PHE A 1 30  ? -23.383 -5.226  -13.293 1.00 30.55  ? 25  PHE A CD1 1 
ATOM   198  C  CD2 . PHE A 1 30  ? -21.158 -4.690  -12.642 1.00 31.44  ? 25  PHE A CD2 1 
ATOM   199  C  CE1 . PHE A 1 30  ? -23.703 -3.855  -13.332 1.00 31.43  ? 25  PHE A CE1 1 
ATOM   200  C  CE2 . PHE A 1 30  ? -21.469 -3.334  -12.682 1.00 32.22  ? 25  PHE A CE2 1 
ATOM   201  C  CZ  . PHE A 1 30  ? -22.740 -2.920  -13.006 1.00 31.69  ? 25  PHE A CZ  1 
ATOM   202  N  N   . MET A 1 31  ? -21.446 -10.036 -11.802 1.00 27.39  ? 26  MET A N   1 
ATOM   203  C  CA  . MET A 1 31  ? -21.117 -11.440 -11.980 1.00 27.31  ? 26  MET A CA  1 
ATOM   204  C  C   . MET A 1 31  ? -22.236 -12.371 -11.495 1.00 26.95  ? 26  MET A C   1 
ATOM   205  O  O   . MET A 1 31  ? -22.457 -13.427 -12.071 1.00 27.25  ? 26  MET A O   1 
ATOM   206  C  CB  . MET A 1 31  ? -19.778 -11.745 -11.316 1.00 27.65  ? 26  MET A CB  1 
ATOM   207  C  CG  . MET A 1 31  ? -18.584 -11.094 -11.983 1.00 26.88  ? 26  MET A CG  1 
ATOM   208  S  SD  . MET A 1 31  ? -18.542 -11.410 -13.758 1.00 28.97  ? 26  MET A SD  1 
ATOM   209  C  CE  . MET A 1 31  ? -18.537 -13.107 -13.748 1.00 29.52  ? 26  MET A CE  1 
ATOM   210  N  N   . LYS A 1 32  ? -22.947 -12.010 -10.419 1.00 27.26  ? 27  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 32  ? -24.116 -12.775 -10.011 1.00 28.13  ? 27  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 32  ? -25.171 -12.886 -11.113 1.00 28.80  ? 27  LYS A C   1 
ATOM   213  O  O   . LYS A 1 32  ? -25.684 -13.975 -11.413 1.00 28.25  ? 27  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 32  ? -24.740 -12.126 -8.763  1.00 29.39  ? 27  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 32  ? -26.003 -12.809 -8.293  1.00 30.89  ? 27  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 32  ? -26.390 -12.330 -6.916  1.00 31.51  ? 27  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 32  ? -27.612 -13.029 -6.335  1.00 34.66  ? 27  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 32  ? -28.866 -12.642 -6.982  1.00 35.23  ? 27  LYS A NZ  1 
ATOM   219  N  N   . GLY A 1 33  ? -25.473 -11.740 -11.725 1.00 27.80  ? 28  GLY A N   1 
ATOM   220  C  CA  . GLY A 1 33  ? -26.406 -11.701 -12.837 1.00 28.25  ? 28  GLY A CA  1 
ATOM   221  C  C   . GLY A 1 33  ? -25.927 -12.588 -13.990 1.00 28.33  ? 28  GLY A C   1 
ATOM   222  O  O   . GLY A 1 33  ? -26.727 -13.296 -14.611 1.00 29.00  ? 28  GLY A O   1 
ATOM   223  N  N   . ALA A 1 34  ? -24.612 -12.579 -14.245 1.00 27.34  ? 29  ALA A N   1 
ATOM   224  C  CA  . ALA A 1 34  ? -24.054 -13.386 -15.329 1.00 27.29  ? 29  ALA A CA  1 
ATOM   225  C  C   . ALA A 1 34  ? -24.182 -14.881 -15.017 1.00 27.61  ? 29  ALA A C   1 
ATOM   226  O  O   . ALA A 1 34  ? -24.561 -15.676 -15.855 1.00 30.05  ? 29  ALA A O   1 
ATOM   227  C  CB  . ALA A 1 34  ? -22.606 -13.021 -15.569 1.00 27.34  ? 29  ALA A CB  1 
ATOM   228  N  N   . VAL A 1 35  ? -23.880 -15.277 -13.779 1.00 27.53  ? 30  VAL A N   1 
ATOM   229  C  CA  . VAL A 1 35  ? -24.022 -16.673 -13.394 1.00 28.55  ? 30  VAL A CA  1 
ATOM   230  C  C   . VAL A 1 35  ? -25.465 -17.126 -13.602 1.00 31.68  ? 30  VAL A C   1 
ATOM   231  O  O   . VAL A 1 35  ? -25.724 -18.216 -14.103 1.00 31.10  ? 30  VAL A O   1 
ATOM   232  C  CB  . VAL A 1 35  ? -23.578 -16.847 -11.929 1.00 27.99  ? 30  VAL A CB  1 
ATOM   233  C  CG1 . VAL A 1 35  ? -23.986 -18.215 -11.355 1.00 30.26  ? 30  VAL A CG1 1 
ATOM   234  C  CG2 . VAL A 1 35  ? -22.089 -16.648 -11.840 1.00 27.27  ? 30  VAL A CG2 1 
ATOM   235  N  N   . GLU A 1 36  ? -26.402 -16.261 -13.219 1.00 32.50  ? 31  GLU A N   1 
ATOM   236  C  CA  . GLU A 1 36  ? -27.807 -16.612 -13.225 1.00 34.36  ? 31  GLU A CA  1 
ATOM   237  C  C   . GLU A 1 36  ? -28.351 -16.839 -14.628 1.00 35.91  ? 31  GLU A C   1 
ATOM   238  O  O   . GLU A 1 36  ? -29.452 -17.360 -14.760 1.00 40.20  ? 31  GLU A O   1 
ATOM   239  C  CB  . GLU A 1 36  ? -28.611 -15.543 -12.482 1.00 34.09  ? 31  GLU A CB  1 
ATOM   240  C  CG  . GLU A 1 36  ? -28.440 -15.694 -10.993 1.00 35.43  ? 31  GLU A CG  1 
ATOM   241  C  CD  . GLU A 1 36  ? -28.960 -14.539 -10.172 1.00 37.92  ? 31  GLU A CD  1 
ATOM   242  O  OE1 . GLU A 1 36  ? -29.302 -13.473 -10.728 1.00 41.78  ? 31  GLU A OE1 1 
ATOM   243  O  OE2 . GLU A 1 36  ? -29.041 -14.713 -8.949  1.00 39.01  ? 31  GLU A OE2 1 
ATOM   244  N  N   . LYS A 1 37  ? -27.568 -16.496 -15.666 1.00 38.28  ? 32  LYS A N   1 
ATOM   245  C  CA  . LYS A 1 37  ? -27.925 -16.857 -17.031 1.00 41.05  ? 32  LYS A CA  1 
ATOM   246  C  C   . LYS A 1 37  ? -27.783 -18.357 -17.266 1.00 41.03  ? 32  LYS A C   1 
ATOM   247  O  O   . LYS A 1 37  ? -28.320 -18.891 -18.219 1.00 46.80  ? 32  LYS A O   1 
ATOM   248  C  CB  . LYS A 1 37  ? -27.077 -16.107 -18.043 1.00 40.11  ? 32  LYS A CB  1 
ATOM   249  C  CG  . LYS A 1 37  ? -27.228 -14.591 -17.996 1.00 42.34  ? 32  LYS A CG  1 
ATOM   250  C  CD  . LYS A 1 37  ? -28.643 -14.145 -18.150 1.00 47.61  ? 32  LYS A CD  1 
ATOM   251  C  CE  . LYS A 1 37  ? -28.757 -12.654 -18.181 1.00 49.33  ? 32  LYS A CE  1 
ATOM   252  N  NZ  . LYS A 1 37  ? -30.176 -12.246 -18.349 1.00 53.53  ? 32  LYS A NZ  1 
ATOM   253  N  N   . GLY A 1 38  ? -27.067 -19.044 -16.383 1.00 42.38  ? 33  GLY A N   1 
ATOM   254  C  CA  . GLY A 1 38  ? -27.053 -20.494 -16.399 1.00 41.68  ? 33  GLY A CA  1 
ATOM   255  C  C   . GLY A 1 38  ? -26.062 -21.112 -17.380 1.00 41.04  ? 33  GLY A C   1 
ATOM   256  O  O   . GLY A 1 38  ? -26.104 -22.320 -17.602 1.00 43.29  ? 33  GLY A O   1 
ATOM   257  N  N   . GLU A 1 39  ? -25.175 -20.298 -17.963 1.00 38.68  ? 34  GLU A N   1 
ATOM   258  C  CA  . GLU A 1 39  ? -24.105 -20.841 -18.785 1.00 37.41  ? 34  GLU A CA  1 
ATOM   259  C  C   . GLU A 1 39  ? -22.861 -20.965 -17.921 1.00 31.80  ? 34  GLU A C   1 
ATOM   260  O  O   . GLU A 1 39  ? -22.737 -20.292 -16.873 1.00 32.65  ? 34  GLU A O   1 
ATOM   261  C  CB  . GLU A 1 39  ? -23.821 -19.993 -20.048 1.00 39.16  ? 34  GLU A CB  1 
ATOM   262  C  CG  . GLU A 1 39  ? -25.008 -19.937 -21.011 1.00 44.30  ? 34  GLU A CG  1 
ATOM   263  C  CD  . GLU A 1 39  ? -25.484 -21.289 -21.555 1.00 49.66  ? 34  GLU A CD  1 
ATOM   264  O  OE1 . GLU A 1 39  ? -24.631 -22.112 -21.973 1.00 56.64  ? 34  GLU A OE1 1 
ATOM   265  O  OE2 . GLU A 1 39  ? -26.715 -21.520 -21.582 1.00 52.35  ? 34  GLU A OE2 1 
ATOM   266  N  N   . GLU A 1 40  ? -21.972 -21.882 -18.316 1.00 30.65  ? 35  GLU A N   1 
ATOM   267  C  CA  . GLU A 1 40  ? -20.687 -21.963 -17.623 1.00 30.66  ? 35  GLU A CA  1 
ATOM   268  C  C   . GLU A 1 40  ? -19.906 -20.652 -17.693 1.00 30.89  ? 35  GLU A C   1 
ATOM   269  O  O   . GLU A 1 40  ? -20.056 -19.847 -18.630 1.00 31.87  ? 35  GLU A O   1 
ATOM   270  C  CB  . GLU A 1 40  ? -19.784 -23.071 -18.201 1.00 34.16  ? 35  GLU A CB  1 
ATOM   271  C  CG  . GLU A 1 40  ? -20.274 -24.489 -17.997 1.00 36.51  ? 35  GLU A CG  1 
ATOM   272  C  CD  . GLU A 1 40  ? -19.398 -25.501 -18.706 1.00 39.18  ? 35  GLU A CD  1 
ATOM   273  O  OE1 . GLU A 1 40  ? -18.313 -25.831 -18.173 1.00 39.10  ? 35  GLU A OE1 1 
ATOM   274  O  OE2 . GLU A 1 40  ? -19.780 -25.928 -19.821 1.00 40.62  ? 35  GLU A OE2 1 
ATOM   275  N  N   . LEU A 1 41  ? -19.020 -20.495 -16.694 1.00 31.98  ? 36  LEU A N   1 
ATOM   276  C  CA  . LEU A 1 41  ? -18.048 -19.426 -16.654 1.00 31.04  ? 36  LEU A CA  1 
ATOM   277  C  C   . LEU A 1 41  ? -16.712 -19.947 -17.151 1.00 28.68  ? 36  LEU A C   1 
ATOM   278  O  O   . LEU A 1 41  ? -16.273 -21.023 -16.746 1.00 30.39  ? 36  LEU A O   1 
ATOM   279  C  CB  . LEU A 1 41  ? -17.838 -18.913 -15.182 1.00 30.86  ? 36  LEU A CB  1 
ATOM   280  C  CG  . LEU A 1 41  ? -19.029 -18.395 -14.489 1.00 32.44  ? 36  LEU A CG  1 
ATOM   281  C  CD1 . LEU A 1 41  ? -18.608 -17.687 -13.166 1.00 33.65  ? 36  LEU A CD1 1 
ATOM   282  C  CD2 . LEU A 1 41  ? -19.821 -17.474 -15.255 1.00 33.44  ? 36  LEU A CD2 1 
ATOM   283  N  N   . SER A 1 42  ? -16.071 -19.149 -18.007 1.00 28.80  ? 37  SER A N   1 
ATOM   284  C  CA  . SER A 1 42  ? -14.690 -19.346 -18.399 1.00 28.40  ? 37  SER A CA  1 
ATOM   285  C  C   . SER A 1 42  ? -13.771 -19.150 -17.205 1.00 27.12  ? 37  SER A C   1 
ATOM   286  O  O   . SER A 1 42  ? -14.190 -18.635 -16.154 1.00 28.37  ? 37  SER A O   1 
ATOM   287  C  CB  . SER A 1 42  ? -14.277 -18.346 -19.487 1.00 28.08  ? 37  SER A CB  1 
ATOM   288  O  OG  . SER A 1 42  ? -14.256 -16.984 -19.047 1.00 29.20  ? 37  SER A OG  1 
ATOM   289  N  N   . CYS A 1 43  ? -12.504 -19.527 -17.389 1.00 27.98  ? 38  CYS A N   1 
ATOM   290  C  CA  A CYS A 1 43  ? -11.486 -19.291 -16.372 0.50 30.49  ? 38  CYS A CA  1 
ATOM   291  C  CA  B CYS A 1 43  ? -11.509 -19.288 -16.364 0.50 28.45  ? 38  CYS A CA  1 
ATOM   292  C  C   . CYS A 1 43  ? -11.441 -17.821 -15.942 1.00 28.47  ? 38  CYS A C   1 
ATOM   293  O  O   . CYS A 1 43  ? -11.478 -17.501 -14.742 1.00 28.07  ? 38  CYS A O   1 
ATOM   294  C  CB  A CYS A 1 43  ? -10.117 -19.778 -16.846 0.50 34.31  ? 38  CYS A CB  1 
ATOM   295  C  CB  B CYS A 1 43  ? -10.164 -19.790 -16.837 0.50 28.07  ? 38  CYS A CB  1 
ATOM   296  S  SG  A CYS A 1 43  ? -9.983  -21.583 -17.058 0.50 42.29  ? 38  CYS A SG  1 
ATOM   297  S  SG  B CYS A 1 43  ? -8.892  -19.662 -15.582 0.50 27.53  ? 38  CYS A SG  1 
ATOM   298  N  N   . GLU A 1 44  ? -11.373 -16.923 -16.924 1.00 28.17  ? 39  GLU A N   1 
ATOM   299  C  CA  . GLU A 1 44  ? -11.364 -15.491 -16.703 1.00 29.14  ? 39  GLU A CA  1 
ATOM   300  C  C   . GLU A 1 44  ? -12.575 -15.059 -15.868 1.00 27.84  ? 39  GLU A C   1 
ATOM   301  O  O   . GLU A 1 44  ? -12.421 -14.279 -14.934 1.00 28.34  ? 39  GLU A O   1 
ATOM   302  C  CB  . GLU A 1 44  ? -11.334 -14.733 -18.035 1.00 32.00  ? 39  GLU A CB  1 
ATOM   303  C  CG  . GLU A 1 44  ? -11.241 -13.237 -17.858 1.00 35.60  ? 39  GLU A CG  1 
ATOM   304  C  CD  . GLU A 1 44  ? -11.305 -12.458 -19.148 1.00 39.49  ? 39  GLU A CD  1 
ATOM   305  O  OE1 . GLU A 1 44  ? -11.695 -13.065 -20.159 1.00 43.48  ? 39  GLU A OE1 1 
ATOM   306  O  OE2 . GLU A 1 44  ? -10.979 -11.251 -19.154 1.00 44.99  ? 39  GLU A OE2 1 
ATOM   307  N  N   . GLU A 1 45  ? -13.762 -15.558 -16.240 1.00 26.90  ? 40  GLU A N   1 
ATOM   308  C  CA  . GLU A 1 45  ? -15.011 -15.192 -15.600 1.00 26.59  ? 40  GLU A CA  1 
ATOM   309  C  C   . GLU A 1 45  ? -15.111 -15.730 -14.172 1.00 26.11  ? 40  GLU A C   1 
ATOM   310  O  O   . GLU A 1 45  ? -15.600 -14.999 -13.310 1.00 26.33  ? 40  GLU A O   1 
ATOM   311  C  CB  . GLU A 1 45  ? -16.212 -15.652 -16.422 1.00 28.60  ? 40  GLU A CB  1 
ATOM   312  C  CG  . GLU A 1 45  ? -16.386 -14.900 -17.745 1.00 29.21  ? 40  GLU A CG  1 
ATOM   313  C  CD  . GLU A 1 45  ? -17.337 -15.534 -18.746 1.00 29.83  ? 40  GLU A CD  1 
ATOM   314  O  OE1 . GLU A 1 45  ? -17.690 -16.729 -18.616 1.00 29.76  ? 40  GLU A OE1 1 
ATOM   315  O  OE2 . GLU A 1 45  ? -17.717 -14.818 -19.700 1.00 31.15  ? 40  GLU A OE2 1 
ATOM   316  N  N   . ARG A 1 46  ? -14.709 -16.992 -13.953 1.00 26.79  ? 41  ARG A N   1 
ATOM   317  C  CA  . ARG A 1 46  ? -14.579 -17.563 -12.611 1.00 28.53  ? 41  ARG A CA  1 
ATOM   318  C  C   . ARG A 1 46  ? -13.763 -16.637 -11.724 1.00 27.46  ? 41  ARG A C   1 
ATOM   319  O  O   . ARG A 1 46  ? -14.086 -16.412 -10.542 1.00 26.60  ? 41  ARG A O   1 
ATOM   320  C  CB  . ARG A 1 46  ? -13.851 -18.946 -12.614 1.00 31.50  ? 41  ARG A CB  1 
ATOM   321  C  CG  . ARG A 1 46  ? -14.728 -20.061 -12.994 1.00 38.96  ? 41  ARG A CG  1 
ATOM   322  C  CD  . ARG A 1 46  ? -14.111 -21.447 -12.794 1.00 42.07  ? 41  ARG A CD  1 
ATOM   323  N  NE  . ARG A 1 46  ? -12.896 -21.645 -13.565 1.00 44.81  ? 41  ARG A NE  1 
ATOM   324  C  CZ  . ARG A 1 46  ? -12.790 -22.359 -14.690 1.00 47.55  ? 41  ARG A CZ  1 
ATOM   325  N  NH1 . ARG A 1 46  ? -13.755 -22.395 -15.607 1.00 44.21  ? 41  ARG A NH1 1 
ATOM   326  N  NH2 . ARG A 1 46  ? -11.644 -22.982 -14.941 1.00 49.78  ? 41  ARG A NH2 1 
ATOM   327  N  N   . ASN A 1 47  ? -12.667 -16.126 -12.275 1.00 27.49  ? 42  ASN A N   1 
ATOM   328  C  CA  . ASN A 1 47  ? -11.781 -15.276 -11.504 1.00 28.89  ? 42  ASN A CA  1 
ATOM   329  C  C   . ASN A 1 47  ? -12.398 -13.907 -11.226 1.00 26.94  ? 42  ASN A C   1 
ATOM   330  O  O   . ASN A 1 47  ? -12.239 -13.386 -10.115 1.00 26.24  ? 42  ASN A O   1 
ATOM   331  C  CB  . ASN A 1 47  ? -10.413 -15.242 -12.138 1.00 31.91  ? 42  ASN A CB  1 
ATOM   332  C  CG  . ASN A 1 47  ? -9.639  -16.489 -11.688 1.00 38.01  ? 42  ASN A CG  1 
ATOM   333  O  OD1 . ASN A 1 47  ? -8.958  -16.477 -10.648 1.00 43.52  ? 42  ASN A OD1 1 
ATOM   334  N  ND2 . ASN A 1 47  ? -9.778  -17.633 -12.407 1.00 43.57  ? 42  ASN A ND2 1 
ATOM   335  N  N   . LEU A 1 48  ? -13.201 -13.386 -12.163 1.00 26.71  ? 43  LEU A N   1 
ATOM   336  C  CA  . LEU A 1 48  ? -13.954 -12.159 -11.914 1.00 26.85  ? 43  LEU A CA  1 
ATOM   337  C  C   . LEU A 1 48  ? -14.903 -12.351 -10.723 1.00 25.16  ? 43  LEU A C   1 
ATOM   338  O  O   . LEU A 1 48  ? -14.977 -11.503 -9.829  1.00 25.60  ? 43  LEU A O   1 
ATOM   339  C  CB  . LEU A 1 48  ? -14.746 -11.733 -13.160 1.00 28.35  ? 43  LEU A CB  1 
ATOM   340  C  CG  . LEU A 1 48  ? -13.912 -11.246 -14.319 1.00 29.23  ? 43  LEU A CG  1 
ATOM   341  C  CD1 . LEU A 1 48  ? -14.785 -11.151 -15.573 1.00 30.74  ? 43  LEU A CD1 1 
ATOM   342  C  CD2 . LEU A 1 48  ? -13.227 -9.918  -14.036 1.00 30.63  ? 43  LEU A CD2 1 
ATOM   343  N  N   . LEU A 1 49  ? -15.614 -13.478 -10.716 1.00 25.31  ? 44  LEU A N   1 
ATOM   344  C  CA  . LEU A 1 49  ? -16.572 -13.766 -9.660  1.00 25.18  ? 44  LEU A CA  1 
ATOM   345  C  C   . LEU A 1 49  ? -15.811 -13.862 -8.339  1.00 25.61  ? 44  LEU A C   1 
ATOM   346  O  O   . LEU A 1 49  ? -16.269 -13.277 -7.326  1.00 24.92  ? 44  LEU A O   1 
ATOM   347  C  CB  . LEU A 1 49  ? -17.304 -15.074 -9.913  1.00 26.75  ? 44  LEU A CB  1 
ATOM   348  C  CG  . LEU A 1 49  ? -18.269 -15.576 -8.860  1.00 26.56  ? 44  LEU A CG  1 
ATOM   349  C  CD1 . LEU A 1 49  ? -19.555 -14.784 -8.867  1.00 27.15  ? 44  LEU A CD1 1 
ATOM   350  C  CD2 . LEU A 1 49  ? -18.513 -17.074 -9.062  1.00 27.85  ? 44  LEU A CD2 1 
ATOM   351  N  N   . SER A 1 50  ? -14.719 -14.643 -8.335  1.00 25.62  ? 45  SER A N   1 
ATOM   352  C  CA  . SER A 1 50  ? -14.000 -14.894 -7.073  1.00 26.79  ? 45  SER A CA  1 
ATOM   353  C  C   . SER A 1 50  ? -13.369 -13.621 -6.507  1.00 25.82  ? 45  SER A C   1 
ATOM   354  O  O   . SER A 1 50  ? -13.443 -13.357 -5.290  1.00 26.09  ? 45  SER A O   1 
ATOM   355  C  CB  . SER A 1 50  ? -12.938 -15.976 -7.241  1.00 28.59  ? 45  SER A CB  1 
ATOM   356  O  OG  . SER A 1 50  ? -12.227 -16.121 -6.011  1.00 31.03  ? 45  SER A OG  1 
ATOM   357  N  N   . VAL A 1 51  ? -12.743 -12.812 -7.368  1.00 25.07  ? 46  VAL A N   1 
ATOM   358  C  CA  . VAL A 1 51  ? -12.141 -11.559 -6.942  1.00 26.00  ? 46  VAL A CA  1 
ATOM   359  C  C   . VAL A 1 51  ? -13.160 -10.586 -6.338  1.00 25.65  ? 46  VAL A C   1 
ATOM   360  O  O   . VAL A 1 51  ? -12.909 -9.990  -5.286  1.00 25.18  ? 46  VAL A O   1 
ATOM   361  C  CB  . VAL A 1 51  ? -11.330 -10.917 -8.095  1.00 27.91  ? 46  VAL A CB  1 
ATOM   362  C  CG1 . VAL A 1 51  ? -10.918 -9.481  -7.794  1.00 30.23  ? 46  VAL A CG1 1 
ATOM   363  C  CG2 . VAL A 1 51  ? -10.105 -11.759 -8.419  1.00 29.59  ? 46  VAL A CG2 1 
ATOM   364  N  N   . ALA A 1 52  ? -14.323 -10.471 -6.984  1.00 26.01  ? 47  ALA A N   1 
ATOM   365  C  CA  . ALA A 1 52  ? -15.370 -9.558  -6.581  1.00 25.17  ? 47  ALA A CA  1 
ATOM   366  C  C   . ALA A 1 52  ? -15.828 -9.918  -5.167  1.00 25.58  ? 47  ALA A C   1 
ATOM   367  O  O   . ALA A 1 52  ? -15.768 -9.068  -4.278  1.00 25.04  ? 47  ALA A O   1 
ATOM   368  C  CB  . ALA A 1 52  ? -16.526 -9.616  -7.540  1.00 24.67  ? 47  ALA A CB  1 
ATOM   369  N  N   . TYR A 1 53  ? -16.301 -11.154 -5.003  1.00 25.60  ? 48  TYR A N   1 
ATOM   370  C  CA  . TYR A 1 53  ? -16.868 -11.567 -3.709  1.00 24.80  ? 48  TYR A CA  1 
ATOM   371  C  C   . TYR A 1 53  ? -15.802 -11.632 -2.625  1.00 24.09  ? 48  TYR A C   1 
ATOM   372  O  O   . TYR A 1 53  ? -16.104 -11.305 -1.457  1.00 24.31  ? 48  TYR A O   1 
ATOM   373  C  CB  . TYR A 1 53  ? -17.633 -12.871 -3.805  1.00 25.24  ? 48  TYR A CB  1 
ATOM   374  C  CG  . TYR A 1 53  ? -19.035 -12.680 -4.294  1.00 24.91  ? 48  TYR A CG  1 
ATOM   375  C  CD1 . TYR A 1 53  ? -19.987 -12.050 -3.519  1.00 25.15  ? 48  TYR A CD1 1 
ATOM   376  C  CD2 . TYR A 1 53  ? -19.387 -12.998 -5.603  1.00 25.69  ? 48  TYR A CD2 1 
ATOM   377  C  CE1 . TYR A 1 53  ? -21.290 -11.881 -3.962  1.00 25.94  ? 48  TYR A CE1 1 
ATOM   378  C  CE2 . TYR A 1 53  ? -20.677 -12.821 -6.049  1.00 25.95  ? 48  TYR A CE2 1 
ATOM   379  C  CZ  . TYR A 1 53  ? -21.623 -12.242 -5.249  1.00 25.77  ? 48  TYR A CZ  1 
ATOM   380  O  OH  . TYR A 1 53  ? -22.903 -12.064 -5.695  1.00 26.56  ? 48  TYR A OH  1 
ATOM   381  N  N   . LYS A 1 54  ? -14.570 -12.024 -2.961  1.00 24.72  ? 49  LYS A N   1 
ATOM   382  C  CA  . LYS A 1 54  ? -13.530 -12.044 -1.926  1.00 25.20  ? 49  LYS A CA  1 
ATOM   383  C  C   . LYS A 1 54  ? -13.174 -10.646 -1.402  1.00 25.56  ? 49  LYS A C   1 
ATOM   384  O  O   . LYS A 1 54  ? -12.901 -10.460 -0.194  1.00 26.29  ? 49  LYS A O   1 
ATOM   385  C  CB  . LYS A 1 54  ? -12.264 -12.764 -2.385  1.00 27.12  ? 49  LYS A CB  1 
ATOM   386  C  CG  . LYS A 1 54  ? -11.208 -12.974 -1.273  1.00 28.61  ? 49  LYS A CG  1 
ATOM   387  C  CD  . LYS A 1 54  ? -11.761 -13.862 -0.152  1.00 30.95  ? 49  LYS A CD  1 
ATOM   388  C  CE  . LYS A 1 54  ? -10.883 -13.963 1.048   1.00 31.12  ? 49  LYS A CE  1 
ATOM   389  N  NZ  . LYS A 1 54  ? -9.597  -14.589 0.734   1.00 34.32  ? 49  LYS A NZ  1 
ATOM   390  N  N   . ASN A 1 55  ? -13.208 -9.642  -2.274  1.00 24.57  ? 50  ASN A N   1 
ATOM   391  C  CA  . ASN A 1 55  ? -12.991 -8.266  -1.880  1.00 25.37  ? 50  ASN A CA  1 
ATOM   392  C  C   . ASN A 1 55  ? -14.098 -7.784  -0.947  1.00 24.56  ? 50  ASN A C   1 
ATOM   393  O  O   . ASN A 1 55  ? -13.792 -7.155  0.077   1.00 25.98  ? 50  ASN A O   1 
ATOM   394  C  CB  . ASN A 1 55  ? -12.857 -7.365  -3.071  1.00 26.70  ? 50  ASN A CB  1 
ATOM   395  C  CG  . ASN A 1 55  ? -11.453 -7.182  -3.499  1.00 29.94  ? 50  ASN A CG  1 
ATOM   396  O  OD1 . ASN A 1 55  ? -10.717 -6.400  -2.915  1.00 34.10  ? 50  ASN A OD1 1 
ATOM   397  N  ND2 . ASN A 1 55  ? -11.059 -7.787  -4.589  1.00 32.28  ? 50  ASN A ND2 1 
ATOM   398  N  N   . VAL A 1 56  ? -15.347 -8.146  -1.265  1.00 25.74  ? 51  VAL A N   1 
ATOM   399  C  CA  . VAL A 1 56  ? -16.504 -7.760  -0.471  1.00 26.61  ? 51  VAL A CA  1 
ATOM   400  C  C   . VAL A 1 56  ? -16.416 -8.432  0.915   1.00 27.84  ? 51  VAL A C   1 
ATOM   401  O  O   . VAL A 1 56  ? -16.462 -7.734  1.939   1.00 27.62  ? 51  VAL A O   1 
ATOM   402  C  CB  . VAL A 1 56  ? -17.838 -8.101  -1.131  1.00 27.33  ? 51  VAL A CB  1 
ATOM   403  C  CG1 . VAL A 1 56  ? -19.050 -7.857  -0.225  1.00 27.80  ? 51  VAL A CG1 1 
ATOM   404  C  CG2 . VAL A 1 56  ? -17.990 -7.305  -2.446  1.00 28.30  ? 51  VAL A CG2 1 
ATOM   405  N  N   . VAL A 1 57  ? -16.307 -9.765  0.938   1.00 28.67  ? 52  VAL A N   1 
ATOM   406  C  CA  . VAL A 1 57  ? -16.286 -10.473 2.231   1.00 29.50  ? 52  VAL A CA  1 
ATOM   407  C  C   . VAL A 1 57  ? -15.021 -10.103 3.000   1.00 29.31  ? 52  VAL A C   1 
ATOM   408  O  O   . VAL A 1 57  ? -15.029 -10.058 4.271   1.00 29.25  ? 52  VAL A O   1 
ATOM   409  C  CB  . VAL A 1 57  ? -16.486 -12.002 2.064   1.00 29.95  ? 52  VAL A CB  1 
ATOM   410  C  CG1 . VAL A 1 57  ? -15.244 -12.669 1.487   1.00 32.25  ? 52  VAL A CG1 1 
ATOM   411  C  CG2 . VAL A 1 57  ? -16.850 -12.683 3.372   1.00 31.71  ? 52  VAL A CG2 1 
ATOM   412  N  N   . GLY A 1 58  ? -13.919 -9.838  2.288   1.00 28.63  ? 53  GLY A N   1 
ATOM   413  C  CA  . GLY A 1 58  ? -12.667 -9.456  2.938   1.00 28.86  ? 53  GLY A CA  1 
ATOM   414  C  C   . GLY A 1 58  ? -12.769 -8.203  3.804   1.00 28.32  ? 53  GLY A C   1 
ATOM   415  O  O   . GLY A 1 58  ? -12.243 -8.142  4.931   1.00 29.21  ? 53  GLY A O   1 
ATOM   416  N  N   . GLY A 1 59  ? -13.485 -7.206  3.294   1.00 28.81  ? 54  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 59  ? -13.725 -5.975  4.018   1.00 29.26  ? 54  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 59  ? -14.545 -6.275  5.273   1.00 29.14  ? 54  GLY A C   1 
ATOM   419  O  O   . GLY A 1 59  ? -14.237 -5.747  6.363   1.00 28.22  ? 54  GLY A O   1 
ATOM   420  N  N   . GLN A 1 60  ? -15.578 -7.124  5.123   1.00 28.87  ? 55  GLN A N   1 
ATOM   421  C  CA  . GLN A 1 60  ? -16.450 -7.429  6.261   1.00 28.81  ? 55  GLN A CA  1 
ATOM   422  C  C   . GLN A 1 60  ? -15.680 -8.244  7.301   1.00 28.99  ? 55  GLN A C   1 
ATOM   423  O  O   . GLN A 1 60  ? -15.829 -8.001  8.536   1.00 29.00  ? 55  GLN A O   1 
ATOM   424  C  CB  . GLN A 1 60  ? -17.723 -8.148  5.811   1.00 29.12  ? 55  GLN A CB  1 
ATOM   425  C  CG  . GLN A 1 60  ? -18.514 -7.338  4.774   1.00 29.99  ? 55  GLN A CG  1 
ATOM   426  C  CD  . GLN A 1 60  ? -19.519 -8.190  4.049   1.00 29.73  ? 55  GLN A CD  1 
ATOM   427  O  OE1 . GLN A 1 60  ? -19.266 -9.369  3.765   1.00 30.32  ? 55  GLN A OE1 1 
ATOM   428  N  NE2 . GLN A 1 60  ? -20.694 -7.618  3.761   1.00 32.57  ? 55  GLN A NE2 1 
ATOM   429  N  N   . ARG A 1 61  ? -14.901 -9.243  6.847   1.00 28.10  ? 56  ARG A N   1 
ATOM   430  C  CA  . ARG A 1 61  ? -14.109 -10.040 7.786   1.00 28.29  ? 56  ARG A CA  1 
ATOM   431  C  C   . ARG A 1 61  ? -13.134 -9.158  8.577   1.00 28.92  ? 56  ARG A C   1 
ATOM   432  O  O   . ARG A 1 61  ? -12.999 -9.293  9.821   1.00 28.78  ? 56  ARG A O   1 
ATOM   433  C  CB  . ARG A 1 61  ? -13.250 -11.109 7.072   1.00 30.65  ? 56  ARG A CB  1 
ATOM   434  C  CG  . ARG A 1 61  ? -13.960 -12.295 6.548   1.00 33.69  ? 56  ARG A CG  1 
ATOM   435  C  CD  . ARG A 1 61  ? -13.047 -13.211 5.704   1.00 36.31  ? 56  ARG A CD  1 
ATOM   436  N  NE  . ARG A 1 61  ? -12.058 -13.984 6.466   1.00 35.43  ? 56  ARG A NE  1 
ATOM   437  C  CZ  . ARG A 1 61  ? -10.999 -14.582 5.913   1.00 32.69  ? 56  ARG A CZ  1 
ATOM   438  N  NH1 . ARG A 1 61  ? -10.399 -14.089 4.844   1.00 34.34  ? 56  ARG A NH1 1 
ATOM   439  N  NH2 . ARG A 1 61  ? -10.515 -15.691 6.455   1.00 29.88  ? 56  ARG A NH2 1 
ATOM   440  N  N   . ALA A 1 62  ? -12.447 -8.239  7.872   1.00 28.36  ? 57  ALA A N   1 
ATOM   441  C  CA  . ALA A 1 62  ? -11.475 -7.386  8.550   1.00 29.19  ? 57  ALA A CA  1 
ATOM   442  C  C   . ALA A 1 62  ? -12.161 -6.532  9.622   1.00 28.32  ? 57  ALA A C   1 
ATOM   443  O  O   . ALA A 1 62  ? -11.650 -6.399  10.760  1.00 28.82  ? 57  ALA A O   1 
ATOM   444  C  CB  . ALA A 1 62  ? -10.718 -6.521  7.549   1.00 30.05  ? 57  ALA A CB  1 
ATOM   445  N  N   . ALA A 1 63  ? -13.337 -5.992  9.276   1.00 27.99  ? 58  ALA A N   1 
ATOM   446  C  CA  . ALA A 1 63  ? -14.136 -5.180  10.188  1.00 28.98  ? 58  ALA A CA  1 
ATOM   447  C  C   . ALA A 1 63  ? -14.636 -6.006  11.376  1.00 28.71  ? 58  ALA A C   1 
ATOM   448  O  O   . ALA A 1 63  ? -14.536 -5.573  12.558  1.00 29.69  ? 58  ALA A O   1 
ATOM   449  C  CB  . ALA A 1 63  ? -15.327 -4.570  9.447   1.00 29.62  ? 58  ALA A CB  1 
ATOM   450  N  N   . TRP A 1 64  ? -15.185 -7.194  11.085  1.00 28.51  ? 59  TRP A N   1 
ATOM   451  C  CA  . TRP A 1 64  ? -15.648 -8.096  12.141  1.00 28.44  ? 59  TRP A CA  1 
ATOM   452  C  C   . TRP A 1 64  ? -14.540 -8.446  13.124  1.00 28.78  ? 59  TRP A C   1 
ATOM   453  O  O   . TRP A 1 64  ? -14.771 -8.480  14.348  1.00 31.69  ? 59  TRP A O   1 
ATOM   454  C  CB  . TRP A 1 64  ? -16.242 -9.377  11.523  1.00 29.06  ? 59  TRP A CB  1 
ATOM   455  C  CG  . TRP A 1 64  ? -16.965 -10.248 12.517  1.00 30.29  ? 59  TRP A CG  1 
ATOM   456  C  CD1 . TRP A 1 64  ? -18.305 -10.268 12.794  1.00 31.53  ? 59  TRP A CD1 1 
ATOM   457  C  CD2 . TRP A 1 64  ? -16.363 -11.251 13.353  1.00 29.57  ? 59  TRP A CD2 1 
ATOM   458  N  NE1 . TRP A 1 64  ? -18.563 -11.211 13.793  1.00 31.59  ? 59  TRP A NE1 1 
ATOM   459  C  CE2 . TRP A 1 64  ? -17.392 -11.840 14.121  1.00 30.69  ? 59  TRP A CE2 1 
ATOM   460  C  CE3 . TRP A 1 64  ? -15.056 -11.728 13.495  1.00 31.17  ? 59  TRP A CE3 1 
ATOM   461  C  CZ2 . TRP A 1 64  ? -17.150 -12.872 15.021  1.00 30.55  ? 59  TRP A CZ2 1 
ATOM   462  C  CZ3 . TRP A 1 64  ? -14.821 -12.744 14.389  1.00 32.81  ? 59  TRP A CZ3 1 
ATOM   463  C  CH2 . TRP A 1 64  ? -15.863 -13.310 15.140  1.00 31.40  ? 59  TRP A CH2 1 
ATOM   464  N  N   . ARG A 1 65  ? -13.329 -8.718  12.614  1.00 28.45  ? 60  ARG A N   1 
ATOM   465  C  CA  . ARG A 1 65  ? -12.219 -9.051  13.505  1.00 29.47  ? 60  ARG A CA  1 
ATOM   466  C  C   . ARG A 1 65  ? -11.828 -7.896  14.428  1.00 30.71  ? 60  ARG A C   1 
ATOM   467  O  O   . ARG A 1 65  ? -11.605 -8.092  15.643  1.00 32.24  ? 60  ARG A O   1 
ATOM   468  C  CB  . ARG A 1 65  ? -11.000 -9.504  12.690  1.00 29.93  ? 60  ARG A CB  1 
ATOM   469  C  CG  . ARG A 1 65  ? -11.177 -10.886 12.055  1.00 29.61  ? 60  ARG A CG  1 
ATOM   470  C  CD  . ARG A 1 65  ? -10.063 -11.209 11.067  1.00 30.99  ? 60  ARG A CD  1 
ATOM   471  N  NE  . ARG A 1 65  ? -10.289 -12.538 10.513  1.00 34.71  ? 60  ARG A NE  1 
ATOM   472  C  CZ  . ARG A 1 65  ? -9.447  -13.202 9.744   1.00 39.83  ? 60  ARG A CZ  1 
ATOM   473  N  NH1 . ARG A 1 65  ? -8.366  -12.624 9.245   1.00 45.85  ? 60  ARG A NH1 1 
ATOM   474  N  NH2 . ARG A 1 65  ? -9.722  -14.465 9.422   1.00 39.99  ? 60  ARG A NH2 1 
ATOM   475  N  N   . VAL A 1 66  ? -11.768 -6.679  13.871  1.00 30.80  ? 61  VAL A N   1 
ATOM   476  C  CA  . VAL A 1 66  ? -11.498 -5.492  14.671  1.00 33.16  ? 61  VAL A CA  1 
ATOM   477  C  C   . VAL A 1 66  ? -12.516 -5.335  15.792  1.00 32.95  ? 61  VAL A C   1 
ATOM   478  O  O   . VAL A 1 66  ? -12.155 -5.089  16.957  1.00 33.09  ? 61  VAL A O   1 
ATOM   479  C  CB  . VAL A 1 66  ? -11.503 -4.230  13.769  1.00 34.45  ? 61  VAL A CB  1 
ATOM   480  C  CG1 . VAL A 1 66  ? -11.753 -2.949  14.589  1.00 38.19  ? 61  VAL A CG1 1 
ATOM   481  C  CG2 . VAL A 1 66  ? -10.199 -4.125  12.999  1.00 34.42  ? 61  VAL A CG2 1 
ATOM   482  N  N   . LEU A 1 67  ? -13.798 -5.451  15.418  1.00 32.62  ? 62  LEU A N   1 
ATOM   483  C  CA  . LEU A 1 67  ? -14.888 -5.255  16.365  1.00 34.15  ? 62  LEU A CA  1 
ATOM   484  C  C   . LEU A 1 67  ? -14.963 -6.380  17.395  1.00 35.44  ? 62  LEU A C   1 
ATOM   485  O  O   . LEU A 1 67  ? -15.140 -6.096  18.598  1.00 37.53  ? 62  LEU A O   1 
ATOM   486  C  CB  . LEU A 1 67  ? -16.201 -5.154  15.581  1.00 33.43  ? 62  LEU A CB  1 
ATOM   487  C  CG  . LEU A 1 67  ? -16.313 -3.945  14.684  1.00 32.71  ? 62  LEU A CG  1 
ATOM   488  C  CD1 . LEU A 1 67  ? -17.616 -3.990  13.892  1.00 33.42  ? 62  LEU A CD1 1 
ATOM   489  C  CD2 . LEU A 1 67  ? -16.237 -2.644  15.422  1.00 33.32  ? 62  LEU A CD2 1 
ATOM   490  N  N   . SER A 1 68  ? -14.808 -7.633  16.944  1.00 36.79  ? 63  SER A N   1 
ATOM   491  C  CA  . SER A 1 68  ? -14.827 -8.780  17.852  1.00 38.11  ? 63  SER A CA  1 
ATOM   492  C  C   . SER A 1 68  ? -13.680 -8.705  18.858  1.00 41.23  ? 63  SER A C   1 
ATOM   493  O  O   . SER A 1 68  ? -13.842 -8.987  20.070  1.00 46.13  ? 63  SER A O   1 
ATOM   494  C  CB  . SER A 1 68  ? -14.804 -10.088 17.027  1.00 39.02  ? 63  SER A CB  1 
ATOM   495  O  OG  . SER A 1 68  ? -14.843 -11.210 17.911  1.00 43.29  ? 63  SER A OG  1 
ATOM   496  N  N   . SER A 1 69  ? -12.509 -8.250  18.407  1.00 42.84  ? 64  SER A N   1 
ATOM   497  C  CA  . SER A 1 69  ? -11.397 -8.106  19.348  1.00 44.71  ? 64  SER A CA  1 
ATOM   498  C  C   . SER A 1 69  ? -11.652 -7.096  20.467  1.00 45.03  ? 64  SER A C   1 
ATOM   499  O  O   . SER A 1 69  ? -11.245 -7.286  21.635  1.00 48.43  ? 64  SER A O   1 
ATOM   500  C  CB  . SER A 1 69  ? -10.140 -7.687  18.591  1.00 47.82  ? 64  SER A CB  1 
ATOM   501  O  OG  . SER A 1 69  ? -9.177  -7.250  19.538  1.00 52.31  ? 64  SER A OG  1 
ATOM   502  N  N   . ILE A 1 70  ? -12.267 -5.971  20.100  1.00 45.34  ? 65  ILE A N   1 
ATOM   503  C  CA  . ILE A 1 70  ? -12.612 -4.944  21.066  1.00 45.41  ? 65  ILE A CA  1 
ATOM   504  C  C   . ILE A 1 70  ? -13.672 -5.506  22.013  1.00 48.89  ? 65  ILE A C   1 
ATOM   505  O  O   . ILE A 1 70  ? -13.535 -5.399  23.240  1.00 51.90  ? 65  ILE A O   1 
ATOM   506  C  CB  . ILE A 1 70  ? -13.051 -3.641  20.358  1.00 45.87  ? 65  ILE A CB  1 
ATOM   507  C  CG1 . ILE A 1 70  ? -11.873 -3.005  19.612  1.00 46.05  ? 65  ILE A CG1 1 
ATOM   508  C  CG2 . ILE A 1 70  ? -13.662 -2.649  21.341  1.00 47.19  ? 65  ILE A CG2 1 
ATOM   509  C  CD1 . ILE A 1 70  ? -12.286 -1.919  18.578  1.00 45.83  ? 65  ILE A CD1 1 
ATOM   510  N  N   . GLU A 1 71  ? -14.708 -6.135  21.435  1.00 49.55  ? 66  GLU A N   1 
ATOM   511  C  CA  . GLU A 1 71  ? -15.792 -6.717  22.219  1.00 51.06  ? 66  GLU A CA  1 
ATOM   512  C  C   . GLU A 1 71  ? -15.288 -7.725  23.253  1.00 54.92  ? 66  GLU A C   1 
ATOM   513  O  O   . GLU A 1 71  ? -15.683 -7.682  24.425  1.00 58.33  ? 66  GLU A O   1 
ATOM   514  C  CB  . GLU A 1 71  ? -16.795 -7.392  21.273  1.00 50.43  ? 66  GLU A CB  1 
ATOM   515  C  CG  . GLU A 1 71  ? -18.094 -7.763  21.948  1.00 50.07  ? 66  GLU A CG  1 
ATOM   516  C  CD  . GLU A 1 71  ? -19.037 -8.589  21.104  1.00 50.74  ? 66  GLU A CD  1 
ATOM   517  O  OE1 . GLU A 1 71  ? -18.742 -8.862  19.911  1.00 50.98  ? 66  GLU A OE1 1 
ATOM   518  O  OE2 . GLU A 1 71  ? -20.087 -8.978  21.659  1.00 51.22  ? 66  GLU A OE2 1 
ATOM   519  N  N   . GLN A 1 72  ? -14.407 -8.633  22.819  1.00 55.27  ? 67  GLN A N   1 
ATOM   520  C  CA  . GLN A 1 72  ? -13.818 -9.618  23.717  1.00 60.84  ? 67  GLN A CA  1 
ATOM   521  C  C   . GLN A 1 72  ? -12.992 -8.981  24.830  1.00 63.76  ? 67  GLN A C   1 
ATOM   522  O  O   . GLN A 1 72  ? -13.039 -9.423  25.979  1.00 65.00  ? 67  GLN A O   1 
ATOM   523  C  CB  . GLN A 1 72  ? -12.905 -10.568 22.946  1.00 62.99  ? 67  GLN A CB  1 
ATOM   524  C  CG  . GLN A 1 72  ? -13.651 -11.613 22.139  1.00 64.82  ? 67  GLN A CG  1 
ATOM   525  C  CD  . GLN A 1 72  ? -12.709 -12.468 21.310  1.00 71.35  ? 67  GLN A CD  1 
ATOM   526  O  OE1 . GLN A 1 72  ? -12.211 -12.052 20.246  1.00 72.47  ? 67  GLN A OE1 1 
ATOM   527  N  NE2 . GLN A 1 72  ? -12.455 -13.698 21.764  1.00 75.42  ? 67  GLN A NE2 1 
ATOM   528  N  N   . LYS A 1 73  ? -12.240 -7.933  24.474  1.00 66.45  ? 68  LYS A N   1 
ATOM   529  C  CA  . LYS A 1 73  ? -11.350 -7.254  25.407  1.00 70.23  ? 68  LYS A CA  1 
ATOM   530  C  C   . LYS A 1 73  ? -12.106 -6.495  26.501  1.00 68.07  ? 68  LYS A C   1 
ATOM   531  O  O   . LYS A 1 73  ? -11.533 -6.111  27.527  1.00 73.14  ? 68  LYS A O   1 
ATOM   532  C  CB  . LYS A 1 73  ? -10.450 -6.287  24.615  1.00 70.88  ? 68  LYS A CB  1 
ATOM   533  C  CG  . LYS A 1 73  ? -9.080  -6.060  25.222  1.00 74.97  ? 68  LYS A CG  1 
ATOM   534  C  CD  . LYS A 1 73  ? -8.237  -5.095  24.392  1.00 76.13  ? 68  LYS A CD  1 
ATOM   535  C  CE  . LYS A 1 73  ? -7.873  -5.663  23.042  1.00 78.86  ? 68  LYS A CE  1 
ATOM   536  N  NZ  . LYS A 1 73  ? -6.971  -4.757  22.287  1.00 81.83  ? 68  LYS A NZ  1 
ATOM   537  N  N   . SER A 1 74  ? -13.402 -6.265  26.269  1.00 69.40  ? 69  SER A N   1 
ATOM   538  C  CA  . SER A 1 74  ? -14.242 -5.551  27.214  1.00 71.91  ? 69  SER A CA  1 
ATOM   539  C  C   . SER A 1 74  ? -15.021 -6.506  28.116  1.00 77.92  ? 69  SER A C   1 
ATOM   540  O  O   . SER A 1 74  ? -15.294 -6.168  29.267  1.00 80.83  ? 69  SER A O   1 
ATOM   541  C  CB  . SER A 1 74  ? -15.197 -4.614  26.487  1.00 74.36  ? 69  SER A CB  1 
ATOM   542  O  OG  . SER A 1 74  ? -16.119 -5.332  25.681  1.00 73.36  ? 69  SER A OG  1 
ATOM   543  N  N   . ASN A 1 75  ? -15.346 -7.704  27.604  1.00 79.52  ? 70  ASN A N   1 
ATOM   544  C  CA  . ASN A 1 75  ? -16.100 -8.690  28.365  1.00 82.64  ? 70  ASN A CA  1 
ATOM   545  C  C   . ASN A 1 75  ? -15.209 -9.478  29.327  1.00 88.37  ? 70  ASN A C   1 
ATOM   546  O  O   . ASN A 1 75  ? -15.396 -10.676 29.547  1.00 85.34  ? 70  ASN A O   1 
ATOM   547  C  CB  . ASN A 1 75  ? -16.901 -9.594  27.423  1.00 80.38  ? 70  ASN A CB  1 
ATOM   548  C  CG  . ASN A 1 75  ? -17.992 -8.825  26.712  1.00 82.55  ? 70  ASN A CG  1 
ATOM   549  O  OD1 . ASN A 1 75  ? -18.075 -8.805  25.475  1.00 81.97  ? 70  ASN A OD1 1 
ATOM   550  N  ND2 . ASN A 1 75  ? -18.846 -8.149  27.483  1.00 82.51  ? 70  ASN A ND2 1 
ATOM   551  N  N   . GLU A 1 76  ? -14.266 -8.757  29.940  1.00 90.83  ? 71  GLU A N   1 
ATOM   552  C  CA  . GLU A 1 76  ? -13.446 -9.283  31.014  1.00 98.49  ? 71  GLU A CA  1 
ATOM   553  C  C   . GLU A 1 76  ? -13.690 -8.339  32.192  1.00 101.73 ? 71  GLU A C   1 
ATOM   554  O  O   . GLU A 1 76  ? -14.489 -8.663  33.069  1.00 109.89 ? 71  GLU A O   1 
ATOM   555  C  CB  . GLU A 1 76  ? -11.970 -9.447  30.566  1.00 98.66  ? 71  GLU A CB  1 
ATOM   556  C  CG  . GLU A 1 76  ? -11.462 -8.389  29.596  1.00 96.17  ? 71  GLU A CG  1 
ATOM   557  C  CD  . GLU A 1 76  ? -10.207 -8.779  28.850  1.00 94.91  ? 71  GLU A CD  1 
ATOM   558  O  OE1 . GLU A 1 76  ? -10.181 -9.891  28.278  1.00 95.35  ? 71  GLU A OE1 1 
ATOM   559  O  OE2 . GLU A 1 76  ? -9.257  -7.965  28.816  1.00 95.07  ? 71  GLU A OE2 1 
ATOM   560  N  N   . GLU A 1 77  ? -13.053 -7.158  32.181  1.00 105.08 ? 72  GLU A N   1 
ATOM   561  C  CA  . GLU A 1 77  ? -13.317 -6.123  33.172  1.00 104.98 ? 72  GLU A CA  1 
ATOM   562  C  C   . GLU A 1 77  ? -13.103 -4.734  32.572  1.00 103.22 ? 72  GLU A C   1 
ATOM   563  O  O   . GLU A 1 77  ? -11.998 -4.398  32.146  1.00 104.24 ? 72  GLU A O   1 
ATOM   564  C  CB  . GLU A 1 77  ? -12.439 -6.291  34.430  1.00 105.54 ? 72  GLU A CB  1 
ATOM   565  C  CG  . GLU A 1 77  ? -12.810 -7.487  35.289  1.00 109.73 ? 72  GLU A CG  1 
ATOM   566  C  CD  . GLU A 1 77  ? -12.361 -8.835  34.758  1.00 113.52 ? 72  GLU A CD  1 
ATOM   567  O  OE1 . GLU A 1 77  ? -11.499 -8.862  33.850  1.00 115.92 ? 72  GLU A OE1 1 
ATOM   568  O  OE2 . GLU A 1 77  ? -12.895 -9.865  35.228  1.00 114.93 ? 72  GLU A OE2 1 
ATOM   569  N  N   . GLY A 1 78  ? -14.181 -3.938  32.546  1.00 99.63  ? 73  GLY A N   1 
ATOM   570  C  CA  . GLY A 1 78  ? -14.153 -2.594  31.993  1.00 97.09  ? 73  GLY A CA  1 
ATOM   571  C  C   . GLY A 1 78  ? -14.174 -2.586  30.482  1.00 95.37  ? 73  GLY A C   1 
ATOM   572  O  O   . GLY A 1 78  ? -13.165 -2.268  29.856  1.00 95.51  ? 73  GLY A O   1 
ATOM   573  N  N   . GLY A 1 83  ? -21.312 -0.087  27.452  1.00 58.17  ? 78  GLY A N   1 
ATOM   574  C  CA  . GLY A 1 83  ? -22.456 0.133   26.580  1.00 54.17  ? 78  GLY A CA  1 
ATOM   575  C  C   . GLY A 1 83  ? -22.608 -0.976  25.542  1.00 51.51  ? 78  GLY A C   1 
ATOM   576  O  O   . GLY A 1 83  ? -21.667 -1.731  25.277  1.00 56.57  ? 78  GLY A O   1 
ATOM   577  N  N   . PRO A 1 84  ? -23.776 -1.061  24.868  1.00 50.18  ? 79  PRO A N   1 
ATOM   578  C  CA  . PRO A 1 84  ? -24.015 -2.090  23.848  1.00 47.69  ? 79  PRO A CA  1 
ATOM   579  C  C   . PRO A 1 84  ? -23.432 -1.822  22.454  1.00 46.66  ? 79  PRO A C   1 
ATOM   580  O  O   . PRO A 1 84  ? -23.606 -2.645  21.539  1.00 43.20  ? 79  PRO A O   1 
ATOM   581  C  CB  . PRO A 1 84  ? -25.547 -2.097  23.781  1.00 48.00  ? 79  PRO A CB  1 
ATOM   582  C  CG  . PRO A 1 84  ? -25.946 -0.672  24.116  1.00 46.77  ? 79  PRO A CG  1 
ATOM   583  C  CD  . PRO A 1 84  ? -24.907 -0.132  25.024  1.00 49.92  ? 79  PRO A CD  1 
ATOM   584  N  N   . GLU A 1 85  ? -22.736 -0.686  22.291  1.00 46.87  ? 80  GLU A N   1 
ATOM   585  C  CA  . GLU A 1 85  ? -22.418 -0.217  20.938  1.00 45.68  ? 80  GLU A CA  1 
ATOM   586  C  C   . GLU A 1 85  ? -21.529 -1.192  20.176  1.00 45.02  ? 80  GLU A C   1 
ATOM   587  O  O   . GLU A 1 85  ? -21.820 -1.491  19.006  1.00 51.55  ? 80  GLU A O   1 
ATOM   588  C  CB  . GLU A 1 85  ? -21.726 1.157   20.944  1.00 45.46  ? 80  GLU A CB  1 
ATOM   589  C  CG  . GLU A 1 85  ? -22.608 2.319   21.398  1.00 46.32  ? 80  GLU A CG  1 
ATOM   590  C  CD  . GLU A 1 85  ? -22.871 2.449   22.893  1.00 47.50  ? 80  GLU A CD  1 
ATOM   591  O  OE1 . GLU A 1 85  ? -22.275 1.698   23.708  1.00 49.60  ? 80  GLU A OE1 1 
ATOM   592  O  OE2 . GLU A 1 85  ? -23.693 3.322   23.257  1.00 51.13  ? 80  GLU A OE2 1 
ATOM   593  N  N   . VAL A 1 86  ? -20.445 -1.658  20.815  1.00 43.31  ? 81  VAL A N   1 
ATOM   594  C  CA  . VAL A 1 86  ? -19.489 -2.553  20.182  1.00 41.36  ? 81  VAL A CA  1 
ATOM   595  C  C   . VAL A 1 86  ? -20.205 -3.828  19.739  1.00 39.81  ? 81  VAL A C   1 
ATOM   596  O  O   . VAL A 1 86  ? -20.128 -4.233  18.578  1.00 39.72  ? 81  VAL A O   1 
ATOM   597  C  CB  . VAL A 1 86  ? -18.259 -2.892  21.048  1.00 44.54  ? 81  VAL A CB  1 
ATOM   598  C  CG1 . VAL A 1 86  ? -17.286 -3.786  20.272  1.00 45.60  ? 81  VAL A CG1 1 
ATOM   599  C  CG2 . VAL A 1 86  ? -17.558 -1.633  21.529  1.00 46.25  ? 81  VAL A CG2 1 
ATOM   600  N  N   . ARG A 1 87  ? -20.950 -4.444  20.652  1.00 40.10  ? 82  ARG A N   1 
ATOM   601  C  CA  . ARG A 1 87  ? -21.698 -5.649  20.339  1.00 39.27  ? 82  ARG A CA  1 
ATOM   602  C  C   . ARG A 1 87  ? -22.651 -5.407  19.158  1.00 36.33  ? 82  ARG A C   1 
ATOM   603  O  O   . ARG A 1 87  ? -22.721 -6.220  18.246  1.00 36.16  ? 82  ARG A O   1 
ATOM   604  C  CB  . ARG A 1 87  ? -22.478 -6.169  21.587  1.00 39.32  ? 82  ARG A CB  1 
ATOM   605  C  CG  . ARG A 1 87  ? -23.307 -7.411  21.271  1.00 41.10  ? 82  ARG A CG  1 
ATOM   606  C  CD  . ARG A 1 87  ? -24.081 -7.924  22.476  1.00 43.26  ? 82  ARG A CD  1 
ATOM   607  N  NE  . ARG A 1 87  ? -24.961 -6.884  23.012  1.00 52.81  ? 82  ARG A NE  1 
ATOM   608  C  CZ  . ARG A 1 87  ? -26.084 -6.453  22.435  1.00 58.54  ? 82  ARG A CZ  1 
ATOM   609  N  NH1 . ARG A 1 87  ? -26.672 -7.137  21.467  1.00 58.89  ? 82  ARG A NH1 1 
ATOM   610  N  NH2 . ARG A 1 87  ? -26.650 -5.329  22.872  1.00 64.65  ? 82  ARG A NH2 1 
ATOM   611  N  N   . GLU A 1 88  ? -23.382 -4.294  19.199  1.00 36.51  ? 83  GLU A N   1 
ATOM   612  C  CA  . GLU A 1 88  ? -24.445 -4.016  18.253  1.00 37.47  ? 83  GLU A CA  1 
ATOM   613  C  C   . GLU A 1 88  ? -23.827 -3.891  16.866  1.00 35.44  ? 83  GLU A C   1 
ATOM   614  O  O   . GLU A 1 88  ? -24.354 -4.425  15.844  1.00 33.24  ? 83  GLU A O   1 
ATOM   615  C  CB  . GLU A 1 88  ? -25.141 -2.694  18.582  1.00 39.22  ? 83  GLU A CB  1 
ATOM   616  C  CG  . GLU A 1 88  ? -26.034 -2.744  19.780  1.00 43.16  ? 83  GLU A CG  1 
ATOM   617  C  CD  . GLU A 1 88  ? -26.736 -1.435  20.067  1.00 47.53  ? 83  GLU A CD  1 
ATOM   618  O  OE1 . GLU A 1 88  ? -26.232 -0.370  19.635  1.00 49.83  ? 83  GLU A OE1 1 
ATOM   619  O  OE2 . GLU A 1 88  ? -27.790 -1.479  20.737  1.00 53.13  ? 83  GLU A OE2 1 
ATOM   620  N  N   . TYR A 1 89  ? -22.696 -3.181  16.832  1.00 36.88  ? 84  TYR A N   1 
ATOM   621  C  CA  . TYR A 1 89  ? -22.049 -2.961  15.517  1.00 36.12  ? 84  TYR A CA  1 
ATOM   622  C  C   . TYR A 1 89  ? -21.402 -4.243  15.001  1.00 35.87  ? 84  TYR A C   1 
ATOM   623  O  O   . TYR A 1 89  ? -21.434 -4.531  13.778  1.00 35.06  ? 84  TYR A O   1 
ATOM   624  C  CB  . TYR A 1 89  ? -21.053 -1.800  15.621  1.00 35.95  ? 84  TYR A CB  1 
ATOM   625  C  CG  . TYR A 1 89  ? -20.529 -1.241  14.325  1.00 33.48  ? 84  TYR A CG  1 
ATOM   626  C  CD1 . TYR A 1 89  ? -21.344 -1.132  13.229  1.00 34.46  ? 84  TYR A CD1 1 
ATOM   627  C  CD2 . TYR A 1 89  ? -19.218 -0.807  14.214  1.00 34.76  ? 84  TYR A CD2 1 
ATOM   628  C  CE1 . TYR A 1 89  ? -20.857 -0.657  12.020  1.00 34.60  ? 84  TYR A CE1 1 
ATOM   629  C  CE2 . TYR A 1 89  ? -18.714 -0.336  13.013  1.00 34.91  ? 84  TYR A CE2 1 
ATOM   630  C  CZ  . TYR A 1 89  ? -19.545 -0.254  11.919  1.00 34.41  ? 84  TYR A CZ  1 
ATOM   631  O  OH  . TYR A 1 89  ? -19.059 0.235   10.742  1.00 37.57  ? 84  TYR A OH  1 
ATOM   632  N  N   . ARG A 1 90  ? -20.820 -5.044  15.895  1.00 34.51  ? 85  ARG A N   1 
ATOM   633  C  CA  . ARG A 1 90  ? -20.297 -6.351  15.545  1.00 34.55  ? 85  ARG A CA  1 
ATOM   634  C  C   . ARG A 1 90  ? -21.404 -7.236  14.967  1.00 33.92  ? 85  ARG A C   1 
ATOM   635  O  O   . ARG A 1 90  ? -21.207 -7.856  13.909  1.00 33.65  ? 85  ARG A O   1 
ATOM   636  C  CB  . ARG A 1 90  ? -19.621 -7.020  16.757  1.00 34.76  ? 85  ARG A CB  1 
ATOM   637  C  CG  . ARG A 1 90  ? -18.945 -8.345  16.442  1.00 35.81  ? 85  ARG A CG  1 
ATOM   638  C  CD  . ARG A 1 90  ? -19.847 -9.556  16.539  1.00 36.38  ? 85  ARG A CD  1 
ATOM   639  N  NE  . ARG A 1 90  ? -20.376 -9.699  17.883  1.00 38.62  ? 85  ARG A NE  1 
ATOM   640  C  CZ  . ARG A 1 90  ? -21.421 -10.441 18.211  1.00 41.07  ? 85  ARG A CZ  1 
ATOM   641  N  NH1 . ARG A 1 90  ? -22.075 -11.158 17.308  1.00 43.99  ? 85  ARG A NH1 1 
ATOM   642  N  NH2 . ARG A 1 90  ? -21.844 -10.435 19.471  1.00 43.29  ? 85  ARG A NH2 1 
ATOM   643  N  N   . GLU A 1 91  ? -22.604 -7.161  15.553  1.00 35.98  ? 86  GLU A N   1 
ATOM   644  C  CA  . GLU A 1 91  ? -23.740 -7.945  15.091  1.00 35.12  ? 86  GLU A CA  1 
ATOM   645  C  C   . GLU A 1 91  ? -24.187 -7.490  13.691  1.00 33.87  ? 86  GLU A C   1 
ATOM   646  O  O   . GLU A 1 91  ? -24.552 -8.332  12.865  1.00 31.54  ? 86  GLU A O   1 
ATOM   647  C  CB  . GLU A 1 91  ? -24.921 -7.901  16.061  1.00 36.57  ? 86  GLU A CB  1 
ATOM   648  C  CG  . GLU A 1 91  ? -24.671 -8.699  17.354  1.00 38.29  ? 86  GLU A CG  1 
ATOM   649  C  CD  . GLU A 1 91  ? -25.773 -8.653  18.405  1.00 44.59  ? 86  GLU A CD  1 
ATOM   650  O  OE1 . GLU A 1 91  ? -26.649 -7.758  18.319  1.00 46.35  ? 86  GLU A OE1 1 
ATOM   651  O  OE2 . GLU A 1 91  ? -25.753 -9.497  19.336  1.00 49.23  ? 86  GLU A OE2 1 
ATOM   652  N  N   . LYS A 1 92  ? -24.211 -6.164  13.463  1.00 32.39  ? 87  LYS A N   1 
ATOM   653  C  CA  . LYS A 1 92  ? -24.577 -5.614  12.159  1.00 30.38  ? 87  LYS A CA  1 
ATOM   654  C  C   . LYS A 1 92  ? -23.625 -6.142  11.103  1.00 28.34  ? 87  LYS A C   1 
ATOM   655  O  O   . LYS A 1 92  ? -24.071 -6.607  10.049  1.00 29.26  ? 87  LYS A O   1 
ATOM   656  C  CB  . LYS A 1 92  ? -24.529 -4.091  12.192  1.00 30.97  ? 87  LYS A CB  1 
ATOM   657  C  CG  . LYS A 1 92  ? -24.802 -3.389  10.848  1.00 33.91  ? 87  LYS A CG  1 
ATOM   658  C  CD  . LYS A 1 92  ? -24.647 -1.889  11.026  1.00 39.43  ? 87  LYS A CD  1 
ATOM   659  C  CE  . LYS A 1 92  ? -24.330 -1.111  9.820   1.00 41.89  ? 87  LYS A CE  1 
ATOM   660  N  NZ  . LYS A 1 92  ? -25.349 -1.312  8.790   1.00 45.94  ? 87  LYS A NZ  1 
ATOM   661  N  N   . VAL A 1 93  ? -22.320 -6.070  11.373  1.00 28.68  ? 88  VAL A N   1 
ATOM   662  C  CA  . VAL A 1 93  ? -21.349 -6.461  10.352  1.00 28.11  ? 88  VAL A CA  1 
ATOM   663  C  C   . VAL A 1 93  ? -21.438 -7.966  10.090  1.00 28.18  ? 88  VAL A C   1 
ATOM   664  O  O   . VAL A 1 93  ? -21.355 -8.447  8.939   1.00 28.29  ? 88  VAL A O   1 
ATOM   665  C  CB  . VAL A 1 93  ? -19.933 -6.020  10.711  1.00 28.66  ? 88  VAL A CB  1 
ATOM   666  C  CG1 . VAL A 1 93  ? -18.872 -6.622  9.771   1.00 27.40  ? 88  VAL A CG1 1 
ATOM   667  C  CG2 . VAL A 1 93  ? -19.845 -4.508  10.749  1.00 29.70  ? 88  VAL A CG2 1 
ATOM   668  N  N   . GLU A 1 94  ? -21.590 -8.744  11.163  1.00 28.76  ? 89  GLU A N   1 
ATOM   669  C  CA  . GLU A 1 94  ? -21.788 -10.180 11.058  1.00 28.67  ? 89  GLU A CA  1 
ATOM   670  C  C   . GLU A 1 94  ? -22.957 -10.597 10.158  1.00 28.33  ? 89  GLU A C   1 
ATOM   671  O  O   . GLU A 1 94  ? -22.825 -11.483 9.285   1.00 26.93  ? 89  GLU A O   1 
ATOM   672  C  CB  . GLU A 1 94  ? -22.017 -10.712 12.521  1.00 30.14  ? 89  GLU A CB  1 
ATOM   673  C  CG  . GLU A 1 94  ? -21.851 -12.190 12.652  1.00 31.30  ? 89  GLU A CG  1 
ATOM   674  C  CD  . GLU A 1 94  ? -21.933 -12.613 14.087  1.00 32.51  ? 89  GLU A CD  1 
ATOM   675  O  OE1 . GLU A 1 94  ? -20.992 -12.278 14.845  1.00 33.49  ? 89  GLU A OE1 1 
ATOM   676  O  OE2 . GLU A 1 94  ? -22.962 -13.230 14.460  1.00 35.41  ? 89  GLU A OE2 1 
