data_9EW7
# 
_entry.id   9EW7 
# 
_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   9EW7         pdb_00009ew7 10.2210/pdb9ew7/pdb 
WWPDB D_1292137214 ?            ?                   
# 
_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                        9EW7 
_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 'RAF proto-oncogene serine/threonine-protein kinase' 1208.175  1   2.7.11.1 ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                       35.453    1   ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                      24.305    2   ?        ? ? ? 
5 non-polymer syn 'CALCIUM ION'                                        40.078    2   ?        ? ? ? 
6 water       nat water                                                18.015    303 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Epithelial cell marker protein 1,Stratifin' 
2 'Proto-oncogene c-RAF,cRaf,Raf-1'            
# 
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 'QRST(SEP)TPNVH' QRSTSTPNVH 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 'CALCIUM ION'   CA  
6 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   GLN n 
2 2   ARG n 
2 3   SER n 
2 4   THR n 
2 5   SEP n 
2 6   THR n 
2 7   PRO n 
2 8   ASN n 
2 9   VAL n 
2 10  HIS 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       10 
_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 
CA  non-polymer         . 'CALCIUM ION'   ?               'Ca 2'           40.078  
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  -4  GLY GLY A . n 
A 1 2   ALA 2   -3  -3  ALA ALA A . n 
A 1 3   MET 3   -2  -2  MET MET A . n 
A 1 4   GLY 4   -1  -1  GLY GLY A . n 
A 1 5   SER 5   0   0   SER SER 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 CSO 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  74  SER SER A . n 
A 1 80  GLU 80  75  75  GLU GLU A . n 
A 1 81  GLU 81  76  76  GLU GLU A . n 
A 1 82  LYS 82  77  77  LYS LYS 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   GLN 1   255 255 GLN GLN P . n 
B 2 2   ARG 2   256 256 ARG ARG P . n 
B 2 3   SER 3   257 257 SER SER P . n 
B 2 4   THR 4   258 258 THR THR P . n 
B 2 5   SEP 5   259 259 SEP SEP P . n 
B 2 6   THR 6   260 260 THR THR P . n 
B 2 7   PRO 7   261 261 PRO PRO P . n 
B 2 8   ASN 8   262 262 ASN ASN P . n 
B 2 9   VAL 9   263 263 VAL VAL P . n 
B 2 10  HIS 10  264 264 HIS HIS 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 4 MG  1   303 234 MG  MG  A . 
F 5 CA  1   304 1   CA  CA  A . 
G 5 CA  1   305 2   CA  CA  A . 
H 6 HOH 1   401 121 HOH HOH A . 
H 6 HOH 2   402 302 HOH HOH A . 
H 6 HOH 3   403 167 HOH HOH A . 
H 6 HOH 4   404 319 HOH HOH A . 
H 6 HOH 5   405 153 HOH HOH A . 
H 6 HOH 6   406 211 HOH HOH A . 
H 6 HOH 7   407 151 HOH HOH A . 
H 6 HOH 8   408 105 HOH HOH A . 
H 6 HOH 9   409 126 HOH HOH A . 
H 6 HOH 10  410 325 HOH HOH A . 
H 6 HOH 11  411 54  HOH HOH A . 
H 6 HOH 12  412 81  HOH HOH A . 
H 6 HOH 13  413 242 HOH HOH A . 
H 6 HOH 14  414 279 HOH HOH A . 
H 6 HOH 15  415 107 HOH HOH A . 
H 6 HOH 16  416 78  HOH HOH A . 
H 6 HOH 17  417 316 HOH HOH A . 
H 6 HOH 18  418 139 HOH HOH A . 
H 6 HOH 19  419 119 HOH HOH A . 
H 6 HOH 20  420 47  HOH HOH A . 
H 6 HOH 21  421 48  HOH HOH A . 
H 6 HOH 22  422 181 HOH HOH A . 
H 6 HOH 23  423 49  HOH HOH A . 
H 6 HOH 24  424 221 HOH HOH A . 
H 6 HOH 25  425 103 HOH HOH A . 
H 6 HOH 26  426 75  HOH HOH A . 
H 6 HOH 27  427 113 HOH HOH A . 
H 6 HOH 28  428 77  HOH HOH A . 
H 6 HOH 29  429 115 HOH HOH A . 
H 6 HOH 30  430 134 HOH HOH A . 
H 6 HOH 31  431 259 HOH HOH A . 
H 6 HOH 32  432 195 HOH HOH A . 
H 6 HOH 33  433 10  HOH HOH A . 
H 6 HOH 34  434 18  HOH HOH A . 
H 6 HOH 35  435 30  HOH HOH A . 
H 6 HOH 36  436 87  HOH HOH A . 
H 6 HOH 37  437 74  HOH HOH A . 
H 6 HOH 38  438 170 HOH HOH A . 
H 6 HOH 39  439 106 HOH HOH A . 
H 6 HOH 40  440 55  HOH HOH A . 
H 6 HOH 41  441 162 HOH HOH A . 
H 6 HOH 42  442 86  HOH HOH A . 
H 6 HOH 43  443 26  HOH HOH A . 
H 6 HOH 44  444 161 HOH HOH A . 
H 6 HOH 45  445 96  HOH HOH A . 
H 6 HOH 46  446 15  HOH HOH A . 
H 6 HOH 47  447 141 HOH HOH A . 
H 6 HOH 48  448 21  HOH HOH A . 
H 6 HOH 49  449 166 HOH HOH A . 
H 6 HOH 50  450 31  HOH HOH A . 
H 6 HOH 51  451 194 HOH HOH A . 
H 6 HOH 52  452 239 HOH HOH A . 
H 6 HOH 53  453 44  HOH HOH A . 
H 6 HOH 54  454 209 HOH HOH A . 
H 6 HOH 55  455 207 HOH HOH A . 
H 6 HOH 56  456 27  HOH HOH A . 
H 6 HOH 57  457 97  HOH HOH A . 
H 6 HOH 58  458 323 HOH HOH A . 
H 6 HOH 59  459 109 HOH HOH A . 
H 6 HOH 60  460 214 HOH HOH A . 
H 6 HOH 61  461 56  HOH HOH A . 
H 6 HOH 62  462 14  HOH HOH A . 
H 6 HOH 63  463 193 HOH HOH A . 
H 6 HOH 64  464 46  HOH HOH A . 
H 6 HOH 65  465 144 HOH HOH A . 
H 6 HOH 66  466 314 HOH HOH A . 
H 6 HOH 67  467 145 HOH HOH A . 
H 6 HOH 68  468 112 HOH HOH A . 
H 6 HOH 69  469 156 HOH HOH A . 
H 6 HOH 70  470 59  HOH HOH A . 
H 6 HOH 71  471 4   HOH HOH A . 
H 6 HOH 72  472 58  HOH HOH A . 
H 6 HOH 73  473 255 HOH HOH A . 
H 6 HOH 74  474 183 HOH HOH A . 
H 6 HOH 75  475 164 HOH HOH A . 
H 6 HOH 76  476 16  HOH HOH A . 
H 6 HOH 77  477 159 HOH HOH A . 
H 6 HOH 78  478 5   HOH HOH A . 
H 6 HOH 79  479 84  HOH HOH A . 
H 6 HOH 80  480 89  HOH HOH A . 
H 6 HOH 81  481 249 HOH HOH A . 
H 6 HOH 82  482 263 HOH HOH A . 
H 6 HOH 83  483 7   HOH HOH A . 
H 6 HOH 84  484 142 HOH HOH A . 
H 6 HOH 85  485 188 HOH HOH A . 
H 6 HOH 86  486 2   HOH HOH A . 
H 6 HOH 87  487 28  HOH HOH A . 
H 6 HOH 88  488 244 HOH HOH A . 
H 6 HOH 89  489 218 HOH HOH A . 
H 6 HOH 90  490 308 HOH HOH A . 
H 6 HOH 91  491 330 HOH HOH A . 
H 6 HOH 92  492 261 HOH HOH A . 
H 6 HOH 93  493 140 HOH HOH A . 
H 6 HOH 94  494 37  HOH HOH A . 
H 6 HOH 95  495 234 HOH HOH A . 
H 6 HOH 96  496 114 HOH HOH A . 
H 6 HOH 97  497 11  HOH HOH A . 
H 6 HOH 98  498 111 HOH HOH A . 
H 6 HOH 99  499 332 HOH HOH A . 
H 6 HOH 100 500 17  HOH HOH A . 
H 6 HOH 101 501 3   HOH HOH A . 
H 6 HOH 102 502 192 HOH HOH A . 
H 6 HOH 103 503 39  HOH HOH A . 
H 6 HOH 104 504 50  HOH HOH A . 
H 6 HOH 105 505 225 HOH HOH A . 
H 6 HOH 106 506 38  HOH HOH A . 
H 6 HOH 107 507 32  HOH HOH A . 
H 6 HOH 108 508 79  HOH HOH A . 
H 6 HOH 109 509 132 HOH HOH A . 
H 6 HOH 110 510 238 HOH HOH A . 
H 6 HOH 111 511 230 HOH HOH A . 
H 6 HOH 112 512 180 HOH HOH A . 
H 6 HOH 113 513 22  HOH HOH A . 
H 6 HOH 114 514 91  HOH HOH A . 
H 6 HOH 115 515 240 HOH HOH A . 
H 6 HOH 116 516 73  HOH HOH A . 
H 6 HOH 117 517 25  HOH HOH A . 
H 6 HOH 118 518 148 HOH HOH A . 
H 6 HOH 119 519 118 HOH HOH A . 
H 6 HOH 120 520 137 HOH HOH A . 
H 6 HOH 121 521 34  HOH HOH A . 
H 6 HOH 122 522 246 HOH HOH A . 
H 6 HOH 123 523 41  HOH HOH A . 
H 6 HOH 124 524 40  HOH HOH A . 
H 6 HOH 125 525 205 HOH HOH A . 
H 6 HOH 126 526 124 HOH HOH A . 
H 6 HOH 127 527 33  HOH HOH A . 
H 6 HOH 128 528 100 HOH HOH A . 
H 6 HOH 129 529 208 HOH HOH A . 
H 6 HOH 130 530 165 HOH HOH A . 
H 6 HOH 131 531 23  HOH HOH A . 
H 6 HOH 132 532 171 HOH HOH A . 
H 6 HOH 133 533 101 HOH HOH A . 
H 6 HOH 134 534 117 HOH HOH A . 
H 6 HOH 135 535 95  HOH HOH A . 
H 6 HOH 136 536 68  HOH HOH A . 
H 6 HOH 137 537 35  HOH HOH A . 
H 6 HOH 138 538 62  HOH HOH A . 
H 6 HOH 139 539 235 HOH HOH A . 
H 6 HOH 140 540 303 HOH HOH A . 
H 6 HOH 141 541 306 HOH HOH A . 
H 6 HOH 142 542 320 HOH HOH A . 
H 6 HOH 143 543 61  HOH HOH A . 
H 6 HOH 144 544 104 HOH HOH A . 
H 6 HOH 145 545 57  HOH HOH A . 
H 6 HOH 146 546 12  HOH HOH A . 
H 6 HOH 147 547 206 HOH HOH A . 
H 6 HOH 148 548 184 HOH HOH A . 
H 6 HOH 149 549 232 HOH HOH A . 
H 6 HOH 150 550 185 HOH HOH A . 
H 6 HOH 151 551 128 HOH HOH A . 
H 6 HOH 152 552 237 HOH HOH A . 
H 6 HOH 153 553 88  HOH HOH A . 
H 6 HOH 154 554 60  HOH HOH A . 
H 6 HOH 155 555 45  HOH HOH A . 
H 6 HOH 156 556 6   HOH HOH A . 
H 6 HOH 157 557 138 HOH HOH A . 
H 6 HOH 158 558 284 HOH HOH A . 
H 6 HOH 159 559 130 HOH HOH A . 
H 6 HOH 160 560 65  HOH HOH A . 
H 6 HOH 161 561 9   HOH HOH A . 
H 6 HOH 162 562 200 HOH HOH A . 
H 6 HOH 163 563 20  HOH HOH A . 
H 6 HOH 164 564 176 HOH HOH A . 
H 6 HOH 165 565 127 HOH HOH A . 
H 6 HOH 166 566 135 HOH HOH A . 
H 6 HOH 167 567 250 HOH HOH A . 
H 6 HOH 168 568 131 HOH HOH A . 
H 6 HOH 169 569 82  HOH HOH A . 
H 6 HOH 170 570 72  HOH HOH A . 
H 6 HOH 171 571 154 HOH HOH A . 
H 6 HOH 172 572 67  HOH HOH A . 
H 6 HOH 173 573 231 HOH HOH A . 
H 6 HOH 174 574 186 HOH HOH A . 
H 6 HOH 175 575 275 HOH HOH A . 
H 6 HOH 176 576 53  HOH HOH A . 
H 6 HOH 177 577 198 HOH HOH A . 
H 6 HOH 178 578 178 HOH HOH A . 
H 6 HOH 179 579 19  HOH HOH A . 
H 6 HOH 180 580 85  HOH HOH A . 
H 6 HOH 181 581 290 HOH HOH A . 
H 6 HOH 182 582 155 HOH HOH A . 
H 6 HOH 183 583 146 HOH HOH A . 
H 6 HOH 184 584 216 HOH HOH A . 
H 6 HOH 185 585 204 HOH HOH A . 
H 6 HOH 186 586 329 HOH HOH A . 
H 6 HOH 187 587 245 HOH HOH A . 
H 6 HOH 188 588 203 HOH HOH A . 
H 6 HOH 189 589 123 HOH HOH A . 
H 6 HOH 190 590 51  HOH HOH A . 
H 6 HOH 191 591 264 HOH HOH A . 
H 6 HOH 192 592 212 HOH HOH A . 
H 6 HOH 193 593 252 HOH HOH A . 
H 6 HOH 194 594 110 HOH HOH A . 
H 6 HOH 195 595 315 HOH HOH A . 
H 6 HOH 196 596 243 HOH HOH A . 
H 6 HOH 197 597 152 HOH HOH A . 
H 6 HOH 198 598 291 HOH HOH A . 
H 6 HOH 199 599 228 HOH HOH A . 
H 6 HOH 200 600 13  HOH HOH A . 
H 6 HOH 201 601 129 HOH HOH A . 
H 6 HOH 202 602 260 HOH HOH A . 
H 6 HOH 203 603 327 HOH HOH A . 
H 6 HOH 204 604 328 HOH HOH A . 
H 6 HOH 205 605 277 HOH HOH A . 
H 6 HOH 206 606 307 HOH HOH A . 
H 6 HOH 207 607 125 HOH HOH A . 
H 6 HOH 208 608 210 HOH HOH A . 
H 6 HOH 209 609 236 HOH HOH A . 
H 6 HOH 210 610 326 HOH HOH A . 
H 6 HOH 211 611 220 HOH HOH A . 
H 6 HOH 212 612 201 HOH HOH A . 
H 6 HOH 213 613 268 HOH HOH A . 
H 6 HOH 214 614 311 HOH HOH A . 
H 6 HOH 215 615 98  HOH HOH A . 
H 6 HOH 216 616 175 HOH HOH A . 
H 6 HOH 217 617 309 HOH HOH A . 
H 6 HOH 218 618 289 HOH HOH A . 
H 6 HOH 219 619 163 HOH HOH A . 
H 6 HOH 220 620 83  HOH HOH A . 
H 6 HOH 221 621 197 HOH HOH A . 
H 6 HOH 222 622 116 HOH HOH A . 
H 6 HOH 223 623 177 HOH HOH A . 
H 6 HOH 224 624 191 HOH HOH A . 
H 6 HOH 225 625 99  HOH HOH A . 
H 6 HOH 226 626 269 HOH HOH A . 
H 6 HOH 227 627 310 HOH HOH A . 
H 6 HOH 228 628 294 HOH HOH A . 
H 6 HOH 229 629 199 HOH HOH A . 
H 6 HOH 230 630 322 HOH HOH A . 
H 6 HOH 231 631 136 HOH HOH A . 
H 6 HOH 232 632 226 HOH HOH A . 
H 6 HOH 233 633 122 HOH HOH A . 
H 6 HOH 234 634 251 HOH HOH A . 
H 6 HOH 235 635 299 HOH HOH A . 
H 6 HOH 236 636 169 HOH HOH A . 
H 6 HOH 237 637 168 HOH HOH A . 
H 6 HOH 238 638 331 HOH HOH A . 
H 6 HOH 239 639 296 HOH HOH A . 
H 6 HOH 240 640 317 HOH HOH A . 
H 6 HOH 241 641 196 HOH HOH A . 
H 6 HOH 242 642 36  HOH HOH A . 
H 6 HOH 243 643 223 HOH HOH A . 
H 6 HOH 244 644 266 HOH HOH A . 
H 6 HOH 245 645 271 HOH HOH A . 
H 6 HOH 246 646 29  HOH HOH A . 
H 6 HOH 247 647 43  HOH HOH A . 
H 6 HOH 248 648 173 HOH HOH A . 
H 6 HOH 249 649 190 HOH HOH A . 
H 6 HOH 250 650 172 HOH HOH A . 
H 6 HOH 251 651 120 HOH HOH A . 
H 6 HOH 252 652 80  HOH HOH A . 
H 6 HOH 253 653 287 HOH HOH A . 
H 6 HOH 254 654 254 HOH HOH A . 
H 6 HOH 255 655 313 HOH HOH A . 
H 6 HOH 256 656 157 HOH HOH A . 
H 6 HOH 257 657 66  HOH HOH A . 
H 6 HOH 258 658 90  HOH HOH A . 
H 6 HOH 259 659 174 HOH HOH A . 
H 6 HOH 260 660 265 HOH HOH A . 
H 6 HOH 261 661 305 HOH HOH A . 
H 6 HOH 262 662 64  HOH HOH A . 
H 6 HOH 263 663 108 HOH HOH A . 
H 6 HOH 264 664 150 HOH HOH A . 
H 6 HOH 265 665 76  HOH HOH A . 
H 6 HOH 266 666 160 HOH HOH A . 
H 6 HOH 267 667 304 HOH HOH A . 
H 6 HOH 268 668 298 HOH HOH A . 
H 6 HOH 269 669 52  HOH HOH A . 
H 6 HOH 270 670 147 HOH HOH A . 
H 6 HOH 271 671 92  HOH HOH A . 
H 6 HOH 272 672 301 HOH HOH A . 
H 6 HOH 273 673 149 HOH HOH A . 
H 6 HOH 274 674 219 HOH HOH A . 
H 6 HOH 275 675 297 HOH HOH A . 
H 6 HOH 276 676 93  HOH HOH A . 
H 6 HOH 277 677 227 HOH HOH A . 
H 6 HOH 278 678 286 HOH HOH A . 
H 6 HOH 279 679 288 HOH HOH A . 
H 6 HOH 280 680 241 HOH HOH A . 
H 6 HOH 281 681 182 HOH HOH A . 
H 6 HOH 282 682 69  HOH HOH A . 
H 6 HOH 283 683 63  HOH HOH A . 
H 6 HOH 284 684 179 HOH HOH A . 
H 6 HOH 285 685 276 HOH HOH A . 
H 6 HOH 286 686 224 HOH HOH A . 
I 6 HOH 1   301 187 HOH HOH P . 
I 6 HOH 2   302 222 HOH HOH P . 
I 6 HOH 3   303 42  HOH HOH P . 
I 6 HOH 4   304 143 HOH HOH P . 
I 6 HOH 5   305 71  HOH HOH P . 
I 6 HOH 6   306 70  HOH HOH P . 
I 6 HOH 7   307 8   HOH HOH P . 
I 6 HOH 8   308 102 HOH HOH P . 
I 6 HOH 9   309 94  HOH HOH P . 
I 6 HOH 10  310 229 HOH HOH P . 
I 6 HOH 11  311 258 HOH HOH P . 
I 6 HOH 12  312 24  HOH HOH P . 
I 6 HOH 13  313 215 HOH HOH P . 
I 6 HOH 14  314 253 HOH HOH P . 
I 6 HOH 15  315 295 HOH HOH P . 
I 6 HOH 16  316 262 HOH HOH P . 
I 6 HOH 17  317 158 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' ? ? ? ? ? ? ? ? ? ? ? DIALS    ? ? ? . 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                     9EW7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.375 
_cell.length_a_esd                 ? 
_cell.length_b                     112.196 
_cell.length_b_esd                 ? 
_cell.length_c                     62.708 
_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                         9EW7 
_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                   9EW7 
_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             2.63 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.26 
_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 PILATUS 200K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-05 
_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   1.541870 
_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                      'SEALED TUBE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-003' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.541870 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EW7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               34.43 
_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                                     27325 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.3 
_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                                    1.8 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1612 
_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                                  0.932 
_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]                            0.49 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.22 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.27 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               13.707 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.940 
_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                                 9EW7 
_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                            1.80 
_refine.ls_d_res_low                             34.43 
_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                     25909 
_refine.ls_number_reflns_R_free                  1397 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16526 
_refine.ls_R_factor_R_free                       0.19251 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16372 
_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                       0.110 
_refine.pdbx_overall_ESU_R_Free                  0.104 
_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                             2.087 
_refine.overall_SU_ML                            0.066 
_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                       1.80 
_refine_hist.d_res_low                        34.43 
_refine_hist.number_atoms_solvent             303 
_refine_hist.number_atoms_total               2247 
_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        1939 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_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' ? 0.015  0.016  1975 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1869 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.293  1.825  2653 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 0.516  1.568  4321 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 5.408  5.290  259  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 13.446 10.000 372  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 0.064  0.200  293  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  2303 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  429  ? r_gen_planes_other     ? ? 
'X-RAY DIFFRACTION' ? 2.373  1.079  984  ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.379  1.080  984  ? r_mcbond_other         ? ? 
'X-RAY DIFFRACTION' ? 3.695  1.924  1221 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 3.705  1.928  1222 ? r_mcangle_other        ? ? 
'X-RAY DIFFRACTION' ? 3.604  1.438  991  ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 3.602  1.442  992  ? r_scbond_other         ? ? 
'X-RAY DIFFRACTION' ? 5.451  2.444  1432 ? r_scangle_other        ? ? 
'X-RAY DIFFRACTION' ? 7.129  16.530 2465 ? r_long_range_B_refined ? ? 
'X-RAY DIFFRACTION' ? 6.917  14.360 2359 ? r_long_range_B_other   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             99 
_refine_ls_shell.number_reflns_R_work             1884 
_refine_ls_shell.percent_reflns_obs               99.95 
_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                  0.195 
_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                  0.221 
# 
_struct.entry_id                     9EW7 
_struct.title                        'Binary structure of 14-3-3s and CRAF phosphopeptide (pS259)' 
_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        9EW7 
_struct_keywords.text            '14-3-3 protein, protein-protein interactions, 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 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
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 RAF1_HUMAN  P04049 ? 2 QRSTSTPNVH 255 
# 
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 9EW7 A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 9EW7 P 1 ? 10  ? P04049 255 ? 264 ? 255 264 
# 
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 9EW7 GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 9EW7 ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 9EW7 MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 9EW7 GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 9EW7 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)' 6060  ? 
1 MORE         -115  ? 
1 'SSA (A^2)'  24010 ? 
# 
_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,H,I 
# 
_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  ? LYS A 37  ? ARG A 18  LYS A 32  1 ? 15 
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  ? SER A 110 ? PRO A 79  SER A 105 1 ? 27 
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 ASP A 143 ? MET A 167 ? ASP A 138 MET A 162 1 ? 25 
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 THR 4   C   ? ? ? 1_555 B SEP 5 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale2  covale both ? B SEP 5   C   ? ? ? 1_555 B THR 6 N  ? ? P SEP 259 P THR 260 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
metalc1  metalc ?    ? A GLN 13  OE1 ? ? ? 1_555 F CA  . CA ? ? A GLN 8   A CA  304 1_555 ? ? ? ? ? ? ? 2.801 ? ? 
metalc2  metalc ?    ? A GLU 40  OE1 ? ? ? 1_555 G CA  . CA ? ? A GLU 35  A CA  305 1_555 ? ? ? ? ? ? ? 2.580 ? ? 
metalc3  metalc ?    ? A GLU 40  OE2 ? ? ? 1_555 G CA  . CA ? ? A GLU 35  A CA  305 1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc4  metalc ?    ? A GLU 80  OE1 ? ? ? 1_555 E MG  . MG ? ? A GLU 75  A MG  303 1_555 ? ? ? ? ? ? ? 2.539 ? ? 
metalc5  metalc ?    ? A LYS 82  O   ? ? ? 1_555 F CA  . CA ? ? A LYS 77  A CA  304 4_555 ? ? ? ? ? ? ? 2.403 ? ? 
metalc6  metalc ?    ? A GLU 85  OE1 ? ? ? 1_555 F CA  . CA ? ? A GLU 80  A CA  304 4_555 ? ? ? ? ? ? ? 2.609 ? ? 
metalc7  metalc ?    ? A GLU 85  OE2 ? ? ? 1_555 F CA  . CA ? ? A GLU 80  A CA  304 4_555 ? ? ? ? ? ? ? 2.964 ? ? 
metalc8  metalc ?    ? A GLU 94  OE2 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc9  metalc ?    ? A GLU 115 O   ? ? ? 1_555 G CA  . CA ? ? A GLU 110 A CA  305 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc10 metalc ?    ? A GLU 166 O   ? ? ? 1_555 E MG  . MG ? ? A GLU 161 A MG  303 7_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc11 metalc ?    ? A GLU 193 OE2 ? ? ? 1_555 G CA  . CA ? ? A GLU 188 A CA  305 6_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc12 metalc ?    ? D MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  302 A HOH 422 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc13 metalc ?    ? D MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  302 A HOH 612 1_555 ? ? ? ? ? ? ? 2.206 ? ? 
metalc14 metalc ?    ? E MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  303 A HOH 488 7_545 ? ? ? ? ? ? ? 2.198 ? ? 
metalc15 metalc ?    ? E MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  303 A HOH 539 1_555 ? ? ? ? ? ? ? 2.506 ? ? 
metalc16 metalc ?    ? E MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  303 A HOH 552 7_545 ? ? ? ? ? ? ? 2.300 ? ? 
metalc17 metalc ?    ? E MG  .   MG  ? ? ? 1_555 H HOH . O  ? ? A MG  303 A HOH 591 4_556 ? ? ? ? ? ? ? 2.370 ? ? 
metalc18 metalc ?    ? F CA  .   CA  ? ? ? 1_555 H HOH . O  ? ? A CA  304 A HOH 442 4_555 ? ? ? ? ? ? ? 2.924 ? ? 
metalc19 metalc ?    ? F CA  .   CA  ? ? ? 1_555 H HOH . O  ? ? A CA  304 A HOH 613 4_555 ? ? ? ? ? ? ? 2.681 ? ? 
metalc20 metalc ?    ? G CA  .   CA  ? ? ? 1_555 H HOH . O  ? ? A CA  305 A HOH 528 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc21 metalc ?    ? G CA  .   CA  ? ? ? 1_555 H HOH . O  ? ? A CA  305 A HOH 540 6_554 ? ? ? ? ? ? ? 2.444 ? ? 
metalc22 metalc ?    ? G CA  .   CA  ? ? ? 1_555 H HOH . O  ? ? A CA  305 A HOH 594 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLN 13  ? A GLN 8   ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? A LYS 82  ? A LYS 77  ? 1_555 30.1  ? 
2  OE1 ? A GLN 13  ? A GLN 8   ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 OE1 ? A GLU 85  ? A GLU 80  ? 1_555 32.2  ? 
3  O   ? A LYS 82  ? A LYS 77  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 OE1 ? A GLU 85  ? A GLU 80  ? 1_555 2.2   ? 
4  OE1 ? A GLN 13  ? A GLN 8   ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 OE2 ? A GLU 85  ? A GLU 80  ? 1_555 34.6  ? 
5  O   ? A LYS 82  ? A LYS 77  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 OE2 ? A GLU 85  ? A GLU 80  ? 1_555 4.5   ? 
6  OE1 ? A GLU 85  ? A GLU 80  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 OE2 ? A GLU 85  ? A GLU 80  ? 1_555 2.6   ? 
7  OE1 ? A GLN 13  ? A GLN 8   ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 442 ? 4_555 130.1 ? 
8  O   ? A LYS 82  ? A LYS 77  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 442 ? 4_555 101.5 ? 
9  OE1 ? A GLU 85  ? A GLU 80  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 442 ? 4_555 99.3  ? 
10 OE2 ? A GLU 85  ? A GLU 80  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 442 ? 4_555 97.3  ? 
11 OE1 ? A GLN 13  ? A GLN 8   ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 613 ? 4_555 88.2  ? 
12 O   ? A LYS 82  ? A LYS 77  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 613 ? 4_555 87.9  ? 
13 OE1 ? A GLU 85  ? A GLU 80  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 613 ? 4_555 87.2  ? 
14 OE2 ? A GLU 85  ? A GLU 80  ? 1_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 613 ? 4_555 88.1  ? 
15 O   ? H HOH .   ? A HOH 442 ? 4_555 CA ? F CA . ? A CA 304 ? 1_555 O   ? H HOH .   ? A HOH 613 ? 4_555 74.4  ? 
16 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 52.2  ? 
17 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? A GLU 115 ? A GLU 110 ? 1_555 87.2  ? 
18 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? A GLU 115 ? A GLU 110 ? 1_555 88.9  ? 
19 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 87.6  ? 
20 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 123.3 ? 
21 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 45.8  ? 
22 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 528 ? 1_555 127.3 ? 
23 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 528 ? 1_555 75.8  ? 
24 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 528 ? 1_555 83.7  ? 
25 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 528 ? 1_555 119.3 ? 
26 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 540 ? 6_554 144.1 ? 
27 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 540 ? 6_554 158.9 ? 
28 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 540 ? 6_554 103.2 ? 
29 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 540 ? 6_554 76.5  ? 
30 O   ? H HOH .   ? A HOH 528 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 540 ? 6_554 88.2  ? 
31 OE1 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 594 ? 1_555 86.0  ? 
32 OE2 ? A GLU 40  ? A GLU 35  ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 594 ? 1_555 79.3  ? 
33 O   ? A GLU 115 ? A GLU 110 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 594 ? 1_555 168.2 ? 
34 OE2 ? A GLU 193 ? A GLU 188 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 594 ? 1_555 143.2 ? 
35 O   ? H HOH .   ? A HOH 528 ? 1_555 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 594 ? 1_555 92.9  ? 
36 O   ? H HOH .   ? A HOH 540 ? 6_554 CA ? G CA . ? A CA 305 ? 1_555 O   ? H HOH .   ? A HOH 594 ? 1_555 87.9  ? 
37 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? A GLU 166 ? A GLU 161 ? 1_555 68.6  ? 
38 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 488 ? 7_545 151.2 ? 
39 O   ? A GLU 166 ? A GLU 161 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 488 ? 7_545 110.8 ? 
40 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 539 ? 1_555 68.5  ? 
41 O   ? A GLU 166 ? A GLU 161 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 539 ? 1_555 115.6 ? 
42 O   ? H HOH .   ? A HOH 488 ? 7_545 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 539 ? 1_555 129.5 ? 
43 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 552 ? 7_545 95.3  ? 
44 O   ? A GLU 166 ? A GLU 161 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 552 ? 7_545 158.2 ? 
45 O   ? H HOH .   ? A HOH 488 ? 7_545 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 552 ? 7_545 76.0  ? 
46 O   ? H HOH .   ? A HOH 539 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 552 ? 7_545 68.5  ? 
47 OE1 ? A GLU 80  ? A GLU 75  ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 591 ? 4_556 125.6 ? 
48 O   ? A GLU 166 ? A GLU 161 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 591 ? 4_556 110.5 ? 
49 O   ? H HOH .   ? A HOH 488 ? 7_545 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 591 ? 4_556 82.4  ? 
50 O   ? H HOH .   ? A HOH 539 ? 1_555 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 591 ? 4_556 63.9  ? 
51 O   ? H HOH .   ? A HOH 552 ? 7_545 MG ? E MG . ? A MG 303 ? 1_555 O   ? H HOH .   ? A HOH 591 ? 4_556 90.8  ? 
52 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? H HOH .   ? A HOH 422 ? 1_555 86.1  ? 
53 OE2 ? A GLU 94  ? A GLU 89  ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? H HOH .   ? A HOH 612 ? 1_555 107.2 ? 
54 O   ? H HOH .   ? A HOH 422 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O   ? H HOH .   ? A HOH 612 ? 1_555 71.4  ? 
