data_9NIH
# 
_entry.id   9NIH 
# 
_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   9NIH         pdb_00009nih 10.2210/pdb9nih/pdb 
WWPDB D_1000293462 ?            ?                   
# 
_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       2025-05-21 
_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                        9NIH 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9NIG 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              jamie.rossjohn@monash.edu 
_pdbx_contact_author.name_first         Jamie 
_pdbx_contact_author.name_last          Rossjohn 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2020-7522 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dao, H.T.'    1 0009-0001-5492-0449 
'Loh, T.J.'    2 0000-0001-8470-6868 
'Lim, J.J.'    3 0000-0002-6097-6238 
'Rossjohn, J.' 4 0000-0002-2020-7522 
# 
_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                     'Crystal structure of HLA-DR4 presenting citrullinated Tenascin C peptide' 
_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 'Dao, H.D.'    1 0009-0001-5492-0449 
primary 'Loh, T.J.'    2 0000-0001-8470-6868 
primary 'Lim, J.J.'    3 0000-0002-6097-6238 
primary 'Rossjohn, J.' 4 0000-0002-2020-7522 
# 
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 'HLA class II histocompatibility antigen, DR alpha chain' 21919.594 1   ? ? 'UNP residues 30-206' ? 
2 polymer     man 'HLA class II histocompatibility antigen DR beta chain'   23080.488 1   ? ? ?                     ? 
3 polymer     syn Tenascin                                                  1714.918  1   ? ? 'residues 1013-1024'  ? 
4 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose                  221.208   2   ? ? ?                     ? 
5 non-polymer syn GLYCEROL                                                  92.094    3   ? ? ?                     ? 
6 water       nat water                                                     18.015    110 ? ? ?                     ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'MHC class II antigen DRA' 
2 'MHC class II antigen' 
3 
;TN,Cytotactin,GMEM,GP 150-225,Glioma-associated-extracellular matrix antigen,Hexabrachion,JI,Myotendinous antigen,Neuronectin,Tenascin-C,TN-C
;
# 
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  
;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT
PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV
YDCRVEHWGLDEPLLKHWEFDTSGDDDDK
;
;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT
PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV
YDCRVEHWGLDEPLLKHWEFDTSGDDDDK
;
A ? 
2 'polypeptide(L)' no no  
;GDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTYCR
HNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTLVM
LETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK
;
;GDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTYCR
HNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTLVM
LETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK
;
B ? 
3 'polypeptide(L)' no yes 'D(CIR)Y(CIR)LNYSLPTGKK' DRYRLNYSLPTGKK C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
5 GLYCEROL                                 GOL 
6 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   LYS n 
1 3   GLU n 
1 4   GLU n 
1 5   HIS n 
1 6   VAL n 
1 7   ILE n 
1 8   ILE n 
1 9   GLN n 
1 10  ALA n 
1 11  GLU n 
1 12  PHE n 
1 13  TYR n 
1 14  LEU n 
1 15  ASN n 
1 16  PRO n 
1 17  ASP n 
1 18  GLN n 
1 19  SER n 
1 20  GLY n 
1 21  GLU n 
1 22  PHE n 
1 23  MET n 
1 24  PHE n 
1 25  ASP n 
1 26  PHE n 
1 27  ASP n 
1 28  GLY n 
1 29  ASP n 
1 30  GLU n 
1 31  ILE n 
1 32  PHE n 
1 33  HIS n 
1 34  VAL n 
1 35  ASP n 
1 36  MET n 
1 37  ALA n 
1 38  LYS n 
1 39  LYS n 
1 40  GLU n 
1 41  THR n 
1 42  VAL n 
1 43  TRP n 
1 44  ARG n 
1 45  LEU n 
1 46  GLU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLY n 
1 50  ARG n 
1 51  PHE n 
1 52  ALA n 
1 53  SER n 
1 54  PHE n 
1 55  GLU n 
1 56  ALA n 
1 57  GLN n 
1 58  GLY n 
1 59  ALA n 
1 60  LEU n 
1 61  ALA n 
1 62  ASN n 
1 63  ILE n 
1 64  ALA n 
1 65  VAL n 
1 66  ASP n 
1 67  LYS n 
1 68  ALA n 
1 69  ASN n 
1 70  LEU n 
1 71  GLU n 
1 72  ILE n 
1 73  MET n 
1 74  THR n 
1 75  LYS n 
1 76  ARG n 
1 77  SER n 
1 78  ASN n 
1 79  TYR n 
1 80  THR n 
1 81  PRO n 
1 82  ILE n 
1 83  THR n 
1 84  ASN n 
1 85  VAL n 
1 86  PRO n 
1 87  PRO n 
1 88  GLU n 
1 89  VAL n 
1 90  THR n 
1 91  VAL n 
1 92  LEU n 
1 93  THR n 
1 94  ASN n 
1 95  SER n 
1 96  PRO n 
1 97  VAL n 
1 98  GLU n 
1 99  LEU n 
1 100 ARG n 
1 101 GLU n 
1 102 PRO n 
1 103 ASN n 
1 104 VAL n 
1 105 LEU n 
1 106 ILE n 
1 107 CYS n 
1 108 PHE n 
1 109 ILE n 
1 110 ASP n 
1 111 LYS n 
1 112 PHE n 
1 113 THR n 
1 114 PRO n 
1 115 PRO n 
1 116 VAL n 
1 117 VAL n 
1 118 ASN n 
1 119 VAL n 
1 120 THR n 
1 121 TRP n 
1 122 LEU n 
1 123 ARG n 
1 124 ASN n 
1 125 GLY n 
1 126 LYS n 
1 127 PRO n 
1 128 VAL n 
1 129 THR n 
1 130 THR n 
1 131 GLY n 
1 132 VAL n 
1 133 SER n 
1 134 GLU n 
1 135 THR n 
1 136 VAL n 
1 137 PHE n 
1 138 LEU n 
1 139 PRO n 
1 140 ARG n 
1 141 GLU n 
1 142 ASP n 
1 143 HIS n 
1 144 LEU n 
1 145 PHE n 
1 146 ARG n 
1 147 LYS n 
1 148 PHE n 
1 149 HIS n 
1 150 TYR n 
1 151 LEU n 
1 152 PRO n 
1 153 PHE n 
1 154 LEU n 
1 155 PRO n 
1 156 SER n 
1 157 THR n 
1 158 GLU n 
1 159 ASP n 
1 160 VAL n 
1 161 TYR n 
1 162 ASP n 
1 163 CYS n 
1 164 ARG n 
1 165 VAL n 
1 166 GLU n 
1 167 HIS n 
1 168 TRP n 
1 169 GLY n 
1 170 LEU n 
1 171 ASP n 
1 172 GLU n 
1 173 PRO n 
1 174 LEU n 
1 175 LEU n 
1 176 LYS n 
1 177 HIS n 
1 178 TRP n 
1 179 GLU n 
1 180 PHE n 
1 181 ASP n 
1 182 THR n 
1 183 SER n 
1 184 GLY n 
1 185 ASP n 
1 186 ASP n 
1 187 ASP n 
1 188 ASP n 
1 189 LYS n 
2 1   GLY n 
2 2   ASP n 
2 3   THR n 
2 4   ARG n 
2 5   PRO n 
2 6   ARG n 
2 7   PHE n 
2 8   LEU n 
2 9   GLU n 
2 10  GLN n 
2 11  VAL n 
2 12  LYS n 
2 13  HIS n 
2 14  GLU n 
2 15  CYS n 
2 16  HIS n 
2 17  PHE n 
2 18  PHE n 
2 19  ASN n 
2 20  GLY n 
2 21  THR n 
2 22  GLU n 
2 23  ARG n 
2 24  VAL n 
2 25  ARG n 
2 26  PHE n 
2 27  LEU n 
2 28  ASP n 
2 29  ARG n 
2 30  TYR n 
2 31  PHE n 
2 32  TYR n 
2 33  HIS n 
2 34  GLN n 
2 35  GLU n 
2 36  GLU n 
2 37  TYR n 
2 38  VAL n 
2 39  ARG n 
2 40  PHE n 
2 41  ASP n 
2 42  SER n 
2 43  ASP n 
2 44  VAL n 
2 45  GLY n 
2 46  GLU n 
2 47  TYR n 
2 48  ARG n 
2 49  ALA n 
2 50  VAL n 
2 51  THR n 
2 52  GLU n 
2 53  LEU n 
2 54  GLY n 
2 55  ARG n 
2 56  PRO n 
2 57  ASP n 
2 58  ALA n 
2 59  GLU n 
2 60  TYR n 
2 61  TRP n 
2 62  ASN n 
2 63  SER n 
2 64  GLN n 
2 65  LYS n 
2 66  ASP n 
2 67  LEU n 
2 68  LEU n 
2 69  GLU n 
2 70  GLN n 
2 71  LYS n 
2 72  ARG n 
2 73  ALA n 
2 74  ALA n 
2 75  VAL n 
2 76  ASP n 
2 77  THR n 
2 78  TYR n 
2 79  CYS n 
2 80  ARG n 
2 81  HIS n 
2 82  ASN n 
2 83  TYR n 
2 84  GLY n 
2 85  VAL n 
2 86  GLY n 
2 87  GLU n 
2 88  SER n 
2 89  PHE n 
2 90  THR n 
2 91  VAL n 
2 92  GLN n 
2 93  ARG n 
2 94  ARG n 
2 95  VAL n 
2 96  TYR n 
2 97  PRO n 
2 98  GLU n 
2 99  VAL n 
2 100 THR n 
2 101 VAL n 
2 102 TYR n 
2 103 PRO n 
2 104 ALA n 
2 105 LYS n 
2 106 THR n 
2 107 GLN n 
2 108 PRO n 
2 109 LEU n 
2 110 GLN n 
2 111 HIS n 
2 112 HIS n 
2 113 ASN n 
2 114 LEU n 
2 115 LEU n 
2 116 VAL n 
2 117 CYS n 
2 118 SER n 
2 119 VAL n 
2 120 ASN n 
2 121 GLY n 
2 122 PHE n 
2 123 TYR n 
2 124 PRO n 
2 125 GLY n 
2 126 SER n 
2 127 ILE n 
2 128 GLU n 
2 129 VAL n 
2 130 ARG n 
2 131 TRP n 
2 132 PHE n 
2 133 ARG n 
2 134 ASN n 
2 135 GLY n 
2 136 GLN n 
2 137 GLU n 
2 138 GLU n 
2 139 LYS n 
2 140 THR n 
2 141 GLY n 
2 142 VAL n 
2 143 VAL n 
2 144 SER n 
2 145 THR n 
2 146 GLY n 
2 147 LEU n 
2 148 ILE n 
2 149 GLN n 
2 150 ASN n 
2 151 GLY n 
2 152 ASP n 
2 153 TRP n 
2 154 THR n 
2 155 PHE n 
2 156 GLN n 
2 157 THR n 
2 158 LEU n 
2 159 VAL n 
2 160 MET n 
2 161 LEU n 
2 162 GLU n 
2 163 THR n 
2 164 VAL n 
2 165 PRO n 
2 166 ARG n 
2 167 SER n 
2 168 GLY n 
2 169 GLU n 
2 170 VAL n 
2 171 TYR n 
2 172 THR n 
2 173 CYS n 
2 174 GLN n 
2 175 VAL n 
2 176 GLU n 
2 177 HIS n 
2 178 PRO n 
2 179 SER n 
2 180 LEU n 
2 181 THR n 
2 182 SER n 
2 183 PRO n 
2 184 LEU n 
2 185 THR n 
2 186 VAL n 
2 187 GLU n 
2 188 TRP n 
2 189 ARG n 
2 190 ALA n 
2 191 THR n 
2 192 GLY n 
2 193 GLY n 
2 194 ASP n 
2 195 ASP n 
2 196 ASP n 
2 197 ASP n 
2 198 LYS n 
3 1   ASP n 
3 2   CIR n 
3 3   TYR n 
3 4   CIR n 
3 5   LEU n 
3 6   ASN n 
3 7   TYR n 
3 8   SER n 
3 9   LEU n 
3 10  PRO n 
3 11  THR n 
3 12  GLY n 
3 13  LYS n 
3 14  LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 189 human ? 'HLA-DRA, HLA-DRA1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 198 human ? HLA-DRB1            ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_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       14 
_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 
CIR 'L-peptide linking'          n CITRULLINE                               ? 'C6 H13 N3 O3'   175.186 
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  
GOL non-polymer                  . GLYCEROL                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       
92.094  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   ILE 1   1    1    ILE ILE A . n 
A 1 2   LYS 2   2    2    LYS LYS A . n 
A 1 3   GLU 3   3    3    GLU GLU A . n 
A 1 4   GLU 4   4    4    GLU GLU A . n 
A 1 5   HIS 5   5    5    HIS HIS A . n 
A 1 6   VAL 6   6    6    VAL VAL A . n 
A 1 7   ILE 7   7    7    ILE ILE A . n 
A 1 8   ILE 8   8    8    ILE ILE A . n 
A 1 9   GLN 9   9    9    GLN GLN A . n 
A 1 10  ALA 10  10   10   ALA ALA A . n 
A 1 11  GLU 11  11   11   GLU GLU A . n 
A 1 12  PHE 12  12   12   PHE PHE A . n 
A 1 13  TYR 13  13   13   TYR TYR A . n 
A 1 14  LEU 14  14   14   LEU LEU A . n 
A 1 15  ASN 15  15   15   ASN ASN A . n 
A 1 16  PRO 16  16   16   PRO PRO A . n 
A 1 17  ASP 17  17   17   ASP ASP A . n 
A 1 18  GLN 18  18   18   GLN GLN A . n 
A 1 19  SER 19  19   19   SER SER A . n 
A 1 20  GLY 20  20   20   GLY GLY A . n 
A 1 21  GLU 21  21   21   GLU GLU A . n 
A 1 22  PHE 22  22   22   PHE PHE A . n 
A 1 23  MET 23  23   23   MET MET A . n 
A 1 24  PHE 24  24   24   PHE PHE A . n 
A 1 25  ASP 25  25   25   ASP ASP A . n 
A 1 26  PHE 26  26   26   PHE PHE A . n 
A 1 27  ASP 27  27   27   ASP ASP A . n 
A 1 28  GLY 28  28   28   GLY GLY A . n 
A 1 29  ASP 29  29   29   ASP ASP A . n 
A 1 30  GLU 30  30   30   GLU GLU A . n 
A 1 31  ILE 31  31   31   ILE ILE A . n 
A 1 32  PHE 32  32   32   PHE PHE A . n 
A 1 33  HIS 33  33   33   HIS HIS A . n 
A 1 34  VAL 34  34   34   VAL VAL A . n 
A 1 35  ASP 35  35   35   ASP ASP A . n 
A 1 36  MET 36  36   36   MET MET A . n 
A 1 37  ALA 37  37   37   ALA ALA A . n 
A 1 38  LYS 38  38   38   LYS LYS A . n 
A 1 39  LYS 39  39   39   LYS LYS A . n 
A 1 40  GLU 40  40   40   GLU GLU A . n 
A 1 41  THR 41  41   41   THR THR A . n 
A 1 42  VAL 42  42   42   VAL VAL A . n 
A 1 43  TRP 43  43   43   TRP TRP A . n 
A 1 44  ARG 44  44   44   ARG ARG A . n 
A 1 45  LEU 45  45   45   LEU LEU A . n 
A 1 46  GLU 46  46   46   GLU GLU A . n 
A 1 47  GLU 47  47   47   GLU GLU A . n 
A 1 48  PHE 48  48   48   PHE PHE A . n 
A 1 49  GLY 49  49   49   GLY GLY A . n 
A 1 50  ARG 50  50   50   ARG ARG A . n 
A 1 51  PHE 51  51   51   PHE PHE A . n 
A 1 52  ALA 52  52   52   ALA ALA A . n 
A 1 53  SER 53  53   53   SER SER A . n 
A 1 54  PHE 54  54   54   PHE PHE A . n 
A 1 55  GLU 55  55   55   GLU GLU A . n 
A 1 56  ALA 56  56   56   ALA ALA A . n 
A 1 57  GLN 57  57   57   GLN GLN A . n 
A 1 58  GLY 58  58   58   GLY GLY A . n 
A 1 59  ALA 59  59   59   ALA ALA A . n 
A 1 60  LEU 60  60   60   LEU LEU A . n 
A 1 61  ALA 61  61   61   ALA ALA A . n 
A 1 62  ASN 62  62   62   ASN ASN A . n 
A 1 63  ILE 63  63   63   ILE ILE A . n 
A 1 64  ALA 64  64   64   ALA ALA A . n 
A 1 65  VAL 65  65   65   VAL VAL A . n 
A 1 66  ASP 66  66   66   ASP ASP A . n 
A 1 67  LYS 67  67   67   LYS LYS A . n 
A 1 68  ALA 68  68   68   ALA ALA A . n 
A 1 69  ASN 69  69   69   ASN ASN A . n 
A 1 70  LEU 70  70   70   LEU LEU A . n 
A 1 71  GLU 71  71   71   GLU GLU A . n 
A 1 72  ILE 72  72   72   ILE ILE A . n 
A 1 73  MET 73  73   73   MET MET A . n 
A 1 74  THR 74  74   74   THR THR A . n 
A 1 75  LYS 75  75   75   LYS LYS A . n 
A 1 76  ARG 76  76   76   ARG ARG A . n 
A 1 77  SER 77  77   77   SER SER A . n 
A 1 78  ASN 78  78   78   ASN ASN A . n 
A 1 79  TYR 79  79   79   TYR TYR A . n 
A 1 80  THR 80  80   80   THR THR A . n 
A 1 81  PRO 81  81   81   PRO PRO A . n 
A 1 82  ILE 82  82   82   ILE ILE A . n 
A 1 83  THR 83  83   83   THR THR A . n 
A 1 84  ASN 84  84   84   ASN ASN A . n 
A 1 85  VAL 85  85   85   VAL VAL A . n 
A 1 86  PRO 86  86   86   PRO PRO A . n 
A 1 87  PRO 87  87   87   PRO PRO A . n 
A 1 88  GLU 88  88   88   GLU GLU A . n 
A 1 89  VAL 89  89   89   VAL VAL A . n 
A 1 90  THR 90  90   90   THR THR A . n 
A 1 91  VAL 91  91   91   VAL VAL A . n 
A 1 92  LEU 92  92   92   LEU LEU A . n 
A 1 93  THR 93  93   93   THR THR A . n 
A 1 94  ASN 94  94   94   ASN ASN A . n 
A 1 95  SER 95  95   95   SER SER A . n 
A 1 96  PRO 96  96   96   PRO PRO A . n 
A 1 97  VAL 97  97   97   VAL VAL A . n 
A 1 98  GLU 98  98   98   GLU GLU A . n 
A 1 99  LEU 99  99   99   LEU LEU A . n 
A 1 100 ARG 100 100  100  ARG ARG A . n 
A 1 101 GLU 101 101  101  GLU GLU A . n 
A 1 102 PRO 102 102  102  PRO PRO A . n 
A 1 103 ASN 103 103  103  ASN ASN A . n 
A 1 104 VAL 104 104  104  VAL VAL A . n 
A 1 105 LEU 105 105  105  LEU LEU A . n 
A 1 106 ILE 106 106  106  ILE ILE A . n 
A 1 107 CYS 107 107  107  CYS CYS A . n 
A 1 108 PHE 108 108  108  PHE PHE A . n 
A 1 109 ILE 109 109  109  ILE ILE A . n 
A 1 110 ASP 110 110  110  ASP ASP A . n 
A 1 111 LYS 111 111  111  LYS LYS A . n 
A 1 112 PHE 112 112  112  PHE PHE A . n 
A 1 113 THR 113 113  113  THR THR A . n 
A 1 114 PRO 114 114  114  PRO PRO A . n 
A 1 115 PRO 115 115  115  PRO PRO A . n 
A 1 116 VAL 116 116  116  VAL VAL A . n 
A 1 117 VAL 117 117  117  VAL VAL A . n 
A 1 118 ASN 118 118  118  ASN ASN A . n 
A 1 119 VAL 119 119  119  VAL VAL A . n 
A 1 120 THR 120 120  120  THR THR A . n 
A 1 121 TRP 121 121  121  TRP TRP A . n 
A 1 122 LEU 122 122  122  LEU LEU A . n 
A 1 123 ARG 123 123  123  ARG ARG A . n 
A 1 124 ASN 124 124  124  ASN ASN A . n 
A 1 125 GLY 125 125  125  GLY GLY A . n 
A 1 126 LYS 126 126  126  LYS LYS A . n 
A 1 127 PRO 127 127  127  PRO PRO A . n 
A 1 128 VAL 128 128  128  VAL VAL A . n 
A 1 129 THR 129 129  129  THR THR A . n 
A 1 130 THR 130 130  130  THR THR A . n 
A 1 131 GLY 131 131  131  GLY GLY A . n 
A 1 132 VAL 132 132  132  VAL VAL A . n 
A 1 133 SER 133 133  133  SER SER A . n 
A 1 134 GLU 134 134  134  GLU GLU A . n 
A 1 135 THR 135 135  135  THR THR A . n 
A 1 136 VAL 136 136  136  VAL VAL A . n 
A 1 137 PHE 137 137  137  PHE PHE A . n 
A 1 138 LEU 138 138  138  LEU LEU A . n 
A 1 139 PRO 139 139  139  PRO PRO A . n 
A 1 140 ARG 140 140  140  ARG ARG A . n 
A 1 141 GLU 141 141  141  GLU GLU A . n 
A 1 142 ASP 142 142  142  ASP ASP A . n 
A 1 143 HIS 143 143  143  HIS HIS A . n 
A 1 144 LEU 144 144  144  LEU LEU A . n 
A 1 145 PHE 145 145  145  PHE PHE A . n 
A 1 146 ARG 146 146  146  ARG ARG A . n 
A 1 147 LYS 147 147  147  LYS LYS A . n 
A 1 148 PHE 148 148  148  PHE PHE A . n 
A 1 149 HIS 149 149  149  HIS HIS A . n 
A 1 150 TYR 150 150  150  TYR TYR A . n 
A 1 151 LEU 151 151  151  LEU LEU A . n 
A 1 152 PRO 152 152  152  PRO PRO A . n 
A 1 153 PHE 153 153  153  PHE PHE A . n 
A 1 154 LEU 154 154  154  LEU LEU A . n 
A 1 155 PRO 155 155  155  PRO PRO A . n 
A 1 156 SER 156 156  156  SER SER A . n 
A 1 157 THR 157 157  157  THR THR A . n 
A 1 158 GLU 158 158  158  GLU GLU A . n 
A 1 159 ASP 159 159  159  ASP ASP A . n 
A 1 160 VAL 160 160  160  VAL VAL A . n 
A 1 161 TYR 161 161  161  TYR TYR A . n 
A 1 162 ASP 162 162  162  ASP ASP A . n 
A 1 163 CYS 163 163  163  CYS CYS A . n 
A 1 164 ARG 164 164  164  ARG ARG A . n 
A 1 165 VAL 165 165  165  VAL VAL A . n 
A 1 166 GLU 166 166  166  GLU GLU A . n 
A 1 167 HIS 167 167  167  HIS HIS A . n 
A 1 168 TRP 168 168  168  TRP TRP A . n 
A 1 169 GLY 169 169  169  GLY GLY A . n 
A 1 170 LEU 170 170  170  LEU LEU A . n 
A 1 171 ASP 171 171  171  ASP ASP A . n 
A 1 172 GLU 172 172  172  GLU GLU A . n 
A 1 173 PRO 173 173  173  PRO PRO A . n 
A 1 174 LEU 174 174  174  LEU LEU A . n 
A 1 175 LEU 175 175  175  LEU LEU A . n 
A 1 176 LYS 176 176  176  LYS LYS A . n 
A 1 177 HIS 177 177  177  HIS HIS A . n 
A 1 178 TRP 178 178  178  TRP TRP A . n 
A 1 179 GLU 179 179  179  GLU GLU A . n 
A 1 180 PHE 180 180  180  PHE PHE A . n 
A 1 181 ASP 181 181  181  ASP ASP A . n 
A 1 182 THR 182 182  182  THR THR A . n 
A 1 183 SER 183 183  ?    ?   ?   A . n 
A 1 184 GLY 184 184  ?    ?   ?   A . n 
A 1 185 ASP 185 185  ?    ?   ?   A . n 
A 1 186 ASP 186 186  ?    ?   ?   A . n 
A 1 187 ASP 187 187  ?    ?   ?   A . n 
A 1 188 ASP 188 188  ?    ?   ?   A . n 
A 1 189 LYS 189 189  ?    ?   ?   A . n 
B 2 1   GLY 1   1    ?    ?   ?   B . n 
B 2 2   ASP 2   2    2    ASP ASP B . n 
B 2 3   THR 3   3    3    THR THR B . n 
B 2 4   ARG 4   4    4    ARG ARG B . n 
B 2 5   PRO 5   5    5    PRO PRO B . n 
B 2 6   ARG 6   6    6    ARG ARG B . n 
B 2 7   PHE 7   7    7    PHE PHE B . n 
B 2 8   LEU 8   8    8    LEU LEU B . n 
B 2 9   GLU 9   9    9    GLU GLU B . n 
B 2 10  GLN 10  10   10   GLN GLN B . n 
B 2 11  VAL 11  11   11   VAL VAL B . n 
B 2 12  LYS 12  12   12   LYS LYS B . n 
B 2 13  HIS 13  13   13   HIS HIS B . n 
B 2 14  GLU 14  14   14   GLU GLU B . n 
B 2 15  CYS 15  15   15   CYS CYS B . n 
B 2 16  HIS 16  16   16   HIS HIS B . n 
B 2 17  PHE 17  17   17   PHE PHE B . n 
B 2 18  PHE 18  18   18   PHE PHE B . n 
B 2 19  ASN 19  19   19   ASN ASN B . n 
B 2 20  GLY 20  20   20   GLY GLY B . n 
B 2 21  THR 21  21   21   THR THR B . n 
B 2 22  GLU 22  22   22   GLU GLU B . n 
B 2 23  ARG 23  23   23   ARG ARG B . n 
B 2 24  VAL 24  24   24   VAL VAL B . n 
B 2 25  ARG 25  25   25   ARG ARG B . n 
B 2 26  PHE 26  26   26   PHE PHE B . n 
B 2 27  LEU 27  27   27   LEU LEU B . n 
B 2 28  ASP 28  28   28   ASP ASP B . n 
B 2 29  ARG 29  29   29   ARG ARG B . n 
B 2 30  TYR 30  30   30   TYR TYR B . n 
B 2 31  PHE 31  31   31   PHE PHE B . n 
B 2 32  TYR 32  32   32   TYR TYR B . n 
B 2 33  HIS 33  33   33   HIS HIS B . n 
B 2 34  GLN 34  34   34   GLN GLN B . n 
B 2 35  GLU 35  35   35   GLU GLU B . n 
B 2 36  GLU 36  36   36   GLU GLU B . n 
B 2 37  TYR 37  37   37   TYR TYR B . n 
B 2 38  VAL 38  38   38   VAL VAL B . n 
B 2 39  ARG 39  39   39   ARG ARG B . n 
B 2 40  PHE 40  40   40   PHE PHE B . n 
B 2 41  ASP 41  41   41   ASP ASP B . n 
B 2 42  SER 42  42   42   SER SER B . n 
B 2 43  ASP 43  43   43   ASP ASP B . n 
B 2 44  VAL 44  44   44   VAL VAL B . n 
B 2 45  GLY 45  45   45   GLY GLY B . n 
B 2 46  GLU 46  46   46   GLU GLU B . n 
B 2 47  TYR 47  47   47   TYR TYR B . n 
B 2 48  ARG 48  48   48   ARG ARG B . n 
B 2 49  ALA 49  49   49   ALA ALA B . n 
B 2 50  VAL 50  50   50   VAL VAL B . n 
B 2 51  THR 51  51   51   THR THR B . n 
B 2 52  GLU 52  52   52   GLU GLU B . n 
B 2 53  LEU 53  53   53   LEU LEU B . n 
B 2 54  GLY 54  54   54   GLY GLY B . n 
B 2 55  ARG 55  55   55   ARG ARG B . n 
B 2 56  PRO 56  56   56   PRO PRO B . n 
B 2 57  ASP 57  57   57   ASP ASP B . n 
B 2 58  ALA 58  58   58   ALA ALA B . n 
B 2 59  GLU 59  59   59   GLU GLU B . n 
B 2 60  TYR 60  60   60   TYR TYR B . n 
B 2 61  TRP 61  61   61   TRP TRP B . n 
B 2 62  ASN 62  62   62   ASN ASN B . n 
B 2 63  SER 63  63   63   SER SER B . n 
B 2 64  GLN 64  64   64   GLN GLN B . n 
B 2 65  LYS 65  65   65   LYS LYS B . n 
B 2 66  ASP 66  66   66   ASP ASP B . n 
B 2 67  LEU 67  67   67   LEU LEU B . n 
B 2 68  LEU 68  68   68   LEU LEU B . n 
B 2 69  GLU 69  69   69   GLU GLU B . n 
B 2 70  GLN 70  70   70   GLN GLN B . n 
B 2 71  LYS 71  71   71   LYS LYS B . n 
B 2 72  ARG 72  72   72   ARG ARG B . n 
B 2 73  ALA 73  73   73   ALA ALA B . n 
B 2 74  ALA 74  74   74   ALA ALA B . n 
B 2 75  VAL 75  75   75   VAL VAL B . n 
B 2 76  ASP 76  76   76   ASP ASP B . n 
B 2 77  THR 77  77   77   THR THR B . n 
B 2 78  TYR 78  78   78   TYR TYR B . n 
B 2 79  CYS 79  79   79   CYS CYS B . n 
B 2 80  ARG 80  80   80   ARG ARG B . n 
B 2 81  HIS 81  81   81   HIS HIS B . n 
B 2 82  ASN 82  82   82   ASN ASN B . n 
B 2 83  TYR 83  83   83   TYR TYR B . n 
B 2 84  GLY 84  84   84   GLY GLY B . n 
B 2 85  VAL 85  85   85   VAL VAL B . n 
B 2 86  GLY 86  86   86   GLY GLY B . n 
B 2 87  GLU 87  87   87   GLU GLU B . n 
B 2 88  SER 88  88   88   SER SER B . n 
B 2 89  PHE 89  89   89   PHE PHE B . n 
B 2 90  THR 90  90   90   THR THR B . n 
B 2 91  VAL 91  91   91   VAL VAL B . n 
B 2 92  GLN 92  92   92   GLN GLN B . n 
B 2 93  ARG 93  93   93   ARG ARG B . n 
B 2 94  ARG 94  94   94   ARG ARG B . n 
B 2 95  VAL 95  95   95   VAL VAL B . n 
B 2 96  TYR 96  96   96   TYR TYR B . n 
B 2 97  PRO 97  97   97   PRO PRO B . n 
B 2 98  GLU 98  98   98   GLU GLU B . n 
B 2 99  VAL 99  99   99   VAL VAL B . n 
B 2 100 THR 100 100  100  THR THR B . n 
B 2 101 VAL 101 101  101  VAL VAL B . n 
B 2 102 TYR 102 102  102  TYR TYR B . n 
B 2 103 PRO 103 103  103  PRO PRO B . n 
B 2 104 ALA 104 104  104  ALA ALA B . n 
B 2 105 LYS 105 105  105  LYS LYS B . n 
B 2 106 THR 106 106  106  THR THR B . n 
B 2 107 GLN 107 107  107  GLN GLN B . n 
B 2 108 PRO 108 108  108  PRO PRO B . n 
B 2 109 LEU 109 109  109  LEU LEU B . n 
B 2 110 GLN 110 110  110  GLN GLN B . n 
B 2 111 HIS 111 111  111  HIS HIS B . n 
B 2 112 HIS 112 112  112  HIS HIS B . n 
B 2 113 ASN 113 113  113  ASN ASN B . n 
B 2 114 LEU 114 114  114  LEU LEU B . n 
B 2 115 LEU 115 115  115  LEU LEU B . n 
B 2 116 VAL 116 116  116  VAL VAL B . n 
B 2 117 CYS 117 117  117  CYS CYS B . n 
B 2 118 SER 118 118  118  SER SER B . n 
B 2 119 VAL 119 119  119  VAL VAL B . n 
B 2 120 ASN 120 120  120  ASN ASN B . n 
B 2 121 GLY 121 121  121  GLY GLY B . n 
B 2 122 PHE 122 122  122  PHE PHE B . n 
B 2 123 TYR 123 123  123  TYR TYR B . n 
B 2 124 PRO 124 124  124  PRO PRO B . n 
B 2 125 GLY 125 125  125  GLY GLY B . n 
B 2 126 SER 126 126  126  SER SER B . n 
B 2 127 ILE 127 127  127  ILE ILE B . n 
B 2 128 GLU 128 128  128  GLU GLU B . n 
B 2 129 VAL 129 129  129  VAL VAL B . n 
B 2 130 ARG 130 130  130  ARG ARG B . n 
B 2 131 TRP 131 131  131  TRP TRP B . n 
B 2 132 PHE 132 132  132  PHE PHE B . n 
B 2 133 ARG 133 133  133  ARG ARG B . n 
B 2 134 ASN 134 134  134  ASN ASN B . n 
B 2 135 GLY 135 135  135  GLY GLY B . n 
B 2 136 GLN 136 136  136  GLN GLN B . n 
B 2 137 GLU 137 137  137  GLU GLU B . n 
B 2 138 GLU 138 138  138  GLU GLU B . n 
B 2 139 LYS 139 139  139  LYS LYS B . n 
B 2 140 THR 140 140  140  THR THR B . n 
B 2 141 GLY 141 141  141  GLY GLY B . n 
B 2 142 VAL 142 142  142  VAL VAL B . n 
B 2 143 VAL 143 143  143  VAL VAL B . n 
B 2 144 SER 144 144  144  SER SER B . n 
B 2 145 THR 145 145  145  THR THR B . n 
B 2 146 GLY 146 146  146  GLY GLY B . n 
B 2 147 LEU 147 147  147  LEU LEU B . n 
B 2 148 ILE 148 148  148  ILE ILE B . n 
B 2 149 GLN 149 149  149  GLN GLN B . n 
B 2 150 ASN 150 150  150  ASN ASN B . n 
B 2 151 GLY 151 151  151  GLY GLY B . n 
B 2 152 ASP 152 152  152  ASP ASP B . n 
B 2 153 TRP 153 153  153  TRP TRP B . n 
B 2 154 THR 154 154  154  THR THR B . n 
B 2 155 PHE 155 155  155  PHE PHE B . n 
B 2 156 GLN 156 156  156  GLN GLN B . n 
B 2 157 THR 157 157  157  THR THR B . n 
B 2 158 LEU 158 158  158  LEU LEU B . n 
B 2 159 VAL 159 159  159  VAL VAL B . n 
B 2 160 MET 160 160  160  MET MET B . n 
B 2 161 LEU 161 161  161  LEU LEU B . n 
B 2 162 GLU 162 162  162  GLU GLU B . n 
B 2 163 THR 163 163  163  THR THR B . n 
B 2 164 VAL 164 164  164  VAL VAL B . n 
B 2 165 PRO 165 165  165  PRO PRO B . n 
B 2 166 ARG 166 166  166  ARG ARG B . n 
B 2 167 SER 167 167  167  SER SER B . n 
B 2 168 GLY 168 168  ?    ?   ?   B . n 
B 2 169 GLU 169 169  169  GLU GLU B . n 
B 2 170 VAL 170 170  170  VAL VAL B . n 
B 2 171 TYR 171 171  171  TYR TYR B . n 
B 2 172 THR 172 172  172  THR THR B . n 
B 2 173 CYS 173 173  173  CYS CYS B . n 
B 2 174 GLN 174 174  174  GLN GLN B . n 
B 2 175 VAL 175 175  175  VAL VAL B . n 
B 2 176 GLU 176 176  176  GLU GLU B . n 
B 2 177 HIS 177 177  177  HIS HIS B . n 
B 2 178 PRO 178 178  178  PRO PRO B . n 
B 2 179 SER 179 179  179  SER SER B . n 
B 2 180 LEU 180 180  180  LEU LEU B . n 
B 2 181 THR 181 181  181  THR THR B . n 
B 2 182 SER 182 182  182  SER SER B . n 
B 2 183 PRO 183 183  183  PRO PRO B . n 
B 2 184 LEU 184 184  184  LEU LEU B . n 
B 2 185 THR 185 185  185  THR THR B . n 
B 2 186 VAL 186 186  186  VAL VAL B . n 
B 2 187 GLU 187 187  187  GLU GLU B . n 
B 2 188 TRP 188 188  188  TRP TRP B . n 
B 2 189 ARG 189 189  189  ARG ARG B . n 
B 2 190 ALA 190 190  190  ALA ALA B . n 
B 2 191 THR 191 191  ?    ?   ?   B . n 
B 2 192 GLY 192 192  ?    ?   ?   B . n 
B 2 193 GLY 193 193  ?    ?   ?   B . n 
B 2 194 ASP 194 194  ?    ?   ?   B . n 
B 2 195 ASP 195 195  ?    ?   ?   B . n 
B 2 196 ASP 196 196  ?    ?   ?   B . n 
B 2 197 ASP 197 197  ?    ?   ?   B . n 
B 2 198 LYS 198 198  ?    ?   ?   B . n 
C 3 1   ASP 1   1013 1013 ASP ASP C . n 
C 3 2   CIR 2   1014 1014 CIR CIR C . n 
C 3 3   TYR 3   1015 1015 TYR TYR C . n 
C 3 4   CIR 4   1016 1016 CIR CIR C . n 
C 3 5   LEU 5   1017 1017 LEU LEU C . n 
C 3 6   ASN 6   1018 1018 ASN ASN C . n 
C 3 7   TYR 7   1019 1019 TYR TYR C . n 
C 3 8   SER 8   1020 1020 SER SER C . n 
C 3 9   LEU 9   1021 1021 LEU LEU C . n 
C 3 10  PRO 10  1022 1022 PRO PRO C . n 
C 3 11  THR 11  1023 1023 THR THR C . n 
C 3 12  GLY 12  1024 ?    ?   ?   C . n 
C 3 13  LYS 13  1025 ?    ?   ?   C . n 
C 3 14  LYS 14  1026 ?    ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CIR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CIR 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
D 4 NAG 1  201  183 NAG NAG A . 
E 5 GOL 1  202  1   GOL GOL A . 
F 4 NAG 1  201  191 NAG NAG B . 
G 5 GOL 1  202  2   GOL GOL B . 
H 5 GOL 1  203  3   GOL GOL B . 
I 6 HOH 1  301  88  HOH HOH A . 
I 6 HOH 2  302  41  HOH HOH A . 
I 6 HOH 3  303  4   HOH HOH A . 
I 6 HOH 4  304  21  HOH HOH A . 
I 6 HOH 5  305  51  HOH HOH A . 
I 6 HOH 6  306  97  HOH HOH A . 
I 6 HOH 7  307  6   HOH HOH A . 
I 6 HOH 8  308  9   HOH HOH A . 
I 6 HOH 9  309  35  HOH HOH A . 
I 6 HOH 10 310  13  HOH HOH A . 
I 6 HOH 11 311  3   HOH HOH A . 
I 6 HOH 12 312  108 HOH HOH A . 
I 6 HOH 13 313  19  HOH HOH A . 
I 6 HOH 14 314  5   HOH HOH A . 
I 6 HOH 15 315  30  HOH HOH A . 
I 6 HOH 16 316  68  HOH HOH A . 
I 6 HOH 17 317  64  HOH HOH A . 
I 6 HOH 18 318  73  HOH HOH A . 
I 6 HOH 19 319  10  HOH HOH A . 
I 6 HOH 20 320  49  HOH HOH A . 
I 6 HOH 21 321  27  HOH HOH A . 
I 6 HOH 22 322  1   HOH HOH A . 
I 6 HOH 23 323  8   HOH HOH A . 
I 6 HOH 24 324  89  HOH HOH A . 
I 6 HOH 25 325  102 HOH HOH A . 
I 6 HOH 26 326  36  HOH HOH A . 
I 6 HOH 27 327  72  HOH HOH A . 
I 6 HOH 28 328  86  HOH HOH A . 
I 6 HOH 29 329  18  HOH HOH A . 
I 6 HOH 30 330  74  HOH HOH A . 
I 6 HOH 31 331  25  HOH HOH A . 
I 6 HOH 32 332  48  HOH HOH A . 
I 6 HOH 33 333  94  HOH HOH A . 
I 6 HOH 34 334  85  HOH HOH A . 
I 6 HOH 35 335  2   HOH HOH A . 
I 6 HOH 36 336  107 HOH HOH A . 
I 6 HOH 37 337  11  HOH HOH A . 
I 6 HOH 38 338  65  HOH HOH A . 
I 6 HOH 39 339  106 HOH HOH A . 
I 6 HOH 40 340  28  HOH HOH A . 
I 6 HOH 41 341  99  HOH HOH A . 
I 6 HOH 42 342  39  HOH HOH A . 
I 6 HOH 43 343  26  HOH HOH A . 
I 6 HOH 44 344  63  HOH HOH A . 
I 6 HOH 45 345  37  HOH HOH A . 
I 6 HOH 46 346  82  HOH HOH A . 
I 6 HOH 47 347  80  HOH HOH A . 
I 6 HOH 48 348  83  HOH HOH A . 
I 6 HOH 49 349  105 HOH HOH A . 
I 6 HOH 50 350  47  HOH HOH A . 
I 6 HOH 51 351  84  HOH HOH A . 
I 6 HOH 52 352  79  HOH HOH A . 
I 6 HOH 53 353  66  HOH HOH A . 
I 6 HOH 54 354  42  HOH HOH A . 
J 6 HOH 1  301  40  HOH HOH B . 
J 6 HOH 2  302  12  HOH HOH B . 
J 6 HOH 3  303  58  HOH HOH B . 
J 6 HOH 4  304  43  HOH HOH B . 
J 6 HOH 5  305  45  HOH HOH B . 
J 6 HOH 6  306  96  HOH HOH B . 
J 6 HOH 7  307  62  HOH HOH B . 
J 6 HOH 8  308  24  HOH HOH B . 
J 6 HOH 9  309  23  HOH HOH B . 
J 6 HOH 10 310  93  HOH HOH B . 
J 6 HOH 11 311  55  HOH HOH B . 
J 6 HOH 12 312  38  HOH HOH B . 
J 6 HOH 13 313  16  HOH HOH B . 
J 6 HOH 14 314  44  HOH HOH B . 
J 6 HOH 15 315  46  HOH HOH B . 
J 6 HOH 16 316  22  HOH HOH B . 
J 6 HOH 17 317  100 HOH HOH B . 
J 6 HOH 18 318  20  HOH HOH B . 
J 6 HOH 19 319  76  HOH HOH B . 
J 6 HOH 20 320  109 HOH HOH B . 
J 6 HOH 21 321  69  HOH HOH B . 
J 6 HOH 22 322  103 HOH HOH B . 
J 6 HOH 23 323  33  HOH HOH B . 
J 6 HOH 24 324  81  HOH HOH B . 
J 6 HOH 25 325  7   HOH HOH B . 
J 6 HOH 26 326  32  HOH HOH B . 
J 6 HOH 27 327  75  HOH HOH B . 
J 6 HOH 28 328  29  HOH HOH B . 
J 6 HOH 29 329  87  HOH HOH B . 
J 6 HOH 30 330  31  HOH HOH B . 
J 6 HOH 31 331  77  HOH HOH B . 
J 6 HOH 32 332  60  HOH HOH B . 
J 6 HOH 33 333  59  HOH HOH B . 
J 6 HOH 34 334  34  HOH HOH B . 
J 6 HOH 35 335  104 HOH HOH B . 
J 6 HOH 36 336  61  HOH HOH B . 
J 6 HOH 37 337  92  HOH HOH B . 
J 6 HOH 38 338  71  HOH HOH B . 
J 6 HOH 39 339  53  HOH HOH B . 
J 6 HOH 40 340  54  HOH HOH B . 
J 6 HOH 41 341  101 HOH HOH B . 
J 6 HOH 42 342  52  HOH HOH B . 
J 6 HOH 43 343  98  HOH HOH B . 
J 6 HOH 44 344  15  HOH HOH B . 
J 6 HOH 45 345  70  HOH HOH B . 
J 6 HOH 46 346  56  HOH HOH B . 
J 6 HOH 47 347  95  HOH HOH B . 
J 6 HOH 48 348  90  HOH HOH B . 
J 6 HOH 49 349  50  HOH HOH B . 
K 6 HOH 1  1101 67  HOH HOH C . 
K 6 HOH 2  1102 17  HOH HOH C . 
K 6 HOH 3  1103 78  HOH HOH C . 
K 6 HOH 4  1104 14  HOH HOH C . 
K 6 HOH 5  1105 91  HOH HOH C . 
K 6 HOH 6  1106 110 HOH HOH C . 
K 6 HOH 7  1107 57  HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ILE 1   ? CG1 ? A ILE 1   CG1 
2  1 Y 1 A ILE 1   ? CG2 ? A ILE 1   CG2 
3  1 Y 1 A ILE 1   ? CD1 ? A ILE 1   CD1 
4  1 Y 1 A GLU 3   ? CG  ? A GLU 3   CG  
5  1 Y 1 A GLU 3   ? CD  ? A GLU 3   CD  
6  1 Y 1 A GLU 3   ? OE1 ? A GLU 3   OE1 
7  1 Y 1 A GLU 3   ? OE2 ? A GLU 3   OE2 
8  1 Y 1 A GLU 55  ? CG  ? A GLU 55  CG  
9  1 Y 1 A GLU 55  ? CD  ? A GLU 55  CD  
10 1 Y 1 A GLU 55  ? OE1 ? A GLU 55  OE1 
11 1 Y 1 A GLU 55  ? OE2 ? A GLU 55  OE2 
12 1 Y 1 A GLU 98  ? CG  ? A GLU 98  CG  
13 1 Y 1 A GLU 98  ? CD  ? A GLU 98  CD  
14 1 Y 1 A GLU 98  ? OE1 ? A GLU 98  OE1 
15 1 Y 1 A GLU 98  ? OE2 ? A GLU 98  OE2 
16 1 Y 1 A ARG 100 ? CG  ? A ARG 100 CG  
17 1 Y 1 A ARG 100 ? CD  ? A ARG 100 CD  
18 1 Y 1 A ARG 100 ? NE  ? A ARG 100 NE  
19 1 Y 1 A ARG 100 ? CZ  ? A ARG 100 CZ  
20 1 Y 1 A ARG 100 ? NH1 ? A ARG 100 NH1 
21 1 Y 1 A ARG 100 ? NH2 ? A ARG 100 NH2 
22 1 Y 1 A GLU 101 ? CG  ? A GLU 101 CG  
23 1 Y 1 A GLU 101 ? CD  ? A GLU 101 CD  
24 1 Y 1 A GLU 101 ? OE1 ? A GLU 101 OE1 
25 1 Y 1 A GLU 101 ? OE2 ? A GLU 101 OE2 
26 1 Y 1 A PHE 108 ? CG  ? A PHE 108 CG  
27 1 Y 1 A PHE 108 ? CD1 ? A PHE 108 CD1 
28 1 Y 1 A PHE 108 ? CD2 ? A PHE 108 CD2 
29 1 Y 1 A PHE 108 ? CE1 ? A PHE 108 CE1 
30 1 Y 1 A PHE 108 ? CE2 ? A PHE 108 CE2 
31 1 Y 1 A PHE 108 ? CZ  ? A PHE 108 CZ  
32 1 Y 1 A LYS 126 ? CG  ? A LYS 126 CG  
33 1 Y 1 A LYS 126 ? CD  ? A LYS 126 CD  
34 1 Y 1 A LYS 126 ? CE  ? A LYS 126 CE  
35 1 Y 1 A LYS 126 ? NZ  ? A LYS 126 NZ  
36 1 Y 1 A GLU 158 ? CG  ? A GLU 158 CG  
37 1 Y 1 A GLU 158 ? CD  ? A GLU 158 CD  
38 1 Y 1 A GLU 158 ? OE1 ? A GLU 158 OE1 
39 1 Y 1 A GLU 158 ? OE2 ? A GLU 158 OE2 
40 1 Y 1 B THR 3   ? OG1 ? B THR 3   OG1 
41 1 Y 1 B THR 3   ? CG2 ? B THR 3   CG2 
42 1 Y 1 B PHE 18  ? CG  ? B PHE 18  CG  
43 1 Y 1 B PHE 18  ? CD1 ? B PHE 18  CD1 
44 1 Y 1 B PHE 18  ? CD2 ? B PHE 18  CD2 
45 1 Y 1 B PHE 18  ? CE1 ? B PHE 18  CE1 
46 1 Y 1 B PHE 18  ? CE2 ? B PHE 18  CE2 
47 1 Y 1 B PHE 18  ? CZ  ? B PHE 18  CZ  
48 1 Y 1 B GLU 52  ? CG  ? B GLU 52  CG  
49 1 Y 1 B GLU 52  ? CD  ? B GLU 52  CD  
50 1 Y 1 B GLU 52  ? OE1 ? B GLU 52  OE1 
51 1 Y 1 B GLU 52  ? OE2 ? B GLU 52  OE2 
52 1 Y 1 B GLU 59  ? CG  ? B GLU 59  CG  
53 1 Y 1 B GLU 59  ? CD  ? B GLU 59  CD  
54 1 Y 1 B GLU 59  ? OE1 ? B GLU 59  OE1 
55 1 Y 1 B GLU 59  ? OE2 ? B GLU 59  OE2 
56 1 Y 1 B LYS 65  ? CG  ? B LYS 65  CG  
57 1 Y 1 B LYS 65  ? CD  ? B LYS 65  CD  
58 1 Y 1 B LYS 65  ? CE  ? B LYS 65  CE  
59 1 Y 1 B LYS 65  ? NZ  ? B LYS 65  NZ  
60 1 Y 1 B ASP 66  ? CG  ? B ASP 66  CG  
61 1 Y 1 B ASP 66  ? OD1 ? B ASP 66  OD1 
62 1 Y 1 B ASP 66  ? OD2 ? B ASP 66  OD2 
63 1 Y 1 B LYS 105 ? CG  ? B LYS 105 CG  
64 1 Y 1 B LYS 105 ? CD  ? B LYS 105 CD  
65 1 Y 1 B LYS 105 ? CE  ? B LYS 105 CE  
66 1 Y 1 B LYS 105 ? NZ  ? B LYS 105 NZ  
67 1 Y 1 B GLU 128 ? CG  ? B GLU 128 CG  
68 1 Y 1 B GLU 128 ? CD  ? B GLU 128 CD  
69 1 Y 1 B GLU 128 ? OE1 ? B GLU 128 OE1 
70 1 Y 1 B GLU 128 ? OE2 ? B GLU 128 OE2 
71 1 Y 1 B GLN 136 ? CG  ? B GLN 136 CG  
72 1 Y 1 B GLN 136 ? CD  ? B GLN 136 CD  
73 1 Y 1 B GLN 136 ? OE1 ? B GLN 136 OE1 
74 1 Y 1 B GLN 136 ? NE2 ? B GLN 136 NE2 
75 1 Y 1 B LYS 139 ? CG  ? B LYS 139 CG  
76 1 Y 1 B LYS 139 ? CD  ? B LYS 139 CD  
77 1 Y 1 B LYS 139 ? CE  ? B LYS 139 CE  
78 1 Y 1 B LYS 139 ? NZ  ? B LYS 139 NZ  
79 1 Y 1 B ARG 189 ? CG  ? B ARG 189 CG  
80 1 Y 1 B ARG 189 ? CD  ? B ARG 189 CD  
81 1 Y 1 B ARG 189 ? NE  ? B ARG 189 NE  
82 1 Y 1 B ARG 189 ? CZ  ? B ARG 189 CZ  
83 1 Y 1 B ARG 189 ? NH1 ? B ARG 189 NH1 
84 1 Y 1 B ARG 189 ? NH2 ? B ARG 189 NH2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NIH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     119.300 
_cell.length_a_esd                 ? 
_cell.length_b                     119.300 
_cell.length_b_esd                 ? 
_cell.length_c                     73.273 
_cell.length_c_esd                 ? 
_cell.volume                       903137.164 
_cell.volume_esd                   ? 
_cell.Z_PDB                        9 
_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                         9NIH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            'R 3' 
_symmetry.space_group_name_H-M             'H 3' 
_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                   9NIH 
_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             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.74 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_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    '0.2 M NaCl, 0.1 M Bis Tris pH 5.5, 29% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95373 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95373 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          38.49 
_reflns.entry_id                                       9NIH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.40 
_reflns.d_resolution_low                               34.53 
_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                                     15161 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.89 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.102 
_reflns.pdbx_Rpim_I_all                                0.045 
_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                              0.092 
_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                                    2.40 
_reflns_shell.d_res_low                                     2.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           7.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1628 
_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                               10.4 
_reflns_shell.pdbx_chi_squared                              0.70 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.391 
_reflns_shell.pdbx_Rpim_I_all                               0.170 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.970 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.352 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               44.39 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NIH 
_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                            2.40 
_refine.ls_d_res_low                             34.53 
_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                     15153 
_refine.ls_number_reflns_R_free                  786 
_refine.ls_number_reflns_R_work                  14367 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.58 
_refine.ls_percent_reflns_R_free                 5.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1860 
_refine.ls_R_factor_R_free                       0.2186 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1842 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2.07 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.0799 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2640 
_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                       2.40 
_refine_hist.d_res_low                        34.53 
_refine_hist.number_atoms_solvent             110 
_refine_hist.number_atoms_total               3232 
_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        3076 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_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' ? 0.0039 ? 3195 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6914 ? 4359 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0450 ? 479  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0054 ? 562  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.3763 ? 436  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.55  . . 142 2394 99.22 . . . . 0.2311 . . . . . . . . . . . . . . . 0.2974 
'X-RAY DIFFRACTION' 2.55 2.75  . . 158 2360 99.37 . . . . 0.2146 . . . . . . . . . . . . . . . 0.2823 
'X-RAY DIFFRACTION' 2.75 3.02  . . 112 2391 99.64 . . . . 0.2148 . . . . . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 3.02 3.46  . . 112 2402 99.64 . . . . 0.1903 . . . . . . . . . . . . . . . 0.2609 
'X-RAY DIFFRACTION' 3.46 4.35  . . 120 2410 99.72 . . . . 0.1654 . . . . . . . . . . . . . . . 0.2000 
'X-RAY DIFFRACTION' 4.36 34.53 . . 142 2410 99.92 . . . . 0.1676 . . . . . . . . . . . . . . . 0.1702 
# 
_struct.entry_id                     9NIH 
_struct.title                        'Crystal structure of HLA-DR4 presenting citrullinated Tenascin C peptide' 
_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        9NIH 
_struct_keywords.text            
'Human Leukocyte Antigen, T cell receptor, citrullinated epitope, rheumatoid arthritis, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 5 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
K 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 DRA_HUMAN        P01903     ? 1 
;HVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPITN
VPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCR
VEHWGLDEPLLKHWEFD
;
30   
2 UNP A0A1V1IGJ9_HUMAN A0A1V1IGJ9 ? 2 
;GDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTYCR
HNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTLVM
LETVPRSGEVYTCQVEHPSLTSPLTVEWRA
;
30   
3 UNP TENA_HUMAN       P24821     ? 3 DRYRLNYSLPTG 1013 
# 
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 9NIH A 5 ? 181 ? P01903     30   ? 206  ? 5    181  
2 2 9NIH B 1 ? 190 ? A0A1V1IGJ9 30   ? 219  ? 1    190  
3 3 9NIH C 1 ? 12  ? P24821     1013 ? 1024 ? 1013 1024 
# 
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 9NIH ILE A 1   ? UNP P01903     ? ? 'expression tag' 1    1  
1 9NIH LYS A 2   ? UNP P01903     ? ? 'expression tag' 2    2  
1 9NIH GLU A 3   ? UNP P01903     ? ? 'expression tag' 3    3  
1 9NIH GLU A 4   ? UNP P01903     ? ? 'expression tag' 4    4  
1 9NIH THR A 182 ? UNP P01903     ? ? 'expression tag' 182  5  
1 9NIH SER A 183 ? UNP P01903     ? ? 'expression tag' 183  6  
1 9NIH GLY A 184 ? UNP P01903     ? ? 'expression tag' 184  7  
1 9NIH ASP A 185 ? UNP P01903     ? ? 'expression tag' 185  8  
1 9NIH ASP A 186 ? UNP P01903     ? ? 'expression tag' 186  9  
1 9NIH ASP A 187 ? UNP P01903     ? ? 'expression tag' 187  10 
1 9NIH ASP A 188 ? UNP P01903     ? ? 'expression tag' 188  11 
1 9NIH LYS A 189 ? UNP P01903     ? ? 'expression tag' 189  12 
2 9NIH THR B 191 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 191  13 
2 9NIH GLY B 192 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 192  14 
2 9NIH GLY B 193 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 193  15 
2 9NIH ASP B 194 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 194  16 
2 9NIH ASP B 195 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 195  17 
2 9NIH ASP B 196 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 196  18 
2 9NIH ASP B 197 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 197  19 
2 9NIH LYS B 198 ? UNP A0A1V1IGJ9 ? ? 'expression tag' 198  20 
3 9NIH LYS C 13  ? UNP P24821     ? ? insertion        1025 21 
3 9NIH LYS C 14  ? UNP P24821     ? ? insertion        1026 22 
# 
_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   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 8700  ? 
1 MORE         -26   ? 
1 'SSA (A^2)'  17660 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLU A 47 ? ALA A 52 ? GLU A 47 ALA A 52 1 ? 6  
HELX_P HELX_P2 AA2 GLU A 55 ? SER A 77 ? GLU A 55 SER A 77 1 ? 23 
HELX_P HELX_P3 AA3 THR B 51 ? LEU B 53 ? THR B 51 LEU B 53 5 ? 3  
HELX_P HELX_P4 AA4 GLY B 54 ? SER B 63 ? GLY B 54 SER B 63 1 ? 10 
HELX_P HELX_P5 AA5 GLN B 64 ? ALA B 73 ? GLN B 64 ALA B 73 1 ? 10 
HELX_P HELX_P6 AA6 ALA B 73 ? TYR B 78 ? ALA B 73 TYR B 78 1 ? 6  
HELX_P HELX_P7 AA7 TYR B 78 ? GLU B 87 ? TYR B 78 GLU B 87 1 ? 10 
HELX_P HELX_P8 AA8 SER B 88 ? THR B 90 ? SER B 88 THR B 90 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 107 SG  ? ? ? 1_555 A CYS 163 SG ? ? A CYS 107  A CYS 163  1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf2 disulf ?    ? B CYS 15  SG  ? ? ? 1_555 B CYS 79  SG ? ? B CYS 15   B CYS 79   1_555 ? ? ? ? ? ? ? 2.048 ? ?               
disulf3 disulf ?    ? B CYS 117 SG  ? ? ? 1_555 B CYS 173 SG ? ? B CYS 117  B CYS 173  1_555 ? ? ? ? ? ? ? 2.026 ? ?               
covale1 covale one  ? A ASN 118 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 118  A NAG 201  1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale2 covale one  ? B ASN 19  ND2 ? ? ? 1_555 F NAG .   C1 ? ? B ASN 19   B NAG 201  1_555 ? ? ? ? ? ? ? 1.446 ? N-Glycosylation 
covale3 covale both ? C ASP 1   C   ? ? ? 1_555 C CIR 2   N  ? ? C ASP 1013 C CIR 1014 1_555 ? ? ? ? ? ? ? 1.429 ? ?               
covale4 covale both ? C CIR 2   C   ? ? ? 1_555 C TYR 3   N  ? ? C CIR 1014 C TYR 1015 1_555 ? ? ? ? ? ? ? 1.429 ? ?               
covale5 covale both ? C TYR 3   C   ? ? ? 1_555 C CIR 4   N  ? ? C TYR 1015 C CIR 1016 1_555 ? ? ? ? ? ? ? 1.430 ? ?               
covale6 covale both ? C CIR 4   C   ? ? ? 1_555 C LEU 5   N  ? ? C CIR 1016 C LEU 1017 1_555 ? ? ? ? ? ? ? 1.428 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CIR C 2   ? .   . .   . CIR C 1014 ? 1_555 .   . .   . .     .  .   ARG 1 CIR Citrullination  'Named protein modification' 
2 CIR C 4   ? .   . .   . CIR C 1016 ? 1_555 .   . .   . .     .  .   ARG 1 CIR Citrullination  'Named protein modification' 
3 NAG D .   ? ASN A 118 ? NAG A 201  ? 1_555 ASN A 118 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate                 
4 NAG F .   ? ASN B 19  ? NAG B 201  ? 1_555 ASN B 19  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate                 
5 CYS A 107 ? CYS A 163 ? CYS A 107  ? 1_555 CYS A 163 ? 1_555 SG SG  .   . .   None            'Disulfide bridge'           
6 CYS B 15  ? CYS B 79  ? CYS B 15   ? 1_555 CYS B 79  ? 1_555 SG SG  .   . .   None            'Disulfide bridge'           
7 CYS B 117 ? CYS B 173 ? CYS B 117  ? 1_555 CYS B 173 ? 1_555 SG SG  .   . .   None            'Disulfide bridge'           
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 15  A . ? ASN 15  A PRO 16  A ? PRO 16  A 1 1.74  
2 THR 113 A . ? THR 113 A PRO 114 A ? PRO 114 A 1 -2.64 
3 TYR 123 B . ? TYR 123 B PRO 124 B ? PRO 124 B 1 -1.35 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 40  ? TRP A 43  ? GLU A 40  TRP A 43  
AA1 2 ASP A 29  ? ASP A 35  ? ASP A 29  ASP A 35  
AA1 3 SER A 19  ? PHE A 26  ? SER A 19  PHE A 26  
AA1 4 GLU A 4   ? ASN A 15  ? GLU A 4   ASN A 15  
AA1 5 PHE B 7   ? PHE B 18  ? PHE B 7   PHE B 18  
AA1 6 ARG B 23  ? TYR B 32  ? ARG B 23  TYR B 32  
AA1 7 GLU B 35  ? ASP B 41  ? GLU B 35  ASP B 41  
AA1 8 TYR B 47  ? ALA B 49  ? TYR B 47  ALA B 49  
AA2 1 GLU A 88  ? THR A 93  ? GLU A 88  THR A 93  
AA2 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 
AA2 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 
AA2 4 SER A 133 ? GLU A 134 ? SER A 133 GLU A 134 
AA3 1 GLU A 88  ? THR A 93  ? GLU A 88  THR A 93  
AA3 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 
AA3 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 
AA3 4 LEU A 138 ? PRO A 139 ? LEU A 138 PRO A 139 
AA4 1 LYS A 126 ? PRO A 127 ? LYS A 126 PRO A 127 
AA4 2 ASN A 118 ? ARG A 123 ? ASN A 118 ARG A 123 
AA4 3 TYR A 161 ? GLU A 166 ? TYR A 161 GLU A 166 
AA4 4 LEU A 174 ? TRP A 178 ? LEU A 174 TRP A 178 
AA5 1 GLU B 98  ? PRO B 103 ? GLU B 98  PRO B 103 
AA5 2 ASN B 113 ? PHE B 122 ? ASN B 113 PHE B 122 
AA5 3 PHE B 155 ? THR B 163 ? PHE B 155 THR B 163 
AA5 4 VAL B 142 ? SER B 144 ? VAL B 142 SER B 144 
AA6 1 GLU B 98  ? PRO B 103 ? GLU B 98  PRO B 103 
AA6 2 ASN B 113 ? PHE B 122 ? ASN B 113 PHE B 122 
AA6 3 PHE B 155 ? THR B 163 ? PHE B 155 THR B 163 
AA6 4 ILE B 148 ? GLN B 149 ? ILE B 148 GLN B 149 
AA7 1 GLN B 136 ? GLU B 137 ? GLN B 136 GLU B 137 
AA7 2 GLU B 128 ? ARG B 133 ? GLU B 128 ARG B 133 
AA7 3 VAL B 170 ? GLU B 176 ? VAL B 170 GLU B 176 
AA7 4 LEU B 184 ? ARG B 189 ? LEU B 184 ARG B 189 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 42  ? O VAL A 42  N HIS A 33  ? N HIS A 33  
AA1 2 3 O ASP A 29  ? O ASP A 29  N PHE A 26  ? N PHE A 26  
AA1 3 4 O ASP A 25  ? O ASP A 25  N ILE A 8   ? N ILE A 8   
AA1 4 5 N HIS A 5   ? N HIS A 5   O PHE B 17  ? O PHE B 17  
AA1 5 6 N HIS B 16  ? N HIS B 16  O ARG B 25  ? O ARG B 25  
AA1 6 7 N TYR B 32  ? N TYR B 32  O GLU B 35  ? O GLU B 35  
AA1 7 8 N ARG B 39  ? N ARG B 39  O ARG B 48  ? O ARG B 48  
AA2 1 2 N LEU A 92  ? N LEU A 92  O ILE A 106 ? O ILE A 106 
AA2 2 3 N ILE A 109 ? N ILE A 109 O LYS A 147 ? O LYS A 147 
AA2 3 4 O TYR A 150 ? O TYR A 150 N SER A 133 ? N SER A 133 
AA3 1 2 N LEU A 92  ? N LEU A 92  O ILE A 106 ? O ILE A 106 
AA3 2 3 N ILE A 109 ? N ILE A 109 O LYS A 147 ? O LYS A 147 
AA3 3 4 O ARG A 146 ? O ARG A 146 N LEU A 138 ? N LEU A 138 
AA4 1 2 O LYS A 126 ? O LYS A 126 N ARG A 123 ? N ARG A 123 
AA4 2 3 N THR A 120 ? N THR A 120 O ARG A 164 ? O ARG A 164 
AA4 3 4 N VAL A 165 ? N VAL A 165 O LEU A 174 ? O LEU A 174 
AA5 1 2 N THR B 100 ? N THR B 100 O SER B 118 ? O SER B 118 
AA5 2 3 N ASN B 113 ? N ASN B 113 O THR B 163 ? O THR B 163 
AA5 3 4 O MET B 160 ? O MET B 160 N VAL B 143 ? N VAL B 143 
AA6 1 2 N THR B 100 ? N THR B 100 O SER B 118 ? O SER B 118 
AA6 2 3 N ASN B 113 ? N ASN B 113 O THR B 163 ? O THR B 163 
AA6 3 4 O GLN B 156 ? O GLN B 156 N ILE B 148 ? N ILE B 148 
AA7 1 2 O GLN B 136 ? O GLN B 136 N ARG B 133 ? N ARG B 133 
AA7 2 3 N ARG B 130 ? N ARG B 130 O GLN B 174 ? O GLN B 174 
AA7 3 4 N VAL B 175 ? N VAL B 175 O LEU B 184 ? O LEU B 184 
# 
_pdbx_entry_details.entry_id                   9NIH 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    322 
_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   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    335 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 NH2 A ARG 50  ? ? 1_555 OD1 A ASN 62  ? ? 9_544 2.03 
2 1 O   A HOH 306 ? ? 1_555 O   B HOH 343 ? ? 5_445 2.12 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA C CIR 1014 ? ? C C CIR 1014 ? ? N C TYR 1015 ? ? 131.56 117.20 14.36  2.20 Y 
2 1 O  C CIR 1014 ? ? C C CIR 1014 ? ? N C TYR 1015 ? ? 107.20 122.70 -15.50 1.60 Y 
3 1 CA C CIR 1016 ? ? C C CIR 1016 ? ? N C LEU 1017 ? ? 87.49  117.20 -29.71 2.20 Y 
4 1 O  C CIR 1016 ? ? C C CIR 1016 ? ? N C LEU 1017 ? ? 137.05 122.70 14.35  1.60 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 100 ? ? 59.72   16.21   
2 1 THR B 3   ? ? -95.23  32.27   
3 1 HIS B 33  ? ? 65.11   -116.79 
4 1 THR B 90  ? ? -117.09 -74.39  
5 1 HIS B 111 ? ? 65.62   -57.96  
6 1 ARG B 166 ? ? -171.99 143.88  
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 ASP C 1013 ? ? -15.02 
2 1 CIR C 1016 ? ? 13.40  
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 C CIR 2 C CIR 1014 ? ARG 'modified residue' 
2 C CIR 4 C CIR 1016 ? ARG 'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z                 
2 -y,x-y,z              
3 -x+y,-x,z             
4 x+1/3,y+2/3,z+2/3     
5 -y+1/3,x-y+2/3,z+2/3  
6 -x+y+1/3,-x+2/3,z+2/3 
7 x+2/3,y+1/3,z+1/3     
8 -y+2/3,x-y+1/3,z+1/3  
9 -x+y+2/3,-x+1/3,z+1/3 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 354 ? 7.63 .    
2 1 O ? B HOH 348 ? .    6.17 
3 1 O ? B HOH 349 ? 6.27 .    