ATOM   677  N  N   . THR A 1 95  ? -24.082 -9.902  10.303  1.00 28.82  ? 90  THR A N   1 
ATOM   678  C  CA  . THR A 1 95  ? -25.298 -10.208 9.572   1.00 28.97  ? 90  THR A CA  1 
ATOM   679  C  C   . THR A 1 95  ? -24.990 -9.925  8.100   1.00 27.47  ? 90  THR A C   1 
ATOM   680  O  O   . THR A 1 95  ? -25.365 -10.698 7.207   1.00 27.00  ? 90  THR A O   1 
ATOM   681  C  CB  . THR A 1 95  ? -26.494 -9.415  10.071  1.00 29.86  ? 90  THR A CB  1 
ATOM   682  O  OG1 . THR A 1 95  ? -26.782 -9.866  11.401  1.00 33.84  ? 90  THR A OG1 1 
ATOM   683  C  CG2 . THR A 1 95  ? -27.742 -9.605  9.238   1.00 32.55  ? 90  THR A CG2 1 
ATOM   684  N  N   . GLU A 1 96  ? -24.325 -8.796  7.858   1.00 27.34  ? 91  GLU A N   1 
ATOM   685  C  CA  . GLU A 1 96  ? -23.950 -8.470  6.475   1.00 28.96  ? 91  GLU A CA  1 
ATOM   686  C  C   . GLU A 1 96  ? -23.064 -9.549  5.854   1.00 26.94  ? 91  GLU A C   1 
ATOM   687  O  O   . GLU A 1 96  ? -23.243 -9.948  4.681   1.00 26.86  ? 91  GLU A O   1 
ATOM   688  C  CB  . GLU A 1 96  ? -23.153 -7.190  6.456   1.00 31.20  ? 91  GLU A CB  1 
ATOM   689  C  CG  . GLU A 1 96  ? -23.906 -5.942  6.246   1.00 38.00  ? 91  GLU A CG  1 
ATOM   690  C  CD  . GLU A 1 96  ? -23.004 -4.800  5.776   1.00 41.86  ? 91  GLU A CD  1 
ATOM   691  O  OE1 . GLU A 1 96  ? -22.026 -5.008  4.999   1.00 41.69  ? 91  GLU A OE1 1 
ATOM   692  O  OE2 . GLU A 1 96  ? -23.316 -3.667  6.190   1.00 43.14  ? 91  GLU A OE2 1 
ATOM   693  N  N   . LEU A 1 97  ? -22.039 -9.962  6.619   1.00 26.25  ? 92  LEU A N   1 
ATOM   694  C  CA  . LEU A 1 97  ? -21.105 -10.974 6.148   1.00 25.71  ? 92  LEU A CA  1 
ATOM   695  C  C   . LEU A 1 97  ? -21.809 -12.296 5.838   1.00 25.04  ? 92  LEU A C   1 
ATOM   696  O  O   . LEU A 1 97  ? -21.532 -12.934 4.817   1.00 26.35  ? 92  LEU A O   1 
ATOM   697  C  CB  . LEU A 1 97  ? -19.984 -11.150 7.169   1.00 25.78  ? 92  LEU A CB  1 
ATOM   698  C  CG  . LEU A 1 97  ? -18.906 -12.173 6.914   1.00 26.97  ? 92  LEU A CG  1 
ATOM   699  C  CD1 . LEU A 1 97  ? -17.622 -11.827 7.649   1.00 30.57  ? 92  LEU A CD1 1 
ATOM   700  C  CD2 . LEU A 1 97  ? -19.323 -13.590 7.330   1.00 28.62  ? 92  LEU A CD2 1 
ATOM   701  N  N   . GLN A 1 98  ? -22.729 -12.713 6.721   1.00 26.83  ? 93  GLN A N   1 
ATOM   702  C  CA  . GLN A 1 98  ? -23.462 -13.948 6.529   1.00 25.97  ? 93  GLN A CA  1 
ATOM   703  C  C   . GLN A 1 98  ? -24.285 -13.861 5.220   1.00 25.30  ? 93  GLN A C   1 
ATOM   704  O  O   . GLN A 1 98  ? -24.367 -14.834 4.478   1.00 25.06  ? 93  GLN A O   1 
ATOM   705  C  CB  . GLN A 1 98  ? -24.346 -14.259 7.719   1.00 26.20  ? 93  GLN A CB  1 
ATOM   706  C  CG  . GLN A 1 98  ? -23.525 -14.578 8.962   1.00 27.30  ? 93  GLN A CG  1 
ATOM   707  C  CD  . GLN A 1 98  ? -24.382 -14.661 10.229  1.00 28.53  ? 93  GLN A CD  1 
ATOM   708  O  OE1 . GLN A 1 98  ? -25.251 -13.824 10.469  1.00 30.21  ? 93  GLN A OE1 1 
ATOM   709  N  NE2 . GLN A 1 98  ? -24.155 -15.683 11.052  1.00 29.68  ? 93  GLN A NE2 1 
ATOM   710  N  N   . GLY A 1 99  ? -24.904 -12.701 4.963   1.00 25.14  ? 94  GLY A N   1 
ATOM   711  C  CA  . GLY A 1 99  ? -25.677 -12.476 3.734   1.00 25.25  ? 94  GLY A CA  1 
ATOM   712  C  C   . GLY A 1 99  ? -24.847 -12.637 2.473   1.00 25.39  ? 94  GLY A C   1 
ATOM   713  O  O   . GLY A 1 99  ? -25.280 -13.316 1.510   1.00 26.09  ? 94  GLY A O   1 
ATOM   714  N  N   . VAL A 1 100 ? -23.634 -12.078 2.484   1.00 25.36  ? 95  VAL A N   1 
ATOM   715  C  CA  . VAL A 1 100 ? -22.766 -12.240 1.305   1.00 26.13  ? 95  VAL A CA  1 
ATOM   716  C  C   . VAL A 1 100 ? -22.332 -13.694 1.103   1.00 24.95  ? 95  VAL A C   1 
ATOM   717  O  O   . VAL A 1 100 ? -22.383 -14.249 -0.019  1.00 23.92  ? 95  VAL A O   1 
ATOM   718  C  CB  . VAL A 1 100 ? -21.562 -11.275 1.352   1.00 26.62  ? 95  VAL A CB  1 
ATOM   719  C  CG1 . VAL A 1 100 ? -20.556 -11.533 0.238   1.00 27.06  ? 95  VAL A CG1 1 
ATOM   720  C  CG2 . VAL A 1 100 ? -22.029 -9.824  1.291   1.00 27.31  ? 95  VAL A CG2 1 
ATOM   721  N  N   . CYS A 1 101 ? -21.873 -14.345 2.187   1.00 24.06  ? 96  CYS A N   1 
ATOM   722  C  CA  . CYS A 1 101 ? -21.492 -15.748 2.122   1.00 24.89  ? 96  CYS A CA  1 
ATOM   723  C  C   . CYS A 1 101 ? -22.661 -16.601 1.619   1.00 25.33  ? 96  CYS A C   1 
ATOM   724  O  O   . CYS A 1 101 ? -22.486 -17.449 0.736   1.00 24.21  ? 96  CYS A O   1 
ATOM   725  C  CB  . CYS A 1 101 ? -20.974 -16.240 3.470   1.00 25.83  ? 96  CYS A CB  1 
ATOM   726  S  SG  . CYS A 1 101 ? -19.409 -15.500 4.003   1.00 26.45  ? 96  CYS A SG  1 
ATOM   727  N  N   . ASP A 1 102 ? -23.867 -16.371 2.171   1.00 25.23  ? 97  ASP A N   1 
ATOM   728  C  CA  . ASP A 1 102 ? -25.038 -17.114 1.748   1.00 25.90  ? 97  ASP A CA  1 
ATOM   729  C  C   . ASP A 1 102 ? -25.320 -16.914 0.246   1.00 26.06  ? 97  ASP A C   1 
ATOM   730  O  O   . ASP A 1 102 ? -25.741 -17.856 -0.424  1.00 28.29  ? 97  ASP A O   1 
ATOM   731  C  CB  . ASP A 1 102 ? -26.247 -16.776 2.584   1.00 27.33  ? 97  ASP A CB  1 
ATOM   732  C  CG  . ASP A 1 102 ? -26.182 -17.275 4.016   1.00 28.44  ? 97  ASP A CG  1 
ATOM   733  O  OD1 . ASP A 1 102 ? -25.304 -18.095 4.324   1.00 30.62  ? 97  ASP A OD1 1 
ATOM   734  O  OD2 . ASP A 1 102 ? -27.005 -16.853 4.808   1.00 31.45  ? 97  ASP A OD2 1 
ATOM   735  N  N   . THR A 1 103 ? -25.099 -15.691 -0.260  1.00 25.30  ? 98  THR A N   1 
ATOM   736  C  CA  . THR A 1 103 ? -25.342 -15.379 -1.670  1.00 26.42  ? 98  THR A CA  1 
ATOM   737  C  C   . THR A 1 103 ? -24.390 -16.172 -2.558  1.00 25.94  ? 98  THR A C   1 
ATOM   738  O  O   . THR A 1 103 ? -24.808 -16.807 -3.538  1.00 26.43  ? 98  THR A O   1 
ATOM   739  C  CB  . THR A 1 103 ? -25.194 -13.883 -1.916  1.00 26.74  ? 98  THR A CB  1 
ATOM   740  O  OG1 . THR A 1 103 ? -26.230 -13.146 -1.260  1.00 29.07  ? 98  THR A OG1 1 
ATOM   741  C  CG2 . THR A 1 103 ? -25.282 -13.545 -3.414  1.00 27.69  ? 98  THR A CG2 1 
ATOM   742  N  N   . VAL A 1 104 ? -23.097 -16.147 -2.213  1.00 24.14  ? 99  VAL A N   1 
ATOM   743  C  CA  . VAL A 1 104 ? -22.115 -16.948 -2.942  1.00 24.71  ? 99  VAL A CA  1 
ATOM   744  C  C   . VAL A 1 104 ? -22.430 -18.446 -2.920  1.00 24.23  ? 99  VAL A C   1 
ATOM   745  O  O   . VAL A 1 104 ? -22.378 -19.133 -3.935  1.00 25.16  ? 99  VAL A O   1 
ATOM   746  C  CB  . VAL A 1 104 ? -20.689 -16.665 -2.352  1.00 26.69  ? 99  VAL A CB  1 
ATOM   747  C  CG1 . VAL A 1 104 ? -19.642 -17.587 -2.979  1.00 28.57  ? 99  VAL A CG1 1 
ATOM   748  C  CG2 . VAL A 1 104 ? -20.291 -15.200 -2.527  1.00 27.84  ? 99  VAL A CG2 1 
ATOM   749  N  N   . LEU A 1 105 ? -22.732 -18.994 -1.725  1.00 24.83  ? 100 LEU A N   1 
ATOM   750  C  CA  . LEU A 1 105 ? -23.046 -20.409 -1.608  1.00 25.26  ? 100 LEU A CA  1 
ATOM   751  C  C   . LEU A 1 105 ? -24.293 -20.758 -2.425  1.00 26.84  ? 100 LEU A C   1 
ATOM   752  O  O   . LEU A 1 105 ? -24.356 -21.835 -3.030  1.00 27.40  ? 100 LEU A O   1 
ATOM   753  C  CB  . LEU A 1 105 ? -23.182 -20.771 -0.133  1.00 26.94  ? 100 LEU A CB  1 
ATOM   754  C  CG  . LEU A 1 105 ? -21.864 -20.690 0.625   1.00 27.31  ? 100 LEU A CG  1 
ATOM   755  C  CD1 . LEU A 1 105 ? -22.113 -20.612 2.109   1.00 28.58  ? 100 LEU A CD1 1 
ATOM   756  C  CD2 . LEU A 1 105 ? -20.987 -21.862 0.294   1.00 28.79  ? 100 LEU A CD2 1 
ATOM   757  N  N   . GLY A 1 106 ? -25.235 -19.807 -2.507  1.00 27.51  ? 101 GLY A N   1 
ATOM   758  C  CA  . GLY A 1 106 ? -26.440 -19.964 -3.311  1.00 28.45  ? 101 GLY A CA  1 
ATOM   759  C  C   . GLY A 1 106 ? -26.132 -20.078 -4.801  1.00 28.35  ? 101 GLY A C   1 
ATOM   760  O  O   . GLY A 1 106 ? -26.720 -20.892 -5.523  1.00 29.50  ? 101 GLY A O   1 
ATOM   761  N  N   . LEU A 1 107 ? -25.209 -19.244 -5.261  1.00 27.55  ? 102 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 107 ? -24.761 -19.330 -6.642  1.00 28.25  ? 102 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 107 ? -24.054 -20.649 -6.944  1.00 29.31  ? 102 LEU A C   1 
ATOM   764  O  O   . LEU A 1 107 ? -24.227 -21.228 -8.023  1.00 30.20  ? 102 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 107 ? -23.823 -18.163 -6.958  1.00 29.52  ? 102 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 107 ? -24.453 -16.781 -7.033  1.00 29.92  ? 102 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 107 ? -23.399 -15.733 -7.248  1.00 31.29  ? 102 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 107 ? -25.503 -16.701 -8.148  1.00 30.33  ? 102 LEU A CD2 1 
ATOM   769  N  N   . LEU A 1 108 ? -23.163 -21.063 -6.036  1.00 28.50  ? 103 LEU A N   1 
ATOM   770  C  CA  . LEU A 1 108 ? -22.461 -22.327 -6.186  1.00 28.70  ? 103 LEU A CA  1 
ATOM   771  C  C   . LEU A 1 108 ? -23.405 -23.532 -6.242  1.00 29.33  ? 103 LEU A C   1 
ATOM   772  O  O   . LEU A 1 108 ? -23.256 -24.408 -7.103  1.00 29.63  ? 103 LEU A O   1 
ATOM   773  C  CB  . LEU A 1 108 ? -21.470 -22.468 -5.021  1.00 29.24  ? 103 LEU A CB  1 
ATOM   774  C  CG  . LEU A 1 108 ? -20.286 -21.512 -5.041  1.00 29.22  ? 103 LEU A CG  1 
ATOM   775  C  CD1 . LEU A 1 108 ? -19.598 -21.479 -3.717  1.00 30.76  ? 103 LEU A CD1 1 
ATOM   776  C  CD2 . LEU A 1 108 ? -19.248 -21.905 -6.140  1.00 30.02  ? 103 LEU A CD2 1 
ATOM   777  N  N   . ASP A 1 109 ? -24.404 -23.577 -5.347  1.00 31.26  ? 104 ASP A N   1 
ATOM   778  C  CA  . ASP A 1 109 ? -25.319 -24.711 -5.291  1.00 36.13  ? 104 ASP A CA  1 
ATOM   779  C  C   . ASP A 1 109 ? -26.435 -24.681 -6.341  1.00 38.01  ? 104 ASP A C   1 
ATOM   780  O  O   . ASP A 1 109 ? -26.892 -25.738 -6.758  1.00 44.49  ? 104 ASP A O   1 
ATOM   781  C  CB  . ASP A 1 109 ? -25.907 -24.859 -3.876  1.00 39.02  ? 104 ASP A CB  1 
ATOM   782  C  CG  . ASP A 1 109 ? -24.860 -25.301 -2.880  1.00 43.84  ? 104 ASP A CG  1 
ATOM   783  O  OD1 . ASP A 1 109 ? -24.033 -26.206 -3.229  1.00 44.02  ? 104 ASP A OD1 1 
ATOM   784  O  OD2 . ASP A 1 109 ? -24.844 -24.752 -1.766  1.00 51.62  ? 104 ASP A OD2 1 
ATOM   785  N  N   . SER A 1 110 ? -26.843 -23.483 -6.793  1.00 35.51  ? 105 SER A N   1 
ATOM   786  C  CA  . SER A 1 110 ? -27.936 -23.340 -7.746  1.00 35.40  ? 105 SER A CA  1 
ATOM   787  C  C   . SER A 1 110 ? -27.453 -23.515 -9.182  1.00 34.24  ? 105 SER A C   1 
ATOM   788  O  O   . SER A 1 110 ? -28.210 -23.938 -10.040 1.00 36.97  ? 105 SER A O   1 
ATOM   789  C  CB  . SER A 1 110 ? -28.589 -21.965 -7.651  1.00 36.22  ? 105 SER A CB  1 
ATOM   790  O  OG  . SER A 1 110 ? -29.388 -21.864 -6.482  1.00 43.90  ? 105 SER A OG  1 
ATOM   791  N  N   . HIS A 1 111 ? -26.201 -23.139 -9.426  1.00 34.86  ? 106 HIS A N   1 
ATOM   792  C  CA  . HIS A 1 111 ? -25.666 -23.051 -10.771 1.00 33.37  ? 106 HIS A CA  1 
ATOM   793  C  C   . HIS A 1 111 ? -24.296 -23.698 -10.942 1.00 32.03  ? 106 HIS A C   1 
ATOM   794  O  O   . HIS A 1 111 ? -24.144 -24.634 -11.726 1.00 36.26  ? 106 HIS A O   1 
ATOM   795  C  CB  . HIS A 1 111 ? -25.639 -21.564 -11.223 1.00 34.96  ? 106 HIS A CB  1 
ATOM   796  C  CG  . HIS A 1 111 ? -26.998 -20.968 -11.475 1.00 39.60  ? 106 HIS A CG  1 
ATOM   797  N  ND1 . HIS A 1 111 ? -27.772 -21.341 -12.570 1.00 40.73  ? 106 HIS A ND1 1 
ATOM   798  C  CD2 . HIS A 1 111 ? -27.691 -20.050 -10.762 1.00 40.75  ? 106 HIS A CD2 1 
ATOM   799  C  CE1 . HIS A 1 111 ? -28.894 -20.636 -12.489 1.00 41.95  ? 106 HIS A CE1 1 
ATOM   800  N  NE2 . HIS A 1 111 ? -28.876 -19.836 -11.424 1.00 43.74  ? 106 HIS A NE2 1 
ATOM   801  N  N   . LEU A 1 112 ? -23.287 -23.193 -10.232 1.00 27.91  ? 107 LEU A N   1 
ATOM   802  C  CA  . LEU A 1 112 ? -21.916 -23.365 -10.680 1.00 28.70  ? 107 LEU A CA  1 
ATOM   803  C  C   . LEU A 1 112 ? -21.369 -24.789 -10.564 1.00 30.57  ? 107 LEU A C   1 
ATOM   804  O  O   . LEU A 1 112 ? -20.765 -25.292 -11.509 1.00 33.54  ? 107 LEU A O   1 
ATOM   805  C  CB  . LEU A 1 112 ? -21.027 -22.384 -9.977  1.00 28.35  ? 107 LEU A CB  1 
ATOM   806  C  CG  . LEU A 1 112 ? -21.338 -20.909 -10.252 1.00 29.48  ? 107 LEU A CG  1 
ATOM   807  C  CD1 . LEU A 1 112 ? -20.609 -19.985 -9.256  1.00 28.77  ? 107 LEU A CD1 1 
ATOM   808  C  CD2 . LEU A 1 112 ? -20.976 -20.521 -11.665 1.00 30.62  ? 107 LEU A CD2 1 
ATOM   809  N  N   . ILE A 1 113 ? -21.609 -25.461 -9.439  1.00 30.72  ? 108 ILE A N   1 
ATOM   810  C  CA  . ILE A 1 113 ? -21.027 -26.769 -9.207  1.00 33.01  ? 108 ILE A CA  1 
ATOM   811  C  C   . ILE A 1 113 ? -21.635 -27.785 -10.163 1.00 36.12  ? 108 ILE A C   1 
ATOM   812  O  O   . ILE A 1 113 ? -20.904 -28.444 -10.890 1.00 37.14  ? 108 ILE A O   1 
ATOM   813  C  CB  . ILE A 1 113 ? -21.144 -27.196 -7.738  1.00 34.98  ? 108 ILE A CB  1 
ATOM   814  C  CG1 . ILE A 1 113 ? -20.273 -26.285 -6.851  1.00 34.92  ? 108 ILE A CG1 1 
ATOM   815  C  CG2 . ILE A 1 113 ? -20.767 -28.673 -7.550  1.00 35.57  ? 108 ILE A CG2 1 
ATOM   816  C  CD1 . ILE A 1 113 ? -20.593 -26.367 -5.395  1.00 35.85  ? 108 ILE A CD1 1 
ATOM   817  N  N   . LYS A 1 114 ? -22.965 -27.864 -10.217 1.00 37.10  ? 109 LYS A N   1 
ATOM   818  C  CA  . LYS A 1 114 ? -23.589 -28.876 -11.066 1.00 41.49  ? 109 LYS A CA  1 
ATOM   819  C  C   . LYS A 1 114 ? -23.454 -28.623 -12.565 1.00 40.27  ? 109 LYS A C   1 
ATOM   820  O  O   . LYS A 1 114 ? -23.549 -29.564 -13.345 1.00 42.26  ? 109 LYS A O   1 
ATOM   821  C  CB  . LYS A 1 114 ? -25.077 -29.053 -10.712 1.00 46.27  ? 109 LYS A CB  1 
ATOM   822  C  CG  . LYS A 1 114 ? -25.993 -27.908 -11.116 1.00 49.86  ? 109 LYS A CG  1 
ATOM   823  C  CD  . LYS A 1 114 ? -27.394 -28.113 -10.587 1.00 53.40  ? 109 LYS A CD  1 
ATOM   824  C  CE  . LYS A 1 114 ? -28.394 -27.166 -11.199 1.00 56.79  ? 109 LYS A CE  1 
ATOM   825  N  NZ  . LYS A 1 114 ? -29.728 -27.271 -10.528 1.00 59.85  ? 109 LYS A NZ  1 
ATOM   826  N  N   . GLU A 1 115 ? -23.268 -27.366 -12.979 1.00 39.03  ? 110 GLU A N   1 
ATOM   827  C  CA  . GLU A 1 115 ? -23.156 -27.048 -14.402 1.00 41.06  ? 110 GLU A CA  1 
ATOM   828  C  C   . GLU A 1 115 ? -21.727 -27.091 -14.941 1.00 40.46  ? 110 GLU A C   1 
ATOM   829  O  O   . GLU A 1 115 ? -21.520 -26.981 -16.145 1.00 39.79  ? 110 GLU A O   1 
ATOM   830  C  CB  . GLU A 1 115 ? -23.783 -25.665 -14.686 1.00 43.70  ? 110 GLU A CB  1 
ATOM   831  C  CG  . GLU A 1 115 ? -25.295 -25.623 -14.430 1.00 45.42  ? 110 GLU A CG  1 
ATOM   832  C  CD  . GLU A 1 115 ? -25.968 -24.254 -14.414 1.00 47.37  ? 110 GLU A CD  1 
ATOM   833  O  OE1 . GLU A 1 115 ? -25.273 -23.226 -14.584 1.00 51.26  ? 110 GLU A OE1 1 
ATOM   834  O  OE2 . GLU A 1 115 ? -27.204 -24.210 -14.206 1.00 51.42  ? 110 GLU A OE2 1 
ATOM   835  N  N   . ALA A 1 116 ? -20.731 -27.260 -14.061 1.00 40.92  ? 111 ALA A N   1 
ATOM   836  C  CA  . ALA A 1 116 ? -19.337 -27.247 -14.493 1.00 40.17  ? 111 ALA A CA  1 
ATOM   837  C  C   . ALA A 1 116 ? -19.021 -28.460 -15.363 1.00 40.92  ? 111 ALA A C   1 
ATOM   838  O  O   . ALA A 1 116 ? -19.366 -29.580 -15.005 1.00 41.88  ? 111 ALA A O   1 
ATOM   839  C  CB  . ALA A 1 116 ? -18.425 -27.227 -13.279 1.00 40.18  ? 111 ALA A CB  1 
ATOM   840  N  N   . GLY A 1 117 ? -18.352 -28.223 -16.502 1.00 42.71  ? 112 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 117 ? -18.126 -29.239 -17.520 1.00 43.73  ? 112 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 117 ? -16.781 -29.960 -17.461 1.00 42.82  ? 112 GLY A C   1 
ATOM   843  O  O   . GLY A 1 117 ? -16.539 -30.859 -18.261 1.00 43.60  ? 112 GLY A O   1 
ATOM   844  N  N   . ASP A 1 118 ? -15.921 -29.569 -16.512 1.00 41.01  ? 113 ASP A N   1 
ATOM   845  C  CA  . ASP A 1 118 ? -14.580 -30.127 -16.392 1.00 40.81  ? 113 ASP A CA  1 
ATOM   846  C  C   . ASP A 1 118 ? -14.091 -30.167 -14.944 1.00 41.00  ? 113 ASP A C   1 
ATOM   847  O  O   . ASP A 1 118 ? -14.643 -29.500 -14.069 1.00 40.44  ? 113 ASP A O   1 
ATOM   848  C  CB  . ASP A 1 118 ? -13.574 -29.309 -17.220 1.00 41.96  ? 113 ASP A CB  1 
ATOM   849  C  CG  . ASP A 1 118 ? -13.516 -27.857 -16.810 1.00 44.75  ? 113 ASP A CG  1 
ATOM   850  O  OD1 . ASP A 1 118 ? -14.410 -27.096 -17.201 1.00 51.37  ? 113 ASP A OD1 1 
ATOM   851  O  OD2 . ASP A 1 118 ? -12.619 -27.497 -16.066 1.00 44.94  ? 113 ASP A OD2 1 
ATOM   852  N  N   . ALA A 1 119 ? -13.001 -30.916 -14.742 1.00 40.50  ? 114 ALA A N   1 
ATOM   853  C  CA  . ALA A 1 119 ? -12.438 -31.167 -13.425 1.00 41.34  ? 114 ALA A CA  1 
ATOM   854  C  C   . ALA A 1 119 ? -11.909 -29.914 -12.722 1.00 41.25  ? 114 ALA A C   1 
ATOM   855  O  O   . ALA A 1 119 ? -12.167 -29.703 -11.524 1.00 40.90  ? 114 ALA A O   1 
ATOM   856  C  CB  . ALA A 1 119 ? -11.333 -32.195 -13.553 1.00 42.26  ? 114 ALA A CB  1 
ATOM   857  N  N   . GLU A 1 120 ? -11.187 -29.078 -13.480 1.00 41.18  ? 115 GLU A N   1 
ATOM   858  C  CA  . GLU A 1 120 ? -10.639 -27.841 -12.942 1.00 40.73  ? 115 GLU A CA  1 
ATOM   859  C  C   . GLU A 1 120 ? -11.724 -26.925 -12.384 1.00 37.57  ? 115 GLU A C   1 
ATOM   860  O  O   . GLU A 1 120 ? -11.604 -26.416 -11.264 1.00 35.41  ? 115 GLU A O   1 
ATOM   861  C  CB  . GLU A 1 120 ? -9.875  -27.073 -14.011 1.00 41.93  ? 115 GLU A CB  1 
ATOM   862  C  CG  . GLU A 1 120 ? -9.526  -25.673 -13.539 1.00 44.31  ? 115 GLU A CG  1 
ATOM   863  C  CD  . GLU A 1 120 ? -8.452  -25.004 -14.356 1.00 46.94  ? 115 GLU A CD  1 
ATOM   864  O  OE1 . GLU A 1 120 ? -7.457  -25.692 -14.677 1.00 50.56  ? 115 GLU A OE1 1 
ATOM   865  O  OE2 . GLU A 1 120 ? -8.584  -23.790 -14.640 1.00 47.03  ? 115 GLU A OE2 1 
ATOM   866  N  N   . SER A 1 121 ? -12.759 -26.694 -13.201 1.00 34.72  ? 116 SER A N   1 
ATOM   867  C  CA  . SER A 1 121 ? -13.914 -25.927 -12.765 1.00 35.13  ? 116 SER A CA  1 
ATOM   868  C  C   . SER A 1 121 ? -14.504 -26.495 -11.476 1.00 33.03  ? 116 SER A C   1 
ATOM   869  O  O   . SER A 1 121 ? -14.821 -25.737 -10.570 1.00 31.13  ? 116 SER A O   1 
ATOM   870  C  CB  . SER A 1 121 ? -14.980 -25.888 -13.854 1.00 37.27  ? 116 SER A CB  1 
ATOM   871  O  OG  . SER A 1 121 ? -14.500 -25.183 -14.990 1.00 39.04  ? 116 SER A OG  1 
ATOM   872  N  N   . ARG A 1 122 ? -14.660 -27.820 -11.401 1.00 33.37  ? 117 ARG A N   1 
ATOM   873  C  CA  . ARG A 1 122 ? -15.301 -28.437 -10.245 1.00 34.55  ? 117 ARG A CA  1 
ATOM   874  C  C   . ARG A 1 122 ? -14.504 -28.217 -8.960  1.00 30.42  ? 117 ARG A C   1 
ATOM   875  O  O   . ARG A 1 122 ? -15.065 -27.855 -7.921  1.00 29.89  ? 117 ARG A O   1 
ATOM   876  C  CB  . ARG A 1 122 ? -15.514 -29.931 -10.482 1.00 38.15  ? 117 ARG A CB  1 
ATOM   877  C  CG  . ARG A 1 122 ? -16.707 -30.174 -11.350 1.00 42.23  ? 117 ARG A CG  1 
ATOM   878  C  CD  . ARG A 1 122 ? -17.075 -31.638 -11.501 1.00 47.80  ? 117 ARG A CD  1 
ATOM   879  N  NE  . ARG A 1 122 ? -18.391 -31.754 -12.125 1.00 54.93  ? 117 ARG A NE  1 
ATOM   880  C  CZ  . ARG A 1 122 ? -19.514 -31.237 -11.627 1.00 58.01  ? 117 ARG A CZ  1 
ATOM   881  N  NH1 . ARG A 1 122 ? -19.767 -31.244 -10.323 1.00 58.93  ? 117 ARG A NH1 1 
ATOM   882  N  NH2 . ARG A 1 122 ? -20.415 -30.721 -12.459 1.00 59.90  ? 117 ARG A NH2 1 
ATOM   883  N  N   . VAL A 1 123 ? -13.188 -28.401 -9.053  1.00 30.25  ? 118 VAL A N   1 
ATOM   884  C  CA  . VAL A 1 123 ? -12.302 -28.160 -7.934  1.00 29.79  ? 118 VAL A CA  1 
ATOM   885  C  C   . VAL A 1 123 ? -12.354 -26.693 -7.502  1.00 28.91  ? 118 VAL A C   1 
ATOM   886  O  O   . VAL A 1 123 ? -12.481 -26.384 -6.310  1.00 28.52  ? 118 VAL A O   1 
ATOM   887  C  CB  . VAL A 1 123 ? -10.878 -28.599 -8.267  1.00 31.66  ? 118 VAL A CB  1 
ATOM   888  C  CG1 . VAL A 1 123 ? -9.911  -28.134 -7.172  1.00 31.46  ? 118 VAL A CG1 1 
ATOM   889  C  CG2 . VAL A 1 123 ? -10.787 -30.108 -8.479  1.00 33.10  ? 118 VAL A CG2 1 
ATOM   890  N  N   . PHE A 1 124 ? -12.282 -25.778 -8.476  1.00 28.36  ? 119 PHE A N   1 
ATOM   891  C  CA  . PHE A 1 124 ? -12.377 -24.351 -8.202  1.00 28.11  ? 119 PHE A CA  1 
ATOM   892  C  C   . PHE A 1 124 ? -13.608 -23.983 -7.377  1.00 26.86  ? 119 PHE A C   1 
ATOM   893  O  O   . PHE A 1 124 ? -13.507 -23.278 -6.351  1.00 26.81  ? 119 PHE A O   1 
ATOM   894  C  CB  . PHE A 1 124 ? -12.349 -23.562 -9.537  1.00 27.93  ? 119 PHE A CB  1 
ATOM   895  C  CG  . PHE A 1 124 ? -12.284 -22.061 -9.354  1.00 28.76  ? 119 PHE A CG  1 
ATOM   896  C  CD1 . PHE A 1 124 ? -13.434 -21.317 -9.135  1.00 27.73  ? 119 PHE A CD1 1 
ATOM   897  C  CD2 . PHE A 1 124 ? -11.069 -21.396 -9.379  1.00 28.48  ? 119 PHE A CD2 1 
ATOM   898  C  CE1 . PHE A 1 124 ? -13.365 -19.924 -8.968  1.00 28.53  ? 119 PHE A CE1 1 
ATOM   899  C  CE2 . PHE A 1 124 ? -11.005 -20.013 -9.220  1.00 29.86  ? 119 PHE A CE2 1 
ATOM   900  C  CZ  . PHE A 1 124 ? -12.151 -19.285 -9.001  1.00 28.79  ? 119 PHE A CZ  1 
ATOM   901  N  N   . TYR A 1 125 ? -14.764 -24.489 -7.803  1.00 26.95  ? 120 TYR A N   1 
ATOM   902  C  CA  . TYR A 1 125 ? -16.029 -24.167 -7.166  1.00 26.68  ? 120 TYR A CA  1 
ATOM   903  C  C   . TYR A 1 125 ? -16.236 -24.868 -5.829  1.00 27.44  ? 120 TYR A C   1 
ATOM   904  O  O   . TYR A 1 125 ? -16.790 -24.253 -4.914  1.00 27.97  ? 120 TYR A O   1 
ATOM   905  C  CB  . TYR A 1 125 ? -17.200 -24.488 -8.090  1.00 26.66  ? 120 TYR A CB  1 
ATOM   906  C  CG  . TYR A 1 125 ? -17.243 -23.651 -9.334  1.00 26.56  ? 120 TYR A CG  1 
ATOM   907  C  CD1 . TYR A 1 125 ? -17.130 -22.268 -9.274  1.00 27.16  ? 120 TYR A CD1 1 
ATOM   908  C  CD2 . TYR A 1 125 ? -17.484 -24.230 -10.576 1.00 27.47  ? 120 TYR A CD2 1 
ATOM   909  C  CE1 . TYR A 1 125 ? -17.167 -21.489 -10.431 1.00 28.03  ? 120 TYR A CE1 1 
ATOM   910  C  CE2 . TYR A 1 125 ? -17.517 -23.466 -11.724 1.00 26.86  ? 120 TYR A CE2 1 
ATOM   911  C  CZ  . TYR A 1 125 ? -17.376 -22.098 -11.653 1.00 26.83  ? 120 TYR A CZ  1 
ATOM   912  O  OH  . TYR A 1 125 ? -17.448 -21.342 -12.822 1.00 29.32  ? 120 TYR A OH  1 
ATOM   913  N  N   . LEU A 1 126 ? -15.791 -26.125 -5.708  1.00 27.81  ? 121 LEU A N   1 
ATOM   914  C  CA  . LEU A 1 126 ? -15.860 -26.818 -4.420  1.00 28.90  ? 121 LEU A CA  1 
ATOM   915  C  C   . LEU A 1 126 ? -14.949 -26.184 -3.362  1.00 27.47  ? 121 LEU A C   1 
ATOM   916  O  O   . LEU A 1 126 ? -15.312 -26.053 -2.175  1.00 27.66  ? 121 LEU A O   1 
ATOM   917  C  CB  . LEU A 1 126 ? -15.571 -28.319 -4.599  1.00 30.59  ? 121 LEU A CB  1 
ATOM   918  C  CG  . LEU A 1 126 ? -16.686 -29.123 -5.295  1.00 32.48  ? 121 LEU A CG  1 
ATOM   919  C  CD1 . LEU A 1 126 ? -16.216 -30.533 -5.681  1.00 35.02  ? 121 LEU A CD1 1 
ATOM   920  C  CD2 . LEU A 1 126 ? -17.916 -29.225 -4.437  1.00 33.99  ? 121 LEU A CD2 1 
ATOM   921  N  N   . LYS A 1 127 ? -13.752 -25.784 -3.768  1.00 26.61  ? 122 LYS A N   1 
ATOM   922  C  CA  . LYS A 1 127 ? -12.883 -24.996 -2.899  1.00 26.70  ? 122 LYS A CA  1 
ATOM   923  C  C   . LYS A 1 127 ? -13.550 -23.701 -2.426  1.00 26.46  ? 122 LYS A C   1 
ATOM   924  O  O   . LYS A 1 127 ? -13.509 -23.343 -1.233  1.00 25.67  ? 122 LYS A O   1 
ATOM   925  C  CB  . LYS A 1 127 ? -11.582 -24.668 -3.658  1.00 27.63  ? 122 LYS A CB  1 
ATOM   926  C  CG  . LYS A 1 127 ? -10.633 -23.772 -2.853  1.00 27.46  ? 122 LYS A CG  1 
ATOM   927  C  CD  . LYS A 1 127 ? -9.406  -23.392 -3.643  1.00 28.14  ? 122 LYS A CD  1 
ATOM   928  C  CE  . LYS A 1 127 ? -8.747  -22.154 -3.142  1.00 29.60  ? 122 LYS A CE  1 
ATOM   929  N  NZ  . LYS A 1 127 ? -9.683  -20.993 -3.112  1.00 30.17  ? 122 LYS A NZ  1 
ATOM   930  N  N   . MET A 1 128 ? -14.167 -22.975 -3.365  1.00 25.42  ? 123 MET A N   1 
ATOM   931  C  CA  . MET A 1 128 ? -14.916 -21.776 -3.024  1.00 26.57  ? 123 MET A CA  1 
ATOM   932  C  C   . MET A 1 128 ? -15.997 -22.108 -2.004  1.00 25.97  ? 123 MET A C   1 
ATOM   933  O  O   . MET A 1 128 ? -16.226 -21.328 -1.084  1.00 24.63  ? 123 MET A O   1 
ATOM   934  C  CB  . MET A 1 128 ? -15.628 -21.157 -4.215  1.00 28.71  ? 123 MET A CB  1 
ATOM   935  C  CG  . MET A 1 128 ? -14.988 -19.957 -4.726  1.00 32.94  ? 123 MET A CG  1 
ATOM   936  S  SD  . MET A 1 128 ? -15.890 -19.282 -6.126  1.00 35.44  ? 123 MET A SD  1 
ATOM   937  C  CE  . MET A 1 128 ? -16.580 -17.904 -5.422  1.00 30.77  ? 123 MET A CE  1 
ATOM   938  N  N   . LYS A 1 129 ? -16.681 -23.236 -2.225  1.00 26.02  ? 124 LYS A N   1 
ATOM   939  C  CA  . LYS A 1 129 ? -17.753 -23.644 -1.334  1.00 26.24  ? 124 LYS A CA  1 
ATOM   940  C  C   . LYS A 1 129 ? -17.150 -23.816 0.057   1.00 26.12  ? 124 LYS A C   1 
ATOM   941  O  O   . LYS A 1 129 ? -17.721 -23.313 1.029   1.00 26.15  ? 124 LYS A O   1 
ATOM   942  C  CB  . LYS A 1 129 ? -18.416 -24.936 -1.795  1.00 28.25  ? 124 LYS A CB  1 
ATOM   943  C  CG  . LYS A 1 129 ? -19.609 -25.335 -0.970  1.00 30.62  ? 124 LYS A CG  1 
ATOM   944  C  CD  . LYS A 1 129 ? -20.369 -26.498 -1.566  1.00 33.03  ? 124 LYS A CD  1 
ATOM   945  C  CE  . LYS A 1 129 ? -21.645 -26.765 -0.835  1.00 35.89  ? 124 LYS A CE  1 
ATOM   946  N  NZ  . LYS A 1 129 ? -22.502 -27.746 -1.547  1.00 38.68  ? 124 LYS A NZ  1 
ATOM   947  N  N   . GLY A 1 130 ? -16.006 -24.505 0.148   1.00 24.13  ? 125 GLY A N   1 
ATOM   948  C  CA  . GLY A 1 130 ? -15.358 -24.703 1.448   1.00 25.46  ? 125 GLY A CA  1 
ATOM   949  C  C   . GLY A 1 130 ? -14.930 -23.384 2.097   1.00 25.37  ? 125 GLY A C   1 
ATOM   950  O  O   . GLY A 1 130 ? -15.103 -23.167 3.312   1.00 25.02  ? 125 GLY A O   1 
ATOM   951  N  N   . ASP A 1 131 ? -14.361 -22.488 1.283   1.00 23.87  ? 126 ASP A N   1 
ATOM   952  C  CA  . ASP A 1 131 ? -13.965 -21.169 1.759   1.00 25.36  ? 126 ASP A CA  1 
ATOM   953  C  C   . ASP A 1 131 ? -15.099 -20.328 2.359   1.00 24.38  ? 126 ASP A C   1 
ATOM   954  O  O   . ASP A 1 131 ? -14.946 -19.744 3.439   1.00 24.55  ? 126 ASP A O   1 
ATOM   955  C  CB  . ASP A 1 131 ? -13.299 -20.393 0.645   1.00 25.66  ? 126 ASP A CB  1 
ATOM   956  C  CG  . ASP A 1 131 ? -11.965 -20.917 0.174   1.00 26.15  ? 126 ASP A CG  1 
ATOM   957  O  OD1 . ASP A 1 131 ? -11.307 -21.699 0.937   1.00 25.31  ? 126 ASP A OD1 1 
ATOM   958  O  OD2 . ASP A 1 131 ? -11.561 -20.563 -0.977  1.00 26.82  ? 126 ASP A OD2 1 
ATOM   959  N  N   . TYR A 1 132 ? -16.246 -20.274 1.681   1.00 24.01  ? 127 TYR A N   1 
ATOM   960  C  CA  . TYR A 1 132 ? -17.332 -19.422 2.139   1.00 23.53  ? 127 TYR A CA  1 
ATOM   961  C  C   . TYR A 1 132 ? -18.002 -20.053 3.363   1.00 23.91  ? 127 TYR A C   1 
ATOM   962  O  O   . TYR A 1 132 ? -18.396 -19.313 4.276   1.00 25.66  ? 127 TYR A O   1 
ATOM   963  C  CB  . TYR A 1 132 ? -18.250 -19.038 0.963   1.00 24.73  ? 127 TYR A CB  1 
ATOM   964  C  CG  . TYR A 1 132 ? -17.583 -17.919 0.197   1.00 23.88  ? 127 TYR A CG  1 
ATOM   965  C  CD1 . TYR A 1 132 ? -16.693 -18.186 -0.843  1.00 24.19  ? 127 TYR A CD1 1 
ATOM   966  C  CD2 . TYR A 1 132 ? -17.807 -16.598 0.526   1.00 25.08  ? 127 TYR A CD2 1 
ATOM   967  C  CE1 . TYR A 1 132 ? -16.020 -17.165 -1.488  1.00 24.80  ? 127 TYR A CE1 1 
ATOM   968  C  CE2 . TYR A 1 132 ? -17.149 -15.564 -0.122  1.00 24.81  ? 127 TYR A CE2 1 
ATOM   969  C  CZ  . TYR A 1 132 ? -16.266 -15.846 -1.147  1.00 24.38  ? 127 TYR A CZ  1 
ATOM   970  O  OH  . TYR A 1 132 ? -15.627 -14.771 -1.746  1.00 24.67  ? 127 TYR A OH  1 
ATOM   971  N  N   . TYR A 1 133 ? -18.047 -21.387 3.443   1.00 23.33  ? 128 TYR A N   1 
ATOM   972  C  CA  . TYR A 1 133 ? -18.461 -22.011 4.700   1.00 24.01  ? 128 TYR A CA  1 
ATOM   973  C  C   . TYR A 1 133 ? -17.476 -21.684 5.827   1.00 24.62  ? 128 TYR A C   1 
ATOM   974  O  O   . TYR A 1 133 ? -17.883 -21.415 6.962   1.00 25.94  ? 128 TYR A O   1 
ATOM   975  C  CB  . TYR A 1 133 ? -18.674 -23.524 4.554   1.00 24.87  ? 128 TYR A CB  1 
ATOM   976  C  CG  . TYR A 1 133 ? -20.044 -23.894 4.013   1.00 26.23  ? 128 TYR A CG  1 
ATOM   977  C  CD1 . TYR A 1 133 ? -21.205 -23.460 4.641   1.00 28.67  ? 128 TYR A CD1 1 
ATOM   978  C  CD2 . TYR A 1 133 ? -20.180 -24.724 2.911   1.00 28.62  ? 128 TYR A CD2 1 
ATOM   979  C  CE1 . TYR A 1 133 ? -22.467 -23.801 4.152   1.00 30.87  ? 128 TYR A CE1 1 
ATOM   980  C  CE2 . TYR A 1 133 ? -21.436 -25.089 2.435   1.00 30.44  ? 128 TYR A CE2 1 
ATOM   981  C  CZ  . TYR A 1 133 ? -22.574 -24.636 3.069   1.00 31.34  ? 128 TYR A CZ  1 
ATOM   982  O  OH  . TYR A 1 133 ? -23.811 -24.983 2.592   1.00 35.12  ? 128 TYR A OH  1 
ATOM   983  N  N   . ARG A 1 134 ? -16.185 -21.668 5.514   1.00 24.82  ? 129 ARG A N   1 
ATOM   984  C  CA  . ARG A 1 134 ? -15.167 -21.340 6.490   1.00 25.41  ? 129 ARG A CA  1 
ATOM   985  C  C   . ARG A 1 134 ? -15.335 -19.917 7.024   1.00 25.10  ? 129 ARG A C   1 
ATOM   986  O  O   . ARG A 1 134 ? -15.234 -19.676 8.229   1.00 24.75  ? 129 ARG A O   1 
ATOM   987  C  CB  . ARG A 1 134 ? -13.780 -21.602 5.925   1.00 24.52  ? 129 ARG A CB  1 
ATOM   988  C  CG  . ARG A 1 134 ? -12.615 -21.104 6.816   1.00 25.26  ? 129 ARG A CG  1 
ATOM   989  C  CD  . ARG A 1 134 ? -11.283 -21.757 6.464   1.00 25.54  ? 129 ARG A CD  1 
ATOM   990  N  NE  . ARG A 1 134 ? -10.854 -21.510 5.085   1.00 26.25  ? 129 ARG A NE  1 
ATOM   991  C  CZ  . ARG A 1 134 ? -10.282 -20.388 4.659   1.00 26.94  ? 129 ARG A CZ  1 
ATOM   992  N  NH1 . ARG A 1 134 ? -9.902  -19.444 5.507   1.00 26.04  ? 129 ARG A NH1 1 
ATOM   993  N  NH2 . ARG A 1 134 ? -10.054 -20.217 3.347   1.00 27.47  ? 129 ARG A NH2 1 
ATOM   994  N  N   . TYR A 1 135 ? -15.608 -18.971 6.147   1.00 23.64  ? 130 TYR A N   1 
ATOM   995  C  CA  . TYR A 1 135 ? -15.857 -17.599 6.571   1.00 23.70  ? 130 TYR A CA  1 
ATOM   996  C  C   . TYR A 1 135 ? -17.109 -17.524 7.451   1.00 24.14  ? 130 TYR A C   1 
ATOM   997  O  O   . TYR A 1 135 ? -17.137 -16.788 8.439   1.00 26.57  ? 130 TYR A O   1 
ATOM   998  C  CB  . TYR A 1 135 ? -15.992 -16.665 5.369   1.00 23.79  ? 130 TYR A CB  1 
ATOM   999  C  CG  . TYR A 1 135 ? -14.833 -16.711 4.397   1.00 23.95  ? 130 TYR A CG  1 
ATOM   1000 C  CD1 . TYR A 1 135 ? -13.573 -17.141 4.788   1.00 24.76  ? 130 TYR A CD1 1 
ATOM   1001 C  CD2 . TYR A 1 135 ? -15.026 -16.433 3.055   1.00 24.27  ? 130 TYR A CD2 1 
ATOM   1002 C  CE1 . TYR A 1 135 ? -12.528 -17.261 3.869   1.00 26.73  ? 130 TYR A CE1 1 
ATOM   1003 C  CE2 . TYR A 1 135 ? -13.992 -16.502 2.151   1.00 25.20  ? 130 TYR A CE2 1 
ATOM   1004 C  CZ  . TYR A 1 135 ? -12.749 -16.940 2.543   1.00 25.58  ? 130 TYR A CZ  1 
ATOM   1005 O  OH  . TYR A 1 135 ? -11.729 -17.019 1.612   1.00 27.78  ? 130 TYR A OH  1 
ATOM   1006 N  N   . LEU A 1 136 ? -18.143 -18.308 7.132   1.00 23.96  ? 131 LEU A N   1 
ATOM   1007 C  CA  . LEU A 1 136 ? -19.320 -18.377 7.998   1.00 24.80  ? 131 LEU A CA  1 
ATOM   1008 C  C   . LEU A 1 136 ? -18.949 -18.952 9.369   1.00 25.76  ? 131 LEU A C   1 
ATOM   1009 O  O   . LEU A 1 136 ? -19.460 -18.502 10.407  1.00 26.53  ? 131 LEU A O   1 
ATOM   1010 C  CB  . LEU A 1 136 ? -20.437 -19.221 7.388   1.00 25.21  ? 131 LEU A CB  1 
ATOM   1011 C  CG  . LEU A 1 136 ? -21.200 -18.544 6.242   1.00 25.81  ? 131 LEU A CG  1 
ATOM   1012 C  CD1 . LEU A 1 136 ? -22.090 -19.517 5.505   1.00 26.85  ? 131 LEU A CD1 1 
ATOM   1013 C  CD2 . LEU A 1 136 ? -22.029 -17.378 6.758   1.00 26.00  ? 131 LEU A CD2 1 
ATOM   1014 N  N   . ALA A 1 137 ? -18.103 -19.985 9.354   1.00 26.70  ? 132 ALA A N   1 
ATOM   1015 C  CA  . ALA A 1 137 ? -17.731 -20.671 10.583  1.00 27.57  ? 132 ALA A CA  1 
ATOM   1016 C  C   . ALA A 1 137 ? -16.975 -19.737 11.517  1.00 28.12  ? 132 ALA A C   1 
ATOM   1017 O  O   . ALA A 1 137 ? -17.127 -19.854 12.741  1.00 30.23  ? 132 ALA A O   1 
ATOM   1018 C  CB  . ALA A 1 137 ? -16.913 -21.897 10.287  1.00 27.93  ? 132 ALA A CB  1 
ATOM   1019 N  N   . GLU A 1 138 ? -16.177 -18.818 10.970  1.00 27.89  ? 133 GLU A N   1 
ATOM   1020 C  CA  . GLU A 1 138 ? -15.446 -17.836 11.769  1.00 28.44  ? 133 GLU A CA  1 
ATOM   1021 C  C   . GLU A 1 138 ? -16.338 -17.004 12.699  1.00 27.53  ? 133 GLU A C   1 
ATOM   1022 O  O   . GLU A 1 138 ? -15.920 -16.687 13.810  1.00 30.89  ? 133 GLU A O   1 
ATOM   1023 C  CB  . GLU A 1 138 ? -14.619 -16.897 10.869  1.00 30.56  ? 133 GLU A CB  1 
ATOM   1024 C  CG  . GLU A 1 138 ? -13.421 -17.559 10.205  1.00 31.79  ? 133 GLU A CG  1 
ATOM   1025 C  CD  . GLU A 1 138 ? -12.770 -16.751 9.091   1.00 33.93  ? 133 GLU A CD  1 
ATOM   1026 O  OE1 . GLU A 1 138 ? -13.246 -15.636 8.771   1.00 35.68  ? 133 GLU A OE1 1 
ATOM   1027 O  OE2 . GLU A 1 138 ? -11.763 -17.244 8.539   1.00 37.49  ? 133 GLU A OE2 1 
ATOM   1028 N  N   . VAL A 1 139 ? -17.581 -16.728 12.300  1.00 26.87  ? 134 VAL A N   1 
ATOM   1029 C  CA  . VAL A 1 139 ? -18.510 -15.905 13.070  1.00 28.31  ? 134 VAL A CA  1 
ATOM   1030 C  C   . VAL A 1 139 ? -19.638 -16.693 13.735  1.00 28.71  ? 134 VAL A C   1 
ATOM   1031 O  O   . VAL A 1 139 ? -20.392 -16.124 14.521  1.00 31.37  ? 134 VAL A O   1 
ATOM   1032 C  CB  . VAL A 1 139 ? -19.091 -14.751 12.187  1.00 27.48  ? 134 VAL A CB  1 
ATOM   1033 C  CG1 . VAL A 1 139 ? -17.971 -13.972 11.507  1.00 28.91  ? 134 VAL A CG1 1 
ATOM   1034 C  CG2 . VAL A 1 139 ? -20.099 -15.270 11.164  1.00 27.09  ? 134 VAL A CG2 1 
ATOM   1035 N  N   . ALA A 1 140 ? -19.731 -17.999 13.462  1.00 27.16  ? 135 ALA A N   1 
ATOM   1036 C  CA  . ALA A 1 140 ? -20.836 -18.808 13.943  1.00 28.14  ? 135 ALA A CA  1 
ATOM   1037 C  C   . ALA A 1 140 ? -20.711 -19.212 15.408  1.00 29.29  ? 135 ALA A C   1 
ATOM   1038 O  O   . ALA A 1 140 ? -19.609 -19.323 15.947  1.00 29.88  ? 135 ALA A O   1 
ATOM   1039 C  CB  . ALA A 1 140 ? -20.962 -20.093 13.162  1.00 28.46  ? 135 ALA A CB  1 
ATOM   1040 N  N   . THR A 1 141 ? -21.875 -19.519 15.966  1.00 30.01  ? 136 THR A N   1 
ATOM   1041 C  CA  . THR A 1 141 ? -21.967 -20.149 17.274  1.00 31.52  ? 136 THR A CA  1 
ATOM   1042 C  C   . THR A 1 141 ? -23.000 -21.271 17.263  1.00 32.04  ? 136 THR A C   1 
ATOM   1043 O  O   . THR A 1 141 ? -23.833 -21.347 16.367  1.00 33.85  ? 136 THR A O   1 
ATOM   1044 C  CB  . THR A 1 141 ? -22.316 -19.125 18.358  1.00 32.60  ? 136 THR A CB  1 
ATOM   1045 O  OG1 . THR A 1 141 ? -23.609 -18.608 18.102  1.00 32.52  ? 136 THR A OG1 1 
ATOM   1046 C  CG2 . THR A 1 141 ? -21.344 -17.985 18.403  1.00 32.60  ? 136 THR A CG2 1 
ATOM   1047 N  N   . GLY A 1 142 ? -22.992 -22.088 18.329  1.00 33.07  ? 137 GLY A N   1 
ATOM   1048 C  CA  . GLY A 1 142 ? -24.005 -23.108 18.536  1.00 32.66  ? 137 GLY A CA  1 
ATOM   1049 C  C   . GLY A 1 142 ? -24.165 -24.101 17.383  1.00 31.06  ? 137 GLY A C   1 
ATOM   1050 O  O   . GLY A 1 142 ? -23.183 -24.556 16.808  1.00 31.43  ? 137 GLY A O   1 
ATOM   1051 N  N   . ASP A 1 143 ? -25.423 -24.445 17.093  1.00 31.31  ? 138 ASP A N   1 
ATOM   1052 C  CA  . ASP A 1 143 ? -25.755 -25.521 16.180  1.00 30.60  ? 138 ASP A CA  1 
ATOM   1053 C  C   . ASP A 1 143 ? -25.343 -25.093 14.771  1.00 29.44  ? 138 ASP A C   1 
ATOM   1054 O  O   . ASP A 1 143 ? -24.877 -25.926 14.000  1.00 29.67  ? 138 ASP A O   1 
ATOM   1055 C  CB  . ASP A 1 143 ? -27.237 -25.879 16.261  1.00 31.48  ? 138 ASP A CB  1 
ATOM   1056 C  CG  . ASP A 1 143 ? -27.690 -26.607 17.521  1.00 33.21  ? 138 ASP A CG  1 
ATOM   1057 O  OD1 . ASP A 1 143 ? -26.836 -26.981 18.321  1.00 37.02  ? 138 ASP A OD1 1 
ATOM   1058 O  OD2 . ASP A 1 143 ? -28.906 -26.821 17.676  1.00 36.84  ? 138 ASP A OD2 1 
ATOM   1059 N  N   . ASP A 1 144 ? -25.484 -23.787 14.480  1.00 29.19  ? 139 ASP A N   1 
ATOM   1060 C  CA  . ASP A 1 144 ? -25.114 -23.208 13.191  1.00 27.13  ? 139 ASP A CA  1 
ATOM   1061 C  C   . ASP A 1 144 ? -23.650 -23.517 12.896  1.00 27.93  ? 139 ASP A C   1 
ATOM   1062 O  O   . ASP A 1 144 ? -23.320 -23.989 11.818  1.00 27.66  ? 139 ASP A O   1 
ATOM   1063 C  CB  . ASP A 1 144 ? -25.362 -21.703 13.196  1.00 27.34  ? 139 ASP A CB  1 
ATOM   1064 C  CG  . ASP A 1 144 ? -24.951 -20.997 11.943  1.00 27.74  ? 139 ASP A CG  1 
ATOM   1065 O  OD1 . ASP A 1 144 ? -25.369 -21.461 10.825  1.00 30.03  ? 139 ASP A OD1 1 
ATOM   1066 O  OD2 . ASP A 1 144 ? -24.236 -19.984 12.045  1.00 27.54  ? 139 ASP A OD2 1 
ATOM   1067 N  N   . LYS A 1 145 ? -22.778 -23.298 13.884  1.00 28.12  ? 140 LYS A N   1 
ATOM   1068 C  CA  . LYS A 1 145 ? -21.358 -23.522 13.705  1.00 27.52  ? 140 LYS A CA  1 
ATOM   1069 C  C   . LYS A 1 145 ? -21.069 -24.983 13.383  1.00 28.23  ? 140 LYS A C   1 
ATOM   1070 O  O   . LYS A 1 145 ? -20.231 -25.266 12.533  1.00 29.17  ? 140 LYS A O   1 
ATOM   1071 C  CB  . LYS A 1 145 ? -20.589 -23.085 14.969  1.00 30.41  ? 140 LYS A CB  1 
ATOM   1072 C  CG  . LYS A 1 145 ? -19.078 -23.192 14.818  1.00 32.74  ? 140 LYS A CG  1 
ATOM   1073 C  CD  . LYS A 1 145 ? -18.328 -22.639 15.961  1.00 36.66  ? 140 LYS A CD  1 
ATOM   1074 C  CE  . LYS A 1 145 ? -16.849 -22.733 15.759  1.00 39.58  ? 140 LYS A CE  1 
ATOM   1075 N  NZ  . LYS A 1 145 ? -16.081 -22.256 16.930  1.00 42.30  ? 140 LYS A NZ  1 
ATOM   1076 N  N   . LYS A 1 146 ? -21.711 -25.909 14.105  1.00 28.93  ? 141 LYS A N   1 
ATOM   1077 C  CA  . LYS A 1 146 ? -21.473 -27.324 13.865  1.00 31.10  ? 141 LYS A CA  1 
ATOM   1078 C  C   . LYS A 1 146 ? -21.853 -27.719 12.447  1.00 30.07  ? 141 LYS A C   1 
ATOM   1079 O  O   . LYS A 1 146 ? -21.060 -28.360 11.764  1.00 30.65  ? 141 LYS A O   1 
ATOM   1080 C  CB  . LYS A 1 146 ? -22.209 -28.196 14.878  1.00 35.35  ? 141 LYS A CB  1 
ATOM   1081 C  CG  . LYS A 1 146 ? -21.549 -28.072 16.183  1.00 38.38  ? 141 LYS A CG  1 
ATOM   1082 C  CD  . LYS A 1 146 ? -22.291 -28.742 17.254  1.00 40.04  ? 141 LYS A CD  1 
ATOM   1083 C  CE  . LYS A 1 146 ? -21.627 -28.657 18.622  1.00 38.88  ? 141 LYS A CE  1 
ATOM   1084 N  NZ  . LYS A 1 146 ? -22.606 -29.142 19.562  1.00 41.21  ? 141 LYS A NZ  1 
ATOM   1085 N  N   . ARG A 1 147 ? -23.047 -27.333 12.006  1.00 28.86  ? 142 ARG A N   1 
ATOM   1086 C  CA  . ARG A 1 147 ? -23.454 -27.731 10.668  1.00 30.38  ? 142 ARG A CA  1 
ATOM   1087 C  C   . ARG A 1 147 ? -22.591 -27.056 9.600   1.00 29.61  ? 142 ARG A C   1 
ATOM   1088 O  O   . ARG A 1 147 ? -22.252 -27.706 8.624   1.00 29.60  ? 142 ARG A O   1 
ATOM   1089 C  CB  . ARG A 1 147 ? -24.951 -27.570 10.403  1.00 31.11  ? 142 ARG A CB  1 
ATOM   1090 C  CG  . ARG A 1 147 ? -25.511 -26.239 10.625  1.00 32.85  ? 142 ARG A CG  1 
ATOM   1091 C  CD  . ARG A 1 147 ? -27.013 -26.272 10.460  1.00 33.34  ? 142 ARG A CD  1 
ATOM   1092 N  NE  . ARG A 1 147 ? -27.580 -24.955 10.708  1.00 32.78  ? 142 ARG A NE  1 
ATOM   1093 C  CZ  . ARG A 1 147 ? -28.256 -24.597 11.794  1.00 32.03  ? 142 ARG A CZ  1 
ATOM   1094 N  NH1 . ARG A 1 147 ? -28.558 -25.466 12.745  1.00 30.81  ? 142 ARG A NH1 1 
ATOM   1095 N  NH2 . ARG A 1 147 ? -28.610 -23.323 11.941  1.00 32.10  ? 142 ARG A NH2 1 
ATOM   1096 N  N   . ILE A 1 148 ? -22.176 -25.801 9.819   1.00 27.78  ? 143 ILE A N   1 
ATOM   1097 C  CA  . ILE A 1 148 ? -21.296 -25.129 8.877   1.00 27.90  ? 143 ILE A CA  1 
ATOM   1098 C  C   . ILE A 1 148 ? -19.951 -25.834 8.755   1.00 28.66  ? 143 ILE A C   1 
ATOM   1099 O  O   . ILE A 1 148 ? -19.428 -25.988 7.650   1.00 27.22  ? 143 ILE A O   1 
ATOM   1100 C  CB  . ILE A 1 148 ? -21.105 -23.665 9.251   1.00 27.47  ? 143 ILE A CB  1 
ATOM   1101 C  CG1 . ILE A 1 148 ? -22.428 -22.898 9.065   1.00 29.95  ? 143 ILE A CG1 1 
ATOM   1102 C  CG2 . ILE A 1 148 ? -19.958 -23.034 8.500   1.00 29.41  ? 143 ILE A CG2 1 
ATOM   1103 C  CD1 . ILE A 1 148 ? -22.405 -21.548 9.678   1.00 33.80  ? 143 ILE A CD1 1 
ATOM   1104 N  N   . ILE A 1 149 ? -19.371 -26.231 9.897   1.00 29.47  ? 144 ILE A N   1 
ATOM   1105 C  CA  . ILE A 1 149 ? -18.076 -26.882 9.882   1.00 31.14  ? 144 ILE A CA  1 
ATOM   1106 C  C   . ILE A 1 149 ? -18.131 -28.193 9.098   1.00 30.94  ? 144 ILE A C   1 
ATOM   1107 O  O   . ILE A 1 149 ? -17.191 -28.490 8.372   1.00 29.30  ? 144 ILE A O   1 
ATOM   1108 C  CB  . ILE A 1 149 ? -17.533 -27.085 11.307  1.00 32.43  ? 144 ILE A CB  1 
ATOM   1109 C  CG1 . ILE A 1 149 ? -17.081 -25.734 11.871  1.00 32.89  ? 144 ILE A CG1 1 
ATOM   1110 C  CG2 . ILE A 1 149 ? -16.398 -28.088 11.322  1.00 33.56  ? 144 ILE A CG2 1 
ATOM   1111 C  CD1 . ILE A 1 149 ? -16.613 -25.793 13.285  1.00 34.63  ? 144 ILE A CD1 1 
ATOM   1112 N  N   . ASP A 1 150 ? -19.206 -28.970 9.306   1.00 31.94  ? 145 ASP A N   1 
ATOM   1113 C  CA  . ASP A 1 150 ? -19.415 -30.230 8.617   1.00 34.69  ? 145 ASP A CA  1 
ATOM   1114 C  C   . ASP A 1 150 ? -19.475 -29.957 7.114   1.00 33.53  ? 145 ASP A C   1 
ATOM   1115 O  O   . ASP A 1 150 ? -18.820 -30.657 6.359   1.00 35.92  ? 145 ASP A O   1 
ATOM   1116 C  CB  . ASP A 1 150 ? -20.663 -30.941 9.114   1.00 38.97  ? 145 ASP A CB  1 
ATOM   1117 C  CG  . ASP A 1 150 ? -20.518 -31.483 10.536  1.00 44.66  ? 145 ASP A CG  1 
ATOM   1118 O  OD1 . ASP A 1 150 ? -19.361 -31.622 11.013  1.00 48.79  ? 145 ASP A OD1 1 
ATOM   1119 O  OD2 . ASP A 1 150 ? -21.560 -31.722 11.196  1.00 49.62  ? 145 ASP A OD2 1 
ATOM   1120 N  N   . SER A 1 151 ? -20.240 -28.932 6.708   1.00 32.52  ? 146 SER A N   1 
ATOM   1121 C  CA  . SER A 1 151 ? -20.386 -28.572 5.300   1.00 32.31  ? 146 SER A CA  1 
ATOM   1122 C  C   . SER A 1 151 ? -19.068 -28.147 4.657   1.00 33.22  ? 146 SER A C   1 
ATOM   1123 O  O   . SER A 1 151 ? -18.787 -28.518 3.504   1.00 34.53  ? 146 SER A O   1 
ATOM   1124 C  CB  . SER A 1 151 ? -21.432 -27.468 5.122   1.00 32.21  ? 146 SER A CB  1 
ATOM   1125 O  OG  . SER A 1 151 ? -22.735 -27.902 5.479   1.00 33.33  ? 146 SER A OG  1 
ATOM   1126 N  N   . ALA A 1 152 ? -18.279 -27.333 5.378   1.00 30.55  ? 147 ALA A N   1 
ATOM   1127 C  CA  . ALA A 1 152 ? -16.970 -26.939 4.879   1.00 31.02  ? 147 ALA A CA  1 
ATOM   1128 C  C   . ALA A 1 152 ? -16.056 -28.143 4.655   1.00 30.82  ? 147 ALA A C   1 
ATOM   1129 O  O   . ALA A 1 152 ? -15.427 -28.261 3.598   1.00 29.53  ? 147 ALA A O   1 
ATOM   1130 C  CB  . ALA A 1 152 ? -16.297 -25.947 5.809   1.00 30.05  ? 147 ALA A CB  1 
ATOM   1131 N  N   . ARG A 1 153 ? -15.952 -29.019 5.663   1.00 31.44  ? 148 ARG A N   1 
ATOM   1132 C  CA  . ARG A 1 153 ? -15.121 -30.198 5.540   1.00 33.89  ? 148 ARG A CA  1 
ATOM   1133 C  C   . ARG A 1 153 ? -15.501 -31.058 4.329   1.00 31.83  ? 148 ARG A C   1 
ATOM   1134 O  O   . ARG A 1 153 ? -14.628 -31.484 3.576   1.00 33.93  ? 148 ARG A O   1 
ATOM   1135 C  CB  . ARG A 1 153 ? -15.178 -31.024 6.837   1.00 35.57  ? 148 ARG A CB  1 
ATOM   1136 C  CG  . ARG A 1 153 ? -14.263 -32.239 6.833   1.00 39.34  ? 148 ARG A CG  1 
ATOM   1137 C  CD  . ARG A 1 153 ? -14.358 -33.024 8.123   1.00 41.46  ? 148 ARG A CD  1 
ATOM   1138 N  NE  . ARG A 1 153 ? -13.647 -32.356 9.211   1.00 45.62  ? 148 ARG A NE  1 
ATOM   1139 C  CZ  . ARG A 1 153 ? -14.210 -31.765 10.259  1.00 46.80  ? 148 ARG A CZ  1 
ATOM   1140 N  NH1 . ARG A 1 153 ? -15.500 -31.895 10.522  1.00 48.36  ? 148 ARG A NH1 1 
ATOM   1141 N  NH2 . ARG A 1 153 ? -13.457 -31.011 11.057  1.00 47.97  ? 148 ARG A NH2 1 
ATOM   1142 N  N   . SER A 1 154 ? -16.804 -31.272 4.129   1.00 32.33  ? 149 SER A N   1 
ATOM   1143 C  CA  A SER A 1 154 ? -17.315 -32.082 3.039   0.50 34.33  ? 149 SER A CA  1 
ATOM   1144 C  CA  B SER A 1 154 ? -17.289 -32.097 3.038   0.50 33.72  ? 149 SER A CA  1 
ATOM   1145 C  C   . SER A 1 154 ? -16.929 -31.509 1.671   1.00 33.93  ? 149 SER A C   1 
ATOM   1146 O  O   . SER A 1 154 ? -16.537 -32.232 0.747   1.00 35.32  ? 149 SER A O   1 
ATOM   1147 C  CB  A SER A 1 154 ? -18.831 -32.173 3.166   0.50 35.70  ? 149 SER A CB  1 
ATOM   1148 C  CB  B SER A 1 154 ? -18.797 -32.274 3.143   0.50 33.92  ? 149 SER A CB  1 
ATOM   1149 O  OG  A SER A 1 154 ? -19.404 -33.099 2.259   0.50 36.93  ? 149 SER A OG  1 
ATOM   1150 O  OG  B SER A 1 154 ? -19.153 -33.155 4.195   0.50 32.62  ? 149 SER A OG  1 
ATOM   1151 N  N   . ALA A 1 155 ? -17.068 -30.194 1.537   1.00 33.42  ? 150 ALA A N   1 
ATOM   1152 C  CA  . ALA A 1 155 ? -16.761 -29.542 0.270   1.00 31.27  ? 150 ALA A CA  1 
ATOM   1153 C  C   . ALA A 1 155 ? -15.267 -29.617 -0.045  1.00 31.76  ? 150 ALA A C   1 
ATOM   1154 O  O   . ALA A 1 155 ? -14.853 -29.986 -1.157  1.00 31.82  ? 150 ALA A O   1 
ATOM   1155 C  CB  . ALA A 1 155 ? -17.228 -28.111 0.300   1.00 32.34  ? 150 ALA A CB  1 
ATOM   1156 N  N   . TYR A 1 156 ? -14.447 -29.260 0.944   1.00 29.92  ? 151 TYR A N   1 