# 
_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                        259 
_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' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           110 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            105 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   HIS 
_struct_mon_prot_cis.pdbx_label_seq_id_2    111 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    HIS 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     106 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       9.75 
# 
_pdbx_entry_details.entry_id                   9EW7 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    490 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    601 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.13 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     110 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OH 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    TYR 
_pdbx_validate_symm_contact.auth_seq_id_2     213 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   8_555 
_pdbx_validate_symm_contact.dist              2.09 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            SD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            MET 
_pdbx_validate_rmsd_bond.auth_seq_id_1             123 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CE 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            MET 
_pdbx_validate_rmsd_bond.auth_seq_id_2             123 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.433 
_pdbx_validate_rmsd_bond.bond_target_value         1.774 
_pdbx_validate_rmsd_bond.bond_deviation            -0.341 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.056 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 18  ? ? -104.94 75.88 
2 1 HIS A 106 ? ? -144.73 36.74 
# 
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  ? ? 0.074 'SIDE CHAIN' 
2 1 ARG A 142 ? ? 0.086 '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      259 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   SER 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
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  
CA  CA   CA N N 74  
CL  CL   CL N N 75  
CYS N    N  N N 76  
CYS CA   C  N R 77  
CYS C    C  N N 78  
CYS O    O  N N 79  
CYS CB   C  N N 80  
CYS SG   S  N N 81  
CYS OXT  O  N N 82  
CYS H    H  N N 83  
CYS H2   H  N N 84  
CYS HA   H  N N 85  
CYS HB2  H  N N 86  
CYS HB3  H  N N 87  
CYS HG   H  N N 88  
CYS HXT  H  N N 89  
GLN N    N  N N 90  
GLN CA   C  N S 91  
GLN C    C  N N 92  
GLN O    O  N N 93  
GLN CB   C  N N 94  
GLN CG   C  N N 95  
GLN CD   C  N N 96  
GLN OE1  O  N N 97  
GLN NE2  N  N N 98  
GLN OXT  O  N N 99  
GLN H    H  N N 100 
GLN H2   H  N N 101 
GLN HA   H  N N 102 
GLN HB2  H  N N 103 
GLN HB3  H  N N 104 
GLN HG2  H  N N 105 
GLN HG3  H  N N 106 
GLN HE21 H  N N 107 
GLN HE22 H  N N 108 
GLN HXT  H  N N 109 
GLU N    N  N N 110 
GLU CA   C  N S 111 
GLU C    C  N N 112 
GLU O    O  N N 113 
GLU CB   C  N N 114 
GLU CG   C  N N 115 
GLU CD   C  N N 116 
GLU OE1  O  N N 117 
GLU OE2  O  N N 118 
GLU OXT  O  N N 119 
GLU H    H  N N 120 
GLU H2   H  N N 121 
GLU HA   H  N N 122 
GLU HB2  H  N N 123 
GLU HB3  H  N N 124 
GLU HG2  H  N N 125 
GLU HG3  H  N N 126 
GLU HE2  H  N N 127 
GLU HXT  H  N N 128 
GLY N    N  N N 129 
GLY CA   C  N N 130 
GLY C    C  N N 131 
GLY O    O  N N 132 
GLY OXT  O  N N 133 
GLY H    H  N N 134 
GLY H2   H  N N 135 
GLY HA2  H  N N 136 
GLY HA3  H  N N 137 
GLY HXT  H  N N 138 
HIS N    N  N N 139 
HIS CA   C  N S 140 
HIS C    C  N N 141 
HIS O    O  N N 142 
HIS CB   C  N N 143 
HIS CG   C  Y N 144 
HIS ND1  N  Y N 145 
HIS CD2  C  Y N 146 
HIS CE1  C  Y N 147 
HIS NE2  N  Y N 148 
HIS OXT  O  N N 149 
HIS H    H  N N 150 
HIS H2   H  N N 151 
HIS HA   H  N N 152 
HIS HB2  H  N N 153 
HIS HB3  H  N N 154 
HIS HD1  H  N N 155 
HIS HD2  H  N N 156 
HIS HE1  H  N N 157 
HIS HE2  H  N N 158 
HIS HXT  H  N N 159 
HOH O    O  N N 160 
HOH H1   H  N N 161 
HOH H2   H  N N 162 
ILE N    N  N N 163 
ILE CA   C  N S 164 
ILE C    C  N N 165 
ILE O    O  N N 166 
ILE CB   C  N S 167 
ILE CG1  C  N N 168 
ILE CG2  C  N N 169 
ILE CD1  C  N N 170 
ILE OXT  O  N N 171 
ILE H    H  N N 172 
ILE H2   H  N N 173 
ILE HA   H  N N 174 
ILE HB   H  N N 175 
ILE HG12 H  N N 176 
ILE HG13 H  N N 177 
ILE HG21 H  N N 178 
ILE HG22 H  N N 179 
ILE HG23 H  N N 180 
ILE HD11 H  N N 181 
ILE HD12 H  N N 182 
ILE HD13 H  N N 183 
ILE HXT  H  N N 184 
LEU N    N  N N 185 
LEU CA   C  N S 186 
LEU C    C  N N 187 
LEU O    O  N N 188 
LEU CB   C  N N 189 
LEU CG   C  N N 190 
LEU CD1  C  N N 191 
LEU CD2  C  N N 192 
LEU OXT  O  N N 193 
LEU H    H  N N 194 
LEU H2   H  N N 195 
LEU HA   H  N N 196 
LEU HB2  H  N N 197 
LEU HB3  H  N N 198 
LEU HG   H  N N 199 
LEU HD11 H  N N 200 
LEU HD12 H  N N 201 
LEU HD13 H  N N 202 
LEU HD21 H  N N 203 
LEU HD22 H  N N 204 
LEU HD23 H  N N 205 
LEU HXT  H  N N 206 
LYS N    N  N N 207 
LYS CA   C  N S 208 
LYS C    C  N N 209 
LYS O    O  N N 210 
LYS CB   C  N N 211 
LYS CG   C  N N 212 
LYS CD   C  N N 213 
LYS CE   C  N N 214 
LYS NZ   N  N N 215 
LYS OXT  O  N N 216 
LYS H    H  N N 217 
LYS H2   H  N N 218 
LYS HA   H  N N 219 
LYS HB2  H  N N 220 
LYS HB3  H  N N 221 
LYS HG2  H  N N 222 
LYS HG3  H  N N 223 
LYS HD2  H  N N 224 
LYS HD3  H  N N 225 
LYS HE2  H  N N 226 
LYS HE3  H  N N 227 
LYS HZ1  H  N N 228 
LYS HZ2  H  N N 229 
LYS HZ3  H  N N 230 
LYS HXT  H  N N 231 
MET N    N  N N 232 
MET CA   C  N S 233 
MET C    C  N N 234 
MET O    O  N N 235 
MET CB   C  N N 236 
MET CG   C  N N 237 
MET SD   S  N N 238 
MET CE   C  N N 239 
MET OXT  O  N N 240 
MET H    H  N N 241 
MET H2   H  N N 242 
MET HA   H  N N 243 
MET HB2  H  N N 244 
MET HB3  H  N N 245 
MET HG2  H  N N 246 
MET HG3  H  N N 247 
MET HE1  H  N N 248 
MET HE2  H  N N 249 
MET HE3  H  N N 250 
MET HXT  H  N N 251 
MG  MG   MG N N 252 
PHE N    N  N N 253 
PHE CA   C  N S 254 
PHE C    C  N N 255 
PHE O    O  N N 256 
PHE CB   C  N N 257 
PHE CG   C  Y N 258 
PHE CD1  C  Y N 259 
PHE CD2  C  Y N 260 
PHE CE1  C  Y N 261 
PHE CE2  C  Y N 262 
PHE CZ   C  Y N 263 
PHE OXT  O  N N 264 
PHE H    H  N N 265 
PHE H2   H  N N 266 
PHE HA   H  N N 267 
PHE HB2  H  N N 268 
PHE HB3  H  N N 269 
PHE HD1  H  N N 270 
PHE HD2  H  N N 271 
PHE HE1  H  N N 272 
PHE HE2  H  N N 273 
PHE HZ   H  N N 274 
PHE HXT  H  N N 275 
PRO N    N  N N 276 
PRO CA   C  N S 277 
PRO C    C  N N 278 
PRO O    O  N N 279 
PRO CB   C  N N 280 
PRO CG   C  N N 281 
PRO CD   C  N N 282 
PRO OXT  O  N N 283 
PRO H    H  N N 284 
PRO HA   H  N N 285 
PRO HB2  H  N N 286 
PRO HB3  H  N N 287 
PRO HG2  H  N N 288 
PRO HG3  H  N N 289 
PRO HD2  H  N N 290 
PRO HD3  H  N N 291 
PRO HXT  H  N N 292 
SEP N    N  N N 293 
SEP CA   C  N S 294 
SEP CB   C  N N 295 
SEP OG   O  N N 296 
SEP C    C  N N 297 
SEP O    O  N N 298 
SEP OXT  O  N N 299 
SEP P    P  N N 300 
SEP O1P  O  N N 301 
SEP O2P  O  N N 302 
SEP O3P  O  N N 303 
SEP H    H  N N 304 
SEP H2   H  N N 305 
SEP HA   H  N N 306 
SEP HB2  H  N N 307 
SEP HB3  H  N N 308 
SEP HXT  H  N N 309 
SEP HOP2 H  N N 310 
SEP HOP3 H  N N 311 
SER N    N  N N 312 
SER CA   C  N S 313 
SER C    C  N N 314 
SER O    O  N N 315 
SER CB   C  N N 316 
SER OG   O  N N 317 
SER OXT  O  N N 318 
SER H    H  N N 319 
SER H2   H  N N 320 
SER HA   H  N N 321 
SER HB2  H  N N 322 
SER HB3  H  N N 323 
SER HG   H  N N 324 
SER HXT  H  N N 325 
THR N    N  N N 326 
THR CA   C  N S 327 
THR C    C  N N 328 
THR O    O  N N 329 
THR CB   C  N R 330 
THR OG1  O  N N 331 
THR CG2  C  N N 332 
THR OXT  O  N N 333 
THR H    H  N N 334 
THR H2   H  N N 335 
THR HA   H  N N 336 
THR HB   H  N N 337 
THR HG1  H  N N 338 
THR HG21 H  N N 339 
THR HG22 H  N N 340 
THR HG23 H  N N 341 
THR HXT  H  N N 342 
TRP N    N  N N 343 
TRP CA   C  N S 344 
TRP C    C  N N 345 
TRP O    O  N N 346 
TRP CB   C  N N 347 
TRP CG   C  Y N 348 
TRP CD1  C  Y N 349 
TRP CD2  C  Y N 350 
TRP NE1  N  Y N 351 
TRP CE2  C  Y N 352 
TRP CE3  C  Y N 353 
TRP CZ2  C  Y N 354 
TRP CZ3  C  Y N 355 
TRP CH2  C  Y N 356 
TRP OXT  O  N N 357 
TRP H    H  N N 358 
TRP H2   H  N N 359 
TRP HA   H  N N 360 
TRP HB2  H  N N 361 
TRP HB3  H  N N 362 
TRP HD1  H  N N 363 
TRP HE1  H  N N 364 
TRP HE3  H  N N 365 
TRP HZ2  H  N N 366 
TRP HZ3  H  N N 367 
TRP HH2  H  N N 368 
TRP HXT  H  N N 369 
TYR N    N  N N 370 
TYR CA   C  N S 371 
TYR C    C  N N 372 
TYR O    O  N N 373 
TYR CB   C  N N 374 
TYR CG   C  Y N 375 
TYR CD1  C  Y N 376 
TYR CD2  C  Y N 377 
TYR CE1  C  Y N 378 
TYR CE2  C  Y N 379 
TYR CZ   C  Y N 380 
TYR OH   O  N N 381 
TYR OXT  O  N N 382 
TYR H    H  N N 383 
TYR H2   H  N N 384 
TYR HA   H  N N 385 
TYR HB2  H  N N 386 
TYR HB3  H  N N 387 
TYR HD1  H  N N 388 
TYR HD2  H  N N 389 
TYR HE1  H  N N 390 
TYR HE2  H  N N 391 
TYR HH   H  N N 392 
TYR HXT  H  N N 393 
VAL N    N  N N 394 
VAL CA   C  N S 395 
VAL C    C  N N 396 
VAL O    O  N N 397 
VAL CB   C  N N 398 
VAL CG1  C  N N 399 
VAL CG2  C  N N 400 
VAL OXT  O  N N 401 
VAL H    H  N N 402 
VAL H2   H  N N 403 
VAL HA   H  N N 404 
VAL HB   H  N N 405 
VAL HG11 H  N N 406 
VAL HG12 H  N N 407 
VAL HG13 H  N N 408 
VAL HG21 H  N N 409 
VAL HG22 H  N N 410 
VAL HG23 H  N N 411 
VAL HXT  H  N N 412 
# 
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                    9EW7 
_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]   0.012140 
_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]   0.008913 
_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]   0.015947 
_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  
CA 
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   . GLY A 1 1   ? 45.492 12.479  -4.136  1.00 34.92 ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 44.212 11.802  -4.112  1.00 27.91 ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 43.979 11.103  -5.440  1.00 26.71 ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 44.510 11.536  -6.473  1.00 18.61 ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 43.176 10.032  -5.387  1.00 20.88 ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 42.954 9.182   -6.540  1.00 20.83 ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 42.217 9.907   -7.665  1.00 14.92 ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 42.306 9.501   -8.826  1.00 18.09 ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 42.199 7.925   -6.135  1.00 25.06 ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 41.501 10.985  -7.331  1.00 14.78 ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? 40.762 11.746  -8.335  1.00 10.98 ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 41.545 12.930  -8.897  1.00 9.01  ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? 41.023 13.690  -9.708  1.00 7.38  ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? 39.450 12.288  -7.723  1.00 11.39 ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.550 11.228  -7.254  1.00 11.90 ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 38.147 10.016  -8.494  1.00 12.68 ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 37.310 8.825   -7.419  1.00 19.71 ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 42.801 13.076  -8.463  1.00 9.26  ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 43.636 14.186  -8.887  1.00 7.86  ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 43.896 14.277  -10.392 1.00 7.34  ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 44.098 15.371  -10.916 1.00 8.04  ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 43.859 13.140  -11.087 1.00 6.57  ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 44.046 13.145  -12.532 1.00 6.40  ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 42.785 13.374  -13.363 1.00 6.37  ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 42.871 13.492  -14.587 1.00 6.84  ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.709 11.837  -12.989 1.00 8.59  ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 43.830 10.748  -12.733 1.00 9.89  ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 41.597 13.395  -12.728 1.00 5.67  ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? 40.366 13.567  -13.475 1.00 6.03  ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? 39.946 15.034  -13.528 1.00 5.90  ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? 39.994 15.728  -12.516 1.00 6.19  ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? 39.249 12.730  -12.874 1.00 6.83  ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 38.201 12.365  -13.910 1.00 7.78  ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 36.791 11.468  -13.265 1.00 9.52  ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 37.642 10.136  -12.403 1.00 10.47 ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 39.485 15.487  -14.699 1.00 5.16  ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 38.905 16.821  -14.832 1.00 6.53  ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 37.775 17.092  -13.831 1.00 5.76  ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? 36.918 16.259  -13.609 1.00 5.03  ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 38.289 17.013  -16.207 1.00 6.51  ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 39.286 17.015  -17.343 1.00 7.20  ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 39.935 18.345  -17.545 1.00 8.88  ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 39.775 19.168  -16.620 1.00 8.95  ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 40.499 18.601  -18.637 1.00 10.39 ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 37.702 18.325  -13.320 1.00 6.18  ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 36.596 18.731  -12.470 1.00 5.78  ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 35.240 18.437  -13.109 1.00 6.05  ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? 34.356 17.900  -12.449 1.00 6.64  ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 36.674 20.232  -12.180 1.00 6.43  ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 35.725 20.725  -11.118 1.00 6.81  ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 35.926 22.219  -10.882 1.00 8.11  ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 35.138 22.704  -9.760  1.00 7.50  ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 33.827 22.928  -9.763  1.00 8.23  ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 33.074 22.682  -10.825 1.00 7.46  ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 33.254 23.395  -8.658  1.00 8.69  ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 35.062 18.779  -14.393 1.00 5.73  ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 33.756 18.584  -15.005 1.00 5.82  ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 33.409 17.090  -15.078 1.00 5.54  ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? 32.246 16.705  -14.934 1.00 5.24  ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 33.669 19.203  -16.368 1.00 6.85  ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? 34.419 16.264  -15.372 1.00 4.65  ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? 34.231 14.817  -15.415 1.00 4.99  ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? 33.813 14.222  -14.068 1.00 4.55  ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? 32.946 13.335  -14.002 1.00 4.79  ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? 35.510 14.164  -15.915 1.00 5.22  ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 35.765 14.627  -17.237 1.00 5.69  ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 34.437 14.713  -12.992 1.00 4.63  ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 34.079 14.330  -11.631 1.00 4.64  ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 32.619 14.670  -11.325 1.00 4.95  ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? 31.882 13.850  -10.803 1.00 4.57  ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 35.031 15.022  -10.668 1.00 4.79  ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 36.452 14.433  -10.638 1.00 5.89  ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 37.395 15.375  -9.998  1.00 6.89  ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 36.479 13.088  -9.917  1.00 5.50  ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 32.171 15.862  -11.728 1.00 5.29  ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 30.789 16.250  -11.510 1.00 6.15  ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 29.849 15.370  -12.336 1.00 5.91  ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? 28.848 14.858  -11.826 1.00 4.69  ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 30.586 17.747  -11.784 1.00 6.61  ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 31.418 18.673  -10.829 1.00 8.63  ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 29.075 18.051  -11.758 1.00 5.88  ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 31.231 18.435  -9.446  1.00 8.78  ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 30.198 15.160  -13.616 1.00 6.12  ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 29.404 14.278  -14.454 1.00 6.96  ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 29.265 12.878  -13.843 1.00 6.09  ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? 28.165 12.324  -13.792 1.00 6.67  ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 30.028 14.249  -15.851 1.00 8.42  ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 29.283 13.401  -16.829 1.00 12.38 ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 29.886 13.456  -18.224 1.00 14.51 ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 30.849 14.212  -18.475 1.00 17.69 ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 29.343 12.638  -19.129 1.00 14.18 ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 30.379 12.311  -13.364 1.00 4.99  ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 30.375 10.975  -12.789 1.00 4.81  ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 29.648 10.945  -11.445 1.00 4.94  ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? 28.995 9.957   -11.135 1.00 4.94  ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 31.789 10.417  -12.682 1.00 5.14  ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 32.378 10.101  -14.051 1.00 5.26  ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 33.761 9.542   -13.961 1.00 5.67  ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 34.412 9.453   -15.313 1.00 5.45  ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 35.787 8.889   -15.236 1.00 6.50  ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 29.701 12.036  -10.674 1.00 4.54  ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 28.926 12.097  -9.446  1.00 5.02  ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 27.434 11.946  -9.770  1.00 4.90  ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? 26.698 11.256  -9.065  1.00 4.58  ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 29.202 13.414  -8.718  1.00 5.47  ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 26.976 12.608  -10.843 1.00 5.12  ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 25.570 12.539  -11.216 1.00 5.93  ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 25.178 11.137  -11.685 1.00 6.02  ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? 24.084 10.642  -11.378 1.00 6.70  ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 25.248 13.572  -12.276 1.00 6.58  ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 25.252 15.002  -11.744 1.00 8.42  ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 25.240 16.010  -12.884 1.00 10.12 ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 25.474 17.416  -12.433 1.00 14.06 ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 25.464 18.398  -13.558 1.00 15.52 ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 26.081 10.492  -12.416 1.00 5.91  ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 25.893 9.100   -12.829 1.00 6.85  ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 25.804 8.143   -11.638 1.00 6.69  ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 24.951 7.270   -11.594 1.00 5.53  ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 27.065 8.674   -13.730 1.00 7.26  ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 27.120 9.313   -15.147 1.00 8.40  ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 28.304 8.870   -15.920 1.00 8.94  ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 25.870 9.008   -15.968 1.00 9.81  ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 26.733 8.282   -10.689 1.00 7.04  ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 26.748 7.493   -9.476  1.00 7.17  ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 25.466 7.653   -8.672  1.00 6.98  ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? 24.923 6.661   -8.165  1.00 8.01  ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 27.960 7.897   -8.643  1.00 7.69  ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 24.963 8.890   -8.572  1.00 7.19  ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 23.659 9.119   -7.961  1.00 7.88  ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 22.551 8.311   -8.654  1.00 9.06  ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? 21.728 7.659   -7.988  1.00 9.88  ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 23.304 10.605  -7.955  1.00 9.66  ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 22.019 10.915  -7.200  1.00 11.88 ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 21.644 12.390  -7.149  1.00 15.44 ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 21.970 13.131  -8.102  1.00 19.83 ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 20.964 12.786  -6.182  1.00 25.37 ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 22.535 8.322   -9.988  1.00 8.85  ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 21.521 7.569   -10.724 1.00 9.90  ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 21.629 6.060   -10.495 1.00 9.59  ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? 20.625 5.338   -10.442 1.00 10.94 ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 21.590 7.876   -12.229 1.00 11.08 ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 21.188 9.285   -12.613 1.00 15.26 ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 21.369 9.492   -14.102 1.00 23.39 ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 20.497 9.166   -14.907 1.00 22.78 ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 22.515 10.019  -14.493 1.00 28.60 ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 22.858 5.583   -10.314 1.00 7.11  ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 23.151 4.189   -10.069 1.00 7.42  ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 23.063 3.796   -8.593  1.00 8.26  ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? 23.340 2.654   -8.243  1.00 8.40  ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 24.512 3.884   -10.608 1.00 8.34  ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 22.701 4.755   -7.745  1.00 9.27  ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 22.720 4.576   -6.294  1.00 11.40 ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 24.055 4.038   -5.777  1.00 10.90 ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? 24.098 3.206   -4.876  1.00 10.60 ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 21.519 3.699   -5.848  1.00 13.37 ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 20.189 4.351   -6.209  1.00 17.80 ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 18.942 3.521   -5.952  1.00 27.29 ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 19.001 2.571   -5.150  1.00 25.23 ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 17.914 3.803   -6.599  1.00 35.27 ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 25.147 4.577   -6.321  1.00 8.69  ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 26.508 4.289   -5.893  1.00 7.12  ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 27.048 5.466   -5.094  1.00 7.02  ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? 27.864 6.259   -5.580  1.00 5.34  ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 27.376 3.998   -7.115  1.00 8.59  ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 26.969 2.707   -7.820  1.00 8.62  ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 27.693 1.554   -7.238  1.00 9.84  ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 29.107 1.665   -7.562  1.00 10.43 ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 29.959 0.663   -7.488  1.00 10.65 ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 29.551 -0.561  -7.215  1.00 10.78 ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 31.247 0.887   -7.700  1.00 10.79 ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 26.586 5.576   -3.840  1.00 6.55  ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 26.832 6.806   -3.106  1.00 6.97  ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 28.265 6.946   -2.613  1.00 6.78  ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? 28.745 8.061   -2.498  1.00 6.57  ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 25.857 6.950   -1.965  1.00 8.09  ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 24.460 7.044   -2.504  1.00 11.12 ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 24.043 8.163   -3.231  1.00 12.25 ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 23.558 6.002   -2.336  1.00 14.11 ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 22.745 8.241   -3.753  1.00 15.46 ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 22.273 6.072   -2.858  1.00 16.87 ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 21.870 7.191   -3.552  1.00 14.12 ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 20.596 7.225   -4.038  1.00 23.62 ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 28.937 5.836   -2.298  1.00 6.49  ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 30.349 5.907   -1.973  1.00 7.63  ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 31.185 6.477   -3.129  1.00 6.16  ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? 32.023 7.370   -2.947  1.00 5.13  ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 30.807 4.532   -1.556  1.00 11.70 ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 32.198 4.506   -1.030  1.00 19.03 ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 32.584 3.108   -0.569  1.00 30.31 ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 31.874 2.592   0.326   1.00 36.68 ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 33.537 2.518   -1.137  1.00 36.95 ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 30.941 5.985   -4.341  1.00 5.21  ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 31.569 6.566   -5.518  1.00 5.42  ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 31.206 8.045   -5.696  1.00 5.42  ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? 32.066 8.885   -6.027  1.00 5.06  ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 31.170 5.836   -6.790  1.00 6.21  ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 31.680 4.413   -6.960  1.00 7.13  ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 32.606 4.032   -6.232  1.00 8.05  ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 31.097 3.674   -7.801  1.00 8.30  ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 29.919 8.363   -5.511  1.00 5.53  ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? 29.448 9.735   -5.674  1.00 4.97  ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? 30.233 10.645  -4.728  1.00 4.88  ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? 30.672 11.725  -5.137  1.00 4.50  ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? 27.923 9.825   -5.392  1.00 4.62  ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 27.313 11.141  -5.736  1.00 4.94  ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 25.616 11.208  -5.148  1.00 5.93  ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 25.122 12.836  -5.704  1.00 4.95  ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 30.419 10.191  -3.476  1.00 4.89  ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 31.142 10.970  -2.489  1.00 5.16  ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 32.610 11.171  -2.846  1.00 4.89  ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? 33.112 12.288  -2.738  1.00 4.16  ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 31.027 10.364  -1.082  1.00 5.55  ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 33.273 10.094  -3.290  1.00 5.17  ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 34.641 10.185  -3.754  1.00 4.88  ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 34.800 11.153  -4.928  1.00 4.85  ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? 35.770 11.917  -4.977  1.00 4.83  ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 35.180 8.792   -4.101  1.00 4.96  ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 33.866 11.119  -5.888  1.00 4.66  ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 33.923 12.026  -7.022  1.00 5.27  ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 33.745 13.472  -6.545  1.00 4.67  ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? 34.451 14.372  -6.987  1.00 3.64  ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 32.859 11.671  -8.068  1.00 4.88  ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 33.049 10.362  -8.791  1.00 4.93  ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 34.297 9.979   -9.247  1.00 6.32  ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 31.971 9.562   -9.094  1.00 5.52  ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 34.475 8.801   -9.959  1.00 5.94  ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 32.148 8.358   -9.789  1.00 5.86  ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 33.409 7.999   -10.232 1.00 6.76  ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 32.795 13.711  -5.631  1.00 4.06  ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? 