data_1N18
# 
_entry.id   1N18 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_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   1N18         pdb_00001n18 10.2210/pdb1n18/pdb 
RCSB  RCSB017391   ?            ?                   
WWPDB D_1000017391 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1M19 
_pdbx_database_related.details        'Structure of the HSOD A4V mutant' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1N18 
_pdbx_database_status.recvd_initial_deposition_date   2002-10-16 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Cardoso, R.M.F.' 1 
'Thayer, M.M.'    2 
'DiDonato, M.'    3 
'Lo, T.P.'        4 
'Bruns, C.K.'     5 
'Getzoff, E.D.'   6 
'Tainer, J.A.'    7 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 
;Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase.
;
J.Mol.Biol.            324 247  256  2002 JMOBAK UK 0022-2836 0070 ? 12441104 '10.1016/S0022-2836(02)01090-2' 
1       'Atomic Structures of Wild-Type and Thermostable mutant recombinant human Cu,Zn superoxide dismutase' 
Proc.Natl.Acad.Sci.USA 89  6109 6113 1992 PNASA6 US 0027-8424 0040 ? ?        ?                               
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cardoso, R.M.F.' 1  ? 
primary 'Thayer, M.M.'    2  ? 
primary 'DiDonato, M.'    3  ? 
primary 'Lo, T.P.'        4  ? 
primary 'Bruns, C.K.'     5  ? 
primary 'Getzoff, E.D.'   6  ? 
primary 'Tainer, J.A.'    7  ? 
1       'Parge, H.E.'     8  ? 
1       'Hallewell, R.A.' 9  ? 
1       'Tainer, J.A.'    10 ? 
# 
_cell.entry_id           1N18 
_cell.length_a           203.200 
_cell.length_b           165.200 
_cell.length_c           144.300 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              80 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1N18 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
# 
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 'Superoxide dismutase [Cu-Zn]' 15910.628 10   1.15.1.1 'C6A, C111S' ? ? 
2 non-polymer syn 'COPPER (I) ION'               63.546    10   ?        ?            ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    10   ?        ?            ? ? 
4 non-polymer syn 'SULFATE ION'                  96.063    1    ?        ?            ? ? 
5 water       nat water                          18.015    1389 ?        ?            ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   ALA n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 SER n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           0 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
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 1N18 A 1 ? 154 ? P00441 0 ? 153 ? 0 153 
2  1 1N18 B 1 ? 154 ? P00441 0 ? 153 ? 0 153 
3  1 1N18 C 1 ? 154 ? P00441 0 ? 153 ? 0 153 
4  1 1N18 D 1 ? 154 ? P00441 0 ? 153 ? 0 153 
5  1 1N18 E 1 ? 154 ? P00441 0 ? 153 ? 0 153 
6  1 1N18 F 1 ? 154 ? P00441 0 ? 153 ? 0 153 
7  1 1N18 G 1 ? 154 ? P00441 0 ? 153 ? 0 153 
8  1 1N18 H 1 ? 154 ? P00441 0 ? 153 ? 0 153 
9  1 1N18 I 1 ? 154 ? P00441 0 ? 153 ? 0 153 
10 1 1N18 J 1 ? 154 ? P00441 0 ? 153 ? 0 153 
# 
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  1N18 ALA A 7   ? UNP P00441 CYS 6   'engineered mutation' 6   1  
1  1N18 SER A 112 ? UNP P00441 CYS 111 'engineered mutation' 111 2  
2  1N18 ALA B 7   ? UNP P00441 CYS 6   'engineered mutation' 6   3  
2  1N18 SER B 112 ? UNP P00441 CYS 111 'engineered mutation' 111 4  
3  1N18 ALA C 7   ? UNP P00441 CYS 6   'engineered mutation' 6   5  
3  1N18 SER C 112 ? UNP P00441 CYS 111 'engineered mutation' 111 6  
4  1N18 ALA D 7   ? UNP P00441 CYS 6   'engineered mutation' 6   7  
4  1N18 SER D 112 ? UNP P00441 CYS 111 'engineered mutation' 111 8  
5  1N18 ALA E 7   ? UNP P00441 CYS 6   'engineered mutation' 6   9  
5  1N18 SER E 112 ? UNP P00441 CYS 111 'engineered mutation' 111 10 
6  1N18 ALA F 7   ? UNP P00441 CYS 6   'engineered mutation' 6   11 
6  1N18 SER F 112 ? UNP P00441 CYS 111 'engineered mutation' 111 12 
7  1N18 ALA G 7   ? UNP P00441 CYS 6   'engineered mutation' 6   13 
7  1N18 SER G 112 ? UNP P00441 CYS 111 'engineered mutation' 111 14 
8  1N18 ALA H 7   ? UNP P00441 CYS 6   'engineered mutation' 6   15 
8  1N18 SER H 112 ? UNP P00441 CYS 111 'engineered mutation' 111 16 
9  1N18 ALA I 7   ? UNP P00441 CYS 6   'engineered mutation' 6   17 
9  1N18 SER I 112 ? UNP P00441 CYS 111 'engineered mutation' 111 18 
10 1N18 ALA J 7   ? UNP P00441 CYS 6   'engineered mutation' 6   19 
10 1N18 SER J 112 ? UNP P00441 CYS 111 'engineered mutation' 111 20 
# 
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 
CU1 non-polymer         . 'COPPER (I) ION' ? 'Cu 1'           63.546  