ATOM   1157 C  CA  . TYR A 1 156 ? -13.008 -29.323 0.791   1.00 30.24  ? 151 TYR A CA  1 
ATOM   1158 C  C   . TYR A 1 156 ? -12.542 -30.732 0.441   1.00 31.94  ? 151 TYR A C   1 
ATOM   1159 O  O   . TYR A 1 156 ? -11.713 -30.914 -0.464  1.00 34.01  ? 151 TYR A O   1 
ATOM   1160 C  CB  . TYR A 1 156 ? -12.313 -28.846 2.056   1.00 30.08  ? 151 TYR A CB  1 
ATOM   1161 C  CG  . TYR A 1 156 ? -12.201 -27.349 2.254   1.00 28.05  ? 151 TYR A CG  1 
ATOM   1162 C  CD1 . TYR A 1 156 ? -11.718 -26.521 1.251   1.00 28.02  ? 151 TYR A CD1 1 
ATOM   1163 C  CD2 . TYR A 1 156 ? -12.513 -26.766 3.470   1.00 27.74  ? 151 TYR A CD2 1 
ATOM   1164 C  CE1 . TYR A 1 156 ? -11.571 -25.153 1.446   1.00 26.95  ? 151 TYR A CE1 1 
ATOM   1165 C  CE2 . TYR A 1 156 ? -12.364 -25.402 3.677   1.00 27.03  ? 151 TYR A CE2 1 
ATOM   1166 C  CZ  . TYR A 1 156 ? -11.886 -24.595 2.668   1.00 26.25  ? 151 TYR A CZ  1 
ATOM   1167 O  OH  . TYR A 1 156 ? -11.719 -23.254 2.892   1.00 25.51  ? 151 TYR A OH  1 
ATOM   1168 N  N   . GLN A 1 157 ? -13.089 -31.727 1.140   1.00 33.18  ? 152 GLN A N   1 
ATOM   1169 C  CA  . GLN A 1 157 ? -12.670 -33.099 0.931   1.00 35.90  ? 152 GLN A CA  1 
ATOM   1170 C  C   . GLN A 1 157 ? -13.014 -33.606 -0.468  1.00 34.90  ? 152 GLN A C   1 
ATOM   1171 O  O   . GLN A 1 157 ? -12.222 -34.319 -1.063  1.00 36.45  ? 152 GLN A O   1 
ATOM   1172 C  CB  . GLN A 1 157 ? -13.275 -34.016 1.990   1.00 37.29  ? 152 GLN A CB  1 
ATOM   1173 C  CG  . GLN A 1 157 ? -12.725 -35.426 1.941   1.00 40.02  ? 152 GLN A CG  1 
ATOM   1174 C  CD  . GLN A 1 157 ? -11.236 -35.457 2.130   1.00 42.26  ? 152 GLN A CD  1 
ATOM   1175 O  OE1 . GLN A 1 157 ? -10.701 -34.996 3.136   1.00 43.84  ? 152 GLN A OE1 1 
ATOM   1176 N  NE2 . GLN A 1 157 ? -10.515 -35.964 1.146   1.00 46.54  ? 152 GLN A NE2 1 
ATOM   1177 N  N   . GLU A 1 158 ? -14.183 -33.238 -0.991  1.00 36.19  ? 153 GLU A N   1 
ATOM   1178 C  CA  . GLU A 1 158 ? -14.548 -33.629 -2.342  1.00 38.66  ? 153 GLU A CA  1 
ATOM   1179 C  C   . GLU A 1 158 ? -13.607 -32.987 -3.363  1.00 36.89  ? 153 GLU A C   1 
ATOM   1180 O  O   . GLU A 1 158 ? -13.144 -33.652 -4.290  1.00 37.35  ? 153 GLU A O   1 
ATOM   1181 C  CB  . GLU A 1 158 ? -15.996 -33.251 -2.613  1.00 42.04  ? 153 GLU A CB  1 
ATOM   1182 C  CG  . GLU A 1 158 ? -16.508 -33.851 -3.909  1.00 47.20  ? 153 GLU A CG  1 
ATOM   1183 C  CD  . GLU A 1 158 ? -17.960 -33.535 -4.203  1.00 52.27  ? 153 GLU A CD  1 
ATOM   1184 O  OE1 . GLU A 1 158 ? -18.648 -32.955 -3.325  1.00 55.50  ? 153 GLU A OE1 1 
ATOM   1185 O  OE2 . GLU A 1 158 ? -18.401 -33.865 -5.328  1.00 54.03  ? 153 GLU A OE2 1 
ATOM   1186 N  N   . ALA A 1 159 ? -13.326 -31.692 -3.182  1.00 36.13  ? 154 ALA A N   1 
ATOM   1187 C  CA  . ALA A 1 159 ? -12.366 -30.974 -4.004  1.00 34.66  ? 154 ALA A CA  1 
ATOM   1188 C  C   . ALA A 1 159 ? -10.984 -31.626 -3.958  1.00 35.09  ? 154 ALA A C   1 
ATOM   1189 O  O   . ALA A 1 159 ? -10.333 -31.790 -4.991  1.00 36.40  ? 154 ALA A O   1 
ATOM   1190 C  CB  . ALA A 1 159 ? -12.286 -29.520 -3.566  1.00 33.14  ? 154 ALA A CB  1 
ATOM   1191 N  N   . MET A 1 160 ? -10.537 -32.010 -2.755  1.00 35.59  ? 155 MET A N   1 
ATOM   1192 C  CA  . MET A 1 160 ? -9.257  -32.680 -2.592  1.00 37.74  ? 155 MET A CA  1 
ATOM   1193 C  C   . MET A 1 160 ? -9.202  -33.983 -3.395  1.00 38.43  ? 155 MET A C   1 
ATOM   1194 O  O   . MET A 1 160 ? -8.209  -34.267 -4.045  1.00 39.51  ? 155 MET A O   1 
ATOM   1195 C  CB  . MET A 1 160 ? -8.994  -32.996 -1.114  1.00 39.40  ? 155 MET A CB  1 
ATOM   1196 C  CG  . MET A 1 160 ? -8.712  -31.777 -0.259  1.00 40.11  ? 155 MET A CG  1 
ATOM   1197 S  SD  . MET A 1 160 ? -7.142  -30.939 -0.501  1.00 42.62  ? 155 MET A SD  1 
ATOM   1198 C  CE  . MET A 1 160 ? -6.024  -32.218 -0.316  1.00 41.12  ? 155 MET A CE  1 
ATOM   1199 N  N   . ASP A 1 161 ? -10.276 -34.777 -3.336  1.00 39.84  ? 156 ASP A N   1 
ATOM   1200 C  CA  . ASP A 1 161 ? -10.338 -36.045 -4.044  1.00 41.62  ? 156 ASP A CA  1 
ATOM   1201 C  C   . ASP A 1 161 ? -10.203 -35.872 -5.556  1.00 41.17  ? 156 ASP A C   1 
ATOM   1202 O  O   . ASP A 1 161 ? -9.465  -36.623 -6.190  1.00 44.10  ? 156 ASP A O   1 
ATOM   1203 C  CB  . ASP A 1 161 ? -11.640 -36.775 -3.677  1.00 44.29  ? 156 ASP A CB  1 
ATOM   1204 C  CG  . ASP A 1 161 ? -11.643 -37.274 -2.242  1.00 46.35  ? 156 ASP A CG  1 
ATOM   1205 O  OD1 . ASP A 1 161 ? -10.566 -37.255 -1.602  1.00 48.71  ? 156 ASP A OD1 1 
ATOM   1206 O  OD2 . ASP A 1 161 ? -12.724 -37.668 -1.750  1.00 51.50  ? 156 ASP A OD2 1 
ATOM   1207 N  N   . ILE A 1 162 ? -10.911 -34.887 -6.122  1.00 36.87  ? 157 ILE A N   1 
ATOM   1208 C  CA  . ILE A 1 162 ? -10.801 -34.593 -7.543  1.00 40.64  ? 157 ILE A CA  1 
ATOM   1209 C  C   . ILE A 1 162 ? -9.394  -34.107 -7.893  1.00 39.62  ? 157 ILE A C   1 
ATOM   1210 O  O   . ILE A 1 162 ? -8.800  -34.564 -8.866  1.00 38.81  ? 157 ILE A O   1 
ATOM   1211 C  CB  . ILE A 1 162 ? -11.870 -33.563 -7.989  1.00 41.16  ? 157 ILE A CB  1 
ATOM   1212 C  CG1 . ILE A 1 162 ? -13.316 -34.051 -7.645  1.00 42.93  ? 157 ILE A CG1 1 
ATOM   1213 C  CG2 . ILE A 1 162 ? -11.720 -33.234 -9.481  1.00 41.55  ? 157 ILE A CG2 1 
ATOM   1214 C  CD1 . ILE A 1 162 ? -14.345 -33.009 -7.710  1.00 42.65  ? 157 ILE A CD1 1 
ATOM   1215 N  N   . SER A 1 163 ? -8.862  -33.175 -7.095  1.00 38.15  ? 158 SER A N   1 
ATOM   1216 C  CA  . SER A 1 163 ? -7.585  -32.557 -7.415  1.00 39.55  ? 158 SER A CA  1 
ATOM   1217 C  C   . SER A 1 163 ? -6.458  -33.589 -7.416  1.00 39.27  ? 158 SER A C   1 
ATOM   1218 O  O   . SER A 1 163 ? -5.559  -33.518 -8.243  1.00 38.38  ? 158 SER A O   1 
ATOM   1219 C  CB  . SER A 1 163 ? -7.288  -31.399 -6.456  1.00 39.35  ? 158 SER A CB  1 
ATOM   1220 O  OG  . SER A 1 163 ? -6.859  -31.884 -5.200  1.00 42.33  ? 158 SER A OG  1 
ATOM   1221 N  N   . LYS A 1 164 ? -6.519  -34.561 -6.495  1.00 42.95  ? 159 LYS A N   1 
ATOM   1222 C  CA  . LYS A 1 164 ? -5.514  -35.610 -6.422  1.00 45.69  ? 159 LYS A CA  1 
ATOM   1223 C  C   . LYS A 1 164 ? -5.544  -36.534 -7.634  1.00 44.59  ? 159 LYS A C   1 
ATOM   1224 O  O   . LYS A 1 164 ? -4.498  -37.019 -8.033  1.00 45.65  ? 159 LYS A O   1 
ATOM   1225 C  CB  . LYS A 1 164 ? -5.653  -36.444 -5.134  1.00 49.55  ? 159 LYS A CB  1 
ATOM   1226 C  CG  . LYS A 1 164 ? -4.926  -35.819 -3.946  1.00 57.04  ? 159 LYS A CG  1 
ATOM   1227 C  CD  . LYS A 1 164 ? -5.152  -36.591 -2.628  1.00 60.98  ? 159 LYS A CD  1 
ATOM   1228 C  CE  . LYS A 1 164 ? -5.044  -35.723 -1.391  1.00 64.99  ? 159 LYS A CE  1 
ATOM   1229 N  NZ  . LYS A 1 164 ? -3.636  -35.524 -0.948  1.00 69.61  ? 159 LYS A NZ  1 
ATOM   1230 N  N   . LYS A 1 165 ? -6.730  -36.753 -8.215  1.00 44.76  ? 160 LYS A N   1 
ATOM   1231 C  CA  . LYS A 1 165 ? -6.870  -37.532 -9.440  1.00 47.34  ? 160 LYS A CA  1 
ATOM   1232 C  C   . LYS A 1 165 ? -6.525  -36.768 -10.711 1.00 45.27  ? 160 LYS A C   1 
ATOM   1233 O  O   . LYS A 1 165 ? -6.049  -37.366 -11.666 1.00 49.60  ? 160 LYS A O   1 
ATOM   1234 C  CB  . LYS A 1 165 ? -8.310  -38.033 -9.611  1.00 50.04  ? 160 LYS A CB  1 
ATOM   1235 C  CG  . LYS A 1 165 ? -8.639  -39.193 -8.698  1.00 57.45  ? 160 LYS A CG  1 
ATOM   1236 C  CD  . LYS A 1 165 ? -10.152 -39.410 -8.525  1.00 61.52  ? 160 LYS A CD  1 
ATOM   1237 C  CE  . LYS A 1 165 ? -10.498 -40.416 -7.432  1.00 64.98  ? 160 LYS A CE  1 
ATOM   1238 N  NZ  . LYS A 1 165 ? -10.033 -39.972 -6.079  1.00 66.39  ? 160 LYS A NZ  1 
ATOM   1239 N  N   . GLU A 1 166 ? -6.818  -35.467 -10.747 1.00 42.43  ? 161 GLU A N   1 
ATOM   1240 C  CA  . GLU A 1 166 ? -6.894  -34.754 -12.016 1.00 44.37  ? 161 GLU A CA  1 
ATOM   1241 C  C   . GLU A 1 166 ? -5.809  -33.702 -12.230 1.00 42.02  ? 161 GLU A C   1 
ATOM   1242 O  O   . GLU A 1 166 ? -5.674  -33.176 -13.331 1.00 44.86  ? 161 GLU A O   1 
ATOM   1243 C  CB  . GLU A 1 166 ? -8.275  -34.075 -12.141 1.00 44.99  ? 161 GLU A CB  1 
ATOM   1244 C  CG  . GLU A 1 166 ? -9.457  -35.037 -12.092 1.00 49.30  ? 161 GLU A CG  1 
ATOM   1245 C  CD  . GLU A 1 166 ? -9.829  -35.749 -13.386 1.00 54.82  ? 161 GLU A CD  1 
ATOM   1246 O  OE1 . GLU A 1 166 ? -9.150  -35.560 -14.426 1.00 59.07  ? 161 GLU A OE1 1 
ATOM   1247 O  OE2 . GLU A 1 166 ? -10.825 -36.508 -13.354 1.00 58.41  ? 161 GLU A OE2 1 
ATOM   1248 N  N   . MET A 1 167 ? -5.045  -33.387 -11.178 1.00 39.57  ? 162 MET A N   1 
ATOM   1249 C  CA  . MET A 1 167 ? -4.119  -32.269 -11.225 1.00 37.59  ? 162 MET A CA  1 
ATOM   1250 C  C   . MET A 1 167 ? -2.760  -32.715 -10.696 1.00 35.95  ? 162 MET A C   1 
ATOM   1251 O  O   . MET A 1 167 ? -2.702  -33.517 -9.765  1.00 37.13  ? 162 MET A O   1 
ATOM   1252 C  CB  . MET A 1 167 ? -4.631  -31.114 -10.344 1.00 38.03  ? 162 MET A CB  1 
ATOM   1253 C  CG  . MET A 1 167 ? -5.873  -30.453 -10.874 1.00 39.14  ? 162 MET A CG  1 
ATOM   1254 S  SD  . MET A 1 167 ? -6.469  -29.181 -9.750  1.00 40.77  ? 162 MET A SD  1 
ATOM   1255 C  CE  . MET A 1 167 ? -7.940  -28.705 -10.554 1.00 42.05  ? 162 MET A CE  1 
ATOM   1256 N  N   . PRO A 1 168 ? -1.635  -32.227 -11.268 1.00 34.33  ? 163 PRO A N   1 
ATOM   1257 C  CA  . PRO A 1 168 ? -0.314  -32.545 -10.741 1.00 33.83  ? 163 PRO A CA  1 
ATOM   1258 C  C   . PRO A 1 168 ? -0.111  -31.837 -9.405  1.00 33.07  ? 163 PRO A C   1 
ATOM   1259 O  O   . PRO A 1 168 ? -0.797  -30.867 -9.104  1.00 32.19  ? 163 PRO A O   1 
ATOM   1260 C  CB  . PRO A 1 168 ? 0.647   -32.043 -11.825 1.00 35.89  ? 163 PRO A CB  1 
ATOM   1261 C  CG  . PRO A 1 168 ? -0.099  -30.972 -12.533 1.00 36.91  ? 163 PRO A CG  1 
ATOM   1262 C  CD  . PRO A 1 168 ? -1.570  -31.367 -12.464 1.00 36.58  ? 163 PRO A CD  1 
ATOM   1263 N  N   . PRO A 1 169 ? 0.852   -32.303 -8.585  1.00 34.05  ? 164 PRO A N   1 
ATOM   1264 C  CA  . PRO A 1 169 ? 1.091   -31.743 -7.250  1.00 33.93  ? 164 PRO A CA  1 
ATOM   1265 C  C   . PRO A 1 169 ? 1.507   -30.276 -7.172  1.00 32.34  ? 164 PRO A C   1 
ATOM   1266 O  O   . PRO A 1 169 ? 1.334   -29.639 -6.136  1.00 34.14  ? 164 PRO A O   1 
ATOM   1267 C  CB  . PRO A 1 169 ? 2.204   -32.645 -6.701  1.00 36.76  ? 164 PRO A CB  1 
ATOM   1268 C  CG  . PRO A 1 169 ? 2.206   -33.882 -7.580  1.00 37.68  ? 164 PRO A CG  1 
ATOM   1269 C  CD  . PRO A 1 169 ? 1.734   -33.430 -8.907  1.00 36.78  ? 164 PRO A CD  1 
ATOM   1270 N  N   . THR A 1 170 ? 2.048   -29.725 -8.271  1.00 29.63  ? 165 THR A N   1 
ATOM   1271 C  CA  . THR A 1 170 ? 2.425   -28.319 -8.292  1.00 30.00  ? 165 THR A CA  1 
ATOM   1272 C  C   . THR A 1 170 ? 1.357   -27.385 -8.852  1.00 29.41  ? 165 THR A C   1 
ATOM   1273 O  O   . THR A 1 170 ? 1.586   -26.174 -8.911  1.00 30.74  ? 165 THR A O   1 
ATOM   1274 C  CB  . THR A 1 170 ? 3.706   -28.137 -9.053  1.00 30.43  ? 165 THR A CB  1 
ATOM   1275 O  OG1 . THR A 1 170 ? 3.493   -28.655 -10.364 1.00 31.41  ? 165 THR A OG1 1 
ATOM   1276 C  CG2 . THR A 1 170 ? 4.875   -28.818 -8.372  1.00 32.28  ? 165 THR A CG2 1 
ATOM   1277 N  N   . ASN A 1 171 ? 0.201   -27.949 -9.245  1.00 30.20  ? 166 ASN A N   1 
ATOM   1278 C  CA  . ASN A 1 171 ? -0.866  -27.172 -9.847  1.00 30.21  ? 166 ASN A CA  1 
ATOM   1279 C  C   . ASN A 1 171 ? -1.321  -26.134 -8.831  1.00 29.39  ? 166 ASN A C   1 
ATOM   1280 O  O   . ASN A 1 171 ? -1.695  -26.484 -7.704  1.00 29.68  ? 166 ASN A O   1 
ATOM   1281 C  CB  . ASN A 1 171 ? -2.017  -28.030 -10.290 1.00 31.06  ? 166 ASN A CB  1 
ATOM   1282 C  CG  . ASN A 1 171 ? -3.170  -27.244 -10.870 1.00 31.71  ? 166 ASN A CG  1 
ATOM   1283 O  OD1 . ASN A 1 171 ? -3.902  -26.568 -10.181 1.00 34.67  ? 166 ASN A OD1 1 
ATOM   1284 N  ND2 . ASN A 1 171 ? -3.360  -27.325 -12.184 1.00 33.61  ? 166 ASN A ND2 1 
ATOM   1285 N  N   . PRO A 1 172 ? -1.287  -24.837 -9.180  1.00 28.25  ? 167 PRO A N   1 
ATOM   1286 C  CA  . PRO A 1 172 ? -1.658  -23.776 -8.242  1.00 28.46  ? 167 PRO A CA  1 
ATOM   1287 C  C   . PRO A 1 172 ? -3.055  -23.891 -7.623  1.00 27.29  ? 167 PRO A C   1 
ATOM   1288 O  O   . PRO A 1 172 ? -3.244  -23.494 -6.481  1.00 28.34  ? 167 PRO A O   1 
ATOM   1289 C  CB  . PRO A 1 172 ? -1.482  -22.506 -9.061  1.00 29.46  ? 167 PRO A CB  1 
ATOM   1290 C  CG  . PRO A 1 172 ? -0.572  -22.899 -10.175 1.00 30.73  ? 167 PRO A CG  1 
ATOM   1291 C  CD  . PRO A 1 172 ? -0.843  -24.313 -10.479 1.00 29.75  ? 167 PRO A CD  1 
ATOM   1292 N  N   . ILE A 1 173 ? -4.051  -24.385 -8.373  1.00 27.46  ? 168 ILE A N   1 
ATOM   1293 C  CA  . ILE A 1 173 ? -5.384  -24.587 -7.828  1.00 28.75  ? 168 ILE A CA  1 
ATOM   1294 C  C   . ILE A 1 173 ? -5.345  -25.677 -6.753  1.00 28.51  ? 168 ILE A C   1 
ATOM   1295 O  O   . ILE A 1 173 ? -5.880  -25.514 -5.648  1.00 29.11  ? 168 ILE A O   1 
ATOM   1296 C  CB  . ILE A 1 173 ? -6.425  -24.879 -8.952  1.00 30.64  ? 168 ILE A CB  1 
ATOM   1297 C  CG1 . ILE A 1 173 ? -6.524  -23.683 -9.896  1.00 33.30  ? 168 ILE A CG1 1 
ATOM   1298 C  CG2 . ILE A 1 173 ? -7.803  -25.234 -8.361  1.00 31.02  ? 168 ILE A CG2 1 
ATOM   1299 C  CD1 . ILE A 1 173 ? -7.389  -23.934 -11.089 1.00 35.17  ? 168 ILE A CD1 1 
ATOM   1300 N  N   . ARG A 1 174 ? -4.722  -26.805 -7.087  1.00 28.69  ? 169 ARG A N   1 
ATOM   1301 C  CA  . ARG A 1 174 ? -4.565  -27.892 -6.144  1.00 28.83  ? 169 ARG A CA  1 
ATOM   1302 C  C   . ARG A 1 174 ? -3.838  -27.392 -4.896  1.00 28.98  ? 169 ARG A C   1 
ATOM   1303 O  O   . ARG A 1 174 ? -4.269  -27.689 -3.793  1.00 29.30  ? 169 ARG A O   1 
ATOM   1304 C  CB  . ARG A 1 174 ? -3.836  -29.059 -6.745  1.00 29.72  ? 169 ARG A CB  1 
ATOM   1305 C  CG  . ARG A 1 174 ? -3.555  -30.197 -5.780  1.00 30.00  ? 169 ARG A CG  1 
ATOM   1306 C  CD  . ARG A 1 174 ? -2.944  -31.409 -6.507  1.00 33.25  ? 169 ARG A CD  1 
ATOM   1307 N  NE  . ARG A 1 174 ? -2.465  -32.417 -5.569  1.00 32.85  ? 169 ARG A NE  1 
ATOM   1308 C  CZ  . ARG A 1 174 ? -1.904  -33.566 -5.909  1.00 33.94  ? 169 ARG A CZ  1 
ATOM   1309 N  NH1 . ARG A 1 174 ? -1.796  -33.943 -7.170  1.00 34.75  ? 169 ARG A NH1 1 
ATOM   1310 N  NH2 . ARG A 1 174 ? -1.391  -34.340 -4.963  1.00 37.22  ? 169 ARG A NH2 1 
ATOM   1311 N  N   . LEU A 1 175 ? -2.756  -26.632 -5.082  1.00 28.57  ? 170 LEU A N   1 
ATOM   1312 C  CA  . LEU A 1 175 ? -1.971  -26.133 -3.966  1.00 27.70  ? 170 LEU A CA  1 
ATOM   1313 C  C   . LEU A 1 175 ? -2.794  -25.201 -3.077  1.00 28.89  ? 170 LEU A C   1 
ATOM   1314 O  O   . LEU A 1 175 ? -2.753  -25.331 -1.844  1.00 30.17  ? 170 LEU A O   1 
ATOM   1315 C  CB  . LEU A 1 175 ? -0.718  -25.425 -4.455  1.00 27.43  ? 170 LEU A CB  1 
ATOM   1316 C  CG  . LEU A 1 175 ? 0.413   -26.297 -4.958  1.00 28.68  ? 170 LEU A CG  1 
ATOM   1317 C  CD1 . LEU A 1 175 ? 1.514   -25.450 -5.536  1.00 29.06  ? 170 LEU A CD1 1 
ATOM   1318 C  CD2 . LEU A 1 175 ? 0.985   -27.171 -3.824  1.00 30.30  ? 170 LEU A CD2 1 
ATOM   1319 N  N   . GLY A 1 176 ? -3.549  -24.282 -3.693  1.00 28.42  ? 171 GLY A N   1 
ATOM   1320 C  CA  . GLY A 1 176 ? -4.346  -23.307 -2.955  1.00 27.54  ? 171 GLY A CA  1 
ATOM   1321 C  C   . GLY A 1 176 ? -5.480  -23.945 -2.157  1.00 27.36  ? 171 GLY A C   1 
ATOM   1322 O  O   . GLY A 1 176 ? -5.785  -23.510 -1.037  1.00 26.87  ? 171 GLY A O   1 
ATOM   1323 N  N   . LEU A 1 177 ? -6.075  -24.998 -2.731  1.00 27.49  ? 172 LEU A N   1 
ATOM   1324 C  CA  . LEU A 1 177 ? -7.094  -25.790 -2.063  1.00 28.93  ? 172 LEU A CA  1 
ATOM   1325 C  C   . LEU A 1 177 ? -6.499  -26.418 -0.799  1.00 28.20  ? 172 LEU A C   1 
ATOM   1326 O  O   . LEU A 1 177 ? -7.075  -26.294 0.307   1.00 29.53  ? 172 LEU A O   1 
ATOM   1327 C  CB  . LEU A 1 177 ? -7.618  -26.857 -3.038  1.00 29.95  ? 172 LEU A CB  1 
ATOM   1328 C  CG  . LEU A 1 177 ? -8.411  -28.012 -2.444  1.00 30.43  ? 172 LEU A CG  1 
ATOM   1329 C  CD1 . LEU A 1 177 ? -9.654  -27.536 -1.737  1.00 29.87  ? 172 LEU A CD1 1 
ATOM   1330 C  CD2 . LEU A 1 177 ? -8.779  -29.009 -3.537  1.00 31.52  ? 172 LEU A CD2 1 
ATOM   1331 N  N   . ALA A 1 178 ? -5.329  -27.058 -0.958  1.00 27.27  ? 173 ALA A N   1 
ATOM   1332 C  CA  . ALA A 1 178 ? -4.697  -27.762 0.157   1.00 29.82  ? 173 ALA A CA  1 
ATOM   1333 C  C   . ALA A 1 178 ? -4.329  -26.786 1.278   1.00 29.15  ? 173 ALA A C   1 
ATOM   1334 O  O   . ALA A 1 178 ? -4.557  -27.068 2.477   1.00 30.28  ? 173 ALA A O   1 
ATOM   1335 C  CB  . ALA A 1 178 ? -3.470  -28.547 -0.318  1.00 31.27  ? 173 ALA A CB  1 
ATOM   1336 N  N   . LEU A 1 179 ? -3.810  -25.620 0.874   1.00 29.41  ? 174 LEU A N   1 
ATOM   1337 C  CA  . LEU A 1 179 ? -3.491  -24.539 1.798   1.00 27.51  ? 174 LEU A CA  1 
ATOM   1338 C  C   . LEU A 1 179 ? -4.730  -24.162 2.605   1.00 27.61  ? 174 LEU A C   1 
ATOM   1339 O  O   . LEU A 1 179 ? -4.693  -24.175 3.842   1.00 28.51  ? 174 LEU A O   1 
ATOM   1340 C  CB  . LEU A 1 179 ? -2.938  -23.316 1.055   1.00 27.25  ? 174 LEU A CB  1 
ATOM   1341 C  CG  . LEU A 1 179 ? -2.742  -22.055 1.832   1.00 28.39  ? 174 LEU A CG  1 
ATOM   1342 C  CD1 . LEU A 1 179 ? -1.673  -22.240 2.920   1.00 31.04  ? 174 LEU A CD1 1 
ATOM   1343 C  CD2 . LEU A 1 179 ? -2.377  -20.892 0.935   1.00 27.22  ? 174 LEU A CD2 1 
ATOM   1344 N  N   . ASN A 1 180 ? -5.835  -23.873 1.914   1.00 26.63  ? 175 ASN A N   1 
ATOM   1345 C  CA  . ASN A 1 180 ? -7.040  -23.414 2.598   1.00 26.74  ? 175 ASN A CA  1 
ATOM   1346 C  C   . ASN A 1 180 ? -7.660  -24.504 3.467   1.00 27.36  ? 175 ASN A C   1 
ATOM   1347 O  O   . ASN A 1 180 ? -8.241  -24.186 4.498   1.00 29.48  ? 175 ASN A O   1 
ATOM   1348 C  CB  . ASN A 1 180 ? -8.063  -22.865 1.621   1.00 27.25  ? 175 ASN A CB  1 
ATOM   1349 C  CG  . ASN A 1 180 ? -7.653  -21.510 1.066   1.00 26.11  ? 175 ASN A CG  1 
ATOM   1350 O  OD1 . ASN A 1 180 ? -6.567  -20.984 1.326   1.00 25.89  ? 175 ASN A OD1 1 
ATOM   1351 N  ND2 . ASN A 1 180 ? -8.530  -20.903 0.281   1.00 26.51  ? 175 ASN A ND2 1 
ATOM   1352 N  N   . PHE A 1 181 ? -7.567  -25.774 3.047   1.00 27.56  ? 176 PHE A N   1 
ATOM   1353 C  CA  . PHE A 1 181 ? -8.101  -26.864 3.850   1.00 27.95  ? 176 PHE A CA  1 
ATOM   1354 C  C   . PHE A 1 181 ? -7.282  -27.012 5.131   1.00 28.55  ? 176 PHE A C   1 
ATOM   1355 O  O   . PHE A 1 181 ? -7.845  -27.279 6.207   1.00 29.35  ? 176 PHE A O   1 
ATOM   1356 C  CB  . PHE A 1 181 ? -8.100  -28.186 3.082   1.00 30.12  ? 176 PHE A CB  1 
ATOM   1357 C  CG  . PHE A 1 181 ? -8.979  -29.278 3.655   1.00 31.63  ? 176 PHE A CG  1 
ATOM   1358 C  CD1 . PHE A 1 181 ? -9.962  -28.990 4.601   1.00 31.85  ? 176 PHE A CD1 1 
ATOM   1359 C  CD2 . PHE A 1 181 ? -8.824  -30.598 3.255   1.00 32.87  ? 176 PHE A CD2 1 
ATOM   1360 C  CE1 . PHE A 1 181 ? -10.762 -29.991 5.125   1.00 33.75  ? 176 PHE A CE1 1 
ATOM   1361 C  CE2 . PHE A 1 181 ? -9.639  -31.599 3.776   1.00 35.16  ? 176 PHE A CE2 1 
ATOM   1362 C  CZ  . PHE A 1 181 ? -10.606 -31.287 4.712   1.00 34.41  ? 176 PHE A CZ  1 
ATOM   1363 N  N   . SER A 1 182 ? -5.960  -26.823 5.014   1.00 27.37  ? 177 SER A N   1 
ATOM   1364 C  CA  . SER A 1 182 ? -5.089  -26.860 6.188   1.00 30.30  ? 177 SER A CA  1 
ATOM   1365 C  C   . SER A 1 182 ? -5.413  -25.724 7.168   1.00 29.98  ? 177 SER A C   1 
ATOM   1366 O  O   . SER A 1 182 ? -5.489  -25.937 8.404   1.00 31.67  ? 177 SER A O   1 
ATOM   1367 C  CB  . SER A 1 182 ? -3.628  -26.868 5.736   1.00 32.01  ? 177 SER A CB  1 
ATOM   1368 O  OG  . SER A 1 182 ? -3.138  -25.590 5.370   1.00 32.57  ? 177 SER A OG  1 
ATOM   1369 N  N   . VAL A 1 183 ? -5.712  -24.535 6.626   1.00 28.75  ? 178 VAL A N   1 
ATOM   1370 C  CA  . VAL A 1 183 ? -6.176  -23.424 7.456   1.00 29.56  ? 178 VAL A CA  1 
ATOM   1371 C  C   . VAL A 1 183 ? -7.484  -23.767 8.181   1.00 29.83  ? 178 VAL A C   1 
ATOM   1372 O  O   . VAL A 1 183 ? -7.627  -23.510 9.392   1.00 30.78  ? 178 VAL A O   1 
ATOM   1373 C  CB  . VAL A 1 183 ? -6.301  -22.116 6.674   1.00 28.76  ? 178 VAL A CB  1 
ATOM   1374 C  CG1 . VAL A 1 183 ? -6.938  -21.016 7.521   1.00 28.97  ? 178 VAL A CG1 1 
ATOM   1375 C  CG2 . VAL A 1 183 ? -4.944  -21.657 6.161   1.00 30.36  ? 178 VAL A CG2 1 
ATOM   1376 N  N   . PHE A 1 184 ? -8.422  -24.378 7.452   1.00 27.46  ? 179 PHE A N   1 
ATOM   1377 C  CA  . PHE A 1 184 ? -9.637  -24.905 8.055   1.00 29.19  ? 179 PHE A CA  1 
ATOM   1378 C  C   . PHE A 1 184 ? -9.346  -25.808 9.255   1.00 30.42  ? 179 PHE A C   1 
ATOM   1379 O  O   . PHE A 1 184 ? -9.909  -25.610 10.341  1.00 29.61  ? 179 PHE A O   1 
ATOM   1380 C  CB  . PHE A 1 184 ? -10.442 -25.697 7.023   1.00 30.78  ? 179 PHE A CB  1 
ATOM   1381 C  CG  . PHE A 1 184 ? -11.636 -26.403 7.577   1.00 30.35  ? 179 PHE A CG  1 
ATOM   1382 C  CD1 . PHE A 1 184 ? -12.768 -25.697 7.916   1.00 31.69  ? 179 PHE A CD1 1 
ATOM   1383 C  CD2 . PHE A 1 184 ? -11.608 -27.774 7.814   1.00 32.41  ? 179 PHE A CD2 1 
ATOM   1384 C  CE1 . PHE A 1 184 ? -13.879 -26.337 8.421   1.00 33.35  ? 179 PHE A CE1 1 
ATOM   1385 C  CE2 . PHE A 1 184 ? -12.716 -28.421 8.362   1.00 34.31  ? 179 PHE A CE2 1 
ATOM   1386 C  CZ  . PHE A 1 184 ? -13.855 -27.696 8.648   1.00 34.22  ? 179 PHE A CZ  1 
ATOM   1387 N  N   . HIS A 1 185 ? -8.480  -26.811 9.048   1.00 30.77  ? 180 HIS A N   1 
ATOM   1388 C  CA  . HIS A 1 185 ? -8.129  -27.753 10.101  1.00 33.54  ? 180 HIS A CA  1 
ATOM   1389 C  C   . HIS A 1 185 ? -7.588  -27.044 11.342  1.00 33.80  ? 180 HIS A C   1 
ATOM   1390 O  O   . HIS A 1 185 ? -7.957  -27.380 12.475  1.00 35.49  ? 180 HIS A O   1 
ATOM   1391 C  CB  . HIS A 1 185 ? -7.102  -28.779 9.609   1.00 33.82  ? 180 HIS A CB  1 
ATOM   1392 C  CG  . HIS A 1 185 ? -7.645  -29.836 8.696   1.00 35.52  ? 180 HIS A CG  1 
ATOM   1393 N  ND1 . HIS A 1 185 ? -8.853  -30.434 8.935   1.00 39.12  ? 180 HIS A ND1 1 
ATOM   1394 C  CD2 . HIS A 1 185 ? -7.118  -30.356 7.559   1.00 35.43  ? 180 HIS A CD2 1 
ATOM   1395 C  CE1 . HIS A 1 185 ? -9.031  -31.313 7.956   1.00 38.79  ? 180 HIS A CE1 1 
ATOM   1396 N  NE2 . HIS A 1 185 ? -8.009  -31.291 7.099   1.00 36.87  ? 180 HIS A NE2 1 
ATOM   1397 N  N   . TYR A 1 186 ? -6.710  -26.059 11.138  1.00 34.52  ? 181 TYR A N   1 
ATOM   1398 C  CA  . TYR A 1 186 ? -6.053  -25.404 12.256  1.00 35.33  ? 181 TYR A CA  1 
ATOM   1399 C  C   . TYR A 1 186 ? -6.956  -24.413 12.993  1.00 33.76  ? 181 TYR A C   1 
ATOM   1400 O  O   . TYR A 1 186 ? -7.096  -24.482 14.232  1.00 34.19  ? 181 TYR A O   1 
ATOM   1401 C  CB  . TYR A 1 186 ? -4.818  -24.656 11.776  1.00 35.56  ? 181 TYR A CB  1 
ATOM   1402 C  CG  . TYR A 1 186 ? -3.928  -24.232 12.929  1.00 39.26  ? 181 TYR A CG  1 
ATOM   1403 C  CD1 . TYR A 1 186 ? -3.001  -25.104 13.469  1.00 42.16  ? 181 TYR A CD1 1 
ATOM   1404 C  CD2 . TYR A 1 186 ? -4.030  -22.962 13.484  1.00 40.09  ? 181 TYR A CD2 1 
ATOM   1405 C  CE1 . TYR A 1 186 ? -2.186  -24.723 14.522  1.00 43.02  ? 181 TYR A CE1 1 
ATOM   1406 C  CE2 . TYR A 1 186 ? -3.225  -22.568 14.542  1.00 43.40  ? 181 TYR A CE2 1 
ATOM   1407 C  CZ  . TYR A 1 186 ? -2.306  -23.451 15.061  1.00 45.25  ? 181 TYR A CZ  1 
ATOM   1408 O  OH  . TYR A 1 186 ? -1.507  -23.073 16.111  1.00 47.91  ? 181 TYR A OH  1 
ATOM   1409 N  N   . GLU A 1 187 ? -7.547  -23.494 12.219  1.00 33.28  ? 182 GLU A N   1 
ATOM   1410 C  CA  . GLU A 1 187 ? -8.302  -22.358 12.737  1.00 34.99  ? 182 GLU A CA  1 
ATOM   1411 C  C   . GLU A 1 187 ? -9.755  -22.666 13.078  1.00 34.03  ? 182 GLU A C   1 
ATOM   1412 O  O   . GLU A 1 187 ? -10.302 -22.097 14.020  1.00 35.43  ? 182 GLU A O   1 
ATOM   1413 C  CB  . GLU A 1 187 ? -8.352  -21.205 11.706  1.00 36.51  ? 182 GLU A CB  1 
ATOM   1414 C  CG  . GLU A 1 187 ? -7.014  -20.686 11.249  1.00 41.21  ? 182 GLU A CG  1 
ATOM   1415 C  CD  . GLU A 1 187 ? -6.282  -19.813 12.221  1.00 44.48  ? 182 GLU A CD  1 
ATOM   1416 O  OE1 . GLU A 1 187 ? -6.775  -19.654 13.354  1.00 48.86  ? 182 GLU A OE1 1 
ATOM   1417 O  OE2 . GLU A 1 187 ? -5.224  -19.266 11.850  1.00 51.66  ? 182 GLU A OE2 1 
ATOM   1418 N  N   . ILE A 1 188 ? -10.384 -23.557 12.313  1.00 32.40  ? 183 ILE A N   1 
ATOM   1419 C  CA  . ILE A 1 188 ? -11.802 -23.812 12.468  1.00 31.96  ? 183 ILE A CA  1 
ATOM   1420 C  C   . ILE A 1 188 ? -12.100 -25.105 13.223  1.00 32.35  ? 183 ILE A C   1 
ATOM   1421 O  O   . ILE A 1 188 ? -12.846 -25.092 14.209  1.00 33.12  ? 183 ILE A O   1 
ATOM   1422 C  CB  . ILE A 1 188 ? -12.503 -23.826 11.116  1.00 31.79  ? 183 ILE A CB  1 
ATOM   1423 C  CG1 . ILE A 1 188 ? -12.131 -22.599 10.264  1.00 33.94  ? 183 ILE A CG1 1 
ATOM   1424 C  CG2 . ILE A 1 188 ? -14.020 -23.968 11.341  1.00 32.17  ? 183 ILE A CG2 1 
ATOM   1425 C  CD1 . ILE A 1 188 ? -12.465 -21.304 10.858  1.00 32.98  ? 183 ILE A CD1 1 
ATOM   1426 N  N   . ALA A 1 189 ? -11.554 -26.216 12.716  1.00 34.84  ? 184 ALA A N   1 
ATOM   1427 C  CA  . ALA A 1 189 ? -11.744 -27.534 13.311  1.00 36.74  ? 184 ALA A CA  1 
ATOM   1428 C  C   . ALA A 1 189 ? -10.934 -27.783 14.576  1.00 38.65  ? 184 ALA A C   1 
ATOM   1429 O  O   . ALA A 1 189 ? -11.107 -28.812 15.210  1.00 43.78  ? 184 ALA A O   1 
ATOM   1430 C  CB  . ALA A 1 189 ? -11.359 -28.607 12.302  1.00 37.61  ? 184 ALA A CB  1 
ATOM   1431 N  N   . ASN A 1 190 ? -10.004 -26.884 14.901  1.00 40.05  ? 185 ASN A N   1 
ATOM   1432 C  CA  . ASN A 1 190 ? -9.073  -27.111 15.995  1.00 42.11  ? 185 ASN A CA  1 
ATOM   1433 C  C   . ASN A 1 190 ? -8.464  -28.521 15.967  1.00 41.53  ? 185 ASN A C   1 
ATOM   1434 O  O   . ASN A 1 190 ? -8.414  -29.237 16.983  1.00 43.21  ? 185 ASN A O   1 
ATOM   1435 C  CB  . ASN A 1 190 ? -9.751  -26.758 17.298  1.00 47.11  ? 185 ASN A CB  1 
ATOM   1436 C  CG  . ASN A 1 190 ? -8.750  -26.632 18.390  1.00 49.64  ? 185 ASN A CG  1 
ATOM   1437 O  OD1 . ASN A 1 190 ? -7.595  -26.226 18.152  1.00 52.46  ? 185 ASN A OD1 1 
ATOM   1438 N  ND2 . ASN A 1 190 ? -9.136  -27.004 19.576  1.00 51.94  ? 185 ASN A ND2 1 
ATOM   1439 N  N   . SER A 1 191 ? -7.953  -28.879 14.770  1.00 41.89  ? 186 SER A N   1 
ATOM   1440 C  CA  . SER A 1 191 ? -7.183  -30.089 14.536  1.00 43.84  ? 186 SER A CA  1 
ATOM   1441 C  C   . SER A 1 191 ? -5.795  -29.675 14.072  1.00 43.41  ? 186 SER A C   1 
ATOM   1442 O  O   . SER A 1 191 ? -5.496  -29.780 12.888  1.00 44.31  ? 186 SER A O   1 
ATOM   1443 C  CB  . SER A 1 191 ? -7.790  -30.977 13.456  1.00 45.77  ? 186 SER A CB  1 
ATOM   1444 O  OG  . SER A 1 191 ? -9.160  -31.235 13.637  1.00 52.30  ? 186 SER A OG  1 
ATOM   1445 N  N   . PRO A 1 192 ? -4.918  -29.186 14.976  1.00 46.35  ? 187 PRO A N   1 
ATOM   1446 C  CA  . PRO A 1 192 ? -3.592  -28.718 14.567  1.00 46.89  ? 187 PRO A CA  1 
ATOM   1447 C  C   . PRO A 1 192 ? -2.750  -29.809 13.914  1.00 47.45  ? 187 PRO A C   1 
ATOM   1448 O  O   . PRO A 1 192 ? -1.964  -29.521 13.011  1.00 45.69  ? 187 PRO A O   1 
ATOM   1449 C  CB  . PRO A 1 192 ? -2.941  -28.248 15.864  1.00 49.91  ? 187 PRO A CB  1 
ATOM   1450 C  CG  . PRO A 1 192 ? -4.064  -28.182 16.927  1.00 50.51  ? 187 PRO A CG  1 
ATOM   1451 C  CD  . PRO A 1 192 ? -5.155  -29.109 16.435  1.00 48.58  ? 187 PRO A CD  1 
ATOM   1452 N  N   . GLU A 1 193 ? -2.911  -31.059 14.372  1.00 48.43  ? 188 GLU A N   1 
ATOM   1453 C  CA  . GLU A 1 193 ? -2.122  -32.153 13.823  1.00 51.03  ? 188 GLU A CA  1 
ATOM   1454 C  C   . GLU A 1 193 ? -2.472  -32.417 12.356  1.00 48.62  ? 188 GLU A C   1 
ATOM   1455 O  O   . GLU A 1 193 ? -1.568  -32.610 11.542  1.00 46.08  ? 188 GLU A O   1 
ATOM   1456 C  CB  . GLU A 1 193 ? -2.268  -33.435 14.654  1.00 55.46  ? 188 GLU A CB  1 
ATOM   1457 C  CG  . GLU A 1 193 ? -1.774  -33.305 16.082  1.00 61.54  ? 188 GLU A CG  1 
ATOM   1458 C  CD  . GLU A 1 193 ? -2.783  -32.779 17.095  1.00 65.44  ? 188 GLU A CD  1 
ATOM   1459 O  OE1 . GLU A 1 193 ? -3.850  -32.243 16.700  1.00 65.84  ? 188 GLU A OE1 1 
ATOM   1460 O  OE2 . GLU A 1 193 ? -2.499  -32.931 18.306  1.00 68.16  ? 188 GLU A OE2 1 
ATOM   1461 N  N   . GLU A 1 194 ? -3.774  -32.421 12.025  1.00 46.32  ? 189 GLU A N   1 
ATOM   1462 C  CA  . GLU A 1 194 ? -4.223  -32.583 10.648  1.00 47.85  ? 189 GLU A CA  1 
ATOM   1463 C  C   . GLU A 1 194 ? -3.772  -31.434 9.747   1.00 44.63  ? 189 GLU A C   1 
ATOM   1464 O  O   . GLU A 1 194 ? -3.467  -31.648 8.572   1.00 43.40  ? 189 GLU A O   1 
ATOM   1465 C  CB  . GLU A 1 194 ? -5.750  -32.672 10.578  1.00 51.17  ? 189 GLU A CB  1 
ATOM   1466 C  CG  . GLU A 1 194 ? -6.328  -34.013 10.971  1.00 55.29  ? 189 GLU A CG  1 
ATOM   1467 C  CD  . GLU A 1 194 ? -7.833  -34.064 10.809  1.00 57.33  ? 189 GLU A CD  1 
ATOM   1468 O  OE1 . GLU A 1 194 ? -8.549  -33.448 11.630  1.00 59.09  ? 189 GLU A OE1 1 
ATOM   1469 O  OE2 . GLU A 1 194 ? -8.296  -34.690 9.831   1.00 65.19  ? 189 GLU A OE2 1 
ATOM   1470 N  N   . ALA A 1 195 ? -3.764  -30.219 10.310  1.00 41.79  ? 190 ALA A N   1 
ATOM   1471 C  CA  . ALA A 1 195 ? -3.343  -29.024 9.597   1.00 40.85  ? 190 ALA A CA  1 
ATOM   1472 C  C   . ALA A 1 195 ? -1.887  -29.136 9.149   1.00 40.71  ? 190 ALA A C   1 
ATOM   1473 O  O   . ALA A 1 195 ? -1.582  -28.978 7.957   1.00 39.45  ? 190 ALA A O   1 
ATOM   1474 C  CB  . ALA A 1 195 ? -3.536  -27.790 10.459  1.00 39.38  ? 190 ALA A CB  1 
ATOM   1475 N  N   . ILE A 1 196 ? -1.019  -29.455 10.118  1.00 40.50  ? 191 ILE A N   1 
ATOM   1476 C  CA  . ILE A 1 196 ? 0.416   -29.560 9.909   1.00 41.55  ? 191 ILE A CA  1 
ATOM   1477 C  C   . ILE A 1 196 ? 0.717   -30.695 8.941   1.00 42.98  ? 191 ILE A C   1 
ATOM   1478 O  O   . ILE A 1 196 ? 1.488   -30.529 7.993   1.00 44.73  ? 191 ILE A O   1 
ATOM   1479 C  CB  . ILE A 1 196 ? 1.138   -29.750 11.278  1.00 42.46  ? 191 ILE A CB  1 
ATOM   1480 C  CG1 . ILE A 1 196 ? 0.959   -28.499 12.140  1.00 43.50  ? 191 ILE A CG1 1 
ATOM   1481 C  CG2 . ILE A 1 196 ? 2.610   -30.072 11.090  1.00 45.26  ? 191 ILE A CG2 1 
ATOM   1482 C  CD1 . ILE A 1 196 ? 1.303   -28.692 13.637  1.00 44.71  ? 191 ILE A CD1 1 
ATOM   1483 N  N   . SER A 1 197 ? 0.077   -31.840 9.183   1.00 44.01  ? 192 SER A N   1 
ATOM   1484 C  CA  . SER A 1 197 ? 0.248   -33.009 8.340   1.00 45.53  ? 192 SER A CA  1 
ATOM   1485 C  C   . SER A 1 197 ? -0.080  -32.714 6.874   1.00 43.48  ? 192 SER A C   1 
ATOM   1486 O  O   . SER A 1 197 ? 0.682   -33.053 5.968   1.00 44.11  ? 192 SER A O   1 
ATOM   1487 C  CB  . SER A 1 197 ? -0.617  -34.140 8.873   1.00 49.78  ? 192 SER A CB  1 
ATOM   1488 O  OG  . SER A 1 197 ? -0.483  -35.284 8.051   1.00 53.96  ? 192 SER A OG  1 
ATOM   1489 N  N   . LEU A 1 198 ? -1.228  -32.076 6.642   1.00 41.19  ? 193 LEU A N   1 
ATOM   1490 C  CA  . LEU A 1 198 ? -1.628  -31.744 5.286   1.00 39.09  ? 193 LEU A CA  1 
ATOM   1491 C  C   . LEU A 1 198 ? -0.690  -30.724 4.639   1.00 37.58  ? 193 LEU A C   1 
ATOM   1492 O  O   . LEU A 1 198 ? -0.276  -30.884 3.481   1.00 37.29  ? 193 LEU A O   1 
ATOM   1493 C  CB  . LEU A 1 198 ? -3.080  -31.232 5.301   1.00 38.09  ? 193 LEU A CB  1 
ATOM   1494 C  CG  . LEU A 1 198 ? -3.599  -30.757 3.914   1.00 36.97  ? 193 LEU A CG  1 
ATOM   1495 C  CD1 . LEU A 1 198 ? -3.523  -31.874 2.913   1.00 37.93  ? 193 LEU A CD1 1 
ATOM   1496 C  CD2 . LEU A 1 198 ? -5.038  -30.218 4.019   1.00 35.83  ? 193 LEU A CD2 1 
ATOM   1497 N  N   . ALA A 1 199 ? -0.337  -29.672 5.385   1.00 36.41  ? 194 ALA A N   1 
ATOM   1498 C  CA  . ALA A 1 199 ? 0.517   -28.625 4.845   1.00 35.87  ? 194 ALA A CA  1 
ATOM   1499 C  C   . ALA A 1 199 ? 1.894   -29.179 4.475   1.00 37.21  ? 194 ALA A C   1 
ATOM   1500 O  O   . ALA A 1 199 ? 2.397   -28.925 3.386   1.00 37.39  ? 194 ALA A O   1 
ATOM   1501 C  CB  . ALA A 1 199 ? 0.634   -27.454 5.814   1.00 36.57  ? 194 ALA A CB  1 
ATOM   1502 N  N   . LYS A 1 200 ? 2.473   -29.998 5.353   1.00 40.38  ? 195 LYS A N   1 
ATOM   1503 C  CA  . LYS A 1 200 ? 3.787   -30.577 5.142   1.00 42.08  ? 195 LYS A CA  1 
ATOM   1504 C  C   . LYS A 1 200 ? 3.784   -31.555 3.972   1.00 42.05  ? 195 LYS A C   1 
ATOM   1505 O  O   . LYS A 1 200 ? 4.697   -31.528 3.155   1.00 43.22  ? 195 LYS A O   1 
ATOM   1506 C  CB  . LYS A 1 200 ? 4.255   -31.287 6.428   1.00 45.23  ? 195 LYS A CB  1 
ATOM   1507 C  CG  . LYS A 1 200 ? 5.746   -31.564 6.456   1.00 52.66  ? 195 LYS A CG  1 
ATOM   1508 C  CD  . LYS A 1 200 ? 6.128   -32.646 7.492   1.00 55.58  ? 195 LYS A CD  1 
ATOM   1509 C  CE  . LYS A 1 200 ? 6.363   -34.014 6.864   1.00 58.36  ? 195 LYS A CE  1 
ATOM   1510 N  NZ  . LYS A 1 200 ? 7.531   -33.994 5.929   1.00 60.22  ? 195 LYS A NZ  1 
ATOM   1511 N  N   . THR A 1 201 ? 2.756   -32.408 3.890   1.00 41.61  ? 196 THR A N   1 
ATOM   1512 C  CA  . THR A 1 201 ? 2.651   -33.366 2.800   1.00 43.55  ? 196 THR A CA  1 
ATOM   1513 C  C   . THR A 1 201 ? 2.490   -32.661 1.455   1.00 41.56  ? 196 THR A C   1 
ATOM   1514 O  O   . THR A 1 201 ? 3.124   -33.019 0.453   1.00 41.53  ? 196 THR A O   1 
ATOM   1515 C  CB  . THR A 1 201 ? 1.475   -34.317 3.024   1.00 46.26  ? 196 THR A CB  1 
ATOM   1516 O  OG1 . THR A 1 201 ? 1.783   -35.163 4.091   1.00 49.23  ? 196 THR A OG1 1 
ATOM   1517 C  CG2 . THR A 1 201 ? 1.171   -35.188 1.792   1.00 47.64  ? 196 THR A CG2 1 
ATOM   1518 N  N   . THR A 1 202 ? 1.618   -31.655 1.438   1.00 38.62  ? 197 THR A N   1 
ATOM   1519 C  CA  . THR A 1 202 ? 1.390   -30.883 0.230   1.00 36.80  ? 197 THR A CA  1 
ATOM   1520 C  C   . THR A 1 202 ? 2.701   -30.253 -0.239  1.00 36.78  ? 197 THR A C   1 
ATOM   1521 O  O   . THR A 1 202 ? 3.056   -30.291 -1.430  1.00 35.74  ? 197 THR A O   1 
ATOM   1522 C  CB  . THR A 1 202 ? 0.317   -29.827 0.468   1.00 36.33  ? 197 THR A CB  1 
ATOM   1523 O  OG1 . THR A 1 202 ? -0.917  -30.425 0.882   1.00 34.74  ? 197 THR A OG1 1 
ATOM   1524 C  CG2 . THR A 1 202 ? 0.075   -29.014 -0.777  1.00 34.96  ? 197 THR A CG2 1 
ATOM   1525 N  N   . PHE A 1 203 ? 3.431   -29.657 0.704   1.00 36.70  ? 198 PHE A N   1 
ATOM   1526 C  CA  . PHE A 1 203 ? 4.671   -28.981 0.358   1.00 37.69  ? 198 PHE A CA  1 
ATOM   1527 C  C   . PHE A 1 203 ? 5.705   -29.953 -0.205  1.00 36.93  ? 198 PHE A C   1 
ATOM   1528 O  O   . PHE A 1 203 ? 6.284   -29.697 -1.263  1.00 36.38  ? 198 PHE A O   1 
ATOM   1529 C  CB  . PHE A 1 203 ? 5.239   -28.249 1.565   1.00 37.86  ? 198 PHE A CB  1 
ATOM   1530 C  CG  . PHE A 1 203 ? 6.427   -27.375 1.270   1.00 37.68  ? 198 PHE A CG  1 
ATOM   1531 C  CD1 . PHE A 1 203 ? 7.688   -27.924 1.103   1.00 41.21  ? 198 PHE A CD1 1 
ATOM   1532 C  CD2 . PHE A 1 203 ? 6.285   -26.008 1.149   1.00 38.96  ? 198 PHE A CD2 1 
ATOM   1533 C  CE1 . PHE A 1 203 ? 8.789   -27.118 0.837   1.00 40.41  ? 198 PHE A CE1 1 
ATOM   1534 C  CE2 . PHE A 1 203 ? 7.381   -25.195 0.869   1.00 40.12  ? 198 PHE A CE2 1 
ATOM   1535 C  CZ  . PHE A 1 203 ? 8.630   -25.751 0.712   1.00 40.48  ? 198 PHE A CZ  1 
ATOM   1536 N  N   . ASP A 1 204 ? 5.908   -31.068 0.502   1.00 37.29  ? 199 ASP A N   1 
ATOM   1537 C  CA  . ASP A 1 204 ? 6.905   -32.065 0.150   1.00 38.04  ? 199 ASP A CA  1 
ATOM   1538 C  C   . ASP A 1 204 ? 6.622   -32.700 -1.210  1.00 36.44  ? 199 ASP A C   1 
ATOM   1539 O  O   . ASP A 1 204 ? 7.547   -32.879 -1.976  1.00 37.98  ? 199 ASP A O   1 
ATOM   1540 C  CB  . ASP A 1 204 ? 6.991   -33.155 1.216   1.00 40.83  ? 199 ASP A CB  1 
ATOM   1541 C  CG  . ASP A 1 204 ? 7.565   -32.657 2.510   1.00 42.94  ? 199 ASP A CG  1 
ATOM   1542 O  OD1 . ASP A 1 204 ? 8.133   -31.542 2.514   1.00 46.67  ? 199 ASP A OD1 1 
ATOM   1543 O  OD2 . ASP A 1 204 ? 7.426   -33.371 3.538   1.00 45.77  ? 199 ASP A OD2 1 
ATOM   1544 N  N   . GLU A 1 205 ? 5.353   -33.023 -1.487  1.00 36.75  ? 200 GLU A N   1 
ATOM   1545 C  CA  . GLU A 1 205 ? 4.965   -33.651 -2.739  1.00 39.31  ? 200 GLU A CA  1 
ATOM   1546 C  C   . GLU A 1 205 ? 5.095   -32.691 -3.916  1.00 37.63  ? 200 GLU A C   1 
ATOM   1547 O  O   . GLU A 1 205 ? 5.355   -33.110 -5.046  1.00 36.79  ? 200 GLU A O   1 
ATOM   1548 C  CB  . GLU A 1 205 ? 3.525   -34.180 -2.643  1.00 42.93  ? 200 GLU A CB  1 
ATOM   1549 C  CG  . GLU A 1 205 ? 3.392   -35.351 -1.691  1.00 44.95  ? 200 GLU A CG  1 
ATOM   1550 C  CD  . GLU A 1 205 ? 2.043   -36.035 -1.658  1.00 47.84  ? 200 GLU A CD  1 
ATOM   1551 O  OE1 . GLU A 1 205 ? 1.058   -35.491 -2.208  1.00 48.83  ? 200 GLU A OE1 1 
ATOM   1552 O  OE2 . GLU A 1 205 ? 1.978   -37.140 -1.073  1.00 53.29  ? 200 GLU A OE2 1 
ATOM   1553 N  N   . ALA A 1 206 ? 4.936   -31.394 -3.652  1.00 36.23  ? 201 ALA A N   1 
ATOM   1554 C  CA  . ALA A 1 206 ? 5.162   -30.394 -4.681  1.00 35.60  ? 201 ALA A CA  1 
ATOM   1555 C  C   . ALA A 1 206 ? 6.650   -30.125 -4.914  1.00 35.54  ? 201 ALA A C   1 
ATOM   1556 O  O   . ALA A 1 206 ? 7.083   -29.992 -6.048  1.00 33.95  ? 201 ALA A O   1 
ATOM   1557 C  CB  . ALA A 1 206 ? 4.448   -29.102 -4.317  1.00 35.23  ? 201 ALA A CB  1 
ATOM   1558 N  N   . MET A 1 207 ? 7.432   -29.978 -3.837  1.00 37.71  ? 202 MET A N   1 
ATOM   1559 C  CA  . MET A 1 207 ? 8.862   -29.702 -3.961  1.00 38.16  ? 202 MET A CA  1 
ATOM   1560 C  C   . MET A 1 207 ? 9.461   -30.738 -4.914  1.00 40.13  ? 202 MET A C   1 
ATOM   1561 O  O   . MET A 1 207 ? 10.243  -30.425 -5.827  1.00 40.57  ? 202 MET A O   1 
ATOM   1562 C  CB  . MET A 1 207 ? 9.512   -29.707 -2.534  1.00 41.37  ? 202 MET A CB  1 
ATOM   1563 C  CG  . MET A 1 207 ? 11.029  -29.444 -2.504  1.00 45.90  ? 202 MET A CG  1 
ATOM   1564 S  SD  . MET A 1 207 ? 11.546  -27.742 -2.939  1.00 51.89  ? 202 MET A SD  1 
ATOM   1565 C  CE  . MET A 1 207 ? 11.016  -26.870 -1.616  1.00 56.40  ? 202 MET A CE  1 
ATOM   1566 N  N   . ALA A 1 208 ? 8.988   -31.974 -4.772  1.00 42.81  ? 203 ALA A N   1 
ATOM   1567 C  CA  . ALA A 1 208 ? 9.470   -33.073 -5.587  1.00 43.52  ? 203 ALA A CA  1 
ATOM   1568 C  C   . ALA A 1 208 ? 9.536   -32.755 -7.078  1.00 41.99  ? 203 ALA A C   1 
ATOM   1569 O  O   . ALA A 1 208 ? 10.445  -33.272 -7.712  1.00 42.84  ? 203 ALA A O   1 
ATOM   1570 C  CB  . ALA A 1 208 ? 8.615   -34.322 -5.353  1.00 46.66  ? 203 ALA A CB  1 
ATOM   1571 N  N   . ASP A 1 209 ? 8.591   -31.935 -7.600  1.00 42.07  ? 204 ASP A N   1 
ATOM   1572 C  CA  . ASP A 1 209 ? 8.429   -31.639 -9.026  1.00 40.30  ? 204 ASP A CA  1 
ATOM   1573 C  C   . ASP A 1 209 ? 8.890   -30.271 -9.535  1.00 39.06  ? 204 ASP A C   1 
ATOM   1574 O  O   . ASP A 1 209 ? 8.769   -29.978 -10.731 1.00 39.27  ? 204 ASP A O   1 
ATOM   1575 C  CB  . ASP A 1 209 ? 6.931   -31.705 -9.422  1.00 42.03  ? 204 ASP A CB  1 
ATOM   1576 C  CG  . ASP A 1 209 ? 6.295   -33.077 -9.439  1.00 46.32  ? 204 ASP A CG  1 
ATOM   1577 O  OD1 . ASP A 1 209 ? 7.025   -34.070 -9.234  1.00 49.74  ? 204 ASP A OD1 1 
ATOM   1578 O  OD2 . ASP A 1 209 ? 5.050   -33.160 -9.637  1.00 47.37  ? 204 ASP A OD2 1 
ATOM   1579 N  N   . LEU A 1 210 ? 9.399   -29.414 -8.645  1.00 35.53  ? 205 LEU A N   1 
ATOM   1580 C  CA  . LEU A 1 210 ? 9.721   -28.052 -9.047  1.00 33.20  ? 205 LEU A CA  1 
ATOM   1581 C  C   . LEU A 1 210 ? 10.843  -27.957 -10.083 1.00 31.76  ? 205 LEU A C   1 
ATOM   1582 O  O   . LEU A 1 210 ? 10.858  -27.004 -10.861 1.00 32.75  ? 205 LEU A O   1 
ATOM   1583 C  CB  . LEU A 1 210 ? 10.105  -27.226 -7.834  1.00 31.65  ? 205 LEU A CB  1 
ATOM   1584 C  CG  . LEU A 1 210 ? 8.981   -26.955 -6.849  1.00 32.93  ? 205 LEU A CG  1 
ATOM   1585 C  CD1 . LEU A 1 210 ? 9.496   -26.188 -5.659  1.00 33.11  ? 205 LEU A CD1 1 
ATOM   1586 C  CD2 . LEU A 1 210 ? 7.834   -26.174 -7.461  1.00 31.97  ? 205 LEU A CD2 1 
ATOM   1587 N  N   . HIS A 1 211 ? 11.760  -28.939 -10.091 1.00 31.68  ? 206 HIS A N   1 
ATOM   1588 C  CA  . HIS A 1 211 ? 12.908  -28.930 -10.987 1.00 31.71  ? 206 HIS A CA  1 
ATOM   1589 C  C   . HIS A 1 211 ? 12.482  -29.128 -12.438 1.00 32.19  ? 206 HIS A C   1 
ATOM   1590 O  O   . HIS A 1 211 ? 13.276  -28.874 -13.345 1.00 33.12  ? 206 HIS A O   1 
ATOM   1591 C  CB  . HIS A 1 211 ? 13.985  -29.955 -10.599 1.00 30.82  ? 206 HIS A CB  1 
ATOM   1592 C  CG  . HIS A 1 211 ? 14.583  -29.676 -9.242  1.00 30.14  ? 206 HIS A CG  1 
ATOM   1593 N  ND1 . HIS A 1 211 ? 15.302  -28.512 -8.997  1.00 30.05  ? 206 HIS A ND1 1 
ATOM   1594 C  CD2 . HIS A 1 211 ? 14.515  -30.386 -8.089  1.00 30.79  ? 206 HIS A CD2 1 
ATOM   1595 C  CE1 . HIS A 1 211 ? 15.643  -28.546 -7.712  1.00 30.29  ? 206 HIS A CE1 1 
ATOM   1596 N  NE2 . HIS A 1 211 ? 15.211  -29.668 -7.135  1.00 30.93  ? 206 HIS A NE2 1 
ATOM   1597 N  N   . THR A 1 212 ? 11.227  -29.561 -12.649 1.00 34.86  ? 207 THR A N   1 
ATOM   1598 C  CA  . THR A 1 212 ? 10.687  -29.742 -13.997 1.00 35.21  ? 207 THR A CA  1 
ATOM   1599 C  C   . THR A 1 212 ? 9.990   -28.508 -14.569 1.00 34.09  ? 207 THR A C   1 
ATOM   1600 O  O   . THR A 1 212 ? 9.671   -28.483 -15.756 1.00 37.48  ? 207 THR A O   1 
ATOM   1601 C  CB  . THR A 1 212 ? 9.692   -30.922 -14.038 1.00 37.86  ? 207 THR A CB  1 
ATOM   1602 O  OG1 . THR A 1 212 ? 8.462   -30.556 -13.393 1.00 39.71  ? 207 THR A OG1 1 
ATOM   1603 C  CG2 . THR A 1 212 ? 10.248  -32.199 -13.351 1.00 40.66  ? 207 THR A CG2 1 
ATOM   1604 N  N   . LEU A 1 213 ? 9.818   -27.457 -13.768 1.00 33.70  ? 208 LEU A N   1 
ATOM   1605 C  CA  . LEU A 1 213 ? 8.974   -26.334 -14.146 1.00 32.51  ? 208 LEU A CA  1 
ATOM   1606 C  C   . LEU A 1 213 ? 9.746   -25.196 -14.805 1.00 31.95  ? 208 LEU A C   1 
ATOM   1607 O  O   . LEU A 1 213 ? 10.878  -24.892 -14.445 1.00 33.01  ? 208 LEU A O   1 
ATOM   1608 C  CB  . LEU A 1 213 ? 8.261   -25.789 -12.899 1.00 32.62  ? 208 LEU A CB  1 
ATOM   1609 C  CG  . LEU A 1 213 ? 7.301   -26.737 -12.219 1.00 34.76  ? 208 LEU A CG  1 
ATOM   1610 C  CD1 . LEU A 1 213 ? 6.552   -26.032 -11.064 1.00 34.61  ? 208 LEU A CD1 1 
ATOM   1611 C  CD2 . LEU A 1 213 ? 6.290   -27.343 -13.191 1.00 36.89  ? 208 LEU A CD2 1 
ATOM   1612 N  N   . SER A 1 214 ? 9.107   -24.579 -15.800 1.00 33.90  ? 209 SER A N   1 
ATOM   1613 C  CA  . SER A 1 214 ? 9.525   -23.294 -16.327 1.00 37.52  ? 209 SER A CA  1 
ATOM   1614 C  C   . SER A 1 214 ? 9.458   -22.207 -15.264 1.00 37.77  ? 209 SER A C   1 
ATOM   1615 O  O   . SER A 1 214 ? 8.773   -22.353 -14.255 1.00 38.10  ? 209 SER A O   1 
ATOM   1616 C  CB  . SER A 1 214 ? 8.624   -22.893 -17.500 1.00 40.19  ? 209 SER A CB  1 
ATOM   1617 O  OG  . SER A 1 214 ? 7.327   -22.519 -17.032 1.00 43.84  ? 209 SER A OG  1 
ATOM   1618 N  N   . GLU A 1 215 ? 10.167  -21.116 -15.536 1.00 39.22  ? 210 GLU A N   1 
ATOM   1619 C  CA  . GLU A 1 215 ? 10.188  -19.925 -14.704 1.00 43.45  ? 210 GLU A CA  1 
ATOM   1620 C  C   . GLU A 1 215 ? 8.799   -19.510 -14.211 1.00 44.02  ? 210 GLU A C   1 
ATOM   1621 O  O   . GLU A 1 215 ? 8.574   -19.376 -13.007 1.00 44.35  ? 210 GLU A O   1 
ATOM   1622 C  CB  . GLU A 1 215 ? 10.894  -18.849 -15.558 1.00 48.87  ? 210 GLU A CB  1 
ATOM   1623 C  CG  . GLU A 1 215 ? 10.911  -17.421 -15.062 1.00 53.71  ? 210 GLU A CG  1 
ATOM   1624 C  CD  . GLU A 1 215 ? 11.539  -16.459 -16.069 1.00 56.41  ? 210 GLU A CD  1 
ATOM   1625 O  OE1 . GLU A 1 215 ? 12.155  -16.916 -17.066 1.00 63.20  ? 210 GLU A OE1 1 
ATOM   1626 O  OE2 . GLU A 1 215 ? 11.395  -15.234 -15.873 1.00 58.88  ? 210 GLU A OE2 1 
ATOM   1627 N  N   . ASP A 1 216 ? 7.856   -19.343 -15.141 1.00 45.28  ? 211 ASP A N   1 
ATOM   1628 C  CA  . ASP A 1 216 ? 6.524   -18.852 -14.812 1.00 46.06  ? 211 ASP A CA  1 
ATOM   1629 C  C   . ASP A 1 216 ? 5.689   -19.828 -13.984 1.00 42.00  ? 211 ASP A C   1 
ATOM   1630 O  O   . ASP A 1 216 ? 5.056   -19.420 -13.011 1.00 42.31  ? 211 ASP A O   1 
ATOM   1631 C  CB  . ASP A 1 216 ? 5.786   -18.475 -16.109 1.00 49.88  ? 211 ASP A CB  1 
ATOM   1632 C  CG  . ASP A 1 216 ? 6.412   -17.280 -16.789 1.00 54.72  ? 211 ASP A CG  1 
ATOM   1633 O  OD1 . ASP A 1 216 ? 6.696   -16.278 -16.093 1.00 60.02  ? 211 ASP A OD1 1 
ATOM   1634 O  OD2 . ASP A 1 216 ? 6.627   -17.344 -18.010 1.00 59.55  ? 211 ASP A OD2 1 
ATOM   1635 N  N   . SER A 1 217 ? 5.689   -21.109 -14.377 1.00 39.30  ? 212 SER A N   1 
ATOM   1636 C  CA  . SER A 1 217 ? 5.062   -22.162 -13.591 1.00 37.05  ? 212 SER A CA  1 