32.590 15.076  -5.153  1.00 4.65  ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 33.743 15.581  -4.282  1.00 4.94  ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 34.125 16.761  -4.333  1.00 4.71  ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? 31.257 15.203  -4.417  1.00 4.66  ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 30.037 15.162  -5.352  1.00 5.35  ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 30.157 16.232  -6.795  1.00 6.50  ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 30.270 17.803  -6.029  1.00 5.34  ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.325 14.687  -3.484  1.00 5.26  ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 35.553 15.015  -2.778  1.00 5.65  ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 36.630 15.482  -3.769  1.00 5.13  ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 37.298 16.508  -3.557  1.00 4.55  ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 36.031 13.821  -1.932  1.00 5.98  ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 37.304 14.112  -1.101  1.00 7.08  ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 37.608 12.991  -0.172  1.00 8.83  ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 38.788 13.204  0.750   1.00 12.28 ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 40.066 13.159  0.007   1.00 13.89 ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 36.804 14.704  -4.848  1.00 5.14  ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 37.786 15.044  -5.870  1.00 4.53  ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.503 16.426  -6.461  1.00 4.32  ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? 38.404 17.240  -6.651  1.00 3.80  ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? 36.222 16.703  -6.731  1.00 4.33  ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 35.813 18.004  -7.238  1.00 5.40  ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 36.130 19.161  -6.297  1.00 4.92  ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? 36.686 20.174  -6.717  1.00 5.50  ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 34.316 18.002  -7.590  1.00 5.42  ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 35.812 18.986  -5.015  1.00 5.38  ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 36.141 19.990  -4.021  1.00 5.33  ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 37.635 20.277  -4.010  1.00 5.50  ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? 38.063 21.434  -3.954  1.00 4.93  ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 35.675 19.562  -2.631  1.00 5.61  ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 36.234 20.513  -1.560  1.00 6.02  ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 34.166 19.504  -2.565  1.00 6.20  ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 38.421 19.202  -4.067  1.00 5.22  ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 39.871 19.308  -3.973  1.00 6.28  ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 40.514 19.975  -5.191  1.00 5.65  ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 41.673 20.376  -5.146  1.00 6.43  ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 40.434 17.916  -3.677  1.00 6.69  ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 40.154 17.484  -2.248  1.00 8.12  ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 40.590 16.081  -1.837  1.00 10.21 ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 41.006 15.307  -2.710  1.00 12.64 ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 40.467 15.751  -0.635  1.00 13.07 ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 39.738 20.221  -6.251  1.00 5.89  ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 40.225 21.087  -7.318  1.00 5.63  ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 40.467 22.537  -6.886  1.00 6.31  ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 41.215 23.244  -7.555  1.00 4.96  ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.307 21.064  -8.505  1.00 6.23  ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 39.119 19.659  -9.122  1.00 6.14  ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.396 19.053  -9.664  1.00 6.02  ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 40.132 17.676  -10.223 1.00 7.29  ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.388 16.893  -10.510 1.00 7.69  ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 39.850 22.961  -5.767  1.00 6.91  ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 40.104 24.265  -5.167  1.00 6.95  ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 39.161 25.388  -5.595  1.00 8.16  ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? 39.251 26.494  -5.066  1.00 8.44  ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? 38.268 25.130  -6.557  1.00 7.47  ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 37.317 26.133  -6.993  1.00 8.98  ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 36.093 26.048  -6.080  1.00 7.92  ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? 35.776 24.992  -5.539  1.00 7.18  ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 36.925 25.962  -8.441  1.00 11.00 ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 38.066 26.061  -9.437  1.00 17.15 ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 38.656 27.449  -9.671  1.00 24.90 ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 38.104 28.458  -9.166  1.00 22.08 ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 39.685 27.522  -10.379 1.00 37.96 ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 35.400 27.177  -5.917  1.00 7.10  ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 34.153 27.160  -5.184  1.00 7.93  ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 33.146 26.251  -5.905  1.00 7.76  ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 33.289 25.914  -7.085  1.00 8.01  ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 33.624 28.620  -4.971  1.00 8.75  ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 34.601 29.446  -4.079  1.00 10.79 ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 34.260 30.913  -3.814  1.00 12.51 ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 33.060 31.185  -3.640  1.00 18.35 ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 35.172 31.769  -3.678  1.00 11.41 ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 32.115 25.854  -5.171  1.00 6.49  ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 31.068 25.015  -5.715  1.00 6.55  ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 29.821 25.837  -6.000  1.00 6.77  ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? 29.389 26.650  -5.181  1.00 6.10  ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 30.667 23.896  -4.747  1.00 8.20  ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 31.735 22.939  -4.268  1.00 11.51 ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 31.110 21.794  -3.460  1.00 10.31 ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 32.537 22.408  -5.348  1.00 11.87 ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 29.217 25.555  -7.150  1.00 6.58  ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? 27.889 26.058  -7.445  1.00 5.88  ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? 26.808 25.510  -6.482  1.00 5.39  ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? 26.995 24.509  -5.823  1.00 5.03  ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? 27.513 25.698  -8.858  1.00 5.77  ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 27.231 24.320  -9.008  1.00 5.75  ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 25.573 26.080  -6.668  1.00 5.62  ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 24.493 25.529  -5.822  1.00 6.50  ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 24.264 24.048  -6.147  1.00 5.90  ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? 24.077 23.254  -5.182  1.00 6.16  ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 23.238 26.355  -6.028  1.00 8.85  ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 21.857 25.811  -4.994  1.00 13.30 ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 24.154 23.703  -7.372  1.00 5.92  ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 23.939 22.294  -7.702  1.00 7.03  ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 25.050 21.378  -7.198  1.00 6.33  ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? 24.787 20.275  -6.709  1.00 6.13  ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 23.826 22.138  -9.240  1.00 10.50 ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 23.531 20.722  -9.708  1.00 15.13 ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 23.299 20.591  -11.210 1.00 21.36 ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 23.470 21.595  -11.935 1.00 21.06 ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 22.902 19.493  -11.654 1.00 23.50 ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 26.296 21.829  -7.333  1.00 5.62  ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 27.452 21.058  -6.872  1.00 5.86  ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 27.478 20.860  -5.348  1.00 6.09  ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? 27.835 19.778  -4.870  1.00 5.22  ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 28.736 21.743  -7.326  1.00 5.71  ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 28.898 21.719  -8.854  1.00 6.19  ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 29.905 22.695  -9.436  1.00 5.82  ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 30.460 23.484  -8.653  1.00 5.99  ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 30.146 22.677  -10.671 1.00 7.67  ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 27.084 21.897  -4.600  1.00 5.46  ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 26.976 21.832  -3.151  1.00 6.16  ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 25.958 20.755  -2.803  1.00 5.38  ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? 26.142 19.962  -1.876  1.00 5.29  ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 26.540 23.182  -2.548  1.00 7.15  ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 27.594 24.194  -2.535  1.00 7.61  ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 27.213 25.410  -1.709  1.00 7.97  ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 26.011 26.080  -2.188  1.00 9.35  ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 25.998 27.146  -2.977  1.00 9.28  ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 27.062 27.511  -3.676  1.00 9.36  ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 24.869 27.836  -3.106  1.00 10.31 ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 24.850 20.747  -3.544  1.00 5.87  ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 23.825 19.755  -3.274  1.00 6.10  ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 24.297 18.333  -3.593  1.00 5.87  ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? 23.957 17.414  -2.875  1.00 5.19  ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 22.536 20.165  -3.944  1.00 8.18  ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 21.803 21.215  -3.078  1.00 12.42 ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 20.989 20.866  -2.193  1.00 19.96 ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 22.122 22.509  -3.166  1.00 15.91 ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 25.080 18.137  -4.662  1.00 5.64  ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 25.632 16.819  -4.945  1.00 5.94  ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 26.534 16.319  -3.808  1.00 5.26  ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? 26.484 15.149  -3.419  1.00 4.97  ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 26.417 16.850  -6.253  1.00 5.94  ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 25.606 17.055  -7.495  1.00 7.02  ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 26.491 17.304  -8.657  1.00 7.04  ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 24.694 15.894  -7.770  1.00 7.27  ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 27.370 17.217  -3.293  1.00 4.40  ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 28.266 16.909  -2.197  1.00 4.62  ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 27.484 16.451  -0.977  1.00 4.69  ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? 27.798 15.417  -0.376  1.00 4.33  ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 29.079 18.124  -1.862  1.00 4.63  ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 30.085 17.961  -0.672  1.00 4.17  ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 31.263 17.055  -1.033  1.00 4.18  ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 30.569 19.326  -0.208  1.00 4.09  ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 26.443 17.238  -0.658  1.00 4.68  ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? 25.567 16.944  0.453   1.00 5.77  ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? 24.849 15.603  0.301   1.00 5.33  ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? 24.895 14.786  1.209   1.00 6.34  ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? 24.574 18.074  0.666   1.00 6.46  ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 23.740 17.758  1.763   1.00 7.81  ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 24.211 15.361  -0.838  1.00 5.18  ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 23.509 14.098  -1.056  1.00 6.39  ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 24.436 12.887  -0.895  1.00 6.02  ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? 24.086 11.886  -0.246  1.00 5.21  ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 22.870 14.121  -2.461  1.00 6.70  ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 22.373 12.715  -2.869  1.00 8.02  ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 21.745 15.166  -2.545  1.00 8.76  ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 25.632 12.985  -1.486  1.00 5.11  ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 26.550 11.856  -1.506  1.00 5.49  ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 26.924 11.463  -0.076  1.00 4.90  ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 26.763 10.302  0.344   1.00 5.33  ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 27.783 12.184  -2.354  1.00 5.88  ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 27.445 12.422  0.688   1.00 4.24  ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 27.907 12.103  2.024   1.00 4.37  ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 26.746 11.787  2.971   1.00 5.04  ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? 26.877 10.945  3.846   1.00 5.67  ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.844 13.223  2.552   1.00 4.43  ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 30.244 13.078  2.039   1.00 4.67  ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 31.082 12.086  2.526   1.00 4.71  ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 30.748 13.937  1.081   1.00 4.77  ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 32.360 11.922  2.043   1.00 5.17  ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 32.055 13.817  0.632   1.00 5.58  ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 32.857 12.783  1.090   1.00 5.15  ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 34.161 12.607  0.641   1.00 5.26  ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 25.570 12.399  2.755   1.00 5.76  ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 24.430 12.121  3.618   1.00 6.80  ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 24.060 10.650  3.478   1.00 6.11  ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? 23.729 9.989   4.455   1.00 5.00  ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 23.215 13.000  3.282   1.00 10.73 ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 21.995 12.724  4.122   1.00 19.58 ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 21.009 13.962  4.240   1.00 31.24 ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 19.778 13.634  5.065   1.00 36.48 ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 20.090 12.838  6.316   1.00 32.42 ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 24.056 10.158  2.237   1.00 6.09  ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 23.732 8.771   1.990   1.00 6.78  ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 24.775 7.826   2.573   1.00 6.12  ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? 24.424 6.798   3.158   1.00 5.67  ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 23.582 8.557   0.491   1.00 9.12  ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 22.236 8.956   -0.011  1.00 16.47 ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 22.048 9.835   -0.849  1.00 16.54 ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 21.264 8.215   0.393   1.00 28.34 ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 26.062 8.163   2.432   1.00 5.28  ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 27.106 7.321   3.001   1.00 5.26  ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.967 7.246   4.519   1.00 5.72  ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? 26.864 6.149   5.083   1.00 5.20  ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.499 7.789   2.572   1.00 5.15  ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 29.601 7.066   3.301   1.00 5.38  ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 28.678 7.611   1.066   1.00 5.52  ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 26.958 8.407   5.179   1.00 5.21  ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 26.901 8.446   6.633   1.00 5.75  ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 25.566 7.881   7.117   1.00 5.79  ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? 25.495 7.315   8.201   1.00 5.69  ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 27.217 9.856   7.174   1.00 6.35  ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 26.021 10.780  7.121   1.00 6.47  ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 27.784 9.825   8.594   1.00 8.79  ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.510 8.021   6.305   1.00 6.02  ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 23.198 7.528   6.670   1.00 7.43  ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 23.181 6.012   6.849   1.00 8.90  ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? 22.604 5.511   7.818   1.00 8.63  ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? 23.811 5.322   5.890   1.00 8.25  ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 24.077 3.899   5.971   1.00 8.23  ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 24.833 3.502   7.236   1.00 7.52  ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 24.454 2.528   7.907   1.00 6.94  ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? 25.902 4.248   7.530   1.00 6.49  ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 26.736 3.963   8.681   1.00 7.08  ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 25.947 4.188   9.973   1.00 6.86  ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? 26.083 3.414   10.927  1.00 5.67  ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 27.981 4.818   8.678   1.00 7.40  ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 28.827 4.565   7.424   1.00 8.79  ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 29.953 5.552   7.328   1.00 9.64  ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 29.766 6.771   7.515   1.00 9.00  ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 31.134 5.051   7.036   1.00 10.83 ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 25.165 5.278   10.028  1.00 6.30  ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 24.404 5.572   11.235  1.00 6.66  ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 23.391 4.461   11.513  1.00 7.11  ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? 23.223 4.045   12.649  1.00 7.12  ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 23.671 6.907   11.131  1.00 6.87  ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 24.626 8.095   11.109  1.00 7.38  ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 23.974 9.384   10.618  1.00 7.03  ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 22.987 9.886   11.569  1.00 7.21  ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 21.973 10.674  11.216  1.00 7.88  ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 21.684 10.887  9.947   1.00 7.35  ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 21.215 11.222  12.159  1.00 7.91  ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 22.683 4.037   10.476  1.00 7.22  ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 21.695 2.978   10.608  1.00 8.39  ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 22.340 1.684   11.096  1.00 7.58  ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 21.806 1.026   12.000  1.00 7.21  ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 20.983 2.736   9.288   1.00 8.73  ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 23.505 1.349   10.528  1.00 6.63  ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 24.235 0.162   10.959  1.00 6.65  ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 24.701 0.266   12.410  1.00 6.49  ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? 24.561 -0.678  13.187  1.00 7.75  ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 25.427 -0.089  10.045  1.00 6.47  ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 25.312 1.407   12.755  1.00 6.81  ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 25.777 1.659   14.105  1.00 6.76  ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 24.641 1.519   15.123  1.00 6.40  ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? 24.831 0.945   16.201  1.00 6.83  ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 26.392 3.067   14.212  1.00 6.18  ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 27.009 3.328   15.542  1.00 6.68  ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 28.304 3.136   15.887  1.00 7.19  ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 26.360 3.865   16.706  1.00 6.87  ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 28.513 3.516   17.193  1.00 7.25  ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 27.334 3.952   17.723  1.00 7.94  ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 25.066 4.285   16.973  1.00 7.30  ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 27.042 4.420   18.998  1.00 8.56  ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 24.768 4.742   18.243  1.00 8.85  ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 25.765 4.825   19.232  1.00 8.52  ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 23.445 1.996   14.765  1.00 7.75  ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 22.331 1.893   15.697  1.00 8.62  ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 21.930 0.450   15.967  1.00 9.48  ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? 21.632 0.093   17.111  1.00 7.96  ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 21.127 2.665   15.203  1.00 9.64  ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 21.384 4.166   15.255  1.00 12.62 ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 20.306 4.913   14.487  1.00 16.28 ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 20.625 6.330   14.503  1.00 19.69 ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 20.047 7.223   13.715  1.00 24.85 ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 19.198 6.855   12.775  1.00 25.25 ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 20.342 8.510   13.864  1.00 24.48 ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 21.893 -0.344  14.891  1.00 9.79  ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 21.607 -1.769  14.986  1.00 10.23 ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 22.585 -2.438  15.942  1.00 10.18 ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? 22.165 -3.147  16.863  1.00 11.15 ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 21.624 -2.456  13.614  1.00 10.68 ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 21.661 -3.982  13.755  1.00 10.50 ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 20.439 -2.017  12.756  1.00 10.46 ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 23.886 -2.217  15.706  1.00 7.85  ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 24.942 -2.856  16.472  1.00 8.68  ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 24.962 -2.359  17.915  1.00 10.13 ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? 25.158 -3.148  18.845  1.00 11.51 ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 26.314 -2.632  15.806  1.00 8.61  ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 26.398 -3.198  14.414  1.00 8.21  ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 27.702 -2.765  13.744  1.00 8.63  ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 26.287 -4.703  14.425  1.00 9.45  ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 24.731 -1.056  18.108  1.00 9.71  ? 63  SER A N   1 
ATOM   515  C  CA  . SER A 1 68  ? 24.712 -0.490  19.450  1.00 11.95 ? 63  SER A CA  1 
ATOM   516  C  C   . SER A 1 68  ? 23.569 -1.098  20.266  1.00 11.06 ? 63  SER A C   1 
ATOM   517  O  O   . SER A 1 68  ? 23.732 -1.433  21.442  1.00 11.52 ? 63  SER A O   1 
ATOM   518  C  CB  . SER A 1 68  ? 24.618 1.040   19.383  1.00 12.73 ? 63  SER A CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 24.653 1.539   20.713  1.00 15.70 ? 63  SER A OG  1 
ATOM   520  N  N   . SER A 1 69  ? 22.416 -1.290  19.624  1.00 11.26 ? 64  SER A N   1 
ATOM   521  C  CA  . SER A 1 69  ? 21.274 -1.899  20.287  1.00 14.35 ? 64  SER A CA  1 
ATOM   522  C  C   . SER A 1 69  ? 21.552 -3.338  20.715  1.00 13.71 ? 64  SER A C   1 
ATOM   523  O  O   . SER A 1 69  ? 21.264 -3.718  21.851  1.00 13.31 ? 64  SER A O   1 
ATOM   524  C  CB  . SER A 1 69  ? 20.062 -1.872  19.382  1.00 15.69 ? 64  SER A CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 18.991 -2.552  20.005  1.00 25.95 ? 64  SER A OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 22.163 -4.109  19.812  1.00 12.39 ? 65  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 22.573 -5.473  20.145  1.00 14.04 ? 65  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 23.547 -5.477  21.318  1.00 14.22 ? 65  ILE A C   1 
ATOM   529  O  O   . ILE A 1 70  ? 23.433 -6.291  22.248  1.00 17.91 ? 65  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 23.150 -6.185  18.900  1.00 12.04 ? 65  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 22.059 -6.343  17.864  1.00 11.65 ? 65  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 23.825 -7.543  19.276  1.00 12.62 ? 65  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 22.535 -6.733  16.473  1.00 12.59 ? 65  ILE A CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 24.479 -4.526  21.295  1.00 12.54 ? 66  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 25.515 -4.437  22.305  1.00 13.71 ? 66  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 24.880 -4.140  23.664  1.00 21.94 ? 66  GLU A C   1 
ATOM   537  O  O   . GLU A 1 71  ? 25.208 -4.777  24.666  1.00 20.20 ? 66  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 26.509 -3.356  21.931  1.00 13.89 ? 66  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 27.730 -3.292  22.805  1.00 13.81 ? 66  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 28.690 -2.196  22.429  1.00 14.50 ? 66  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 28.305 -1.337  21.603  1.00 15.61 ? 66  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 29.820 -2.175  22.973  1.00 14.32 ? 66  GLU A OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 23.933 -3.198  23.688  1.00 18.70 ? 67  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 23.308 -2.811  24.947  1.00 23.08 ? 67  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 22.571 -3.995  25.562  1.00 25.55 ? 67  GLN A C   1 
ATOM   546  O  O   . GLN A 1 72  ? 22.645 -4.219  26.774  1.00 27.88 ? 67  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 22.349 -1.632  24.764  1.00 25.19 ? 67  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 23.040 -0.289  24.429  1.00 31.43 ? 67  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 24.268 -0.015  25.281  1.00 43.39 ? 67  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 24.207 0.015   26.522  1.00 47.91 ? 67  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 25.420 0.173   24.628  1.00 46.60 ? 67  GLN A NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 21.884 -4.752  24.709  1.00 23.79 ? 68  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 21.169 -5.941  25.137  1.00 29.47 ? 68  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 22.088 -7.035  25.669  1.00 32.49 ? 68  LYS A C   1 
ATOM   555  O  O   . LYS A 1 73  ? 21.698 -7.754  26.586  1.00 35.51 ? 68  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 20.301 -6.459  24.003  1.00 28.07 ? 68  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 73  ? 19.092 -5.562  23.836  1.00 38.01 ? 68  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 73  ? 18.316 -5.779  22.564  1.00 47.74 ? 68  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 73  ? 17.223 -4.747  22.446  1.00 53.39 ? 68  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 73  ? 16.864 -4.490  21.028  1.00 53.03 ? 68  LYS A NZ  1 
ATOM   561  N  N   . SER A 1 74  ? 23.297 -7.151  25.114  1.00 24.83 ? 69  SER A N   1 
ATOM   562  C  CA  . SER A 1 74  ? 24.281 -8.083  25.647  1.00 29.48 ? 69  SER A CA  1 
ATOM   563  C  C   . SER A 1 74  ? 24.729 -7.711  27.060  1.00 33.39 ? 69  SER A C   1 