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 183  ? A SER 183 
2  1 Y 1 A GLY 184  ? A GLY 184 
3  1 Y 1 A ASP 185  ? A ASP 185 
4  1 Y 1 A ASP 186  ? A ASP 186 
5  1 Y 1 A ASP 187  ? A ASP 187 
6  1 Y 1 A ASP 188  ? A ASP 188 
7  1 Y 1 A LYS 189  ? A LYS 189 
8  1 Y 1 B GLY 1    ? B GLY 1   
9  1 Y 1 B GLY 168  ? B GLY 168 
10 1 Y 1 B THR 191  ? B THR 191 
11 1 Y 1 B GLY 192  ? B GLY 192 
12 1 Y 1 B GLY 193  ? B GLY 193 
13 1 Y 1 B ASP 194  ? B ASP 194 
14 1 Y 1 B ASP 195  ? B ASP 195 
15 1 Y 1 B ASP 196  ? B ASP 196 
16 1 Y 1 B ASP 197  ? B ASP 197 
17 1 Y 1 B LYS 198  ? B LYS 198 
18 1 Y 1 C GLY 1024 ? C GLY 12  
19 1 Y 1 C LYS 1025 ? C LYS 13  
20 1 Y 1 C LYS 1026 ? C LYS 14  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIR C    C N N 74  
CIR O    O N N 75  
CIR OXT  O N N 76  
CIR CA   C N S 77  
CIR N    N N N 78  
CIR C3   C N N 79  
CIR C4   C N N 80  
CIR C5   C N N 81  
CIR N6   N N N 82  
CIR C7   C N N 83  
CIR O7   O N N 84  
CIR N8   N N N 85  
CIR HXT  H N N 86  
CIR HA   H N N 87  
CIR H2   H N N 88  
CIR H    H N N 89  
CIR H31  H N N 90  
CIR H32  H N N 91  
CIR H41  H N N 92  
CIR H42  H N N 93  
CIR H51  H N N 94  
CIR H52  H N N 95  
CIR HN6  H N N 96  
CIR HN81 H N N 97  
CIR HN82 H N N 98  
CYS N    N N N 99  
CYS CA   C N R 100 
CYS C    C N N 101 
CYS O    O N N 102 
CYS CB   C N N 103 
CYS SG   S N N 104 
CYS OXT  O N N 105 
CYS H    H N N 106 
CYS H2   H N N 107 
CYS HA   H N N 108 
CYS HB2  H N N 109 
CYS HB3  H N N 110 
CYS HG   H N N 111 
CYS HXT  H N N 112 
GLN N    N N N 113 
GLN CA   C N S 114 
GLN C    C N N 115 
GLN O    O N N 116 
GLN CB   C N N 117 
GLN CG   C N N 118 
GLN CD   C N N 119 
GLN OE1  O N N 120 
GLN NE2  N N N 121 
GLN OXT  O N N 122 
GLN H    H N N 123 
GLN H2   H N N 124 
GLN HA   H N N 125 
GLN HB2  H N N 126 
GLN HB3  H N N 127 
GLN HG2  H N N 128 
GLN HG3  H N N 129 
GLN HE21 H N N 130 
GLN HE22 H N N 131 
GLN HXT  H N N 132 
GLU N    N N N 133 
GLU CA   C N S 134 
GLU C    C N N 135 
GLU O    O N N 136 
GLU CB   C N N 137 
GLU CG   C N N 138 
GLU CD   C N N 139 
GLU OE1  O N N 140 
GLU OE2  O N N 141 
GLU OXT  O N N 142 
GLU H    H N N 143 
GLU H2   H N N 144 
GLU HA   H N N 145 
GLU HB2  H N N 146 
GLU HB3  H N N 147 
GLU HG2  H N N 148 
GLU HG3  H N N 149 
GLU HE2  H N N 150 
GLU HXT  H N N 151 
GLY N    N N N 152 
GLY CA   C N N 153 
GLY C    C N N 154 
GLY O    O N N 155 
GLY OXT  O N N 156 
GLY H    H N N 157 
GLY H2   H N N 158 
GLY HA2  H N N 159 
GLY HA3  H N N 160 
GLY HXT  H N N 161 
GOL C1   C N N 162 
GOL O1   O N N 163 
GOL C2   C N N 164 
GOL O2   O N N 165 
GOL C3   C N N 166 
GOL O3   O N N 167 
GOL H11  H N N 168 
GOL H12  H N N 169 
GOL HO1  H N N 170 
GOL H2   H N N 171 
GOL HO2  H N N 172 
GOL H31  H N N 173 
GOL H32  H N N 174 
GOL HO3  H N N 175 
HIS N    N N N 176 
HIS CA   C N S 177 
HIS C    C N N 178 
HIS O    O N N 179 
HIS CB   C N N 180 
HIS CG   C Y N 181 
HIS ND1  N Y N 182 
HIS CD2  C Y N 183 
HIS CE1  C Y N 184 
HIS NE2  N Y N 185 
HIS OXT  O N N 186 
HIS H    H N N 187 
HIS H2   H N N 188 
HIS HA   H N N 189 
HIS HB2  H N N 190 
HIS HB3  H N N 191 
HIS HD1  H N N 192 
HIS HD2  H N N 193 
HIS HE1  H N N 194 
HIS HE2  H N N 195 
HIS HXT  H N N 196 
HOH O    O N N 197 
HOH H1   H N N 198 
HOH H2   H N N 199 
ILE N    N N N 200 
ILE CA   C N S 201 
ILE C    C N N 202 
ILE O    O N N 203 
ILE CB   C N S 204 
ILE CG1  C N N 205 
ILE CG2  C N N 206 
ILE CD1  C N N 207 
ILE OXT  O N N 208 
ILE H    H N N 209 
ILE H2   H N N 210 
ILE HA   H N N 211 
ILE HB   H N N 212 
ILE HG12 H N N 213 
ILE HG13 H N N 214 
ILE HG21 H N N 215 
ILE HG22 H N N 216 
ILE HG23 H N N 217 
ILE HD11 H N N 218 
ILE HD12 H N N 219 
ILE HD13 H N N 220 
ILE HXT  H N N 221 
LEU N    N N N 222 
LEU CA   C N S 223 
LEU C    C N N 224 
LEU O    O N N 225 
LEU CB   C N N 226 
LEU CG   C N N 227 
LEU CD1  C N N 228 
LEU CD2  C N N 229 
LEU OXT  O N N 230 
LEU H    H N N 231 
LEU H2   H N N 232 
LEU HA   H N N 233 
LEU HB2  H N N 234 
LEU HB3  H N N 235 
LEU HG   H N N 236 
LEU HD11 H N N 237 
LEU HD12 H N N 238 
LEU HD13 H N N 239 
LEU HD21 H N N 240 
LEU HD22 H N N 241 
LEU HD23 H N N 242 
LEU HXT  H N N 243 
LYS N    N N N 244 
LYS CA   C N S 245 
LYS C    C N N 246 
LYS O    O N N 247 
LYS CB   C N N 248 
LYS CG   C N N 249 
LYS CD   C N N 250 
LYS CE   C N N 251 
LYS NZ   N N N 252 
LYS OXT  O N N 253 
LYS H    H N N 254 
LYS H2   H N N 255 
LYS HA   H N N 256 
LYS HB2  H N N 257 
LYS HB3  H N N 258 
LYS HG2  H N N 259 
LYS HG3  H N N 260 
LYS HD2  H N N 261 
LYS HD3  H N N 262 
LYS HE2  H N N 263 
LYS HE3  H N N 264 
LYS HZ1  H N N 265 
LYS HZ2  H N N 266 
LYS HZ3  H N N 267 
LYS HXT  H N N 268 
MET N    N N N 269 
MET CA   C N S 270 
MET C    C N N 271 
MET O    O N N 272 
MET CB   C N N 273 
MET CG   C N N 274 
MET SD   S N N 275 
MET CE   C N N 276 
MET OXT  O N N 277 
MET H    H N N 278 
MET H2   H N N 279 
MET HA   H N N 280 
MET HB2  H N N 281 
MET HB3  H N N 282 
MET HG2  H N N 283 
MET HG3  H N N 284 
MET HE1  H N N 285 
MET HE2  H N N 286 
MET HE3  H N N 287 
MET HXT  H N N 288 
NAG C1   C N R 289 
NAG C2   C N R 290 
NAG C3   C N R 291 
NAG C4   C N S 292 
NAG C5   C N R 293 
NAG C6   C N N 294 
NAG C7   C N N 295 
NAG C8   C N N 296 
NAG N2   N N N 297 
NAG O1   O N N 298 
NAG O3   O N N 299 
NAG O4   O N N 300 
NAG O5   O N N 301 
NAG O6   O N N 302 
NAG O7   O N N 303 
NAG H1   H N N 304 
NAG H2   H N N 305 
NAG H3   H N N 306 
NAG H4   H N N 307 
NAG H5   H N N 308 
NAG H61  H N N 309 
NAG H62  H N N 310 
NAG H81  H N N 311 
NAG H82  H N N 312 
NAG H83  H N N 313 
NAG HN2  H N N 314 
NAG HO1  H N N 315 
NAG HO3  H N N 316 
NAG HO4  H N N 317 
NAG HO6  H N N 318 
PHE N    N N N 319 
PHE CA   C N S 320 
PHE C    C N N 321 
PHE O    O N N 322 
PHE CB   C N N 323 
PHE CG   C Y N 324 
PHE CD1  C Y N 325 
PHE CD2  C Y N 326 
PHE CE1  C Y N 327 
PHE CE2  C Y N 328 
PHE CZ   C Y N 329 
PHE OXT  O N N 330 
PHE H    H N N 331 
PHE H2   H N N 332 
PHE HA   H N N 333 
PHE HB2  H N N 334 
PHE HB3  H N N 335 
PHE HD1  H N N 336 
PHE HD2  H N N 337 
PHE HE1  H N N 338 
PHE HE2  H N N 339 
PHE HZ   H N N 340 
PHE HXT  H N N 341 
PRO N    N N N 342 
PRO CA   C N S 343 
PRO C    C N N 344 
PRO O    O N N 345 
PRO CB   C N N 346 
PRO CG   C N N 347 
PRO CD   C N N 348 
PRO OXT  O N N 349 
PRO H    H N N 350 
PRO HA   H N N 351 
PRO HB2  H N N 352 
PRO HB3  H N N 353 
PRO HG2  H N N 354 
PRO HG3  H N N 355 
PRO HD2  H N N 356 
PRO HD3  H N N 357 
PRO HXT  H N N 358 
SER N    N N N 359 
SER CA   C N S 360 
SER C    C N N 361 
SER O    O N N 362 
SER CB   C N N 363 
SER OG   O N N 364 
SER OXT  O N N 365 
SER H    H N N 366 
SER H2   H N N 367 
SER HA   H N N 368 
SER HB2  H N N 369 
SER HB3  H N N 370 
SER HG   H N N 371 
SER HXT  H N N 372 
THR N    N N N 373 
THR CA   C N S 374 
THR C    C N N 375 
THR O    O N N 376 
THR CB   C N R 377 
THR OG1  O N N 378 
THR CG2  C N N 379 
THR OXT  O N N 380 
THR H    H N N 381 
THR H2   H N N 382 
THR HA   H N N 383 
THR HB   H N N 384 
THR HG1  H N N 385 
THR HG21 H N N 386 
THR HG22 H N N 387 
THR HG23 H N N 388 
THR HXT  H N N 389 
TRP N    N N N 390 
TRP CA   C N S 391 
TRP C    C N N 392 
TRP O    O N N 393 
TRP CB   C N N 394 
TRP CG   C Y N 395 
TRP CD1  C Y N 396 
TRP CD2  C Y N 397 
TRP NE1  N Y N 398 
TRP CE2  C Y N 399 
TRP CE3  C Y N 400 
TRP CZ2  C Y N 401 
TRP CZ3  C Y N 402 
TRP CH2  C Y N 403 
TRP OXT  O N N 404 
TRP H    H N N 405 
TRP H2   H N N 406 
TRP HA   H N N 407 
TRP HB2  H N N 408 
TRP HB3  H N N 409 
TRP HD1  H N N 410 
TRP HE1  H N N 411 
TRP HE3  H N N 412 
TRP HZ2  H N N 413 
TRP HZ3  H N N 414 
TRP HH2  H N N 415 
TRP HXT  H N N 416 
TYR N    N N N 417 
TYR CA   C N S 418 
TYR C    C N N 419 
TYR O    O N N 420 
TYR CB   C N N 421 
TYR CG   C Y N 422 
TYR CD1  C Y N 423 
TYR CD2  C Y N 424 
TYR CE1  C Y N 425 
TYR CE2  C Y N 426 
TYR CZ   C Y N 427 
TYR OH   O N N 428 
TYR OXT  O N N 429 
TYR H    H N N 430 
TYR H2   H N N 431 
TYR HA   H N N 432 
TYR HB2  H N N 433 
TYR HB3  H N N 434 
TYR HD1  H N N 435 
TYR HD2  H N N 436 
TYR HE1  H N N 437 
TYR HE2  H N N 438 
TYR HH   H N N 439 
TYR HXT  H N N 440 
VAL N    N N N 441 
VAL CA   C N S 442 
VAL C    C N N 443 
VAL O    O N N 444 
VAL CB   C N N 445 
VAL CG1  C N N 446 
VAL CG2  C N N 447 
VAL OXT  O N N 448 
VAL H    H N N 449 
VAL H2   H N N 450 
VAL HA   H N N 451 
VAL HB   H N N 452 
VAL HG11 H N N 453 
VAL HG12 H N N 454 
VAL HG13 H N N 455 
VAL HG21 H N N 456 
VAL HG22 H N N 457 
VAL HG23 H N N 458 
VAL HXT  H N N 459 
# 
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  
CIR C   O    doub N N 70  
CIR C   OXT  sing N N 71  
CIR C   CA   sing N N 72  
CIR OXT HXT  sing N N 73  
CIR CA  N    sing N N 74  
CIR CA  C3   sing N N 75  
CIR CA  HA   sing N N 76  
CIR N   H2   sing N N 77  
CIR N   H    sing N N 78  
CIR C3  C4   sing N N 79  
CIR C3  H31  sing N N 80  
CIR C3  H32  sing N N 81  
CIR C4  C5   sing N N 82  
CIR C4  H41  sing N N 83  
CIR C4  H42  sing N N 84  
CIR C5  N6   sing N N 85  
CIR C5  H51  sing N N 86  
CIR C5  H52  sing N N 87  
CIR N6  C7   sing N N 88  
CIR N6  HN6  sing N N 89  
CIR C7  O7   doub N N 90  
CIR C7  N8   sing N N 91  
CIR N8  HN81 sing N N 92  
CIR N8  HN82 sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
GOL C1  O1   sing N N 153 
GOL C1  C2   sing N N 154 
GOL C1  H11  sing N N 155 
GOL C1  H12  sing N N 156 
GOL O1  HO1  sing N N 157 
GOL C2  O2   sing N N 158 
GOL C2  C3   sing N N 159 
GOL C2  H2   sing N N 160 
GOL O2  HO2  sing N N 161 
GOL C3  O3   sing N N 162 
GOL C3  H31  sing N N 163 
GOL C3  H32  sing N N 164 
GOL O3  HO3  sing N N 165 
HIS N   CA   sing N N 166 
HIS N   H    sing N N 167 
HIS N   H2   sing N N 168 
HIS CA  C    sing N N 169 
HIS CA  CB   sing N N 170 
HIS CA  HA   sing N N 171 
HIS C   O    doub N N 172 
HIS C   OXT  sing N N 173 
HIS CB  CG   sing N N 174 
HIS CB  HB2  sing N N 175 
HIS CB  HB3  sing N N 176 
HIS CG  ND1  sing Y N 177 
HIS CG  CD2  doub Y N 178 
HIS ND1 CE1  doub Y N 179 
HIS ND1 HD1  sing N N 180 
HIS CD2 NE2  sing Y N 181 
HIS CD2 HD2  sing N N 182 
HIS CE1 NE2  sing Y N 183 
HIS CE1 HE1  sing N N 184 
HIS NE2 HE2  sing N N 185 
HIS OXT HXT  sing N N 186 
HOH O   H1   sing N N 187 
HOH O   H2   sing N N 188 
ILE N   CA   sing N N 189 
ILE N   H    sing N N 190 
ILE N   H2   sing N N 191 
ILE CA  C    sing N N 192 
ILE CA  CB   sing N N 193 
ILE CA  HA   sing N N 194 
ILE C   O    doub N N 195 
ILE C   OXT  sing N N 196 
ILE CB  CG1  sing N N 197 
ILE CB  CG2  sing N N 198 
ILE CB  HB   sing N N 199 
ILE CG1 CD1  sing N N 200 
ILE CG1 HG12 sing N N 201 
ILE CG1 HG13 sing N N 202 
ILE CG2 HG21 sing N N 203 
ILE CG2 HG22 sing N N 204 
ILE CG2 HG23 sing N N 205 
ILE CD1 HD11 sing N N 206 
ILE CD1 HD12 sing N N 207 
ILE CD1 HD13 sing N N 208 
ILE OXT HXT  sing N N 209 
LEU N   CA   sing N N 210 
LEU N   H    sing N N 211 
LEU N   H2   sing N N 212 
LEU CA  C    sing N N 213 
LEU CA  CB   sing N N 214 
LEU CA  HA   sing N N 215 
LEU C   O    doub N N 216 
LEU C   OXT  sing N N 217 
LEU CB  CG   sing N N 218 
LEU CB  HB2  sing N N 219 
LEU CB  HB3  sing N N 220 
LEU CG  CD1  sing N N 221 
LEU CG  CD2  sing N N 222 
LEU CG  HG   sing N N 223 
LEU CD1 HD11 sing N N 224 
LEU CD1 HD12 sing N N 225 
LEU CD1 HD13 sing N N 226 
LEU CD2 HD21 sing N N 227 
LEU CD2 HD22 sing N N 228 
LEU CD2 HD23 sing N N 229 
LEU OXT HXT  sing N N 230 
LYS N   CA   sing N N 231 
LYS N   H    sing N N 232 
LYS N   H2   sing N N 233 
LYS CA  C    sing N N 234 
LYS CA  CB   sing N N 235 
LYS CA  HA   sing N N 236 
LYS C   O    doub N N 237 
LYS C   OXT  sing N N 238 
LYS CB  CG   sing N N 239 
LYS CB  HB2  sing N N 240 
LYS CB  HB3  sing N N 241 
LYS CG  CD   sing N N 242 
LYS CG  HG2  sing N N 243 
LYS CG  HG3  sing N N 244 
LYS CD  CE   sing N N 245 
LYS CD  HD2  sing N N 246 
LYS CD  HD3  sing N N 247 
LYS CE  NZ   sing N N 248 
LYS CE  HE2  sing N N 249 
LYS CE  HE3  sing N N 250 
LYS NZ  HZ1  sing N N 251 
LYS NZ  HZ2  sing N N 252 
LYS NZ  HZ3  sing N N 253 
LYS OXT HXT  sing N N 254 
MET N   CA   sing N N 255 
MET N   H    sing N N 256 
MET N   H2   sing N N 257 
MET CA  C    sing N N 258 
MET CA  CB   sing N N 259 
MET CA  HA   sing N N 260 
MET C   O    doub N N 261 
MET C   OXT  sing N N 262 
MET CB  CG   sing N N 263 
MET CB  HB2  sing N N 264 
MET CB  HB3  sing N N 265 
MET CG  SD   sing N N 266 
MET CG  HG2  sing N N 267 
MET CG  HG3  sing N N 268 
MET SD  CE   sing N N 269 
MET CE  HE1  sing N N 270 
MET CE  HE2  sing N N 271 
MET CE  HE3  sing N N 272 
MET OXT HXT  sing N N 273 
NAG C1  C2   sing N N 274 
NAG C1  O1   sing N N 275 
NAG C1  O5   sing N N 276 
NAG C1  H1   sing N N 277 
NAG C2  C3   sing N N 278 
NAG C2  N2   sing N N 279 
NAG C2  H2   sing N N 280 
NAG C3  C4   sing N N 281 
NAG C3  O3   sing N N 282 
NAG C3  H3   sing N N 283 
NAG C4  C5   sing N N 284 
NAG C4  O4   sing N N 285 
NAG C4  H4   sing N N 286 
NAG C5  C6   sing N N 287 
NAG C5  O5   sing N N 288 
NAG C5  H5   sing N N 289 
NAG C6  O6   sing N N 290 
NAG C6  H61  sing N N 291 
NAG C6  H62  sing N N 292 
NAG C7  C8   sing N N 293 
NAG C7  N2   sing N N 294 
NAG C7  O7   doub N N 295 
NAG C8  H81  sing N N 296 
NAG C8  H82  sing N N 297 
NAG C8  H83  sing N N 298 
NAG N2  HN2  sing N N 299 
NAG O1  HO1  sing N N 300 
NAG O3  HO3  sing N N 301 
NAG O4  HO4  sing N N 302 
NAG O6  HO6  sing N N 303 
PHE N   CA   sing N N 304 
PHE N   H    sing N N 305 
PHE N   H2   sing N N 306 
PHE CA  C    sing N N 307 
PHE CA  CB   sing N N 308 
PHE CA  HA   sing N N 309 
PHE C   O    doub N N 310 
PHE C   OXT  sing N N 311 
PHE CB  CG   sing N N 312 
PHE CB  HB2  sing N N 313 
PHE CB  HB3  sing N N 314 
PHE CG  CD1  doub Y N 315 
PHE CG  CD2  sing Y N 316 
PHE CD1 CE1  sing Y N 317 
PHE CD1 HD1  sing N N 318 
PHE CD2 CE2  doub Y N 319 
PHE CD2 HD2  sing N N 320 
PHE CE1 CZ   doub Y N 321 
PHE CE1 HE1  sing N N 322 
PHE CE2 CZ   sing Y N 323 
PHE CE2 HE2  sing N N 324 
PHE CZ  HZ   sing N N 325 
PHE OXT HXT  sing N N 326 
PRO N   CA   sing N N 327 
PRO N   CD   sing N N 328 
PRO N   H    sing N N 329 
PRO CA  C    sing N N 330 
PRO CA  CB   sing N N 331 
PRO CA  HA   sing N N 332 
PRO C   O    doub N N 333 
PRO C   OXT  sing N N 334 
PRO CB  CG   sing N N 335 
PRO CB  HB2  sing N N 336 
PRO CB  HB3  sing N N 337 
PRO CG  CD   sing N N 338 
PRO CG  HG2  sing N N 339 
PRO CG  HG3  sing N N 340 
PRO CD  HD2  sing N N 341 
PRO CD  HD3  sing N N 342 
PRO OXT HXT  sing N N 343 
SER N   CA   sing N N 344 
SER N   H    sing N N 345 
SER N   H2   sing N N 346 
SER CA  C    sing N N 347 
SER CA  CB   sing N N 348 
SER CA  HA   sing N N 349 
SER C   O    doub N N 350 
SER C   OXT  sing N N 351 
SER CB  OG   sing N N 352 
SER CB  HB2  sing N N 353 
SER CB  HB3  sing N N 354 
SER OG  HG   sing N N 355 
SER OXT HXT  sing N N 356 
THR N   CA   sing N N 357 
THR N   H    sing N N 358 
THR N   H2   sing N N 359 
THR CA  C    sing N N 360 
THR CA  CB   sing N N 361 
THR CA  HA   sing N N 362 
THR C   O    doub N N 363 
THR C   OXT  sing N N 364 
THR CB  OG1  sing N N 365 
THR CB  CG2  sing N N 366 
THR CB  HB   sing N N 367 
THR OG1 HG1  sing N N 368 
THR CG2 HG21 sing N N 369 
THR CG2 HG22 sing N N 370 
THR CG2 HG23 sing N N 371 
THR OXT HXT  sing N N 372 
TRP N   CA   sing N N 373 
TRP N   H    sing N N 374 
TRP N   H2   sing N N 375 
TRP CA  C    sing N N 376 
TRP CA  CB   sing N N 377 
TRP CA  HA   sing N N 378 
TRP C   O    doub N N 379 
TRP C   OXT  sing N N 380 
TRP CB  CG   sing N N 381 
TRP CB  HB2  sing N N 382 
TRP CB  HB3  sing N N 383 
TRP CG  CD1  doub Y N 384 
TRP CG  CD2  sing Y N 385 
TRP CD1 NE1  sing Y N 386 
TRP CD1 HD1  sing N N 387 
TRP CD2 CE2  doub Y N 388 
TRP CD2 CE3  sing Y N 389 
TRP NE1 CE2  sing Y N 390 
TRP NE1 HE1  sing N N 391 
TRP CE2 CZ2  sing Y N 392 
TRP CE3 CZ3  doub Y N 393 
TRP CE3 HE3  sing N N 394 
TRP CZ2 CH2  doub Y N 395 
TRP CZ2 HZ2  sing N N 396 
TRP CZ3 CH2  sing Y N 397 
TRP CZ3 HZ3  sing N N 398 
TRP CH2 HH2  sing N N 399 
TRP OXT HXT  sing N N 400 
TYR N   CA   sing N N 401 
TYR N   H    sing N N 402 
TYR N   H2   sing N N 403 
TYR CA  C    sing N N 404 
TYR CA  CB   sing N N 405 
TYR CA  HA   sing N N 406 
TYR C   O    doub N N 407 
TYR C   OXT  sing N N 408 
TYR CB  CG   sing N N 409 
TYR CB  HB2  sing N N 410 
TYR CB  HB3  sing N N 411 
TYR CG  CD1  doub Y N 412 
TYR CG  CD2  sing Y N 413 
TYR CD1 CE1  sing Y N 414 
TYR CD1 HD1  sing N N 415 
TYR CD2 CE2  doub Y N 416 
TYR CD2 HD2  sing N N 417 
TYR CE1 CZ   doub Y N 418 
TYR CE1 HE1  sing N N 419 
TYR CE2 CZ   sing Y N 420 
TYR CE2 HE2  sing N N 421 
TYR CZ  OH   sing N N 422 
TYR OH  HH   sing N N 423 
TYR OXT HXT  sing N N 424 
VAL N   CA   sing N N 425 
VAL N   H    sing N N 426 
VAL N   H2   sing N N 427 
VAL CA  C    sing N N 428 
VAL CA  CB   sing N N 429 
VAL CA  HA   sing N N 430 
VAL C   O    doub N N 431 
VAL C   OXT  sing N N 432 
VAL CB  CG1  sing N N 433 
VAL CB  CG2  sing N N 434 
VAL CB  HB   sing N N 435 
VAL CG1 HG11 sing N N 436 
VAL CG1 HG12 sing N N 437 
VAL CG1 HG13 sing N N 438 
VAL CG2 HG21 sing N N 439 
VAL CG2 HG22 sing N N 440 
VAL CG2 HG23 sing N N 441 
VAL OXT HXT  sing N N 442 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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   6V1A 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'R 3 :H' 
_space_group.name_Hall        'R 3' 
_space_group.IT_number        146 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9NIH 
_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]   0.008382 
_atom_sites.fract_transf_matrix[1][2]   0.004839 
_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]   0.009679 
_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]   0.013648 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ILE A 1 1   ? -10.55936 -21.52783 -14.91124 1.000 79.82000  ? 1    ILE A N   1 
ATOM   2    C CA  . ILE A 1 1   ? -10.77923 -22.77939 -15.62542 1.000 82.64000  ? 1    ILE A CA  1 
ATOM   3    C C   . ILE A 1 1   ? -10.82374 -23.93860 -14.63713 1.000 76.37000  ? 1    ILE A C   1 
ATOM   4    O O   . ILE A 1 1   ? -11.86183 -24.21287 -14.03473 1.000 82.42000  ? 1    ILE A O   1 
ATOM   5    C CB  . ILE A 1 1   ? -9.69795  -23.00893 -16.69497 1.000 87.96000  ? 1    ILE A CB  1 
ATOM   6    N N   . LYS A 1 2   ? -9.69396  -24.62319 -14.47822 1.000 74.97000  ? 2    LYS A N   1 
ATOM   7    C CA  . LYS A 1 2   ? -9.58088  -25.68340 -13.48206 1.000 66.08000  ? 2    LYS A CA  1 
ATOM   8    C C   . LYS A 1 2   ? -9.48034  -25.04851 -12.10187 1.000 59.97000  ? 2    LYS A C   1 
ATOM   9    O O   . LYS A 1 2   ? -8.49235  -24.37680 -11.78831 1.000 62.24000  ? 2    LYS A O   1 
ATOM   10   C CB  . LYS A 1 2   ? -8.36811  -26.56448 -13.77565 1.000 63.38000  ? 2    LYS A CB  1 
ATOM   11   C CG  . LYS A 1 2   ? -8.52505  -28.02546 -13.36340 1.000 67.01000  ? 2    LYS A CG  1 
ATOM   12   C CD  . LYS A 1 2   ? -7.71029  -28.94956 -14.25840 1.000 64.83000  ? 2    LYS A CD  1 
ATOM   13   C CE  . LYS A 1 2   ? -6.92138  -29.96348 -13.44129 1.000 67.11000  ? 2    LYS A CE  1 
ATOM   14   N NZ  . LYS A 1 2   ? -7.80309  -30.86430 -12.64270 1.000 68.83000  ? 2    LYS A NZ  1 
ATOM   15   N N   . GLU A 1 3   ? -10.51098 -25.24044 -11.27970 1.000 58.98000  ? 3    GLU A N   1 
ATOM   16   C CA  . GLU A 1 3   ? -10.47840 -24.69863 -9.92818  1.000 61.55000  ? 3    GLU A CA  1 
ATOM   17   C C   . GLU A 1 3   ? -9.60161  -25.53299 -9.00301  1.000 59.26000  ? 3    GLU A C   1 
ATOM   18   O O   . GLU A 1 3   ? -8.98891  -24.98661 -8.07746  1.000 52.70000  ? 3    GLU A O   1 
ATOM   19   C CB  . GLU A 1 3   ? -11.89855 -24.60223 -9.36749  1.000 66.18000  ? 3    GLU A CB  1 
ATOM   20   N N   . GLU A 1 4   ? -9.51681  -26.83930 -9.24205  1.000 56.52000  ? 4    GLU A N   1 
ATOM   21   C CA  . GLU A 1 4   ? -8.78896  -27.74859 -8.37076  1.000 56.00000  ? 4    GLU A CA  1 
ATOM   22   C C   . GLU A 1 4   ? -7.42777  -28.09436 -8.96350  1.000 49.83000  ? 4    GLU A C   1 
ATOM   23   O O   . GLU A 1 4   ? -7.28822  -28.28455 -10.17592 1.000 44.32000  ? 4    GLU A O   1 
ATOM   24   C CB  . GLU A 1 4   ? -9.58773  -29.03432 -8.12443  1.000 58.98000  ? 4    GLU A CB  1 
ATOM   25   C CG  . GLU A 1 4   ? -9.23539  -29.73940 -6.81214  1.000 67.77000  ? 4    GLU A CG  1 
ATOM   26   C CD  . GLU A 1 4   ? -9.11615  -31.25413 -6.95155  1.000 70.08000  ? 4    GLU A CD  1 
ATOM   27   O OE1 . GLU A 1 4   ? -9.12099  -31.75228 -8.09771  1.000 73.31000  ? 4    GLU A OE1 1 
ATOM   28   O OE2 . GLU A 1 4   ? -9.00343  -31.94554 -5.91367  1.000 57.62000  ? 4    GLU A OE2 1 
ATOM   29   N N   . HIS A 1 5   ? -6.42669  -28.17095 -8.09431  1.000 40.51000  ? 5    HIS A N   1 
ATOM   30   C CA  . HIS A 1 5   ? -5.11623  -28.69256 -8.43865  1.000 37.68000  ? 5    HIS A CA  1 
ATOM   31   C C   . HIS A 1 5   ? -4.69069  -29.67090 -7.35618  1.000 35.14000  ? 5    HIS A C   1 
ATOM   32   O O   . HIS A 1 5   ? -5.02342  -29.50273 -6.17828  1.000 29.43000  ? 5    HIS A O   1 
ATOM   33   C CB  . HIS A 1 5   ? -4.07959  -27.57560 -8.58303  1.000 38.76000  ? 5    HIS A CB  1 
ATOM   34   C CG  . HIS A 1 5   ? -4.32959  -26.67300 -9.74862  1.000 40.86000  ? 5    HIS A CG  1 
ATOM   35   N ND1 . HIS A 1 5   ? -4.17606  -27.08590 -11.05560 1.000 42.45000  ? 5    HIS A ND1 1 
ATOM   36   C CD2 . HIS A 1 5   ? -4.73251  -25.38179 -9.80590  1.000 41.76000  ? 5    HIS A CD2 1 
ATOM   37   C CE1 . HIS A 1 5   ? -4.46497  -26.08527 -11.86803 1.000 48.33000  ? 5    HIS A CE1 1 
ATOM   38   N NE2 . HIS A 1 5   ? -4.80625  -25.03971 -11.13547 1.000 41.37000  ? 5    HIS A NE2 1 
ATOM   39   N N   . VAL A 1 6   ? -3.97087  -30.70868 -7.76629  1.000 33.47000  ? 6    VAL A N   1 
ATOM   40   C CA  . VAL A 1 6   ? -3.51325  -31.74714 -6.85530  1.000 34.34000  ? 6    VAL A CA  1 
ATOM   41   C C   . VAL A 1 6   ? -2.02322  -31.96206 -7.07721  1.000 34.79000  ? 6    VAL A C   1 
ATOM   42   O O   . VAL A 1 6   ? -1.59098  -32.21011 -8.21002  1.000 31.47000  ? 6    VAL A O   1 
ATOM   43   C CB  . VAL A 1 6   ? -4.28449  -33.06621 -7.05718  1.000 34.89000  ? 6    VAL A CB  1 
ATOM   44   C CG1 . VAL A 1 6   ? -3.92432  -34.06768 -5.96122  1.000 38.72000  ? 6    VAL A CG1 1 
ATOM   45   C CG2 . VAL A 1 6   ? -5.77961  -32.81200 -7.08162  1.000 40.76000  ? 6    VAL A CG2 1 
ATOM   46   N N   . ILE A 1 7   ? -1.24203  -31.85265 -6.00136  1.000 32.76000  ? 7    ILE A N   1 
ATOM   47   C CA  . ILE A 1 7   ? 0.16113   -32.25469 -5.98428  1.000 32.04000  ? 7    ILE A CA  1 
ATOM   48   C C   . ILE A 1 7   ? 0.25953   -33.51173 -5.13188  1.000 33.27000  ? 7    ILE A C   1 
ATOM   49   O O   . ILE A 1 7   ? -0.14680  -33.51070 -3.96210  1.000 33.74000  ? 7    ILE A O   1 
ATOM   50   C CB  . ILE A 1 7   ? 1.07889   -31.14904 -5.43924  1.000 30.97000  ? 7    ILE A CB  1 
ATOM   51   C CG1 . ILE A 1 7   ? 0.95113   -29.86373 -6.25870  1.000 32.87000  ? 7    ILE A CG1 1 
ATOM   52   C CG2 . ILE A 1 7   ? 2.52246   -31.61347 -5.44345  1.000 30.97000  ? 7    ILE A CG2 1 
ATOM   53   C CD1 . ILE A 1 7   ? 1.69139   -28.68247 -5.63985  1.000 31.67000  ? 7    ILE A CD1 1 
ATOM   54   N N   . ILE A 1 8   ? 0.79609   -34.58178 -5.71107  1.000 32.02000  ? 8    ILE A N   1 
ATOM   55   C CA  . ILE A 1 8   ? 0.88333   -35.87615 -5.04707  1.000 31.68000  ? 8    ILE A CA  1 
ATOM   56   C C   . ILE A 1 8   ? 2.34643   -36.28183 -4.94424  1.000 29.62000  ? 8    ILE A C   1 
ATOM   57   O O   . ILE A 1 8   ? 3.04039   -36.40610 -5.96255  1.000 27.01000  ? 8    ILE A O   1 
ATOM   58   C CB  . ILE A 1 8   ? 0.08386   -36.95875 -5.78665  1.000 33.82000  ? 8    ILE A CB  1 
ATOM   59   C CG1 . ILE A 1 8   ? -1.40584  -36.62360 -5.78211  1.000 36.48000  ? 8    ILE A CG1 1 
ATOM   60   C CG2 . ILE A 1 8   ? 0.33468   -38.32241 -5.15162  1.000 35.71000  ? 8    ILE A CG2 1 
ATOM   61   C CD1 . ILE A 1 8   ? -2.25926  -37.68923 -6.42346  1.000 37.30000  ? 8    ILE A CD1 1 
ATOM   62   N N   . GLN A 1 9   ? 2.80718   -36.49651 -3.71907  1.000 27.36000  ? 9    GLN A N   1 
ATOM   63   C CA  . GLN A 1 9   ? 4.06484   -37.18266 -3.46521  1.000 27.79000  ? 9    GLN A CA  1 
ATOM   64   C C   . GLN A 1 9   ? 3.74344   -38.66981 -3.35553  1.000 27.40000  ? 9    GLN A C   1 
ATOM   65   O O   . GLN A 1 9   ? 3.12351   -39.11298 -2.38146  1.000 30.55000  ? 9    GLN A O   1 
ATOM   66   C CB  . GLN A 1 9   ? 4.70987   -36.63595 -2.19853  1.000 30.19000  ? 9    GLN A CB  1 
ATOM   67   C CG  . GLN A 1 9   ? 6.02712   -37.24734 -1.79795  1.000 32.94000  ? 9    GLN A CG  1 
ATOM   68   C CD  . GLN A 1 9   ? 6.43124   -36.80689 -0.39965  1.000 32.38000  ? 9    GLN A CD  1 
ATOM   69   O OE1 . GLN A 1 9   ? 6.51161   -35.61141 -0.11762  1.000 34.25000  ? 9    GLN A OE1 1 
ATOM   70   N NE2 . GLN A 1 9   ? 6.67143   -37.76805 0.48236   1.000 32.48000  ? 9    GLN A NE2 1 
ATOM   71   N N   . ALA A 1 10  ? 4.12089   -39.43172 -4.37194  1.000 26.93000  ? 10   ALA A N   1 
ATOM   72   C CA  . ALA A 1 10  ? 3.73848   -40.82966 -4.48577  1.000 29.07000  ? 10   ALA A CA  1 
ATOM   73   C C   . ALA A 1 10  ? 4.97312   -41.70227 -4.33479  1.000 28.03000  ? 10   ALA A C   1 
ATOM   74   O O   . ALA A 1 10  ? 6.03184   -41.39841 -4.89308  1.000 30.75000  ? 10   ALA A O   1 
ATOM   75   C CB  . ALA A 1 10  ? 3.04710   -41.10744 -5.82739  1.000 27.68000  ? 10   ALA A CB  1 
ATOM   76   N N   . GLU A 1 11  ? 4.82747   -42.78297 -3.57538  1.000 27.54000  ? 11   GLU A N   1 
ATOM   77   C CA  . GLU A 1 11  ? 5.92696   -43.67186 -3.23946  1.000 29.70000  ? 11   GLU A CA  1 
ATOM   78   C C   . GLU A 1 11  ? 5.44033   -45.11003 -3.29903  1.000 29.73000  ? 11   GLU A C   1 
ATOM   79   O O   . GLU A 1 11  ? 4.26698   -45.39259 -3.04059  1.000 33.97000  ? 11   GLU A O   1 
ATOM   80   C CB  . GLU A 1 11  ? 6.47819   -43.38422 -1.83477  1.000 29.83000  ? 11   GLU A CB  1 
ATOM   81   C CG  . GLU A 1 11  ? 6.87217   -41.92950 -1.59013  1.000 31.39000  ? 11   GLU A CG  1 
ATOM   82   C CD  . GLU A 1 11  ? 6.94123   -41.56853 -0.10923  1.000 32.95000  ? 11   GLU A CD  1 
ATOM   83   O OE1 . GLU A 1 11  ? 7.16647   -42.47885 0.72360   1.000 36.80000  ? 11   GLU A OE1 1 
ATOM   84   O OE2 . GLU A 1 11  ? 6.79698   -40.36996 0.22127   1.000 34.77000  ? 11   GLU A OE2 1 
ATOM   85   N N   . PHE A 1 12  ? 6.34624   -46.02117 -3.63932  1.000 28.65000  ? 12   PHE A N   1 
ATOM   86   C CA  . PHE A 1 12  ? 6.03676   -47.42667 -3.45953  1.000 28.89000  ? 12   PHE A CA  1 
ATOM   87   C C   . PHE A 1 12  ? 7.31585   -48.20430 -3.20601  1.000 29.65000  ? 12   PHE A C   1 
ATOM   88   O O   . PHE A 1 12  ? 8.41956   -47.75626 -3.52337  1.000 26.70000  ? 12   PHE A O   1 
ATOM   89   C CB  . PHE A 1 12  ? 5.23301   -48.01420 -4.64318  1.000 29.25000  ? 12   PHE A CB  1 
ATOM   90   C CG  . PHE A 1 12  ? 6.01921   -48.22777 -5.92398  1.000 29.43000  ? 12   PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 12  ? 6.98643   -49.22046 -6.02996  1.000 30.17000  ? 12   PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 12  ? 5.72280   -47.47669 -7.05372  1.000 33.25000  ? 12   PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 12  ? 7.68027   -49.41804 -7.21864  1.000 30.61000  ? 12   PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 12  ? 6.40893   -47.67355 -8.25305  1.000 31.14000  ? 12   PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 12  ? 7.39072   -48.64348 -8.33117  1.000 30.04000  ? 12   PHE A CZ  1 
ATOM   96   N N   . TYR A 1 13  ? 7.14116   -49.37878 -2.61033  1.000 30.92000  ? 13   TYR A N   1 
ATOM   97   C CA  . TYR A 1 13  ? 8.19421   -50.36940 -2.47107  1.000 29.97000  ? 13   TYR A CA  1 
ATOM   98   C C   . TYR A 1 13  ? 7.60831   -51.72788 -2.80702  1.000 30.74000  ? 13   TYR A C   1 
ATOM   99   O O   . TYR A 1 13  ? 6.50549   -52.05763 -2.36486  1.000 33.91000  ? 13   TYR A O   1 
ATOM   100  C CB  . TYR A 1 13  ? 8.78834   -50.39947 -1.05983  1.000 31.68000  ? 13   TYR A CB  1 
ATOM   101  C CG  . TYR A 1 13  ? 10.13842  -51.05773 -1.04431  1.000 31.89000  ? 13   TYR A CG  1 
ATOM   102  C CD1 . TYR A 1 13  ? 10.26328  -52.43996 -0.93078  1.000 35.81000  ? 13   TYR A CD1 1 
ATOM   103  C CD2 . TYR A 1 13  ? 11.28968  -50.30311 -1.18394  1.000 32.99000  ? 13   TYR A CD2 1 
ATOM   104  C CE1 . TYR A 1 13  ? 11.50870  -53.04612 -0.94029  1.000 36.79000  ? 13   TYR A CE1 1 
ATOM   105  C CE2 . TYR A 1 13  ? 12.53204  -50.89426 -1.19121  1.000 34.28000  ? 13   TYR A CE2 1 
ATOM   106  C CZ  . TYR A 1 13  ? 12.63991  -52.26278 -1.06928  1.000 33.23000  ? 13   TYR A CZ  1 
ATOM   107  O OH  . TYR A 1 13  ? 13.89029  -52.83182 -1.08184  1.000 37.31000  ? 13   TYR A OH  1 
ATOM   108  N N   . LEU A 1 14  ? 8.35082   -52.51333 -3.58023  1.000 34.21000  ? 14   LEU A N   1 
ATOM   109  C CA  . LEU A 1 14  ? 7.88970   -53.80771 -4.06502  1.000 32.97000  ? 14   LEU A CA  1 
ATOM   110  C C   . LEU A 1 14  ? 8.86121   -54.89756 -3.63503  1.000 34.92000  ? 14   LEU A C   1 
ATOM   111  O O   . LEU A 1 14  ? 10.04955  -54.84417 -3.97525  1.000 35.97000  ? 14   LEU A O   1 
ATOM   112  C CB  . LEU A 1 14  ? 7.75454   -53.79691 -5.58565  1.000 32.79000  ? 14   LEU A CB  1 
ATOM   113  C CG  . LEU A 1 14  ? 7.24101   -55.10133 -6.18625  1.000 33.31000  ? 14   LEU A CG  1 
ATOM   114  C CD1 . LEU A 1 14  ? 5.79726   -55.34639 -5.76911  1.000 33.48000  ? 14   LEU A CD1 1 
ATOM   115  C CD2 . LEU A 1 14  ? 7.36989   -55.04004 -7.68083  1.000 35.33000  ? 14   LEU A CD2 1 
ATOM   116  N N   . ASN A 1 15  ? 8.34672   -55.89742 -2.88801  1.000 35.10000  ? 15   ASN A N   1 
ATOM   117  C CA  . ASN A 1 15  ? 9.07872   -57.11126 -2.56840  1.000 36.90000  ? 15   ASN A CA  1 
ATOM   118  C C   . ASN A 1 15  ? 8.57192   -58.27401 -3.41710  1.000 40.44000  ? 15   ASN A C   1 
ATOM   119  O O   . ASN A 1 15  ? 7.38762   -58.32722 -3.76802  1.000 39.14000  ? 15   ASN A O   1 
ATOM   120  C CB  . ASN A 1 15  ? 8.93440   -57.46794 -1.08586  1.000 34.79000  ? 15   ASN A CB  1 
ATOM   121  C CG  . ASN A 1 15  ? 9.99393   -56.80782 -0.21472  1.000 35.31000  ? 15   ASN A CG  1 
ATOM   122  O OD1 . ASN A 1 15  ? 9.76264   -56.56236 0.96823   1.000 35.40000  ? 15   ASN A OD1 1 
ATOM   123  N ND2 . ASN A 1 15  ? 11.16331  -56.52095 -0.79542  1.000 32.31000  ? 15   ASN A ND2 1 
ATOM   124  N N   . PRO A 1 16  ? 9.43794   -59.23789 -3.76628  1.000 39.02000  ? 16   PRO A N   1 
ATOM   125  C CA  . PRO A 1 16  ? 10.84863  -59.30645 -3.37602  1.000 37.79000  ? 16   PRO A CA  1 
ATOM   126  C C   . PRO A 1 16  ? 11.79181  -58.60434 -4.35119  1.000 38.09000  ? 16   PRO A C   1 
ATOM   127  O O   . PRO A 1 16  ? 12.99770  -58.81892 -4.26135  1.000 45.97000  ? 16   PRO A O   1 
ATOM   128  C CB  . PRO A 1 16  ? 11.11808  -60.80847 -3.37591  1.000 34.59000  ? 16   PRO A CB  1 
ATOM   129  C CG  . PRO A 1 16  ? 10.29247  -61.28985 -4.54450  1.000 34.68000  ? 16   PRO A CG  1 
ATOM   130  C CD  . PRO A 1 16  ? 9.03703   -60.42791 -4.54097  1.000 35.33000  ? 16   PRO A CD  1 
ATOM   131  N N   . ASP A 1 17  ? 11.26663  -57.79585 -5.27449  1.000 37.42000  ? 17   ASP A N   1 
ATOM   132  C CA  . ASP A 1 17  ? 12.14071  -57.14499 -6.24622  1.000 37.35000  ? 17   ASP A CA  1 
ATOM   133  C C   . ASP A 1 17  ? 13.07941  -56.12561 -5.60669  1.000 33.98000  ? 17   ASP A C   1 
ATOM   134  O O   . ASP A 1 17  ? 14.10274  -55.78594 -6.21040  1.000 41.67000  ? 17   ASP A O   1 
ATOM   135  C CB  . ASP A 1 17  ? 11.31141  -56.46394 -7.33387  1.000 40.15000  ? 17   ASP A CB  1 
ATOM   136  C CG  . ASP A 1 17  ? 10.21866  -57.35716 -7.88196  1.000 41.53000  ? 17   ASP A CG  1 
ATOM   137  O OD1 . ASP A 1 17  ? 9.30881   -57.72863 -7.11313  1.000 40.29000  ? 17   ASP A OD1 1 
ATOM   138  O OD2 . ASP A 1 17  ? 10.26940  -57.68403 -9.08862  1.000 43.38000  ? 17   ASP A OD2 1 
ATOM   139  N N   . GLN A 1 18  ? 12.76419  -55.65140 -4.39946  1.000 31.47000  ? 18   GLN A N   1 
ATOM   140  C CA  . GLN A 1 18  ? 13.45043  -54.51451 -3.77721  1.000 32.29000  ? 18   GLN A CA  1 
ATOM   141  C C   . GLN A 1 18  ? 13.48475  -53.30995 -4.72010  1.000 32.78000  ? 18   GLN A C   1 
ATOM   142  O O   . GLN A 1 18  ? 14.49923  -52.62401 -4.86112  1.000 33.23000  ? 18   GLN A O   1 
ATOM   143  C CB  . GLN A 1 18  ? 14.85588  -54.89913 -3.29699  1.000 31.29000  ? 18   GLN A CB  1 
ATOM   144  C CG  . GLN A 1 18  ? 14.84280  -55.71430 -1.99372  1.000 31.84000  ? 18   GLN A CG  1 
ATOM   145  C CD  . GLN A 1 18  ? 16.21003  -55.83819 -1.33384  1.000 30.52000  ? 18   GLN A CD  1 
ATOM   146  O OE1 . GLN A 1 18  ? 17.23614  -55.49611 -1.92315  1.000 34.44000  ? 18   GLN A OE1 1 
ATOM   147  N NE2 . GLN A 1 18  ? 16.22580  -56.34328 -0.10261  1.000 29.83000  ? 18   GLN A NE2 1 
ATOM   148  N N   . SER A 1 19  ? 12.35015  -53.04767 -5.36751  1.000 35.13000  ? 19   SER A N   1 
ATOM   149  C CA  . SER A 1 19  ? 12.17020  -51.87238 -6.20982  1.000 32.15000  ? 19   SER A CA  1 
ATOM   150  C C   . SER A 1 19  ? 11.36726  -50.81358 -5.46974  1.000 28.48000  ? 19   SER A C   1 
ATOM   151  O O   . SER A 1 19  ? 10.27636  -51.09371 -4.95486  1.000 25.41000  ? 19   SER A O   1 
ATOM   152  C CB  . SER A 1 19  ? 11.46673  -52.22044 -7.51911  1.000 32.38000  ? 19   SER A CB  1 
ATOM   153  O OG  . SER A 1 19  ? 12.29641  -53.03110 -8.31382  1.000 44.54000  ? 19   SER A OG  1 
ATOM   154  N N   . GLY A 1 20  ? 11.90487  -49.59414 -5.44398  1.000 27.54000  ? 20   GLY A N   1 
ATOM   155  C CA  . GLY A 1 20  ? 11.22169  -48.47619 -4.84221  1.000 29.40000  ? 20   GLY A CA  1 
ATOM   156  C C   . GLY A 1 20  ? 11.08982  -47.32598 -5.82317  1.000 30.53000  ? 20   GLY A C   1 
ATOM   157  O O   . GLY A 1 20  ? 11.79384  -47.24366 -6.83221  1.000 32.40000  ? 20   GLY A O   1 
ATOM   158  N N   . GLU A 1 21  ? 10.15617  -46.43600 -5.50984  1.000 27.79000  ? 21   GLU A N   1 
ATOM   159  C CA  . GLU A 1 21  ? 9.93236   -45.26364 -6.33386  1.000 28.06000  ? 21   GLU A CA  1 
ATOM   160  C C   . GLU A 1 21  ? 9.46127   -44.12275 -5.45070  1.000 27.56000  ? 21   GLU A C   1 
ATOM   161  O O   . GLU A 1 21  ? 8.71668   -44.32757 -4.48851  1.000 27.75000  ? 21   GLU A O   1 
ATOM   162  C CB  . GLU A 1 21  ? 8.90865   -45.52752 -7.44729  1.000 30.47000  ? 21   GLU A CB  1 
ATOM   163  C CG  . GLU A 1 21  ? 8.59925   -44.29235 -8.26881  1.000 29.90000  ? 21   GLU A CG  1 
ATOM   164  C CD  . GLU A 1 21  ? 7.71677   -44.56219 -9.47113  1.000 31.42000  ? 21   GLU A CD  1 
ATOM   165  O OE1 . GLU A 1 21  ? 8.09338   -45.37530 -10.34375 1.000 30.82000  ? 21   GLU A OE1 1 
ATOM   166  O OE2 . GLU A 1 21  ? 6.64511   -43.93422 -9.54329  1.000 31.62000  ? 21   GLU A OE2 1 
ATOM   167  N N   . PHE A 1 22  ? 9.91606   -42.92508 -5.78851  1.000 28.22000  ? 22   PHE A N   1 
ATOM   168  C CA  . PHE A 1 22  ? 9.49867   -41.69842 -5.13351  1.000 28.49000  ? 22   PHE A CA  1 
ATOM   169  C C   . PHE A 1 22  ? 9.33989   -40.67029 -6.23528  1.000 27.38000  ? 22   PHE A C   1 
ATOM   170  O O   . PHE A 1 22  ? 10.27968  -40.44904 -7.00242  1.000 29.08000  ? 22   PHE A O   1 
ATOM   171  C CB  . PHE A 1 22  ? 10.53858  -41.24734 -4.10093  1.000 29.75000  ? 22   PHE A CB  1 
ATOM   172  C CG  . PHE A 1 22  ? 10.19574  -39.96309 -3.40407  1.000 28.19000  ? 22   PHE A CG  1 
ATOM   173  C CD1 . PHE A 1 22  ? 10.37951  -38.74596 -4.03227  1.000 27.99000  ? 22   PHE A CD1 1 
ATOM   174  C CD2 . PHE A 1 22  ? 9.71542   -39.97530 -2.10542  1.000 30.03000  ? 22   PHE A CD2 1 
ATOM   175  C CE1 . PHE A 1 22  ? 10.07432  -37.56237 -3.39049  1.000 30.73000  ? 22   PHE A CE1 1 
ATOM   176  C CE2 . PHE A 1 22  ? 9.40696   -38.79449 -1.45626  1.000 31.64000  ? 22   PHE A CE2 1 
ATOM   177  C CZ  . PHE A 1 22  ? 9.58794   -37.58413 -2.10201  1.000 29.22000  ? 22   PHE A CZ  1 
ATOM   178  N N   . MET A 1 23  ? 8.16672   -40.05166 -6.32830  1.000 28.07000  ? 23   MET A N   1 
ATOM   179  C CA  . MET A 1 23  ? 7.95948   -39.04732 -7.36023  1.000 27.90000  ? 23   MET A CA  1 
ATOM   180  C C   . MET A 1 23  ? 6.92841   -38.02711 -6.90299  1.000 28.17000  ? 23   MET A C   1 
ATOM   181  O O   . MET A 1 23  ? 6.09940   -38.29921 -6.02926  1.000 27.60000  ? 23   MET A O   1 
ATOM   182  C CB  . MET A 1 23  ? 7.57749   -39.69972 -8.70261  1.000 30.82000  ? 23   MET A CB  1 
ATOM   183  C CG  . MET A 1 23  ? 6.24142   -40.45265 -8.77850  1.000 36.30000  ? 23   MET A CG  1 
ATOM   184  S SD  . MET A 1 23  ? 4.76847   -39.45280 -9.07515  1.000 41.92000  ? 23   MET A SD  1 
ATOM   185  C CE  . MET A 1 23  ? 4.80086   -39.35076 -10.86392 1.000 40.75000  ? 23   MET A CE  1 
ATOM   186  N N   . PHE A 1 24  ? 7.03233   -36.82963 -7.46975  1.000 29.03000  ? 24   PHE A N   1 
ATOM   187  C CA  . PHE A 1 24  ? 6.03330   -35.78476 -7.31001  1.000 29.31000  ? 24   PHE A CA  1 
ATOM   188  C C   . PHE A 1 24  ? 5.19536   -35.69561 -8.57837  1.000 29.66000  ? 24   PHE A C   1 
ATOM   189  O O   . PHE A 1 24  ? 5.72577   -35.73478 -9.69245  1.000 30.55000  ? 24   PHE A O   1 
ATOM   190  C CB  . PHE A 1 24  ? 6.67639   -34.42746 -7.02795  1.000 27.59000  ? 24   PHE A CB  1 
ATOM   191  C CG  . PHE A 1 24  ? 6.85935   -34.12496 -5.57141  1.000 29.37000  ? 24   PHE A CG  1 
ATOM   192  C CD1 . PHE A 1 24  ? 7.61352   -34.95877 -4.76131  1.000 32.22000  ? 24   PHE A CD1 1 
ATOM   193  C CD2 . PHE A 1 24  ? 6.29587   -32.98675 -5.01566  1.000 30.11000  ? 24   PHE A CD2 1 
ATOM   194  C CE1 . PHE A 1 24  ? 7.80306   -34.66138 -3.41964  1.000 32.62000  ? 24   PHE A CE1 1 
ATOM   195  C CE2 . PHE A 1 24  ? 6.47417   -32.68830 -3.67513  1.000 31.81000  ? 24   PHE A CE2 1 
ATOM   196  C CZ  . PHE A 1 24  ? 7.23009   -33.52806 -2.87610  1.000 32.91000  ? 24   PHE A CZ  1 
ATOM   197  N N   . ASP A 1 25  ? 3.88688   -35.55328 -8.39540  1.000 30.97000  ? 25   ASP A N   1 
ATOM   198  C CA  . ASP A 1 25  ? 2.91208   -35.59131 -9.47336  1.000 33.44000  ? 25   ASP A CA  1 
ATOM   199  C C   . ASP A 1 25  ? 2.00945   -34.37233 -9.35705  1.000 31.17000  ? 25   ASP A C   1 
ATOM   200  O O   . ASP A 1 25  ? 1.43362   -34.13234 -8.29178  1.000 26.31000  ? 25   ASP A O   1 
ATOM   201  C CB  . ASP A 1 25  ? 2.09460   -36.88627 -9.39033  1.000 39.00000  ? 25   ASP A CB  1 
ATOM   202  C CG  . ASP A 1 25  ? 1.12794   -37.04606 -10.53733 1.000 47.93000  ? 25   ASP A CG  1 
ATOM   203  O OD1 . ASP A 1 25  ? 0.00571   -36.50317 -10.44750 1.000 63.03000  ? 25   ASP A OD1 1 
ATOM   204  O OD2 . ASP A 1 25  ? 1.48690   -37.72318 -11.52670 1.000 53.61000  ? 25   ASP A OD2 1 
ATOM   205  N N   . PHE A 1 26  ? 1.89280   -33.59815 -10.43727 1.000 30.22000  ? 26   PHE A N   1 
ATOM   206  C CA  . PHE A 1 26  ? 0.99919   -32.44453 -10.48501 1.000 29.08000  ? 26   PHE A CA  1 
ATOM   207  C C   . PHE A 1 26  ? -0.07413  -32.70929 -11.52701 1.000 30.46000  ? 26   PHE A C   1 
ATOM   208  O O   . PHE A 1 26  ? 0.23648   -32.85444 -12.71543 1.000 30.18000  ? 26   PHE A O   1 
ATOM   209  C CB  . PHE A 1 26  ? 1.75538   -31.15387 -10.81667 1.000 29.59000  ? 26   PHE A CB  1 
ATOM   210  C CG  . PHE A 1 26  ? 0.85665   -29.95431 -11.04490 1.000 29.93000  ? 26   PHE A CG  1 
ATOM   211  C CD1 . PHE A 1 26  ? 0.38821   -29.20298 -9.97399  1.000 30.81000  ? 26   PHE A CD1 1 
ATOM   212  C CD2 . PHE A 1 26  ? 0.49180   -29.57182 -12.32925 1.000 29.22000  ? 26   PHE A CD2 1 
ATOM   213  C CE1 . PHE A 1 26  ? -0.42991  -28.09370 -10.17871 1.000 30.57000  ? 26   PHE A CE1 1 
ATOM   214  C CE2 . PHE A 1 26  ? -0.32883  -28.46936 -12.54317 1.000 28.06000  ? 26   PHE A CE2 1 
ATOM   215  C CZ  . PHE A 1 26  ? -0.78941  -27.72923 -11.46908 1.000 28.68000  ? 26   PHE A CZ  1 
ATOM   216  N N   . ASP A 1 27  ? -1.33048  -32.77114 -11.08160 1.000 32.83000  ? 27   ASP A N   1 
ATOM   217  C CA  . ASP A 1 27  ? -2.47751  -32.96188 -11.97385 1.000 32.13000  ? 27   ASP A CA  1 
ATOM   218  C C   . ASP A 1 27  ? -2.24555  -34.10329 -12.96792 1.000 31.79000  ? 27   ASP A C   1 
ATOM   219  O O   . ASP A 1 27  ? -2.66652  -34.04186 -14.12524 1.000 33.51000  ? 27   ASP A O   1 
ATOM   220  C CB  . ASP A 1 27  ? -2.82011  -31.66284 -12.70975 1.000 32.99000  ? 27   ASP A CB  1 
ATOM   221  C CG  . ASP A 1 27  ? -3.34469  -30.57494 -11.77643 1.000 36.53000  ? 27   ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 27  ? -3.64548  -30.87022 -10.60056 1.000 37.39000  ? 27   ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 27  ? -3.47383  -29.41828 -12.22517 1.000 37.22000  ? 27   ASP A OD2 1 
ATOM   224  N N   . GLY A 1 28  ? -1.55445  -35.15278 -12.51872 1.000 32.17000  ? 28   GLY A N   1 
ATOM   225  C CA  . GLY A 1 28  ? -1.35719  -36.34062 -13.32812 1.000 30.21000  ? 28   GLY A CA  1 
ATOM   226  C C   . GLY A 1 28  ? -0.05507  -36.40234 -14.09833 1.000 28.96000  ? 28   GLY A C   1 
ATOM   227  O O   . GLY A 1 28  ? 0.20156   -37.41532 -14.76194 1.000 31.36000  ? 28   GLY A O   1 
ATOM   228  N N   . ASP A 1 29  ? 0.77085   -35.35906 -14.03868 1.000 28.60000  ? 29   ASP A N   1 
ATOM   229  C CA  . ASP A 1 29  ? 2.05161   -35.31757 -14.72677 1.000 27.93000  ? 29   ASP A CA  1 
ATOM   230  C C   . ASP A 1 29  ? 3.18725   -35.33141 -13.71246 1.000 26.45000  ? 29   ASP A C   1 
ATOM   231  O O   . ASP A 1 29  ? 3.07015   -34.75219 -12.62805 1.000 28.61000  ? 29   ASP A O   1 
ATOM   232  C CB  . ASP A 1 29  ? 2.15560   -34.07412 -15.61100 1.000 29.95000  ? 29   ASP A CB  1 
ATOM   233  C CG  . ASP A 1 29  ? 1.47646   -34.26149 -16.95190 1.000 34.49000  ? 29   ASP A CG  1 
ATOM   234  O OD1 . ASP A 1 29  ? 1.98102   -35.07080 -17.76926 1.000 30.03000  ? 29   ASP A OD1 1 
ATOM   235  O OD2 . ASP A 1 29  ? 0.43832   -33.60294 -17.18736 1.000 36.19000  ? 29   ASP A OD2 1 
ATOM   236  N N   . GLU A 1 30  ? 4.28933   -35.98675 -14.07016 1.000 26.87000  ? 30   GLU A N   1 
ATOM   237  C CA  . GLU A 1 30  ? 5.42592   -36.10891 -13.16672 1.000 27.54000  ? 30   GLU A CA  1 
ATOM   238  C C   . GLU A 1 30  ? 6.24403   -34.82304 -13.15297 1.000 27.15000  ? 30   GLU A C   1 
ATOM   239  O O   . GLU A 1 30  ? 6.64466   -34.32308 -14.20727 1.000 25.42000  ? 30   GLU A O   1 
ATOM   240  C CB  . GLU A 1 30  ? 6.31680   -37.28319 -13.57597 1.000 29.26000  ? 30   GLU A CB  1 
ATOM   241  C CG  . GLU A 1 30  ? 7.68933   -37.23893 -12.90140 1.000 30.40000  ? 30   GLU A CG  1 
ATOM   242  C CD  . GLU A 1 30  ? 8.66848   -38.28772 -13.41125 1.000 34.46000  ? 30   GLU A CD  1 
ATOM   243  O OE1 . GLU A 1 30  ? 8.34131   -39.01014 -14.37540 1.000 34.46000  ? 30   GLU A OE1 1 
ATOM   244  O OE2 . GLU A 1 30  ? 9.78352   -38.38099 -12.84603 1.000 39.60000  ? 30   GLU A OE2 1 
ATOM   245  N N   . ILE A 1 31  ? 6.48818   -34.28320 -11.95821 1.000 28.56000  ? 31   ILE A N   1 
ATOM   246  C CA  . ILE A 1 31  ? 7.45545   -33.19798 -11.81905 1.000 28.78000  ? 31   ILE A CA  1 
ATOM   247  C C   . ILE A 1 31  ? 8.86702   -33.75602 -11.72621 1.000 28.14000  ? 31   ILE A C   1 
ATOM   248  O O   . ILE A 1 31  ? 9.77543   -33.33003 -12.45063 1.000 33.68000  ? 31   ILE A O   1 
ATOM   249  C CB  . ILE A 1 31  ? 7.12822   -32.33079 -10.59242 1.000 29.08000  ? 31   ILE A CB  1 
ATOM   250  C CG1 . ILE A 1 31  ? 5.67954   -31.83857 -10.63658 1.000 27.16000  ? 31   ILE A CG1 1 
ATOM   251  C CG2 . ILE A 1 31  ? 8.12782   -31.17077 -10.47599 1.000 28.60000  ? 31   ILE A CG2 1 
ATOM   252  C CD1 . ILE A 1 31  ? 5.23805   -31.22076 -9.32468  1.000 28.86000  ? 31   ILE A CD1 1 
ATOM   253  N N   . PHE A 1 32  ? 9.07454   -34.71346 -10.82881 1.000 27.86000  ? 32   PHE A N   1 
ATOM   254  C CA  . PHE A 1 32  ? 10.37303  -35.35088 -10.70268 1.000 28.49000  ? 32   PHE A CA  1 
ATOM   255  C C   . PHE A 1 32  ? 10.19760  -36.69346 -10.01664 1.000 28.98000  ? 32   PHE A C   1 
ATOM   256  O O   . PHE A 1 32  ? 9.16555   -36.97587 -9.40279  1.000 25.83000  ? 32   PHE A O   1 
ATOM   257  C CB  . PHE A 1 32  ? 11.37202  -34.46942 -9.93063  1.000 30.70000  ? 32   PHE A CB  1 
ATOM   258  C CG  . PHE A 1 32  ? 11.07500  -34.33105 -8.45444  1.000 29.64000  ? 32   PHE A CG  1 
ATOM   259  C CD1 . PHE A 1 32  ? 11.51675  -35.28335 -7.54261  1.000 29.38000  ? 32   PHE A CD1 1 
ATOM   260  C CD2 . PHE A 1 32  ? 10.37683  -33.23387 -7.97533  1.000 32.68000  ? 32   PHE A CD2 1 
ATOM   261  C CE1 . PHE A 1 32  ? 11.24716  -35.15590 -6.19019  1.000 30.50000  ? 32   PHE A CE1 1 
ATOM   262  C CE2 . PHE A 1 32  ? 10.10871  -33.09905 -6.61716  1.000 32.78000  ? 32   PHE A CE2 1 
ATOM   263  C CZ  . PHE A 1 32  ? 10.55344  -34.05849 -5.72550  1.000 29.46000  ? 32   PHE A CZ  1 
ATOM   264  N N   . HIS A 1 33  ? 11.22731  -37.51698 -10.13118 1.000 28.11000  ? 33   HIS A N   1 
ATOM   265  C CA  . HIS A 1 33  ? 11.35269  -38.70193 -9.31007  1.000 29.23000  ? 33   HIS A CA  1 
ATOM   266  C C   . HIS A 1 33  ? 12.77642  -38.75974 -8.78742  1.000 30.42000  ? 33   HIS A C   1 
ATOM   267  O O   . HIS A 1 33  ? 13.64433  -37.98214 -9.19476  1.000 31.17000  ? 33   HIS A O   1 
ATOM   268  C CB  . HIS A 1 33  ? 10.98253  -39.97459 -10.08002 1.000 27.32000  ? 33   HIS A CB  1 
ATOM   269  C CG  . HIS A 1 33  ? 12.01619  -40.40923 -11.07012 1.000 29.80000  ? 33   HIS A CG  1 
ATOM   270  N ND1 . HIS A 1 33  ? 12.04460  -39.94070 -12.36655 1.000 29.05000  ? 33   HIS A ND1 1 
ATOM   271  C CD2 . HIS A 1 33  ? 13.04328  -41.28711 -10.96293 1.000 30.65000  ? 33   HIS A CD2 1 
ATOM   272  C CE1 . HIS A 1 33  ? 13.05373  -40.49958 -13.01144 1.000 30.89000  ? 33   HIS A CE1 1 
ATOM   273  N NE2 . HIS A 1 33  ? 13.67220  -41.32387 -12.18442 1.000 28.45000  ? 33   HIS A NE2 1 
ATOM   274  N N   . VAL A 1 34  ? 13.00816  -39.67123 -7.85343  1.000 29.51000  ? 34   VAL A N   1 
ATOM   275  C CA  . VAL A 1 34  ? 14.33728  -39.89936 -7.30618  1.000 32.79000  ? 34   VAL A CA  1 
ATOM   276  C C   . VAL A 1 34  ? 14.83063  -41.23465 -7.83476  1.000 34.43000  ? 34   VAL A C   1 
ATOM   277  O O   . VAL A 1 34  ? 14.17857  -42.26905 -7.64299  1.000 34.85000  ? 34   VAL A O   1 
ATOM   278  C CB  . VAL A 1 34  ? 14.34063  -39.86890 -5.77197  1.000 34.94000  ? 34   VAL A CB  1 
ATOM   279  C CG1 . VAL A 1 34  ? 15.72581  -40.22388 -5.25134  1.000 36.11000  ? 34   VAL A CG1 1 
ATOM   280  C CG2 . VAL A 1 34  ? 13.92171  -38.49464 -5.28978  1.000 37.59000  ? 34   VAL A CG2 1 
ATOM   281  N N   . ASP A 1 35  ? 15.96354  -41.20246 -8.52799  1.000 36.00000  ? 35   ASP A N   1 
ATOM   282  C CA  . ASP A 1 35  ? 16.60142  -42.42217 -8.99628  1.000 38.88000  ? 35   ASP A CA  1 
ATOM   283  C C   . ASP A 1 35  ? 17.17911  -43.17450 -7.80296  1.000 39.14000  ? 35   ASP A C   1 
ATOM   284  O O   . ASP A 1 35  ? 18.05788  -42.65906 -7.09904  1.000 35.88000  ? 35   ASP A O   1 
ATOM   285  C CB  . ASP A 1 35  ? 17.68834  -42.08051 -10.01023 1.000 41.63000  ? 35   ASP A CB  1 
ATOM   286  C CG  . ASP A 1 35  ? 18.17599  -43.29352 -10.77659 1.000 41.32000  ? 35   ASP A CG  1 
ATOM   287  O OD1 . ASP A 1 35  ? 18.68788  -44.23711 -10.14085 1.000 41.27000  ? 35   ASP A OD1 1 
ATOM   288  O OD2 . ASP A 1 35  ? 18.04109  -43.30118 -12.01925 1.000 53.31000  ? 35   ASP A OD2 1 
ATOM   289  N N   . MET A 1 36  ? 16.67478  -44.38893 -7.57311  1.000 40.38000  ? 36   MET A N   1 
ATOM   290  C CA  . MET A 1 36  ? 17.10896  -45.17633 -6.42393  1.000 46.57000  ? 36   MET A CA  1 
ATOM   291  C C   . MET A 1 36  ? 18.59119  -45.51167 -6.50942  1.000 45.15000  ? 36   MET A C   1 
ATOM   292  O O   . MET A 1 36  ? 19.34047  -45.32604 -5.54258  1.000 49.90000  ? 36   MET A O   1 
ATOM   293  C CB  . MET A 1 36  ? 16.28531  -46.45753 -6.33295  1.000 50.43000  ? 36   MET A CB  1 
ATOM   294  C CG  . MET A 1 36  ? 14.81637  -46.23166 -6.09882  1.000 57.83000  ? 36   MET A CG  1 
ATOM   295  S SD  . MET A 1 36  ? 14.56944  -45.48648 -4.47982  1.000 63.91000  ? 36   MET A SD  1 
ATOM   296  C CE  . MET A 1 36  ? 13.90011  -43.87885 -4.91318  1.000 63.72000  ? 36   MET A CE  1 
ATOM   297  N N   . ALA A 1 37  ? 19.02850  -46.01919 -7.66365  1.000 41.74000  ? 37   ALA A N   1 
ATOM   298  C CA  . ALA A 1 37  ? 20.40833  -46.46693 -7.80736  1.000 42.20000  ? 37   ALA A CA  1 
ATOM   299  C C   . ALA A 1 37  ? 21.38809  -45.30161 -7.72926  1.000 39.39000  ? 37   ALA A C   1 
ATOM   300  O O   . ALA A 1 37  ? 22.45062  -45.41791 -7.10480  1.000 39.34000  ? 37   ALA A O   1 
ATOM   301  C CB  . ALA A 1 37  ? 20.56835  -47.22301 -9.12591  1.000 40.58000  ? 37   ALA A CB  1 
ATOM   302  N N   . LYS A 1 38  ? 21.04495  -44.16872 -8.34407  1.000 38.54000  ? 38   LYS A N   1 
ATOM   303  C CA  . LYS A 1 38  ? 21.94600  -43.02805 -8.44013  1.000 41.48000  ? 38   LYS A CA  1 
ATOM   304  C C   . LYS A 1 38  ? 21.73467  -41.98503 -7.35149  1.000 37.53000  ? 38   LYS A C   1 
ATOM   305  O O   . LYS A 1 38  ? 22.51764  -41.03267 -7.27738  1.000 32.23000  ? 38   LYS A O   1 
ATOM   306  C CB  . LYS A 1 38  ? 21.80308  -42.35767 -9.81118  1.000 48.55000  ? 38   LYS A CB  1 
ATOM   307  C CG  . LYS A 1 38  ? 22.07951  -43.28524 -10.98105 1.000 55.03000  ? 38   LYS A CG  1 
ATOM   308  C CD  . LYS A 1 38  ? 23.39999  -44.03218 -10.80035 1.000 65.57000  ? 38   LYS A CD  1 
ATOM   309  C CE  . LYS A 1 38  ? 23.27591  -45.49825 -11.19665 1.000 72.18000  ? 38   LYS A CE  1 
ATOM   310  N NZ  . LYS A 1 38  ? 24.45032  -46.30496 -10.75664 1.000 74.85000  ? 38   LYS A NZ  1 