ATOM   1637 C  C   . SER A 1 217 ? 5.643   -22.196 -12.176 1.00 34.35  ? 212 SER A C   1 
ATOM   1638 O  O   . SER A 1 217 ? 4.902   -22.263 -11.194 1.00 35.50  ? 212 SER A O   1 
ATOM   1639 C  CB  . SER A 1 217 ? 5.226   -23.532 -14.254 1.00 37.76  ? 212 SER A CB  1 
ATOM   1640 O  OG  . SER A 1 217 ? 4.505   -23.594 -15.482 1.00 44.22  ? 212 SER A OG  1 
ATOM   1641 N  N   . TYR A 1 218 ? 6.970   -22.144 -12.088 1.00 33.41  ? 213 TYR A N   1 
ATOM   1642 C  CA  . TYR A 1 218 ? 7.646   -22.192 -10.802 1.00 32.51  ? 213 TYR A CA  1 
ATOM   1643 C  C   . TYR A 1 218 ? 7.185   -21.063 -9.882  1.00 34.43  ? 213 TYR A C   1 
ATOM   1644 O  O   . TYR A 1 218 ? 6.914   -21.296 -8.687  1.00 34.39  ? 213 TYR A O   1 
ATOM   1645 C  CB  . TYR A 1 218 ? 9.156   -22.127 -11.018 1.00 32.22  ? 213 TYR A CB  1 
ATOM   1646 C  CG  . TYR A 1 218 ? 9.961   -22.117 -9.756  1.00 31.43  ? 213 TYR A CG  1 
ATOM   1647 C  CD1 . TYR A 1 218 ? 10.332  -23.304 -9.135  1.00 31.82  ? 213 TYR A CD1 1 
ATOM   1648 C  CD2 . TYR A 1 218 ? 10.371  -20.920 -9.180  1.00 31.40  ? 213 TYR A CD2 1 
ATOM   1649 C  CE1 . TYR A 1 218 ? 11.071  -23.296 -7.954  1.00 30.93  ? 213 TYR A CE1 1 
ATOM   1650 C  CE2 . TYR A 1 218 ? 11.127  -20.904 -8.028  1.00 31.06  ? 213 TYR A CE2 1 
ATOM   1651 C  CZ  . TYR A 1 218 ? 11.465  -22.093 -7.416  1.00 31.74  ? 213 TYR A CZ  1 
ATOM   1652 O  OH  . TYR A 1 218 ? 12.222  -22.065 -6.279  1.00 33.29  ? 213 TYR A OH  1 
ATOM   1653 N  N   . LYS A 1 219 ? 7.107   -19.849 -10.442 1.00 35.43  ? 214 LYS A N   1 
ATOM   1654 C  CA  . LYS A 1 219 ? 6.676   -18.688 -9.681  1.00 38.92  ? 214 LYS A CA  1 
ATOM   1655 C  C   . LYS A 1 219 ? 5.259   -18.874 -9.144  1.00 37.57  ? 214 LYS A C   1 
ATOM   1656 O  O   . LYS A 1 219 ? 5.019   -18.600 -7.973  1.00 40.32  ? 214 LYS A O   1 
ATOM   1657 C  CB  . LYS A 1 219 ? 6.757   -17.394 -10.475 1.00 42.10  ? 214 LYS A CB  1 
ATOM   1658 C  CG  . LYS A 1 219 ? 8.171   -16.838 -10.562 1.00 49.31  ? 214 LYS A CG  1 
ATOM   1659 C  CD  . LYS A 1 219 ? 8.211   -15.472 -11.276 1.00 55.65  ? 214 LYS A CD  1 
ATOM   1660 C  CE  . LYS A 1 219 ? 9.506   -15.233 -12.030 1.00 58.41  ? 214 LYS A CE  1 
ATOM   1661 N  NZ  . LYS A 1 219 ? 9.340   -14.189 -13.078 1.00 61.49  ? 214 LYS A NZ  1 
ATOM   1662 N  N   . ASP A 1 220 ? 4.337   -19.365 -9.985  1.00 37.83  ? 215 ASP A N   1 
ATOM   1663 C  CA  . ASP A 1 220 ? 2.958   -19.589 -9.570  1.00 36.96  ? 215 ASP A CA  1 
ATOM   1664 C  C   . ASP A 1 220 ? 2.839   -20.636 -8.463  1.00 36.43  ? 215 ASP A C   1 
ATOM   1665 O  O   . ASP A 1 220 ? 2.079   -20.453 -7.507  1.00 38.48  ? 215 ASP A O   1 
ATOM   1666 C  CB  . ASP A 1 220 ? 2.105   -20.023 -10.773 1.00 39.25  ? 215 ASP A CB  1 
ATOM   1667 C  CG  . ASP A 1 220 ? 1.890   -18.945 -11.821 1.00 43.29  ? 215 ASP A CG  1 
ATOM   1668 O  OD1 . ASP A 1 220 ? 2.049   -17.747 -11.486 1.00 44.76  ? 215 ASP A OD1 1 
ATOM   1669 O  OD2 . ASP A 1 220 ? 1.586   -19.305 -13.002 1.00 47.76  ? 215 ASP A OD2 1 
ATOM   1670 N  N   . SER A 1 221 ? 3.599   -21.727 -8.582  1.00 33.24  ? 216 SER A N   1 
ATOM   1671 C  CA  . SER A 1 221 ? 3.549   -22.789 -7.590  1.00 31.81  ? 216 SER A CA  1 
ATOM   1672 C  C   . SER A 1 221 ? 4.193   -22.368 -6.266  1.00 32.07  ? 216 SER A C   1 
ATOM   1673 O  O   . SER A 1 221 ? 3.608   -22.627 -5.224  1.00 31.61  ? 216 SER A O   1 
ATOM   1674 C  CB  . SER A 1 221 ? 4.180   -24.072 -8.112  1.00 32.47  ? 216 SER A CB  1 
ATOM   1675 O  OG  . SER A 1 221 ? 3.487   -24.557 -9.257  1.00 33.01  ? 216 SER A OG  1 
ATOM   1676 N  N   . THR A 1 222 ? 5.375   -21.734 -6.319  1.00 32.07  ? 217 THR A N   1 
ATOM   1677 C  CA  . THR A 1 222 ? 6.112   -21.389 -5.112  1.00 33.87  ? 217 THR A CA  1 
ATOM   1678 C  C   . THR A 1 222 ? 5.467   -20.246 -4.334  1.00 35.41  ? 217 THR A C   1 
ATOM   1679 O  O   . THR A 1 222 ? 5.667   -20.155 -3.121  1.00 36.03  ? 217 THR A O   1 
ATOM   1680 C  CB  . THR A 1 222 ? 7.583   -21.109 -5.402  1.00 35.02  ? 217 THR A CB  1 
ATOM   1681 O  OG1 . THR A 1 222 ? 7.688   -20.094 -6.370  1.00 36.57  ? 217 THR A OG1 1 
ATOM   1682 C  CG2 . THR A 1 222 ? 8.296   -22.331 -5.844  1.00 34.63  ? 217 THR A CG2 1 
ATOM   1683 N  N   . LEU A 1 223 ? 4.682   -19.391 -5.007  1.00 35.95  ? 218 LEU A N   1 
ATOM   1684 C  CA  . LEU A 1 223 ? 3.897   -18.393 -4.288  1.00 39.01  ? 218 LEU A CA  1 
ATOM   1685 C  C   . LEU A 1 223 ? 3.065   -19.051 -3.187  1.00 37.09  ? 218 LEU A C   1 
ATOM   1686 O  O   . LEU A 1 223 ? 3.035   -18.595 -2.037  1.00 36.74  ? 218 LEU A O   1 
ATOM   1687 C  CB  . LEU A 1 223 ? 2.946   -17.651 -5.232  1.00 41.91  ? 218 LEU A CB  1 
ATOM   1688 C  CG  . LEU A 1 223 ? 2.133   -16.517 -4.592  1.00 45.45  ? 218 LEU A CG  1 
ATOM   1689 C  CD1 . LEU A 1 223 ? 2.992   -15.275 -4.374  1.00 47.54  ? 218 LEU A CD1 1 
ATOM   1690 C  CD2 . LEU A 1 223 ? 0.928   -16.167 -5.429  1.00 47.73  ? 218 LEU A CD2 1 
ATOM   1691 N  N   . ILE A 1 224 ? 2.368   -20.126 -3.567  1.00 33.89  ? 219 ILE A N   1 
ATOM   1692 C  CA  . ILE A 1 224 ? 1.488   -20.815 -2.648  1.00 34.61  ? 219 ILE A CA  1 
ATOM   1693 C  C   . ILE A 1 224 ? 2.323   -21.654 -1.679  1.00 33.30  ? 219 ILE A C   1 
ATOM   1694 O  O   . ILE A 1 224 ? 2.026   -21.708 -0.480  1.00 34.12  ? 219 ILE A O   1 
ATOM   1695 C  CB  . ILE A 1 224 ? 0.447   -21.625 -3.404  1.00 34.63  ? 219 ILE A CB  1 
ATOM   1696 C  CG1 . ILE A 1 224 ? -0.387  -20.703 -4.330  1.00 36.87  ? 219 ILE A CG1 1 
ATOM   1697 C  CG2 . ILE A 1 224 ? -0.436  -22.397 -2.429  1.00 33.73  ? 219 ILE A CG2 1 
ATOM   1698 C  CD1 . ILE A 1 224 ? -1.218  -21.359 -5.106  1.00 39.12  ? 219 ILE A CD1 1 
ATOM   1699 N  N   . MET A 1 225 ? 3.380   -22.294 -2.192  1.00 33.20  ? 220 MET A N   1 
ATOM   1700 C  CA  . MET A 1 225 ? 4.220   -23.140 -1.352  1.00 33.09  ? 220 MET A CA  1 
ATOM   1701 C  C   . MET A 1 225 ? 4.830   -22.340 -0.203  1.00 34.16  ? 220 MET A C   1 
ATOM   1702 O  O   . MET A 1 225 ? 4.992   -22.877 0.890   1.00 34.10  ? 220 MET A O   1 
ATOM   1703 C  CB  . MET A 1 225 ? 5.320   -23.861 -2.159  1.00 33.78  ? 220 MET A CB  1 
ATOM   1704 C  CG  . MET A 1 225 ? 4.756   -24.997 -2.998  1.00 35.48  ? 220 MET A CG  1 
ATOM   1705 S  SD  . MET A 1 225 ? 5.985   -25.723 -4.042  1.00 37.49  ? 220 MET A SD  1 
ATOM   1706 C  CE  . MET A 1 225 ? 6.875   -26.716 -2.827  1.00 37.44  ? 220 MET A CE  1 
ATOM   1707 N  N   . GLN A 1 226 ? 5.144   -21.060 -0.437  1.00 33.62  ? 221 GLN A N   1 
ATOM   1708 C  CA  . GLN A 1 226 ? 5.734   -20.234 0.603   1.00 34.95  ? 221 GLN A CA  1 
ATOM   1709 C  C   . GLN A 1 226 ? 4.737   -20.009 1.741   1.00 33.11  ? 221 GLN A C   1 
ATOM   1710 O  O   . GLN A 1 226 ? 5.138   -19.970 2.899   1.00 35.35  ? 221 GLN A O   1 
ATOM   1711 C  CB  . GLN A 1 226 ? 6.192   -18.891 0.055   1.00 38.18  ? 221 GLN A CB  1 
ATOM   1712 C  CG  . GLN A 1 226 ? 6.934   -18.021 1.063   1.00 40.51  ? 221 GLN A CG  1 
ATOM   1713 C  CD  . GLN A 1 226 ? 8.139   -18.726 1.662   1.00 43.10  ? 221 GLN A CD  1 
ATOM   1714 O  OE1 . GLN A 1 226 ? 9.047   -19.168 0.972   1.00 45.89  ? 221 GLN A OE1 1 
ATOM   1715 N  NE2 . GLN A 1 226 ? 8.173   -18.868 2.972   1.00 46.71  ? 221 GLN A NE2 1 
ATOM   1716 N  N   . LEU A 1 227 ? 3.452   -19.864 1.397   1.00 32.08  ? 222 LEU A N   1 
ATOM   1717 C  CA  . LEU A 1 227 ? 2.396   -19.692 2.384   1.00 33.34  ? 222 LEU A CA  1 
ATOM   1718 C  C   . LEU A 1 227 ? 2.226   -20.935 3.265   1.00 33.79  ? 222 LEU A C   1 
ATOM   1719 O  O   . LEU A 1 227 ? 1.989   -20.811 4.476   1.00 33.69  ? 222 LEU A O   1 
ATOM   1720 C  CB  . LEU A 1 227 ? 1.070   -19.327 1.667   1.00 33.46  ? 222 LEU A CB  1 
ATOM   1721 C  CG  . LEU A 1 227 ? 1.073   -17.996 0.865   1.00 33.70  ? 222 LEU A CG  1 
ATOM   1722 C  CD1 . LEU A 1 227 ? -0.235  -17.808 0.124   1.00 33.64  ? 222 LEU A CD1 1 
ATOM   1723 C  CD2 . LEU A 1 227 ? 1.359   -16.793 1.772   1.00 34.70  ? 222 LEU A CD2 1 
ATOM   1724 N  N   . LEU A 1 228 ? 2.322   -22.128 2.656   1.00 33.30  ? 223 LEU A N   1 
ATOM   1725 C  CA  . LEU A 1 228 ? 2.293   -23.371 3.417   1.00 33.92  ? 223 LEU A CA  1 
ATOM   1726 C  C   . LEU A 1 228 ? 3.437   -23.375 4.424   1.00 36.99  ? 223 LEU A C   1 
ATOM   1727 O  O   . LEU A 1 228 ? 3.235   -23.702 5.602   1.00 40.27  ? 223 LEU A O   1 
ATOM   1728 C  CB  . LEU A 1 228 ? 2.437   -24.603 2.529   1.00 33.69  ? 223 LEU A CB  1 
ATOM   1729 C  CG  . LEU A 1 228 ? 1.327   -24.867 1.564   1.00 34.05  ? 223 LEU A CG  1 
ATOM   1730 C  CD1 . LEU A 1 228 ? 1.780   -25.901 0.488   1.00 35.56  ? 223 LEU A CD1 1 
ATOM   1731 C  CD2 . LEU A 1 228 ? 0.098   -25.355 2.254   1.00 34.46  ? 223 LEU A CD2 1 
ATOM   1732 N  N   . ARG A 1 229 ? 4.626   -22.982 3.951   1.00 39.11  ? 224 ARG A N   1 
ATOM   1733 C  CA  . ARG A 1 229 ? 5.799   -22.844 4.801   1.00 42.08  ? 224 ARG A CA  1 
ATOM   1734 C  C   . ARG A 1 229 ? 5.577   -21.841 5.932   1.00 41.43  ? 224 ARG A C   1 
ATOM   1735 O  O   . ARG A 1 229 ? 5.934   -22.112 7.079   1.00 43.56  ? 224 ARG A O   1 
ATOM   1736 C  CB  . ARG A 1 229 ? 7.006   -22.414 3.921   1.00 45.33  ? 224 ARG A CB  1 
ATOM   1737 C  CG  . ARG A 1 229 ? 8.338   -22.194 4.635   1.00 48.13  ? 224 ARG A CG  1 
ATOM   1738 C  CD  . ARG A 1 229 ? 8.758   -23.406 5.424   1.00 55.21  ? 224 ARG A CD  1 
ATOM   1739 N  NE  . ARG A 1 229 ? 8.699   -24.652 4.661   1.00 60.56  ? 224 ARG A NE  1 
ATOM   1740 C  CZ  . ARG A 1 229 ? 8.549   -25.860 5.203   1.00 62.69  ? 224 ARG A CZ  1 
ATOM   1741 N  NH1 . ARG A 1 229 ? 8.694   -26.060 6.507   1.00 63.72  ? 224 ARG A NH1 1 
ATOM   1742 N  NH2 . ARG A 1 229 ? 8.239   -26.890 4.416   1.00 59.48  ? 224 ARG A NH2 1 
ATOM   1743 N  N   . ASP A 1 230 ? 5.017   -20.671 5.595   1.00 40.51  ? 225 ASP A N   1 
ATOM   1744 C  CA  . ASP A 1 230 ? 4.761   -19.625 6.575   1.00 42.27  ? 225 ASP A CA  1 
ATOM   1745 C  C   . ASP A 1 230 ? 3.833   -20.115 7.685   1.00 42.54  ? 225 ASP A C   1 
ATOM   1746 O  O   . ASP A 1 230 ? 4.075   -19.828 8.856   1.00 43.42  ? 225 ASP A O   1 
ATOM   1747 C  CB  . ASP A 1 230 ? 4.129   -18.390 5.929   1.00 43.07  ? 225 ASP A CB  1 
ATOM   1748 C  CG  . ASP A 1 230 ? 5.015   -17.603 4.977   1.00 44.75  ? 225 ASP A CG  1 
ATOM   1749 O  OD1 . ASP A 1 230 ? 6.272   -17.791 5.028   1.00 45.51  ? 225 ASP A OD1 1 
ATOM   1750 O  OD2 . ASP A 1 230 ? 4.458   -16.804 4.168   1.00 44.23  ? 225 ASP A OD2 1 
ATOM   1751 N  N   . ASN A 1 231 ? 2.759   -20.817 7.290   1.00 40.27  ? 226 ASN A N   1 
ATOM   1752 C  CA  . ASN A 1 231 ? 1.852   -21.445 8.235   1.00 39.34  ? 226 ASN A CA  1 
ATOM   1753 C  C   . ASN A 1 231 ? 2.558   -22.501 9.079   1.00 41.90  ? 226 ASN A C   1 
ATOM   1754 O  O   . ASN A 1 231 ? 2.350   -22.545 10.289  1.00 40.69  ? 226 ASN A O   1 
ATOM   1755 C  CB  . ASN A 1 231 ? 0.631   -22.020 7.527   1.00 36.60  ? 226 ASN A CB  1 
ATOM   1756 C  CG  . ASN A 1 231 ? -0.317  -20.946 7.036   1.00 34.60  ? 226 ASN A CG  1 
ATOM   1757 O  OD1 . ASN A 1 231 ? -0.277  -19.778 7.485   1.00 36.61  ? 226 ASN A OD1 1 
ATOM   1758 N  ND2 . ASN A 1 231 ? -1.200  -21.301 6.096   1.00 32.64  ? 226 ASN A ND2 1 
ATOM   1759 N  N   . LEU A 1 232 ? 3.394   -23.346 8.465   1.00 43.51  ? 227 LEU A N   1 
ATOM   1760 C  CA  . LEU A 1 232 ? 4.104   -24.355 9.248   1.00 47.61  ? 227 LEU A CA  1 
ATOM   1761 C  C   . LEU A 1 232 ? 4.984   -23.730 10.334  1.00 50.07  ? 227 LEU A C   1 
ATOM   1762 O  O   . LEU A 1 232 ? 5.040   -24.203 11.493  1.00 50.17  ? 227 LEU A O   1 
ATOM   1763 C  CB  . LEU A 1 232 ? 4.923   -25.250 8.289   1.00 49.42  ? 227 LEU A CB  1 
ATOM   1764 C  CG  . LEU A 1 232 ? 4.100   -26.280 7.503   1.00 48.51  ? 227 LEU A CG  1 
ATOM   1765 C  CD1 . LEU A 1 232 ? 4.919   -26.929 6.385   1.00 49.55  ? 227 LEU A CD1 1 
ATOM   1766 C  CD2 . LEU A 1 232 ? 3.546   -27.361 8.424   1.00 47.72  ? 227 LEU A CD2 1 
ATOM   1767 N  N   . THR A 1 233 ? 5.634   -22.611 9.991   1.00 48.98  ? 228 THR A N   1 
ATOM   1768 C  CA  . THR A 1 233 ? 6.414   -21.881 10.983  1.00 52.39  ? 228 THR A CA  1 
ATOM   1769 C  C   . THR A 1 233 ? 5.522   -21.410 12.132  1.00 53.18  ? 228 THR A C   1 
ATOM   1770 O  O   . THR A 1 233 ? 5.847   -21.574 13.309  1.00 52.94  ? 228 THR A O   1 
ATOM   1771 C  CB  . THR A 1 233 ? 7.167   -20.726 10.325  1.00 54.73  ? 228 THR A CB  1 
ATOM   1772 O  OG1 . THR A 1 233 ? 8.115   -21.271 9.405   1.00 56.09  ? 228 THR A OG1 1 
ATOM   1773 C  CG2 . THR A 1 233 ? 7.893   -19.848 11.337  1.00 55.70  ? 228 THR A CG2 1 
ATOM   1774 N  N   . LEU A 1 234 ? 4.377   -20.827 11.774  1.00 51.96  ? 229 LEU A N   1 
ATOM   1775 C  CA  . LEU A 1 234 ? 3.440   -20.319 12.756  1.00 51.79  ? 229 LEU A CA  1 
ATOM   1776 C  C   . LEU A 1 234 ? 2.930   -21.427 13.672  1.00 51.33  ? 229 LEU A C   1 
ATOM   1777 O  O   . LEU A 1 234 ? 2.816   -21.225 14.876  1.00 53.31  ? 229 LEU A O   1 
ATOM   1778 C  CB  . LEU A 1 234 ? 2.278   -19.672 12.016  1.00 51.24  ? 229 LEU A CB  1 
ATOM   1779 C  CG  . LEU A 1 234 ? 1.467   -18.659 12.764  1.00 53.43  ? 229 LEU A CG  1 
ATOM   1780 C  CD1 . LEU A 1 234 ? 2.275   -17.368 13.022  1.00 54.74  ? 229 LEU A CD1 1 
ATOM   1781 C  CD2 . LEU A 1 234 ? 0.186   -18.358 12.005  1.00 55.08  ? 229 LEU A CD2 1 
ATOM   1782 N  N   . TRP A 1 235 ? 2.638   -22.594 13.084  1.00 51.09  ? 230 TRP A N   1 
ATOM   1783 C  CA  . TRP A 1 235 ? 1.937   -23.678 13.757  1.00 50.86  ? 230 TRP A CA  1 
ATOM   1784 C  C   . TRP A 1 235 ? 2.809   -24.609 14.595  1.00 55.11  ? 230 TRP A C   1 
ATOM   1785 O  O   . TRP A 1 235 ? 2.287   -25.404 15.378  1.00 58.89  ? 230 TRP A O   1 
ATOM   1786 C  CB  . TRP A 1 235 ? 1.206   -24.522 12.707  1.00 47.91  ? 230 TRP A CB  1 
ATOM   1787 C  CG  . TRP A 1 235 ? 0.135   -23.785 11.968  1.00 42.79  ? 230 TRP A CG  1 
ATOM   1788 C  CD1 . TRP A 1 235 ? -0.399  -22.568 12.277  1.00 43.64  ? 230 TRP A CD1 1 
ATOM   1789 C  CD2 . TRP A 1 235 ? -0.536  -24.229 10.792  1.00 42.22  ? 230 TRP A CD2 1 
ATOM   1790 N  NE1 . TRP A 1 235 ? -1.343  -22.216 11.341  1.00 42.88  ? 230 TRP A NE1 1 
ATOM   1791 C  CE2 . TRP A 1 235 ? -1.461  -23.229 10.430  1.00 41.68  ? 230 TRP A CE2 1 
ATOM   1792 C  CE3 . TRP A 1 235 ? -0.441  -25.378 9.996   1.00 42.79  ? 230 TRP A CE3 1 
ATOM   1793 C  CZ2 . TRP A 1 235 ? -2.290  -23.349 9.320   1.00 40.18  ? 230 TRP A CZ2 1 
ATOM   1794 C  CZ3 . TRP A 1 235 ? -1.262  -25.491 8.891   1.00 39.52  ? 230 TRP A CZ3 1 
ATOM   1795 C  CH2 . TRP A 1 235 ? -2.176  -24.489 8.566   1.00 40.53  ? 230 TRP A CH2 1 
ATOM   1796 N  N   . THR A 1 236 ? 4.129   -24.511 14.421  1.00 58.63  ? 231 THR A N   1 
ATOM   1797 C  CA  . THR A 1 236 ? 5.070   -25.323 15.172  1.00 65.03  ? 231 THR A CA  1 
ATOM   1798 C  C   . THR A 1 236 ? 5.763   -24.460 16.216  1.00 68.83  ? 231 THR A C   1 
ATOM   1799 O  O   . THR A 1 236 ? 6.632   -24.940 16.943  1.00 71.01  ? 231 THR A O   1 
ATOM   1800 C  CB  . THR A 1 236 ? 6.044   -25.993 14.223  1.00 68.88  ? 231 THR A CB  1 
ATOM   1801 O  OG1 . THR A 1 236 ? 6.714   -24.979 13.463  1.00 73.52  ? 231 THR A OG1 1 
ATOM   1802 C  CG2 . THR A 1 236 ? 5.345   -26.985 13.292  1.00 71.78  ? 231 THR A CG2 1 
ATOM   1803 O  OXT . THR A 1 236 ? 5.440   -23.278 16.342  1.00 70.70  ? 231 THR A OXT 1 
ATOM   1804 N  N   . ASP B 2 1   ? -0.947  -14.678 15.679  1.00 61.40  ? 361 ASP P N   1 
ATOM   1805 C  CA  . ASP B 2 1   ? -1.207  -14.258 14.296  1.00 59.08  ? 361 ASP P CA  1 
ATOM   1806 C  C   . ASP B 2 1   ? -2.088  -15.265 13.567  1.00 54.11  ? 361 ASP P C   1 
ATOM   1807 O  O   . ASP B 2 1   ? -2.059  -16.456 13.859  1.00 54.30  ? 361 ASP P O   1 
ATOM   1808 C  CB  . ASP B 2 1   ? 0.088   -14.077 13.496  1.00 64.23  ? 361 ASP P CB  1 
ATOM   1809 C  CG  . ASP B 2 1   ? 0.823   -12.787 13.757  1.00 69.66  ? 361 ASP P CG  1 
ATOM   1810 O  OD1 . ASP B 2 1   ? 0.548   -12.147 14.788  1.00 73.27  ? 361 ASP P OD1 1 
ATOM   1811 O  OD2 . ASP B 2 1   ? 1.659   -12.404 12.916  1.00 75.29  ? 361 ASP P OD2 1 
ATOM   1812 N  N   . ARG B 2 2   ? -2.848  -14.760 12.594  1.00 50.94  ? 362 ARG P N   1 
ATOM   1813 C  CA  . ARG B 2 2   ? -3.753  -15.574 11.803  1.00 47.47  ? 362 ARG P CA  1 
ATOM   1814 C  C   . ARG B 2 2   ? -3.000  -16.268 10.671  1.00 42.64  ? 362 ARG P C   1 
ATOM   1815 O  O   . ARG B 2 2   ? -2.022  -15.738 10.164  1.00 41.18  ? 362 ARG P O   1 
ATOM   1816 C  CB  . ARG B 2 2   ? -4.879  -14.694 11.263  1.00 47.67  ? 362 ARG P CB  1 
ATOM   1817 C  CG  . ARG B 2 2   ? -5.663  -13.998 12.378  1.00 52.51  ? 362 ARG P CG  1 
ATOM   1818 C  CD  . ARG B 2 2   ? -6.853  -13.280 11.812  1.00 56.30  ? 362 ARG P CD  1 
ATOM   1819 N  NE  . ARG B 2 2   ? -7.909  -13.084 12.795  1.00 56.39  ? 362 ARG P NE  1 
ATOM   1820 C  CZ  . ARG B 2 2   ? -8.653  -14.053 13.322  1.00 57.41  ? 362 ARG P CZ  1 
ATOM   1821 N  NH1 . ARG B 2 2   ? -8.473  -15.327 13.002  1.00 54.75  ? 362 ARG P NH1 1 
ATOM   1822 N  NH2 . ARG B 2 2   ? -9.590  -13.735 14.208  1.00 61.04  ? 362 ARG P NH2 1 
ATOM   1823 N  N   . SER B 2 3   ? -3.446  -17.481 10.325  1.00 40.41  ? 363 SER P N   1 
ATOM   1824 C  CA  . SER B 2 3   ? -2.847  -18.253 9.253   1.00 38.42  ? 363 SER P CA  1 
ATOM   1825 C  C   . SER B 2 3   ? -3.104  -17.577 7.912   1.00 37.44  ? 363 SER P C   1 
ATOM   1826 O  O   . SER B 2 3   ? -4.114  -16.901 7.736   1.00 37.61  ? 363 SER P O   1 
ATOM   1827 C  CB  . SER B 2 3   ? -3.414  -19.670 9.223   1.00 39.53  ? 363 SER P CB  1 
ATOM   1828 O  OG  . SER B 2 3   ? -3.422  -20.245 10.514  1.00 40.35  ? 363 SER P OG  1 
ATOM   1829 N  N   . SER B 2 4   ? -2.186  -17.787 6.969   1.00 33.86  ? 364 SER P N   1 
ATOM   1830 C  CA  . SER B 2 4   ? -2.367  -17.293 5.606   1.00 33.40  ? 364 SER P CA  1 
ATOM   1831 C  C   . SER B 2 4   ? -3.160  -18.264 4.734   1.00 29.93  ? 364 SER P C   1 
ATOM   1832 O  O   . SER B 2 4   ? -2.918  -19.471 4.785   1.00 29.54  ? 364 SER P O   1 
ATOM   1833 C  CB  . SER B 2 4   ? -1.006  -17.032 4.971   1.00 35.23  ? 364 SER P CB  1 
ATOM   1834 O  OG  . SER B 2 4   ? -0.222  -16.192 5.798   1.00 38.64  ? 364 SER P OG  1 
HETATM 1835 N  N   . SEP B 2 5   ? -4.069  -17.726 3.899   1.00 28.76  ? 365 SEP P N   1 
HETATM 1836 C  CA  . SEP B 2 5   ? -4.821  -18.539 2.957   1.00 27.77  ? 365 SEP P CA  1 
HETATM 1837 C  CB  . SEP B 2 5   ? -6.318  -18.451 3.237   1.00 26.50  ? 365 SEP P CB  1 
HETATM 1838 O  OG  . SEP B 2 5   ? -6.767  -17.077 3.096   1.00 25.77  ? 365 SEP P OG  1 
HETATM 1839 C  C   . SEP B 2 5   ? -4.457  -18.114 1.535   1.00 27.52  ? 365 SEP P C   1 
HETATM 1840 O  O   . SEP B 2 5   ? -3.644  -17.209 1.341   1.00 29.72  ? 365 SEP P O   1 
HETATM 1841 P  P   . SEP B 2 5   ? -8.311  -16.751 3.376   1.00 25.97  ? 365 SEP P P   1 
HETATM 1842 O  O1P . SEP B 2 5   ? -9.128  -17.625 2.453   1.00 26.05  ? 365 SEP P O1P 1 
HETATM 1843 O  O2P . SEP B 2 5   ? -8.544  -17.021 4.856   1.00 27.16  ? 365 SEP P O2P 1 
HETATM 1844 O  O3P . SEP B 2 5   ? -8.451  -15.283 3.105   1.00 26.04  ? 365 SEP P O3P 1 
ATOM   1845 N  N   . ALA B 2 6   ? -5.045  -18.806 0.555   1.00 27.24  ? 366 ALA P N   1 
ATOM   1846 C  CA  . ALA B 2 6   ? -4.708  -18.596 -0.843  1.00 28.98  ? 366 ALA P CA  1 
ATOM   1847 C  C   . ALA B 2 6   ? -5.078  -17.183 -1.313  1.00 29.86  ? 366 ALA P C   1 
ATOM   1848 O  O   . ALA B 2 6   ? -6.151  -16.667 -1.012  1.00 28.63  ? 366 ALA P O   1 
ATOM   1849 C  CB  . ALA B 2 6   ? -5.410  -19.646 -1.687  1.00 29.77  ? 366 ALA P CB  1 
ATOM   1850 N  N   . PRO B 2 7   ? -4.169  -16.473 -2.002  1.00 31.55  ? 367 PRO P N   1 
ATOM   1851 C  CA  . PRO B 2 7   ? -4.438  -15.108 -2.454  1.00 34.04  ? 367 PRO P CA  1 
ATOM   1852 C  C   . PRO B 2 7   ? -5.307  -15.077 -3.706  1.00 38.47  ? 367 PRO P C   1 
ATOM   1853 O  O   . PRO B 2 7   ? -5.403  -16.089 -4.391  1.00 38.43  ? 367 PRO P O   1 
ATOM   1854 C  CB  . PRO B 2 7   ? -3.021  -14.577 -2.743  1.00 34.89  ? 367 PRO P CB  1 
ATOM   1855 C  CG  . PRO B 2 7   ? -2.276  -15.773 -3.181  1.00 34.66  ? 367 PRO P CG  1 
ATOM   1856 C  CD  . PRO B 2 7   ? -2.795  -16.901 -2.308  1.00 34.51  ? 367 PRO P CD  1 
ATOM   1857 N  N   . ASN B 2 8   ? -5.948  -13.932 -3.979  1.00 45.06  ? 368 ASN P N   1 
ATOM   1858 C  CA  A ASN B 2 8   ? -6.590  -13.694 -5.268  0.50 48.39  ? 368 ASN P CA  1 
ATOM   1859 C  CA  B ASN B 2 8   ? -6.608  -13.675 -5.258  0.50 48.82  ? 368 ASN P CA  1 
ATOM   1860 C  C   . ASN B 2 8   ? -5.828  -12.600 -6.006  1.00 51.36  ? 368 ASN P C   1 
ATOM   1861 O  O   . ASN B 2 8   ? -5.407  -11.624 -5.406  1.00 57.76  ? 368 ASN P O   1 
ATOM   1862 C  CB  A ASN B 2 8   ? -8.100  -13.349 -5.137  0.50 50.14  ? 368 ASN P CB  1 
ATOM   1863 C  CB  B ASN B 2 8   ? -8.079  -13.216 -5.096  0.50 52.41  ? 368 ASN P CB  1 
ATOM   1864 C  CG  A ASN B 2 8   ? -8.457  -12.186 -4.225  0.50 49.22  ? 368 ASN P CG  1 
ATOM   1865 C  CG  B ASN B 2 8   ? -9.131  -14.264 -5.430  0.50 53.86  ? 368 ASN P CG  1 
ATOM   1866 O  OD1 A ASN B 2 8   ? -9.275  -11.310 -4.553  0.50 46.63  ? 368 ASN P OD1 1 
ATOM   1867 O  OD1 B ASN B 2 8   ? -9.145  -14.865 -6.494  0.50 54.40  ? 368 ASN P OD1 1 
ATOM   1868 N  ND2 A ASN B 2 8   ? -7.910  -12.177 -3.037  0.50 49.83  ? 368 ASN P ND2 1 
ATOM   1869 N  ND2 B ASN B 2 8   ? -10.049 -14.503 -4.530  0.50 57.21  ? 368 ASN P ND2 1 
ATOM   1870 N  N   . VAL B 2 9   ? -5.660  -12.775 -7.326  1.00 56.72  ? 369 VAL P N   1 
ATOM   1871 C  CA  . VAL B 2 9   ? -4.935  -11.820 -8.152  1.00 59.48  ? 369 VAL P CA  1 
ATOM   1872 C  C   . VAL B 2 9   ? -5.648  -10.434 -8.215  1.00 57.92  ? 369 VAL P C   1 
ATOM   1873 O  O   . VAL B 2 9   ? -5.036  -9.385  -7.983  1.00 55.03  ? 369 VAL P O   1 
ATOM   1874 C  CB  . VAL B 2 9   ? -4.729  -12.395 -9.587  1.00 63.22  ? 369 VAL P CB  1 
ATOM   1875 C  CG1 . VAL B 2 9   ? -4.007  -11.389 -10.497 1.00 63.39  ? 369 VAL P CG1 1 
ATOM   1876 C  CG2 . VAL B 2 9   ? -3.993  -13.740 -9.554  1.00 63.87  ? 369 VAL P CG2 1 
ATOM   1877 O  OXT . VAL B 2 9   ? -6.824  -10.375 -8.543  1.00 60.49  ? 369 VAL P OXT 1 
HETATM 1878 CL CL  . CL  C 3 .   ? -24.857 -0.666  15.000  1.00 64.30  ? 301 CL  A CL  1 
HETATM 1879 MG MG  . MG  D 4 .   ? -25.540 -13.046 12.956  1.00 52.75  2 302 MG  A MG  1 
HETATM 1880 CL CL  . CL  E 3 .   ? -28.096 -12.209 -24.896 1.00 97.06  ? 303 CL  A CL  1 
HETATM 1881 O  O   . HOH F 5 .   ? -8.308  -38.807 -5.082  1.00 56.85  ? 401 HOH A O   1 
HETATM 1882 O  O   . HOH F 5 .   ? -21.937 -26.733 -20.371 1.00 50.33  ? 402 HOH A O   1 
HETATM 1883 O  O   . HOH F 5 .   ? -24.737 -12.013 -24.363 1.00 46.90  ? 403 HOH A O   1 
HETATM 1884 O  O   . HOH F 5 .   ? 5.300   -21.693 -18.032 1.00 62.56  ? 404 HOH A O   1 
HETATM 1885 O  O   . HOH F 5 .   ? -26.760 -8.679  -28.433 1.00 61.93  ? 405 HOH A O   1 
HETATM 1886 O  O   . HOH F 5 .   ? 11.383  -31.856 -9.430  1.00 43.64  ? 406 HOH A O   1 
HETATM 1887 O  O   . HOH F 5 .   ? -15.843 -1.961  -3.248  1.00 48.19  ? 407 HOH A O   1 
HETATM 1888 O  O   . HOH F 5 .   ? -12.838 -3.298  -19.649 1.00 50.83  ? 408 HOH A O   1 
HETATM 1889 O  O   . HOH F 5 .   ? 5.414   -17.841 9.620   1.00 54.66  ? 409 HOH A O   1 
HETATM 1890 O  O   . HOH F 5 .   ? 2.104   -18.649 -15.375 1.00 58.54  ? 410 HOH A O   1 
HETATM 1891 O  O   . HOH F 5 .   ? -16.097 -27.239 -19.067 1.00 46.51  ? 411 HOH A O   1 
HETATM 1892 O  O   . HOH F 5 .   ? -9.337  -4.105  -9.176  1.00 47.02  ? 412 HOH A O   1 
HETATM 1893 O  O   . HOH F 5 .   ? 8.455   -19.082 -17.781 1.00 45.32  ? 413 HOH A O   1 
HETATM 1894 O  O   . HOH F 5 .   ? -10.271 -22.182 -12.955 1.00 42.66  ? 414 HOH A O   1 
HETATM 1895 O  O   . HOH F 5 .   ? -16.296 -1.924  -21.789 1.00 48.48  ? 415 HOH A O   1 
HETATM 1896 O  O   . HOH F 5 .   ? -0.093  -33.225 -2.537  1.00 36.40  ? 416 HOH A O   1 
HETATM 1897 O  O   . HOH F 5 .   ? -27.104 -22.520 9.260   1.00 39.07  ? 417 HOH A O   1 
HETATM 1898 O  O   . HOH F 5 .   ? -15.565 -14.555 8.462   1.00 30.89  ? 418 HOH A O   1 
HETATM 1899 O  O   . HOH F 5 .   ? -26.958 -9.183  -9.340  1.00 38.91  ? 419 HOH A O   1 
HETATM 1900 O  O   . HOH F 5 .   ? -16.437 -13.286 -21.338 1.00 45.85  ? 420 HOH A O   1 
HETATM 1901 O  O   . HOH F 5 .   ? -6.931  -13.452 7.257   1.00 62.00  ? 421 HOH A O   1 
HETATM 1902 O  O   . HOH F 5 .   ? -23.959 -31.172 10.389  1.00 50.71  ? 422 HOH A O   1 
HETATM 1903 O  O   . HOH F 5 .   ? -27.973 -14.460 5.144   1.00 51.73  ? 423 HOH A O   1 
HETATM 1904 O  O   . HOH F 5 .   ? -29.247 -12.703 -14.979 1.00 44.90  ? 424 HOH A O   1 
HETATM 1905 O  O   . HOH F 5 .   ? 3.572   -31.234 -10.824 1.00 39.51  ? 425 HOH A O   1 
HETATM 1906 O  O   . HOH F 5 .   ? -11.466 -24.828 -16.795 1.00 58.43  ? 426 HOH A O   1 
HETATM 1907 O  O   . HOH F 5 .   ? -11.456 -6.170  0.748   1.00 54.41  ? 427 HOH A O   1 
HETATM 1908 O  O   . HOH F 5 .   ? -25.688 -3.785  7.306   1.00 51.36  ? 428 HOH A O   1 
HETATM 1909 O  O   . HOH F 5 .   ? -20.434 -14.249 16.488  1.00 38.45  ? 429 HOH A O   1 
HETATM 1910 O  O   . HOH F 5 .   ? -9.055  -6.881  10.957  1.00 35.07  ? 430 HOH A O   1 
HETATM 1911 O  O   . HOH F 5 .   ? -16.969 -5.142  2.153   1.00 34.34  ? 431 HOH A O   1 
HETATM 1912 O  O   . HOH F 5 .   ? -11.437 -4.326  -1.426  1.00 46.60  ? 432 HOH A O   1 
HETATM 1913 O  O   . HOH F 5 .   ? 12.644  -24.300 -4.909  1.00 46.10  ? 433 HOH A O   1 
HETATM 1914 O  O   . HOH F 5 .   ? 5.057   -35.677 -5.669  1.00 43.96  ? 434 HOH A O   1 
HETATM 1915 O  O   . HOH F 5 .   ? -23.503 -17.785 -17.317 1.00 34.08  ? 435 HOH A O   1 
HETATM 1916 O  O   . HOH F 5 .   ? 6.285   -16.669 -6.647  1.00 47.31  ? 436 HOH A O   1 
HETATM 1917 O  O   . HOH F 5 .   ? -3.033  -36.090 -10.381 1.00 54.50  ? 437 HOH A O   1 
HETATM 1918 O  O   . HOH F 5 .   ? -12.519 -0.406  -3.493  1.00 45.87  ? 438 HOH A O   1 
HETATM 1919 O  O   . HOH F 5 .   ? -18.483 -22.717 -14.871 1.00 30.27  ? 439 HOH A O   1 
HETATM 1920 O  O   . HOH F 5 .   ? -20.830 -3.802  23.801  1.00 49.41  ? 440 HOH A O   1 
HETATM 1921 O  O   . HOH F 5 .   ? -10.861 -31.404 10.523  1.00 54.37  ? 441 HOH A O   1 
HETATM 1922 O  O   . HOH F 5 .   ? 8.450   -23.722 8.357   1.00 62.11  ? 442 HOH A O   1 
HETATM 1923 O  O   . HOH F 5 .   ? -11.134 -5.810  -15.540 1.00 49.25  ? 443 HOH A O   1 
HETATM 1924 O  O   . HOH F 5 .   ? -8.899  1.258   -16.471 1.00 56.56  ? 444 HOH A O   1 
HETATM 1925 O  O   . HOH F 5 .   ? -21.194 -13.419 -22.281 1.00 39.62  ? 445 HOH A O   1 
HETATM 1926 O  O   . HOH F 5 .   ? -1.955  -32.441 -0.588  1.00 39.44  ? 446 HOH A O   1 
HETATM 1927 O  O   . HOH F 5 .   ? -13.589 -22.846 15.521  1.00 40.13  ? 447 HOH A O   1 
HETATM 1928 O  O   . HOH F 5 .   ? -10.072 -9.706  5.338   1.00 39.33  ? 448 HOH A O   1 
HETATM 1929 O  O   . HOH F 5 .   ? -23.688 -29.884 7.894   1.00 41.17  ? 449 HOH A O   1 
HETATM 1930 O  O   . HOH F 5 .   ? -17.000 -24.693 -16.093 1.00 36.12  ? 450 HOH A O   1 
HETATM 1931 O  O   . HOH F 5 .   ? -26.997 -4.684  15.299  1.00 39.91  ? 451 HOH A O   1 
HETATM 1932 O  O   . HOH F 5 .   ? -0.795  -24.255 5.662   1.00 36.33  ? 452 HOH A O   1 
HETATM 1933 O  O   . HOH F 5 .   ? -20.677 -29.256 1.702   1.00 34.64  ? 453 HOH A O   1 
HETATM 1934 O  O   . HOH F 5 .   ? -13.927 -15.867 -3.570  1.00 34.93  ? 454 HOH A O   1 
HETATM 1935 O  O   . HOH F 5 .   ? -29.292 -27.166 20.352  1.00 49.20  ? 455 HOH A O   1 
HETATM 1936 O  O   . HOH F 5 .   ? -20.856 -25.270 18.035  1.00 35.92  ? 456 HOH A O   1 
HETATM 1937 O  O   . HOH F 5 .   ? -11.742 -18.744 -5.444  1.00 38.16  ? 457 HOH A O   1 
HETATM 1938 O  O   . HOH F 5 .   ? 0.411   -36.385 -5.084  1.00 61.97  ? 458 HOH A O   1 
HETATM 1939 O  O   . HOH F 5 .   ? 4.057   -35.578 -10.424 1.00 57.35  ? 459 HOH A O   1 
HETATM 1940 O  O   . HOH F 5 .   ? -24.252 -18.669 14.441  1.00 32.08  ? 460 HOH A O   1 
HETATM 1941 O  O   . HOH F 5 .   ? -15.107 -37.353 -3.058  1.00 65.53  ? 461 HOH A O   1 
HETATM 1942 O  O   . HOH F 5 .   ? -24.550 -26.424 -8.426  1.00 48.05  ? 462 HOH A O   1 
HETATM 1943 O  O   . HOH F 5 .   ? -25.988 -28.423 14.147  1.00 46.53  ? 463 HOH A O   1 
HETATM 1944 O  O   . HOH F 5 .   ? -10.224 -11.547 3.839   1.00 46.84  ? 464 HOH A O   1 
HETATM 1945 O  O   . HOH F 5 .   ? -24.345 -26.721 19.438  1.00 41.69  ? 465 HOH A O   1 
HETATM 1946 O  O   . HOH F 5 .   ? -26.852 -20.156 0.581   1.00 43.91  ? 466 HOH A O   1 
HETATM 1947 O  O   . HOH F 5 .   ? -27.741 -13.029 -22.365 1.00 58.76  ? 467 HOH A O   1 
HETATM 1948 O  O   . HOH F 5 .   ? 2.270   -15.316 4.906   1.00 48.14  ? 468 HOH A O   1 
HETATM 1949 O  O   . HOH F 5 .   ? -22.899 -7.124  -4.512  1.00 36.34  ? 469 HOH A O   1 
HETATM 1950 O  O   . HOH F 5 .   ? -25.248 -8.958  3.057   1.00 33.66  ? 470 HOH A O   1 
HETATM 1951 O  O   . HOH F 5 .   ? -17.882 -31.910 -14.918 1.00 70.00  ? 471 HOH A O   1 
HETATM 1952 O  O   . HOH F 5 .   ? -19.255 -29.846 13.240  1.00 36.75  ? 472 HOH A O   1 
HETATM 1953 O  O   . HOH F 5 .   ? -19.980 -0.579  23.410  1.00 47.71  ? 473 HOH A O   1 
HETATM 1954 O  O   . HOH F 5 .   ? -23.860 -6.877  -24.881 1.00 59.90  ? 474 HOH A O   1 
HETATM 1955 O  O   . HOH F 5 .   ? 2.197   -26.983 -12.166 1.00 35.92  ? 475 HOH A O   1 
HETATM 1956 O  O   . HOH F 5 .   ? -12.797 -13.643 10.980  1.00 41.89  ? 476 HOH A O   1 
HETATM 1957 O  O   . HOH F 5 .   ? -24.104 -9.741  -4.738  1.00 33.97  ? 477 HOH A O   1 
HETATM 1958 O  O   . HOH F 5 .   ? -26.450 -5.891  8.785   1.00 36.47  ? 478 HOH A O   1 
HETATM 1959 O  O   . HOH F 5 .   ? 1.382   -17.542 7.747   1.00 47.70  ? 479 HOH A O   1 
HETATM 1960 O  O   . HOH F 5 .   ? 0.971   -16.433 -9.264  1.00 58.24  ? 480 HOH A O   1 
HETATM 1961 O  O   . HOH F 5 .   ? 4.730   -15.643 1.633   1.00 51.34  ? 481 HOH A O   1 
HETATM 1962 O  O   . HOH F 5 .   ? -7.051  -33.315 5.414   1.00 46.44  ? 482 HOH A O   1 
HETATM 1963 O  O   . HOH F 5 .   ? 12.505  -28.787 -5.572  1.00 40.74  ? 483 HOH A O   1 
HETATM 1964 O  O   . HOH F 5 .   ? 1.393   -31.060 -3.557  1.00 39.40  ? 484 HOH A O   1 
HETATM 1965 O  O   . HOH F 5 .   ? -9.927  -19.367 8.446   1.00 30.99  ? 485 HOH A O   1 
HETATM 1966 O  O   . HOH F 5 .   ? -13.177 -3.142  6.383   1.00 44.76  ? 486 HOH A O   1 
HETATM 1967 O  O   . HOH F 5 .   ? -16.980 -35.001 1.032   1.00 56.43  ? 487 HOH A O   1 
HETATM 1968 O  O   . HOH F 5 .   ? 2.575   -24.199 -11.904 1.00 36.46  ? 488 HOH A O   1 
HETATM 1969 O  O   . HOH F 5 .   ? -27.430 -16.539 -4.557  1.00 34.07  ? 489 HOH A O   1 
HETATM 1970 O  O   . HOH F 5 .   ? -24.630 -26.310 6.845   1.00 36.91  ? 490 HOH A O   1 
HETATM 1971 O  O   . HOH F 5 .   ? -18.598 -9.249  -22.720 1.00 39.94  ? 491 HOH A O   1 
HETATM 1972 O  O   . HOH F 5 .   ? -3.372  -31.962 -2.912  1.00 47.54  ? 492 HOH A O   1 
HETATM 1973 O  O   . HOH F 5 .   ? 14.454  -28.525 -15.913 1.00 48.32  ? 493 HOH A O   1 
HETATM 1974 O  O   . HOH F 5 .   ? -4.188  -34.086 7.259   1.00 56.45  ? 494 HOH A O   1 
HETATM 1975 O  O   . HOH F 5 .   ? -18.046 -33.264 7.286   1.00 51.81  ? 495 HOH A O   1 
HETATM 1976 O  O   . HOH F 5 .   ? -15.417 -3.932  -20.025 1.00 40.15  ? 496 HOH A O   1 
HETATM 1977 O  O   . HOH F 5 .   ? -8.793  -7.151  -6.245  1.00 43.69  ? 497 HOH A O   1 
HETATM 1978 O  O   . HOH F 5 .   ? -10.803 -10.766 16.343  1.00 49.81  ? 498 HOH A O   1 
HETATM 1979 O  O   . HOH F 5 .   ? -12.723 -35.090 5.183   1.00 65.62  ? 499 HOH A O   1 
HETATM 1980 O  O   . HOH F 5 .   ? -9.507  2.393   -9.829  1.00 56.69  ? 500 HOH A O   1 
HETATM 1981 O  O   . HOH F 5 .   ? -20.604 -24.041 -14.105 1.00 33.13  ? 501 HOH A O   1 
HETATM 1982 O  O   . HOH F 5 .   ? -11.428 -21.369 -5.722  1.00 28.40  ? 502 HOH A O   1 
HETATM 1983 O  O   . HOH F 5 .   ? -28.115 -28.323 12.683  1.00 47.06  ? 503 HOH A O   1 
HETATM 1984 O  O   . HOH F 5 .   ? -22.434 -21.774 -23.844 1.00 42.14  ? 504 HOH A O   1 
HETATM 1985 O  O   . HOH F 5 .   ? -0.263  -36.365 -7.647  1.00 54.04  ? 505 HOH A O   1 
HETATM 1986 O  O   . HOH F 5 .   ? -17.673 -11.433 19.068  1.00 56.13  ? 506 HOH A O   1 
HETATM 1987 O  O   . HOH F 5 .   ? -17.077 0.004   -4.335  1.00 44.28  ? 507 HOH A O   1 
HETATM 1988 O  O   . HOH F 5 .   ? 6.555   -25.599 -16.773 1.00 40.80  ? 508 HOH A O   1 
HETATM 1989 O  O   . HOH F 5 .   ? -23.843 -16.008 14.266  1.00 70.86  ? 509 HOH A O   1 
HETATM 1990 O  O   . HOH F 5 .   ? -16.053 -22.939 -18.943 1.00 39.73  ? 510 HOH A O   1 
HETATM 1991 O  O   . HOH F 5 .   ? -27.600 -23.176 18.586  1.00 37.39  ? 511 HOH A O   1 
HETATM 1992 O  O   . HOH F 5 .   ? -27.693 -12.485 6.946   1.00 32.95  ? 512 HOH A O   1 
HETATM 1993 O  O   . HOH F 5 .   ? -10.448 -12.114 -14.560 1.00 42.66  ? 513 HOH A O   1 
HETATM 1994 O  O   . HOH F 5 .   ? -10.080 -29.748 -16.137 1.00 48.51  ? 514 HOH A O   1 
HETATM 1995 O  O   . HOH F 5 .   ? 13.275  -25.947 -15.870 1.00 32.89  ? 515 HOH A O   1 
HETATM 1996 O  O   . HOH F 5 .   ? -10.719 -17.608 -19.754 1.00 34.99  ? 516 HOH A O   1 
HETATM 1997 O  O   . HOH F 5 .   ? -19.160 -1.211  -5.809  1.00 30.94  ? 517 HOH A O   1 
HETATM 1998 O  O   . HOH F 5 .   ? -16.295 -8.415  -21.839 1.00 45.91  ? 518 HOH A O   1 
HETATM 1999 O  O   . HOH F 5 .   ? -22.468 -18.110 10.476  1.00 28.00  ? 519 HOH A O   1 
HETATM 2000 O  O   . HOH F 5 .   ? -16.914 3.963   -4.635  1.00 40.41  ? 520 HOH A O   1 
HETATM 2001 O  O   . HOH F 5 .   ? -8.739  -6.675  -9.071  1.00 41.60  ? 521 HOH A O   1 
HETATM 2002 O  O   . HOH F 5 .   ? -23.920 -3.959  -9.971  1.00 37.63  ? 522 HOH A O   1 
HETATM 2003 O  O   . HOH F 5 .   ? -28.116 -5.789  -22.185 1.00 70.00  ? 523 HOH A O   1 
HETATM 2004 O  O   . HOH F 5 .   ? 8.797   -31.210 6.637   1.00 60.14  ? 524 HOH A O   1 
HETATM 2005 O  O   . HOH F 5 .   ? 13.836  -15.344 -19.211 1.00 38.23  ? 525 HOH A O   1 
HETATM 2006 O  O   . HOH F 5 .   ? -8.492  -20.462 -11.789 1.00 39.88  ? 526 HOH A O   1 
HETATM 2007 O  O   . HOH F 5 .   ? -0.359  -27.471 -13.206 1.00 41.11  ? 527 HOH A O   1 
HETATM 2008 O  O   . HOH F 5 .   ? 1.017   -22.472 -13.425 1.00 48.25  ? 528 HOH A O   1 
HETATM 2009 O  O   . HOH F 5 .   ? -24.751 -3.409  -7.647  1.00 55.46  ? 529 HOH A O   1 
HETATM 2010 O  O   . HOH F 5 .   ? -26.983 -22.423 -0.949  1.00 52.03  ? 530 HOH A O   1 
HETATM 2011 O  O   . HOH F 5 .   ? -21.333 -0.035  -4.608  1.00 46.23  ? 531 HOH A O   1 
HETATM 2012 O  O   . HOH F 5 .   ? -14.190 0.856   29.197  1.00 77.06  ? 532 HOH A O   1 
HETATM 2013 O  O   . HOH F 5 .   ? -2.702  -35.226 -12.808 1.00 66.49  ? 533 HOH A O   1 
HETATM 2014 O  O   . HOH F 5 .   ? -19.801 -30.617 -1.118  1.00 64.38  ? 534 HOH A O   1 
HETATM 2015 O  O   . HOH F 5 .   ? 3.304   -16.596 -15.423 1.00 61.07  ? 535 HOH A O   1 
HETATM 2016 O  O   . HOH F 5 .   ? 15.623  -16.327 -17.391 1.00 53.45  ? 536 HOH A O   1 
HETATM 2017 O  O   . HOH F 5 .   ? -15.554 -35.247 11.668  1.00 64.42  ? 537 HOH A O   1 
HETATM 2018 O  O   . HOH F 5 .   ? -6.932  -0.742  -10.764 1.00 66.19  ? 538 HOH A O   1 
HETATM 2019 O  O   . HOH F 5 .   ? -23.845 -6.682  2.243   1.00 44.62  ? 539 HOH A O   1 
HETATM 2020 O  O   . HOH F 5 .   ? 13.409  -26.528 -6.582  1.00 39.02  ? 540 HOH A O   1 
HETATM 2021 O  O   . HOH F 5 .   ? -24.607 -30.566 12.891  1.00 55.52  ? 541 HOH A O   1 
HETATM 2022 O  O   . HOH F 5 .   ? -27.723 -13.337 -27.604 1.00 82.74  ? 542 HOH A O   1 
HETATM 2023 O  O   . HOH F 5 .   ? -8.007  -8.914  9.344   1.00 38.52  ? 543 HOH A O   1 
HETATM 2024 O  O   . HOH F 5 .   ? -23.879 -10.202 -1.781  1.00 40.94  ? 544 HOH A O   1 
HETATM 2025 O  O   . HOH F 5 .   ? -8.008  -7.286  13.450  1.00 44.77  ? 545 HOH A O   1 
HETATM 2026 O  O   . HOH F 5 .   ? -30.153 -10.413 -24.099 1.00 80.36  ? 546 HOH A O   1 
HETATM 2027 O  O   . HOH F 5 .   ? -29.800 -12.234 11.083  1.00 51.80  ? 547 HOH A O   1 
HETATM 2028 O  O   . HOH F 5 .   ? -23.346 -13.918 -24.324 1.00 51.26  ? 548 HOH A O   1 
HETATM 2029 O  O   . HOH F 5 .   ? -15.148 -12.497 10.226  1.00 32.50  ? 549 HOH A O   1 
HETATM 2030 O  O   . HOH F 5 .   ? -27.597 -7.078  6.569   1.00 46.77  ? 550 HOH A O   1 
HETATM 2031 O  O   . HOH F 5 .   ? -25.669 -19.392 -24.746 1.00 48.30  ? 551 HOH A O   1 
HETATM 2032 O  O   . HOH F 5 .   ? -8.698  -21.613 -6.946  1.00 38.33  ? 552 HOH A O   1 
HETATM 2033 O  O   . HOH F 5 .   ? -27.576 -8.620  4.557   1.00 45.74  ? 553 HOH A O   1 
HETATM 2034 O  O   . HOH F 5 .   ? -26.402 -28.609 7.104   1.00 47.39  ? 554 HOH A O   1 
HETATM 2035 O  O   . HOH F 5 .   ? -29.084 -15.269 -3.255  1.00 42.22  ? 555 HOH A O   1 
HETATM 2036 O  O   . HOH F 5 .   ? 11.117  -31.310 -0.776  1.00 53.34  ? 556 HOH A O   1 
HETATM 2037 O  O   . HOH F 5 .   ? -8.321  -13.892 -15.120 1.00 46.75  ? 557 HOH A O   1 
HETATM 2038 O  O   . HOH F 5 .   ? -30.071 -23.741 -2.767  1.00 67.89  ? 558 HOH A O   1 
HETATM 2039 O  O   . HOH F 5 .   ? -14.934 -2.010  4.488   1.00 41.73  ? 559 HOH A O   1 
HETATM 2040 O  O   . HOH F 5 .   ? -5.946  -5.394  -6.191  1.00 72.94  ? 560 HOH A O   1 
HETATM 2041 O  O   . HOH F 5 .   ? -6.219  -20.603 -13.040 1.00 47.81  ? 561 HOH A O   1 
HETATM 2042 O  O   . HOH F 5 .   ? -29.017 -10.970 4.970   1.00 44.29  ? 562 HOH A O   1 
HETATM 2043 O  O   . HOH F 5 .   ? -10.736 -3.469  5.202   1.00 46.43  ? 563 HOH A O   1 
HETATM 2044 O  O   . HOH F 5 .   ? -29.347 -13.525 3.281   1.00 54.25  ? 564 HOH A O   1 
HETATM 2045 O  O   . HOH F 5 .   ? 3.667   -31.668 -13.497 1.00 50.27  ? 565 HOH A O   1 
HETATM 2046 O  O   . HOH F 5 .   ? -23.361 -2.330  1.836   1.00 67.91  ? 566 HOH A O   1 
HETATM 2047 O  O   . HOH F 5 .   ? -28.231 -5.428  10.696  1.00 54.38  ? 567 HOH A O   1 
HETATM 2048 O  O   . HOH F 5 .   ? -18.959 -11.835 -23.060 1.00 37.31  ? 568 HOH A O   1 
HETATM 2049 O  O   . HOH F 5 .   ? -15.331 -5.807  -21.947 1.00 46.24  ? 569 HOH A O   1 
HETATM 2050 O  O   . HOH F 5 .   ? -22.063 -6.008  -0.112  1.00 42.53  ? 570 HOH A O   1 
HETATM 2051 O  O   . HOH F 5 .   ? -18.736 -13.928 18.500  1.00 45.18  ? 571 HOH A O   1 
HETATM 2052 O  O   . HOH F 5 .   ? -7.602  -20.429 -8.957  1.00 39.50  ? 572 HOH A O   1 
HETATM 2053 O  O   . HOH F 5 .   ? -26.340 -8.884  -5.936  1.00 51.30  ? 573 HOH A O   1 
HETATM 2054 O  O   . HOH F 5 .   ? -6.237  -9.931  -13.342 1.00 59.34  ? 574 HOH A O   1 
HETATM 2055 O  O   . HOH F 5 .   ? 2.423   -37.087 -9.183  1.00 62.96  ? 575 HOH A O   1 
HETATM 2056 O  O   . HOH F 5 .   ? -25.844 0.822   13.021  1.00 50.22  ? 576 HOH A O   1 
HETATM 2057 O  O   . HOH F 5 .   ? -17.812 -28.586 15.275  1.00 42.12  ? 577 HOH A O   1 
HETATM 2058 O  O   . HOH F 5 .   ? -22.143 -8.046  -2.044  1.00 34.89  ? 578 HOH A O   1 
HETATM 2059 O  O   . HOH F 5 .   ? -27.595 -29.826 8.957   1.00 48.16  ? 579 HOH A O   1 
HETATM 2060 O  O   . HOH G 5 .   ? -7.272  -13.977 -8.790  1.00 60.02  ? 401 HOH P O   1 
HETATM 2061 O  O   . HOH G 5 .   ? -2.590  -14.832 1.284   1.00 53.16  ? 402 HOH P O   1 
HETATM 2062 O  O   . HOH G 5 .   ? -8.323  -17.977 -0.056  1.00 25.38  ? 403 HOH P O   1 
HETATM 2063 O  O   . HOH G 5 .   ? -6.683  -13.480 4.166   1.00 42.40  ? 404 HOH P O   1 
HETATM 2064 O  O   . HOH G 5 .   ? -4.218  -14.764 4.076   1.00 34.99  ? 405 HOH P O   1 
HETATM 2065 O  O   . HOH G 5 .   ? -5.517  -6.242  -9.682  1.00 65.46  ? 406 HOH P O   1 
HETATM 2066 O  O   . HOH G 5 .   ? -5.781  -12.561 -12.714 1.00 72.82  ? 407 HOH P 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 6   ? 0.9775 1.0642 0.5984 0.1084  -0.0698 -0.1070 1   MET A N   
2    C  CA  . MET A 6   ? 1.0054 1.0599 0.6087 0.1051  -0.0655 -0.1060 1   MET A CA  
3    C  C   . MET A 6   ? 0.8660 1.0663 0.5452 0.1327  -0.0858 -0.0070 1   MET A C   
4    O  O   . MET A 6   ? 0.8491 1.0749 0.6594 0.1298  -0.1027 -0.0100 1   MET A O   
5    C  CB  . MET A 6   ? 1.1088 1.1100 0.7558 0.0509  -0.0683 -0.1432 1   MET A CB  
6    C  CG  . MET A 6   ? 1.1547 1.1707 0.8693 0.0249  -0.0907 -0.1529 1   MET A CG  
7    S  SD  . MET A 6   ? 1.3225 1.2256 1.1902 -0.0113 -0.0733 -0.1667 1   MET A SD  
8    C  CE  . MET A 6   ? 1.2173 1.1548 1.1719 0.0200  -0.0488 -0.1397 1   MET A CE  
9    N  N   . GLU A 7   ? 0.7182 1.0112 0.3764 0.1577  -0.1749 -0.0517 2   GLU A N   
10   C  CA  . GLU A 7   ? 0.6524 0.9048 0.2134 0.1440  -0.1711 -0.0402 2   GLU A CA  
11   C  C   . GLU A 7   ? 0.5866 0.8277 0.2091 0.0852  -0.1317 -0.0660 2   GLU A C   
12   O  O   . GLU A 7   ? 0.5690 0.8272 0.0951 0.0790  -0.1529 -0.0360 2   GLU A O   
13   C  CB  . GLU A 7   ? 0.6941 0.9284 0.1973 0.1693  -0.1694 -0.0248 2   GLU A CB  
14   C  CG  . GLU A 7   ? 0.7148 0.9125 0.1458 0.2177  -0.1372 -0.0356 2   GLU A CG  
15   C  CD  . GLU A 7   ? 0.8501 0.9599 0.1589 0.2074  -0.1108 -0.0409 2   GLU A CD  
16   O  OE1 . GLU A 7   ? 0.8235 0.9489 0.4959 0.1776  -0.1161 0.0066  2   GLU A OE1 
17   O  OE2 . GLU A 7   ? 0.9343 0.9968 0.2309 0.1950  -0.0628 -0.1126 2   GLU A OE2 
18   N  N   . ARG A 8   ? 0.5561 0.7867 0.1546 0.0435  -0.1449 -0.0853 3   ARG A N   
19   C  CA  . ARG A 8   ? 0.5667 0.7682 0.0458 0.0262  -0.1001 -0.0430 3   ARG A CA  
20   C  C   . ARG A 8   ? 0.5833 0.7619 0.0363 0.0259  -0.0720 -0.0382 3   ARG A C   
21   O  O   . ARG A 8   ? 0.5605 0.7508 0.0512 0.0428  -0.1154 -0.0365 3   ARG A O   
22   C  CB  . ARG A 8   ? 0.5470 0.7457 0.1316 -0.0022 -0.1015 -0.0402 3   ARG A CB  
23   C  CG  . ARG A 8   ? 0.5195 0.7385 0.1702 -0.0169 -0.0937 -0.0547 3   ARG A CG  
24   C  CD  . ARG A 8   ? 0.4957 0.7364 0.1555 -0.0286 -0.0806 -0.0537 3   ARG A CD  
25   N  NE  . ARG A 8   ? 0.4691 0.7346 0.1562 -0.0478 -0.0657 -0.0687 3   ARG A NE  
26   C  CZ  . ARG A 8   ? 0.4852 0.7220 0.1105 -0.0498 -0.0800 -0.0491 3   ARG A CZ  
27   N  NH1 . ARG A 8   ? 0.4812 0.7504 0.0392 -0.0606 -0.0572 -0.0412 3   ARG A NH1 
28   N  NH2 . ARG A 8   ? 0.4836 0.7224 0.1118 -0.0591 -0.0735 -0.0217 3   ARG A NH2 
29   N  N   . ALA A 9   ? 0.6483 0.7599 0.0369 0.0258  -0.0332 -0.0863 4   ALA A N   
30   C  CA  . ALA A 9   ? 0.6481 0.7372 0.0374 0.0192  -0.0369 -0.0849 4   ALA A CA  
31   C  C   . ALA A 9   ? 0.6259 0.7225 0.0286 0.0265  -0.0343 -0.0317 4   ALA A C   
32   O  O   . ALA A 9   ? 0.6338 0.7225 0.0255 0.0331  -0.0068 -0.0082 4   ALA A O   
33   C  CB  . ALA A 9   ? 0.6872 0.7416 0.0471 0.0059  -0.0248 -0.1224 4   ALA A CB  
34   N  N   . SER A 10  ? 0.6039 0.7274 0.0383 0.0319  -0.0866 -0.0106 5   SER A N   
35   C  CA  . SER A 10  ? 0.5968 0.7289 0.0336 0.0464  -0.0686 -0.0108 5   SER A CA  
36   C  C   . SER A 10  ? 0.5847 0.6887 0.0352 0.0465  -0.0740 -0.0139 5   SER A C   
37   O  O   . SER A 10  ? 0.5826 0.6468 0.0290 0.0639  -0.0222 0.0390  5   SER A O   
38   C  CB  . SER A 10  ? 0.6144 0.7674 0.0686 0.0470  -0.0919 0.0088  5   SER A CB  
39   O  OG  . SER A 10  ? 0.7090 0.8384 0.0545 0.0695  -0.0744 -0.0306 5   SER A OG  
40   N  N   . LEU A 11  ? 0.5299 0.6865 0.0333 0.0406  -0.0582 -0.0339 6   LEU A N   
41   C  CA  . LEU A 11  ? 0.5357 0.6900 0.0372 0.0437  -0.0774 0.0005  6   LEU A CA  
42   C  C   . LEU A 11  ? 0.5229 0.6482 0.0385 0.0293  -0.0414 -0.0240 6   LEU A C   
43   O  O   . LEU A 11  ? 0.5166 0.6378 0.0264 0.0457  -0.0197 -0.0138 6   LEU A O   
44   C  CB  . LEU A 11  ? 0.5232 0.7059 0.0373 0.0507  -0.0767 0.0028  6   LEU A CB  
45   C  CG  . LEU A 11  ? 0.5152 0.7194 0.0825 0.0347  -0.0898 -0.0095 6   LEU A CG  
46   C  CD1 . LEU A 11  ? 0.5238 0.7111 0.0822 0.0351  -0.0876 0.0137  6   LEU A CD1 
47   C  CD2 . LEU A 11  ? 0.5047 0.7164 0.1688 0.0443  -0.0867 -0.0082 6   LEU A CD2 
48   N  N   . ILE A 12  ? 0.5249 0.6028 0.0262 0.0203  -0.0136 -0.0168 7   ILE A N   
49   C  CA  . ILE A 12  ? 0.5362 0.5949 0.0260 0.0257  0.0101  -0.0166 7   ILE A CA  
50   C  C   . ILE A 12  ? 0.5599 0.5916 0.0270 0.0380  0.0163  -0.0247 7   ILE A C   
51   O  O   . ILE A 12  ? 0.5760 0.6184 0.0263 0.0137  0.0227  -0.0058 7   ILE A O   
52   C  CB  . ILE A 12  ? 0.5132 0.5747 0.0275 0.0208  -0.0158 -0.0308 7   ILE A CB  
53   C  CG1 . ILE A 12  ? 0.5177 0.6104 0.0268 0.0274  -0.0155 -0.0246 7   ILE A CG1 