ATOM   564  O  O   . SER A 1 74  ? 25.106 -8.581  27.845  1.00 31.76 ? 69  SER A O   1 
ATOM   565  C  CB  . SER A 1 74  ? 25.517 -8.169  24.763  1.00 26.70 ? 69  SER A CB  1 
ATOM   566  O  OG  . SER A 1 74  ? 26.383 -7.065  25.016  1.00 28.12 ? 69  SER A OG  1 
ATOM   567  N  N   . ASN A 1 75  ? 24.692 -6.413  27.377  1.00 34.39 ? 70  ASN A N   1 
ATOM   568  C  CA  . ASN A 1 75  ? 25.113 -5.928  28.682  1.00 43.37 ? 70  ASN A CA  1 
ATOM   569  C  C   . ASN A 1 75  ? 24.007 -5.859  29.732  1.00 38.81 ? 70  ASN A C   1 
ATOM   570  O  O   . ASN A 1 75  ? 24.233 -5.334  30.815  1.00 49.31 ? 70  ASN A O   1 
ATOM   571  C  CB  . ASN A 1 75  ? 25.787 -4.566  28.512  1.00 44.84 ? 70  ASN A CB  1 
ATOM   572  C  CG  . ASN A 1 75  ? 27.061 -4.702  27.732  1.00 48.90 ? 70  ASN A CG  1 
ATOM   573  O  OD1 . ASN A 1 75  ? 27.611 -5.804  27.602  1.00 56.85 ? 70  ASN A OD1 1 
ATOM   574  N  ND2 . ASN A 1 75  ? 27.561 -3.609  27.183  1.00 52.76 ? 70  ASN A ND2 1 
ATOM   575  N  N   . GLU A 1 76  ? 22.824 -6.404  29.428  1.00 38.02 ? 71  GLU A N   1 
ATOM   576  C  CA  . GLU A 1 76  ? 21.776 -6.534  30.431  1.00 40.00 ? 71  GLU A CA  1 
ATOM   577  C  C   . GLU A 1 76  ? 22.022 -7.748  31.328  1.00 52.78 ? 71  GLU A C   1 
ATOM   578  O  O   . GLU A 1 76  ? 22.646 -8.720  30.903  1.00 53.93 ? 71  GLU A O   1 
ATOM   579  C  CB  . GLU A 1 76  ? 20.410 -6.682  29.765  1.00 42.49 ? 71  GLU A CB  1 
ATOM   580  C  CG  . GLU A 1 76  ? 19.895 -5.424  29.097  1.00 44.84 ? 71  GLU A CG  1 
ATOM   581  C  CD  . GLU A 1 76  ? 18.578 -5.635  28.372  1.00 55.19 ? 71  GLU A CD  1 
ATOM   582  O  OE1 . GLU A 1 76  ? 18.138 -6.803  28.265  1.00 63.59 ? 71  GLU A OE1 1 
ATOM   583  O  OE2 . GLU A 1 76  ? 17.980 -4.634  27.915  1.00 67.77 ? 71  GLU A OE2 1 
ATOM   584  N  N   . GLU A 1 77  ? 21.513 -7.691  32.566  1.00 66.88 ? 72  GLU A N   1 
ATOM   585  C  CA  . GLU A 1 77  ? 21.550 -8.831  33.471  1.00 65.07 ? 72  GLU A CA  1 
ATOM   586  C  C   . GLU A 1 77  ? 20.734 -9.983  32.882  1.00 58.43 ? 72  GLU A C   1 
ATOM   587  O  O   . GLU A 1 77  ? 19.628 -9.771  32.390  1.00 55.37 ? 72  GLU A O   1 
ATOM   588  C  CB  . GLU A 1 77  ? 20.998 -8.448  34.857  1.00 73.23 ? 72  GLU A CB  1 
ATOM   589  C  CG  . GLU A 1 77  ? 21.288 -9.474  35.946  1.00 80.13 ? 72  GLU A CG  1 
ATOM   590  C  CD  . GLU A 1 77  ? 20.447 -9.331  37.202  1.00 80.80 ? 72  GLU A CD  1 
ATOM   591  O  OE1 . GLU A 1 77  ? 20.294 -8.185  37.682  1.00 77.34 ? 72  GLU A OE1 1 
ATOM   592  O  OE2 . GLU A 1 77  ? 19.953 -10.363 37.715  1.00 70.69 ? 72  GLU A OE2 1 
ATOM   593  N  N   . GLY A 1 78  ? 21.295 -11.199 32.921  1.00 57.41 ? 73  GLY A N   1 
ATOM   594  C  CA  . GLY A 1 78  ? 20.628 -12.380 32.389  1.00 57.73 ? 73  GLY A CA  1 
ATOM   595  C  C   . GLY A 1 78  ? 21.032 -12.728 30.957  1.00 59.89 ? 73  GLY A C   1 
ATOM   596  O  O   . GLY A 1 78  ? 20.691 -13.803 30.459  1.00 61.02 ? 73  GLY A O   1 
ATOM   597  N  N   . SER A 1 79  ? 21.750 -11.800 30.307  1.00 54.72 ? 74  SER A N   1 
ATOM   598  C  CA  . SER A 1 79  ? 22.270 -12.004 28.965  1.00 54.49 ? 74  SER A CA  1 
ATOM   599  C  C   . SER A 1 79  ? 23.534 -12.864 28.995  1.00 48.53 ? 74  SER A C   1 
ATOM   600  O  O   . SER A 1 79  ? 24.442 -12.625 29.785  1.00 49.29 ? 74  SER A O   1 
ATOM   601  C  CB  . SER A 1 79  ? 22.551 -10.661 28.293  1.00 52.11 ? 74  SER A CB  1 
ATOM   602  O  OG  . SER A 1 79  ? 23.047 -10.834 26.974  1.00 65.86 ? 74  SER A OG  1 
ATOM   603  N  N   . GLU A 1 80  ? 23.583 -13.865 28.113  1.00 46.35 ? 75  GLU A N   1 
ATOM   604  C  CA  . GLU A 1 80  ? 24.721 -14.766 28.016  1.00 42.33 ? 75  GLU A CA  1 
ATOM   605  C  C   . GLU A 1 80  ? 25.931 -14.022 27.445  1.00 44.14 ? 75  GLU A C   1 
ATOM   606  O  O   . GLU A 1 80  ? 25.793 -13.242 26.507  1.00 40.37 ? 75  GLU A O   1 
ATOM   607  C  CB  . GLU A 1 80  ? 24.314 -15.997 27.144  1.00 40.81 ? 75  GLU A CB  1 
ATOM   608  C  CG  . GLU A 1 80  ? 25.192 -17.231 27.314  1.00 37.54 ? 75  GLU A CG  1 
ATOM   609  C  CD  . GLU A 1 80  ? 25.373 -17.681 28.752  1.00 31.16 ? 75  GLU A CD  1 
ATOM   610  O  OE1 . GLU A 1 80  ? 24.363 -17.839 29.480  1.00 39.81 ? 75  GLU A OE1 1 
ATOM   611  O  OE2 . GLU A 1 80  ? 26.542 -17.858 29.157  1.00 47.95 ? 75  GLU A OE2 1 
ATOM   612  N  N   . GLU A 1 81  ? 27.111 -14.237 28.045  1.00 39.05 ? 76  GLU A N   1 
ATOM   613  C  CA  . GLU A 1 81  ? 28.358 -13.660 27.562  1.00 39.05 ? 76  GLU A CA  1 
ATOM   614  C  C   . GLU A 1 81  ? 28.715 -14.172 26.171  1.00 36.89 ? 76  GLU A C   1 
ATOM   615  O  O   . GLU A 1 81  ? 28.880 -15.377 25.993  1.00 37.51 ? 76  GLU A O   1 
ATOM   616  C  CB  . GLU A 1 81  ? 29.508 -14.037 28.500  1.00 37.47 ? 76  GLU A CB  1 
ATOM   617  C  CG  . GLU A 1 81  ? 30.886 -13.675 27.974  1.00 39.09 ? 76  GLU A CG  1 
ATOM   618  C  CD  . GLU A 1 81  ? 31.061 -12.186 27.761  1.00 42.33 ? 76  GLU A CD  1 
ATOM   619  O  OE1 . GLU A 1 81  ? 30.671 -11.423 28.673  1.00 41.35 ? 76  GLU A OE1 1 
ATOM   620  O  OE2 . GLU A 1 81  ? 31.595 -11.782 26.701  1.00 37.20 ? 76  GLU A OE2 1 
ATOM   621  N  N   . LYS A 1 82  ? 28.874 -13.273 25.193  1.00 28.31 ? 77  LYS A N   1 
ATOM   622  C  CA  . LYS A 1 82  ? 29.210 -13.728 23.849  1.00 34.45 ? 77  LYS A CA  1 
ATOM   623  C  C   . LYS A 1 82  ? 30.590 -13.293 23.363  1.00 33.47 ? 77  LYS A C   1 
ATOM   624  O  O   . LYS A 1 82  ? 30.919 -13.472 22.184  1.00 32.63 ? 77  LYS A O   1 
ATOM   625  C  CB  . LYS A 1 82  ? 28.133 -13.296 22.833  1.00 40.82 ? 77  LYS A CB  1 
ATOM   626  C  CG  . LYS A 1 82  ? 26.781 -13.987 23.001  1.00 42.09 ? 77  LYS A CG  1 
ATOM   627  C  CD  . LYS A 1 82  ? 26.869 -15.503 23.337  1.00 43.72 ? 77  LYS A CD  1 
ATOM   628  C  CE  . LYS A 1 82  ? 25.584 -16.252 23.086  1.00 48.94 ? 77  LYS A CE  1 
ATOM   629  N  NZ  . LYS A 1 82  ? 24.381 -15.439 23.423  1.00 52.10 ? 77  LYS A NZ  1 
ATOM   630  N  N   . GLY A 1 83  ? 31.415 -12.781 24.287  1.00 24.71 ? 78  GLY A N   1 
ATOM   631  C  CA  . GLY A 1 83  ? 32.772 -12.402 23.937  1.00 18.08 ? 78  GLY A CA  1 
ATOM   632  C  C   . GLY A 1 83  ? 32.801 -11.000 23.347  1.00 12.59 ? 78  GLY A C   1 
ATOM   633  O  O   . GLY A 1 83  ? 31.791 -10.295 23.379  1.00 12.01 ? 78  GLY A O   1 
ATOM   634  N  N   . PRO A 1 84  ? 33.947 -10.597 22.762  1.00 10.02 ? 79  PRO A N   1 
ATOM   635  C  CA  . PRO A 1 84  ? 34.181 -9.204  22.385  1.00 9.03  ? 79  PRO A CA  1 
ATOM   636  C  C   . PRO A 1 84  ? 33.673 -8.796  21.004  1.00 8.25  ? 79  PRO A C   1 
ATOM   637  O  O   . PRO A 1 84  ? 33.839 -7.638  20.620  1.00 8.02  ? 79  PRO A O   1 
ATOM   638  C  CB  . PRO A 1 84  ? 35.724 -9.125  22.426  1.00 9.62  ? 79  PRO A CB  1 
ATOM   639  C  CG  . PRO A 1 84  ? 36.146 -10.529 21.960  1.00 10.12 ? 79  PRO A CG  1 
ATOM   640  C  CD  . PRO A 1 84  ? 35.128 -11.454 22.561  1.00 10.19 ? 79  PRO A CD  1 
ATOM   641  N  N   . GLU A 1 85  ? 33.030 -9.722  20.280  1.00 6.95  ? 80  GLU A N   1 
ATOM   642  C  CA  . GLU A 1 85  ? 32.793 -9.523  18.862  1.00 7.45  ? 80  GLU A CA  1 
ATOM   643  C  C   . GLU A 1 85  ? 31.810 -8.377  18.596  1.00 7.09  ? 80  GLU A C   1 
ATOM   644  O  O   . GLU A 1 85  ? 32.002 -7.601  17.663  1.00 7.51  ? 80  GLU A O   1 
ATOM   645  C  CB  . GLU A 1 85  ? 32.291 -10.819 18.196  1.00 8.50  ? 80  GLU A CB  1 
ATOM   646  C  CG  . GLU A 1 85  ? 33.384 -11.891 18.084  1.00 8.73  ? 80  GLU A CG  1 
ATOM   647  C  CD  . GLU A 1 85  ? 33.518 -12.789 19.297  1.00 9.91  ? 80  GLU A CD  1 
ATOM   648  O  OE1 . GLU A 1 85  ? 32.832 -12.534 20.324  1.00 7.47  ? 80  GLU A OE1 1 
ATOM   649  O  OE2 . GLU A 1 85  ? 34.326 -13.747 19.228  1.00 11.15 ? 80  GLU A OE2 1 
ATOM   650  N  N   . VAL A 1 86  ? 30.725 -8.306  19.359  1.00 6.88  ? 81  VAL A N   1 
ATOM   651  C  CA  . VAL A 1 86  ? 29.744 -7.245  19.160  1.00 8.96  ? 81  VAL A CA  1 
ATOM   652  C  C   . VAL A 1 86  ? 30.375 -5.870  19.344  1.00 8.44  ? 81  VAL A C   1 
ATOM   653  O  O   . VAL A 1 86  ? 30.199 -4.990  18.501  1.00 7.89  ? 81  VAL A O   1 
ATOM   654  C  CB  . VAL A 1 86  ? 28.530 -7.418  20.086  1.00 12.19 ? 81  VAL A CB  1 
ATOM   655  C  CG1 . VAL A 1 86  ? 27.625 -6.182  20.049  1.00 14.96 ? 81  VAL A CG1 1 
ATOM   656  C  CG2 . VAL A 1 86  ? 27.735 -8.635  19.704  1.00 14.73 ? 81  VAL A CG2 1 
ATOM   657  N  N   . ARG A 1 87  ? 31.107 -5.688  20.449  1.00 7.32  ? 82  ARG A N   1 
ATOM   658  C  CA  . ARG A 1 87  ? 31.790 -4.434  20.705  1.00 7.49  ? 82  ARG A CA  1 
ATOM   659  C  C   . ARG A 1 87  ? 32.801 -4.154  19.592  1.00 7.24  ? 82  ARG A C   1 
ATOM   660  O  O   . ARG A 1 87  ? 32.880 -3.030  19.090  1.00 7.78  ? 82  ARG A O   1 
ATOM   661  C  CB  . ARG A 1 87  ? 32.518 -4.444  22.074  1.00 9.20  ? 82  ARG A CB  1 
ATOM   662  C  CG  . ARG A 1 87  ? 33.459 -3.255  22.252  1.00 11.40 ? 82  ARG A CG  1 
ATOM   663  C  CD  . ARG A 1 87  ? 34.303 -3.256  23.534  1.00 14.49 ? 82  ARG A CD  1 
ATOM   664  N  NE  . ARG A 1 87  ? 35.139 -4.440  23.660  1.00 19.36 ? 82  ARG A NE  1 
ATOM   665  C  CZ  . ARG A 1 87  ? 36.211 -4.735  22.921  1.00 19.74 ? 82  ARG A CZ  1 
ATOM   666  N  NH1 . ARG A 1 87  ? 36.752 -3.857  22.099  1.00 21.19 ? 82  ARG A NH1 1 
ATOM   667  N  NH2 . ARG A 1 87  ? 36.773 -5.934  23.046  1.00 21.90 ? 82  ARG A NH2 1 
ATOM   668  N  N   . GLU A 1 88  ? 33.594 -5.167  19.217  1.00 6.14  ? 83  GLU A N   1 
ATOM   669  C  CA  . GLU A 1 88  ? 34.597 -4.988  18.175  1.00 5.70  ? 83  GLU A CA  1 
ATOM   670  C  C   . GLU A 1 88  ? 33.987 -4.493  16.864  1.00 5.94  ? 83  GLU A C   1 
ATOM   671  O  O   . GLU A 1 88  ? 34.509 -3.567  16.250  1.00 7.20  ? 83  GLU A O   1 
ATOM   672  C  CB  . GLU A 1 88  ? 35.348 -6.289  17.872  1.00 5.86  ? 83  GLU A CB  1 
ATOM   673  C  CG  . GLU A 1 88  ? 36.360 -6.653  18.931  1.00 6.28  ? 83  GLU A CG  1 
ATOM   674  C  CD  . GLU A 1 88  ? 36.897 -8.067  18.826  1.00 8.01  ? 83  GLU A CD  1 
ATOM   675  O  OE1 . GLU A 1 88  ? 36.414 -8.800  17.940  1.00 7.92  ? 83  GLU A OE1 1 
ATOM   676  O  OE2 . GLU A 1 88  ? 37.841 -8.404  19.581  1.00 8.01  ? 83  GLU A OE2 1 
ATOM   677  N  N   . TYR A 1 89  ? 32.884 -5.124  16.453  1.00 5.38  ? 84  TYR A N   1 
ATOM   678  C  CA  . TYR A 1 89  ? 32.275 -4.783  15.177  1.00 6.51  ? 84  TYR A CA  1 
ATOM   679  C  C   . TYR A 1 89  ? 31.551 -3.428  15.233  1.00 6.17  ? 84  TYR A C   1 
ATOM   680  O  O   . TYR A 1 89  ? 31.661 -2.626  14.300  1.00 5.20  ? 84  TYR A O   1 
ATOM   681  C  CB  . TYR A 1 89  ? 31.348 -5.889  14.708  1.00 5.80  ? 84  TYR A CB  1 
ATOM   682  C  CG  . TYR A 1 89  ? 30.847 -5.663  13.296  1.00 5.68  ? 84  TYR A CG  1 
ATOM   683  C  CD1 . TYR A 1 89  ? 31.710 -5.286  12.280  1.00 5.64  ? 84  TYR A CD1 1 
ATOM   684  C  CD2 . TYR A 1 89  ? 29.509 -5.783  12.992  1.00 6.04  ? 84  TYR A CD2 1 
ATOM   685  C  CE1 . TYR A 1 89  ? 31.240 -5.027  10.991  1.00 5.45  ? 84  TYR A CE1 1 
ATOM   686  C  CE2 . TYR A 1 89  ? 29.033 -5.550  11.713  1.00 5.89  ? 84  TYR A CE2 1 
ATOM   687  C  CZ  . TYR A 1 89  ? 29.900 -5.154  10.722  1.00 5.61  ? 84  TYR A CZ  1 
ATOM   688  O  OH  . TYR A 1 89  ? 29.390 -4.901  9.498   1.00 6.76  ? 84  TYR A OH  1 
ATOM   689  N  N   . ARG A 1 90  ? 30.891 -3.131  16.361  1.00 5.44  ? 85  ARG A N   1 
ATOM   690  C  CA  . ARG A 1 90  ? 30.337 -1.793  16.559  1.00 6.50  ? 85  ARG A CA  1 
ATOM   691  C  C   . ARG A 1 90  ? 31.456 -0.750  16.482  1.00 7.34  ? 85  ARG A C   1 
ATOM   692  O  O   . ARG A 1 90  ? 31.300 0.283   15.841  1.00 7.02  ? 85  ARG A O   1 
ATOM   693  C  CB  . ARG A 1 90  ? 29.588 -1.710  17.881  1.00 7.54  ? 85  ARG A CB  1 
ATOM   694  C  CG  . ARG A 1 90  ? 28.783 -0.430  18.142  1.00 7.06  ? 85  ARG A CG  1 
ATOM   695  C  CD  . ARG A 1 90  ? 29.591 0.599   18.828  1.00 8.06  ? 85  ARG A CD  1 
ATOM   696  N  NE  . ARG A 1 90  ? 29.999 0.171   20.163  1.00 8.25  ? 85  ARG A NE  1 
ATOM   697  C  CZ  . ARG A 1 90  ? 31.074 0.597   20.798  1.00 11.37 ? 85  ARG A CZ  1 
ATOM   698  N  NH1 . ARG A 1 90  ? 31.820 1.579   20.317  1.00 12.05 ? 85  ARG A NH1 1 
ATOM   699  N  NH2 . ARG A 1 90  ? 31.412 0.025   21.954  1.00 11.70 ? 85  ARG A NH2 1 
ATOM   700  N  N   . GLU A 1 91  ? 32.597 -1.021  17.118  1.00 7.02  ? 86  GLU A N   1 
ATOM   701  C  CA  . GLU A 1 91  ? 33.740 -0.125  17.070  1.00 7.64  ? 86  GLU A CA  1 
ATOM   702  C  C   . GLU A 1 91  ? 34.263 0.089   15.653  1.00 7.71  ? 86  GLU A C   1 
ATOM   703  O  O   . GLU A 1 91  ? 34.683 1.188   15.304  1.00 8.35  ? 86  GLU A O   1 
ATOM   704  C  CB  . GLU A 1 91  ? 34.873 -0.615  17.948  1.00 9.30  ? 86  GLU A CB  1 
ATOM   705  C  CG  . GLU A 1 91  ? 34.612 -0.408  19.428  1.00 12.55 ? 86  GLU A CG  1 
ATOM   706  C  CD  . GLU A 1 91  ? 35.669 -0.984  20.381  1.00 22.52 ? 86  GLU A CD  1 
ATOM   707  O  OE1 . GLU A 1 91  ? 36.492 -1.826  19.948  1.00 24.16 ? 86  GLU A OE1 1 
ATOM   708  O  OE2 . GLU A 1 91  ? 35.678 -0.573  21.567  1.00 22.79 ? 86  GLU A OE2 1 
ATOM   709  N  N   . LYS A 1 92  ? 34.247 -0.968  14.850  1.00 8.03  ? 87  LYS A N   1 
ATOM   710  C  CA  . LYS A 1 92  ? 34.716 -0.890  13.476  1.00 8.03  ? 87  LYS A CA  1 
ATOM   711  C  C   . LYS A 1 92  ? 33.815 0.044   12.665  1.00 6.57  ? 87  LYS A C   1 
ATOM   712  O  O   . LYS A 1 92  ? 34.305 0.904   11.935  1.00 6.27  ? 87  LYS A O   1 
ATOM   713  C  CB  . LYS A 1 92  ? 34.716 -2.298  12.872  1.00 10.45 ? 87  LYS A CB  1 
ATOM   714  C  CG  . LYS A 1 92  ? 35.019 -2.347  11.360  1.00 16.15 ? 87  LYS A CG  1 
ATOM   715  C  CD  . LYS A 1 92  ? 34.727 -3.773  10.784  1.00 19.57 ? 87  LYS A CD  1 
ATOM   716  C  CE  . LYS A 1 92  ? 34.605 -3.811  9.288   1.00 25.03 ? 87  LYS A CE  1 
ATOM   717  N  NZ  . LYS A 1 92  ? 35.883 -3.403  8.682   1.00 29.12 ? 87  LYS A NZ  1 
ATOM   718  N  N   . VAL A 1 93  ? 32.499 -0.173  12.768  1.00 5.54  ? 88  VAL A N   1 
ATOM   719  C  CA  . VAL A 1 93  ? 31.536 0.665   12.070  1.00 6.27  ? 88  VAL A CA  1 
ATOM   720  C  C   . VAL A 1 93  ? 31.637 2.109   12.553  1.00 6.39  ? 88  VAL A C   1 
ATOM   721  O  O   . VAL A 1 93  ? 31.664 3.047   11.756  1.00 6.37  ? 88  VAL A O   1 
ATOM   722  C  CB  . VAL A 1 93  ? 30.121 0.138   12.194  1.00 5.92  ? 88  VAL A CB  1 
ATOM   723  C  CG1 . VAL A 1 93  ? 29.128 1.117   11.615  1.00 6.44  ? 88  VAL A CG1 1 
ATOM   724  C  CG2 . VAL A 1 93  ? 29.988 -1.235  11.523  1.00 6.08  ? 88  VAL A CG2 1 
ATOM   725  N  N   . GLU A 1 94  ? 31.731 2.281   13.874  1.00 6.35  ? 89  GLU A N   1 
ATOM   726  C  CA  . GLU A 1 94  ? 31.886 3.594   14.477  1.00 6.81  ? 89  GLU A CA  1 
ATOM   727  C  C   . GLU A 1 94  ? 33.104 4.349   13.958  1.00 6.36  ? 89  GLU A C   1 
ATOM   728  O  O   . GLU A 1 94  ? 33.034 5.532   13.647  1.00 5.04  ? 89  GLU A O   1 
ATOM   729  C  CB  . GLU A 1 94  ? 31.965 3.410   15.987  1.00 6.65  ? 89  GLU A CB  1 
ATOM   730  C  CG  . GLU A 1 94  ? 32.027 4.688   16.768  1.00 7.59  ? 89  GLU A CG  1 
ATOM   731  C  CD  . GLU A 1 94  ? 31.917 4.445   18.252  1.00 7.79  ? 89  GLU A CD  1 
ATOM   732  O  OE1 . GLU A 1 94  ? 30.891 3.883   18.690  1.00 7.75  ? 89  GLU A OE1 1 
ATOM   733  O  OE2 . GLU A 1 94  ? 32.845 4.858   18.976  1.00 9.58  ? 89  GLU A OE2 1 
ATOM   734  N  N   . THR A 1 95  ? 34.243 3.661   13.890  1.00 6.76  ? 90  THR A N   1 
ATOM   735  C  CA  . THR A 1 95  ? 35.452 4.272   13.376  1.00 7.68  ? 90  THR A CA  1 
ATOM   736  C  C   . THR A 1 95  ? 35.292 4.728   11.933  1.00 6.58  ? 90  THR A C   1 
ATOM   737  O  O   . THR A 1 95  ? 35.788 5.792   11.562  1.00 7.39  ? 90  THR A O   1 
ATOM   738  C  CB  . THR A 1 95  ? 36.632 3.278   13.589  1.00 11.22 ? 90  THR A CB  1 
ATOM   739  O  OG1 . THR A 1 95  ? 36.731 3.018   14.995  1.00 12.17 ? 90  THR A OG1 1 
ATOM   740  C  CG2 . THR A 1 95  ? 37.911 3.823   13.101  1.00 13.42 ? 90  THR A CG2 1 
ATOM   741  N  N   . GLU A 1 96  ? 34.647 3.906   11.106  1.00 6.51  ? 91  GLU A N   1 
ATOM   742  C  CA  . GLU A 1 96  ? 34.440 4.250   9.713   1.00 7.29  ? 91  GLU A CA  1 
ATOM   743  C  C   . GLU A 1 96  ? 33.528 5.470   9.582   1.00 6.39  ? 91  GLU A C   1 
ATOM   744  O  O   . GLU A 1 96  ? 33.798 6.371   8.784   1.00 5.55  ? 91  GLU A O   1 
ATOM   745  C  CB  . GLU A 1 96  ? 33.838 3.094   8.917   1.00 10.57 ? 91  GLU A CB  1 
ATOM   746  C  CG  . GLU A 1 96  ? 34.809 1.976   8.745   1.00 15.34 ? 91  GLU A CG  1 
ATOM   747  C  CD  . GLU A 1 96  ? 34.399 0.808   7.859   1.00 20.48 ? 91  GLU A CD  1 
ATOM   748  O  OE1 . GLU A 1 96  ? 33.427 0.906   7.058   1.00 13.99 ? 91  GLU A OE1 1 
ATOM   749  O  OE2 . GLU A 1 96  ? 35.140 -0.208  7.960   1.00 23.71 ? 91  GLU A OE2 1 
ATOM   750  N  N   . LEU A 1 97  ? 32.467 5.485   10.390  1.00 5.95  ? 92  LEU A N   1 
ATOM   751  C  CA  . LEU A 1 97  ? 31.568 6.627   10.470  1.00 6.54  ? 92  LEU A CA  1 
ATOM   752  C  C   . LEU A 1 97  ? 32.308 7.902   10.877  1.00 6.57  ? 92  LEU A C   1 
ATOM   753  O  O   . LEU A 1 97  ? 32.145 8.946   10.247  1.00 6.06  ? 92  LEU A O   1 
ATOM   754  C  CB  . LEU A 1 97  ? 30.456 6.270   11.486  1.00 7.61  ? 92  LEU A CB  1 
ATOM   755  C  CG  . LEU A 1 97  ? 29.267 7.261   11.689  1.00 8.79  ? 92  LEU A CG  1 
ATOM   756  C  CD1 . LEU A 1 97  ? 28.081 6.584   12.339  1.00 9.05  ? 92  LEU A CD1 1 
ATOM   757  C  CD2 . LEU A 1 97  ? 29.678 8.424   12.544  1.00 11.22 ? 92  LEU A CD2 1 
ATOM   758  N  N   . GLN A 1 98  ? 33.125 7.831   11.936  1.00 6.95  ? 93  GLN A N   1 
ATOM   759  C  CA  . GLN A 1 98  ? 33.882 8.996   12.377  1.00 7.77  ? 93  GLN A CA  1 
ATOM   760  C  C   . GLN A 1 98  ? 34.827 9.452   11.267  1.00 8.62  ? 93  GLN A C   1 
ATOM   761  O  O   . GLN A 1 98  ? 35.071 10.646  11.065  1.00 7.31  ? 93  GLN A O   1 
ATOM   762  C  CB  . GLN A 1 98  ? 34.637 8.697   13.668  1.00 7.98  ? 93  GLN A CB  1 
ATOM   763  C  CG  . GLN A 1 98  ? 33.708 8.484   14.853  1.00 7.85  ? 93  GLN A CG  1 
ATOM   764  C  CD  . GLN A 1 98  ? 34.438 7.879   16.033  1.00 9.15  ? 93  GLN A CD  1 
ATOM   765  O  OE1 . GLN A 1 98  ? 35.335 6.998   15.867  1.00 8.33  ? 93  GLN A OE1 1 
ATOM   766  N  NE2 . GLN A 1 98  ? 34.086 8.292   17.241  1.00 9.88  ? 93  GLN A NE2 1 
ATOM   767  N  N   . GLY A 1 99  ? 35.382 8.489   10.526  1.00 8.73  ? 94  GLY A N   1 
ATOM   768  C  CA  . GLY A 1 99  ? 36.257 8.838   9.429   1.00 7.24  ? 94  GLY A CA  1 
ATOM   769  C  C   . GLY A 1 99  ? 35.562 9.626   8.328   1.00 6.48  ? 94  GLY A C   1 
ATOM   770  O  O   . GLY A 1 99  ? 36.114 10.567  7.801   1.00 7.10  ? 94  GLY A O   1 
ATOM   771  N  N   . VAL A 1 100 ? 34.358 9.209   7.976   1.00 6.07  ? 95  VAL A N   1 
ATOM   772  C  CA  . VAL A 1 100 ? 33.543 9.913   6.999   1.00 6.47  ? 95  VAL A CA  1 
ATOM   773  C  C   . VAL A 1 100 ? 33.216 11.322  7.497   1.00 6.32  ? 95  VAL A C   1 
ATOM   774  O  O   . VAL A 1 100 ? 33.383 12.281  6.766   1.00 5.61  ? 95  VAL A O   1 
ATOM   775  C  CB  . VAL A 1 100 ? 32.283 9.131   6.611   1.00 7.69  ? 95  VAL A CB  1 
ATOM   776  C  CG1 . VAL A 1 100 ? 31.280 10.015  5.857   1.00 9.52  ? 95  VAL A CG1 1 
ATOM   777  C  CG2 . VAL A 1 100 ? 32.649 7.898   5.795   1.00 9.39  ? 95  VAL A CG2 1 
ATOM   778  N  N   . CYS A 1 101 ? 32.799 11.452  8.762   1.00 6.54  ? 96  CYS A N   1 
ATOM   779  C  CA  . CYS A 1 101 ? 32.557 12.762  9.340   1.00 5.99  ? 96  CYS A CA  1 
ATOM   780  C  C   . CYS A 1 101 ? 33.787 13.651  9.295   1.00 6.42  ? 96  CYS A C   1 
ATOM   781  O  O   . CYS A 1 101 ? 33.680 14.831  8.943   1.00 5.71  ? 96  CYS A O   1 
ATOM   782  C  CB  . CYS A 1 101 ? 32.026 12.670  10.773  1.00 5.89  ? 96  CYS A CB  1 
ATOM   783  S  SG  . CYS A 1 101 ? 30.410 11.899  10.890  1.00 7.06  ? 96  CYS A SG  1 
ATOM   784  N  N   . ASP A 1 102 ? 34.945 13.092  9.675   1.00 6.30  ? 97  ASP A N   1 
ATOM   785  C  CA  . ASP A 1 102 ? 36.177 13.857  9.652   1.00 7.03  ? 97  ASP A CA  1 
ATOM   786  C  C   . ASP A 1 102 ? 36.564 14.323  8.245   1.00 6.12  ? 97  ASP A C   1 
ATOM   787  O  O   . ASP A 1 102 ? 37.041 15.441  8.065   1.00 5.12  ? 97  ASP A O   1 
ATOM   788  C  CB  . ASP A 1 102 ? 37.311 13.046  10.281  1.00 8.94  ? 97  ASP A CB  1 
ATOM   789  C  CG  . ASP A 1 102 ? 37.260 12.830  11.796  1.00 13.48 ? 97  ASP A CG  1 
ATOM   790  O  OD1 . ASP A 1 102 ? 36.510 13.521  12.459  1.00 13.45 ? 97  ASP A OD1 1 
ATOM   791  O  OD2 . ASP A 1 102 ? 37.981 11.944  12.286  1.00 15.54 ? 97  ASP A OD2 1 
ATOM   792  N  N   . THR A 1 103 ? 36.336 13.473  7.250   1.00 6.40  ? 98  THR A N   1 
ATOM   793  C  CA  . THR A 1 103 ? 36.577 13.823  5.860   1.00 6.11  ? 98  THR A CA  1 
ATOM   794  C  C   . THR A 1 103 ? 35.732 15.016  5.433   1.00 5.73  ? 98  THR A C   1 
ATOM   795  O  O   . THR A 1 103 ? 36.241 15.970  4.858   1.00 5.58  ? 98  THR A O   1 
ATOM   796  C  CB  . THR A 1 103 ? 36.307 12.605  4.983   1.00 9.15  ? 98  THR A CB  1 
ATOM   797  O  OG1 . THR A 1 103 ? 37.302 11.601  5.240   1.00 9.04  ? 98  THR A OG1 1 
ATOM   798  C  CG2 . THR A 1 103 ? 36.307 12.939  3.504   1.00 9.79  ? 98  THR A CG2 1 
ATOM   799  N  N   . VAL A 1 104 ? 34.429 14.969  5.729   1.00 4.48  ? 99  VAL A N   1 
ATOM   800  C  CA  . VAL A 1 104 ? 33.540 16.076  5.377   1.00 4.65  ? 99  VAL A CA  1 
ATOM   801  C  C   . VAL A 1 104 ? 33.956 17.359  6.100   1.00 4.47  ? 99  VAL A C   1 
ATOM   802  O  O   . VAL A 1 104 ? 34.097 18.415  5.489   1.00 4.99  ? 99  VAL A O   1 
ATOM   803  C  CB  . VAL A 1 104 ? 32.085 15.736  5.689   1.00 4.74  ? 99  VAL A CB  1 
ATOM   804  C  CG1 . VAL A 1 104 ? 31.208 16.972  5.512   1.00 5.73  ? 99  VAL A CG1 1 
ATOM   805  C  CG2 . VAL A 1 104 ? 31.621 14.578  4.807   1.00 5.07  ? 99  VAL A CG2 1 
ATOM   806  N  N   . LEU A 1 105 ? 34.208 17.264  7.416   1.00 4.74  ? 100 LEU A N   1 
ATOM   807  C  CA  . LEU A 1 105 ? 34.654 18.423  8.171   1.00 4.93  ? 100 LEU A CA  1 
ATOM   808  C  C   . LEU A 1 105 ? 35.967 18.996  7.653   1.00 5.42  ? 100 LEU A C   1 
ATOM   809  O  O   . LEU A 1 105 ? 36.152 20.222  7.623   1.00 5.33  ? 100 LEU A O   1 
ATOM   810  C  CB  . LEU A 1 105 ? 34.765 18.079  9.680   1.00 4.44  ? 100 LEU A CB  1 
ATOM   811  C  CG  . LEU A 1 105 ? 33.439 17.747  10.317  1.00 4.89  ? 100 LEU A CG  1 
ATOM   812  C  CD1 . LEU A 1 105 ? 33.608 17.124  11.672  1.00 5.48  ? 100 LEU A CD1 1 
ATOM   813  C  CD2 . LEU A 1 105 ? 32.568 18.963  10.443  1.00 5.17  ? 100 LEU A CD2 1 
ATOM   814  N  N   . GLY A 1 106 ? 36.841 18.102  7.194   1.00 6.10  ? 101 GLY A N   1 
ATOM   815  C  CA  . GLY A 1 106 ? 38.095 18.513  6.580   1.00 6.66  ? 101 GLY A CA  1 
ATOM   816  C  C   . GLY A 1 106 ? 37.912 19.326  5.305   1.00 8.21  ? 101 GLY A C   1 
ATOM   817  O  O   . GLY A 1 106 ? 38.607 20.318  5.100   1.00 10.38 ? 101 GLY A O   1 
ATOM   818  N  N   . LEU A 1 107 ? 36.952 18.918  4.468   1.00 6.15  ? 102 LEU A N   1 
ATOM   819  C  CA  . LEU A 1 107 ? 36.664 19.626  3.236   1.00 6.04  ? 102 LEU A CA  1 
ATOM   820  C  C   . LEU A 1 107 ? 36.083 20.996  3.546   1.00 5.87  ? 102 LEU A C   1 
ATOM   821  O  O   . LEU A 1 107 ? 36.420 21.984  2.885   1.00 6.15  ? 102 LEU A O   1 
ATOM   822  C  CB  . LEU A 1 107 ? 35.682 18.843  2.367   1.00 6.74  ? 102 LEU A CB  1 
ATOM   823  C  CG  . LEU A 1 107 ? 36.223 17.505  1.852   1.00 7.93  ? 102 LEU A CG  1 
ATOM   824  C  CD1 . LEU A 1 107 ? 35.149 16.745  1.229   1.00 11.23 ? 102 LEU A CD1 1 
ATOM   825  C  CD2 . LEU A 1 107 ? 37.350 17.672  0.881   1.00 9.19  ? 102 LEU A CD2 1 
ATOM   826  N  N   . LEU A 1 108 ? 35.206 21.044  4.548   1.00 5.87  ? 103 LEU A N   1 
ATOM   827  C  CA  . LEU A 1 108 ? 34.606 22.318  4.923   1.00 6.86  ? 103 LEU A CA  1 
ATOM   828  C  C   . LEU A 1 108 ? 35.687 23.276  5.430   1.00 6.22  ? 103 LEU A C   1 
ATOM   829  O  O   . LEU A 1 108 ? 35.647 24.469  5.147   1.00 7.57  ? 103 LEU A O   1 
ATOM   830  C  CB  . LEU A 1 108 ? 33.512 22.095  5.994   1.00 7.15  ? 103 LEU A CB  1 
ATOM   831  C  CG  . LEU A 1 108 ? 32.323 21.316  5.516   1.00 7.19  ? 103 LEU A CG  1 
ATOM   832  C  CD1 . LEU A 1 108 ? 31.384 20.950  6.663   1.00 8.25  ? 103 LEU A CD1 1 
ATOM   833  C  CD2 . LEU A 1 108 ? 31.541 22.052  4.432   1.00 8.12  ? 103 LEU A CD2 1 
ATOM   834  N  N   . ASP A 1 109 ? 36.632 22.764  6.215   1.00 6.99  ? 104 ASP A N   1 
ATOM   835  C  CA  . ASP A 1 109 ? 37.694 23.575  6.795   1.00 8.64  ? 104 ASP A CA  1 
ATOM   836  C  C   . ASP A 1 109 ? 38.821 23.894  5.815   1.00 9.25  ? 104 ASP A C   1 
ATOM   837  O  O   . ASP A 1 109 ? 39.581 24.839  6.048   1.00 12.89 ? 104 ASP A O   1 
ATOM   838  C  CB  . ASP A 1 109 ? 38.283 22.873  8.034   1.00 11.98 ? 104 ASP A CB  1 
ATOM   839  C  CG  . ASP A 1 109 ? 39.001 23.851  8.957   1.00 19.47 ? 104 ASP A CG  1 
ATOM   840  O  OD1 . ASP A 1 109 ? 38.415 24.938  9.255   1.00 19.95 ? 104 ASP A OD1 1 
ATOM   841  O  OD2 . ASP A 1 109 ? 40.120 23.541  9.392   1.00 20.12 ? 104 ASP A OD2 1 
ATOM   842  N  N   . SER A 1 110 ? 38.961 23.059  4.782   1.00 9.64  ? 105 SER A N   1 
ATOM   843  C  CA  . SER A 1 110 ? 40.010 23.178  3.786   1.00 11.87 ? 105 SER A CA  1 
ATOM   844  C  C   . SER A 1 110 ? 39.508 23.030  2.350   1.00 11.70 ? 105 SER A C   1 
ATOM   845  O  O   . SER A 1 110 ? 39.739 21.983  1.732   1.00 15.26 ? 105 SER A O   1 
ATOM   846  C  CB  . SER A 1 110 ? 41.102 22.134  4.059   1.00 13.32 ? 105 SER A CB  1 
ATOM   847  O  OG  . SER A 1 110 ? 41.623 22.305  5.364   1.00 19.53 ? 105 SER A OG  1 
ATOM   848  N  N   . HIS A 1 111 ? 38.849 24.059  1.781   1.00 10.40 ? 106 HIS A N   1 
ATOM   849  C  CA  . HIS A 1 111 ? 38.717 25.406  2.314   1.00 11.06 ? 106 HIS A CA  1 
ATOM   850  C  C   . HIS A 1 111 ? 37.344 26.004  1.980   1.00 9.83  ? 106 HIS A C   1 
ATOM   851  O  O   . HIS A 1 111 ? 37.224 27.195  1.734   1.00 9.88  ? 106 HIS A O   1 
ATOM   852  C  CB  . HIS A 1 111 ? 39.863 26.313  1.753   1.00 10.72 ? 106 HIS A CB  1 
ATOM   853  C  CG  . HIS A 1 111 ? 41.228 25.925  2.229   1.00 13.16 ? 106 HIS A CG  1 
ATOM   854  N  ND1 . HIS A 1 111 ? 42.067 25.116  1.467   1.00 16.39 ? 106 HIS A ND1 1 
ATOM   855  C  CD2 . HIS A 1 111 ? 41.840 26.191  3.408   1.00 12.02 ? 106 HIS A CD2 1 
ATOM   856  C  CE1 . HIS A 1 111 ? 43.162 24.927  2.215   1.00 12.61 ? 106 HIS A CE1 1 
ATOM   857  N  NE2 . HIS A 1 111 ? 43.048 25.538  3.397   1.00 17.18 ? 106 HIS A NE2 1 
ATOM   858  N  N   . LEU A 1 112 ? 36.294 25.174  1.997   1.00 7.71  ? 107 LEU A N   1 
ATOM   859  C  CA  . LEU A 1 112 ? 34.993 25.575  1.493   1.00 6.76  ? 107 LEU A CA  1 
ATOM   860  C  C   . LEU A 1 112 ? 34.434 26.752  2.290   1.00 6.88  ? 107 LEU A C   1 
ATOM   861  O  O   . LEU A 1 112 ? 33.933 27.714  1.712   1.00 9.10  ? 107 LEU A O   1 
ATOM   862  C  CB  . LEU A 1 112 ? 34.035 24.384  1.544   1.00 7.04  ? 107 LEU A CB  1 
ATOM   863  C  CG  . LEU A 1 112 ? 34.272 23.300  0.521   1.00 7.36  ? 107 LEU A CG  1 
ATOM   864  C  CD1 . LEU A 1 112 ? 33.394 22.138  0.723   1.00 6.76  ? 107 LEU A CD1 1 
ATOM   865  C  CD2 . LEU A 1 112 ? 34.070 23.812  -0.903  1.00 8.53  ? 107 LEU A CD2 1 
ATOM   866  N  N   . ILE A 1 113 ? 34.496 26.676  3.627   1.00 7.18  ? 108 ILE A N   1 
ATOM   867  C  CA  . ILE A 1 113 ? 33.811 27.666  4.438   1.00 8.16  ? 108 ILE A CA  1 
ATOM   868  C  C   . ILE A 1 113 ? 34.494 29.022  4.276   1.00 9.37  ? 108 ILE A C   1 
ATOM   869  O  O   . ILE A 1 113 ? 33.822 30.048  4.128   1.00 9.16  ? 108 ILE A O   1 
ATOM   870  C  CB  . ILE A 1 113 ? 33.699 27.237  5.901   1.00 8.91  ? 108 ILE A CB  1 
ATOM   871  C  CG1 . ILE A 1 113 ? 32.657 26.093  6.007   1.00 9.33  ? 108 ILE A CG1 1 
ATOM   872  C  CG2 . ILE A 1 113 ? 33.342 28.431  6.814   1.00 8.18  ? 108 ILE A CG2 1 
ATOM   873  C  CD1 . ILE A 1 113 ? 32.573 25.482  7.366   1.00 8.64  ? 108 ILE A CD1 1 
ATOM   874  N  N   . LYS A 1 114 ? 35.833 29.019  4.322   1.00 9.68  ? 109 LYS A N   1 
ATOM   875  C  CA  . LYS A 1 114 ? 36.524 30.289  4.316   1.00 10.64 ? 109 LYS A CA  1 
ATOM   876  C  C   . LYS A 1 114 ? 36.343 31.038  3.006   1.00 10.35 ? 109 LYS A C   1 
ATOM   877  O  O   . LYS A 1 114 ? 36.454 32.257  2.995   1.00 11.09 ? 109 LYS A O   1 
ATOM   878  C  CB  . LYS A 1 114 ? 38.017 30.149  4.647   1.00 12.64 ? 109 LYS A CB  1 
ATOM   879  C  CG  . LYS A 1 114 ? 38.850 29.474  3.631   1.00 14.80 ? 109 LYS A CG  1 
ATOM   880  C  CD  . LYS A 1 114 ? 40.368 29.484  4.017   1.00 14.05 ? 109 LYS A CD  1 
ATOM   881  C  CE  . LYS A 1 114 ? 40.685 29.076  5.432   1.00 16.93 ? 109 LYS A CE  1 
ATOM   882  N  NZ  . LYS A 1 114 ? 40.421 27.638  5.678   1.00 15.34 ? 109 LYS A NZ  1 
ATOM   883  N  N   . GLU A 1 115 ? 36.090 30.329  1.901   1.00 8.49  ? 110 GLU A N   1 
ATOM   884  C  CA  . GLU A 1 115 ? 35.881 31.020  0.645   1.00 10.20 ? 110 GLU A CA  1 
ATOM   885  C  C   . GLU A 1 115 ? 34.418 31.367  0.377   1.00 9.48  ? 110 GLU A C   1 
ATOM   886  O  O   . GLU A 1 115 ? 34.148 32.072  -0.583  1.00 8.36  ? 110 GLU A O   1 
ATOM   887  C  CB  . GLU A 1 115 ? 36.474 30.211  -0.510  1.00 12.78 ? 110 GLU A CB  1 
ATOM   888  C  CG  . GLU A 1 115 ? 38.011 30.125  -0.460  1.00 14.60 ? 110 GLU A CG  1 
ATOM   889  C  CD  . GLU A 1 115 ? 38.768 31.455  -0.545  1.00 26.13 ? 110 GLU A CD  1 
ATOM   890  O  OE1 . GLU A 1 115 ? 38.169 32.505  -0.910  1.00 25.72 ? 110 GLU A OE1 1 
ATOM   891  O  OE2 . GLU A 1 115 ? 39.985 31.443  -0.226  1.00 34.89 ? 110 GLU A OE2 1 
ATOM   892  N  N   . ALA A 1 116 ? 33.503 30.892  1.226   1.00 8.65  ? 111 ALA A N   1 
ATOM   893  C  CA  . ALA A 1 116 ? 32.077 31.086  0.999   1.00 9.21  ? 111 ALA A CA  1 
ATOM   894  C  C   . ALA A 1 116 ? 31.629 32.428  1.577   1.00 11.17 ? 111 ALA A C   1 
ATOM   895  O  O   . ALA A 1 116 ? 31.559 32.603  2.792   1.00 14.79 ? 111 ALA A O   1 
ATOM   896  C  CB  . ALA A 1 116 ? 31.248 29.963  1.622   1.00 9.03  ? 111 ALA A CB  1 
ATOM   897  N  N   . GLY A 1 117 ? 31.271 33.349  0.697   1.00 11.75 ? 112 GLY A N   1 
ATOM   898  C  CA  . GLY A 1 117 ? 30.897 34.701  1.093   1.00 13.11 ? 112 GLY A CA  1 
ATOM   899  C  C   . GLY A 1 117 ? 29.411 35.010  0.960   1.00 15.20 ? 112 GLY A C   1 
ATOM   900  O  O   . GLY A 1 117 ? 28.862 35.807  1.723   1.00 16.21 ? 112 GLY A O   1 
ATOM   901  N  N   . ASP A 1 118 ? 28.750 34.372  -0.004  1.00 10.55 ? 113 ASP A N   1 
ATOM   902  C  CA  . ASP A 1 118 ? 27.326 34.568  -0.154  1.00 11.78 ? 113 ASP A CA  1 