ATOM   311  N N   . LYS A 1 39  ? 20.71057  -42.14055 -6.50923  1.000 41.42000  ? 39   LYS A N   1 
ATOM   312  C CA  . LYS A 1 39  ? 20.42500  -41.19965 -5.41804  1.000 42.44000  ? 39   LYS A CA  1 
ATOM   313  C C   . LYS A 1 39  ? 20.29445  -39.76971 -5.93625  1.000 39.71000  ? 39   LYS A C   1 
ATOM   314  O O   . LYS A 1 39  ? 20.73326  -38.81373 -5.29730  1.000 40.35000  ? 39   LYS A O   1 
ATOM   315  C CB  . LYS A 1 39  ? 21.48965  -41.26959 -4.31461  1.000 48.02000  ? 39   LYS A CB  1 
ATOM   316  C CG  . LYS A 1 39  ? 22.17829  -42.61686 -4.13688  1.000 56.24000  ? 39   LYS A CG  1 
ATOM   317  C CD  . LYS A 1 39  ? 21.45074  -43.49439 -3.13340  1.000 61.34000  ? 39   LYS A CD  1 
ATOM   318  C CE  . LYS A 1 39  ? 21.88858  -44.94798 -3.25193  1.000 69.35000  ? 39   LYS A CE  1 
ATOM   319  N NZ  . LYS A 1 39  ? 20.77684  -45.89703 -2.95732  1.000 69.87000  ? 39   LYS A NZ  1 
ATOM   320  N N   . GLU A 1 40  ? 19.68718  -39.61460 -7.10580  1.000 38.95000  ? 40   GLU A N   1 
ATOM   321  C CA  . GLU A 1 40  ? 19.60017  -38.31746 -7.75795  1.000 44.54000  ? 40   GLU A CA  1 
ATOM   322  C C   . GLU A 1 40  ? 18.15099  -37.94300 -8.02601  1.000 39.22000  ? 40   GLU A C   1 
ATOM   323  O O   . GLU A 1 40  ? 17.33232  -38.79508 -8.38463  1.000 33.45000  ? 40   GLU A O   1 
ATOM   324  C CB  . GLU A 1 40  ? 20.38220  -38.30968 -9.07185  1.000 48.85000  ? 40   GLU A CB  1 
ATOM   325  C CG  . GLU A 1 40  ? 21.77025  -37.71758 -8.94903  1.000 59.26000  ? 40   GLU A CG  1 
ATOM   326  C CD  . GLU A 1 40  ? 22.44278  -37.55125 -10.29154 1.000 69.55000  ? 40   GLU A CD  1 
ATOM   327  O OE1 . GLU A 1 40  ? 23.64634  -37.20332 -10.32208 1.000 74.87000  ? 40   GLU A OE1 1 
ATOM   328  O OE2 . GLU A 1 40  ? 21.76209  -37.77249 -11.31680 1.000 69.31000  ? 40   GLU A OE2 1 
ATOM   329  N N   . THR A 1 41  ? 17.84119  -36.66310 -7.84462  1.000 35.91000  ? 41   THR A N   1 
ATOM   330  C CA  . THR A 1 41  ? 16.57191  -36.13540 -8.31723  1.000 35.81000  ? 41   THR A CA  1 
ATOM   331  C C   . THR A 1 41  ? 16.61390  -36.01825 -9.83529  1.000 36.53000  ? 41   THR A C   1 
ATOM   332  O O   . THR A 1 41  ? 17.54023  -35.42333 -10.39661 1.000 31.00000  ? 41   THR A O   1 
ATOM   333  C CB  . THR A 1 41  ? 16.28533  -34.77498 -7.68586  1.000 33.51000  ? 41   THR A CB  1 
ATOM   334  O OG1 . THR A 1 41  ? 16.39085  -34.87574 -6.26136  1.000 36.79000  ? 41   THR A OG1 1 
ATOM   335  C CG2 . THR A 1 41  ? 14.89007  -34.30587 -8.04905  1.000 33.56000  ? 41   THR A CG2 1 
ATOM   336  N N   . VAL A 1 42  ? 15.61987  -36.60302 -10.49974 1.000 32.15000  ? 42   VAL A N   1 
ATOM   337  C CA  . VAL A 1 42  ? 15.51080  -36.57878 -11.95422 1.000 30.23000  ? 42   VAL A CA  1 
ATOM   338  C C   . VAL A 1 42  ? 14.24302  -35.80879 -12.30249 1.000 30.58000  ? 42   VAL A C   1 
ATOM   339  O O   . VAL A 1 42  ? 13.12946  -36.31635 -12.11036 1.000 31.39000  ? 42   VAL A O   1 
ATOM   340  C CB  . VAL A 1 42  ? 15.48170  -37.99261 -12.55189 1.000 32.93000  ? 42   VAL A CB  1 
ATOM   341  C CG1 . VAL A 1 42  ? 15.33348  -37.93828 -14.07178 1.000 31.60000  ? 42   VAL A CG1 1 
ATOM   342  C CG2 . VAL A 1 42  ? 16.73140  -38.76112 -12.15715 1.000 32.34000  ? 42   VAL A CG2 1 
ATOM   343  N N   . TRP A 1 43  ? 14.40511  -34.58639 -12.80873 1.000 29.07000  ? 43   TRP A N   1 
ATOM   344  C CA  . TRP A 1 43  ? 13.26489  -33.77031 -13.19881 1.000 27.25000  ? 43   TRP A CA  1 
ATOM   345  C C   . TRP A 1 43  ? 12.70355  -34.25705 -14.52764 1.000 29.27000  ? 43   TRP A C   1 
ATOM   346  O O   . TRP A 1 43  ? 13.45354  -34.57857 -15.45292 1.000 24.99000  ? 43   TRP A O   1 
ATOM   347  C CB  . TRP A 1 43  ? 13.67357  -32.29966 -13.29432 1.000 27.92000  ? 43   TRP A CB  1 
ATOM   348  C CG  . TRP A 1 43  ? 14.31556  -31.80438 -12.02534 1.000 28.91000  ? 43   TRP A CG  1 
ATOM   349  C CD1 . TRP A 1 43  ? 15.64945  -31.80259 -11.72815 1.000 30.79000  ? 43   TRP A CD1 1 
ATOM   350  C CD2 . TRP A 1 43  ? 13.64735  -31.27606 -10.87198 1.000 28.08000  ? 43   TRP A CD2 1 
ATOM   351  N NE1 . TRP A 1 43  ? 15.85203  -31.29230 -10.46776 1.000 30.60000  ? 43   TRP A NE1 1 
ATOM   352  C CE2 . TRP A 1 43  ? 14.64018  -30.96300 -9.92086  1.000 28.73000  ? 43   TRP A CE2 1 
ATOM   353  C CE3 . TRP A 1 43  ? 12.30640  -31.02976 -10.55386 1.000 29.95000  ? 43   TRP A CE3 1 
ATOM   354  C CZ2 . TRP A 1 43  ? 14.33562  -30.41606 -8.67375  1.000 28.88000  ? 43   TRP A CZ2 1 
ATOM   355  C CZ3 . TRP A 1 43  ? 12.00524  -30.48770 -9.31203  1.000 28.89000  ? 43   TRP A CZ3 1 
ATOM   356  C CH2 . TRP A 1 43  ? 13.01493  -30.18799 -8.38912  1.000 27.97000  ? 43   TRP A CH2 1 
ATOM   357  N N   . ARG A 1 44  ? 11.37134  -34.33124 -14.60842 1.000 29.07000  ? 44   ARG A N   1 
ATOM   358  C CA  . ARG A 1 44  ? 10.73163  -34.84248 -15.81480 1.000 28.07000  ? 44   ARG A CA  1 
ATOM   359  C C   . ARG A 1 44  ? 11.02857  -33.95193 -17.01423 1.000 30.66000  ? 44   ARG A C   1 
ATOM   360  O O   . ARG A 1 44  ? 11.30133  -34.44635 -18.11542 1.000 32.38000  ? 44   ARG A O   1 
ATOM   361  C CB  . ARG A 1 44  ? 9.22780   -34.96122 -15.59360 1.000 27.68000  ? 44   ARG A CB  1 
ATOM   362  C CG  . ARG A 1 44  ? 8.45151   -35.52296 -16.77799 1.000 26.91000  ? 44   ARG A CG  1 
ATOM   363  C CD  . ARG A 1 44  ? 8.90994   -36.91435 -17.14001 1.000 27.45000  ? 44   ARG A CD  1 
ATOM   364  N NE  . ARG A 1 44  ? 8.29384   -37.37434 -18.37874 1.000 29.74000  ? 44   ARG A NE  1 
ATOM   365  C CZ  . ARG A 1 44  ? 8.81173   -37.16680 -19.58234 1.000 29.26000  ? 44   ARG A CZ  1 
ATOM   366  N NH1 . ARG A 1 44  ? 9.93445   -36.48442 -19.74222 1.000 29.68000  ? 44   ARG A NH1 1 
ATOM   367  N NH2 . ARG A 1 44  ? 8.19151   -37.65868 -20.65050 1.000 29.89000  ? 44   ARG A NH2 1 
ATOM   368  N N   . LEU A 1 45  ? 10.94586  -32.63997 -16.82633 1.000 30.86000  ? 45   LEU A N   1 
ATOM   369  C CA  . LEU A 1 45  ? 11.47413  -31.66235 -17.76306 1.000 31.08000  ? 45   LEU A CA  1 
ATOM   370  C C   . LEU A 1 45  ? 12.67545  -31.00007 -17.10362 1.000 32.35000  ? 45   LEU A C   1 
ATOM   371  O O   . LEU A 1 45  ? 12.57927  -30.54379 -15.95940 1.000 30.80000  ? 45   LEU A O   1 
ATOM   372  C CB  . LEU A 1 45  ? 10.41833  -30.61678 -18.13153 1.000 29.56000  ? 45   LEU A CB  1 
ATOM   373  C CG  . LEU A 1 45  ? 9.04842   -31.06825 -18.65768 1.000 32.75000  ? 45   LEU A CG  1 
ATOM   374  C CD1 . LEU A 1 45  ? 8.26217   -29.87018 -19.15499 1.000 30.62000  ? 45   LEU A CD1 1 
ATOM   375  C CD2 . LEU A 1 45  ? 9.16915   -32.11836 -19.76104 1.000 32.55000  ? 45   LEU A CD2 1 
ATOM   376  N N   . GLU A 1 46  ? 13.80589  -30.95875 -17.81341 1.000 33.86000  ? 46   GLU A N   1 
ATOM   377  C CA  . GLU A 1 46  ? 15.00918  -30.35519 -17.24356 1.000 35.28000  ? 46   GLU A CA  1 
ATOM   378  C C   . GLU A 1 46  ? 14.76154  -28.93081 -16.74724 1.000 34.43000  ? 46   GLU A C   1 
ATOM   379  O O   . GLU A 1 46  ? 15.37560  -28.50630 -15.76147 1.000 37.70000  ? 46   GLU A O   1 
ATOM   380  C CB  . GLU A 1 46  ? 16.14637  -30.37297 -18.26742 1.000 38.44000  ? 46   GLU A CB  1 
ATOM   381  C CG  . GLU A 1 46  ? 17.53283  -30.47539 -17.63527 1.000 47.33000  ? 46   GLU A CG  1 
ATOM   382  C CD  . GLU A 1 46  ? 18.66352  -30.44061 -18.65611 1.000 48.95000  ? 46   GLU A CD  1 
ATOM   383  O OE1 . GLU A 1 46  ? 18.90771  -31.47605 -19.31604 1.000 45.48000  ? 46   GLU A OE1 1 
ATOM   384  O OE2 . GLU A 1 46  ? 19.30296  -29.37298 -18.80173 1.000 47.76000  ? 46   GLU A OE2 1 
ATOM   385  N N   . GLU A 1 47  ? 13.86536  -28.18320 -17.40181 1.000 34.10000  ? 47   GLU A N   1 
ATOM   386  C CA  . GLU A 1 47  ? 13.56430  -26.82373 -16.95703 1.000 36.29000  ? 47   GLU A CA  1 
ATOM   387  C C   . GLU A 1 47  ? 13.11349  -26.78025 -15.49878 1.000 33.92000  ? 47   GLU A C   1 
ATOM   388  O O   . GLU A 1 47  ? 13.41584  -25.81167 -14.79325 1.000 32.49000  ? 47   GLU A O   1 
ATOM   389  C CB  . GLU A 1 47  ? 12.49509  -26.19532 -17.85459 1.000 37.46000  ? 47   GLU A CB  1 
ATOM   390  C CG  . GLU A 1 47  ? 11.12656  -26.85419 -17.73663 1.000 41.38000  ? 47   GLU A CG  1 
ATOM   391  C CD  . GLU A 1 47  ? 10.13564  -26.35947 -18.77483 1.000 42.90000  ? 47   GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 47  ? 10.19260  -26.86804 -19.91706 1.000 47.20000  ? 47   GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 47  ? 9.28812   -25.49072 -18.44701 1.000 43.79000  ? 47   GLU A OE2 1 
ATOM   394  N N   . PHE A 1 48  ? 12.39180  -27.80692 -15.03012 1.000 29.95000  ? 48   PHE A N   1 
ATOM   395  C CA  . PHE A 1 48  ? 11.92678  -27.80913 -13.64494 1.000 29.25000  ? 48   PHE A CA  1 
ATOM   396  C C   . PHE A 1 48  ? 13.09443  -27.70437 -12.67849 1.000 28.96000  ? 48   PHE A C   1 
ATOM   397  O O   . PHE A 1 48  ? 13.02639  -26.96368 -11.69062 1.000 30.31000  ? 48   PHE A O   1 
ATOM   398  C CB  . PHE A 1 48  ? 11.11281  -29.06988 -13.34808 1.000 30.23000  ? 48   PHE A CB  1 
ATOM   399  C CG  . PHE A 1 48  ? 9.85442   -29.18351 -14.14796 1.000 27.93000  ? 48   PHE A CG  1 
ATOM   400  C CD1 . PHE A 1 48  ? 9.31556   -28.07553 -14.78579 1.000 29.74000  ? 48   PHE A CD1 1 
ATOM   401  C CD2 . PHE A 1 48  ? 9.21910   -30.40748 -14.28381 1.000 27.83000  ? 48   PHE A CD2 1 
ATOM   402  C CE1 . PHE A 1 48  ? 8.16049   -28.17794 -15.52750 1.000 29.26000  ? 48   PHE A CE1 1 
ATOM   403  C CE2 . PHE A 1 48  ? 8.06278   -30.51839 -15.02199 1.000 29.86000  ? 48   PHE A CE2 1 
ATOM   404  C CZ  . PHE A 1 48  ? 7.52888   -29.39947 -15.64420 1.000 29.94000  ? 48   PHE A CZ  1 
ATOM   405  N N   . GLY A 1 49  ? 14.17835  -28.43217 -12.95550 1.000 29.42000  ? 49   GLY A N   1 
ATOM   406  C CA  . GLY A 1 49  ? 15.37565  -28.38287 -12.13647 1.000 30.50000  ? 49   GLY A CA  1 
ATOM   407  C C   . GLY A 1 49  ? 16.13871  -27.08003 -12.21800 1.000 31.38000  ? 49   GLY A C   1 
ATOM   408  O O   . GLY A 1 49  ? 17.06078  -26.87057 -11.42380 1.000 34.10000  ? 49   GLY A O   1 
ATOM   409  N N   . ARG A 1 50  ? 15.78854  -26.20637 -13.15441 1.000 31.52000  ? 50   ARG A N   1 
ATOM   410  C CA  . ARG A 1 50  ? 16.38149  -24.88156 -13.15402 1.000 33.31000  ? 50   ARG A CA  1 
ATOM   411  C C   . ARG A 1 50  ? 15.64180  -23.91951 -12.23900 1.000 32.10000  ? 50   ARG A C   1 
ATOM   412  O O   . ARG A 1 50  ? 16.24162  -22.94261 -11.78531 1.000 36.69000  ? 50   ARG A O   1 
ATOM   413  C CB  . ARG A 1 50  ? 16.43518  -24.33642 -14.58175 1.000 34.27000  ? 50   ARG A CB  1 
ATOM   414  C CG  . ARG A 1 50  ? 16.75213  -25.40766 -15.61966 1.000 37.21000  ? 50   ARG A CG  1 
ATOM   415  C CD  . ARG A 1 50  ? 18.25528  -25.62844 -15.77057 1.000 39.83000  ? 50   ARG A CD  1 
ATOM   416  N NE  . ARG A 1 50  ? 18.77394  -24.70095 -16.76239 1.000 44.69000  ? 50   ARG A NE  1 
ATOM   417  C CZ  . ARG A 1 50  ? 19.20921  -25.03731 -17.96622 1.000 39.50000  ? 50   ARG A CZ  1 
ATOM   418  N NH1 . ARG A 1 50  ? 19.34927  -26.30088 -18.32970 1.000 38.91000  ? 50   ARG A NH1 1 
ATOM   419  N NH2 . ARG A 1 50  ? 19.51278  -24.07892 -18.82808 1.000 48.45000  ? 50   ARG A NH2 1 
ATOM   420  N N   . PHE A 1 51  ? 14.36959  -24.18697 -11.93907 1.000 35.47000  ? 51   PHE A N   1 
ATOM   421  C CA  . PHE A 1 51  ? 13.54561  -23.32504 -11.09315 1.000 35.67000  ? 51   PHE A CA  1 
ATOM   422  C C   . PHE A 1 51  ? 13.43892  -23.80746 -9.65486  1.000 33.89000  ? 51   PHE A C   1 
ATOM   423  O O   . PHE A 1 51  ? 13.26748  -22.98898 -8.74473  1.000 30.49000  ? 51   PHE A O   1 
ATOM   424  C CB  . PHE A 1 51  ? 12.12105  -23.21579 -11.65441 1.000 35.99000  ? 51   PHE A CB  1 
ATOM   425  C CG  . PHE A 1 51  ? 12.04936  -22.70604 -13.06839 1.000 36.65000  ? 51   PHE A CG  1 
ATOM   426  C CD1 . PHE A 1 51  ? 12.55812  -21.45948 -13.39998 1.000 42.87000  ? 51   PHE A CD1 1 
ATOM   427  C CD2 . PHE A 1 51  ? 11.44449  -23.46403 -14.06079 1.000 36.57000  ? 51   PHE A CD2 1 
ATOM   428  C CE1 . PHE A 1 51  ? 12.48046  -20.98762 -14.70482 1.000 39.26000  ? 51   PHE A CE1 1 
ATOM   429  C CE2 . PHE A 1 51  ? 11.35936  -23.00043 -15.35987 1.000 38.05000  ? 51   PHE A CE2 1 
ATOM   430  C CZ  . PHE A 1 51  ? 11.87606  -21.76032 -15.68363 1.000 39.83000  ? 51   PHE A CZ  1 
ATOM   431  N N   . ALA A 1 52  ? 13.50720  -25.11185 -9.43169  1.000 30.46000  ? 52   ALA A N   1 
ATOM   432  C CA  . ALA A 1 52  ? 13.27589  -25.68966 -8.12250  1.000 31.05000  ? 52   ALA A CA  1 
ATOM   433  C C   . ALA A 1 52  ? 14.38816  -26.67786 -7.80839  1.000 31.90000  ? 52   ALA A C   1 
ATOM   434  O O   . ALA A 1 52  ? 15.16679  -27.07520 -8.67954  1.000 33.44000  ? 52   ALA A O   1 
ATOM   435  C CB  . ALA A 1 52  ? 11.90413  -26.37643 -8.05251  1.000 31.30000  ? 52   ALA A CB  1 
ATOM   436  N N   . SER A 1 53  ? 14.45458  -27.07156 -6.54188  1.000 32.73000  ? 53   SER A N   1 
ATOM   437  C CA  . SER A 1 53  ? 15.43360  -28.03950 -6.08430  1.000 35.19000  ? 53   SER A CA  1 
ATOM   438  C C   . SER A 1 53  ? 14.75894  -28.99953 -5.11536  1.000 35.35000  ? 53   SER A C   1 
ATOM   439  O O   . SER A 1 53  ? 13.66496  -28.74043 -4.61176  1.000 32.47000  ? 53   SER A O   1 
ATOM   440  C CB  . SER A 1 53  ? 16.63862  -27.34683 -5.43081  1.000 36.07000  ? 53   SER A CB  1 
ATOM   441  O OG  . SER A 1 53  ? 16.23771  -26.59303 -4.29894  1.000 42.81000  ? 53   SER A OG  1 
ATOM   442  N N   . PHE A 1 54  ? 15.41841  -30.12870 -4.87730  1.000 33.44000  ? 54   PHE A N   1 
ATOM   443  C CA  . PHE A 1 54  ? 14.90074  -31.14216 -3.97299  1.000 33.42000  ? 54   PHE A CA  1 
ATOM   444  C C   . PHE A 1 54  ? 16.06339  -31.99667 -3.49214  1.000 35.09000  ? 54   PHE A C   1 
ATOM   445  O O   . PHE A 1 54  ? 16.90573  -32.40754 -4.29352  1.000 34.76000  ? 54   PHE A O   1 
ATOM   446  C CB  . PHE A 1 54  ? 13.84341  -32.02119 -4.65125  1.000 34.16000  ? 54   PHE A CB  1 
ATOM   447  C CG  . PHE A 1 54  ? 13.34181  -33.13281 -3.77718  1.000 34.06000  ? 54   PHE A CG  1 
ATOM   448  C CD1 . PHE A 1 54  ? 12.46445  -32.86830 -2.73857  1.000 32.17000  ? 54   PHE A CD1 1 
ATOM   449  C CD2 . PHE A 1 54  ? 13.76305  -34.43737 -3.98023  1.000 33.84000  ? 54   PHE A CD2 1 
ATOM   450  C CE1 . PHE A 1 54  ? 12.00393  -33.88553 -1.92139  1.000 32.50000  ? 54   PHE A CE1 1 
ATOM   451  C CE2 . PHE A 1 54  ? 13.30860  -35.46326 -3.16798  1.000 31.75000  ? 54   PHE A CE2 1 
ATOM   452  C CZ  . PHE A 1 54  ? 12.42902  -35.18525 -2.13681  1.000 32.89000  ? 54   PHE A CZ  1 
ATOM   453  N N   . GLU A 1 55  ? 16.10213  -32.25775 -2.18657  1.000 36.23000  ? 55   GLU A N   1 
ATOM   454  C CA  . GLU A 1 55  ? 17.14286  -33.08606 -1.58627  1.000 37.76000  ? 55   GLU A CA  1 
ATOM   455  C C   . GLU A 1 55  ? 16.69415  -34.54181 -1.65604  1.000 32.48000  ? 55   GLU A C   1 
ATOM   456  O O   . GLU A 1 55  ? 15.72430  -34.93100 -0.99979  1.000 37.20000  ? 55   GLU A O   1 
ATOM   457  C CB  . GLU A 1 55  ? 17.41270  -32.65463 -0.14735  1.000 43.08000  ? 55   GLU A CB  1 
ATOM   458  N N   . ALA A 1 56  ? 17.40050  -35.34555 -2.45476  1.000 32.65000  ? 56   ALA A N   1 
ATOM   459  C CA  . ALA A 1 56  ? 16.98573  -36.72696 -2.68472  1.000 34.10000  ? 56   ALA A CA  1 
ATOM   460  C C   . ALA A 1 56  ? 17.08724  -37.57650 -1.42218  1.000 35.14000  ? 56   ALA A C   1 
ATOM   461  O O   . ALA A 1 56  ? 16.37090  -38.57648 -1.29303  1.000 35.97000  ? 56   ALA A O   1 
ATOM   462  C CB  . ALA A 1 56  ? 17.82646  -37.34126 -3.80863  1.000 31.99000  ? 56   ALA A CB  1 
ATOM   463  N N   . GLN A 1 57  ? 17.95470  -37.18810 -0.48316  1.000 38.51000  ? 57   GLN A N   1 
ATOM   464  C CA  . GLN A 1 57  ? 18.22496  -38.01092 0.69470   1.000 39.46000  ? 57   GLN A CA  1 
ATOM   465  C C   . GLN A 1 57  ? 16.95213  -38.31126 1.48470   1.000 32.41000  ? 57   GLN A C   1 
ATOM   466  O O   . GLN A 1 57  ? 16.72182  -39.45353 1.90278   1.000 33.88000  ? 57   GLN A O   1 
ATOM   467  C CB  . GLN A 1 57  ? 19.25460  -37.30854 1.57481   1.000 41.06000  ? 57   GLN A CB  1 
ATOM   468  C CG  . GLN A 1 57  ? 19.59809  -38.04228 2.84179   1.000 48.29000  ? 57   GLN A CG  1 
ATOM   469  C CD  . GLN A 1 57  ? 20.84777  -37.49127 3.49297   1.000 49.73000  ? 57   GLN A CD  1 
ATOM   470  O OE1 . GLN A 1 57  ? 21.94155  -37.57380 2.93174   1.000 50.71000  ? 57   GLN A OE1 1 
ATOM   471  N NE2 . GLN A 1 57  ? 20.68949  -36.90558 4.67548   1.000 48.36000  ? 57   GLN A NE2 1 
ATOM   472  N N   . GLY A 1 58  ? 16.11362  -37.29639 1.70609   1.000 32.03000  ? 58   GLY A N   1 
ATOM   473  C CA  . GLY A 1 58  ? 14.86714  -37.52850 2.42147   1.000 30.86000  ? 58   GLY A CA  1 
ATOM   474  C C   . GLY A 1 58  ? 13.95629  -38.51001 1.70805   1.000 29.37000  ? 58   GLY A C   1 
ATOM   475  O O   . GLY A 1 58  ? 13.30795  -39.35017 2.34290   1.000 32.72000  ? 58   GLY A O   1 
ATOM   476  N N   . ALA A 1 59  ? 13.90097  -38.42655 0.37747   1.000 29.01000  ? 59   ALA A N   1 
ATOM   477  C CA  . ALA A 1 59  ? 13.07047  -39.35670 -0.38090  1.000 28.46000  ? 59   ALA A CA  1 
ATOM   478  C C   . ALA A 1 59  ? 13.52163  -40.79447 -0.16841  1.000 27.58000  ? 59   ALA A C   1 
ATOM   479  O O   . ALA A 1 59  ? 12.69262  -41.69363 0.01678   1.000 28.59000  ? 59   ALA A O   1 
ATOM   480  C CB  . ALA A 1 59  ? 13.10332  -39.00164 -1.86664  1.000 27.80000  ? 59   ALA A CB  1 
ATOM   481  N N   . LEU A 1 60  ? 14.83667  -41.02910 -0.19173  1.000 31.66000  ? 60   LEU A N   1 
ATOM   482  C CA  . LEU A 1 60  ? 15.35212  -42.38230 -0.01612  1.000 31.76000  ? 60   LEU A CA  1 
ATOM   483  C C   . LEU A 1 60  ? 15.03560  -42.91699 1.37651   1.000 27.89000  ? 60   LEU A C   1 
ATOM   484  O O   . LEU A 1 60  ? 14.74854  -44.10834 1.54057   1.000 27.92000  ? 60   LEU A O   1 
ATOM   485  C CB  . LEU A 1 60  ? 16.85753  -42.39436 -0.28517  1.000 32.29000  ? 60   LEU A CB  1 
ATOM   486  C CG  . LEU A 1 60  ? 17.20387  -41.91614 -1.69878  1.000 34.59000  ? 60   LEU A CG  1 
ATOM   487  C CD1 . LEU A 1 60  ? 18.65766  -41.48187 -1.81639  1.000 36.23000  ? 60   LEU A CD1 1 
ATOM   488  C CD2 . LEU A 1 60  ? 16.88668  -43.00022 -2.70961  1.000 35.72000  ? 60   LEU A CD2 1 
ATOM   489  N N   . ALA A 1 61  ? 15.07395  -42.04528 2.39066   1.000 27.83000  ? 61   ALA A N   1 
ATOM   490  C CA  . ALA A 1 61  ? 14.68745  -42.45106 3.73878   1.000 29.37000  ? 61   ALA A CA  1 
ATOM   491  C C   . ALA A 1 61  ? 13.22324  -42.86166 3.78343   1.000 28.59000  ? 61   ALA A C   1 
ATOM   492  O O   . ALA A 1 61  ? 12.87826  -43.87792 4.39837   1.000 29.06000  ? 61   ALA A O   1 
ATOM   493  C CB  . ALA A 1 61  ? 14.96265  -41.32136 4.73014   1.000 29.64000  ? 61   ALA A CB  1 
ATOM   494  N N   . ASN A 1 62  ? 12.35004  -42.08723 3.12517   1.000 28.85000  ? 62   ASN A N   1 
ATOM   495  C CA  . ASN A 1 62  ? 10.94879  -42.47607 2.98093   1.000 28.32000  ? 62   ASN A CA  1 
ATOM   496  C C   . ASN A 1 62  ? 10.83067  -43.87902 2.39271   1.000 29.79000  ? 62   ASN A C   1 
ATOM   497  O O   . ASN A 1 62  ? 10.07541  -44.72006 2.89826   1.000 28.39000  ? 62   ASN A O   1 
ATOM   498  C CB  . ASN A 1 62  ? 10.21194  -41.47181 2.09017   1.000 27.92000  ? 62   ASN A CB  1 
ATOM   499  C CG  . ASN A 1 62  ? 9.48062   -40.39927 2.88035   1.000 28.92000  ? 62   ASN A CG  1 
ATOM   500  O OD1 . ASN A 1 62  ? 9.91458   -39.99939 3.95020   1.000 32.00000  ? 62   ASN A OD1 1 
ATOM   501  N ND2 . ASN A 1 62  ? 8.36505   -39.92626 2.34642   1.000 29.72000  ? 62   ASN A ND2 1 
ATOM   502  N N   . ILE A 1 63  ? 11.58407  -44.15128 1.32158   1.000 30.88000  ? 63   ILE A N   1 
ATOM   503  C CA  . ILE A 1 63  ? 11.50655  -45.45814 0.67051   1.000 32.70000  ? 63   ILE A CA  1 
ATOM   504  C C   . ILE A 1 63  ? 11.89047  -46.56578 1.64349   1.000 30.15000  ? 63   ILE A C   1 
ATOM   505  O O   . ILE A 1 63  ? 11.26178  -47.63015 1.67335   1.000 30.00000  ? 63   ILE A O   1 
ATOM   506  C CB  . ILE A 1 63  ? 12.38846  -45.48576 -0.59325  1.000 35.76000  ? 63   ILE A CB  1 
ATOM   507  C CG1 . ILE A 1 63  ? 11.88346  -44.47975 -1.63058  1.000 36.21000  ? 63   ILE A CG1 1 
ATOM   508  C CG2 . ILE A 1 63  ? 12.42666  -46.88780 -1.19148  1.000 36.85000  ? 63   ILE A CG2 1 
ATOM   509  C CD1 . ILE A 1 63  ? 10.37596  -44.37480 -1.70422  1.000 37.94000  ? 63   ILE A CD1 1 
ATOM   510  N N   . ALA A 1 64  ? 12.91129  -46.32801 2.46910   1.000 30.80000  ? 64   ALA A N   1 
ATOM   511  C CA  . ALA A 1 64  ? 13.32301  -47.33733 3.44142   1.000 31.02000  ? 64   ALA A CA  1 
ATOM   512  C C   . ALA A 1 64  ? 12.23540  -47.58233 4.48575   1.000 31.98000  ? 64   ALA A C   1 
ATOM   513  O O   . ALA A 1 64  ? 12.00665  -48.72618 4.89686   1.000 36.08000  ? 64   ALA A O   1 
ATOM   514  C CB  . ALA A 1 64  ? 14.63374  -46.91040 4.10380   1.000 29.23000  ? 64   ALA A CB  1 
ATOM   515  N N   . VAL A 1 65  ? 11.55693  -46.51843 4.92399   1.000 33.05000  ? 65   VAL A N   1 
ATOM   516  C CA  . VAL A 1 65  ? 10.41619  -46.66336 5.82611   1.000 34.08000  ? 65   VAL A CA  1 
ATOM   517  C C   . VAL A 1 65  ? 9.29553   -47.44484 5.14942   1.000 34.49000  ? 65   VAL A C   1 
ATOM   518  O O   . VAL A 1 65  ? 8.67724   -48.32693 5.75891   1.000 36.12000  ? 65   VAL A O   1 
ATOM   519  C CB  . VAL A 1 65  ? 9.93033   -45.27756 6.29576   1.000 33.61000  ? 65   VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 65  ? 8.55459   -45.37736 6.92961   1.000 33.39000  ? 65   VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 65  ? 10.92576  -44.65841 7.25419   1.000 31.84000  ? 65   VAL A CG2 1 
ATOM   522  N N   . ASP A 1 66  ? 9.01082   -47.13072 3.88142   1.000 35.21000  ? 66   ASP A N   1 
ATOM   523  C CA  . ASP A 1 66  ? 7.99959   -47.88653 3.14715   1.000 37.01000  ? 66   ASP A CA  1 
ATOM   524  C C   . ASP A 1 66  ? 8.37884   -49.35256 3.01883   1.000 37.45000  ? 66   ASP A C   1 
ATOM   525  O O   . ASP A 1 66  ? 7.49637   -50.21792 2.99825   1.000 37.75000  ? 66   ASP A O   1 
ATOM   526  C CB  . ASP A 1 66  ? 7.78454   -47.29895 1.75474   1.000 37.44000  ? 66   ASP A CB  1 
ATOM   527  C CG  . ASP A 1 66  ? 7.48751   -45.82446 1.78521   1.000 39.45000  ? 66   ASP A CG  1 
ATOM   528  O OD1 . ASP A 1 66  ? 6.83509   -45.36627 2.75082   1.000 40.20000  ? 66   ASP A OD1 1 
ATOM   529  O OD2 . ASP A 1 66  ? 7.90639   -45.12814 0.83353   1.000 34.44000  ? 66   ASP A OD2 1 
ATOM   530  N N   . LYS A 1 67  ? 9.67593   -49.65021 2.90370   1.000 38.36000  ? 67   LYS A N   1 
ATOM   531  C CA  . LYS A 1 67  ? 10.11105  -51.04278 2.88852   1.000 37.77000  ? 67   LYS A CA  1 
ATOM   532  C C   . LYS A 1 67  ? 9.85219   -51.70563 4.23158   1.000 35.33000  ? 67   LYS A C   1 
ATOM   533  O O   . LYS A 1 67  ? 9.31265   -52.81566 4.29326   1.000 31.04000  ? 67   LYS A O   1 
ATOM   534  C CB  . LYS A 1 67  ? 11.59326  -51.14166 2.52712   1.000 37.30000  ? 67   LYS A CB  1 
ATOM   535  C CG  . LYS A 1 67  ? 12.09745  -52.57869 2.43438   1.000 38.26000  ? 67   LYS A CG  1 
ATOM   536  C CD  . LYS A 1 67  ? 13.60117  -52.64999 2.26182   1.000 43.01000  ? 67   LYS A CD  1 
ATOM   537  C CE  . LYS A 1 67  ? 14.03358  -54.06199 1.88813   1.000 45.94000  ? 67   LYS A CE  1 
ATOM   538  N NZ  . LYS A 1 67  ? 14.28112  -54.91621 3.08169   1.000 48.19000  ? 67   LYS A NZ  1 
ATOM   539  N N   . ALA A 1 68  ? 10.23707  -51.03897 5.31980   1.000 35.09000  ? 68   ALA A N   1 
ATOM   540  C CA  . ALA A 1 68  ? 9.97947   -51.58878 6.64544   1.000 36.21000  ? 68   ALA A CA  1 
ATOM   541  C C   . ALA A 1 68  ? 8.48418   -51.77368 6.87221   1.000 34.83000  ? 68   ALA A C   1 
ATOM   542  O O   . ALA A 1 68  ? 8.03132   -52.85547 7.26660   1.000 35.00000  ? 68   ALA A O   1 
ATOM   543  C CB  . ALA A 1 68  ? 10.58970  -50.68410 7.71748   1.000 33.75000  ? 68   ALA A CB  1 
ATOM   544  N N   . ASN A 1 69  ? 7.69821   -50.72844 6.60468   1.000 34.60000  ? 69   ASN A N   1 
ATOM   545  C CA  . ASN A 1 69  ? 6.24947   -50.83610 6.74711   1.000 36.87000  ? 69   ASN A CA  1 
ATOM   546  C C   . ASN A 1 69  ? 5.69189   -51.96875 5.89739   1.000 36.54000  ? 69   ASN A C   1 
ATOM   547  O O   . ASN A 1 69  ? 4.75756   -52.66325 6.31408   1.000 41.48000  ? 69   ASN A O   1 
ATOM   548  C CB  . ASN A 1 69  ? 5.58412   -49.51154 6.37503   1.000 34.45000  ? 69   ASN A CB  1 
ATOM   549  C CG  . ASN A 1 69  ? 5.64662   -48.50705 7.49707   1.000 36.88000  ? 69   ASN A CG  1 
ATOM   550  O OD1 . ASN A 1 69  ? 6.06248   -48.83766 8.60996   1.000 35.89000  ? 69   ASN A OD1 1 
ATOM   551  N ND2 . ASN A 1 69  ? 5.23640   -47.27267 7.22051   1.000 37.26000  ? 69   ASN A ND2 1 
ATOM   552  N N   . LEU A 1 70  ? 6.25946   -52.17780 4.70799   1.000 36.93000  ? 70   LEU A N   1 
ATOM   553  C CA  . LEU A 1 70  ? 5.75237   -53.21739 3.81868   1.000 37.57000  ? 70   LEU A CA  1 
ATOM   554  C C   . LEU A 1 70  ? 5.91925   -54.59784 4.43890   1.000 38.64000  ? 70   LEU A C   1 
ATOM   555  O O   . LEU A 1 70  ? 5.00482   -55.42891 4.39071   1.000 36.85000  ? 70   LEU A O   1 
ATOM   556  C CB  . LEU A 1 70  ? 6.46250   -53.14542 2.46698   1.000 34.81000  ? 70   LEU A CB  1 
ATOM   557  C CG  . LEU A 1 70  ? 6.26107   -54.33866 1.53427   1.000 33.86000  ? 70   LEU A CG  1 
ATOM   558  C CD1 . LEU A 1 70  ? 4.78243   -54.54130 1.21721   1.000 36.78000  ? 70   LEU A CD1 1 
ATOM   559  C CD2 . LEU A 1 70  ? 7.06686   -54.14554 0.26244   1.000 34.44000  ? 70   LEU A CD2 1 
ATOM   560  N N   . GLU A 1 71  ? 7.08470   -54.86147 5.03013   1.000 41.59000  ? 71   GLU A N   1 
ATOM   561  C CA  . GLU A 1 71  ? 7.31982   -56.17739 5.61091   1.000 46.71000  ? 71   GLU A CA  1 
ATOM   562  C C   . GLU A 1 71  ? 6.34196   -56.45127 6.74791   1.000 40.58000  ? 71   GLU A C   1 
ATOM   563  O O   . GLU A 1 71  ? 5.87807   -57.58455 6.92298   1.000 38.84000  ? 71   GLU A O   1 
ATOM   564  C CB  . GLU A 1 71  ? 8.77298   -56.28556 6.07751   1.000 50.19000  ? 71   GLU A CB  1 
ATOM   565  C CG  . GLU A 1 71  ? 9.67619   -56.98533 5.06035   1.000 58.56000  ? 71   GLU A CG  1 
ATOM   566  C CD  . GLU A 1 71  ? 11.01288  -56.28540 4.86143   1.000 64.00000  ? 71   GLU A CD  1 
ATOM   567  O OE1 . GLU A 1 71  ? 11.46464  -56.18307 3.69764   1.000 67.54000  ? 71   GLU A OE1 1 
ATOM   568  O OE2 . GLU A 1 71  ? 11.61854  -55.85035 5.86761   1.000 58.77000  ? 71   GLU A OE2 1 
ATOM   569  N N   . ILE A 1 72  ? 5.98646   -55.41463 7.50544   1.000 37.59000  ? 72   ILE A N   1 
ATOM   570  C CA  . ILE A 1 72  ? 4.99201   -55.56684 8.56088   1.000 41.62000  ? 72   ILE A CA  1 
ATOM   571  C C   . ILE A 1 72  ? 3.59890   -55.76594 7.97033   1.000 42.60000  ? 72   ILE A C   1 
ATOM   572  O O   . ILE A 1 72  ? 2.84969   -56.64986 8.40453   1.000 43.11000  ? 72   ILE A O   1 
ATOM   573  C CB  . ILE A 1 72  ? 5.05704   -54.35738 9.50856   1.000 42.69000  ? 72   ILE A CB  1 
ATOM   574  C CG1 . ILE A 1 72  ? 6.34965   -54.43251 10.32538  1.000 42.66000  ? 72   ILE A CG1 1 
ATOM   575  C CG2 . ILE A 1 72  ? 3.82414   -54.29955 10.39402  1.000 40.38000  ? 72   ILE A CG2 1 
ATOM   576  C CD1 . ILE A 1 72  ? 6.65393   -53.21266 11.13692  1.000 47.99000  ? 72   ILE A CD1 1 
ATOM   577  N N   . MET A 1 73  ? 3.23419   -54.96661 6.96052   1.000 42.20000  ? 73   MET A N   1 
ATOM   578  C CA  . MET A 1 73  ? 1.93391   -55.13477 6.31389   1.000 42.45000  ? 73   MET A CA  1 
ATOM   579  C C   . MET A 1 73  ? 1.79971   -56.52036 5.69893   1.000 41.36000  ? 73   MET A C   1 
ATOM   580  O O   . MET A 1 73  ? 0.69400   -57.06771 5.62746   1.000 43.52000  ? 73   MET A O   1 
ATOM   581  C CB  . MET A 1 73  ? 1.73745   -54.06579 5.23493   1.000 45.33000  ? 73   MET A CB  1 
ATOM   582  C CG  . MET A 1 73  ? 1.28015   -52.67531 5.70933   1.000 46.19000  ? 73   MET A CG  1 
ATOM   583  S SD  . MET A 1 73  ? 0.52616   -52.55011 7.34631   1.000 45.38000  ? 73   MET A SD  1 
ATOM   584  C CE  . MET A 1 73  ? -1.13947  -53.06785 6.95448   1.000 46.87000  ? 73   MET A CE  1 
ATOM   585  N N   . THR A 1 74  ? 2.91566   -57.09668 5.25259   1.000 39.72000  ? 74   THR A N   1 
ATOM   586  C CA  . THR A 1 74  ? 2.89739   -58.41094 4.61972   1.000 42.98000  ? 74   THR A CA  1 
ATOM   587  C C   . THR A 1 74  ? 2.57153   -59.51072 5.62643   1.000 44.13000  ? 74   THR A C   1 
ATOM   588  O O   . THR A 1 74  ? 1.72713   -60.37553 5.36476   1.000 40.69000  ? 74   THR A O   1 
ATOM   589  C CB  . THR A 1 74  ? 4.24862   -58.67150 3.95038   1.000 40.78000  ? 74   THR A CB  1 
ATOM   590  O OG1 . THR A 1 74  ? 4.41475   -57.76849 2.85269   1.000 44.38000  ? 74   THR A OG1 1 
ATOM   591  C CG2 . THR A 1 74  ? 4.33704   -60.09655 3.44751   1.000 40.04000  ? 74   THR A CG2 1 
ATOM   592  N N   . LYS A 1 75  ? 3.25202   -59.50828 6.77535   1.000 51.40000  ? 75   LYS A N   1 
ATOM   593  C CA  . LYS A 1 75  ? 2.91995   -60.45632 7.83468   1.000 52.82000  ? 75   LYS A CA  1 
ATOM   594  C C   . LYS A 1 75  ? 1.49950   -60.22977 8.33010   1.000 48.88000  ? 75   LYS A C   1 
ATOM   595  O O   . LYS A 1 75  ? 0.72036   -61.17902 8.47535   1.000 50.19000  ? 75   LYS A O   1 
ATOM   596  C CB  . LYS A 1 75  ? 3.91163   -60.32700 8.99243   1.000 53.48000  ? 75   LYS A CB  1 
ATOM   597  C CG  . LYS A 1 75  ? 5.25320   -60.99117 8.75924   1.000 59.13000  ? 75   LYS A CG  1 
ATOM   598  C CD  . LYS A 1 75  ? 6.37857   -60.15693 9.35221   1.000 67.63000  ? 75   LYS A CD  1 
ATOM   599  C CE  . LYS A 1 75  ? 7.74649   -60.67852 8.93832   1.000 73.33000  ? 75   LYS A CE  1 
ATOM   600  N NZ  . LYS A 1 75  ? 8.75823   -60.46999 10.01417  1.000 75.74000  ? 75   LYS A NZ  1 
ATOM   601  N N   . ARG A 1 76  ? 1.14581   -58.96500 8.58466   1.000 44.67000  ? 76   ARG A N   1 
ATOM   602  C CA  . ARG A 1 76  ? -0.18100  -58.63437 9.09392   1.000 48.11000  ? 76   ARG A CA  1 
ATOM   603  C C   . ARG A 1 76  ? -1.28978  -59.20129 8.21727   1.000 43.85000  ? 76   ARG A C   1 
ATOM   604  O O   . ARG A 1 76  ? -2.34757  -59.58881 8.72617   1.000 51.27000  ? 76   ARG A O   1 
ATOM   605  C CB  . ARG A 1 76  ? -0.33104  -57.11649 9.21465   1.000 49.24000  ? 76   ARG A CB  1 
ATOM   606  C CG  . ARG A 1 76  ? -1.22079  -56.68120 10.36167  1.000 50.36000  ? 76   ARG A CG  1 
ATOM   607  C CD  . ARG A 1 76  ? -1.60724  -55.21136 10.24664  1.000 51.20000  ? 76   ARG A CD  1 
ATOM   608  N NE  . ARG A 1 76  ? -0.56704  -54.31936 10.74291  1.000 51.81000  ? 76   ARG A NE  1 
ATOM   609  C CZ  . ARG A 1 76  ? -0.65987  -52.99667 10.75028  1.000 52.71000  ? 76   ARG A CZ  1 
ATOM   610  N NH1 . ARG A 1 76  ? -1.72495  -52.37659 10.26452  1.000 55.32000  ? 76   ARG A NH1 1 
ATOM   611  N NH2 . ARG A 1 76  ? 0.33905   -52.27801 11.26033  1.000 52.40000  ? 76   ARG A NH2 1 
ATOM   612  N N   . SER A 1 77  ? -1.06859  -59.26844 6.90781   1.000 44.10000  ? 77   SER A N   1 
ATOM   613  C CA  . SER A 1 77  ? -2.05585  -59.80059 5.98177   1.000 45.24000  ? 77   SER A CA  1 
ATOM   614  C C   . SER A 1 77  ? -1.95610  -61.30991 5.82125   1.000 45.42000  ? 77   SER A C   1 
ATOM   615  O O   . SER A 1 77  ? -2.55782  -61.85763 4.89293   1.000 41.18000  ? 77   SER A O   1 
ATOM   616  C CB  . SER A 1 77  ? -1.90719  -59.13399 4.61078   1.000 43.18000  ? 77   SER A CB  1 
ATOM   617  O OG  . SER A 1 77  ? -0.72037  -59.56822 3.96354   1.000 45.81000  ? 77   SER A OG  1 
ATOM   618  N N   . ASN A 1 78  ? -1.21016  -61.98806 6.69467   1.000 50.31000  ? 78   ASN A N   1 
ATOM   619  C CA  . ASN A 1 78  ? -0.91447  -63.41218 6.53339   1.000 52.92000  ? 78   ASN A CA  1 
ATOM   620  C C   . ASN A 1 78  ? -0.34566  -63.68556 5.14117   1.000 47.96000  ? 78   ASN A C   1 
ATOM   621  O O   . ASN A 1 78  ? -0.74368  -64.62948 4.45377   1.000 44.18000  ? 78   ASN A O   1 
ATOM   622  C CB  . ASN A 1 78  ? -2.14929  -64.28155 6.80802   1.000 51.90000  ? 78   ASN A CB  1 
ATOM   623  C CG  . ASN A 1 78  ? -2.64031  -64.18058 8.25048   1.000 55.17000  ? 78   ASN A CG  1 
ATOM   624  O OD1 . ASN A 1 78  ? -1.84642  -64.09195 9.18945   1.000 61.04000  ? 78   ASN A OD1 1 
ATOM   625  N ND2 . ASN A 1 78  ? -3.96119  -64.21171 8.42790   1.000 57.64000  ? 78   ASN A ND2 1 
ATOM   626  N N   . TYR A 1 79  ? 0.57539   -62.81982 4.71307   1.000 43.19000  ? 79   TYR A N   1 
ATOM   627  C CA  . TYR A 1 79  ? 1.32194   -62.99764 3.46861   1.000 43.37000  ? 79   TYR A CA  1 
ATOM   628  C C   . TYR A 1 79  ? 0.39919   -63.03830 2.25066   1.000 45.59000  ? 79   TYR A C   1 
ATOM   629  O O   . TYR A 1 79  ? 0.58327   -63.84657 1.33795   1.000 44.52000  ? 79   TYR A O   1 
ATOM   630  C CB  . TYR A 1 79  ? 2.20814   -64.24680 3.53489   1.000 46.56000  ? 79   TYR A CB  1 
ATOM   631  C CG  . TYR A 1 79  ? 3.34865   -64.10439 4.52081   1.000 51.19000  ? 79   TYR A CG  1 
ATOM   632  C CD1 . TYR A 1 79  ? 4.52789   -63.46286 4.16098   1.000 53.80000  ? 79   TYR A CD1 1 
ATOM   633  C CD2 . TYR A 1 79  ? 3.23677   -64.58696 5.81907   1.000 51.85000  ? 79   TYR A CD2 1 
ATOM   634  C CE1 . TYR A 1 79  ? 5.56732   -63.31363 5.06364   1.000 57.78000  ? 79   TYR A CE1 1 
ATOM   635  C CE2 . TYR A 1 79  ? 4.27169   -64.44421 6.72846   1.000 56.47000  ? 79   TYR A CE2 1 
ATOM   636  C CZ  . TYR A 1 79  ? 5.43332   -63.80722 6.34580   1.000 56.27000  ? 79   TYR A CZ  1 
ATOM   637  O OH  . TYR A 1 79  ? 6.46483   -63.66661 7.24698   1.000 62.42000  ? 79   TYR A OH  1 
ATOM   638  N N   . THR A 1 80  ? -0.58665  -62.14372 2.22282   1.000 46.23000  ? 80   THR A N   1 
ATOM   639  C CA  . THR A 1 80  ? -1.47787  -62.03748 1.06865   1.000 46.68000  ? 80   THR A CA  1 
ATOM   640  C C   . THR A 1 80  ? -0.80158  -61.25360 -0.05121  1.000 47.18000  ? 80   THR A C   1 
ATOM   641  O O   . THR A 1 80  ? -0.45239  -60.08320 0.14897   1.000 49.31000  ? 80   THR A O   1 
ATOM   642  C CB  . THR A 1 80  ? -2.78763  -61.35944 1.44969   1.000 46.19000  ? 80   THR A CB  1 
ATOM   643  O OG1 . THR A 1 80  ? -3.36620  -62.02992 2.57750   1.000 46.85000  ? 80   THR A OG1 1 
ATOM   644  C CG2 . THR A 1 80  ? -3.76361  -61.39705 0.27721   1.000 46.19000  ? 80   THR A CG2 1 
ATOM   645  N N   . PRO A 1 81  ? -0.61796  -61.83853 -1.23022  1.000 44.75000  ? 81   PRO A N   1 
ATOM   646  C CA  . PRO A 1 81  ? 0.09241   -61.15553 -2.31150  1.000 43.02000  ? 81   PRO A CA  1 
ATOM   647  C C   . PRO A 1 81  ? -0.83403  -60.29274 -3.16205  1.000 45.50000  ? 81   PRO A C   1 
ATOM   648  O O   . PRO A 1 81  ? -2.05821  -60.30482 -3.01675  1.000 48.25000  ? 81   PRO A O   1 
ATOM   649  C CB  . PRO A 1 81  ? 0.65790   -62.31844 -3.13527  1.000 44.62000  ? 81   PRO A CB  1 
ATOM   650  C CG  . PRO A 1 81  ? -0.35678  -63.40878 -2.96173  1.000 44.06000  ? 81   PRO A CG  1 
ATOM   651  C CD  . PRO A 1 81  ? -0.99938  -63.21368 -1.59844  1.000 44.27000  ? 81   PRO A CD  1 
ATOM   652  N N   . ILE A 1 82  ? -0.21038  -59.53713 -4.06157  1.000 43.28000  ? 82   ILE A N   1 
ATOM   653  C CA  . ILE A 1 82  ? -0.92395  -58.63884 -4.96046  1.000 41.77000  ? 82   ILE A CA  1 
ATOM   654  C C   . ILE A 1 82  ? -1.50571  -59.43787 -6.12047  1.000 39.39000  ? 82   ILE A C   1 
ATOM   655  O O   . ILE A 1 82  ? -0.88014  -60.37470 -6.63468  1.000 38.07000  ? 82   ILE A O   1 
ATOM   656  C CB  . ILE A 1 82  ? 0.02024   -57.52594 -5.45896  1.000 39.52000  ? 82   ILE A CB  1 
ATOM   657  C CG1 . ILE A 1 82  ? -0.73035  -56.50070 -6.31350  1.000 39.76000  ? 82   ILE A CG1 1 
ATOM   658  C CG2 . ILE A 1 82  ? 1.18341   -58.11292 -6.24526  1.000 38.63000  ? 82   ILE A CG2 1 
ATOM   659  C CD1 . ILE A 1 82  ? -0.04756  -55.14609 -6.36731  1.000 41.62000  ? 82   ILE A CD1 1 
ATOM   660  N N   . THR A 1 83  ? -2.71589  -59.07464 -6.53221  1.000 37.68000  ? 83   THR A N   1 
ATOM   661  C CA  . THR A 1 83  ? -3.31100  -59.63708 -7.73691  1.000 36.18000  ? 83   THR A CA  1 
ATOM   662  C C   . THR A 1 83  ? -2.70340  -58.97621 -8.96441  1.000 35.92000  ? 83   THR A C   1 
ATOM   663  O O   . THR A 1 83  ? -2.69125  -57.74748 -9.07132  1.000 37.90000  ? 83   THR A O   1 
ATOM   664  C CB  . THR A 1 83  ? -4.82403  -59.41921 -7.74142  1.000 36.90000  ? 83   THR A CB  1 
ATOM   665  O OG1 . THR A 1 83  ? -5.36322  -59.73333 -6.44884  1.000 37.58000  ? 83   THR A OG1 1 
ATOM   666  C CG2 . THR A 1 83  ? -5.48924  -60.27598 -8.81367  1.000 36.19000  ? 83   THR A CG2 1 
ATOM   667  N N   . ASN A 1 84  ? -2.20318  -59.78620 -9.89061  1.000 36.90000  ? 84   ASN A N   1 
ATOM   668  C CA  . ASN A 1 84  ? -1.76195  -59.25138 -11.17069 1.000 39.61000  ? 84   ASN A CA  1 
ATOM   669  C C   . ASN A 1 84  ? -2.93347  -58.60841 -11.90402 1.000 44.55000  ? 84   ASN A C   1 
ATOM   670  O O   . ASN A 1 84  ? -4.00164  -59.20860 -12.03856 1.000 45.49000  ? 84   ASN A O   1 
ATOM   671  C CB  . ASN A 1 84  ? -1.15573  -60.36033 -12.02658 1.000 38.16000  ? 84   ASN A CB  1 
ATOM   672  C CG  . ASN A 1 84  ? 0.17018   -60.85282 -11.48973 1.000 39.51000  ? 84   ASN A CG  1 
ATOM   673  O OD1 . ASN A 1 84  ? 0.98250   -60.06905 -11.00407 1.000 37.67000  ? 84   ASN A OD1 1 
ATOM   674  N ND2 . ASN A 1 84  ? 0.39803   -62.16102 -11.57768 1.000 39.37000  ? 84   ASN A ND2 1 
ATOM   675  N N   . VAL A 1 85  ? -2.73738  -57.38093 -12.36979 1.000 43.19000  ? 85   VAL A N   1 
ATOM   676  C CA  . VAL A 1 85  ? -3.72896  -56.71415 -13.21028 1.000 41.44000  ? 85   VAL A CA  1 
ATOM   677  C C   . VAL A 1 85  ? -3.05442  -56.34119 -14.52599 1.000 41.59000  ? 85   VAL A C   1 
ATOM   678  O O   . VAL A 1 85  ? -2.18662  -55.45807 -14.54502 1.000 40.40000  ? 85   VAL A O   1 
ATOM   679  C CB  . VAL A 1 85  ? -4.32902  -55.48022 -12.51420 1.000 39.94000  ? 85   VAL A CB  1 
ATOM   680  C CG1 . VAL A 1 85  ? -5.24459  -54.72819 -13.46836 1.000 36.69000  ? 85   VAL A CG1 1 
ATOM   681  C CG2 . VAL A 1 85  ? -5.08249  -55.88518 -11.24955 1.000 36.36000  ? 85   VAL A CG2 1 
ATOM   682  N N   . PRO A 1 86  ? -3.41883  -56.97924 -15.64164 1.000 42.06000  ? 86   PRO A N   1 
ATOM   683  C CA  . PRO A 1 86  ? -2.68016  -56.75215 -16.88463 1.000 39.77000  ? 86   PRO A CA  1 
ATOM   684  C C   . PRO A 1 86  ? -2.89345  -55.35027 -17.40832 1.000 38.86000  ? 86   PRO A C   1 
ATOM   685  O O   . PRO A 1 86  ? -3.94736  -54.72711 -17.17279 1.000 38.51000  ? 86   PRO A O   1 
ATOM   686  C CB  . PRO A 1 86  ? -3.26648  -57.80693 -17.84371 1.000 41.32000  ? 86   PRO A CB  1 
ATOM   687  C CG  . PRO A 1 86  ? -4.55141  -58.22882 -17.24266 1.000 39.89000  ? 86   PRO A CG  1 
ATOM   688  C CD  . PRO A 1 86  ? -4.42675  -58.04384 -15.76405 1.000 41.47000  ? 86   PRO A CD  1 
ATOM   689  N N   . PRO A 1 87  ? -1.92387  -54.79705 -18.12950 1.000 39.37000  ? 87   PRO A N   1 
ATOM   690  C CA  . PRO A 1 87  ? -2.06763  -53.44538 -18.66176 1.000 39.54000  ? 87   PRO A CA  1 
ATOM   691  C C   . PRO A 1 87  ? -2.90413  -53.42470 -19.92969 1.000 39.35000  ? 87   PRO A C   1 
ATOM   692  O O   . PRO A 1 87  ? -3.10684  -54.43945 -20.59890 1.000 39.51000  ? 87   PRO A O   1 
ATOM   693  C CB  . PRO A 1 87  ? -0.62285  -53.04518 -18.96544 1.000 38.09000  ? 87   PRO A CB  1 
ATOM   694  C CG  . PRO A 1 87  ? 0.00727   -54.34612 -19.37164 1.000 38.26000  ? 87   PRO A CG  1 
ATOM   695  C CD  . PRO A 1 87  ? -0.61463  -55.38675 -18.47221 1.000 37.93000  ? 87   PRO A CD  1 
ATOM   696  N N   . GLU A 1 88  ? -3.37802  -52.23190 -20.26017 1.000 38.27000  ? 88   GLU A N   1 
ATOM   697  C CA  . GLU A 1 88  ? -3.91726  -51.94994 -21.58024 1.000 43.23000  ? 88   GLU A CA  1 
ATOM   698  C C   . GLU A 1 88  ? -2.91680  -51.07332 -22.31418 1.000 43.34000  ? 88   GLU A C   1 
ATOM   699  O O   . GLU A 1 88  ? -2.40625  -50.10142 -21.74765 1.000 45.35000  ? 88   GLU A O   1 
ATOM   700  C CB  . GLU A 1 88  ? -5.28042  -51.26893 -21.49648 1.000 48.29000  ? 88   GLU A CB  1 
ATOM   701  C CG  . GLU A 1 88  ? -6.20819  -51.91617 -20.48971 1.000 61.31000  ? 88   GLU A CG  1 
ATOM   702  C CD  . GLU A 1 88  ? -7.57751  -51.28707 -20.50147 1.000 69.53000  ? 88   GLU A CD  1 
ATOM   703  O OE1 . GLU A 1 88  ? -7.70933  -50.18714 -21.08178 1.000 74.94000  ? 88   GLU A OE1 1 
ATOM   704  O OE2 . GLU A 1 88  ? -8.51360  -51.88286 -19.92448 1.000 76.09000  ? 88   GLU A OE2 1 
ATOM   705  N N   . VAL A 1 89  ? -2.61800  -51.42798 -23.55829 1.000 39.73000  ? 89   VAL A N   1 
ATOM   706  C CA  . VAL A 1 89  ? -1.53094  -50.80266 -24.29395 1.000 41.91000  ? 89   VAL A CA  1 
ATOM   707  C C   . VAL A 1 89  ? -2.09553  -50.08402 -25.50699 1.000 44.80000  ? 89   VAL A C   1 
ATOM   708  O O   . VAL A 1 89  ? -2.95980  -50.61062 -26.21697 1.000 44.23000  ? 89   VAL A O   1 
ATOM   709  C CB  . VAL A 1 89  ? -0.45651  -51.82728 -24.70729 1.000 40.10000  ? 89   VAL A CB  1 
ATOM   710  C CG1 . VAL A 1 89  ? 0.66770   -51.13603 -25.45580 1.000 40.64000  ? 89   VAL A CG1 1 
ATOM   711  C CG2 . VAL A 1 89  ? 0.08099   -52.53842 -23.47191 1.000 38.55000  ? 89   VAL A CG2 1 
ATOM   712  N N   . THR A 1 90  ? -1.60118  -48.87160 -25.72773 1.000 44.31000  ? 90   THR A N   1 
ATOM   713  C CA  . THR A 1 90  ? -1.95039  -48.04132 -26.86575 1.000 42.42000  ? 90   THR A CA  1 
ATOM   714  C C   . THR A 1 90  ? -0.66022  -47.49665 -27.45592 1.000 42.79000  ? 90   THR A C   1 
ATOM   715  O O   . THR A 1 90  ? 0.26058   -47.12811 -26.71917 1.000 42.25000  ? 90   THR A O   1 
ATOM   716  C CB  . THR A 1 90  ? -2.88147  -46.89499 -26.44490 1.000 43.69000  ? 90   THR A CB  1 
ATOM   717  O OG1 . THR A 1 90  ? -4.06225  -47.44098 -25.84746 1.000 51.23000  ? 90   THR A OG1 1 
ATOM   718  C CG2 . THR A 1 90  ? -3.27627  -46.04220 -27.63531 1.000 41.58000  ? 90   THR A CG2 1 
ATOM   719  N N   . VAL A 1 91  ? -0.57968  -47.47745 -28.78054 1.000 38.48000  ? 91   VAL A N   1 
ATOM   720  C CA  . VAL A 1 91  ? 0.57849   -46.95207 -29.48830 1.000 39.93000  ? 91   VAL A CA  1 
ATOM   721  C C   . VAL A 1 91  ? 0.10606   -45.79940 -30.35322 1.000 39.74000  ? 91   VAL A C   1 
ATOM   722  O O   . VAL A 1 91  ? -0.88318  -45.92852 -31.08188 1.000 40.07000  ? 91   VAL A O   1 
ATOM   723  C CB  . VAL A 1 91  ? 1.27529   -48.03314 -30.33495 1.000 43.00000  ? 91   VAL A CB  1 
ATOM   724  C CG1 . VAL A 1 91  ? 2.24793   -47.39831 -31.31467 1.000 48.27000  ? 91   VAL A CG1 1 
ATOM   725  C CG2 . VAL A 1 91  ? 2.00964   -48.99927 -29.43582 1.000 46.30000  ? 91   VAL A CG2 1 
ATOM   726  N N   . LEU A 1 92  ? 0.79630   -44.67105 -30.25690 1.000 39.27000  ? 92   LEU A N   1 
ATOM   727  C CA  . LEU A 1 92  ? 0.44949   -43.50691 -31.05357 1.000 37.77000  ? 92   LEU A CA  1 
ATOM   728  C C   . LEU A 1 92  ? 1.70528   -42.66989 -31.23458 1.000 33.63000  ? 92   LEU A C   1 
ATOM   729  O O   . LEU A 1 92  ? 2.76021   -42.96226 -30.66491 1.000 34.07000  ? 92   LEU A O   1 
ATOM   730  C CB  . LEU A 1 92  ? -0.69199  -42.70303 -30.41047 1.000 44.26000  ? 92   LEU A CB  1 
ATOM   731  C CG  . LEU A 1 92  ? -0.47988  -41.94773 -29.09249 1.000 47.84000  ? 92   LEU A CG  1 
ATOM   732  C CD1 . LEU A 1 92  ? -1.56612  -40.89656 -28.90588 1.000 50.21000  ? 92   LEU A CD1 1 
ATOM   733  C CD2 . LEU A 1 92  ? -0.44722  -42.88312 -27.88260 1.000 50.24000  ? 92   LEU A CD2 1 
ATOM   734  N N   . THR A 1 93  ? 1.58853   -41.63874 -32.06177 1.000 33.04000  ? 93   THR A N   1 
ATOM   735  C CA  . THR A 1 93  ? 2.66873   -40.69854 -32.30335 1.000 34.67000  ? 93   THR A CA  1 
ATOM   736  C C   . THR A 1 93  ? 2.37312   -39.38253 -31.59900 1.000 35.61000  ? 93   THR A C   1 
ATOM   737  O O   . THR A 1 93  ? 1.22498   -39.06499 -31.27829 1.000 35.05000  ? 93   THR A O   1 
ATOM   738  C CB  . THR A 1 93  ? 2.86623   -40.44483 -33.80233 1.000 35.66000  ? 93   THR A CB  1 
ATOM   739  O OG1 . THR A 1 93  ? 1.68909   -39.82191 -34.33669 1.000 35.44000  ? 93   THR A OG1 1 
ATOM   740  C CG2 . THR A 1 93  ? 3.13723   -41.75263 -34.54319 1.000 34.06000  ? 93   THR A CG2 1 
ATOM   741  N N   . ASN A 1 94  ? 3.43291   -38.60835 -31.37109 1.000 39.83000  ? 94   ASN A N   1 
ATOM   742  C CA  . ASN A 1 94  ? 3.28730   -37.33666 -30.68110 1.000 46.23000  ? 94   ASN A CA  1 
ATOM   743  C C   . ASN A 1 94  ? 2.68203   -36.25663 -31.57365 1.000 44.10000  ? 94   ASN A C   1 
ATOM   744  O O   . ASN A 1 94  ? 2.05613   -35.32294 -31.05764 1.000 44.09000  ? 94   ASN A O   1 
ATOM   745  C CB  . ASN A 1 94  ? 4.64946   -36.90028 -30.13133 1.000 51.42000  ? 94   ASN A CB  1 
ATOM   746  C CG  . ASN A 1 94  ? 4.66680   -35.45698 -29.68347 1.000 57.93000  ? 94   ASN A CG  1 
ATOM   747  O OD1 . ASN A 1 94  ? 4.24215   -35.13294 -28.57090 1.000 72.76000  ? 94   ASN A OD1 1 
ATOM   748  N ND2 . ASN A 1 94  ? 5.16571   -34.57707 -30.54470 1.000 59.07000  ? 94   ASN A ND2 1 
ATOM   749  N N   . SER A 1 95  ? 2.82411   -36.37418 -32.88818 1.000 42.47000  ? 95   SER A N   1 
ATOM   750  C CA  . SER A 1 95  ? 2.29362   -35.38919 -33.81979 1.000 43.15000  ? 95   SER A CA  1 
ATOM   751  C C   . SER A 1 95  ? 1.84873   -36.11780 -35.07464 1.000 40.75000  ? 95   SER A C   1 
ATOM   752  O O   . SER A 1 95  ? 2.12232   -37.31682 -35.23486 1.000 41.32000  ? 95   SER A O   1 
ATOM   753  C CB  . SER A 1 95  ? 3.33737   -34.30918 -34.13996 1.000 43.04000  ? 95   SER A CB  1 
ATOM   754  O OG  . SER A 1 95  ? 4.41811   -34.84001 -34.88415 1.000 44.13000  ? 95   SER A OG  1 
ATOM   755  N N   . PRO A 1 96  ? 1.12387   -35.44484 -35.97684 1.000 43.97000  ? 96   PRO A N   1 
ATOM   756  C CA  . PRO A 1 96  ? 0.69536   -36.11487 -37.21224 1.000 41.54000  ? 96   PRO A CA  1 
ATOM   757  C C   . PRO A 1 96  ? 1.88210   -36.57358 -38.05106 1.000 41.29000  ? 96   PRO A C   1 
ATOM   758  O O   . PRO A 1 96  ? 2.89835   -35.88334 -38.16141 1.000 42.21000  ? 96   PRO A O   1 
ATOM   759  C CB  . PRO A 1 96  ? -0.12807  -35.04153 -37.93195 1.000 42.63000  ? 96   PRO A CB  1 
ATOM   760  C CG  . PRO A 1 96  ? -0.64709  -34.18580 -36.83593 1.000 46.55000  ? 96   PRO A CG  1 
ATOM   761  C CD  . PRO A 1 96  ? 0.47221   -34.12639 -35.83307 1.000 45.72000  ? 96   PRO A CD  1 
ATOM   762  N N   . VAL A 1 97  ? 1.73277   -37.75343 -38.64886 1.000 44.50000  ? 97   VAL A N   1 
ATOM   763  C CA  . VAL A 1 97  ? 2.82629   -38.42559 -39.34039 1.000 49.55000  ? 97   VAL A CA  1 
ATOM   764  C C   . VAL A 1 97  ? 3.09140   -37.74888 -40.67599 1.000 52.79000  ? 97   VAL A C   1 
ATOM   765  O O   . VAL A 1 97  ? 2.16249   -37.40841 -41.42007 1.000 54.48000  ? 97   VAL A O   1 
ATOM   766  C CB  . VAL A 1 97  ? 2.50052   -39.91702 -39.53208 1.000 52.50000  ? 97   VAL A CB  1 
ATOM   767  C CG1 . VAL A 1 97  ? 3.76327   -40.70142 -39.82762 1.000 54.78000  ? 97   VAL A CG1 1 
ATOM   768  C CG2 . VAL A 1 97  ? 1.79957   -40.46725 -38.29798 1.000 57.87000  ? 97   VAL A CG2 1 
ATOM   769  N N   . GLU A 1 98  ? 4.37046   -37.55426 -40.98246 1.000 54.41000  ? 98   GLU A N   1 
ATOM   770  C CA  . GLU A 1 98  ? 4.80472   -37.01535 -42.26096 1.000 56.14000  ? 98   GLU A CA  1 
ATOM   771  C C   . GLU A 1 98  ? 6.09054   -37.71792 -42.66314 1.000 53.83000  ? 98   GLU A C   1 
ATOM   772  O O   . GLU A 1 98  ? 6.96548   -37.94951 -41.82319 1.000 47.11000  ? 98   GLU A O   1 
ATOM   773  C CB  . GLU A 1 98  ? 5.02187   -35.49862 -42.19468 1.000 64.36000  ? 98   GLU A CB  1 
ATOM   774  N N   . LEU A 1 99  ? 6.18883   -38.06077 -43.94780 1.000 52.48000  ? 99   LEU A N   1 
ATOM   775  C CA  . LEU A 1 99  ? 7.33599   -38.80167 -44.45713 1.000 58.10000  ? 99   LEU A CA  1 
ATOM   776  C C   . LEU A 1 99  ? 8.63214   -38.05157 -44.18943 1.000 54.76000  ? 99   LEU A C   1 
ATOM   777  O O   . LEU A 1 99  ? 8.73163   -36.84829 -44.44394 1.000 52.48000  ? 99   LEU A O   1 
ATOM   778  C CB  . LEU A 1 99  ? 7.17949   -39.04410 -45.95658 1.000 67.83000  ? 99   LEU A CB  1 
ATOM   779  C CG  . LEU A 1 99  ? 6.28117   -40.19503 -46.40209 1.000 79.52000  ? 99   LEU A CG  1 
ATOM   780  C CD1 . LEU A 1 99  ? 6.15378   -40.20234 -47.92313 1.000 83.70000  ? 99   LEU A CD1 1 
ATOM   781  C CD2 . LEU A 1 99  ? 6.83505   -41.51548 -45.89583 1.000 84.14000  ? 99   LEU A CD2 1 
ATOM   782  N N   . ARG A 1 100 ? 9.62145   -38.76955 -43.66004 1.000 52.69000  ? 100  ARG A N   1 
ATOM   783  C CA  . ARG A 1 100 ? 10.97280  -38.25535 -43.44812 1.000 61.47000  ? 100  ARG A CA  1 
ATOM   784  C C   . ARG A 1 100 ? 11.00984  -37.03956 -42.52208 1.000 59.18000  ? 100  ARG A C   1 
ATOM   785  O O   . ARG A 1 100 ? 12.01301  -36.31702 -42.48355 1.000 58.80000  ? 100  ARG A O   1 
ATOM   786  C CB  . ARG A 1 100 ? 11.65068  -37.92168 -44.78355 1.000 62.09000  ? 100  ARG A CB  1 
ATOM   787  N N   . GLU A 1 101 ? 9.93796   -36.78734 -41.76893 1.000 51.67000  ? 101  GLU A N   1 
ATOM   788  C CA  . GLU A 1 101 ? 9.94009   -35.73161 -40.76243 1.000 44.47000  ? 101  GLU A CA  1 
ATOM   789  C C   . GLU A 1 101 ? 9.99738   -36.37627 -39.38643 1.000 37.87000  ? 101  GLU A C   1 
ATOM   790  O O   . GLU A 1 101 ? 9.10323   -37.16546 -39.05178 1.000 37.40000  ? 101  GLU A O   1 
ATOM   791  C CB  . GLU A 1 101 ? 8.70322   -34.84153 -40.89220 1.000 44.72000  ? 101  GLU A CB  1 
ATOM   792  N N   . PRO A 1 102 ? 11.01748  -36.09226 -38.57586 1.000 38.65000  ? 102  PRO A N   1 
ATOM   793  C CA  . PRO A 1 102 ? 11.16756  -36.78805 -37.28951 1.000 38.23000  ? 102  PRO A CA  1 
ATOM   794  C C   . PRO A 1 102 ? 9.88711   -36.77510 -36.46332 1.000 38.83000  ? 102  PRO A C   1 
ATOM   795  O O   . PRO A 1 102 ? 9.15910   -35.78030 -36.41197 1.000 34.64000  ? 102  PRO A O   1 
ATOM   796  C CB  . PRO A 1 102 ? 12.29185  -36.01058 -36.60034 1.000 38.09000  ? 102  PRO A CB  1 