54   C  CG2 . ILE A 12  ? 0.5081 0.5669 0.0420 0.0377  0.0182  -0.0403 7   ILE A CG2 
55   C  CD1 . ILE A 12  ? 0.5223 0.6247 0.0340 -0.0111 -0.0512 -0.0442 7   ILE A CD1 
56   N  N   . GLN A 13  ? 0.6766 0.5977 0.0307 0.0313  0.0008  -0.0553 8   GLN A N   
57   C  CA  . GLN A 13  ? 0.6988 0.6193 0.0291 0.0338  0.0045  -0.0469 8   GLN A CA  
58   C  C   . GLN A 13  ? 0.6566 0.6071 0.0288 0.0466  -0.0119 -0.0444 8   GLN A C   
59   O  O   . GLN A 13  ? 0.6966 0.6408 0.0262 0.0352  -0.0069 -0.0219 8   GLN A O   
60   C  CB  . GLN A 13  ? 0.7248 0.6177 0.0266 0.0518  0.0016  0.0272  8   GLN A CB  
61   C  CG  . GLN A 13  ? 0.7993 0.6667 0.0575 0.0332  0.0049  -0.0024 8   GLN A CG  
62   C  CD  . GLN A 13  ? 0.8491 0.7240 0.1425 0.0227  -0.0312 0.0357  8   GLN A CD  
63   O  OE1 . GLN A 13  ? 0.9382 0.8193 0.0972 0.0296  -0.0876 0.0152  8   GLN A OE1 
64   N  NE2 . GLN A 13  ? 0.8620 0.7800 0.1946 0.0070  0.0230  0.0904  8   GLN A NE2 
65   N  N   . LYS A 14  ? 0.6289 0.6183 0.0268 0.0566  -0.0126 -0.0281 9   LYS A N   
66   C  CA  . LYS A 14  ? 0.6114 0.6048 0.0271 0.0671  -0.0257 -0.0218 9   LYS A CA  
67   C  C   . LYS A 14  ? 0.5437 0.5520 0.0291 0.0592  -0.0358 0.0223  9   LYS A C   
68   O  O   . LYS A 14  ? 0.5815 0.5596 0.0263 0.0419  0.0068  0.0227  9   LYS A O   
69   C  CB  . LYS A 14  ? 0.6561 0.6385 0.0269 0.0893  -0.0299 -0.0144 9   LYS A CB  
70   C  CG  . LYS A 14  ? 0.6545 0.6533 0.0284 0.1294  -0.0352 0.0185  9   LYS A CG  
71   C  CD  . LYS A 14  ? 0.7005 0.7334 0.1131 0.1312  -0.0238 0.0087  9   LYS A CD  
72   C  CE  . LYS A 14  ? 0.7231 0.7700 0.1734 0.1475  -0.0234 0.0110  9   LYS A CE  
73   N  NZ  . LYS A 14  ? 0.7719 0.8048 0.1834 0.1430  -0.0304 -0.0198 9   LYS A NZ  
74   N  N   . ALA A 15  ? 0.5072 0.5323 0.0257 0.0364  -0.0128 0.0046  10  ALA A N   
75   C  CA  . ALA A 15  ? 0.5050 0.5418 0.0255 0.0244  -0.0084 -0.0062 10  ALA A CA  
76   C  C   . ALA A 15  ? 0.5126 0.5858 0.0259 0.0051  0.0055  -0.0162 10  ALA A C   
77   O  O   . ALA A 15  ? 0.5642 0.5712 0.0266 0.0000  -0.0175 -0.0197 10  ALA A O   
78   C  CB  . ALA A 15  ? 0.5051 0.5441 0.0273 0.0228  -0.0263 -0.0172 10  ALA A CB  
79   N  N   . LYS A 16  ? 0.5740 0.5834 0.0259 0.0061  -0.0124 -0.0131 11  LYS A N   
80   C  CA  . LYS A 16  ? 0.5801 0.6005 0.0255 0.0173  0.0020  -0.0108 11  LYS A CA  
81   C  C   . LYS A 16  ? 0.6057 0.6323 0.0281 0.0125  0.0346  -0.0204 11  LYS A C   
82   O  O   . LYS A 16  ? 0.5863 0.6135 0.0343 0.0207  0.0470  0.0147  11  LYS A O   
83   C  CB  . LYS A 16  ? 0.5730 0.5877 0.0323 0.0222  0.0491  -0.0362 11  LYS A CB  
84   C  CG  . LYS A 16  ? 0.5692 0.6138 0.0342 0.0344  0.0597  -0.0329 11  LYS A CG  
85   C  CD  . LYS A 16  ? 0.6291 0.6398 0.0398 0.0344  0.0812  -0.0418 11  LYS A CD  
86   C  CE  . LYS A 16  ? 0.6430 0.6523 0.0695 0.0290  0.0867  -0.0360 11  LYS A CE  
87   N  NZ  . LYS A 16  ? 0.7050 0.7125 0.0718 0.0312  0.0858  -0.0327 11  LYS A NZ  
88   N  N   . LEU A 17  ? 0.6610 0.6337 0.0268 0.0223  0.0299  -0.0072 12  LEU A N   
89   C  CA  . LEU A 17  ? 0.6618 0.6257 0.0287 0.0216  0.0444  -0.0122 12  LEU A CA  
90   C  C   . LEU A 17  ? 0.6351 0.6018 0.0260 0.0037  0.0038  -0.0198 12  LEU A C   
91   O  O   . LEU A 17  ? 0.6432 0.6044 0.0281 -0.0129 0.0371  0.0168  12  LEU A O   
92   C  CB  . LEU A 17  ? 0.6750 0.6246 0.0307 0.0264  0.0558  -0.0158 12  LEU A CB  
93   C  CG  . LEU A 17  ? 0.7021 0.6390 0.0292 0.0218  0.0512  0.0045  12  LEU A CG  
94   C  CD1 . LEU A 17  ? 0.7239 0.6545 0.0279 0.0283  0.0207  0.0362  12  LEU A CD1 
95   C  CD2 . LEU A 17  ? 0.7149 0.6289 0.0293 0.0068  0.0358  0.0365  12  LEU A CD2 
96   N  N   . ALA A 18  ? 0.6034 0.5857 0.0265 0.0123  -0.0261 -0.0045 13  ALA A N   
97   C  CA  . ALA A 18  ? 0.5762 0.5816 0.0287 -0.0071 -0.0384 -0.0192 13  ALA A CA  
98   C  C   . ALA A 18  ? 0.5589 0.5726 0.0254 -0.0071 0.0044  -0.0043 13  ALA A C   
99   O  O   . ALA A 18  ? 0.5278 0.5527 0.0285 -0.0180 -0.0308 -0.0246 13  ALA A O   
100  C  CB  . ALA A 18  ? 0.5748 0.6041 0.0368 0.0032  -0.0779 -0.0168 13  ALA A CB  
101  N  N   . GLU A 19  ? 0.5621 0.5771 0.0267 -0.0046 0.0094  -0.0261 14  GLU A N   
102  C  CA  . GLU A 19  ? 0.5568 0.5678 0.0263 0.0059  0.0168  -0.0156 14  GLU A CA  
103  C  C   . GLU A 19  ? 0.5769 0.5432 0.0253 -0.0095 -0.0030 -0.0008 14  GLU A C   
104  O  O   . GLU A 19  ? 0.5419 0.5538 0.0643 -0.0037 -0.0169 -0.0290 14  GLU A O   
105  C  CB  . GLU A 19  ? 0.5527 0.5614 0.0450 0.0171  -0.0069 -0.0335 14  GLU A CB  
106  C  CG  . GLU A 19  ? 0.5497 0.5872 0.1571 0.0296  0.0088  -0.0551 14  GLU A CG  
107  C  CD  . GLU A 19  ? 0.5764 0.6066 0.2298 0.0443  0.0289  -0.0362 14  GLU A CD  
108  O  OE1 . GLU A 19  ? 0.5686 0.6265 0.2110 0.0249  0.0738  -0.0645 14  GLU A OE1 
109  O  OE2 . GLU A 19  ? 0.5914 0.6408 0.3200 0.0526  0.0789  0.0159  14  GLU A OE2 
110  N  N   . GLN A 20  ? 0.5824 0.5386 0.0292 -0.0172 0.0436  -0.0168 15  GLN A N   
111  C  CA  . GLN A 20  ? 0.6003 0.5513 0.0411 -0.0257 0.0356  -0.0263 15  GLN A CA  
112  C  C   . GLN A 20  ? 0.5776 0.5345 0.0665 -0.0366 0.0324  -0.0031 15  GLN A C   
113  O  O   . GLN A 20  ? 0.5591 0.5920 0.0905 -0.0491 0.0273  -0.0204 15  GLN A O   
114  C  CB  . GLN A 20  ? 0.6552 0.5788 0.0771 -0.0234 0.0404  0.0253  15  GLN A CB  
115  C  CG  . GLN A 20  ? 0.7064 0.6267 0.1353 -0.0230 0.0544  -0.0035 15  GLN A CG  
116  C  CD  . GLN A 20  ? 0.8079 0.6711 0.1480 -0.0315 0.0826  0.0370  15  GLN A CD  
117  O  OE1 . GLN A 20  ? 0.8321 0.7201 0.2505 -0.0263 0.2031  0.0292  15  GLN A OE1 
118  N  NE2 . GLN A 20  ? 0.8373 0.7415 0.2442 -0.0337 0.0606  0.0548  15  GLN A NE2 
119  N  N   . ALA A 21  ? 0.5572 0.5291 0.0577 -0.0290 0.0273  0.0178  16  ALA A N   
120  C  CA  . ALA A 21  ? 0.5382 0.5274 0.0282 -0.0321 0.0215  0.0300  16  ALA A CA  
121  C  C   . ALA A 21  ? 0.5511 0.5248 0.0267 -0.0260 -0.0128 0.0232  16  ALA A C   
122  O  O   . ALA A 21  ? 0.5824 0.5312 0.0821 0.0007  -0.0057 0.0292  16  ALA A O   
123  C  CB  . ALA A 21  ? 0.5229 0.5506 0.0306 -0.0333 0.0383  0.0325  16  ALA A CB  
124  N  N   . GLU A 22  ? 0.5587 0.5175 0.0256 -0.0242 -0.0050 0.0096  17  GLU A N   
125  C  CA  . GLU A 22  ? 0.5733 0.5145 0.0445 -0.0114 -0.0067 0.0304  17  GLU A CA  
126  C  C   . GLU A 22  ? 0.5437 0.5098 0.0317 -0.0120 -0.0111 0.0070  17  GLU A C   
127  O  O   . GLU A 22  ? 0.5840 0.5638 0.0394 -0.0258 0.0156  -0.0096 17  GLU A O   
128  C  CB  . GLU A 22  ? 0.5903 0.5497 0.0788 -0.0192 -0.0084 0.0054  17  GLU A CB  
129  C  CG  . GLU A 22  ? 0.6068 0.6344 0.1941 -0.0233 0.0043  -0.0194 17  GLU A CG  
130  C  CD  . GLU A 22  ? 0.6232 0.7153 0.2715 -0.0399 0.0075  -0.0844 17  GLU A CD  
131  O  OE1 . GLU A 22  ? 0.6938 0.7947 0.2564 -0.0842 0.0294  -0.1095 17  GLU A OE1 
132  O  OE2 . GLU A 22  ? 0.6239 0.8213 0.4173 -0.0524 -0.0055 -0.0588 17  GLU A OE2 
133  N  N   . ARG A 23  ? 0.5343 0.4925 0.0263 0.0021  -0.0215 0.0064  18  ARG A N   
134  C  CA  . ARG A 23  ? 0.5296 0.4992 0.0260 0.0178  -0.0182 -0.0055 18  ARG A CA  
135  C  C   . ARG A 23  ? 0.5115 0.4993 0.0284 0.0182  -0.0377 0.0064  18  ARG A C   
136  O  O   . ARG A 23  ? 0.5722 0.5462 0.0278 -0.0038 -0.0366 0.0010  18  ARG A O   
137  C  CB  . ARG A 23  ? 0.5471 0.5013 0.0526 0.0368  -0.0093 -0.0183 18  ARG A CB  
138  C  CG  . ARG A 23  ? 0.5625 0.5297 0.0879 0.0285  0.0216  -0.0073 18  ARG A CG  
139  C  CD  . ARG A 23  ? 0.5596 0.5327 0.1281 0.0248  0.0493  -0.0097 18  ARG A CD  
140  N  NE  . ARG A 23  ? 0.5468 0.5316 0.1641 0.0145  0.0611  -0.0039 18  ARG A NE  
141  C  CZ  . ARG A 23  ? 0.5525 0.5479 0.0743 -0.0095 0.1071  0.0007  18  ARG A CZ  
142  N  NH1 . ARG A 23  ? 0.5862 0.5470 0.2014 -0.0137 0.1363  -0.0403 18  ARG A NH1 
143  N  NH2 . ARG A 23  ? 0.5531 0.5678 0.0895 0.0042  0.1196  0.0082  18  ARG A NH2 
144  N  N   . TYR A 24  ? 0.5629 0.5303 0.0333 0.0034  -0.0601 -0.0256 19  TYR A N   
145  C  CA  . TYR A 24  ? 0.5393 0.5281 0.0331 0.0191  -0.0546 -0.0335 19  TYR A CA  
146  C  C   . TYR A 24  ? 0.5311 0.5323 0.0298 0.0424  -0.0465 0.0066  19  TYR A C   
147  O  O   . TYR A 24  ? 0.5567 0.5530 0.0269 0.0177  -0.0185 0.0212  19  TYR A O   
148  C  CB  . TYR A 24  ? 0.5188 0.5360 0.0369 0.0133  -0.0649 -0.0408 19  TYR A CB  
149  C  CG  . TYR A 24  ? 0.4940 0.5680 0.0379 -0.0014 -0.0604 -0.0322 19  TYR A CG  
150  C  CD1 . TYR A 24  ? 0.4879 0.5939 0.0373 -0.0050 -0.0665 -0.0171 19  TYR A CD1 
151  C  CD2 . TYR A 24  ? 0.4914 0.5885 0.0820 -0.0200 -0.0642 -0.0161 19  TYR A CD2 
152  C  CE1 . TYR A 24  ? 0.4841 0.6266 0.0645 -0.0191 -0.0639 -0.0023 19  TYR A CE1 
153  C  CE2 . TYR A 24  ? 0.5093 0.6078 0.1318 -0.0226 -0.0587 -0.0204 19  TYR A CE2 
154  C  CZ  . TYR A 24  ? 0.4884 0.6281 0.1229 -0.0211 -0.0486 -0.0044 19  TYR A CZ  
155  O  OH  . TYR A 24  ? 0.5376 0.6987 0.1903 -0.0485 -0.0467 0.0471  19  TYR A OH  
156  N  N   . GLU A 25  ? 0.5507 0.5283 0.0321 0.0469  -0.0589 -0.0155 20  GLU A N   
157  C  CA  . GLU A 25  ? 0.5509 0.5642 0.0363 0.0502  -0.0709 -0.0339 20  GLU A CA  
158  C  C   . GLU A 25  ? 0.5256 0.5481 0.0388 0.0317  -0.0819 -0.0124 20  GLU A C   
159  O  O   . GLU A 25  ? 0.5347 0.5360 0.0284 0.0313  -0.0388 -0.0115 20  GLU A O   
160  C  CB  . GLU A 25  ? 0.5596 0.5716 0.0661 0.0776  -0.0807 -0.0305 20  GLU A CB  
161  C  CG  . GLU A 25  ? 0.6373 0.6660 0.1040 0.0611  -0.1300 -0.0106 20  GLU A CG  
162  C  CD  . GLU A 25  ? 0.7219 0.7379 0.2043 0.0354  -0.1143 -0.0395 20  GLU A CD  
163  O  OE1 . GLU A 25  ? 0.8257 0.7162 0.1519 0.0816  -0.0704 -0.1212 20  GLU A OE1 
164  O  OE2 . GLU A 25  ? 0.8245 0.7878 0.1985 0.0546  -0.1153 -0.0898 20  GLU A OE2 
165  N  N   . ASP A 26  ? 0.5235 0.5427 0.0339 0.0374  -0.0643 -0.0159 21  ASP A N   
166  C  CA  . ASP A 26  ? 0.5040 0.5303 0.0348 0.0337  -0.0669 -0.0114 21  ASP A CA  
167  C  C   . ASP A 26  ? 0.4767 0.5179 0.0291 0.0311  -0.0398 0.0087  21  ASP A C   
168  O  O   . ASP A 26  ? 0.4725 0.4782 0.0372 0.0206  -0.0155 -0.0320 21  ASP A O   
169  C  CB  . ASP A 26  ? 0.5249 0.5429 0.0291 0.0315  -0.0433 -0.0040 21  ASP A CB  
170  C  CG  . ASP A 26  ? 0.5347 0.5462 0.0261 0.0470  -0.0027 0.0200  21  ASP A CG  
171  O  OD1 . ASP A 26  ? 0.5613 0.5547 0.0785 0.0898  0.0744  -0.0169 21  ASP A OD1 
172  O  OD2 . ASP A 26  ? 0.5839 0.5657 0.0480 0.0446  -0.0115 0.0189  21  ASP A OD2 
173  N  N   . MET A 27  ? 0.4845 0.5197 0.0297 0.0319  -0.0391 0.0196  22  MET A N   
174  C  CA  . MET A 27  ? 0.4774 0.5331 0.0296 0.0388  -0.0157 0.0420  22  MET A CA  
175  C  C   . MET A 27  ? 0.4937 0.5317 0.0281 0.0247  -0.0192 0.0307  22  MET A C   
176  O  O   . MET A 27  ? 0.4782 0.5827 0.0283 0.0483  -0.0361 0.0045  22  MET A O   
177  C  CB  . MET A 27  ? 0.4588 0.5314 0.0264 0.0242  -0.0028 0.0231  22  MET A CB  
178  C  CG  . MET A 27  ? 0.4411 0.4994 0.0282 0.0180  -0.0141 0.0331  22  MET A CG  
179  S  SD  . MET A 27  ? 0.4438 0.5372 0.0261 0.0100  -0.0138 -0.0120 22  MET A SD  
180  C  CE  . MET A 27  ? 0.4404 0.5265 0.0727 0.0379  -0.0034 0.0003  22  MET A CE  
181  N  N   . ALA A 28  ? 0.4933 0.5497 0.0295 0.0185  -0.0412 0.0144  23  ALA A N   
182  C  CA  . ALA A 28  ? 0.4844 0.5610 0.0273 0.0114  -0.0298 -0.0030 23  ALA A CA  
183  C  C   . ALA A 28  ? 0.4861 0.5515 0.0255 0.0076  -0.0019 0.0100  23  ALA A C   
184  O  O   . ALA A 28  ? 0.4402 0.5050 0.0392 -0.0076 -0.0295 0.0102  23  ALA A O   
185  C  CB  . ALA A 28  ? 0.5030 0.5658 0.0285 0.0046  -0.0377 0.0103  23  ALA A CB  
186  N  N   . ALA A 29  ? 0.4674 0.5529 0.0254 0.0229  0.0057  0.0011  24  ALA A N   
187  C  CA  . ALA A 29  ? 0.4793 0.5756 0.0272 0.0213  -0.0242 -0.0192 24  ALA A CA  
188  C  C   . ALA A 29  ? 0.4868 0.5821 0.0309 0.0148  -0.0450 -0.0271 24  ALA A C   
189  O  O   . ALA A 29  ? 0.5181 0.5909 0.0329 0.0155  -0.0592 -0.0180 24  ALA A O   
190  C  CB  . ALA A 29  ? 0.4636 0.5987 0.0292 0.0164  -0.0413 -0.0054 24  ALA A CB  
191  N  N   . PHE A 30  ? 0.4459 0.5623 0.0381 0.0348  -0.0397 -0.0727 25  PHE A N   
192  C  CA  . PHE A 30  ? 0.4548 0.5721 0.0343 0.0270  -0.0397 -0.0560 25  PHE A CA  
193  C  C   . PHE A 30  ? 0.4382 0.5741 0.0325 0.0168  -0.0390 -0.0452 25  PHE A C   
194  O  O   . PHE A 30  ? 0.4407 0.5348 0.0583 -0.0079 -0.0531 -0.0400 25  PHE A O   
195  C  CB  . PHE A 30  ? 0.4761 0.5940 0.0294 0.0599  -0.0355 -0.0316 25  PHE A CB  
196  C  CG  . PHE A 30  ? 0.5033 0.6193 0.0260 0.0567  -0.0066 0.0172  25  PHE A CG  
197  C  CD1 . PHE A 30  ? 0.5195 0.6135 0.0279 0.0553  0.0347  -0.0045 25  PHE A CD1 
198  C  CD2 . PHE A 30  ? 0.5112 0.6572 0.0264 0.0564  -0.0171 0.0145  25  PHE A CD2 
199  C  CE1 . PHE A 30  ? 0.5413 0.6261 0.0269 0.0531  0.0277  -0.0022 25  PHE A CE1 
200  C  CE2 . PHE A 30  ? 0.5178 0.6791 0.0272 0.0650  -0.0015 -0.0346 25  PHE A CE2 
201  C  CZ  . PHE A 30  ? 0.5355 0.6399 0.0286 0.0589  0.0357  -0.0169 25  PHE A CZ  
202  N  N   . MET A 31  ? 0.4482 0.5571 0.0352 0.0226  -0.0398 -0.0593 26  MET A N   
203  C  CA  . MET A 31  ? 0.4412 0.5602 0.0363 0.0156  -0.0578 -0.0417 26  MET A CA  
204  C  C   . MET A 31  ? 0.4439 0.5476 0.0323 0.0143  -0.0383 -0.0438 26  MET A C   
205  O  O   . MET A 31  ? 0.4533 0.5509 0.0313 0.0115  -0.0275 -0.0476 26  MET A O   
206  C  CB  . MET A 31  ? 0.4540 0.5491 0.0474 -0.0017 -0.0773 -0.0651 26  MET A CB  
207  C  CG  . MET A 31  ? 0.4389 0.5370 0.0453 -0.0036 -0.0715 -0.0618 26  MET A CG  
208  S  SD  . MET A 31  ? 0.4923 0.5787 0.0297 0.0094  -0.0225 -0.0431 26  MET A SD  
209  C  CE  . MET A 31  ? 0.4883 0.5994 0.0339 -0.0053 -0.0250 -0.0643 26  MET A CE  
210  N  N   . LYS A 32  ? 0.4279 0.5755 0.0324 0.0167  -0.0450 -0.0356 27  LYS A N   
211  C  CA  . LYS A 32  ? 0.4424 0.5960 0.0302 0.0101  -0.0374 -0.0304 27  LYS A CA  
212  C  C   . LYS A 32  ? 0.4120 0.5965 0.0858 0.0040  -0.0671 -0.0245 27  LYS A C   
213  O  O   . LYS A 32  ? 0.4258 0.6111 0.0363 0.0009  -0.0489 -0.0169 27  LYS A O   
214  C  CB  . LYS A 32  ? 0.4559 0.6328 0.0279 -0.0036 -0.0219 -0.0292 27  LYS A CB  
215  C  CG  . LYS A 32  ? 0.4762 0.6576 0.0397 0.0011  -0.0326 -0.0014 27  LYS A CG  
216  C  CD  . LYS A 32  ? 0.4928 0.6765 0.0278 0.0151  -0.0171 0.0344  27  LYS A CD  
217  C  CE  . LYS A 32  ? 0.4786 0.7176 0.1208 0.0240  -0.0305 0.0299  27  LYS A CE  
218  N  NZ  . LYS A 32  ? 0.4949 0.7305 0.1131 0.0294  -0.0057 0.0276  27  LYS A NZ  
219  N  N   . GLY A 33  ? 0.4028 0.5864 0.0671 0.0119  -0.0539 -0.0247 28  GLY A N   
220  C  CA  . GLY A 33  ? 0.4047 0.6047 0.0639 0.0076  -0.0521 -0.0368 28  GLY A CA  
221  C  C   . GLY A 33  ? 0.4007 0.6046 0.0710 0.0011  -0.0428 -0.0594 28  GLY A C   
222  O  O   . GLY A 33  ? 0.4342 0.6162 0.0514 0.0115  -0.0353 -0.0959 28  GLY A O   
223  N  N   . ALA A 34  ? 0.3978 0.5883 0.0529 0.0153  -0.0560 -0.0395 29  ALA A N   
224  C  CA  . ALA A 34  ? 0.4103 0.5854 0.0412 0.0128  -0.0477 -0.0205 29  ALA A CA  
225  C  C   . ALA A 34  ? 0.4050 0.5892 0.0548 -0.0070 -0.0640 -0.0402 29  ALA A C   
226  O  O   . ALA A 34  ? 0.4471 0.6018 0.0927 -0.0241 -0.0456 -0.0722 29  ALA A O   
227  C  CB  . ALA A 34  ? 0.4301 0.5790 0.0296 -0.0018 -0.0254 0.0111  29  ALA A CB  
228  N  N   . VAL A 35  ? 0.4229 0.5886 0.0345 -0.0152 -0.0453 -0.0454 30  VAL A N   
229  C  CA  . VAL A 35  ? 0.4228 0.6131 0.0488 -0.0243 -0.0570 -0.0835 30  VAL A CA  
230  C  C   . VAL A 35  ? 0.4313 0.6456 0.1267 -0.0188 -0.0458 -0.0961 30  VAL A C   
231  O  O   . VAL A 35  ? 0.4039 0.6498 0.1280 -0.0210 -0.0115 -0.1145 30  VAL A O   
232  C  CB  . VAL A 35  ? 0.4242 0.5857 0.0537 -0.0247 -0.0543 -0.0535 30  VAL A CB  
233  C  CG1 . VAL A 35  ? 0.4260 0.5856 0.1381 -0.0210 -0.0508 -0.0576 30  VAL A CG1 
234  C  CG2 . VAL A 35  ? 0.4263 0.5779 0.0320 -0.0186 -0.0411 -0.0350 30  VAL A CG2 
235  N  N   . GLU A 36  ? 0.4235 0.6957 0.1157 0.0034  -0.0568 -0.1023 31  GLU A N   
236  C  CA  . GLU A 36  ? 0.4286 0.7397 0.1373 0.0029  -0.0722 -0.1094 31  GLU A CA  
237  C  C   . GLU A 36  ? 0.4096 0.7946 0.1601 -0.0078 -0.0908 -0.1243 31  GLU A C   
238  O  O   . GLU A 36  ? 0.4234 0.8057 0.2983 -0.0204 -0.0655 -0.1291 31  GLU A O   
239  C  CB  . GLU A 36  ? 0.4440 0.7374 0.1139 0.0092  -0.0839 -0.1109 31  GLU A CB  
240  C  CG  . GLU A 36  ? 0.4573 0.7640 0.1247 0.0036  -0.0538 -0.0625 31  GLU A CG  
241  C  CD  . GLU A 36  ? 0.5344 0.7780 0.1284 0.0146  -0.0639 -0.0627 31  GLU A CD  
242  O  OE1 . GLU A 36  ? 0.6177 0.7850 0.1846 0.0642  -0.0843 -0.0729 31  GLU A OE1 
243  O  OE2 . GLU A 36  ? 0.5083 0.8370 0.1370 0.0182  -0.0272 0.0011  31  GLU A OE2 
244  N  N   . LYS A 37  ? 0.4634 0.8405 0.1506 -0.0135 -0.0803 -0.1424 32  LYS A N   
245  C  CA  . LYS A 37  ? 0.4880 0.8996 0.1720 -0.0232 -0.1145 -0.1479 32  LYS A CA  
246  C  C   . LYS A 37  ? 0.5137 0.8796 0.1657 -0.0249 -0.1050 -0.1822 32  LYS A C   
247  O  O   . LYS A 37  ? 0.5732 1.0024 0.2026 -0.0826 -0.1225 -0.2024 32  LYS A O   
248  C  CB  . LYS A 37  ? 0.5136 0.9414 0.0690 0.0074  -0.0669 -0.1626 32  LYS A CB  
249  C  CG  . LYS A 37  ? 0.5290 0.9715 0.1083 0.0315  -0.0703 -0.1174 32  LYS A CG  
250  C  CD  . LYS A 37  ? 0.5906 1.0073 0.2110 0.0485  -0.0321 -0.0857 32  LYS A CD  
251  C  CE  . LYS A 37  ? 0.6362 1.0256 0.2126 0.0587  -0.0019 -0.0577 32  LYS A CE  
252  N  NZ  . LYS A 37  ? 0.6673 1.0752 0.2914 0.0603  0.0296  -0.0278 32  LYS A NZ  
253  N  N   . GLY A 38  ? 0.5395 0.8439 0.2269 -0.0063 -0.0727 -0.1483 33  GLY A N   
254  C  CA  . GLY A 38  ? 0.5434 0.8296 0.2105 -0.0264 -0.0646 -0.1539 33  GLY A CA  
255  C  C   . GLY A 38  ? 0.5767 0.8075 0.1751 -0.0316 -0.0409 -0.1317 33  GLY A C   
256  O  O   . GLY A 38  ? 0.6410 0.8072 0.1966 0.0018  -0.0262 -0.1074 33  GLY A O   
257  N  N   . GLU A 39  ? 0.5262 0.7913 0.1523 -0.0300 -0.0282 -0.1468 34  GLU A N   
258  C  CA  . GLU A 39  ? 0.5211 0.7979 0.1023 -0.0230 -0.0143 -0.1193 34  GLU A CA  
259  C  C   . GLU A 39  ? 0.4624 0.7075 0.0384 -0.0385 0.0080  -0.0943 34  GLU A C   
260  O  O   . GLU A 39  ? 0.4831 0.7110 0.0464 -0.0427 0.0058  -0.1201 34  GLU A O   
261  C  CB  . GLU A 39  ? 0.6026 0.8338 0.0515 -0.0090 -0.0242 -0.1422 34  GLU A CB  
262  C  CG  . GLU A 39  ? 0.5951 0.9214 0.1666 -0.0121 -0.0276 -0.1671 34  GLU A CG  
263  C  CD  . GLU A 39  ? 0.6567 1.0027 0.2272 -0.0059 -0.0015 -0.1652 34  GLU A CD  
264  O  OE1 . GLU A 39  ? 0.6848 1.0263 0.4408 0.0237  0.0159  -0.0979 34  GLU A OE1 
265  O  OE2 . GLU A 39  ? 0.6565 1.1712 0.1614 0.0339  0.0097  -0.1557 34  GLU A OE2 
266  N  N   . GLU A 40  ? 0.4421 0.6887 0.0338 -0.0240 -0.0340 -0.0595 35  GLU A N   
267  C  CA  . GLU A 40  ? 0.4500 0.6683 0.0465 -0.0205 -0.0316 -0.1083 35  GLU A CA  
268  C  C   . GLU A 40  ? 0.4423 0.6832 0.0480 -0.0238 -0.0667 -0.0849 35  GLU A C   
269  O  O   . GLU A 40  ? 0.4813 0.6851 0.0446 -0.0305 -0.0517 -0.0906 35  GLU A O   
270  C  CB  . GLU A 40  ? 0.5012 0.6761 0.1207 -0.0057 0.0237  -0.1052 35  GLU A CB  
271  C  CG  . GLU A 40  ? 0.5476 0.6950 0.1447 0.0169  0.0407  -0.1108 35  GLU A CG  
272  C  CD  . GLU A 40  ? 0.5664 0.7240 0.1981 0.0314  0.0263  -0.1188 35  GLU A CD  
273  O  OE1 . GLU A 40  ? 0.5722 0.7123 0.2010 0.0273  0.0387  -0.0526 35  GLU A OE1 
274  O  OE2 . GLU A 40  ? 0.6161 0.7774 0.1497 0.0666  0.0124  -0.1086 35  GLU A OE2 
275  N  N   . LEU A 41  ? 0.5100 0.6567 0.0484 -0.0324 -0.0271 -0.1148 36  LEU A N   
276  C  CA  . LEU A 41  ? 0.4965 0.6427 0.0401 -0.0212 -0.0322 -0.0865 36  LEU A CA  
277  C  C   . LEU A 41  ? 0.4687 0.5803 0.0407 -0.0120 -0.0490 -0.0731 36  LEU A C   
278  O  O   . LEU A 41  ? 0.4993 0.5493 0.1062 -0.0012 -0.0065 -0.0838 36  LEU A O   
279  C  CB  . LEU A 41  ? 0.4866 0.6496 0.0363 -0.0140 -0.0282 -0.0752 36  LEU A CB  
280  C  CG  . LEU A 41  ? 0.5094 0.6894 0.0338 -0.0087 -0.0405 -0.0572 36  LEU A CG  
281  C  CD1 . LEU A 41  ? 0.5310 0.7154 0.0323 0.0045  -0.0124 -0.0679 36  LEU A CD1 
282  C  CD2 . LEU A 41  ? 0.5394 0.7005 0.0306 0.0064  -0.0053 -0.0592 36  LEU A CD2 
283  N  N   . SER A 42  ? 0.4578 0.5854 0.0510 -0.0125 -0.0244 -0.0512 37  SER A N   
284  C  CA  . SER A 42  ? 0.4383 0.5657 0.0749 -0.0126 -0.0322 -0.0572 37  SER A CA  
285  C  C   . SER A 42  ? 0.4166 0.5542 0.0598 -0.0169 -0.0112 -0.0775 37  SER A C   
286  O  O   . SER A 42  ? 0.4492 0.5653 0.0636 -0.0062 -0.0257 -0.1045 37  SER A O   
287  C  CB  . SER A 42  ? 0.4528 0.5598 0.0544 -0.0105 -0.0102 -0.0545 37  SER A CB  
288  O  OG  . SER A 42  ? 0.4445 0.5631 0.1020 -0.0161 -0.0105 -0.0511 37  SER A OG  
289  N  N   . CYS A 43  ? 0.4370 0.5823 0.0439 -0.0089 0.0049  -0.0654 38  CYS A N   
290  C  CA  A CYS A 43  ? 0.4397 0.6082 0.1107 -0.0142 -0.0013 -0.0717 38  CYS A CA  
291  C  CA  B CYS A 43  ? 0.4113 0.5824 0.0873 -0.0010 -0.0075 -0.0658 38  CYS A CA  
292  C  C   . CYS A 43  ? 0.4285 0.5790 0.0741 0.0066  0.0106  -0.0871 38  CYS A C   
293  O  O   . CYS A 43  ? 0.4324 0.5541 0.0802 -0.0210 0.0058  -0.1024 38  CYS A O   
294  C  CB  A CYS A 43  ? 0.4826 0.6523 0.1686 -0.0072 0.0367  -0.0591 38  CYS A CB  
295  C  CB  B CYS A 43  ? 0.4092 0.5753 0.0821 0.0124  -0.0115 -0.0524 38  CYS A CB  
296  S  SG  A CYS A 43  ? 0.5858 0.7396 0.2814 -0.0067 0.0586  -0.0702 38  CYS A SG  
297  S  SG  B CYS A 43  ? 0.3991 0.5786 0.0684 0.0385  -0.0275 -0.0543 38  CYS A SG  
298  N  N   . GLU A 44  ? 0.4296 0.5709 0.0698 -0.0018 0.0377  -0.1047 39  GLU A N   
299  C  CA  . GLU A 44  ? 0.4551 0.5745 0.0778 0.0024  0.0403  -0.0800 39  GLU A CA  
300  C  C   . GLU A 44  ? 0.4397 0.5404 0.0778 -0.0033 0.0323  -0.0641 39  GLU A C   
301  O  O   . GLU A 44  ? 0.4634 0.5497 0.0637 0.0018  0.0029  -0.0644 39  GLU A O   
302  C  CB  . GLU A 44  ? 0.5199 0.5898 0.1060 -0.0186 0.0435  -0.0728 39  GLU A CB  
303  C  CG  . GLU A 44  ? 0.5728 0.6234 0.1565 -0.0281 0.0530  -0.0526 39  GLU A CG  
304  C  CD  . GLU A 44  ? 0.6465 0.6620 0.1921 -0.0402 0.0514  -0.0441 39  GLU A CD  
305  O  OE1 . GLU A 44  ? 0.7438 0.7410 0.1673 -0.0479 0.0425  -0.0384 39  GLU A OE1 
306  O  OE2 . GLU A 44  ? 0.6937 0.7118 0.3039 -0.0544 0.1228  0.0064  39  GLU A OE2 
307  N  N   . GLU A 45  ? 0.4280 0.5445 0.0494 0.0039  0.0048  -0.0454 40  GLU A N   
308  C  CA  . GLU A 45  ? 0.4266 0.5399 0.0437 0.0089  -0.0043 -0.0422 40  GLU A CA  
309  C  C   . GLU A 45  ? 0.4272 0.5334 0.0313 0.0132  -0.0001 -0.0553 40  GLU A C   
310  O  O   . GLU A 45  ? 0.4306 0.5196 0.0504 -0.0042 0.0120  -0.0774 40  GLU A O   
311  C  CB  . GLU A 45  ? 0.4442 0.5696 0.0727 0.0128  -0.0271 -0.0203 40  GLU A CB  
312  C  CG  . GLU A 45  ? 0.4562 0.5723 0.0814 0.0056  -0.0095 -0.0151 40  GLU A CG  
313  C  CD  . GLU A 45  ? 0.4565 0.5787 0.0982 0.0098  -0.0505 0.0055  40  GLU A CD  
314  O  OE1 . GLU A 45  ? 0.4568 0.5892 0.0848 0.0107  -0.0459 -0.0020 40  GLU A OE1 
315  O  OE2 . GLU A 45  ? 0.4818 0.6184 0.0832 0.0199  -0.0796 -0.0238 40  GLU A OE2 
316  N  N   . ARG A 46  ? 0.4344 0.5516 0.0318 0.0022  -0.0266 -0.0500 41  ARG A N   
317  C  CA  . ARG A 46  ? 0.4846 0.5718 0.0277 0.0015  0.0023  -0.0094 41  ARG A CA  
318  C  C   . ARG A 46  ? 0.4560 0.5593 0.0280 0.0011  0.0040  -0.0377 41  ARG A C   
319  O  O   . ARG A 46  ? 0.4607 0.5225 0.0275 -0.0063 0.0194  -0.0262 41  ARG A O   
320  C  CB  . ARG A 46  ? 0.5699 0.5716 0.0553 -0.0188 -0.0017 -0.0140 41  ARG A CB  
321  C  CG  . ARG A 46  ? 0.6364 0.6082 0.2357 -0.0102 0.0304  0.0060  41  ARG A CG  
322  C  CD  . ARG A 46  ? 0.6705 0.6247 0.3031 0.0329  0.0450  0.0203  41  ARG A CD  
323  N  NE  . ARG A 46  ? 0.7119 0.6287 0.3619 0.0391  0.0985  0.0084  41  ARG A NE  
324  C  CZ  . ARG A 46  ? 0.7041 0.6743 0.4283 0.0612  0.0655  -0.0524 41  ARG A CZ  
325  N  NH1 . ARG A 46  ? 0.6888 0.6606 0.3305 0.0674  0.1141  -0.0590 41  ARG A NH1 
326  N  NH2 . ARG A 46  ? 0.7295 0.6682 0.4936 0.0992  0.0504  -0.0725 41  ARG A NH2 
327  N  N   . ASN A 47  ? 0.4291 0.5847 0.0308 -0.0014 -0.0227 -0.0482 42  ASN A N   
328  C  CA  . ASN A 47  ? 0.4254 0.5902 0.0819 -0.0092 -0.0258 -0.0622 42  ASN A CA  
329  C  C   . ASN A 47  ? 0.4179 0.5472 0.0584 -0.0236 -0.0204 -0.0584 42  ASN A C   
330  O  O   . ASN A 47  ? 0.4267 0.5398 0.0306 0.0041  -0.0094 -0.0497 42  ASN A O   
331  C  CB  . ASN A 47  ? 0.4235 0.6419 0.1469 -0.0121 -0.0387 -0.0767 42  ASN A CB  
332  C  CG  . ASN A 47  ? 0.4741 0.7414 0.2287 0.0052  -0.0671 -0.0606 42  ASN A CG  
333  O  OD1 . ASN A 47  ? 0.5454 0.8652 0.2431 0.0357  -0.0731 -0.0011 42  ASN A OD1 
334  N  ND2 . ASN A 47  ? 0.5126 0.8178 0.3250 0.0393  -0.0769 -0.0215 42  ASN A ND2 
335  N  N   . LEU A 48  ? 0.4328 0.5509 0.0313 -0.0179 -0.0149 -0.0525 43  LEU A N   
336  C  CA  . LEU A 48  ? 0.4355 0.5563 0.0283 -0.0230 0.0077  -0.0389 43  LEU A CA  
337  C  C   . LEU A 48  ? 0.4104 0.5176 0.0278 -0.0155 0.0174  -0.0297 43  LEU A C   
338  O  O   . LEU A 48  ? 0.4419 0.4770 0.0537 -0.0095 0.0006  -0.0219 43  LEU A O   
339  C  CB  . LEU A 48  ? 0.4834 0.5622 0.0315 -0.0186 0.0037  -0.0209 43  LEU A CB  
340  C  CG  . LEU A 48  ? 0.5084 0.5743 0.0280 -0.0240 -0.0036 -0.0376 43  LEU A CG  
341  C  CD1 . LEU A 48  ? 0.5536 0.5855 0.0289 -0.0271 -0.0183 -0.0392 43  LEU A CD1 
342  C  CD2 . LEU A 48  ? 0.5393 0.5987 0.0259 -0.0120 0.0167  -0.0005 43  LEU A CD2 
343  N  N   . LEU A 49  ? 0.4068 0.5252 0.0297 -0.0112 0.0323  -0.0299 44  LEU A N   
344  C  CA  . LEU A 49  ? 0.3901 0.5403 0.0265 -0.0223 0.0103  -0.0218 44  LEU A CA  
345  C  C   . LEU A 49  ? 0.4051 0.5411 0.0270 -0.0031 -0.0068 -0.0283 44  LEU A C   
346  O  O   . LEU A 49  ? 0.3900 0.5300 0.0268 -0.0036 0.0206  -0.0132 44  LEU A O   
347  C  CB  . LEU A 49  ? 0.4264 0.5634 0.0266 -0.0256 0.0023  -0.0256 44  LEU A CB  
348  C  CG  . LEU A 49  ? 0.4296 0.5419 0.0375 -0.0533 -0.0165 -0.0285 44  LEU A CG  
349  C  CD1 . LEU A 49  ? 0.4361 0.5588 0.0366 -0.0411 -0.0043 -0.0371 44  LEU A CD1 
350  C  CD2 . LEU A 49  ? 0.4686 0.5539 0.0356 -0.0557 -0.0232 -0.0074 44  LEU A CD2 
351  N  N   . SER A 50  ? 0.4191 0.5283 0.0262 -0.0028 -0.0086 -0.0188 45  SER A N   
352  C  CA  . SER A 50  ? 0.4468 0.5441 0.0269 0.0147  -0.0253 0.0008  45  SER A CA  
353  C  C   . SER A 50  ? 0.4466 0.5085 0.0259 -0.0005 -0.0037 -0.0166 45  SER A C   
354  O  O   . SER A 50  ? 0.4789 0.4865 0.0259 -0.0071 -0.0161 0.0028  45  SER A O   
355  C  CB  . SER A 50  ? 0.4899 0.5311 0.0652 0.0309  -0.0499 0.0051  45  SER A CB  
356  O  OG  . SER A 50  ? 0.5382 0.5909 0.0497 0.0549  -0.0110 0.0088  45  SER A OG  
357  N  N   . VAL A 51  ? 0.4254 0.5018 0.0255 0.0035  -0.0085 -0.0036 46  VAL A N   
358  C  CA  . VAL A 51  ? 0.4419 0.5089 0.0371 -0.0161 0.0092  0.0052  46  VAL A CA  
359  C  C   . VAL A 51  ? 0.4288 0.4972 0.0485 -0.0131 -0.0173 -0.0062 46  VAL A C   
360  O  O   . VAL A 51  ? 0.4246 0.4975 0.0347 -0.0091 -0.0492 -0.0011 46  VAL A O   
361  C  CB  . VAL A 51  ? 0.4734 0.5321 0.0550 -0.0348 0.0125  -0.0070 46  VAL A CB  
362  C  CG1 . VAL A 51  ? 0.4995 0.5454 0.1038 -0.0452 0.0292  -0.0165 46  VAL A CG1 
363  C  CG2 . VAL A 51  ? 0.4909 0.5276 0.1056 -0.0364 -0.0190 -0.0140 46  VAL A CG2 
364  N  N   . ALA A 52  ? 0.4352 0.5264 0.0267 0.0059  -0.0199 0.0133  47  ALA A N   
365  C  CA  . ALA A 52  ? 0.4274 0.5013 0.0276 -0.0129 -0.0081 0.0320  47  ALA A CA  
366  C  C   . ALA A 52  ? 0.4464 0.4994 0.0261 -0.0165 0.0105  0.0157  47  ALA A C   
367  O  O   . ALA A 52  ? 0.4294 0.4891 0.0330 -0.0123 0.0094  -0.0075 47  ALA A O   
368  C  CB  . ALA A 52  ? 0.3844 0.5119 0.0410 -0.0145 0.0067  -0.0004 47  ALA A CB  
369  N  N   . TYR A 53  ? 0.4361 0.5093 0.0273 -0.0232 0.0148  0.0252  48  TYR A N   
370  C  CA  . TYR A 53  ? 0.4119 0.5019 0.0286 -0.0084 0.0169  0.0341  48  TYR A CA  
371  C  C   . TYR A 53  ? 0.4075 0.4816 0.0262 -0.0147 -0.0182 0.0036  48  TYR A C   
372  O  O   . TYR A 53  ? 0.4211 0.4762 0.0265 0.0020  -0.0034 0.0225  48  TYR A O   
373  C  CB  . TYR A 53  ? 0.4184 0.5147 0.0259 -0.0009 0.0144  0.0052  48  TYR A CB  
374  C  CG  . TYR A 53  ? 0.4006 0.5200 0.0258 -0.0087 0.0135  0.0001  48  TYR A CG  
375  C  CD1 . TYR A 53  ? 0.4007 0.5293 0.0253 0.0104  0.0022  0.0000  48  TYR A CD1 
376  C  CD2 . TYR A 53  ? 0.4215 0.5290 0.0255 -0.0051 -0.0049 0.0062  48  TYR A CD2 
377  C  CE1 . TYR A 53  ? 0.4142 0.5447 0.0267 0.0154  0.0231  -0.0003 48  TYR A CE1 
378  C  CE2 . TYR A 53  ? 0.4158 0.5448 0.0255 -0.0047 -0.0065 0.0036  48  TYR A CE2 
379  C  CZ  . TYR A 53  ? 0.4051 0.5460 0.0278 0.0145  -0.0297 -0.0110 48  TYR A CZ  
380  O  OH  . TYR A 53  ? 0.4220 0.5616 0.0256 0.0094  -0.0098 -0.0034 48  TYR A OH  
381  N  N   . LYS A 54  ? 0.4088 0.5018 0.0287 -0.0267 -0.0348 -0.0077 49  LYS A N   
382  C  CA  . LYS A 54  ? 0.4158 0.5106 0.0309 -0.0146 -0.0468 0.0036  49  LYS A CA  
383  C  C   . LYS A 54  ? 0.4393 0.4984 0.0336 -0.0065 -0.0580 -0.0056 49  LYS A C   
384  O  O   . LYS A 54  ? 0.4866 0.4800 0.0321 -0.0020 -0.0556 0.0066  49  LYS A O   
385  C  CB  . LYS A 54  ? 0.4479 0.5254 0.0572 0.0052  -0.0521 0.0052  49  LYS A CB  
386  C  CG  . LYS A 54  ? 0.4576 0.5553 0.0740 0.0107  -0.0491 0.0006  49  LYS A CG  
387  C  CD  . LYS A 54  ? 0.4729 0.5824 0.1206 0.0236  -0.0792 0.0148  49  LYS A CD  
388  C  CE  . LYS A 54  ? 0.4889 0.6047 0.0888 0.0360  -0.0715 0.0318  49  LYS A CE  
389  N  NZ  . LYS A 54  ? 0.5158 0.6192 0.1690 0.0521  -0.0271 0.0132  49  LYS A NZ  
390  N  N   . ASN A 55  ? 0.4333 0.4741 0.0260 -0.0132 -0.0159 0.0025  50  ASN A N   
391  C  CA  . ASN A 55  ? 0.4360 0.5012 0.0267 -0.0122 -0.0221 0.0097  50  ASN A CA  
392  C  C   . ASN A 55  ? 0.4410 0.4658 0.0262 -0.0070 -0.0151 0.0123  50  ASN A C   
393  O  O   . ASN A 55  ? 0.4604 0.4925 0.0342 -0.0233 -0.0236 -0.0120 50  ASN A O   
394  C  CB  . ASN A 55  ? 0.4482 0.5390 0.0273 -0.0167 -0.0288 0.0061  50  ASN A CB  
395  C  CG  . ASN A 55  ? 0.4719 0.5910 0.0748 -0.0572 -0.0317 -0.0435 50  ASN A CG  
396  O  OD1 . ASN A 55  ? 0.5309 0.6745 0.0901 -0.0755 -0.0667 -0.0334 50  ASN A OD1 
397  N  ND2 . ASN A 55  ? 0.4754 0.6212 0.1297 -0.0646 -0.0075 -0.1089 50  ASN A ND2 
398  N  N   . VAL A 56  ? 0.4540 0.4917 0.0323 0.0026  -0.0387 0.0398  51  VAL A N   
399  C  CA  . VAL A 56  ? 0.4762 0.5000 0.0350 0.0032  -0.0166 0.0654  51  VAL A CA  
400  C  C   . VAL A 56  ? 0.5138 0.5083 0.0357 0.0095  -0.0360 0.0604  51  VAL A C   
401  O  O   . VAL A 56  ? 0.5014 0.4635 0.0846 0.0028  -0.0129 -0.0177 51  VAL A O   
402  C  CB  . VAL A 56  ? 0.4861 0.5197 0.0325 -0.0039 -0.0026 0.0594  51  VAL A CB  
403  C  CG1 . VAL A 56  ? 0.4899 0.5330 0.0332 0.0109  -0.0129 0.0616  51  VAL A CG1 
404  C  CG2 . VAL A 56  ? 0.5104 0.5318 0.0332 0.0116  -0.0288 0.0552  51  VAL A CG2 
405  N  N   . VAL A 57  ? 0.5327 0.5226 0.0339 0.0110  -0.0452 0.0463  52  VAL A N   
406  C  CA  . VAL A 57  ? 0.5541 0.5301 0.0367 0.0173  -0.0206 0.0723  52  VAL A CA  
407  C  C   . VAL A 57  ? 0.5560 0.5280 0.0295 -0.0129 -0.0366 0.0299  52  VAL A C   
408  O  O   . VAL A 57  ? 0.5550 0.5259 0.0303 -0.0357 -0.0282 0.0436  52  VAL A O   
409  C  CB  . VAL A 57  ? 0.5730 0.5337 0.0314 0.0349  -0.0142 0.0528  52  VAL A CB  
410  C  CG1 . VAL A 57  ? 0.6181 0.5760 0.0313 0.0243  -0.0337 0.0458  52  VAL A CG1 
411  C  CG2 . VAL A 57  ? 0.6160 0.5475 0.0414 0.0097  0.0091  0.0848  52  VAL A CG2 
412  N  N   . GLY A 58  ? 0.5036 0.5484 0.0356 -0.0095 -0.0695 0.0119  53  GLY A N   
413  C  CA  . GLY A 58  ? 0.4932 0.5579 0.0454 -0.0230 -0.0388 -0.0057 53  GLY A CA  
414  C  C   . GLY A 58  ? 0.4911 0.5499 0.0349 -0.0437 -0.0661 -0.0028 53  GLY A C   
415  O  O   . GLY A 58  ? 0.5029 0.5759 0.0309 -0.0524 -0.0514 0.0020  53  GLY A O   
416  N  N   . GLY A 59  ? 0.5335 0.5341 0.0269 -0.0397 -0.0282 0.0048  54  GLY A N   
417  C  CA  . GLY A 59  ? 0.5452 0.5402 0.0262 -0.0265 0.0044  0.0206  54  GLY A CA  
418  C  C   . GLY A 59  ? 0.5470 0.5327 0.0276 -0.0117 0.0093  0.0324  54  GLY A C   
419  O  O   . GLY A 59  ? 0.5406 0.4886 0.0432 -0.0369 -0.0154 -0.0089 54  GLY A O   
420  N  N   . GLN A 60  ? 0.5347 0.5337 0.0286 0.0097  -0.0109 0.0388  55  GLN A N   
421  C  CA  . GLN A 60  ? 0.5133 0.5525 0.0287 -0.0088 0.0146  0.0393  55  GLN A CA  
422  C  C   . GLN A 60  ? 0.5270 0.5436 0.0309 -0.0107 0.0138  0.0514  55  GLN A C   
423  O  O   . GLN A 60  ? 0.5160 0.5601 0.0259 0.0140  0.0097  0.0149  55  GLN A O   
424  C  CB  . GLN A 60  ? 0.5337 0.5457 0.0272 0.0000  -0.0289 0.0101  55  GLN A CB  
425  C  CG  . GLN A 60  ? 0.5498 0.5381 0.0517 -0.0156 -0.0522 0.0058  55  GLN A CG  
426  C  CD  . GLN A 60  ? 0.5477 0.5420 0.0400 -0.0157 -0.0400 0.0217  55  GLN A CD  
427  O  OE1 . GLN A 60  ? 0.5580 0.5683 0.0257 -0.0243 -0.0115 0.0091  55  GLN A OE1 
428  N  NE2 . GLN A 60  ? 0.5519 0.5674 0.1180 -0.0232 -0.0343 0.0033  55  GLN A NE2 
429  N  N   . ARG A 61  ? 0.5066 0.5285 0.0326 -0.0145 -0.0018 0.0605  56  ARG A N   
430  C  CA  . ARG A 61  ? 0.5088 0.5365 0.0296 -0.0009 -0.0120 0.0452  56  ARG A CA  
431  C  C   . ARG A 61  ? 0.5283 0.5415 0.0289 -0.0138 -0.0361 0.0237  56  ARG A C   
432  O  O   . ARG A 61  ? 0.5160 0.5450 0.0326 -0.0149 -0.0560 0.0235  56  ARG A O   
433  C  CB  . ARG A 61  ? 0.5292 0.5374 0.0981 -0.0203 0.0186  0.0059  56  ARG A CB  
434  C  CG  . ARG A 61  ? 0.5240 0.5709 0.1852 -0.0187 0.0566  0.0271  56  ARG A CG  
435  C  CD  . ARG A 61  ? 0.5171 0.6174 0.2453 0.0088  0.0775  0.0160  56  ARG A CD  
436  N  NE  . ARG A 61  ? 0.4881 0.6180 0.2401 0.0202  0.0633  0.0214  56  ARG A NE  
437  C  CZ  . ARG A 61  ? 0.4775 0.5721 0.1926 0.0149  0.0709  -0.0024 56  ARG A CZ  
438  N  NH1 . ARG A 61  ? 0.5026 0.5723 0.2297 0.0266  0.0911  0.0053  56  ARG A NH1 
439  N  NH2 . ARG A 61  ? 0.4647 0.5718 0.0989 0.0056  0.0977  -0.0273 56  ARG A NH2 
440  N  N   . ALA A 62  ? 0.5098 0.5215 0.0463 -0.0220 -0.0515 -0.0141 57  ALA A N   
441  C  CA  . ALA A 62  ? 0.5362 0.5196 0.0534 -0.0207 -0.0482 0.0041  57  ALA A CA  
442  C  C   . ALA A 62  ? 0.5347 0.5113 0.0299 -0.0177 -0.0475 -0.0054 57  ALA A C   
443  O  O   . ALA A 62  ? 0.5209 0.5038 0.0703 -0.0250 -0.0998 -0.0151 57  ALA A O   
444  C  CB  . ALA A 62  ? 0.5478 0.5254 0.0685 -0.0090 -0.0233 0.0024  57  ALA A CB  
445  N  N   . ALA A 63  ? 0.5223 0.5157 0.0255 -0.0128 -0.0031 0.0090  58  ALA A N   
446  C  CA  . ALA A 63  ? 0.5413 0.5163 0.0436 -0.0061 -0.0313 -0.0034 58  ALA A CA  
447  C  C   . ALA A 63  ? 0.5644 0.5001 0.0262 0.0155  -0.0159 -0.0139 58  ALA A C   
448  O  O   . ALA A 63  ? 0.5558 0.5419 0.0305 0.0229  -0.0298 -0.0435 58  ALA A O   
449  C  CB  . ALA A 63  ? 0.5370 0.5123 0.0762 -0.0131 -0.0214 0.0349  58  ALA A CB  
450  N  N   . TRP A 64  ? 0.5523 0.5044 0.0264 0.0081  -0.0107 0.0205  59  TRP A N   
451  C  CA  . TRP A 64  ? 0.5597 0.4934 0.0275 -0.0060 -0.0163 0.0284  59  TRP A CA  
452  C  C   . TRP A 64  ? 0.5625 0.5042 0.0268 -0.0043 -0.0035 0.0263  59  TRP A C   
453  O  O   . TRP A 64  ? 0.6015 0.5692 0.0334 -0.0075 -0.0519 0.0434  59  TRP A O   
454  C  CB  . TRP A 64  ? 0.5565 0.5016 0.0459 -0.0075 -0.0228 0.0401  59  TRP A CB  
455  C  CG  . TRP A 64  ? 0.5848 0.5358 0.0303 0.0114  -0.0266 0.0426  59  TRP A CG  
456  C  CD1 . TRP A 64  ? 0.6110 0.5599 0.0271 0.0196  -0.0086 0.0289  59  TRP A CD1 
457  C  CD2 . TRP A 64  ? 0.5810 0.5131 0.0293 0.0247  -0.0211 0.0383  59  TRP A CD2 
458  N  NE1 . TRP A 64  ? 0.6081 0.5583 0.0338 0.0241  0.0054  0.0672  59  TRP A NE1 
459  C  CE2 . TRP A 64  ? 0.5916 0.5435 0.0311 0.0449  -0.0066 0.0534  59  TRP A CE2 
460  C  CE3 . TRP A 64  ? 0.6109 0.5407 0.0329 0.0051  -0.0462 0.0446  59  TRP A CE3 
461  C  CZ2 . TRP A 64  ? 0.5909 0.5379 0.0319 0.0462  -0.0333 0.0457  59  TRP A CZ2 
462  C  CZ3 . TRP A 64  ? 0.6092 0.5643 0.0731 0.0122  -0.0525 0.0552  59  TRP A CZ3 
463  C  CH2 . TRP A 64  ? 0.5938 0.5598 0.0397 0.0249  -0.0413 0.0395  59  TRP A CH2 
464  N  N   . ARG A 65  ? 0.5464 0.5076 0.0270 0.0023  -0.0276 0.0094  60  ARG A N   
465  C  CA  . ARG A 65  ? 0.5562 0.5264 0.0369 0.0140  -0.0398 0.0280  60  ARG A CA  
466  C  C   . ARG A 65  ? 0.5826 0.5516 0.0327 0.0174  -0.0569 0.0266  60  ARG A C   
467  O  O   . ARG A 65  ? 0.5907 0.5874 0.0468 0.0293  -0.1092 0.0087  60  ARG A O   
468  C  CB  . ARG A 65  ? 0.5520 0.5223 0.0630 0.0130  -0.0283 0.0071  60  ARG A CB  
469  C  CG  . ARG A 65  ? 0.5387 0.5237 0.0626 0.0189  -0.0325 0.0163  60  ARG A CG  
470  C  CD  . ARG A 65  ? 0.5516 0.5454 0.0806 0.0164  -0.0188 0.0148  60  ARG A CD  
471  N  NE  . ARG A 65  ? 0.5822 0.5726 0.1639 -0.0020 0.0236  0.0036  60  ARG A NE  
472  C  CZ  . ARG A 65  ? 0.6299 0.6164 0.2669 -0.0313 0.0604  -0.0355 60  ARG A CZ  
473  N  NH1 . ARG A 65  ? 0.6627 0.6825 0.3969 -0.0686 0.0766  -0.0878 60  ARG A NH1 
474  N  NH2 . ARG A 65  ? 0.6338 0.6246 0.2612 -0.0338 0.0344  -0.0183 60  ARG A NH2 
475  N  N   . VAL A 66  ? 0.5831 0.5332 0.0540 0.0078  -0.0420 -0.0046 61  VAL A N   
476  C  CA  . VAL A 66  ? 0.6275 0.5511 0.0811 0.0037  -0.0555 -0.0071 61  VAL A CA  
477  C  C   . VAL A 66  ? 0.6480 0.5669 0.0371 -0.0038 -0.0850 0.0098  61  VAL A C   
478  O  O   . VAL A 66  ? 0.6404 0.5819 0.0350 -0.0117 -0.0657 -0.0369 61  VAL A O   
479  C  CB  . VAL A 66  ? 0.6529 0.5661 0.0898 -0.0163 -0.0486 -0.0146 61  VAL A CB  
480  C  CG1 . VAL A 66  ? 0.6811 0.5984 0.1714 -0.0188 -0.0325 -0.0320 61  VAL A CG1 
481  C  CG2 . VAL A 66  ? 0.6573 0.5707 0.0798 -0.0196 -0.0733 -0.0046 61  VAL A CG2 
482  N  N   . LEU A 67  ? 0.6483 0.5562 0.0349 0.0133  -0.0595 0.0443  62  LEU A N   
483  C  CA  . LEU A 67  ? 0.6752 0.5904 0.0320 0.0453  -0.0613 0.0182  62  LEU A CA  
484  C  C   . LEU A 67  ? 0.7179 0.6025 0.0263 0.0480  -0.0160 0.0167  62  LEU A C   
485  O  O   . LEU A 67  ? 0.7653 0.6321 0.0286 0.0325  -0.0489 -0.0052 62  LEU A O   
486  C  CB  . LEU A 67  ? 0.6662 0.5674 0.0367 0.0486  -0.0752 0.0312  62  LEU A CB  
487  C  CG  . LEU A 67  ? 0.6667 0.5404 0.0359 0.0547  -0.0779 0.0173  62  LEU A CG  
488  C  CD1 . LEU A 67  ? 0.6991 0.5287 0.0421 0.0559  -0.1005 0.0218  62  LEU A CD1 
489  C  CD2 . LEU A 67  ? 0.6714 0.5499 0.0447 0.0566  -0.0972 0.0412  62  LEU A CD2 
490  N  N   . SER A 68  ? 0.7497 0.6129 0.0350 0.0589  -0.0269 0.0688  63  SER A N   
491  C  CA  . SER A 68  ? 0.7982 0.6181 0.0318 0.0838  -0.0084 0.0600  63  SER A CA  
492  C  C   . SER A 68  ? 0.8244 0.7046 0.0376 0.0971  -0.0014 0.0904  63  SER A C   
493  O  O   . SER A 68  ? 0.8869 0.8239 0.0421 0.1123  -0.0666 0.0867  63  SER A O   
494  C  CB  . SER A 68  ? 0.8320 0.5970 0.0537 0.0849  0.0137  0.0534  63  SER A CB  
495  O  OG  . SER A 68  ? 0.8968 0.6194 0.1286 0.0625  -0.0323 0.0438  63  SER A OG  
496  N  N   . SER A 69  ? 0.8138 0.7736 0.0403 0.1125  -0.0765 0.0635  64  SER A N   
497  C  CA  . SER A 69  ? 0.7875 0.8144 0.0968 0.1200  -0.1472 0.0482  64  SER A CA  
498  C  C   . SER A 69  ? 0.8148 0.8435 0.0525 0.1370  -0.1325 0.0400  64  SER A C   
499  O  O   . SER A 69  ? 0.8645 0.8923 0.0833 0.1403  -0.1936 0.0738  64  SER A O   
500  C  CB  . SER A 69  ? 0.7838 0.8500 0.1831 0.1181  -0.1228 0.0610  64  SER A CB  
501  O  OG  . SER A 69  ? 0.8356 0.9151 0.2367 0.0897  -0.0928 0.0699  64  SER A OG  
502  N  N   . ILE A 70  ? 0.8375 0.8338 0.0512 0.1225  -0.1424 -0.0480 65  ILE A N   
503  C  CA  . ILE A 70  ? 0.8747 0.7894 0.0614 0.1006  -0.1632 -0.0787 65  ILE A CA  
504  C  C   . ILE A 70  ? 0.9272 0.8261 0.1042 0.0930  -0.1397 -0.0754 65  ILE A C   
505  O  O   . ILE A 70  ? 0.9927 0.8899 0.0892 0.0997  -0.0849 -0.0700 65  ILE A O   
506  C  CB  . ILE A 70  ? 0.8853 0.7739 0.0836 0.0777  -0.1231 -0.1013 65  ILE A CB  
507  C  CG1 . ILE A 70  ? 0.8570 0.7639 0.1286 0.0757  -0.1030 -0.0908 65  ILE A CG1 
508  C  CG2 . ILE A 70  ? 0.8901 0.7695 0.1334 0.0744  -0.1203 -0.1256 65  ILE A CG2 
509  C  CD1 . ILE A 70  ? 0.8573 0.7670 0.1170 0.0457  -0.1270 -0.1074 65  ILE A CD1 
510  N  N   . GLU A 71  ? 0.9376 0.8181 0.1268 0.1117  -0.1493 -0.0162 66  GLU A N   
511  C  CA  . GLU A 71  ? 0.9703 0.8502 0.1194 0.1088  -0.1057 -0.0205 66  GLU A CA  
512  C  C   . GLU A 71  ? 1.0317 0.9136 0.1415 0.1217  -0.1130 0.0157  66  GLU A C   
513  O  O   . GLU A 71  ? 1.0240 1.0544 0.1378 0.0965  -0.1588 0.0320  66  GLU A O   
514  C  CB  . GLU A 71  ? 0.9650 0.8318 0.1192 0.1182  -0.0691 -0.0051 66  GLU A CB  
515  C  CG  . GLU A 71  ? 0.9612 0.8263 0.1150 0.1298  -0.0250 0.0431  66  GLU A CG  
516  C  CD  . GLU A 71  ? 0.9733 0.8079 0.1467 0.1172  0.0111  0.0125  66  GLU A CD  
517  O  OE1 . GLU A 71  ? 0.9930 0.8275 0.1163 0.1599  -0.0123 0.0580  66  GLU A OE1 
518  O  OE2 . GLU A 71  ? 0.9920 0.7973 0.1569 0.1145  0.0452  0.0127  66  GLU A OE2 
519  N  N   . GLN A 72  ? 1.0817 0.9515 0.0668 0.1327  -0.0950 0.0654  67  GLN A N   
520  C  CA  . GLN A 72  ? 1.1581 0.9906 0.1628 0.1298  -0.0942 0.1285  67  GLN A CA  
521  C  C   . GLN A 72  ? 1.2034 1.0794 0.1399 0.0968  -0.0794 0.1023  67  GLN A C   
522  O  O   . GLN A 72  ? 1.2031 1.0506 0.2161 0.1180  -0.1574 0.2245  67  GLN A O   
523  C  CB  . GLN A 72  ? 1.1951 0.9787 0.2193 0.1424  -0.0685 0.1478  67  GLN A CB  
524  C  CG  . GLN A 72  ? 1.2616 0.9733 0.2279 0.1289  -0.0535 0.2024  67  GLN A CG  
525  C  CD  . GLN A 72  ? 1.3265 1.0432 0.3412 0.1193  -0.0201 0.1694  67  GLN A CD  
526  O  OE1 . GLN A 72  ? 1.3452 1.1410 0.2672 0.0862  -0.0062 0.0744  67  GLN A OE1 
527  N  NE2 . GLN A 72  ? 1.3763 1.0597 0.4296 0.1001  0.0097  0.1550  67  GLN A NE2 
528  N  N   . LYS A 73  ? 1.2018 1.1527 0.1702 0.0870  -0.0786 0.0730  68  LYS A N   
529  C  CA  . LYS A 73  ? 1.1838 1.2322 0.2525 0.0898  -0.1466 0.0523  68  LYS A CA  
530  C  C   . LYS A 73  ? 1.2322 1.3071 0.0471 0.0714  -0.1571 0.0315  68  LYS A C   
531  O  O   . LYS A 73  ? 1.2516 1.4368 0.0906 0.0494  -0.1401 -0.1219 68  LYS A O   
532  C  CB  . LYS A 73  ? 1.1558 1.2271 0.3101 0.0789  -0.1757 0.0926  68  LYS A CB  
533  C  CG  . LYS A 73  ? 1.1361 1.2592 0.4533 0.0694  -0.1589 0.0876  68  LYS A CG  
534  C  CD  . LYS A 73  ? 1.1350 1.2754 0.4822 0.0817  -0.1689 0.1133  68  LYS A CD  
535  C  CE  . LYS A 73  ? 1.1392 1.2785 0.5788 0.0625  -0.1547 0.0782  68  LYS A CE  
536  N  NZ  . LYS A 73  ? 1.1381 1.2929 0.6780 0.0538  -0.1446 0.0617  68  LYS A NZ  
537  N  N   . SER A 74  ? 1.2601 1.3385 0.0381 0.0638  -0.1215 -0.0398 69  SER A N   
538  C  CA  . SER A 74  ? 1.2854 1.3737 0.0732 0.1055  -0.0513 0.0160  69  SER A CA  
539  C  C   . SER A 74  ? 1.3392 1.4396 0.1819 0.0532  0.0215  -0.0119 69  SER A C   
540  O  O   . SER A 74  ? 1.3394 1.4444 0.2872 0.0465  0.1457  -0.0914 69  SER A O   
541  C  CB  . SER A 74  ? 1.2526 1.3299 0.2430 0.1415  -0.1119 0.0167  69  SER A CB  
542  O  OG  . SER A 74  ? 1.2448 1.2988 0.2436 0.2297  -0.1834 0.0302  69  SER A OG  
543  N  N   . ASN A 75  ? 1.3376 1.4622 0.2216 0.0289  0.0448  -0.0298 70  ASN A N   
544  C  CA  . ASN A 75  ? 1.3310 1.5128 0.2960 0.0226  0.0420  0.0710  70  ASN A CA  
545  C  C   . ASN A 75  ? 1.3532 1.5525 0.4520 0.0365  -0.0070 0.1169  70  ASN A C   
546  O  O   . ASN A 75  ? 1.3365 1.5571 0.3491 0.0400  0.0235  0.2571  70  ASN A O   
547  C  CB  . ASN A 75  ? 1.2774 1.5016 0.2750 0.0012  0.1175  0.0892  70  ASN A CB  
548  C  CG  . ASN A 75  ? 1.2334 1.5093 0.3939 -0.0236 0.1341  0.0997  70  ASN A CG  
549  O  OD1 . ASN A 75  ? 1.1897 1.4929 0.4319 -0.0629 0.0985  0.1143  70  ASN A OD1 
550  N  ND2 . ASN A 75  ? 1.2029 1.5385 0.3937 -0.0533 0.1746  0.1671  70  ASN A ND2 
551  N  N   . GLU A 76  ? 1.3875 1.6452 0.4182 0.0289  -0.0555 0.0910  71  GLU A N   
552  C  CA  . GLU A 76  ? 1.3957 1.6817 0.6649 0.0196  -0.0870 0.1479  71  GLU A CA  
553  C  C   . GLU A 76  ? 1.4768 1.7120 0.6762 -0.0250 -0.0707 0.1751  71  GLU A C   
554  O  O   . GLU A 76  ? 1.4963 1.7302 0.9486 -0.0729 0.0289  0.2081  71  GLU A O   
555  C  CB  . GLU A 76  ? 1.3806 1.6718 0.6961 0.0358  -0.0900 0.0993  71  GLU A CB  
556  C  CG  . GLU A 76  ? 1.3516 1.6327 0.6697 0.0318  -0.0974 0.0840  71  GLU A CG  