ATOM   903  C  C   . ASP A 1 118 ? 26.577 33.813  0.939   1.00 11.19 ? 113 ASP A C   1 
ATOM   904  O  O   . ASP A 1 118 ? 27.013 32.762  1.407   1.00 11.84 ? 113 ASP A O   1 
ATOM   905  C  CB  . ASP A 1 118 ? 26.841 34.122  -1.531  1.00 11.79 ? 113 ASP A CB  1 
ATOM   906  C  CG  . ASP A 1 118 ? 27.418 34.954  -2.641  1.00 13.04 ? 113 ASP A CG  1 
ATOM   907  O  OD1 . ASP A 1 118 ? 28.122 35.936  -2.339  1.00 14.83 ? 113 ASP A OD1 1 
ATOM   908  O  OD2 . ASP A 1 118 ? 27.188 34.617  -3.813  1.00 10.12 ? 113 ASP A OD2 1 
ATOM   909  N  N   . ALA A 1 119 ? 25.433 34.358  1.343   1.00 11.01 ? 114 ALA A N   1 
ATOM   910  C  CA  . ALA A 1 119 ? 24.673 33.736  2.406   1.00 11.51 ? 114 ALA A CA  1 
ATOM   911  C  C   . ALA A 1 119 ? 24.279 32.298  2.068   1.00 10.00 ? 114 ALA A C   1 
ATOM   912  O  O   . ALA A 1 119 ? 24.348 31.435  2.933   1.00 12.09 ? 114 ALA A O   1 
ATOM   913  C  CB  . ALA A 1 119 ? 23.439 34.581  2.724   1.00 12.19 ? 114 ALA A CB  1 
ATOM   914  N  N   . GLU A 1 120 ? 23.897 32.025  0.809   1.00 9.48  ? 115 GLU A N   1 
ATOM   915  C  CA  . GLU A 1 120 ? 23.409 30.706  0.433   1.00 11.09 ? 115 GLU A CA  1 
ATOM   916  C  C   . GLU A 1 120 ? 24.491 29.625  0.548   1.00 11.24 ? 115 GLU A C   1 
ATOM   917  O  O   . GLU A 1 120 ? 24.219 28.528  1.039   1.00 15.42 ? 115 GLU A O   1 
ATOM   918  C  CB  . GLU A 1 120 ? 22.782 30.724  -0.973  1.00 15.43 ? 115 GLU A CB  1 
ATOM   919  C  CG  . GLU A 1 120 ? 21.531 31.629  -1.062  1.00 20.30 ? 115 GLU A CG  1 
ATOM   920  C  CD  . GLU A 1 120 ? 21.736 33.142  -0.854  1.00 28.35 ? 115 GLU A CD  1 
ATOM   921  O  OE1 . GLU A 1 120 ? 22.836 33.687  -1.170  1.00 18.71 ? 115 GLU A OE1 1 
ATOM   922  O  OE2 . GLU A 1 120 ? 20.792 33.770  -0.303  1.00 30.50 ? 115 GLU A OE2 1 
ATOM   923  N  N   . SER A 1 121 ? 25.729 29.956  0.178   1.00 9.12  ? 116 SER A N   1 
ATOM   924  C  CA  . SER A 1 121 ? 26.821 29.005  0.321   1.00 8.27  ? 116 SER A CA  1 
ATOM   925  C  C   . SER A 1 121 ? 27.300 28.919  1.766   1.00 8.54  ? 116 SER A C   1 
ATOM   926  O  O   . SER A 1 121 ? 27.527 27.829  2.275   1.00 7.49  ? 116 SER A O   1 
ATOM   927  C  CB  . SER A 1 121 ? 27.952 29.377  -0.617  1.00 10.65 ? 116 SER A CB  1 
ATOM   928  O  OG  . SER A 1 121 ? 28.417 30.665  -0.273  1.00 14.20 ? 116 SER A OG  1 
ATOM   929  N  N   . ARG A 1 122 ? 27.451 30.073  2.437   1.00 7.75  ? 117 ARG A N   1 
ATOM   930  C  CA  . ARG A 1 122 ? 28.011 30.073  3.779   1.00 8.96  ? 117 ARG A CA  1 
ATOM   931  C  C   . ARG A 1 122 ? 27.072 29.361  4.752   1.00 6.66  ? 117 ARG A C   1 
ATOM   932  O  O   . ARG A 1 122 ? 27.525 28.543  5.557   1.00 5.87  ? 117 ARG A O   1 
ATOM   933  C  CB  . ARG A 1 122 ? 28.315 31.474  4.247   1.00 9.60  ? 117 ARG A CB  1 
ATOM   934  C  CG  . ARG A 1 122 ? 29.077 31.480  5.506   1.00 12.54 ? 117 ARG A CG  1 
ATOM   935  C  CD  . ARG A 1 122 ? 29.742 32.822  5.752   1.00 15.13 ? 117 ARG A CD  1 
ATOM   936  N  NE  . ARG A 1 122 ? 30.675 32.689  6.865   1.00 16.52 ? 117 ARG A NE  1 
ATOM   937  C  CZ  . ARG A 1 122 ? 31.905 32.198  6.760   1.00 19.73 ? 117 ARG A CZ  1 
ATOM   938  N  NH1 . ARG A 1 122 ? 32.458 31.952  5.582   1.00 18.74 ? 117 ARG A NH1 1 
ATOM   939  N  NH2 . ARG A 1 122 ? 32.606 31.975  7.866   1.00 22.97 ? 117 ARG A NH2 1 
ATOM   940  N  N   . VAL A 1 123 ? 25.764 29.621  4.640   1.00 5.48  ? 118 VAL A N   1 
ATOM   941  C  CA  . VAL A 1 123 ? 24.815 28.944  5.512   1.00 5.68  ? 118 VAL A CA  1 
ATOM   942  C  C   . VAL A 1 123 ? 24.782 27.457  5.212   1.00 5.11  ? 118 VAL A C   1 
ATOM   943  O  O   . VAL A 1 123 ? 24.740 26.638  6.129   1.00 4.63  ? 118 VAL A O   1 
ATOM   944  C  CB  . VAL A 1 123 ? 23.424 29.570  5.429   1.00 6.99  ? 118 VAL A CB  1 
ATOM   945  C  CG1 . VAL A 1 123 ? 22.422 28.742  6.205   1.00 7.35  ? 118 VAL A CG1 1 
ATOM   946  C  CG2 . VAL A 1 123 ? 23.468 31.000  5.939   1.00 7.49  ? 118 VAL A CG2 1 
ATOM   947  N  N   . PHE A 1 124 ? 24.817 27.101  3.917   1.00 5.41  ? 119 PHE A N   1 
ATOM   948  C  CA  . PHE A 1 124 ? 24.820 25.699  3.534   1.00 5.31  ? 119 PHE A CA  1 
ATOM   949  C  C   . PHE A 1 124 ? 25.981 24.965  4.205   1.00 4.48  ? 119 PHE A C   1 
ATOM   950  O  O   . PHE A 1 124 ? 25.784 23.887  4.767   1.00 4.46  ? 119 PHE A O   1 
ATOM   951  C  CB  . PHE A 1 124 ? 24.863 25.600  1.998   1.00 6.19  ? 119 PHE A CB  1 
ATOM   952  C  CG  . PHE A 1 124 ? 24.707 24.195  1.478   1.00 8.94  ? 119 PHE A CG  1 
ATOM   953  C  CD1 . PHE A 1 124 ? 25.787 23.347  1.412   1.00 9.72  ? 119 PHE A CD1 1 
ATOM   954  C  CD2 . PHE A 1 124 ? 23.466 23.730  1.061   1.00 9.96  ? 119 PHE A CD2 1 
ATOM   955  C  CE1 . PHE A 1 124 ? 25.625 22.023  0.941   1.00 10.34 ? 119 PHE A CE1 1 
ATOM   956  C  CE2 . PHE A 1 124 ? 23.318 22.435  0.558   1.00 13.19 ? 119 PHE A CE2 1 
ATOM   957  C  CZ  . PHE A 1 124 ? 24.399 21.594  0.521   1.00 10.34 ? 119 PHE A CZ  1 
ATOM   958  N  N   . TYR A 1 125 ? 27.192 25.541  4.130   1.00 4.45  ? 120 TYR A N   1 
ATOM   959  C  CA  . TYR A 1 125 ? 28.383 24.861  4.625   1.00 4.51  ? 120 TYR A CA  1 
ATOM   960  C  C   . TYR A 1 125 ? 28.379 24.789  6.142   1.00 5.34  ? 120 TYR A C   1 
ATOM   961  O  O   . TYR A 1 125 ? 28.795 23.775  6.721   1.00 5.75  ? 120 TYR A O   1 
ATOM   962  C  CB  . TYR A 1 125 ? 29.657 25.492  4.116   1.00 4.67  ? 120 TYR A CB  1 
ATOM   963  C  CG  . TYR A 1 125 ? 29.906 25.322  2.623   1.00 4.73  ? 120 TYR A CG  1 
ATOM   964  C  CD1 . TYR A 1 125 ? 29.746 24.084  2.002   1.00 5.04  ? 120 TYR A CD1 1 
ATOM   965  C  CD2 . TYR A 1 125 ? 30.296 26.390  1.842   1.00 4.70  ? 120 TYR A CD2 1 
ATOM   966  C  CE1 . TYR A 1 125 ? 29.933 23.938  0.642   1.00 4.80  ? 120 TYR A CE1 1 
ATOM   967  C  CE2 . TYR A 1 125 ? 30.517 26.250  0.484   1.00 4.90  ? 120 TYR A CE2 1 
ATOM   968  C  CZ  . TYR A 1 125 ? 30.363 25.019  -0.111  1.00 4.89  ? 120 TYR A CZ  1 
ATOM   969  O  OH  . TYR A 1 125 ? 30.533 24.896  -1.475  1.00 5.80  ? 120 TYR A OH  1 
ATOM   970  N  N   . LEU A 1 126 ? 27.903 25.859  6.785   1.00 5.15  ? 121 LEU A N   1 
ATOM   971  C  CA  . LEU A 1 126 ? 27.900 25.894  8.235   1.00 6.27  ? 121 LEU A CA  1 
ATOM   972  C  C   . LEU A 1 126 ? 26.857 24.913  8.777   1.00 6.06  ? 121 LEU A C   1 
ATOM   973  O  O   . LEU A 1 126 ? 27.103 24.275  9.795   1.00 6.82  ? 121 LEU A O   1 
ATOM   974  C  CB  . LEU A 1 126 ? 27.665 27.281  8.784   1.00 7.04  ? 121 LEU A CB  1 
ATOM   975  C  CG  . LEU A 1 126 ? 28.847 28.246  8.689   1.00 8.20  ? 121 LEU A CG  1 
ATOM   976  C  CD1 . LEU A 1 126 ? 28.364 29.658  8.984   1.00 9.43  ? 121 LEU A CD1 1 
ATOM   977  C  CD2 . LEU A 1 126 ? 29.958 27.818  9.604   1.00 8.47  ? 121 LEU A CD2 1 
ATOM   978  N  N   . LYS A 1 127 ? 25.710 24.795  8.106   1.00 4.92  ? 122 LYS A N   1 
ATOM   979  C  CA  . LYS A 1 127 ? 24.751 23.757  8.437   1.00 5.52  ? 122 LYS A CA  1 
ATOM   980  C  C   . LYS A 1 127 ? 25.382 22.365  8.334   1.00 5.83  ? 122 LYS A C   1 
ATOM   981  O  O   . LYS A 1 127 ? 25.199 21.532  9.217   1.00 5.29  ? 122 LYS A O   1 
ATOM   982  C  CB  . LYS A 1 127 ? 23.514 23.827  7.535   1.00 5.64  ? 122 LYS A CB  1 
ATOM   983  C  CG  . LYS A 1 127 ? 22.483 22.731  7.787   1.00 6.91  ? 122 LYS A CG  1 
ATOM   984  C  CD  . LYS A 1 127 ? 21.357 22.782  6.715   1.00 8.48  ? 122 LYS A CD  1 
ATOM   985  C  CE  . LYS A 1 127 ? 20.649 21.452  6.588   1.00 10.93 ? 122 LYS A CE  1 
ATOM   986  N  NZ  . LYS A 1 127 ? 21.603 20.377  6.141   1.00 12.86 ? 122 LYS A NZ  1 
ATOM   987  N  N   . MET A 1 128 ? 26.110 22.107  7.239   1.00 6.12  ? 123 MET A N   1 
ATOM   988  C  CA  . MET A 1 128 ? 26.808 20.842  7.090   1.00 6.86  ? 123 MET A CA  1 
ATOM   989  C  C   . MET A 1 128 ? 27.782 20.579  8.240   1.00 5.39  ? 123 MET A C   1 
ATOM   990  O  O   . MET A 1 128 ? 27.886 19.454  8.710   1.00 4.42  ? 123 MET A O   1 
ATOM   991  C  CB  . MET A 1 128 ? 27.610 20.797  5.772   1.00 9.15  ? 123 MET A CB  1 
ATOM   992  C  CG  . MET A 1 128 ? 26.770 20.442  4.608   1.00 16.29 ? 123 MET A CG  1 
ATOM   993  S  SD  . MET A 1 128 ? 27.802 20.106  3.110   1.00 17.87 ? 123 MET A SD  1 
ATOM   994  C  CE  . MET A 1 128 ? 28.708 19.132  3.642   1.00 10.45 ? 123 MET A CE  1 
ATOM   995  N  N   . LYS A 1 129 ? 28.519 21.621  8.650   1.00 5.26  ? 124 LYS A N   1 
ATOM   996  C  CA  . LYS A 1 129 ? 29.483 21.519  9.732   1.00 4.74  ? 124 LYS A CA  1 
ATOM   997  C  C   . LYS A 1 129 ? 28.766 21.109  11.020  1.00 4.89  ? 124 LYS A C   1 
ATOM   998  O  O   . LYS A 1 129 ? 29.164 20.152  11.682  1.00 4.90  ? 124 LYS A O   1 
ATOM   999  C  CB  . LYS A 1 129 ? 30.240 22.811  9.886   1.00 5.48  ? 124 LYS A CB  1 
ATOM   1000 C  CG  . LYS A 1 129 ? 31.289 22.756  10.948  1.00 6.74  ? 124 LYS A CG  1 
ATOM   1001 C  CD  . LYS A 1 129 ? 32.161 24.000  10.940  1.00 9.31  ? 124 LYS A CD  1 
ATOM   1002 C  CE  . LYS A 1 129 ? 33.241 23.953  11.989  1.00 13.97 ? 124 LYS A CE  1 
ATOM   1003 N  NZ  . LYS A 1 129 ? 34.125 25.129  11.880  1.00 16.46 ? 124 LYS A NZ  1 
ATOM   1004 N  N   . GLY A 1 130 ? 27.631 21.749  11.294  1.00 4.67  ? 125 GLY A N   1 
ATOM   1005 C  CA  . GLY A 1 130 ? 26.774 21.371  12.410  1.00 4.61  ? 125 GLY A CA  1 
ATOM   1006 C  C   . GLY A 1 130 ? 26.321 19.916  12.294  1.00 4.44  ? 125 GLY A C   1 
ATOM   1007 O  O   . GLY A 1 130 ? 26.399 19.155  13.253  1.00 4.58  ? 125 GLY A O   1 
ATOM   1008 N  N   . ASP A 1 131 ? 25.810 19.547  11.126  1.00 4.55  ? 126 ASP A N   1 
ATOM   1009 C  CA  . ASP A 1 131 ? 25.325 18.204  10.897  1.00 4.52  ? 126 ASP A CA  1 
ATOM   1010 C  C   . ASP A 1 131 ? 26.394 17.142  11.174  1.00 4.26  ? 126 ASP A C   1 
ATOM   1011 O  O   . ASP A 1 131 ? 26.112 16.149  11.832  1.00 3.84  ? 126 ASP A O   1 
ATOM   1012 C  CB  . ASP A 1 131 ? 24.794 18.049  9.485   1.00 4.76  ? 126 ASP A CB  1 
ATOM   1013 C  CG  . ASP A 1 131 ? 23.470 18.792  9.195   1.00 5.13  ? 126 ASP A CG  1 
ATOM   1014 O  OD1 . ASP A 1 131 ? 22.751 19.126  10.161  1.00 4.87  ? 126 ASP A OD1 1 
ATOM   1015 O  OD2 . ASP A 1 131 ? 23.169 19.019  7.988   1.00 6.51  ? 126 ASP A OD2 1 
ATOM   1016 N  N   . TYR A 1 132 ? 27.625 17.347  10.701  1.00 4.83  ? 127 TYR A N   1 
ATOM   1017 C  CA  . TYR A 1 132 ? 28.606 16.276  10.799  1.00 4.99  ? 127 TYR A CA  1 
ATOM   1018 C  C   . TYR A 1 132 ? 29.189 16.220  12.213  1.00 4.99  ? 127 TYR A C   1 
ATOM   1019 O  O   . TYR A 1 132 ? 29.506 15.139  12.697  1.00 4.94  ? 127 TYR A O   1 
ATOM   1020 C  CB  . TYR A 1 132 ? 29.646 16.296  9.609   1.00 4.93  ? 127 TYR A CB  1 
ATOM   1021 C  CG  . TYR A 1 132 ? 28.992 15.728  8.362   1.00 5.06  ? 127 TYR A CG  1 
ATOM   1022 C  CD1 . TYR A 1 132 ? 28.178 16.514  7.566   1.00 5.14  ? 127 TYR A CD1 1 
ATOM   1023 C  CD2 . TYR A 1 132 ? 29.077 14.370  8.060   1.00 4.65  ? 127 TYR A CD2 1 
ATOM   1024 C  CE1 . TYR A 1 132 ? 27.511 15.984  6.466   1.00 5.82  ? 127 TYR A CE1 1 
ATOM   1025 C  CE2 . TYR A 1 132 ? 28.410 13.827  6.962   1.00 5.47  ? 127 TYR A CE2 1 
ATOM   1026 C  CZ  . TYR A 1 132 ? 27.595 14.630  6.189   1.00 5.50  ? 127 TYR A CZ  1 
ATOM   1027 O  OH  . TYR A 1 132 ? 26.926 14.105  5.100   1.00 5.86  ? 127 TYR A OH  1 
ATOM   1028 N  N   . TYR A 1 133 ? 29.249 17.355  12.920  1.00 5.85  ? 128 TYR A N   1 
ATOM   1029 C  CA  . TYR A 1 133 ? 29.526 17.288  14.345  1.00 5.38  ? 128 TYR A CA  1 
ATOM   1030 C  C   . TYR A 1 133 ? 28.393 16.616  15.125  1.00 5.04  ? 128 TYR A C   1 
ATOM   1031 O  O   . TYR A 1 133 ? 28.654 15.909  16.106  1.00 4.81  ? 128 TYR A O   1 
ATOM   1032 C  CB  . TYR A 1 133 ? 29.853 18.666  14.926  1.00 5.47  ? 128 TYR A CB  1 
ATOM   1033 C  CG  . TYR A 1 133 ? 31.290 19.085  14.746  1.00 6.78  ? 128 TYR A CG  1 
ATOM   1034 C  CD1 . TYR A 1 133 ? 32.311 18.437  15.423  1.00 6.44  ? 128 TYR A CD1 1 
ATOM   1035 C  CD2 . TYR A 1 133 ? 31.633 20.134  13.909  1.00 7.35  ? 128 TYR A CD2 1 
ATOM   1036 C  CE1 . TYR A 1 133 ? 33.630 18.830  15.285  1.00 7.46  ? 128 TYR A CE1 1 
ATOM   1037 C  CE2 . TYR A 1 133 ? 32.960 20.530  13.762  1.00 8.43  ? 128 TYR A CE2 1 
ATOM   1038 C  CZ  . TYR A 1 133 ? 33.949 19.871  14.455  1.00 9.29  ? 128 TYR A CZ  1 
ATOM   1039 O  OH  . TYR A 1 133 ? 35.287 20.224  14.332  1.00 11.33 ? 128 TYR A OH  1 
ATOM   1040 N  N   . ARG A 1 134 ? 27.139 16.836  14.702  1.00 5.03  ? 129 ARG A N   1 
ATOM   1041 C  CA  . ARG A 1 134 ? 26.017 16.157  15.320  1.00 4.78  ? 129 ARG A CA  1 
ATOM   1042 C  C   . ARG A 1 134 ? 26.149 14.635  15.136  1.00 5.01  ? 129 ARG A C   1 
ATOM   1043 O  O   . ARG A 1 134 ? 25.938 13.860  16.069  1.00 5.41  ? 129 ARG A O   1 
ATOM   1044 C  CB  . ARG A 1 134 ? 24.672 16.696  14.807  1.00 4.61  ? 129 ARG A CB  1 
ATOM   1045 C  CG  . ARG A 1 134 ? 23.450 15.894  15.271  1.00 4.25  ? 129 ARG A CG  1 
ATOM   1046 C  CD  . ARG A 1 134 ? 22.162 16.676  15.114  1.00 4.21  ? 129 ARG A CD  1 
ATOM   1047 N  NE  . ARG A 1 134 ? 21.928 17.056  13.723  1.00 3.85  ? 129 ARG A NE  1 
ATOM   1048 C  CZ  . ARG A 1 134 ? 21.262 16.335  12.835  1.00 3.94  ? 129 ARG A CZ  1 
ATOM   1049 N  NH1 . ARG A 1 134 ? 20.756 15.150  13.139  1.00 4.38  ? 129 ARG A NH1 1 
ATOM   1050 N  NH2 . ARG A 1 134 ? 21.143 16.787  11.590  1.00 3.94  ? 129 ARG A NH2 1 
ATOM   1051 N  N   . TYR A 1 135 ? 26.545 14.197  13.949  1.00 4.74  ? 130 TYR A N   1 
ATOM   1052 C  CA  . TYR A 1 135 ? 26.714 12.766  13.733  1.00 4.86  ? 130 TYR A CA  1 
ATOM   1053 C  C   . TYR A 1 135 ? 27.847 12.210  14.588  1.00 4.48  ? 130 TYR A C   1 
ATOM   1054 O  O   . TYR A 1 135 ? 27.757 11.095  15.110  1.00 5.89  ? 130 TYR A O   1 
ATOM   1055 C  CB  . TYR A 1 135 ? 26.864 12.419  12.241  1.00 4.54  ? 130 TYR A CB  1 
ATOM   1056 C  CG  . TYR A 1 135 ? 25.772 12.976  11.335  1.00 4.43  ? 130 TYR A CG  1 
ATOM   1057 C  CD1 . TYR A 1 135 ? 24.456 13.086  11.768  1.00 4.70  ? 130 TYR A CD1 1 
ATOM   1058 C  CD2 . TYR A 1 135 ? 26.056 13.377  10.053  1.00 4.54  ? 130 TYR A CD2 1 
ATOM   1059 C  CE1 . TYR A 1 135 ? 23.475 13.645  10.950  1.00 4.89  ? 130 TYR A CE1 1 
ATOM   1060 C  CE2 . TYR A 1 135 ? 25.087 13.911  9.227   1.00 5.38  ? 130 TYR A CE2 1 
ATOM   1061 C  CZ  . TYR A 1 135 ? 23.785 14.028  9.668   1.00 5.22  ? 130 TYR A CZ  1 
ATOM   1062 O  OH  . TYR A 1 135 ? 22.849 14.565  8.803   1.00 6.13  ? 130 TYR A OH  1 
ATOM   1063 N  N   . LEU A 1 136 ? 28.933 12.959  14.740  1.00 4.23  ? 131 LEU A N   1 
ATOM   1064 C  CA  . LEU A 1 136 ? 29.955 12.563  15.686  1.00 4.86  ? 131 LEU A CA  1 
ATOM   1065 C  C   . LEU A 1 136 ? 29.411 12.477  17.108  1.00 5.56  ? 131 LEU A C   1 
ATOM   1066 O  O   . LEU A 1 136 ? 29.722 11.537  17.839  1.00 5.43  ? 131 LEU A O   1 
ATOM   1067 C  CB  . LEU A 1 136 ? 31.130 13.548  15.624  1.00 4.78  ? 131 LEU A CB  1 
ATOM   1068 C  CG  . LEU A 1 136 ? 31.987 13.457  14.349  1.00 5.05  ? 131 LEU A CG  1 
ATOM   1069 C  CD1 . LEU A 1 136 ? 33.101 14.515  14.346  1.00 6.06  ? 131 LEU A CD1 1 
ATOM   1070 C  CD2 . LEU A 1 136 ? 32.627 12.075  14.194  1.00 5.20  ? 131 LEU A CD2 1 
ATOM   1071 N  N   . ALA A 1 137 ? 28.588 13.456  17.494  1.00 5.47  ? 132 ALA A N   1 
ATOM   1072 C  CA  . ALA A 1 137 ? 28.006 13.486  18.834  1.00 5.87  ? 132 ALA A CA  1 
ATOM   1073 C  C   . ALA A 1 137 ? 27.145 12.263  19.137  1.00 6.44  ? 132 ALA A C   1 
ATOM   1074 O  O   . ALA A 1 137 ? 27.108 11.797  20.278  1.00 8.14  ? 132 ALA A O   1 
ATOM   1075 C  CB  . ALA A 1 137 ? 27.178 14.752  19.036  1.00 5.86  ? 132 ALA A CB  1 
ATOM   1076 N  N   . GLU A 1 138 ? 26.431 11.767  18.120  1.00 7.12  ? 133 GLU A N   1 
ATOM   1077 C  CA  . GLU A 1 138 ? 25.572 10.613  18.278  1.00 7.22  ? 133 GLU A CA  1 
ATOM   1078 C  C   . GLU A 1 138 ? 26.344 9.400   18.819  1.00 7.26  ? 133 GLU A C   1 
ATOM   1079 O  O   . GLU A 1 138 ? 25.755 8.551   19.483  1.00 7.36  ? 133 GLU A O   1 
ATOM   1080 C  CB  . GLU A 1 138 ? 24.897 10.261  16.948  1.00 7.68  ? 133 GLU A CB  1 
ATOM   1081 C  CG  . GLU A 1 138 ? 23.741 11.148  16.567  1.00 8.65  ? 133 GLU A CG  1 
ATOM   1082 C  CD  . GLU A 1 138 ? 23.129 10.846  15.209  1.00 11.13 ? 133 GLU A CD  1 
ATOM   1083 O  OE1 . GLU A 1 138 ? 23.710 10.106  14.385  1.00 10.06 ? 133 GLU A OE1 1 
ATOM   1084 O  OE2 . GLU A 1 138 ? 22.001 11.302  15.007  1.00 11.11 ? 133 GLU A OE2 1 
ATOM   1085 N  N   . VAL A 1 139 ? 27.620 9.264   18.454  1.00 6.24  ? 134 VAL A N   1 
ATOM   1086 C  CA  . VAL A 1 139 ? 28.411 8.100   18.850  1.00 8.14  ? 134 VAL A CA  1 
ATOM   1087 C  C   . VAL A 1 139 ? 29.461 8.402   19.906  1.00 10.87 ? 134 VAL A C   1 
ATOM   1088 O  O   . VAL A 1 139 ? 30.181 7.499   20.344  1.00 12.58 ? 134 VAL A O   1 
ATOM   1089 C  CB  . VAL A 1 139 ? 29.073 7.411   17.639  1.00 7.43  ? 134 VAL A CB  1 
ATOM   1090 C  CG1 . VAL A 1 139 ? 28.020 7.070   16.592  1.00 7.21  ? 134 VAL A CG1 1 
ATOM   1091 C  CG2 . VAL A 1 139 ? 30.217 8.243   17.019  1.00 7.93  ? 134 VAL A CG2 1 
ATOM   1092 N  N   . ALA A 1 140 ? 29.527 9.659   20.356  1.00 10.76 ? 135 ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 140 ? 30.565 10.087  21.277  1.00 11.51 ? 135 ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 140 ? 30.186 9.726   22.712  1.00 14.58 ? 135 ALA A C   1 
ATOM   1095 O  O   . ALA A 1 140 ? 29.012 9.764   23.069  1.00 15.01 ? 135 ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 140 ? 30.797 11.588  21.151  1.00 11.01 ? 135 ALA A CB  1 
ATOM   1097 N  N   . THR A 1 141 ? 31.185 9.336   23.506  1.00 17.63 ? 136 THR A N   1 
ATOM   1098 C  CA  . THR A 1 141 ? 30.955 9.003   24.905  1.00 29.39 ? 136 THR A CA  1 
ATOM   1099 C  C   . THR A 1 141 ? 31.981 9.682   25.809  1.00 48.54 ? 136 THR A C   1 
ATOM   1100 O  O   . THR A 1 141 ? 33.161 9.332   25.790  1.00 51.63 ? 136 THR A O   1 
ATOM   1101 C  CB  . THR A 1 141 ? 30.927 7.460   25.130  1.00 30.66 ? 136 THR A CB  1 
ATOM   1102 O  OG1 . THR A 1 141 ? 32.092 6.812   24.599  1.00 33.27 ? 136 THR A OG1 1 
ATOM   1103 C  CG2 . THR A 1 141 ? 29.726 6.822   24.500  1.00 28.57 ? 136 THR A CG2 1 
ATOM   1104 N  N   . GLY A 1 142 ? 31.516 10.668  26.589  1.00 58.52 ? 137 GLY A N   1 
ATOM   1105 C  CA  . GLY A 1 142 ? 32.307 11.238  27.671  1.00 60.76 ? 137 GLY A CA  1 
ATOM   1106 C  C   . GLY A 1 142 ? 32.408 12.761  27.654  1.00 58.63 ? 137 GLY A C   1 
ATOM   1107 O  O   . GLY A 1 142 ? 31.407 13.453  27.461  1.00 57.90 ? 137 GLY A O   1 
ATOM   1108 N  N   . ASP A 1 143 ? 33.623 13.274  27.892  1.00 66.98 ? 138 ASP A N   1 
ATOM   1109 C  CA  . ASP A 1 143 ? 33.875 14.707  27.878  1.00 65.96 ? 138 ASP A CA  1 
ATOM   1110 C  C   . ASP A 1 143 ? 34.180 15.174  26.458  1.00 61.12 ? 138 ASP A C   1 
ATOM   1111 O  O   . ASP A 1 143 ? 33.779 16.264  26.053  1.00 49.66 ? 138 ASP A O   1 
ATOM   1112 C  CB  . ASP A 1 143 ? 35.031 15.106  28.824  1.00 71.60 ? 138 ASP A CB  1 
ATOM   1113 C  CG  . ASP A 1 143 ? 34.697 15.073  30.309  1.00 54.42 ? 138 ASP A CG  1 
ATOM   1114 O  OD1 . ASP A 1 143 ? 33.619 15.587  30.690  1.00 55.10 ? 138 ASP A OD1 1 
ATOM   1115 O  OD2 . ASP A 1 143 ? 35.523 14.567  31.085  1.00 44.21 ? 138 ASP A OD2 1 
ATOM   1116 N  N   . ASP A 1 144 ? 34.867 14.343  25.671  1.00 49.92 ? 139 ASP A N   1 
ATOM   1117 C  CA  . ASP A 1 144 ? 35.023 14.716  24.280  1.00 47.90 ? 139 ASP A CA  1 
ATOM   1118 C  C   . ASP A 1 144 ? 33.625 14.857  23.663  1.00 28.40 ? 139 ASP A C   1 
ATOM   1119 O  O   . ASP A 1 144 ? 33.423 15.665  22.769  1.00 21.78 ? 139 ASP A O   1 
ATOM   1120 C  CB  . ASP A 1 144 ? 35.945 13.759  23.528  1.00 59.96 ? 139 ASP A CB  1 
ATOM   1121 C  CG  . ASP A 1 144 ? 36.805 14.491  22.526  1.00 70.73 ? 139 ASP A CG  1 
ATOM   1122 O  OD1 . ASP A 1 144 ? 37.618 15.345  22.953  1.00 64.95 ? 139 ASP A OD1 1 
ATOM   1123 O  OD2 . ASP A 1 144 ? 36.656 14.231  21.317  1.00 87.43 ? 139 ASP A OD2 1 
ATOM   1124 N  N   . LYS A 1 145 ? 32.628 14.137  24.188  1.00 19.53 ? 140 LYS A N   1 
ATOM   1125 C  CA  . LYS A 1 145 ? 31.257 14.380  23.777  1.00 20.54 ? 140 LYS A CA  1 
ATOM   1126 C  C   . LYS A 1 145 ? 30.866 15.849  23.956  1.00 19.65 ? 140 LYS A C   1 
ATOM   1127 O  O   . LYS A 1 145 ? 30.187 16.426  23.102  1.00 14.78 ? 140 LYS A O   1 
ATOM   1128 C  CB  . LYS A 1 145 ? 30.276 13.498  24.544  1.00 23.79 ? 140 LYS A CB  1 
ATOM   1129 C  CG  . LYS A 1 145 ? 28.954 13.317  23.816  1.00 28.37 ? 140 LYS A CG  1 
ATOM   1130 C  CD  . LYS A 1 145 ? 27.936 12.593  24.655  1.00 38.93 ? 140 LYS A CD  1 
ATOM   1131 C  CE  . LYS A 1 145 ? 26.627 12.510  23.963  1.00 34.08 ? 140 LYS A CE  1 
ATOM   1132 N  NZ  . LYS A 1 145 ? 25.580 12.032  24.895  1.00 41.08 ? 140 LYS A NZ  1 
ATOM   1133 N  N   . LYS A 1 146 ? 31.266 16.451  25.080  1.00 17.75 ? 141 LYS A N   1 
ATOM   1134 C  CA  . LYS A 1 146 ? 30.896 17.837  25.330  1.00 18.78 ? 141 LYS A CA  1 
ATOM   1135 C  C   . LYS A 1 146 ? 31.454 18.800  24.300  1.00 14.96 ? 141 LYS A C   1 
ATOM   1136 O  O   . LYS A 1 146 ? 30.744 19.716  23.898  1.00 12.78 ? 141 LYS A O   1 
ATOM   1137 C  CB  . LYS A 1 146 ? 31.317 18.333  26.732  1.00 19.55 ? 141 LYS A CB  1 
ATOM   1138 C  CG  . LYS A 1 146 ? 30.509 17.694  27.791  1.00 19.01 ? 141 LYS A CG  1 
ATOM   1139 C  CD  . LYS A 1 146 ? 30.905 18.205  29.206  1.00 25.27 ? 141 LYS A CD  1 
ATOM   1140 C  CE  . LYS A 1 146 ? 30.318 17.334  30.273  1.00 31.00 ? 141 LYS A CE  1 
ATOM   1141 N  NZ  . LYS A 1 146 ? 30.469 17.986  31.609  1.00 29.90 ? 141 LYS A NZ  1 
ATOM   1142 N  N   . ARG A 1 147 ? 32.739 18.634  23.934  1.00 13.74 ? 142 ARG A N   1 
ATOM   1143 C  CA  . ARG A 1 147 ? 33.359 19.553  22.996  1.00 14.43 ? 142 ARG A CA  1 
ATOM   1144 C  C   . ARG A 1 147 ? 32.761 19.348  21.603  1.00 9.90  ? 142 ARG A C   1 
ATOM   1145 O  O   . ARG A 1 147 ? 32.571 20.313  20.875  1.00 9.37  ? 142 ARG A O   1 
ATOM   1146 C  CB  . ARG A 1 147 ? 34.910 19.475  22.983  1.00 19.25 ? 142 ARG A CB  1 
ATOM   1147 C  CG  . ARG A 1 147 ? 35.532 20.578  23.911  1.00 28.02 ? 142 ARG A CG  1 
ATOM   1148 C  CD  . ARG A 1 147 ? 37.053 20.589  23.968  1.00 34.64 ? 142 ARG A CD  1 
ATOM   1149 N  NE  . ARG A 1 147 ? 37.556 19.476  24.770  1.00 31.70 ? 142 ARG A NE  1 
ATOM   1150 C  CZ  . ARG A 1 147 ? 37.845 19.556  26.066  1.00 34.96 ? 142 ARG A CZ  1 
ATOM   1151 N  NH1 . ARG A 1 147 ? 38.001 20.727  26.668  1.00 26.81 ? 142 ARG A NH1 1 
ATOM   1152 N  NH2 . ARG A 1 147 ? 37.951 18.434  26.779  1.00 38.13 ? 142 ARG A NH2 1 
ATOM   1153 N  N   . ILE A 1 148 ? 32.415 18.101  21.257  1.00 9.67  ? 143 ILE A N   1 
ATOM   1154 C  CA  . ILE A 1 148 ? 31.782 17.833  19.980  1.00 8.82  ? 143 ILE A CA  1 
ATOM   1155 C  C   . ILE A 1 148 ? 30.409 18.508  19.904  1.00 9.68  ? 143 ILE A C   1 
ATOM   1156 O  O   . ILE A 1 148 ? 30.071 19.092  18.887  1.00 8.33  ? 143 ILE A O   1 
ATOM   1157 C  CB  . ILE A 1 148 ? 31.695 16.337  19.746  1.00 11.53 ? 143 ILE A CB  1 
ATOM   1158 C  CG1 . ILE A 1 148 ? 33.108 15.710  19.649  1.00 14.83 ? 143 ILE A CG1 1 
ATOM   1159 C  CG2 . ILE A 1 148 ? 30.829 16.027  18.536  1.00 11.36 ? 143 ILE A CG2 1 
ATOM   1160 C  CD1 . ILE A 1 148 ? 33.109 14.201  19.737  1.00 18.95 ? 143 ILE A CD1 1 
ATOM   1161 N  N   . ILE A 1 149 ? 29.607 18.384  20.971  1.00 7.64  ? 144 ILE A N   1 
ATOM   1162 C  CA  . ILE A 1 149 ? 28.303 19.020  21.043  1.00 9.28  ? 144 ILE A CA  1 
ATOM   1163 C  C   . ILE A 1 149 ? 28.457 20.527  20.894  1.00 8.50  ? 144 ILE A C   1 
ATOM   1164 O  O   . ILE A 1 149 ? 27.683 21.169  20.191  1.00 7.60  ? 144 ILE A O   1 
ATOM   1165 C  CB  . ILE A 1 149 ? 27.591 18.609  22.331  1.00 10.41 ? 144 ILE A CB  1 
ATOM   1166 C  CG1 . ILE A 1 149 ? 27.154 17.128  22.235  1.00 12.80 ? 144 ILE A CG1 1 
ATOM   1167 C  CG2 . ILE A 1 149 ? 26.396 19.508  22.674  1.00 11.76 ? 144 ILE A CG2 1 
ATOM   1168 C  CD1 . ILE A 1 149 ? 26.600 16.530  23.556  1.00 13.94 ? 144 ILE A CD1 1 
ATOM   1169 N  N   . ASP A 1 150 ? 29.439 21.110  21.585  1.00 7.19  ? 145 ASP A N   1 
ATOM   1170 C  CA  . ASP A 1 150 ? 29.626 22.544  21.483  1.00 9.39  ? 145 ASP A CA  1 
ATOM   1171 C  C   . ASP A 1 150 ? 30.045 22.966  20.073  1.00 7.58  ? 145 ASP A C   1 
ATOM   1172 O  O   . ASP A 1 150 ? 29.633 24.032  19.595  1.00 6.71  ? 145 ASP A O   1 
ATOM   1173 C  CB  . ASP A 1 150 ? 30.618 23.092  22.506  1.00 12.81 ? 145 ASP A CB  1 
ATOM   1174 C  CG  . ASP A 1 150 ? 30.386 24.602  22.768  1.00 21.12 ? 145 ASP A CG  1 
ATOM   1175 O  OD1 . ASP A 1 150 ? 29.168 25.037  22.915  1.00 26.75 ? 145 ASP A OD1 1 
ATOM   1176 O  OD2 . ASP A 1 150 ? 31.357 25.326  22.850  1.00 28.50 ? 145 ASP A OD2 1 
ATOM   1177 N  N   . SER A 1 151 ? 30.885 22.152  19.411  1.00 6.67  ? 146 SER A N   1 
ATOM   1178 C  CA  . SER A 1 151 ? 31.226 22.425  18.020  1.00 6.42  ? 146 SER A CA  1 
ATOM   1179 C  C   . SER A 1 151 ? 30.008 22.407  17.095  1.00 5.81  ? 146 SER A C   1 
ATOM   1180 O  O   . SER A 1 151 ? 29.844 23.289  16.247  1.00 7.12  ? 146 SER A O   1 
ATOM   1181 C  CB  . SER A 1 151 ? 32.263 21.437  17.520  1.00 8.30  ? 146 SER A CB  1 
ATOM   1182 O  OG  . SER A 1 151 ? 33.504 21.711  18.153  1.00 9.33  ? 146 SER A OG  1 
ATOM   1183 N  N   . ALA A 1 152 ? 29.153 21.404  17.253  1.00 5.70  ? 147 ALA A N   1 
ATOM   1184 C  CA  . ALA A 1 152 ? 27.915 21.388  16.474  1.00 6.30  ? 147 ALA A CA  1 
ATOM   1185 C  C   . ALA A 1 152 ? 27.085 22.646  16.754  1.00 7.32  ? 147 ALA A C   1 
ATOM   1186 O  O   . ALA A 1 152 ? 26.607 23.314  15.828  1.00 6.58  ? 147 ALA A O   1 
ATOM   1187 C  CB  . ALA A 1 152 ? 27.115 20.117  16.747  1.00 6.28  ? 147 ALA A CB  1 
ATOM   1188 N  N   . ARG A 1 153 ? 26.869 22.958  18.036  1.00 7.24  ? 148 ARG A N   1 
ATOM   1189 C  CA  A ARG A 1 153 ? 26.039 24.094  18.420  0.50 8.18  ? 148 ARG A CA  1 
ATOM   1190 C  CA  B ARG A 1 153 ? 26.033 24.089  18.415  0.50 7.23  ? 148 ARG A CA  1 
ATOM   1191 C  C   . ARG A 1 153 ? 26.579 25.391  17.820  1.00 7.68  ? 148 ARG A C   1 
ATOM   1192 O  O   . ARG A 1 153 ? 25.838 26.237  17.350  1.00 6.68  ? 148 ARG A O   1 
ATOM   1193 C  CB  A ARG A 1 153 ? 25.990 24.244  19.951  0.50 9.47  ? 148 ARG A CB  1 
ATOM   1194 C  CB  B ARG A 1 153 ? 25.970 24.163  19.953  0.50 7.00  ? 148 ARG A CB  1 
ATOM   1195 C  CG  A ARG A 1 153 ? 25.207 25.493  20.412  0.50 10.57 ? 148 ARG A CG  1 
ATOM   1196 C  CG  B ARG A 1 153 ? 24.919 25.136  20.512  0.50 6.71  ? 148 ARG A CG  1 
ATOM   1197 C  CD  A ARG A 1 153 ? 25.573 25.954  21.809  0.50 11.71 ? 148 ARG A CD  1 
ATOM   1198 C  CD  B ARG A 1 153 ? 25.166 25.455  21.981  0.50 6.07  ? 148 ARG A CD  1 
ATOM   1199 N  NE  A ARG A 1 153 ? 26.968 26.373  21.899  0.50 11.58 ? 148 ARG A NE  1 
ATOM   1200 N  NE  B ARG A 1 153 ? 25.175 24.262  22.811  0.50 5.67  ? 148 ARG A NE  1 
ATOM   1201 C  CZ  A ARG A 1 153 ? 27.516 27.384  21.234  0.50 11.15 ? 148 ARG A CZ  1 
ATOM   1202 C  CZ  B ARG A 1 153 ? 24.081 23.642  23.207  0.50 5.06  ? 148 ARG A CZ  1 
ATOM   1203 N  NH1 A ARG A 1 153 ? 26.783 28.276  20.579  0.50 10.15 ? 148 ARG A NH1 1 
ATOM   1204 N  NH1 B ARG A 1 153 ? 22.891 24.197  23.066  0.50 4.19  ? 148 ARG A NH1 1 
ATOM   1205 N  NH2 A ARG A 1 153 ? 28.838 27.492  21.217  0.50 11.31 ? 148 ARG A NH2 1 
ATOM   1206 N  NH2 B ARG A 1 153 ? 24.186 22.446  23.777  0.50 4.88  ? 148 ARG A NH2 1 
ATOM   1207 N  N   . SER A 1 154 ? 27.901 25.560  17.870  1.00 8.52  ? 149 SER A N   1 
ATOM   1208 C  CA  . SER A 1 154 ? 28.524 26.778  17.403  1.00 9.40  ? 149 SER A CA  1 
ATOM   1209 C  C   . SER A 1 154 ? 28.321 26.964  15.901  1.00 8.43  ? 149 SER A C   1 
ATOM   1210 O  O   . SER A 1 154 ? 28.043 28.065  15.432  1.00 8.32  ? 149 SER A O   1 
ATOM   1211 C  CB  . SER A 1 154 ? 30.005 26.736  17.763  1.00 12.39 ? 149 SER A CB  1 
ATOM   1212 O  OG  . SER A 1 154 ? 30.629 27.930  17.346  1.00 18.95 ? 149 SER A OG  1 
ATOM   1213 N  N   . ALA A 1 155 ? 28.430 25.869  15.153  1.00 6.42  ? 150 ALA A N   1 
ATOM   1214 C  CA  . ALA A 1 155 ? 28.285 25.945  13.713  1.00 6.61  ? 150 ALA A CA  1 
ATOM   1215 C  C   . ALA A 1 155 ? 26.840 26.264  13.365  1.00 6.29  ? 150 ALA A C   1 
ATOM   1216 O  O   . ALA A 1 155 ? 26.577 27.137  12.522  1.00 6.33  ? 150 ALA A O   1 
ATOM   1217 C  CB  . ALA A 1 155 ? 28.732 24.656  13.056  1.00 6.83  ? 150 ALA A CB  1 
ATOM   1218 N  N   . TYR A 1 156 ? 25.910 25.549  14.008  1.00 5.71  ? 151 TYR A N   1 
ATOM   1219 C  CA  . TYR A 1 156 ? 24.507 25.828  13.766  1.00 5.78  ? 151 TYR A CA  1 
ATOM   1220 C  C   . TYR A 1 156 ? 24.159 27.280  14.097  1.00 7.10  ? 151 TYR A C   1 
ATOM   1221 O  O   . TYR A 1 156 ? 23.398 27.918  13.373  1.00 7.91  ? 151 TYR A O   1 
ATOM   1222 C  CB  . TYR A 1 156 ? 23.615 24.914  14.540  1.00 5.69  ? 151 TYR A CB  1 
ATOM   1223 C  CG  . TYR A 1 156 ? 23.520 23.494  14.029  1.00 5.07  ? 151 TYR A CG  1 
ATOM   1224 C  CD1 . TYR A 1 156 ? 23.254 23.226  12.683  1.00 5.24  ? 151 TYR A CD1 1 
ATOM   1225 C  CD2 . TYR A 1 156 ? 23.589 22.427  14.894  1.00 5.28  ? 151 TYR A CD2 1 
ATOM   1226 C  CE1 . TYR A 1 156 ? 23.083 21.917  12.225  1.00 5.13  ? 151 TYR A CE1 1 
ATOM   1227 C  CE2 . TYR A 1 156 ? 23.386 21.118  14.455  1.00 5.60  ? 151 TYR A CE2 1 
ATOM   1228 C  CZ  . TYR A 1 156 ? 23.161 20.864  13.110  1.00 5.95  ? 151 TYR A CZ  1 
ATOM   1229 O  OH  . TYR A 1 156 ? 22.981 19.553  12.651  1.00 5.76  ? 151 TYR A OH  1 
ATOM   1230 N  N   . GLN A 1 157 ? 24.677 27.780  15.218  1.00 7.43  ? 152 GLN A N   1 
ATOM   1231 C  CA  . GLN A 1 157 ? 24.345 29.125  15.674  1.00 8.84  ? 152 GLN A CA  1 
ATOM   1232 C  C   . GLN A 1 157 ? 24.835 30.189  14.693  1.00 9.44  ? 152 GLN A C   1 
ATOM   1233 O  O   . GLN A 1 157 ? 24.145 31.167  14.419  1.00 8.19  ? 152 GLN A O   1 
ATOM   1234 C  CB  . GLN A 1 157 ? 24.943 29.405  17.086  1.00 11.02 ? 152 GLN A CB  1 
ATOM   1235 C  CG  . GLN A 1 157 ? 24.445 30.739  17.665  1.00 15.22 ? 152 GLN A CG  1 
ATOM   1236 C  CD  . GLN A 1 157 ? 22.943 30.686  17.735  1.00 17.17 ? 152 GLN A CD  1 
ATOM   1237 O  OE1 . GLN A 1 157 ? 22.405 29.859  18.466  1.00 19.83 ? 152 GLN A OE1 1 
ATOM   1238 N  NE2 . GLN A 1 157 ? 22.239 31.550  16.987  1.00 18.71 ? 152 GLN A NE2 1 
ATOM   1239 N  N   . GLU A 1 158 ? 26.067 30.025  14.203  1.00 9.08  ? 153 GLU A N   1 
ATOM   1240 C  CA  . GLU A 1 158 ? 26.613 30.963  13.231  1.00 9.80  ? 153 GLU A CA  1 