ATOM   797  C CG  . PRO A 1 102 ? 13.09290  -35.44804 -37.72670 1.000 39.19000  ? 102  PRO A CG  1 
ATOM   798  C CD  . PRO A 1 102 ? 12.13265  -35.17051 -38.84874 1.000 38.49000  ? 102  PRO A CD  1 
ATOM   799  N N   . ASN A 1 103 ? 9.60215   -37.91567 -35.84017 1.000 38.06000  ? 103  ASN A N   1 
ATOM   800  C CA  . ASN A 1 103 ? 8.42702   -38.08707 -35.00184 1.000 34.56000  ? 103  ASN A CA  1 
ATOM   801  C C   . ASN A 1 103 ? 8.82247   -38.93691 -33.80274 1.000 30.17000  ? 103  ASN A C   1 
ATOM   802  O O   . ASN A 1 103 ? 9.99135   -39.29804 -33.63209 1.000 33.03000  ? 103  ASN A O   1 
ATOM   803  C CB  . ASN A 1 103 ? 7.26848   -38.71986 -35.78392 1.000 34.02000  ? 103  ASN A CB  1 
ATOM   804  C CG  . ASN A 1 103 ? 5.91192   -38.23165 -35.31322 1.000 36.72000  ? 103  ASN A CG  1 
ATOM   805  O OD1 . ASN A 1 103 ? 5.54343   -38.40693 -34.14968 1.000 35.78000  ? 103  ASN A OD1 1 
ATOM   806  N ND2 . ASN A 1 103 ? 5.15331   -37.62822 -36.22044 1.000 39.13000  ? 103  ASN A ND2 1 
ATOM   807  N N   . VAL A 1 104 ? 7.84403   -39.24975 -32.95523 1.000 28.50000  ? 104  VAL A N   1 
ATOM   808  C CA  . VAL A 1 104 ? 8.07541   -40.05775 -31.76425 1.000 28.95000  ? 104  VAL A CA  1 
ATOM   809  C C   . VAL A 1 104 ? 6.90326   -41.00875 -31.59641 1.000 29.48000  ? 104  VAL A C   1 
ATOM   810  O O   . VAL A 1 104 ? 5.74899   -40.57190 -31.55017 1.000 30.33000  ? 104  VAL A O   1 
ATOM   811  C CB  . VAL A 1 104 ? 8.24320   -39.20641 -30.49462 1.000 30.67000  ? 104  VAL A CB  1 
ATOM   812  C CG1 . VAL A 1 104 ? 8.33669   -40.11025 -29.27076 1.000 31.66000  ? 104  VAL A CG1 1 
ATOM   813  C CG2 . VAL A 1 104 ? 9.47917   -38.31056 -30.60097 1.000 28.14000  ? 104  VAL A CG2 1 
ATOM   814  N N   . LEU A 1 105 ? 7.19167   -42.30099 -31.50608 1.000 30.98000  ? 105  LEU A N   1 
ATOM   815  C CA  . LEU A 1 105 ? 6.17043   -43.27231 -31.15181 1.000 33.15000  ? 105  LEU A CA  1 
ATOM   816  C C   . LEU A 1 105 ? 6.04712   -43.33463 -29.63820 1.000 32.58000  ? 105  LEU A C   1 
ATOM   817  O O   . LEU A 1 105 ? 7.04999   -43.46468 -28.92984 1.000 33.71000  ? 105  LEU A O   1 
ATOM   818  C CB  . LEU A 1 105 ? 6.51187   -44.65171 -31.71422 1.000 37.42000  ? 105  LEU A CB  1 
ATOM   819  C CG  . LEU A 1 105 ? 6.19775   -44.86193 -33.19711 1.000 40.36000  ? 105  LEU A CG  1 
ATOM   820  C CD1 . LEU A 1 105 ? 6.89652   -46.10587 -33.69269 1.000 43.54000  ? 105  LEU A CD1 1 
ATOM   821  C CD2 . LEU A 1 105 ? 4.69578   -44.94722 -33.44829 1.000 39.44000  ? 105  LEU A CD2 1 
ATOM   822  N N   . ILE A 1 106 ? 4.81957   -43.22704 -29.14554 1.000 33.06000  ? 106  ILE A N   1 
ATOM   823  C CA  . ILE A 1 106 ? 4.51827   -43.33730 -27.72480 1.000 34.85000  ? 106  ILE A CA  1 
ATOM   824  C C   . ILE A 1 106 ? 3.80586   -44.65820 -27.49212 1.000 34.62000  ? 106  ILE A C   1 
ATOM   825  O O   . ILE A 1 106 ? 2.81730   -44.96326 -28.16868 1.000 32.54000  ? 106  ILE A O   1 
ATOM   826  C CB  . ILE A 1 106 ? 3.65300   -42.16542 -27.23223 1.000 35.76000  ? 106  ILE A CB  1 
ATOM   827  C CG1 . ILE A 1 106 ? 4.23918   -40.83249 -27.69977 1.000 36.08000  ? 106  ILE A CG1 1 
ATOM   828  C CG2 . ILE A 1 106 ? 3.52522   -42.20853 -25.71818 1.000 37.78000  ? 106  ILE A CG2 1 
ATOM   829  C CD1 . ILE A 1 106 ? 3.30003   -39.67032 -27.51772 1.000 35.53000  ? 106  ILE A CD1 1 
ATOM   830  N N   . CYS A 1 107 ? 4.30349   -45.43407 -26.53550 1.000 36.42000  ? 107  CYS A N   1 
ATOM   831  C CA  . CYS A 1 107 ? 3.65422   -46.65451 -26.07613 1.000 36.47000  ? 107  CYS A CA  1 
ATOM   832  C C   . CYS A 1 107 ? 3.07459   -46.37130 -24.69684 1.000 36.19000  ? 107  CYS A C   1 
ATOM   833  O O   . CYS A 1 107 ? 3.81878   -46.27523 -23.71270 1.000 31.86000  ? 107  CYS A O   1 
ATOM   834  C CB  . CYS A 1 107 ? 4.63539   -47.82373 -26.03763 1.000 38.88000  ? 107  CYS A CB  1 
ATOM   835  S SG  . CYS A 1 107 ? 3.83163   -49.42324 -25.81472 1.000 43.37000  ? 107  CYS A SG  1 
ATOM   836  N N   . PHE A 1 108 ? 1.75354   -46.21858 -24.63200 1.000 38.82000  ? 108  PHE A N   1 
ATOM   837  C CA  . PHE A 1 108 ? 1.06047   -45.90081 -23.38951 1.000 42.83000  ? 108  PHE A CA  1 
ATOM   838  C C   . PHE A 1 108 ? 0.63240   -47.19620 -22.71289 1.000 37.19000  ? 108  PHE A C   1 
ATOM   839  O O   . PHE A 1 108 ? -0.14779  -47.96807 -23.27834 1.000 41.35000  ? 108  PHE A O   1 
ATOM   840  C CB  . PHE A 1 108 ? -0.14873  -45.00509 -23.65790 1.000 55.41000  ? 108  PHE A CB  1 
ATOM   841  N N   . ILE A 1 109 ? 1.14851   -47.43496 -21.51269 1.000 35.56000  ? 109  ILE A N   1 
ATOM   842  C CA  . ILE A 1 109 ? 0.87383   -48.64537 -20.74810 1.000 36.85000  ? 109  ILE A CA  1 
ATOM   843  C C   . ILE A 1 109 ? 0.07842   -48.23168 -19.51646 1.000 36.30000  ? 109  ILE A C   1 
ATOM   844  O O   . ILE A 1 109 ? 0.58643   -47.48681 -18.67052 1.000 34.95000  ? 109  ILE A O   1 
ATOM   845  C CB  . ILE A 1 109 ? 2.17602   -49.35869 -20.36278 1.000 35.77000  ? 109  ILE A CB  1 
ATOM   846  C CG1 . ILE A 1 109 ? 3.04978   -49.54422 -21.60320 1.000 37.17000  ? 109  ILE A CG1 1 
ATOM   847  C CG2 . ILE A 1 109 ? 1.88867   -50.70421 -19.74496 1.000 32.81000  ? 109  ILE A CG2 1 
ATOM   848  C CD1 . ILE A 1 109 ? 4.52077   -49.53648 -21.30782 1.000 39.71000  ? 109  ILE A CD1 1 
ATOM   849  N N   . ASP A 1 110 ? -1.16532  -48.71093 -19.40884 1.000 40.46000  ? 110  ASP A N   1 
ATOM   850  C CA  . ASP A 1 110 ? -2.13737  -48.14235 -18.48023 1.000 38.44000  ? 110  ASP A CA  1 
ATOM   851  C C   . ASP A 1 110 ? -2.83685  -49.21301 -17.64775 1.000 36.28000  ? 110  ASP A C   1 
ATOM   852  O O   . ASP A 1 110 ? -3.06525  -50.33711 -18.10415 1.000 38.20000  ? 110  ASP A O   1 
ATOM   853  C CB  . ASP A 1 110 ? -3.19277  -47.31372 -19.23981 1.000 35.03000  ? 110  ASP A CB  1 
ATOM   854  C CG  . ASP A 1 110 ? -3.80758  -46.20857 -18.38306 1.000 37.50000  ? 110  ASP A CG  1 
ATOM   855  O OD1 . ASP A 1 110 ? -3.22429  -45.86941 -17.33027 1.000 33.87000  ? 110  ASP A OD1 1 
ATOM   856  O OD2 . ASP A 1 110 ? -4.87027  -45.66904 -18.77109 1.000 40.18000  ? 110  ASP A OD2 1 
ATOM   857  N N   . LYS A 1 111 ? -3.17642  -48.83161 -16.41049 1.000 37.88000  ? 111  LYS A N   1 
ATOM   858  C CA  . LYS A 1 111 ? -4.04309  -49.59893 -15.50947 1.000 40.19000  ? 111  LYS A CA  1 
ATOM   859  C C   . LYS A 1 111 ? -3.47211  -50.98477 -15.19513 1.000 38.03000  ? 111  LYS A C   1 
ATOM   860  O O   . LYS A 1 111 ? -4.11338  -52.01929 -15.41477 1.000 38.34000  ? 111  LYS A O   1 
ATOM   861  C CB  . LYS A 1 111 ? -5.46123  -49.70650 -16.08276 1.000 45.64000  ? 111  LYS A CB  1 
ATOM   862  C CG  . LYS A 1 111 ? -5.99613  -48.39306 -16.63585 1.000 54.10000  ? 111  LYS A CG  1 
ATOM   863  C CD  . LYS A 1 111 ? -7.48423  -48.44808 -16.95003 1.000 60.13000  ? 111  LYS A CD  1 
ATOM   864  C CE  . LYS A 1 111 ? -7.73695  -48.49874 -18.45152 1.000 64.19000  ? 111  LYS A CE  1 
ATOM   865  N NZ  . LYS A 1 111 ? -8.03833  -47.16367 -19.04409 1.000 66.08000  ? 111  LYS A NZ  1 
ATOM   866  N N   . PHE A 1 112 ? -2.26312  -50.99935 -14.64049 1.000 34.62000  ? 112  PHE A N   1 
ATOM   867  C CA  . PHE A 1 112 ? -1.64405  -52.27435 -14.34215 1.000 32.62000  ? 112  PHE A CA  1 
ATOM   868  C C   . PHE A 1 112 ? -0.97191  -52.23277 -12.98636 1.000 32.62000  ? 112  PHE A C   1 
ATOM   869  O O   . PHE A 1 112 ? -0.65203  -51.17496 -12.43879 1.000 30.44000  ? 112  PHE A O   1 
ATOM   870  C CB  . PHE A 1 112 ? -0.62620  -52.68026 -15.40677 1.000 33.92000  ? 112  PHE A CB  1 
ATOM   871  C CG  . PHE A 1 112 ? 0.53525   -51.73441 -15.53192 1.000 35.46000  ? 112  PHE A CG  1 
ATOM   872  C CD1 . PHE A 1 112 ? 0.44199   -50.62333 -16.35217 1.000 34.25000  ? 112  PHE A CD1 1 
ATOM   873  C CD2 . PHE A 1 112 ? 1.72564   -51.96366 -14.85510 1.000 34.33000  ? 112  PHE A CD2 1 
ATOM   874  C CE1 . PHE A 1 112 ? 1.49189   -49.76031 -16.48879 1.000 34.57000  ? 112  PHE A CE1 1 
ATOM   875  C CE2 . PHE A 1 112 ? 2.79257   -51.09680 -14.99760 1.000 32.32000  ? 112  PHE A CE2 1 
ATOM   876  C CZ  . PHE A 1 112 ? 2.66862   -49.99431 -15.81958 1.000 34.35000  ? 112  PHE A CZ  1 
ATOM   877  N N   . THR A 1 113 ? -0.74312  -53.42917 -12.46959 1.000 32.64000  ? 113  THR A N   1 
ATOM   878  C CA  . THR A 1 113 ? -0.01201  -53.62492 -11.23141 1.000 35.64000  ? 113  THR A CA  1 
ATOM   879  C C   . THR A 1 113 ? 0.34347   -55.09607 -11.15032 1.000 34.09000  ? 113  THR A C   1 
ATOM   880  O O   . THR A 1 113 ? -0.36162  -55.92466 -11.73482 1.000 32.95000  ? 113  THR A O   1 
ATOM   881  C CB  . THR A 1 113 ? -0.83326  -53.18569 -10.01266 1.000 38.95000  ? 113  THR A CB  1 
ATOM   882  O OG1 . THR A 1 113 ? 0.05173   -52.84749 -8.94386  1.000 38.86000  ? 113  THR A OG1 1 
ATOM   883  C CG2 . THR A 1 113 ? -1.77243  -54.30560 -9.56800  1.000 36.35000  ? 113  THR A CG2 1 
ATOM   884  N N   . PRO A 1 114 ? 1.44866   -55.45889 -10.47755 1.000 32.18000  ? 114  PRO A N   1 
ATOM   885  C CA  . PRO A 1 114 ? 2.46271   -54.64543 -9.80688  1.000 31.82000  ? 114  PRO A CA  1 
ATOM   886  C C   . PRO A 1 114 ? 3.22585   -53.78233 -10.78986 1.000 31.32000  ? 114  PRO A C   1 
ATOM   887  O O   . PRO A 1 114 ? 3.16555   -54.04445 -11.99381 1.000 31.94000  ? 114  PRO A O   1 
ATOM   888  C CB  . PRO A 1 114 ? 3.37747   -55.69437 -9.15105  1.000 31.06000  ? 114  PRO A CB  1 
ATOM   889  C CG  . PRO A 1 114 ? 3.24232   -56.87927 -10.02792 1.000 30.85000  ? 114  PRO A CG  1 
ATOM   890  C CD  . PRO A 1 114 ? 1.80947   -56.88718 -10.46008 1.000 32.20000  ? 114  PRO A CD  1 
ATOM   891  N N   . PRO A 1 115 ? 3.89692   -52.75435 -10.29426 1.000 31.19000  ? 115  PRO A N   1 
ATOM   892  C CA  . PRO A 1 115 ? 4.69105   -51.87704 -11.17033 1.000 34.41000  ? 115  PRO A CA  1 
ATOM   893  C C   . PRO A 1 115 ? 5.97625   -52.52873 -11.66598 1.000 34.18000  ? 115  PRO A C   1 
ATOM   894  O O   . PRO A 1 115 ? 7.07466   -52.09892 -11.30011 1.000 35.32000  ? 115  PRO A O   1 
ATOM   895  C CB  . PRO A 1 115 ? 4.99404   -50.67824 -10.26221 1.000 31.99000  ? 115  PRO A CB  1 
ATOM   896  C CG  . PRO A 1 115 ? 4.93466   -51.25680 -8.87720  1.000 32.61000  ? 115  PRO A CG  1 
ATOM   897  C CD  . PRO A 1 115 ? 3.86225   -52.28248 -8.90184  1.000 31.67000  ? 115  PRO A CD  1 
ATOM   898  N N   . VAL A 1 116 ? 5.85129   -53.58295 -12.46963 1.000 36.23000  ? 116  VAL A N   1 
ATOM   899  C CA  . VAL A 1 116 ? 6.98234   -54.23452 -13.12570 1.000 36.97000  ? 116  VAL A CA  1 
ATOM   900  C C   . VAL A 1 116 ? 6.52110   -54.61338 -14.52140 1.000 37.62000  ? 116  VAL A C   1 
ATOM   901  O O   . VAL A 1 116 ? 5.53582   -55.34238 -14.67057 1.000 36.07000  ? 116  VAL A O   1 
ATOM   902  C CB  . VAL A 1 116 ? 7.48063   -55.48767 -12.37952 1.000 38.25000  ? 116  VAL A CB  1 
ATOM   903  C CG1 . VAL A 1 116 ? 8.49768   -56.24372 -13.23046 1.000 36.22000  ? 116  VAL A CG1 1 
ATOM   904  C CG2 . VAL A 1 116 ? 8.09643   -55.11436 -11.05906 1.000 37.13000  ? 116  VAL A CG2 1 
ATOM   905  N N   . VAL A 1 117 ? 7.21830   -54.12406 -15.53993 1.000 39.38000  ? 117  VAL A N   1 
ATOM   906  C CA  . VAL A 1 117 ? 6.82670   -54.38565 -16.91953 1.000 40.71000  ? 117  VAL A CA  1 
ATOM   907  C C   . VAL A 1 117 ? 8.08680   -54.45587 -17.77377 1.000 42.65000  ? 117  VAL A C   1 
ATOM   908  O O   . VAL A 1 117 ? 9.05541   -53.72579 -17.54048 1.000 45.34000  ? 117  VAL A O   1 
ATOM   909  C CB  . VAL A 1 117 ? 5.83099   -53.31191 -17.42023 1.000 43.27000  ? 117  VAL A CB  1 
ATOM   910  C CG1 . VAL A 1 117 ? 6.53013   -51.97640 -17.64784 1.000 45.42000  ? 117  VAL A CG1 1 
ATOM   911  C CG2 . VAL A 1 117 ? 5.12498   -53.77282 -18.68246 1.000 46.47000  ? 117  VAL A CG2 1 
ATOM   912  N N   . ASN A 1 118 ? 8.08897   -55.36164 -18.74594 1.000 47.02000  ? 118  ASN A N   1 
ATOM   913  C CA  . ASN A 1 118 ? 9.18275   -55.47171 -19.70547 1.000 47.93000  ? 118  ASN A CA  1 
ATOM   914  C C   . ASN A 1 118 ? 8.66258   -54.97596 -21.05047 1.000 42.91000  ? 118  ASN A C   1 
ATOM   915  O O   . ASN A 1 118 ? 7.75898   -55.58063 -21.63619 1.000 39.33000  ? 118  ASN A O   1 
ATOM   916  C CB  . ASN A 1 118 ? 9.70593   -56.90557 -19.79622 1.000 54.02000  ? 118  ASN A CB  1 
ATOM   917  C CG  . ASN A 1 118 ? 11.02643  -57.00003 -20.54732 1.000 64.17000  ? 118  ASN A CG  1 
ATOM   918  O OD1 . ASN A 1 118 ? 11.59165  -55.98586 -20.96203 1.000 70.29000  ? 118  ASN A OD1 1 
ATOM   919  N ND2 . ASN A 1 118 ? 11.52015  -58.22118 -20.73380 1.000 77.69000  ? 118  ASN A ND2 1 
ATOM   920  N N   . VAL A 1 119 ? 9.21764   -53.86799 -21.52974 1.000 41.61000  ? 119  VAL A N   1 
ATOM   921  C CA  . VAL A 1 119 ? 8.79686   -53.25950 -22.78475 1.000 41.61000  ? 119  VAL A CA  1 
ATOM   922  C C   . VAL A 1 119 ? 9.95316   -53.32792 -23.76972 1.000 45.36000  ? 119  VAL A C   1 
ATOM   923  O O   . VAL A 1 119 ? 11.11391  -53.12749 -23.39538 1.000 52.69000  ? 119  VAL A O   1 
ATOM   924  C CB  . VAL A 1 119 ? 8.33087   -51.80148 -22.59008 1.000 40.73000  ? 119  VAL A CB  1 
ATOM   925  C CG1 . VAL A 1 119 ? 7.70579   -51.27097 -23.86975 1.000 41.06000  ? 119  VAL A CG1 1 
ATOM   926  C CG2 . VAL A 1 119 ? 7.35055   -51.71088 -21.43220 1.000 40.05000  ? 119  VAL A CG2 1 
ATOM   927  N N   . THR A 1 120 ? 9.63237   -53.62431 -25.02534 1.000 47.08000  ? 120  THR A N   1 
ATOM   928  C CA  . THR A 1 120 ? 10.61542  -53.66806 -26.09748 1.000 49.22000  ? 120  THR A CA  1 
ATOM   929  C C   . THR A 1 120 ? 9.97392   -53.12547 -27.36311 1.000 47.80000  ? 120  THR A C   1 
ATOM   930  O O   . THR A 1 120 ? 8.85501   -53.51391 -27.71104 1.000 49.86000  ? 120  THR A O   1 
ATOM   931  C CB  . THR A 1 120 ? 11.13164  -55.09584 -26.33229 1.000 51.09000  ? 120  THR A CB  1 
ATOM   932  O OG1 . THR A 1 120 ? 11.83996  -55.55049 -25.17185 1.000 53.93000  ? 120  THR A OG1 1 
ATOM   933  C CG2 . THR A 1 120 ? 12.05625  -55.14198 -27.53233 1.000 51.42000  ? 120  THR A CG2 1 
ATOM   934  N N   . TRP A 1 121 ? 10.67137  -52.21800 -28.03619 1.000 44.93000  ? 121  TRP A N   1 
ATOM   935  C CA  . TRP A 1 121 ? 10.24743  -51.74283 -29.34332 1.000 45.53000  ? 121  TRP A CA  1 
ATOM   936  C C   . TRP A 1 121 ? 10.82328  -52.64766 -30.42320 1.000 49.78000  ? 121  TRP A C   1 
ATOM   937  O O   . TRP A 1 121 ? 11.98740  -53.05145 -30.35094 1.000 49.60000  ? 121  TRP A O   1 
ATOM   938  C CB  . TRP A 1 121 ? 10.71337  -50.30873 -29.57866 1.000 42.57000  ? 121  TRP A CB  1 
ATOM   939  C CG  . TRP A 1 121 ? 10.03047  -49.26627 -28.75798 1.000 41.56000  ? 121  TRP A CG  1 
ATOM   940  C CD1 . TRP A 1 121 ? 10.50374  -48.68265 -27.61975 1.000 40.58000  ? 121  TRP A CD1 1 
ATOM   941  C CD2 . TRP A 1 121 ? 8.76764   -48.64635 -29.03198 1.000 39.30000  ? 121  TRP A CD2 1 
ATOM   942  N NE1 . TRP A 1 121 ? 9.60862   -47.74662 -27.15959 1.000 43.35000  ? 121  TRP A NE1 1 
ATOM   943  C CE2 . TRP A 1 121 ? 8.53529   -47.70409 -28.01012 1.000 40.64000  ? 121  TRP A CE2 1 
ATOM   944  C CE3 . TRP A 1 121 ? 7.81021   -48.79811 -30.04019 1.000 39.83000  ? 121  TRP A CE3 1 
ATOM   945  C CZ2 . TRP A 1 121 ? 7.38428   -46.91831 -27.96592 1.000 37.82000  ? 121  TRP A CZ2 1 
ATOM   946  C CZ3 . TRP A 1 121 ? 6.66526   -48.01553 -29.99394 1.000 38.31000  ? 121  TRP A CZ3 1 
ATOM   947  C CH2 . TRP A 1 121 ? 6.46396   -47.08892 -28.96350 1.000 36.02000  ? 121  TRP A CH2 1 
ATOM   948  N N   . LEU A 1 122 ? 10.00547  -52.95686 -31.42810 1.000 51.10000  ? 122  LEU A N   1 
ATOM   949  C CA  . LEU A 1 122 ? 10.41994  -53.76592 -32.56730 1.000 52.63000  ? 122  LEU A CA  1 
ATOM   950  C C   . LEU A 1 122 ? 10.20307  -52.97770 -33.85021 1.000 50.00000  ? 122  LEU A C   1 
ATOM   951  O O   . LEU A 1 122 ? 9.09640   -52.48883 -34.10005 1.000 46.89000  ? 122  LEU A O   1 
ATOM   952  C CB  . LEU A 1 122 ? 9.63092   -55.07486 -32.64008 1.000 53.06000  ? 122  LEU A CB  1 
ATOM   953  C CG  . LEU A 1 122 ? 9.86157   -56.18383 -31.61414 1.000 56.33000  ? 122  LEU A CG  1 
ATOM   954  C CD1 . LEU A 1 122 ? 9.64268   -57.53983 -32.26117 1.000 57.02000  ? 122  LEU A CD1 1 
ATOM   955  C CD2 . LEU A 1 122 ? 11.23930  -56.10371 -31.01825 1.000 60.79000  ? 122  LEU A CD2 1 
ATOM   956  N N   . ARG A 1 123 ? 11.25149  -52.85158 -34.65988 1.000 55.10000  ? 123  ARG A N   1 
ATOM   957  C CA  . ARG A 1 123 ? 11.13000  -52.32610 -36.01599 1.000 55.39000  ? 123  ARG A CA  1 
ATOM   958  C C   . ARG A 1 123 ? 11.31310  -53.49451 -36.97323 1.000 56.61000  ? 123  ARG A C   1 
ATOM   959  O O   . ARG A 1 123 ? 12.39440  -54.09171 -37.03009 1.000 50.39000  ? 123  ARG A O   1 
ATOM   960  C CB  . ARG A 1 123 ? 12.14526  -51.22198 -36.30112 1.000 53.35000  ? 123  ARG A CB  1 
ATOM   961  C CG  . ARG A 1 123 ? 12.04114  -50.68729 -37.72916 1.000 55.71000  ? 123  ARG A CG  1 
ATOM   962  C CD  . ARG A 1 123 ? 13.23160  -49.82751 -38.12455 1.000 57.60000  ? 123  ARG A CD  1 
ATOM   963  N NE  . ARG A 1 123 ? 13.11604  -48.46904 -37.60860 1.000 64.87000  ? 123  ARG A NE  1 
ATOM   964  C CZ  . ARG A 1 123 ? 13.99357  -47.89639 -36.79413 1.000 72.26000  ? 123  ARG A CZ  1 
ATOM   965  N NH1 . ARG A 1 123 ? 15.07671  -48.53768 -36.38352 1.000 70.34000  ? 123  ARG A NH1 1 
ATOM   966  N NH2 . ARG A 1 123 ? 13.77976  -46.64778 -36.38190 1.000 70.94000  ? 123  ARG A NH2 1 
ATOM   967  N N   . ASN A 1 124 ? 10.25621  -53.81716 -37.71739 1.000 63.30000  ? 124  ASN A N   1 
ATOM   968  C CA  . ASN A 1 124 ? 10.25668  -54.95695 -38.63207 1.000 67.19000  ? 124  ASN A CA  1 
ATOM   969  C C   . ASN A 1 124 ? 10.67953  -56.23367 -37.90563 1.000 67.53000  ? 124  ASN A C   1 
ATOM   970  O O   . ASN A 1 124 ? 11.52640  -56.99726 -38.37278 1.000 66.22000  ? 124  ASN A O   1 
ATOM   971  C CB  . ASN A 1 124 ? 11.15664  -54.68907 -39.84055 1.000 65.17000  ? 124  ASN A CB  1 
ATOM   972  C CG  . ASN A 1 124 ? 10.82994  -53.38024 -40.53754 1.000 61.10000  ? 124  ASN A CG  1 
ATOM   973  O OD1 . ASN A 1 124 ? 9.65932   -53.02447 -40.71286 1.000 60.96000  ? 124  ASN A OD1 1 
ATOM   974  N ND2 . ASN A 1 124 ? 11.86865  -52.65678 -40.94612 1.000 59.92000  ? 124  ASN A ND2 1 
ATOM   975  N N   . GLY A 1 125 ? 10.09240  -56.45077 -36.73111 1.000 68.00000  ? 125  GLY A N   1 
ATOM   976  C CA  . GLY A 1 125 ? 10.41481  -57.60768 -35.92323 1.000 64.38000  ? 125  GLY A CA  1 
ATOM   977  C C   . GLY A 1 125 ? 11.77826  -57.59562 -35.26430 1.000 62.75000  ? 125  GLY A C   1 
ATOM   978  O O   . GLY A 1 125 ? 12.12973  -58.57819 -34.59866 1.000 64.08000  ? 125  GLY A O   1 
ATOM   979  N N   . LYS A 1 126 ? 12.55847  -56.52232 -35.41427 1.000 64.34000  ? 126  LYS A N   1 
ATOM   980  C CA  . LYS A 1 126 ? 13.89014  -56.44971 -34.82662 1.000 69.74000  ? 126  LYS A CA  1 
ATOM   981  C C   . LYS A 1 126 ? 13.92154  -55.41974 -33.70826 1.000 66.91000  ? 126  LYS A C   1 
ATOM   982  O O   . LYS A 1 126 ? 13.43126  -54.29783 -33.89490 1.000 64.44000  ? 126  LYS A O   1 
ATOM   983  C CB  . LYS A 1 126 ? 14.93119  -56.09287 -35.89415 1.000 76.48000  ? 126  LYS A CB  1 
ATOM   984  N N   . PRO A 1 127 ? 14.48640  -55.75222 -32.54663 1.000 63.58000  ? 127  PRO A N   1 
ATOM   985  C CA  . PRO A 1 127 ? 14.47652  -54.80468 -31.42501 1.000 62.25000  ? 127  PRO A CA  1 
ATOM   986  C C   . PRO A 1 127 ? 15.26468  -53.54629 -31.75014 1.000 63.30000  ? 127  PRO A C   1 
ATOM   987  O O   . PRO A 1 127 ? 16.29495  -53.59048 -32.42576 1.000 62.27000  ? 127  PRO A O   1 
ATOM   988  C CB  . PRO A 1 127 ? 15.12208  -55.59651 -30.27956 1.000 64.92000  ? 127  PRO A CB  1 
ATOM   989  C CG  . PRO A 1 127 ? 15.03348  -57.03193 -30.69208 1.000 62.20000  ? 127  PRO A CG  1 
ATOM   990  C CD  . PRO A 1 127 ? 15.11182  -57.03446 -32.18527 1.000 63.20000  ? 127  PRO A CD  1 
ATOM   991  N N   . VAL A 1 128 ? 14.76536  -52.41435 -31.26014 1.000 62.95000  ? 128  VAL A N   1 
ATOM   992  C CA  . VAL A 1 128 ? 15.37102  -51.11268 -31.50763 1.000 59.62000  ? 128  VAL A CA  1 
ATOM   993  C C   . VAL A 1 128 ? 15.55741  -50.40200 -30.17597 1.000 59.25000  ? 128  VAL A C   1 
ATOM   994  O O   . VAL A 1 128 ? 14.60432  -50.26292 -29.40254 1.000 64.22000  ? 128  VAL A O   1 
ATOM   995  C CB  . VAL A 1 128 ? 14.52096  -50.26309 -32.47113 1.000 63.46000  ? 128  VAL A CB  1 
ATOM   996  C CG1 . VAL A 1 128 ? 14.81031  -50.65908 -33.90279 1.000 69.62000  ? 128  VAL A CG1 1 
ATOM   997  C CG2 . VAL A 1 128 ? 13.05072  -50.45648 -32.18374 1.000 61.62000  ? 128  VAL A CG2 1 
ATOM   998  N N   . THR A 1 129 ? 16.78871  -49.96778 -29.90561 1.000 60.22000  ? 129  THR A N   1 
ATOM   999  C CA  . THR A 1 129 ? 17.12023  -49.25100 -28.68352 1.000 60.81000  ? 129  THR A CA  1 
ATOM   1000 C C   . THR A 1 129 ? 17.71355  -47.87489 -28.94350 1.000 60.09000  ? 129  THR A C   1 
ATOM   1001 O O   . THR A 1 129 ? 18.12093  -47.20187 -27.98908 1.000 60.31000  ? 129  THR A O   1 
ATOM   1002 C CB  . THR A 1 129 ? 18.10141  -50.06601 -27.82920 1.000 63.02000  ? 129  THR A CB  1 
ATOM   1003 O OG1 . THR A 1 129 ? 19.33232  -50.23524 -28.54487 1.000 61.97000  ? 129  THR A OG1 1 
ATOM   1004 C CG2 . THR A 1 129 ? 17.51370  -51.42959 -27.48580 1.000 63.28000  ? 129  THR A CG2 1 
ATOM   1005 N N   . THR A 1 130 ? 17.77531  -47.43573 -30.19683 1.000 61.09000  ? 130  THR A N   1 
ATOM   1006 C CA  . THR A 1 130 ? 18.36908  -46.14367 -30.51819 1.000 57.62000  ? 130  THR A CA  1 
ATOM   1007 C C   . THR A 1 130 ? 17.43169  -45.02464 -30.08468 1.000 50.23000  ? 130  THR A C   1 
ATOM   1008 O O   . THR A 1 130 ? 16.35336  -44.84479 -30.66095 1.000 54.26000  ? 130  THR A O   1 
ATOM   1009 C CB  . THR A 1 130 ? 18.66508  -46.05200 -32.01057 1.000 59.46000  ? 130  THR A CB  1 
ATOM   1010 O OG1 . THR A 1 130 ? 19.14422  -47.31916 -32.47894 1.000 61.09000  ? 130  THR A OG1 1 
ATOM   1011 C CG2 . THR A 1 130 ? 19.71338  -44.97487 -32.27457 1.000 56.39000  ? 130  THR A CG2 1 
ATOM   1012 N N   . GLY A 1 131 ? 17.84303  -44.27109 -29.07050 1.000 46.93000  ? 131  GLY A N   1 
ATOM   1013 C CA  . GLY A 1 131 ? 17.11015  -43.09690 -28.65422 1.000 50.14000  ? 131  GLY A CA  1 
ATOM   1014 C C   . GLY A 1 131 ? 15.86631  -43.35589 -27.83777 1.000 44.96000  ? 131  GLY A C   1 
ATOM   1015 O O   . GLY A 1 131 ? 15.14252  -42.39960 -27.53973 1.000 46.19000  ? 131  GLY A O   1 
ATOM   1016 N N   . VAL A 1 132 ? 15.59305  -44.61098 -27.46208 1.000 40.06000  ? 132  VAL A N   1 
ATOM   1017 C CA  . VAL A 1 132 ? 14.40831  -44.91069 -26.66576 1.000 41.92000  ? 132  VAL A CA  1 
ATOM   1018 C C   . VAL A 1 132 ? 14.52158  -44.25108 -25.29559 1.000 42.64000  ? 132  VAL A C   1 
ATOM   1019 O O   . VAL A 1 132 ? 15.62013  -44.07180 -24.74829 1.000 45.44000  ? 132  VAL A O   1 
ATOM   1020 C CB  . VAL A 1 132 ? 14.19652  -46.42915 -26.51729 1.000 41.75000  ? 132  VAL A CB  1 
ATOM   1021 C CG1 . VAL A 1 132 ? 14.00629  -47.07951 -27.87459 1.000 44.01000  ? 132  VAL A CG1 1 
ATOM   1022 C CG2 . VAL A 1 132 ? 15.35921  -47.06054 -25.77250 1.000 45.58000  ? 132  VAL A CG2 1 
ATOM   1023 N N   . SER A 1 133 ? 13.37269  -43.87629 -24.73631 1.000 39.11000  ? 133  SER A N   1 
ATOM   1024 C CA  . SER A 1 133 ? 13.31781  -43.39694 -23.36457 1.000 36.65000  ? 133  SER A CA  1 
ATOM   1025 C C   . SER A 1 133 ? 11.99676  -43.84339 -22.76000 1.000 36.08000  ? 133  SER A C   1 
ATOM   1026 O O   . SER A 1 133 ? 11.14403  -44.42341 -23.43691 1.000 34.30000  ? 133  SER A O   1 
ATOM   1027 C CB  . SER A 1 133 ? 13.48144  -41.87416 -23.27886 1.000 34.07000  ? 133  SER A CB  1 
ATOM   1028 O OG  . SER A 1 133 ? 12.44528  -41.20022 -23.96876 1.000 35.15000  ? 133  SER A OG  1 
ATOM   1029 N N   . GLU A 1 134 ? 11.83435  -43.56561 -21.47002 1.000 35.61000  ? 134  GLU A N   1 
ATOM   1030 C CA  . GLU A 1 134 ? 10.64725  -44.00724 -20.75859 1.000 35.17000  ? 134  GLU A CA  1 
ATOM   1031 C C   . GLU A 1 134 ? 10.50267  -43.19073 -19.48556 1.000 35.54000  ? 134  GLU A C   1 
ATOM   1032 O O   . GLU A 1 134 ? 11.44373  -42.53440 -19.03734 1.000 31.15000  ? 134  GLU A O   1 
ATOM   1033 C CB  . GLU A 1 134 ? 10.72751  -45.49120 -20.41377 1.000 40.36000  ? 134  GLU A CB  1 
ATOM   1034 C CG  . GLU A 1 134 ? 11.81128  -45.78218 -19.40313 1.000 40.49000  ? 134  GLU A CG  1 
ATOM   1035 C CD  . GLU A 1 134 ? 12.52269  -47.08086 -19.68280 1.000 46.90000  ? 134  GLU A CD  1 
ATOM   1036 O OE1 . GLU A 1 134 ? 13.31775  -47.12697 -20.64714 1.000 49.78000  ? 134  GLU A OE1 1 
ATOM   1037 O OE2 . GLU A 1 134 ? 12.28149  -48.05451 -18.93159 1.000 50.03000  ? 134  GLU A OE2 1 
ATOM   1038 N N   . THR A 1 135 ? 9.31409   -43.25789 -18.90112 1.000 34.62000  ? 135  THR A N   1 
ATOM   1039 C CA  . THR A 1 135 ? 9.02864   -42.61244 -17.63106 1.000 30.51000  ? 135  THR A CA  1 
ATOM   1040 C C   . THR A 1 135 ? 9.07456   -43.64356 -16.50794 1.000 29.36000  ? 135  THR A C   1 
ATOM   1041 O O   . THR A 1 135 ? 9.18356   -44.84972 -16.73861 1.000 26.87000  ? 135  THR A O   1 
ATOM   1042 C CB  . THR A 1 135 ? 7.65558   -41.92511 -17.66699 1.000 29.69000  ? 135  THR A CB  1 
ATOM   1043 O OG1 . THR A 1 135 ? 6.61990   -42.92023 -17.68231 1.000 27.00000  ? 135  THR A OG1 1 
ATOM   1044 C CG2 . THR A 1 135 ? 7.52453   -41.04315 -18.90030 1.000 28.85000  ? 135  THR A CG2 1 
ATOM   1045 N N   . VAL A 1 136 ? 8.99481   -43.15726 -15.27181 1.000 30.77000  ? 136  VAL A N   1 
ATOM   1046 C CA  . VAL A 1 136 ? 8.76932   -44.06237 -14.15251 1.000 30.78000  ? 136  VAL A CA  1 
ATOM   1047 C C   . VAL A 1 136 ? 7.28642   -44.40947 -14.14936 1.000 33.76000  ? 136  VAL A C   1 
ATOM   1048 O O   . VAL A 1 136 ? 6.53004   -43.96187 -15.02390 1.000 26.22000  ? 136  VAL A O   1 
ATOM   1049 C CB  . VAL A 1 136 ? 9.20693   -43.44875 -12.81197 1.000 33.49000  ? 136  VAL A CB  1 
ATOM   1050 C CG1 . VAL A 1 136 ? 10.73084  -43.36104 -12.74121 1.000 31.73000  ? 136  VAL A CG1 1 
ATOM   1051 C CG2 . VAL A 1 136 ? 8.55808   -42.08613 -12.61051 1.000 33.21000  ? 136  VAL A CG2 1 
ATOM   1052 N N   . PHE A 1 137 ? 6.85994   -45.21158 -13.17657 1.000 34.44000  ? 137  PHE A N   1 
ATOM   1053 C CA  . PHE A 1 137 ? 5.45963   -45.59795 -13.08261 1.000 33.01000  ? 137  PHE A CA  1 
ATOM   1054 C C   . PHE A 1 137 ? 4.63761   -44.45001 -12.50211 1.000 36.47000  ? 137  PHE A C   1 
ATOM   1055 O O   . PHE A 1 137 ? 4.97267   -43.90203 -11.45019 1.000 34.32000  ? 137  PHE A O   1 
ATOM   1056 C CB  . PHE A 1 137 ? 5.32121   -46.86146 -12.23608 1.000 32.84000  ? 137  PHE A CB  1 
ATOM   1057 C CG  . PHE A 1 137 ? 6.09764   -48.04118 -12.77560 1.000 33.92000  ? 137  PHE A CG  1 
ATOM   1058 C CD1 . PHE A 1 137 ? 5.51634   -48.91481 -13.68193 1.000 32.57000  ? 137  PHE A CD1 1 
ATOM   1059 C CD2 . PHE A 1 137 ? 7.40880   -48.27407 -12.37855 1.000 36.09000  ? 137  PHE A CD2 1 
ATOM   1060 C CE1 . PHE A 1 137 ? 6.22141   -50.00286 -14.18225 1.000 35.77000  ? 137  PHE A CE1 1 
ATOM   1061 C CE2 . PHE A 1 137 ? 8.12088   -49.36235 -12.87698 1.000 36.30000  ? 137  PHE A CE2 1 
ATOM   1062 C CZ  . PHE A 1 137 ? 7.52388   -50.22700 -13.78040 1.000 37.43000  ? 137  PHE A CZ  1 
ATOM   1063 N N   . LEU A 1 138 ? 3.57628   -44.06742 -13.20425 1.000 34.95000  ? 138  LEU A N   1 
ATOM   1064 C CA  . LEU A 1 138 ? 2.83334   -42.95944 -12.62463 1.000 36.09000  ? 138  LEU A CA  1 
ATOM   1065 C C   . LEU A 1 138 ? 1.62851   -43.47824 -11.84551 1.000 34.34000  ? 138  LEU A C   1 
ATOM   1066 O O   . LEU A 1 138 ? 1.00975   -44.47256 -12.24266 1.000 33.47000  ? 138  LEU A O   1 
ATOM   1067 C CB  . LEU A 1 138 ? 2.37120   -41.98612 -13.71568 1.000 38.24000  ? 138  LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 138 ? 3.34468   -41.73018 -14.88103 1.000 41.89000  ? 138  LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 138 ? 2.68538   -40.93096 -15.99880 1.000 43.02000  ? 138  LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 138 ? 4.59632   -41.01082 -14.40261 1.000 42.16000  ? 138  LEU A CD2 1 
ATOM   1071 N N   . PRO A 1 139 ? 1.27634   -42.84292 -10.73239 1.000 32.96000  ? 139  PRO A N   1 
ATOM   1072 C CA  . PRO A 1 139 ? 0.14004   -43.32805 -9.93767  1.000 34.82000  ? 139  PRO A CA  1 
ATOM   1073 C C   . PRO A 1 139 ? -1.19264  -42.98903 -10.58983 1.000 35.91000  ? 139  PRO A C   1 
ATOM   1074 O O   . PRO A 1 139 ? -1.34278  -41.96554 -11.26344 1.000 36.57000  ? 139  PRO A O   1 
ATOM   1075 C CB  . PRO A 1 139 ? 0.30341   -42.58779 -8.60572  1.000 36.21000  ? 139  PRO A CB  1 
ATOM   1076 C CG  . PRO A 1 139 ? 0.94490   -41.28185 -9.00804  1.000 36.30000  ? 139  PRO A CG  1 
ATOM   1077 C CD  . PRO A 1 139 ? 1.88058   -41.62503 -10.15822 1.000 31.63000  ? 139  PRO A CD  1 
ATOM   1078 N N   . ARG A 1 140 ? -2.16956  -43.86742 -10.37694 1.000 36.40000  ? 140  ARG A N   1 
ATOM   1079 C CA  . ARG A 1 140 ? -3.53953  -43.65608 -10.81942 1.000 33.69000  ? 140  ARG A CA  1 
ATOM   1080 C C   . ARG A 1 140 ? -4.43842  -43.57789 -9.59475  1.000 30.36000  ? 140  ARG A C   1 
ATOM   1081 O O   . ARG A 1 140 ? -4.07231  -44.03919 -8.51151  1.000 34.26000  ? 140  ARG A O   1 
ATOM   1082 C CB  . ARG A 1 140 ? -4.01443  -44.78257 -11.74798 1.000 33.16000  ? 140  ARG A CB  1 
ATOM   1083 C CG  . ARG A 1 140 ? -3.27452  -44.86167 -13.06267 1.000 33.55000  ? 140  ARG A CG  1 
ATOM   1084 C CD  . ARG A 1 140 ? -3.64836  -46.12670 -13.82700 1.000 36.04000  ? 140  ARG A CD  1 
ATOM   1085 N NE  . ARG A 1 140 ? -5.08952  -46.34665 -13.85086 1.000 36.47000  ? 140  ARG A NE  1 
ATOM   1086 C CZ  . ARG A 1 140 ? -5.91589  -45.73602 -14.68999 1.000 39.23000  ? 140  ARG A CZ  1 
ATOM   1087 N NH1 . ARG A 1 140 ? -5.47435  -44.86384 -15.58147 1.000 36.15000  ? 140  ARG A NH1 1 
ATOM   1088 N NH2 . ARG A 1 140 ? -7.21530  -46.01069 -14.63729 1.000 40.45000  ? 140  ARG A NH2 1 
ATOM   1089 N N   . GLU A 1 141 ? -5.62769  -42.99555 -9.76374  1.000 31.54000  ? 141  GLU A N   1 
ATOM   1090 C CA  . GLU A 1 141 ? -6.52732  -42.84486 -8.62308  1.000 35.96000  ? 141  GLU A CA  1 
ATOM   1091 C C   . GLU A 1 141 ? -7.21786  -44.15176 -8.23489  1.000 32.10000  ? 141  GLU A C   1 
ATOM   1092 O O   . GLU A 1 141 ? -7.76949  -44.23660 -7.13236  1.000 33.01000  ? 141  GLU A O   1 
ATOM   1093 C CB  . GLU A 1 141 ? -7.57061  -41.75789 -8.90051  1.000 42.73000  ? 141  GLU A CB  1 
ATOM   1094 C CG  . GLU A 1 141 ? -7.42293  -40.47128 -8.05950  1.000 50.93000  ? 141  GLU A CG  1 
ATOM   1095 C CD  . GLU A 1 141 ? -7.59335  -40.64015 -6.53383  1.000 59.20000  ? 141  GLU A CD  1 
ATOM   1096 O OE1 . GLU A 1 141 ? -7.87375  -41.75559 -6.02444  1.000 59.57000  ? 141  GLU A OE1 1 
ATOM   1097 O OE2 . GLU A 1 141 ? -7.45127  -39.61361 -5.83172  1.000 69.58000  ? 141  GLU A OE2 1 
ATOM   1098 N N   . ASP A 1 142 ? -7.20631  -45.16958 -9.09884  1.000 31.66000  ? 142  ASP A N   1 
ATOM   1099 C CA  . ASP A 1 142 ? -7.53329  -46.52435 -8.67074  1.000 32.35000  ? 142  ASP A CA  1 
ATOM   1100 C C   . ASP A 1 142 ? -6.31534  -47.24963 -8.10503  1.000 33.70000  ? 142  ASP A C   1 
ATOM   1101 O O   . ASP A 1 142 ? -6.39808  -48.44896 -7.80957  1.000 32.72000  ? 142  ASP A O   1 
ATOM   1102 C CB  . ASP A 1 142 ? -8.14855  -47.33084 -9.82094  1.000 33.87000  ? 142  ASP A CB  1 
ATOM   1103 C CG  . ASP A 1 142 ? -7.33083  -47.26103 -11.10151 1.000 37.77000  ? 142  ASP A CG  1 
ATOM   1104 O OD1 . ASP A 1 142 ? -6.09489  -47.10598 -11.01515 1.000 39.38000  ? 142  ASP A OD1 1 
ATOM   1105 O OD2 . ASP A 1 142 ? -7.92879  -47.36469 -12.19826 1.000 37.34000  ? 142  ASP A OD2 1 
ATOM   1106 N N   . HIS A 1 143 ? -5.18844  -46.54282 -7.96031  1.000 31.07000  ? 143  HIS A N   1 
ATOM   1107 C CA  . HIS A 1 143 ? -3.95734  -47.04574 -7.34941  1.000 31.74000  ? 143  HIS A CA  1 
ATOM   1108 C C   . HIS A 1 143 ? -3.33481  -48.17835 -8.14663  1.000 29.52000  ? 143  HIS A C   1 
ATOM   1109 O O   . HIS A 1 143 ? -2.54966  -48.96913 -7.61012  1.000 27.51000  ? 143  HIS A O   1 
ATOM   1110 C CB  . HIS A 1 143 ? -4.19999  -47.45319 -5.89527  1.000 33.19000  ? 143  HIS A CB  1 
ATOM   1111 C CG  . HIS A 1 143 ? -5.05361  -46.47424 -5.15637  1.000 30.47000  ? 143  HIS A CG  1 
ATOM   1112 N ND1 . HIS A 1 143 ? -4.73927  -45.13432 -5.07217  1.000 30.27000  ? 143  HIS A ND1 1 
ATOM   1113 C CD2 . HIS A 1 143 ? -6.24006  -46.62351 -4.52228  1.000 30.68000  ? 143  HIS A CD2 1 
ATOM   1114 C CE1 . HIS A 1 143 ? -5.68328  -44.50422 -4.39562  1.000 31.82000  ? 143  HIS A CE1 1 
ATOM   1115 N NE2 . HIS A 1 143 ? -6.60490  -45.38558 -4.04858  1.000 32.53000  ? 143  HIS A NE2 1 
ATOM   1116 N N   . LEU A 1 144 ? -3.69230  -48.26728 -9.42004  1.000 27.18000  ? 144  LEU A N   1 
ATOM   1117 C CA  . LEU A 1 144 ? -2.88977  -48.95897 -10.40986 1.000 27.41000  ? 144  LEU A CA  1 
ATOM   1118 C C   . LEU A 1 144 ? -1.78693  -48.01192 -10.89824 1.000 30.05000  ? 144  LEU A C   1 
ATOM   1119 O O   . LEU A 1 144 ? -1.53557  -46.95535 -10.30601 1.000 33.41000  ? 144  LEU A O   1 
ATOM   1120 C CB  . LEU A 1 144 ? -3.78857  -49.44649 -11.56432 1.000 28.15000  ? 144  LEU A CB  1 
ATOM   1121 C CG  . LEU A 1 144 ? -4.86767  -50.46217 -11.16352 1.000 28.81000  ? 144  LEU A CG  1 
ATOM   1122 C CD1 . LEU A 1 144 ? -5.83798  -50.71899 -12.30183 1.000 30.57000  ? 144  LEU A CD1 1 
ATOM   1123 C CD2 . LEU A 1 144 ? -4.24533  -51.77340 -10.69308 1.000 30.65000  ? 144  LEU A CD2 1 
ATOM   1124 N N   . PHE A 1 145 ? -1.13790  -48.38137 -12.00300 1.000 26.51000  ? 145  PHE A N   1 
ATOM   1125 C CA  . PHE A 1 145 ? -0.04249  -47.58526 -12.53775 1.000 28.57000  ? 145  PHE A CA  1 
ATOM   1126 C C   . PHE A 1 145 ? -0.16647  -47.36366 -14.04240 1.000 30.03000  ? 145  PHE A C   1 
ATOM   1127 O O   . PHE A 1 145 ? -0.91562  -48.03780 -14.75462 1.000 29.92000  ? 145  PHE A O   1 
ATOM   1128 C CB  . PHE A 1 145 ? 1.30809   -48.23732 -12.20361 1.000 27.56000  ? 145  PHE A CB  1 
ATOM   1129 C CG  . PHE A 1 145 ? 1.57366   -48.36157 -10.72945 1.000 24.73000  ? 145  PHE A CG  1 
ATOM   1130 C CD1 . PHE A 1 145 ? 2.14398   -47.32056 -10.01827 1.000 26.32000  ? 145  PHE A CD1 1 
ATOM   1131 C CD2 . PHE A 1 145 ? 1.22413   -49.51776 -10.04478 1.000 25.28000  ? 145  PHE A CD2 1 
ATOM   1132 C CE1 . PHE A 1 145 ? 2.38945   -47.43593 -8.65174  1.000 24.70000  ? 145  PHE A CE1 1 
ATOM   1133 C CE2 . PHE A 1 145 ? 1.46055   -49.64880 -8.69117  1.000 24.52000  ? 145  PHE A CE2 1 
ATOM   1134 C CZ  . PHE A 1 145 ? 2.04339   -48.60447 -7.98624  1.000 26.17000  ? 145  PHE A CZ  1 
ATOM   1135 N N   . ARG A 1 146 ? 0.60200   -46.38144 -14.50515 1.000 30.11000  ? 146  ARG A N   1 
ATOM   1136 C CA  . ARG A 1 146 ? 0.65142   -45.96280 -15.89445 1.000 32.59000  ? 146  ARG A CA  1 
ATOM   1137 C C   . ARG A 1 146 ? 2.11376   -45.72871 -16.24939 1.000 31.79000  ? 146  ARG A C   1 
ATOM   1138 O O   . ARG A 1 146 ? 2.92180   -45.37675 -15.38681 1.000 30.15000  ? 146  ARG A O   1 
ATOM   1139 C CB  . ARG A 1 146 ? -0.20220  -44.70136 -16.10699 1.000 38.40000  ? 146  ARG A CB  1 
ATOM   1140 C CG  . ARG A 1 146 ? -0.17303  -44.12161 -17.50054 1.000 46.03000  ? 146  ARG A CG  1 
ATOM   1141 C CD  . ARG A 1 146 ? -0.86013  -42.76116 -17.54712 1.000 54.24000  ? 146  ARG A CD  1 
ATOM   1142 N NE  . ARG A 1 146 ? -2.31194  -42.88175 -17.64521 1.000 61.30000  ? 146  ARG A NE  1 
ATOM   1143 C CZ  . ARG A 1 146 ? -3.10689  -41.99447 -18.23172 1.000 64.26000  ? 146  ARG A CZ  1 
ATOM   1144 N NH1 . ARG A 1 146 ? -2.62567  -40.89485 -18.78941 1.000 62.65000  ? 146  ARG A NH1 1 
ATOM   1145 N NH2 . ARG A 1 146 ? -4.41953  -42.21259 -18.25285 1.000 57.12000  ? 146  ARG A NH2 1 
ATOM   1146 N N   . LYS A 1 147 ? 2.46351   -45.96082 -17.51080 1.000 30.65000  ? 147  LYS A N   1 
ATOM   1147 C CA  . LYS A 1 147 ? 3.85359   -45.85286 -17.92485 1.000 29.39000  ? 147  LYS A CA  1 
ATOM   1148 C C   . LYS A 1 147 ? 3.91001   -45.48887 -19.39715 1.000 29.19000  ? 147  LYS A C   1 
ATOM   1149 O O   . LYS A 1 147 ? 3.06113   -45.91993 -20.18190 1.000 28.04000  ? 147  LYS A O   1 
ATOM   1150 C CB  . LYS A 1 147 ? 4.61481   -47.16111 -17.68338 1.000 30.07000  ? 147  LYS A CB  1 
ATOM   1151 C CG  . LYS A 1 147 ? 6.12773   -47.00778 -17.64258 1.000 30.22000  ? 147  LYS A CG  1 
ATOM   1152 C CD  . LYS A 1 147 ? 6.78655   -48.30597 -17.19066 1.000 30.29000  ? 147  LYS A CD  1 
ATOM   1153 C CE  . LYS A 1 147 ? 8.15094   -48.06604 -16.57290 1.000 30.38000  ? 147  LYS A CE  1 
ATOM   1154 N NZ  . LYS A 1 147 ? 9.06484   -47.40929 -17.54403 1.000 33.40000  ? 147  LYS A NZ  1 
ATOM   1155 N N   . PHE A 1 148 ? 4.91777   -44.70093 -19.76081 1.000 27.29000  ? 148  PHE A N   1 
ATOM   1156 C CA  . PHE A 1 148 ? 5.15002   -44.29369 -21.13664 1.000 26.71000  ? 148  PHE A CA  1 
ATOM   1157 C C   . PHE A 1 148 ? 6.52315   -44.75633 -21.59187 1.000 29.55000  ? 148  PHE A C   1 
ATOM   1158 O O   . PHE A 1 148 ? 7.51133   -44.60087 -20.87120 1.000 30.61000  ? 148  PHE A O   1 
ATOM   1159 C CB  . PHE A 1 148 ? 5.05994   -42.77589 -21.29993 1.000 29.25000  ? 148  PHE A CB  1 
ATOM   1160 C CG  . PHE A 1 148 ? 3.70774   -42.21803 -21.01287 1.000 28.37000  ? 148  PHE A CG  1 
ATOM   1161 C CD1 . PHE A 1 148 ? 3.32904   -41.91618 -19.71353 1.000 27.80000  ? 148  PHE A CD1 1 
ATOM   1162 C CD2 . PHE A 1 148 ? 2.81050   -41.98690 -22.04595 1.000 30.32000  ? 148  PHE A CD2 1 
ATOM   1163 C CE1 . PHE A 1 148 ? 2.07974   -41.39775 -19.44939 1.000 28.93000  ? 148  PHE A CE1 1 
ATOM   1164 C CE2 . PHE A 1 148 ? 1.55017   -41.47050 -21.79011 1.000 31.30000  ? 148  PHE A CE2 1 
ATOM   1165 C CZ  . PHE A 1 148 ? 1.18573   -41.17231 -20.48960 1.000 30.63000  ? 148  PHE A CZ  1 
ATOM   1166 N N   . HIS A 1 149 ? 6.57496   -45.30727 -22.79828 1.000 30.82000  ? 149  HIS A N   1 
ATOM   1167 C CA  . HIS A 1 149 ? 7.81844   -45.58277 -23.50053 1.000 32.05000  ? 149  HIS A CA  1 
ATOM   1168 C C   . HIS A 1 149 ? 7.79136   -44.83206 -24.82129 1.000 31.74000  ? 149  HIS A C   1 
ATOM   1169 O O   . HIS A 1 149 ? 6.74964   -44.75977 -25.48257 1.000 27.46000  ? 149  HIS A O   1 
ATOM   1170 C CB  . HIS A 1 149 ? 8.00905   -47.08049 -23.73490 1.000 35.43000  ? 149  HIS A CB  1 
ATOM   1171 C CG  . HIS A 1 149 ? 8.55257   -47.80701 -22.54440 1.000 38.88000  ? 149  HIS A CG  1 
ATOM   1172 N ND1 . HIS A 1 149 ? 7.81249   -48.01231 -21.39799 1.000 38.73000  ? 149  HIS A ND1 1 
ATOM   1173 C CD2 . HIS A 1 149 ? 9.75801   -48.38116 -22.32162 1.000 45.06000  ? 149  HIS A CD2 1 
ATOM   1174 C CE1 . HIS A 1 149 ? 8.54172   -48.67495 -20.51803 1.000 45.14000  ? 149  HIS A CE1 1 
ATOM   1175 N NE2 . HIS A 1 149 ? 9.72586   -48.91149 -21.05442 1.000 43.48000  ? 149  HIS A NE2 1 
ATOM   1176 N N   . TYR A 1 150 ? 8.92838   -44.24939 -25.18637 1.000 30.25000  ? 150  TYR A N   1 
ATOM   1177 C CA  . TYR A 1 150 ? 9.02825   -43.40857 -26.36748 1.000 31.19000  ? 150  TYR A CA  1 
ATOM   1178 C C   . TYR A 1 150 ? 10.08065  -43.95243 -27.31760 1.000 32.29000  ? 150  TYR A C   1 
ATOM   1179 O O   . TYR A 1 150 ? 11.09854  -44.50559 -26.89133 1.000 30.74000  ? 150  TYR A O   1 
ATOM   1180 C CB  . TYR A 1 150 ? 9.38586   -41.97204 -26.00658 1.000 31.37000  ? 150  TYR A CB  1 
ATOM   1181 C CG  . TYR A 1 150 ? 8.50231   -41.35255 -24.95734 1.000 35.04000  ? 150  TYR A CG  1 
ATOM   1182 C CD1 . TYR A 1 150 ? 7.25507   -40.83931 -25.29071 1.000 36.14000  ? 150  TYR A CD1 1 
ATOM   1183 C CD2 . TYR A 1 150 ? 8.92133   -41.26030 -23.63387 1.000 33.77000  ? 150  TYR A CD2 1 
ATOM   1184 C CE1 . TYR A 1 150 ? 6.44914   -40.25490 -24.33687 1.000 33.41000  ? 150  TYR A CE1 1 
ATOM   1185 C CE2 . TYR A 1 150 ? 8.12273   -40.68046 -22.67525 1.000 33.82000  ? 150  TYR A CE2 1 
ATOM   1186 C CZ  . TYR A 1 150 ? 6.88812   -40.17927 -23.03142 1.000 35.02000  ? 150  TYR A CZ  1 
ATOM   1187 O OH  . TYR A 1 150 ? 6.08285   -39.59928 -22.07971 1.000 33.06000  ? 150  TYR A OH  1 
ATOM   1188 N N   . LEU A 1 151 ? 9.82411   -43.78083 -28.61271 1.000 33.56000  ? 151  LEU A N   1 
ATOM   1189 C CA  . LEU A 1 151 ? 10.76803  -44.18321 -29.64629 1.000 37.39000  ? 151  LEU A CA  1 
ATOM   1190 C C   . LEU A 1 151 ? 10.80801  -43.12966 -30.74830 1.000 37.20000  ? 151  LEU A C   1 
ATOM   1191 O O   . LEU A 1 151 ? 9.85327   -43.00872 -31.53097 1.000 36.27000  ? 151  LEU A O   1 
ATOM   1192 C CB  . LEU A 1 151 ? 10.39985  -45.55377 -30.22165 1.000 39.58000  ? 151  LEU A CB  1 
ATOM   1193 C CG  . LEU A 1 151 ? 11.18250  -46.00203 -31.46379 1.000 40.41000  ? 151  LEU A CG  1 
ATOM   1194 C CD1 . LEU A 1 151 ? 12.64376  -46.23090 -31.12676 1.000 41.15000  ? 151  LEU A CD1 1 
ATOM   1195 C CD2 . LEU A 1 151 ? 10.58445  -47.26076 -32.05785 1.000 40.51000  ? 151  LEU A CD2 1 
ATOM   1196 N N   . PRO A 1 152 ? 11.87838  -42.33642 -30.82663 1.000 38.72000  ? 152  PRO A N   1 
ATOM   1197 C CA  . PRO A 1 152 ? 12.02159  -41.40610 -31.95039 1.000 40.24000  ? 152  PRO A CA  1 
ATOM   1198 C C   . PRO A 1 152 ? 12.32828  -42.17866 -33.22242 1.000 40.70000  ? 152  PRO A C   1 
ATOM   1199 O O   . PRO A 1 152 ? 13.08600  -43.15333 -33.20809 1.000 41.81000  ? 152  PRO A O   1 
ATOM   1200 C CB  . PRO A 1 152 ? 13.20368  -40.51806 -31.53771 1.000 40.39000  ? 152  PRO A CB  1 
ATOM   1201 C CG  . PRO A 1 152 ? 13.49063  -40.86034 -30.10451 1.000 41.87000  ? 152  PRO A CG  1 
ATOM   1202 C CD  . PRO A 1 152 ? 13.02590  -42.26296 -29.91265 1.000 41.32000  ? 152  PRO A CD  1 
ATOM   1203 N N   . PHE A 1 153 ? 11.73245  -41.73957 -34.32780 1.000 42.60000  ? 153  PHE A N   1 
ATOM   1204 C CA  . PHE A 1 153 ? 11.83898  -42.49558 -35.56536 1.000 43.28000  ? 153  PHE A CA  1 
ATOM   1205 C C   . PHE A 1 153 ? 11.59602  -41.57056 -36.74729 1.000 40.88000  ? 153  PHE A C   1 
ATOM   1206 O O   . PHE A 1 153 ? 11.03073  -40.48377 -36.60613 1.000 42.20000  ? 153  PHE A O   1 
ATOM   1207 C CB  . PHE A 1 153 ? 10.85677  -43.67705 -35.57565 1.000 42.75000  ? 153  PHE A CB  1 
ATOM   1208 C CG  . PHE A 1 153 ? 9.42947   -43.28375 -35.82717 1.000 40.86000  ? 153  PHE A CG  1 
ATOM   1209 C CD1 . PHE A 1 153 ? 8.73010   -42.52455 -34.90009 1.000 40.51000  ? 153  PHE A CD1 1 
ATOM   1210 C CD2 . PHE A 1 153 ? 8.78496   -43.67936 -36.98877 1.000 37.25000  ? 153  PHE A CD2 1 
ATOM   1211 C CE1 . PHE A 1 153 ? 7.41061   -42.16096 -35.12828 1.000 39.57000  ? 153  PHE A CE1 1 
ATOM   1212 C CE2 . PHE A 1 153 ? 7.46759   -43.32165 -37.22866 1.000 40.12000  ? 153  PHE A CE2 1 
ATOM   1213 C CZ  . PHE A 1 153 ? 6.77758   -42.55970 -36.29687 1.000 39.20000  ? 153  PHE A CZ  1 
ATOM   1214 N N   . LEU A 1 154 ? 12.05118  -42.01595 -37.91859 1.000 46.84000  ? 154  LEU A N   1 
ATOM   1215 C CA  . LEU A 1 154 ? 11.77461  -41.32122 -39.16628 1.000 49.34000  ? 154  LEU A CA  1 
ATOM   1216 C C   . LEU A 1 154 ? 10.69055  -42.07368 -39.91849 1.000 46.20000  ? 154  LEU A C   1 
ATOM   1217 O O   . LEU A 1 154 ? 10.92178  -43.22209 -40.32838 1.000 42.16000  ? 154  LEU A O   1 
ATOM   1218 C CB  . LEU A 1 154 ? 13.03445  -41.21452 -40.01571 1.000 56.79000  ? 154  LEU A CB  1 
ATOM   1219 C CG  . LEU A 1 154 ? 13.75577  -39.86634 -39.98472 1.000 60.98000  ? 154  LEU A CG  1 
ATOM   1220 C CD1 . LEU A 1 154 ? 14.70851  -39.75813 -41.15244 1.000 65.28000  ? 154  LEU A CD1 1 
ATOM   1221 C CD2 . LEU A 1 154 ? 12.75980  -38.71998 -40.00920 1.000 62.74000  ? 154  LEU A CD2 1 
ATOM   1222 N N   . PRO A 1 155 ? 9.50907   -41.48949 -40.11535 1.000 48.46000  ? 155  PRO A N   1 
ATOM   1223 C CA  . PRO A 1 155 ? 8.40901   -42.24153 -40.72605 1.000 49.66000  ? 155  PRO A CA  1 
ATOM   1224 C C   . PRO A 1 155 ? 8.69339   -42.57450 -42.18023 1.000 53.82000  ? 155  PRO A C   1 
ATOM   1225 O O   . PRO A 1 155 ? 9.25395   -41.77019 -42.92904 1.000 54.00000  ? 155  PRO A O   1 
ATOM   1226 C CB  . PRO A 1 155 ? 7.21253   -41.28853 -40.60332 1.000 47.92000  ? 155  PRO A CB  1 
ATOM   1227 C CG  . PRO A 1 155 ? 7.61262   -40.29075 -39.56872 1.000 45.78000  ? 155  PRO A CG  1 
ATOM   1228 C CD  . PRO A 1 155 ? 9.09239   -40.12924 -39.75030 1.000 44.79000  ? 155  PRO A CD  1 
ATOM   1229 N N   . SER A 1 156 ? 8.28674   -43.77632 -42.57216 1.000 53.60000  ? 156  SER A N   1 
ATOM   1230 C CA  . SER A 1 156 ? 8.40338   -44.22774 -43.94758 1.000 60.44000  ? 156  SER A CA  1 
ATOM   1231 C C   . SER A 1 156 ? 7.40784   -45.35545 -44.15655 1.000 63.75000  ? 156  SER A C   1 
ATOM   1232 O O   . SER A 1 156 ? 7.10082   -46.10591 -43.22654 1.000 58.82000  ? 156  SER A O   1 
ATOM   1233 C CB  . SER A 1 156 ? 9.82441   -44.69855 -44.26488 1.000 56.65000  ? 156  SER A CB  1 
ATOM   1234 O OG  . SER A 1 156 ? 10.17532  -45.79664 -43.44448 1.000 54.74000  ? 156  SER A OG  1 
ATOM   1235 N N   . THR A 1 157 ? 6.89899   -45.46054 -45.38429 1.000 68.55000  ? 157  THR A N   1 
ATOM   1236 C CA  . THR A 1 157 ? 6.01757   -46.56874 -45.72919 1.000 72.23000  ? 157  THR A CA  1 
ATOM   1237 C C   . THR A 1 157 ? 6.73600   -47.91068 -45.70625 1.000 69.79000  ? 157  THR A C   1 
ATOM   1238 O O   . THR A 1 157 ? 6.07388   -48.95310 -45.76564 1.000 65.83000  ? 157  THR A O   1 
ATOM   1239 C CB  . THR A 1 157 ? 5.39920   -46.33032 -47.10583 1.000 78.56000  ? 157  THR A CB  1 
ATOM   1240 O OG1 . THR A 1 157 ? 6.42669   -45.93903 -48.02643 1.000 77.28000  ? 157  THR A OG1 1 
ATOM   1241 C CG2 . THR A 1 157 ? 4.34700   -45.23483 -47.03137 1.000 74.59000  ? 157  THR A CG2 1 
ATOM   1242 N N   . GLU A 1 158 ? 8.06667   -47.90467 -45.60494 1.000 72.17000  ? 158  GLU A N   1 
ATOM   1243 C CA  . GLU A 1 158 ? 8.82385   -49.14986 -45.59494 1.000 75.58000  ? 158  GLU A CA  1 
ATOM   1244 C C   . GLU A 1 158 ? 8.71762   -49.86490 -44.25024 1.000 75.84000  ? 158  GLU A C   1 
ATOM   1245 O O   . GLU A 1 158 ? 8.66610   -51.09943 -44.20283 1.000 75.64000  ? 158  GLU A O   1 
ATOM   1246 C CB  . GLU A 1 158 ? 10.28705  -48.86397 -45.93878 1.000 71.62000  ? 158  GLU A CB  1 
ATOM   1247 N N   . ASP A 1 159 ? 8.66899   -49.11435 -43.15156 1.000 74.82000  ? 159  ASP A N   1 
ATOM   1248 C CA  . ASP A 1 159 ? 8.83505   -49.67258 -41.81688 1.000 66.85000  ? 159  ASP A CA  1 
ATOM   1249 C C   . ASP A 1 159 ? 7.50310   -49.89771 -41.10939 1.000 62.93000  ? 159  ASP A C   1 
ATOM   1250 O O   . ASP A 1 159 ? 6.54461   -49.14075 -41.28384 1.000 65.41000  ? 159  ASP A O   1 
ATOM   1251 C CB  . ASP A 1 159 ? 9.71070   -48.75564 -40.96565 1.000 67.01000  ? 159  ASP A CB  1 
ATOM   1252 C CG  . ASP A 1 159 ? 11.14088  -48.72627 -41.43868 1.000 72.16000  ? 159  ASP A CG  1 
ATOM   1253 O OD1 . ASP A 1 159 ? 11.87461  -47.79107 -41.05820 1.000 75.05000  ? 159  ASP A OD1 1 
ATOM   1254 O OD2 . ASP A 1 159 ? 11.53180  -49.64432 -42.18912 1.000 77.24000  ? 159  ASP A OD2 1 
ATOM   1255 N N   . VAL A 1 160 ? 7.45990   -50.95954 -40.30337 1.000 58.19000  ? 160  VAL A N   1 
ATOM   1256 C CA  . VAL A 1 160 ? 6.37833   -51.20995 -39.35849 1.000 56.43000  ? 160  VAL A CA  1 
ATOM   1257 C C   . VAL A 1 160 ? 6.98679   -51.34987 -37.96787 1.000 51.04000  ? 160  VAL A C   1 
ATOM   1258 O O   . VAL A 1 160 ? 8.14922   -51.74166 -37.81196 1.000 48.49000  ? 160  VAL A O   1 
ATOM   1259 C CB  . VAL A 1 160 ? 5.54125   -52.45900 -39.72415 1.000 59.40000  ? 160  VAL A CB  1 
ATOM   1260 C CG1 . VAL A 1 160 ? 5.25945   -52.49540 -41.21553 1.000 62.41000  ? 160  VAL A CG1 1 
ATOM   1261 C CG2 . VAL A 1 160 ? 6.24116   -53.73167 -39.27795 1.000 61.00000  ? 160  VAL A CG2 1 
ATOM   1262 N N   . TYR A 1 161 ? 6.19702   -51.01253 -36.94995 1.000 49.44000  ? 161  TYR A N   1 
ATOM   1263 C CA  . TYR A 1 161 ? 6.69221   -50.95982 -35.58169 1.000 47.32000  ? 161  TYR A CA  1 
ATOM   1264 C C   . TYR A 1 161 ? 5.75101   -51.68823 -34.63419 1.000 45.28000  ? 161  TYR A C   1 
ATOM   1265 O O   . TYR A 1 161 ? 4.53259   -51.71597 -34.83378 1.000 50.62000  ? 161  TYR A O   1 
ATOM   1266 C CB  . TYR A 1 161 ? 6.86311   -49.52074 -35.09934 1.000 41.98000  ? 161  TYR A CB  1 
ATOM   1267 C CG  . TYR A 1 161 ? 7.96594   -48.76016 -35.78853 1.000 40.19000  ? 161  TYR A CG  1 
ATOM   1268 C CD1 . TYR A 1 161 ? 7.73304   -48.09403 -36.98389 1.000 39.89000  ? 161  TYR A CD1 1 
ATOM   1269 C CD2 . TYR A 1 161 ? 9.24210   -48.69822 -35.24042 1.000 39.99000  ? 161  TYR A CD2 1 
ATOM   1270 C CE1 . TYR A 1 161 ? 8.74190   -47.38862 -37.61636 1.000 40.55000  ? 161  TYR A CE1 1 
ATOM   1271 C CE2 . TYR A 1 161 ? 10.25717  -47.99119 -35.86503 1.000 40.07000  ? 161  TYR A CE2 1 
ATOM   1272 C CZ  . TYR A 1 161 ? 10.00117  -47.33981 -37.05090 1.000 40.94000  ? 161  TYR A CZ  1 
ATOM   1273 O OH  . TYR A 1 161 ? 11.00187  -46.63805 -37.68000 1.000 43.41000  ? 161  TYR A OH  1 
ATOM   1274 N N   . ASP A 1 162 ? 6.33392   -52.26535 -33.58760 1.000 42.96000  ? 162  ASP A N   1 
ATOM   1275 C CA  . ASP A 1 162 ? 5.58106   -52.93609 -32.54245 1.000 47.58000  ? 162  ASP A CA  1 
ATOM   1276 C C   . ASP A 1 162 ? 6.08830   -52.48854 -31.18198 1.000 47.06000  ? 162  ASP A C   1 
ATOM   1277 O O   . ASP A 1 162 ? 7.28071   -52.22731 -30.99722 1.000 46.20000  ? 162  ASP A O   1 
ATOM   1278 C CB  . ASP A 1 162 ? 5.69444   -54.46259 -32.64270 1.000 51.20000  ? 162  ASP A CB  1 
ATOM   1279 C CG  . ASP A 1 162 ? 4.97487   -55.02191 -33.84699 1.000 54.41000  ? 162  ASP A CG  1 
ATOM   1280 O OD1 . ASP A 1 162 ? 3.75334   -54.78793 -33.97959 1.000 56.67000  ? 162  ASP A OD1 1 
ATOM   1281 O OD2 . ASP A 1 162 ? 5.64234   -55.68105 -34.67322 1.000 56.40000  ? 162  ASP A OD2 1 
ATOM   1282 N N   . CYS A 1 163 ? 5.16759   -52.40310 -30.23181 1.000 46.65000  ? 163  CYS A N   1 
ATOM   1283 C CA  . CYS A 1 163 ? 5.50363   -52.24647 -28.82512 1.000 45.64000  ? 163  CYS A CA  1 