557  C  CD  . GLU A 76  ? 1.3242 1.5829 0.6990 0.0383  -0.1468 0.0526  71  GLU A CD  
558  O  OE1 . GLU A 76  ? 1.3295 1.5649 0.7282 0.0468  -0.1561 0.0338  71  GLU A OE1 
559  O  OE2 . GLU A 76  ? 1.3111 1.5378 0.7632 0.0472  -0.2302 0.0218  71  GLU A OE2 
560  N  N   . GLU A 77  ? 1.4622 1.7422 0.7881 -0.0496 -0.0955 0.2673  72  GLU A N   
561  C  CA  . GLU A 77  ? 1.3782 1.7368 0.8736 -0.0776 -0.1030 0.2973  72  GLU A CA  
562  C  C   . GLU A 77  ? 1.2866 1.7579 0.8774 -0.1228 -0.0762 0.3197  72  GLU A C   
563  O  O   . GLU A 77  ? 1.2472 1.7811 0.9323 -0.1835 -0.1326 0.3208  72  GLU A O   
564  C  CB  . GLU A 77  ? 1.3943 1.7536 0.8621 -0.0647 -0.1221 0.3390  72  GLU A CB  
565  C  CG  . GLU A 77  ? 1.4278 1.7967 0.9447 -0.0696 -0.0982 0.3548  72  GLU A CG  
566  C  CD  . GLU A 77  ? 1.4794 1.8255 1.0084 -0.0623 -0.0897 0.3737  72  GLU A CD  
567  O  OE1 . GLU A 77  ? 1.5300 1.8711 1.0032 -0.0425 -0.1231 0.4088  72  GLU A OE1 
568  O  OE2 . GLU A 77  ? 1.5000 1.8156 1.0514 -0.0458 -0.0557 0.4338  72  GLU A OE2 
569  N  N   . GLY A 78  ? 1.1957 1.7380 0.8519 -0.1478 0.0008  0.3494  73  GLY A N   
570  C  CA  . GLY A 78  ? 1.1575 1.7132 0.8183 -0.1367 0.0021  0.3600  73  GLY A CA  
571  C  C   . GLY A 78  ? 1.1478 1.6992 0.7765 -0.1540 0.0634  0.3709  73  GLY A C   
572  O  O   . GLY A 78  ? 1.2135 1.6963 0.7190 -0.1852 0.0844  0.3445  73  GLY A O   
573  N  N   . GLY A 83  ? 1.0308 0.9172 0.2620 0.0471  0.0461  -0.0821 78  GLY A N   
574  C  CA  . GLY A 83  ? 1.0059 0.8902 0.1621 0.0483  0.0916  -0.0521 78  GLY A CA  
575  C  C   . GLY A 83  ? 0.9929 0.8723 0.0920 0.0662  0.0742  -0.0294 78  GLY A C   
576  O  O   . GLY A 83  ? 1.0637 0.9263 0.1595 0.0936  0.1113  -0.0387 78  GLY A O   
577  N  N   . PRO A 84  ? 0.9293 0.8368 0.1405 0.0352  0.1505  -0.0559 79  PRO A N   
578  C  CA  . PRO A 84  ? 0.9245 0.8196 0.0680 -0.0086 0.1891  0.0466  79  PRO A CA  
579  C  C   . PRO A 84  ? 0.9313 0.7894 0.0522 0.0143  0.1556  0.0143  79  PRO A C   
580  O  O   . PRO A 84  ? 0.8407 0.7055 0.0949 -0.0382 0.1154  -0.0172 79  PRO A O   
581  C  CB  . PRO A 84  ? 0.9000 0.8027 0.1210 0.0074  0.1819  0.0428  79  PRO A CB  
582  C  CG  . PRO A 84  ? 0.8789 0.8033 0.0947 0.0363  0.1755  -0.0023 79  PRO A CG  
583  C  CD  . PRO A 84  ? 0.9067 0.8173 0.1728 0.0395  0.1838  -0.0365 79  PRO A CD  
584  N  N   . GLU A 85  ? 0.9603 0.7791 0.0413 0.0131  0.1213  -0.0121 80  GLU A N   
585  C  CA  . GLU A 85  ? 0.9226 0.7757 0.0373 0.0397  0.1032  -0.0044 80  GLU A CA  
586  C  C   . GLU A 85  ? 0.9081 0.7715 0.0310 0.0171  0.0097  -0.0642 80  GLU A C   
587  O  O   . GLU A 85  ? 1.0475 0.8632 0.0479 0.0798  0.1494  -0.0128 80  GLU A O   
588  C  CB  . GLU A 85  ? 0.9195 0.7593 0.0483 0.0536  0.1433  0.0060  80  GLU A CB  
589  C  CG  . GLU A 85  ? 0.9433 0.7514 0.0651 0.0559  0.1383  0.0081  80  GLU A CG  
590  C  CD  . GLU A 85  ? 0.9533 0.7623 0.0891 0.0663  0.1825  -0.0377 80  GLU A CD  
591  O  OE1 . GLU A 85  ? 0.9563 0.7298 0.1985 0.0456  0.1168  -0.0503 80  GLU A OE1 
592  O  OE2 . GLU A 85  ? 0.9589 0.7183 0.2655 0.0334  0.2021  -0.0384 80  GLU A OE2 
593  N  N   . VAL A 86  ? 0.8696 0.7489 0.0273 0.0343  0.0313  -0.0227 81  VAL A N   
594  C  CA  . VAL A 86  ? 0.8267 0.7186 0.0261 0.0309  0.0129  -0.0192 81  VAL A CA  
595  C  C   . VAL A 86  ? 0.7880 0.6893 0.0351 0.0189  0.0846  -0.0148 81  VAL A C   
596  O  O   . VAL A 86  ? 0.7670 0.7023 0.0400 0.0608  0.0685  0.0806  81  VAL A O   
597  C  CB  . VAL A 86  ? 0.8395 0.7306 0.1222 0.0297  -0.0101 -0.0384 81  VAL A CB  
598  C  CG1 . VAL A 86  ? 0.8654 0.7495 0.1176 0.0334  -0.0197 -0.0415 81  VAL A CG1 
599  C  CG2 . VAL A 86  ? 0.8681 0.7307 0.1586 0.0203  -0.0403 -0.0206 81  VAL A CG2 
600  N  N   . ARG A 87  ? 0.7816 0.7101 0.0318 0.0265  0.0398  0.0562  82  ARG A N   
601  C  CA  . ARG A 87  ? 0.7593 0.6963 0.0363 0.0079  0.0690  0.0554  82  ARG A CA  
602  C  C   . ARG A 87  ? 0.6778 0.6660 0.0366 0.0068  0.0686  0.0514  82  ARG A C   
603  O  O   . ARG A 87  ? 0.7236 0.5797 0.0706 0.0049  0.0518  0.0284  82  ARG A O   
604  C  CB  . ARG A 87  ? 0.7500 0.6834 0.0605 -0.0098 0.1237  0.0944  82  ARG A CB  
605  C  CG  . ARG A 87  ? 0.7455 0.7158 0.1003 -0.0102 0.1148  0.0859  82  ARG A CG  
606  C  CD  . ARG A 87  ? 0.7472 0.7733 0.1230 -0.0278 0.1251  0.0751  82  ARG A CD  
607  N  NE  . ARG A 87  ? 0.7896 0.8711 0.3460 -0.0112 0.0780  0.0109  82  ARG A NE  
608  C  CZ  . ARG A 87  ? 0.8230 0.9830 0.4184 0.0021  0.0363  -0.0697 82  ARG A CZ  
609  N  NH1 . ARG A 87  ? 0.8360 1.0544 0.3472 -0.0211 0.0225  -0.0785 82  ARG A NH1 
610  N  NH2 . ARG A 87  ? 0.8658 1.0075 0.5829 0.0333  0.0307  -0.0861 82  ARG A NH2 
611  N  N   . GLU A 88  ? 0.6853 0.6575 0.0445 0.0041  0.1092  0.0270  83  GLU A N   
612  C  CA  . GLU A 88  ? 0.6525 0.6995 0.0716 0.0002  0.1643  0.0468  83  GLU A CA  
613  C  C   . GLU A 88  ? 0.6512 0.6499 0.0454 -0.0064 0.1095  0.0228  83  GLU A C   
614  O  O   . GLU A 88  ? 0.6028 0.6241 0.0363 -0.0256 0.0754  0.0223  83  GLU A O   
615  C  CB  . GLU A 88  ? 0.7274 0.7001 0.0627 0.0145  0.1587  0.0348  83  GLU A CB  
616  C  CG  . GLU A 88  ? 0.7285 0.7742 0.1371 0.0020  0.2140  0.0340  83  GLU A CG  
617  C  CD  . GLU A 88  ? 0.7520 0.7962 0.2576 0.0297  0.2341  0.0206  83  GLU A CD  
618  O  OE1 . GLU A 88  ? 0.8211 0.8259 0.2464 0.0465  0.1646  0.0519  83  GLU A OE1 
619  O  OE2 . GLU A 88  ? 0.7709 0.8807 0.3671 -0.0089 0.3022  0.0459  83  GLU A OE2 
620  N  N   . TYR A 89  ? 0.6654 0.6978 0.0382 0.0006  0.0906  0.0029  84  TYR A N   
621  C  CA  . TYR A 89  ? 0.6516 0.6868 0.0342 0.0137  0.0739  0.0116  84  TYR A CA  
622  C  C   . TYR A 89  ? 0.6637 0.6720 0.0272 0.0392  0.0343  0.0078  84  TYR A C   
623  O  O   . TYR A 89  ? 0.6192 0.6841 0.0287 0.0784  0.0403  0.0263  84  TYR A O   
624  C  CB  . TYR A 89  ? 0.6472 0.6818 0.0370 -0.0055 0.0795  0.0307  84  TYR A CB  
625  C  CG  . TYR A 89  ? 0.6057 0.6278 0.0387 -0.0420 0.0818  0.0271  84  TYR A CG  
626  C  CD1 . TYR A 89  ? 0.5946 0.6812 0.0334 -0.0673 0.0593  0.0277  84  TYR A CD1 
627  C  CD2 . TYR A 89  ? 0.6399 0.6528 0.0282 -0.0396 0.0416  -0.0004 84  TYR A CD2 
628  C  CE1 . TYR A 89  ? 0.6471 0.6410 0.0265 -0.0566 0.0256  -0.0091 84  TYR A CE1 
629  C  CE2 . TYR A 89  ? 0.6073 0.6880 0.0313 -0.0522 0.0364  0.0461  84  TYR A CE2 
630  C  CZ  . TYR A 89  ? 0.6399 0.6385 0.0291 -0.0451 0.0285  -0.0411 84  TYR A CZ  
631  O  OH  . TYR A 89  ? 0.6786 0.6766 0.0723 -0.0854 0.0971  0.0580  84  TYR A OH  
632  N  N   . ARG A 90  ? 0.6203 0.6630 0.0279 0.0511  0.0364  0.0184  85  ARG A N   
633  C  CA  . ARG A 90  ? 0.6346 0.6504 0.0277 0.0554  -0.0008 0.0379  85  ARG A CA  
634  C  C   . ARG A 90  ? 0.6375 0.6218 0.0295 0.0684  0.0096  0.0499  85  ARG A C   
635  O  O   . ARG A 90  ? 0.6382 0.6066 0.0336 0.0766  0.0640  0.0379  85  ARG A O   
636  C  CB  . ARG A 90  ? 0.6361 0.6520 0.0327 0.0682  0.0047  0.0677  85  ARG A CB  
637  C  CG  . ARG A 90  ? 0.6475 0.6836 0.0295 0.0536  0.0054  0.0524  85  ARG A CG  
638  C  CD  . ARG A 90  ? 0.6718 0.6800 0.0303 0.0540  0.0295  0.0511  85  ARG A CD  
639  N  NE  . ARG A 90  ? 0.7252 0.7011 0.0411 0.0342  0.0654  0.0615  85  ARG A NE  
640  C  CZ  . ARG A 90  ? 0.7274 0.7210 0.1121 0.0274  0.0819  0.0305  85  ARG A CZ  
641  N  NH1 . ARG A 90  ? 0.7703 0.7399 0.1611 0.0285  0.1030  0.0085  85  ARG A NH1 
642  N  NH2 . ARG A 90  ? 0.7790 0.7581 0.1076 0.0198  0.0838  0.0132  85  ARG A NH2 
643  N  N   . GLU A 91  ? 0.6470 0.6917 0.0285 0.0606  0.0279  0.0384  86  GLU A N   
644  C  CA  . GLU A 91  ? 0.6515 0.6528 0.0301 0.0496  0.0287  0.0487  86  GLU A CA  
645  C  C   . GLU A 91  ? 0.6158 0.6412 0.0299 0.0469  0.0372  0.0396  86  GLU A C   
646  O  O   . GLU A 91  ? 0.5461 0.5598 0.0927 0.0259  0.0279  0.0467  86  GLU A O   
647  C  CB  . GLU A 91  ? 0.6580 0.7008 0.0308 0.0302  0.0438  0.0427  86  GLU A CB  
648  C  CG  . GLU A 91  ? 0.6920 0.7089 0.0541 0.0280  0.0522  0.0645  86  GLU A CG  
649  C  CD  . GLU A 91  ? 0.7224 0.7745 0.1971 0.0300  0.1062  0.1155  86  GLU A CD  
650  O  OE1 . GLU A 91  ? 0.7371 0.8140 0.2099 0.0608  0.2237  0.1010  86  GLU A OE1 
651  O  OE2 . GLU A 91  ? 0.7979 0.8615 0.2109 0.0132  0.0846  0.1385  86  GLU A OE2 
652  N  N   . LYS A 92  ? 0.5801 0.6226 0.0279 0.0532  0.0218  0.0341  87  LYS A N   
653  C  CA  . LYS A 92  ? 0.5234 0.5997 0.0314 0.0534  0.0066  0.0589  87  LYS A CA  
654  C  C   . LYS A 92  ? 0.4739 0.5766 0.0264 0.0415  0.0134  0.0209  87  LYS A C   
655  O  O   . LYS A 92  ? 0.4805 0.5702 0.0610 0.0333  0.0069  0.0018  87  LYS A O   
656  C  CB  . LYS A 92  ? 0.5343 0.6094 0.0328 0.0752  -0.0026 0.0652  87  LYS A CB  
657  C  CG  . LYS A 92  ? 0.6187 0.6371 0.0326 0.0847  -0.0451 0.0416  87  LYS A CG  
658  C  CD  . LYS A 92  ? 0.6677 0.6850 0.1455 0.0928  -0.0457 0.0586  87  LYS A CD  
659  C  CE  . LYS A 92  ? 0.6672 0.7526 0.1716 0.0943  -0.0593 0.0775  87  LYS A CE  
660  N  NZ  . LYS A 92  ? 0.7260 0.7988 0.2206 0.1138  -0.1056 0.0769  87  LYS A NZ  
661  N  N   . VAL A 93  ? 0.4760 0.5870 0.0267 0.0319  0.0210  0.0165  88  VAL A N   
662  C  CA  . VAL A 93  ? 0.4723 0.5682 0.0274 0.0225  0.0221  0.0241  88  VAL A CA  
663  C  C   . VAL A 93  ? 0.4907 0.5520 0.0279 0.0280  0.0305  0.0192  88  VAL A C   
664  O  O   . VAL A 93  ? 0.4761 0.5730 0.0258 -0.0114 0.0002  0.0167  88  VAL A O   
665  C  CB  . VAL A 93  ? 0.4784 0.5834 0.0272 0.0128  0.0103  0.0301  88  VAL A CB  
666  C  CG1 . VAL A 93  ? 0.4397 0.5748 0.0267 0.0163  -0.0052 0.0269  88  VAL A CG1 
667  C  CG2 . VAL A 93  ? 0.4911 0.6110 0.0264 0.0115  0.0018  0.0253  88  VAL A CG2 
668  N  N   . GLU A 94  ? 0.4745 0.5896 0.0285 0.0226  0.0127  0.0407  89  GLU A N   
669  C  CA  . GLU A 94  ? 0.4847 0.5731 0.0317 0.0348  0.0305  0.0507  89  GLU A CA  
670  C  C   . GLU A 94  ? 0.4848 0.5567 0.0350 0.0213  0.0512  0.0481  89  GLU A C   
671  O  O   . GLU A 94  ? 0.4742 0.5082 0.0407 0.0311  0.0472  0.0497  89  GLU A O   
672  C  CB  . GLU A 94  ? 0.5211 0.5867 0.0375 0.0360  0.0241  0.0801  89  GLU A CB  
673  C  CG  . GLU A 94  ? 0.5418 0.6144 0.0328 0.0487  0.0077  0.0663  89  GLU A CG  
674  C  CD  . GLU A 94  ? 0.5587 0.6259 0.0506 0.0217  0.0517  0.1122  89  GLU A CD  
675  O  OE1 . GLU A 94  ? 0.5365 0.6353 0.1007 0.0119  0.0467  0.0451  89  GLU A OE1 
676  O  OE2 . GLU A 94  ? 0.6322 0.6520 0.0613 -0.0050 0.0534  0.1394  89  GLU A OE2 
677  N  N   . THR A 95  ? 0.4851 0.5771 0.0327 0.0187  0.0549  0.0237  90  THR A N   
678  C  CA  . THR A 95  ? 0.4836 0.5818 0.0354 0.0009  0.0579  0.0396  90  THR A CA  
679  C  C   . THR A 95  ? 0.4559 0.5558 0.0318 0.0062  0.0403  0.0383  90  THR A C   
680  O  O   . THR A 95  ? 0.4075 0.5250 0.0932 0.0018  0.0243  0.0045  90  THR A O   
681  C  CB  . THR A 95  ? 0.4827 0.6224 0.0292 0.0076  0.0418  0.0073  90  THR A CB  
682  O  OG1 . THR A 95  ? 0.5311 0.6775 0.0771 -0.0073 0.1297  0.0299  90  THR A OG1 
683  C  CG2 . THR A 95  ? 0.5035 0.6146 0.1185 -0.0045 0.0553  -0.0054 90  THR A CG2 
684  N  N   . GLU A 96  ? 0.4515 0.5557 0.0315 0.0082  0.0238  0.0513  91  GLU A N   
685  C  CA  . GLU A 96  ? 0.4878 0.5821 0.0304 0.0129  0.0122  0.0518  91  GLU A CA  
686  C  C   . GLU A 96  ? 0.4599 0.5372 0.0265 0.0123  -0.0152 0.0179  91  GLU A C   
687  O  O   . GLU A 96  ? 0.4545 0.5387 0.0273 0.0426  0.0289  0.0035  91  GLU A O   
688  C  CB  . GLU A 96  ? 0.5536 0.5894 0.0425 0.0045  -0.0118 0.0975  91  GLU A CB  
689  C  CG  . GLU A 96  ? 0.6158 0.6414 0.1868 0.0018  -0.0476 0.0862  91  GLU A CG  
690  C  CD  . GLU A 96  ? 0.6718 0.6302 0.2885 -0.0309 -0.0339 0.0773  91  GLU A CD  
691  O  OE1 . GLU A 96  ? 0.7215 0.6698 0.1927 -0.0013 -0.0972 0.1161  91  GLU A OE1 
692  O  OE2 . GLU A 96  ? 0.7070 0.6349 0.2973 -0.0312 -0.0682 0.0058  91  GLU A OE2 
693  N  N   . LEU A 97  ? 0.4255 0.5453 0.0267 0.0276  0.0017  0.0266  92  LEU A N   
694  C  CA  . LEU A 97  ? 0.4154 0.5353 0.0263 0.0132  -0.0081 0.0196  92  LEU A CA  
695  C  C   . LEU A 97  ? 0.4070 0.5179 0.0264 0.0165  0.0193  0.0057  92  LEU A C   
696  O  O   . LEU A 97  ? 0.4278 0.5460 0.0272 0.0271  0.0002  0.0313  92  LEU A O   
697  C  CB  . LEU A 97  ? 0.4110 0.5428 0.0257 -0.0049 -0.0054 0.0124  92  LEU A CB  
698  C  CG  . LEU A 97  ? 0.4298 0.5604 0.0345 -0.0006 -0.0306 -0.0061 92  LEU A CG  
699  C  CD1 . LEU A 97  ? 0.4505 0.5950 0.1158 0.0112  -0.0440 0.0051  92  LEU A CD1 
700  C  CD2 . LEU A 97  ? 0.4476 0.5825 0.0572 0.0026  -0.0039 -0.0177 92  LEU A CD2 
701  N  N   . GLN A 98  ? 0.4298 0.5641 0.0255 -0.0057 0.0072  0.0015  93  GLN A N   
702  C  CA  . GLN A 98  ? 0.4105 0.5506 0.0258 -0.0051 -0.0084 0.0115  93  GLN A CA  
703  C  C   . GLN A 98  ? 0.4017 0.5318 0.0276 -0.0018 -0.0137 0.0304  93  GLN A C   
704  O  O   . GLN A 98  ? 0.3907 0.4815 0.0801 -0.0227 0.0251  0.0125  93  GLN A O   
705  C  CB  . GLN A 98  ? 0.4003 0.5588 0.0366 0.0010  -0.0054 0.0391  93  GLN A CB  
706  C  CG  . GLN A 98  ? 0.4452 0.5623 0.0298 0.0100  -0.0097 0.0454  93  GLN A CG  
707  C  CD  . GLN A 98  ? 0.4398 0.5739 0.0703 0.0339  0.0126  0.0785  93  GLN A CD  
708  O  OE1 . GLN A 98  ? 0.4249 0.6079 0.1150 0.0491  0.0151  0.1055  93  GLN A OE1 
709  N  NE2 . GLN A 98  ? 0.4770 0.5575 0.0931 0.0238  0.0046  0.0875  93  GLN A NE2 
710  N  N   . GLY A 99  ? 0.3929 0.5352 0.0270 0.0002  0.0031  0.0292  94  GLY A N   
711  C  CA  . GLY A 99  ? 0.4026 0.5315 0.0254 -0.0063 0.0023  0.0046  94  GLY A CA  
712  C  C   . GLY A 99  ? 0.3963 0.5281 0.0402 -0.0036 0.0187  0.0142  94  GLY A C   
713  O  O   . GLY A 99  ? 0.3937 0.5564 0.0411 0.0084  -0.0047 -0.0114 94  GLY A O   
714  N  N   . VAL A 100 ? 0.4071 0.5287 0.0277 0.0126  0.0286  0.0107  95  VAL A N   
715  C  CA  . VAL A 100 ? 0.4366 0.5299 0.0264 0.0174  0.0104  0.0204  95  VAL A CA  
716  C  C   . VAL A 100 ? 0.4143 0.5071 0.0264 0.0179  -0.0034 0.0217  95  VAL A C   
717  O  O   . VAL A 100 ? 0.4162 0.4641 0.0284 0.0030  -0.0312 0.0154  95  VAL A O   
718  C  CB  . VAL A 100 ? 0.4539 0.5307 0.0268 0.0101  0.0245  0.0068  95  VAL A CB  
719  C  CG1 . VAL A 100 ? 0.4461 0.5467 0.0351 0.0034  0.0528  -0.0216 95  VAL A CG1 
720  C  CG2 . VAL A 100 ? 0.4628 0.5474 0.0274 0.0020  0.0253  0.0172  95  VAL A CG2 
721  N  N   . CYS A 101 ? 0.4020 0.4831 0.0291 0.0402  0.0026  0.0417  96  CYS A N   
722  C  CA  . CYS A 101 ? 0.4235 0.4946 0.0277 0.0229  0.0100  0.0323  96  CYS A CA  
723  C  C   . CYS A 101 ? 0.4172 0.4978 0.0473 0.0270  0.0142  0.0218  96  CYS A C   
724  O  O   . CYS A 101 ? 0.4132 0.4618 0.0449 0.0208  -0.0049 0.0325  96  CYS A O   
725  C  CB  . CYS A 101 ? 0.4435 0.5007 0.0371 0.0315  -0.0103 0.0492  96  CYS A CB  
726  S  SG  . CYS A 101 ? 0.4290 0.5481 0.0280 0.0140  -0.0238 0.0097  96  CYS A SG  
727  N  N   . ASP A 102 ? 0.4072 0.5252 0.0263 0.0128  0.0134  -0.0147 97  ASP A N   
728  C  CA  . ASP A 102 ? 0.4027 0.5549 0.0262 0.0120  -0.0182 -0.0046 97  ASP A CA  
729  C  C   . ASP A 102 ? 0.4198 0.5424 0.0279 0.0102  -0.0293 -0.0140 97  ASP A C   
730  O  O   . ASP A 102 ? 0.4253 0.5434 0.1064 0.0041  -0.0316 0.0146  97  ASP A O   
731  C  CB  . ASP A 102 ? 0.4116 0.5787 0.0479 0.0027  -0.0251 -0.0188 97  ASP A CB  
732  C  CG  . ASP A 102 ? 0.4265 0.5872 0.0669 0.0076  -0.0142 -0.0064 97  ASP A CG  
733  O  OD1 . ASP A 102 ? 0.4611 0.6314 0.0710 0.0229  -0.0385 0.0065  97  ASP A OD1 
734  O  OD2 . ASP A 102 ? 0.4731 0.6627 0.0591 -0.0341 0.0434  -0.0013 97  ASP A OD2 
735  N  N   . THR A 103 ? 0.4027 0.5301 0.0286 0.0274  -0.0350 -0.0014 98  THR A N   
736  C  CA  . THR A 103 ? 0.4265 0.5476 0.0297 0.0240  -0.0371 0.0203  98  THR A CA  
737  C  C   . THR A 103 ? 0.3932 0.5221 0.0702 0.0151  -0.0511 -0.0023 98  THR A C   
738  O  O   . THR A 103 ? 0.4209 0.5491 0.0343 0.0195  -0.0194 -0.0234 98  THR A O   
739  C  CB  . THR A 103 ? 0.4318 0.5514 0.0327 0.0495  -0.0397 0.0376  98  THR A CB  
740  O  OG1 . THR A 103 ? 0.4948 0.5682 0.0417 0.0403  -0.0483 0.0265  98  THR A OG1 
741  C  CG2 . THR A 103 ? 0.4558 0.5627 0.0334 0.0352  -0.0485 0.0337  98  THR A CG2 
742  N  N   . VAL A 104 ? 0.3706 0.5115 0.0353 0.0136  -0.0474 0.0080  99  VAL A N   
743  C  CA  . VAL A 104 ? 0.3770 0.5229 0.0391 0.0070  -0.0195 0.0209  99  VAL A CA  
744  C  C   . VAL A 104 ? 0.3822 0.5120 0.0263 -0.0008 -0.0173 -0.0091 99  VAL A C   
745  O  O   . VAL A 104 ? 0.4028 0.5052 0.0481 -0.0038 -0.0294 -0.0263 99  VAL A O   
746  C  CB  . VAL A 104 ? 0.3777 0.5275 0.1089 -0.0064 0.0081  0.0187  99  VAL A CB  
747  C  CG1 . VAL A 104 ? 0.4101 0.5551 0.1203 0.0065  -0.0021 0.0222  99  VAL A CG1 
748  C  CG2 . VAL A 104 ? 0.4028 0.5432 0.1117 -0.0082 0.0135  -0.0053 99  VAL A CG2 
749  N  N   . LEU A 105 ? 0.3967 0.5194 0.0272 -0.0092 -0.0258 0.0075  100 LEU A N   
750  C  CA  . LEU A 105 ? 0.3995 0.5241 0.0362 0.0015  -0.0184 -0.0018 100 LEU A CA  
751  C  C   . LEU A 105 ? 0.3965 0.5316 0.0917 -0.0106 -0.0027 -0.0257 100 LEU A C   
752  O  O   . LEU A 105 ? 0.4159 0.5236 0.1016 -0.0069 -0.0112 -0.0496 100 LEU A O   
753  C  CB  . LEU A 105 ? 0.4323 0.5379 0.0535 -0.0017 0.0019  0.0116  100 LEU A CB  
754  C  CG  . LEU A 105 ? 0.4448 0.5317 0.0610 0.0214  -0.0124 0.0161  100 LEU A CG  
755  C  CD1 . LEU A 105 ? 0.4574 0.5609 0.0675 0.0215  -0.0032 0.0002  100 LEU A CD1 
756  C  CD2 . LEU A 105 ? 0.4631 0.5700 0.0607 0.0223  -0.0054 0.0297  100 LEU A CD2 
757  N  N   . GLY A 106 ? 0.4256 0.5505 0.0691 0.0036  -0.0196 -0.0398 101 GLY A N   
758  C  CA  . GLY A 106 ? 0.4321 0.5731 0.0759 -0.0025 -0.0132 -0.0217 101 GLY A CA  
759  C  C   . GLY A 106 ? 0.4174 0.5849 0.0747 -0.0251 -0.0173 -0.0451 101 GLY A C   
760  O  O   . GLY A 106 ? 0.4269 0.5971 0.0968 -0.0338 0.0153  -0.0459 101 GLY A O   
761  N  N   . LEU A 107 ? 0.4055 0.6034 0.0379 -0.0246 -0.0369 -0.0536 102 LEU A N   
762  C  CA  . LEU A 107 ? 0.4197 0.6112 0.0423 -0.0174 -0.0276 -0.0493 102 LEU A CA  
763  C  C   . LEU A 107 ? 0.4356 0.6015 0.0766 -0.0228 -0.0351 -0.0429 102 LEU A C   
764  O  O   . LEU A 107 ? 0.4759 0.6099 0.0616 -0.0103 -0.0442 -0.0420 102 LEU A O   
765  C  CB  . LEU A 107 ? 0.4471 0.6111 0.0635 -0.0194 -0.0510 -0.0528 102 LEU A CB  
766  C  CG  . LEU A 107 ? 0.4508 0.6144 0.0715 -0.0171 -0.0548 -0.0487 102 LEU A CG  
767  C  CD1 . LEU A 107 ? 0.4644 0.6271 0.0974 -0.0236 -0.0331 -0.0240 102 LEU A CD1 
768  C  CD2 . LEU A 107 ? 0.4454 0.6296 0.0774 -0.0109 -0.0447 -0.0302 102 LEU A CD2 
769  N  N   . LEU A 108 ? 0.4634 0.5877 0.0316 -0.0039 -0.0280 -0.0500 103 LEU A N   
770  C  CA  . LEU A 108 ? 0.4661 0.5834 0.0408 -0.0019 -0.0357 -0.0521 103 LEU A CA  
771  C  C   . LEU A 108 ? 0.4679 0.5802 0.0662 -0.0145 -0.0224 -0.0757 103 LEU A C   
772  O  O   . LEU A 108 ? 0.4793 0.5548 0.0916 -0.0170 -0.0156 -0.0719 103 LEU A O   
773  C  CB  . LEU A 108 ? 0.4495 0.5732 0.0883 -0.0122 -0.0569 -0.0705 103 LEU A CB  
774  C  CG  . LEU A 108 ? 0.4318 0.5858 0.0926 -0.0001 -0.0427 -0.0802 103 LEU A CG  
775  C  CD1 . LEU A 108 ? 0.4685 0.6078 0.0925 -0.0150 -0.0491 -0.0781 103 LEU A CD1 
776  C  CD2 . LEU A 108 ? 0.4769 0.6244 0.0394 -0.0131 -0.0508 -0.0692 103 LEU A CD2 
777  N  N   . ASP A 109 ? 0.4783 0.6121 0.0972 -0.0355 0.0109  -0.0981 104 ASP A N   
778  C  CA  . ASP A 109 ? 0.5453 0.6598 0.1677 -0.0341 0.0031  -0.1005 104 ASP A CA  
779  C  C   . ASP A 109 ? 0.5087 0.6735 0.2620 -0.0492 -0.0302 -0.1178 104 ASP A C   
780  O  O   . ASP A 109 ? 0.6117 0.6692 0.4095 -0.0810 -0.0070 -0.0962 104 ASP A O   
781  C  CB  . ASP A 109 ? 0.5748 0.6735 0.2342 -0.0488 0.0316  -0.0633 104 ASP A CB  
782  C  CG  . ASP A 109 ? 0.6702 0.7032 0.2925 -0.0431 0.0007  -0.0415 104 ASP A CG  
783  O  OD1 . ASP A 109 ? 0.6753 0.6755 0.3215 -0.0742 0.0003  -0.0041 104 ASP A OD1 
784  O  OD2 . ASP A 109 ? 0.8311 0.7824 0.3479 -0.0044 0.0068  -0.0576 104 ASP A OD2 
785  N  N   . SER A 110 ? 0.4609 0.7168 0.1714 -0.0285 -0.0253 -0.0970 105 SER A N   
786  C  CA  . SER A 110 ? 0.4510 0.7503 0.1436 -0.0330 -0.0203 -0.0985 105 SER A CA  
787  C  C   . SER A 110 ? 0.4179 0.7283 0.1546 -0.0344 -0.0306 -0.0932 105 SER A C   
788  O  O   . SER A 110 ? 0.4278 0.7708 0.2060 -0.0420 -0.0498 -0.1229 105 SER A O   
789  C  CB  . SER A 110 ? 0.4521 0.8015 0.1225 -0.0134 -0.0209 -0.0908 105 SER A CB  
790  O  OG  . SER A 110 ? 0.5319 0.8631 0.2731 -0.0155 0.0476  -0.0592 105 SER A OG  
791  N  N   . HIS A 111 ? 0.4199 0.7195 0.1852 -0.0180 -0.0204 -0.0700 106 HIS A N   
792  C  CA  . HIS A 111 ? 0.4457 0.6750 0.1470 -0.0312 -0.0449 -0.0709 106 HIS A CA  
793  C  C   . HIS A 111 ? 0.4560 0.6322 0.1290 -0.0354 -0.0290 -0.0487 106 HIS A C   
794  O  O   . HIS A 111 ? 0.4564 0.6727 0.2484 -0.0312 -0.0182 -0.0949 106 HIS A O   
795  C  CB  . HIS A 111 ? 0.4661 0.6819 0.1802 -0.0342 -0.0490 -0.0734 106 HIS A CB  
796  C  CG  . HIS A 111 ? 0.4974 0.7232 0.2842 -0.0289 -0.0463 -0.0523 106 HIS A CG  
797  N  ND1 . HIS A 111 ? 0.5022 0.7512 0.2941 -0.0153 -0.0394 -0.0176 106 HIS A ND1 
798  C  CD2 . HIS A 111 ? 0.4860 0.7192 0.3430 -0.0156 -0.0645 -0.0571 106 HIS A CD2 
799  C  CE1 . HIS A 111 ? 0.5224 0.7575 0.3137 -0.0072 -0.0403 -0.0053 106 HIS A CE1 
800  N  NE2 . HIS A 111 ? 0.5135 0.7497 0.3989 -0.0105 -0.0245 -0.0312 106 HIS A NE2 
801  N  N   . LEU A 112 ? 0.4446 0.5888 0.0268 -0.0232 0.0020  -0.0244 107 LEU A N   
802  C  CA  . LEU A 112 ? 0.4366 0.5730 0.0809 -0.0190 0.0243  -0.0278 107 LEU A CA  
803  C  C   . LEU A 112 ? 0.4479 0.5647 0.1489 -0.0238 0.0273  -0.0519 107 LEU A C   
804  O  O   . LEU A 112 ? 0.4719 0.5931 0.2095 -0.0143 0.0559  -0.0554 107 LEU A O   
805  C  CB  . LEU A 112 ? 0.4456 0.5653 0.0661 -0.0127 0.0302  -0.0278 107 LEU A CB  
806  C  CG  . LEU A 112 ? 0.4458 0.5689 0.1053 -0.0110 0.0195  -0.0228 107 LEU A CG  
807  C  CD1 . LEU A 112 ? 0.4310 0.5584 0.1038 -0.0142 -0.0086 -0.0214 107 LEU A CD1 
808  C  CD2 . LEU A 112 ? 0.4672 0.5709 0.1253 -0.0124 0.0056  0.0099  107 LEU A CD2 
809  N  N   . ILE A 113 ? 0.4682 0.5498 0.1492 -0.0189 0.0055  -0.0676 108 ILE A N   
810  C  CA  . ILE A 113 ? 0.5132 0.5579 0.1831 -0.0225 0.0266  -0.0863 108 ILE A CA  
811  C  C   . ILE A 113 ? 0.5307 0.5889 0.2527 -0.0456 0.0091  -0.0823 108 ILE A C   
812  O  O   . ILE A 113 ? 0.5446 0.6035 0.2631 -0.0189 0.0192  -0.0994 108 ILE A O   
813  C  CB  . ILE A 113 ? 0.5397 0.5642 0.2252 -0.0079 0.0368  -0.0612 108 ILE A CB  
814  C  CG1 . ILE A 113 ? 0.5242 0.5732 0.2292 -0.0080 0.0367  -0.0513 108 ILE A CG1 
815  C  CG2 . ILE A 113 ? 0.5692 0.5609 0.2213 -0.0105 0.0535  -0.0712 108 ILE A CG2 
816  C  CD1 . ILE A 113 ? 0.5286 0.5952 0.2382 -0.0063 0.0405  -0.0280 108 ILE A CD1 
817  N  N   . LYS A 114 ? 0.5297 0.6347 0.2451 -0.0953 0.0456  -0.0910 109 LYS A N   
818  C  CA  . LYS A 114 ? 0.6089 0.6742 0.2935 -0.0908 0.0262  -0.0713 109 LYS A CA  
819  C  C   . LYS A 114 ? 0.6271 0.6527 0.2504 -0.0846 0.0462  -0.1224 109 LYS A C   
820  O  O   . LYS A 114 ? 0.6966 0.6689 0.2401 -0.0593 0.0032  -0.1095 109 LYS A O   
821  C  CB  . LYS A 114 ? 0.6214 0.7478 0.3890 -0.0829 0.0483  -0.0462 109 LYS A CB  
822  C  CG  . LYS A 114 ? 0.6371 0.7969 0.4605 -0.0755 0.0684  -0.0352 109 LYS A CG  
823  C  CD  . LYS A 114 ? 0.6281 0.8305 0.5705 -0.0824 0.0930  -0.0403 109 LYS A CD  
824  C  CE  . LYS A 114 ? 0.6577 0.8681 0.6318 -0.0836 0.0956  -0.0357 109 LYS A CE  
825  N  NZ  . LYS A 114 ? 0.6596 0.9193 0.6949 -0.0820 0.1049  -0.0538 109 LYS A NZ  
826  N  N   . GLU A 115 ? 0.6387 0.6732 0.1711 -0.0759 0.0508  -0.1053 110 GLU A N   
827  C  CA  . GLU A 115 ? 0.6094 0.7339 0.2168 -0.0576 0.0193  -0.0465 110 GLU A CA  
828  C  C   . GLU A 115 ? 0.5867 0.7395 0.2109 -0.0651 0.0145  -0.0648 110 GLU A C   
829  O  O   . GLU A 115 ? 0.5462 0.7656 0.2000 -0.0882 -0.0115 -0.0095 110 GLU A O   
830  C  CB  . GLU A 115 ? 0.6296 0.7496 0.2812 -0.0415 0.0224  -0.0140 110 GLU A CB  
831  C  CG  . GLU A 115 ? 0.6164 0.7908 0.3184 -0.0350 0.0296  0.0041  110 GLU A CG  
832  C  CD  . GLU A 115 ? 0.6165 0.8406 0.3428 -0.0319 0.0127  0.0453  110 GLU A CD  
833  O  OE1 . GLU A 115 ? 0.6988 0.8314 0.4174 -0.0348 0.0292  0.0652  110 GLU A OE1 
834  O  OE2 . GLU A 115 ? 0.6421 0.9005 0.4111 0.0438  0.0357  0.0524  110 GLU A OE2 
835  N  N   . ALA A 116 ? 0.5769 0.6793 0.2987 -0.0460 0.0181  -0.0894 111 ALA A N   
836  C  CA  . ALA A 116 ? 0.5764 0.6692 0.2807 -0.0428 0.0431  -0.0979 111 ALA A CA  
837  C  C   . ALA A 116 ? 0.6054 0.7113 0.2380 -0.0514 0.0889  -0.0972 111 ALA A C   
838  O  O   . ALA A 116 ? 0.6344 0.7342 0.2224 -0.0750 0.1768  -0.1234 111 ALA A O   
839  C  CB  . ALA A 116 ? 0.5866 0.6589 0.2810 -0.0422 0.0204  -0.0926 111 ALA A CB  
840  N  N   . GLY A 117 ? 0.6050 0.7657 0.2520 -0.0254 0.1083  -0.1474 112 GLY A N   
841  C  CA  . GLY A 117 ? 0.6002 0.7252 0.3360 -0.0199 0.0465  -0.1704 112 GLY A CA  
842  C  C   . GLY A 117 ? 0.6085 0.7197 0.2988 -0.0155 0.0413  -0.1714 112 GLY A C   
843  O  O   . GLY A 117 ? 0.6188 0.7481 0.2896 0.0010  0.0113  -0.1628 112 GLY A O   
844  N  N   . ASP A 118 ? 0.6353 0.7266 0.1964 0.0065  0.0276  -0.1333 113 ASP A N   
845  C  CA  . ASP A 118 ? 0.6634 0.6732 0.2140 0.0243  0.0422  -0.1131 113 ASP A CA  
846  C  C   . ASP A 118 ? 0.6753 0.6696 0.2127 0.0325  0.0521  -0.0858 113 ASP A C   
847  O  O   . ASP A 118 ? 0.6634 0.6270 0.2460 -0.0005 0.0924  -0.0885 113 ASP A O   
848  C  CB  . ASP A 118 ? 0.6617 0.6566 0.2760 0.0117  0.0308  -0.0963 113 ASP A CB  
849  C  CG  . ASP A 118 ? 0.6902 0.6616 0.3486 -0.0191 -0.0177 -0.0638 113 ASP A CG  
850  O  OD1 . ASP A 118 ? 0.7872 0.6706 0.4939 -0.0097 -0.0018 -0.0506 113 ASP A OD1 
851  O  OD2 . ASP A 118 ? 0.7602 0.6762 0.2713 -0.0442 -0.0251 -0.0541 113 ASP A OD2 
852  N  N   . ALA A 119 ? 0.7044 0.6537 0.1808 0.0571  0.0761  -0.0577 114 ALA A N   
853  C  CA  . ALA A 119 ? 0.7134 0.6652 0.1922 0.0640  0.0692  -0.0613 114 ALA A CA  
854  C  C   . ALA A 119 ? 0.7133 0.6394 0.2147 0.0593  0.0894  -0.0456 114 ALA A C   
855  O  O   . ALA A 119 ? 0.7558 0.6256 0.1727 0.0959  0.0551  -0.0502 114 ALA A O   
856  C  CB  . ALA A 119 ? 0.7217 0.6324 0.2517 0.0626  0.0738  -0.0476 114 ALA A CB  
857  N  N   . GLU A 120 ? 0.6454 0.6397 0.2796 0.0709  0.0727  -0.0314 115 GLU A N   
858  C  CA  . GLU A 120 ? 0.6407 0.6312 0.2758 0.0565  0.0620  -0.0226 115 GLU A CA  
859  C  C   . GLU A 120 ? 0.5854 0.6261 0.2158 0.0505  0.0345  -0.0538 115 GLU A C   
860  O  O   . GLU A 120 ? 0.5250 0.6388 0.1817 0.0379  0.0171  -0.0405 115 GLU A O   
861  C  CB  . GLU A 120 ? 0.6505 0.6503 0.2924 0.0503  0.0516  -0.0015 115 GLU A CB  
862  C  CG  . GLU A 120 ? 0.6839 0.6902 0.3093 0.0224  0.0461  0.0069  115 GLU A CG  
863  C  CD  . GLU A 120 ? 0.7142 0.7298 0.3396 0.0168  0.0721  0.0057  115 GLU A CD  
864  O  OE1 . GLU A 120 ? 0.7978 0.7635 0.3597 0.0272  0.1368  -0.0462 115 GLU A OE1 
865  O  OE2 . GLU A 120 ? 0.7766 0.7578 0.2523 -0.0275 0.0426  0.0423  115 GLU A OE2 
866  N  N   . SER A 121 ? 0.5533 0.5890 0.1770 0.0482  0.0356  -0.0432 116 SER A N   
867  C  CA  . SER A 121 ? 0.5502 0.5894 0.1951 0.0232  0.0328  -0.0502 116 SER A CA  
868  C  C   . SER A 121 ? 0.5201 0.5406 0.1944 0.0191  0.0265  -0.0668 116 SER A C   
869  O  O   . SER A 121 ? 0.4857 0.5366 0.1605 0.0156  -0.0057 -0.0792 116 SER A O   
870  C  CB  . SER A 121 ? 0.5737 0.6090 0.2333 0.0336  0.0250  -0.0290 116 SER A CB  
871  O  OG  . SER A 121 ? 0.6483 0.6289 0.2060 0.0366  0.0341  -0.1001 116 SER A OG  
872  N  N   . ARG A 122 ? 0.5210 0.5432 0.2038 -0.0050 0.0306  -0.0766 117 ARG A N   
873  C  CA  . ARG A 122 ? 0.5143 0.5409 0.2574 -0.0067 0.0475  -0.0727 117 ARG A CA  
874  C  C   . ARG A 122 ? 0.4363 0.4976 0.2219 0.0052  0.0623  -0.0864 117 ARG A C   
875  O  O   . ARG A 122 ? 0.4269 0.5402 0.1685 0.0069  0.0387  -0.0889 117 ARG A O   
876  C  CB  . ARG A 122 ? 0.5589 0.5662 0.3242 -0.0303 0.0196  -0.0863 117 ARG A CB  
877  C  CG  . ARG A 122 ? 0.5943 0.6420 0.3681 -0.0433 -0.0009 -0.0595 117 ARG A CG  
878  C  CD  . ARG A 122 ? 0.6601 0.6782 0.4779 -0.0413 -0.0222 -0.0743 117 ARG A CD  
879  N  NE  . ARG A 122 ? 0.7247 0.7809 0.5814 -0.0168 -0.0524 -0.0902 117 ARG A NE  
880  C  CZ  . ARG A 122 ? 0.7452 0.8042 0.6548 0.0286  -0.0358 -0.0915 117 ARG A CZ  
881  N  NH1 . ARG A 122 ? 0.7697 0.7742 0.6950 0.0215  0.0062  -0.1015 117 ARG A NH1 
882  N  NH2 . ARG A 122 ? 0.7693 0.8128 0.6937 0.0371  -0.0504 -0.0850 117 ARG A NH2 
883  N  N   . VAL A 123 ? 0.4460 0.4829 0.2204 0.0038  0.0589  -0.0758 118 VAL A N   
884  C  CA  . VAL A 123 ? 0.4106 0.5089 0.2126 0.0102  0.0432  -0.0414 118 VAL A CA  
885  C  C   . VAL A 123 ? 0.4110 0.4929 0.1945 0.0086  0.0329  -0.0243 118 VAL A C   
886  O  O   . VAL A 123 ? 0.4377 0.4643 0.1815 0.0380  0.0159  -0.0427 118 VAL A O   
887  C  CB  . VAL A 123 ? 0.4371 0.4953 0.2705 0.0212  0.0395  -0.0482 118 VAL A CB  
888  C  CG1 . VAL A 123 ? 0.4278 0.4901 0.2774 0.0229  0.0245  -0.0512 118 VAL A CG1 
889  C  CG2 . VAL A 123 ? 0.4537 0.5114 0.2926 0.0141  0.0372  -0.0470 118 VAL A CG2 
890  N  N   . PHE A 124 ? 0.4075 0.4900 0.1801 0.0011  0.0238  -0.0281 119 PHE A N   
891  C  CA  . PHE A 124 ? 0.4045 0.4955 0.1680 -0.0039 0.0102  -0.0054 119 PHE A CA  
892  C  C   . PHE A 124 ? 0.4021 0.4776 0.1408 -0.0131 0.0120  -0.0283 119 PHE A C   
893  O  O   . PHE A 124 ? 0.4093 0.4659 0.1433 -0.0022 -0.0113 -0.0210 119 PHE A O   
894  C  CB  . PHE A 124 ? 0.4168 0.5085 0.1360 -0.0189 0.0268  -0.0144 119 PHE A CB  
895  C  CG  . PHE A 124 ? 0.4345 0.5100 0.1482 -0.0142 0.0044  -0.0134 119 PHE A CG  
896  C  CD1 . PHE A 124 ? 0.4457 0.5043 0.1035 -0.0123 -0.0044 -0.0277 119 PHE A CD1 
897  C  CD2 . PHE A 124 ? 0.4443 0.5089 0.1290 -0.0088 -0.0224 -0.0296 119 PHE A CD2 
898  C  CE1 . PHE A 124 ? 0.4587 0.5278 0.0976 -0.0198 -0.0176 -0.0056 119 PHE A CE1 
899  C  CE2 . PHE A 124 ? 0.4565 0.5264 0.1517 0.0007  -0.0413 -0.0273 119 PHE A CE2 
900  C  CZ  . PHE A 124 ? 0.4532 0.5273 0.1134 -0.0068 -0.0217 -0.0359 119 PHE A CZ  
901  N  N   . TYR A 125 ? 0.4069 0.4951 0.1218 -0.0085 0.0187  -0.0343 120 TYR A N   
902  C  CA  . TYR A 125 ? 0.3930 0.4739 0.1466 -0.0197 0.0173  -0.0222 120 TYR A CA  
903  C  C   . TYR A 125 ? 0.4168 0.4779 0.1478 -0.0124 0.0171  -0.0163 120 TYR A C   
904  O  O   . TYR A 125 ? 0.4127 0.4728 0.1773 0.0004  0.0338  -0.0032 120 TYR A O   
905  C  CB  . TYR A 125 ? 0.4075 0.4777 0.1277 -0.0148 0.0101  -0.0244 120 TYR A CB  
906  C  CG  . TYR A 125 ? 0.4178 0.4696 0.1217 -0.0099 -0.0007 -0.0465 120 TYR A CG  
907  C  CD1 . TYR A 125 ? 0.4303 0.4841 0.1174 -0.0207 0.0051  -0.0384 120 TYR A CD1 
908  C  CD2 . TYR A 125 ? 0.4574 0.4810 0.1052 -0.0009 -0.0030 -0.0487 120 TYR A CD2 
909  C  CE1 . TYR A 125 ? 0.4594 0.4960 0.1096 -0.0056 -0.0053 -0.0490 120 TYR A CE1 
910  C  CE2 . TYR A 125 ? 0.4438 0.4937 0.0831 -0.0094 -0.0008 -0.0457 120 TYR A CE2 
911  C  CZ  . TYR A 125 ? 0.4463 0.4987 0.0743 -0.0136 -0.0084 -0.0230 120 TYR A CZ  
912  O  OH  . TYR A 125 ? 0.5029 0.5826 0.0286 -0.0087 -0.0045 -0.0426 120 TYR A OH  
913  N  N   . LEU A 126 ? 0.4433 0.4858 0.1278 -0.0195 0.0386  -0.0350 121 LEU A N   
914  C  CA  . LEU A 126 ? 0.4197 0.4973 0.1811 -0.0294 0.0468  -0.0072 121 LEU A CA  
915  C  C   . LEU A 126 ? 0.4066 0.4983 0.1389 -0.0221 0.0470  -0.0022 121 LEU A C   
916  O  O   . LEU A 126 ? 0.4274 0.4990 0.1244 -0.0159 0.0456  -0.0122 121 LEU A O   
917  C  CB  . LEU A 126 ? 0.4244 0.5073 0.2304 -0.0098 0.0465  -0.0325 121 LEU A CB  
918  C  CG  . LEU A 126 ? 0.4541 0.4884 0.2917 -0.0191 0.0550  -0.0320 121 LEU A CG  
919  C  CD1 . LEU A 126 ? 0.4842 0.5224 0.3241 -0.0079 0.0595  -0.0415 121 LEU A CD1 
920  C  CD2 . LEU A 126 ? 0.4691 0.4898 0.3326 -0.0135 0.0495  -0.0286 121 LEU A CD2 
921  N  N   . LYS A 127 ? 0.3963 0.5019 0.1128 -0.0249 0.0368  -0.0065 122 LYS A N   
922  C  CA  . LYS A 127 ? 0.4027 0.4828 0.1290 -0.0133 0.0144  0.0112  122 LYS A CA  
923  C  C   . LYS A 127 ? 0.4111 0.4796 0.1146 0.0031  -0.0066 0.0148  122 LYS A C   
924  O  O   . LYS A 127 ? 0.3755 0.4785 0.1211 0.0090  0.0224  0.0006  122 LYS A O   
925  C  CB  . LYS A 127 ? 0.3912 0.4882 0.1702 0.0050  0.0162  0.0099  122 LYS A CB  
926  C  CG  . LYS A 127 ? 0.4097 0.5108 0.1228 -0.0038 -0.0033 0.0130  122 LYS A CG  
927  C  CD  . LYS A 127 ? 0.4379 0.5126 0.1186 -0.0049 -0.0023 0.0361  122 LYS A CD  
928  C  CE  . LYS A 127 ? 0.4856 0.5235 0.1154 -0.0040 -0.0004 0.0183  122 LYS A CE  
929  N  NZ  . LYS A 127 ? 0.4978 0.5256 0.1228 -0.0060 -0.0105 0.0189  122 LYS A NZ  
930  N  N   . MET A 128 ? 0.4119 0.4508 0.1030 -0.0001 -0.0162 0.0255  123 MET A N   
931  C  CA  . MET A 128 ? 0.4044 0.4915 0.1137 -0.0032 -0.0195 0.0363  123 MET A CA  
932  C  C   . MET A 128 ? 0.3966 0.4717 0.1182 -0.0095 0.0012  0.0235  123 MET A C   
933  O  O   . MET A 128 ? 0.4030 0.4489 0.0837 -0.0092 -0.0198 0.0020  123 MET A O   
934  C  CB  . MET A 128 ? 0.4469 0.5202 0.1237 -0.0289 -0.0631 0.0408  123 MET A CB  
935  C  CG  . MET A 128 ? 0.4973 0.5491 0.2053 -0.0428 -0.1037 0.0359  123 MET A CG  
936  S  SD  . MET A 128 ? 0.5896 0.5627 0.1944 -0.0113 -0.1098 0.0422  123 MET A SD  
937  C  CE  . MET A 128 ? 0.5115 0.5636 0.0939 0.0126  -0.0688 0.0687  123 MET A CE  
938  N  N   . LYS A 129 ? 0.3978 0.5025 0.0885 -0.0077 0.0140  0.0310  124 LYS A N   
939  C  CA  . LYS A 129 ? 0.3911 0.5071 0.0987 -0.0134 0.0139  0.0477  124 LYS A CA  
940  C  C   . LYS A 129 ? 0.3855 0.5077 0.0993 -0.0030 -0.0001 0.0110  124 LYS A C   
941  O  O   . LYS A 129 ? 0.3752 0.5427 0.0756 0.0004  0.0423  0.0409  124 LYS A O   
942  C  CB  . LYS A 129 ? 0.4031 0.5420 0.1285 -0.0218 0.0042  0.0272  124 LYS A CB  
943  C  CG  . LYS A 129 ? 0.4258 0.5533 0.1844 -0.0372 0.0258  0.0257  124 LYS A CG  
944  C  CD  . LYS A 129 ? 0.4688 0.5802 0.2061 -0.0504 0.0194  0.0230  124 LYS A CD  
945  C  CE  . LYS A 129 ? 0.5189 0.6135 0.2313 -0.0684 0.0501  0.0242  124 LYS A CE  
946  N  NZ  . LYS A 129 ? 0.5617 0.6566 0.2512 -0.0767 0.0500  0.0331  124 LYS A NZ  
947  N  N   . GLY A 130 ? 0.3739 0.4883 0.0546 -0.0187 0.0111  0.0240  125 GLY A N   
948  C  CA  . GLY A 130 ? 0.3880 0.4954 0.0838 -0.0042 -0.0099 0.0267  125 GLY A CA  
949  C  C   . GLY A 130 ? 0.4084 0.4780 0.0774 -0.0073 -0.0011 0.0326  125 GLY A C   
950  O  O   . GLY A 130 ? 0.4312 0.4495 0.0699 0.0079  0.0038  0.0252  125 GLY A O   
951  N  N   . ASP A 131 ? 0.3897 0.4489 0.0685 -0.0014 -0.0262 0.0436  126 ASP A N   
952  C  CA  . ASP A 131 ? 0.3958 0.4621 0.1058 -0.0043 -0.0219 0.0442  126 ASP A CA  
953  C  C   . ASP A 131 ? 0.3676 0.4770 0.0818 -0.0024 -0.0176 0.0227  126 ASP A C   
954  O  O   . ASP A 131 ? 0.3866 0.4476 0.0986 0.0007  -0.0446 0.0015  126 ASP A O   
955  C  CB  . ASP A 131 ? 0.3894 0.4772 0.1083 -0.0227 -0.0065 0.0368  126 ASP A CB  
956  C  CG  . ASP A 131 ? 0.4004 0.4721 0.1211 -0.0309 0.0074  0.0498  126 ASP A CG  
957  O  OD1 . ASP A 131 ? 0.3781 0.4852 0.0984 -0.0104 0.0067  0.0094  126 ASP A OD1 
958  O  OD2 . ASP A 131 ? 0.4170 0.5276 0.0743 -0.0212 0.0003  0.0362  126 ASP A OD2 
959  N  N   . TYR A 132 ? 0.3757 0.4783 0.0582 0.0182  -0.0072 0.0345  127 TYR A N   
960  C  CA  . TYR A 132 ? 0.3806 0.4821 0.0312 0.0125  -0.0149 0.0286  127 TYR A CA  
961  C  C   . TYR A 132 ? 0.3824 0.4641 0.0619 0.0074  0.0048  0.0270  127 TYR A C   
962  O  O   . TYR A 132 ? 0.4088 0.4984 0.0677 0.0135  0.0275  0.0113  127 TYR A O   
963  C  CB  . TYR A 132 ? 0.4053 0.4976 0.0366 0.0113  -0.0311 0.0046  127 TYR A CB  
964  C  CG  . TYR A 132 ? 0.4065 0.4702 0.0307 0.0160  -0.0437 0.0104  127 TYR A CG  
965  C  CD1 . TYR A 132 ? 0.4276 0.4599 0.0317 0.0167  -0.0213 0.0055  127 TYR A CD1 
966  C  CD2 . TYR A 132 ? 0.4440 0.4802 0.0286 0.0135  -0.0369 0.0004  127 TYR A CD2 
967  C  CE1 . TYR A 132 ? 0.4505 0.4647 0.0273 0.0084  -0.0254 0.0130  127 TYR A CE1 
968  C  CE2 . TYR A 132 ? 0.4457 0.4689 0.0279 0.0145  -0.0331 -0.0003 127 TYR A CE2 
969  C  CZ  . TYR A 132 ? 0.4474 0.4521 0.0268 0.0003  -0.0199 0.0157  127 TYR A CZ  
970  O  OH  . TYR A 132 ? 0.4724 0.4381 0.0269 -0.0087 -0.0149 0.0217  127 TYR A OH  
971  N  N   . TYR A 133 ? 0.3820 0.4660 0.0384 -0.0096 0.0283  0.0448  128 TYR A N   
972  C  CA  . TYR A 133 ? 0.3891 0.4730 0.0501 -0.0157 0.0235  0.0537  128 TYR A CA  
973  C  C   . TYR A 133 ? 0.3918 0.4834 0.0600 -0.0146 0.0294  0.0409  128 TYR A C   
974  O  O   . TYR A 133 ? 0.4164 0.5250 0.0442 -0.0066 0.0266  0.0586  128 TYR A O   
975  C  CB  . TYR A 133 ? 0.3977 0.4964 0.0510 -0.0239 0.0371  0.0364  128 TYR A CB  
976  C  CG  . TYR A 133 ? 0.3883 0.4996 0.1087 -0.0295 0.0385  0.0246  128 TYR A CG  
977  C  CD1 . TYR A 133 ? 0.3905 0.5296 0.1693 -0.0243 0.0326  0.0297  128 TYR A CD1 
978  C  CD2 . TYR A 133 ? 0.4172 0.5465 0.1238 -0.0234 0.0341  0.0031  128 TYR A CD2 
979  C  CE1 . TYR A 133 ? 0.4210 0.5467 0.2053 -0.0222 0.0355  0.0149  128 TYR A CE1 
980  C  CE2 . TYR A 133 ? 0.4214 0.5630 0.1722 -0.0344 0.0547  -0.0041 128 TYR A CE2 
981  C  CZ  . TYR A 133 ? 0.4143 0.5672 0.2092 -0.0309 0.0310  0.0212  128 TYR A CZ  
982  O  OH  . TYR A 133 ? 0.4649 0.6256 0.2439 -0.0780 0.0535  0.0368  128 TYR A OH  
983  N  N   . ARG A 134 ? 0.3905 0.4928 0.0599 -0.0121 0.0068  0.0462  129 ARG A N   
984  C  CA  . ARG A 134 ? 0.4039 0.4856 0.0761 -0.0056 -0.0097 0.0547  129 ARG A CA  
985  C  C   . ARG A 134 ? 0.3865 0.4813 0.0859 0.0090  -0.0190 0.0494  129 ARG A C   
986  O  O   . ARG A 134 ? 0.3984 0.4858 0.0563 0.0101  -0.0150 0.0649  129 ARG A O   
987  C  CB  . ARG A 134 ? 0.3938 0.4947 0.0432 0.0012  -0.0069 0.0630  129 ARG A CB  
988  C  CG  . ARG A 134 ? 0.4216 0.5022 0.0362 -0.0051 -0.0127 0.0707  129 ARG A CG  
989  C  CD  . ARG A 134 ? 0.4293 0.5108 0.0304 -0.0065 -0.0047 0.0494  129 ARG A CD  
990  N  NE  . ARG A 134 ? 0.4454 0.5174 0.0346 0.0000  0.0189  0.0473  129 ARG A NE  
991  C  CZ  . ARG A 134 ? 0.4581 0.5139 0.0517 -0.0123 0.0132  0.0426  129 ARG A CZ  
992  N  NH1 . ARG A 134 ? 0.4431 0.5057 0.0405 -0.0081 0.0167  0.0287  129 ARG A NH1 
993  N  NH2 . ARG A 134 ? 0.4722 0.5277 0.0438 -0.0187 -0.0083 0.0491  129 ARG A NH2 
994  N  N   . TYR A 135 ? 0.3829 0.4709 0.0445 0.0000  -0.0053 0.0494  130 TYR A N   
995  C  CA  . TYR A 135 ? 0.3887 0.4804 0.0315 0.0125  -0.0163 0.0406  130 TYR A CA  
996  C  C   . TYR A 135 ? 0.3876 0.4816 0.0481 0.0083  -0.0066 0.0434  130 TYR A C   
997  O  O   . TYR A 135 ? 0.4764 0.5033 0.0299 0.0029  -0.0068 0.0460  130 TYR A O   
998  C  CB  . TYR A 135 ? 0.3879 0.4788 0.0371 0.0077  -0.0069 0.0478  130 TYR A CB  
999  C  CG  . TYR A 135 ? 0.3971 0.4814 0.0314 0.0118  -0.0087 0.0516  130 TYR A CG  
1000 C  CD1 . TYR A 135 ? 0.4070 0.5014 0.0323 -0.0004 0.0211  0.0526  130 TYR A CD1 
1001 C  CD2 . TYR A 135 ? 0.4008 0.4891 0.0324 0.0027  -0.0144 0.0549  130 TYR A CD2 
1002 C  CE1 . TYR A 135 ? 0.4172 0.5295 0.0690 -0.0006 0.0179  0.0663  130 TYR A CE1 
1003 C  CE2 . TYR A 135 ? 0.3891 0.5019 0.0663 -0.0061 -0.0067 0.0318  130 TYR A CE2 
1004 C  CZ  . TYR A 135 ? 0.4002 0.5112 0.0607 0.0054  0.0151  0.0533  130 TYR A CZ  
1005 O  OH  . TYR A 135 ? 0.3997 0.5664 0.0895 -0.0114 0.0356  0.0416  130 TYR A OH  
1006 N  N   . LEU A 136 ? 0.3810 0.4988 0.0306 0.0079  -0.0126 0.0475  131 LEU A N   
1007 C  CA  . LEU A 136 ? 0.3968 0.5125 0.0328 0.0206  0.0050  0.0604  131 LEU A CA  
1008 C  C   . LEU A 136 ? 0.4201 0.5264 0.0321 0.0276  -0.0124 0.0556  131 LEU A C   
1009 O  O   . LEU A 136 ? 0.4103 0.5488 0.0488 0.0110  0.0317  0.0467  131 LEU A O   
1010 C  CB  . LEU A 136 ? 0.3960 0.5284 0.0335 0.0214  0.0096  0.0636  131 LEU A CB  
1011 C  CG  . LEU A 136 ? 0.4004 0.5270 0.0533 0.0265  -0.0077 0.0505  131 LEU A CG  
1012 C  CD1 . LEU A 136 ? 0.4091 0.5267 0.0843 0.0090  0.0035  0.0334  131 LEU A CD1 
1013 C  CD2 . LEU A 136 ? 0.4224 0.5346 0.0309 0.0249  -0.0125 0.0505  131 LEU A CD2 
1014 N  N   . ALA A 137 ? 0.4286 0.5487 0.0371 0.0338  -0.0284 0.0688  132 ALA A N   
1015 C  CA  . ALA A 137 ? 0.4630 0.5447 0.0398 0.0340  -0.0213 0.0817  132 ALA A CA  
1016 C  C   . ALA A 137 ? 0.4836 0.5467 0.0381 0.0224  -0.0173 0.0787  132 ALA A C   
1017 O  O   . ALA A 137 ? 0.5404 0.5679 0.0404 0.0149  -0.0194 0.0876  132 ALA A O   
1018 C  CB  . ALA A 137 ? 0.4672 0.5470 0.0472 0.0429  -0.0302 0.0982  132 ALA A CB  
1019 N  N   . GLU A 138 ? 0.4810 0.5402 0.0384 0.0133  -0.0305 0.0746  133 GLU A N   
1020 C  CA  . GLU A 138 ? 0.4832 0.5608 0.0366 0.0100  -0.0292 0.0704  133 GLU A CA  
1021 C  C   . GLU A 138 ? 0.4724 0.5422 0.0314 -0.0038 -0.0460 0.0266  133 GLU A C   
1022 O  O   . GLU A 138 ? 0.5010 0.6391 0.0336 0.0065  -0.0463 0.0476  133 GLU A O   
1023 C  CB  . GLU A 138 ? 0.4704 0.5877 0.1031 0.0079  -0.0234 0.0662  133 GLU A CB  
1024 C  CG  . GLU A 138 ? 0.4649 0.5935 0.1494 0.0183  -0.0192 0.0583  133 GLU A CG  
1025 C  CD  . GLU A 138 ? 0.4795 0.6156 0.1941 0.0224  0.0118  0.0571  133 GLU A CD  
1026 O  OE1 . GLU A 138 ? 0.5293 0.6177 0.2088 0.0208  0.0091  0.0502  133 GLU A OE1 
1027 O  OE2 . GLU A 138 ? 0.5221 0.6717 0.2308 0.0276  0.0449  0.0434  133 GLU A OE2 
1028 N  N   . VAL A 139 ? 0.4729 0.5194 0.0288 0.0117  -0.0060 0.0406  134 VAL A N   
1029 C  CA  . VAL A 139 ? 0.4883 0.5295 0.0579 0.0090  0.0003  0.0229  134 VAL A CA  
1030 C  C   . VAL A 139 ? 0.4696 0.5338 0.0873 0.0138  0.0059  0.0237  134 VAL A C   
1031 O  O   . VAL A 139 ? 0.4862 0.5610 0.1446 0.0194  0.0596  0.0347  134 VAL A O   
1032 C  CB  . VAL A 139 ? 0.4560 0.5313 0.0568 0.0010  -0.0143 0.0136  134 VAL A CB  
1033 C  CG1 . VAL A 139 ? 0.4825 0.5367 0.0791 -0.0101 -0.0243 0.0191  134 VAL A CG1 
1034 C  CG2 . VAL A 139 ? 0.4629 0.5398 0.0267 -0.0021 0.0059  0.0259  134 VAL A CG2 
1035 N  N   . ALA A 140 ? 0.4553 0.5321 0.0445 0.0119  -0.0189 0.0409  135 ALA A N   
1036 C  CA  . ALA A 140 ? 0.4711 0.5607 0.0374 0.0021  -0.0186 0.0776  135 ALA A CA  
1037 C  C   . ALA A 140 ? 0.4938 0.5712 0.0479 0.0191  -0.0279 0.1056  135 ALA A C   
1038 O  O   . ALA A 140 ? 0.4971 0.6057 0.0324 0.0000  0.0010  0.0640  135 ALA A O   
1039 C  CB  . ALA A 140 ? 0.4754 0.5673 0.0387 0.0029  0.0006  0.0851  135 ALA A CB  
1040 N  N   . THR A 141 ? 0.4884 0.6001 0.0519 0.0261  -0.0408 0.1124  136 THR A N   
1041 C  CA  . THR A 141 ? 0.5067 0.6463 0.0445 0.0163  0.0142  0.1084  136 THR A CA  
1042 C  C   . THR A 141 ? 0.5107 0.6560 0.0506 0.0056  0.0011  0.1263  136 THR A C   
1043 O  O   . THR A 141 ? 0.5388 0.6821 0.0654 0.0128  0.0202  0.1610  136 THR A O   
1044 C  CB  . THR A 141 ? 0.4998 0.6627 0.0760 0.0316  -0.0096 0.0574  136 THR A CB  
1045 O  OG1 . THR A 141 ? 0.4891 0.6913 0.0554 0.0386  -0.0188 0.0643  136 THR A OG1 
1046 C  CG2 . THR A 141 ? 0.5101 0.6908 0.0377 0.0267  -0.0071 0.0567  136 THR A CG2 
1047 N  N   . GLY A 142 ? 0.5161 0.6787 0.0616 -0.0127 0.0078  0.1534  137 GLY A N   
1048 C  CA  . GLY A 142 ? 0.5270 0.6555 0.0586 -0.0013 0.0000  0.1108  137 GLY A CA  
1049 C  C   . GLY A 142 ? 0.4985 0.6329 0.0486 0.0103  0.0278  0.1153  137 GLY A C   
1050 O  O   . GLY A 142 ? 0.4927 0.6078 0.0936 0.0317  0.0116  0.1104  137 GLY A O   
1051 N  N   . ASP A 143 ? 0.4988 0.6337 0.0573 0.0167  0.0313  0.1016  138 ASP A N   
1052 C  CA  . ASP A 143 ? 0.4876 0.6290 0.0461 0.0008  0.0263  0.1058  138 ASP A CA  
1053 C  C   . ASP A 143 ? 0.4785 0.5823 0.0577 0.0076  0.0235  0.1201  138 ASP A C   
1054 O  O   . ASP A 143 ? 0.4721 0.5646 0.0904 -0.0078 0.0140  0.0918  138 ASP A O   
1055 C  CB  . ASP A 143 ? 0.4919 0.6538 0.0503 0.0025  -0.0015 0.1253  138 ASP A CB  
1056 C  CG  . ASP A 143 ? 0.4957 0.6632 0.1027 -0.0053 0.0089  0.1507  138 ASP A CG  
1057 O  OD1 . ASP A 143 ? 0.5258 0.6966 0.1842 0.0027  -0.0387 0.1614  138 ASP A OD1 
1058 O  OD2 . ASP A 143 ? 0.5434 0.6821 0.1742 0.0014  0.0536  0.1579  138 ASP A OD2 
1059 N  N   . ASP A 144 ? 0.4735 0.5797 0.0559 -0.0083 0.0399  0.1202  139 ASP A N   
1060 C  CA  . ASP A 144 ? 0.4434 0.5379 0.0497 -0.0085 0.0231  0.1083  139 ASP A CA  