ATOM   1241 C  C   . GLU A 1 158 ? 25.754 30.948  11.960  1.00 8.26  ? 153 GLU A C   1 
ATOM   1242 O  O   . GLU A 1 158 ? 25.458 32.011  11.384  1.00 7.01  ? 153 GLU A O   1 
ATOM   1243 C  CB  . GLU A 1 158 ? 28.096 30.623  12.951  1.00 12.02 ? 153 GLU A CB  1 
ATOM   1244 C  CG  . GLU A 1 158 ? 28.741 31.520  11.939  1.00 19.55 ? 153 GLU A CG  1 
ATOM   1245 C  CD  . GLU A 1 158 ? 30.230 31.349  11.647  1.00 27.14 ? 153 GLU A CD  1 
ATOM   1246 O  OE1 . GLU A 1 158 ? 30.930 30.561  12.332  1.00 29.70 ? 153 GLU A OE1 1 
ATOM   1247 O  OE2 . GLU A 1 158 ? 30.686 32.048  10.713  1.00 37.00 ? 153 GLU A OE2 1 
ATOM   1248 N  N   . ALA A 1 159 ? 25.349 29.742  11.535  1.00 6.84  ? 154 ALA A N   1 
ATOM   1249 C  CA  . ALA A 1 159 ? 24.497 29.593  10.363  1.00 6.58  ? 154 ALA A CA  1 
ATOM   1250 C  C   . ALA A 1 159 ? 23.147 30.266  10.592  1.00 6.21  ? 154 ALA A C   1 
ATOM   1251 O  O   . ALA A 1 159 ? 22.619 30.912  9.697   1.00 6.79  ? 154 ALA A O   1 
ATOM   1252 C  CB  . ALA A 1 159 ? 24.300 28.108  9.995   1.00 6.48  ? 154 ALA A CB  1 
ATOM   1253 N  N   . MET A 1 160 ? 22.564 30.073  11.783  1.00 7.00  ? 155 MET A N   1 
ATOM   1254 C  CA  . MET A 1 160 ? 21.263 30.656  12.094  1.00 7.48  ? 155 MET A CA  1 
ATOM   1255 C  C   . MET A 1 160 ? 21.346 32.182  12.027  1.00 7.19  ? 155 MET A C   1 
ATOM   1256 O  O   . MET A 1 160 ? 20.463 32.850  11.491  1.00 7.78  ? 155 MET A O   1 
ATOM   1257 C  CB  . MET A 1 160 ? 20.791 30.259  13.476  1.00 8.46  ? 155 MET A CB  1 
ATOM   1258 C  CG  . MET A 1 160 ? 20.388 28.832  13.586  1.00 10.38 ? 155 MET A CG  1 
ATOM   1259 S  SD  . MET A 1 160 ? 18.803 28.371  12.835  1.00 13.83 ? 155 MET A SD  1 
ATOM   1260 C  CE  . MET A 1 160 ? 17.765 29.580  13.586  1.00 18.08 ? 155 MET A CE  1 
ATOM   1261 N  N   . ASP A 1 161 ? 22.396 32.747  12.619  1.00 7.97  ? 156 ASP A N   1 
ATOM   1262 C  CA  . ASP A 1 161 ? 22.499 34.201  12.692  1.00 10.43 ? 156 ASP A CA  1 
ATOM   1263 C  C   . ASP A 1 161 ? 22.535 34.796  11.277  1.00 11.02 ? 156 ASP A C   1 
ATOM   1264 O  O   . ASP A 1 161 ? 21.839 35.781  10.994  1.00 8.97  ? 156 ASP A O   1 
ATOM   1265 C  CB  . ASP A 1 161 ? 23.728 34.626  13.514  1.00 13.05 ? 156 ASP A CB  1 
ATOM   1266 C  CG  . ASP A 1 161 ? 23.743 34.260  14.981  1.00 15.18 ? 156 ASP A CG  1 
ATOM   1267 O  OD1 . ASP A 1 161 ? 22.681 34.018  15.535  1.00 15.69 ? 156 ASP A OD1 1 
ATOM   1268 O  OD2 . ASP A 1 161 ? 24.848 34.198  15.565  1.00 15.51 ? 156 ASP A OD2 1 
ATOM   1269 N  N   . ILE A 1 162 ? 23.330 34.179  10.377  1.00 8.80  ? 157 ILE A N   1 
ATOM   1270 C  CA  . ILE A 1 162 ? 23.426 34.649  9.003   1.00 8.61  ? 157 ILE A CA  1 
ATOM   1271 C  C   . ILE A 1 162 ? 22.082 34.477  8.289   1.00 7.48  ? 157 ILE A C   1 
ATOM   1272 O  O   . ILE A 1 162 ? 21.623 35.379  7.598   1.00 8.10  ? 157 ILE A O   1 
ATOM   1273 C  CB  . ILE A 1 162 ? 24.566 33.945  8.210   1.00 8.53  ? 157 ILE A CB  1 
ATOM   1274 C  CG1 . ILE A 1 162 ? 25.925 34.195  8.836   1.00 10.14 ? 157 ILE A CG1 1 
ATOM   1275 C  CG2 . ILE A 1 162 ? 24.536 34.376  6.747   1.00 8.51  ? 157 ILE A CG2 1 
ATOM   1276 C  CD1 . ILE A 1 162 ? 26.998 33.236  8.306   1.00 12.58 ? 157 ILE A CD1 1 
ATOM   1277 N  N   . SER A 1 163 ? 21.455 33.306  8.447   1.00 6.77  ? 158 SER A N   1 
ATOM   1278 C  CA  . SER A 1 163 ? 20.225 33.013  7.728   1.00 8.46  ? 158 SER A CA  1 
ATOM   1279 C  C   . SER A 1 163 ? 19.125 33.999  8.134   1.00 8.44  ? 158 SER A C   1 
ATOM   1280 O  O   . SER A 1 163 ? 18.305 34.399  7.307   1.00 8.75  ? 158 SER A O   1 
ATOM   1281 C  CB  . SER A 1 163 ? 19.758 31.556  7.927   1.00 8.74  ? 158 SER A CB  1 
ATOM   1282 O  OG  . SER A 1 163 ? 19.279 31.304  9.231   1.00 11.93 ? 158 SER A OG  1 
ATOM   1283 N  N   . LYS A 1 164 ? 19.093 34.353  9.427   1.00 9.04  ? 159 LYS A N   1 
ATOM   1284 C  CA  . LYS A 1 164 ? 18.069 35.263  9.908   1.00 10.67 ? 159 LYS A CA  1 
ATOM   1285 C  C   . LYS A 1 164 ? 18.272 36.662  9.352   1.00 11.66 ? 159 LYS A C   1 
ATOM   1286 O  O   . LYS A 1 164 ? 17.307 37.365  9.073   1.00 11.92 ? 159 LYS A O   1 
ATOM   1287 C  CB  . LYS A 1 164 ? 18.028 35.253  11.433  1.00 14.44 ? 159 LYS A CB  1 
ATOM   1288 C  CG  . LYS A 1 164 ? 17.378 33.974  11.981  1.00 21.07 ? 159 LYS A CG  1 
ATOM   1289 C  CD  . LYS A 1 164 ? 17.151 34.080  13.476  1.00 26.98 ? 159 LYS A CD  1 
ATOM   1290 C  CE  . LYS A 1 164 ? 16.229 33.043  14.002  1.00 37.62 ? 159 LYS A CE  1 
ATOM   1291 N  NZ  . LYS A 1 164 ? 15.834 33.361  15.407  1.00 45.00 ? 159 LYS A NZ  1 
ATOM   1292 N  N   . LYS A 1 165 ? 19.528 37.070  9.192   1.00 10.05 ? 160 LYS A N   1 
ATOM   1293 C  CA  . LYS A 1 165 ? 19.836 38.380  8.648   1.00 13.70 ? 160 LYS A CA  1 
ATOM   1294 C  C   . LYS A 1 165 ? 19.644 38.449  7.138   1.00 13.04 ? 160 LYS A C   1 
ATOM   1295 O  O   . LYS A 1 165 ? 19.251 39.494  6.627   1.00 11.56 ? 160 LYS A O   1 
ATOM   1296 C  CB  . LYS A 1 165 ? 21.266 38.787  8.954   1.00 17.30 ? 160 LYS A CB  1 
ATOM   1297 C  CG  . LYS A 1 165 ? 21.479 39.213  10.366  1.00 28.64 ? 160 LYS A CG  1 
ATOM   1298 C  CD  . LYS A 1 165 ? 22.883 39.788  10.578  1.00 42.14 ? 160 LYS A CD  1 
ATOM   1299 C  CE  . LYS A 1 165 ? 23.191 40.008  12.051  1.00 49.79 ? 160 LYS A CE  1 
ATOM   1300 N  NZ  . LYS A 1 165 ? 24.350 40.929  12.231  1.00 52.00 ? 160 LYS A NZ  1 
ATOM   1301 N  N   . GLU A 1 166 ? 19.954 37.355  6.429   1.00 9.76  ? 161 GLU A N   1 
ATOM   1302 C  CA  . GLU A 1 166 ? 20.174 37.433  4.994   1.00 10.11 ? 161 GLU A CA  1 
ATOM   1303 C  C   . GLU A 1 166 ? 19.164 36.715  4.101   1.00 10.50 ? 161 GLU A C   1 
ATOM   1304 O  O   . GLU A 1 166 ? 19.220 36.898  2.890   1.00 12.93 ? 161 GLU A O   1 
ATOM   1305 C  CB  . GLU A 1 166 ? 21.594 36.896  4.640   1.00 12.89 ? 161 GLU A CB  1 
ATOM   1306 C  CG  . GLU A 1 166 ? 22.706 37.647  5.303   1.00 14.09 ? 161 GLU A CG  1 
ATOM   1307 C  CD  . GLU A 1 166 ? 22.811 39.096  4.873   1.00 22.40 ? 161 GLU A CD  1 
ATOM   1308 O  OE1 . GLU A 1 166 ? 22.263 39.443  3.799   1.00 26.48 ? 161 GLU A OE1 1 
ATOM   1309 O  OE2 . GLU A 1 166 ? 23.422 39.887  5.625   1.00 29.28 ? 161 GLU A OE2 1 
ATOM   1310 N  N   . MET A 1 167 ? 18.292 35.883  4.678   1.00 9.02  ? 162 MET A N   1 
ATOM   1311 C  CA  . MET A 1 167 ? 17.386 35.040  3.911   1.00 8.81  ? 162 MET A CA  1 
ATOM   1312 C  C   . MET A 1 167 ? 15.968 35.216  4.416   1.00 10.51 ? 162 MET A C   1 
ATOM   1313 O  O   . MET A 1 167 ? 15.770 35.464  5.602   1.00 9.12  ? 162 MET A O   1 
ATOM   1314 C  CB  . MET A 1 167 ? 17.714 33.527  4.035   1.00 10.62 ? 162 MET A CB  1 
ATOM   1315 C  CG  . MET A 1 167 ? 19.067 33.192  3.476   1.00 11.90 ? 162 MET A CG  1 
ATOM   1316 S  SD  . MET A 1 167 ? 19.519 31.526  4.052   1.00 15.44 ? 162 MET A SD  1 
ATOM   1317 C  CE  . MET A 1 167 ? 20.971 31.295  3.148   1.00 19.19 ? 162 MET A CE  1 
ATOM   1318 N  N   . PRO A 1 168 ? 14.962 35.064  3.529   1.00 10.19 ? 163 PRO A N   1 
ATOM   1319 C  CA  . PRO A 1 168 ? 13.558 35.098  3.940   1.00 11.33 ? 163 PRO A CA  1 
ATOM   1320 C  C   . PRO A 1 168 ? 13.235 33.865  4.765   1.00 10.29 ? 163 PRO A C   1 
ATOM   1321 O  O   . PRO A 1 168 ? 13.914 32.847  4.636   1.00 10.17 ? 163 PRO A O   1 
ATOM   1322 C  CB  . PRO A 1 168 ? 12.786 35.078  2.623   1.00 11.91 ? 163 PRO A CB  1 
ATOM   1323 C  CG  . PRO A 1 168 ? 13.707 34.528  1.637   1.00 14.40 ? 163 PRO A CG  1 
ATOM   1324 C  CD  . PRO A 1 168 ? 15.118 34.844  2.082   1.00 13.92 ? 163 PRO A CD  1 
ATOM   1325 N  N   . PRO A 1 169 ? 12.215 33.946  5.636   1.00 11.45 ? 164 PRO A N   1 
ATOM   1326 C  CA  . PRO A 1 169 ? 11.831 32.820  6.492   1.00 10.94 ? 164 PRO A CA  1 
ATOM   1327 C  C   . PRO A 1 169 ? 11.437 31.543  5.771   1.00 10.88 ? 164 PRO A C   1 
ATOM   1328 O  O   . PRO A 1 169 ? 11.483 30.477  6.381   1.00 10.86 ? 164 PRO A O   1 
ATOM   1329 C  CB  . PRO A 1 169 ? 10.643 33.360  7.302   1.00 11.40 ? 164 PRO A CB  1 
ATOM   1330 C  CG  . PRO A 1 169 ? 10.605 34.850  7.052   1.00 12.92 ? 164 PRO A CG  1 
ATOM   1331 C  CD  . PRO A 1 169 ? 11.428 35.170  5.870   1.00 12.65 ? 164 PRO A CD  1 
ATOM   1332 N  N   . THR A 1 170 ? 11.071 31.653  4.478   1.00 10.26 ? 165 THR A N   1 
ATOM   1333 C  CA  . THR A 1 170 ? 10.722 30.492  3.677   1.00 8.20  ? 165 THR A CA  1 
ATOM   1334 C  C   . THR A 1 170 ? 11.880 29.875  2.887   1.00 7.69  ? 165 THR A C   1 
ATOM   1335 O  O   . THR A 1 170 ? 11.704 28.873  2.201   1.00 6.73  ? 165 THR A O   1 
ATOM   1336 C  CB  . THR A 1 170 ? 9.632  30.837  2.649   1.00 7.85  ? 165 THR A CB  1 
ATOM   1337 O  OG1 . THR A 1 170 ? 10.029 32.047  2.016   1.00 8.50  ? 165 THR A OG1 1 
ATOM   1338 C  CG2 . THR A 1 170 ? 8.247  30.999  3.292   1.00 8.75  ? 165 THR A CG2 1 
ATOM   1339 N  N   . ASN A 1 171 ? 13.050 30.506  2.927   1.00 7.56  ? 166 ASN A N   1 
ATOM   1340 C  CA  . ASN A 1 171 ? 14.197 29.968  2.206   1.00 10.16 ? 166 ASN A CA  1 
ATOM   1341 C  C   . ASN A 1 171 ? 14.455 28.505  2.603   1.00 9.04  ? 166 ASN A C   1 
ATOM   1342 O  O   . ASN A 1 171 ? 14.601 28.203  3.783   1.00 7.46  ? 166 ASN A O   1 
ATOM   1343 C  CB  . ASN A 1 171 ? 15.408 30.851  2.454   1.00 10.38 ? 166 ASN A CB  1 
ATOM   1344 C  CG  . ASN A 1 171 ? 16.596 30.348  1.717   1.00 18.08 ? 166 ASN A CG  1 
ATOM   1345 O  OD1 . ASN A 1 171 ? 17.223 29.372  2.139   1.00 16.34 ? 166 ASN A OD1 1 
ATOM   1346 N  ND2 . ASN A 1 171 ? 16.924 31.006  0.603   1.00 17.49 ? 166 ASN A ND2 1 
ATOM   1347 N  N   . PRO A 1 172 ? 14.462 27.525  1.671   1.00 8.28  ? 167 PRO A N   1 
ATOM   1348 C  CA  . PRO A 1 172 ? 14.663 26.117  2.038   1.00 7.89  ? 167 PRO A CA  1 
ATOM   1349 C  C   . PRO A 1 172 ? 15.938 25.825  2.824   1.00 7.47  ? 167 PRO A C   1 
ATOM   1350 O  O   . PRO A 1 172 ? 15.926 24.967  3.699   1.00 6.38  ? 167 PRO A O   1 
ATOM   1351 C  CB  . PRO A 1 172 ? 14.653 25.417  0.706   1.00 8.97  ? 167 PRO A CB  1 
ATOM   1352 C  CG  . PRO A 1 172 ? 13.784 26.308  -0.138  1.00 11.46 ? 167 PRO A CG  1 
ATOM   1353 C  CD  . PRO A 1 172 ? 14.108 27.663  0.257   1.00 11.82 ? 167 PRO A CD  1 
ATOM   1354 N  N   . ILE A 1 173 ? 17.014 26.567  2.547   1.00 7.34  ? 168 ILE A N   1 
ATOM   1355 C  CA  . ILE A 1 173 ? 18.243 26.340  3.296   1.00 8.48  ? 168 ILE A CA  1 
ATOM   1356 C  C   . ILE A 1 173 ? 17.979 26.761  4.739   1.00 6.93  ? 168 ILE A C   1 
ATOM   1357 O  O   . ILE A 1 173 ? 18.363 26.082  5.676   1.00 5.83  ? 168 ILE A O   1 
ATOM   1358 C  CB  . ILE A 1 173 ? 19.454 27.097  2.709   1.00 11.93 ? 168 ILE A CB  1 
ATOM   1359 C  CG1 . ILE A 1 173 ? 19.668 26.768  1.229   1.00 17.89 ? 168 ILE A CG1 1 
ATOM   1360 C  CG2 . ILE A 1 173 ? 20.717 26.812  3.517   1.00 12.19 ? 168 ILE A CG2 1 
ATOM   1361 C  CD1 . ILE A 1 173 ? 20.560 27.770  0.596   1.00 25.84 ? 168 ILE A CD1 1 
ATOM   1362 N  N   . ARG A 1 174 ? 17.393 27.946  4.918   1.00 6.27  ? 169 ARG A N   1 
ATOM   1363 C  CA  . ARG A 1 174 ? 17.066 28.449  6.253   1.00 6.39  ? 169 ARG A CA  1 
ATOM   1364 C  C   . ARG A 1 174 ? 16.148 27.491  7.011   1.00 5.63  ? 169 ARG A C   1 
ATOM   1365 O  O   . ARG A 1 174 ? 16.394 27.180  8.189   1.00 4.89  ? 169 ARG A O   1 
ATOM   1366 C  CB  . ARG A 1 174 ? 16.464 29.853  6.170   1.00 6.47  ? 169 ARG A CB  1 
ATOM   1367 C  CG  . ARG A 1 174 ? 16.126 30.432  7.543   1.00 7.90  ? 169 ARG A CG  1 
ATOM   1368 C  CD  . ARG A 1 174 ? 15.676 31.894  7.475   1.00 9.34  ? 169 ARG A CD  1 
ATOM   1369 N  NE  . ARG A 1 174 ? 15.088 32.328  8.738   1.00 9.49  ? 169 ARG A NE  1 
ATOM   1370 C  CZ  . ARG A 1 174 ? 14.560 33.536  8.924   1.00 10.61 ? 169 ARG A CZ  1 
ATOM   1371 N  NH1 . ARG A 1 174 ? 14.660 34.488  8.003   1.00 11.79 ? 169 ARG A NH1 1 
ATOM   1372 N  NH2 . ARG A 1 174 ? 13.931 33.797  10.058  1.00 10.28 ? 169 ARG A NH2 1 
ATOM   1373 N  N   . LEU A 1 175 ? 15.121 26.978  6.323   1.00 5.69  ? 170 LEU A N   1 
ATOM   1374 C  CA  . LEU A 1 175 ? 14.190 26.032  6.923   1.00 5.09  ? 170 LEU A CA  1 
ATOM   1375 C  C   . LEU A 1 175 ? 14.870 24.728  7.318   1.00 4.73  ? 170 LEU A C   1 
ATOM   1376 O  O   . LEU A 1 175 ? 14.649 24.222  8.420   1.00 5.82  ? 170 LEU A O   1 
ATOM   1377 C  CB  . LEU A 1 175 ? 13.027 25.720  5.977   1.00 5.47  ? 170 LEU A CB  1 
ATOM   1378 C  CG  . LEU A 1 175 ? 12.069 26.865  5.741   1.00 6.18  ? 170 LEU A CG  1 
ATOM   1379 C  CD1 . LEU A 1 175 ? 11.018 26.497  4.650   1.00 7.19  ? 170 LEU A CD1 1 
ATOM   1380 C  CD2 . LEU A 1 175 ? 11.380 27.256  7.001   1.00 7.46  ? 170 LEU A CD2 1 
ATOM   1381 N  N   . GLY A 1 176 ? 15.699 24.198  6.423   1.00 4.71  ? 171 GLY A N   1 
ATOM   1382 C  CA  . GLY A 1 176 ? 16.399 22.947  6.693   1.00 4.59  ? 171 GLY A CA  1 
ATOM   1383 C  C   . GLY A 1 176 ? 17.392 23.080  7.835   1.00 4.69  ? 171 GLY A C   1 
ATOM   1384 O  O   . GLY A 1 176 ? 17.590 22.149  8.634   1.00 4.44  ? 171 GLY A O   1 
ATOM   1385 N  N   . LEU A 1 177 ? 18.030 24.250  7.899   1.00 4.52  ? 172 LEU A N   1 
ATOM   1386 C  CA  . LEU A 1 177 ? 18.951 24.546  8.978   1.00 5.10  ? 172 LEU A CA  1 
ATOM   1387 C  C   . LEU A 1 177 ? 18.195 24.548  10.303  1.00 4.84  ? 172 LEU A C   1 
ATOM   1388 O  O   . LEU A 1 177 ? 18.603 23.889  11.247  1.00 4.28  ? 172 LEU A O   1 
ATOM   1389 C  CB  . LEU A 1 177 ? 19.650 25.879  8.755   1.00 5.51  ? 172 LEU A CB  1 
ATOM   1390 C  CG  . LEU A 1 177 ? 20.308 26.471  9.969   1.00 6.35  ? 172 LEU A CG  1 
ATOM   1391 C  CD1 . LEU A 1 177 ? 21.447 25.595  10.481  1.00 6.61  ? 172 LEU A CD1 1 
ATOM   1392 C  CD2 . LEU A 1 177 ? 20.829 27.827  9.637   1.00 6.67  ? 172 LEU A CD2 1 
ATOM   1393 N  N   . ALA A 1 178 ? 17.078 25.281  10.364  1.00 4.58  ? 173 ALA A N   1 
ATOM   1394 C  CA  . ALA A 1 178 ? 16.303 25.339  11.596  1.00 5.00  ? 173 ALA A CA  1 
ATOM   1395 C  C   . ALA A 1 178 ? 15.776 23.961  11.994  1.00 4.60  ? 173 ALA A C   1 
ATOM   1396 O  O   . ALA A 1 178 ? 15.804 23.587  13.161  1.00 4.60  ? 173 ALA A O   1 
ATOM   1397 C  CB  . ALA A 1 178 ? 15.176 26.363  11.450  1.00 4.68  ? 173 ALA A CB  1 
ATOM   1398 N  N   . LEU A 1 179 ? 15.264 23.201  11.027  1.00 5.32  ? 174 LEU A N   1 
ATOM   1399 C  CA  . LEU A 1 179 ? 14.866 21.825  11.285  1.00 4.96  ? 174 LEU A CA  1 
ATOM   1400 C  C   . LEU A 1 179 ? 15.987 21.037  11.965  1.00 4.84  ? 174 LEU A C   1 
ATOM   1401 O  O   . LEU A 1 179 ? 15.772 20.441  13.024  1.00 4.73  ? 174 LEU A O   1 
ATOM   1402 C  CB  . LEU A 1 179 ? 14.451 21.142  9.980   1.00 5.29  ? 174 LEU A CB  1 
ATOM   1403 C  CG  . LEU A 1 179 ? 14.075 19.664  10.051  1.00 5.42  ? 174 LEU A CG  1 
ATOM   1404 C  CD1 . LEU A 1 179 ? 12.911 19.483  10.932  1.00 7.04  ? 174 LEU A CD1 1 
ATOM   1405 C  CD2 . LEU A 1 179 ? 13.730 19.120  8.640   1.00 5.87  ? 174 LEU A CD2 1 
ATOM   1406 N  N   . ASN A 1 180 ? 17.177 21.050  11.361  1.00 4.61  ? 175 ASN A N   1 
ATOM   1407 C  CA  . ASN A 1 180 ? 18.262 20.230  11.887  1.00 4.86  ? 175 ASN A CA  1 
ATOM   1408 C  C   . ASN A 1 180 ? 18.762 20.747  13.234  1.00 4.55  ? 175 ASN A C   1 
ATOM   1409 O  O   . ASN A 1 180 ? 19.110 19.942  14.092  1.00 5.47  ? 175 ASN A O   1 
ATOM   1410 C  CB  . ASN A 1 180 ? 19.382 20.138  10.905  1.00 5.91  ? 175 ASN A CB  1 
ATOM   1411 C  CG  . ASN A 1 180 ? 19.048 19.252  9.732   1.00 6.48  ? 175 ASN A CG  1 
ATOM   1412 O  OD1 . ASN A 1 180 ? 17.910 18.884  9.494   1.00 6.53  ? 175 ASN A OD1 1 
ATOM   1413 N  ND2 . ASN A 1 180 ? 20.084 18.878  8.978   1.00 6.87  ? 175 ASN A ND2 1 
ATOM   1414 N  N   . PHE A 1 181 ? 18.770 22.072  13.448  1.00 4.16  ? 176 PHE A N   1 
ATOM   1415 C  CA  . PHE A 1 181 ? 19.166 22.608  14.737  1.00 4.40  ? 176 PHE A CA  1 
ATOM   1416 C  C   . PHE A 1 181 ? 18.144 22.201  15.800  1.00 4.39  ? 176 PHE A C   1 
ATOM   1417 O  O   . PHE A 1 181 ? 18.510 21.913  16.947  1.00 3.72  ? 176 PHE A O   1 
ATOM   1418 C  CB  . PHE A 1 181 ? 19.359 24.131  14.648  1.00 4.83  ? 176 PHE A CB  1 
ATOM   1419 C  CG  . PHE A 1 181 ? 20.121 24.820  15.770  1.00 5.30  ? 176 PHE A CG  1 
ATOM   1420 C  CD1 . PHE A 1 181 ? 20.934 24.103  16.632  1.00 5.76  ? 176 PHE A CD1 1 
ATOM   1421 C  CD2 . PHE A 1 181 ? 19.982 26.176  15.983  1.00 6.32  ? 176 PHE A CD2 1 
ATOM   1422 C  CE1 . PHE A 1 181 ? 21.647 24.741  17.633  1.00 5.61  ? 176 PHE A CE1 1 
ATOM   1423 C  CE2 . PHE A 1 181 ? 20.700 26.816  16.977  1.00 8.26  ? 176 PHE A CE2 1 
ATOM   1424 C  CZ  . PHE A 1 181 ? 21.541 26.094  17.796  1.00 6.46  ? 176 PHE A CZ  1 
ATOM   1425 N  N   . SER A 1 182 ? 16.861 22.150  15.420  1.00 4.84  ? 177 SER A N   1 
ATOM   1426 C  CA  . SER A 1 182 ? 15.845 21.682  16.354  1.00 6.03  ? 177 SER A CA  1 
ATOM   1427 C  C   . SER A 1 182 ? 16.072 20.212  16.722  1.00 5.88  ? 177 SER A C   1 
ATOM   1428 O  O   . SER A 1 182 ? 15.895 19.841  17.877  1.00 6.63  ? 177 SER A O   1 
ATOM   1429 C  CB  . SER A 1 182 ? 14.419 21.941  15.832  1.00 5.90  ? 177 SER A CB  1 
ATOM   1430 O  OG  . SER A 1 182 ? 13.979 21.057  14.818  1.00 6.98  ? 177 SER A OG  1 
ATOM   1431 N  N   . VAL A 1 183 ? 16.465 19.379  15.751  1.00 5.83  ? 178 VAL A N   1 
ATOM   1432 C  CA  . VAL A 1 183 ? 16.799 17.980  16.011  1.00 6.20  ? 178 VAL A CA  1 
ATOM   1433 C  C   . VAL A 1 183 ? 18.003 17.878  16.946  1.00 5.59  ? 178 VAL A C   1 
ATOM   1434 O  O   . VAL A 1 183 ? 18.000 17.080  17.861  1.00 6.66  ? 178 VAL A O   1 
ATOM   1435 C  CB  . VAL A 1 183 ? 17.036 17.179  14.707  1.00 6.53  ? 178 VAL A CB  1 
ATOM   1436 C  CG1 . VAL A 1 183 ? 17.602 15.785  15.012  1.00 6.60  ? 178 VAL A CG1 1 
ATOM   1437 C  CG2 . VAL A 1 183 ? 15.730 17.083  13.881  1.00 7.63  ? 178 VAL A CG2 1 
ATOM   1438 N  N   . PHE A 1 184 ? 19.025 18.700  16.720  1.00 6.06  ? 179 PHE A N   1 
ATOM   1439 C  CA  . PHE A 1 184 ? 20.148 18.805  17.638  1.00 5.45  ? 179 PHE A CA  1 
ATOM   1440 C  C   . PHE A 1 184 ? 19.656 19.052  19.062  1.00 5.75  ? 179 PHE A C   1 
ATOM   1441 O  O   . PHE A 1 184 ? 20.069 18.372  19.987  1.00 6.71  ? 179 PHE A O   1 
ATOM   1442 C  CB  . PHE A 1 184 ? 21.089 19.925  17.190  1.00 5.00  ? 179 PHE A CB  1 
ATOM   1443 C  CG  . PHE A 1 184 ? 22.144 20.289  18.187  1.00 4.98  ? 179 PHE A CG  1 
ATOM   1444 C  CD1 . PHE A 1 184 ? 23.314 19.547  18.288  1.00 5.58  ? 179 PHE A CD1 1 
ATOM   1445 C  CD2 . PHE A 1 184 ? 21.960 21.353  19.050  1.00 5.69  ? 179 PHE A CD2 1 
ATOM   1446 C  CE1 . PHE A 1 184 ? 24.279 19.867  19.226  1.00 5.65  ? 179 PHE A CE1 1 
ATOM   1447 C  CE2 . PHE A 1 184 ? 22.932 21.667  20.005  1.00 6.39  ? 179 PHE A CE2 1 
ATOM   1448 C  CZ  . PHE A 1 184 ? 24.107 20.942  20.046  1.00 6.57  ? 179 PHE A CZ  1 
ATOM   1449 N  N   . HIS A 1 185 ? 18.794 20.063  19.253  1.00 5.49  ? 180 HIS A N   1 
ATOM   1450 C  CA  . HIS A 1 185 ? 18.332 20.395  20.592  1.00 5.66  ? 180 HIS A CA  1 
ATOM   1451 C  C   . HIS A 1 185 ? 17.642 19.194  21.243  1.00 6.02  ? 180 HIS A C   1 
ATOM   1452 O  O   . HIS A 1 185 ? 17.836 18.894  22.430  1.00 5.59  ? 180 HIS A O   1 
ATOM   1453 C  CB  . HIS A 1 185 ? 17.410 21.668  20.562  1.00 6.07  ? 180 HIS A CB  1 
ATOM   1454 C  CG  . HIS A 1 185 ? 18.124 22.963  20.296  1.00 6.71  ? 180 HIS A CG  1 
ATOM   1455 N  ND1 . HIS A 1 185 ? 19.224 23.362  21.058  1.00 7.13  ? 180 HIS A ND1 1 
ATOM   1456 C  CD2 . HIS A 1 185 ? 17.879 23.912  19.361  1.00 7.08  ? 180 HIS A CD2 1 
ATOM   1457 C  CE1 . HIS A 1 185 ? 19.590 24.534  20.573  1.00 7.10  ? 180 HIS A CE1 1 
ATOM   1458 N  NE2 . HIS A 1 185 ? 18.795 24.922  19.563  1.00 6.27  ? 180 HIS A NE2 1 
ATOM   1459 N  N   . TYR A 1 186 ? 16.791 18.519  20.472  1.00 6.53  ? 181 TYR A N   1 
ATOM   1460 C  CA  . TYR A 1 186 ? 15.940 17.486  21.028  1.00 7.02  ? 181 TYR A CA  1 
ATOM   1461 C  C   . TYR A 1 186 ? 16.711 16.190  21.269  1.00 8.22  ? 181 TYR A C   1 
ATOM   1462 O  O   . TYR A 1 186 ? 16.582 15.562  22.321  1.00 7.68  ? 181 TYR A O   1 
ATOM   1463 C  CB  . TYR A 1 186 ? 14.774 17.197  20.075  1.00 8.66  ? 181 TYR A CB  1 
ATOM   1464 C  CG  . TYR A 1 186 ? 13.729 16.325  20.702  1.00 9.12  ? 181 TYR A CG  1 
ATOM   1465 C  CD1 . TYR A 1 186 ? 13.850 14.947  20.695  1.00 11.01 ? 181 TYR A CD1 1 
ATOM   1466 C  CD2 . TYR A 1 186 ? 12.647 16.881  21.364  1.00 12.86 ? 181 TYR A CD2 1 
ATOM   1467 C  CE1 . TYR A 1 186 ? 12.874 14.133  21.276  1.00 13.29 ? 181 TYR A CE1 1 
ATOM   1468 C  CE2 . TYR A 1 186 ? 11.673 16.081  21.958  1.00 13.29 ? 181 TYR A CE2 1 
ATOM   1469 C  CZ  . TYR A 1 186 ? 11.796 14.709  21.921  1.00 13.45 ? 181 TYR A CZ  1 
ATOM   1470 O  OH  . TYR A 1 186 ? 10.807 13.941  22.523  1.00 15.43 ? 181 TYR A OH  1 
ATOM   1471 N  N   . GLU A 1 187 ? 17.514 15.810  20.279  1.00 8.07  ? 182 GLU A N   1 
ATOM   1472 C  CA  . GLU A 1 187 ? 18.131 14.498  20.255  1.00 8.61  ? 182 GLU A CA  1 
ATOM   1473 C  C   . GLU A 1 187 ? 19.522 14.471  20.892  1.00 9.68  ? 182 GLU A C   1 
ATOM   1474 O  O   . GLU A 1 187 ? 19.945 13.436  21.379  1.00 11.42 ? 182 GLU A O   1 
ATOM   1475 C  CB  . GLU A 1 187 ? 18.195 13.967  18.796  1.00 10.37 ? 182 GLU A CB  1 
ATOM   1476 C  CG  . GLU A 1 187 ? 16.848 13.663  18.163  1.00 9.83  ? 182 GLU A CG  1 
ATOM   1477 C  CD  . GLU A 1 187 ? 16.061 12.467  18.704  1.00 14.35 ? 182 GLU A CD  1 
ATOM   1478 O  OE1 . GLU A 1 187 ? 16.599 11.710  19.544  1.00 17.01 ? 182 GLU A OE1 1 
ATOM   1479 O  OE2 . GLU A 1 187 ? 14.887 12.310  18.312  1.00 11.88 ? 182 GLU A OE2 1 
ATOM   1480 N  N   . ILE A 1 188 ? 20.241 15.582  20.868  1.00 8.48  ? 183 ILE A N   1 
ATOM   1481 C  CA  . ILE A 1 188 ? 21.641 15.611  21.283  1.00 8.42  ? 183 ILE A CA  1 
ATOM   1482 C  C   . ILE A 1 188 ? 21.830 16.414  22.559  1.00 9.38  ? 183 ILE A C   1 
ATOM   1483 O  O   . ILE A 1 188 ? 22.587 16.007  23.447  1.00 8.81  ? 183 ILE A O   1 
ATOM   1484 C  CB  . ILE A 1 188 ? 22.545 16.193  20.170  1.00 9.04  ? 183 ILE A CB  1 
ATOM   1485 C  CG1 . ILE A 1 188 ? 22.359 15.476  18.840  1.00 10.69 ? 183 ILE A CG1 1 
ATOM   1486 C  CG2 . ILE A 1 188 ? 24.019 16.228  20.612  1.00 9.55  ? 183 ILE A CG2 1 
ATOM   1487 C  CD1 . ILE A 1 188 ? 22.675 14.048  18.815  1.00 12.23 ? 183 ILE A CD1 1 
ATOM   1488 N  N   . ALA A 1 189 ? 21.179 17.598  22.624  1.00 7.86  ? 184 ALA A N   1 
ATOM   1489 C  CA  . ALA A 1 189 ? 21.492 18.588  23.643  1.00 8.19  ? 184 ALA A CA  1 
ATOM   1490 C  C   . ALA A 1 189 ? 20.578 18.505  24.864  1.00 7.48  ? 184 ALA A C   1 
ATOM   1491 O  O   . ALA A 1 189 ? 20.703 19.298  25.794  1.00 9.97  ? 184 ALA A O   1 
ATOM   1492 C  CB  . ALA A 1 189 ? 21.453 19.984  23.043  1.00 8.72  ? 184 ALA A CB  1 
ATOM   1493 N  N   . ASN A 1 190 ? 19.675 17.544  24.869  1.00 8.57  ? 185 ASN A N   1 
ATOM   1494 C  CA  . ASN A 1 190 ? 18.774 17.363  25.997  1.00 11.16 ? 185 ASN A CA  1 
ATOM   1495 C  C   . ASN A 1 190 ? 17.987 18.646  26.252  1.00 10.18 ? 185 ASN A C   1 
ATOM   1496 O  O   . ASN A 1 190 ? 17.739 19.016  27.407  1.00 8.83  ? 185 ASN A O   1 
ATOM   1497 C  CB  . ASN A 1 190 ? 19.550 16.917  27.254  1.00 13.87 ? 185 ASN A CB  1 
ATOM   1498 C  CG  . ASN A 1 190 ? 18.648 16.436  28.368  1.00 19.47 ? 185 ASN A CG  1 
ATOM   1499 O  OD1 . ASN A 1 190 ? 17.579 15.873  28.139  1.00 21.27 ? 185 ASN A OD1 1 
ATOM   1500 N  ND2 . ASN A 1 190 ? 19.025 16.716  29.612  1.00 23.76 ? 185 ASN A ND2 1 
ATOM   1501 N  N   . SER A 1 191 ? 17.538 19.306  25.169  1.00 8.44  ? 186 SER A N   1 
ATOM   1502 C  CA  . SER A 1 191 ? 16.806 20.560  25.296  1.00 7.81  ? 186 SER A CA  1 
ATOM   1503 C  C   . SER A 1 191 ? 15.515 20.517  24.498  1.00 7.70  ? 186 SER A C   1 
ATOM   1504 O  O   . SER A 1 191 ? 15.396 21.240  23.522  1.00 6.25  ? 186 SER A O   1 
ATOM   1505 C  CB  . SER A 1 191 ? 17.651 21.718  24.824  1.00 8.78  ? 186 SER A CB  1 
ATOM   1506 O  OG  . SER A 1 191 ? 18.888 21.831  25.500  1.00 9.24  ? 186 SER A OG  1 
ATOM   1507 N  N   . PRO A 1 192 ? 14.552 19.630  24.841  1.00 8.17  ? 187 PRO A N   1 
ATOM   1508 C  CA  . PRO A 1 192 ? 13.332 19.495  24.042  1.00 8.60  ? 187 PRO A CA  1 
ATOM   1509 C  C   . PRO A 1 192 ? 12.548 20.805  23.972  1.00 7.54  ? 187 PRO A C   1 
ATOM   1510 O  O   . PRO A 1 192 ? 11.911 21.100  22.962  1.00 7.25  ? 187 PRO A O   1 
ATOM   1511 C  CB  . PRO A 1 192 ? 12.590 18.352  24.730  1.00 8.91  ? 187 PRO A CB  1 
ATOM   1512 C  CG  . PRO A 1 192 ? 13.147 18.342  26.153  1.00 8.64  ? 187 PRO A CG  1 
ATOM   1513 C  CD  . PRO A 1 192 ? 14.570 18.736  26.019  1.00 8.61  ? 187 PRO A CD  1 
ATOM   1514 N  N   . GLU A 1 193 ? 12.564 21.618  25.032  1.00 8.01  ? 188 GLU A N   1 
ATOM   1515 C  CA  . GLU A 1 193 ? 11.801 22.863  24.962  1.00 7.69  ? 188 GLU A CA  1 
ATOM   1516 C  C   . GLU A 1 193 ? 12.369 23.852  23.944  1.00 7.38  ? 188 GLU A C   1 
ATOM   1517 O  O   . GLU A 1 193 ? 11.622 24.517  23.210  1.00 6.63  ? 188 GLU A O   1 
ATOM   1518 C  CB  . GLU A 1 193 ? 11.716 23.516  26.339  1.00 9.15  ? 188 GLU A CB  1 
ATOM   1519 C  CG  . GLU A 1 193 ? 10.854 22.682  27.267  1.00 10.10 ? 188 GLU A CG  1 
ATOM   1520 C  CD  . GLU A 1 193 ? 10.695 23.202  28.676  1.00 13.06 ? 188 GLU A CD  1 
ATOM   1521 O  OE1 . GLU A 1 193 ? 11.655 23.805  29.206  1.00 14.28 ? 188 GLU A OE1 1 
ATOM   1522 O  OE2 . GLU A 1 193 ? 9.640  22.917  29.289  1.00 16.90 ? 188 GLU A OE2 1 
ATOM   1523 N  N   . GLU A 1 194 ? 13.703 23.944  23.888  1.00 5.67  ? 189 GLU A N   1 
ATOM   1524 C  CA  . GLU A 1 194 ? 14.362 24.726  22.862  1.00 5.79  ? 189 GLU A CA  1 
ATOM   1525 C  C   . GLU A 1 194 ? 14.003 24.207  21.465  1.00 5.90  ? 189 GLU A C   1 
ATOM   1526 O  O   . GLU A 1 194 ? 13.700 24.995  20.560  1.00 7.32  ? 189 GLU A O   1 
ATOM   1527 C  CB  . GLU A 1 194 ? 15.890 24.725  23.068  1.00 6.38  ? 189 GLU A CB  1 
ATOM   1528 C  CG  . GLU A 1 194 ? 16.621 25.722  22.190  1.00 6.88  ? 189 GLU A CG  1 
ATOM   1529 C  CD  . GLU A 1 194 ? 16.344 27.209  22.470  1.00 8.07  ? 189 GLU A CD  1 
ATOM   1530 O  OE1 . GLU A 1 194 ? 15.777 27.531  23.538  1.00 7.54  ? 189 GLU A OE1 1 
ATOM   1531 O  OE2 . GLU A 1 194 ? 16.719 28.038  21.612  1.00 7.32  ? 189 GLU A OE2 1 
ATOM   1532 N  N   . ALA A 1 195 ? 14.045 22.886  21.287  1.00 6.01  ? 190 ALA A N   1 
ATOM   1533 C  CA  . ALA A 1 195 ? 13.649 22.251  20.033  1.00 6.16  ? 190 ALA A CA  1 
ATOM   1534 C  C   . ALA A 1 195 ? 12.232 22.635  19.585  1.00 7.03  ? 190 ALA A C   1 
ATOM   1535 O  O   . ALA A 1 195 ? 12.014 23.039  18.441  1.00 6.11  ? 190 ALA A O   1 
ATOM   1536 C  CB  . ALA A 1 195 ? 13.772 20.745  20.166  1.00 6.47  ? 190 ALA A CB  1 
ATOM   1537 N  N   . ILE A 1 196 ? 11.268 22.500  20.493  1.00 6.96  ? 191 ILE A N   1 
ATOM   1538 C  CA  . ILE A 1 196 ? 9.873  22.809  20.216  1.00 7.21  ? 191 ILE A CA  1 
ATOM   1539 C  C   . ILE A 1 196 ? 9.701  24.290  19.855  1.00 6.26  ? 191 ILE A C   1 
ATOM   1540 O  O   . ILE A 1 196 ? 9.001  24.633  18.900  1.00 6.80  ? 191 ILE A O   1 
ATOM   1541 C  CB  . ILE A 1 196 ? 9.010  22.362  21.436  1.00 7.62  ? 191 ILE A CB  1 
ATOM   1542 C  CG1 . ILE A 1 196 ? 8.979  20.840  21.583  1.00 7.64  ? 191 ILE A CG1 1 
ATOM   1543 C  CG2 . ILE A 1 196 ? 7.591  22.940  21.349  1.00 8.05  ? 191 ILE A CG2 1 
ATOM   1544 C  CD1 . ILE A 1 196 ? 8.545  20.289  22.928  1.00 7.80  ? 191 ILE A CD1 1 
ATOM   1545 N  N   . SER A 1 197 ? 10.296 25.167  20.661  1.00 7.51  ? 192 SER A N   1 
ATOM   1546 C  CA  . SER A 1 197 ? 10.187 26.603  20.445  1.00 8.15  ? 192 SER A CA  1 
ATOM   1547 C  C   . SER A 1 197 ? 10.759 26.990  19.096  1.00 7.86  ? 192 SER A C   1 
ATOM   1548 O  O   . SER A 1 197 ? 10.145 27.718  18.314  1.00 8.56  ? 192 SER A O   1 
ATOM   1549 C  CB  . SER A 1 197 ? 10.874 27.395  21.554  1.00 11.00 ? 192 SER A CB  1 
ATOM   1550 O  OG  . SER A 1 197 ? 10.698 28.802  21.329  1.00 14.26 ? 192 SER A OG  1 
ATOM   1551 N  N   . LEU A 1 198 ? 11.942 26.450  18.792  1.00 7.46  ? 193 LEU A N   1 
ATOM   1552 C  CA  . LEU A 1 198 ? 12.533 26.752  17.506  1.00 7.43  ? 193 LEU A CA  1 
ATOM   1553 C  C   . LEU A 1 198 ? 11.642 26.267  16.362  1.00 6.26  ? 193 LEU A C   1 
ATOM   1554 O  O   . LEU A 1 198 ? 11.430 26.995  15.384  1.00 7.13  ? 193 LEU A O   1 
ATOM   1555 C  CB  . LEU A 1 198 ? 13.938 26.135  17.426  1.00 6.70  ? 193 LEU A CB  1 
ATOM   1556 C  CG  . LEU A 1 198 ? 14.641 26.286  16.083  1.00 6.49  ? 193 LEU A CG  1 
ATOM   1557 C  CD1 . LEU A 1 198 ? 14.710 27.716  15.626  1.00 6.89  ? 193 LEU A CD1 1 
ATOM   1558 C  CD2 . LEU A 1 198 ? 16.069 25.739  16.189  1.00 7.70  ? 193 LEU A CD2 1 
ATOM   1559 N  N   . ALA A 1 199 ? 11.156 25.017  16.437  1.00 6.73  ? 194 ALA A N   1 
ATOM   1560 C  CA  . ALA A 1 199 ? 10.333 24.470  15.360  1.00 7.26  ? 194 ALA A CA  1 
ATOM   1561 C  C   . ALA A 1 199 ? 9.056  25.282  15.147  1.00 7.04  ? 194 ALA A C   1 
ATOM   1562 O  O   . ALA A 1 199 ? 8.659  25.552  14.014  1.00 7.01  ? 194 ALA A O   1 
ATOM   1563 C  CB  . ALA A 1 199 ? 9.951  23.029  15.660  1.00 8.20  ? 194 ALA A CB  1 
ATOM   1564 N  N   . LYS A 1 200 ? 8.408  25.637  16.263  1.00 7.74  ? 195 LYS A N   1 
ATOM   1565 C  CA  . LYS A 1 200 ? 7.185  26.425  16.225  1.00 9.22  ? 195 LYS A CA  1 
ATOM   1566 C  C   . LYS A 1 200 ? 7.384  27.804  15.607  1.00 7.14  ? 195 LYS A C   1 
ATOM   1567 O  O   . LYS A 1 200 ? 6.645  28.181  14.697  1.00 7.32  ? 195 LYS A O   1 
ATOM   1568 C  CB  . LYS A 1 200 ? 6.576  26.597  17.619  1.00 11.13 ? 195 LYS A CB  1 
ATOM   1569 C  CG  . LYS A 1 200 ? 5.805  25.474  18.117  1.00 16.55 ? 195 LYS A CG  1 
ATOM   1570 C  CD  . LYS A 1 200 ? 5.408  25.732  19.588  1.00 25.41 ? 195 LYS A CD  1 
ATOM   1571 C  CE  . LYS A 1 200 ? 4.293  24.870  20.082  1.00 29.52 ? 195 LYS A CE  1 
ATOM   1572 N  NZ  . LYS A 1 200 ? 4.157  25.012  21.552  1.00 36.87 ? 195 LYS A NZ  1 
ATOM   1573 N  N   . THR A 1 201 ? 8.406  28.536  16.058  1.00 7.15  ? 196 THR A N   1 
ATOM   1574 C  CA  . THR A 1 201 ? 8.679  29.871  15.553  1.00 7.65  ? 196 THR A CA  1 
ATOM   1575 C  C   . THR A 1 201 ? 9.064  29.833  14.075  1.00 6.98  ? 196 THR A C   1 
ATOM   1576 O  O   . THR A 1 201 ? 8.640  30.694  13.298  1.00 6.89  ? 196 THR A O   1 
ATOM   1577 C  CB  . THR A 1 201 ? 9.748  30.560  16.407  1.00 10.05 ? 196 THR A CB  1 
ATOM   1578 O  OG1 . THR A 1 201 ? 9.181  30.854  17.703  1.00 12.72 ? 196 THR A OG1 1 