ATOM   1284 C C   . CYS A 1 163 ? 5.21888   -53.57700 -28.14276 1.000 44.97000  ? 163  CYS A C   1 
ATOM   1285 O O   . CYS A 1 163 ? 4.05634   -53.95762 -27.96827 1.000 49.08000  ? 163  CYS A O   1 
ATOM   1286 C CB  . CYS A 1 163 ? 4.71096   -51.11218 -28.18448 1.000 47.54000  ? 163  CYS A CB  1 
ATOM   1287 S SG  . CYS A 1 163 ? 5.18814   -50.79638 -26.47650 1.000 50.87000  ? 163  CYS A SG  1 
ATOM   1288 N N   . ARG A 1 164 ? 6.27516   -54.29014 -27.77943 1.000 44.42000  ? 164  ARG A N   1 
ATOM   1289 C CA  . ARG A 1 164 ? 6.14377   -55.55798 -27.07960 1.000 45.74000  ? 164  ARG A CA  1 
ATOM   1290 C C   . ARG A 1 164 ? 6.10585   -55.29430 -25.57906 1.000 43.41000  ? 164  ARG A C   1 
ATOM   1291 O O   . ARG A 1 164 ? 7.06157   -54.75129 -25.01365 1.000 41.89000  ? 164  ARG A O   1 
ATOM   1292 C CB  . ARG A 1 164 ? 7.29723   -56.48921 -27.44113 1.000 49.85000  ? 164  ARG A CB  1 
ATOM   1293 C CG  . ARG A 1 164 ? 7.15800   -57.89138 -26.89148 1.000 51.57000  ? 164  ARG A CG  1 
ATOM   1294 C CD  . ARG A 1 164 ? 8.05655   -58.84901 -27.65193 1.000 58.03000  ? 164  ARG A CD  1 
ATOM   1295 N NE  . ARG A 1 164 ? 7.91314   -60.21511 -27.16941 1.000 65.23000  ? 164  ARG A NE  1 
ATOM   1296 C CZ  . ARG A 1 164 ? 8.63045   -60.73775 -26.18552 1.000 74.96000  ? 164  ARG A CZ  1 
ATOM   1297 N NH1 . ARG A 1 164 ? 9.57198   -60.04043 -25.57084 1.000 84.11000  ? 164  ARG A NH1 1 
ATOM   1298 N NH2 . ARG A 1 164 ? 8.39388   -61.98953 -25.80352 1.000 72.52000  ? 164  ARG A NH2 1 
ATOM   1299 N N   . VAL A 1 165 ? 5.00309   -55.67374 -24.94082 1.000 38.46000  ? 165  VAL A N   1 
ATOM   1300 C CA  . VAL A 1 165 ? 4.80850   -55.49137 -23.51009 1.000 39.58000  ? 165  VAL A CA  1 
ATOM   1301 C C   . VAL A 1 165 ? 4.65336   -56.86015 -22.86703 1.000 40.21000  ? 165  VAL A C   1 
ATOM   1302 O O   . VAL A 1 165 ? 3.83344   -57.67256 -23.31211 1.000 38.41000  ? 165  VAL A O   1 
ATOM   1303 C CB  . VAL A 1 165 ? 3.58130   -54.60998 -23.21957 1.000 39.74000  ? 165  VAL A CB  1 
ATOM   1304 C CG1 . VAL A 1 165 ? 3.37839   -54.45526 -21.72246 1.000 39.96000  ? 165  VAL A CG1 1 
ATOM   1305 C CG2 . VAL A 1 165 ? 3.73397   -53.25063 -23.89272 1.000 39.39000  ? 165  VAL A CG2 1 
ATOM   1306 N N   . GLU A 1 166 ? 5.43738   -57.11282 -21.82480 1.000 42.24000  ? 166  GLU A N   1 
ATOM   1307 C CA  . GLU A 1 166 ? 5.33633   -58.33066 -21.03431 1.000 43.54000  ? 166  GLU A CA  1 
ATOM   1308 C C   . GLU A 1 166 ? 4.94390   -57.96337 -19.61270 1.000 40.52000  ? 166  GLU A C   1 
ATOM   1309 O O   . GLU A 1 166 ? 5.53634   -57.05657 -19.01731 1.000 37.98000  ? 166  GLU A O   1 
ATOM   1310 C CB  . GLU A 1 166 ? 6.65534   -59.10391 -21.01630 1.000 50.62000  ? 166  GLU A CB  1 
ATOM   1311 C CG  . GLU A 1 166 ? 6.95635   -59.90268 -22.26548 1.000 57.10000  ? 166  GLU A CG  1 
ATOM   1312 C CD  . GLU A 1 166 ? 8.38255   -60.42665 -22.26637 1.000 68.70000  ? 166  GLU A CD  1 
ATOM   1313 O OE1 . GLU A 1 166 ? 9.02257   -60.43467 -23.33821 1.000 75.24000  ? 166  GLU A OE1 1 
ATOM   1314 O OE2 . GLU A 1 166 ? 8.86997   -60.82132 -21.18443 1.000 78.68000  ? 166  GLU A OE2 1 
ATOM   1315 N N   . HIS A 1 167 ? 3.96322   -58.67885 -19.06624 1.000 38.59000  ? 167  HIS A N   1 
ATOM   1316 C CA  . HIS A 1 167 ? 3.51297   -58.45344 -17.70223 1.000 38.50000  ? 167  HIS A CA  1 
ATOM   1317 C C   . HIS A 1 167 ? 3.00087   -59.77370 -17.14589 1.000 41.13000  ? 167  HIS A C   1 
ATOM   1318 O O   . HIS A 1 167 ? 2.45546   -60.60026 -17.88388 1.000 41.69000  ? 167  HIS A O   1 
ATOM   1319 C CB  . HIS A 1 167 ? 2.42635   -57.36887 -17.65693 1.000 36.52000  ? 167  HIS A CB  1 
ATOM   1320 C CG  . HIS A 1 167 ? 2.13357   -56.84777 -16.28218 1.000 36.61000  ? 167  HIS A CG  1 
ATOM   1321 N ND1 . HIS A 1 167 ? 1.11432   -57.34609 -15.49714 1.000 34.38000  ? 167  HIS A ND1 1 
ATOM   1322 C CD2 . HIS A 1 167 ? 2.71202   -55.85770 -15.56134 1.000 36.45000  ? 167  HIS A CD2 1 
ATOM   1323 C CE1 . HIS A 1 167 ? 1.08543   -56.69399 -14.34862 1.000 33.94000  ? 167  HIS A CE1 1 
ATOM   1324 N NE2 . HIS A 1 167 ? 2.04539   -55.78611 -14.36133 1.000 34.52000  ? 167  HIS A NE2 1 
ATOM   1325 N N   . TRP A 1 168 ? 3.18978   -59.97174 -15.83678 1.000 37.15000  ? 168  TRP A N   1 
ATOM   1326 C CA  . TRP A 1 168 ? 2.75741   -61.22128 -15.21442 1.000 41.45000  ? 168  TRP A CA  1 
ATOM   1327 C C   . TRP A 1 168 ? 1.26152   -61.46209 -15.39703 1.000 43.42000  ? 168  TRP A C   1 
ATOM   1328 O O   . TRP A 1 168 ? 0.83490   -62.61036 -15.56269 1.000 43.64000  ? 168  TRP A O   1 
ATOM   1329 C CB  . TRP A 1 168 ? 3.11708   -61.22468 -13.72923 1.000 40.26000  ? 168  TRP A CB  1 
ATOM   1330 C CG  . TRP A 1 168 ? 4.57776   -61.32925 -13.46785 1.000 43.63000  ? 168  TRP A CG  1 
ATOM   1331 C CD1 . TRP A 1 168 ? 5.42558   -62.28631 -13.93722 1.000 44.99000  ? 168  TRP A CD1 1 
ATOM   1332 C CD2 . TRP A 1 168 ? 5.37285   -60.44439 -12.66950 1.000 49.40000  ? 168  TRP A CD2 1 
ATOM   1333 N NE1 . TRP A 1 168 ? 6.69988   -62.05240 -13.48670 1.000 46.66000  ? 168  TRP A NE1 1 
ATOM   1334 C CE2 . TRP A 1 168 ? 6.69611   -60.92735 -12.70569 1.000 48.25000  ? 168  TRP A CE2 1 
ATOM   1335 C CE3 . TRP A 1 168 ? 5.09526   -59.29003 -11.92883 1.000 50.36000  ? 168  TRP A CE3 1 
ATOM   1336 C CZ2 . TRP A 1 168 ? 7.73995   -60.29642 -12.03017 1.000 50.62000  ? 168  TRP A CZ2 1 
ATOM   1337 C CZ3 . TRP A 1 168 ? 6.13212   -58.66513 -11.26024 1.000 51.45000  ? 168  TRP A CZ3 1 
ATOM   1338 C CH2 . TRP A 1 168 ? 7.43780   -59.16776 -11.31630 1.000 51.08000  ? 168  TRP A CH2 1 
ATOM   1339 N N   . GLY A 1 169 ? 0.45352   -60.40154 -15.38047 1.000 46.12000  ? 169  GLY A N   1 
ATOM   1340 C CA  . GLY A 1 169 ? -0.98579  -60.53555 -15.54667 1.000 47.01000  ? 169  GLY A CA  1 
ATOM   1341 C C   . GLY A 1 169 ? -1.43906  -60.89085 -16.95143 1.000 49.41000  ? 169  GLY A C   1 
ATOM   1342 O O   . GLY A 1 169 ? -2.62452  -61.18806 -17.14072 1.000 50.63000  ? 169  GLY A O   1 
ATOM   1343 N N   . LEU A 1 170 ? -0.54017  -60.86070 -17.93012 1.000 48.37000  ? 170  LEU A N   1 
ATOM   1344 C CA  . LEU A 1 170 ? -0.86788  -61.25099 -19.29249 1.000 54.34000  ? 170  LEU A CA  1 
ATOM   1345 C C   . LEU A 1 170 ? -0.58744  -62.73602 -19.50884 1.000 53.45000  ? 170  LEU A C   1 
ATOM   1346 O O   . LEU A 1 170 ? 0.21162   -63.35601 -18.80222 1.000 56.93000  ? 170  LEU A O   1 
ATOM   1347 C CB  . LEU A 1 170 ? -0.07298  -60.42111 -20.30123 1.000 50.59000  ? 170  LEU A CB  1 
ATOM   1348 C CG  . LEU A 1 170 ? -0.39953  -58.93078 -20.34765 1.000 49.70000  ? 170  LEU A CG  1 
ATOM   1349 C CD1 . LEU A 1 170 ? 0.72159   -58.16711 -21.03009 1.000 46.28000  ? 170  LEU A CD1 1 
ATOM   1350 C CD2 . LEU A 1 170 ? -1.73014  -58.69787 -21.04714 1.000 49.99000  ? 170  LEU A CD2 1 
ATOM   1351 N N   . ASP A 1 171 ? -1.26281  -63.30452 -20.50499 1.000 56.49000  ? 171  ASP A N   1 
ATOM   1352 C CA  . ASP A 1 171 ? -1.05866  -64.70486 -20.85229 1.000 62.69000  ? 171  ASP A CA  1 
ATOM   1353 C C   . ASP A 1 171 ? 0.04544   -64.85922 -21.88833 1.000 63.29000  ? 171  ASP A C   1 
ATOM   1354 O O   . ASP A 1 171 ? 0.95264   -65.67951 -21.72332 1.000 71.76000  ? 171  ASP A O   1 
ATOM   1355 C CB  . ASP A 1 171 ? -2.36613  -65.31394 -21.36445 1.000 62.68000  ? 171  ASP A CB  1 
ATOM   1356 C CG  . ASP A 1 171 ? -3.39414  -65.49247 -20.26243 1.000 62.47000  ? 171  ASP A CG  1 
ATOM   1357 O OD1 . ASP A 1 171 ? -3.00522  -65.89761 -19.14446 1.000 67.64000  ? 171  ASP A OD1 1 
ATOM   1358 O OD2 . ASP A 1 171 ? -4.58983  -65.22670 -20.51313 1.000 59.86000  ? 171  ASP A OD2 1 
ATOM   1359 N N   . GLU A 1 172 ? -0.02420  -64.07621 -22.95548 1.000 65.43000  ? 172  GLU A N   1 
ATOM   1360 C CA  . GLU A 1 172 ? 1.01356   -63.96873 -23.95810 1.000 67.00000  ? 172  GLU A CA  1 
ATOM   1361 C C   . GLU A 1 172 ? 1.54617   -62.53993 -23.96442 1.000 66.77000  ? 172  GLU A C   1 
ATOM   1362 O O   . GLU A 1 172 ? 0.81178   -61.60470 -23.62307 1.000 58.70000  ? 172  GLU A O   1 
ATOM   1363 C CB  . GLU A 1 172 ? 0.47090   -64.33737 -25.34732 1.000 69.33000  ? 172  GLU A CB  1 
ATOM   1364 C CG  . GLU A 1 172 ? 1.52385   -64.77950 -26.35420 1.000 74.15000  ? 172  GLU A CG  1 
ATOM   1365 C CD  . GLU A 1 172 ? 1.73708   -63.76026 -27.46281 1.000 80.92000  ? 172  GLU A CD  1 
ATOM   1366 O OE1 . GLU A 1 172 ? 0.81867   -62.95047 -27.70701 1.000 81.65000  ? 172  GLU A OE1 1 
ATOM   1367 O OE2 . GLU A 1 172 ? 2.82018   -63.76422 -28.08969 1.000 71.50000  ? 172  GLU A OE2 1 
ATOM   1368 N N   . PRO A 1 173 ? 2.82262   -62.34060 -24.29317 1.000 60.53000  ? 173  PRO A N   1 
ATOM   1369 C CA  . PRO A 1 173 ? 3.32847   -60.97470 -24.46232 1.000 56.91000  ? 173  PRO A CA  1 
ATOM   1370 C C   . PRO A 1 173 ? 2.44682   -60.17778 -25.41231 1.000 50.73000  ? 173  PRO A C   1 
ATOM   1371 O O   . PRO A 1 173 ? 1.99378   -60.68063 -26.44039 1.000 53.86000  ? 173  PRO A O   1 
ATOM   1372 C CB  . PRO A 1 173 ? 4.73254   -61.19084 -25.03051 1.000 59.54000  ? 173  PRO A CB  1 
ATOM   1373 C CG  . PRO A 1 173 ? 5.16011   -62.48808 -24.42629 1.000 58.07000  ? 173  PRO A CG  1 
ATOM   1374 C CD  . PRO A 1 173 ? 3.91215   -63.33381 -24.30837 1.000 60.40000  ? 173  PRO A CD  1 
ATOM   1375 N N   . LEU A 1 174 ? 2.18282   -58.93010 -25.04506 1.000 46.91000  ? 174  LEU A N   1 
ATOM   1376 C CA  . LEU A 1 174 ? 1.25417   -58.09057 -25.78520 1.000 47.47000  ? 174  LEU A CA  1 
ATOM   1377 C C   . LEU A 1 174 ? 2.02302   -57.28979 -26.83079 1.000 50.56000  ? 174  LEU A C   1 
ATOM   1378 O O   . LEU A 1 174 ? 3.03746   -56.65951 -26.51465 1.000 54.73000  ? 174  LEU A O   1 
ATOM   1379 C CB  . LEU A 1 174 ? 0.50025   -57.17430 -24.81954 1.000 50.70000  ? 174  LEU A CB  1 
ATOM   1380 C CG  . LEU A 1 174 ? -0.79192  -56.50765 -25.28934 1.000 51.04000  ? 174  LEU A CG  1 
ATOM   1381 C CD1 . LEU A 1 174 ? -1.65264  -56.10412 -24.10938 1.000 55.92000  ? 174  LEU A CD1 1 
ATOM   1382 C CD2 . LEU A 1 174 ? -0.46518  -55.29146 -26.11892 1.000 50.59000  ? 174  LEU A CD2 1 
ATOM   1383 N N   . LEU A 1 175 ? 1.55303   -57.33656 -28.07873 1.000 50.60000  ? 175  LEU A N   1 
ATOM   1384 C CA  . LEU A 1 175 ? 2.17838   -56.62329 -29.19178 1.000 52.11000  ? 175  LEU A CA  1 
ATOM   1385 C C   . LEU A 1 175 ? 1.17666   -55.63162 -29.76570 1.000 48.07000  ? 175  LEU A C   1 
ATOM   1386 O O   . LEU A 1 175 ? 0.13948   -56.03182 -30.30493 1.000 51.32000  ? 175  LEU A O   1 
ATOM   1387 C CB  . LEU A 1 175 ? 2.66094   -57.58117 -30.28152 1.000 53.90000  ? 175  LEU A CB  1 
ATOM   1388 C CG  . LEU A 1 175 ? 3.96502   -58.33907 -30.04027 1.000 58.96000  ? 175  LEU A CG  1 
ATOM   1389 C CD1 . LEU A 1 175 ? 3.83292   -59.33575 -28.89595 1.000 61.87000  ? 175  LEU A CD1 1 
ATOM   1390 C CD2 . LEU A 1 175 ? 4.41636   -59.03134 -31.31392 1.000 61.36000  ? 175  LEU A CD2 1 
ATOM   1391 N N   . LYS A 1 176 ? 1.48540   -54.34429 -29.65443 1.000 47.48000  ? 176  LYS A N   1 
ATOM   1392 C CA  . LYS A 1 176 ? 0.67300   -53.29384 -30.25040 1.000 48.37000  ? 176  LYS A CA  1 
ATOM   1393 C C   . LYS A 1 176 ? 1.36521   -52.78843 -31.50807 1.000 48.54000  ? 176  LYS A C   1 
ATOM   1394 O O   . LYS A 1 176 ? 2.53874   -52.40701 -31.46732 1.000 51.96000  ? 176  LYS A O   1 
ATOM   1395 C CB  . LYS A 1 176 ? 0.43554   -52.15101 -29.26395 1.000 49.51000  ? 176  LYS A CB  1 
ATOM   1396 C CG  . LYS A 1 176 ? -1.03679  -51.86984 -28.97625 1.000 54.56000  ? 176  LYS A CG  1 
ATOM   1397 C CD  . LYS A 1 176 ? -1.76696  -53.12207 -28.51654 1.000 55.03000  ? 176  LYS A CD  1 
ATOM   1398 C CE  . LYS A 1 176 ? -3.25520  -53.09509 -28.83809 1.000 60.10000  ? 176  LYS A CE  1 
ATOM   1399 N NZ  . LYS A 1 176 ? -3.96874  -54.18972 -28.10985 1.000 62.30000  ? 176  LYS A NZ  1 
ATOM   1400 N N   . HIS A 1 177 ? 0.63139   -52.77933 -32.61412 1.000 48.53000  ? 177  HIS A N   1 
ATOM   1401 C CA  . HIS A 1 177 ? 1.19289   -52.57953 -33.94072 1.000 50.64000  ? 177  HIS A CA  1 
ATOM   1402 C C   . HIS A 1 177 ? 0.93204   -51.15884 -34.42849 1.000 51.00000  ? 177  HIS A C   1 
ATOM   1403 O O   . HIS A 1 177 ? -0.11998  -50.57799 -34.14581 1.000 53.79000  ? 177  HIS A O   1 
ATOM   1404 C CB  . HIS A 1 177 ? 0.58722   -53.59544 -34.91367 1.000 51.85000  ? 177  HIS A CB  1 
ATOM   1405 C CG  . HIS A 1 177 ? 1.24039   -53.61599 -36.25850 1.000 52.30000  ? 177  HIS A CG  1 
ATOM   1406 N ND1 . HIS A 1 177 ? 2.40430   -54.31115 -36.50870 1.000 60.06000  ? 177  HIS A ND1 1 
ATOM   1407 C CD2 . HIS A 1 177 ? 0.88911   -53.03399 -37.42901 1.000 58.59000  ? 177  HIS A CD2 1 
ATOM   1408 C CE1 . HIS A 1 177 ? 2.74568   -54.15073 -37.77450 1.000 62.58000  ? 177  HIS A CE1 1 
ATOM   1409 N NE2 . HIS A 1 177 ? 1.84258   -53.38091 -38.35514 1.000 63.69000  ? 177  HIS A NE2 1 
ATOM   1410 N N   . TRP A 1 178 ? 1.89438   -50.60485 -35.16655 1.000 46.17000  ? 178  TRP A N   1 
ATOM   1411 C CA  . TRP A 1 178 ? 1.74917   -49.28747 -35.77338 1.000 47.09000  ? 178  TRP A CA  1 
ATOM   1412 C C   . TRP A 1 178 ? 2.38872   -49.28894 -37.15521 1.000 51.95000  ? 178  TRP A C   1 
ATOM   1413 O O   . TRP A 1 178 ? 3.53033   -49.73288 -37.31187 1.000 53.85000  ? 178  TRP A O   1 
ATOM   1414 C CB  . TRP A 1 178 ? 2.38875   -48.19679 -34.90090 1.000 45.26000  ? 178  TRP A CB  1 
ATOM   1415 C CG  . TRP A 1 178 ? 2.15142   -46.79614 -35.40805 1.000 40.79000  ? 178  TRP A CG  1 
ATOM   1416 C CD1 . TRP A 1 178 ? 1.17991   -45.92737 -34.99437 1.000 40.03000  ? 178  TRP A CD1 1 
ATOM   1417 C CD2 . TRP A 1 178 ? 2.89274   -46.11049 -36.43113 1.000 39.07000  ? 178  TRP A CD2 1 
ATOM   1418 N NE1 . TRP A 1 178 ? 1.27333   -44.74548 -35.69205 1.000 39.43000  ? 178  TRP A NE1 1 
ATOM   1419 C CE2 . TRP A 1 178 ? 2.31449   -44.83164 -36.58006 1.000 38.92000  ? 178  TRP A CE2 1 
ATOM   1420 C CE3 . TRP A 1 178 ? 3.99179   -46.45187 -37.22996 1.000 38.53000  ? 178  TRP A CE3 1 
ATOM   1421 C CZ2 . TRP A 1 178 ? 2.79676   -43.89394 -37.49845 1.000 38.44000  ? 178  TRP A CZ2 1 
ATOM   1422 C CZ3 . TRP A 1 178 ? 4.46921   -45.52135 -38.14074 1.000 36.43000  ? 178  TRP A CZ3 1 
ATOM   1423 C CH2 . TRP A 1 178 ? 3.86992   -44.25755 -38.26866 1.000 37.47000  ? 178  TRP A CH2 1 
ATOM   1424 N N   . GLU A 1 179 ? 1.65509   -48.78856 -38.14701 1.000 54.31000  ? 179  GLU A N   1 
ATOM   1425 C CA  . GLU A 1 179 ? 2.14728   -48.56464 -39.50281 1.000 58.32000  ? 179  GLU A CA  1 
ATOM   1426 C C   . GLU A 1 179 ? 1.92684   -47.10332 -39.88209 1.000 59.68000  ? 179  GLU A C   1 
ATOM   1427 O O   . GLU A 1 179 ? 1.32258   -46.33088 -39.13381 1.000 60.05000  ? 179  GLU A O   1 
ATOM   1428 C CB  . GLU A 1 179 ? 1.45604   -49.48901 -40.50912 1.000 64.07000  ? 179  GLU A CB  1 
ATOM   1429 C CG  . GLU A 1 179 ? 1.95754   -50.92088 -40.50249 1.000 74.67000  ? 179  GLU A CG  1 
ATOM   1430 C CD  . GLU A 1 179 ? 1.01222   -51.87261 -41.21543 1.000 77.84000  ? 179  GLU A CD  1 
ATOM   1431 O OE1 . GLU A 1 179 ? 0.52545   -51.52064 -42.31245 1.000 81.58000  ? 179  GLU A OE1 1 
ATOM   1432 O OE2 . GLU A 1 179 ? 0.75002   -52.96917 -40.67502 1.000 82.07000  ? 179  GLU A OE2 1 
ATOM   1433 N N   . PHE A 1 180 ? 2.41149   -46.73414 -41.07207 1.000 62.47000  ? 180  PHE A N   1 
ATOM   1434 C CA  . PHE A 1 180 ? 2.32008   -45.34542 -41.51801 1.000 66.50000  ? 180  PHE A CA  1 
ATOM   1435 C C   . PHE A 1 180 ? 0.88174   -44.84121 -41.49724 1.000 71.08000  ? 180  PHE A C   1 
ATOM   1436 O O   . PHE A 1 180 ? 0.62842   -43.67994 -41.15396 1.000 66.52000  ? 180  PHE A O   1 
ATOM   1437 C CB  . PHE A 1 180 ? 2.91761   -45.20528 -42.91939 1.000 70.46000  ? 180  PHE A CB  1 
ATOM   1438 C CG  . PHE A 1 180 ? 2.87183   -43.80120 -43.46781 1.000 75.37000  ? 180  PHE A CG  1 
ATOM   1439 C CD1 . PHE A 1 180 ? 3.98287   -42.98001 -43.37759 1.000 77.27000  ? 180  PHE A CD1 1 
ATOM   1440 C CD2 . PHE A 1 180 ? 1.73654   -43.31435 -44.10271 1.000 79.06000  ? 180  PHE A CD2 1 
ATOM   1441 C CE1 . PHE A 1 180 ? 3.95758   -41.69154 -43.88086 1.000 78.74000  ? 180  PHE A CE1 1 
ATOM   1442 C CE2 . PHE A 1 180 ? 1.70535   -42.02729 -44.60563 1.000 85.11000  ? 180  PHE A CE2 1 
ATOM   1443 C CZ  . PHE A 1 180 ? 2.81939   -41.21615 -44.49841 1.000 81.96000  ? 180  PHE A CZ  1 
ATOM   1444 N N   . ASP A 1 181 ? -0.07413  -45.69783 -41.85424 1.000 75.00000  ? 181  ASP A N   1 
ATOM   1445 C CA  . ASP A 1 181 ? -1.45987  -45.26924 -42.00092 1.000 76.85000  ? 181  ASP A CA  1 
ATOM   1446 C C   . ASP A 1 181 ? -2.22903  -45.23057 -40.68556 1.000 77.30000  ? 181  ASP A C   1 
ATOM   1447 O O   . ASP A 1 181 ? -3.33998  -44.68966 -40.65760 1.000 86.03000  ? 181  ASP A O   1 
ATOM   1448 C CB  . ASP A 1 181 ? -2.18025  -46.18669 -42.98939 1.000 78.13000  ? 181  ASP A CB  1 
ATOM   1449 C CG  . ASP A 1 181 ? -1.71096  -45.98566 -44.41320 1.000 81.91000  ? 181  ASP A CG  1 
ATOM   1450 O OD1 . ASP A 1 181 ? -1.75682  -44.83548 -44.90184 1.000 83.86000  ? 181  ASP A OD1 1 
ATOM   1451 O OD2 . ASP A 1 181 ? -1.28231  -46.97792 -45.03857 1.000 81.87000  ? 181  ASP A OD2 1 
ATOM   1452 N N   . THR A 1 182 ? -1.67438  -45.77686 -39.60734 1.000 77.51000  ? 182  THR A N   1 
ATOM   1453 C CA  . THR A 1 182 ? -2.36119  -45.81696 -38.31826 1.000 75.66000  ? 182  THR A CA  1 
ATOM   1454 C C   . THR A 1 182 ? -2.55871  -44.42217 -37.73172 1.000 77.35000  ? 182  THR A C   1 
ATOM   1455 O O   . THR A 1 182 ? -1.95634  -43.45338 -38.19423 1.000 74.31000  ? 182  THR A O   1 
ATOM   1456 C CB  . THR A 1 182 ? -1.59149  -46.67611 -37.30287 1.000 74.32000  ? 182  THR A CB  1 
ATOM   1457 O OG1 . THR A 1 182 ? -1.24245  -47.93005 -37.90430 1.000 67.94000  ? 182  THR A OG1 1 
ATOM   1458 C CG2 . THR A 1 182 ? -2.44102  -46.92305 -36.06675 1.000 70.16000  ? 182  THR A CG2 1 
ATOM   1459 N N   . ASP B 2 2   ? 9.65710   -65.24879 -13.76319 1.000 63.92000  ? 2    ASP B N   1 
ATOM   1460 C CA  . ASP B 2 2   ? 9.67820   -65.23776 -12.30400 1.000 65.66000  ? 2    ASP B CA  1 
ATOM   1461 C C   . ASP B 2 2   ? 8.28444   -64.93489 -11.76569 1.000 65.25000  ? 2    ASP B C   1 
ATOM   1462 O O   . ASP B 2 2   ? 7.88911   -63.77485 -11.64259 1.000 71.33000  ? 2    ASP B O   1 
ATOM   1463 C CB  . ASP B 2 2   ? 10.70113  -64.21613 -11.78930 1.000 66.89000  ? 2    ASP B CB  1 
ATOM   1464 C CG  . ASP B 2 2   ? 10.65875  -64.03599 -10.27348 1.000 69.41000  ? 2    ASP B CG  1 
ATOM   1465 O OD1 . ASP B 2 2   ? 10.15749  -64.92649 -9.55417  1.000 70.69000  ? 2    ASP B OD1 1 
ATOM   1466 O OD2 . ASP B 2 2   ? 11.14543  -62.99052 -9.79850  1.000 63.07000  ? 2    ASP B OD2 1 
ATOM   1467 N N   . THR B 2 3   ? 7.54194   -65.99209 -11.44625 1.000 66.84000  ? 3    THR B N   1 
ATOM   1468 C CA  . THR B 2 3   ? 6.18320   -65.87530 -10.92231 1.000 67.12000  ? 3    THR B CA  1 
ATOM   1469 C C   . THR B 2 3   ? 6.15250   -65.91923 -9.39985  1.000 56.12000  ? 3    THR B C   1 
ATOM   1470 O O   . THR B 2 3   ? 5.19323   -66.42589 -8.80890  1.000 50.95000  ? 3    THR B O   1 
ATOM   1471 C CB  . THR B 2 3   ? 5.29225   -66.96937 -11.50700 1.000 30.00000  ? 3    THR B CB  1 
ATOM   1472 N N   . ARG B 2 4   ? 7.19474   -65.40784 -8.74435  1.000 52.17000  ? 4    ARG B N   1 
ATOM   1473 C CA  . ARG B 2 4   ? 7.15998   -65.24185 -7.29996  1.000 53.45000  ? 4    ARG B CA  1 
ATOM   1474 C C   . ARG B 2 4   ? 6.01169   -64.30846 -6.91532  1.000 50.82000  ? 4    ARG B C   1 
ATOM   1475 O O   . ARG B 2 4   ? 5.71616   -63.34699 -7.63320  1.000 48.95000  ? 4    ARG B O   1 
ATOM   1476 C CB  . ARG B 2 4   ? 8.48265   -64.66532 -6.79451  1.000 51.76000  ? 4    ARG B CB  1 
ATOM   1477 C CG  . ARG B 2 4   ? 9.53604   -65.69914 -6.44545  1.000 53.07000  ? 4    ARG B CG  1 
ATOM   1478 C CD  . ARG B 2 4   ? 10.83459  -65.03809 -6.00505  1.000 53.73000  ? 4    ARG B CD  1 
ATOM   1479 N NE  . ARG B 2 4   ? 11.34525  -64.08596 -6.98610  1.000 52.69000  ? 4    ARG B NE  1 
ATOM   1480 C CZ  . ARG B 2 4   ? 12.36900  -63.26935 -6.76908  1.000 54.73000  ? 4    ARG B CZ  1 
ATOM   1481 N NH1 . ARG B 2 4   ? 13.02598  -63.27431 -5.61999  1.000 58.85000  ? 4    ARG B NH1 1 
ATOM   1482 N NH2 . ARG B 2 4   ? 12.74178  -62.42481 -7.72697  1.000 51.24000  ? 4    ARG B NH2 1 
ATOM   1483 N N   . PRO B 2 5   ? 5.35032   -64.56148 -5.78849  1.000 48.84000  ? 5    PRO B N   1 
ATOM   1484 C CA  . PRO B 2 5   ? 4.30549   -63.63519 -5.33564  1.000 49.91000  ? 5    PRO B CA  1 
ATOM   1485 C C   . PRO B 2 5   ? 4.90508   -62.29292 -4.93819  1.000 49.02000  ? 5    PRO B C   1 
ATOM   1486 O O   . PRO B 2 5   ? 5.94694   -62.22746 -4.28031  1.000 48.87000  ? 5    PRO B O   1 
ATOM   1487 C CB  . PRO B 2 5   ? 3.67788   -64.34800 -4.13230  1.000 51.15000  ? 5    PRO B CB  1 
ATOM   1488 C CG  . PRO B 2 5   ? 4.61034   -65.45781 -3.76053  1.000 53.99000  ? 5    PRO B CG  1 
ATOM   1489 C CD  . PRO B 2 5   ? 5.68634   -65.58888 -4.78934  1.000 52.58000  ? 5    PRO B CD  1 
ATOM   1490 N N   . ARG B 2 6   ? 4.23906   -61.21562 -5.34859  1.000 44.39000  ? 6    ARG B N   1 
ATOM   1491 C CA  . ARG B 2 6   ? 4.71964   -59.86333 -5.10721  1.000 38.26000  ? 6    ARG B CA  1 
ATOM   1492 C C   . ARG B 2 6   ? 3.92302   -59.19262 -3.99810  1.000 35.14000  ? 6    ARG B C   1 
ATOM   1493 O O   . ARG B 2 6   ? 2.74534   -59.49296 -3.78568  1.000 34.45000  ? 6    ARG B O   1 
ATOM   1494 C CB  . ARG B 2 6   ? 4.64261   -59.01671 -6.37683  1.000 36.48000  ? 6    ARG B CB  1 
ATOM   1495 C CG  . ARG B 2 6   ? 5.99249   -58.77883 -7.00369  1.000 36.61000  ? 6    ARG B CG  1 
ATOM   1496 C CD  . ARG B 2 6   ? 6.54038   -60.07898 -7.55461  1.000 35.81000  ? 6    ARG B CD  1 
ATOM   1497 N NE  . ARG B 2 6   ? 7.85730   -59.90218 -8.14774  1.000 37.25000  ? 6    ARG B NE  1 
ATOM   1498 C CZ  . ARG B 2 6   ? 8.50137   -60.84277 -8.82232  1.000 37.28000  ? 6    ARG B CZ  1 
ATOM   1499 N NH1 . ARG B 2 6   ? 7.96237   -62.03460 -9.02954  1.000 38.11000  ? 6    ARG B NH1 1 
ATOM   1500 N NH2 . ARG B 2 6   ? 9.71187   -60.57814 -9.30611  1.000 31.70000  ? 6    ARG B NH2 1 
ATOM   1501 N N   . PHE B 2 7   ? 4.58301   -58.27134 -3.29508  1.000 35.81000  ? 7    PHE B N   1 
ATOM   1502 C CA  . PHE B 2 7   ? 3.96946   -57.50283 -2.22064  1.000 33.98000  ? 7    PHE B CA  1 
ATOM   1503 C C   . PHE B 2 7   ? 4.34477   -56.04011 -2.39055  1.000 37.68000  ? 7    PHE B C   1 
ATOM   1504 O O   . PHE B 2 7   ? 5.53231   -55.70178 -2.45641  1.000 33.52000  ? 7    PHE B O   1 
ATOM   1505 C CB  . PHE B 2 7   ? 4.40931   -58.01553 -0.84693  1.000 39.81000  ? 7    PHE B CB  1 
ATOM   1506 C CG  . PHE B 2 7   ? 4.17624   -59.47963 -0.65306  1.000 36.58000  ? 7    PHE B CG  1 
ATOM   1507 C CD1 . PHE B 2 7   ? 5.14655   -60.40144 -1.00347  1.000 37.73000  ? 7    PHE B CD1 1 
ATOM   1508 C CD2 . PHE B 2 7   ? 2.97732   -59.93863 -0.13671  1.000 38.07000  ? 7    PHE B CD2 1 
ATOM   1509 C CE1 . PHE B 2 7   ? 4.92960   -61.75263 -0.83127  1.000 40.00000  ? 7    PHE B CE1 1 
ATOM   1510 C CE2 . PHE B 2 7   ? 2.75711   -61.29207 0.04308   1.000 37.62000  ? 7    PHE B CE2 1 
ATOM   1511 C CZ  . PHE B 2 7   ? 3.73249   -62.19727 -0.30732  1.000 36.34000  ? 7    PHE B CZ  1 
ATOM   1512 N N   . LEU B 2 8   ? 3.33443   -55.17919 -2.45910  1.000 36.75000  ? 8    LEU B N   1 
ATOM   1513 C CA  . LEU B 2 8   ? 3.51757   -53.78180 -2.81625  1.000 32.72000  ? 8    LEU B CA  1 
ATOM   1514 C C   . LEU B 2 8   ? 2.97513   -52.88505 -1.71476  1.000 32.26000  ? 8    LEU B C   1 
ATOM   1515 O O   . LEU B 2 8   ? 1.84551   -53.07191 -1.25046  1.000 32.08000  ? 8    LEU B O   1 
ATOM   1516 C CB  . LEU B 2 8   ? 2.82343   -53.45689 -4.14343  1.000 33.57000  ? 8    LEU B CB  1 
ATOM   1517 C CG  . LEU B 2 8   ? 2.82352   -51.97140 -4.52172  1.000 33.82000  ? 8    LEU B CG  1 
ATOM   1518 C CD1 . LEU B 2 8   ? 4.22145   -51.50887 -4.90073  1.000 34.65000  ? 8    LEU B CD1 1 
ATOM   1519 C CD2 . LEU B 2 8   ? 1.82640   -51.67178 -5.63777  1.000 35.32000  ? 8    LEU B CD2 1 
ATOM   1520 N N   . GLU B 2 9   ? 3.78202   -51.91305 -1.30838  1.000 31.14000  ? 9    GLU B N   1 
ATOM   1521 C CA  . GLU B 2 9   ? 3.37587   -50.86277 -0.38707  1.000 30.53000  ? 9    GLU B CA  1 
ATOM   1522 C C   . GLU B 2 9   ? 3.36891   -49.54741 -1.14806  1.000 30.04000  ? 9    GLU B C   1 
ATOM   1523 O O   . GLU B 2 9   ? 4.33269   -49.23562 -1.85127  1.000 28.97000  ? 9    GLU B O   1 
ATOM   1524 C CB  . GLU B 2 9   ? 4.33622   -50.78878 0.80295   1.000 32.06000  ? 9    GLU B CB  1 
ATOM   1525 C CG  . GLU B 2 9   ? 4.09836   -49.63445 1.75622   1.000 33.64000  ? 9    GLU B CG  1 
ATOM   1526 C CD  . GLU B 2 9   ? 2.98090   -49.92001 2.74378   1.000 38.40000  ? 9    GLU B CD  1 
ATOM   1527 O OE1 . GLU B 2 9   ? 2.59334   -51.10352 2.87154   1.000 35.96000  ? 9    GLU B OE1 1 
ATOM   1528 O OE2 . GLU B 2 9   ? 2.49587   -48.96532 3.38960   1.000 38.39000  ? 9    GLU B OE2 1 
ATOM   1529 N N   . GLN B 2 10  ? 2.28619   -48.79059 -1.03688  1.000 28.42000  ? 10   GLN B N   1 
ATOM   1530 C CA  . GLN B 2 10  ? 2.24353   -47.46102 -1.62198  1.000 30.08000  ? 10   GLN B CA  1 
ATOM   1531 C C   . GLN B 2 10  ? 1.91654   -46.43810 -0.55154  1.000 30.72000  ? 10   GLN B C   1 
ATOM   1532 O O   . GLN B 2 10  ? 1.21274   -46.73287 0.41614   1.000 29.40000  ? 10   GLN B O   1 
ATOM   1533 C CB  . GLN B 2 10  ? 1.21275   -47.33629 -2.74975  1.000 27.12000  ? 10   GLN B CB  1 
ATOM   1534 C CG  . GLN B 2 10  ? 1.18814   -48.45746 -3.75014  1.000 26.48000  ? 10   GLN B CG  1 
ATOM   1535 C CD  . GLN B 2 10  ? 0.23557   -48.14069 -4.88786  1.000 27.17000  ? 10   GLN B CD  1 
ATOM   1536 O OE1 . GLN B 2 10  ? 0.33657   -47.08534 -5.51182  1.000 31.11000  ? 10   GLN B OE1 1 
ATOM   1537 N NE2 . GLN B 2 10  ? -0.72796  -49.02034 -5.12380  1.000 26.35000  ? 10   GLN B NE2 1 
ATOM   1538 N N   . VAL B 2 11  ? 2.44658   -45.23293 -0.73601  1.000 32.00000  ? 11   VAL B N   1 
ATOM   1539 C CA  . VAL B 2 11  ? 2.12436   -44.08442 0.10127   1.000 32.12000  ? 11   VAL B CA  1 
ATOM   1540 C C   . VAL B 2 11  ? 1.88707   -42.89723 -0.81770  1.000 31.84000  ? 11   VAL B C   1 
ATOM   1541 O O   . VAL B 2 11  ? 2.69997   -42.62017 -1.70623  1.000 33.31000  ? 11   VAL B O   1 
ATOM   1542 C CB  . VAL B 2 11  ? 3.23903   -43.75879 1.11526   1.000 30.65000  ? 11   VAL B CB  1 
ATOM   1543 C CG1 . VAL B 2 11  ? 2.76911   -42.68831 2.08627   1.000 32.43000  ? 11   VAL B CG1 1 
ATOM   1544 C CG2 . VAL B 2 11  ? 3.68197   -45.01575 1.86002   1.000 31.22000  ? 11   VAL B CG2 1 
ATOM   1545 N N   . LYS B 2 12  ? 0.77600   -42.19778 -0.61084  1.000 29.86000  ? 12   LYS B N   1 
ATOM   1546 C CA  . LYS B 2 12  ? 0.46412   -40.99656 -1.37644  1.000 31.12000  ? 12   LYS B CA  1 
ATOM   1547 C C   . LYS B 2 12  ? 0.21149   -39.86132 -0.39673  1.000 31.73000  ? 12   LYS B C   1 
ATOM   1548 O O   . LYS B 2 12  ? -0.77397  -39.88287 0.34850   1.000 33.67000  ? 12   LYS B O   1 
ATOM   1549 C CB  . LYS B 2 12  ? -0.73305  -41.22103 -2.30101  1.000 28.10000  ? 12   LYS B CB  1 
ATOM   1550 C CG  . LYS B 2 12  ? -0.41197  -42.15100 -3.46181  1.000 30.28000  ? 12   LYS B CG  1 
ATOM   1551 C CD  . LYS B 2 12  ? -1.62436  -42.47857 -4.30412  1.000 31.36000  ? 12   LYS B CD  1 
ATOM   1552 C CE  . LYS B 2 12  ? -1.40016  -43.75532 -5.10134  1.000 31.95000  ? 12   LYS B CE  1 
ATOM   1553 N NZ  . LYS B 2 12  ? -2.29790  -43.83846 -6.28225  1.000 32.92000  ? 12   LYS B NZ  1 
ATOM   1554 N N   . HIS B 2 13  ? 1.12238   -38.89455 -0.37336  1.000 32.36000  ? 13   HIS B N   1 
ATOM   1555 C CA  . HIS B 2 13  ? 0.91576   -37.64720 0.34721   1.000 30.86000  ? 13   HIS B CA  1 
ATOM   1556 C C   . HIS B 2 13  ? 0.32698   -36.65583 -0.65151  1.000 31.51000  ? 13   HIS B C   1 
ATOM   1557 O O   . HIS B 2 13  ? 1.00069   -36.25257 -1.60726  1.000 30.90000  ? 13   HIS B O   1 
ATOM   1558 C CB  . HIS B 2 13  ? 2.22338   -37.13520 0.95549   1.000 31.02000  ? 13   HIS B CB  1 
ATOM   1559 C CG  . HIS B 2 13  ? 3.09051   -38.20678 1.55408   1.000 31.06000  ? 13   HIS B CG  1 
ATOM   1560 N ND1 . HIS B 2 13  ? 3.22578   -38.38231 2.91611   1.000 32.38000  ? 13   HIS B ND1 1 
ATOM   1561 C CD2 . HIS B 2 13  ? 3.89297   -39.13453 0.97735   1.000 34.06000  ? 13   HIS B CD2 1 
ATOM   1562 C CE1 . HIS B 2 13  ? 4.05691   -39.38256 3.15115   1.000 35.44000  ? 13   HIS B CE1 1 
ATOM   1563 N NE2 . HIS B 2 13  ? 4.47685   -39.85592 1.99189   1.000 32.95000  ? 13   HIS B NE2 1 
ATOM   1564 N N   . GLU B 2 14  ? -0.93145  -36.27497 -0.44402  1.000 34.91000  ? 14   GLU B N   1 
ATOM   1565 C CA  . GLU B 2 14  ? -1.69220  -35.51221 -1.42524  1.000 34.91000  ? 14   GLU B CA  1 
ATOM   1566 C C   . GLU B 2 14  ? -2.03330  -34.12515 -0.89724  1.000 36.82000  ? 14   GLU B C   1 
ATOM   1567 O O   . GLU B 2 14  ? -2.43723  -33.97219 0.25869   1.000 35.04000  ? 14   GLU B O   1 
ATOM   1568 C CB  . GLU B 2 14  ? -2.97252  -36.24533 -1.79073  1.000 33.62000  ? 14   GLU B CB  1 
ATOM   1569 C CG  . GLU B 2 14  ? -2.74463  -37.68986 -2.17731  1.000 37.19000  ? 14   GLU B CG  1 
ATOM   1570 C CD  . GLU B 2 14  ? -3.96220  -38.30297 -2.81309  1.000 39.59000  ? 14   GLU B CD  1 
ATOM   1571 O OE1 . GLU B 2 14  ? -4.95422  -37.56828 -3.00266  1.000 48.76000  ? 14   GLU B OE1 1 
ATOM   1572 O OE2 . GLU B 2 14  ? -3.93005  -39.50874 -3.13665  1.000 45.91000  ? 14   GLU B OE2 1 
ATOM   1573 N N   . CYS B 2 15  ? -1.88190  -33.11851 -1.75995  1.000 40.50000  ? 15   CYS B N   1 
ATOM   1574 C CA  . CYS B 2 15  ? -2.23187  -31.73383 -1.45234  1.000 36.35000  ? 15   CYS B CA  1 
ATOM   1575 C C   . CYS B 2 15  ? -3.26486  -31.26267 -2.46629  1.000 36.58000  ? 15   CYS B C   1 
ATOM   1576 O O   . CYS B 2 15  ? -2.95658  -31.12186 -3.65371  1.000 37.46000  ? 15   CYS B O   1 
ATOM   1577 C CB  . CYS B 2 15  ? -0.99870  -30.83606 -1.47336  1.000 38.16000  ? 15   CYS B CB  1 
ATOM   1578 S SG  . CYS B 2 15  ? 0.13896   -31.13399 -0.10863  1.000 40.56000  ? 15   CYS B SG  1 
ATOM   1579 N N   . HIS B 2 16  ? -4.48441  -31.01777 -2.00200  1.000 36.19000  ? 16   HIS B N   1 
ATOM   1580 C CA  . HIS B 2 16  ? -5.58186  -30.60556 -2.86613  1.000 34.60000  ? 16   HIS B CA  1 
ATOM   1581 C C   . HIS B 2 16  ? -5.82627  -29.11333 -2.69443  1.000 36.32000  ? 16   HIS B C   1 
ATOM   1582 O O   . HIS B 2 16  ? -5.99365  -28.63218 -1.56964  1.000 37.68000  ? 16   HIS B O   1 
ATOM   1583 C CB  . HIS B 2 16  ? -6.83868  -31.41467 -2.54790  1.000 32.76000  ? 16   HIS B CB  1 
ATOM   1584 C CG  . HIS B 2 16  ? -6.68094  -32.87726 -2.82199  1.000 33.07000  ? 16   HIS B CG  1 
ATOM   1585 N ND1 . HIS B 2 16  ? -7.19497  -33.48396 -3.94808  1.000 36.39000  ? 16   HIS B ND1 1 
ATOM   1586 C CD2 . HIS B 2 16  ? -6.02737  -33.84774 -2.13934  1.000 33.59000  ? 16   HIS B CD2 1 
ATOM   1587 C CE1 . HIS B 2 16  ? -6.88067  -34.76803 -3.93964  1.000 31.19000  ? 16   HIS B CE1 1 
ATOM   1588 N NE2 . HIS B 2 16  ? -6.17686  -35.01598 -2.85044  1.000 32.31000  ? 16   HIS B NE2 1 
ATOM   1589 N N   . PHE B 2 17  ? -5.82359  -28.38419 -3.80484  1.000 35.21000  ? 17   PHE B N   1 
ATOM   1590 C CA  . PHE B 2 17  ? -5.91282  -26.93286 -3.79038  1.000 34.83000  ? 17   PHE B CA  1 
ATOM   1591 C C   . PHE B 2 17  ? -7.18949  -26.46908 -4.47542  1.000 33.14000  ? 17   PHE B C   1 
ATOM   1592 O O   . PHE B 2 17  ? -7.58805  -27.01594 -5.50844  1.000 35.31000  ? 17   PHE B O   1 
ATOM   1593 C CB  . PHE B 2 17  ? -4.69725  -26.30999 -4.47817  1.000 32.23000  ? 17   PHE B CB  1 
ATOM   1594 C CG  . PHE B 2 17  ? -3.39538  -26.68958 -3.84531  1.000 32.90000  ? 17   PHE B CG  1 
ATOM   1595 C CD1 . PHE B 2 17  ? -2.87891  -25.94551 -2.79298  1.000 32.88000  ? 17   PHE B CD1 1 
ATOM   1596 C CD2 . PHE B 2 17  ? -2.70024  -27.80815 -4.28227  1.000 30.47000  ? 17   PHE B CD2 1 
ATOM   1597 C CE1 . PHE B 2 17  ? -1.69020  -26.29897 -2.20452  1.000 30.77000  ? 17   PHE B CE1 1 
ATOM   1598 C CE2 . PHE B 2 17  ? -1.51258  -28.16402 -3.70049  1.000 30.21000  ? 17   PHE B CE2 1 
ATOM   1599 C CZ  . PHE B 2 17  ? -1.00542  -27.41122 -2.65812  1.000 30.60000  ? 17   PHE B CZ  1 
ATOM   1600 N N   . PHE B 2 18  ? -7.82902  -25.46033 -3.88823  1.000 34.04000  ? 18   PHE B N   1 
ATOM   1601 C CA  . PHE B 2 18  ? -8.98117  -24.80449 -4.49312  1.000 38.95000  ? 18   PHE B CA  1 
ATOM   1602 C C   . PHE B 2 18  ? -8.80637  -23.30447 -4.34308  1.000 35.96000  ? 18   PHE B C   1 
ATOM   1603 O O   . PHE B 2 18  ? -8.51304  -22.82349 -3.24435  1.000 36.30000  ? 18   PHE B O   1 
ATOM   1604 C CB  . PHE B 2 18  ? -10.30002 -25.25177 -3.84741  1.000 42.28000  ? 18   PHE B CB  1 
ATOM   1605 N N   . ASN B 2 19  ? -9.00019  -22.57492 -5.43948  1.000 36.37000  ? 19   ASN B N   1 
ATOM   1606 C CA  . ASN B 2 19  ? -8.77753  -21.13090 -5.48420  1.000 42.61000  ? 19   ASN B CA  1 
ATOM   1607 C C   . ASN B 2 19  ? -7.36325  -20.79291 -5.01563  1.000 41.33000  ? 19   ASN B C   1 
ATOM   1608 O O   . ASN B 2 19  ? -7.15313  -20.14024 -3.99160  1.000 42.43000  ? 19   ASN B O   1 
ATOM   1609 C CB  . ASN B 2 19  ? -9.82857  -20.37964 -4.65840  1.000 44.13000  ? 19   ASN B CB  1 
ATOM   1610 C CG  . ASN B 2 19  ? -9.75273  -18.86992 -4.85020  1.000 47.95000  ? 19   ASN B CG  1 
ATOM   1611 O OD1 . ASN B 2 19  ? -9.21979  -18.38972 -5.85114  1.000 49.35000  ? 19   ASN B OD1 1 
ATOM   1612 N ND2 . ASN B 2 19  ? -10.29087 -18.11713 -3.89005  1.000 52.66000  ? 19   ASN B ND2 1 
ATOM   1613 N N   . GLY B 2 20  ? -6.38947  -21.25508 -5.79153  1.000 43.61000  ? 20   GLY B N   1 
ATOM   1614 C CA  . GLY B 2 20  ? -4.99734  -21.10524 -5.39377  1.000 41.20000  ? 20   GLY B CA  1 
ATOM   1615 C C   . GLY B 2 20  ? -4.72376  -21.85562 -4.10324  1.000 41.58000  ? 20   GLY B C   1 
ATOM   1616 O O   . GLY B 2 20  ? -4.94081  -23.06939 -4.00306  1.000 47.16000  ? 20   GLY B O   1 
ATOM   1617 N N   . THR B 2 21  ? -4.25458  -21.12813 -3.08936  1.000 38.54000  ? 21   THR B N   1 
ATOM   1618 C CA  . THR B 2 21  ? -3.96470  -21.69442 -1.77768  1.000 40.89000  ? 21   THR B CA  1 
ATOM   1619 C C   . THR B 2 21  ? -4.91755  -21.18009 -0.70342  1.000 40.22000  ? 21   THR B C   1 
ATOM   1620 O O   . THR B 2 21  ? -4.56564  -21.15118 0.47774   1.000 40.39000  ? 21   THR B O   1 
ATOM   1621 C CB  . THR B 2 21  ? -2.52002  -21.40654 -1.36903  1.000 42.07000  ? 21   THR B CB  1 
ATOM   1622 O OG1 . THR B 2 21  ? -2.34259  -19.99544 -1.18466  1.000 35.42000  ? 21   THR B OG1 1 
ATOM   1623 C CG2 . THR B 2 21  ? -1.55488  -21.90754 -2.42236  1.000 47.86000  ? 21   THR B CG2 1 
ATOM   1624 N N   . GLU B 2 22  ? -6.12269  -20.76080 -1.09530  1.000 42.68000  ? 22   GLU B N   1 
ATOM   1625 C CA  . GLU B 2 22  ? -7.10784  -20.35209 -0.09980  1.000 48.69000  ? 22   GLU B CA  1 
ATOM   1626 C C   . GLU B 2 22  ? -7.66548  -21.55883 0.63925   1.000 43.94000  ? 22   GLU B C   1 
ATOM   1627 O O   . GLU B 2 22  ? -7.81338  -21.53324 1.86564   1.000 46.49000  ? 22   GLU B O   1 
ATOM   1628 C CB  . GLU B 2 22  ? -8.23552  -19.56124 -0.76171  1.000 52.03000  ? 22   GLU B CB  1 
ATOM   1629 C CG  . GLU B 2 22  ? -7.82594  -18.16561 -1.17369  1.000 58.94000  ? 22   GLU B CG  1 
ATOM   1630 C CD  . GLU B 2 22  ? -7.25117  -17.36136 -0.02152  1.000 66.07000  ? 22   GLU B CD  1 
ATOM   1631 O OE1 . GLU B 2 22  ? -7.74546  -17.51075 1.11783   1.000 64.60000  ? 22   GLU B OE1 1 
ATOM   1632 O OE2 . GLU B 2 22  ? -6.29904  -16.58369 -0.25875  1.000 67.61000  ? 22   GLU B OE2 1 
ATOM   1633 N N   . ARG B 2 23  ? -7.96542  -22.62651 -0.08994  1.000 46.11000  ? 23   ARG B N   1 
ATOM   1634 C CA  . ARG B 2 23  ? -8.48088  -23.85979 0.47834   1.000 42.61000  ? 23   ARG B CA  1 
ATOM   1635 C C   . ARG B 2 23  ? -7.53413  -24.99108 0.11504   1.000 37.36000  ? 23   ARG B C   1 
ATOM   1636 O O   . ARG B 2 23  ? -7.21288  -25.18577 -1.06170  1.000 42.79000  ? 23   ARG B O   1 
ATOM   1637 C CB  . ARG B 2 23  ? -9.89664  -24.13563 -0.02682  1.000 47.84000  ? 23   ARG B CB  1 
ATOM   1638 C CG  . ARG B 2 23  ? -10.87394 -23.04550 0.38912   1.000 54.61000  ? 23   ARG B CG  1 
ATOM   1639 C CD  . ARG B 2 23  ? -12.31702 -23.34770 0.00804   1.000 52.50000  ? 23   ARG B CD  1 
ATOM   1640 N NE  . ARG B 2 23  ? -12.95945 -22.18305 -0.58541  1.000 53.62000  ? 23   ARG B NE  1 
ATOM   1641 C CZ  . ARG B 2 23  ? -14.15957 -22.19314 -1.14718  1.000 60.98000  ? 23   ARG B CZ  1 
ATOM   1642 N NH1 . ARG B 2 23  ? -14.88548 -23.29867 -1.20720  1.000 68.73000  ? 23   ARG B NH1 1 
ATOM   1643 N NH2 . ARG B 2 23  ? -14.64834 -21.06245 -1.65143  1.000 59.71000  ? 23   ARG B NH2 1 
ATOM   1644 N N   . VAL B 2 24  ? -7.06590  -25.71113 1.12860   1.000 38.04000  ? 24   VAL B N   1 
ATOM   1645 C CA  . VAL B 2 24  ? -6.09790  -26.78468 0.95301   1.000 37.17000  ? 24   VAL B CA  1 
ATOM   1646 C C   . VAL B 2 24  ? -6.53384  -27.96583 1.80129   1.000 38.13000  ? 24   VAL B C   1 
ATOM   1647 O O   . VAL B 2 24  ? -6.91685  -27.80010 2.96276   1.000 36.83000  ? 24   VAL B O   1 
ATOM   1648 C CB  . VAL B 2 24  ? -4.67245  -26.33886 1.33787   1.000 37.50000  ? 24   VAL B CB  1 
ATOM   1649 C CG1 . VAL B 2 24  ? -3.69506  -27.49717 1.19842   1.000 34.97000  ? 24   VAL B CG1 1 
ATOM   1650 C CG2 . VAL B 2 24  ? -4.22997  -25.15860 0.48879   1.000 40.89000  ? 24   VAL B CG2 1 
ATOM   1651 N N   . ARG B 2 25  ? -6.48487  -29.15917 1.21988   1.000 37.07000  ? 25   ARG B N   1 
ATOM   1652 C CA  . ARG B 2 25  ? -6.70134  -30.39553 1.95693   1.000 38.58000  ? 25   ARG B CA  1 
ATOM   1653 C C   . ARG B 2 25  ? -5.47209  -31.27943 1.79690   1.000 39.42000  ? 25   ARG B C   1 
ATOM   1654 O O   . ARG B 2 25  ? -5.06968  -31.58858 0.66841   1.000 36.82000  ? 25   ARG B O   1 
ATOM   1655 C CB  . ARG B 2 25  ? -7.95304  -31.12636 1.47136   1.000 41.34000  ? 25   ARG B CB  1 
ATOM   1656 C CG  . ARG B 2 25  ? -8.26017  -32.35740 2.29525   1.000 44.00000  ? 25   ARG B CG  1 
ATOM   1657 C CD  . ARG B 2 25  ? -9.70133  -32.77387 2.17175   1.000 46.42000  ? 25   ARG B CD  1 
ATOM   1658 N NE  . ARG B 2 25  ? -9.90769  -33.66879 1.04138   1.000 50.87000  ? 25   ARG B NE  1 
ATOM   1659 C CZ  . ARG B 2 25  ? -10.42041 -34.88808 1.13973   1.000 53.87000  ? 25   ARG B CZ  1 
ATOM   1660 N NH1 . ARG B 2 25  ? -10.78082 -35.39402 2.30844   1.000 56.37000  ? 25   ARG B NH1 1 
ATOM   1661 N NH2 . ARG B 2 25  ? -10.57547 -35.61803 0.03756   1.000 58.88000  ? 25   ARG B NH2 1 
ATOM   1662 N N   . PHE B 2 26  ? -4.87970  -31.68044 2.92055   1.000 39.96000  ? 26   PHE B N   1 
ATOM   1663 C CA  . PHE B 2 26  ? -3.74679  -32.59548 2.92968   1.000 36.46000  ? 26   PHE B CA  1 
ATOM   1664 C C   . PHE B 2 26  ? -4.22187  -33.98994 3.32116   1.000 32.64000  ? 26   PHE B C   1 
ATOM   1665 O O   . PHE B 2 26  ? -4.93656  -34.14906 4.31393   1.000 36.87000  ? 26   PHE B O   1 
ATOM   1666 C CB  . PHE B 2 26  ? -2.66129  -32.11430 3.89582   1.000 36.65000  ? 26   PHE B CB  1 
ATOM   1667 C CG  . PHE B 2 26  ? -1.65109  -33.17274 4.24771   1.000 38.22000  ? 26   PHE B CG  1 
ATOM   1668 C CD1 . PHE B 2 26  ? -0.76068  -33.64207 3.29509   1.000 35.90000  ? 26   PHE B CD1 1 
ATOM   1669 C CD2 . PHE B 2 26  ? -1.60087  -33.70937 5.52655   1.000 36.06000  ? 26   PHE B CD2 1 
ATOM   1670 C CE1 . PHE B 2 26  ? 0.16417   -34.61576 3.61097   1.000 36.43000  ? 26   PHE B CE1 1 
ATOM   1671 C CE2 . PHE B 2 26  ? -0.67396  -34.68714 5.84661   1.000 36.48000  ? 26   PHE B CE2 1 
ATOM   1672 C CZ  . PHE B 2 26  ? 0.21045   -35.13757 4.88502   1.000 36.21000  ? 26   PHE B CZ  1 
ATOM   1673 N N   . LEU B 2 27  ? -3.83467  -34.99117 2.53561   1.000 31.46000  ? 27   LEU B N   1 
ATOM   1674 C CA  . LEU B 2 27  ? -4.12705  -36.38840 2.82234   1.000 34.83000  ? 27   LEU B CA  1 
ATOM   1675 C C   . LEU B 2 27  ? -2.82786  -37.17871 2.90738   1.000 37.99000  ? 27   LEU B C   1 
ATOM   1676 O O   . LEU B 2 27  ? -1.93644  -37.01390 2.06805   1.000 36.97000  ? 27   LEU B O   1 
ATOM   1677 C CB  . LEU B 2 27  ? -5.03037  -37.00513 1.75090   1.000 40.24000  ? 27   LEU B CB  1 
ATOM   1678 C CG  . LEU B 2 27  ? -6.37345  -36.32237 1.50065   1.000 42.78000  ? 27   LEU B CG  1 
ATOM   1679 C CD1 . LEU B 2 27  ? -6.93883  -36.73283 0.15087   1.000 44.79000  ? 27   LEU B CD1 1 
ATOM   1680 C CD2 . LEU B 2 27  ? -7.34606  -36.65499 2.61682   1.000 44.11000  ? 27   LEU B CD2 1 
ATOM   1681 N N   . ASP B 2 28  ? -2.72468  -38.03445 3.92408   1.000 35.21000  ? 28   ASP B N   1 
ATOM   1682 C CA  . ASP B 2 28  ? -1.59421  -38.94693 4.10019   1.000 35.79000  ? 28   ASP B CA  1 
ATOM   1683 C C   . ASP B 2 28  ? -2.15184  -40.36077 3.97779   1.000 35.38000  ? 28   ASP B C   1 
ATOM   1684 O O   . ASP B 2 28  ? -2.71425  -40.89384 4.93845   1.000 32.93000  ? 28   ASP B O   1 
ATOM   1685 C CB  . ASP B 2 28  ? -0.90553  -38.72446 5.44716   1.000 40.18000  ? 28   ASP B CB  1 
ATOM   1686 C CG  . ASP B 2 28  ? 0.54173   -39.20972 5.46199   1.000 42.49000  ? 28   ASP B CG  1 
ATOM   1687 O OD1 . ASP B 2 28  ? 1.23980   -39.06228 4.43600   1.000 50.06000  ? 28   ASP B OD1 1 
ATOM   1688 O OD2 . ASP B 2 28  ? 0.98781   -39.73528 6.50541   1.000 43.20000  ? 28   ASP B OD2 1 
ATOM   1689 N N   . ARG B 2 29  ? -2.00100  -40.96820 2.80262   1.000 31.83000  ? 29   ARG B N   1 
ATOM   1690 C CA  . ARG B 2 29  ? -2.68459  -42.21023 2.46917   1.000 30.49000  ? 29   ARG B CA  1 
ATOM   1691 C C   . ARG B 2 29  ? -1.68789  -43.35259 2.33156   1.000 32.36000  ? 29   ARG B C   1 
ATOM   1692 O O   . ARG B 2 29  ? -0.62192  -43.19060 1.73380   1.000 30.49000  ? 29   ARG B O   1 
ATOM   1693 C CB  . ARG B 2 29  ? -3.48124  -42.04765 1.17628   1.000 31.58000  ? 29   ARG B CB  1 
ATOM   1694 C CG  . ARG B 2 29  ? -4.24108  -40.72873 1.09389   1.000 32.08000  ? 29   ARG B CG  1 
ATOM   1695 C CD  . ARG B 2 29  ? -4.89225  -40.55687 -0.26629  1.000 32.54000  ? 29   ARG B CD  1 
ATOM   1696 N NE  . ARG B 2 29  ? -5.94627  -41.53949 -0.47764  1.000 30.88000  ? 29   ARG B NE  1 
ATOM   1697 C CZ  . ARG B 2 29  ? -6.53683  -41.76504 -1.64299  1.000 33.87000  ? 29   ARG B CZ  1 
ATOM   1698 N NH1 . ARG B 2 29  ? -6.21518  -41.07283 -2.72723  1.000 32.06000  ? 29   ARG B NH1 1 
ATOM   1699 N NH2 . ARG B 2 29  ? -7.46603  -42.71462 -1.72553  1.000 33.97000  ? 29   ARG B NH2 1 
ATOM   1700 N N   . TYR B 2 30  ? -2.04392  -44.50744 2.88596   1.000 30.94000  ? 30   TYR B N   1 
ATOM   1701 C CA  . TYR B 2 30  ? -1.16699  -45.66790 2.95300   1.000 28.87000  ? 30   TYR B CA  1 
ATOM   1702 C C   . TYR B 2 30  ? -1.90107  -46.86504 2.37892   1.000 31.49000  ? 30   TYR B C   1 
ATOM   1703 O O   . TYR B 2 30  ? -3.06430  -47.10481 2.72379   1.000 30.08000  ? 30   TYR B O   1 
ATOM   1704 C CB  . TYR B 2 30  ? -0.72732  -45.95602 4.39623   1.000 29.19000  ? 30   TYR B CB  1 
ATOM   1705 C CG  . TYR B 2 30  ? 0.19605   -44.90875 4.95810   1.000 29.29000  ? 30   TYR B CG  1 
ATOM   1706 C CD1 . TYR B 2 30  ? -0.28777  -43.66400 5.33760   1.000 29.74000  ? 30   TYR B CD1 1 
ATOM   1707 C CD2 . TYR B 2 30  ? 1.55750   -45.15591 5.09330   1.000 31.00000  ? 30   TYR B CD2 1 
ATOM   1708 C CE1 . TYR B 2 30  ? 0.55271   -42.69605 5.83753   1.000 31.57000  ? 30   TYR B CE1 1 
ATOM   1709 C CE2 . TYR B 2 30  ? 2.40767   -44.19611 5.60321   1.000 31.13000  ? 30   TYR B CE2 1 
ATOM   1710 C CZ  . TYR B 2 30  ? 1.90081   -42.96751 5.96922   1.000 32.18000  ? 30   TYR B CZ  1 
ATOM   1711 O OH  . TYR B 2 30  ? 2.74356   -42.00050 6.46490   1.000 34.45000  ? 30   TYR B OH  1 
ATOM   1712 N N   . PHE B 2 31  ? -1.21471  -47.62126 1.52030   1.000 30.97000  ? 31   PHE B N   1 
ATOM   1713 C CA  . PHE B 2 31  ? -1.83337  -48.67457 0.73025   1.000 29.77000  ? 31   PHE B CA  1 
ATOM   1714 C C   . PHE B 2 31  ? -1.04693  -49.97057 0.85830   1.000 29.37000  ? 31   PHE B C   1 
ATOM   1715 O O   . PHE B 2 31  ? 0.18722   -49.96363 0.85082   1.000 29.86000  ? 31   PHE B O   1 
ATOM   1716 C CB  . PHE B 2 31  ? -1.91039  -48.28560 -0.75014  1.000 31.03000  ? 31   PHE B CB  1 
ATOM   1717 C CG  . PHE B 2 31  ? -2.60826  -46.97860 -1.00693  1.000 32.14000  ? 31   PHE B CG  1 
ATOM   1718 C CD1 . PHE B 2 31  ? -1.94509  -45.77184 -0.83381  1.000 29.17000  ? 31   PHE B CD1 1 
ATOM   1719 C CD2 . PHE B 2 31  ? -3.92523  -46.95952 -1.45085  1.000 29.50000  ? 31   PHE B CD2 1 
ATOM   1720 C CE1 . PHE B 2 31  ? -2.59020  -44.56975 -1.07579  1.000 31.46000  ? 31   PHE B CE1 1 
ATOM   1721 C CE2 . PHE B 2 31  ? -4.57209  -45.76052 -1.69361  1.000 30.72000  ? 31   PHE B CE2 1 
ATOM   1722 C CZ  . PHE B 2 31  ? -3.90438  -44.56503 -1.50766  1.000 29.00000  ? 31   PHE B CZ  1 
ATOM   1723 N N   . TYR B 2 32  ? -1.76958  -51.07968 0.97281   1.000 33.43000  ? 32   TYR B N   1 
ATOM   1724 C CA  . TYR B 2 32  ? -1.21991  -52.41819 0.79519   1.000 34.33000  ? 32   TYR B CA  1 
ATOM   1725 C C   . TYR B 2 32  ? -1.81856  -52.95721 -0.49839  1.000 33.98000  ? 32   TYR B C   1 
ATOM   1726 O O   . TYR B 2 32  ? -3.02688  -53.19897 -0.56645  1.000 35.89000  ? 32   TYR B O   1 
ATOM   1727 C CB  . TYR B 2 32  ? -1.54322  -53.31634 1.98695   1.000 35.91000  ? 32   TYR B CB  1 
ATOM   1728 C CG  . TYR B 2 32  ? -0.91226  -54.68406 1.89536   1.000 40.58000  ? 32   TYR B CG  1 
ATOM   1729 C CD1 . TYR B 2 32  ? 0.46695   -54.83695 1.97521   1.000 42.55000  ? 32   TYR B CD1 1 
ATOM   1730 C CD2 . TYR B 2 32  ? -1.69122  -55.82148 1.72487   1.000 39.06000  ? 32   TYR B CD2 1 
ATOM   1731 C CE1 . TYR B 2 32  ? 1.05386   -56.08362 1.88746   1.000 39.38000  ? 32   TYR B CE1 1 
ATOM   1732 C CE2 . TYR B 2 32  ? -1.11549  -57.07482 1.63146   1.000 39.28000  ? 32   TYR B CE2 1 
ATOM   1733 C CZ  . TYR B 2 32  ? 0.25976   -57.19982 1.71602   1.000 40.34000  ? 32   TYR B CZ  1 
ATOM   1734 O OH  . TYR B 2 32  ? 0.84041   -58.44220 1.62407   1.000 38.00000  ? 32   TYR B OH  1 
ATOM   1735 N N   . HIS B 2 33  ? -0.98179  -53.11448 -1.52719  1.000 33.12000  ? 33   HIS B N   1 
ATOM   1736 C CA  . HIS B 2 33  ? -1.40859  -53.46382 -2.90242  1.000 37.18000  ? 33   HIS B CA  1 
ATOM   1737 C C   . HIS B 2 33  ? -2.24056  -52.29312 -3.42668  1.000 36.99000  ? 33   HIS B C   1 
ATOM   1738 O O   . HIS B 2 33  ? -1.70297  -51.18461 -3.58369  1.000 42.32000  ? 33   HIS B O   1 
ATOM   1739 C CB  . HIS B 2 33  ? -2.11040  -54.81842 -2.92053  1.000 38.73000  ? 33   HIS B CB  1 
ATOM   1740 C CG  . HIS B 2 33  ? -1.31822  -55.92954 -2.30628  1.000 42.75000  ? 33   HIS B CG  1 
ATOM   1741 N ND1 . HIS B 2 33  ? 0.04596   -55.86309 -2.11673  1.000 38.27000  ? 33   HIS B ND1 1 
ATOM   1742 C CD2 . HIS B 2 33  ? -1.70174  -57.14875 -1.85854  1.000 42.73000  ? 33   HIS B CD2 1 
ATOM   1743 C CE1 . HIS B 2 33  ? 0.46554   -56.98779 -1.56444  1.000 42.27000  ? 33   HIS B CE1 1 
ATOM   1744 N NE2 . HIS B 2 33  ? -0.57490  -57.78492 -1.39927  1.000 43.09000  ? 33   HIS B NE2 1 
ATOM   1745 N N   . GLN B 2 34  ? -3.52538  -52.48307 -3.72627  1.000 37.13000  ? 34   GLN B N   1 
ATOM   1746 C CA  . GLN B 2 34  ? -4.40779  -51.37630 -4.06525  1.000 38.22000  ? 34   GLN B CA  1 
ATOM   1747 C C   . GLN B 2 34  ? -5.25540  -50.92215 -2.89170  1.000 39.22000  ? 34   GLN B C   1 
ATOM   1748 O O   . GLN B 2 34  ? -6.07866  -50.01652 -3.06071  1.000 44.18000  ? 34   GLN B O   1 
ATOM   1749 C CB  . GLN B 2 34  ? -5.35109  -51.75519 -5.20389  1.000 38.36000  ? 34   GLN B CB  1 
ATOM   1750 C CG  . GLN B 2 34  ? -4.72878  -52.01908 -6.54292  1.000 40.92000  ? 34   GLN B CG  1 
ATOM   1751 C CD  . GLN B 2 34  ? -5.80254  -52.25611 -7.59075  1.000 46.34000  ? 34   GLN B CD  1 
ATOM   1752 O OE1 . GLN B 2 34  ? -6.09576  -53.39740 -7.94708  1.000 47.57000  ? 34   GLN B OE1 1 
ATOM   1753 N NE2 . GLN B 2 34  ? -6.42394  -51.17610 -8.05991  1.000 44.49000  ? 34   GLN B NE2 1 
ATOM   1754 N N   . GLU B 2 35  ? -5.10006  -51.54072 -1.72569  1.000 40.63000  ? 35   GLU B N   1 
ATOM   1755 C CA  . GLU B 2 35  ? -6.01642  -51.34139 -0.61049  1.000 41.02000  ? 35   GLU B CA  1 
ATOM   1756 C C   . GLU B 2 35  ? -5.49427  -50.21637 0.26810   1.000 39.27000  ? 35   GLU B C   1 
ATOM   1757 O O   . GLU B 2 35  ? -4.47084  -50.37020 0.94008   1.000 37.24000  ? 35   GLU B O   1 
ATOM   1758 C CB  . GLU B 2 35  ? -6.17166  -52.63125 0.19015   1.000 42.69000  ? 35   GLU B CB  1 
ATOM   1759 C CG  . GLU B 2 35  ? -7.18573  -52.52779 1.30898   1.000 44.88000  ? 35   GLU B CG  1 
ATOM   1760 C CD  . GLU B 2 35  ? -7.12108  -53.70151 2.26959   1.000 47.93000  ? 35   GLU B CD  1 
ATOM   1761 O OE1 . GLU B 2 35  ? -6.84338  -54.83000 1.80585   1.000 46.71000  ? 35   GLU B OE1 1 
ATOM   1762 O OE2 . GLU B 2 35  ? -7.35374  -53.50012 3.48252   1.000 53.28000  ? 35   GLU B OE2 1 
ATOM   1763 N N   . GLU B 2 36  ? -6.18592  -49.08437 0.25261   1.000 41.51000  ? 36   GLU B N   1 
ATOM   1764 C CA  . GLU B 2 36  ? -5.90700  -48.03527 1.21826   1.000 39.75000  ? 36   GLU B CA  1 
ATOM   1765 C C   . GLU B 2 36  ? -6.34269  -48.51241 2.59128   1.000 45.08000  ? 36   GLU B C   1 
ATOM   1766 O O   . GLU B 2 36  ? -7.52378  -48.80648 2.80340   1.000 48.45000  ? 36   GLU B O   1 
ATOM   1767 C CB  . GLU B 2 36  ? -6.63769  -46.75083 0.84537   1.000 39.34000  ? 36   GLU B CB  1 
ATOM   1768 C CG  . GLU B 2 36  ? -6.27609  -45.56722 1.72732   1.000 36.47000  ? 36   GLU B CG  1 
ATOM   1769 C CD  . GLU B 2 36  ? -7.01641  -44.30324 1.33310   1.000 37.74000  ? 36   GLU B CD  1 
ATOM   1770 O OE1 . GLU B 2 36  ? -7.94247  -44.40773 0.50048   1.000 41.19000  ? 36   GLU B OE1 1 