CYS 'L-peptide linking' y CYSTEINE         ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE        ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'  ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE          ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE        ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER            ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE       ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE          ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE           ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE       ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE    ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE          ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE           ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'    ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE        ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN       ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE           ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'       ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1N18 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.80 
_exptl_crystal.density_percent_sol   67.67 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    'Ammonium Sulfate, NaCl, Tris, EDTA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           90 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1996-02-25 
_diffrn_detector.details                monochromator 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si (111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.08 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL7-1' 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL7-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.08 
# 
_reflns.entry_id                     1N18 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             20.0 
_reflns.d_resolution_high            2.0 
_reflns.number_obs                   162732 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.2 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.069 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        19.7 
_reflns.pdbx_redundancy              6.2 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.00 
_reflns_shell.d_res_low              2.07 
_reflns_shell.percent_possible_all   99.7 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.416 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1N18 
_refine.ls_number_reflns_obs                     161466 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             19.86 
_refine.ls_d_res_high                            2.00 
_refine.ls_percent_reflns_obs                    99.2 
_refine.ls_R_factor_obs                          0.218 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.218 
_refine.ls_R_factor_R_free                       0.25 
_refine.ls_R_factor_R_free_error                 0.003 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  8091 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               35.4 
_refine.aniso_B[1][1]                            0.47 
_refine.aniso_B[2][2]                            5.25 
_refine.aniso_B[3][3]                            -5.73 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.347926 
_refine.solvent_model_param_bsol                 51.8641 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1N18 
_refine_analyze.Luzzati_coordinate_error_obs    0.26 
_refine_analyze.Luzzati_sigma_a_obs             0.23 
_refine_analyze.Luzzati_d_res_low_obs           5 
_refine_analyze.Luzzati_coordinate_error_free   0.29 
_refine_analyze.Luzzati_sigma_a_free            0.25 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11090 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             1389 
_refine_hist.number_atoms_total               12504 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        19.86 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.005 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.3   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      24.9  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.68  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.39  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            2.16  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             2.08  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            3.14  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.00 
_refine_ls_shell.d_res_low                        2.13 
_refine_ls_shell.number_reflns_R_work             25418 
_refine_ls_shell.R_factor_R_work                  0.275 
_refine_ls_shell.percent_reflns_obs               99.3 
_refine_ls_shell.R_factor_R_free                  0.305 
_refine_ls_shell.R_factor_R_free_error            0.008 
_refine_ls_shell.percent_reflns_R_free            4.9 
_refine_ls_shell.number_reflns_R_free             1301 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 
2 ION.PARAM         ?           'X-RAY DIFFRACTION' 
3 WATER_REP.PARAM   ?           'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  1N18 
_struct.title                     'Thermostable mutant of Human Superoxide Dismutase, C6A, C111S' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1N18 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'greek key beta barrel, oxidoreductase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 4 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 2 ? 