ATOM   1579 C  CG2 . THR A 1 201 ? 10.255 31.861  15.791  1.00 11.35 ? 196 THR A CG2 1 
ATOM   1580 N  N   . THR A 1 202 ? 9.881  28.844  13.707  1.00 6.03  ? 197 THR A N   1 
ATOM   1581 C  CA  . THR A 1 202 ? 10.311 28.683  12.323  1.00 5.89  ? 197 THR A CA  1 
ATOM   1582 C  C   . THR A 1 202 ? 9.098  28.441  11.430  1.00 6.92  ? 197 THR A C   1 
ATOM   1583 O  O   . THR A 1 202 ? 8.971  29.046  10.366  1.00 7.35  ? 197 THR A O   1 
ATOM   1584 C  CB  . THR A 1 202 ? 11.284 27.522  12.190  1.00 6.52  ? 197 THR A CB  1 
ATOM   1585 O  OG1 . THR A 1 202 ? 12.475 27.753  12.991  1.00 6.49  ? 197 THR A OG1 1 
ATOM   1586 C  CG2 . THR A 1 202 ? 11.708 27.300  10.709  1.00 6.60  ? 197 THR A CG2 1 
ATOM   1587 N  N   . PHE A 1 203 ? 8.208  27.554  11.885  1.00 6.21  ? 198 PHE A N   1 
ATOM   1588 C  CA  . PHE A 1 203 ? 7.040  27.188  11.099  1.00 7.21  ? 198 PHE A CA  1 
ATOM   1589 C  C   . PHE A 1 203 ? 6.128  28.404  10.901  1.00 7.58  ? 198 PHE A C   1 
ATOM   1590 O  O   . PHE A 1 203 ? 5.733  28.714  9.776   1.00 8.29  ? 198 PHE A O   1 
ATOM   1591 C  CB  . PHE A 1 203 ? 6.325  26.011  11.771  1.00 7.24  ? 198 PHE A CB  1 
ATOM   1592 C  CG  . PHE A 1 203 ? 5.086  25.567  11.031  1.00 8.07  ? 198 PHE A CG  1 
ATOM   1593 C  CD1 . PHE A 1 203 ? 3.894  26.275  11.152  1.00 9.40  ? 198 PHE A CD1 1 
ATOM   1594 C  CD2 . PHE A 1 203 ? 5.113  24.461  10.201  1.00 9.43  ? 198 PHE A CD2 1 
ATOM   1595 C  CE1 . PHE A 1 203 ? 2.763  25.869  10.462  1.00 10.24 ? 198 PHE A CE1 1 
ATOM   1596 C  CE2 . PHE A 1 203 ? 3.990  24.066  9.515   1.00 10.67 ? 198 PHE A CE2 1 
ATOM   1597 C  CZ  . PHE A 1 203 ? 2.812  24.761  9.663   1.00 12.57 ? 198 PHE A CZ  1 
ATOM   1598 N  N   . ASP A 1 204 ? 5.859  29.116  11.994  1.00 7.91  ? 199 ASP A N   1 
ATOM   1599 C  CA  . ASP A 1 204 ? 4.947  30.248  11.992  1.00 9.67  ? 199 ASP A CA  1 
ATOM   1600 C  C   . ASP A 1 204 ? 5.473  31.396  11.138  1.00 9.01  ? 199 ASP A C   1 
ATOM   1601 O  O   . ASP A 1 204 ? 4.706  32.005  10.409  1.00 10.83 ? 199 ASP A O   1 
ATOM   1602 C  CB  . ASP A 1 204 ? 4.683  30.699  13.458  1.00 11.99 ? 199 ASP A CB  1 
ATOM   1603 C  CG  . ASP A 1 204 ? 3.798  29.734  14.200  1.00 14.21 ? 199 ASP A CG  1 
ATOM   1604 O  OD1 . ASP A 1 204 ? 3.117  28.915  13.531  1.00 23.77 ? 199 ASP A OD1 1 
ATOM   1605 O  OD2 . ASP A 1 204 ? 3.823  29.743  15.444  1.00 23.10 ? 199 ASP A OD2 1 
ATOM   1606 N  N   . GLU A 1 205 ? 6.779  31.666  11.180  1.00 7.36  ? 200 GLU A N   1 
ATOM   1607 C  CA  . GLU A 1 205 ? 7.339  32.758  10.406  1.00 9.63  ? 200 GLU A CA  1 
ATOM   1608 C  C   . GLU A 1 205 ? 7.357  32.411  8.921   1.00 9.74  ? 200 GLU A C   1 
ATOM   1609 O  O   . GLU A 1 205 ? 7.219  33.293  8.072   1.00 9.72  ? 200 GLU A O   1 
ATOM   1610 C  CB  . GLU A 1 205 ? 8.737  33.121  10.863  1.00 13.58 ? 200 GLU A CB  1 
ATOM   1611 C  CG  . GLU A 1 205 ? 8.846  33.780  12.203  1.00 20.80 ? 200 GLU A CG  1 
ATOM   1612 C  CD  . GLU A 1 205 ? 10.183 34.503  12.299  1.00 35.95 ? 200 GLU A CD  1 
ATOM   1613 O  OE1 . GLU A 1 205 ? 10.297 35.652  11.798  1.00 41.37 ? 200 GLU A OE1 1 
ATOM   1614 O  OE2 . GLU A 1 205 ? 11.148 33.872  12.780  1.00 33.00 ? 200 GLU A OE2 1 
ATOM   1615 N  N   . ALA A 1 206 ? 7.536  31.128  8.608   1.00 8.06  ? 201 ALA A N   1 
ATOM   1616 C  CA  . ALA A 1 206 ? 7.502  30.699  7.222   1.00 7.67  ? 201 ALA A CA  1 
ATOM   1617 C  C   . ALA A 1 206 ? 6.068  30.785  6.685   1.00 8.04  ? 201 ALA A C   1 
ATOM   1618 O  O   . ALA A 1 206 ? 5.847  31.264  5.576   1.00 6.55  ? 201 ALA A O   1 
ATOM   1619 C  CB  . ALA A 1 206 ? 8.060  29.294  7.080   1.00 8.38  ? 201 ALA A CB  1 
ATOM   1620 N  N   . MET A 1 207 ? 5.100  30.329  7.479   1.00 8.44  ? 202 MET A N   1 
ATOM   1621 C  CA  . MET A 1 207 ? 3.697  30.379  7.093   1.00 9.32  ? 202 MET A CA  1 
ATOM   1622 C  C   . MET A 1 207 ? 3.303  31.771  6.621   1.00 7.72  ? 202 MET A C   1 
ATOM   1623 O  O   . MET A 1 207 ? 2.640  31.943  5.603   1.00 7.97  ? 202 MET A O   1 
ATOM   1624 C  CB  . MET A 1 207 ? 2.807  30.037  8.299   1.00 11.62 ? 202 MET A CB  1 
ATOM   1625 C  CG  . MET A 1 207 ? 2.601  28.583  8.505   1.00 15.19 ? 202 MET A CG  1 
ATOM   1626 S  SD  . MET A 1 207 ? 1.667  27.728  7.186   1.00 24.01 ? 202 MET A SD  1 
ATOM   1627 C  CE  . MET A 1 207 ? 0.544  28.867  6.797   1.00 18.30 ? 202 MET A CE  1 
ATOM   1628 N  N   . ALA A 1 208 ? 3.765  32.762  7.368   1.00 7.12  ? 203 ALA A N   1 
ATOM   1629 C  CA  . ALA A 1 208 ? 3.414  34.151  7.124   1.00 7.92  ? 203 ALA A CA  1 
ATOM   1630 C  C   . ALA A 1 208 ? 4.089  34.772  5.902   1.00 9.52  ? 203 ALA A C   1 
ATOM   1631 O  O   . ALA A 1 208 ? 3.687  35.847  5.467   1.00 9.39  ? 203 ALA A O   1 
ATOM   1632 C  CB  . ALA A 1 208 ? 3.713  34.963  8.373   1.00 10.54 ? 203 ALA A CB  1 
ATOM   1633 N  N   . ASP A 1 209 ? 5.115  34.098  5.356   1.00 7.26  ? 204 ASP A N   1 
ATOM   1634 C  CA  . ASP A 1 209 ? 5.811  34.550  4.162   1.00 8.73  ? 204 ASP A CA  1 
ATOM   1635 C  C   . ASP A 1 209 ? 5.475  33.760  2.887   1.00 8.73  ? 204 ASP A C   1 
ATOM   1636 O  O   . ASP A 1 209 ? 5.964  34.083  1.791   1.00 8.55  ? 204 ASP A O   1 
ATOM   1637 C  CB  . ASP A 1 209 ? 7.349  34.471  4.477   1.00 10.61 ? 204 ASP A CB  1 
ATOM   1638 C  CG  . ASP A 1 209 ? 8.271  35.089  3.446   1.00 13.21 ? 204 ASP A CG  1 
ATOM   1639 O  OD1 . ASP A 1 209 ? 8.135  36.285  3.189   1.00 12.28 ? 204 ASP A OD1 1 
ATOM   1640 O  OD2 . ASP A 1 209 ? 9.206  34.361  2.927   1.00 15.66 ? 204 ASP A OD2 1 
ATOM   1641 N  N   . LEU A 1 210 ? 4.632  32.723  3.011   1.00 8.11  ? 205 LEU A N   1 
ATOM   1642 C  CA  . LEU A 1 210 ? 4.312  31.861  1.891   1.00 9.46  ? 205 LEU A CA  1 
ATOM   1643 C  C   . LEU A 1 210 ? 3.666  32.648  0.749   1.00 9.40  ? 205 LEU A C   1 
ATOM   1644 O  O   . LEU A 1 210 ? 3.840  32.306  -0.418  1.00 9.73  ? 205 LEU A O   1 
ATOM   1645 C  CB  . LEU A 1 210 ? 3.379  30.717  2.301   1.00 8.56  ? 205 LEU A CB  1 
ATOM   1646 C  CG  . LEU A 1 210 ? 4.039  29.595  3.132   1.00 9.36  ? 205 LEU A CG  1 
ATOM   1647 C  CD1 . LEU A 1 210 ? 3.030  28.602  3.551   1.00 8.80  ? 205 LEU A CD1 1 
ATOM   1648 C  CD2 . LEU A 1 210 ? 5.187  28.903  2.325   1.00 8.45  ? 205 LEU A CD2 1 
ATOM   1649 N  N   . HIS A 1 211 ? 2.916  33.686  1.100   1.00 8.79  ? 206 HIS A N   1 
ATOM   1650 C  CA  . HIS A 1 211 ? 2.176  34.468  0.119   1.00 9.16  ? 206 HIS A CA  1 
ATOM   1651 C  C   . HIS A 1 211 ? 3.067  35.136  -0.935  1.00 12.07 ? 206 HIS A C   1 
ATOM   1652 O  O   . HIS A 1 211 ? 2.578  35.518  -1.996  1.00 10.49 ? 206 HIS A O   1 
ATOM   1653 C  CB  . HIS A 1 211 ? 1.296  35.498  0.862   1.00 10.34 ? 206 HIS A CB  1 
ATOM   1654 C  CG  . HIS A 1 211 ? 2.023  36.702  1.390   1.00 10.04 ? 206 HIS A CG  1 
ATOM   1655 N  ND1 . HIS A 1 211 ? 2.594  36.724  2.663   1.00 9.76  ? 206 HIS A ND1 1 
ATOM   1656 C  CD2 . HIS A 1 211 ? 2.241  37.900  0.801   1.00 9.38  ? 206 HIS A CD2 1 
ATOM   1657 C  CE1 . HIS A 1 211 ? 3.156  37.927  2.782   1.00 10.31 ? 206 HIS A CE1 1 
ATOM   1658 N  NE2 . HIS A 1 211 ? 2.936  38.663  1.699   1.00 12.59 ? 206 HIS A NE2 1 
ATOM   1659 N  N   . THR A 1 212 ? 4.372  35.279  -0.629  1.00 11.01 ? 207 THR A N   1 
ATOM   1660 C  CA  . THR A 1 212 ? 5.315  35.956  -1.494  1.00 12.43 ? 207 THR A CA  1 
ATOM   1661 C  C   . THR A 1 212 ? 5.856  35.056  -2.603  1.00 10.14 ? 207 THR A C   1 
ATOM   1662 O  O   . THR A 1 212 ? 6.551  35.548  -3.487  1.00 12.13 ? 207 THR A O   1 
ATOM   1663 C  CB  . THR A 1 212 ? 6.531  36.485  -0.684  1.00 11.07 ? 207 THR A CB  1 
ATOM   1664 O  OG1 . THR A 1 212 ? 7.252  35.349  -0.189  1.00 11.34 ? 207 THR A OG1 1 
ATOM   1665 C  CG2 . THR A 1 212 ? 6.138  37.409  0.428   1.00 12.29 ? 207 THR A CG2 1 
ATOM   1666 N  N   . LEU A 1 213 ? 5.588  33.750  -2.498  1.00 11.43 ? 208 LEU A N   1 
ATOM   1667 C  CA  . LEU A 1 213 ? 6.265  32.732  -3.279  1.00 11.91 ? 208 LEU A CA  1 
ATOM   1668 C  C   . LEU A 1 213 ? 5.502  32.291  -4.526  1.00 14.75 ? 208 LEU A C   1 
ATOM   1669 O  O   . LEU A 1 213 ? 4.274  32.259  -4.543  1.00 11.26 ? 208 LEU A O   1 
ATOM   1670 C  CB  . LEU A 1 213 ? 6.479  31.517  -2.417  1.00 12.39 ? 208 LEU A CB  1 
ATOM   1671 C  CG  . LEU A 1 213 ? 7.329  31.711  -1.096  1.00 10.84 ? 208 LEU A CG  1 
ATOM   1672 C  CD1 . LEU A 1 213 ? 7.576  30.392  -0.455  1.00 11.39 ? 208 LEU A CD1 1 
ATOM   1673 C  CD2 . LEU A 1 213 ? 8.653  32.454  -1.379  1.00 13.43 ? 208 LEU A CD2 1 
ATOM   1674 N  N   . SER A 1 214 ? 6.258  31.885  -5.550  1.00 12.36 ? 209 SER A N   1 
ATOM   1675 C  CA  . SER A 1 214 ? 5.700  31.160  -6.681  1.00 14.49 ? 209 SER A CA  1 
ATOM   1676 C  C   . SER A 1 214 ? 5.181  29.786  -6.271  1.00 15.00 ? 209 SER A C   1 
ATOM   1677 O  O   . SER A 1 214 ? 5.516  29.283  -5.199  1.00 14.37 ? 209 SER A O   1 
ATOM   1678 C  CB  . SER A 1 214 ? 6.759  30.989  -7.774  1.00 12.01 ? 209 SER A CB  1 
ATOM   1679 O  OG  . SER A 1 214 ? 7.770  30.096  -7.326  1.00 12.60 ? 209 SER A OG  1 
ATOM   1680 N  N   . GLU A 1 215 ? 4.399  29.157  -7.162  1.00 14.65 ? 210 GLU A N   1 
ATOM   1681 C  CA  . GLU A 1 215 ? 3.913  27.812  -6.912  1.00 17.37 ? 210 GLU A CA  1 
ATOM   1682 C  C   . GLU A 1 215 ? 5.056  26.828  -6.634  1.00 16.92 ? 210 GLU A C   1 
ATOM   1683 O  O   . GLU A 1 215 ? 4.975  26.008  -5.725  1.00 14.88 ? 210 GLU A O   1 
ATOM   1684 C  CB  . GLU A 1 215 ? 3.076  27.345  -8.089  1.00 24.42 ? 210 GLU A CB  1 
ATOM   1685 C  CG  . GLU A 1 215 ? 2.492  25.956  -7.905  1.00 32.66 ? 210 GLU A CG  1 
ATOM   1686 C  CD  . GLU A 1 215 ? 1.573  25.547  -9.038  1.00 45.88 ? 210 GLU A CD  1 
ATOM   1687 O  OE1 . GLU A 1 215 ? 1.377  26.368  -9.964  1.00 46.06 ? 210 GLU A OE1 1 
ATOM   1688 O  OE2 . GLU A 1 215 ? 1.054  24.408  -9.003  1.00 59.26 ? 210 GLU A OE2 1 
ATOM   1689 N  N   . ASP A 1 216 ? 6.143  26.906  -7.407  1.00 16.27 ? 211 ASP A N   1 
ATOM   1690 C  CA  . ASP A 1 216 ? 7.247  25.981  -7.200  1.00 17.37 ? 211 ASP A CA  1 
ATOM   1691 C  C   . ASP A 1 216 ? 8.020  26.235  -5.902  1.00 14.49 ? 211 ASP A C   1 
ATOM   1692 O  O   . ASP A 1 216 ? 8.372  25.290  -5.202  1.00 17.28 ? 211 ASP A O   1 
ATOM   1693 C  CB  . ASP A 1 216 ? 8.206  26.036  -8.372  1.00 21.02 ? 211 ASP A CB  1 
ATOM   1694 C  CG  . ASP A 1 216 ? 7.651  25.453  -9.673  1.00 28.13 ? 211 ASP A CG  1 
ATOM   1695 O  OD1 . ASP A 1 216 ? 6.483  25.001  -9.682  1.00 24.94 ? 211 ASP A OD1 1 
ATOM   1696 O  OD2 . ASP A 1 216 ? 8.378  25.450  -10.660 1.00 34.07 ? 211 ASP A OD2 1 
ATOM   1697 N  N   . SER A 1 217 ? 8.274  27.504  -5.576  1.00 12.73 ? 212 SER A N   1 
ATOM   1698 C  CA  . SER A 1 217 ? 8.927  27.841  -4.320  1.00 12.45 ? 212 SER A CA  1 
ATOM   1699 C  C   . SER A 1 217 ? 8.042  27.455  -3.137  1.00 11.98 ? 212 SER A C   1 
ATOM   1700 O  O   . SER A 1 217 ? 8.517  26.965  -2.115  1.00 11.80 ? 212 SER A O   1 
ATOM   1701 C  CB  . SER A 1 217 ? 9.289  29.309  -4.261  1.00 14.56 ? 212 SER A CB  1 
ATOM   1702 O  OG  . SER A 1 217 ? 10.259 29.640  -5.249  1.00 14.59 ? 212 SER A OG  1 
ATOM   1703 N  N   . TYR A 1 218 ? 6.735  27.702  -3.278  1.00 10.14 ? 213 TYR A N   1 
ATOM   1704 C  CA  . TYR A 1 218 ? 5.784  27.294  -2.265  1.00 11.45 ? 213 TYR A CA  1 
ATOM   1705 C  C   . TYR A 1 218 ? 5.874  25.798  -1.969  1.00 11.96 ? 213 TYR A C   1 
ATOM   1706 O  O   . TYR A 1 218 ? 5.961  25.389  -0.803  1.00 13.00 ? 213 TYR A O   1 
ATOM   1707 C  CB  . TYR A 1 218 ? 4.407  27.688  -2.736  1.00 11.51 ? 213 TYR A CB  1 
ATOM   1708 C  CG  . TYR A 1 218 ? 3.263  27.277  -1.855  1.00 12.40 ? 213 TYR A CG  1 
ATOM   1709 C  CD1 . TYR A 1 218 ? 2.666  26.023  -1.987  1.00 14.91 ? 213 TYR A CD1 1 
ATOM   1710 C  CD2 . TYR A 1 218 ? 2.729  28.161  -0.940  1.00 15.42 ? 213 TYR A CD2 1 
ATOM   1711 C  CE1 . TYR A 1 218 ? 1.571  25.663  -1.195  1.00 18.11 ? 213 TYR A CE1 1 
ATOM   1712 C  CE2 . TYR A 1 218 ? 1.656  27.809  -0.139  1.00 23.32 ? 213 TYR A CE2 1 
ATOM   1713 C  CZ  . TYR A 1 218 ? 1.077  26.572  -0.275  1.00 16.41 ? 213 TYR A CZ  1 
ATOM   1714 O  OH  . TYR A 1 218 ? 0.026  26.310  0.561   1.00 29.12 ? 213 TYR A OH  1 
ATOM   1715 N  N   . LYS A 1 219 ? 5.909  24.983  -3.029  1.00 12.44 ? 214 LYS A N   1 
ATOM   1716 C  CA  . LYS A 1 219 ? 6.063  23.553  -2.841  1.00 14.26 ? 214 LYS A CA  1 
ATOM   1717 C  C   . LYS A 1 219 ? 7.363  23.209  -2.116  1.00 13.49 ? 214 LYS A C   1 
ATOM   1718 O  O   . LYS A 1 219 ? 7.340  22.360  -1.236  1.00 13.70 ? 214 LYS A O   1 
ATOM   1719 C  CB  . LYS A 1 219 ? 5.931  22.820  -4.187  1.00 21.27 ? 214 LYS A CB  1 
ATOM   1720 C  CG  . LYS A 1 219 ? 4.473  22.829  -4.662  1.00 29.01 ? 214 LYS A CG  1 
ATOM   1721 C  CD  . LYS A 1 219 ? 4.192  22.020  -5.939  1.00 46.48 ? 214 LYS A CD  1 
ATOM   1722 C  CE  . LYS A 1 219 ? 2.739  22.169  -6.378  1.00 52.34 ? 214 LYS A CE  1 
ATOM   1723 N  NZ  . LYS A 1 219 ? 2.491  21.554  -7.712  1.00 59.79 ? 214 LYS A NZ  1 
ATOM   1724 N  N   . ASP A 1 220 ? 8.476  23.857  -2.484  1.00 11.97 ? 215 ASP A N   1 
ATOM   1725 C  CA  . ASP A 1 220 ? 9.765  23.593  -1.851  1.00 13.23 ? 215 ASP A CA  1 
ATOM   1726 C  C   . ASP A 1 220 ? 9.773  23.919  -0.356  1.00 13.65 ? 215 ASP A C   1 
ATOM   1727 O  O   . ASP A 1 220 ? 10.237 23.132  0.467   1.00 10.70 ? 215 ASP A O   1 
ATOM   1728 C  CB  . ASP A 1 220 ? 10.857 24.406  -2.519  1.00 14.90 ? 215 ASP A CB  1 
ATOM   1729 C  CG  . ASP A 1 220 ? 11.247 23.956  -3.927  1.00 19.71 ? 215 ASP A CG  1 
ATOM   1730 O  OD1 . ASP A 1 220 ? 11.009 22.785  -4.261  1.00 20.23 ? 215 ASP A OD1 1 
ATOM   1731 O  OD2 . ASP A 1 220 ? 11.745 24.791  -4.681  1.00 23.11 ? 215 ASP A OD2 1 
ATOM   1732 N  N   . SER A 1 221 ? 9.231  25.092  -0.006  1.00 10.92 ? 216 SER A N   1 
ATOM   1733 C  CA  . SER A 1 221 ? 9.137  25.511  1.388   1.00 9.50  ? 216 SER A CA  1 
ATOM   1734 C  C   . SER A 1 221 ? 8.187  24.659  2.233   1.00 8.42  ? 216 SER A C   1 
ATOM   1735 O  O   . SER A 1 221 ? 8.498  24.261  3.358   1.00 8.84  ? 216 SER A O   1 
ATOM   1736 C  CB  . SER A 1 221 ? 8.718  26.982  1.436   1.00 9.63  ? 216 SER A CB  1 
ATOM   1737 O  OG  . SER A 1 221 ? 9.730  27.831  0.915   1.00 10.77 ? 216 SER A OG  1 
ATOM   1738 N  N   . THR A 1 222 ? 6.991  24.386  1.711   1.00 8.30  ? 217 THR A N   1 
ATOM   1739 C  CA  . THR A 1 222 ? 6.001  23.669  2.486   1.00 8.59  ? 217 THR A CA  1 
ATOM   1740 C  C   . THR A 1 222 ? 6.442  22.227  2.725   1.00 9.42  ? 217 THR A C   1 
ATOM   1741 O  O   . THR A 1 222 ? 6.130  21.639  3.759   1.00 10.55 ? 217 THR A O   1 
ATOM   1742 C  CB  . THR A 1 222 ? 4.631  23.757  1.827   1.00 10.09 ? 217 THR A CB  1 
ATOM   1743 O  OG1 . THR A 1 222 ? 4.701  23.191  0.522   1.00 9.95  ? 217 THR A OG1 1 
ATOM   1744 C  CG2 . THR A 1 222 ? 4.118  25.184  1.833   1.00 10.57 ? 217 THR A CG2 1 
ATOM   1745 N  N   . LEU A 1 223 ? 7.226  21.660  1.806   1.00 10.89 ? 218 LEU A N   1 
ATOM   1746 C  CA  . LEU A 1 223 ? 7.768  20.328  2.070   1.00 12.94 ? 218 LEU A CA  1 
ATOM   1747 C  C   . LEU A 1 223 ? 8.563  20.273  3.385   1.00 11.61 ? 218 LEU A C   1 
ATOM   1748 O  O   . LEU A 1 223 ? 8.422  19.337  4.170   1.00 11.21 ? 218 LEU A O   1 
ATOM   1749 C  CB  . LEU A 1 223 ? 8.637  19.870  0.905   1.00 14.91 ? 218 LEU A CB  1 
ATOM   1750 C  CG  . LEU A 1 223 ? 9.138  18.430  0.994   1.00 23.95 ? 218 LEU A CG  1 
ATOM   1751 C  CD1 . LEU A 1 223 ? 9.496  17.893  -0.395  1.00 31.78 ? 218 LEU A CD1 1 
ATOM   1752 C  CD2 . LEU A 1 223 ? 10.350 18.285  1.933   1.00 29.04 ? 218 LEU A CD2 1 
ATOM   1753 N  N   . ILE A 1 224 ? 9.454  21.239  3.602   1.00 9.54  ? 219 ILE A N   1 
ATOM   1754 C  CA  . ILE A 1 224 ? 10.252 21.240  4.818   1.00 9.58  ? 219 ILE A CA  1 
ATOM   1755 C  C   . ILE A 1 224 ? 9.430  21.647  6.039   1.00 9.08  ? 219 ILE A C   1 
ATOM   1756 O  O   . ILE A 1 224 ? 9.662  21.187  7.149   1.00 8.85  ? 219 ILE A O   1 
ATOM   1757 C  CB  . ILE A 1 224 ? 11.496 22.106  4.649   1.00 11.01 ? 219 ILE A CB  1 
ATOM   1758 C  CG1 . ILE A 1 224 ? 12.333 21.624  3.432   1.00 12.07 ? 219 ILE A CG1 1 
ATOM   1759 C  CG2 . ILE A 1 224 ? 12.325 22.127  5.958   1.00 11.53 ? 219 ILE A CG2 1 
ATOM   1760 C  CD1 . ILE A 1 224 ? 13.407 22.583  3.058   1.00 14.04 ? 219 ILE A CD1 1 
ATOM   1761 N  N   . MET A 1 225 ? 8.477  22.562  5.845   1.00 10.54 ? 220 MET A N   1 
ATOM   1762 C  CA  . MET A 1 225 ? 7.616  22.981  6.936   1.00 9.16  ? 220 MET A CA  1 
ATOM   1763 C  C   . MET A 1 225 ? 6.858  21.784  7.492   1.00 8.82  ? 220 MET A C   1 
ATOM   1764 O  O   . MET A 1 225 ? 6.611  21.711  8.698   1.00 7.75  ? 220 MET A O   1 
ATOM   1765 C  CB  . MET A 1 225 ? 6.645  24.069  6.464   1.00 8.87  ? 220 MET A CB  1 
ATOM   1766 C  CG  . MET A 1 225 ? 7.316  25.384  6.203   1.00 9.21  ? 220 MET A CG  1 
ATOM   1767 S  SD  . MET A 1 225 ? 6.173  26.545  5.326   1.00 11.69 ? 220 MET A SD  1 
ATOM   1768 C  CE  . MET A 1 225 ? 5.095  26.832  6.577   1.00 10.97 ? 220 MET A CE  1 
ATOM   1769 N  N   . GLN A 1 226 ? 6.456  20.860  6.612   1.00 8.56  ? 221 GLN A N   1 
ATOM   1770 C  CA  . GLN A 1 226 ? 5.749  19.677  7.057   1.00 8.72  ? 221 GLN A CA  1 
ATOM   1771 C  C   . GLN A 1 226 ? 6.592  18.801  7.990   1.00 8.73  ? 221 GLN A C   1 
ATOM   1772 O  O   . GLN A 1 226 ? 6.057  18.210  8.934   1.00 7.73  ? 221 GLN A O   1 
ATOM   1773 C  CB  . GLN A 1 226 ? 5.252  18.838  5.850   1.00 13.17 ? 221 GLN A CB  1 
ATOM   1774 C  CG  . GLN A 1 226 ? 4.472  17.567  6.251   1.00 18.54 ? 221 GLN A CG  1 
ATOM   1775 C  CD  . GLN A 1 226 ? 3.211  17.898  7.010   1.00 24.85 ? 221 GLN A CD  1 
ATOM   1776 O  OE1 . GLN A 1 226 ? 2.400  18.719  6.561   1.00 29.24 ? 221 GLN A OE1 1 
ATOM   1777 N  NE2 . GLN A 1 226 ? 3.024  17.282  8.181   1.00 21.34 ? 221 GLN A NE2 1 
ATOM   1778 N  N   . LEU A 1 227 ? 7.910  18.760  7.751   1.00 7.66  ? 222 LEU A N   1 
ATOM   1779 C  CA  . LEU A 1 227 ? 8.802  18.031  8.634   1.00 8.38  ? 222 LEU A CA  1 
ATOM   1780 C  C   . LEU A 1 227 ? 8.884  18.661  10.026  1.00 8.21  ? 222 LEU A C   1 
ATOM   1781 O  O   . LEU A 1 227 ? 8.941  17.944  11.012  1.00 9.17  ? 222 LEU A O   1 
ATOM   1782 C  CB  . LEU A 1 227 ? 10.170 17.976  7.996   1.00 8.56  ? 222 LEU A CB  1 
ATOM   1783 C  CG  . LEU A 1 227 ? 10.217 17.357  6.607   1.00 10.28 ? 222 LEU A CG  1 
ATOM   1784 C  CD1 . LEU A 1 227 ? 11.636 17.327  6.105   1.00 10.63 ? 222 LEU A CD1 1 
ATOM   1785 C  CD2 . LEU A 1 227 ? 9.572  15.949  6.607   1.00 11.10 ? 222 LEU A CD2 1 
ATOM   1786 N  N   . LEU A 1 228 ? 8.895  20.008  10.100  1.00 8.55  ? 223 LEU A N   1 
ATOM   1787 C  CA  . LEU A 1 228 ? 8.831  20.705  11.373  1.00 8.51  ? 223 LEU A CA  1 
ATOM   1788 C  C   . LEU A 1 228 ? 7.564  20.303  12.116  1.00 9.34  ? 223 LEU A C   1 
ATOM   1789 O  O   . LEU A 1 228 ? 7.587  20.018  13.316  1.00 9.12  ? 223 LEU A O   1 
ATOM   1790 C  CB  . LEU A 1 228 ? 8.837  22.241  11.162  1.00 8.26  ? 223 LEU A CB  1 
ATOM   1791 C  CG  . LEU A 1 228 ? 10.112 22.850  10.596  1.00 7.97  ? 223 LEU A CG  1 
ATOM   1792 C  CD1 . LEU A 1 228 ? 9.851  24.256  10.035  1.00 9.52  ? 223 LEU A CD1 1 
ATOM   1793 C  CD2 . LEU A 1 228 ? 11.237 22.922  11.685  1.00 8.78  ? 223 LEU A CD2 1 
ATOM   1794 N  N   . ARG A 1 229 ? 6.445  20.299  11.390  1.00 10.69 ? 224 ARG A N   1 
ATOM   1795 C  CA  . ARG A 1 229 ? 5.170  19.898  11.977  1.00 10.62 ? 224 ARG A CA  1 
ATOM   1796 C  C   . ARG A 1 229 ? 5.159  18.434  12.419  1.00 8.81  ? 224 ARG A C   1 
ATOM   1797 O  O   . ARG A 1 229 ? 4.667  18.114  13.501  1.00 11.01 ? 224 ARG A O   1 
ATOM   1798 C  CB  . ARG A 1 229 ? 4.068  20.178  10.953  1.00 14.13 ? 224 ARG A CB  1 
ATOM   1799 C  CG  . ARG A 1 229 ? 2.715  19.590  11.215  1.00 21.39 ? 224 ARG A CG  1 
ATOM   1800 C  CD  . ARG A 1 229 ? 2.013  20.209  12.396  1.00 33.41 ? 224 ARG A CD  1 
ATOM   1801 N  NE  . ARG A 1 229 ? 2.011  21.668  12.347  1.00 35.59 ? 224 ARG A NE  1 
ATOM   1802 C  CZ  . ARG A 1 229 ? 2.200  22.457  13.401  1.00 50.83 ? 224 ARG A CZ  1 
ATOM   1803 N  NH1 . ARG A 1 229 ? 2.126  21.989  14.640  1.00 45.93 ? 224 ARG A NH1 1 
ATOM   1804 N  NH2 . ARG A 1 229 ? 2.442  23.752  13.209  1.00 48.32 ? 224 ARG A NH2 1 
ATOM   1805 N  N   . ASP A 1 230 ? 5.767  17.547  11.629  1.00 9.02  ? 225 ASP A N   1 
ATOM   1806 C  CA  . ASP A 1 230 ? 5.855  16.145  12.000  1.00 8.93  ? 225 ASP A CA  1 
ATOM   1807 C  C   . ASP A 1 230 ? 6.624  15.968  13.311  1.00 7.58  ? 225 ASP A C   1 
ATOM   1808 O  O   . ASP A 1 230 ? 6.219  15.199  14.190  1.00 7.84  ? 225 ASP A O   1 
ATOM   1809 C  CB  . ASP A 1 230 ? 6.541  15.317  10.933  1.00 10.82 ? 225 ASP A CB  1 
ATOM   1810 C  CG  . ASP A 1 230 ? 5.845  15.161  9.603   1.00 13.73 ? 225 ASP A CG  1 
ATOM   1811 O  OD1 . ASP A 1 230 ? 4.602  15.377  9.548   1.00 15.30 ? 225 ASP A OD1 1 
ATOM   1812 O  OD2 . ASP A 1 230 ? 6.539  14.808  8.621   1.00 14.74 ? 225 ASP A OD2 1 
ATOM   1813 N  N   . ASN A 1 231 ? 7.753  16.682  13.440  1.00 8.68  ? 226 ASN A N   1 
ATOM   1814 C  CA  . ASN A 1 231 ? 8.491  16.682  14.696  1.00 8.15  ? 226 ASN A CA  1 
ATOM   1815 C  C   . ASN A 1 231 ? 7.692  17.251  15.875  1.00 8.93  ? 226 ASN A C   1 
ATOM   1816 O  O   . ASN A 1 231 ? 7.718  16.707  16.980  1.00 9.26  ? 226 ASN A O   1 
ATOM   1817 C  CB  . ASN A 1 231 ? 9.813  17.421  14.529  1.00 7.74  ? 226 ASN A CB  1 
ATOM   1818 C  CG  . ASN A 1 231 ? 10.851 16.620  13.787  1.00 7.98  ? 226 ASN A CG  1 
ATOM   1819 O  OD1 . ASN A 1 231 ? 10.721 15.384  13.636  1.00 8.80  ? 226 ASN A OD1 1 
ATOM   1820 N  ND2 . ASN A 1 231 ? 11.893 17.300  13.266  1.00 8.53  ? 226 ASN A ND2 1 
ATOM   1821 N  N   . LEU A 1 232 ? 7.009  18.374  15.678  1.00 8.95  ? 227 LEU A N   1 
ATOM   1822 C  CA  . LEU A 1 232 ? 6.206  18.920  16.756  1.00 8.84  ? 227 LEU A CA  1 
ATOM   1823 C  C   . LEU A 1 232 ? 5.126  17.934  17.192  1.00 10.09 ? 227 LEU A C   1 
ATOM   1824 O  O   . LEU A 1 232 ? 4.860  17.840  18.386  1.00 12.44 ? 227 LEU A O   1 
ATOM   1825 C  CB  . LEU A 1 232 ? 5.583  20.229  16.341  1.00 8.36  ? 227 LEU A CB  1 
ATOM   1826 C  CG  . LEU A 1 232 ? 6.571  21.399  16.278  1.00 8.67  ? 227 LEU A CG  1 
ATOM   1827 C  CD1 . LEU A 1 232 ? 5.951  22.534  15.485  1.00 10.78 ? 227 LEU A CD1 1 
ATOM   1828 C  CD2 . LEU A 1 232 ? 7.012  21.793  17.686  1.00 8.06  ? 227 LEU A CD2 1 
ATOM   1829 N  N   . THR A 1 233 ? 4.572  17.169  16.243  1.00 11.51 ? 228 THR A N   1 
ATOM   1830 C  CA  . THR A 1 233 ? 3.589  16.141  16.592  1.00 14.04 ? 228 THR A CA  1 
ATOM   1831 C  C   . THR A 1 233 ? 4.215  15.014  17.419  1.00 17.40 ? 228 THR A C   1 
ATOM   1832 O  O   . THR A 1 233 ? 3.627  14.502  18.380  1.00 14.30 ? 228 THR A O   1 
ATOM   1833 C  CB  . THR A 1 233 ? 2.914  15.639  15.324  1.00 13.64 ? 228 THR A CB  1 
ATOM   1834 O  OG1 . THR A 1 233 ? 2.269  16.747  14.724  1.00 16.54 ? 228 THR A OG1 1 
ATOM   1835 C  CG2 . THR A 1 233 ? 1.928  14.508  15.596  1.00 17.80 ? 228 THR A CG2 1 
ATOM   1836 N  N   . LEU A 1 234 ? 5.440  14.646  17.043  1.00 13.06 ? 229 LEU A N   1 
ATOM   1837 C  CA  . LEU A 1 234 ? 6.187  13.610  17.723  1.00 14.71 ? 229 LEU A CA  1 
ATOM   1838 C  C   . LEU A 1 234 ? 6.564  14.100  19.117  1.00 14.58 ? 229 LEU A C   1 
ATOM   1839 O  O   . LEU A 1 234 ? 6.549  13.320  20.055  1.00 13.98 ? 229 LEU A O   1 
ATOM   1840 C  CB  . LEU A 1 234 ? 7.436  13.291  16.898  1.00 17.07 ? 229 LEU A CB  1 
ATOM   1841 C  CG  . LEU A 1 234 ? 8.381  12.255  17.449  1.00 20.73 ? 229 LEU A CG  1 
ATOM   1842 C  CD1 . LEU A 1 234 ? 7.746  10.864  17.399  1.00 21.35 ? 229 LEU A CD1 1 
ATOM   1843 C  CD2 . LEU A 1 234 ? 9.663  12.222  16.652  1.00 22.01 ? 229 LEU A CD2 1 
ATOM   1844 N  N   . TRP A 1 235 ? 6.870  15.398  19.252  1.00 12.83 ? 230 TRP A N   1 
ATOM   1845 C  CA  . TRP A 1 235 ? 7.449  15.928  20.479  1.00 13.36 ? 230 TRP A CA  1 
ATOM   1846 C  C   . TRP A 1 235 ? 6.439  16.386  21.523  1.00 16.84 ? 230 TRP A C   1 
ATOM   1847 O  O   . TRP A 1 235 ? 6.825  16.632  22.658  1.00 15.23 ? 230 TRP A O   1 
ATOM   1848 C  CB  . TRP A 1 235 ? 8.347  17.133  20.155  1.00 13.27 ? 230 TRP A CB  1 
ATOM   1849 C  CG  . TRP A 1 235 ? 9.556  16.780  19.341  1.00 11.44 ? 230 TRP A CG  1 
ATOM   1850 C  CD1 . TRP A 1 235 ? 10.067 15.532  19.122  1.00 10.67 ? 230 TRP A CD1 1 
ATOM   1851 C  CD2 . TRP A 1 235 ? 10.380 17.689  18.589  1.00 10.42 ? 230 TRP A CD2 1 
ATOM   1852 N  NE1 . TRP A 1 235 ? 11.182 15.613  18.312  1.00 9.98  ? 230 TRP A NE1 1 
ATOM   1853 C  CE2 . TRP A 1 235 ? 11.401 16.924  17.977  1.00 9.22  ? 230 TRP A CE2 1 
ATOM   1854 C  CE3 . TRP A 1 235 ? 10.352 19.072  18.369  1.00 9.68  ? 230 TRP A CE3 1 
ATOM   1855 C  CZ2 . TRP A 1 235 ? 12.389 17.496  17.160  1.00 9.59  ? 230 TRP A CZ2 1 
ATOM   1856 C  CZ3 . TRP A 1 235 ? 11.341 19.639  17.560  1.00 9.02  ? 230 TRP A CZ3 1 
ATOM   1857 C  CH2 . TRP A 1 235 ? 12.355 18.848  16.989  1.00 8.50  ? 230 TRP A CH2 1 
ATOM   1858 N  N   . THR A 1 236 ? 5.185  16.578  21.102  1.00 18.48 ? 231 THR A N   1 
ATOM   1859 C  CA  . THR A 1 236 ? 4.146  17.104  21.970  1.00 20.64 ? 231 THR A CA  1 
ATOM   1860 C  C   . THR A 1 236 ? 2.928  16.175  21.976  1.00 27.05 ? 231 THR A C   1 
ATOM   1861 O  O   . THR A 1 236 ? 1.892  16.500  22.576  1.00 34.54 ? 231 THR A O   1 
ATOM   1862 C  CB  . THR A 1 236 ? 3.809  18.532  21.531  1.00 21.35 ? 231 THR A CB  1 
ATOM   1863 O  OG1 . THR A 1 236 ? 3.229  18.518  20.221  1.00 20.17 ? 231 THR A OG1 1 
ATOM   1864 C  CG2 . THR A 1 236 ? 5.020  19.426  21.529  1.00 20.37 ? 231 THR A CG2 1 
ATOM   1865 O  OXT . THR A 1 236 ? 2.970  15.096  21.379  1.00 33.81 ? 231 THR A OXT 1 
ATOM   1866 N  N   . GLN B 2 1   ? 10.976 6.237   17.934  1.00 39.01 ? 255 GLN P N   1 
ATOM   1867 C  CA  . GLN B 2 1   ? 10.936 6.998   16.687  1.00 32.57 ? 255 GLN P CA  1 
ATOM   1868 C  C   . GLN B 2 1   ? 11.765 8.275   16.807  1.00 27.46 ? 255 GLN P C   1 
ATOM   1869 O  O   . GLN B 2 1   ? 11.421 9.169   17.574  1.00 29.08 ? 255 GLN P O   1 
ATOM   1870 C  CB  . GLN B 2 1   ? 9.510  7.380   16.310  1.00 34.88 ? 255 GLN P CB  1 
ATOM   1871 C  CG  . GLN B 2 1   ? 9.446  7.973   14.922  1.00 37.99 ? 255 GLN P CG  1 
ATOM   1872 C  CD  . GLN B 2 1   ? 8.075  8.443   14.560  1.00 45.31 ? 255 GLN P CD  1 
ATOM   1873 O  OE1 . GLN B 2 1   ? 7.898  9.199   13.594  1.00 50.47 ? 255 GLN P OE1 1 
ATOM   1874 N  NE2 . GLN B 2 1   ? 7.075  8.030   15.333  1.00 47.43 ? 255 GLN P NE2 1 
ATOM   1875 N  N   . ARG B 2 2   ? 12.841 8.355   16.024  1.00 25.00 ? 256 ARG P N   1 
ATOM   1876 C  CA  . ARG B 2 2   ? 13.720 9.514   16.034  1.00 22.87 ? 256 ARG P CA  1 
ATOM   1877 C  C   . ARG B 2 2   ? 13.138 10.683  15.258  1.00 17.27 ? 256 ARG P C   1 
ATOM   1878 O  O   . ARG B 2 2   ? 12.323 10.516  14.358  1.00 19.96 ? 256 ARG P O   1 
ATOM   1879 C  CB  . ARG B 2 2   ? 15.080 9.181   15.443  1.00 24.56 ? 256 ARG P CB  1 
ATOM   1880 C  CG  . ARG B 2 2   ? 15.838 8.238   16.303  1.00 33.42 ? 256 ARG P CG  1 
ATOM   1881 C  CD  . ARG B 2 2   ? 17.120 7.775   15.683  1.00 34.21 ? 256 ARG P CD  1 
ATOM   1882 N  NE  . ARG B 2 2   ? 17.571 6.594   16.413  1.00 41.28 ? 256 ARG P NE  1 
ATOM   1883 C  CZ  . ARG B 2 2   ? 18.507 6.604   17.351  1.00 38.13 ? 256 ARG P CZ  1 
ATOM   1884 N  NH1 . ARG B 2 2   ? 19.215 7.694   17.608  1.00 32.47 ? 256 ARG P NH1 1 
ATOM   1885 N  NH2 . ARG B 2 2   ? 18.757 5.487   18.030  1.00 36.41 ? 256 ARG P NH2 1 
ATOM   1886 N  N   . SER B 2 3   ? 13.608 11.875  15.610  1.00 16.39 ? 257 SER P N   1 
ATOM   1887 C  CA  . SER B 2 3   ? 13.196 13.078  14.923  1.00 14.76 ? 257 SER P CA  1 
ATOM   1888 C  C   . SER B 2 3   ? 13.640 13.030  13.462  1.00 14.05 ? 257 SER P C   1 
ATOM   1889 O  O   . SER B 2 3   ? 14.653 12.412  13.128  1.00 15.15 ? 257 SER P O   1 
ATOM   1890 C  CB  . SER B 2 3   ? 13.769 14.294  15.636  1.00 14.58 ? 257 SER P CB  1 
ATOM   1891 O  OG  . SER B 2 3   ? 13.501 14.239  17.036  1.00 11.93 ? 257 SER P OG  1 
ATOM   1892 N  N   . THR B 2 4   ? 12.855 13.695  12.611  1.00 10.59 ? 258 THR P N   1 
ATOM   1893 C  CA  . THR B 2 4   ? 13.161 13.808  11.200  1.00 10.39 ? 258 THR P CA  1 
ATOM   1894 C  C   . THR B 2 4   ? 14.074 14.997  10.963  1.00 8.06  ? 258 THR P C   1 
ATOM   1895 O  O   . THR B 2 4   ? 13.748 16.113  11.360  1.00 6.92  ? 258 THR P O   1 
ATOM   1896 C  CB  . THR B 2 4   ? 11.906 13.974  10.370  1.00 10.59 ? 258 THR P CB  1 
ATOM   1897 O  OG1 . THR B 2 4   ? 11.026 12.940  10.707  1.00 11.00 ? 258 THR P OG1 1 
ATOM   1898 C  CG2 . THR B 2 4   ? 12.199 13.918  8.896   1.00 10.93 ? 258 THR P CG2 1 
HETATM 1899 N  N   . SEP B 2 5   ? 15.200 14.753  10.282  1.00 7.94  ? 259 SEP P N   1 
HETATM 1900 C  CA  . SEP B 2 5   ? 16.046 15.845  9.842   1.00 6.64  ? 259 SEP P CA  1 
HETATM 1901 C  CB  . SEP B 2 5   ? 17.503 15.583  10.198  1.00 7.24  ? 259 SEP P CB  1 
HETATM 1902 O  OG  . SEP B 2 5   ? 17.923 14.379  9.539   1.00 5.74  ? 259 SEP P OG  1 
HETATM 1903 C  C   . SEP B 2 5   ? 15.847 16.085  8.349   1.00 6.86  ? 259 SEP P C   1 
HETATM 1904 O  O   . SEP B 2 5   ? 15.064 15.395  7.701   1.00 8.24  ? 259 SEP P O   1 
HETATM 1905 P  P   . SEP B 2 5   ? 19.366 13.803  9.935   1.00 6.47  ? 259 SEP P P   1 
HETATM 1906 O  O1P . SEP B 2 5   ? 19.498 12.600  9.028   1.00 6.33  ? 259 SEP P O1P 1 
HETATM 1907 O  O2P . SEP B 2 5   ? 20.343 14.904  9.637   1.00 7.00  ? 259 SEP P O2P 1 
HETATM 1908 O  O3P . SEP B 2 5   ? 19.339 13.442  11.393  1.00 6.45  ? 259 SEP P O3P 1 
ATOM   1909 N  N   . THR B 2 6   ? 16.575 17.064  7.806   1.00 6.86  ? 260 THR P N   1 
ATOM   1910 C  CA  . THR B 2 6   ? 16.352 17.491  6.440   1.00 8.87  ? 260 THR P CA  1 
ATOM   1911 C  C   . THR B 2 6   ? 16.710 16.349  5.506   1.00 11.59 ? 260 THR P C   1 
ATOM   1912 O  O   . THR B 2 6   ? 17.771 15.760  5.621   1.00 12.53 ? 260 THR P O   1 
ATOM   1913 C  CB  . THR B 2 6   ? 17.146 18.747  6.075   1.00 13.06 ? 260 THR P CB  1 
ATOM   1914 O  OG1 . THR B 2 6   ? 16.794 19.796  6.949   1.00 13.32 ? 260 THR P OG1 1 
ATOM   1915 C  CG2 . THR B 2 6   ? 16.881 19.173  4.659   1.00 16.26 ? 260 THR P CG2 1 
ATOM   1916 N  N   . PRO B 2 7   ? 15.828 15.977  4.562   1.00 11.30 ? 261 PRO P N   1 
ATOM   1917 C  CA  . PRO B 2 7   ? 16.150 14.924  3.600   1.00 14.24 ? 261 PRO P CA  1 