ATOM   1771 O OE2 . GLU B 2 36  ? -6.68023  -43.21005 1.85136   1.000 35.78000  ? 36   GLU B OE2 1 
ATOM   1772 N N   . TYR B 2 37  ? -5.39883  -48.60229 3.52750   1.000 45.37000  ? 37   TYR B N   1 
ATOM   1773 C CA  . TYR B 2 37  ? -5.74119  -49.11435 4.84105   1.000 40.31000  ? 37   TYR B CA  1 
ATOM   1774 C C   . TYR B 2 37  ? -5.73254  -48.06541 5.93927   1.000 37.37000  ? 37   TYR B C   1 
ATOM   1775 O O   . TYR B 2 37  ? -6.40776  -48.26505 6.95217   1.000 36.64000  ? 37   TYR B O   1 
ATOM   1776 C CB  . TYR B 2 37  ? -4.82129  -50.28520 5.22796   1.000 42.02000  ? 37   TYR B CB  1 
ATOM   1777 C CG  . TYR B 2 37  ? -3.33434  -50.01129 5.27580   1.000 42.77000  ? 37   TYR B CG  1 
ATOM   1778 C CD1 . TYR B 2 37  ? -2.72731  -49.55120 6.43652   1.000 44.57000  ? 37   TYR B CD1 1 
ATOM   1779 C CD2 . TYR B 2 37  ? -2.53024  -50.26308 4.17477   1.000 44.84000  ? 37   TYR B CD2 1 
ATOM   1780 C CE1 . TYR B 2 37  ? -1.36557  -49.32158 6.48825   1.000 46.11000  ? 37   TYR B CE1 1 
ATOM   1781 C CE2 . TYR B 2 37  ? -1.16815  -50.04211 4.21808   1.000 46.08000  ? 37   TYR B CE2 1 
ATOM   1782 C CZ  . TYR B 2 37  ? -0.59108  -49.57386 5.37710   1.000 43.32000  ? 37   TYR B CZ  1 
ATOM   1783 O OH  . TYR B 2 37  ? 0.76247   -49.35154 5.41845   1.000 42.38000  ? 37   TYR B OH  1 
ATOM   1784 N N   . VAL B 2 38  ? -5.02656  -46.94962 5.76730   1.000 34.18000  ? 38   VAL B N   1 
ATOM   1785 C CA  . VAL B 2 38  ? -5.04693  -45.89034 6.76938   1.000 34.16000  ? 38   VAL B CA  1 
ATOM   1786 C C   . VAL B 2 38  ? -4.87334  -44.55107 6.06668   1.000 35.09000  ? 38   VAL B C   1 
ATOM   1787 O O   . VAL B 2 38  ? -4.28054  -44.46618 4.98697   1.000 39.60000  ? 38   VAL B O   1 
ATOM   1788 C CB  . VAL B 2 38  ? -3.97368  -46.12070 7.86240   1.000 35.72000  ? 38   VAL B CB  1 
ATOM   1789 C CG1 . VAL B 2 38  ? -2.59218  -45.83011 7.33417   1.000 36.22000  ? 38   VAL B CG1 1 
ATOM   1790 C CG2 . VAL B 2 38  ? -4.27272  -45.27569 9.09737   1.000 34.50000  ? 38   VAL B CG2 1 
ATOM   1791 N N   . ARG B 2 39  ? -5.41457  -43.49809 6.67803   1.000 34.29000  ? 39   ARG B N   1 
ATOM   1792 C CA  . ARG B 2 39  ? -5.45722  -42.19330 6.03292   1.000 35.80000  ? 39   ARG B CA  1 
ATOM   1793 C C   . ARG B 2 39  ? -5.49880  -41.09225 7.08040   1.000 37.25000  ? 39   ARG B C   1 
ATOM   1794 O O   . ARG B 2 39  ? -6.28382  -41.16849 8.03035   1.000 35.17000  ? 39   ARG B O   1 
ATOM   1795 C CB  . ARG B 2 39  ? -6.67990  -42.08088 5.11415   1.000 40.14000  ? 39   ARG B CB  1 
ATOM   1796 C CG  . ARG B 2 39  ? -7.04560  -40.65168 4.76572   1.000 45.21000  ? 39   ARG B CG  1 
ATOM   1797 C CD  . ARG B 2 39  ? -8.41709  -40.54174 4.13169   1.000 45.75000  ? 39   ARG B CD  1 
ATOM   1798 N NE  . ARG B 2 39  ? -8.65300  -41.56717 3.12415   1.000 51.29000  ? 39   ARG B NE  1 
ATOM   1799 C CZ  . ARG B 2 39  ? -9.64609  -41.52923 2.24632   1.000 57.42000  ? 39   ARG B CZ  1 
ATOM   1800 N NH1 . ARG B 2 39  ? -10.50008 -40.51689 2.21199   1.000 55.46000  ? 39   ARG B NH1 1 
ATOM   1801 N NH2 . ARG B 2 39  ? -9.78189  -42.52631 1.37614   1.000 55.06000  ? 39   ARG B NH2 1 
ATOM   1802 N N   . PHE B 2 40  ? -4.65640  -40.07689 6.90343   1.000 34.15000  ? 40   PHE B N   1 
ATOM   1803 C CA  . PHE B 2 40  ? -4.79941  -38.81058 7.60565   1.000 36.93000  ? 40   PHE B CA  1 
ATOM   1804 C C   . PHE B 2 40  ? -5.46469  -37.82587 6.65775   1.000 35.62000  ? 40   PHE B C   1 
ATOM   1805 O O   . PHE B 2 40  ? -4.94515  -37.56439 5.57086   1.000 38.33000  ? 40   PHE B O   1 
ATOM   1806 C CB  . PHE B 2 40  ? -3.45212  -38.26005 8.07737   1.000 35.34000  ? 40   PHE B CB  1 
ATOM   1807 C CG  . PHE B 2 40  ? -3.54567  -36.90872 8.75004   1.000 36.48000  ? 40   PHE B CG  1 
ATOM   1808 C CD1 . PHE B 2 40  ? -3.49958  -35.73620 8.00475   1.000 35.77000  ? 40   PHE B CD1 1 
ATOM   1809 C CD2 . PHE B 2 40  ? -3.67865  -36.81135 10.12765  1.000 36.36000  ? 40   PHE B CD2 1 
ATOM   1810 C CE1 . PHE B 2 40  ? -3.58564  -34.49673 8.61697   1.000 32.43000  ? 40   PHE B CE1 1 
ATOM   1811 C CE2 . PHE B 2 40  ? -3.76198  -35.56647 10.74898  1.000 33.16000  ? 40   PHE B CE2 1 
ATOM   1812 C CZ  . PHE B 2 40  ? -3.71512  -34.41128 9.99177   1.000 33.62000  ? 40   PHE B CZ  1 
ATOM   1813 N N   . ASP B 2 41  ? -6.60186  -37.28115 7.07475   1.000 39.91000  ? 41   ASP B N   1 
ATOM   1814 C CA  . ASP B 2 41  ? -7.29705  -36.21840 6.35976   1.000 37.21000  ? 41   ASP B CA  1 
ATOM   1815 C C   . ASP B 2 41  ? -7.21493  -34.96054 7.21742   1.000 36.33000  ? 41   ASP B C   1 
ATOM   1816 O O   . ASP B 2 41  ? -7.62400  -34.97907 8.38291   1.000 40.32000  ? 41   ASP B O   1 
ATOM   1817 C CB  . ASP B 2 41  ? -8.74794  -36.62253 6.08866   1.000 39.63000  ? 41   ASP B CB  1 
ATOM   1818 C CG  . ASP B 2 41  ? -9.48137  -35.64804 5.18440   1.000 44.50000  ? 41   ASP B CG  1 
ATOM   1819 O OD1 . ASP B 2 41  ? -9.11237  -34.45578 5.12963   1.000 45.10000  ? 41   ASP B OD1 1 
ATOM   1820 O OD2 . ASP B 2 41  ? -10.44362 -36.08665 4.52210   1.000 49.77000  ? 41   ASP B OD2 1 
ATOM   1821 N N   . SER B 2 42  ? -6.67200  -33.87635 6.65177   1.000 33.40000  ? 42   SER B N   1 
ATOM   1822 C CA  . SER B 2 42  ? -6.49420  -32.65736 7.44141   1.000 36.77000  ? 42   SER B CA  1 
ATOM   1823 C C   . SER B 2 42  ? -7.83274  -32.06900 7.86519   1.000 39.44000  ? 42   SER B C   1 
ATOM   1824 O O   . SER B 2 42  ? -7.91122  -31.37769 8.88757   1.000 43.52000  ? 42   SER B O   1 
ATOM   1825 C CB  . SER B 2 42  ? -5.66957  -31.61408 6.67264   1.000 34.24000  ? 42   SER B CB  1 
ATOM   1826 O OG  . SER B 2 42  ? -6.29974  -31.19835 5.47240   1.000 34.85000  ? 42   SER B OG  1 
ATOM   1827 N N   . ASP B 2 43  ? -8.89447  -32.34189 7.10632   1.000 44.45000  ? 43   ASP B N   1 
ATOM   1828 C CA  . ASP B 2 43  ? -10.22859 -31.94145 7.53232   1.000 53.39000  ? 43   ASP B CA  1 
ATOM   1829 C C   . ASP B 2 43  ? -10.70857 -32.74300 8.73668   1.000 56.69000  ? 43   ASP B C   1 
ATOM   1830 O O   . ASP B 2 43  ? -11.60466 -32.28382 9.45235   1.000 56.74000  ? 43   ASP B O   1 
ATOM   1831 C CB  . ASP B 2 43  ? -11.22123 -32.08230 6.37378   1.000 50.83000  ? 43   ASP B CB  1 
ATOM   1832 C CG  . ASP B 2 43  ? -10.97247 -31.07286 5.26046   1.000 56.47000  ? 43   ASP B CG  1 
ATOM   1833 O OD1 . ASP B 2 43  ? -9.96821  -30.32836 5.32245   1.000 49.77000  ? 43   ASP B OD1 1 
ATOM   1834 O OD2 . ASP B 2 43  ? -11.78895 -31.01305 4.32013   1.000 68.09000  ? 43   ASP B OD2 1 
ATOM   1835 N N   . VAL B 2 44  ? -10.13485 -33.91949 8.97766   1.000 53.06000  ? 44   VAL B N   1 
ATOM   1836 C CA  . VAL B 2 44  ? -10.49932 -34.72050 10.14285  1.000 50.10000  ? 44   VAL B CA  1 
ATOM   1837 C C   . VAL B 2 44  ? -9.58043  -34.43074 11.32317  1.000 49.88000  ? 44   VAL B C   1 
ATOM   1838 O O   . VAL B 2 44  ? -10.04015 -34.32500 12.46149  1.000 47.06000  ? 44   VAL B O   1 
ATOM   1839 C CB  . VAL B 2 44  ? -10.49503 -36.21820 9.77855   1.000 53.44000  ? 44   VAL B CB  1 
ATOM   1840 C CG1 . VAL B 2 44  ? -10.80663 -37.06358 10.99913  1.000 57.86000  ? 44   VAL B CG1 1 
ATOM   1841 C CG2 . VAL B 2 44  ? -11.49648 -36.49629 8.67065   1.000 52.11000  ? 44   VAL B CG2 1 
ATOM   1842 N N   . GLY B 2 45  ? -8.27900  -34.29145 11.07870  1.000 48.72000  ? 45   GLY B N   1 
ATOM   1843 C CA  . GLY B 2 45  ? -7.33584  -33.93910 12.11832  1.000 41.21000  ? 45   GLY B CA  1 
ATOM   1844 C C   . GLY B 2 45  ? -6.60017  -35.09872 12.75539  1.000 42.03000  ? 45   GLY B C   1 
ATOM   1845 O O   . GLY B 2 45  ? -5.73248  -34.86418 13.60353  1.000 42.96000  ? 45   GLY B O   1 
ATOM   1846 N N   . GLU B 2 46  ? -6.90886  -36.33553 12.37864  1.000 43.22000  ? 46   GLU B N   1 
ATOM   1847 C CA  . GLU B 2 46  ? -6.20755  -37.48766 12.92072  1.000 44.79000  ? 46   GLU B CA  1 
ATOM   1848 C C   . GLU B 2 46  ? -6.23578  -38.60512 11.88934  1.000 39.62000  ? 46   GLU B C   1 
ATOM   1849 O O   . GLU B 2 46  ? -6.96522  -38.54543 10.89557  1.000 44.02000  ? 46   GLU B O   1 
ATOM   1850 C CB  . GLU B 2 46  ? -6.82663  -37.95388 14.24477  1.000 48.82000  ? 46   GLU B CB  1 
ATOM   1851 C CG  . GLU B 2 46  ? -8.21667  -38.57390 14.10877  1.000 54.53000  ? 46   GLU B CG  1 
ATOM   1852 C CD  . GLU B 2 46  ? -8.82462  -38.97373 15.45013  1.000 61.24000  ? 46   GLU B CD  1 
ATOM   1853 O OE1 . GLU B 2 46  ? -8.51534  -38.31988 16.47069  1.000 57.10000  ? 46   GLU B OE1 1 
ATOM   1854 O OE2 . GLU B 2 46  ? -9.61451  -39.94314 15.48281  1.000 67.50000  ? 46   GLU B OE2 1 
ATOM   1855 N N   . TYR B 2 47  ? -5.42421  -39.63037 12.13346  1.000 38.69000  ? 47   TYR B N   1 
ATOM   1856 C CA  . TYR B 2 47  ? -5.43875  -40.81453 11.29040  1.000 40.11000  ? 47   TYR B CA  1 
ATOM   1857 C C   . TYR B 2 47  ? -6.66879  -41.65727 11.58416  1.000 45.50000  ? 47   TYR B C   1 
ATOM   1858 O O   . TYR B 2 47  ? -7.06845  -41.82786 12.74099  1.000 47.22000  ? 47   TYR B O   1 
ATOM   1859 C CB  . TYR B 2 47  ? -4.17914  -41.64875 11.50433  1.000 39.76000  ? 47   TYR B CB  1 
ATOM   1860 C CG  . TYR B 2 47  ? -2.97402  -41.08771 10.79808  1.000 38.03000  ? 47   TYR B CG  1 
ATOM   1861 C CD1 . TYR B 2 47  ? -2.17264  -40.13298 11.40837  1.000 39.23000  ? 47   TYR B CD1 1 
ATOM   1862 C CD2 . TYR B 2 47  ? -2.64545  -41.49682 9.51494   1.000 37.76000  ? 47   TYR B CD2 1 
ATOM   1863 C CE1 . TYR B 2 47  ? -1.07405  -39.61013 10.76635  1.000 36.71000  ? 47   TYR B CE1 1 
ATOM   1864 C CE2 . TYR B 2 47  ? -1.54233  -40.97533 8.86368   1.000 37.79000  ? 47   TYR B CE2 1 
ATOM   1865 C CZ  . TYR B 2 47  ? -0.76414  -40.03329 9.49567   1.000 34.95000  ? 47   TYR B CZ  1 
ATOM   1866 O OH  . TYR B 2 47  ? 0.33091   -39.50975 8.85302   1.000 39.70000  ? 47   TYR B OH  1 
ATOM   1867 N N   . ARG B 2 48  ? -7.26628  -42.18513 10.52343  1.000 46.57000  ? 48   ARG B N   1 
ATOM   1868 C CA  . ARG B 2 48  ? -8.41677  -43.06470 10.62503  1.000 48.07000  ? 48   ARG B CA  1 
ATOM   1869 C C   . ARG B 2 48  ? -8.17424  -44.25848 9.72192   1.000 50.83000  ? 48   ARG B C   1 
ATOM   1870 O O   . ARG B 2 48  ? -7.75198  -44.09154 8.57073   1.000 47.10000  ? 48   ARG B O   1 
ATOM   1871 C CB  . ARG B 2 48  ? -9.70632  -42.34733 10.22228  1.000 47.35000  ? 48   ARG B CB  1 
ATOM   1872 C CG  . ARG B 2 48  ? -10.10909 -41.22356 11.15292  1.000 47.02000  ? 48   ARG B CG  1 
ATOM   1873 C CD  . ARG B 2 48  ? -10.70219 -41.76040 12.43666  1.000 51.01000  ? 48   ARG B CD  1 
ATOM   1874 N NE  . ARG B 2 48  ? -11.04970 -40.68508 13.35729  1.000 54.86000  ? 48   ARG B NE  1 
ATOM   1875 C CZ  . ARG B 2 48  ? -12.19614 -40.01869 13.32028  1.000 58.63000  ? 48   ARG B CZ  1 
ATOM   1876 N NH1 . ARG B 2 48  ? -13.11802 -40.28189 12.40765  1.000 57.01000  ? 48   ARG B NH1 1 
ATOM   1877 N NH2 . ARG B 2 48  ? -12.42421 -39.06593 14.22103  1.000 60.63000  ? 48   ARG B NH2 1 
ATOM   1878 N N   . ALA B 2 49  ? -8.41994  -45.45532 10.25201  1.000 47.14000  ? 49   ALA B N   1 
ATOM   1879 C CA  . ALA B 2 49  ? -8.31525  -46.65666 9.44044   1.000 48.78000  ? 49   ALA B CA  1 
ATOM   1880 C C   . ALA B 2 49  ? -9.34393  -46.60489 8.31640   1.000 49.25000  ? 49   ALA B C   1 
ATOM   1881 O O   . ALA B 2 49  ? -10.42723 -46.03421 8.47103   1.000 49.83000  ? 49   ALA B O   1 
ATOM   1882 C CB  . ALA B 2 49  ? -8.51290  -47.90136 10.31027  1.000 46.88000  ? 49   ALA B CB  1 
ATOM   1883 N N   . VAL B 2 50  ? -8.98709  -47.16600 7.16269   1.000 50.04000  ? 50   VAL B N   1 
ATOM   1884 C CA  . VAL B 2 50  ? -9.89932  -47.18947 6.02553   1.000 47.11000  ? 50   VAL B CA  1 
ATOM   1885 C C   . VAL B 2 50  ? -10.41357 -48.61143 5.85445   1.000 52.66000  ? 50   VAL B C   1 
ATOM   1886 O O   . VAL B 2 50  ? -11.54362 -48.82785 5.40061   1.000 50.49000  ? 50   VAL B O   1 
ATOM   1887 C CB  . VAL B 2 50  ? -9.21755  -46.66203 4.75176   1.000 45.65000  ? 50   VAL B CB  1 
ATOM   1888 C CG1 . VAL B 2 50  ? -10.21185 -46.58792 3.60060   1.000 42.45000  ? 50   VAL B CG1 1 
ATOM   1889 C CG2 . VAL B 2 50  ? -8.64114  -45.28379 5.01988   1.000 44.57000  ? 50   VAL B CG2 1 
ATOM   1890 N N   . THR B 2 51  ? -9.58818  -49.58867 6.22057   1.000 47.36000  ? 51   THR B N   1 
ATOM   1891 C CA  . THR B 2 51  ? -10.00901 -50.97611 6.31596   1.000 51.04000  ? 51   THR B CA  1 
ATOM   1892 C C   . THR B 2 51  ? -9.57331  -51.51943 7.66592   1.000 56.43000  ? 51   THR B C   1 
ATOM   1893 O O   . THR B 2 51  ? -8.96227  -50.81855 8.47852   1.000 55.19000  ? 51   THR B O   1 
ATOM   1894 C CB  . THR B 2 51  ? -9.43475  -51.84202 5.18567   1.000 46.81000  ? 51   THR B CB  1 
ATOM   1895 O OG1 . THR B 2 51  ? -8.01385  -51.67345 5.12091   1.000 46.98000  ? 51   THR B OG1 1 
ATOM   1896 C CG2 . THR B 2 51  ? -10.05322 -51.46886 3.84678   1.000 46.64000  ? 51   THR B CG2 1 
ATOM   1897 N N   . GLU B 2 52  ? -9.90800  -52.78865 7.89872   1.000 61.56000  ? 52   GLU B N   1 
ATOM   1898 C CA  . GLU B 2 52  ? -9.49845  -53.45195 9.12934   1.000 62.38000  ? 52   GLU B CA  1 
ATOM   1899 C C   . GLU B 2 52  ? -7.98202  -53.51716 9.24458   1.000 56.92000  ? 52   GLU B C   1 
ATOM   1900 O O   . GLU B 2 52  ? -7.43777  -53.47088 10.35507  1.000 54.04000  ? 52   GLU B O   1 
ATOM   1901 C CB  . GLU B 2 52  ? -10.10512 -54.85448 9.18149   1.000 67.15000  ? 52   GLU B CB  1 
ATOM   1902 N N   . LEU B 2 53  ? -7.28976  -53.59853 8.10604   1.000 52.14000  ? 53   LEU B N   1 
ATOM   1903 C CA  . LEU B 2 53  ? -5.83723  -53.70530 8.08308   1.000 49.12000  ? 53   LEU B CA  1 
ATOM   1904 C C   . LEU B 2 53  ? -5.14486  -52.49377 8.69201   1.000 48.99000  ? 53   LEU B C   1 
ATOM   1905 O O   . LEU B 2 53  ? -3.95680  -52.57772 9.02097   1.000 53.56000  ? 53   LEU B O   1 
ATOM   1906 C CB  . LEU B 2 53  ? -5.36767  -53.89032 6.64070   1.000 52.86000  ? 53   LEU B CB  1 
ATOM   1907 C CG  . LEU B 2 53  ? -4.17737  -54.80388 6.36689   1.000 55.04000  ? 53   LEU B CG  1 
ATOM   1908 C CD1 . LEU B 2 53  ? -4.36346  -56.14866 7.04254   1.000 59.86000  ? 53   LEU B CD1 1 
ATOM   1909 C CD2 . LEU B 2 53  ? -3.98260  -54.96398 4.86968   1.000 57.11000  ? 53   LEU B CD2 1 
ATOM   1910 N N   . GLY B 2 54  ? -5.84845  -51.37428 8.84647   1.000 51.54000  ? 54   GLY B N   1 
ATOM   1911 C CA  . GLY B 2 54  ? -5.25155  -50.13814 9.29871   1.000 48.03000  ? 54   GLY B CA  1 
ATOM   1912 C C   . GLY B 2 54  ? -5.54355  -49.72820 10.71975  1.000 50.70000  ? 54   GLY B C   1 
ATOM   1913 O O   . GLY B 2 54  ? -5.08482  -48.66274 11.14436  1.000 60.24000  ? 54   GLY B O   1 
ATOM   1914 N N   . ARG B 2 55  ? -6.29870  -50.52802 11.47040  1.000 52.10000  ? 55   ARG B N   1 
ATOM   1915 C CA  . ARG B 2 55  ? -6.55291  -50.19837 12.87247  1.000 53.46000  ? 55   ARG B CA  1 
ATOM   1916 C C   . ARG B 2 55  ? -5.27188  -50.02827 13.68117  1.000 48.28000  ? 55   ARG B C   1 
ATOM   1917 O O   . ARG B 2 55  ? -5.17126  -49.03460 14.42290  1.000 50.06000  ? 55   ARG B O   1 
ATOM   1918 C CB  . ARG B 2 55  ? -7.47367  -51.25431 13.49602  1.000 60.57000  ? 55   ARG B CB  1 
ATOM   1919 C CG  . ARG B 2 55  ? -8.95218  -51.01178 13.25267  1.000 65.31000  ? 55   ARG B CG  1 
ATOM   1920 C CD  . ARG B 2 55  ? -9.73628  -52.31141 13.28462  1.000 76.55000  ? 55   ARG B CD  1 
ATOM   1921 N NE  . ARG B 2 55  ? -10.96768 -52.18609 14.05597  1.000 86.36000  ? 55   ARG B NE  1 
ATOM   1922 C CZ  . ARG B 2 55  ? -11.54095 -53.18035 14.72149  1.000 95.65000  ? 55   ARG B CZ  1 
ATOM   1923 N NH1 . ARG B 2 55  ? -11.02702 -54.39940 14.72128  1.000 97.35000  ? 55   ARG B NH1 1 
ATOM   1924 N NH2 . ARG B 2 55  ? -12.65906 -52.94598 15.40361  1.000 96.12000  ? 55   ARG B NH2 1 
ATOM   1925 N N   . PRO B 2 56  ? -4.26965  -50.92039 13.59689  1.000 43.88000  ? 56   PRO B N   1 
ATOM   1926 C CA  . PRO B 2 56  ? -3.03846  -50.69487 14.38338  1.000 47.58000  ? 56   PRO B CA  1 
ATOM   1927 C C   . PRO B 2 56  ? -2.37554  -49.35339 14.11836  1.000 48.38000  ? 56   PRO B C   1 
ATOM   1928 O O   . PRO B 2 56  ? -1.99729  -48.65269 15.06527  1.000 57.82000  ? 56   PRO B O   1 
ATOM   1929 C CB  . PRO B 2 56  ? -2.13266  -51.86237 13.96054  1.000 48.52000  ? 56   PRO B CB  1 
ATOM   1930 C CG  . PRO B 2 56  ? -3.03211  -52.90642 13.46991  1.000 47.78000  ? 56   PRO B CG  1 
ATOM   1931 C CD  . PRO B 2 56  ? -4.25379  -52.23367 12.92265  1.000 46.85000  ? 56   PRO B CD  1 
ATOM   1932 N N   . ASP B 2 57  ? -2.22471  -48.97296 12.84862  1.000 47.94000  ? 57   ASP B N   1 
ATOM   1933 C CA  . ASP B 2 57  ? -1.49376  -47.75181 12.52813  1.000 46.07000  ? 57   ASP B CA  1 
ATOM   1934 C C   . ASP B 2 57  ? -2.22877  -46.51655 13.02591  1.000 42.88000  ? 57   ASP B C   1 
ATOM   1935 O O   . ASP B 2 57  ? -1.60817  -45.60606 13.58940  1.000 39.90000  ? 57   ASP B O   1 
ATOM   1936 C CB  . ASP B 2 57  ? -1.26539  -47.66402 11.02215  1.000 50.48000  ? 57   ASP B CB  1 
ATOM   1937 C CG  . ASP B 2 57  ? -0.47660  -48.83205 10.49430  1.000 52.86000  ? 57   ASP B CG  1 
ATOM   1938 O OD1 . ASP B 2 57  ? 0.57297   -49.15491 11.08122  1.000 52.80000  ? 57   ASP B OD1 1 
ATOM   1939 O OD2 . ASP B 2 57  ? -0.91864  -49.44036 9.50324   1.000 56.34000  ? 57   ASP B OD2 1 
ATOM   1940 N N   . ALA B 2 58  ? -3.54821  -46.46438 12.82083  1.000 46.28000  ? 58   ALA B N   1 
ATOM   1941 C CA  . ALA B 2 58  ? -4.32130  -45.30417 13.25276  1.000 48.91000  ? 58   ALA B CA  1 
ATOM   1942 C C   . ALA B 2 58  ? -4.14191  -45.05403 14.74458  1.000 49.07000  ? 58   ALA B C   1 
ATOM   1943 O O   . ALA B 2 58  ? -3.82532  -43.93605 15.16246  1.000 51.28000  ? 58   ALA B O   1 
ATOM   1944 C CB  . ALA B 2 58  ? -5.79778  -45.49596 12.90509  1.000 51.52000  ? 58   ALA B CB  1 
ATOM   1945 N N   . GLU B 2 59  ? -4.30514  -46.09801 15.56247  1.000 53.26000  ? 59   GLU B N   1 
ATOM   1946 C CA  . GLU B 2 59  ? -4.12929  -45.94170 17.00356  1.000 51.53000  ? 59   GLU B CA  1 
ATOM   1947 C C   . GLU B 2 59  ? -2.69681  -45.54984 17.35252  1.000 50.74000  ? 59   GLU B C   1 
ATOM   1948 O O   . GLU B 2 59  ? -2.47354  -44.63812 18.15935  1.000 56.33000  ? 59   GLU B O   1 
ATOM   1949 C CB  . GLU B 2 59  ? -4.52281  -47.23287 17.72145  1.000 55.70000  ? 59   GLU B CB  1 
ATOM   1950 N N   . TYR B 2 60  ? -1.71331  -46.21609 16.74192  1.000 49.39000  ? 60   TYR B N   1 
ATOM   1951 C CA  . TYR B 2 60  ? -0.31487  -45.99169 17.10247  1.000 49.18000  ? 60   TYR B CA  1 
ATOM   1952 C C   . TYR B 2 60  ? 0.13287   -44.57211 16.76569  1.000 46.68000  ? 60   TYR B C   1 
ATOM   1953 O O   . TYR B 2 60  ? 0.72675   -43.88143 17.60122  1.000 50.21000  ? 60   TYR B O   1 
ATOM   1954 C CB  . TYR B 2 60  ? 0.56429   -47.02231 16.39726  1.000 49.91000  ? 60   TYR B CB  1 
ATOM   1955 C CG  . TYR B 2 60  ? 2.04778   -46.81716 16.57935  1.000 54.01000  ? 60   TYR B CG  1 
ATOM   1956 C CD1 . TYR B 2 60  ? 2.64591   -46.97718 17.82065  1.000 58.92000  ? 60   TYR B CD1 1 
ATOM   1957 C CD2 . TYR B 2 60  ? 2.85535   -46.48608 15.50188  1.000 54.34000  ? 60   TYR B CD2 1 
ATOM   1958 C CE1 . TYR B 2 60  ? 4.00692   -46.80160 17.98412  1.000 59.32000  ? 60   TYR B CE1 1 
ATOM   1959 C CE2 . TYR B 2 60  ? 4.21268   -46.30625 15.65358  1.000 55.66000  ? 60   TYR B CE2 1 
ATOM   1960 C CZ  . TYR B 2 60  ? 4.78518   -46.46583 16.89591  1.000 59.87000  ? 60   TYR B CZ  1 
ATOM   1961 O OH  . TYR B 2 60  ? 6.14124   -46.28389 17.04454  1.000 59.75000  ? 60   TYR B OH  1 
ATOM   1962 N N   . TRP B 2 61  ? -0.13374  -44.11896 15.54095  1.000 47.72000  ? 61   TRP B N   1 
ATOM   1963 C CA  . TRP B 2 61  ? 0.29300   -42.77737 15.16172  1.000 46.20000  ? 61   TRP B CA  1 
ATOM   1964 C C   . TRP B 2 61  ? -0.51937  -41.70857 15.87693  1.000 46.38000  ? 61   TRP B C   1 
ATOM   1965 O O   . TRP B 2 61  ? 0.00476   -40.62541 16.16419  1.000 47.21000  ? 61   TRP B O   1 
ATOM   1966 C CB  . TRP B 2 61  ? 0.19251   -42.59501 13.64562  1.000 45.55000  ? 61   TRP B CB  1 
ATOM   1967 C CG  . TRP B 2 61  ? 1.09007   -43.51077 12.86966  1.000 44.68000  ? 61   TRP B CG  1 
ATOM   1968 C CD1 . TRP B 2 61  ? 2.26064   -44.06002 13.29628  1.000 40.26000  ? 61   TRP B CD1 1 
ATOM   1969 C CD2 . TRP B 2 61  ? 0.89060   -43.98044 11.52740  1.000 40.64000  ? 61   TRP B CD2 1 
ATOM   1970 N NE1 . TRP B 2 61  ? 2.80286   -44.84649 12.30700  1.000 42.44000  ? 61   TRP B NE1 1 
ATOM   1971 C CE2 . TRP B 2 61  ? 1.98337   -44.81199 11.21003  1.000 36.71000  ? 61   TRP B CE2 1 
ATOM   1972 C CE3 . TRP B 2 61  ? -0.10410  -43.77657 10.56442  1.000 37.69000  ? 61   TRP B CE3 1 
ATOM   1973 C CZ2 . TRP B 2 61  ? 2.11198   -45.43881 9.97033   1.000 36.60000  ? 61   TRP B CZ2 1 
ATOM   1974 C CZ3 . TRP B 2 61  ? 0.02816   -44.39714 9.33056   1.000 38.08000  ? 61   TRP B CZ3 1 
ATOM   1975 C CH2 . TRP B 2 61  ? 1.12605   -45.22196 9.04752   1.000 38.13000  ? 61   TRP B CH2 1 
ATOM   1976 N N   . ASN B 2 62  ? -1.79278  -41.98736 16.17362  1.000 51.38000  ? 62   ASN B N   1 
ATOM   1977 C CA  . ASN B 2 62  ? -2.61722  -41.00099 16.86120  1.000 52.26000  ? 62   ASN B CA  1 
ATOM   1978 C C   . ASN B 2 62  ? -2.19765  -40.80215 18.31204  1.000 54.93000  ? 62   ASN B C   1 
ATOM   1979 O O   . ASN B 2 62  ? -2.57444  -39.79453 18.91732  1.000 62.94000  ? 62   ASN B O   1 
ATOM   1980 C CB  . ASN B 2 62  ? -4.09142  -41.39937 16.78828  1.000 50.77000  ? 62   ASN B CB  1 
ATOM   1981 C CG  . ASN B 2 62  ? -4.72888  -41.03346 15.45636  1.000 51.23000  ? 62   ASN B CG  1 
ATOM   1982 O OD1 . ASN B 2 62  ? -4.21892  -40.18468 14.72695  1.000 49.26000  ? 62   ASN B OD1 1 
ATOM   1983 N ND2 . ASN B 2 62  ? -5.84541  -41.67743 15.13168  1.000 49.55000  ? 62   ASN B ND2 1 
ATOM   1984 N N   . SER B 2 63  ? -1.42342  -41.72385 18.88029  1.000 55.82000  ? 63   SER B N   1 
ATOM   1985 C CA  . SER B 2 63  ? -0.96321  -41.61189 20.25937  1.000 56.17000  ? 63   SER B CA  1 
ATOM   1986 C C   . SER B 2 63  ? 0.32318   -40.80645 20.39031  1.000 55.71000  ? 63   SER B C   1 
ATOM   1987 O O   . SER B 2 63  ? 0.88533   -40.73290 21.48678  1.000 57.53000  ? 63   SER B O   1 
ATOM   1988 C CB  . SER B 2 63  ? -0.77120  -43.00503 20.86578  1.000 53.60000  ? 63   SER B CB  1 
ATOM   1989 O OG  . SER B 2 63  ? 0.38702   -43.63891 20.35285  1.000 51.72000  ? 63   SER B OG  1 
ATOM   1990 N N   . GLN B 2 64  ? 0.79516   -40.20121 19.30403  1.000 54.69000  ? 64   GLN B N   1 
ATOM   1991 C CA  . GLN B 2 64  ? 2.03241   -39.42516 19.28887  1.000 52.79000  ? 64   GLN B CA  1 
ATOM   1992 C C   . GLN B 2 64  ? 1.67248   -37.98996 18.91962  1.000 54.68000  ? 64   GLN B C   1 
ATOM   1993 O O   . GLN B 2 64  ? 1.46398   -37.67854 17.74219  1.000 55.19000  ? 64   GLN B O   1 
ATOM   1994 C CB  . GLN B 2 64  ? 3.03329   -40.02919 18.31296  1.000 54.47000  ? 64   GLN B CB  1 
ATOM   1995 C CG  . GLN B 2 64  ? 2.88042   -41.53065 18.16384  1.000 58.37000  ? 64   GLN B CG  1 
ATOM   1996 C CD  . GLN B 2 64  ? 4.12336   -42.19154 17.62093  1.000 60.51000  ? 64   GLN B CD  1 
ATOM   1997 O OE1 . GLN B 2 64  ? 5.20908   -41.61581 17.65555  1.000 60.77000  ? 64   GLN B OE1 1 
ATOM   1998 N NE2 . GLN B 2 64  ? 3.97500   -43.41404 17.12225  1.000 61.59000  ? 64   GLN B NE2 1 
ATOM   1999 N N   . LYS B 2 65  ? 1.60297   -37.12156 19.93393  1.000 57.09000  ? 65   LYS B N   1 
ATOM   2000 C CA  . LYS B 2 65  ? 1.12520   -35.75797 19.72263  1.000 59.55000  ? 65   LYS B CA  1 
ATOM   2001 C C   . LYS B 2 65  ? 2.03414   -34.98573 18.77454  1.000 58.96000  ? 65   LYS B C   1 
ATOM   2002 O O   . LYS B 2 65  ? 1.55207   -34.23257 17.91940  1.000 63.45000  ? 65   LYS B O   1 
ATOM   2003 C CB  . LYS B 2 65  ? 1.00617   -35.03000 21.06290  1.000 59.19000  ? 65   LYS B CB  1 
ATOM   2004 N N   . ASP B 2 66  ? 3.35211   -35.15429 18.91032  1.000 58.19000  ? 66   ASP B N   1 
ATOM   2005 C CA  . ASP B 2 66  ? 4.27326   -34.46628 18.01228  1.000 65.81000  ? 66   ASP B CA  1 
ATOM   2006 C C   . ASP B 2 66  ? 4.07216   -34.90527 16.56716  1.000 56.77000  ? 66   ASP B C   1 
ATOM   2007 O O   . ASP B 2 66  ? 4.36481   -34.14498 15.63872  1.000 54.74000  ? 66   ASP B O   1 
ATOM   2008 C CB  . ASP B 2 66  ? 5.71740   -34.70994 18.45419  1.000 71.35000  ? 66   ASP B CB  1 
ATOM   2009 N N   . LEU B 2 67  ? 3.56621   -36.11933 16.35954  1.000 50.68000  ? 67   LEU B N   1 
ATOM   2010 C CA  . LEU B 2 67  ? 3.30979   -36.61119 15.01280  1.000 52.77000  ? 67   LEU B CA  1 
ATOM   2011 C C   . LEU B 2 67  ? 2.05344   -35.97853 14.42930  1.000 51.89000  ? 67   LEU B C   1 
ATOM   2012 O O   . LEU B 2 67  ? 2.04707   -35.53546 13.27496  1.000 44.64000  ? 67   LEU B O   1 
ATOM   2013 C CB  . LEU B 2 67  ? 3.18337   -38.13255 15.03846  1.000 56.26000  ? 67   LEU B CB  1 
ATOM   2014 C CG  . LEU B 2 67  ? 3.94482   -38.93330 13.99015  1.000 63.48000  ? 67   LEU B CG  1 
ATOM   2015 C CD1 . LEU B 2 67  ? 5.44374   -38.68494 14.10581  1.000 70.30000  ? 67   LEU B CD1 1 
ATOM   2016 C CD2 . LEU B 2 67  ? 3.62265   -40.40597 14.16662  1.000 60.20000  ? 67   LEU B CD2 1 
ATOM   2017 N N   . LEU B 2 68  ? 0.97669   -35.93061 15.21274  1.000 49.82000  ? 68   LEU B N   1 
ATOM   2018 C CA  . LEU B 2 68  ? -0.24103  -35.29675 14.72873  1.000 55.67000  ? 68   LEU B CA  1 
ATOM   2019 C C   . LEU B 2 68  ? -0.02690  -33.81011 14.50138  1.000 49.49000  ? 68   LEU B C   1 
ATOM   2020 O O   . LEU B 2 68  ? -0.55140  -33.24005 13.53873  1.000 47.22000  ? 68   LEU B O   1 
ATOM   2021 C CB  . LEU B 2 68  ? -1.38341  -35.52921 15.71091  1.000 56.97000  ? 68   LEU B CB  1 
ATOM   2022 C CG  . LEU B 2 68  ? -1.90006  -36.96046 15.75082  1.000 59.81000  ? 68   LEU B CG  1 
ATOM   2023 C CD1 . LEU B 2 68  ? -2.42000  -37.27716 17.13528  1.000 59.62000  ? 68   LEU B CD1 1 
ATOM   2024 C CD2 . LEU B 2 68  ? -2.97773  -37.14788 14.70120  1.000 62.60000  ? 68   LEU B CD2 1 
ATOM   2025 N N   . GLU B 2 69  ? 0.74870   -33.16475 15.37053  1.000 50.30000  ? 69   GLU B N   1 
ATOM   2026 C CA  . GLU B 2 69  ? 0.97495   -31.73460 15.21274  1.000 57.54000  ? 69   GLU B CA  1 
ATOM   2027 C C   . GLU B 2 69  ? 1.79213   -31.43052 13.96500  1.000 53.77000  ? 69   GLU B C   1 
ATOM   2028 O O   . GLU B 2 69  ? 1.69782   -30.32799 13.41439  1.000 55.76000  ? 69   GLU B O   1 
ATOM   2029 C CB  . GLU B 2 69  ? 1.66218   -31.17661 16.45586  1.000 61.69000  ? 69   GLU B CB  1 
ATOM   2030 C CG  . GLU B 2 69  ? 1.54187   -29.66972 16.61342  1.000 72.47000  ? 69   GLU B CG  1 
ATOM   2031 C CD  . GLU B 2 69  ? 0.20667   -29.22439 17.19690  1.000 82.56000  ? 69   GLU B CD  1 
ATOM   2032 O OE1 . GLU B 2 69  ? 0.17975   -28.16100 17.85677  1.000 82.76000  ? 69   GLU B OE1 1 
ATOM   2033 O OE2 . GLU B 2 69  ? -0.81332  -29.92272 16.99783  1.000 83.29000  ? 69   GLU B OE2 1 
ATOM   2034 N N   . GLN B 2 70  ? 2.59690   -32.38758 13.50683  1.000 52.38000  ? 70   GLN B N   1 
ATOM   2035 C CA  . GLN B 2 70  ? 3.34104   -32.19888 12.26792  1.000 55.08000  ? 70   GLN B CA  1 
ATOM   2036 C C   . GLN B 2 70  ? 2.43131   -32.35828 11.05585  1.000 43.79000  ? 70   GLN B C   1 
ATOM   2037 O O   . GLN B 2 70  ? 2.50446   -31.56362 10.11234  1.000 40.65000  ? 70   GLN B O   1 
ATOM   2038 C CB  . GLN B 2 70  ? 4.50889   -33.18553 12.20731  1.000 58.73000  ? 70   GLN B CB  1 
ATOM   2039 C CG  . GLN B 2 70  ? 5.54773   -32.88076 11.14248  1.000 69.81000  ? 70   GLN B CG  1 
ATOM   2040 C CD  . GLN B 2 70  ? 6.78537   -33.75728 11.27185  1.000 79.14000  ? 70   GLN B CD  1 
ATOM   2041 O OE1 . GLN B 2 70  ? 7.91870   -33.28128 11.15855  1.000 73.83000  ? 70   GLN B OE1 1 
ATOM   2042 N NE2 . GLN B 2 70  ? 6.57077   -35.04743 11.51457  1.000 78.32000  ? 70   GLN B NE2 1 
ATOM   2043 N N   . LYS B 2 71  ? 1.55462   -33.36545 11.07709  1.000 40.32000  ? 71   LYS B N   1 
ATOM   2044 C CA  . LYS B 2 71  ? 0.64729   -33.58466 9.95713   1.000 40.62000  ? 71   LYS B CA  1 
ATOM   2045 C C   . LYS B 2 71  ? -0.43182  -32.51283 9.88085   1.000 43.62000  ? 71   LYS B C   1 
ATOM   2046 O O   . LYS B 2 71  ? -0.92224  -32.21132 8.78726   1.000 46.94000  ? 71   LYS B O   1 
ATOM   2047 C CB  . LYS B 2 71  ? 0.00625   -34.96470 10.06284  1.000 42.15000  ? 71   LYS B CB  1 
ATOM   2048 C CG  . LYS B 2 71  ? 0.97825   -36.11073 9.88102   1.000 45.86000  ? 71   LYS B CG  1 
ATOM   2049 C CD  . LYS B 2 71  ? 1.51379   -36.18118 8.46235   1.000 48.01000  ? 71   LYS B CD  1 
ATOM   2050 C CE  . LYS B 2 71  ? 2.81873   -36.96018 8.42536   1.000 49.46000  ? 71   LYS B CE  1 
ATOM   2051 N NZ  . LYS B 2 71  ? 2.88594   -37.87920 7.26240   1.000 48.22000  ? 71   LYS B NZ  1 
ATOM   2052 N N   . ARG B 2 72  ? -0.81932  -31.93330 11.01994  1.000 45.38000  ? 72   ARG B N   1 
ATOM   2053 C CA  . ARG B 2 72  ? -1.82404  -30.87837 11.01128  1.000 45.69000  ? 72   ARG B CA  1 
ATOM   2054 C C   . ARG B 2 72  ? -1.28092  -29.56352 10.47882  1.000 42.13000  ? 72   ARG B C   1 
ATOM   2055 O O   . ARG B 2 72  ? -2.06610  -28.71589 10.04508  1.000 42.41000  ? 72   ARG B O   1 
ATOM   2056 C CB  . ARG B 2 72  ? -2.37881  -30.66254 12.41355  1.000 47.65000  ? 72   ARG B CB  1 
ATOM   2057 C CG  . ARG B 2 72  ? -3.29730  -31.75966 12.87635  1.000 53.41000  ? 72   ARG B CG  1 
ATOM   2058 C CD  . ARG B 2 72  ? -3.45434  -31.72058 14.37487  1.000 56.85000  ? 72   ARG B CD  1 
ATOM   2059 N NE  . ARG B 2 72  ? -4.43834  -32.69362 14.82879  1.000 62.26000  ? 72   ARG B NE  1 
ATOM   2060 C CZ  . ARG B 2 72  ? -4.64030  -33.01442 16.09891  1.000 64.74000  ? 72   ARG B CZ  1 
ATOM   2061 N NH1 . ARG B 2 72  ? -3.94166  -32.45243 17.07328  1.000 61.33000  ? 72   ARG B NH1 1 
ATOM   2062 N NH2 . ARG B 2 72  ? -5.56557  -33.92186 16.39897  1.000 63.87000  ? 72   ARG B NH2 1 
ATOM   2063 N N   . ALA B 2 73  ? 0.03293   -29.36428 10.51259  1.000 37.06000  ? 73   ALA B N   1 
ATOM   2064 C CA  . ALA B 2 73  ? 0.64359   -28.19086 9.90177   1.000 36.96000  ? 73   ALA B CA  1 
ATOM   2065 C C   . ALA B 2 73  ? 1.08173   -28.44143 8.46353   1.000 34.86000  ? 73   ALA B C   1 
ATOM   2066 O O   . ALA B 2 73  ? 1.60589   -27.52304 7.82187   1.000 39.48000  ? 73   ALA B O   1 
ATOM   2067 C CB  . ALA B 2 73  ? 1.84197   -27.71719 10.73519  1.000 37.53000  ? 73   ALA B CB  1 
ATOM   2068 N N   . ALA B 2 74  ? 0.87004   -29.65821 7.94650   1.000 33.07000  ? 74   ALA B N   1 
ATOM   2069 C CA  . ALA B 2 74  ? 1.28671   -29.98156 6.58594   1.000 34.67000  ? 74   ALA B CA  1 
ATOM   2070 C C   . ALA B 2 74  ? 0.58744   -29.10917 5.55300   1.000 37.95000  ? 74   ALA B C   1 
ATOM   2071 O O   . ALA B 2 74  ? 1.18544   -28.78355 4.51904   1.000 37.94000  ? 74   ALA B O   1 
ATOM   2072 C CB  . ALA B 2 74  ? 1.02724   -31.45844 6.28966   1.000 39.66000  ? 74   ALA B CB  1 
ATOM   2073 N N   . VAL B 2 75  ? -0.66445  -28.70995 5.81099   1.000 38.58000  ? 75   VAL B N   1 
ATOM   2074 C CA  . VAL B 2 75  ? -1.36927  -27.85139 4.86048   1.000 39.59000  ? 75   VAL B CA  1 
ATOM   2075 C C   . VAL B 2 75  ? -0.59657  -26.56473 4.61159   1.000 40.66000  ? 75   VAL B C   1 
ATOM   2076 O O   . VAL B 2 75  ? -0.62916  -26.01950 3.50206   1.000 37.88000  ? 75   VAL B O   1 
ATOM   2077 C CB  . VAL B 2 75  ? -2.80067  -27.54723 5.34431   1.000 43.86000  ? 75   VAL B CB  1 
ATOM   2078 C CG1 . VAL B 2 75  ? -3.73478  -28.70457 5.01105   1.000 43.89000  ? 75   VAL B CG1 1 
ATOM   2079 C CG2 . VAL B 2 75  ? -2.80456  -27.22610 6.83426   1.000 43.44000  ? 75   VAL B CG2 1 
ATOM   2080 N N   . ASP B 2 76  ? 0.11259   -26.06154 5.62094   1.000 37.98000  ? 76   ASP B N   1 
ATOM   2081 C CA  . ASP B 2 76  ? 0.92625   -24.86117 5.46551   1.000 40.51000  ? 76   ASP B CA  1 
ATOM   2082 C C   . ASP B 2 76  ? 2.38852   -25.16973 5.16838   1.000 41.20000  ? 76   ASP B C   1 
ATOM   2083 O O   . ASP B 2 76  ? 2.94230   -24.65325 4.19403   1.000 37.27000  ? 76   ASP B O   1 
ATOM   2084 C CB  . ASP B 2 76  ? 0.82994   -23.98562 6.72117   1.000 43.71000  ? 76   ASP B CB  1 
ATOM   2085 C CG  . ASP B 2 76  ? -0.55160  -23.41387 6.91942   1.000 45.80000  ? 76   ASP B CG  1 
ATOM   2086 O OD1 . ASP B 2 76  ? -1.02624  -22.69752 6.01150   1.000 59.68000  ? 76   ASP B OD1 1 
ATOM   2087 O OD2 . ASP B 2 76  ? -1.16595  -23.68690 7.97609   1.000 46.98000  ? 76   ASP B OD2 1 
ATOM   2088 N N   . THR B 2 77  ? 3.02725   -26.00334 5.99343   1.000 42.07000  ? 77   THR B N   1 
ATOM   2089 C CA  . THR B 2 77  ? 4.45900   -26.24711 5.86108   1.000 37.83000  ? 77   THR B CA  1 
ATOM   2090 C C   . THR B 2 77  ? 4.80880   -27.07959 4.63678   1.000 36.95000  ? 77   THR B C   1 
ATOM   2091 O O   . THR B 2 77  ? 5.95344   -27.03341 4.17691   1.000 35.80000  ? 77   THR B O   1 
ATOM   2092 C CB  . THR B 2 77  ? 4.97911   -26.95818 7.10148   1.000 40.83000  ? 77   THR B CB  1 
ATOM   2093 O OG1 . THR B 2 77  ? 4.32498   -28.22591 7.21462   1.000 40.98000  ? 77   THR B OG1 1 
ATOM   2094 C CG2 . THR B 2 77  ? 4.68673   -26.13124 8.34210   1.000 44.17000  ? 77   THR B CG2 1 
ATOM   2095 N N   . TYR B 2 78  ? 3.86016   -27.84660 4.10705   1.000 32.97000  ? 78   TYR B N   1 
ATOM   2096 C CA  . TYR B 2 78  ? 4.13456   -28.77203 3.01428   1.000 33.62000  ? 78   TYR B CA  1 
ATOM   2097 C C   . TYR B 2 78  ? 3.33932   -28.42152 1.76354   1.000 33.00000  ? 78   TYR B C   1 
ATOM   2098 O O   . TYR B 2 78  ? 3.93319   -28.12533 0.72437   1.000 34.27000  ? 78   TYR B O   1 
ATOM   2099 C CB  . TYR B 2 78  ? 3.83844   -30.19984 3.49316   1.000 29.58000  ? 78   TYR B CB  1 
ATOM   2100 C CG  . TYR B 2 78  ? 3.90858   -31.26768 2.43375   1.000 30.70000  ? 78   TYR B CG  1 
ATOM   2101 C CD1 . TYR B 2 78  ? 5.12274   -31.62918 1.85910   1.000 32.53000  ? 78   TYR B CD1 1 
ATOM   2102 C CD2 . TYR B 2 78  ? 2.76202   -31.94191 2.03193   1.000 29.95000  ? 78   TYR B CD2 1 
ATOM   2103 C CE1 . TYR B 2 78  ? 5.18748   -32.61834 0.89518   1.000 29.12000  ? 78   TYR B CE1 1 
ATOM   2104 C CE2 . TYR B 2 78  ? 2.81421   -32.93221 1.07508   1.000 28.75000  ? 78   TYR B CE2 1 
ATOM   2105 C CZ  . TYR B 2 78  ? 4.02692   -33.26563 0.50938   1.000 29.95000  ? 78   TYR B CZ  1 
ATOM   2106 O OH  . TYR B 2 78  ? 4.06801   -34.25081 -0.44386  1.000 29.76000  ? 78   TYR B OH  1 
ATOM   2107 N N   . CYS B 2 79  ? 2.01087   -28.41135 1.84370   1.000 31.72000  ? 79   CYS B N   1 
ATOM   2108 C CA  . CYS B 2 79  ? 1.18392   -28.14476 0.67457   1.000 31.41000  ? 79   CYS B CA  1 
ATOM   2109 C C   . CYS B 2 79  ? 1.38931   -26.72725 0.15274   1.000 30.27000  ? 79   CYS B C   1 
ATOM   2110 O O   . CYS B 2 79  ? 1.76863   -26.52651 -1.00874  1.000 29.40000  ? 79   CYS B O   1 
ATOM   2111 C CB  . CYS B 2 79  ? -0.28044  -28.38139 1.03000   1.000 33.48000  ? 79   CYS B CB  1 
ATOM   2112 S SG  . CYS B 2 79  ? -0.64251  -30.08208 1.46565   1.000 35.66000  ? 79   CYS B SG  1 
ATOM   2113 N N   . ARG B 2 80  ? 1.12366   -25.72522 0.99516   1.000 31.95000  ? 80   ARG B N   1 
ATOM   2114 C CA  . ARG B 2 80  ? 1.19212   -24.34120 0.53501   1.000 33.90000  ? 80   ARG B CA  1 
ATOM   2115 C C   . ARG B 2 80  ? 2.61007   -23.95767 0.12868   1.000 32.09000  ? 80   ARG B C   1 
ATOM   2116 O O   . ARG B 2 80  ? 2.80671   -23.18602 -0.81724  1.000 34.08000  ? 80   ARG B O   1 
ATOM   2117 C CB  . ARG B 2 80  ? 0.66637   -23.39947 1.61846   1.000 37.01000  ? 80   ARG B CB  1 
ATOM   2118 C CG  . ARG B 2 80  ? -0.85068  -23.38481 1.72235   1.000 41.01000  ? 80   ARG B CG  1 
ATOM   2119 C CD  . ARG B 2 80  ? -1.34081  -22.29711 2.66593   1.000 42.81000  ? 80   ARG B CD  1 
ATOM   2120 N NE  . ARG B 2 80  ? -2.77477  -22.06571 2.53206   1.000 43.63000  ? 80   ARG B NE  1 
ATOM   2121 C CZ  . ARG B 2 80  ? -3.70739  -22.69805 3.23393   1.000 44.71000  ? 80   ARG B CZ  1 
ATOM   2122 N NH1 . ARG B 2 80  ? -3.39213  -23.60054 4.14817   1.000 45.34000  ? 80   ARG B NH1 1 
ATOM   2123 N NH2 . ARG B 2 80  ? -4.99023  -22.41767 3.01203   1.000 44.55000  ? 80   ARG B NH2 1 
ATOM   2124 N N   . HIS B 2 81  ? 3.61271   -24.48048 0.83365   1.000 33.73000  ? 81   HIS B N   1 
ATOM   2125 C CA  . HIS B 2 81  ? 4.99422   -24.21802 0.44605   1.000 31.76000  ? 81   HIS B CA  1 
ATOM   2126 C C   . HIS B 2 81  ? 5.28850   -24.79243 -0.93406  1.000 31.55000  ? 81   HIS B C   1 
ATOM   2127 O O   . HIS B 2 81  ? 5.80107   -24.09289 -1.81428  1.000 32.22000  ? 81   HIS B O   1 
ATOM   2128 C CB  . HIS B 2 81  ? 5.95258   -24.79979 1.48447   1.000 32.90000  ? 81   HIS B CB  1 
ATOM   2129 C CG  . HIS B 2 81  ? 7.38582   -24.76697 1.06017   1.000 33.78000  ? 81   HIS B CG  1 
ATOM   2130 N ND1 . HIS B 2 81  ? 8.21060   -23.69092 1.31076   1.000 38.76000  ? 81   HIS B ND1 1 
ATOM   2131 C CD2 . HIS B 2 81  ? 8.14350   -25.67557 0.40212   1.000 36.10000  ? 81   HIS B CD2 1 
ATOM   2132 C CE1 . HIS B 2 81  ? 9.41263   -23.93518 0.82073   1.000 38.37000  ? 81   HIS B CE1 1 
ATOM   2133 N NE2 . HIS B 2 81  ? 9.39979   -25.13423 0.26705   1.000 36.70000  ? 81   HIS B NE2 1 
ATOM   2134 N N   . ASN B 2 82  ? 4.96399   -26.07198 -1.14267  1.000 27.42000  ? 82   ASN B N   1 
ATOM   2135 C CA  . ASN B 2 82  ? 5.29008   -26.70968 -2.41292  1.000 28.58000  ? 82   ASN B CA  1 
ATOM   2136 C C   . ASN B 2 82  ? 4.50359   -26.10514 -3.56604  1.000 29.79000  ? 82   ASN B C   1 
ATOM   2137 O O   . ASN B 2 82  ? 5.01933   -26.02228 -4.68740  1.000 28.01000  ? 82   ASN B O   1 
ATOM   2138 C CB  . ASN B 2 82  ? 5.05126   -28.21478 -2.31869  1.000 27.05000  ? 82   ASN B CB  1 
ATOM   2139 C CG  . ASN B 2 82  ? 6.16452   -28.92023 -1.56999  1.000 26.41000  ? 82   ASN B CG  1 
ATOM   2140 O OD1 . ASN B 2 82  ? 7.21818   -28.32954 -1.32691  1.000 23.43000  ? 82   ASN B OD1 1 
ATOM   2141 N ND2 . ASN B 2 82  ? 5.93615   -30.17471 -1.18414  1.000 26.29000  ? 82   ASN B ND2 1 
ATOM   2142 N N   . TYR B 2 83  ? 3.27159   -25.66188 -3.31190  1.000 30.35000  ? 83   TYR B N   1 
ATOM   2143 C CA  . TYR B 2 83  ? 2.50933   -24.97311 -4.34798  1.000 33.10000  ? 83   TYR B CA  1 
ATOM   2144 C C   . TYR B 2 83  ? 3.25923   -23.74340 -4.83953  1.000 34.06000  ? 83   TYR B C   1 
ATOM   2145 O O   . TYR B 2 83  ? 3.37010   -23.50904 -6.04870  1.000 35.29000  ? 83   TYR B O   1 
ATOM   2146 C CB  . TYR B 2 83  ? 1.12978   -24.58738 -3.80893  1.000 33.72000  ? 83   TYR B CB  1 
ATOM   2147 C CG  . TYR B 2 83  ? 0.18774   -23.96765 -4.82193  1.000 34.74000  ? 83   TYR B CG  1 
ATOM   2148 C CD1 . TYR B 2 83  ? 0.28758   -22.62099 -5.16199  1.000 38.13000  ? 83   TYR B CD1 1 
ATOM   2149 C CD2 . TYR B 2 83  ? -0.81752  -24.71698 -5.41460  1.000 33.23000  ? 83   TYR B CD2 1 
ATOM   2150 C CE1 . TYR B 2 83  ? -0.57820  -22.04378 -6.06837  1.000 36.60000  ? 83   TYR B CE1 1 
ATOM   2151 C CE2 . TYR B 2 83  ? -1.68771  -24.14844 -6.32897  1.000 35.72000  ? 83   TYR B CE2 1 
ATOM   2152 C CZ  . TYR B 2 83  ? -1.56217  -22.80953 -6.65336  1.000 39.80000  ? 83   TYR B CZ  1 
ATOM   2153 O OH  . TYR B 2 83  ? -2.42249  -22.22631 -7.56123  1.000 41.41000  ? 83   TYR B OH  1 
ATOM   2154 N N   . GLY B 2 84  ? 3.78650   -22.94586 -3.90799  1.000 35.37000  ? 84   GLY B N   1 
ATOM   2155 C CA  . GLY B 2 84  ? 4.52131   -21.75550 -4.29194  1.000 34.66000  ? 84   GLY B CA  1 
ATOM   2156 C C   . GLY B 2 84  ? 5.83715   -22.06104 -4.97470  1.000 35.48000  ? 84   GLY B C   1 
ATOM   2157 O O   . GLY B 2 84  ? 6.30245   -21.27601 -5.80783  1.000 37.59000  ? 84   GLY B O   1 
ATOM   2158 N N   . VAL B 2 85  ? 6.45017   -23.20168 -4.64952  1.000 35.90000  ? 85   VAL B N   1 
ATOM   2159 C CA  . VAL B 2 85  ? 7.72820   -23.54957 -5.26515  1.000 35.68000  ? 85   VAL B CA  1 
ATOM   2160 C C   . VAL B 2 85  ? 7.56474   -23.72074 -6.77157  1.000 35.64000  ? 85   VAL B C   1 
ATOM   2161 O O   . VAL B 2 85  ? 8.37088   -23.21667 -7.56228  1.000 34.36000  ? 85   VAL B O   1 
ATOM   2162 C CB  . VAL B 2 85  ? 8.31734   -24.81437 -4.61390  1.000 36.83000  ? 85   VAL B CB  1 
ATOM   2163 C CG1 . VAL B 2 85  ? 9.51349   -25.30712 -5.40848  1.000 35.21000  ? 85   VAL B CG1 1 
ATOM   2164 C CG2 . VAL B 2 85  ? 8.72071   -24.52975 -3.17135  1.000 35.93000  ? 85   VAL B CG2 1 
ATOM   2165 N N   . GLY B 2 86  ? 6.50886   -24.41351 -7.19290  1.000 33.37000  ? 86   GLY B N   1 
ATOM   2166 C CA  . GLY B 2 86  ? 6.36574   -24.75573 -8.59504  1.000 32.22000  ? 86   GLY B CA  1 
ATOM   2167 C C   . GLY B 2 86  ? 5.26257   -24.03144 -9.34163  1.000 34.13000  ? 86   GLY B C   1 
ATOM   2168 O O   . GLY B 2 86  ? 4.99515   -24.33725 -10.51090 1.000 35.67000  ? 86   GLY B O   1 
ATOM   2169 N N   . GLU B 2 87  ? 4.62727   -23.05894 -8.68003  1.000 35.91000  ? 87   GLU B N   1 
ATOM   2170 C CA  . GLU B 2 87  ? 3.48398   -22.36984 -9.27149  1.000 38.11000  ? 87   GLU B CA  1 
ATOM   2171 C C   . GLU B 2 87  ? 3.79620   -21.82354 -10.66279 1.000 38.27000  ? 87   GLU B C   1 
ATOM   2172 O O   . GLU B 2 87  ? 2.97636   -21.94044 -11.58029 1.000 35.38000  ? 87   GLU B O   1 
ATOM   2173 C CB  . GLU B 2 87  ? 3.02059   -21.23929 -8.35291  1.000 41.36000  ? 87   GLU B CB  1 
ATOM   2174 C CG  . GLU B 2 87  ? 1.59708   -20.79129 -8.65498  1.000 51.53000  ? 87   GLU B CG  1 
ATOM   2175 C CD  . GLU B 2 87  ? 1.26423   -19.41583 -8.10322  1.000 57.91000  ? 87   GLU B CD  1 
ATOM   2176 O OE1 . GLU B 2 87  ? 1.80040   -19.04585 -7.03656  1.000 63.91000  ? 87   GLU B OE1 1 
ATOM   2177 O OE2 . GLU B 2 87  ? 0.46373   -18.70377 -8.74675  1.000 61.79000  ? 87   GLU B OE2 1 
ATOM   2178 N N   . SER B 2 88  ? 4.98818   -21.25027 -10.84759 1.000 34.01000  ? 88   SER B N   1 
ATOM   2179 C CA  . SER B 2 88  ? 5.28939   -20.57068 -12.10509 1.000 34.75000  ? 88   SER B CA  1 
ATOM   2180 C C   . SER B 2 88  ? 5.30724   -21.53530 -13.29145 1.000 36.87000  ? 88   SER B C   1 
ATOM   2181 O O   . SER B 2 88  ? 4.90007   -21.16226 -14.39735 1.000 38.93000  ? 88   SER B O   1 
ATOM   2182 C CB  . SER B 2 88  ? 6.62256   -19.83403 -11.99798 1.000 32.41000  ? 88   SER B CB  1 
ATOM   2183 O OG  . SER B 2 88  ? 7.68742   -20.75499 -11.85865 1.000 38.11000  ? 88   SER B OG  1 
ATOM   2184 N N   . PHE B 2 89  ? 5.76838   -22.77324 -13.09604 1.000 35.63000  ? 89   PHE B N   1 
ATOM   2185 C CA  . PHE B 2 89  ? 5.88422   -23.71837 -14.20387 1.000 32.21000  ? 89   PHE B CA  1 
ATOM   2186 C C   . PHE B 2 89  ? 4.86660   -24.85162 -14.16090 1.000 31.78000  ? 89   PHE B C   1 
ATOM   2187 O O   . PHE B 2 89  ? 4.92156   -25.74383 -15.01331 1.000 34.58000  ? 89   PHE B O   1 
ATOM   2188 C CB  . PHE B 2 89  ? 7.30285   -24.30379 -14.27491 1.000 31.99000  ? 89   PHE B CB  1 
ATOM   2189 C CG  . PHE B 2 89  ? 7.78781   -24.92786 -12.98866 1.000 33.89000  ? 89   PHE B CG  1 
ATOM   2190 C CD1 . PHE B 2 89  ? 7.52561   -26.26010 -12.70224 1.000 34.78000  ? 89   PHE B CD1 1 
ATOM   2191 C CD2 . PHE B 2 89  ? 8.53137   -24.18647 -12.08047 1.000 33.69000  ? 89   PHE B CD2 1 
ATOM   2192 C CE1 . PHE B 2 89  ? 7.98713   -26.83679 -11.53469 1.000 34.82000  ? 89   PHE B CE1 1 
ATOM   2193 C CE2 . PHE B 2 89  ? 8.99148   -24.75574 -10.90657 1.000 34.04000  ? 89   PHE B CE2 1 
ATOM   2194 C CZ  . PHE B 2 89  ? 8.72520   -26.08249 -10.63573 1.000 36.12000  ? 89   PHE B CZ  1 
ATOM   2195 N N   . THR B 2 90  ? 3.93559   -24.84029 -13.20673 1.000 30.76000  ? 90   THR B N   1 
ATOM   2196 C CA  . THR B 2 90  ? 2.87346   -25.84273 -13.15118 1.000 32.46000  ? 90   THR B CA  1 
ATOM   2197 C C   . THR B 2 90  ? 1.51237   -25.18411 -13.32443 1.000 34.60000  ? 90   THR B C   1 
ATOM   2198 O O   . THR B 2 90  ? 0.91189   -25.29945 -14.39546 1.000 36.26000  ? 90   THR B O   1 
ATOM   2199 C CB  . THR B 2 90  ? 2.93913   -26.61459 -11.83338 1.000 32.85000  ? 90   THR B CB  1 
ATOM   2200 O OG1 . THR B 2 90  ? 2.84803   -25.68151 -10.75116 1.000 32.36000  ? 90   THR B OG1 1 
ATOM   2201 C CG2 . THR B 2 90  ? 4.23966   -27.40019 -11.72393 1.000 31.53000  ? 90   THR B CG2 1 
ATOM   2202 N N   . VAL B 2 91  ? 1.01255   -24.48609 -12.29927 1.000 36.71000  ? 91   VAL B N   1 
ATOM   2203 C CA  . VAL B 2 91  ? -0.29189  -23.83226 -12.37167 1.000 35.43000  ? 91   VAL B CA  1 
ATOM   2204 C C   . VAL B 2 91  ? -0.33640  -22.82826 -13.52190 1.000 40.05000  ? 91   VAL B C   1 
ATOM   2205 O O   . VAL B 2 91  ? -1.36625  -22.67658 -14.18973 1.000 41.13000  ? 91   VAL B O   1 
ATOM   2206 C CB  . VAL B 2 91  ? -0.61376  -23.16504 -11.01866 1.000 37.11000  ? 91   VAL B CB  1 
ATOM   2207 C CG1 . VAL B 2 91  ? -1.89839  -22.36462 -11.09664 1.000 37.58000  ? 91   VAL B CG1 1 
ATOM   2208 C CG2 . VAL B 2 91  ? -0.69948  -24.20619 -9.90995  1.000 36.94000  ? 91   VAL B CG2 1 
ATOM   2209 N N   . GLN B 2 92  ? 0.77361   -22.12992 -13.77654 1.000 37.97000  ? 92   GLN B N   1 
ATOM   2210 C CA  . GLN B 2 92  ? 0.82176   -21.08199 -14.79269 1.000 39.76000  ? 92   GLN B CA  1 
ATOM   2211 C C   . GLN B 2 92  ? 1.38053   -21.55749 -16.12416 1.000 35.96000  ? 92   GLN B C   1 
ATOM   2212 O O   . GLN B 2 92  ? 1.55413   -20.73997 -17.03148 1.000 39.47000  ? 92   GLN B O   1 
ATOM   2213 C CB  . GLN B 2 92  ? 1.65098   -19.88700 -14.30325 1.000 40.50000  ? 92   GLN B CB  1 
ATOM   2214 C CG  . GLN B 2 92  ? 1.50150   -19.57140 -12.82898 1.000 44.23000  ? 92   GLN B CG  1 
ATOM   2215 C CD  . GLN B 2 92  ? 0.30205   -18.69376 -12.52687 1.000 54.28000  ? 92   GLN B CD  1 
ATOM   2216 O OE1 . GLN B 2 92  ? -0.82705  -19.00203 -12.91789 1.000 62.39000  ? 92   GLN B OE1 1 
ATOM   2217 N NE2 . GLN B 2 92  ? 0.53941   -17.59619 -11.81307 1.000 57.77000  ? 92   GLN B NE2 1 
ATOM   2218 N N   . ARG B 2 93  ? 1.67405   -22.84492 -16.26374 1.000 34.45000  ? 93   ARG B N   1 
ATOM   2219 C CA  . ARG B 2 93  ? 2.17374   -23.36271 -17.52769 1.000 31.04000  ? 93   ARG B CA  1 
ATOM   2220 C C   . ARG B 2 93  ? 1.04486   -23.39730 -18.54989 1.000 29.67000  ? 93   ARG B C   1 
ATOM   2221 O O   . ARG B 2 93  ? 0.00858   -24.02925 -18.32015 1.000 29.78000  ? 93   ARG B O   1 
ATOM   2222 C CB  . ARG B 2 93  ? 2.76812   -24.75203 -17.32907 1.000 32.37000  ? 93   ARG B CB  1 
ATOM   2223 C CG  . ARG B 2 93  ? 3.08561   -25.47810 -18.62030 1.000 32.81000  ? 93   ARG B CG  1 
ATOM   2224 C CD  . ARG B 2 93  ? 3.50568   -26.90867 -18.34819 1.000 34.17000  ? 93   ARG B CD  1 
ATOM   2225 N NE  . ARG B 2 93  ? 3.74696   -27.64313 -19.58254 1.000 39.07000  ? 93   ARG B NE  1 
ATOM   2226 C CZ  . ARG B 2 93  ? 4.88144   -27.60102 -20.26953 1.000 36.81000  ? 93   ARG B CZ  1 
ATOM   2227 N NH1 . ARG B 2 93  ? 5.91492   -26.88565 -19.85370 1.000 36.28000  ? 93   ARG B NH1 1 
ATOM   2228 N NH2 . ARG B 2 93  ? 4.98252   -28.29797 -21.39931 1.000 32.13000  ? 93   ARG B NH2 1 
ATOM   2229 N N   . ARG B 2 94  ? 1.24521   -22.71619 -19.67687 1.000 28.71000  ? 94   ARG B N   1 
ATOM   2230 C CA  . ARG B 2 94  ? 0.25338   -22.65692 -20.74316 1.000 33.36000  ? 94   ARG B CA  1 
ATOM   2231 C C   . ARG B 2 94  ? 0.97472   -22.75744 -22.07517 1.000 30.85000  ? 94   ARG B C   1 
ATOM   2232 O O   . ARG B 2 94  ? 1.80460   -21.90243 -22.40062 1.000 30.60000  ? 94   ARG B O   1 
ATOM   2233 C CB  . ARG B 2 94  ? -0.57069  -21.36865 -20.66199 1.000 37.26000  ? 94   ARG B CB  1 
ATOM   2234 C CG  . ARG B 2 94  ? -1.58605  -21.36843 -19.52457 1.000 42.92000  ? 94   ARG B CG  1 
ATOM   2235 C CD  . ARG B 2 94  ? -2.25183  -20.01464 -19.38916 1.000 53.42000  ? 94   ARG B CD  1 
ATOM   2236 N NE  . ARG B 2 94  ? -2.99028  -19.89281 -18.13856 1.000 60.61000  ? 94   ARG B NE  1 
ATOM   2237 C CZ  . ARG B 2 94  ? -2.56054  -19.22702 -17.07439 1.000 67.88000  ? 94   ARG B CZ  1 
ATOM   2238 N NH1 . ARG B 2 94  ? -1.40173  -18.58519 -17.08004 1.000 68.31000  ? 94   ARG B NH1 1 
ATOM   2239 N NH2 . ARG B 2 94  ? -3.31205  -19.20449 -15.97648 1.000 72.84000  ? 94   ARG B NH2 1 
ATOM   2240 N N   . VAL B 2 95  ? 0.66627   -23.80888 -22.83072 1.000 28.81000  ? 95   VAL B N   1 
ATOM   2241 C CA  . VAL B 2 95  ? 1.31312   -24.10478 -24.10238 1.000 30.63000  ? 95   VAL B CA  1 
ATOM   2242 C C   . VAL B 2 95  ? 0.23056   -24.21348 -25.16350 1.000 32.00000  ? 95   VAL B C   1 
ATOM   2243 O O   . VAL B 2 95  ? -0.74233  -24.95660 -24.98675 1.000 32.78000  ? 95   VAL B O   1 
ATOM   2244 C CB  . VAL B 2 95  ? 2.14345   -25.40119 -24.04117 1.000 33.31000  ? 95   VAL B CB  1 
ATOM   2245 C CG1 . VAL B 2 95  ? 2.81347   -25.67053 -25.39078 1.000 33.04000  ? 95   VAL B CG1 1 
ATOM   2246 C CG2 . VAL B 2 95  ? 3.18552   -25.32300 -22.93805 1.000 35.45000  ? 95   VAL B CG2 1 
ATOM   2247 N N   . TYR B 2 96  ? 0.40943   -23.48637 -26.26371 1.000 28.99000  ? 96   TYR B N   1 
ATOM   2248 C CA  . TYR B 2 96  ? -0.60161  -23.45275 -27.31169 1.000 30.93000  ? 96   TYR B CA  1 
ATOM   2249 C C   . TYR B 2 96  ? -0.83921  -24.84428 -27.88947 1.000 30.02000  ? 96   TYR B C   1 
ATOM   2250 O O   . TYR B 2 96  ? 0.10534   -25.63087 -28.03111 1.000 29.82000  ? 96   TYR B O   1 
ATOM   2251 C CB  . TYR B 2 96  ? -0.18067  -22.52748 -28.44874 1.000 31.64000  ? 96   TYR B CB  1 
ATOM   2252 C CG  . TYR B 2 96  ? -0.08593  -21.08695 -28.07288 1.000 32.76000  ? 96   TYR B CG  1 
ATOM   2253 C CD1 . TYR B 2 96  ? -1.00751  -20.51181 -27.21316 1.000 33.14000  ? 96   TYR B CD1 1 
ATOM   2254 C CD2 . TYR B 2 96  ? 0.92658   -20.29350 -28.58400 1.000 35.22000  ? 96   TYR B CD2 1 
ATOM   2255 C CE1 . TYR B 2 96  ? -0.91768  -19.17557 -26.86703 1.000 35.40000  ? 96   TYR B CE1 1 
ATOM   2256 C CE2 . TYR B 2 96  ? 1.02286   -18.96559 -28.24924 1.000 39.29000  ? 96   TYR B CE2 1 
ATOM   2257 C CZ  . TYR B 2 96  ? 0.09937   -18.40922 -27.39303 1.000 35.73000  ? 96   TYR B CZ  1 
ATOM   2258 O OH  . TYR B 2 96  ? 0.19861   -17.08288 -27.06056 1.000 37.88000  ? 96   TYR B OH  1 