1061 C  C   . ASP A 144 ? 0.4255 0.5447 0.0910 -0.0014 0.0014  0.0949  139 ASP A C   
1062 O  O   . ASP A 144 ? 0.3793 0.5786 0.0930 0.0125  -0.0034 0.0824  139 ASP A O   
1063 C  CB  . ASP A 144 ? 0.4462 0.5413 0.0512 -0.0066 0.0155  0.0717  139 ASP A CB  
1064 C  CG  . ASP A 144 ? 0.4556 0.5393 0.0591 -0.0277 0.0202  0.0584  139 ASP A CG  
1065 O  OD1 . ASP A 144 ? 0.5008 0.5833 0.0569 0.0092  -0.0199 0.0524  139 ASP A OD1 
1066 O  OD2 . ASP A 144 ? 0.4656 0.5442 0.0363 -0.0237 0.0295  0.0447  139 ASP A OD2 
1067 N  N   . LYS A 145 ? 0.4231 0.5408 0.1046 -0.0019 -0.0148 0.0904  140 LYS A N   
1068 C  CA  . LYS A 145 ? 0.4169 0.5316 0.0971 0.0080  -0.0215 0.1056  140 LYS A CA  
1069 C  C   . LYS A 145 ? 0.4093 0.5430 0.1203 0.0073  -0.0115 0.1070  140 LYS A C   
1070 O  O   . LYS A 145 ? 0.4497 0.5147 0.1437 0.0101  0.0177  0.1112  140 LYS A O   
1071 C  CB  . LYS A 145 ? 0.4379 0.5709 0.1467 -0.0071 -0.0299 0.0956  140 LYS A CB  
1072 C  CG  . LYS A 145 ? 0.4610 0.6047 0.1782 0.0092  -0.0011 0.0946  140 LYS A CG  
1073 C  CD  . LYS A 145 ? 0.4928 0.6541 0.2460 -0.0009 -0.0179 0.0678  140 LYS A CD  
1074 C  CE  . LYS A 145 ? 0.5252 0.7168 0.2619 0.0047  -0.0080 0.0360  140 LYS A CE  
1075 N  NZ  . LYS A 145 ? 0.5862 0.7454 0.2756 0.0228  -0.0554 0.0458  140 LYS A NZ  
1076 N  N   . LYS A 146 ? 0.4336 0.5385 0.1271 0.0146  -0.0137 0.1098  141 LYS A N   
1077 C  CA  . LYS A 146 ? 0.4534 0.5839 0.1443 -0.0030 -0.0018 0.1019  141 LYS A CA  
1078 C  C   . LYS A 146 ? 0.4275 0.5700 0.1450 0.0156  0.0135  0.0945  141 LYS A C   
1079 O  O   . LYS A 146 ? 0.4620 0.5691 0.1335 0.0294  -0.0051 0.0736  141 LYS A O   
1080 C  CB  . LYS A 146 ? 0.5065 0.6505 0.1861 -0.0062 0.0290  0.1044  141 LYS A CB  
1081 C  CG  . LYS A 146 ? 0.5414 0.7086 0.2082 -0.0145 0.0208  0.1187  141 LYS A CG  
1082 C  CD  . LYS A 146 ? 0.5836 0.7550 0.1828 -0.0019 0.0415  0.1198  141 LYS A CD  
1083 C  CE  . LYS A 146 ? 0.5505 0.7655 0.1611 0.0257  0.0481  0.1344  141 LYS A CE  
1084 N  NZ  . LYS A 146 ? 0.5215 0.8168 0.2275 0.0147  0.0649  0.1236  141 LYS A NZ  
1085 N  N   . ARG A 147 ? 0.3927 0.5638 0.1399 0.0085  0.0149  0.0786  142 ARG A N   
1086 C  CA  . ARG A 147 ? 0.4160 0.5817 0.1565 -0.0006 0.0157  0.0637  142 ARG A CA  
1087 C  C   . ARG A 147 ? 0.4062 0.5460 0.1728 0.0011  0.0172  0.0757  142 ARG A C   
1088 O  O   . ARG A 147 ? 0.4259 0.5433 0.1553 0.0134  0.0268  0.0645  142 ARG A O   
1089 C  CB  . ARG A 147 ? 0.4230 0.5908 0.1680 0.0129  0.0107  0.0562  142 ARG A CB  
1090 C  CG  . ARG A 147 ? 0.4326 0.6010 0.2144 0.0186  -0.0089 0.0489  142 ARG A CG  
1091 C  CD  . ARG A 147 ? 0.4370 0.6155 0.2143 0.0184  -0.0189 0.0500  142 ARG A CD  
1092 N  NE  . ARG A 147 ? 0.4543 0.6111 0.1799 0.0381  -0.0053 0.0763  142 ARG A NE  
1093 C  CZ  . ARG A 147 ? 0.4414 0.6110 0.1645 0.0368  -0.0065 0.0888  142 ARG A CZ  
1094 N  NH1 . ARG A 147 ? 0.4354 0.6189 0.1165 0.0485  0.0065  0.0921  142 ARG A NH1 
1095 N  NH2 . ARG A 147 ? 0.4536 0.6231 0.1431 0.0431  -0.0060 0.0760  142 ARG A NH2 
1096 N  N   . ILE A 148 ? 0.4032 0.5245 0.1279 -0.0093 0.0179  0.1014  143 ILE A N   
1097 C  CA  . ILE A 148 ? 0.4481 0.5346 0.0775 -0.0126 0.0136  0.0904  143 ILE A CA  
1098 C  C   . ILE A 148 ? 0.4406 0.5572 0.0912 -0.0063 0.0378  0.0868  143 ILE A C   
1099 O  O   . ILE A 148 ? 0.4278 0.5174 0.0889 -0.0053 0.0456  0.0939  143 ILE A O   
1100 C  CB  . ILE A 148 ? 0.4826 0.5083 0.0526 -0.0238 0.0146  0.0817  143 ILE A CB  
1101 C  CG1 . ILE A 148 ? 0.5203 0.5172 0.1005 -0.0228 0.0181  0.0522  143 ILE A CG1 
1102 C  CG2 . ILE A 148 ? 0.4821 0.5192 0.1161 -0.0361 0.0113  0.0574  143 ILE A CG2 
1103 C  CD1 . ILE A 148 ? 0.5550 0.5554 0.1739 -0.0098 0.0418  0.0467  143 ILE A CD1 
1104 N  N   . ILE A 149 ? 0.4254 0.5647 0.1298 0.0077  0.0262  0.0919  144 ILE A N   
1105 C  CA  . ILE A 149 ? 0.4530 0.5789 0.1514 0.0153  0.0186  0.0933  144 ILE A CA  
1106 C  C   . ILE A 149 ? 0.4418 0.5774 0.1564 0.0220  0.0170  0.0850  144 ILE A C   
1107 O  O   . ILE A 149 ? 0.4290 0.5430 0.1413 0.0069  0.0133  0.0519  144 ILE A O   
1108 C  CB  . ILE A 149 ? 0.4588 0.6194 0.1540 0.0114  0.0299  0.1047  144 ILE A CB  
1109 C  CG1 . ILE A 149 ? 0.4410 0.6440 0.1647 0.0012  0.0266  0.0762  144 ILE A CG1 
1110 C  CG2 . ILE A 149 ? 0.4852 0.6159 0.1742 0.0091  0.0448  0.1237  144 ILE A CG2 
1111 C  CD1 . ILE A 149 ? 0.4645 0.6705 0.1807 -0.0063 0.0054  0.0667  144 ILE A CD1 
1112 N  N   . ASP A 150 ? 0.4491 0.5975 0.1671 0.0097  0.0433  0.0839  145 ASP A N   
1113 C  CA  . ASP A 150 ? 0.4783 0.5905 0.2493 0.0144  0.0654  0.1046  145 ASP A CA  
1114 C  C   . ASP A 150 ? 0.4773 0.5712 0.2256 0.0006  0.0429  0.0723  145 ASP A C   
1115 O  O   . ASP A 150 ? 0.4954 0.5458 0.3236 0.0077  0.0478  0.0759  145 ASP A O   
1116 C  CB  . ASP A 150 ? 0.5098 0.6272 0.3435 0.0200  0.0792  0.1151  145 ASP A CB  
1117 C  CG  . ASP A 150 ? 0.5601 0.6899 0.4470 0.0166  0.1018  0.1571  145 ASP A CG  
1118 O  OD1 . ASP A 150 ? 0.5776 0.7423 0.5336 0.0115  0.1003  0.1644  145 ASP A OD1 
1119 O  OD2 . ASP A 150 ? 0.6277 0.7254 0.5321 0.0153  0.1813  0.1676  145 ASP A OD2 
1120 N  N   . SER A 151 ? 0.4792 0.5601 0.1963 -0.0188 0.0585  0.0821  146 SER A N   
1121 C  CA  . SER A 151 ? 0.4730 0.5598 0.1949 0.0029  0.0542  0.0622  146 SER A CA  
1122 C  C   . SER A 151 ? 0.4617 0.5604 0.2401 0.0014  0.0612  0.0523  146 SER A C   
1123 O  O   . SER A 151 ? 0.4693 0.5773 0.2652 0.0088  0.0986  0.0504  146 SER A O   
1124 C  CB  . SER A 151 ? 0.4583 0.5714 0.1941 -0.0051 0.0323  0.0566  146 SER A CB  
1125 O  OG  . SER A 151 ? 0.4531 0.5712 0.2420 0.0103  0.0426  0.0414  146 SER A OG  
1126 N  N   . ALA A 152 ? 0.4308 0.5340 0.1961 0.0113  0.0967  0.0617  147 ALA A N   
1127 C  CA  . ALA A 152 ? 0.4469 0.5138 0.2178 -0.0031 0.0976  0.0666  147 ALA A CA  
1128 C  C   . ALA A 152 ? 0.4585 0.4754 0.2372 -0.0148 0.1239  0.0744  147 ALA A C   
1129 O  O   . ALA A 152 ? 0.4290 0.4890 0.2040 -0.0061 0.1000  0.0248  147 ALA A O   
1130 C  CB  . ALA A 152 ? 0.4454 0.5249 0.1715 0.0159  0.0858  0.0618  147 ALA A CB  
1131 N  N   . ARG A 153 ? 0.4730 0.4826 0.2388 0.0079  0.0768  0.0719  148 ARG A N   
1132 C  CA  . ARG A 153 ? 0.4958 0.4987 0.2931 0.0072  0.0753  0.0951  148 ARG A CA  
1133 C  C   . ARG A 153 ? 0.4645 0.4759 0.2689 0.0117  0.0803  0.0997  148 ARG A C   
1134 O  O   . ARG A 153 ? 0.4762 0.4964 0.3166 0.0401  0.0866  0.0643  148 ARG A O   
1135 C  CB  . ARG A 153 ? 0.5302 0.5090 0.3122 0.0013  0.0761  0.1150  148 ARG A CB  
1136 C  CG  . ARG A 153 ? 0.5837 0.5247 0.3862 0.0168  0.0596  0.1077  148 ARG A CG  
1137 C  CD  . ARG A 153 ? 0.6234 0.5533 0.3983 0.0214  0.0510  0.1331  148 ARG A CD  
1138 N  NE  . ARG A 153 ? 0.7059 0.5884 0.4389 0.0200  0.0717  0.1328  148 ARG A NE  
1139 C  CZ  . ARG A 153 ? 0.7358 0.6318 0.4104 0.0246  0.0632  0.1733  148 ARG A CZ  
1140 N  NH1 . ARG A 153 ? 0.7463 0.6579 0.4332 0.0377  0.0652  0.1990  148 ARG A NH1 
1141 N  NH2 . ARG A 153 ? 0.7656 0.6873 0.3698 0.0210  0.0411  0.1373  148 ARG A NH2 
1142 N  N   . SER A 154 ? 0.4708 0.4855 0.2720 -0.0193 0.1027  0.0878  149 SER A N   
1143 C  CA  A SER A 154 ? 0.4912 0.5124 0.3006 -0.0209 0.0866  0.0611  149 SER A CA  
1144 C  CA  B SER A 154 ? 0.4820 0.5001 0.2991 -0.0211 0.0872  0.0714  149 SER A CA  
1145 C  C   . SER A 154 ? 0.4729 0.4998 0.3163 -0.0169 0.1064  0.0726  149 SER A C   
1146 O  O   . SER A 154 ? 0.4793 0.5098 0.3528 -0.0119 0.0525  0.0225  149 SER A O   
1147 C  CB  A SER A 154 ? 0.5050 0.5293 0.3222 -0.0332 0.0882  0.0351  149 SER A CB  
1148 C  CB  B SER A 154 ? 0.4896 0.5003 0.2988 -0.0342 0.0974  0.0690  149 SER A CB  
1149 O  OG  A SER A 154 ? 0.5300 0.5575 0.3157 -0.0349 0.0554  0.0129  149 SER A OG  
1150 O  OG  B SER A 154 ? 0.4856 0.4843 0.2695 -0.0381 0.0672  0.0686  149 SER A OG  
1151 N  N   . ALA A 155 ? 0.4502 0.5066 0.3131 -0.0113 0.0967  0.0632  150 ALA A N   
1152 C  CA  . ALA A 155 ? 0.4433 0.4948 0.2500 -0.0051 0.0681  0.0524  150 ALA A CA  
1153 C  C   . ALA A 155 ? 0.4438 0.4983 0.2647 0.0053  0.0717  0.0283  150 ALA A C   
1154 O  O   . ALA A 155 ? 0.4239 0.5361 0.2488 -0.0028 0.0838  0.0290  150 ALA A O   
1155 C  CB  . ALA A 155 ? 0.4469 0.5227 0.2593 0.0227  0.0511  0.0186  150 ALA A CB  
1156 N  N   . TYR A 156 ? 0.4021 0.4660 0.2685 0.0022  0.0661  0.0373  151 TYR A N   
1157 C  CA  . TYR A 156 ? 0.4007 0.4838 0.2643 -0.0036 0.0714  0.0347  151 TYR A CA  
1158 C  C   . TYR A 156 ? 0.3986 0.4945 0.3202 -0.0046 0.0720  0.0325  151 TYR A C   
1159 O  O   . TYR A 156 ? 0.4183 0.5219 0.3522 -0.0029 0.0991  0.0230  151 TYR A O   
1160 C  CB  . TYR A 156 ? 0.3967 0.4906 0.2555 0.0153  0.0493  0.0429  151 TYR A CB  
1161 C  CG  . TYR A 156 ? 0.3824 0.4773 0.2058 0.0109  0.0570  0.0487  151 TYR A CG  
1162 C  CD1 . TYR A 156 ? 0.3759 0.4705 0.2182 0.0152  0.0500  0.0554  151 TYR A CD1 
1163 C  CD2 . TYR A 156 ? 0.3821 0.4798 0.1921 0.0224  0.0450  0.0500  151 TYR A CD2 
1164 C  CE1 . TYR A 156 ? 0.3637 0.4827 0.1777 0.0191  0.0472  0.0526  151 TYR A CE1 
1165 C  CE2 . TYR A 156 ? 0.3837 0.4710 0.1725 0.0284  0.0333  0.0503  151 TYR A CE2 
1166 C  CZ  . TYR A 156 ? 0.3585 0.4677 0.1712 0.0273  0.0328  0.0515  151 TYR A CZ  
1167 O  OH  . TYR A 156 ? 0.3609 0.4975 0.1110 0.0383  0.0132  0.0351  151 TYR A OH  
1168 N  N   . GLN A 157 ? 0.4457 0.4706 0.3445 -0.0053 0.0651  0.0255  152 GLN A N   
1169 C  CA  . GLN A 157 ? 0.4887 0.4831 0.3923 0.0002  0.0706  0.0088  152 GLN A CA  
1170 C  C   . GLN A 157 ? 0.4952 0.4667 0.3641 0.0033  0.0948  -0.0031 152 GLN A C   
1171 O  O   . GLN A 157 ? 0.5248 0.4761 0.3841 -0.0007 0.0976  -0.0344 152 GLN A O   
1172 C  CB  . GLN A 157 ? 0.5333 0.4874 0.3960 -0.0116 0.0643  0.0213  152 GLN A CB  
1173 C  CG  . GLN A 157 ? 0.5698 0.5275 0.4233 -0.0045 0.0737  0.0208  152 GLN A CG  
1174 C  CD  . GLN A 157 ? 0.5997 0.5514 0.4546 0.0040  0.0753  0.0163  152 GLN A CD  
1175 O  OE1 . GLN A 157 ? 0.6501 0.5693 0.4465 -0.0047 0.0034  0.0695  152 GLN A OE1 
1176 N  NE2 . GLN A 157 ? 0.6615 0.5645 0.5425 0.0355  0.0819  -0.0037 152 GLN A NE2 
1177 N  N   . GLU A 158 ? 0.5128 0.4956 0.3668 -0.0083 0.1027  -0.0230 153 GLU A N   
1178 C  CA  . GLU A 158 ? 0.5363 0.5233 0.4093 -0.0252 0.0861  -0.0133 153 GLU A CA  
1179 C  C   . GLU A 158 ? 0.5107 0.5133 0.3778 -0.0053 0.1167  -0.0393 153 GLU A C   
1180 O  O   . GLU A 158 ? 0.5369 0.5444 0.3379 -0.0103 0.1653  -0.0198 153 GLU A O   
1181 C  CB  . GLU A 158 ? 0.5504 0.5642 0.4825 -0.0461 0.0567  -0.0140 153 GLU A CB  
1182 C  CG  . GLU A 158 ? 0.5980 0.6248 0.5706 -0.0541 0.0371  -0.0111 153 GLU A CG  
1183 C  CD  . GLU A 158 ? 0.6021 0.7220 0.6620 -0.0698 0.0133  -0.0160 153 GLU A CD  
1184 O  OE1 . GLU A 158 ? 0.6251 0.7520 0.7315 -0.0651 0.0668  -0.0054 153 GLU A OE1 
1185 O  OE2 . GLU A 158 ? 0.6384 0.7791 0.6352 -0.0570 0.0074  -0.0175 153 GLU A OE2 
1186 N  N   . ALA A 159 ? 0.4779 0.5356 0.3595 -0.0198 0.1170  0.0069  154 ALA A N   
1187 C  CA  . ALA A 159 ? 0.4745 0.5297 0.3127 -0.0120 0.1007  0.0094  154 ALA A CA  
1188 C  C   . ALA A 159 ? 0.4691 0.5270 0.3372 0.0039  0.1151  0.0170  154 ALA A C   
1189 O  O   . ALA A 159 ? 0.4618 0.5425 0.3789 0.0346  0.1319  0.0226  154 ALA A O   
1190 C  CB  . ALA A 159 ? 0.4503 0.5153 0.2935 -0.0124 0.0989  0.0176  154 ALA A CB  
1191 N  N   . MET A 160 ? 0.4820 0.5284 0.3419 0.0141  0.1145  0.0025  155 MET A N   
1192 C  CA  . MET A 160 ? 0.5165 0.5416 0.3757 0.0226  0.0993  0.0240  155 MET A CA  
1193 C  C   . MET A 160 ? 0.5182 0.5278 0.4140 0.0381  0.0900  0.0233  155 MET A C   
1194 O  O   . MET A 160 ? 0.5444 0.5265 0.4301 0.0452  0.0953  0.0147  155 MET A O   
1195 C  CB  . MET A 160 ? 0.5255 0.5823 0.3893 0.0184  0.0980  0.0112  155 MET A CB  
1196 C  CG  . MET A 160 ? 0.5398 0.6156 0.3685 0.0361  0.0798  0.0165  155 MET A CG  
1197 S  SD  . MET A 160 ? 0.5720 0.6764 0.3708 0.0346  0.0637  0.0546  155 MET A SD  
1198 C  CE  . MET A 160 ? 0.5458 0.6501 0.3666 0.0077  0.0233  0.0865  155 MET A CE  
1199 N  N   . ASP A 161 ? 0.5636 0.5003 0.4500 0.0198  0.0821  0.0002  156 ASP A N   
1200 C  CA  . ASP A 161 ? 0.5754 0.5276 0.4785 0.0317  0.0935  0.0149  156 ASP A CA  
1201 C  C   . ASP A 161 ? 0.5550 0.5315 0.4779 0.0213  0.1379  -0.0054 156 ASP A C   
1202 O  O   . ASP A 161 ? 0.6177 0.5557 0.5022 0.0326  0.1474  -0.0036 156 ASP A O   
1203 C  CB  . ASP A 161 ? 0.6237 0.5300 0.5293 0.0102  0.0880  0.0214  156 ASP A CB  
1204 C  CG  . ASP A 161 ? 0.6558 0.5545 0.5507 -0.0009 0.0964  0.0000  156 ASP A CG  
1205 O  OD1 . ASP A 161 ? 0.6967 0.5684 0.5857 0.0181  0.0514  0.0307  156 ASP A OD1 
1206 O  OD2 . ASP A 161 ? 0.7178 0.6053 0.6335 -0.0302 0.1200  -0.0213 156 ASP A OD2 
1207 N  N   . ILE A 162 ? 0.4955 0.5108 0.3945 0.0091  0.1381  -0.0139 157 ILE A N   
1208 C  CA  . ILE A 162 ? 0.5116 0.5593 0.4733 0.0072  0.1065  -0.0235 157 ILE A CA  
1209 C  C   . ILE A 162 ? 0.5069 0.5356 0.4630 0.0121  0.0969  -0.0342 157 ILE A C   
1210 O  O   . ILE A 162 ? 0.5017 0.5328 0.4400 0.0220  0.0708  -0.0585 157 ILE A O   
1211 C  CB  . ILE A 162 ? 0.5151 0.5556 0.4931 0.0122  0.1191  -0.0290 157 ILE A CB  
1212 C  CG1 . ILE A 162 ? 0.5208 0.5663 0.5440 0.0059  0.1121  -0.0443 157 ILE A CG1 
1213 C  CG2 . ILE A 162 ? 0.5172 0.5648 0.4966 0.0181  0.1000  -0.0422 157 ILE A CG2 
1214 C  CD1 . ILE A 162 ? 0.5201 0.5705 0.5299 0.0053  0.1162  -0.0396 157 ILE A CD1 
1215 N  N   . SER A 163 ? 0.4772 0.5339 0.4385 -0.0096 0.0596  -0.0324 158 SER A N   
1216 C  CA  . SER A 163 ? 0.5224 0.5446 0.4357 -0.0220 0.0762  -0.0220 158 SER A CA  
1217 C  C   . SER A 163 ? 0.5153 0.5651 0.4117 -0.0155 0.1121  -0.0414 158 SER A C   
1218 O  O   . SER A 163 ? 0.5446 0.5827 0.3311 0.0017  0.1184  -0.0572 158 SER A O   
1219 C  CB  . SER A 163 ? 0.5261 0.5637 0.4052 -0.0211 0.0717  -0.0355 158 SER A CB  
1220 O  OG  . SER A 163 ? 0.5669 0.5771 0.4641 -0.0474 0.0740  -0.0297 158 SER A OG  
1221 N  N   . LYS A 164 ? 0.5732 0.5942 0.4643 0.0098  0.0986  -0.0232 159 LYS A N   
1222 C  CA  . LYS A 164 ? 0.5873 0.6497 0.4991 0.0248  0.1003  -0.0213 159 LYS A CA  
1223 C  C   . LYS A 164 ? 0.5652 0.6481 0.4809 0.0394  0.1051  -0.0361 159 LYS A C   
1224 O  O   . LYS A 164 ? 0.5721 0.6936 0.4688 0.0715  0.0866  -0.0563 159 LYS A O   
1225 C  CB  . LYS A 164 ? 0.6565 0.6967 0.5293 0.0329  0.0802  0.0192  159 LYS A CB  
1226 C  CG  . LYS A 164 ? 0.7296 0.7688 0.6688 0.0135  0.0645  0.0194  159 LYS A CG  
1227 C  CD  . LYS A 164 ? 0.7944 0.8074 0.7150 0.0247  0.0431  0.0526  159 LYS A CD  
1228 C  CE  . LYS A 164 ? 0.8136 0.8443 0.8116 0.0396  0.0399  0.0373  159 LYS A CE  
1229 N  NZ  . LYS A 164 ? 0.8193 0.9073 0.9182 0.0417  0.0556  0.0598  159 LYS A NZ  
1230 N  N   . LYS A 165 ? 0.5482 0.6497 0.5027 -0.0032 0.1214  -0.0647 160 LYS A N   
1231 C  CA  . LYS A 165 ? 0.5865 0.6831 0.5291 0.0039  0.1266  -0.0771 160 LYS A CA  
1232 C  C   . LYS A 165 ? 0.5533 0.6837 0.4832 0.0145  0.1194  -0.0915 160 LYS A C   
1233 O  O   . LYS A 165 ? 0.5920 0.7200 0.5727 0.0129  0.1618  -0.0894 160 LYS A O   
1234 C  CB  . LYS A 165 ? 0.6311 0.6986 0.5717 -0.0390 0.1121  -0.0646 160 LYS A CB  
1235 C  CG  . LYS A 165 ? 0.7293 0.7519 0.7015 -0.0325 0.1079  -0.0457 160 LYS A CG  
1236 C  CD  . LYS A 165 ? 0.7674 0.8144 0.7558 -0.0292 0.0974  -0.0194 160 LYS A CD  
1237 C  CE  . LYS A 165 ? 0.8603 0.8137 0.7951 -0.0301 0.0688  0.0153  160 LYS A CE  
1238 N  NZ  . LYS A 165 ? 0.9162 0.8205 0.7859 -0.0213 0.0788  0.0076  160 LYS A NZ  
1239 N  N   . GLU A 166 ? 0.5362 0.6776 0.3983 0.0060  0.1062  -0.1251 161 GLU A N   
1240 C  CA  . GLU A 166 ? 0.5663 0.7036 0.4158 0.0015  0.0488  -0.1309 161 GLU A CA  
1241 C  C   . GLU A 166 ? 0.5451 0.6706 0.3810 0.0136  0.0198  -0.1270 161 GLU A C   
1242 O  O   . GLU A 166 ? 0.5355 0.7041 0.4648 0.0145  -0.0127 -0.1120 161 GLU A O   
1243 C  CB  . GLU A 166 ? 0.5777 0.7315 0.4001 0.0104  0.0362  -0.1406 161 GLU A CB  
1244 C  CG  . GLU A 166 ? 0.6144 0.7779 0.4808 -0.0071 0.0508  -0.1256 161 GLU A CG  
1245 C  CD  . GLU A 166 ? 0.6499 0.8670 0.5658 -0.0435 0.0310  -0.1332 161 GLU A CD  
1246 O  OE1 . GLU A 166 ? 0.6808 0.9393 0.6245 -0.0625 0.0299  -0.1231 161 GLU A OE1 
1247 O  OE2 . GLU A 166 ? 0.6611 0.9441 0.6140 -0.0513 0.0361  -0.1415 161 GLU A OE2 
1248 N  N   . MET A 167 ? 0.5027 0.6106 0.3901 0.0387  0.0059  -0.1190 162 MET A N   
1249 C  CA  . MET A 167 ? 0.4823 0.6114 0.3344 0.0451  0.0361  -0.0671 162 MET A CA  
1250 C  C   . MET A 167 ? 0.4826 0.5946 0.2886 0.0326  0.0244  -0.0293 162 MET A C   
1251 O  O   . MET A 167 ? 0.5226 0.5988 0.2894 0.0205  0.0330  -0.0241 162 MET A O   
1252 C  CB  . MET A 167 ? 0.4842 0.6077 0.3532 0.0771  0.0361  -0.0610 162 MET A CB  
1253 C  CG  . MET A 167 ? 0.4990 0.6309 0.3570 0.0605  0.0260  -0.0590 162 MET A CG  
1254 S  SD  . MET A 167 ? 0.5332 0.6715 0.3444 0.0624  0.0123  -0.0662 162 MET A SD  
1255 C  CE  . MET A 167 ? 0.5566 0.7191 0.3221 0.0408  0.0195  -0.0549 162 MET A CE  
1256 N  N   . PRO A 168 ? 0.4733 0.6011 0.2300 0.0245  0.0291  -0.0111 163 PRO A N   
1257 C  CA  . PRO A 168 ? 0.4751 0.5987 0.2114 0.0251  0.0500  0.0008  163 PRO A CA  
1258 C  C   . PRO A 168 ? 0.4544 0.5968 0.2052 0.0240  0.0283  0.0029  163 PRO A C   
1259 O  O   . PRO A 168 ? 0.4618 0.6075 0.1536 0.0120  0.0119  0.0183  163 PRO A O   
1260 C  CB  . PRO A 168 ? 0.4839 0.6026 0.2772 0.0233  0.0590  -0.0011 163 PRO A CB  
1261 C  CG  . PRO A 168 ? 0.4991 0.6077 0.2955 0.0287  0.0457  -0.0057 163 PRO A CG  
1262 C  CD  . PRO A 168 ? 0.4907 0.6078 0.2912 0.0167  0.0343  0.0113  163 PRO A CD  
1263 N  N   . PRO A 169 ? 0.4761 0.6165 0.2013 0.0330  0.0610  0.0374  164 PRO A N   
1264 C  CA  . PRO A 169 ? 0.4782 0.6079 0.2032 0.0188  0.0401  0.0260  164 PRO A CA  
1265 C  C   . PRO A 169 ? 0.4537 0.6057 0.1693 0.0247  0.0557  0.0393  164 PRO A C   
1266 O  O   . PRO A 169 ? 0.4758 0.6010 0.2204 0.0055  0.0681  0.0201  164 PRO A O   
1267 C  CB  . PRO A 169 ? 0.5016 0.6237 0.2715 0.0334  0.0241  0.0115  164 PRO A CB  
1268 C  CG  . PRO A 169 ? 0.5244 0.6377 0.2697 0.0440  0.0240  0.0310  164 PRO A CG  
1269 C  CD  . PRO A 169 ? 0.5256 0.6289 0.2430 0.0430  0.0476  0.0309  164 PRO A CD  
1270 N  N   . THR A 170 ? 0.4068 0.5933 0.1256 0.0186  0.0217  0.0336  165 THR A N   
1271 C  CA  . THR A 170 ? 0.4129 0.6091 0.1176 0.0222  0.0076  0.0088  165 THR A CA  
1272 C  C   . THR A 170 ? 0.4175 0.5924 0.1076 0.0232  0.0227  0.0071  165 THR A C   
1273 O  O   . THR A 170 ? 0.4287 0.6071 0.1322 0.0315  -0.0037 -0.0164 165 THR A O   
1274 C  CB  . THR A 170 ? 0.3840 0.6222 0.1500 0.0268  0.0063  0.0247  165 THR A CB  
1275 O  OG1 . THR A 170 ? 0.4192 0.6440 0.1301 0.0409  0.0388  0.0020  165 THR A OG1 
1276 C  CG2 . THR A 170 ? 0.3913 0.6496 0.1854 0.0189  0.0183  0.0292  165 THR A CG2 
1277 N  N   . ASN A 171 ? 0.4298 0.5891 0.1286 0.0237  0.0269  0.0033  166 ASN A N   
1278 C  CA  . ASN A 171 ? 0.4095 0.6044 0.1339 0.0240  0.0208  0.0099  166 ASN A CA  
1279 C  C   . ASN A 171 ? 0.3715 0.5665 0.1786 0.0088  0.0262  0.0091  166 ASN A C   
1280 O  O   . ASN A 171 ? 0.3918 0.5748 0.1609 0.0320  0.0055  0.0025  166 ASN A O   
1281 C  CB  . ASN A 171 ? 0.4373 0.6166 0.1263 0.0214  0.0203  0.0166  166 ASN A CB  
1282 C  CG  . ASN A 171 ? 0.4618 0.6324 0.1105 0.0438  0.0057  -0.0152 166 ASN A CG  
1283 O  OD1 . ASN A 171 ? 0.4430 0.6594 0.2148 0.0505  0.0001  -0.0076 166 ASN A OD1 
1284 N  ND2 . ASN A 171 ? 0.5022 0.6843 0.0905 0.0808  0.0292  0.0165  166 ASN A ND2 
1285 N  N   . PRO A 172 ? 0.3602 0.5601 0.1530 -0.0052 0.0078  0.0295  167 PRO A N   
1286 C  CA  . PRO A 172 ? 0.3877 0.5494 0.1442 -0.0056 -0.0129 0.0157  167 PRO A CA  
1287 C  C   . PRO A 172 ? 0.3689 0.5247 0.1432 -0.0100 -0.0135 0.0094  167 PRO A C   
1288 O  O   . PRO A 172 ? 0.4203 0.5495 0.1070 -0.0118 -0.0431 0.0299  167 PRO A O   
1289 C  CB  . PRO A 172 ? 0.3943 0.5525 0.1723 -0.0130 0.0161  0.0147  167 PRO A CB  
1290 C  CG  . PRO A 172 ? 0.4025 0.5797 0.1852 -0.0244 0.0412  0.0399  167 PRO A CG  
1291 C  CD  . PRO A 172 ? 0.3928 0.5606 0.1768 -0.0310 0.0498  0.0222  167 PRO A CD  
1292 N  N   . ILE A 173 ? 0.3797 0.5311 0.1324 -0.0033 -0.0151 0.0198  168 ILE A N   
1293 C  CA  . ILE A 173 ? 0.3890 0.5235 0.1798 0.0010  -0.0326 0.0199  168 ILE A CA  
1294 C  C   . ILE A 173 ? 0.3954 0.5168 0.1712 0.0151  -0.0028 0.0307  168 ILE A C   
1295 O  O   . ILE A 173 ? 0.4113 0.5064 0.1884 0.0289  0.0092  0.0227  168 ILE A O   
1296 C  CB  . ILE A 173 ? 0.4096 0.5590 0.1956 0.0001  -0.0563 0.0390  168 ILE A CB  
1297 C  CG1 . ILE A 173 ? 0.4445 0.5946 0.2259 -0.0054 -0.0846 0.0473  168 ILE A CG1 
1298 C  CG2 . ILE A 173 ? 0.4311 0.5622 0.1851 -0.0031 -0.0598 0.0521  168 ILE A CG2 
1299 C  CD1 . ILE A 173 ? 0.4984 0.6022 0.2359 -0.0069 -0.0882 0.0284  168 ILE A CD1 
1300 N  N   . ARG A 174 ? 0.4130 0.5211 0.1561 0.0061  0.0063  0.0349  169 ARG A N   
1301 C  CA  . ARG A 174 ? 0.3990 0.5097 0.1866 0.0066  -0.0229 0.0423  169 ARG A CA  
1302 C  C   . ARG A 174 ? 0.3833 0.5165 0.2015 -0.0041 -0.0204 0.0377  169 ARG A C   
1303 O  O   . ARG A 174 ? 0.3900 0.5103 0.2128 0.0120  -0.0008 0.0664  169 ARG A O   
1304 C  CB  . ARG A 174 ? 0.3996 0.5164 0.2133 -0.0027 -0.0050 0.0278  169 ARG A CB  
1305 C  CG  . ARG A 174 ? 0.4257 0.5137 0.2004 0.0172  0.0168  0.0298  169 ARG A CG  
1306 C  CD  . ARG A 174 ? 0.4729 0.5206 0.2700 0.0244  0.0253  0.0395  169 ARG A CD  
1307 N  NE  . ARG A 174 ? 0.4875 0.5304 0.2304 0.0255  0.0576  0.0556  169 ARG A NE  
1308 C  CZ  . ARG A 174 ? 0.5163 0.5111 0.2621 0.0198  0.0527  0.0529  169 ARG A CZ  
1309 N  NH1 . ARG A 174 ? 0.5301 0.5099 0.2804 0.0197  0.0578  0.0480  169 ARG A NH1 
1310 N  NH2 . ARG A 174 ? 0.5615 0.5537 0.2990 0.0251  0.0702  0.0288  169 ARG A NH2 
1311 N  N   . LEU A 175 ? 0.3731 0.5138 0.1987 0.0263  -0.0109 0.0238  170 LEU A N   
1312 C  CA  . LEU A 175 ? 0.3829 0.5203 0.1494 0.0193  -0.0195 0.0332  170 LEU A CA  
1313 C  C   . LEU A 175 ? 0.3995 0.5159 0.1824 0.0382  -0.0095 0.0427  170 LEU A C   
1314 O  O   . LEU A 175 ? 0.4181 0.5600 0.1682 0.0214  -0.0332 0.0510  170 LEU A O   
1315 C  CB  . LEU A 175 ? 0.3656 0.5362 0.1404 0.0267  -0.0439 0.0268  170 LEU A CB  
1316 C  CG  . LEU A 175 ? 0.3686 0.5614 0.1596 0.0244  -0.0452 0.0372  170 LEU A CG  
1317 C  CD1 . LEU A 175 ? 0.3800 0.5873 0.1368 0.0199  -0.0268 0.0259  170 LEU A CD1 
1318 C  CD2 . LEU A 175 ? 0.3835 0.5818 0.1859 0.0396  -0.0312 0.0522  170 LEU A CD2 
1319 N  N   . GLY A 176 ? 0.3937 0.5119 0.1744 0.0359  0.0020  0.0277  171 GLY A N   
1320 C  CA  . GLY A 176 ? 0.3968 0.5104 0.1393 0.0210  -0.0107 0.0221  171 GLY A CA  
1321 C  C   . GLY A 176 ? 0.3780 0.4938 0.1676 0.0125  0.0064  0.0068  171 GLY A C   
1322 O  O   . GLY A 176 ? 0.3858 0.5008 0.1341 -0.0124 0.0070  0.0262  171 GLY A O   
1323 N  N   . LEU A 177 ? 0.3812 0.5109 0.1525 -0.0115 0.0074  0.0225  172 LEU A N   
1324 C  CA  . LEU A 177 ? 0.4178 0.4981 0.1834 -0.0145 -0.0008 0.0318  172 LEU A CA  
1325 C  C   . LEU A 177 ? 0.4213 0.5136 0.1365 0.0003  0.0334  0.0479  172 LEU A C   
1326 O  O   . LEU A 177 ? 0.4198 0.5363 0.1658 -0.0048 0.0733  0.0290  172 LEU A O   
1327 C  CB  . LEU A 177 ? 0.4146 0.4985 0.2247 -0.0144 -0.0002 0.0228  172 LEU A CB  
1328 C  CG  . LEU A 177 ? 0.4125 0.4916 0.2521 -0.0138 0.0011  0.0103  172 LEU A CG  
1329 C  CD1 . LEU A 177 ? 0.4199 0.4952 0.2197 -0.0087 0.0205  0.0232  172 LEU A CD1 
1330 C  CD2 . LEU A 177 ? 0.4181 0.4793 0.3001 -0.0211 -0.0162 -0.0034 172 LEU A CD2 
1331 N  N   . ALA A 178 ? 0.4149 0.5235 0.0977 0.0060  0.0144  0.0718  173 ALA A N   
1332 C  CA  . ALA A 178 ? 0.4133 0.5480 0.1716 0.0391  0.0003  0.0785  173 ALA A CA  
1333 C  C   . ALA A 178 ? 0.4272 0.5354 0.1450 0.0251  0.0242  0.0733  173 ALA A C   
1334 O  O   . ALA A 178 ? 0.4451 0.5681 0.1373 0.0256  -0.0287 0.1045  173 ALA A O   
1335 C  CB  . ALA A 178 ? 0.4502 0.5606 0.1773 0.0419  0.0273  0.0631  173 ALA A CB  
1336 N  N   . LEU A 179 ? 0.3923 0.5361 0.1889 0.0280  0.0197  0.0535  174 LEU A N   
1337 C  CA  . LEU A 179 ? 0.3736 0.5447 0.1270 0.0140  0.0044  0.0643  174 LEU A CA  
1338 C  C   . LEU A 179 ? 0.3559 0.5502 0.1429 0.0156  0.0019  0.0664  174 LEU A C   
1339 O  O   . LEU A 179 ? 0.3911 0.5723 0.1196 0.0248  -0.0014 0.0710  174 LEU A O   
1340 C  CB  . LEU A 179 ? 0.3692 0.5459 0.1203 0.0146  -0.0011 0.0620  174 LEU A CB  
1341 C  CG  . LEU A 179 ? 0.3885 0.5442 0.1459 0.0112  0.0214  0.0566  174 LEU A CG  
1342 C  CD1 . LEU A 179 ? 0.3919 0.5644 0.2230 0.0214  -0.0096 0.0384  174 LEU A CD1 
1343 C  CD2 . LEU A 179 ? 0.4026 0.5667 0.0649 0.0206  0.0356  0.0313  174 LEU A CD2 
1344 N  N   . ASN A 180 ? 0.3378 0.5137 0.1603 0.0148  0.0192  0.0708  175 ASN A N   
1345 C  CA  . ASN A 180 ? 0.3366 0.5207 0.1586 0.0142  0.0001  0.0556  175 ASN A CA  
1346 C  C   . ASN A 180 ? 0.3442 0.5216 0.1738 0.0187  0.0007  0.0616  175 ASN A C   
1347 O  O   . ASN A 180 ? 0.3736 0.5517 0.1946 0.0254  0.0477  0.0766  175 ASN A O   
1348 C  CB  . ASN A 180 ? 0.3790 0.5144 0.1419 0.0276  -0.0066 0.0575  175 ASN A CB  
1349 C  CG  . ASN A 180 ? 0.3505 0.4998 0.1418 -0.0037 0.0099  0.0423  175 ASN A CG  
1350 O  OD1 . ASN A 180 ? 0.3743 0.5025 0.1067 -0.0287 0.0101  0.0478  175 ASN A OD1 
1351 N  ND2 . ASN A 180 ? 0.3664 0.5115 0.1294 -0.0125 0.0061  0.0355  175 ASN A ND2 
1352 N  N   . PHE A 181 ? 0.3463 0.5136 0.1872 0.0273  0.0076  0.0965  176 PHE A N   
1353 C  CA  . PHE A 181 ? 0.3699 0.5103 0.1818 0.0240  0.0005  0.0906  176 PHE A CA  
1354 C  C   . PHE A 181 ? 0.3928 0.5267 0.1654 0.0122  0.0051  0.0921  176 PHE A C   
1355 O  O   . PHE A 181 ? 0.4244 0.5373 0.1536 -0.0019 0.0171  0.1004  176 PHE A O   
1356 C  CB  . PHE A 181 ? 0.4118 0.5270 0.2058 0.0277  -0.0061 0.0650  176 PHE A CB  
1357 C  CG  . PHE A 181 ? 0.4386 0.5207 0.2426 0.0279  0.0204  0.0471  176 PHE A CG  
1358 C  CD1 . PHE A 181 ? 0.4319 0.5257 0.2526 0.0179  0.0308  0.0506  176 PHE A CD1 
1359 C  CD2 . PHE A 181 ? 0.4637 0.5299 0.2554 0.0361  0.0446  0.0495  176 PHE A CD2 
1360 C  CE1 . PHE A 181 ? 0.4710 0.5238 0.2874 0.0361  0.0150  0.0330  176 PHE A CE1 
1361 C  CE2 . PHE A 181 ? 0.4914 0.5333 0.3112 0.0242  0.0416  0.0300  176 PHE A CE2 
1362 C  CZ  . PHE A 181 ? 0.4674 0.5339 0.3059 0.0291  0.0440  0.0441  176 PHE A CZ  
1363 N  N   . SER A 182 ? 0.4026 0.5298 0.1073 0.0226  -0.0040 0.0915  177 SER A N   
1364 C  CA  . SER A 182 ? 0.4272 0.5687 0.1553 0.0337  -0.0281 0.0943  177 SER A CA  
1365 C  C   . SER A 182 ? 0.4459 0.5713 0.1219 0.0429  -0.0049 0.0957  177 SER A C   
1366 O  O   . SER A 182 ? 0.4637 0.6253 0.1143 0.0686  0.0011  0.0835  177 SER A O   
1367 C  CB  . SER A 182 ? 0.4518 0.5791 0.1853 0.0420  -0.0176 0.0953  177 SER A CB  
1368 O  OG  . SER A 182 ? 0.4292 0.6147 0.1936 0.0513  -0.0049 0.1163  177 SER A OG  
1369 N  N   . VAL A 183 ? 0.4313 0.5701 0.0910 0.0230  0.0114  0.0760  178 VAL A N   
1370 C  CA  . VAL A 183 ? 0.4452 0.5607 0.1174 0.0252  0.0134  0.0752  178 VAL A CA  
1371 C  C   . VAL A 183 ? 0.4267 0.5694 0.1371 0.0361  0.0187  0.0670  178 VAL A C   
1372 O  O   . VAL A 183 ? 0.4634 0.5953 0.1108 0.0353  0.0168  0.0855  178 VAL A O   
1373 C  CB  . VAL A 183 ? 0.4245 0.5533 0.1149 0.0211  -0.0036 0.0778  178 VAL A CB  
1374 C  CG1 . VAL A 183 ? 0.4422 0.5540 0.1044 0.0166  -0.0164 0.0853  178 VAL A CG1 
1375 C  CG2 . VAL A 183 ? 0.4646 0.5622 0.1267 0.0021  -0.0044 0.0929  178 VAL A CG2 
1376 N  N   . PHE A 184 ? 0.3912 0.5635 0.0886 0.0333  0.0141  0.0761  179 PHE A N   
1377 C  CA  . PHE A 184 ? 0.4146 0.5733 0.1211 0.0371  0.0286  0.0860  179 PHE A CA  
1378 C  C   . PHE A 184 ? 0.4203 0.5894 0.1460 0.0564  0.0432  0.1109  179 PHE A C   
1379 O  O   . PHE A 184 ? 0.3917 0.5819 0.1515 0.0618  0.0531  0.1049  179 PHE A O   
1380 C  CB  . PHE A 184 ? 0.4208 0.5767 0.1720 0.0339  0.0110  0.0856  179 PHE A CB  
1381 C  CG  . PHE A 184 ? 0.4436 0.5857 0.1237 0.0310  0.0333  0.0924  179 PHE A CG  
1382 C  CD1 . PHE A 184 ? 0.4453 0.5866 0.1720 0.0368  0.0178  0.1063  179 PHE A CD1 
1383 C  CD2 . PHE A 184 ? 0.4459 0.5877 0.1977 0.0161  0.0638  0.0537  179 PHE A CD2 
1384 C  CE1 . PHE A 184 ? 0.4645 0.5909 0.2116 0.0230  0.0214  0.1055  179 PHE A CE1 
1385 C  CE2 . PHE A 184 ? 0.4840 0.5960 0.2237 0.0023  0.0531  0.0918  179 PHE A CE2 
1386 C  CZ  . PHE A 184 ? 0.4621 0.5945 0.2434 0.0046  0.0604  0.0795  179 PHE A CZ  
1387 N  N   . HIS A 185 ? 0.4578 0.5861 0.1251 0.0639  0.0481  0.1355  180 HIS A N   
1388 C  CA  . HIS A 185 ? 0.4817 0.6147 0.1780 0.0691  0.0389  0.1619  180 HIS A CA  
1389 C  C   . HIS A 185 ? 0.4674 0.6720 0.1449 0.0697  0.0302  0.1681  180 HIS A C   
1390 O  O   . HIS A 185 ? 0.5012 0.6855 0.1617 0.0582  0.0459  0.1759  180 HIS A O   
1391 C  CB  . HIS A 185 ? 0.4801 0.6255 0.1795 0.0547  0.0534  0.1526  180 HIS A CB  
1392 C  CG  . HIS A 185 ? 0.4929 0.6331 0.2236 0.0520  0.0483  0.1344  180 HIS A CG  
1393 N  ND1 . HIS A 185 ? 0.5421 0.6819 0.2622 0.0435  0.0196  0.1064  180 HIS A ND1 
1394 C  CD2 . HIS A 185 ? 0.4853 0.6451 0.2157 0.0407  0.0685  0.1241  180 HIS A CD2 
1395 C  CE1 . HIS A 185 ? 0.5028 0.6833 0.2878 0.0511  0.0332  0.0841  180 HIS A CE1 
1396 N  NE2 . HIS A 185 ? 0.5054 0.6666 0.2289 0.0431  0.0192  0.0970  180 HIS A NE2 
1397 N  N   . TYR A 186 ? 0.4809 0.7167 0.1141 0.0792  0.0014  0.1387  181 TYR A N   
1398 C  CA  . TYR A 186 ? 0.4615 0.7750 0.1059 0.0706  -0.0114 0.1187  181 TYR A CA  
1399 C  C   . TYR A 186 ? 0.4650 0.7776 0.0401 0.0697  0.0306  0.1016  181 TYR A C   
1400 O  O   . TYR A 186 ? 0.4755 0.7871 0.0365 0.0570  0.0430  0.0751  181 TYR A O   
1401 C  CB  . TYR A 186 ? 0.4179 0.8297 0.1035 0.0684  -0.0104 0.0973  181 TYR A CB  
1402 C  CG  . TYR A 186 ? 0.4648 0.8581 0.1689 0.0442  -0.0594 0.1176  181 TYR A CG  
1403 C  CD1 . TYR A 186 ? 0.5048 0.8892 0.2080 0.0243  -0.0926 0.1221  181 TYR A CD1 
1404 C  CD2 . TYR A 186 ? 0.4747 0.8853 0.1633 0.0479  -0.0846 0.0919  181 TYR A CD2 
1405 C  CE1 . TYR A 186 ? 0.5093 0.9183 0.2069 0.0307  -0.1122 0.1114  181 TYR A CE1 
1406 C  CE2 . TYR A 186 ? 0.5085 0.9141 0.2263 0.0359  -0.0874 0.1057  181 TYR A CE2 
1407 C  CZ  . TYR A 186 ? 0.5277 0.9367 0.2549 0.0371  -0.1153 0.1123  181 TYR A CZ  
1408 O  OH  . TYR A 186 ? 0.5497 1.0108 0.2599 0.0527  -0.1131 0.0945  181 TYR A OH  
1409 N  N   . GLU A 187 ? 0.4468 0.7518 0.0659 0.0795  0.0196  0.0723  182 GLU A N   
1410 C  CA  . GLU A 187 ? 0.5071 0.7657 0.0566 0.0673  0.0458  0.0540  182 GLU A CA  
1411 C  C   . GLU A 187 ? 0.5021 0.7377 0.0532 0.0530  0.0420  0.0516  182 GLU A C   
1412 O  O   . GLU A 187 ? 0.5082 0.7694 0.0687 0.0513  -0.0019 0.0041  182 GLU A O   
1413 C  CB  . GLU A 187 ? 0.5417 0.7675 0.0778 0.0600  0.0922  0.0520  182 GLU A CB  
1414 C  CG  . GLU A 187 ? 0.5795 0.8249 0.1614 0.0353  0.0911  0.0131  182 GLU A CG  
1415 C  CD  . GLU A 187 ? 0.6388 0.8543 0.1970 0.0321  0.1289  -0.0343 182 GLU A CD  
1416 O  OE1 . GLU A 187 ? 0.7213 0.9859 0.1491 0.0344  0.0923  -0.0038 182 GLU A OE1 
1417 O  OE2 . GLU A 187 ? 0.7409 0.9295 0.2925 -0.0301 0.1256  -0.1020 182 GLU A OE2 
1418 N  N   . ILE A 188 ? 0.4791 0.6918 0.0603 0.0484  0.0568  0.0922  183 ILE A N   
1419 C  CA  . ILE A 188 ? 0.4670 0.6741 0.0733 0.0747  0.0496  0.1107  183 ILE A CA  
1420 C  C   . ILE A 188 ? 0.4652 0.6730 0.0909 0.0798  0.0822  0.1443  183 ILE A C   
1421 O  O   . ILE A 188 ? 0.5019 0.7058 0.0506 0.0979  0.0499  0.1252  183 ILE A O   
1422 C  CB  . ILE A 188 ? 0.4689 0.6396 0.0995 0.0756  0.0247  0.1398  183 ILE A CB  
1423 C  CG1 . ILE A 188 ? 0.4957 0.6248 0.1691 0.0861  -0.0029 0.1445  183 ILE A CG1 
1424 C  CG2 . ILE A 188 ? 0.4839 0.6222 0.1164 0.0888  0.0065  0.1385  183 ILE A CG2 
1425 C  CD1 . ILE A 188 ? 0.5203 0.6126 0.1203 0.0768  -0.0198 0.1460  183 ILE A CD1 
1426 N  N   . ALA A 189 ? 0.4956 0.6925 0.1355 0.0754  0.0771  0.1456  184 ALA A N   
1427 C  CA  . ALA A 189 ? 0.5146 0.7117 0.1697 0.0885  0.0677  0.1545  184 ALA A CA  
1428 C  C   . ALA A 189 ? 0.4982 0.7589 0.2116 0.1036  0.0887  0.1898  184 ALA A C   
1429 O  O   . ALA A 189 ? 0.5442 0.7504 0.3687 0.0790  0.0896  0.2149  184 ALA A O   
1430 C  CB  . ALA A 189 ? 0.5422 0.7270 0.1598 0.0833  0.0848  0.1570  184 ALA A CB  
1431 N  N   . ASN A 190 ? 0.5277 0.8089 0.1853 0.1254  0.0535  0.1657  185 ASN A N   
1432 C  CA  . ASN A 190 ? 0.5849 0.8726 0.1426 0.1443  0.0592  0.1932  185 ASN A CA  
1433 C  C   . ASN A 190 ? 0.6114 0.8818 0.0846 0.1506  0.0656  0.2230  185 ASN A C   
1434 O  O   . ASN A 190 ? 0.6502 0.8287 0.1628 0.1582  0.1152  0.2664  185 ASN A O   
1435 C  CB  . ASN A 190 ? 0.6167 0.9699 0.2032 0.1385  0.0515  0.1602  185 ASN A CB  
1436 C  CG  . ASN A 190 ? 0.6511 1.0438 0.1913 0.1406  0.0394  0.1452  185 ASN A CG  
1437 O  OD1 . ASN A 190 ? 0.6995 1.1240 0.1697 0.1278  0.0498  0.1717  185 ASN A OD1 
1438 N  ND2 . ASN A 190 ? 0.6689 1.0862 0.2182 0.1481  0.0880  0.1385  185 ASN A ND2 
1439 N  N   . SER A 191 ? 0.5642 0.8925 0.1350 0.1560  0.1269  0.2131  186 SER A N   
1440 C  CA  . SER A 191 ? 0.5826 0.9272 0.1559 0.1463  0.1197  0.2144  186 SER A CA  
1441 C  C   . SER A 191 ? 0.5544 0.9012 0.1939 0.1533  0.1238  0.2502  186 SER A C   
1442 O  O   . SER A 191 ? 0.5599 0.8974 0.2263 0.1841  0.1284  0.2302  186 SER A O   
1443 C  CB  . SER A 191 ? 0.6175 0.9693 0.1523 0.1231  0.1930  0.1524  186 SER A CB  
1444 O  OG  . SER A 191 ? 0.6890 0.9577 0.3404 0.1047  0.1352  0.1386  186 SER A OG  
1445 N  N   . PRO A 192 ? 0.5678 0.9635 0.2295 0.1462  0.1092  0.2681  187 PRO A N   
1446 C  CA  . PRO A 192 ? 0.5652 0.9811 0.2352 0.1442  0.0951  0.2875  187 PRO A CA  
1447 C  C   . PRO A 192 ? 0.5597 1.0009 0.2421 0.1391  0.1174  0.2769  187 PRO A C   
1448 O  O   . PRO A 192 ? 0.5279 1.0313 0.1767 0.1239  0.0583  0.2967  187 PRO A O   
1449 C  CB  . PRO A 192 ? 0.5716 1.0202 0.3047 0.1255  0.0919  0.2372  187 PRO A CB  
1450 C  CG  . PRO A 192 ? 0.5996 1.0159 0.3037 0.1027  0.1178  0.2548  187 PRO A CG  
1451 C  CD  . PRO A 192 ? 0.5930 1.0006 0.2522 0.1112  0.1316  0.2707  187 PRO A CD  
1452 N  N   . GLU A 193 ? 0.5996 1.0019 0.2385 0.1587  0.1372  0.2647  188 GLU A N   
1453 C  CA  . GLU A 193 ? 0.6437 0.9988 0.2963 0.1749  0.1206  0.2561  188 GLU A CA  
1454 C  C   . GLU A 193 ? 0.6250 0.9532 0.2691 0.1864  0.1422  0.2611  188 GLU A C   
1455 O  O   . GLU A 193 ? 0.6040 0.9098 0.2370 0.2070  0.1235  0.2826  188 GLU A O   
1456 C  CB  . GLU A 193 ? 0.7472 1.0434 0.3165 0.1825  0.1124  0.2680  188 GLU A CB  
1457 C  CG  . GLU A 193 ? 0.8211 1.1161 0.4009 0.1903  0.0730  0.2536  188 GLU A CG  
1458 C  CD  . GLU A 193 ? 0.8904 1.1960 0.4001 0.1785  0.0891  0.2674  188 GLU A CD  
1459 O  OE1 . GLU A 193 ? 0.9286 1.1752 0.3980 0.1939  0.1286  0.3194  188 GLU A OE1 
1460 O  OE2 . GLU A 193 ? 0.9204 1.1981 0.4711 0.2285  0.0244  0.3978  188 GLU A OE2 
1461 N  N   . GLU A 194 ? 0.6354 0.8904 0.2340 0.1866  0.1334  0.2469  189 GLU A N   
1462 C  CA  . GLU A 194 ? 0.6306 0.8662 0.3213 0.1736  0.0986  0.2258  189 GLU A CA  
1463 C  C   . GLU A 194 ? 0.5833 0.8405 0.2721 0.1681  0.1006  0.2059  189 GLU A C   
1464 O  O   . GLU A 194 ? 0.5679 0.8104 0.2706 0.1705  0.0700  0.1810  189 GLU A O   
1465 C  CB  . GLU A 194 ? 0.6458 0.8765 0.4218 0.1607  0.1277  0.2019  189 GLU A CB  
1466 C  CG  . GLU A 194 ? 0.7071 0.8845 0.5094 0.1568  0.1102  0.1536  189 GLU A CG  
1467 C  CD  . GLU A 194 ? 0.7400 0.9043 0.5338 0.1283  0.1052  0.1185  189 GLU A CD  
1468 O  OE1 . GLU A 194 ? 0.8111 0.8957 0.5382 0.1384  0.1109  0.1141  189 GLU A OE1 
1469 O  OE2 . GLU A 194 ? 0.8344 0.9693 0.6732 0.0762  0.0973  0.0331  189 GLU A OE2 
1470 N  N   . ALA A 195 ? 0.5298 0.8144 0.2435 0.1722  0.0736  0.2076  190 ALA A N   
1471 C  CA  . ALA A 195 ? 0.5093 0.8257 0.2170 0.1722  0.0647  0.1953  190 ALA A CA  
1472 C  C   . ALA A 195 ? 0.5044 0.8318 0.2106 0.1678  0.0557  0.2091  190 ALA A C   
1473 O  O   . ALA A 195 ? 0.5465 0.7821 0.1702 0.1260  0.0246  0.1662  190 ALA A O   
1474 C  CB  . ALA A 195 ? 0.4747 0.8247 0.1969 0.1742  0.0501  0.1954  190 ALA A CB  
1475 N  N   . ILE A 196 ? 0.5094 0.8738 0.1557 0.1483  0.0562  0.2018  191 ILE A N   
1476 C  CA  . ILE A 196 ? 0.5087 0.8886 0.1815 0.1739  0.0531  0.2042  191 ILE A CA  
1477 C  C   . ILE A 196 ? 0.5204 0.8715 0.2411 0.1691  0.0613  0.2104  191 ILE A C   
1478 O  O   . ILE A 196 ? 0.5404 0.9046 0.2546 0.1807  0.0927  0.1751  191 ILE A O   
1479 C  CB  . ILE A 196 ? 0.4950 0.9110 0.2074 0.1607  0.0524  0.2134  191 ILE A CB  
1480 C  CG1 . ILE A 196 ? 0.4830 0.9644 0.2052 0.1364  0.0697  0.1883  191 ILE A CG1 
1481 C  CG2 . ILE A 196 ? 0.5036 0.9161 0.3000 0.1686  0.0590  0.2147  191 ILE A CG2 
1482 C  CD1 . ILE A 196 ? 0.4925 0.9851 0.2213 0.1542  0.0560  0.1883  191 ILE A CD1 
1483 N  N   . SER A 197 ? 0.5825 0.8500 0.2396 0.1558  0.1063  0.2291  192 SER A N   
1484 C  CA  . SER A 197 ? 0.6253 0.8337 0.2708 0.1561  0.1043  0.1962  192 SER A CA  
1485 C  C   . SER A 197 ? 0.5891 0.7808 0.2822 0.1592  0.1208  0.2185  192 SER A C   
1486 O  O   . SER A 197 ? 0.6058 0.7551 0.3150 0.1869  0.1426  0.2088  192 SER A O   
1487 C  CB  . SER A 197 ? 0.7009 0.8418 0.3488 0.1522  0.1076  0.1499  192 SER A CB  
1488 O  OG  . SER A 197 ? 0.7965 0.9205 0.3333 0.1756  0.0981  0.1230  192 SER A OG  
1489 N  N   . LEU A 198 ? 0.5587 0.7587 0.2475 0.1271  0.1034  0.2082  193 LEU A N   
1490 C  CA  . LEU A 198 ? 0.5276 0.6995 0.2582 0.1264  0.0647  0.1714  193 LEU A CA  
1491 C  C   . LEU A 198 ? 0.5134 0.6951 0.2192 0.1231  0.1036  0.1477  193 LEU A C   
1492 O  O   . LEU A 198 ? 0.5026 0.6535 0.2608 0.0968  0.1320  0.1288  193 LEU A O   
1493 C  CB  . LEU A 198 ? 0.5075 0.6911 0.2485 0.1052  0.0500  0.1694  193 LEU A CB  
1494 C  CG  . LEU A 198 ? 0.5163 0.6616 0.2269 0.0788  0.0308  0.1446  193 LEU A CG  
1495 C  CD1 . LEU A 198 ? 0.5156 0.6619 0.2638 0.0806  0.0422  0.1416  193 LEU A CD1 
1496 C  CD2 . LEU A 198 ? 0.5178 0.6344 0.2092 0.0712  0.0473  0.1554  193 LEU A CD2 
1497 N  N   . ALA A 199 ? 0.4759 0.6983 0.2091 0.1282  0.1081  0.1585  194 ALA A N   
1498 C  CA  . ALA A 199 ? 0.5073 0.7244 0.1312 0.1232  0.0778  0.1768  194 ALA A CA  
1499 C  C   . ALA A 199 ? 0.4849 0.7558 0.1730 0.1219  0.0659  0.1965  194 ALA A C   
1500 O  O   . ALA A 199 ? 0.4797 0.7408 0.2002 0.0864  0.0826  0.1979  194 ALA A O   
1501 C  CB  . ALA A 199 ? 0.4907 0.6960 0.2029 0.1397  0.0717  0.1832  194 ALA A CB  
1502 N  N   . LYS A 200 ? 0.5065 0.8056 0.2221 0.1455  0.0509  0.2020  195 LYS A N   
1503 C  CA  . LYS A 200 ? 0.5283 0.8373 0.2334 0.1637  0.0880  0.2135  195 LYS A CA  
1504 C  C   . LYS A 200 ? 0.5246 0.8067 0.2663 0.1589  0.0776  0.2149  195 LYS A C   
1505 O  O   . LYS A 200 ? 0.5207 0.8835 0.2381 0.1584  0.0691  0.1818  195 LYS A O   
1506 C  CB  . LYS A 200 ? 0.5490 0.8859 0.2836 0.2015  0.0533  0.2230  195 LYS A CB  
1507 C  CG  . LYS A 200 ? 0.6282 0.9749 0.3977 0.2055  0.0440  0.1964  195 LYS A CG  
1508 C  CD  . LYS A 200 ? 0.6778 0.9867 0.4473 0.2140  0.0610  0.2102  195 LYS A CD  
1509 C  CE  . LYS A 200 ? 0.6951 1.0271 0.4954 0.2031  0.0906  0.1738  195 LYS A CE  
1510 N  NZ  . LYS A 200 ? 0.6809 1.0363 0.5710 0.1969  0.0894  0.1731  195 LYS A NZ  
1511 N  N   . THR A 201 ? 0.5525 0.7736 0.2549 0.1612  0.1092  0.2221  196 THR A N   
1512 C  CA  . THR A 201 ? 0.5732 0.7581 0.3234 0.1497  0.1085  0.1907  196 THR A CA  
1513 C  C   . THR A 201 ? 0.5389 0.7259 0.3143 0.1216  0.1361  0.1711  196 THR A C   
1514 O  O   . THR A 201 ? 0.5289 0.7052 0.3437 0.1052  0.1675  0.1386  196 THR A O   
1515 C  CB  . THR A 201 ? 0.6271 0.7677 0.3627 0.1470  0.1173  0.2040  196 THR A CB  
1516 O  OG1 . THR A 201 ? 0.6765 0.7894 0.4044 0.1789  0.1583  0.2055  196 THR A OG1 
1517 C  CG2 . THR A 201 ? 0.6487 0.7521 0.4094 0.1515  0.1396  0.1944  196 THR A CG2 
1518 N  N   . THR A 202 ? 0.5065 0.7031 0.2578 0.1075  0.1246  0.1716  197 THR A N   
1519 C  CA  . THR A 202 ? 0.4882 0.6820 0.2279 0.0885  0.0885  0.1609  197 THR A CA  
1520 C  C   . THR A 202 ? 0.4753 0.7005 0.2217 0.0830  0.0840  0.1519  197 THR A C   
1521 O  O   . THR A 202 ? 0.4407 0.6789 0.2382 0.0862  0.1178  0.1698  197 THR A O   
1522 C  CB  . THR A 202 ? 0.4779 0.6644 0.2379 0.0680  0.0757  0.1605  197 THR A CB  
1523 O  OG1 . THR A 202 ? 0.4459 0.6688 0.2051 0.0915  0.0892  0.1493  197 THR A OG1 
1524 C  CG2 . THR A 202 ? 0.4386 0.6557 0.2340 0.0867  0.0466  0.1598  197 THR A CG2 
1525 N  N   . PHE A 203 ? 0.4682 0.7247 0.2015 0.0710  0.0676  0.1784  198 PHE A N   
1526 C  CA  . PHE A 203 ? 0.4733 0.7426 0.2160 0.0658  0.0634  0.1522  198 PHE A CA  
1527 C  C   . PHE A 203 ? 0.4680 0.7411 0.1941 0.0655  0.0869  0.1606  198 PHE A C   
1528 O  O   . PHE A 203 ? 0.4476 0.7542 0.1804 0.0603  0.0559  0.1916  198 PHE A O   
1529 C  CB  . PHE A 203 ? 0.4836 0.7571 0.1978 0.0575  0.0371  0.1416  198 PHE A CB  
1530 C  CG  . PHE A 203 ? 0.4459 0.7617 0.2239 0.0526  -0.0112 0.1375  198 PHE A CG  
1531 C  CD1 . PHE A 203 ? 0.4825 0.7819 0.3012 0.0340  -0.0351 0.1353  198 PHE A CD1 
1532 C  CD2 . PHE A 203 ? 0.4203 0.7906 0.2693 0.0456  -0.0406 0.1079  198 PHE A CD2 
1533 C  CE1 . PHE A 203 ? 0.4650 0.8049 0.2653 0.0388  -0.0368 0.1284  198 PHE A CE1 
1534 C  CE2 . PHE A 203 ? 0.4650 0.7981 0.2614 0.0571  -0.0363 0.1315  198 PHE A CE2 
1535 C  CZ  . PHE A 203 ? 0.4451 0.8065 0.2865 0.0485  -0.0484 0.1139  198 PHE A CZ  
1536 N  N   . ASP A 204 ? 0.4891 0.7266 0.2013 0.0899  0.0809  0.1431  199 ASP A N   
1537 C  CA  . ASP A 204 ? 0.4791 0.7410 0.2253 0.0807  0.0849  0.1360  199 ASP A CA  
1538 C  C   . ASP A 204 ? 0.4620 0.7152 0.2073 0.0938  0.0961  0.1160  199 ASP A C   
1539 O  O   . ASP A 204 ? 0.4315 0.7398 0.2720 0.1031  0.0903  0.0875  199 ASP A O   
1540 C  CB  . ASP A 204 ? 0.5139 0.7494 0.2879 0.0958  0.0705  0.1484  199 ASP A CB  
1541 C  CG  . ASP A 204 ? 0.5404 0.7730 0.3180 0.0946  0.0249  0.1702  199 ASP A CG  
1542 O  OD1 . ASP A 204 ? 0.5645 0.7915 0.4175 0.1019  0.0063  0.1626  199 ASP A OD1 
1543 O  OD2 . ASP A 204 ? 0.5988 0.8535 0.2866 0.1153  0.0489  0.1723  199 ASP A OD2 
1544 N  N   . GLU A 205 ? 0.4874 0.6937 0.2152 0.0738  0.0852  0.1276  200 GLU A N   
1545 C  CA  . GLU A 205 ? 0.4907 0.7051 0.2976 0.0726  0.0888  0.1021  200 GLU A CA  
1546 C  C   . GLU A 205 ? 0.4973 0.7058 0.2267 0.0708  0.0729  0.0723  200 GLU A C   
1547 O  O   . GLU A 205 ? 0.5118 0.7579 0.1281 0.0631  0.0376  0.0841  200 GLU A O   
1548 C  CB  . GLU A 205 ? 0.5102 0.7124 0.4086 0.0832  0.1288  0.1152  200 GLU A CB  
1549 C  CG  . GLU A 205 ? 0.5400 0.7152 0.4528 0.0889  0.1524  0.1178  200 GLU A CG  
1550 C  CD  . GLU A 205 ? 0.5731 0.7292 0.5153 0.0811  0.1602  0.1348  200 GLU A CD  
1551 O  OE1 . GLU A 205 ? 0.5874 0.7695 0.4985 0.0829  0.1620  0.1610  200 GLU A OE1 
1552 O  OE2 . GLU A 205 ? 0.6440 0.7371 0.6435 0.0812  0.1721  0.1254  200 GLU A OE2 
1553 N  N   . ALA A 206 ? 0.4640 0.6888 0.2239 0.0660  0.0410  0.0979  201 ALA A N   
1554 C  CA  . ALA A 206 ? 0.4291 0.7108 0.2129 0.0564  -0.0134 0.1208  201 ALA A CA  
1555 C  C   . ALA A 206 ? 0.4295 0.7342 0.1866 0.0602  -0.0244 0.1371  201 ALA A C   
1556 O  O   . ALA A 206 ? 0.4186 0.7059 0.1656 0.0627  -0.0144 0.1383  201 ALA A O   
1557 C  CB  . ALA A 206 ? 0.4206 0.7032 0.2149 0.0635  -0.0159 0.1337  201 ALA A CB  
1558 N  N   . MET A 207 ? 0.4634 0.7910 0.1786 0.0208  -0.0565 0.1426  202 MET A N   
1559 C  CA  . MET A 207 ? 0.4532 0.8099 0.1867 0.0426  -0.0691 0.1718  202 MET A CA  
1560 C  C   . MET A 207 ? 0.4570 0.7690 0.2987 0.0276  -0.0559 0.1691  202 MET A C   
1561 O  O   . MET A 207 ? 0.4127 0.7898 0.3389 0.0220  -0.0232 0.1043  202 MET A O   
1562 C  CB  . MET A 207 ? 0.5125 0.8687 0.1908 0.0110  -0.0693 0.1574  202 MET A CB  
1563 C  CG  . MET A 207 ? 0.5734 0.9126 0.2577 0.0113  -0.0564 0.1131  202 MET A CG  