ATOM   1918 C  C   . PRO B 2 7   ? 16.985 15.447  2.432   1.00 15.36 ? 261 PRO P C   1 
ATOM   1919 O  O   . PRO B 2 7   ? 17.256 16.647  2.333   1.00 14.37 ? 261 PRO P O   1 
ATOM   1920 C  CB  . PRO B 2 7   ? 14.753 14.449  3.156   1.00 15.36 ? 261 PRO P CB  1 
ATOM   1921 C  CG  . PRO B 2 7   ? 13.923 15.697  3.206   1.00 14.67 ? 261 PRO P CG  1 
ATOM   1922 C  CD  . PRO B 2 7   ? 14.465 16.515  4.405   1.00 13.74 ? 261 PRO P CD  1 
ATOM   1923 N  N   . ASN B 2 8   ? 17.371 14.548  1.524   1.00 18.26 ? 262 ASN P N   1 
ATOM   1924 C  CA  . ASN B 2 8   ? 17.993 14.949  0.265   1.00 17.41 ? 262 ASN P CA  1 
ATOM   1925 C  C   . ASN B 2 8   ? 16.999 15.639  -0.668  1.00 30.41 ? 262 ASN P C   1 
ATOM   1926 O  O   . ASN B 2 8   ? 16.020 15.028  -1.078  1.00 35.65 ? 262 ASN P O   1 
ATOM   1927 C  CB  . ASN B 2 8   ? 18.599 13.745  -0.381  1.00 21.12 ? 262 ASN P CB  1 
ATOM   1928 C  CG  . ASN B 2 8   ? 19.827 13.268  0.378   1.00 28.19 ? 262 ASN P CG  1 
ATOM   1929 O  OD1 . ASN B 2 8   ? 20.678 14.060  0.864   1.00 25.08 ? 262 ASN P OD1 1 
ATOM   1930 N  ND2 . ASN B 2 8   ? 19.951 11.977  0.540   1.00 31.23 ? 262 ASN P ND2 1 
ATOM   1931 N  N   . VAL B 2 9   ? 17.249 16.926  -0.941  1.00 42.70 ? 263 VAL P N   1 
ATOM   1932 C  CA  . VAL B 2 9   ? 16.366 17.807  -1.700  1.00 59.49 ? 263 VAL P CA  1 
ATOM   1933 C  C   . VAL B 2 9   ? 17.208 19.062  -1.938  1.00 59.69 ? 263 VAL P C   1 
ATOM   1934 O  O   . VAL B 2 9   ? 18.194 19.263  -1.236  1.00 76.16 ? 263 VAL P O   1 
ATOM   1935 C  CB  . VAL B 2 9   ? 14.999 18.154  -1.002  1.00 65.39 ? 263 VAL P CB  1 
ATOM   1936 C  CG1 . VAL B 2 9   ? 14.002 16.989  -1.016  1.00 67.99 ? 263 VAL P CG1 1 
ATOM   1937 C  CG2 . VAL B 2 9   ? 15.197 18.672  0.415   1.00 61.32 ? 263 VAL P CG2 1 
ATOM   1938 N  N   . HIS B 2 10  ? 16.832 19.916  -2.903  1.00 50.67 ? 264 HIS P N   1 
ATOM   1939 C  CA  . HIS B 2 10  ? 17.748 20.952  -3.380  1.00 55.49 ? 264 HIS P CA  1 
ATOM   1940 C  C   . HIS B 2 10  ? 18.122 22.006  -2.294  1.00 40.21 ? 264 HIS P C   1 
ATOM   1941 O  O   . HIS B 2 10  ? 17.327 22.859  -1.909  1.00 40.82 ? 264 HIS P O   1 
ATOM   1942 C  CB  . HIS B 2 10  ? 17.225 21.676  -4.656  1.00 49.38 ? 264 HIS P CB  1 
ATOM   1943 C  CG  . HIS B 2 10  ? 18.322 22.294  -5.477  1.00 52.00 ? 264 HIS P CG  1 
ATOM   1944 N  ND1 . HIS B 2 10  ? 19.327 21.516  -6.048  1.00 54.48 ? 264 HIS P ND1 1 
ATOM   1945 C  CD2 . HIS B 2 10  ? 18.559 23.590  -5.785  1.00 51.37 ? 264 HIS P CD2 1 
ATOM   1946 C  CE1 . HIS B 2 10  ? 20.129 22.358  -6.689  1.00 48.26 ? 264 HIS P CE1 1 
ATOM   1947 N  NE2 . HIS B 2 10  ? 19.710 23.620  -6.551  1.00 49.23 ? 264 HIS P NE2 1 
HETATM 1948 CL CL  . CL  C 3 .   ? 35.408 -6.241  13.523  1.00 11.38 ? 301 CL  A CL  1 
HETATM 1949 MG MG  . MG  D 4 .   ? 35.088 4.259   19.489  1.00 24.23 2 302 MG  A MG  1 
HETATM 1950 MG MG  . MG  E 4 .   ? 22.151 -18.449 30.566  1.00 16.02 2 303 MG  A MG  1 
HETATM 1951 CA CA  . CA  F 5 .   ? 32.164 15.007  -20.817 1.00 43.63 2 304 CA  A CA  1 
HETATM 1952 CA CA  . CA  G 5 .   ? 33.852 33.341  -2.466  1.00 14.48 2 305 CA  A CA  1 
HETATM 1953 O  O   . HOH H 6 .   ? 31.741 2.318   6.423   1.00 14.21 ? 401 HOH A O   1 
HETATM 1954 O  O   . HOH H 6 .   ? 1.945  13.746  19.796  1.00 15.45 ? 402 HOH A O   1 
HETATM 1955 O  O   . HOH H 6 .   ? 38.040 -2.962  18.591  1.00 25.84 ? 403 HOH A O   1 
HETATM 1956 O  O   . HOH H 6 .   ? 34.139 0.761   22.761  1.00 28.06 ? 404 HOH A O   1 
HETATM 1957 O  O   . HOH H 6 .   ? 23.512 12.033  -15.373 1.00 21.55 ? 405 HOH A O   1 
HETATM 1958 O  O   . HOH H 6 .   ? 5.124  31.249  16.850  1.00 23.60 ? 406 HOH A O   1 
HETATM 1959 O  O   . HOH H 6 .   ? 40.408 16.826  1.599   1.00 22.98 ? 407 HOH A O   1 
HETATM 1960 O  O   . HOH H 6 .   ? 30.214 -3.765  24.840  1.00 21.19 ? 408 HOH A O   1 
HETATM 1961 O  O   . HOH H 6 .   ? 34.998 18.167  27.096  1.00 27.68 ? 409 HOH A O   1 
HETATM 1962 O  O   . HOH H 6 .   ? 10.286 26.910  -11.388 1.00 28.78 ? 410 HOH A O   1 
HETATM 1963 O  O   . HOH H 6 .   ? 7.381  35.813  8.270   1.00 15.28 ? 411 HOH A O   1 
HETATM 1964 O  O   . HOH H 6 .   ? 22.989 0.673   6.988   1.00 24.69 ? 412 HOH A O   1 
HETATM 1965 O  O   . HOH H 6 .   ? 20.489 15.229  -6.693  1.00 34.61 ? 413 HOH A O   1 
HETATM 1966 O  O   . HOH H 6 .   ? 41.896 26.409  7.352   1.00 37.47 ? 414 HOH A O   1 
HETATM 1967 O  O   . HOH H 6 .   ? 27.194 38.104  -1.367  1.00 15.89 ? 415 HOH A O   1 
HETATM 1968 O  O   . HOH H 6 .   ? 38.716 -7.108  21.598  1.00 15.44 ? 416 HOH A O   1 
HETATM 1969 O  O   . HOH H 6 .   ? 6.681  37.662  4.779   1.00 32.47 ? 417 HOH A O   1 
HETATM 1970 O  O   . HOH H 6 .   ? 24.278 -12.101 24.782  1.00 25.61 ? 418 HOH A O   1 
HETATM 1971 O  O   . HOH H 6 .   ? 22.805 7.443   15.311  1.00 17.05 ? 419 HOH A O   1 
HETATM 1972 O  O   . HOH H 6 .   ? 37.016 -2.966  16.192  1.00 12.35 ? 420 HOH A O   1 
HETATM 1973 O  O   . HOH H 6 .   ? 28.895 21.681  -12.710 1.00 12.46 ? 421 HOH A O   1 
HETATM 1974 O  O   . HOH H 6 .   ? 35.585 5.014   17.516  1.00 22.28 ? 422 HOH A O   1 
HETATM 1975 O  O   . HOH H 6 .   ? 17.252 30.573  21.782  1.00 8.79  ? 423 HOH A O   1 
HETATM 1976 O  O   . HOH H 6 .   ? 27.239 34.513  14.598  1.00 34.58 ? 424 HOH A O   1 
HETATM 1977 O  O   . HOH H 6 .   ? 26.905 1.016   21.900  1.00 19.09 ? 425 HOH A O   1 
HETATM 1978 O  O   . HOH H 6 .   ? 41.870 14.910  -5.132  1.00 13.57 ? 426 HOH A O   1 
HETATM 1979 O  O   . HOH H 6 .   ? 14.136 31.394  15.552  1.00 17.95 ? 427 HOH A O   1 
HETATM 1980 O  O   . HOH H 6 .   ? 27.269 3.763   4.123   1.00 16.43 ? 428 HOH A O   1 
HETATM 1981 O  O   . HOH H 6 .   ? 41.477 10.078  -11.228 1.00 26.53 ? 429 HOH A O   1 
HETATM 1982 O  O   . HOH H 6 .   ? 33.931 1.796   -5.972  1.00 26.50 ? 430 HOH A O   1 
HETATM 1983 O  O   . HOH H 6 .   ? 37.738 7.288   14.850  1.00 36.22 ? 431 HOH A O   1 
HETATM 1984 O  O   . HOH H 6 .   ? 8.925  15.548  23.808  1.00 30.42 ? 432 HOH A O   1 
HETATM 1985 O  O   . HOH H 6 .   ? 30.088 4.820   21.012  1.00 9.79  ? 433 HOH A O   1 
HETATM 1986 O  O   . HOH H 6 .   ? 35.772 6.172   7.055   1.00 15.23 ? 434 HOH A O   1 
HETATM 1987 O  O   . HOH H 6 .   ? 25.408 15.891  3.900   1.00 12.55 ? 435 HOH A O   1 
HETATM 1988 O  O   . HOH H 6 .   ? 11.095 30.817  19.678  1.00 16.13 ? 436 HOH A O   1 
HETATM 1989 O  O   . HOH H 6 .   ? 20.756 37.285  12.869  1.00 16.99 ? 437 HOH A O   1 
HETATM 1990 O  O   . HOH H 6 .   ? 4.947  12.936  13.716  1.00 22.23 ? 438 HOH A O   1 
HETATM 1991 O  O   . HOH H 6 .   ? 28.782 -6.851  23.937  1.00 28.27 ? 439 HOH A O   1 
HETATM 1992 O  O   . HOH H 6 .   ? 31.191 20.519  31.781  1.00 13.33 ? 440 HOH A O   1 
HETATM 1993 O  O   . HOH H 6 .   ? 19.872 10.913  -4.671  1.00 31.80 ? 441 HOH A O   1 
HETATM 1994 O  O   . HOH H 6 .   ? 34.996 -14.865 21.529  1.00 18.09 ? 442 HOH A O   1 
HETATM 1995 O  O   . HOH H 6 .   ? 33.535 7.610   -0.785  1.00 7.95  ? 443 HOH A O   1 
HETATM 1996 O  O   . HOH H 6 .   ? 20.733 1.870   18.859  1.00 21.34 ? 444 HOH A O   1 
HETATM 1997 O  O   . HOH H 6 .   ? 20.335 6.608   8.642   1.00 22.55 ? 445 HOH A O   1 
HETATM 1998 O  O   . HOH H 6 .   ? 37.075 23.787  -3.234  1.00 10.12 ? 446 HOH A O   1 
HETATM 1999 O  O   . HOH H 6 .   ? 23.157 8.023   19.410  1.00 23.70 ? 447 HOH A O   1 
HETATM 2000 O  O   . HOH H 6 .   ? 42.400 20.247  -17.794 1.00 6.24  ? 448 HOH A O   1 
HETATM 2001 O  O   . HOH H 6 .   ? 23.478 19.538  3.713   1.00 24.99 ? 449 HOH A O   1 
HETATM 2002 O  O   . HOH H 6 .   ? 20.208 23.508  23.521  1.00 9.08  ? 450 HOH A O   1 
HETATM 2003 O  O   . HOH H 6 .   ? 27.933 30.358  19.395  1.00 32.38 ? 451 HOH A O   1 
HETATM 2004 O  O   . HOH H 6 .   ? 20.511 9.796   -17.490 1.00 40.10 ? 452 HOH A O   1 
HETATM 2005 O  O   . HOH H 6 .   ? 28.750 20.833  25.264  1.00 12.94 ? 453 HOH A O   1 
HETATM 2006 O  O   . HOH H 6 .   ? 13.509 10.628  19.852  1.00 30.56 ? 454 HOH A O   1 
HETATM 2007 O  O   . HOH H 6 .   ? 22.306 17.515  -9.971  1.00 27.22 ? 455 HOH A O   1 
HETATM 2008 O  O   . HOH H 6 .   ? 26.307 24.019  -11.493 1.00 16.78 ? 456 HOH A O   1 
HETATM 2009 O  O   . HOH H 6 .   ? 33.224 26.944  -9.551  1.00 14.76 ? 457 HOH A O   1 
HETATM 2010 O  O   . HOH H 6 .   ? 27.169 33.967  12.026  1.00 30.47 ? 458 HOH A O   1 
HETATM 2011 O  O   . HOH H 6 .   ? 23.700 13.582  23.667  1.00 22.26 ? 459 HOH A O   1 
HETATM 2012 O  O   . HOH H 6 .   ? -0.342 17.521  21.504  1.00 30.80 ? 460 HOH A O   1 
HETATM 2013 O  O   . HOH H 6 .   ? 22.076 12.344  -10.870 1.00 13.90 ? 461 HOH A O   1 
HETATM 2014 O  O   . HOH H 6 .   ? 33.802 27.773  -0.965  1.00 7.98  ? 462 HOH A O   1 
HETATM 2015 O  O   . HOH H 6 .   ? 23.239 16.467  26.014  1.00 24.30 ? 463 HOH A O   1 
HETATM 2016 O  O   . HOH H 6 .   ? 36.301 29.384  -7.399  1.00 14.10 ? 464 HOH A O   1 
HETATM 2017 O  O   . HOH H 6 .   ? 38.774 20.198  -19.943 1.00 23.26 ? 465 HOH A O   1 
HETATM 2018 O  O   . HOH H 6 .   ? 18.818 -5.120  19.225  1.00 24.63 ? 466 HOH A O   1 
HETATM 2019 O  O   . HOH H 6 .   ? 24.498 18.353  5.745   1.00 18.16 ? 467 HOH A O   1 
HETATM 2020 O  O   . HOH H 6 .   ? 14.966 15.626  24.480  1.00 17.86 ? 468 HOH A O   1 
HETATM 2021 O  O   . HOH H 6 .   ? 29.958 29.253  -5.631  1.00 18.26 ? 469 HOH A O   1 
HETATM 2022 O  O   . HOH H 6 .   ? 41.755 23.260  -10.205 1.00 17.57 ? 470 HOH A O   1 
HETATM 2023 O  O   . HOH H 6 .   ? 26.180 9.072   13.973  1.00 4.35  ? 471 HOH A O   1 
HETATM 2024 O  O   . HOH H 6 .   ? 35.832 16.816  -18.833 1.00 13.00 ? 472 HOH A O   1 
HETATM 2025 O  O   . HOH H 6 .   ? 5.906  14.404  6.016   1.00 30.49 ? 473 HOH A O   1 
HETATM 2026 O  O   . HOH H 6 .   ? 12.838 34.049  14.894  1.00 32.82 ? 474 HOH A O   1 
HETATM 2027 O  O   . HOH H 6 .   ? 22.951 2.263   -2.606  1.00 23.92 ? 475 HOH A O   1 
HETATM 2028 O  O   . HOH H 6 .   ? 12.266 31.806  11.423  1.00 7.73  ? 476 HOH A O   1 
HETATM 2029 O  O   . HOH H 6 .   ? 43.137 24.361  6.288   1.00 31.74 ? 477 HOH A O   1 
HETATM 2030 O  O   . HOH H 6 .   ? 36.350 22.896  -7.171  1.00 8.03  ? 478 HOH A O   1 
HETATM 2031 O  O   . HOH H 6 .   ? 35.065 10.054  0.409   1.00 13.77 ? 479 HOH A O   1 
HETATM 2032 O  O   . HOH H 6 .   ? 12.030 21.258  -0.347  1.00 17.30 ? 480 HOH A O   1 
HETATM 2033 O  O   . HOH H 6 .   ? 2.401  22.106  -0.439  1.00 29.68 ? 481 HOH A O   1 
HETATM 2034 O  O   . HOH H 6 .   ? 21.491 -14.286 26.427  1.00 32.58 ? 482 HOH A O   1 
HETATM 2035 O  O   . HOH H 6 .   ? 31.717 27.110  -2.520  1.00 6.71  ? 483 HOH A O   1 
HETATM 2036 O  O   . HOH H 6 .   ? 9.182  25.184  24.211  1.00 15.44 ? 484 HOH A O   1 
HETATM 2037 O  O   . HOH H 6 .   ? 12.754 36.386  10.886  1.00 40.34 ? 485 HOH A O   1 
HETATM 2038 O  O   . HOH H 6 .   ? 1.530  33.615  3.764   1.00 6.68  ? 486 HOH A O   1 
HETATM 2039 O  O   . HOH H 6 .   ? 38.818 15.716  4.015   1.00 11.89 ? 487 HOH A O   1 
HETATM 2040 O  O   . HOH H 6 .   ? 20.993 36.649  0.831   1.00 38.00 ? 488 HOH A O   1 
HETATM 2041 O  O   . HOH H 6 .   ? 7.268  16.876  3.908   1.00 18.42 ? 489 HOH A O   1 
HETATM 2042 O  O   . HOH H 6 .   ? 32.982 27.578  11.455  1.00 31.48 ? 490 HOH A O   1 
HETATM 2043 O  O   . HOH H 6 .   ? 2.892  22.587  21.433  1.00 34.90 ? 491 HOH A O   1 
HETATM 2044 O  O   . HOH H 6 .   ? 15.686 9.257   20.351  1.00 38.40 ? 492 HOH A O   1 
HETATM 2045 O  O   . HOH H 6 .   ? 9.096  13.386  12.691  1.00 17.49 ? 493 HOH A O   1 
HETATM 2046 O  O   . HOH H 6 .   ? 31.985 24.661  15.212  1.00 13.36 ? 494 HOH A O   1 
HETATM 2047 O  O   . HOH H 6 .   ? 23.123 36.417  -1.238  1.00 36.01 ? 495 HOH A O   1 
HETATM 2048 O  O   . HOH H 6 .   ? 11.475 20.214  14.067  1.00 12.10 ? 496 HOH A O   1 
HETATM 2049 O  O   . HOH H 6 .   ? 27.442 17.601  -15.296 1.00 11.39 ? 497 HOH A O   1 
HETATM 2050 O  O   . HOH H 6 .   ? 30.784 36.620  -2.211  1.00 17.71 ? 498 HOH A O   1 
HETATM 2051 O  O   . HOH H 6 .   ? 24.694 11.815  21.600  1.00 30.83 ? 499 HOH A O   1 
HETATM 2052 O  O   . HOH H 6 .   ? 13.694 30.220  13.069  1.00 9.51  ? 500 HOH A O   1 
HETATM 2053 O  O   . HOH H 6 .   ? 41.075 16.692  -7.071  1.00 6.77  ? 501 HOH A O   1 
HETATM 2054 O  O   . HOH H 6 .   ? 21.333 0.804   -8.651  1.00 19.02 ? 502 HOH A O   1 
HETATM 2055 O  O   . HOH H 6 .   ? 19.095 1.443   12.340  1.00 13.69 ? 503 HOH A O   1 
HETATM 2056 O  O   . HOH H 6 .   ? 27.231 22.978  24.141  1.00 14.73 ? 504 HOH A O   1 
HETATM 2057 O  O   . HOH H 6 .   ? 38.451 16.810  10.012  1.00 27.52 ? 505 HOH A O   1 
HETATM 2058 O  O   . HOH H 6 .   ? 35.675 24.547  9.355   1.00 16.30 ? 506 HOH A O   1 
HETATM 2059 O  O   . HOH H 6 .   ? 11.008 30.535  9.222   1.00 8.13  ? 507 HOH A O   1 
HETATM 2060 O  O   . HOH H 6 .   ? 18.061 27.698  19.211  1.00 13.40 ? 508 HOH A O   1 
HETATM 2061 O  O   . HOH H 6 .   ? 40.843 19.488  2.221   1.00 21.82 ? 509 HOH A O   1 
HETATM 2062 O  O   . HOH H 6 .   ? 28.641 -10.537 25.574  1.00 31.56 ? 510 HOH A O   1 
HETATM 2063 O  O   . HOH H 6 .   ? 6.102  17.929  25.000  1.00 33.08 ? 511 HOH A O   1 
HETATM 2064 O  O   . HOH H 6 .   ? 42.958 13.796  -1.442  1.00 23.10 ? 512 HOH A O   1 
HETATM 2065 O  O   . HOH H 6 .   ? 25.807 32.455  -4.877  1.00 8.97  ? 513 HOH A O   1 
HETATM 2066 O  O   . HOH H 6 .   ? 36.027 21.452  11.953  1.00 19.82 ? 514 HOH A O   1 
HETATM 2067 O  O   . HOH H 6 .   ? 9.083  23.034  -6.659  1.00 41.73 ? 515 HOH A O   1 
HETATM 2068 O  O   . HOH H 6 .   ? 17.977 23.535  27.500  1.00 14.40 ? 516 HOH A O   1 
HETATM 2069 O  O   . HOH H 6 .   ? 20.672 13.671  15.613  1.00 7.45  ? 517 HOH A O   1 
HETATM 2070 O  O   . HOH H 6 .   ? 38.099 7.220   12.192  1.00 17.83 ? 518 HOH A O   1 
HETATM 2071 O  O   . HOH H 6 .   ? 2.545  33.452  11.416  1.00 19.88 ? 519 HOH A O   1 
HETATM 2072 O  O   . HOH H 6 .   ? 39.538 21.863  -1.054  1.00 20.52 ? 520 HOH A O   1 
HETATM 2073 O  O   . HOH H 6 .   ? 30.098 18.391  -15.541 1.00 10.79 ? 521 HOH A O   1 
HETATM 2074 O  O   . HOH H 6 .   ? 22.281 21.601  26.030  1.00 31.91 ? 522 HOH A O   1 
HETATM 2075 O  O   . HOH H 6 .   ? 23.279 26.307  -1.371  1.00 13.23 ? 523 HOH A O   1 
HETATM 2076 O  O   . HOH H 6 .   ? 23.820 28.597  20.536  1.00 15.37 ? 524 HOH A O   1 
HETATM 2077 O  O   . HOH H 6 .   ? 36.898 0.843   10.847  1.00 17.83 ? 525 HOH A O   1 
HETATM 2078 O  O   . HOH H 6 .   ? 3.445  30.706  -9.313  1.00 23.39 ? 526 HOH A O   1 
HETATM 2079 O  O   . HOH H 6 .   ? 26.642 29.647  -5.473  1.00 15.14 ? 527 HOH A O   1 
HETATM 2080 O  O   . HOH H 6 .   ? 36.064 34.006  -2.053  1.00 18.93 ? 528 HOH A O   1 
HETATM 2081 O  O   . HOH H 6 .   ? 39.997 30.333  -10.369 1.00 43.09 ? 529 HOH A O   1 
HETATM 2082 O  O   . HOH H 6 .   ? 26.236 20.744  -12.178 1.00 26.06 ? 530 HOH A O   1 
HETATM 2083 O  O   . HOH H 6 .   ? 38.091 11.072  -3.597  1.00 9.21  ? 531 HOH A O   1 
HETATM 2084 O  O   . HOH H 6 .   ? 41.208 20.063  7.048   1.00 25.83 ? 532 HOH A O   1 
HETATM 2085 O  O   . HOH H 6 .   ? 29.849 -10.369 21.315  1.00 15.26 ? 533 HOH A O   1 
HETATM 2086 O  O   . HOH H 6 .   ? 32.939 7.376   20.993  1.00 20.44 ? 534 HOH A O   1 
HETATM 2087 O  O   . HOH H 6 .   ? 22.420 18.811  -7.254  1.00 19.61 ? 535 HOH A O   1 
HETATM 2088 O  O   . HOH H 6 .   ? 18.901 14.973  23.845  1.00 12.28 ? 536 HOH A O   1 
HETATM 2089 O  O   . HOH H 6 .   ? 2.129  37.848  6.740   1.00 10.13 ? 537 HOH A O   1 
HETATM 2090 O  O   . HOH H 6 .   ? 11.143 28.859  -1.321  1.00 14.42 ? 538 HOH A O   1 
HETATM 2091 O  O   . HOH H 6 .   ? 24.069 -18.770 32.146  1.00 45.00 ? 539 HOH A O   1 
HETATM 2092 O  O   . HOH H 6 .   ? 8.069  20.602  29.777  1.00 17.52 ? 540 HOH A O   1 
HETATM 2093 O  O   . HOH H 6 .   ? 21.042 17.718  5.315   1.00 27.30 ? 541 HOH A O   1 
HETATM 2094 O  O   . HOH H 6 .   ? 42.147 9.144   -2.892  1.00 28.14 ? 542 HOH A O   1 
HETATM 2095 O  O   . HOH H 6 .   ? 35.008 21.966  9.559   1.00 12.76 ? 543 HOH A O   1 
HETATM 2096 O  O   . HOH H 6 .   ? 15.607 30.658  10.989  1.00 17.33 ? 544 HOH A O   1 
HETATM 2097 O  O   . HOH H 6 .   ? 41.056 12.361  -4.866  1.00 18.54 ? 545 HOH A O   1 
HETATM 2098 O  O   . HOH H 6 .   ? 11.945 31.748  -0.091  1.00 10.67 ? 546 HOH A O   1 
HETATM 2099 O  O   . HOH H 6 .   ? 27.431 35.252  4.148   1.00 33.34 ? 547 HOH A O   1 
HETATM 2100 O  O   . HOH H 6 .   ? 17.512 28.886  10.210  1.00 18.40 ? 548 HOH A O   1 
HETATM 2101 O  O   . HOH H 6 .   ? 39.514 10.294  10.498  1.00 39.43 ? 549 HOH A O   1 
HETATM 2102 O  O   . HOH H 6 .   ? 28.465 30.483  16.931  1.00 22.31 ? 550 HOH A O   1 
HETATM 2103 O  O   . HOH H 6 .   ? 11.823 25.935  -7.320  1.00 25.94 ? 551 HOH A O   1 
HETATM 2104 O  O   . HOH H 6 .   ? 18.531 35.422  0.517   1.00 26.82 ? 552 HOH A O   1 
HETATM 2105 O  O   . HOH H 6 .   ? 22.380 10.673  6.906   1.00 13.65 ? 553 HOH A O   1 
HETATM 2106 O  O   . HOH H 6 .   ? 23.696 21.958  4.286   1.00 8.99  ? 554 HOH A O   1 
HETATM 2107 O  O   . HOH H 6 .   ? 26.187 12.835  -15.827 1.00 9.11  ? 555 HOH A O   1 
HETATM 2108 O  O   . HOH H 6 .   ? 37.343 26.797  5.412   1.00 10.03 ? 556 HOH A O   1 
HETATM 2109 O  O   . HOH H 6 .   ? 19.436 -4.099  16.710  1.00 17.85 ? 557 HOH A O   1 
HETATM 2110 O  O   . HOH H 6 .   ? 2.450  21.552  7.169   1.00 36.80 ? 558 HOH A O   1 
HETATM 2111 O  O   . HOH H 6 .   ? 19.829 10.422  16.719  1.00 25.60 ? 559 HOH A O   1 
HETATM 2112 O  O   . HOH H 6 .   ? 30.785 29.594  -2.776  1.00 18.05 ? 560 HOH A O   1 
HETATM 2113 O  O   . HOH H 6 .   ? 32.523 10.748  17.864  1.00 7.02  ? 561 HOH A O   1 
HETATM 2114 O  O   . HOH H 6 .   ? 46.010 17.154  -9.622  1.00 29.73 ? 562 HOH A O   1 
HETATM 2115 O  O   . HOH H 6 .   ? 36.916 20.441  -15.925 1.00 6.40  ? 563 HOH A O   1 
HETATM 2116 O  O   . HOH H 6 .   ? 19.461 10.436  -2.079  1.00 20.05 ? 564 HOH A O   1 
HETATM 2117 O  O   . HOH H 6 .   ? 38.079 24.802  -0.947  1.00 23.96 ? 565 HOH A O   1 
HETATM 2118 O  O   . HOH H 6 .   ? 39.047 10.634  7.773   1.00 21.70 ? 566 HOH A O   1 
HETATM 2119 O  O   . HOH H 6 .   ? 21.078 24.747  -1.581  1.00 16.47 ? 567 HOH A O   1 
HETATM 2120 O  O   . HOH H 6 .   ? -0.232 22.557  10.676  1.00 40.26 ? 568 HOH A O   1 
HETATM 2121 O  O   . HOH H 6 .   ? 34.109 22.815  20.863  1.00 17.24 ? 569 HOH A O   1 
HETATM 2122 O  O   . HOH H 6 .   ? 31.058 -7.506  22.822  1.00 12.20 ? 570 HOH A O   1 
HETATM 2123 O  O   . HOH H 6 .   ? 40.376 26.381  -2.354  1.00 18.02 ? 571 HOH A O   1 
HETATM 2124 O  O   . HOH H 6 .   ? 33.364 21.826  -13.623 1.00 17.00 ? 572 HOH A O   1 
HETATM 2125 O  O   . HOH H 6 .   ? 6.931  30.057  19.431  1.00 19.74 ? 573 HOH A O   1 
HETATM 2126 O  O   . HOH H 6 .   ? 21.579 5.294   0.659   1.00 34.17 ? 574 HOH A O   1 
HETATM 2127 O  O   . HOH H 6 .   ? 26.826 7.756   22.124  1.00 26.64 ? 575 HOH A O   1 
HETATM 2128 O  O   . HOH H 6 .   ? 43.848 17.908  -9.197  1.00 12.95 ? 576 HOH A O   1 
HETATM 2129 O  O   . HOH H 6 .   ? 35.538 31.599  7.529   1.00 24.14 ? 577 HOH A O   1 
HETATM 2130 O  O   . HOH H 6 .   ? 18.446 7.739   -0.434  1.00 43.84 ? 578 HOH A O   1 
HETATM 2131 O  O   . HOH H 6 .   ? 9.166  32.518  -5.545  1.00 13.44 ? 579 HOH A O   1 
HETATM 2132 O  O   . HOH H 6 .   ? 6.394  28.304  -10.025 1.00 17.85 ? 580 HOH A O   1 
HETATM 2133 O  O   . HOH H 6 .   ? 27.038 -1.374  -5.831  1.00 11.86 ? 581 HOH A O   1 
HETATM 2134 O  O   . HOH H 6 .   ? 22.055 26.718  21.690  1.00 16.02 ? 582 HOH A O   1 
HETATM 2135 O  O   . HOH H 6 .   ? 24.917 37.190  0.525   1.00 22.13 ? 583 HOH A O   1 
HETATM 2136 O  O   . HOH H 6 .   ? 18.767 7.703   -7.495  1.00 38.58 ? 584 HOH A O   1 
HETATM 2137 O  O   . HOH H 6 .   ? 17.485 22.458  3.139   1.00 33.78 ? 585 HOH A O   1 
HETATM 2138 O  O   . HOH H 6 .   ? 41.967 12.757  2.310   1.00 31.96 ? 586 HOH A O   1 
HETATM 2139 O  O   . HOH H 6 .   ? 36.451 23.834  13.303  1.00 36.44 ? 587 HOH A O   1 
HETATM 2140 O  O   . HOH H 6 .   ? 36.464 12.013  15.092  1.00 30.18 ? 588 HOH A O   1 
HETATM 2141 O  O   . HOH H 6 .   ? 35.539 19.498  18.599  1.00 28.65 ? 589 HOH A O   1 
HETATM 2142 O  O   . HOH H 6 .   ? 26.511 11.983  -18.238 1.00 23.04 ? 590 HOH A O   1 
HETATM 2143 O  O   . HOH H 6 .   ? 21.647 18.249  29.835  1.00 30.59 ? 591 HOH A O   1 
HETATM 2144 O  O   . HOH H 6 .   ? 36.363 8.709   5.065   1.00 31.04 ? 592 HOH A O   1 
HETATM 2145 O  O   . HOH H 6 .   ? 11.500 20.185  -2.750  1.00 34.52 ? 593 HOH A O   1 
HETATM 2146 O  O   . HOH H 6 .   ? 33.833 34.339  -4.657  1.00 13.08 ? 594 HOH A O   1 
HETATM 2147 O  O   . HOH H 6 .   ? 23.762 -15.905 20.460  1.00 31.71 ? 595 HOH A O   1 
HETATM 2148 O  O   . HOH H 6 .   ? 32.268 4.523   22.564  1.00 27.12 ? 596 HOH A O   1 
HETATM 2149 O  O   . HOH H 6 .   ? 23.074 16.163  6.189   1.00 24.40 ? 597 HOH A O   1 
HETATM 2150 O  O   . HOH H 6 .   ? 23.080 29.901  -4.528  1.00 24.48 ? 598 HOH A O   1 
HETATM 2151 O  O   . HOH H 6 .   ? 2.790  27.642  17.453  1.00 34.03 ? 599 HOH A O   1 
HETATM 2152 O  O   . HOH H 6 .   ? 29.438 3.284   -4.456  1.00 5.94  ? 600 HOH A O   1 
HETATM 2153 O  O   . HOH H 6 .   ? 34.675 27.652  10.161  1.00 33.69 ? 601 HOH A O   1 
HETATM 2154 O  O   . HOH H 6 .   ? 34.233 11.735  23.043  1.00 28.14 ? 602 HOH A O   1 
HETATM 2155 O  O   . HOH H 6 .   ? 39.140 22.034  -15.573 1.00 36.48 ? 603 HOH A O   1 
HETATM 2156 O  O   . HOH H 6 .   ? 24.800 0.269   -5.660  1.00 34.80 ? 604 HOH A O   1 
HETATM 2157 O  O   . HOH H 6 .   ? 37.437 16.503  12.905  1.00 36.44 ? 605 HOH A O   1 
HETATM 2158 O  O   . HOH H 6 .   ? 34.411 7.065   -7.225  1.00 20.46 ? 606 HOH A O   1 
HETATM 2159 O  O   . HOH H 6 .   ? 17.806 9.643   11.838  1.00 18.32 ? 607 HOH A O   1 
HETATM 2160 O  O   . HOH H 6 .   ? 37.459 27.638  7.700   1.00 34.45 ? 608 HOH A O   1 
HETATM 2161 O  O   . HOH H 6 .   ? 38.209 1.389   17.429  1.00 30.04 ? 609 HOH A O   1 
HETATM 2162 O  O   . HOH H 6 .   ? 4.138  24.602  24.842  1.00 26.56 ? 610 HOH A O   1 
HETATM 2163 O  O   . HOH H 6 .   ? 31.474 1.732   -4.109  1.00 28.09 ? 611 HOH A O   1 
HETATM 2164 O  O   . HOH H 6 .   ? 35.620 2.554   18.195  1.00 34.86 ? 612 HOH A O   1 
HETATM 2165 O  O   . HOH H 6 .   ? 33.363 -16.934 19.390  1.00 26.81 ? 613 HOH A O   1 
HETATM 2166 O  O   . HOH H 6 .   ? 36.148 -7.769  25.758  1.00 29.06 ? 614 HOH A O   1 
HETATM 2167 O  O   . HOH H 6 .   ? 32.970 -6.578  25.019  1.00 23.24 ? 615 HOH A O   1 
HETATM 2168 O  O   . HOH H 6 .   ? 12.480 27.772  -3.365  1.00 23.86 ? 616 HOH A O   1 
HETATM 2169 O  O   . HOH H 6 .   ? 34.699 -9.860  25.957  1.00 27.72 ? 617 HOH A O   1 
HETATM 2170 O  O   . HOH H 6 .   ? 0.139  31.911  1.814   1.00 15.39 ? 618 HOH A O   1 
HETATM 2171 O  O   . HOH H 6 .   ? 27.643 2.723   -2.163  1.00 29.85 ? 619 HOH A O   1 
HETATM 2172 O  O   . HOH H 6 .   ? 18.188 3.785   11.786  1.00 24.12 ? 620 HOH A O   1 
HETATM 2173 O  O   . HOH H 6 .   ? 30.900 3.103   3.522   1.00 36.24 ? 621 HOH A O   1 
HETATM 2174 O  O   . HOH H 6 .   ? 37.804 -0.173  15.352  1.00 22.50 ? 622 HOH A O   1 
HETATM 2175 O  O   . HOH H 6 .   ? 34.561 23.857  15.728  1.00 32.57 ? 623 HOH A O   1 
HETATM 2176 O  O   . HOH H 6 .   ? 35.108 5.544   -1.377  1.00 38.70 ? 624 HOH A O   1 
HETATM 2177 O  O   . HOH H 6 .   ? 31.663 27.000  13.384  1.00 28.43 ? 625 HOH A O   1 
HETATM 2178 O  O   . HOH H 6 .   ? 42.361 11.054  -1.497  1.00 32.20 ? 626 HOH A O   1 
HETATM 2179 O  O   . HOH H 6 .   ? 34.547 35.089  2.325   1.00 28.94 ? 627 HOH A O   1 
HETATM 2180 O  O   . HOH H 6 .   ? 22.784 10.938  -17.861 1.00 34.55 ? 628 HOH A O   1 
HETATM 2181 O  O   . HOH H 6 .   ? 12.780 14.580  25.375  1.00 24.03 ? 629 HOH A O   1 
HETATM 2182 O  O   . HOH H 6 .   ? 25.341 38.068  7.973   1.00 37.01 ? 630 HOH A O   1 
HETATM 2183 O  O   . HOH H 6 .   ? 16.819 11.847  5.264   1.00 24.59 ? 631 HOH A O   1 
HETATM 2184 O  O   . HOH H 6 .   ? 34.088 10.411  20.177  1.00 20.90 ? 632 HOH A O   1 
HETATM 2185 O  O   . HOH H 6 .   ? 7.338  26.448  22.592  1.00 19.36 ? 633 HOH A O   1 
HETATM 2186 O  O   . HOH H 6 .   ? 27.784 -9.761  22.990  1.00 27.01 ? 634 HOH A O   1 
HETATM 2187 O  O   . HOH H 6 .   ? 35.880 -5.745  5.880   1.00 27.70 ? 635 HOH A O   1 
HETATM 2188 O  O   . HOH H 6 .   ? 15.817 7.877   11.753  1.00 29.02 ? 636 HOH A O   1 
HETATM 2189 O  O   . HOH H 6 .   ? 18.286 0.394   14.773  1.00 23.21 ? 637 HOH A O   1 
HETATM 2190 O  O   . HOH H 6 .   ? 40.303 13.589  4.448   1.00 31.82 ? 638 HOH A O   1 
HETATM 2191 O  O   . HOH H 6 .   ? 2.989  32.377  17.910  1.00 33.68 ? 639 HOH A O   1 
HETATM 2192 O  O   . HOH H 6 .   ? 25.375 37.272  10.676  1.00 36.95 ? 640 HOH A O   1 
HETATM 2193 O  O   . HOH H 6 .   ? 46.650 14.644  -6.940  1.00 26.34 ? 641 HOH A O   1 
HETATM 2194 O  O   . HOH H 6 .   ? 25.246 6.645   14.614  1.00 11.76 ? 642 HOH A O   1 
HETATM 2195 O  O   . HOH H 6 .   ? 38.090 2.896   9.753   1.00 25.47 ? 643 HOH A O   1 
HETATM 2196 O  O   . HOH H 6 .   ? 34.371 4.454   5.037   1.00 33.77 ? 644 HOH A O   1 
HETATM 2197 O  O   . HOH H 6 .   ? 32.316 -4.253  26.280  1.00 37.83 ? 645 HOH A O   1 
HETATM 2198 O  O   . HOH H 6 .   ? 36.146 26.855  -2.114  1.00 15.13 ? 646 HOH A O   1 
HETATM 2199 O  O   . HOH H 6 .   ? 18.269 12.296  15.535  1.00 14.19 ? 647 HOH A O   1 
HETATM 2200 O  O   . HOH H 6 .   ? 32.707 5.100   3.194   1.00 27.73 ? 648 HOH A O   1 
HETATM 2201 O  O   . HOH H 6 .   ? 36.483 19.378  -18.702 1.00 20.16 ? 649 HOH A O   1 
HETATM 2202 O  O   . HOH H 6 .   ? 4.074  11.151  15.909  1.00 29.36 ? 650 HOH A O   1 
HETATM 2203 O  O   . HOH H 6 .   ? 13.137 30.303  18.314  1.00 22.18 ? 651 HOH A O   1 
HETATM 2204 O  O   . HOH H 6 .   ? 37.838 -4.783  14.394  1.00 19.10 ? 652 HOH A O   1 
HETATM 2205 O  O   . HOH H 6 .   ? 38.891 31.382  -5.114  1.00 25.54 ? 653 HOH A O   1 
HETATM 2206 O  O   . HOH H 6 .   ? 18.493 -0.456  10.200  1.00 38.49 ? 654 HOH A O   1 
HETATM 2207 O  O   . HOH H 6 .   ? 22.111 2.660   3.290   1.00 26.68 ? 655 HOH A O   1 
HETATM 2208 O  O   . HOH H 6 .   ? 34.888 12.300  17.052  1.00 22.38 ? 656 HOH A O   1 
HETATM 2209 O  O   . HOH H 6 .   ? 19.453 25.989  24.535  1.00 15.78 ? 657 HOH A O   1 
HETATM 2210 O  O   . HOH H 6 .   ? 29.567 21.674  30.025  1.00 18.55 ? 658 HOH A O   1 
HETATM 2211 O  O   . HOH H 6 .   ? 19.374 8.598   7.406   1.00 32.87 ? 659 HOH A O   1 
HETATM 2212 O  O   . HOH H 6 .   ? 39.485 7.438   -11.054 1.00 28.93 ? 660 HOH A O   1 
HETATM 2213 O  O   . HOH H 6 .   ? 37.113 -6.618  10.997  1.00 14.95 ? 661 HOH A O   1 
HETATM 2214 O  O   . HOH H 6 .   ? 35.094 22.826  -15.351 1.00 18.26 ? 662 HOH A O   1 
HETATM 2215 O  O   . HOH H 6 .   ? 34.790 9.176   2.977   1.00 22.04 ? 663 HOH A O   1 
HETATM 2216 O  O   . HOH H 6 .   ? 39.343 8.778   -4.345  1.00 24.99 ? 664 HOH A O   1 
HETATM 2217 O  O   . HOH H 6 .   ? 26.123 15.485  -16.487 1.00 17.58 ? 665 HOH A O   1 
HETATM 2218 O  O   . HOH H 6 .   ? 12.504 23.983  -8.722  1.00 32.62 ? 666 HOH A O   1 
HETATM 2219 O  O   . HOH H 6 .   ? 9.287  19.434  26.557  1.00 20.92 ? 667 HOH A O   1 
HETATM 2220 O  O   . HOH H 6 .   ? 41.720 35.292  -0.819  1.00 35.89 ? 668 HOH A O   1 
HETATM 2221 O  O   . HOH H 6 .   ? 30.869 20.928  -14.502 1.00 13.33 ? 669 HOH A O   1 
HETATM 2222 O  O   . HOH H 6 .   ? 30.083 22.300  27.291  1.00 18.50 ? 670 HOH A O   1 
HETATM 2223 O  O   . HOH H 6 .   ? 28.417 3.426   22.529  1.00 20.01 ? 671 HOH A O   1 
HETATM 2224 O  O   . HOH H 6 .   ? 20.630 28.670  -2.906  1.00 28.99 ? 672 HOH A O   1 
HETATM 2225 O  O   . HOH H 6 .   ? 38.504 -0.203  12.549  1.00 30.53 ? 673 HOH A O   1 
HETATM 2226 O  O   . HOH H 6 .   ? 17.918 -2.168  15.616  1.00 33.30 ? 674 HOH A O   1 
HETATM 2227 O  O   . HOH H 6 .   ? 4.901  17.062  2.433   1.00 35.40 ? 675 HOH A O   1 
HETATM 2228 O  O   . HOH H 6 .   ? 27.224 20.404  29.504  1.00 25.65 ? 676 HOH A O   1 
HETATM 2229 O  O   . HOH H 6 .   ? 25.016 11.393  -19.933 1.00 28.94 ? 677 HOH A O   1 
HETATM 2230 O  O   . HOH H 6 .   ? 42.880 22.410  -19.615 1.00 8.10  ? 678 HOH A O   1 
HETATM 2231 O  O   . HOH H 6 .   ? 17.834 29.607  17.258  1.00 20.99 ? 679 HOH A O   1 
HETATM 2232 O  O   . HOH H 6 .   ? 37.313 9.553   -0.971  1.00 21.18 ? 680 HOH A O   1 
HETATM 2233 O  O   . HOH H 6 .   ? 26.354 5.232   23.058  1.00 25.60 ? 681 HOH A O   1 
HETATM 2234 O  O   . HOH H 6 .   ? 27.073 19.062  26.798  1.00 13.33 ? 682 HOH A O   1 
HETATM 2235 O  O   . HOH H 6 .   ? 32.833 7.483   1.995   1.00 18.08 ? 683 HOH A O   1 
HETATM 2236 O  O   . HOH H 6 .   ? 1.778  24.356  4.887   1.00 31.09 ? 684 HOH A O   1 
HETATM 2237 O  O   . HOH H 6 .   ? 38.527 -6.638  4.880   1.00 31.29 ? 685 HOH A O   1 
HETATM 2238 O  O   . HOH H 6 .   ? 40.661 3.012   10.744  1.00 27.87 ? 686 HOH A O   1 
HETATM 2239 O  O   . HOH I 6 .   ? 20.443 18.221  -0.874  1.00 31.04 ? 301 HOH P O   1 
HETATM 2240 O  O   . HOH I 6 .   ? 20.870 4.521   19.067  1.00 34.63 ? 302 HOH P O   1 
HETATM 2241 O  O   . HOH I 6 .   ? 14.797 13.070  6.622   1.00 22.14 ? 303 HOH P O   1 
HETATM 2242 O  O   . HOH I 6 .   ? 17.878 10.550  9.376   1.00 18.94 ? 304 HOH P O   1 
HETATM 2243 O  O   . HOH I 6 .   ? 21.355 16.639  0.989   1.00 16.30 ? 305 HOH P O   1 
HETATM 2244 O  O   . HOH I 6 .   ? 17.473 12.179  12.832  1.00 11.28 ? 306 HOH P O   1 
HETATM 2245 O  O   . HOH I 6 .   ? 19.801 16.392  7.431   1.00 9.71  ? 307 HOH P O   1 
HETATM 2246 O  O   . HOH I 6 .   ? 8.791  13.189  9.063   1.00 16.48 ? 308 HOH P O   1 
HETATM 2247 O  O   . HOH I 6 .   ? 19.771 17.327  3.379   1.00 22.69 ? 309 HOH P O   1 
HETATM 2248 O  O   . HOH I 6 .   ? 14.321 10.130  11.352  1.00 40.42 ? 310 HOH P O   1 
HETATM 2249 O  O   . HOH I 6 .   ? 19.859 10.363  2.969   1.00 35.51 ? 311 HOH P O   1 
HETATM 2250 O  O   . HOH I 6 .   ? 15.539 11.978  9.432   1.00 13.26 ? 312 HOH P O   1 
HETATM 2251 O  O   . HOH I 6 .   ? 7.039  11.879  12.626  1.00 31.41 ? 313 HOH P O   1 
HETATM 2252 O  O   . HOH I 6 .   ? 16.168 20.339  2.019   1.00 42.13 ? 314 HOH P O   1 
HETATM 2253 O  O   . HOH I 6 .   ? 19.248 26.159  -2.522  1.00 28.89 ? 315 HOH P O   1 
HETATM 2254 O  O   . HOH I 6 .   ? 6.924  10.926  10.125  1.00 33.51 ? 316 HOH P O   1 
HETATM 2255 O  O   . HOH I 6 .   ? 9.701  12.167  6.529   1.00 20.31 ? 317 HOH P O   1 
# 