ATOM   2259 N N   . PRO B 2 97  ? -2.07687  -25.16881 -28.25117 1.000 30.44000  ? 97   PRO B N   1 
ATOM   2260 C CA  . PRO B 2 97  ? -2.31391  -26.34134 -29.09755 1.000 30.83000  ? 97   PRO B CA  1 
ATOM   2261 C C   . PRO B 2 97  ? -1.86417  -26.09570 -30.53139 1.000 34.82000  ? 97   PRO B C   1 
ATOM   2262 O O   . PRO B 2 97  ? -2.01866  -24.99672 -31.07235 1.000 32.59000  ? 97   PRO B O   1 
ATOM   2263 C CB  . PRO B 2 97  ? -3.83260  -26.52619 -29.03139 1.000 31.35000  ? 97   PRO B CB  1 
ATOM   2264 C CG  . PRO B 2 97  ? -4.37151  -25.18080 -28.68409 1.000 32.55000  ? 97   PRO B CG  1 
ATOM   2265 C CD  . PRO B 2 97  ? -3.32080  -24.48508 -27.86377 1.000 30.45000  ? 97   PRO B CD  1 
ATOM   2266 N N   . GLU B 2 98  ? -1.31359  -27.14575 -31.14207 1.000 36.59000  ? 98   GLU B N   1 
ATOM   2267 C CA  . GLU B 2 98  ? -1.00557  -27.18809 -32.56951 1.000 39.20000  ? 98   GLU B CA  1 
ATOM   2268 C C   . GLU B 2 98  ? -2.19276  -27.84535 -33.26410 1.000 36.28000  ? 98   GLU B C   1 
ATOM   2269 O O   . GLU B 2 98  ? -2.47292  -29.02398 -33.02755 1.000 33.26000  ? 98   GLU B O   1 
ATOM   2270 C CB  . GLU B 2 98  ? 0.26661   -28.00115 -32.81077 1.000 45.42000  ? 98   GLU B CB  1 
ATOM   2271 C CG  . GLU B 2 98  ? 1.60920   -27.26930 -32.67960 1.000 55.52000  ? 98   GLU B CG  1 
ATOM   2272 C CD  . GLU B 2 98  ? 1.54942   -25.77171 -32.94329 1.000 68.62000  ? 98   GLU B CD  1 
ATOM   2273 O OE1 . GLU B 2 98  ? 1.02705   -25.35894 -34.00536 1.000 69.69000  ? 98   GLU B OE1 1 
ATOM   2274 O OE2 . GLU B 2 98  ? 2.08299   -25.01094 -32.10942 1.000 81.69000  ? 98   GLU B OE2 1 
ATOM   2275 N N   . VAL B 2 99  ? -2.89164  -27.10528 -34.11670 1.000 32.54000  ? 99   VAL B N   1 
ATOM   2276 C CA  . VAL B 2 99  ? -4.07301  -27.62938 -34.79384 1.000 32.19000  ? 99   VAL B CA  1 
ATOM   2277 C C   . VAL B 2 99  ? -3.72974  -27.91878 -36.25086 1.000 33.08000  ? 99   VAL B C   1 
ATOM   2278 O O   . VAL B 2 99  ? -3.31040  -27.01781 -36.98803 1.000 31.11000  ? 99   VAL B O   1 
ATOM   2279 C CB  . VAL B 2 99  ? -5.26004  -26.66187 -34.68357 1.000 30.53000  ? 99   VAL B CB  1 
ATOM   2280 C CG1 . VAL B 2 99  ? -6.51304  -27.31061 -35.26412 1.000 31.94000  ? 99   VAL B CG1 1 
ATOM   2281 C CG2 . VAL B 2 99  ? -5.48108  -26.27823 -33.22934 1.000 29.43000  ? 99   VAL B CG2 1 
ATOM   2282 N N   . THR B 2 100 ? -3.90879  -29.17969 -36.66012 1.000 32.00000  ? 100  THR B N   1 
ATOM   2283 C CA  . THR B 2 100 ? -3.73061  -29.62544 -38.03797 1.000 36.84000  ? 100  THR B CA  1 
ATOM   2284 C C   . THR B 2 100 ? -4.99620  -30.31595 -38.52124 1.000 35.56000  ? 100  THR B C   1 
ATOM   2285 O O   . THR B 2 100 ? -5.56570  -31.15198 -37.81372 1.000 35.71000  ? 100  THR B O   1 
ATOM   2286 C CB  . THR B 2 100 ? -2.55907  -30.60624 -38.19522 1.000 39.12000  ? 100  THR B CB  1 
ATOM   2287 O OG1 . THR B 2 100 ? -1.39896  -30.10021 -37.53314 1.000 44.46000  ? 100  THR B OG1 1 
ATOM   2288 C CG2 . THR B 2 100 ? -2.23047  -30.79384 -39.66483 1.000 45.51000  ? 100  THR B CG2 1 
ATOM   2289 N N   . VAL B 2 101 ? -5.42048  -29.98522 -39.73697 1.000 33.88000  ? 101  VAL B N   1 
ATOM   2290 C CA  . VAL B 2 101 ? -6.60524  -30.57479 -40.34569 1.000 36.26000  ? 101  VAL B CA  1 
ATOM   2291 C C   . VAL B 2 101 ? -6.18301  -31.27813 -41.62838 1.000 37.01000  ? 101  VAL B C   1 
ATOM   2292 O O   . VAL B 2 101 ? -5.46775  -30.69730 -42.45294 1.000 37.56000  ? 101  VAL B O   1 
ATOM   2293 C CB  . VAL B 2 101 ? -7.68209  -29.51073 -40.61838 1.000 35.27000  ? 101  VAL B CB  1 
ATOM   2294 C CG1 . VAL B 2 101 ? -8.78335  -30.07555 -41.49884 1.000 36.49000  ? 101  VAL B CG1 1 
ATOM   2295 C CG2 . VAL B 2 101 ? -8.24840  -29.01639 -39.30589 1.000 34.35000  ? 101  VAL B CG2 1 
ATOM   2296 N N   . TYR B 2 102 ? -6.61553  -32.52800 -41.79265 1.000 35.98000  ? 102  TYR B N   1 
ATOM   2297 C CA  . TYR B 2 102 ? -6.22626  -33.31026 -42.95822 1.000 40.31000  ? 102  TYR B CA  1 
ATOM   2298 C C   . TYR B 2 102 ? -7.19011  -34.47428 -43.11525 1.000 37.88000  ? 102  TYR B C   1 
ATOM   2299 O O   . TYR B 2 102 ? -7.68526  -35.00521 -42.11323 1.000 34.41000  ? 102  TYR B O   1 
ATOM   2300 C CB  . TYR B 2 102 ? -4.78232  -33.82756 -42.83000 1.000 38.37000  ? 102  TYR B CB  1 
ATOM   2301 C CG  . TYR B 2 102 ? -4.52540  -34.63092 -41.57700 1.000 40.72000  ? 102  TYR B CG  1 
ATOM   2302 C CD1 . TYR B 2 102 ? -4.14483  -34.01065 -40.39018 1.000 39.16000  ? 102  TYR B CD1 1 
ATOM   2303 C CD2 . TYR B 2 102 ? -4.66793  -36.01262 -41.57582 1.000 45.32000  ? 102  TYR B CD2 1 
ATOM   2304 C CE1 . TYR B 2 102 ? -3.91121  -34.75108 -39.23766 1.000 41.44000  ? 102  TYR B CE1 1 
ATOM   2305 C CE2 . TYR B 2 102 ? -4.43778  -36.75785 -40.43296 1.000 44.87000  ? 102  TYR B CE2 1 
ATOM   2306 C CZ  . TYR B 2 102 ? -4.06063  -36.12537 -39.26909 1.000 44.73000  ? 102  TYR B CZ  1 
ATOM   2307 O OH  . TYR B 2 102 ? -3.83466  -36.87561 -38.13946 1.000 46.03000  ? 102  TYR B OH  1 
ATOM   2308 N N   . PRO B 2 103 ? -7.47190  -34.89592 -44.34551 1.000 38.40000  ? 103  PRO B N   1 
ATOM   2309 C CA  . PRO B 2 103 ? -8.26252  -36.11669 -44.53727 1.000 40.91000  ? 103  PRO B CA  1 
ATOM   2310 C C   . PRO B 2 103 ? -7.49380  -37.33761 -44.05708 1.000 42.62000  ? 103  PRO B C   1 
ATOM   2311 O O   . PRO B 2 103 ? -6.28070  -37.44697 -44.25014 1.000 47.11000  ? 103  PRO B O   1 
ATOM   2312 C CB  . PRO B 2 103 ? -8.49887  -36.15948 -46.05074 1.000 41.91000  ? 103  PRO B CB  1 
ATOM   2313 C CG  . PRO B 2 103 ? -7.43768  -35.29298 -46.63998 1.000 41.45000  ? 103  PRO B CG  1 
ATOM   2314 C CD  . PRO B 2 103 ? -7.06989  -34.27036 -45.61599 1.000 41.32000  ? 103  PRO B CD  1 
ATOM   2315 N N   . ALA B 2 104 ? -8.21278  -38.25372 -43.41493 1.000 48.84000  ? 104  ALA B N   1 
ATOM   2316 C CA  . ALA B 2 104 ? -7.57967  -39.43559 -42.84543 1.000 51.02000  ? 104  ALA B CA  1 
ATOM   2317 C C   . ALA B 2 104 ? -6.92290  -40.27395 -43.93541 1.000 53.82000  ? 104  ALA B C   1 
ATOM   2318 O O   . ALA B 2 104 ? -7.50781  -40.50196 -44.99950 1.000 59.40000  ? 104  ALA B O   1 
ATOM   2319 C CB  . ALA B 2 104 ? -8.61036  -40.26619 -42.07974 1.000 46.89000  ? 104  ALA B CB  1 
ATOM   2320 N N   . LYS B 2 105 ? -5.69270  -40.72419 -43.66770 1.000 58.81000  ? 105  LYS B N   1 
ATOM   2321 C CA  . LYS B 2 105 ? -4.96545  -41.57798 -44.60149 1.000 66.20000  ? 105  LYS B CA  1 
ATOM   2322 C C   . LYS B 2 105 ? -5.61390  -42.94435 -44.77340 1.000 68.98000  ? 105  LYS B C   1 
ATOM   2323 O O   . LYS B 2 105 ? -5.26833  -43.65988 -45.71978 1.000 73.73000  ? 105  LYS B O   1 
ATOM   2324 C CB  . LYS B 2 105 ? -3.51600  -41.74855 -44.14142 1.000 66.81000  ? 105  LYS B CB  1 
ATOM   2325 N N   . THR B 2 106 ? -6.53080  -43.32138 -43.88543 1.000 81.29000  ? 106  THR B N   1 
ATOM   2326 C CA  . THR B 2 106 ? -7.33591  -44.53348 -44.01905 1.000 83.13000  ? 106  THR B CA  1 
ATOM   2327 C C   . THR B 2 106 ? -8.79274  -44.09583 -44.14757 1.000 78.68000  ? 106  THR B C   1 
ATOM   2328 O O   . THR B 2 106 ? -9.42707  -43.74165 -43.14897 1.000 83.83000  ? 106  THR B O   1 
ATOM   2329 C CB  . THR B 2 106 ? -7.14097  -45.46666 -42.82492 1.000 91.29000  ? 106  THR B CB  1 
ATOM   2330 O OG1 . THR B 2 106 ? -7.50351  -44.78328 -41.61792 1.000 96.37000  ? 106  THR B OG1 1 
ATOM   2331 C CG2 . THR B 2 106 ? -5.69479  -45.91616 -42.72677 1.000 96.14000  ? 106  THR B CG2 1 
ATOM   2332 N N   . GLN B 2 107 ? -9.32058  -44.11379 -45.37601 1.000 71.56000  ? 107  GLN B N   1 
ATOM   2333 C CA  . GLN B 2 107 ? -10.69987 -43.71249 -45.64463 1.000 68.55000  ? 107  GLN B CA  1 
ATOM   2334 C C   . GLN B 2 107 ? -11.60869 -44.93899 -45.66662 1.000 68.71000  ? 107  GLN B C   1 
ATOM   2335 O O   . GLN B 2 107 ? -11.68348 -45.63861 -46.68571 1.000 60.10000  ? 107  GLN B O   1 
ATOM   2336 C CB  . GLN B 2 107 ? -10.78744 -42.95020 -46.96972 1.000 66.35000  ? 107  GLN B CB  1 
ATOM   2337 C CG  . GLN B 2 107 ? -10.13768 -41.56997 -46.94262 1.000 67.02000  ? 107  GLN B CG  1 
ATOM   2338 C CD  . GLN B 2 107 ? -10.75533 -40.64431 -45.90121 1.000 69.46000  ? 107  GLN B CD  1 
ATOM   2339 O OE1 . GLN B 2 107 ? -11.96857 -40.65492 -45.67998 1.000 59.48000  ? 107  GLN B OE1 1 
ATOM   2340 N NE2 . GLN B 2 107 ? -9.91771  -39.84026 -45.25523 1.000 64.96000  ? 107  GLN B NE2 1 
ATOM   2341 N N   . PRO B 2 108 ? -12.33598 -45.21999 -44.57420 1.000 71.64000  ? 108  PRO B N   1 
ATOM   2342 C CA  . PRO B 2 108 ? -12.92661 -46.55564 -44.40557 1.000 74.17000  ? 108  PRO B CA  1 
ATOM   2343 C C   . PRO B 2 108 ? -14.38139 -46.69167 -44.83670 1.000 76.16000  ? 108  PRO B C   1 
ATOM   2344 O O   . PRO B 2 108 ? -14.90130 -47.81133 -44.88962 1.000 75.26000  ? 108  PRO B O   1 
ATOM   2345 C CB  . PRO B 2 108 ? -12.78462 -46.78211 -42.89696 1.000 68.35000  ? 108  PRO B CB  1 
ATOM   2346 C CG  . PRO B 2 108 ? -13.02292 -45.40548 -42.33149 1.000 67.97000  ? 108  PRO B CG  1 
ATOM   2347 C CD  . PRO B 2 108 ? -12.49944 -44.40325 -43.35687 1.000 67.66000  ? 108  PRO B CD  1 
ATOM   2348 N N   . LEU B 2 109 ? -15.05683 -45.58823 -45.14156 1.000 72.24000  ? 109  LEU B N   1 
ATOM   2349 C CA  . LEU B 2 109 ? -16.49158 -45.63361 -45.37312 1.000 73.20000  ? 109  LEU B CA  1 
ATOM   2350 C C   . LEU B 2 109 ? -16.82707 -45.10084 -46.76056 1.000 69.30000  ? 109  LEU B C   1 
ATOM   2351 O O   . LEU B 2 109 ? -16.03522 -44.39919 -47.39713 1.000 67.07000  ? 109  LEU B O   1 
ATOM   2352 C CB  . LEU B 2 109 ? -17.26742 -44.86075 -44.28341 1.000 76.06000  ? 109  LEU B CB  1 
ATOM   2353 C CG  . LEU B 2 109 ? -17.13034 -43.35142 -44.03755 1.000 77.52000  ? 109  LEU B CG  1 
ATOM   2354 C CD1 . LEU B 2 109 ? -18.08359 -42.93422 -42.92758 1.000 77.80000  ? 109  LEU B CD1 1 
ATOM   2355 C CD2 . LEU B 2 109 ? -15.71559 -42.90791 -43.69550 1.000 80.76000  ? 109  LEU B CD2 1 
ATOM   2356 N N   . GLN B 2 110 ? -18.01796 -45.47119 -47.22470 1.000 67.56000  ? 110  GLN B N   1 
ATOM   2357 C CA  . GLN B 2 110 ? -18.52179 -45.09309 -48.53535 1.000 63.84000  ? 110  GLN B CA  1 
ATOM   2358 C C   . GLN B 2 110 ? -19.31385 -43.79490 -48.45506 1.000 65.61000  ? 110  GLN B C   1 
ATOM   2359 O O   . GLN B 2 110 ? -19.95785 -43.50097 -47.44267 1.000 68.93000  ? 110  GLN B O   1 
ATOM   2360 C CB  . GLN B 2 110 ? -19.40836 -46.20170 -49.10392 1.000 60.56000  ? 110  GLN B CB  1 
ATOM   2361 C CG  . GLN B 2 110 ? -19.31388 -46.35935 -50.60705 1.000 57.05000  ? 110  GLN B CG  1 
ATOM   2362 C CD  . GLN B 2 110 ? -20.35995 -45.54708 -51.34604 1.000 56.43000  ? 110  GLN B CD  1 
ATOM   2363 O OE1 . GLN B 2 110 ? -21.33832 -45.08808 -50.75228 1.000 52.44000  ? 110  GLN B OE1 1 
ATOM   2364 N NE2 . GLN B 2 110 ? -20.15253 -45.35294 -52.64660 1.000 58.75000  ? 110  GLN B NE2 1 
ATOM   2365 N N   . HIS B 2 111 ? -19.26820 -43.02888 -49.54963 1.000 69.27000  ? 111  HIS B N   1 
ATOM   2366 C CA  . HIS B 2 111 ? -19.89537 -41.71275 -49.67339 1.000 72.72000  ? 111  HIS B CA  1 
ATOM   2367 C C   . HIS B 2 111 ? -19.24524 -40.70204 -48.73307 1.000 76.65000  ? 111  HIS B C   1 
ATOM   2368 O O   . HIS B 2 111 ? -18.74382 -39.66804 -49.18390 1.000 76.84000  ? 111  HIS B O   1 
ATOM   2369 C CB  . HIS B 2 111 ? -21.40931 -41.78333 -49.42497 1.000 68.60000  ? 111  HIS B CB  1 
ATOM   2370 C CG  . HIS B 2 111 ? -22.10428 -40.45827 -49.53352 1.000 79.21000  ? 111  HIS B CG  1 
ATOM   2371 N ND1 . HIS B 2 111 ? -22.31587 -39.82425 -50.73969 1.000 78.29000  ? 111  HIS B ND1 1 
ATOM   2372 C CD2 . HIS B 2 111 ? -22.64122 -39.65110 -48.58686 1.000 82.43000  ? 111  HIS B CD2 1 
ATOM   2373 C CE1 . HIS B 2 111 ? -22.94750 -38.68241 -50.53108 1.000 79.98000  ? 111  HIS B CE1 1 
ATOM   2374 N NE2 . HIS B 2 111 ? -23.15707 -38.55333 -49.23330 1.000 80.80000  ? 111  HIS B NE2 1 
ATOM   2375 N N   . HIS B 2 112 ? -19.24665 -40.98204 -47.43246 1.000 73.80000  ? 112  HIS B N   1 
ATOM   2376 C CA  . HIS B 2 112 ? -18.60426 -40.09895 -46.47125 1.000 76.08000  ? 112  HIS B CA  1 
ATOM   2377 C C   . HIS B 2 112 ? -17.09616 -40.33493 -46.44473 1.000 75.04000  ? 112  HIS B C   1 
ATOM   2378 O O   . HIS B 2 112 ? -16.62143 -41.46161 -46.61947 1.000 75.40000  ? 112  HIS B O   1 
ATOM   2379 C CB  . HIS B 2 112 ? -19.19217 -40.30919 -45.07324 1.000 78.29000  ? 112  HIS B CB  1 
ATOM   2380 C CG  . HIS B 2 112 ? -20.61001 -39.84537 -44.92915 1.000 84.24000  ? 112  HIS B CG  1 
ATOM   2381 N ND1 . HIS B 2 112 ? -20.93932 -38.55738 -44.56481 1.000 85.75000  ? 112  HIS B ND1 1 
ATOM   2382 C CD2 . HIS B 2 112 ? -21.78412 -40.49878 -45.09641 1.000 88.20000  ? 112  HIS B CD2 1 
ATOM   2383 C CE1 . HIS B 2 112 ? -22.25411 -38.43788 -44.51292 1.000 86.01000  ? 112  HIS B CE1 1 
ATOM   2384 N NE2 . HIS B 2 112 ? -22.79035 -39.60208 -44.83117 1.000 92.63000  ? 112  HIS B NE2 1 
ATOM   2385 N N   . ASN B 2 113 ? -16.34304 -39.26028 -46.23762 1.000 68.82000  ? 113  ASN B N   1 
ATOM   2386 C CA  . ASN B 2 113 ? -14.91386 -39.34059 -45.98514 1.000 67.50000  ? 113  ASN B CA  1 
ATOM   2387 C C   . ASN B 2 113 ? -14.62485 -38.88437 -44.56070 1.000 61.37000  ? 113  ASN B C   1 
ATOM   2388 O O   . ASN B 2 113 ? -15.44035 -38.21118 -43.92516 1.000 58.40000  ? 113  ASN B O   1 
ATOM   2389 C CB  . ASN B 2 113 ? -14.11997 -38.49309 -46.98704 1.000 70.01000  ? 113  ASN B CB  1 
ATOM   2390 C CG  . ASN B 2 113 ? -13.75950 -39.26211 -48.24058 1.000 76.86000  ? 113  ASN B CG  1 
ATOM   2391 O OD1 . ASN B 2 113 ? -13.41703 -38.67523 -49.26589 1.000 82.48000  ? 113  ASN B OD1 1 
ATOM   2392 N ND2 . ASN B 2 113 ? -13.84180 -40.58663 -48.16637 1.000 80.00000  ? 113  ASN B ND2 1 
ATOM   2393 N N   . LEU B 2 114 ? -13.45230 -39.26325 -44.05964 1.000 58.32000  ? 114  LEU B N   1 
ATOM   2394 C CA  . LEU B 2 114 ? -13.04750 -38.95214 -42.69418 1.000 55.32000  ? 114  LEU B CA  1 
ATOM   2395 C C   . LEU B 2 114 ? -12.07400 -37.77890 -42.70156 1.000 50.24000  ? 114  LEU B C   1 
ATOM   2396 O O   . LEU B 2 114 ? -10.98340 -37.87357 -43.27796 1.000 50.45000  ? 114  LEU B O   1 
ATOM   2397 C CB  . LEU B 2 114 ? -12.41285 -40.16861 -42.02214 1.000 60.91000  ? 114  LEU B CB  1 
ATOM   2398 C CG  . LEU B 2 114 ? -13.36943 -41.08390 -41.25581 1.000 66.25000  ? 114  LEU B CG  1 
ATOM   2399 C CD1 . LEU B 2 114 ? -12.59396 -42.05684 -40.38462 1.000 67.83000  ? 114  LEU B CD1 1 
ATOM   2400 C CD2 . LEU B 2 114 ? -14.33916 -40.26780 -40.42085 1.000 65.87000  ? 114  LEU B CD2 1 
ATOM   2401 N N   . LEU B 2 115 ? -12.46848 -36.68140 -42.05926 1.000 40.41000  ? 115  LEU B N   1 
ATOM   2402 C CA  . LEU B 2 115 ? -11.62604 -35.50298 -41.89690 1.000 38.18000  ? 115  LEU B CA  1 
ATOM   2403 C C   . LEU B 2 115 ? -11.13119 -35.45258 -40.45751 1.000 34.83000  ? 115  LEU B C   1 
ATOM   2404 O O   . LEU B 2 115 ? -11.91747 -35.63371 -39.51859 1.000 34.06000  ? 115  LEU B O   1 
ATOM   2405 C CB  . LEU B 2 115 ? -12.39131 -34.22515 -42.25173 1.000 39.77000  ? 115  LEU B CB  1 
ATOM   2406 C CG  . LEU B 2 115 ? -11.55087 -33.01653 -42.66764 1.000 45.06000  ? 115  LEU B CG  1 
ATOM   2407 C CD1 . LEU B 2 115 ? -10.79426 -33.29220 -43.95871 1.000 46.23000  ? 115  LEU B CD1 1 
ATOM   2408 C CD2 . LEU B 2 115 ? -12.42562 -31.78268 -42.81976 1.000 46.57000  ? 115  LEU B CD2 1 
ATOM   2409 N N   . VAL B 2 116 ? -9.83421  -35.21320 -40.28322 1.000 33.65000  ? 116  VAL B N   1 
ATOM   2410 C CA  . VAL B 2 116 ? -9.19206  -35.28172 -38.97574 1.000 33.86000  ? 116  VAL B CA  1 
ATOM   2411 C C   . VAL B 2 116 ? -8.80967  -33.87398 -38.54109 1.000 31.54000  ? 116  VAL B C   1 
ATOM   2412 O O   . VAL B 2 116 ? -8.20982  -33.11886 -39.31488 1.000 34.02000  ? 116  VAL B O   1 
ATOM   2413 C CB  . VAL B 2 116 ? -7.95731  -36.20002 -39.00353 1.000 38.66000  ? 116  VAL B CB  1 
ATOM   2414 C CG1 . VAL B 2 116 ? -7.62779  -36.70030 -37.60306 1.000 42.33000  ? 116  VAL B CG1 1 
ATOM   2415 C CG2 . VAL B 2 116 ? -8.17802  -37.36418 -39.95389 1.000 41.35000  ? 116  VAL B CG2 1 
ATOM   2416 N N   . CYS B 2 117 ? -9.16597  -33.51809 -37.30802 1.000 29.65000  ? 117  CYS B N   1 
ATOM   2417 C CA  . CYS B 2 117 ? -8.64053  -32.32652 -36.64898 1.000 29.46000  ? 117  CYS B CA  1 
ATOM   2418 C C   . CYS B 2 117 ? -7.71101  -32.81251 -35.54480 1.000 28.58000  ? 117  CYS B C   1 
ATOM   2419 O O   . CYS B 2 117 ? -8.16737  -33.23852 -34.47834 1.000 27.86000  ? 117  CYS B O   1 
ATOM   2420 C CB  . CYS B 2 117 ? -9.74212  -31.43377 -36.08415 1.000 30.42000  ? 117  CYS B CB  1 
ATOM   2421 S SG  . CYS B 2 117 ? -9.05452  -29.91674 -35.36176 1.000 33.30000  ? 117  CYS B SG  1 
ATOM   2422 N N   . SER B 2 118 ? -6.41105  -32.75428 -35.81400 1.000 29.94000  ? 118  SER B N   1 
ATOM   2423 C CA  . SER B 2 118 ? -5.38796  -33.16119 -34.86105 1.000 29.73000  ? 118  SER B CA  1 
ATOM   2424 C C   . SER B 2 118 ? -4.95428  -31.95560 -34.03532 1.000 29.05000  ? 118  SER B C   1 
ATOM   2425 O O   . SER B 2 118 ? -4.42871  -30.97752 -34.58250 1.000 31.64000  ? 118  SER B O   1 
ATOM   2426 C CB  . SER B 2 118 ? -4.19320  -33.76210 -35.59482 1.000 29.14000  ? 118  SER B CB  1 
ATOM   2427 O OG  . SER B 2 118 ? -3.34807  -34.44755 -34.69439 1.000 32.48000  ? 118  SER B OG  1 
ATOM   2428 N N   . VAL B 2 119 ? -5.16704  -32.03024 -32.72409 1.000 29.25000  ? 119  VAL B N   1 
ATOM   2429 C CA  . VAL B 2 119 ? -4.77558  -30.98309 -31.78497 1.000 28.43000  ? 119  VAL B CA  1 
ATOM   2430 C C   . VAL B 2 119 ? -3.67130  -31.55339 -30.90784 1.000 25.74000  ? 119  VAL B C   1 
ATOM   2431 O O   . VAL B 2 119 ? -3.87778  -32.56448 -30.22800 1.000 28.63000  ? 119  VAL B O   1 
ATOM   2432 C CB  . VAL B 2 119 ? -5.97029  -30.51048 -30.94250 1.000 28.23000  ? 119  VAL B CB  1 
ATOM   2433 C CG1 . VAL B 2 119 ? -5.62963  -29.22987 -30.21054 1.000 27.45000  ? 119  VAL B CG1 1 
ATOM   2434 C CG2 . VAL B 2 119 ? -7.21350  -30.33317 -31.82403 1.000 29.32000  ? 119  VAL B CG2 1 
ATOM   2435 N N   . ASN B 2 120 ? -2.49899  -30.92544 -30.92103 1.000 25.61000  ? 120  ASN B N   1 
ATOM   2436 C CA  . ASN B 2 120 ? -1.31008  -31.54134 -30.34952 1.000 28.08000  ? 120  ASN B CA  1 
ATOM   2437 C C   . ASN B 2 120 ? -0.52785  -30.56676 -29.48235 1.000 28.50000  ? 120  ASN B C   1 
ATOM   2438 O O   . ASN B 2 120 ? -0.54387  -29.35058 -29.70252 1.000 31.25000  ? 120  ASN B O   1 
ATOM   2439 C CB  . ASN B 2 120 ? -0.38502  -32.07774 -31.44586 1.000 32.70000  ? 120  ASN B CB  1 
ATOM   2440 C CG  . ASN B 2 120 ? -1.07299  -33.08016 -32.33600 1.000 36.56000  ? 120  ASN B CG  1 
ATOM   2441 O OD1 . ASN B 2 120 ? -1.69981  -32.71150 -33.33387 1.000 43.54000  ? 120  ASN B OD1 1 
ATOM   2442 N ND2 . ASN B 2 120 ? -0.98616  -34.35594 -31.97151 1.000 39.11000  ? 120  ASN B ND2 1 
ATOM   2443 N N   . GLY B 2 121 ? 0.16348   -31.13313 -28.49307 1.000 27.37000  ? 121  GLY B N   1 
ATOM   2444 C CA  . GLY B 2 121 ? 1.18881   -30.42057 -27.75533 1.000 27.59000  ? 121  GLY B CA  1 
ATOM   2445 C C   . GLY B 2 121 ? 0.70790   -29.29622 -26.86959 1.000 27.74000  ? 121  GLY B C   1 
ATOM   2446 O O   . GLY B 2 121 ? 1.47949   -28.37831 -26.58358 1.000 34.13000  ? 121  GLY B O   1 
ATOM   2447 N N   . PHE B 2 122 ? -0.53871  -29.33678 -26.41621 1.000 28.60000  ? 122  PHE B N   1 
ATOM   2448 C CA  . PHE B 2 122 ? -1.04156  -28.27683 -25.55791 1.000 27.77000  ? 122  PHE B CA  1 
ATOM   2449 C C   . PHE B 2 122 ? -0.94470  -28.67201 -24.09197 1.000 26.69000  ? 122  PHE B C   1 
ATOM   2450 O O   . PHE B 2 122 ? -0.79568  -29.84455 -23.73778 1.000 24.81000  ? 122  PHE B O   1 
ATOM   2451 C CB  . PHE B 2 122 ? -2.48871  -27.90349 -25.90169 1.000 26.80000  ? 122  PHE B CB  1 
ATOM   2452 C CG  . PHE B 2 122 ? -3.45536  -29.05771 -25.86807 1.000 27.41000  ? 122  PHE B CG  1 
ATOM   2453 C CD1 . PHE B 2 122 ? -3.67112  -29.83038 -27.00120 1.000 26.70000  ? 122  PHE B CD1 1 
ATOM   2454 C CD2 . PHE B 2 122 ? -4.17647  -29.34364 -24.72177 1.000 27.03000  ? 122  PHE B CD2 1 
ATOM   2455 C CE1 . PHE B 2 122 ? -4.57137  -30.87544 -26.98405 1.000 26.50000  ? 122  PHE B CE1 1 
ATOM   2456 C CE2 . PHE B 2 122 ? -5.07960  -30.38438 -24.69890 1.000 28.07000  ? 122  PHE B CE2 1 
ATOM   2457 C CZ  . PHE B 2 122 ? -5.27491  -31.15699 -25.83185 1.000 25.88000  ? 122  PHE B CZ  1 
ATOM   2458 N N   . TYR B 2 123 ? -1.00807  -27.65033 -23.23970 1.000 26.85000  ? 123  TYR B N   1 
ATOM   2459 C CA  . TYR B 2 123 ? -1.06163  -27.79474 -21.79842 1.000 28.74000  ? 123  TYR B CA  1 
ATOM   2460 C C   . TYR B 2 123 ? -1.70840  -26.52198 -21.28903 1.000 30.72000  ? 123  TYR B C   1 
ATOM   2461 O O   . TYR B 2 123 ? -1.41908  -25.44784 -21.83359 1.000 32.17000  ? 123  TYR B O   1 
ATOM   2462 C CB  . TYR B 2 123 ? 0.32688   -27.99352 -21.16723 1.000 29.08000  ? 123  TYR B CB  1 
ATOM   2463 C CG  . TYR B 2 123 ? 0.22261   -28.39220 -19.71924 1.000 29.49000  ? 123  TYR B CG  1 
ATOM   2464 C CD1 . TYR B 2 123 ? 0.09676   -27.42362 -18.72270 1.000 28.97000  ? 123  TYR B CD1 1 
ATOM   2465 C CD2 . TYR B 2 123 ? 0.19243   -29.72807 -19.34652 1.000 28.89000  ? 123  TYR B CD2 1 
ATOM   2466 C CE1 . TYR B 2 123 ? -0.04026  -27.77061 -17.40554 1.000 29.83000  ? 123  TYR B CE1 1 
ATOM   2467 C CE2 . TYR B 2 123 ? 0.06282   -30.08854 -18.01765 1.000 31.28000  ? 123  TYR B CE2 1 
ATOM   2468 C CZ  . TYR B 2 123 ? -0.05336  -29.10214 -17.05294 1.000 30.83000  ? 123  TYR B CZ  1 
ATOM   2469 O OH  . TYR B 2 123 ? -0.18673  -29.43901 -15.72740 1.000 31.62000  ? 123  TYR B OH  1 
ATOM   2470 N N   . PRO B 2 124 ? -2.60158  -26.59017 -20.28580 1.000 31.13000  ? 124  PRO B N   1 
ATOM   2471 C CA  . PRO B 2 124 ? -3.07774  -27.80145 -19.59973 1.000 33.20000  ? 124  PRO B CA  1 
ATOM   2472 C C   . PRO B 2 124 ? -4.04250  -28.63165 -20.42987 1.000 32.69000  ? 124  PRO B C   1 
ATOM   2473 O O   . PRO B 2 124 ? -4.24743  -28.32979 -21.60566 1.000 28.94000  ? 124  PRO B O   1 
ATOM   2474 C CB  . PRO B 2 124 ? -3.77593  -27.24652 -18.36027 1.000 31.45000  ? 124  PRO B CB  1 
ATOM   2475 C CG  . PRO B 2 124 ? -4.24648  -25.89259 -18.78721 1.000 32.11000  ? 124  PRO B CG  1 
ATOM   2476 C CD  . PRO B 2 124 ? -3.18890  -25.36563 -19.71503 1.000 31.45000  ? 124  PRO B CD  1 
ATOM   2477 N N   . GLY B 2 125 ? -4.63613  -29.65774 -19.81086 1.000 35.24000  ? 125  GLY B N   1 
ATOM   2478 C CA  . GLY B 2 125 ? -5.40469  -30.64244 -20.55245 1.000 42.39000  ? 125  GLY B CA  1 
ATOM   2479 C C   . GLY B 2 125 ? -6.79923  -30.21190 -20.95738 1.000 40.02000  ? 125  GLY B C   1 
ATOM   2480 O O   . GLY B 2 125 ? -7.37027  -30.80174 -21.87946 1.000 52.75000  ? 125  GLY B O   1 
ATOM   2481 N N   . SER B 2 126 ? -7.36077  -29.20761 -20.29644 1.000 40.73000  ? 126  SER B N   1 
ATOM   2482 C CA  . SER B 2 126 ? -8.72414  -28.77929 -20.58399 1.000 41.46000  ? 126  SER B CA  1 
ATOM   2483 C C   . SER B 2 126 ? -8.79983  -28.16675 -21.98179 1.000 41.43000  ? 126  SER B C   1 
ATOM   2484 O O   . SER B 2 126 ? -8.06510  -27.22493 -22.29177 1.000 39.25000  ? 126  SER B O   1 
ATOM   2485 C CB  . SER B 2 126 ? -9.18378  -27.78053 -19.52297 1.000 41.63000  ? 126  SER B CB  1 
ATOM   2486 O OG  . SER B 2 126 ? -10.37888 -27.13063 -19.91884 1.000 51.06000  ? 126  SER B OG  1 
ATOM   2487 N N   . ILE B 2 127 ? -9.68333  -28.69975 -22.82743 1.000 37.37000  ? 127  ILE B N   1 
ATOM   2488 C CA  . ILE B 2 127 ? -9.79784  -28.24081 -24.20722 1.000 32.41000  ? 127  ILE B CA  1 
ATOM   2489 C C   . ILE B 2 127 ? -11.19624 -28.55248 -24.72142 1.000 35.00000  ? 127  ILE B C   1 
ATOM   2490 O O   . ILE B 2 127 ? -11.85213 -29.49117 -24.26082 1.000 33.63000  ? 127  ILE B O   1 
ATOM   2491 C CB  . ILE B 2 127 ? -8.71149  -28.88346 -25.10560 1.000 32.57000  ? 127  ILE B CB  1 
ATOM   2492 C CG1 . ILE B 2 127 ? -8.49674  -28.05153 -26.37546 1.000 32.12000  ? 127  ILE B CG1 1 
ATOM   2493 C CG2 . ILE B 2 127 ? -9.07457  -30.32185 -25.46118 1.000 31.89000  ? 127  ILE B CG2 1 
ATOM   2494 C CD1 . ILE B 2 127 ? -7.13971  -28.25251 -26.99994 1.000 31.61000  ? 127  ILE B CD1 1 
ATOM   2495 N N   . GLU B 2 128 ? -11.64946 -27.75526 -25.68795 1.000 37.46000  ? 128  GLU B N   1 
ATOM   2496 C CA  . GLU B 2 128 ? -12.91666 -27.96747 -26.37492 1.000 42.15000  ? 128  GLU B CA  1 
ATOM   2497 C C   . GLU B 2 128 ? -12.64978 -27.87927 -27.86791 1.000 37.81000  ? 128  GLU B C   1 
ATOM   2498 O O   . GLU B 2 128 ? -12.16438 -26.85205 -28.35403 1.000 34.16000  ? 128  GLU B O   1 
ATOM   2499 C CB  . GLU B 2 128 ? -13.96644 -26.93772 -25.94766 1.000 48.71000  ? 128  GLU B CB  1 
ATOM   2500 N N   . VAL B 2 129 ? -12.93452 -28.95887 -28.58671 1.000 36.79000  ? 129  VAL B N   1 
ATOM   2501 C CA  . VAL B 2 129 ? -12.73994 -29.01911 -30.02904 1.000 37.74000  ? 129  VAL B CA  1 
ATOM   2502 C C   . VAL B 2 129 ? -14.10740 -29.18808 -30.66969 1.000 39.64000  ? 129  VAL B C   1 
ATOM   2503 O O   . VAL B 2 129 ? -14.91490 -30.00618 -30.21284 1.000 49.85000  ? 129  VAL B O   1 
ATOM   2504 C CB  . VAL B 2 129 ? -11.79081 -30.16326 -30.43249 1.000 38.47000  ? 129  VAL B CB  1 
ATOM   2505 C CG1 . VAL B 2 129 ? -11.62393 -30.21531 -31.94561 1.000 38.11000  ? 129  VAL B CG1 1 
ATOM   2506 C CG2 . VAL B 2 129 ? -10.43654 -30.00233 -29.74229 1.000 36.50000  ? 129  VAL B CG2 1 
ATOM   2507 N N   . ARG B 2 130 ? -14.36904 -28.40943 -31.71581 1.000 40.28000  ? 130  ARG B N   1 
ATOM   2508 C CA  . ARG B 2 130 ? -15.66872 -28.40419 -32.36073 1.000 40.75000  ? 130  ARG B CA  1 
ATOM   2509 C C   . ARG B 2 130 ? -15.49358 -28.36297 -33.86917 1.000 38.59000  ? 130  ARG B C   1 
ATOM   2510 O O   . ARG B 2 130 ? -14.49533 -27.85439 -34.38347 1.000 38.58000  ? 130  ARG B O   1 
ATOM   2511 C CB  . ARG B 2 130 ? -16.51258 -27.22012 -31.89019 1.000 47.02000  ? 130  ARG B CB  1 
ATOM   2512 C CG  . ARG B 2 130 ? -17.16361 -27.46869 -30.55145 1.000 53.38000  ? 130  ARG B CG  1 
ATOM   2513 C CD  . ARG B 2 130 ? -17.37346 -26.17875 -29.79249 1.000 60.89000  ? 130  ARG B CD  1 
ATOM   2514 N NE  . ARG B 2 130 ? -18.46156 -25.39795 -30.36240 1.000 67.43000  ? 130  ARG B NE  1 
ATOM   2515 C CZ  . ARG B 2 130 ? -18.52779 -24.07545 -30.32957 1.000 71.99000  ? 130  ARG B CZ  1 
ATOM   2516 N NH1 . ARG B 2 130 ? -17.57932 -23.35045 -29.75921 1.000 83.48000  ? 130  ARG B NH1 1 
ATOM   2517 N NH2 . ARG B 2 130 ? -19.57359 -23.46596 -30.87902 1.000 65.43000  ? 130  ARG B NH2 1 
ATOM   2518 N N   . TRP B 2 131 ? -16.48540 -28.90116 -34.56937 1.000 37.80000  ? 131  TRP B N   1 
ATOM   2519 C CA  . TRP B 2 131 ? -16.49285 -28.97905 -36.02026 1.000 38.29000  ? 131  TRP B CA  1 
ATOM   2520 C C   . TRP B 2 131 ? -17.65182 -28.15691 -36.56324 1.000 35.82000  ? 131  TRP B C   1 
ATOM   2521 O O   . TRP B 2 131 ? -18.77010 -28.23550 -36.04614 1.000 37.41000  ? 131  TRP B O   1 
ATOM   2522 C CB  . TRP B 2 131 ? -16.63502 -30.42933 -36.48616 1.000 38.10000  ? 131  TRP B CB  1 
ATOM   2523 C CG  . TRP B 2 131 ? -15.34543 -31.14528 -36.73467 1.000 35.02000  ? 131  TRP B CG  1 
ATOM   2524 C CD1 . TRP B 2 131 ? -14.87296 -32.23565 -36.06174 1.000 35.25000  ? 131  TRP B CD1 1 
ATOM   2525 C CD2 . TRP B 2 131 ? -14.37614 -30.84885 -37.74994 1.000 32.14000  ? 131  TRP B CD2 1 
ATOM   2526 N NE1 . TRP B 2 131 ? -13.66757 -32.62840 -36.58842 1.000 33.08000  ? 131  TRP B NE1 1 
ATOM   2527 C CE2 . TRP B 2 131 ? -13.34003 -31.79388 -37.62496 1.000 31.75000  ? 131  TRP B CE2 1 
ATOM   2528 C CE3 . TRP B 2 131 ? -14.28223 -29.87291 -38.74794 1.000 34.76000  ? 131  TRP B CE3 1 
ATOM   2529 C CZ2 . TRP B 2 131 ? -12.22435 -31.79459 -38.45978 1.000 32.14000  ? 131  TRP B CZ2 1 
ATOM   2530 C CZ3 . TRP B 2 131 ? -13.16870 -29.87638 -39.57926 1.000 33.28000  ? 131  TRP B CZ3 1 
ATOM   2531 C CH2 . TRP B 2 131 ? -12.15474 -30.82867 -39.42566 1.000 36.30000  ? 131  TRP B CH2 1 
ATOM   2532 N N   . PHE B 2 132 ? -17.38918 -27.37737 -37.61094 1.000 37.85000  ? 132  PHE B N   1 
ATOM   2533 C CA  . PHE B 2 132 ? -18.42575 -26.60993 -38.28696 1.000 41.56000  ? 132  PHE B CA  1 
ATOM   2534 C C   . PHE B 2 132 ? -18.37340 -26.88182 -39.78130 1.000 46.85000  ? 132  PHE B C   1 
ATOM   2535 O O   . PHE B 2 132 ? -17.30032 -27.08390 -40.35467 1.000 46.44000  ? 132  PHE B O   1 
ATOM   2536 C CB  . PHE B 2 132 ? -18.28998 -25.10094 -38.03004 1.000 38.04000  ? 132  PHE B CB  1 
ATOM   2537 C CG  . PHE B 2 132 ? -18.46975 -24.71811 -36.59142 1.000 38.80000  ? 132  PHE B CG  1 
ATOM   2538 C CD1 . PHE B 2 132 ? -17.42101 -24.83599 -35.69241 1.000 37.07000  ? 132  PHE B CD1 1 
ATOM   2539 C CD2 . PHE B 2 132 ? -19.69361 -24.24933 -36.13459 1.000 38.69000  ? 132  PHE B CD2 1 
ATOM   2540 C CE1 . PHE B 2 132 ? -17.58580 -24.48883 -34.36514 1.000 37.78000  ? 132  PHE B CE1 1 
ATOM   2541 C CE2 . PHE B 2 132 ? -19.86569 -23.90194 -34.80992 1.000 38.37000  ? 132  PHE B CE2 1 
ATOM   2542 C CZ  . PHE B 2 132 ? -18.80726 -24.02187 -33.92356 1.000 41.58000  ? 132  PHE B CZ  1 
ATOM   2543 N N   . ARG B 2 133 ? -19.54994 -26.88961 -40.40384 1.000 58.40000  ? 133  ARG B N   1 
ATOM   2544 C CA  . ARG B 2 133 ? -19.69702 -27.12617 -41.83921 1.000 67.66000  ? 133  ARG B CA  1 
ATOM   2545 C C   . ARG B 2 133 ? -20.31713 -25.87609 -42.45600 1.000 73.36000  ? 133  ARG B C   1 
ATOM   2546 O O   . ARG B 2 133 ? -21.52896 -25.65913 -42.34457 1.000 73.55000  ? 133  ARG B O   1 
ATOM   2547 C CB  . ARG B 2 133 ? -20.54516 -28.36789 -42.10733 1.000 75.84000  ? 133  ARG B CB  1 
ATOM   2548 C CG  . ARG B 2 133 ? -20.76452 -28.66880 -43.58036 1.000 79.22000  ? 133  ARG B CG  1 
ATOM   2549 C CD  . ARG B 2 133 ? -21.79692 -29.76657 -43.77150 1.000 85.82000  ? 133  ARG B CD  1 
ATOM   2550 N NE  . ARG B 2 133 ? -21.54477 -30.90098 -42.89156 1.000 95.71000  ? 133  ARG B NE  1 
ATOM   2551 C CZ  . ARG B 2 133 ? -21.03924 -32.06130 -43.28940 1.000 97.20000  ? 133  ARG B CZ  1 
ATOM   2552 N NH1 . ARG B 2 133 ? -20.73011 -32.28300 -44.55723 1.000 99.42000  ? 133  ARG B NH1 1 
ATOM   2553 N NH2 . ARG B 2 133 ? -20.83680 -33.02301 -42.39230 1.000 88.35000  ? 133  ARG B NH2 1 
ATOM   2554 N N   . ASN B 2 134 ? -19.47536 -25.05831 -43.09608 1.000 80.38000  ? 134  ASN B N   1 
ATOM   2555 C CA  . ASN B 2 134 ? -19.89523 -23.80514 -43.72903 1.000 76.95000  ? 134  ASN B CA  1 
ATOM   2556 C C   . ASN B 2 134 ? -20.74717 -22.96282 -42.78006 1.000 77.98000  ? 134  ASN B C   1 
ATOM   2557 O O   . ASN B 2 134 ? -21.71966 -22.32277 -43.18586 1.000 80.40000  ? 134  ASN B O   1 
ATOM   2558 C CB  . ASN B 2 134 ? -20.63675 -24.07256 -45.04305 1.000 80.78000  ? 134  ASN B CB  1 
ATOM   2559 C CG  . ASN B 2 134 ? -20.05368 -23.29687 -46.22070 1.000 78.42000  ? 134  ASN B CG  1 
ATOM   2560 O OD1 . ASN B 2 134 ? -19.56782 -22.17671 -46.06425 1.000 70.04000  ? 134  ASN B OD1 1 
ATOM   2561 N ND2 . ASN B 2 134 ? -20.10607 -23.89420 -47.40752 1.000 79.61000  ? 134  ASN B ND2 1 
ATOM   2562 N N   . GLY B 2 135 ? -20.38655 -22.97887 -41.49529 1.000 70.24000  ? 135  GLY B N   1 
ATOM   2563 C CA  . GLY B 2 135 ? -21.02934 -22.15659 -40.48910 1.000 69.72000  ? 135  GLY B CA  1 
ATOM   2564 C C   . GLY B 2 135 ? -21.97123 -22.88830 -39.55777 1.000 67.45000  ? 135  GLY B C   1 
ATOM   2565 O O   . GLY B 2 135 ? -22.46437 -22.27284 -38.60257 1.000 63.46000  ? 135  GLY B O   1 
ATOM   2566 N N   . GLN B 2 136 ? -22.23612 -24.17172 -39.78996 1.000 63.47000  ? 136  GLN B N   1 
ATOM   2567 C CA  . GLN B 2 136 ? -23.16105 -24.94966 -38.97355 1.000 64.66000  ? 136  GLN B CA  1 
ATOM   2568 C C   . GLN B 2 136 ? -22.38686 -25.95042 -38.12556 1.000 63.40000  ? 136  GLN B C   1 
ATOM   2569 O O   . GLN B 2 136 ? -21.58161 -26.72379 -38.65648 1.000 70.93000  ? 136  GLN B O   1 
ATOM   2570 C CB  . GLN B 2 136 ? -24.17920 -25.68289 -39.85117 1.000 68.30000  ? 136  GLN B CB  1 
ATOM   2571 N N   . GLU B 2 137 ? -22.63613 -25.93792 -36.81428 1.000 54.76000  ? 137  GLU B N   1 
ATOM   2572 C CA  . GLU B 2 137 ? -21.97231 -26.87904 -35.92087 1.000 55.23000  ? 137  GLU B CA  1 
ATOM   2573 C C   . GLU B 2 137 ? -22.36402 -28.31288 -36.25695 1.000 64.38000  ? 137  GLU B C   1 
ATOM   2574 O O   . GLU B 2 137 ? -23.53488 -28.61744 -36.50075 1.000 71.93000  ? 137  GLU B O   1 
ATOM   2575 C CB  . GLU B 2 137 ? -22.31030 -26.57123 -34.46103 1.000 55.62000  ? 137  GLU B CB  1 
ATOM   2576 C CG  . GLU B 2 137 ? -21.90366 -27.68791 -33.50155 1.000 60.87000  ? 137  GLU B CG  1 
ATOM   2577 C CD  . GLU B 2 137 ? -21.06792 -27.21092 -32.33152 1.000 65.77000  ? 137  GLU B CD  1 
ATOM   2578 O OE1 . GLU B 2 137 ? -20.94349 -25.98228 -32.13968 1.000 73.49000  ? 137  GLU B OE1 1 
ATOM   2579 O OE2 . GLU B 2 137 ? -20.52935 -28.07408 -31.60453 1.000 68.46000  ? 137  GLU B OE2 1 
ATOM   2580 N N   . GLU B 2 138 ? -21.37083 -29.19846 -36.26412 1.000 60.74000  ? 138  GLU B N   1 
ATOM   2581 C CA  . GLU B 2 138 ? -21.55978 -30.59188 -36.64398 1.000 59.30000  ? 138  GLU B CA  1 
ATOM   2582 C C   . GLU B 2 138 ? -21.57012 -31.45304 -35.38809 1.000 58.26000  ? 138  GLU B C   1 
ATOM   2583 O O   . GLU B 2 138 ? -20.55576 -31.55931 -34.69145 1.000 56.94000  ? 138  GLU B O   1 
ATOM   2584 C CB  . GLU B 2 138 ? -20.46504 -31.03323 -37.61166 1.000 60.68000  ? 138  GLU B CB  1 
ATOM   2585 C CG  . GLU B 2 138 ? -20.61556 -30.47558 -39.02284 1.000 65.00000  ? 138  GLU B CG  1 
ATOM   2586 C CD  . GLU B 2 138 ? -21.99102 -30.73492 -39.62763 1.000 75.22000  ? 138  GLU B CD  1 
ATOM   2587 O OE1 . GLU B 2 138 ? -22.94918 -29.98435 -39.32295 1.000 80.96000  ? 138  GLU B OE1 1 
ATOM   2588 O OE2 . GLU B 2 138 ? -22.11310 -31.70451 -40.40672 1.000 79.89000  ? 138  GLU B OE2 1 
ATOM   2589 N N   . LYS B 2 139 ? -22.71823 -32.06475 -35.10185 1.000 64.64000  ? 139  LYS B N   1 
ATOM   2590 C CA  . LYS B 2 139 ? -22.86743 -32.96949 -33.96952 1.000 65.40000  ? 139  LYS B CA  1 
ATOM   2591 C C   . LYS B 2 139 ? -23.12226 -34.40764 -34.40419 1.000 61.81000  ? 139  LYS B C   1 
ATOM   2592 O O   . LYS B 2 139 ? -23.39018 -35.26473 -33.55611 1.000 74.63000  ? 139  LYS B O   1 
ATOM   2593 C CB  . LYS B 2 139 ? -23.99689 -32.48907 -33.05405 1.000 72.96000  ? 139  LYS B CB  1 
ATOM   2594 N N   . THR B 2 140 ? -23.04718 -34.69029 -35.70196 1.000 57.52000  ? 140  THR B N   1 
ATOM   2595 C CA  . THR B 2 140 ? -23.32202 -36.01324 -36.24814 1.000 59.72000  ? 140  THR B CA  1 
ATOM   2596 C C   . THR B 2 140 ? -22.12461 -36.45524 -37.07676 1.000 49.18000  ? 140  THR B C   1 
ATOM   2597 O O   . THR B 2 140 ? -21.61501 -35.68322 -37.89536 1.000 58.01000  ? 140  THR B O   1 
ATOM   2598 C CB  . THR B 2 140 ? -24.60235 -36.00773 -37.10456 1.000 62.09000  ? 140  THR B CB  1 
ATOM   2599 O OG1 . THR B 2 140 ? -25.75571 -35.94955 -36.25329 1.000 57.01000  ? 140  THR B OG1 1 
ATOM   2600 C CG2 . THR B 2 140 ? -24.68187 -37.25406 -37.97330 1.000 61.61000  ? 140  THR B CG2 1 
ATOM   2601 N N   . GLY B 2 141 ? -21.67744 -37.69017 -36.86177 1.000 43.40000  ? 141  GLY B N   1 
ATOM   2602 C CA  . GLY B 2 141 ? -20.47318 -38.16159 -37.51337 1.000 47.83000  ? 141  GLY B CA  1 
ATOM   2603 C C   . GLY B 2 141 ? -19.19210 -37.62078 -36.92128 1.000 47.25000  ? 141  GLY B C   1 
ATOM   2604 O O   . GLY B 2 141 ? -18.17345 -37.56246 -37.61613 1.000 45.14000  ? 141  GLY B O   1 
ATOM   2605 N N   . VAL B 2 142 ? -19.21665 -37.21206 -35.65595 1.000 42.06000  ? 142  VAL B N   1 
ATOM   2606 C CA  . VAL B 2 142 ? -18.04244 -36.69321 -34.96613 1.000 45.49000  ? 142  VAL B CA  1 
ATOM   2607 C C   . VAL B 2 142 ? -17.51195 -37.78348 -34.04882 1.000 47.34000  ? 142  VAL B C   1 
ATOM   2608 O O   . VAL B 2 142 ? -18.22045 -38.25007 -33.14814 1.000 50.85000  ? 142  VAL B O   1 
ATOM   2609 C CB  . VAL B 2 142 ? -18.36781 -35.42155 -34.16876 1.000 45.81000  ? 142  VAL B CB  1 
ATOM   2610 C CG1 . VAL B 2 142 ? -17.27877 -35.15771 -33.13009 1.000 44.16000  ? 142  VAL B CG1 1 
ATOM   2611 C CG2 . VAL B 2 142 ? -18.52318 -34.23760 -35.09989 1.000 46.75000  ? 142  VAL B CG2 1 
ATOM   2612 N N   . VAL B 2 143 ? -16.26703 -38.18676 -34.28090 1.000 47.80000  ? 143  VAL B N   1 
ATOM   2613 C CA  . VAL B 2 143 ? -15.56370 -39.16249 -33.45832 1.000 46.94000  ? 143  VAL B CA  1 
ATOM   2614 C C   . VAL B 2 143 ? -14.34489 -38.47359 -32.86393 1.000 43.90000  ? 143  VAL B C   1 
ATOM   2615 O O   . VAL B 2 143 ? -13.62499 -37.75909 -33.57140 1.000 48.27000  ? 143  VAL B O   1 
ATOM   2616 C CB  . VAL B 2 143 ? -15.14366 -40.39755 -34.27811 1.000 53.28000  ? 143  VAL B CB  1 
ATOM   2617 C CG1 . VAL B 2 143 ? -14.62937 -41.49750 -33.36429 1.000 57.31000  ? 143  VAL B CG1 1 
ATOM   2618 C CG2 . VAL B 2 143 ? -16.30202 -40.89510 -35.12723 1.000 56.02000  ? 143  VAL B CG2 1 
ATOM   2619 N N   . SER B 2 144 ? -14.11292 -38.68861 -31.57450 1.000 41.40000  ? 144  SER B N   1 
ATOM   2620 C CA  . SER B 2 144 ? -12.98464 -38.10424 -30.86599 1.000 42.42000  ? 144  SER B CA  1 
ATOM   2621 C C   . SER B 2 144 ? -12.27690 -39.15927 -30.02617 1.000 41.20000  ? 144  SER B C   1 
ATOM   2622 O O   . SER B 2 144 ? -12.91414 -40.04418 -29.44405 1.000 42.19000  ? 144  SER B O   1 
ATOM   2623 C CB  . SER B 2 144 ? -13.43312 -36.94848 -29.96802 1.000 41.54000  ? 144  SER B CB  1 
ATOM   2624 O OG  . SER B 2 144 ? -12.38511 -36.52159 -29.10833 1.000 44.33000  ? 144  SER B OG  1 
ATOM   2625 N N   . THR B 2 145 ? -10.95035 -39.05139 -29.96004 1.000 36.38000  ? 145  THR B N   1 
ATOM   2626 C CA  . THR B 2 145 ? -10.15389 -39.90559 -29.08823 1.000 35.23000  ? 145  THR B CA  1 
ATOM   2627 C C   . THR B 2 145 ? -10.31401 -39.55584 -27.61622 1.000 32.98000  ? 145  THR B C   1 
ATOM   2628 O O   . THR B 2 145 ? -9.82925  -40.30530 -26.76541 1.000 35.64000  ? 145  THR B O   1 
ATOM   2629 C CB  . THR B 2 145 ? -8.67383  -39.78468 -29.44853 1.000 37.10000  ? 145  THR B CB  1 
ATOM   2630 O OG1 . THR B 2 145 ? -8.28700  -38.40777 -29.34296 1.000 30.06000  ? 145  THR B OG1 1 
ATOM   2631 C CG2 . THR B 2 145 ? -8.42077  -40.26794 -30.86588 1.000 38.47000  ? 145  THR B CG2 1 
ATOM   2632 N N   . GLY B 2 146 ? -10.95763 -38.44028 -27.29652 1.000 29.72000  ? 146  GLY B N   1 
ATOM   2633 C CA  . GLY B 2 146 ? -10.85355 -37.87885 -25.96828 1.000 30.69000  ? 146  GLY B CA  1 
ATOM   2634 C C   . GLY B 2 146 ? -9.44211  -37.37202 -25.71934 1.000 32.42000  ? 146  GLY B C   1 
ATOM   2635 O O   . GLY B 2 146 ? -8.55177  -37.45423 -26.56420 1.000 35.69000  ? 146  GLY B O   1 
ATOM   2636 N N   . LEU B 2 147 ? -9.24572  -36.84368 -24.51626 1.000 30.54000  ? 147  LEU B N   1 
ATOM   2637 C CA  . LEU B 2 147 ? -7.95962  -36.27994 -24.13602 1.000 32.28000  ? 147  LEU B CA  1 
ATOM   2638 C C   . LEU B 2 147 ? -6.91294  -37.37926 -23.99078 1.000 30.84000  ? 147  LEU B C   1 
ATOM   2639 O O   . LEU B 2 147 ? -7.15655  -38.39482 -23.33343 1.000 33.91000  ? 147  LEU B O   1 
ATOM   2640 C CB  . LEU B 2 147 ? -8.10654  -35.51115 -22.82413 1.000 31.95000  ? 147  LEU B CB  1 
ATOM   2641 C CG  . LEU B 2 147 ? -6.91031  -34.68288 -22.36590 1.000 32.90000  ? 147  LEU B CG  1 
ATOM   2642 C CD1 . LEU B 2 147 ? -6.66087  -33.54270 -23.33190 1.000 33.17000  ? 147  LEU B CD1 1 
ATOM   2643 C CD2 . LEU B 2 147 ? -7.13456  -34.17036 -20.94351 1.000 33.19000  ? 147  LEU B CD2 1 
ATOM   2644 N N   . ILE B 2 148 ? -5.74206  -37.17496 -24.59137 1.000 32.80000  ? 148  ILE B N   1 
ATOM   2645 C CA  . ILE B 2 148 ? -4.63204  -38.11958 -24.49001 1.000 33.28000  ? 148  ILE B CA  1 
ATOM   2646 C C   . ILE B 2 148 ? -3.43144  -37.40919 -23.87662 1.000 32.64000  ? 148  ILE B C   1 
ATOM   2647 O O   . ILE B 2 148 ? -2.92995  -36.42151 -24.43172 1.000 29.23000  ? 148  ILE B O   1 
ATOM   2648 C CB  . ILE B 2 148 ? -4.26033  -38.73072 -25.84782 1.000 35.92000  ? 148  ILE B CB  1 
ATOM   2649 C CG1 . ILE B 2 148 ? -5.45376  -39.47469 -26.44686 1.000 35.87000  ? 148  ILE B CG1 1 
ATOM   2650 C CG2 . ILE B 2 148 ? -3.07555  -39.67195 -25.69010 1.000 38.54000  ? 148  ILE B CG2 1 
ATOM   2651 C CD1 . ILE B 2 148 ? -5.31697  -39.74159 -27.93963 1.000 36.25000  ? 148  ILE B CD1 1 
ATOM   2652 N N   . GLN B 2 149 ? -2.97330  -37.91509 -22.73540 1.000 36.27000  ? 149  GLN B N   1 
ATOM   2653 C CA  . GLN B 2 149 ? -1.76855  -37.40841 -22.09850 1.000 36.99000  ? 149  GLN B CA  1 
ATOM   2654 C C   . GLN B 2 149 ? -0.55190  -38.07695 -22.72348 1.000 31.32000  ? 149  GLN B C   1 
ATOM   2655 O O   . GLN B 2 149 ? -0.46433  -39.30578 -22.76357 1.000 33.24000  ? 149  GLN B O   1 
ATOM   2656 C CB  . GLN B 2 149 ? -1.81006  -37.67588 -20.59165 1.000 43.28000  ? 149  GLN B CB  1 
ATOM   2657 C CG  . GLN B 2 149 ? -0.47331  -37.47159 -19.88025 1.000 47.19000  ? 149  GLN B CG  1 
ATOM   2658 C CD  . GLN B 2 149 ? -0.45598  -38.05718 -18.47700 1.000 52.32000  ? 149  GLN B CD  1 
ATOM   2659 O OE1 . GLN B 2 149 ? -1.32198  -38.85590 -18.11878 1.000 53.24000  ? 149  GLN B OE1 1 
ATOM   2660 N NE2 . GLN B 2 149 ? 0.54408   -37.67756 -17.68245 1.000 51.94000  ? 149  GLN B NE2 1 
ATOM   2661 N N   . ASN B 2 150 ? 0.38472   -37.27158 -23.21772 1.000 29.97000  ? 150  ASN B N   1 
ATOM   2662 C CA  . ASN B 2 150 ? 1.60553   -37.81467 -23.80426 1.000 29.01000  ? 150  ASN B CA  1 
ATOM   2663 C C   . ASN B 2 150 ? 2.66226   -38.18481 -22.76580 1.000 30.26000  ? 150  ASN B C   1 
ATOM   2664 O O   . ASN B 2 150 ? 3.65559   -38.82662 -23.12295 1.000 31.96000  ? 150  ASN B O   1 
ATOM   2665 C CB  . ASN B 2 150 ? 2.19392   -36.81261 -24.80098 1.000 30.92000  ? 150  ASN B CB  1 
ATOM   2666 C CG  . ASN B 2 150 ? 1.28118   -36.56956 -25.98117 1.000 31.40000  ? 150  ASN B CG  1 
ATOM   2667 O OD1 . ASN B 2 150 ? 0.66025   -37.49802 -26.50044 1.000 30.79000  ? 150  ASN B OD1 1 
ATOM   2668 N ND2 . ASN B 2 150 ? 1.18348   -35.31810 -26.40519 1.000 35.52000  ? 150  ASN B ND2 1 
ATOM   2669 N N   . GLY B 2 151 ? 2.48231   -37.79926 -21.50177 1.000 30.84000  ? 151  GLY B N   1 
ATOM   2670 C CA  . GLY B 2 151 ? 3.44134   -38.11368 -20.46397 1.000 30.09000  ? 151  GLY B CA  1 
ATOM   2671 C C   . GLY B 2 151 ? 4.61182   -37.16370 -20.36256 1.000 30.22000  ? 151  GLY B C   1 
ATOM   2672 O O   . GLY B 2 151 ? 5.50602   -37.39546 -19.53964 1.000 34.31000  ? 151  GLY B O   1 
ATOM   2673 N N   . ASP B 2 152 ? 4.63440   -36.10171 -21.16602 1.000 32.35000  ? 152  ASP B N   1 
ATOM   2674 C CA  . ASP B 2 152 ? 5.72661   -35.14126 -21.18731 1.000 30.56000  ? 152  ASP B CA  1 
ATOM   2675 C C   . ASP B 2 152 ? 5.21639   -33.72464 -20.95687 1.000 27.30000  ? 152  ASP B C   1 
ATOM   2676 O O   . ASP B 2 152 ? 5.80058   -32.75689 -21.45623 1.000 26.41000  ? 152  ASP B O   1 
ATOM   2677 C CB  . ASP B 2 152 ? 6.50575   -35.24360 -22.50211 1.000 32.74000  ? 152  ASP B CB  1 
ATOM   2678 C CG  . ASP B 2 152 ? 5.69103   -34.79759 -23.73183 1.000 36.18000  ? 152  ASP B CG  1 
ATOM   2679 O OD1 . ASP B 2 152 ? 4.46184   -34.56178 -23.62831 1.000 35.65000  ? 152  ASP B OD1 1 
ATOM   2680 O OD2 . ASP B 2 152 ? 6.29193   -34.72137 -24.82686 1.000 41.69000  ? 152  ASP B OD2 1 
ATOM   2681 N N   . TRP B 2 153 ? 4.12437   -33.59339 -20.19967 1.000 27.07000  ? 153  TRP B N   1 
ATOM   2682 C CA  . TRP B 2 153 ? 3.49082   -32.30754 -19.91367 1.000 27.74000  ? 153  TRP B CA  1 
ATOM   2683 C C   . TRP B 2 153 ? 2.88668   -31.66837 -21.15607 1.000 26.09000  ? 153  TRP B C   1 
ATOM   2684 O O   . TRP B 2 153 ? 2.72496   -30.44746 -21.21479 1.000 28.60000  ? 153  TRP B O   1 
ATOM   2685 C CB  . TRP B 2 153 ? 4.46476   -31.33239 -19.24515 1.000 28.89000  ? 153  TRP B CB  1 
ATOM   2686 C CG  . TRP B 2 153 ? 4.80832   -31.74375 -17.86388 1.000 27.40000  ? 153  TRP B CG  1 
ATOM   2687 C CD1 . TRP B 2 153 ? 5.62413   -32.77050 -17.49799 1.000 28.89000  ? 153  TRP B CD1 1 
ATOM   2688 C CD2 . TRP B 2 153 ? 4.33831   -31.14903 -16.65180 1.000 26.70000  ? 153  TRP B CD2 1 
ATOM   2689 N NE1 . TRP B 2 153 ? 5.69711   -32.85031 -16.13167 1.000 30.31000  ? 153  TRP B NE1 1 
ATOM   2690 C CE2 . TRP B 2 153 ? 4.91725   -31.86357 -15.58768 1.000 27.23000  ? 153  TRP B CE2 1 
ATOM   2691 C CE3 . TRP B 2 153 ? 3.48726   -30.07819 -16.36313 1.000 28.03000  ? 153  TRP B CE3 1 
ATOM   2692 C CZ2 . TRP B 2 153 ? 4.66927   -31.54776 -14.25663 1.000 27.54000  ? 153  TRP B CZ2 1 
ATOM   2693 C CZ3 . TRP B 2 153 ? 3.24408   -29.76454 -15.04372 1.000 30.68000  ? 153  TRP B CZ3 1 
ATOM   2694 C CH2 . TRP B 2 153 ? 3.83039   -30.49856 -14.00478 1.000 28.22000  ? 153  TRP B CH2 1 
ATOM   2695 N N   . THR B 2 154 ? 2.55948   -32.47533 -22.15815 1.000 26.03000  ? 154  THR B N   1 
ATOM   2696 C CA  . THR B 2 154 ? 1.70683   -32.05216 -23.25305 1.000 28.68000  ? 154  THR B CA  1 
ATOM   2697 C C   . THR B 2 154 ? 0.57230   -33.05661 -23.39944 1.000 29.72000  ? 154  THR B C   1 
ATOM   2698 O O   . THR B 2 154 ? 0.66420   -34.20668 -22.95790 1.000 26.78000  ? 154  THR B O   1 
ATOM   2699 C CB  . THR B 2 154 ? 2.47386   -31.92001 -24.58248 1.000 28.59000  ? 154  THR B CB  1 
ATOM   2700 O OG1 . THR B 2 154 ? 2.96055   -33.20748 -24.98241 1.000 28.96000  ? 154  THR B OG1 1 
ATOM   2701 C CG2 . THR B 2 154 ? 3.64024   -30.94141 -24.45099 1.000 28.31000  ? 154  THR B CG2 1 
ATOM   2702 N N   . PHE B 2 155 ? -0.50915  -32.59241 -24.01187 1.000 27.98000  ? 155  PHE B N   1 
ATOM   2703 C CA  . PHE B 2 155 ? -1.67787  -33.40048 -24.30429 1.000 28.46000  ? 155  PHE B CA  1 
ATOM   2704 C C   . PHE B 2 155 ? -1.96744  -33.33660 -25.79581 1.000 30.06000  ? 155  PHE B C   1 
ATOM   2705 O O   . PHE B 2 155 ? -1.47822  -32.45508 -26.51171 1.000 28.92000  ? 155  PHE B O   1 
ATOM   2706 C CB  . PHE B 2 155 ? -2.91219  -32.91154 -23.53030 1.000 30.96000  ? 155  PHE B CB  1 
ATOM   2707 C CG  . PHE B 2 155 ? -2.80582  -33.07632 -22.04368 1.000 34.63000  ? 155  PHE B CG  1 
ATOM   2708 C CD1 . PHE B 2 155 ? -2.19000  -32.10653 -21.26884 1.000 37.77000  ? 155  PHE B CD1 1 
ATOM   2709 C CD2 . PHE B 2 155 ? -3.33790  -34.19101 -21.41829 1.000 34.81000  ? 155  PHE B CD2 1 
ATOM   2710 C CE1 . PHE B 2 155 ? -2.09360  -32.25548 -19.89688 1.000 39.86000  ? 155  PHE B CE1 1 
ATOM   2711 C CE2 . PHE B 2 155 ? -3.24885  -34.34668 -20.05159 1.000 33.97000  ? 155  PHE B CE2 1 
ATOM   2712 C CZ  . PHE B 2 155 ? -2.62524  -33.38023 -19.28757 1.000 36.92000  ? 155  PHE B CZ  1 
ATOM   2713 N N   . GLN B 2 156 ? -2.79086  -34.27140 -26.25528 1.000 27.00000  ? 156  GLN B N   1 
ATOM   2714 C CA  . GLN B 2 156 ? -3.28738  -34.21526 -27.61421 1.000 29.90000  ? 156  GLN B CA  1 
ATOM   2715 C C   . GLN B 2 156 ? -4.66472  -34.85392 -27.65048 1.000 29.08000  ? 156  GLN B C   1 
ATOM   2716 O O   . GLN B 2 156 ? -5.05075  -35.60880 -26.75366 1.000 30.72000  ? 156  GLN B O   1 
ATOM   2717 C CB  . GLN B 2 156 ? -2.33244  -34.89995 -28.60373 1.000 29.69000  ? 156  GLN B CB  1 
ATOM   2718 C CG  . GLN B 2 156 ? -2.05855  -36.35734 -28.30209 1.000 31.15000  ? 156  GLN B CG  1 
ATOM   2719 C CD  . GLN B 2 156 ? -1.35982  -37.07963 -29.45233 1.000 30.51000  ? 156  GLN B CD  1 
ATOM   2720 O OE1 . GLN B 2 156 ? -1.87948  -37.14923 -30.56643 1.000 31.40000  ? 156  GLN B OE1 1 
ATOM   2721 N NE2 . GLN B 2 156 ? -0.18004  -37.63073 -29.17629 1.000 30.05000  ? 156  GLN B NE2 1 
ATOM   2722 N N   . THR B 2 157 ? -5.40660  -34.51927 -28.69829 1.000 28.18000  ? 157  THR B N   1 
ATOM   2723 C CA  . THR B 2 157 ? -6.70138  -35.11919 -28.95456 1.000 33.03000  ? 157  THR B CA  1 
ATOM   2724 C C   . THR B 2 157 ? -6.93852  -35.08581 -30.45761 1.000 33.51000  ? 157  THR B C   1 
ATOM   2725 O O   . THR B 2 157 ? -6.46084  -34.18394 -31.14902 1.000 35.63000  ? 157  THR B O   1 
ATOM   2726 C CB  . THR B 2 157 ? -7.81399  -34.39616 -28.19121 1.000 32.58000  ? 157  THR B CB  1 
ATOM   2727 O OG1 . THR B 2 157 ? -9.05284  -35.08569 -28.37761 1.000 38.25000  ? 157  THR B OG1 1 
ATOM   2728 C CG2 . THR B 2 157 ? -7.96855  -32.98035 -28.70136 1.000 33.85000  ? 157  THR B CG2 1 
ATOM   2729 N N   . LEU B 2 158 ? -7.63015  -36.10093 -30.95998 1.000 36.59000  ? 158  LEU B N   1 
ATOM   2730 C CA  . LEU B 2 158 ? -7.94336  -36.22402 -32.37483 1.000 38.24000  ? 158  LEU B CA  1 
ATOM   2731 C C   . LEU B 2 158 ? -9.45081  -36.32191 -32.51681 1.000 37.01000  ? 158  LEU B C   1 
ATOM   2732 O O   . LEU B 2 158 ? -10.07600 -37.19789 -31.91960 1.000 36.26000  ? 158  LEU B O   1 
ATOM   2733 C CB  . LEU B 2 158 ? -7.26609  -37.44499 -32.99681 1.000 42.08000  ? 158  LEU B CB  1 
ATOM   2734 C CG  . LEU B 2 158 ? -5.95455  -37.10904 -33.70453 1.000 52.05000  ? 158  LEU B CG  1 
ATOM   2735 C CD1 . LEU B 2 158 ? -4.86855  -36.85516 -32.67089 1.000 57.77000  ? 158  LEU B CD1 1 
ATOM   2736 C CD2 . LEU B 2 158 ? -5.54941  -38.20561 -34.67119 1.000 53.09000  ? 158  LEU B CD2 1 
ATOM   2737 N N   . VAL B 2 159 ? -10.03010 -35.42301 -33.30100 1.000 33.52000  ? 159  VAL B N   1 
ATOM   2738 C CA  . VAL B 2 159 ? -11.47499 -35.33249 -33.46971 1.000 33.10000  ? 159  VAL B CA  1 
ATOM   2739 C C   . VAL B 2 159 ? -11.77546 -35.44890 -34.94877 1.000 34.42000  ? 159  VAL B C   1 
ATOM   2740 O O   . VAL B 2 159 ? -11.37783 -34.58035 -35.73237 1.000 36.34000  ? 159  VAL B O   1 
ATOM   2741 C CB  . VAL B 2 159 ? -12.03976 -34.02385 -32.89761 1.000 33.82000  ? 159  VAL B CB  1 
ATOM   2742 C CG1 . VAL B 2 159 ? -13.53866 -34.00707 -33.04468 1.000 35.94000  ? 159  VAL B CG1 1 
ATOM   2743 C CG2 . VAL B 2 159 ? -11.62464 -33.85419 -31.43448 1.000 33.28000  ? 159  VAL B CG2 1 
ATOM   2744 N N   . MET B 2 160 ? -12.48356 -36.50646 -35.32780 1.000 38.74000  ? 160  MET B N   1 
ATOM   2745 C CA  . MET B 2 160 ? -12.70138 -36.84477 -36.72339 1.000 42.53000  ? 160  MET B CA  1 