1564 S  SD  . MET A 207 ? 0.6860 0.9189 0.3666 0.0082  -0.0082 0.0629  202 MET A SD  
1565 C  CE  . MET A 207 ? 0.7478 0.9457 0.4496 0.0234  -0.0022 0.0191  202 MET A CE  
1566 N  N   . ALA A 208 ? 0.5019 0.7625 0.3622 0.0341  -0.0087 0.1596  203 ALA A N   
1567 C  CA  . ALA A 208 ? 0.5043 0.7793 0.3701 0.0390  0.0201  0.1160  203 ALA A CA  
1568 C  C   . ALA A 208 ? 0.4807 0.7600 0.3548 0.0616  0.0464  0.1112  203 ALA A C   
1569 O  O   . ALA A 208 ? 0.4816 0.7885 0.3574 0.0985  -0.0085 0.0794  203 ALA A O   
1570 C  CB  . ALA A 208 ? 0.5458 0.7960 0.4311 0.0378  0.0316  0.1279  203 ALA A CB  
1571 N  N   . ASP A 209 ? 0.4935 0.7023 0.4025 0.0540  0.0551  0.0595  204 ASP A N   
1572 C  CA  . ASP A 209 ? 0.4900 0.6671 0.3741 0.0204  0.0643  0.0241  204 ASP A CA  
1573 C  C   . ASP A 209 ? 0.4940 0.6775 0.3125 -0.0103 0.0525  0.0121  204 ASP A C   
1574 O  O   . ASP A 209 ? 0.4557 0.7095 0.3267 -0.0204 0.0461  0.0055  204 ASP A O   
1575 C  CB  . ASP A 209 ? 0.4856 0.6704 0.4409 0.0250  0.0699  0.0235  204 ASP A CB  
1576 C  CG  . ASP A 209 ? 0.5002 0.6825 0.5771 0.0314  0.0399  0.0014  204 ASP A CG  
1577 O  OD1 . ASP A 209 ? 0.5259 0.7011 0.6627 0.0159  0.0934  0.0227  204 ASP A OD1 
1578 O  OD2 . ASP A 209 ? 0.5098 0.7061 0.5838 -0.0067 0.0373  0.0122  204 ASP A OD2 
1579 N  N   . LEU A 210 ? 0.5080 0.6475 0.1943 -0.0108 0.0507  0.0392  205 LEU A N   
1580 C  CA  . LEU A 210 ? 0.4930 0.6475 0.1210 -0.0160 0.0540  0.0329  205 LEU A CA  
1581 C  C   . LEU A 210 ? 0.4778 0.6130 0.1160 -0.0093 0.0422  0.0356  205 LEU A C   
1582 O  O   . LEU A 210 ? 0.4978 0.5918 0.1548 -0.0124 0.0478  0.0191  205 LEU A O   
1583 C  CB  . LEU A 210 ? 0.4743 0.6662 0.0618 0.0128  0.0112  0.0564  205 LEU A CB  
1584 C  CG  . LEU A 210 ? 0.4884 0.6773 0.0854 0.0079  0.0255  0.0637  205 LEU A CG  
1585 C  CD1 . LEU A 210 ? 0.5278 0.6837 0.0467 0.0166  0.0081  0.0585  205 LEU A CD1 
1586 C  CD2 . LEU A 210 ? 0.4782 0.7050 0.0314 0.0146  0.0343  0.0496  205 LEU A CD2 
1587 N  N   . HIS A 211 ? 0.5028 0.5999 0.1009 -0.0159 0.0362  0.0418  206 HIS A N   
1588 C  CA  . HIS A 211 ? 0.4906 0.6162 0.0981 -0.0281 0.0196  0.0367  206 HIS A CA  
1589 C  C   . HIS A 211 ? 0.4788 0.6473 0.0969 -0.0266 0.0263  0.0013  206 HIS A C   
1590 O  O   . HIS A 211 ? 0.4821 0.6586 0.1178 -0.0456 0.0501  -0.0047 206 HIS A O   
1591 C  CB  . HIS A 211 ? 0.4895 0.6108 0.0709 -0.0204 0.0077  0.0534  206 HIS A CB  
1592 C  CG  . HIS A 211 ? 0.4872 0.6156 0.0422 -0.0050 0.0197  0.0795  206 HIS A CG  
1593 N  ND1 . HIS A 211 ? 0.4995 0.6060 0.0363 -0.0070 0.0194  0.0766  206 HIS A ND1 
1594 C  CD2 . HIS A 211 ? 0.5002 0.6113 0.0583 -0.0047 0.0394  0.0903  206 HIS A CD2 
1595 C  CE1 . HIS A 211 ? 0.4629 0.6353 0.0524 -0.0011 -0.0098 0.1150  206 HIS A CE1 
1596 N  NE2 . HIS A 211 ? 0.4846 0.6237 0.0668 0.0095  0.0349  0.0943  206 HIS A NE2 
1597 N  N   . THR A 212 ? 0.5152 0.7004 0.1091 -0.0574 0.0264  -0.0249 207 THR A N   
1598 C  CA  . THR A 212 ? 0.5392 0.7109 0.0877 -0.0581 0.0241  0.0015  207 THR A CA  
1599 C  C   . THR A 212 ? 0.5388 0.7312 0.0255 -0.0432 0.0092  -0.0014 207 THR A C   
1600 O  O   . THR A 212 ? 0.6074 0.7894 0.0272 -0.0491 -0.0173 -0.0305 207 THR A O   
1601 C  CB  . THR A 212 ? 0.5198 0.7267 0.1921 -0.0618 0.0073  -0.0249 207 THR A CB  
1602 O  OG1 . THR A 212 ? 0.4575 0.7262 0.3249 -0.1125 0.0278  -0.0321 207 THR A OG1 
1603 C  CG2 . THR A 212 ? 0.5498 0.7227 0.2725 -0.0503 0.0168  -0.0195 207 THR A CG2 
1604 N  N   . LEU A 213 ? 0.4961 0.6974 0.0868 -0.0539 0.0316  0.0449  208 LEU A N   
1605 C  CA  . LEU A 213 ? 0.5008 0.7063 0.0279 -0.0422 0.0015  0.0418  208 LEU A CA  
1606 C  C   . LEU A 213 ? 0.4651 0.7007 0.0481 -0.0366 -0.0292 0.0484  208 LEU A C   
1607 O  O   . LEU A 213 ? 0.4631 0.6996 0.0914 -0.0449 0.0013  0.0464  208 LEU A O   
1608 C  CB  . LEU A 213 ? 0.5154 0.6958 0.0283 -0.0351 -0.0013 0.0389  208 LEU A CB  
1609 C  CG  . LEU A 213 ? 0.5271 0.7071 0.0865 -0.0403 -0.0059 0.0400  208 LEU A CG  
1610 C  CD1 . LEU A 213 ? 0.5296 0.7264 0.0590 -0.0412 0.0146  0.0659  208 LEU A CD1 
1611 C  CD2 . LEU A 213 ? 0.5289 0.7307 0.1420 -0.0492 0.0002  0.0176  208 LEU A CD2 
1612 N  N   . SER A 214 ? 0.4848 0.7173 0.0858 -0.0127 -0.0284 0.0874  209 SER A N   
1613 C  CA  . SER A 214 ? 0.5112 0.7338 0.1803 -0.0268 -0.0436 0.0838  209 SER A CA  
1614 C  C   . SER A 214 ? 0.4806 0.7239 0.2305 -0.0164 -0.0492 0.0877  209 SER A C   
1615 O  O   . SER A 214 ? 0.5263 0.7355 0.1857 -0.0503 -0.0564 0.0475  209 SER A O   
1616 C  CB  . SER A 214 ? 0.5087 0.7529 0.2652 -0.0159 -0.0700 0.1103  209 SER A CB  
1617 O  OG  . SER A 214 ? 0.5605 0.7768 0.3283 -0.0349 -0.0174 0.1122  209 SER A OG  
1618 N  N   . GLU A 215 ? 0.5196 0.7007 0.2698 0.0028  -0.0550 0.1332  210 GLU A N   
1619 C  CA  . GLU A 215 ? 0.5626 0.7309 0.3574 0.0211  -0.0299 0.1136  210 GLU A CA  
1620 C  C   . GLU A 215 ? 0.5599 0.7225 0.3901 0.0139  -0.0330 0.1319  210 GLU A C   
1621 O  O   . GLU A 215 ? 0.5532 0.7168 0.4152 0.0148  -0.0103 0.1368  210 GLU A O   
1622 C  CB  . GLU A 215 ? 0.6286 0.7327 0.4955 0.0094  -0.0235 0.0914  210 GLU A CB  
1623 C  CG  . GLU A 215 ? 0.6790 0.7708 0.5910 0.0185  -0.0092 0.0367  210 GLU A CG  
1624 C  CD  . GLU A 215 ? 0.7773 0.7748 0.5910 0.0391  0.0014  0.0458  210 GLU A CD  
1625 O  OE1 . GLU A 215 ? 0.8536 0.8056 0.7421 0.0693  -0.0073 0.0748  210 GLU A OE1 
1626 O  OE2 . GLU A 215 ? 0.8638 0.8147 0.5584 0.0704  0.0837  0.0206  210 GLU A OE2 
1627 N  N   . ASP A 216 ? 0.5734 0.7195 0.4274 0.0191  -0.0206 0.1425  211 ASP A N   
1628 C  CA  . ASP A 216 ? 0.5961 0.7465 0.4073 0.0151  -0.0049 0.1471  211 ASP A CA  
1629 C  C   . ASP A 216 ? 0.5308 0.7248 0.3403 0.0302  -0.0433 0.1350  211 ASP A C   
1630 O  O   . ASP A 216 ? 0.4826 0.7321 0.3929 0.0455  0.0009  0.1412  211 ASP A O   
1631 C  CB  . ASP A 216 ? 0.6606 0.7751 0.4595 0.0253  0.0043  0.1494  211 ASP A CB  
1632 C  CG  . ASP A 216 ? 0.7900 0.8110 0.4779 0.0042  0.0441  0.1494  211 ASP A CG  
1633 O  OD1 . ASP A 216 ? 0.8680 0.8415 0.5710 -0.0264 0.0543  0.1284  211 ASP A OD1 
1634 O  OD2 . ASP A 216 ? 0.8655 0.8757 0.5213 0.0065  0.1143  0.1473  211 ASP A OD2 
1635 N  N   . SER A 217 ? 0.5185 0.7128 0.2620 0.0086  -0.0738 0.1378  212 SER A N   
1636 C  CA  . SER A 217 ? 0.4593 0.7224 0.2262 0.0021  -0.0883 0.1353  212 SER A CA  
1637 C  C   . SER A 217 ? 0.4233 0.6832 0.1985 -0.0086 -0.0570 0.1134  212 SER A C   
1638 O  O   . SER A 217 ? 0.4348 0.6706 0.2434 -0.0084 -0.0196 0.0723  212 SER A O   
1639 C  CB  . SER A 217 ? 0.4553 0.7302 0.2490 -0.0129 -0.1077 0.1341  212 SER A CB  
1640 O  OG  . SER A 217 ? 0.5267 0.8173 0.3359 -0.0374 -0.1209 0.1102  212 SER A OG  
1641 N  N   . TYR A 218 ? 0.4216 0.6573 0.1905 -0.0055 -0.0487 0.1097  213 TYR A N   
1642 C  CA  . TYR A 218 ? 0.3985 0.6447 0.1921 -0.0088 -0.0353 0.0650  213 TYR A CA  
1643 C  C   . TYR A 218 ? 0.4026 0.6363 0.2692 -0.0079 -0.0129 0.0694  213 TYR A C   
1644 O  O   . TYR A 218 ? 0.4187 0.6266 0.2614 -0.0128 -0.0123 0.0367  213 TYR A O   
1645 C  CB  . TYR A 218 ? 0.4058 0.6295 0.1887 -0.0132 -0.0219 0.0544  213 TYR A CB  
1646 C  CG  . TYR A 218 ? 0.4014 0.6221 0.1707 -0.0064 -0.0105 0.0572  213 TYR A CG  
1647 C  CD1 . TYR A 218 ? 0.4143 0.6362 0.1584 0.0035  -0.0396 0.0474  213 TYR A CD1 
1648 C  CD2 . TYR A 218 ? 0.4041 0.6307 0.1583 -0.0200 -0.0206 0.0606  213 TYR A CD2 
1649 C  CE1 . TYR A 218 ? 0.3855 0.6330 0.1565 0.0054  -0.0520 0.0295  213 TYR A CE1 
1650 C  CE2 . TYR A 218 ? 0.3962 0.6257 0.1581 -0.0068 -0.0440 0.0488  213 TYR A CE2 
1651 C  CZ  . TYR A 218 ? 0.3953 0.6348 0.1758 -0.0021 -0.0679 0.0380  213 TYR A CZ  
1652 O  OH  . TYR A 218 ? 0.4598 0.6713 0.1340 -0.0193 -0.0712 0.0169  213 TYR A OH  
1653 N  N   . LYS A 219 ? 0.4292 0.6429 0.2741 -0.0094 0.0035  0.1021  214 LYS A N   
1654 C  CA  . LYS A 219 ? 0.4754 0.6647 0.3388 -0.0102 -0.0072 0.0978  214 LYS A CA  
1655 C  C   . LYS A 219 ? 0.4508 0.6382 0.3384 -0.0146 -0.0167 0.0947  214 LYS A C   
1656 O  O   . LYS A 219 ? 0.5169 0.6480 0.3670 -0.0073 -0.0419 0.0459  214 LYS A O   
1657 C  CB  . LYS A 219 ? 0.5206 0.6945 0.3844 -0.0302 0.0287  0.1202  214 LYS A CB  
1658 C  CG  . LYS A 219 ? 0.6172 0.7515 0.5047 -0.0417 0.0181  0.1324  214 LYS A CG  
1659 C  CD  . LYS A 219 ? 0.7109 0.7947 0.6086 -0.0485 0.0314  0.1588  214 LYS A CD  
1660 C  CE  . LYS A 219 ? 0.7538 0.8340 0.6316 -0.0539 0.0379  0.1856  214 LYS A CE  
1661 N  NZ  . LYS A 219 ? 0.8008 0.8636 0.6718 -0.0349 0.0030  0.1908  214 LYS A NZ  
1662 N  N   . ASP A 220 ? 0.4596 0.6395 0.3383 -0.0067 -0.0268 0.0884  215 ASP A N   
1663 C  CA  . ASP A 220 ? 0.4588 0.6449 0.3007 0.0022  -0.0186 0.0633  215 ASP A CA  
1664 C  C   . ASP A 220 ? 0.4459 0.6273 0.3109 0.0021  0.0267  0.0501  215 ASP A C   
1665 O  O   . ASP A 220 ? 0.4876 0.6565 0.3179 0.0286  0.0703  0.0954  215 ASP A O   
1666 C  CB  . ASP A 220 ? 0.4689 0.6857 0.3366 0.0190  -0.0542 0.0565  215 ASP A CB  
1667 C  CG  . ASP A 220 ? 0.5434 0.7222 0.3792 0.0143  -0.0667 0.0596  215 ASP A CG  
1668 O  OD1 . ASP A 220 ? 0.5545 0.7240 0.4223 0.0020  -0.0368 0.0707  215 ASP A OD1 
1669 O  OD2 . ASP A 220 ? 0.6234 0.8305 0.3607 0.0130  -0.1245 0.0916  215 ASP A OD2 
1670 N  N   . SER A 221 ? 0.4265 0.5924 0.2439 -0.0006 0.0257  0.0397  216 SER A N   
1671 C  CA  . SER A 221 ? 0.4108 0.6079 0.1899 -0.0155 -0.0072 0.0220  216 SER A CA  
1672 C  C   . SER A 221 ? 0.3968 0.6150 0.2067 -0.0041 -0.0122 0.0150  216 SER A C   
1673 O  O   . SER A 221 ? 0.3873 0.6368 0.1770 0.0057  0.0005  -0.0169 216 SER A O   
1674 C  CB  . SER A 221 ? 0.4078 0.5984 0.2274 -0.0322 -0.0258 0.0317  216 SER A CB  
1675 O  OG  . SER A 221 ? 0.3879 0.6167 0.2495 -0.0614 -0.0202 0.0241  216 SER A OG  
1676 N  N   . THR A 222 ? 0.3960 0.6320 0.1906 -0.0029 -0.0420 -0.0189 217 THR A N   
1677 C  CA  . THR A 222 ? 0.4056 0.6428 0.2384 -0.0136 -0.0389 -0.0230 217 THR A CA  
1678 C  C   . THR A 222 ? 0.4147 0.6446 0.2861 0.0032  -0.0150 -0.0274 217 THR A C   
1679 O  O   . THR A 222 ? 0.4344 0.6553 0.2791 -0.0141 0.0157  -0.0439 217 THR A O   
1680 C  CB  . THR A 222 ? 0.4260 0.6431 0.2613 0.0064  0.0041  -0.0039 217 THR A CB  
1681 O  OG1 . THR A 222 ? 0.4255 0.6485 0.3153 -0.0344 0.0354  0.0360  217 THR A OG1 
1682 C  CG2 . THR A 222 ? 0.4107 0.6739 0.2309 0.0001  0.0248  -0.0203 217 THR A CG2 
1683 N  N   . LEU A 223 ? 0.4417 0.6404 0.2839 0.0101  -0.0099 -0.0274 218 LEU A N   
1684 C  CA  . LEU A 223 ? 0.4719 0.6559 0.3543 0.0129  0.0210  0.0052  218 LEU A CA  
1685 C  C   . LEU A 223 ? 0.4799 0.6426 0.2868 0.0182  0.0136  0.0056  218 LEU A C   
1686 O  O   . LEU A 223 ? 0.4475 0.6378 0.3108 0.0006  0.0612  -0.0380 218 LEU A O   
1687 C  CB  . LEU A 223 ? 0.5327 0.6733 0.3865 0.0237  0.0070  0.0139  218 LEU A CB  
1688 C  CG  . LEU A 223 ? 0.5650 0.7089 0.4530 0.0175  0.0075  0.0055  218 LEU A CG  
1689 C  CD1 . LEU A 223 ? 0.5825 0.7220 0.5020 0.0084  0.0077  -0.0106 218 LEU A CD1 
1690 C  CD2 . LEU A 223 ? 0.5836 0.7350 0.4950 0.0270  -0.0208 0.0005  218 LEU A CD2 
1691 N  N   . ILE A 224 ? 0.4419 0.6250 0.2207 0.0179  0.0068  0.0408  219 ILE A N   
1692 C  CA  . ILE A 224 ? 0.4238 0.6244 0.2667 0.0150  0.0115  0.0419  219 ILE A CA  
1693 C  C   . ILE A 224 ? 0.3928 0.6198 0.2528 0.0303  0.0157  0.0486  219 ILE A C   
1694 O  O   . ILE A 224 ? 0.3977 0.6382 0.2604 0.0099  0.0497  0.0357  219 ILE A O   
1695 C  CB  . ILE A 224 ? 0.4403 0.6226 0.2528 0.0101  0.0034  0.0364  219 ILE A CB  
1696 C  CG1 . ILE A 224 ? 0.4700 0.6592 0.2715 -0.0208 -0.0265 0.0307  219 ILE A CG1 
1697 C  CG2 . ILE A 224 ? 0.4323 0.6119 0.2375 0.0084  0.0116  0.0142  219 ILE A CG2 
1698 C  CD1 . ILE A 224 ? 0.5147 0.6678 0.3039 -0.0230 -0.0216 0.0085  219 ILE A CD1 
1699 N  N   . MET A 225 ? 0.4185 0.5928 0.2500 0.0556  -0.0067 0.0388  220 MET A N   
1700 C  CA  . MET A 225 ? 0.4153 0.6138 0.2282 0.0547  -0.0031 0.0367  220 MET A CA  
1701 C  C   . MET A 225 ? 0.4278 0.6133 0.2566 0.0327  -0.0002 0.0135  220 MET A C   
1702 O  O   . MET A 225 ? 0.4539 0.5925 0.2491 0.0724  -0.0232 -0.0214 220 MET A O   
1703 C  CB  . MET A 225 ? 0.4172 0.6339 0.2323 0.0494  -0.0009 0.0365  220 MET A CB  
1704 C  CG  . MET A 225 ? 0.4449 0.6296 0.2736 0.0495  0.0160  0.0495  220 MET A CG  
1705 S  SD  . MET A 225 ? 0.5162 0.6758 0.2326 0.0353  0.0333  0.0745  220 MET A SD  
1706 C  CE  . MET A 225 ? 0.5010 0.6760 0.2454 0.0404  0.0117  0.0948  220 MET A CE  
1707 N  N   . GLN A 226 ? 0.4242 0.6136 0.2394 0.0156  0.0084  -0.0051 221 GLN A N   
1708 C  CA  . GLN A 226 ? 0.4120 0.6946 0.2214 -0.0078 0.0187  -0.0123 221 GLN A CA  
1709 C  C   . GLN A 226 ? 0.3935 0.6775 0.1869 -0.0100 0.0038  -0.0220 221 GLN A C   
1710 O  O   . GLN A 226 ? 0.4127 0.7195 0.2110 -0.0102 -0.0542 0.0146  221 GLN A O   
1711 C  CB  . GLN A 226 ? 0.4444 0.7208 0.2853 -0.0312 0.0222  -0.0203 221 GLN A CB  
1712 C  CG  . GLN A 226 ? 0.4768 0.7695 0.2930 -0.0524 0.0338  -0.0461 221 GLN A CG  
1713 C  CD  . GLN A 226 ? 0.4623 0.8203 0.3551 -0.0482 0.0392  -0.0668 221 GLN A CD  
1714 O  OE1 . GLN A 226 ? 0.4786 0.8587 0.4063 -0.0696 0.0869  -0.1150 221 GLN A OE1 
1715 N  NE2 . GLN A 226 ? 0.4874 0.8797 0.4075 -0.0803 -0.0109 -0.0599 221 GLN A NE2 
1716 N  N   . LEU A 227 ? 0.3943 0.6400 0.1847 0.0217  0.0207  0.0086  222 LEU A N   
1717 C  CA  . LEU A 227 ? 0.3843 0.6548 0.2275 0.0131  0.0003  0.0073  222 LEU A CA  
1718 C  C   . LEU A 227 ? 0.4118 0.6641 0.2081 0.0180  -0.0030 0.0208  222 LEU A C   
1719 O  O   . LEU A 227 ? 0.4125 0.6809 0.1869 -0.0007 -0.0039 0.0346  222 LEU A O   
1720 C  CB  . LEU A 227 ? 0.4144 0.6187 0.2381 0.0305  -0.0206 0.0147  222 LEU A CB  
1721 C  CG  . LEU A 227 ? 0.4094 0.6190 0.2520 0.0164  -0.0098 0.0067  222 LEU A CG  
1722 C  CD1 . LEU A 227 ? 0.4133 0.6246 0.2404 0.0242  -0.0124 0.0187  222 LEU A CD1 
1723 C  CD2 . LEU A 227 ? 0.4649 0.6148 0.2388 0.0101  0.0112  0.0012  222 LEU A CD2 
1724 N  N   . LEU A 228 ? 0.3883 0.6621 0.2150 0.0475  -0.0063 0.0356  223 LEU A N   
1725 C  CA  . LEU A 228 ? 0.4170 0.6788 0.1929 0.0453  -0.0100 0.0552  223 LEU A CA  
1726 C  C   . LEU A 228 ? 0.4311 0.7424 0.2317 0.0418  -0.0358 0.0647  223 LEU A C   
1727 O  O   . LEU A 228 ? 0.5094 0.7971 0.2237 0.0781  -0.0403 0.1095  223 LEU A O   
1728 C  CB  . LEU A 228 ? 0.4208 0.6781 0.1810 0.0486  -0.0075 0.0357  223 LEU A CB  
1729 C  CG  . LEU A 228 ? 0.4461 0.6740 0.1735 0.0551  -0.0114 0.0154  223 LEU A CG  
1730 C  CD1 . LEU A 228 ? 0.4658 0.6989 0.1862 0.0705  0.0019  0.0070  223 LEU A CD1 
1731 C  CD2 . LEU A 228 ? 0.4614 0.6671 0.1808 0.0418  -0.0176 0.0307  223 LEU A CD2 
1732 N  N   . ARG A 229 ? 0.4059 0.7923 0.2878 0.0646  -0.0560 0.0591  224 ARG A N   
1733 C  CA  . ARG A 229 ? 0.4656 0.8404 0.2928 0.0292  -0.0820 0.0378  224 ARG A CA  
1734 C  C   . ARG A 229 ? 0.4441 0.8675 0.2626 0.0302  -0.0431 0.0409  224 ARG A C   
1735 O  O   . ARG A 229 ? 0.4167 0.9324 0.3059 0.0167  -0.0981 0.0292  224 ARG A O   
1736 C  CB  . ARG A 229 ? 0.5088 0.8604 0.3532 0.0145  -0.0588 0.0401  224 ARG A CB  
1737 C  CG  . ARG A 229 ? 0.5851 0.8870 0.3565 0.0181  -0.1112 0.0322  224 ARG A CG  
1738 C  CD  . ARG A 229 ? 0.6753 0.9183 0.5042 0.0058  -0.0764 0.0293  224 ARG A CD  
1739 N  NE  . ARG A 229 ? 0.7742 0.9652 0.5617 0.0256  -0.0729 0.0097  224 ARG A NE  
1740 C  CZ  . ARG A 229 ? 0.8012 0.9644 0.6163 0.0129  -0.0556 0.0289  224 ARG A CZ  
1741 N  NH1 . ARG A 229 ? 0.8029 0.9880 0.6301 0.0001  -0.1020 0.0505  224 ARG A NH1 
1742 N  NH2 . ARG A 229 ? 0.7591 0.9660 0.5348 0.0153  -0.0430 0.0235  224 ARG A NH2 
1743 N  N   . ASP A 230 ? 0.4237 0.8978 0.2177 0.0284  -0.0743 0.0157  225 ASP A N   
1744 C  CA  . ASP A 230 ? 0.4680 0.8949 0.2431 0.0077  -0.0215 0.0104  225 ASP A CA  
1745 C  C   . ASP A 230 ? 0.4853 0.9070 0.2239 0.0039  -0.0285 0.0117  225 ASP A C   
1746 O  O   . ASP A 230 ? 0.4870 0.9436 0.2190 0.0070  -0.0151 0.0066  225 ASP A O   
1747 C  CB  . ASP A 230 ? 0.4916 0.8922 0.2528 -0.0095 -0.0188 -0.0078 225 ASP A CB  
1748 C  CG  . ASP A 230 ? 0.4980 0.9030 0.2993 -0.0294 0.0018  -0.0321 225 ASP A CG  
1749 O  OD1 . ASP A 230 ? 0.4940 0.9413 0.2939 -0.0451 0.0166  -0.0302 225 ASP A OD1 
1750 O  OD2 . ASP A 230 ? 0.5402 0.8282 0.3120 -0.0537 -0.0034 -0.0706 225 ASP A OD2 
1751 N  N   . ASN A 231 ? 0.4681 0.8829 0.1790 0.0138  -0.0418 0.0314  226 ASN A N   
1752 C  CA  . ASN A 231 ? 0.4588 0.8675 0.1683 0.0134  -0.0629 0.0464  226 ASN A CA  
1753 C  C   . ASN A 231 ? 0.5001 0.9036 0.1882 0.0380  -0.0470 0.0794  226 ASN A C   
1754 O  O   . ASN A 231 ? 0.5055 0.9142 0.1262 0.0243  -0.1065 0.0978  226 ASN A O   
1755 C  CB  . ASN A 231 ? 0.4602 0.8262 0.1041 0.0182  -0.0365 0.0166  226 ASN A CB  
1756 C  CG  . ASN A 231 ? 0.4076 0.7870 0.1200 0.0057  -0.0725 0.0043  226 ASN A CG  
1757 O  OD1 . ASN A 231 ? 0.4370 0.7871 0.1669 -0.0077 -0.0617 0.0290  226 ASN A OD1 
1758 N  ND2 . ASN A 231 ? 0.4301 0.7516 0.0583 0.0249  -0.0768 0.0067  226 ASN A ND2 
1759 N  N   . LEU A 232 ? 0.4885 0.9390 0.2255 0.0798  -0.0392 0.0964  227 LEU A N   
1760 C  CA  . LEU A 232 ? 0.5288 0.9896 0.2905 0.0853  -0.0463 0.1146  227 LEU A CA  
1761 C  C   . LEU A 232 ? 0.5712 1.0660 0.2650 0.0737  -0.0547 0.1193  227 LEU A C   
1762 O  O   . LEU A 232 ? 0.5816 1.1077 0.2170 0.1236  -0.1039 0.0724  227 LEU A O   
1763 C  CB  . LEU A 232 ? 0.5247 0.9836 0.3694 0.0998  -0.0432 0.1050  227 LEU A CB  
1764 C  CG  . LEU A 232 ? 0.5132 0.9624 0.3676 0.0954  -0.0459 0.1368  227 LEU A CG  
1765 C  CD1 . LEU A 232 ? 0.5357 0.9450 0.4021 0.0946  -0.0367 0.1563  227 LEU A CD1 
1766 C  CD2 . LEU A 232 ? 0.5459 0.9580 0.3094 0.1035  -0.1008 0.1696  227 LEU A CD2 
1767 N  N   . THR A 233 ? 0.5524 1.1239 0.1845 0.0555  -0.0734 0.1182  228 THR A N   
1768 C  CA  . THR A 233 ? 0.5462 1.1769 0.2674 0.0253  -0.1295 0.0578  228 THR A CA  
1769 C  C   . THR A 233 ? 0.5661 1.1883 0.2663 0.0297  -0.1709 0.0337  228 THR A C   
1770 O  O   . THR A 233 ? 0.5727 1.2154 0.2233 0.0059  -0.1736 -0.0819 228 THR A O   
1771 C  CB  . THR A 233 ? 0.5945 1.1735 0.3116 0.0139  -0.1356 0.0673  228 THR A CB  
1772 O  OG1 . THR A 233 ? 0.5372 1.2091 0.3847 0.0215  -0.1560 0.0482  228 THR A OG1 
1773 C  CG2 . THR A 233 ? 0.6119 1.1660 0.3385 -0.0017 -0.1160 0.0804  228 THR A CG2 
1774 N  N   . LEU A 234 ? 0.5383 1.1573 0.2784 0.0130  -0.1580 0.0161  229 LEU A N   
1775 C  CA  . LEU A 234 ? 0.5761 1.1151 0.2766 -0.0001 -0.1029 0.0387  229 LEU A CA  
1776 C  C   . LEU A 234 ? 0.6037 1.1050 0.2418 0.0282  -0.0927 0.0622  229 LEU A C   
1777 O  O   . LEU A 234 ? 0.6134 1.1471 0.2650 -0.0041 -0.0955 -0.0173 229 LEU A O   
1778 C  CB  . LEU A 234 ? 0.5898 1.1008 0.2562 -0.0119 -0.1128 0.0590  229 LEU A CB  
1779 C  CG  . LEU A 234 ? 0.6023 1.1158 0.3121 -0.0232 -0.0649 0.1009  229 LEU A CG  
1780 C  CD1 . LEU A 234 ? 0.6117 1.1168 0.3514 -0.0232 -0.0867 0.1330  229 LEU A CD1 
1781 C  CD2 . LEU A 234 ? 0.6223 1.1237 0.3466 -0.0325 -0.0502 0.0910  229 LEU A CD2 
1782 N  N   . TRP A 235 ? 0.6100 1.0808 0.2502 0.0236  -0.0704 0.1094  230 TRP A N   
1783 C  CA  . TRP A 235 ? 0.6477 1.0585 0.2264 0.0413  -0.0923 0.1535  230 TRP A CA  
1784 C  C   . TRP A 235 ? 0.7005 1.1178 0.2755 0.0590  -0.1135 0.1989  230 TRP A C   
1785 O  O   . TRP A 235 ? 0.7592 1.1077 0.3705 0.0462  -0.2069 0.2710  230 TRP A O   
1786 C  CB  . TRP A 235 ? 0.6035 1.0027 0.2142 0.0388  -0.0752 0.1523  230 TRP A CB  
1787 C  CG  . TRP A 235 ? 0.5578 0.9273 0.1407 0.0255  -0.0522 0.1461  230 TRP A CG  
1788 C  CD1 . TRP A 235 ? 0.5692 0.9112 0.1777 0.0285  -0.0786 0.1731  230 TRP A CD1 
1789 C  CD2 . TRP A 235 ? 0.5451 0.9019 0.1570 0.0374  -0.0605 0.1337  230 TRP A CD2 
1790 N  NE1 . TRP A 235 ? 0.5505 0.9321 0.1465 0.0337  -0.0540 0.1282  230 TRP A NE1 
1791 C  CE2 . TRP A 235 ? 0.5236 0.9029 0.1570 0.0295  -0.0585 0.1245  230 TRP A CE2 
1792 C  CE3 . TRP A 235 ? 0.5397 0.9018 0.1843 0.0423  -0.0690 0.1264  230 TRP A CE3 
1793 C  CZ2 . TRP A 235 ? 0.5267 0.8949 0.1051 0.0425  -0.0329 0.1349  230 TRP A CZ2 
1794 C  CZ3 . TRP A 235 ? 0.5394 0.8666 0.0955 0.0410  -0.0281 0.1470  230 TRP A CZ3 
1795 C  CH2 . TRP A 235 ? 0.5067 0.8732 0.1600 0.0458  -0.0344 0.1240  230 TRP A CH2 
1796 N  N   . THR A 236 ? 0.7577 1.1763 0.2934 0.0747  -0.1114 0.2132  231 THR A N   
1797 C  CA  . THR A 236 ? 0.8053 1.1916 0.4738 0.1110  -0.1413 0.2157  231 THR A CA  
1798 C  C   . THR A 236 ? 0.8315 1.2305 0.5533 0.1074  -0.1823 0.1748  231 THR A C   
1799 O  O   . THR A 236 ? 0.8191 1.2538 0.6251 0.1362  -0.1807 0.1531  231 THR A O   
1800 C  CB  . THR A 236 ? 0.8377 1.2262 0.5531 0.1320  -0.1267 0.2120  231 THR A CB  
1801 O  OG1 . THR A 236 ? 0.8694 1.2277 0.6964 0.1457  -0.1310 0.2530  231 THR A OG1 
1802 C  CG2 . THR A 236 ? 0.8421 1.2055 0.6797 0.1201  -0.1106 0.1748  231 THR A CG2 
1803 O  OXT . THR A 236 ? 0.8904 1.2582 0.5378 0.1133  -0.2475 0.1529  231 THR A OXT 
1804 N  N   . ASP B 1   ? 0.9271 1.0220 0.3839 0.0644  -0.0864 -0.0035 361 ASP P N   
1805 C  CA  . ASP B 1   ? 0.8856 0.9959 0.3632 0.0500  -0.0585 -0.0314 361 ASP P CA  
1806 C  C   . ASP B 1   ? 0.8228 0.9701 0.2629 0.0645  -0.0327 -0.0096 361 ASP P C   
1807 O  O   . ASP B 1   ? 0.8612 1.0127 0.1892 0.0808  -0.0525 -0.0247 361 ASP P O   
1808 C  CB  . ASP B 1   ? 0.9339 1.0278 0.4788 0.0230  -0.0494 -0.0297 361 ASP P CB  
1809 C  CG  . ASP B 1   ? 0.9916 1.0697 0.5855 0.0081  -0.0285 -0.0477 361 ASP P CG  
1810 O  OD1 . ASP B 1   ? 1.0405 1.0771 0.6664 0.0109  -0.0621 -0.1036 361 ASP P OD1 
1811 O  OD2 . ASP B 1   ? 0.9960 1.1247 0.7400 -0.0339 -0.0127 -0.0270 361 ASP P OD2 
1812 N  N   . ARG B 2   ? 0.7378 0.9254 0.2722 0.0466  -0.0285 -0.0280 362 ARG P N   
1813 C  CA  . ARG B 2   ? 0.6819 0.8838 0.2378 0.0416  0.0072  -0.0384 362 ARG P CA  
1814 C  C   . ARG B 2   ? 0.5882 0.8589 0.1731 0.0119  -0.0116 -0.0044 362 ARG P C   
1815 O  O   . ARG B 2   ? 0.5340 0.8429 0.1876 0.0071  -0.0351 0.0163  362 ARG P O   
1816 C  CB  . ARG B 2   ? 0.7306 0.8983 0.1822 0.0540  -0.0018 0.0036  362 ARG P CB  
1817 C  CG  . ARG B 2   ? 0.7684 0.8981 0.3285 0.0794  0.0123  0.0137  362 ARG P CG  
1818 C  CD  . ARG B 2   ? 0.8236 0.9303 0.3851 0.0741  0.0353  0.0670  362 ARG P CD  
1819 N  NE  . ARG B 2   ? 0.9040 0.9165 0.3221 0.0829  0.0664  0.0980  362 ARG P NE  
1820 C  CZ  . ARG B 2   ? 0.9332 0.9327 0.3153 0.0911  0.0855  0.1602  362 ARG P CZ  
1821 N  NH1 . ARG B 2   ? 0.9814 0.8654 0.2335 0.0600  0.0807  0.1812  362 ARG P NH1 
1822 N  NH2 . ARG B 2   ? 0.9434 0.9898 0.3859 0.1055  0.0707  0.2332  362 ARG P NH2 
1823 N  N   . SER B 3   ? 0.5669 0.8426 0.1257 0.0253  -0.0060 -0.0632 363 SER P N   
1824 C  CA  . SER B 3   ? 0.5093 0.8194 0.1312 0.0312  0.0093  -0.0315 363 SER P CA  
1825 C  C   . SER B 3   ? 0.4797 0.7873 0.1555 0.0367  0.0054  -0.0137 363 SER P C   
1826 O  O   . SER B 3   ? 0.4956 0.7960 0.1375 0.0555  -0.0490 -0.0437 363 SER P O   
1827 C  CB  . SER B 3   ? 0.5279 0.8289 0.1450 0.0433  0.0132  -0.0395 363 SER P CB  
1828 O  OG  . SER B 3   ? 0.5297 0.8496 0.1538 0.0284  -0.0112 -0.0342 363 SER P OG  
1829 N  N   . SER B 4   ? 0.4928 0.7240 0.0695 0.0317  0.0059  -0.0013 364 SER P N   
1830 C  CA  . SER B 4   ? 0.4688 0.6889 0.1114 0.0089  -0.0196 0.0459  364 SER P CA  
1831 C  C   . SER B 4   ? 0.4280 0.6153 0.0940 0.0244  -0.0110 0.0522  364 SER P C   
1832 O  O   . SER B 4   ? 0.4098 0.6396 0.0731 0.0185  0.0014  0.0634  364 SER P O   
1833 C  CB  . SER B 4   ? 0.4882 0.7069 0.1435 -0.0208 -0.0139 0.0326  364 SER P CB  
1834 O  OG  . SER B 4   ? 0.5295 0.7157 0.2229 -0.0454 -0.0583 0.0407  364 SER P OG  
1835 N  N   . SEP B 5   ? 0.4006 0.5942 0.0979 0.0148  -0.0333 0.0038  365 SEP P N   
1836 C  CA  . SEP B 5   ? 0.3997 0.5695 0.0861 -0.0049 -0.0144 0.0307  365 SEP P CA  
1837 C  CB  . SEP B 5   ? 0.3963 0.5395 0.0710 0.0132  -0.0230 0.0094  365 SEP P CB  
1838 O  OG  . SEP B 5   ? 0.4012 0.5381 0.0397 -0.0109 -0.0366 0.0018  365 SEP P OG  
1839 C  C   . SEP B 5   ? 0.4113 0.5284 0.1061 -0.0086 -0.0010 0.0369  365 SEP P C   
1840 O  O   . SEP B 5   ? 0.4260 0.5545 0.1487 -0.0049 -0.0197 0.0182  365 SEP P O   
1841 P  P   . SEP B 5   ? 0.4039 0.5198 0.0632 -0.0093 -0.0061 0.0069  365 SEP P P   
1842 O  O1P . SEP B 5   ? 0.3706 0.5135 0.1056 -0.0243 -0.0420 0.0206  365 SEP P O1P 
1843 O  O2P . SEP B 5   ? 0.4547 0.5365 0.0409 0.0046  -0.0117 0.0061  365 SEP P O2P 
1844 O  O3P . SEP B 5   ? 0.4244 0.5166 0.0485 -0.0182 0.0093  0.0228  365 SEP P O3P 
1845 N  N   . ALA B 6   ? 0.4024 0.5355 0.0970 -0.0149 -0.0144 0.0492  366 ALA P N   
1846 C  CA  . ALA B 6   ? 0.4247 0.5505 0.1259 -0.0294 0.0245  0.0484  366 ALA P CA  
1847 C  C   . ALA B 6   ? 0.4055 0.5453 0.1838 0.0024  -0.0053 0.0515  366 ALA P C   
1848 O  O   . ALA B 6   ? 0.4036 0.5178 0.1662 0.0229  -0.0026 0.0500  366 ALA P O   
1849 C  CB  . ALA B 6   ? 0.4525 0.5701 0.1085 -0.0318 0.0303  0.0181  366 ALA P CB  
1850 N  N   . PRO B 7   ? 0.4349 0.5823 0.1815 -0.0044 0.0053  0.0668  367 PRO P N   
1851 C  CA  . PRO B 7   ? 0.4521 0.6151 0.2262 0.0059  -0.0077 0.0803  367 PRO P CA  
1852 C  C   . PRO B 7   ? 0.5076 0.7045 0.2494 -0.0114 -0.0543 0.0934  367 PRO P C   
1853 O  O   . PRO B 7   ? 0.4606 0.7167 0.2829 -0.0223 -0.0479 0.0994  367 PRO P O   
1854 C  CB  . PRO B 7   ? 0.4615 0.6134 0.2510 0.0124  -0.0278 0.0844  367 PRO P CB  
1855 C  CG  . PRO B 7   ? 0.4487 0.6113 0.2568 0.0082  0.0161  0.0770  367 PRO P CG  
1856 C  CD  . PRO B 7   ? 0.4636 0.5940 0.2535 0.0130  0.0081  0.0784  367 PRO P CD  
1857 N  N   . ASN B 8   ? 0.6305 0.7804 0.3011 -0.0199 -0.0878 0.1030  368 ASN P N   
1858 C  CA  A ASN B 8   ? 0.6928 0.8399 0.3060 -0.0299 -0.1290 0.1013  368 ASN P CA  
1859 C  CA  B ASN B 8   ? 0.6993 0.8414 0.3144 -0.0317 -0.1229 0.0964  368 ASN P CA  
1860 C  C   . ASN B 8   ? 0.7710 0.8826 0.2977 -0.0509 -0.1519 0.1038  368 ASN P C   
1861 O  O   . ASN B 8   ? 0.9763 0.9268 0.2915 -0.0458 -0.1510 0.0745  368 ASN P O   
1862 C  CB  A ASN B 8   ? 0.7169 0.8415 0.3468 -0.0186 -0.1603 0.1179  368 ASN P CB  
1863 C  CB  B ASN B 8   ? 0.7401 0.8446 0.4066 -0.0209 -0.1261 0.0944  368 ASN P CB  
1864 C  CG  A ASN B 8   ? 0.7085 0.8185 0.3433 -0.0123 -0.1853 0.1243  368 ASN P CG  
1865 C  CG  B ASN B 8   ? 0.7590 0.8351 0.4522 -0.0288 -0.1119 0.0914  368 ASN P CG  
1866 O  OD1 A ASN B 8   ? 0.6688 0.8423 0.2606 -0.0409 -0.2740 0.1731  368 ASN P OD1 
1867 O  OD1 B ASN B 8   ? 0.7886 0.7953 0.4830 -0.0207 -0.2079 0.0939  368 ASN P OD1 
1868 N  ND2 A ASN B 8   ? 0.7235 0.8262 0.3436 -0.0050 -0.1702 0.1458  368 ASN P ND2 
1869 N  ND2 B ASN B 8   ? 0.7376 0.8453 0.5907 -0.0295 -0.0715 0.0461  368 ASN P ND2 
1870 N  N   . VAL B 9   ? 0.7787 1.0048 0.3716 -0.0568 -0.0951 0.0359  369 VAL P N   
1871 C  CA  . VAL B 9   ? 0.7297 1.0584 0.4720 -0.0584 -0.0643 0.0397  369 VAL P CA  
1872 C  C   . VAL B 9   ? 0.6552 1.0791 0.4664 -0.0328 -0.0773 0.0104  369 VAL P C   
1873 O  O   . VAL B 9   ? 0.6581 1.0936 0.3393 -0.0152 -0.1290 -0.0077 369 VAL P O   
1874 C  CB  . VAL B 9   ? 0.7502 1.0833 0.5684 -0.0405 -0.0456 -0.0010 369 VAL P CB  
1875 C  CG1 . VAL B 9   ? 0.6847 1.1068 0.6170 -0.0618 0.0137  0.0045  369 VAL P CG1 
1876 C  CG2 . VAL B 9   ? 0.7443 1.0558 0.6266 -0.0296 -0.0450 0.0040  369 VAL P CG2 
1877 O  OXT . VAL B 9   ? 0.5800 1.0983 0.6201 -0.0245 -0.0155 0.0149  369 VAL P OXT 
1878 CL CL  . CL  C .   ? 1.0145 1.0725 0.3561 0.0642  -0.0481 -0.1616 301 CL  A CL  
1879 MG MG  . MG  D .   ? 0.7249 0.9096 0.3700 -0.0179 0.0906  -0.1702 302 MG  A MG  
1880 CL CL  . CL  E .   ? 1.3159 1.1218 1.2501 -0.3341 -0.2971 0.0164  303 CL  A CL  
1881 O  O   . HOH F .   ? 0.6452 0.6937 0.8213 0.0403  0.1712  -0.0009 401 HOH A O   
1882 O  O   . HOH F .   ? 0.6942 1.0063 0.2119 -0.0021 -0.1298 -0.2573 402 HOH A O   
1883 O  O   . HOH F .   ? 0.6360 0.9476 0.1984 -0.0229 -0.0859 -0.2294 403 HOH A O   
1884 O  O   . HOH F .   ? 0.7443 1.0388 0.5938 -0.1379 -0.0277 0.2897  404 HOH A O   
1885 O  O   . HOH F .   ? 0.9857 0.7926 0.5746 0.1187  0.0637  -0.0972 405 HOH A O   
1886 O  O   . HOH F .   ? 0.8910 0.5445 0.2228 0.0149  -0.1383 0.0428  406 HOH A O   
1887 O  O   . HOH F .   ? 0.9123 0.7437 0.1750 0.0218  -0.1282 0.0494  407 HOH A O   
1888 O  O   . HOH F .   ? 0.7303 0.8758 0.3253 -0.0367 0.0316  -0.0479 408 HOH A O   
1889 O  O   . HOH F .   ? 0.5579 1.2091 0.3099 -0.0981 -0.0534 -0.1547 409 HOH A O   
1890 O  O   . HOH F .   ? 0.9140 0.7312 0.5789 0.0611  -0.2450 0.0413  410 HOH A O   
1891 O  O   . HOH F .   ? 0.7468 0.8185 0.2020 0.1061  0.1342  -0.0983 411 HOH A O   
1892 O  O   . HOH F .   ? 0.8273 0.8147 0.1445 -0.0958 -0.0483 -0.0346 412 HOH A O   
1893 O  O   . HOH F .   ? 0.6645 0.8158 0.2415 0.0432  0.0800  0.0509  413 HOH A O   
1894 O  O   . HOH F .   ? 0.6895 0.7532 0.1781 0.0434  -0.0622 -0.0291 414 HOH A O   
1895 O  O   . HOH F .   ? 0.9696 0.8462 0.0263 -0.0446 0.0254  0.0134  415 HOH A O   
1896 O  O   . HOH F .   ? 0.5145 0.5447 0.3239 -0.0136 0.1020  0.0713  416 HOH A O   
1897 O  O   . HOH F .   ? 0.7196 0.6632 0.1016 -0.0719 -0.0759 0.0417  417 HOH A O   
1898 O  O   . HOH F .   ? 0.5136 0.6261 0.0339 0.0263  -0.0629 0.0126  418 HOH A O   
1899 O  O   . HOH F .   ? 0.5330 0.7031 0.2422 0.0209  0.0429  -0.0613 419 HOH A O   
1900 O  O   . HOH F .   ? 0.7549 0.7053 0.2818 0.0155  0.2309  0.0100  420 HOH A O   
1901 O  O   . HOH F .   ? 0.6373 0.8905 0.8280 -0.1913 0.3551  -0.4011 421 HOH A O   
1902 O  O   . HOH F .   ? 0.6870 0.7970 0.4428 0.0482  0.1872  0.2404  422 HOH A O   
1903 O  O   . HOH F .   ? 0.5395 0.7491 0.6767 -0.0377 0.1895  -0.0057 423 HOH A O   
1904 O  O   . HOH F .   ? 0.4634 1.0409 0.2015 0.0610  -0.1330 -0.0967 424 HOH A O   
1905 O  O   . HOH F .   ? 0.4618 0.7107 0.3286 -0.0521 0.0309  0.0727  425 HOH A O   
1906 O  O   . HOH F .   ? 0.7837 0.7149 0.7216 0.0148  0.1534  -0.1719 426 HOH A O   
1907 O  O   . HOH F .   ? 0.6674 1.1062 0.2936 -0.2018 0.0930  -0.1833 427 HOH A O   
1908 O  O   . HOH F .   ? 1.0744 0.6284 0.2486 0.0400  0.0008  0.0310  428 HOH A O   
1909 O  O   . HOH F .   ? 0.7553 0.6484 0.0574 0.0761  0.0778  0.1168  429 HOH A O   
1910 O  O   . HOH F .   ? 0.5350 0.6788 0.1186 -0.0101 -0.0758 0.0050  430 HOH A O   
1911 O  O   . HOH F .   ? 0.7118 0.5039 0.0891 -0.0062 0.0146  0.0300  431 HOH A O   
1912 O  O   . HOH F .   ? 0.7364 0.8900 0.1441 -0.0915 -0.0273 -0.0590 432 HOH A O   
1913 O  O   . HOH F .   ? 0.6678 0.9387 0.1452 0.0310  0.1134  -0.0412 433 HOH A O   
1914 O  O   . HOH F .   ? 0.6596 0.5925 0.4181 0.0103  -0.0344 -0.0171 434 HOH A O   
1915 O  O   . HOH F .   ? 0.4917 0.6709 0.1323 0.0049  0.0036  -0.1352 435 HOH A O   
1916 O  O   . HOH F .   ? 0.5982 0.7815 0.4176 0.0430  0.0838  -0.0265 436 HOH A O   
1917 O  O   . HOH F .   ? 0.7306 0.7715 0.5686 0.0526  -0.0172 -0.0527 437 HOH A O   
1918 O  O   . HOH F .   ? 0.9082 0.7610 0.0735 0.0198  -0.0574 0.0919  438 HOH A O   
1919 O  O   . HOH F .   ? 0.4584 0.6338 0.0581 0.0029  -0.0605 -0.0479 439 HOH A O   
1920 O  O   . HOH F .   ? 0.9747 0.8623 0.0402 -0.2022 0.0171  0.0286  440 HOH A O   
1921 O  O   . HOH F .   ? 0.9163 0.6810 0.4685 0.1014  0.3485  0.1242  441 HOH A O   
1922 O  O   . HOH F .   ? 0.5201 1.1732 0.6665 0.0849  -0.1377 0.1154  442 HOH A O   
1923 O  O   . HOH F .   ? 0.6680 1.0525 0.1509 -0.1105 0.0969  -0.2061 443 HOH A O   
1924 O  O   . HOH F .   ? 0.9650 0.9059 0.2782 0.1884  0.0659  -0.0309 444 HOH A O   
1925 O  O   . HOH F .   ? 0.7257 0.7218 0.0578 0.1093  -0.1442 -0.0661 445 HOH A O   
1926 O  O   . HOH F .   ? 0.5679 0.5742 0.3566 0.0614  0.2092  0.1611  446 HOH A O   
1927 O  O   . HOH F .   ? 0.5395 0.8068 0.1782 0.0789  -0.0103 0.1392  447 HOH A O   
1928 O  O   . HOH F .   ? 0.5377 0.8134 0.1432 -0.0194 -0.0885 0.0294  448 HOH A O   
1929 O  O   . HOH F .   ? 0.6347 0.6748 0.2549 -0.0397 0.0888  -0.0377 449 HOH A O   
1930 O  O   . HOH F .   ? 0.6215 0.6683 0.0825 0.0053  0.0152  -0.0462 450 HOH A O   
1931 O  O   . HOH F .   ? 0.5511 0.8369 0.1283 -0.0306 0.0578  -0.0063 451 HOH A O   
1932 O  O   . HOH F .   ? 0.5577 0.6581 0.1645 0.0548  -0.0822 0.0865  452 HOH A O   
1933 O  O   . HOH F .   ? 0.4327 0.5861 0.2974 -0.0506 -0.0476 0.0456  453 HOH A O   
1934 O  O   . HOH F .   ? 0.5849 0.6875 0.0547 -0.1268 0.0161  -0.0329 454 HOH A O   
1935 O  O   . HOH F .   ? 0.9994 0.6678 0.2022 0.1841  0.1918  0.2172  455 HOH A O   
1936 O  O   . HOH F .   ? 0.5256 0.7624 0.0768 -0.0338 -0.1239 0.0483  456 HOH A O   
1937 O  O   . HOH F .   ? 0.6794 0.6392 0.1312 -0.0016 0.0269  0.0268  457 HOH A O   
1938 O  O   . HOH F .   ? 0.5523 0.8518 0.9504 0.1362  0.0363  -0.0088 458 HOH A O   
1939 O  O   . HOH F .   ? 0.5753 0.7027 0.9010 0.0219  0.0706  -0.1253 459 HOH A O   
1940 O  O   . HOH F .   ? 0.5327 0.6359 0.0503 0.0087  -0.0638 0.1006  460 HOH A O   
1941 O  O   . HOH F .   ? 0.9459 0.6888 0.8552 0.1012  0.3777  0.1385  461 HOH A O   
1942 O  O   . HOH F .   ? 0.8013 0.7188 0.3056 -0.1852 0.1662  -0.1361 462 HOH A O   
1943 O  O   . HOH F .   ? 0.8283 0.7560 0.1837 -0.0684 0.1963  0.0927  463 HOH A O   
1944 O  O   . HOH F .   ? 0.7303 0.8756 0.1740 -0.0513 -0.1521 -0.0752 464 HOH A O   
1945 O  O   . HOH F .   ? 0.7538 0.7388 0.0915 -0.0466 0.0591  0.1347  465 HOH A O   
1946 O  O   . HOH F .   ? 0.7523 0.7539 0.1620 -0.0661 -0.0230 0.0829  466 HOH A O   
1947 O  O   . HOH F .   ? 0.5559 1.3483 0.3283 -0.0974 -0.1992 -0.1788 467 HOH A O   
1948 O  O   . HOH F .   ? 0.5838 0.9112 0.3341 -0.1645 -0.0422 -0.2295 468 HOH A O   
1949 O  O   . HOH F .   ? 0.5823 0.7691 0.0294 0.0687  0.0455  -0.0112 469 HOH A O   
1950 O  O   . HOH F .   ? 0.4838 0.7240 0.0711 0.0452  -0.1086 0.0412  470 HOH A O   
1951 O  O   . HOH F .   ? 0.7262 0.7554 1.1781 0.0447  0.2733  -0.1079 471 HOH A O   
1952 O  O   . HOH F .   ? 0.5466 0.6699 0.1799 0.0476  0.0133  0.1586  472 HOH A O   
1953 O  O   . HOH F .   ? 0.8226 0.7760 0.2141 -0.0575 0.0301  -0.0161 473 HOH A O   
1954 O  O   . HOH F .   ? 0.9798 1.0978 0.1984 0.1363  -0.1425 0.0256  474 HOH A O   
1955 O  O   . HOH F .   ? 0.5102 0.7035 0.1512 0.0211  -0.0641 0.0642  475 HOH A O   
1956 O  O   . HOH F .   ? 0.4960 0.8500 0.2455 -0.0462 0.0212  -0.0995 476 HOH A O   
1957 O  O   . HOH F .   ? 0.5234 0.6426 0.1249 0.0091  -0.0093 -0.0574 477 HOH A O   
1958 O  O   . HOH F .   ? 0.6560 0.6193 0.1104 0.0618  -0.0641 0.0369  478 HOH A O   
1959 O  O   . HOH F .   ? 0.5506 0.8159 0.4460 0.0466  -0.1127 -0.0934 479 HOH A O   
1960 O  O   . HOH F .   ? 1.0113 0.6470 0.5546 0.0313  0.0494  0.0867  480 HOH A O   
1961 O  O   . HOH F .   ? 0.7753 0.9372 0.2380 -0.0948 0.0916  -0.0521 481 HOH A O   
1962 O  O   . HOH F .   ? 0.7366 0.6850 0.3429 0.1445  0.1524  0.0867  482 HOH A O   
1963 O  O   . HOH F .   ? 0.5428 0.7981 0.2072 -0.0114 -0.0293 0.2079  483 HOH A O   
1964 O  O   . HOH F .   ? 0.4809 0.7084 0.3076 0.0478  0.0927  0.0205  484 HOH A O   
1965 O  O   . HOH F .   ? 0.4940 0.5742 0.1094 0.0143  -0.0385 0.0664  485 HOH A O   
1966 O  O   . HOH F .   ? 0.9713 0.7025 0.0268 -0.2170 0.0128  -0.0316 486 HOH A O   
1967 O  O   . HOH F .   ? 0.7461 0.6145 0.7835 -0.0971 0.1322  -0.0069 487 HOH A O   
1968 O  O   . HOH F .   ? 0.4277 0.8312 0.1264 0.0013  0.0304  0.1039  488 HOH A O   
1969 O  O   . HOH F .   ? 0.4611 0.7329 0.1007 0.0362  -0.0942 -0.0882 489 HOH A O   
1970 O  O   . HOH F .   ? 0.4818 0.7857 0.1349 0.0433  0.0765  0.0965  490 HOH A O   
1971 O  O   . HOH F .   ? 0.7036 0.7864 0.0275 0.0309  -0.0290 -0.0285 491 HOH A O   
1972 O  O   . HOH F .   ? 0.7568 0.8609 0.1887 0.2756  0.0695  0.0971  492 HOH A O   
1973 O  O   . HOH F .   ? 0.5728 0.9043 0.3589 -0.0891 -0.0485 -0.1957 493 HOH A O   
1974 O  O   . HOH F .   ? 1.0040 0.6798 0.4609 0.0954  0.1095  0.0754  494 HOH A O   
1975 O  O   . HOH F .   ? 0.8204 0.4952 0.6529 -0.0032 0.1700  0.0681  495 HOH A O   
1976 O  O   . HOH F .   ? 0.6899 0.8055 0.0300 -0.0046 0.0478  0.0309  496 HOH A O   
1977 O  O   . HOH F .   ? 0.7633 0.7141 0.1824 -0.1429 0.1372  -0.1066 497 HOH A O   
1978 O  O   . HOH F .   ? 0.8394 0.8207 0.2324 0.0400  -0.1805 0.1757  498 HOH A O   
1979 O  O   . HOH F .   ? 1.3475 0.5238 0.6220 0.1587  0.1216  0.0305  499 HOH A O   
1980 O  O   . HOH F .   ? 0.9069 0.8928 0.3544 -0.0075 0.0627  0.1689  500 HOH A O   
1981 O  O   . HOH F .   ? 0.5105 0.6921 0.0560 -0.0264 0.0166  -0.0964 501 HOH A O   
1982 O  O   . HOH F .   ? 0.4290 0.5399 0.1101 -0.0238 -0.0315 -0.0009 502 HOH A O   
1983 O  O   . HOH F .   ? 0.5683 0.8190 0.4009 0.1474  0.2199  0.1948  503 HOH A O   
1984 O  O   . HOH F .   ? 0.5786 0.8433 0.1791 -0.0589 0.0951  -0.1269 504 HOH A O   
1985 O  O   . HOH F .   ? 0.7382 0.6505 0.6646 0.0900  -0.0047 -0.0874 505 HOH A O   
1986 O  O   . HOH F .   ? 0.9344 0.9150 0.2832 -0.0795 -0.2600 0.0961  506 HOH A O   
1987 O  O   . HOH F .   ? 0.8027 0.6919 0.1879 0.1400  0.0110  -0.0049 507 HOH A O   
1988 O  O   . HOH F .   ? 0.5770 0.8063 0.1669 -0.1136 -0.0589 0.0527  508 HOH A O   
1989 O  O   . HOH F .   ? 1.5983 0.5372 0.5566 -0.1098 0.3333  -0.0788 509 HOH A O   
1990 O  O   . HOH F .   ? 0.5052 0.7049 0.2993 -0.0532 0.1134  -0.2164 510 HOH A O   
1991 O  O   . HOH F .   ? 0.6101 0.6089 0.2017 0.0402  0.0793  0.0016  511 HOH A O   
1992 O  O   . HOH F .   ? 0.3695 0.7964 0.0863 -0.0014 0.0296  -0.0324 512 HOH A O   
1993 O  O   . HOH F .   ? 0.6704 0.8415 0.1089 -0.0591 0.0477  -0.0681 513 HOH A O   
1994 O  O   . HOH F .   ? 0.8393 0.8197 0.1842 0.0964  0.1921  0.0533  514 HOH A O   
1995 O  O   . HOH F .   ? 0.5208 0.6299 0.0989 0.0070  -0.1088 0.0561  515 HOH A O   
1996 O  O   . HOH F .   ? 0.5672 0.6820 0.0800 0.0228  0.0049  -0.1459 516 HOH A O   
1997 O  O   . HOH F .   ? 0.6361 0.5118 0.0275 0.0353  0.0337  -0.0094 517 HOH A O   
1998 O  O   . HOH F .   ? 0.7794 0.7973 0.1678 0.0214  -0.0422 0.0398  518 HOH A O   
1999 O  O   . HOH F .   ? 0.4547 0.5646 0.0448 0.0366  0.0113  0.0403  519 HOH A O   
2000 O  O   . HOH F .   ? 0.6365 0.5964 0.3024 -0.0295 -0.0579 0.0530  520 HOH A O   
2001 O  O   . HOH F .   ? 0.6491 0.6765 0.2552 0.0588  -0.0358 0.0072  521 HOH A O   
2002 O  O   . HOH F .   ? 0.5602 0.7473 0.1224 -0.0106 -0.0801 0.1073  522 HOH A O   
2003 O  O   . HOH F .   ? 0.8140 0.8486 0.9972 0.1659  -0.5006 -0.0015 523 HOH A O   
2004 O  O   . HOH F .   ? 0.5931 1.1771 0.5148 0.0021  -0.1202 0.1688  524 HOH A O   
2005 O  O   . HOH F .   ? 0.7114 0.6553 0.0857 -0.0755 0.0776  -0.0217 525 HOH A O   
2006 O  O   . HOH F .   ? 0.5435 0.7316 0.2400 -0.0076 0.0762  0.0299  526 HOH A O   
2007 O  O   . HOH F .   ? 0.4782 0.8090 0.2748 -0.0027 0.1062  0.0079  527 HOH A O   
2008 O  O   . HOH F .   ? 0.5875 1.0971 0.1488 0.0708  0.1156  0.1917  528 HOH A O   
2009 O  O   . HOH F .   ? 1.0402 0.8205 0.2465 0.1682  0.0105  0.0004  529 HOH A O   
2010 O  O   . HOH F .   ? 1.0011 0.7871 0.1885 -0.1224 0.1103  -0.0216 530 HOH A O   
2011 O  O   . HOH F .   ? 0.8684 0.7053 0.1828 0.1658  0.2534  0.0891  531 HOH A O   
2012 O  O   . HOH F .   ? 0.9977 0.9775 0.9528 -0.1793 -0.0850 -0.1247 532 HOH A O   
2013 O  O   . HOH F .   ? 1.0640 0.9666 0.4958 0.3936  0.2274  0.0422  533 HOH A O   
2014 O  O   . HOH F .   ? 0.7162 1.4397 0.2902 -0.3983 -0.1792 0.1705  534 HOH A O   
2015 O  O   . HOH F .   ? 0.8335 1.0132 0.4736 -0.1483 0.0906  -0.0650 535 HOH A O   
2016 O  O   . HOH F .   ? 0.7944 0.8658 0.3707 -0.0873 -0.1212 0.2777  536 HOH A O   
2017 O  O   . HOH F .   ? 1.1431 0.7231 0.5812 0.1136  0.4036  0.1480  537 HOH A O   
2018 O  O   . HOH F .   ? 1.2456 0.6623 0.6071 -0.1875 -0.0874 0.0210  538 HOH A O   
2019 O  O   . HOH F .   ? 0.8052 0.6929 0.1972 0.1142  0.1233  0.0868  539 HOH A O   
2020 O  O   . HOH F .   ? 0.5454 0.7075 0.2297 0.0025  -0.0360 0.0382  540 HOH A O   
2021 O  O   . HOH F .   ? 0.9974 0.6349 0.4771 0.1032  0.1934  -0.0240 541 HOH A O   
2022 O  O   . HOH F .   ? 1.2067 0.6177 1.3193 -0.1089 -0.1755 -0.1903 542 HOH A O   
2023 O  O   . HOH F .   ? 0.5376 0.7468 0.1793 0.0159  -0.0016 -0.0661 543 HOH A O   
2024 O  O   . HOH F .   ? 0.6454 0.6890 0.2213 0.0793  -0.0415 -0.1317 544 HOH A O   
2025 O  O   . HOH F .   ? 0.7981 0.8177 0.0852 -0.0873 -0.0886 -0.0088 545 HOH A O   
2026 O  O   . HOH F .   ? 1.1281 0.9318 0.9932 0.0884  -0.4535 0.1969  546 HOH A O   
2027 O  O   . HOH F .   ? 0.7681 1.0230 0.1771 0.0032  0.1471  -0.0026 547 HOH A O   
2028 O  O   . HOH F .   ? 0.8521 1.0164 0.0793 0.0922  -0.1380 -0.1895 548 HOH A O   
2029 O  O   . HOH F .   ? 0.5752 0.6050 0.0546 -0.0083 -0.0266 -0.0176 549 HOH A O   
2030 O  O   . HOH F .   ? 0.5266 0.8041 0.4462 -0.0725 -0.0072 -0.1271 550 HOH A O   
2031 O  O   . HOH F .   ? 0.8271 0.7427 0.2654 0.1533  -0.0608 -0.0924 551 HOH A O   
2032 O  O   . HOH F .   ? 0.5554 0.6795 0.2215 0.1194  -0.0770 0.0991  552 HOH A O   
2033 O  O   . HOH F .   ? 0.5965 0.8541 0.2872 0.1136  -0.0399 -0.0645 553 HOH A O   
2034 O  O   . HOH F .   ? 0.6117 0.8733 0.3154 -0.0967 0.0838  0.0242  554 HOH A O   
2035 O  O   . HOH F .   ? 0.6151 0.6543 0.3347 0.0005  0.0102  -0.0024 555 HOH A O   
2036 O  O   . HOH F .   ? 0.6260 1.3662 0.0344 0.1189  0.0198  0.0425  556 HOH A O   
2037 O  O   . HOH F .   ? 0.6210 0.9668 0.1884 0.0551  0.0208  0.0124  557 HOH A O   
2038 O  O   . HOH F .   ? 1.0041 1.0693 0.5058 0.2777  0.4762  0.2568  558 HOH A O   
2039 O  O   . HOH F .   ? 0.8077 0.6541 0.1239 -0.1375 0.0569  -0.0570 559 HOH A O   
2040 O  O   . HOH F .   ? 0.9562 1.2583 0.5568 -0.0283 -0.3208 -0.3284 560 HOH A O   
2041 O  O   . HOH F .   ? 0.6131 0.9836 0.2199 0.0014  -0.0391 0.1277  561 HOH A O   
2042 O  O   . HOH F .   ? 0.5487 0.7282 0.4058 0.0406  0.0822  0.1019  562 HOH A O   
2043 O  O   . HOH F .   ? 0.8568 0.6667 0.2407 -0.0337 0.1959  0.0188  563 HOH A O   
2044 O  O   . HOH F .   ? 0.5537 1.2832 0.2244 -0.1201 -0.0827 0.0310  564 HOH A O   
2045 O  O   . HOH F .   ? 0.5389 1.0897 0.2816 -0.0875 -0.0343 -0.1278 565 HOH A O   
2046 O  O   . HOH F .   ? 1.1224 0.9787 0.4791 0.0984  -0.5459 -0.0386 566 HOH A O   
2047 O  O   . HOH F .   ? 0.7906 0.9653 0.3103 0.0071  0.1649  -0.1120 567 HOH A O   
2048 O  O   . HOH F .   ? 0.6199 0.7147 0.0831 0.0532  -0.0385 -0.0098 568 HOH A O   
2049 O  O   . HOH F .   ? 0.8313 0.6868 0.2388 -0.0016 0.0693  -0.0297 569 HOH A O   
2050 O  O   . HOH F .   ? 0.7433 0.7410 0.1318 0.1297  -0.0301 0.0321  570 HOH A O   
2051 O  O   . HOH F .   ? 0.7380 0.8748 0.1037 -0.0943 -0.0316 0.0948  571 HOH A O   
2052 O  O   . HOH F .   ? 0.5235 0.7852 0.1922 -0.0009 -0.0214 0.1111  572 HOH A O   
2053 O  O   . HOH F .   ? 0.7102 0.7623 0.4768 0.1746  0.0299  -0.1113 573 HOH A O   
2054 O  O   . HOH F .   ? 0.7432 1.2472 0.2641 0.0045  -0.0828 -0.1099 574 HOH A O   
2055 O  O   . HOH F .   ? 0.6350 0.9359 0.8212 -0.0158 -0.0555 -0.1578 575 HOH A O   
2056 O  O   . HOH F .   ? 0.9116 0.8401 0.1566 -0.2289 0.0844  0.0796  576 HOH A O   
2057 O  O   . HOH F .   ? 0.6481 0.8098 0.1425 0.0622  0.0595  0.1365  577 HOH A O   
2058 O  O   . HOH F .   ? 0.5688 0.7095 0.0474 -0.0178 -0.0116 0.0127  578 HOH A O   
2059 O  O   . HOH F .   ? 0.6461 0.7082 0.4756 0.0286  -0.1890 0.0427  579 HOH A O   
2060 O  O   . HOH G .   ? 0.8696 0.9772 0.4337 0.2270  -0.3448 -0.1751 401 HOH P O   
2061 O  O   . HOH G .   ? 0.7669 0.5766 0.6764 -0.0940 0.0788  0.0253  402 HOH P O   
2062 O  O   . HOH G .   ? 0.4010 0.4816 0.0815 -0.0046 -0.0517 0.0416  403 HOH P O   
2063 O  O   . HOH G .   ? 0.5933 0.7303 0.2875 -0.0216 -0.1290 -0.0134 404 HOH P O   
2064 O  O   . HOH G .   ? 0.4597 0.6208 0.2489 -0.0051 -0.1150 -0.0399 405 HOH P O   
2065 O  O   . HOH G .   ? 1.0124 1.0142 0.4604 -0.2375 0.0563  -0.3222 406 HOH P O   
2066 O  O   . HOH G .   ? 0.9136 1.0674 0.7860 0.1168  0.3424  0.3259  407 HOH P O   
# 