ATOM   2746 C C   . MET B 2 160 ? -14.13300 -36.53278 -37.12679 1.000 39.88000  ? 160  MET B C   1 
ATOM   2747 O O   . MET B 2 160 ? -15.07122 -36.72693 -36.34782 1.000 35.69000  ? 160  MET B O   1 
ATOM   2748 C CB  . MET B 2 160 ? -12.41685 -38.32657 -36.97804 1.000 46.77000  ? 160  MET B CB  1 
ATOM   2749 C CG  . MET B 2 160 ? -10.95537 -38.68656 -36.94042 1.000 56.76000  ? 160  MET B CG  1 
ATOM   2750 S SD  . MET B 2 160 ? -10.69383 -40.35209 -36.30229 1.000 72.45000  ? 160  MET B SD  1 
ATOM   2751 C CE  . MET B 2 160 ? -10.22030 -40.01645 -34.60678 1.000 65.75000  ? 160  MET B CE  1 
ATOM   2752 N N   . LEU B 2 161 ? -14.29271 -36.07038 -38.36339 1.000 39.50000  ? 161  LEU B N   1 
ATOM   2753 C CA  . LEU B 2 161 ? -15.59354 -35.71707 -38.91004 1.000 44.74000  ? 161  LEU B CA  1 
ATOM   2754 C C   . LEU B 2 161 ? -15.88053 -36.58549 -40.12604 1.000 46.70000  ? 161  LEU B C   1 
ATOM   2755 O O   . LEU B 2 161 ? -15.01198 -36.75544 -40.98814 1.000 42.30000  ? 161  LEU B O   1 
ATOM   2756 C CB  . LEU B 2 161 ? -15.63133 -34.23528 -39.29309 1.000 43.78000  ? 161  LEU B CB  1 
ATOM   2757 C CG  . LEU B 2 161 ? -16.97553 -33.70292 -39.77343 1.000 44.71000  ? 161  LEU B CG  1 
ATOM   2758 C CD1 . LEU B 2 161 ? -17.97500 -33.76055 -38.64011 1.000 43.64000  ? 161  LEU B CD1 1 
ATOM   2759 C CD2 . LEU B 2 161 ? -16.83624 -32.27848 -40.28866 1.000 45.61000  ? 161  LEU B CD2 1 
ATOM   2760 N N   . GLU B 2 162 ? -17.08552 -37.14933 -40.18545 1.000 54.36000  ? 162  GLU B N   1 
ATOM   2761 C CA  . GLU B 2 162 ? -17.55596 -37.82105 -41.39813 1.000 59.37000  ? 162  GLU B CA  1 
ATOM   2762 C C   . GLU B 2 162 ? -18.09119 -36.75078 -42.34058 1.000 57.71000  ? 162  GLU B C   1 
ATOM   2763 O O   . GLU B 2 162 ? -19.18821 -36.22413 -42.14413 1.000 68.35000  ? 162  GLU B O   1 
ATOM   2764 C CB  . GLU B 2 162 ? -18.62595 -38.85847 -41.07942 1.000 59.10000  ? 162  GLU B CB  1 
ATOM   2765 C CG  . GLU B 2 162 ? -18.27624 -39.82066 -39.95767 1.000 62.99000  ? 162  GLU B CG  1 
ATOM   2766 C CD  . GLU B 2 162 ? -19.35006 -40.87945 -39.75568 1.000 64.63000  ? 162  GLU B CD  1 
ATOM   2767 O OE1 . GLU B 2 162 ? -20.02507 -41.24330 -40.74291 1.000 62.19000  ? 162  GLU B OE1 1 
ATOM   2768 O OE2 . GLU B 2 162 ? -19.52768 -41.34107 -38.60891 1.000 67.17000  ? 162  GLU B OE2 1 
ATOM   2769 N N   . THR B 2 163 ? -17.31187 -36.41612 -43.36114 1.000 57.54000  ? 163  THR B N   1 
ATOM   2770 C CA  . THR B 2 163 ? -17.64637 -35.34827 -44.28876 1.000 58.98000  ? 163  THR B CA  1 
ATOM   2771 C C   . THR B 2 163 ? -18.27614 -35.92432 -45.55081 1.000 66.51000  ? 163  THR B C   1 
ATOM   2772 O O   . THR B 2 163 ? -18.11496 -37.10358 -45.87242 1.000 60.36000  ? 163  THR B O   1 
ATOM   2773 C CB  . THR B 2 163 ? -16.39630 -34.54823 -44.66327 1.000 65.24000  ? 163  THR B CB  1 
ATOM   2774 O OG1 . THR B 2 163 ? -15.31056 -35.44975 -44.90077 1.000 73.40000  ? 163  THR B OG1 1 
ATOM   2775 C CG2 . THR B 2 163 ? -16.00607 -33.62233 -43.53144 1.000 65.00000  ? 163  THR B CG2 1 
ATOM   2776 N N   . VAL B 2 164 ? -19.00179 -35.07395 -46.26772 1.000 70.77000  ? 164  VAL B N   1 
ATOM   2777 C CA  . VAL B 2 164 ? -19.47114 -35.42174 -47.60665 1.000 75.50000  ? 164  VAL B CA  1 
ATOM   2778 C C   . VAL B 2 164 ? -18.49286 -34.79686 -48.59458 1.000 81.86000  ? 164  VAL B C   1 
ATOM   2779 O O   . VAL B 2 164 ? -18.61634 -33.60440 -48.91090 1.000 80.58000  ? 164  VAL B O   1 
ATOM   2780 C CB  . VAL B 2 164 ? -20.91421 -34.94740 -47.84666 1.000 72.70000  ? 164  VAL B CB  1 
ATOM   2781 C CG1 . VAL B 2 164 ? -21.35646 -35.29082 -49.25738 1.000 75.19000  ? 164  VAL B CG1 1 
ATOM   2782 C CG2 . VAL B 2 164 ? -21.85528 -35.57070 -46.82758 1.000 70.88000  ? 164  VAL B CG2 1 
ATOM   2783 N N   . PRO B 2 165 ? -17.50319 -35.54547 -49.08423 1.000 98.35000  ? 165  PRO B N   1 
ATOM   2784 C CA  . PRO B 2 165 ? -16.47169 -34.94852 -49.94823 1.000 105.66000 ? 165  PRO B CA  1 
ATOM   2785 C C   . PRO B 2 165 ? -17.08179 -34.34023 -51.20483 1.000 109.48000 ? 165  PRO B C   1 
ATOM   2786 O O   . PRO B 2 165 ? -17.80302 -35.00468 -51.95795 1.000 119.27000 ? 165  PRO B O   1 
ATOM   2787 C CB  . PRO B 2 165 ? -15.55580 -36.13285 -50.27924 1.000 103.93000 ? 165  PRO B CB  1 
ATOM   2788 C CG  . PRO B 2 165 ? -16.37099 -37.35364 -49.98445 1.000 104.54000 ? 165  PRO B CG  1 
ATOM   2789 C CD  . PRO B 2 165 ? -17.27163 -36.97779 -48.85722 1.000 103.79000 ? 165  PRO B CD  1 
ATOM   2790 N N   . ARG B 2 166 ? -16.78301 -33.05775 -51.42180 1.000 105.87000 ? 166  ARG B N   1 
ATOM   2791 C CA  . ARG B 2 166 ? -17.30244 -32.25487 -52.52487 1.000 102.25000 ? 166  ARG B CA  1 
ATOM   2792 C C   . ARG B 2 166 ? -16.56814 -30.92097 -52.52637 1.000 101.50000 ? 166  ARG B C   1 
ATOM   2793 O O   . ARG B 2 166 ? -16.18251 -30.40795 -51.47116 1.000 104.35000 ? 166  ARG B O   1 
ATOM   2794 C CB  . ARG B 2 166 ? -18.80795 -32.06148 -52.41876 1.000 100.51000 ? 166  ARG B CB  1 
ATOM   2795 C CG  . ARG B 2 166 ? -19.41391 -31.14270 -53.46038 1.000 98.35000  ? 166  ARG B CG  1 
ATOM   2796 C CD  . ARG B 2 166 ? -20.88020 -30.88778 -53.16578 1.000 97.49000  ? 166  ARG B CD  1 
ATOM   2797 N NE  . ARG B 2 166 ? -21.74708 -31.54580 -54.13414 1.000 98.43000  ? 166  ARG B NE  1 
ATOM   2798 C CZ  . ARG B 2 166 ? -22.85797 -32.19528 -53.81915 1.000 92.27000  ? 166  ARG B CZ  1 
ATOM   2799 N NH1 . ARG B 2 166 ? -23.26907 -32.29232 -52.56604 1.000 92.55000  ? 166  ARG B NH1 1 
ATOM   2800 N NH2 . ARG B 2 166 ? -23.57261 -32.76315 -54.78488 1.000 92.05000  ? 166  ARG B NH2 1 
ATOM   2801 N N   . SER B 2 167 ? -16.31888 -30.41327 -53.73516 1.000 109.41000 ? 167  SER B N   1 
ATOM   2802 C CA  . SER B 2 167 ? -15.70038 -29.11106 -53.97253 1.000 109.29000 ? 167  SER B CA  1 
ATOM   2803 C C   . SER B 2 167 ? -14.77961 -28.61152 -52.85945 1.000 112.95000 ? 167  SER B C   1 
ATOM   2804 O O   . SER B 2 167 ? -14.86085 -27.44965 -52.45339 1.000 132.12000 ? 167  SER B O   1 
ATOM   2805 C CB  . SER B 2 167 ? -16.78877 -28.06840 -54.20431 1.000 116.19000 ? 167  SER B CB  1 
ATOM   2806 O OG  . SER B 2 167 ? -17.60737 -27.86675 -53.06196 1.000 127.81000 ? 167  SER B OG  1 
ATOM   2807 N N   . GLU B 2 169 ? -17.47774 -26.64412 -50.42466 1.000 88.78000  ? 169  GLU B N   1 
ATOM   2808 C CA  . GLU B 2 169 ? -17.83640 -26.75182 -49.02054 1.000 81.01000  ? 169  GLU B CA  1 
ATOM   2809 C C   . GLU B 2 169 ? -16.59555 -26.51053 -48.16703 1.000 78.29000  ? 169  GLU B C   1 
ATOM   2810 O O   . GLU B 2 169 ? -15.47050 -26.80430 -48.58400 1.000 78.06000  ? 169  GLU B O   1 
ATOM   2811 C CB  . GLU B 2 169 ? -18.45897 -28.12725 -48.72171 1.000 82.33000  ? 169  GLU B CB  1 
ATOM   2812 C CG  . GLU B 2 169 ? -19.87492 -28.07199 -48.14998 1.000 81.76000  ? 169  GLU B CG  1 
ATOM   2813 C CD  . GLU B 2 169 ? -19.94058 -27.46261 -46.76970 1.000 81.39000  ? 169  GLU B CD  1 
ATOM   2814 O OE1 . GLU B 2 169 ? -18.91790 -27.51807 -46.05453 1.000 94.90000  ? 169  GLU B OE1 1 
ATOM   2815 O OE2 . GLU B 2 169 ? -21.01777 -26.93593 -46.40215 1.000 85.29000  ? 169  GLU B OE2 1 
ATOM   2816 N N   . VAL B 2 170 ? -16.81144 -25.96223 -46.97323 1.000 70.48000  ? 170  VAL B N   1 
ATOM   2817 C CA  . VAL B 2 170 ? -15.73674 -25.54795 -46.08271 1.000 66.33000  ? 170  VAL B CA  1 
ATOM   2818 C C   . VAL B 2 170 ? -16.04713 -26.05247 -44.68199 1.000 58.65000  ? 170  VAL B C   1 
ATOM   2819 O O   . VAL B 2 170 ? -17.10028 -25.73038 -44.12271 1.000 53.14000  ? 170  VAL B O   1 
ATOM   2820 C CB  . VAL B 2 170 ? -15.55104 -24.02247 -46.07262 1.000 65.57000  ? 170  VAL B CB  1 
ATOM   2821 C CG1 . VAL B 2 170 ? -14.62262 -23.62466 -44.93489 1.000 64.79000  ? 170  VAL B CG1 1 
ATOM   2822 C CG2 . VAL B 2 170 ? -15.00363 -23.53940 -47.40886 1.000 70.34000  ? 170  VAL B CG2 1 
ATOM   2823 N N   . TYR B 2 171 ? -15.11840 -26.81716 -44.11327 1.000 53.32000  ? 171  TYR B N   1 
ATOM   2824 C CA  . TYR B 2 171 ? -15.21164 -27.35591 -42.76290 1.000 52.04000  ? 171  TYR B CA  1 
ATOM   2825 C C   . TYR B 2 171 ? -14.21296 -26.63834 -41.86322 1.000 48.06000  ? 171  TYR B C   1 
ATOM   2826 O O   . TYR B 2 171 ? -13.04797 -26.46141 -42.23558 1.000 48.61000  ? 171  TYR B O   1 
ATOM   2827 C CB  . TYR B 2 171 ? -14.95007 -28.86748 -42.76216 1.000 51.88000  ? 171  TYR B CB  1 
ATOM   2828 C CG  . TYR B 2 171 ? -15.82780 -29.61604 -43.73678 1.000 52.42000  ? 171  TYR B CG  1 
ATOM   2829 C CD1 . TYR B 2 171 ? -15.46006 -29.77208 -45.06986 1.000 55.97000  ? 171  TYR B CD1 1 
ATOM   2830 C CD2 . TYR B 2 171 ? -17.04109 -30.14808 -43.32991 1.000 55.15000  ? 171  TYR B CD2 1 
ATOM   2831 C CE1 . TYR B 2 171 ? -16.26845 -30.44648 -45.96219 1.000 60.20000  ? 171  TYR B CE1 1 
ATOM   2832 C CE2 . TYR B 2 171 ? -17.85912 -30.82261 -44.21240 1.000 55.25000  ? 171  TYR B CE2 1 
ATOM   2833 C CZ  . TYR B 2 171 ? -17.46621 -30.97143 -45.52533 1.000 61.12000  ? 171  TYR B CZ  1 
ATOM   2834 O OH  . TYR B 2 171 ? -18.28547 -31.64798 -46.39907 1.000 73.38000  ? 171  TYR B OH  1 
ATOM   2835 N N   . THR B 2 172 ? -14.67033 -26.22306 -40.68711 1.000 40.40000  ? 172  THR B N   1 
ATOM   2836 C CA  . THR B 2 172 ? -13.84118 -25.50749 -39.73078 1.000 41.04000  ? 172  THR B CA  1 
ATOM   2837 C C   . THR B 2 172 ? -13.68823 -26.32658 -38.45858 1.000 34.54000  ? 172  THR B C   1 
ATOM   2838 O O   . THR B 2 172 ? -14.68613 -26.73817 -37.85356 1.000 33.73000  ? 172  THR B O   1 
ATOM   2839 C CB  . THR B 2 172 ? -14.44133 -24.14162 -39.38154 1.000 44.02000  ? 172  THR B CB  1 
ATOM   2840 O OG1 . THR B 2 172 ? -14.61266 -23.36527 -40.57422 1.000 43.86000  ? 172  THR B OG1 1 
ATOM   2841 C CG2 . THR B 2 172 ? -13.53324 -23.39447 -38.40510 1.000 41.81000  ? 172  THR B CG2 1 
ATOM   2842 N N   . CYS B 2 173 ? -12.44311 -26.54467 -38.04775 1.000 33.23000  ? 173  CYS B N   1 
ATOM   2843 C CA  . CYS B 2 173 ? -12.15799 -27.02052 -36.70471 1.000 32.81000  ? 173  CYS B CA  1 
ATOM   2844 C C   . CYS B 2 173 ? -11.89774 -25.81011 -35.82090 1.000 29.17000  ? 173  CYS B C   1 
ATOM   2845 O O   . CYS B 2 173 ? -11.04831 -24.97256 -36.14173 1.000 31.53000  ? 173  CYS B O   1 
ATOM   2846 C CB  . CYS B 2 173 ? -10.95558 -27.96373 -36.68888 1.000 31.73000  ? 173  CYS B CB  1 
ATOM   2847 S SG  . CYS B 2 173 ? -10.62200 -28.67235 -35.04741 1.000 37.90000  ? 173  CYS B SG  1 
ATOM   2848 N N   . GLN B 2 174 ? -12.64351 -25.70774 -34.72692 1.000 27.97000  ? 174  GLN B N   1 
ATOM   2849 C CA  . GLN B 2 174 ? -12.51608 -24.60558 -33.78645 1.000 29.02000  ? 174  GLN B CA  1 
ATOM   2850 C C   . GLN B 2 174 ? -12.05379 -25.16018 -32.45278 1.000 26.43000  ? 174  GLN B C   1 
ATOM   2851 O O   . GLN B 2 174 ? -12.66028 -26.09799 -31.92779 1.000 30.05000  ? 174  GLN B O   1 
ATOM   2852 C CB  . GLN B 2 174 ? -13.84141 -23.86271 -33.61944 1.000 29.42000  ? 174  GLN B CB  1 
ATOM   2853 C CG  . GLN B 2 174 ? -13.77926 -22.71878 -32.63332 1.000 31.21000  ? 174  GLN B CG  1 
ATOM   2854 C CD  . GLN B 2 174 ? -14.97557 -21.79738 -32.74668 1.000 33.03000  ? 174  GLN B CD  1 
ATOM   2855 O OE1 . GLN B 2 174 ? -15.32705 -21.34555 -33.84074 1.000 37.85000  ? 174  GLN B OE1 1 
ATOM   2856 N NE2 . GLN B 2 174 ? -15.61726 -21.52090 -31.61410 1.000 32.84000  ? 174  GLN B NE2 1 
ATOM   2857 N N   . VAL B 2 175 ? -10.98321 -24.58663 -31.91075 1.000 27.37000  ? 175  VAL B N   1 
ATOM   2858 C CA  . VAL B 2 175 ? -10.36712 -25.06430 -30.67888 1.000 28.50000  ? 175  VAL B CA  1 
ATOM   2859 C C   . VAL B 2 175 ? -10.36960 -23.93468 -29.66111 1.000 29.09000  ? 175  VAL B C   1 
ATOM   2860 O O   . VAL B 2 175 ? -9.95194  -22.81155 -29.96688 1.000 29.25000  ? 175  VAL B O   1 
ATOM   2861 C CB  . VAL B 2 175 ? -8.93664  -25.57694 -30.92534 1.000 27.18000  ? 175  VAL B CB  1 
ATOM   2862 C CG1 . VAL B 2 175 ? -8.31933  -26.06556 -29.63230 1.000 27.93000  ? 175  VAL B CG1 1 
ATOM   2863 C CG2 . VAL B 2 175 ? -8.95192  -26.68567 -31.97121 1.000 26.84000  ? 175  VAL B CG2 1 
ATOM   2864 N N   . GLU B 2 176 ? -10.83865 -24.23616 -28.45547 1.000 30.66000  ? 176  GLU B N   1 
ATOM   2865 C CA  . GLU B 2 176 ? -10.82337 -23.30804 -27.33592 1.000 33.74000  ? 176  GLU B CA  1 
ATOM   2866 C C   . GLU B 2 176 ? -9.99886  -23.92478 -26.21573 1.000 33.15000  ? 176  GLU B C   1 
ATOM   2867 O O   . GLU B 2 176 ? -10.17533 -25.10289 -25.89038 1.000 33.31000  ? 176  GLU B O   1 
ATOM   2868 C CB  . GLU B 2 176 ? -12.24670 -22.99210 -26.86702 1.000 37.42000  ? 176  GLU B CB  1 
ATOM   2869 C CG  . GLU B 2 176 ? -12.97443 -21.97625 -27.75343 1.000 40.58000  ? 176  GLU B CG  1 
ATOM   2870 C CD  . GLU B 2 176 ? -14.40368 -22.38682 -28.08205 1.000 47.60000  ? 176  GLU B CD  1 
ATOM   2871 O OE1 . GLU B 2 176 ? -15.13728 -22.79042 -27.15335 1.000 57.40000  ? 176  GLU B OE1 1 
ATOM   2872 O OE2 . GLU B 2 176 ? -14.79695 -22.29601 -29.26736 1.000 58.95000  ? 176  GLU B OE2 1 
ATOM   2873 N N   . HIS B 2 177 ? -9.09414  -23.12772 -25.63345 1.000 34.99000  ? 177  HIS B N   1 
ATOM   2874 C CA  . HIS B 2 177 ? -8.09216  -23.63718 -24.70903 1.000 35.10000  ? 177  HIS B CA  1 
ATOM   2875 C C   . HIS B 2 177 ? -7.62867  -22.51264 -23.79794 1.000 34.65000  ? 177  HIS B C   1 
ATOM   2876 O O   . HIS B 2 177 ? -7.52420  -21.36771 -24.25663 1.000 38.81000  ? 177  HIS B O   1 
ATOM   2877 C CB  . HIS B 2 177 ? -6.90300  -24.23515 -25.47562 1.000 34.67000  ? 177  HIS B CB  1 
ATOM   2878 C CG  . HIS B 2 177 ? -5.86276  -24.85415 -24.59459 1.000 31.42000  ? 177  HIS B CG  1 
ATOM   2879 N ND1 . HIS B 2 177 ? -4.71053  -24.19274 -24.22413 1.000 32.19000  ? 177  HIS B ND1 1 
ATOM   2880 C CD2 . HIS B 2 177 ? -5.80557  -26.07050 -24.00093 1.000 31.24000  ? 177  HIS B CD2 1 
ATOM   2881 C CE1 . HIS B 2 177 ? -3.98699  -24.97625 -23.44266 1.000 33.61000  ? 177  HIS B CE1 1 
ATOM   2882 N NE2 . HIS B 2 177 ? -4.62923  -26.12148 -23.29094 1.000 29.40000  ? 177  HIS B NE2 1 
ATOM   2883 N N   . PRO B 2 178 ? -7.34210  -22.79157 -22.52304 1.000 34.24000  ? 178  PRO B N   1 
ATOM   2884 C CA  . PRO B 2 178 ? -6.97343  -21.71371 -21.58577 1.000 35.61000  ? 178  PRO B CA  1 
ATOM   2885 C C   . PRO B 2 178 ? -5.72009  -20.94242 -21.95819 1.000 35.24000  ? 178  PRO B C   1 
ATOM   2886 O O   . PRO B 2 178 ? -5.47058  -19.89178 -21.35749 1.000 35.31000  ? 178  PRO B O   1 
ATOM   2887 C CB  . PRO B 2 178 ? -6.77531  -22.45400 -20.25813 1.000 35.10000  ? 178  PRO B CB  1 
ATOM   2888 C CG  . PRO B 2 178 ? -7.61331  -23.67940 -20.38255 1.000 36.95000  ? 178  PRO B CG  1 
ATOM   2889 C CD  . PRO B 2 178 ? -7.60757  -24.06574 -21.83471 1.000 33.82000  ? 178  PRO B CD  1 
ATOM   2890 N N   . SER B 2 179 ? -4.91280  -21.42264 -22.89672 1.000 33.09000  ? 179  SER B N   1 
ATOM   2891 C CA  . SER B 2 179 ? -3.74844  -20.65221 -23.30563 1.000 29.35000  ? 179  SER B CA  1 
ATOM   2892 C C   . SER B 2 179 ? -4.08559  -19.58455 -24.33472 1.000 29.62000  ? 179  SER B C   1 
ATOM   2893 O O   . SER B 2 179 ? -3.21410  -18.77079 -24.66313 1.000 33.35000  ? 179  SER B O   1 
ATOM   2894 C CB  . SER B 2 179 ? -2.67902  -21.57588 -23.87827 1.000 30.14000  ? 179  SER B CB  1 
ATOM   2895 O OG  . SER B 2 179 ? -3.08848  -22.06802 -25.14251 1.000 31.94000  ? 179  SER B OG  1 
ATOM   2896 N N   . LEU B 2 180 ? -5.31648  -19.57150 -24.84541 1.000 29.68000  ? 180  LEU B N   1 
ATOM   2897 C CA  . LEU B 2 180 ? -5.72312  -18.71076 -25.94837 1.000 31.00000  ? 180  LEU B CA  1 
ATOM   2898 C C   . LEU B 2 180 ? -6.64211  -17.60438 -25.45182 1.000 33.27000  ? 180  LEU B C   1 
ATOM   2899 O O   . LEU B 2 180 ? -7.45112  -17.81726 -24.54232 1.000 32.17000  ? 180  LEU B O   1 
ATOM   2900 C CB  . LEU B 2 180 ? -6.44916  -19.51439 -27.02844 1.000 31.15000  ? 180  LEU B CB  1 
ATOM   2901 C CG  . LEU B 2 180 ? -5.75699  -20.78687 -27.51679 1.000 32.80000  ? 180  LEU B CG  1 
ATOM   2902 C CD1 . LEU B 2 180 ? -6.70713  -21.63362 -28.33944 1.000 30.77000  ? 180  LEU B CD1 1 
ATOM   2903 C CD2 . LEU B 2 180 ? -4.52563  -20.42403 -28.31768 1.000 32.99000  ? 180  LEU B CD2 1 
ATOM   2904 N N   . THR B 2 181 ? -6.52225  -16.42584 -26.06181 1.000 35.02000  ? 181  THR B N   1 
ATOM   2905 C CA  . THR B 2 181 ? -7.44480  -15.32360 -25.82281 1.000 38.58000  ? 181  THR B CA  1 
ATOM   2906 C C   . THR B 2 181 ? -8.53282  -15.24237 -26.88352 1.000 39.52000  ? 181  THR B C   1 
ATOM   2907 O O   . THR B 2 181 ? -9.33584  -14.30514 -26.86447 1.000 44.33000  ? 181  THR B O   1 
ATOM   2908 C CB  . THR B 2 181 ? -6.68381  -13.99413 -25.76369 1.000 36.95000  ? 181  THR B CB  1 
ATOM   2909 O OG1 . THR B 2 181 ? -5.96564  -13.80550 -26.98781 1.000 34.60000  ? 181  THR B OG1 1 
ATOM   2910 C CG2 . THR B 2 181 ? -5.69873  -13.99468 -24.60484 1.000 39.87000  ? 181  THR B CG2 1 
ATOM   2911 N N   . SER B 2 182 ? -8.56709  -16.19207 -27.81357 1.000 37.11000  ? 182  SER B N   1 
ATOM   2912 C CA  . SER B 2 182 ? -9.57849  -16.22687 -28.85875 1.000 38.58000  ? 182  SER B CA  1 
ATOM   2913 C C   . SER B 2 182 ? -9.66612  -17.65390 -29.36888 1.000 37.85000  ? 182  SER B C   1 
ATOM   2914 O O   . SER B 2 182 ? -8.68284  -18.39809 -29.27639 1.000 39.61000  ? 182  SER B O   1 
ATOM   2915 C CB  . SER B 2 182 ? -9.23345  -15.26366 -30.00761 1.000 39.46000  ? 182  SER B CB  1 
ATOM   2916 O OG  . SER B 2 182 ? -8.10810  -15.71452 -30.74236 1.000 40.37000  ? 182  SER B OG  1 
ATOM   2917 N N   . PRO B 2 183 ? -10.81735 -18.07443 -29.88750 1.000 35.86000  ? 183  PRO B N   1 
ATOM   2918 C CA  . PRO B 2 183 ? -10.89548 -19.41457 -30.47727 1.000 34.63000  ? 183  PRO B CA  1 
ATOM   2919 C C   . PRO B 2 183 ? -9.90185  -19.54915 -31.61973 1.000 31.60000  ? 183  PRO B C   1 
ATOM   2920 O O   . PRO B 2 183 ? -9.68234  -18.61433 -32.39267 1.000 33.73000  ? 183  PRO B O   1 
ATOM   2921 C CB  . PRO B 2 183 ? -12.34385 -19.50439 -30.97069 1.000 33.32000  ? 183  PRO B CB  1 
ATOM   2922 C CG  . PRO B 2 183 ? -13.08191 -18.48212 -30.16241 1.000 34.17000  ? 183  PRO B CG  1 
ATOM   2923 C CD  . PRO B 2 183 ? -12.10600 -17.36684 -29.95703 1.000 34.42000  ? 183  PRO B CD  1 
ATOM   2924 N N   . LEU B 2 184 ? -9.27731  -20.71677 -31.69987 1.000 33.44000  ? 184  LEU B N   1 
ATOM   2925 C CA  . LEU B 2 184 ? -8.39346  -21.05032 -32.80633 1.000 36.29000  ? 184  LEU B CA  1 
ATOM   2926 C C   . LEU B 2 184 ? -9.20711  -21.81281 -33.84282 1.000 34.31000  ? 184  LEU B C   1 
ATOM   2927 O O   . LEU B 2 184 ? -9.83427  -22.82464 -33.51518 1.000 32.25000  ? 184  LEU B O   1 
ATOM   2928 C CB  . LEU B 2 184 ? -7.21711  -21.88788 -32.31141 1.000 39.27000  ? 184  LEU B CB  1 
ATOM   2929 C CG  . LEU B 2 184 ? -5.83865  -21.72298 -32.94373 1.000 40.72000  ? 184  LEU B CG  1 
ATOM   2930 C CD1 . LEU B 2 184 ? -4.83680  -22.53558 -32.14328 1.000 41.03000  ? 184  LEU B CD1 1 
ATOM   2931 C CD2 . LEU B 2 184 ? -5.82729  -22.14340 -34.40395 1.000 44.89000  ? 184  LEU B CD2 1 
ATOM   2932 N N   . THR B 2 185 ? -9.21565  -21.32834 -35.07977 1.000 35.17000  ? 185  THR B N   1 
ATOM   2933 C CA  . THR B 2 185 ? -9.98156  -21.96195 -36.14348 1.000 34.94000  ? 185  THR B CA  1 
ATOM   2934 C C   . THR B 2 185 ? -9.06083  -22.33462 -37.29258 1.000 35.30000  ? 185  THR B C   1 
ATOM   2935 O O   . THR B 2 185 ? -8.17348  -21.56140 -37.67101 1.000 32.19000  ? 185  THR B O   1 
ATOM   2936 C CB  . THR B 2 185 ? -11.10006 -21.05321 -36.66970 1.000 33.51000  ? 185  THR B CB  1 
ATOM   2937 O OG1 . THR B 2 185 ? -10.52480 -19.89504 -37.28573 1.000 35.26000  ? 185  THR B OG1 1 
ATOM   2938 C CG2 . THR B 2 185 ? -12.01908 -20.61524 -35.53462 1.000 34.82000  ? 185  THR B CG2 1 
ATOM   2939 N N   . VAL B 2 186 ? -9.27227  -23.52935 -37.83454 1.000 34.45000  ? 186  VAL B N   1 
ATOM   2940 C CA  . VAL B 2 186 ? -8.60229  -23.98207 -39.04234 1.000 33.67000  ? 186  VAL B CA  1 
ATOM   2941 C C   . VAL B 2 186 ? -9.67727  -24.43348 -40.01336 1.000 36.19000  ? 186  VAL B C   1 
ATOM   2942 O O   . VAL B 2 186 ? -10.53881 -25.24551 -39.65617 1.000 33.34000  ? 186  VAL B O   1 
ATOM   2943 C CB  . VAL B 2 186 ? -7.61031  -25.12398 -38.76061 1.000 35.04000  ? 186  VAL B CB  1 
ATOM   2944 C CG1 . VAL B 2 186 ? -6.97955  -25.60967 -40.06243 1.000 34.58000  ? 186  VAL B CG1 1 
ATOM   2945 C CG2 . VAL B 2 186 ? -6.54722  -24.67061 -37.77161 1.000 37.04000  ? 186  VAL B CG2 1 
ATOM   2946 N N   . GLU B 2 187 ? -9.63653  -23.89772 -41.22732 1.000 38.66000  ? 187  GLU B N   1 
ATOM   2947 C CA  . GLU B 2 187 ? -10.62593 -24.18958 -42.25363 1.000 46.75000  ? 187  GLU B CA  1 
ATOM   2948 C C   . GLU B 2 187 ? -10.05042 -25.15804 -43.27877 1.000 47.88000  ? 187  GLU B C   1 
ATOM   2949 O O   . GLU B 2 187 ? -8.87655  -25.06281 -43.65300 1.000 43.88000  ? 187  GLU B O   1 
ATOM   2950 C CB  . GLU B 2 187 ? -11.07708 -22.90751 -42.95607 1.000 49.95000  ? 187  GLU B CB  1 
ATOM   2951 C CG  . GLU B 2 187 ? -11.87244 -21.94513 -42.08895 1.000 56.95000  ? 187  GLU B CG  1 
ATOM   2952 C CD  . GLU B 2 187 ? -11.58954 -20.48618 -42.42971 1.000 65.32000  ? 187  GLU B CD  1 
ATOM   2953 O OE1 . GLU B 2 187 ? -11.31908 -19.69556 -41.49547 1.000 73.96000  ? 187  GLU B OE1 1 
ATOM   2954 O OE2 . GLU B 2 187 ? -11.62634 -20.13362 -43.63092 1.000 74.07000  ? 187  GLU B OE2 1 
ATOM   2955 N N   . TRP B 2 188 ? -10.88589 -26.08782 -43.73491 1.000 46.42000  ? 188  TRP B N   1 
ATOM   2956 C CA  . TRP B 2 188 ? -10.50897 -27.02971 -44.78063 1.000 48.90000  ? 188  TRP B CA  1 
ATOM   2957 C C   . TRP B 2 188 ? -11.54315 -26.95973 -45.89201 1.000 48.70000  ? 188  TRP B C   1 
ATOM   2958 O O   . TRP B 2 188 ? -12.72780 -27.22350 -45.65875 1.000 42.80000  ? 188  TRP B O   1 
ATOM   2959 C CB  . TRP B 2 188 ? -10.39726 -28.45628 -44.23619 1.000 49.75000  ? 188  TRP B CB  1 
ATOM   2960 C CG  . TRP B 2 188 ? -9.69414  -29.37992 -45.17638 1.000 51.95000  ? 188  TRP B CG  1 
ATOM   2961 C CD1 . TRP B 2 188 ? -8.34935  -29.46160 -45.39334 1.000 51.08000  ? 188  TRP B CD1 1 
ATOM   2962 C CD2 . TRP B 2 188 ? -10.29946 -30.35065 -46.03454 1.000 50.80000  ? 188  TRP B CD2 1 
ATOM   2963 N NE1 . TRP B 2 188 ? -8.07955  -30.42737 -46.33005 1.000 55.21000  ? 188  TRP B NE1 1 
ATOM   2964 C CE2 . TRP B 2 188 ? -9.26028  -30.98943 -46.73992 1.000 55.96000  ? 188  TRP B CE2 1 
ATOM   2965 C CE3 . TRP B 2 188 ? -11.61833 -30.74716 -46.26995 1.000 54.70000  ? 188  TRP B CE3 1 
ATOM   2966 C CZ2 . TRP B 2 188 ? -9.49970  -32.00295 -47.66683 1.000 59.98000  ? 188  TRP B CZ2 1 
ATOM   2967 C CZ3 . TRP B 2 188 ? -11.85361 -31.75646 -47.18311 1.000 61.05000  ? 188  TRP B CZ3 1 
ATOM   2968 C CH2 . TRP B 2 188 ? -10.80032 -32.36843 -47.87730 1.000 63.50000  ? 188  TRP B CH2 1 
ATOM   2969 N N   . ARG B 2 189 ? -11.09935 -26.58562 -47.08640 1.000 59.03000  ? 189  ARG B N   1 
ATOM   2970 C CA  . ARG B 2 189 ? -11.93596 -26.57085 -48.27965 1.000 67.59000  ? 189  ARG B CA  1 
ATOM   2971 C C   . ARG B 2 189 ? -11.49819 -27.73354 -49.15891 1.000 68.69000  ? 189  ARG B C   1 
ATOM   2972 O O   . ARG B 2 189 ? -10.31034 -27.85317 -49.47937 1.000 64.49000  ? 189  ARG B O   1 
ATOM   2973 C CB  . ARG B 2 189 ? -11.80858 -25.24063 -49.02369 1.000 70.61000  ? 189  ARG B CB  1 
ATOM   2974 N N   . ALA B 2 190 ? -12.43896 -28.59963 -49.52573 1.000 66.76000  ? 190  ALA B N   1 
ATOM   2975 C CA  . ALA B 2 190 ? -12.07667 -29.79230 -50.28699 1.000 68.73000  ? 190  ALA B CA  1 
ATOM   2976 C C   . ALA B 2 190 ? -11.90461 -29.44667 -51.76295 1.000 67.78000  ? 190  ALA B C   1 
ATOM   2977 O O   . ALA B 2 190 ? -10.78618 -29.43282 -52.28030 1.000 63.27000  ? 190  ALA B O   1 
ATOM   2978 C CB  . ALA B 2 190 ? -13.12481 -30.89340 -50.10475 1.000 72.69000  ? 190  ALA B CB  1 
ATOM   2979 N N   . ASP C 3 1   ? 13.48635  -22.33134 -5.63519  1.000 54.18000  ? 1013 ASP C N   1 
ATOM   2980 C CA  . ASP C 3 1   ? 13.24417  -22.73151 -4.25439  1.000 51.05000  ? 1013 ASP C CA  1 
ATOM   2981 C C   . ASP C 3 1   ? 13.29182  -24.24636 -4.10965  1.000 46.90000  ? 1013 ASP C C   1 
ATOM   2982 O O   . ASP C 3 1   ? 12.88103  -24.98411 -5.00661  1.000 41.95000  ? 1013 ASP C O   1 
ATOM   2983 C CB  . ASP C 3 1   ? 11.89576  -22.19609 -3.77645  1.000 61.59000  ? 1013 ASP C CB  1 
ATOM   2984 C CG  . ASP C 3 1   ? 11.75531  -20.70198 -3.99814  1.000 73.82000  ? 1013 ASP C CG  1 
ATOM   2985 O OD1 . ASP C 3 1   ? 12.67534  -20.10306 -4.60036  1.000 79.81000  ? 1013 ASP C OD1 1 
ATOM   2986 O OD2 . ASP C 3 1   ? 10.72348  -20.12910 -3.58271  1.000 84.10000  ? 1013 ASP C OD2 1 
HETATM 2987 C C   . CIR C 3 2   ? 11.95807  -26.63304 -2.35657  1.000 35.03000  ? 1014 CIR C C   1 
HETATM 2988 O O   . CIR C 3 2   ? 10.97102  -26.22984 -1.45440  1.000 34.05000  ? 1014 CIR C O   1 
HETATM 2989 C CA  . CIR C 3 2   ? 13.32947  -25.97224 -2.33359  1.000 40.53000  ? 1014 CIR C CA  1 
HETATM 2990 N N   . CIR C 3 2   ? 13.16768  -24.58926 -2.72833  1.000 41.18000  ? 1014 CIR C N   1 
HETATM 2991 C C3  . CIR C 3 2   ? 13.89784  -25.99212 -0.91707  1.000 45.11000  ? 1014 CIR C C3  1 
HETATM 2992 C C4  . CIR C 3 2   ? 14.01391  -27.42084 -0.39994  1.000 54.70000  ? 1014 CIR C C4  1 
HETATM 2993 C C5  . CIR C 3 2   ? 15.48898  -27.72607 -0.16988  1.000 65.12000  ? 1014 CIR C C5  1 
HETATM 2994 N N6  . CIR C 3 2   ? 15.96050  -28.52281 -1.28560  1.000 83.18000  ? 1014 CIR C N6  1 
HETATM 2995 C C7  . CIR C 3 2   ? 17.30637  -28.32256 -1.82020  1.000 88.24000  ? 1014 CIR C C7  1 
HETATM 2996 O O7  . CIR C 3 2   ? 18.14972  -27.35957 -1.26088  1.000 94.98000  ? 1014 CIR C O7  1 
HETATM 2997 N N8  . CIR C 3 2   ? 17.74718  -29.09449 -2.88730  1.000 84.16000  ? 1014 CIR C N8  1 
ATOM   2998 N N   . TYR C 3 3   ? 11.49197  -27.82782 -2.98668  1.000 30.91000  ? 1015 TYR C N   1 
ATOM   2999 C CA  . TYR C 3 3   ? 10.42286  -28.75003 -2.63409  1.000 31.16000  ? 1015 TYR C CA  1 
ATOM   3000 C C   . TYR C 3 3   ? 10.65137  -29.38542 -1.26216  1.000 33.41000  ? 1015 TYR C C   1 
ATOM   3001 O O   . TYR C 3 3   ? 11.77228  -29.76936 -0.91477  1.000 34.89000  ? 1015 TYR C O   1 
ATOM   3002 C CB  . TYR C 3 3   ? 10.28873  -29.83418 -3.70434  1.000 30.55000  ? 1015 TYR C CB  1 
ATOM   3003 C CG  . TYR C 3 3   ? 9.41581   -29.40825 -4.86017  1.000 32.41000  ? 1015 TYR C CG  1 
ATOM   3004 C CD1 . TYR C 3 3   ? 8.06169   -29.17293 -4.67292  1.000 35.01000  ? 1015 TYR C CD1 1 
ATOM   3005 C CD2 . TYR C 3 3   ? 9.94130   -29.22702 -6.12970  1.000 32.28000  ? 1015 TYR C CD2 1 
ATOM   3006 C CE1 . TYR C 3 3   ? 7.25082   -28.77849 -5.71894  1.000 35.67000  ? 1015 TYR C CE1 1 
ATOM   3007 C CE2 . TYR C 3 3   ? 9.13580   -28.82940 -7.18592  1.000 34.92000  ? 1015 TYR C CE2 1 
ATOM   3008 C CZ  . TYR C 3 3   ? 7.79020   -28.60687 -6.97057  1.000 36.00000  ? 1015 TYR C CZ  1 
ATOM   3009 O OH  . TYR C 3 3   ? 6.97178   -28.20745 -8.00201  1.000 40.29000  ? 1015 TYR C OH  1 
HETATM 3010 C C   . CIR C 3 4   ? 8.61553   -31.49341 0.73517   1.000 35.72000  ? 1016 CIR C C   1 
HETATM 3011 O O   . CIR C 3 4   ? 8.07934   -31.58399 -0.07986  1.000 30.54000  ? 1016 CIR C O   1 
HETATM 3012 C CA  . CIR C 3 4   ? 9.50661   -30.27209 0.98291   1.000 35.70000  ? 1016 CIR C CA  1 
HETATM 3013 N N   . CIR C 3 4   ? 9.66147   -29.50065 -0.23693  1.000 33.27000  ? 1016 CIR C N   1 
HETATM 3014 C C3  . CIR C 3 4   ? 8.84097   -29.39203 2.03081   1.000 40.14000  ? 1016 CIR C C3  1 
HETATM 3015 C C4  . CIR C 3 4   ? 9.75748   -28.22982 2.38844   1.000 48.63000  ? 1016 CIR C C4  1 
HETATM 3016 C C5  . CIR C 3 4   ? 9.21942   -27.59708 3.66571   1.000 56.13000  ? 1016 CIR C C5  1 
HETATM 3017 N N6  . CIR C 3 4   ? 9.35791   -26.15390 3.60145   1.000 64.07000  ? 1016 CIR C N6  1 
HETATM 3018 C C7  . CIR C 3 4   ? 8.69308   -25.22500 4.79058   1.000 68.72000  ? 1016 CIR C C7  1 
HETATM 3019 O O7  . CIR C 3 4   ? 8.80318   -24.01334 4.74973   1.000 64.05000  ? 1016 CIR C O7  1 
HETATM 3020 N N8  . CIR C 3 4   ? 8.01876   -25.81682 5.82386   1.000 63.68000  ? 1016 CIR C N8  1 
ATOM   3021 N N   . LEU C 3 5   ? 9.58816   -32.26724 1.43753   1.000 36.19000  ? 1017 LEU C N   1 
ATOM   3022 C CA  . LEU C 3 5   ? 9.17795   -33.65035 1.64192   1.000 38.97000  ? 1017 LEU C CA  1 
ATOM   3023 C C   . LEU C 3 5   ? 8.16104   -33.78416 2.77638   1.000 35.82000  ? 1017 LEU C C   1 
ATOM   3024 O O   . LEU C 3 5   ? 8.24296   -33.07099 3.77604   1.000 29.12000  ? 1017 LEU C O   1 
ATOM   3025 C CB  . LEU C 3 5   ? 10.40926  -34.51100 1.94572   1.000 46.39000  ? 1017 LEU C CB  1 
ATOM   3026 C CG  . LEU C 3 5   ? 10.21963  -35.98647 2.30287   1.000 51.18000  ? 1017 LEU C CG  1 
ATOM   3027 C CD1 . LEU C 3 5   ? 10.51970  -36.86146 1.10803   1.000 56.65000  ? 1017 LEU C CD1 1 
ATOM   3028 C CD2 . LEU C 3 5   ? 11.09979  -36.37075 3.48109   1.000 55.15000  ? 1017 LEU C CD2 1 
ATOM   3029 N N   . ASN C 3 6   ? 7.20322   -34.69573 2.61595   1.000 31.64000  ? 1018 ASN C N   1 
ATOM   3030 C CA  . ASN C 3 6   ? 6.35032   -35.13934 3.70878   1.000 29.96000  ? 1018 ASN C CA  1 
ATOM   3031 C C   . ASN C 3 6   ? 6.77586   -36.54243 4.12724   1.000 30.40000  ? 1018 ASN C C   1 
ATOM   3032 O O   . ASN C 3 6   ? 6.99632   -37.41377 3.27768   1.000 28.38000  ? 1018 ASN C O   1 
ATOM   3033 C CB  . ASN C 3 6   ? 4.87117   -35.12662 3.31547   1.000 31.46000  ? 1018 ASN C CB  1 
ATOM   3034 C CG  . ASN C 3 6   ? 3.94901   -35.11061 4.52875   1.000 31.24000  ? 1018 ASN C CG  1 
ATOM   3035 O OD1 . ASN C 3 6   ? 3.31155   -36.11162 4.85404   1.000 32.78000  ? 1018 ASN C OD1 1 
ATOM   3036 N ND2 . ASN C 3 6   ? 3.89958   -33.97231 5.22087   1.000 31.50000  ? 1018 ASN C ND2 1 
ATOM   3037 N N   . TYR C 3 7   ? 6.90046   -36.75360 5.43707   1.000 30.92000  ? 1019 TYR C N   1 
ATOM   3038 C CA  . TYR C 3 7   ? 7.47035   -37.98893 5.96045   1.000 36.09000  ? 1019 TYR C CA  1 
ATOM   3039 C C   . TYR C 3 7   ? 6.45476   -39.11960 5.91151   1.000 36.89000  ? 1019 TYR C C   1 
ATOM   3040 O O   . TYR C 3 7   ? 5.30270   -38.95344 6.32449   1.000 42.09000  ? 1019 TYR C O   1 
ATOM   3041 C CB  . TYR C 3 7   ? 7.95630   -37.78996 7.39748   1.000 35.97000  ? 1019 TYR C CB  1 
ATOM   3042 C CG  . TYR C 3 7   ? 9.05120   -36.75968 7.52067   1.000 38.51000  ? 1019 TYR C CG  1 
ATOM   3043 C CD1 . TYR C 3 7   ? 10.34813  -37.04929 7.12806   1.000 41.13000  ? 1019 TYR C CD1 1 
ATOM   3044 C CD2 . TYR C 3 7   ? 8.78200   -35.48683 8.00911   1.000 46.40000  ? 1019 TYR C CD2 1 
ATOM   3045 C CE1 . TYR C 3 7   ? 11.35341  -36.10887 7.22744   1.000 44.26000  ? 1019 TYR C CE1 1 
ATOM   3046 C CE2 . TYR C 3 7   ? 9.78210   -34.53433 8.11170   1.000 47.86000  ? 1019 TYR C CE2 1 
ATOM   3047 C CZ  . TYR C 3 7   ? 11.06702  -34.85423 7.71821   1.000 48.40000  ? 1019 TYR C CZ  1 
ATOM   3048 O OH  . TYR C 3 7   ? 12.07123  -33.91903 7.81846   1.000 51.80000  ? 1019 TYR C OH  1 
ATOM   3049 N N   . SER C 3 8   ? 6.88808   -40.26940 5.40427   1.000 34.98000  ? 1020 SER C N   1 
ATOM   3050 C CA  . SER C 3 8   ? 6.10680   -41.49219 5.51019   1.000 35.86000  ? 1020 SER C CA  1 
ATOM   3051 C C   . SER C 3 8   ? 6.34542   -42.10500 6.88420   1.000 36.81000  ? 1020 SER C C   1 
ATOM   3052 O O   . SER C 3 8   ? 7.49302   -42.31812 7.28742   1.000 35.81000  ? 1020 SER C O   1 
ATOM   3053 C CB  . SER C 3 8   ? 6.49058   -42.46899 4.40056   1.000 34.14000  ? 1020 SER C CB  1 
ATOM   3054 O OG  . SER C 3 8   ? 6.20628   -41.92216 3.12389   1.000 30.64000  ? 1020 SER C OG  1 
ATOM   3055 N N   . LEU C 3 9   ? 5.27857   -42.36959 7.60029   1.000 35.31000  ? 1021 LEU C N   1 
ATOM   3056 C CA  . LEU C 3 9   ? 5.44885   -42.70270 9.01142   1.000 34.17000  ? 1021 LEU C CA  1 
ATOM   3057 C C   . LEU C 3 9   ? 5.74853   -44.18792 9.18242   1.000 34.15000  ? 1021 LEU C C   1 
ATOM   3058 O O   . LEU C 3 9   ? 5.06082   -45.02720 8.58421   1.000 34.00000  ? 1021 LEU C O   1 
ATOM   3059 C CB  . LEU C 3 9   ? 4.20171   -42.33858 9.79842   1.000 32.32000  ? 1021 LEU C CB  1 
ATOM   3060 C CG  . LEU C 3 9   ? 3.81061   -40.86120 9.76081   1.000 35.16000  ? 1021 LEU C CG  1 
ATOM   3061 C CD1 . LEU C 3 9   ? 2.66629   -40.59751 10.71766  1.000 37.93000  ? 1021 LEU C CD1 1 
ATOM   3062 C CD2 . LEU C 3 9   ? 5.00068   -39.96641 10.07892  1.000 36.34000  ? 1021 LEU C CD2 1 
ATOM   3063 N N   . PRO C 3 10  ? 6.75730   -44.54385 9.97767   1.000 35.70000  ? 1022 PRO C N   1 
ATOM   3064 C CA  . PRO C 3 10  ? 6.97262   -45.95766 10.30251  1.000 38.61000  ? 1022 PRO C CA  1 
ATOM   3065 C C   . PRO C 3 10  ? 5.91609   -46.44828 11.27815  1.000 37.51000  ? 1022 PRO C C   1 
ATOM   3066 O O   . PRO C 3 10  ? 5.52729   -45.73688 12.20664  1.000 41.41000  ? 1022 PRO C O   1 
ATOM   3067 C CB  . PRO C 3 10  ? 8.36609   -45.96341 10.94018  1.000 36.24000  ? 1022 PRO C CB  1 
ATOM   3068 C CG  . PRO C 3 10  ? 8.48124   -44.60762 11.56204  1.000 36.20000  ? 1022 PRO C CG  1 
ATOM   3069 C CD  . PRO C 3 10  ? 7.73883   -43.66586 10.64303  1.000 36.53000  ? 1022 PRO C CD  1 
ATOM   3070 N N   . THR C 3 11  ? 5.44850   -47.67007 11.06326  1.000 40.19000  ? 1023 THR C N   1 
ATOM   3071 C CA  . THR C 3 11  ? 4.46544   -48.25279 11.96679  1.000 54.93000  ? 1023 THR C CA  1 
ATOM   3072 C C   . THR C 3 11  ? 5.10859   -48.85876 13.20733  1.000 52.48000  ? 1023 THR C C   1 
ATOM   3073 O O   . THR C 3 11  ? 6.31493   -48.74452 13.40623  1.000 58.21000  ? 1023 THR C O   1 
ATOM   3074 C CB  . THR C 3 11  ? 3.63738   -49.32711 11.27175  1.000 64.22000  ? 1023 THR C CB  1 
ATOM   3075 O OG1 . THR C 3 11  ? 2.48307   -49.62058 12.06962  1.000 74.92000  ? 1023 THR C OG1 1 
ATOM   3076 C CG2 . THR C 3 11  ? 4.45251   -50.57744 11.07932  1.000 71.28000  ? 1023 THR C CG2 1 
HETATM 3077 C C1  . NAG D 4 .   ? 12.75531  -58.40191 -21.45642 1.000 86.06000  ? 201  NAG A C1  1 
HETATM 3078 C C2  . NAG D 4 .   ? 13.81835  -59.14565 -20.65528 1.000 94.60000  ? 201  NAG A C2  1 
HETATM 3079 C C3  . NAG D 4 .   ? 15.08728  -59.30027 -21.48767 1.000 99.20000  ? 201  NAG A C3  1 
HETATM 3080 C C4  . NAG D 4 .   ? 14.76573  -59.98285 -22.81057 1.000 100.79000 ? 201  NAG A C4  1 
HETATM 3081 C C5  . NAG D 4 .   ? 13.65747  -59.22679 -23.53930 1.000 99.27000  ? 201  NAG A C5  1 
HETATM 3082 C C6  . NAG D 4 .   ? 13.19161  -59.93153 -24.79182 1.000 98.00000  ? 201  NAG A C6  1 
HETATM 3083 C C7  . NAG D 4 .   ? 13.37944  -58.64770 -18.29546 1.000 99.74000  ? 201  NAG A C7  1 
HETATM 3084 C C8  . NAG D 4 .   ? 13.81078  -57.86594 -17.09087 1.000 101.67000 ? 201  NAG A C8  1 
HETATM 3085 N N2  . NAG D 4 .   ? 14.10428  -58.46435 -19.40358 1.000 96.81000  ? 201  NAG A N2  1 
HETATM 3086 O O3  . NAG D 4 .   ? 16.04656  -60.06347 -20.76461 1.000 97.56000  ? 201  NAG A O3  1 
HETATM 3087 O O4  . NAG D 4 .   ? 15.92505  -60.03039 -23.63461 1.000 106.37000 ? 201  NAG A O4  1 
HETATM 3088 O O5  . NAG D 4 .   ? 12.50703  -59.09652 -22.68986 1.000 91.79000  ? 201  NAG A O5  1 
HETATM 3089 O O6  . NAG D 4 .   ? 12.34504  -59.09911 -25.57226 1.000 92.73000  ? 201  NAG A O6  1 
HETATM 3090 O O7  . NAG D 4 .   ? 12.41523  -59.40787 -18.26825 1.000 90.35000  ? 201  NAG A O7  1 
HETATM 3091 C C1  . GOL E 5 .   ? -7.27048  -45.87627 -32.32486 1.000 75.51000  ? 202  GOL A C1  1 
HETATM 3092 O O1  . GOL E 5 .   ? -6.46835  -44.74829 -32.47136 1.000 78.98000  ? 202  GOL A O1  1 
HETATM 3093 C C2  . GOL E 5 .   ? -6.74996  -46.94697 -33.31835 1.000 73.11000  ? 202  GOL A C2  1 
HETATM 3094 O O2  . GOL E 5 .   ? -7.32317  -48.18422 -33.08351 1.000 69.44000  ? 202  GOL A O2  1 
HETATM 3095 C C3  . GOL E 5 .   ? -7.08992  -46.40366 -34.73337 1.000 72.92000  ? 202  GOL A C3  1 
HETATM 3096 O O3  . GOL E 5 .   ? -8.47784  -46.22999 -34.78821 1.000 69.84000  ? 202  GOL A O3  1 
HETATM 3097 C C1  . NAG F 4 .   ? -10.30109 -16.67189 -3.94397  1.000 62.12000  ? 201  NAG B C1  1 
HETATM 3098 C C2  . NAG F 4 .   ? -11.61021 -16.12905 -3.33407  1.000 69.14000  ? 201  NAG B C2  1 
HETATM 3099 C C3  . NAG F 4 .   ? -11.59663 -14.59678 -3.27429  1.000 72.12000  ? 201  NAG B C3  1 
HETATM 3100 C C4  . NAG F 4 .   ? -10.31770 -14.07871 -2.63035  1.000 73.92000  ? 201  NAG B C4  1 
HETATM 3101 C C5  . NAG F 4 .   ? -9.11510  -14.66692 -3.35615  1.000 74.56000  ? 201  NAG B C5  1 
HETATM 3102 C C6  . NAG F 4 .   ? -7.78853  -14.22966 -2.77854  1.000 72.74000  ? 201  NAG B C6  1 
HETATM 3103 C C7  . NAG F 4 .   ? -13.45839 -17.68667 -3.80239  1.000 66.49000  ? 201  NAG B C7  1 
HETATM 3104 C C8  . NAG F 4 .   ? -14.60239 -18.00226 -4.71875  1.000 74.04000  ? 201  NAG B C8  1 
HETATM 3105 N N2  . NAG F 4 .   ? -12.75611 -16.58985 -4.10219  1.000 68.98000  ? 201  NAG B N2  1 
HETATM 3106 O O3  . NAG F 4 .   ? -12.72529 -14.14916 -2.53172  1.000 71.83000  ? 201  NAG B O3  1 
HETATM 3107 O O4  . NAG F 4 .   ? -10.27389 -12.65647 -2.69571  1.000 72.79000  ? 201  NAG B O4  1 
HETATM 3108 O O5  . NAG F 4 .   ? -9.16890  -16.09746 -3.26290  1.000 66.55000  ? 201  NAG B O5  1 
HETATM 3109 O O6  . NAG F 4 .   ? -7.58934  -14.74834 -1.47102  1.000 68.17000  ? 201  NAG B O6  1 
HETATM 3110 O O7  . NAG F 4 .   ? -13.18412 -18.39130 -2.83721  1.000 79.90000  ? 201  NAG B O7  1 
HETATM 3111 C C1  . GOL G 5 .   ? -10.67157 -46.89347 -31.43976 1.000 72.84000  ? 202  GOL B C1  1 
HETATM 3112 O O1  . GOL G 5 .   ? -10.11087 -45.80713 -30.77191 1.000 71.97000  ? 202  GOL B O1  1 
HETATM 3113 C C2  . GOL G 5 .   ? -10.27395 -48.15410 -30.64381 1.000 75.26000  ? 202  GOL B C2  1 
HETATM 3114 O O2  . GOL G 5 .   ? -10.67150 -48.07194 -29.31638 1.000 67.58000  ? 202  GOL B O2  1 
HETATM 3115 C C3  . GOL G 5 .   ? -10.95052 -49.32838 -31.39036 1.000 77.24000  ? 202  GOL B C3  1 
HETATM 3116 O O3  . GOL G 5 .   ? -10.42223 -49.34585 -32.67867 1.000 77.08000  ? 202  GOL B O3  1 
HETATM 3117 C C1  . GOL H 5 .   ? -9.59111  -49.81543 -0.08449  1.000 66.53000  ? 203  GOL B C1  1 
HETATM 3118 O O1  . GOL H 5 .   ? -9.80249  -48.67322 0.68681   1.000 63.08000  ? 203  GOL B O1  1 
HETATM 3119 C C2  . GOL H 5 .   ? -10.98153 -50.41291 -0.36494  1.000 67.11000  ? 203  GOL B C2  1 
HETATM 3120 O O2  . GOL H 5 .   ? -11.85075 -50.23237 0.70638   1.000 75.57000  ? 203  GOL B O2  1 
HETATM 3121 C C3  . GOL H 5 .   ? -11.46983 -49.69954 -1.63898  1.000 64.92000  ? 203  GOL B C3  1 
HETATM 3122 O O3  . GOL H 5 .   ? -12.74641 -50.19574 -1.90752  1.000 56.30000  ? 203  GOL B O3  1 
HETATM 3123 O O   . HOH I 6 .   ? -4.88689  -63.54161 10.36291  1.000 30.00000  ? 301  HOH A O   1 
HETATM 3124 O O   . HOH I 6 .   ? 11.85348  -37.56390 -33.33478 1.000 33.32000  ? 302  HOH A O   1 
HETATM 3125 O O   . HOH I 6 .   ? 10.05785  -40.61924 -15.47194 1.000 32.30000  ? 303  HOH A O   1 
HETATM 3126 O O   . HOH I 6 .   ? 1.08732   -33.97999 -29.02024 1.000 33.54000  ? 304  HOH A O   1 
HETATM 3127 O O   . HOH I 6 .   ? -3.07565  -28.95375 -14.78791 1.000 36.43000  ? 305  HOH A O   1 
HETATM 3128 O O   . HOH I 6 .   ? 13.22786  -57.51538 0.51374   1.000 30.00000  ? 306  HOH A O   1 
HETATM 3129 O O   . HOH I 6 .   ? 1.67778   -35.24987 -20.42758 1.000 21.95000  ? 307  HOH A O   1 
HETATM 3130 O O   . HOH I 6 .   ? 13.95468  -44.30892 -37.69630 1.000 53.53000  ? 308  HOH A O   1 
HETATM 3131 O O   . HOH I 6 .   ? -7.46052  -43.29158 -34.54758 1.000 56.13000  ? 309  HOH A O   1 
HETATM 3132 O O   . HOH I 6 .   ? -0.81500  -45.85630 -7.91421  1.000 28.29000  ? 310  HOH A O   1 
HETATM 3133 O O   . HOH I 6 .   ? 2.87245   -60.68963 -9.10363  1.000 37.27000  ? 311  HOH A O   1 
HETATM 3134 O O   . HOH I 6 .   ? 5.21696   -58.08503 -14.69475 1.000 30.00000  ? 312  HOH A O   1 
HETATM 3135 O O   . HOH I 6 .   ? 1.61992   -61.52715 -6.95041  1.000 28.54000  ? 313  HOH A O   1 
HETATM 3136 O O   . HOH I 6 .   ? 11.60184  -43.16719 -8.13725  1.000 31.21000  ? 314  HOH A O   1 
HETATM 3137 O O   . HOH I 6 .   ? 4.47135   -36.62752 -16.76553 1.000 35.61000  ? 315  HOH A O   1 
HETATM 3138 O O   . HOH I 6 .   ? -5.00060  -33.42747 -15.55957 1.000 30.00000  ? 316  HOH A O   1 
HETATM 3139 O O   . HOH I 6 .   ? 2.77891   -63.66282 -17.54082 1.000 30.00000  ? 317  HOH A O   1 
HETATM 3140 O O   . HOH I 6 .   ? 2.45384   -44.90637 -5.25149  1.000 30.00000  ? 318  HOH A O   1 
HETATM 3141 O O   . HOH I 6 .   ? 26.457    -36.478   -10.583   1.000 59.22000  ? 319  HOH A O   1 
HETATM 3142 O O   . HOH I 6 .   ? 6.21062   -36.71762 -38.83309 1.000 33.65000  ? 320  HOH A O   1 
HETATM 3143 O O   . HOH I 6 .   ? 16.14939  -50.95215 -1.16599  1.000 38.12000  ? 321  HOH A O   1 
HETATM 3144 O O   . HOH I 6 .   ? 17.09168  -34.13896 -13.91705 1.000 40.50000  ? 322  HOH A O   1 
HETATM 3145 O O   . HOH I 6 .   ? -1.12411  -54.26071 -42.53891 1.000 49.62000  ? 323  HOH A O   1 
HETATM 3146 O O   . HOH I 6 .   ? 8.33593   -23.38215 -20.30940 1.000 30.00000  ? 324  HOH A O   1 
HETATM 3147 O O   . HOH I 6 .   ? 10.95875  -46.34331 -10.26352 1.000 30.00000  ? 325  HOH A O   1 
HETATM 3148 O O   . HOH I 6 .   ? 14.41151  -42.70164 -20.12185 1.000 44.79000  ? 326  HOH A O   1 
HETATM 3149 O O   . HOH I 6 .   ? 14.31897  -50.52560 5.71509   1.000 30.00000  ? 327  HOH A O   1 
HETATM 3150 O O   . HOH I 6 .   ? -0.36670  -35.72051 -41.53589 1.000 30.00000  ? 328  HOH A O   1 
HETATM 3151 O O   . HOH I 6 .   ? 20.07696  -34.89976 -6.73853  1.000 32.79000  ? 329  HOH A O   1 
HETATM 3152 O O   . HOH I 6 .   ? -5.40481  -56.37866 -21.28981 1.000 30.00000  ? 330  HOH A O   1 
HETATM 3153 O O   . HOH I 6 .   ? 13.56718  -30.96689 -20.92260 1.000 31.80000  ? 331  HOH A O   1 
HETATM 3154 O O   . HOH I 6 .   ? -4.86893  -53.09874 -24.93020 1.000 47.81000  ? 332  HOH A O   1 
HETATM 3155 O O   . HOH I 6 .   ? 9.38146   -37.44467 -23.54577 1.000 30.00000  ? 333  HOH A O   1 
HETATM 3156 O O   . HOH I 6 .   ? -5.90933  -22.11432 -11.43571 1.000 30.00000  ? 334  HOH A O   1 
HETATM 3157 O O   . HOH I 6 .   ? 17.82374  -30.65642 -6.85299  1.000 37.07000  ? 335  HOH A O   1 
HETATM 3158 O O   . HOH I 6 .   ? 12.15683  -52.79875 -20.42856 1.000 30.00000  ? 336  HOH A O   1 
HETATM 3159 O O   . HOH I 6 .   ? 13.14075  -28.61694 -20.45993 1.000 28.11000  ? 337  HOH A O   1 
HETATM 3160 O O   . HOH I 6 .   ? -4.796    -62.125   -14.978   1.000 30.00000  ? 338  HOH A O   1 
HETATM 3161 O O   . HOH I 6 .   ? 19.89620  -34.63523 -0.49428  1.000 30.00000  ? 339  HOH A O   1 
HETATM 3162 O O   . HOH I 6 .   ? 9.96899   -52.73155 -14.61572 1.000 37.99000  ? 340  HOH A O   1 
HETATM 3163 O O   . HOH I 6 .   ? -5.34995  -22.86651 -13.46756 1.000 30.00000  ? 341  HOH A O   1 
HETATM 3164 O O   . HOH I 6 .   ? -4.80124  -57.09102 -4.63843  1.000 46.98000  ? 342  HOH A O   1 
HETATM 3165 O O   . HOH I 6 .   ? 15.40497  -53.86749 -8.80689  1.000 45.50000  ? 343  HOH A O   1 
HETATM 3166 O O   . HOH I 6 .   ? 3.36957   -64.18827 -19.59093 1.000 30.00000  ? 344  HOH A O   1 
HETATM 3167 O O   . HOH I 6 .   ? 13.87417  -49.11393 -8.73150  1.000 45.04000  ? 345  HOH A O   1 
HETATM 3168 O O   . HOH I 6 .   ? -7.092    -65.499   -18.207   1.000 30.00000  ? 346  HOH A O   1 
HETATM 3169 O O   . HOH I 6 .   ? 14.80659  -45.11476 -10.45644 1.000 30.00000  ? 347  HOH A O   1 
HETATM 3170 O O   . HOH I 6 .   ? 9.16664   -59.73805 -16.49349 1.000 30.00000  ? 348  HOH A O   1 
HETATM 3171 O O   . HOH I 6 .   ? 3.55320   -31.23581 -31.29038 1.000 30.00000  ? 349  HOH A O   1 
HETATM 3172 O O   . HOH I 6 .   ? -7.92450  -42.57481 -13.13652 1.000 51.47000  ? 350  HOH A O   1 
HETATM 3173 O O   . HOH I 6 .   ? 7.12920   -60.09593 -17.30146 1.000 30.00000  ? 351  HOH A O   1 
HETATM 3174 O O   . HOH I 6 .   ? 12.57063  -39.02107 -16.56271 1.000 30.00000  ? 352  HOH A O   1 
HETATM 3175 O O   . HOH I 6 .   ? 16.29089  -49.52664 1.15976   1.000 30.00000  ? 353  HOH A O   1 
HETATM 3176 O O   . HOH I 6 .   ? 0.85522   -57.92794 -46.46691 1.000 53.64000  ? 354  HOH A O   1 
HETATM 3177 O O   . HOH J 6 .   ? -7.68843  -29.16097 5.78528   1.000 50.79000  ? 301  HOH B O   1 
HETATM 3178 O O   . HOH J 6 .   ? -0.55944  -31.94459 -15.47822 1.000 39.57000  ? 302  HOH B O   1 
HETATM 3179 O O   . HOH J 6 .   ? 10.49920  -21.85849 -7.00139  1.000 30.00000  ? 303  HOH B O   1 
HETATM 3180 O O   . HOH J 6 .   ? -23.283   -25.541   -44.252   1.000 53.48000  ? 304  HOH B O   1 
HETATM 3181 O O   . HOH J 6 .   ? -1.31706  -30.74273 -34.98625 1.000 28.51000  ? 305  HOH B O   1 
HETATM 3182 O O   . HOH J 6 .   ? 8.80023   -35.43197 -25.31369 1.000 30.00000  ? 306  HOH B O   1 
HETATM 3183 O O   . HOH J 6 .   ? -25.234   -30.799   -51.587   1.000 30.00000  ? 307  HOH B O   1 
HETATM 3184 O O   . HOH J 6 .   ? -9.585    -11.765   -27.598   1.000 34.12000  ? 308  HOH B O   1 
HETATM 3185 O O   . HOH J 6 .   ? 2.10766   -33.44212 -2.06342  1.000 29.66000  ? 309  HOH B O   1 
HETATM 3186 O O   . HOH J 6 .   ? 7.92835   -68.46733 -12.38697 1.000 30.00000  ? 310  HOH B O   1 
HETATM 3187 O O   . HOH J 6 .   ? -15.351   -53.259   15.216    1.000 30.00000  ? 311  HOH B O   1 
HETATM 3188 O O   . HOH J 6 .   ? -10.10143 -33.60481 -1.78635  1.000 49.57000  ? 312  HOH B O   1 
HETATM 3189 O O   . HOH J 6 .   ? -5.49792  -24.64249 5.59287   1.000 50.24000  ? 313  HOH B O   1 
HETATM 3190 O O   . HOH J 6 .   ? 6.34624   -25.49028 -17.51189 1.000 40.43000  ? 314  HOH B O   1 
HETATM 3191 O O   . HOH J 6 .   ? -4.87912  -16.36754 -28.29737 1.000 36.20000  ? 315  HOH B O   1 
HETATM 3192 O O   . HOH J 6 .   ? 3.22941   -30.67697 -1.78675  1.000 40.23000  ? 316  HOH B O   1 
HETATM 3193 O O   . HOH J 6 .   ? 2.81207   -25.89111 -28.81381 1.000 30.00000  ? 317  HOH B O   1 
HETATM 3194 O O   . HOH J 6 .   ? 4.15937   -28.11015 -27.64165 1.000 38.55000  ? 318  HOH B O   1 
HETATM 3195 O O   . HOH J 6 .   ? 7.15083   -29.31926 -23.02495 1.000 30.00000  ? 319  HOH B O   1 
HETATM 3196 O O   . HOH J 6 .   ? -4.37125  -18.22458 -3.19249  1.000 30.00000  ? 320  HOH B O   1 
HETATM 3197 O O   . HOH J 6 .   ? 7.92724   -31.57250 -23.04861 1.000 30.00000  ? 321  HOH B O   1 
HETATM 3198 O O   . HOH J 6 .   ? -12.85871 -33.92309 -27.80205 1.000 30.00000  ? 322  HOH B O   1 
HETATM 3199 O O   . HOH J 6 .   ? -2.09169  -24.29843 -34.89452 1.000 45.62000  ? 323  HOH B O   1 
HETATM 3200 O O   . HOH J 6 .   ? -14.286   -36.454   -26.649   1.000 30.00000  ? 324  HOH B O   1 
HETATM 3201 O O   . HOH J 6 .   ? -13.648   -48.592   2.654     1.000 52.53000  ? 325  HOH B O   1 
HETATM 3202 O O   . HOH J 6 .   ? -3.76336  -27.82402 -41.37192 1.000 36.52000  ? 326  HOH B O   1 
HETATM 3203 O O   . HOH J 6 .   ? -17.051   -20.782   -36.459   1.000 30.00000  ? 327  HOH B O   1 
HETATM 3204 O O   . HOH J 6 .   ? -9.60688  -45.42711 13.21270  1.000 44.45000  ? 328  HOH B O   1 
HETATM 3205 O O   . HOH J 6 .   ? 2.02452   -20.03950 -1.18916  1.000 30.00000  ? 329  HOH B O   1 
HETATM 3206 O O   . HOH J 6 .   ? 1.60118   -17.73210 -18.58399 1.000 46.52000  ? 330  HOH B O   1 
HETATM 3207 O O   . HOH J 6 .   ? -11.45169 -24.14348 -22.86144 1.000 30.00000  ? 331  HOH B O   1 
HETATM 3208 O O   . HOH J 6 .   ? -11.61090 -41.15152 -50.81757 1.000 30.00000  ? 332  HOH B O   1 
HETATM 3209 O O   . HOH J 6 .   ? -7.42559  -39.74210 -48.36084 1.000 30.00000  ? 333  HOH B O   1 
HETATM 3210 O O   . HOH J 6 .   ? -3.94029  -31.30043 -16.82031 1.000 41.34000  ? 334  HOH B O   1 
HETATM 3211 O O   . HOH J 6 .   ? -11.45973 -33.82226 -26.18358 1.000 30.00000  ? 335  HOH B O   1 
HETATM 3212 O O   . HOH J 6 .   ? 1.594     -42.563   24.380    1.000 30.00000  ? 336  HOH B O   1 
HETATM 3213 O O   . HOH J 6 .   ? 7.29584   -65.67371 -16.33440 1.000 30.00000  ? 337  HOH B O   1 
HETATM 3214 O O   . HOH J 6 .   ? 4.51798   -37.74344 22.02501  1.000 30.00000  ? 338  HOH B O   1 
HETATM 3215 O O   . HOH J 6 .   ? 5.32141   -70.08859 -8.72699  1.000 51.48000  ? 339  HOH B O   1 
HETATM 3216 O O   . HOH J 6 .   ? 5.61208   -69.33802 -6.54702  1.000 48.24000  ? 340  HOH B O   1 
HETATM 3217 O O   . HOH J 6 .   ? -6.09733  -31.80971 -17.15430 1.000 30.00000  ? 341  HOH B O   1 
HETATM 3218 O O   . HOH J 6 .   ? -4.28792  -16.35788 -20.47523 1.000 53.64000  ? 342  HOH B O   1 
HETATM 3219 O O   . HOH J 6 .   ? 1.307     -16.608   -23.186   1.000 30.00000  ? 343  HOH B O   1 
HETATM 3220 O O   . HOH J 6 .   ? 9.82853   -37.50532 11.43279  1.000 55.96000  ? 344  HOH B O   1 
HETATM 3221 O O   . HOH J 6 .   ? -6.02947  -53.87625 16.38276  1.000 30.00000  ? 345  HOH B O   1 
HETATM 3222 O O   . HOH J 6 .   ? -0.36429  -25.72358 13.10588  1.000 30.00000  ? 346  HOH B O   1 
HETATM 3223 O O   . HOH J 6 .   ? 9.66540   -37.44304 -26.00601 1.000 30.00000  ? 347  HOH B O   1 
HETATM 3224 O O   . HOH J 6 .   ? -11.66134 -53.95898 -27.75499 1.000 30.00000  ? 348  HOH B O   1 
HETATM 3225 O O   . HOH J 6 .   ? -15.04693 -50.01942 -39.02633 1.000 50.76000  ? 349  HOH B O   1 
HETATM 3226 O O   . HOH K 6 .   ? 9.46827   -41.26257 8.60564   1.000 30.00000  ? 1101 HOH C O   1 
HETATM 3227 O O   . HOH K 6 .   ? 14.06458  -31.26558 -0.08261  1.000 36.35000  ? 1102 HOH C O   1 
HETATM 3228 O O   . HOH K 6 .   ? 12.59040  -22.77195 -0.56092  1.000 30.00000  ? 1103 HOH C O   1 
HETATM 3229 O O   . HOH K 6 .   ? 11.99718  -31.63433 3.17956   1.000 38.07000  ? 1104 HOH C O   1 
HETATM 3230 O O   . HOH K 6 .   ? 6.17968   -43.59256 14.38957  1.000 30.00000  ? 1105 HOH C O   1 
HETATM 3231 O O   . HOH K 6 .   ? 5.53025   -34.99666 7.80474   1.000 30.00000  ? 1106 HOH C O   1 
HETATM 3232 O O   . HOH K 6 .   ? 21.63199  -23.61009 -0.91640  1.000 30.00000  ? 1107 HOH C O   1 
# 