CA N N 3 ? 
DA N N 2 ? 
EA N N 3 ? 
FA N N 5 ? 
GA N N 5 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 5 ? 
KA N N 5 ? 
LA N N 5 ? 
MA N N 5 ? 
NA N N 5 ? 
OA N N 5 ? 
# 
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  1  ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  ASN A 132 ? THR A 136 ? ASN A 131 THR A 135 5 ? 5 
HELX_P HELX_P3  3  ALA B 56  ? GLY B 62  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4  4  ALA C 56  ? GLY C 62  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P5  5  ASN C 132 ? THR C 138 ? ASN C 131 THR C 137 1 ? 7 
HELX_P HELX_P6  6  CYS D 58  ? GLY D 62  ? CYS D 57  GLY D 61  5 ? 5 
HELX_P HELX_P7  7  GLU D 133 ? LYS D 137 ? GLU D 132 LYS D 136 5 ? 5 
HELX_P HELX_P8  8  ALA E 56  ? GLY E 62  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P9  9  GLU E 133 ? LYS E 137 ? GLU E 132 LYS E 136 5 ? 5 
HELX_P HELX_P10 10 ALA F 56  ? GLY F 62  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P11 11 ASN F 132 ? THR F 136 ? ASN F 131 THR F 135 5 ? 5 
HELX_P HELX_P12 12 CYS G 58  ? GLY G 62  ? CYS G 57  GLY G 61  5 ? 5 
HELX_P HELX_P13 13 CYS H 58  ? GLY H 62  ? CYS H 57  GLY H 61  5 ? 5 
HELX_P HELX_P14 14 GLU H 133 ? LYS H 137 ? GLU H 132 LYS H 136 5 ? 5 
HELX_P HELX_P15 15 ALA I 56  ? GLY I 62  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P16 16 GLU I 133 ? LYS I 137 ? GLU I 132 LYS I 136 5 ? 5 
HELX_P HELX_P17 17 ALA J 56  ? GLY J 62  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P18 18 SER J 108 ? SER J 112 ? SER J 107 SER J 111 5 ? 5 
HELX_P HELX_P19 19 GLU J 133 ? LYS J 137 ? GLU J 132 LYS J 136 5 ? 5 
# 
_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 58  SG  ? ? ? 1_555 A  CYS 147 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf2  disulf ? ? B CYS 58  SG  ? ? ? 1_555 B  CYS 147 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf3  disulf ? ? C CYS 58  SG  ? ? ? 1_555 C  CYS 147 SG ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf4  disulf ? ? D CYS 58  SG  ? ? ? 1_555 D  CYS 147 SG ? ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf5  disulf ? ? E CYS 58  SG  ? ? ? 1_555 E  CYS 147 SG ? ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf6  disulf ? ? F CYS 58  SG  ? ? ? 1_555 F  CYS 147 SG ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf7  disulf ? ? G CYS 58  SG  ? ? ? 1_555 G  CYS 147 SG ? ? G CYS 57  G CYS 146 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf8  disulf ? ? H CYS 58  SG  ? ? ? 1_555 H  CYS 147 SG ? ? H CYS 57  H CYS 146 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf9  disulf ? ? I CYS 58  SG  ? ? ? 1_555 I  CYS 147 SG ? ? I CYS 57  I CYS 146 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf10 disulf ? ? J CYS 58  SG  ? ? ? 1_555 J  CYS 147 SG ? ? J CYS 57  J CYS 146 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc1  metalc ? ? A HIS 47  ND1 ? ? ? 1_555 K  CU1 .   CU ? ? A HIS 46  A CU1 154 1_555 ? ? ? ? ? ? ? 2.146 ? ? 
metalc2  metalc ? ? A HIS 49  NE2 ? ? ? 1_555 K  CU1 .   CU ? ? A HIS 48  A CU1 154 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc3  metalc ? ? A HIS 64  ND1 ? ? ? 1_555 L  ZN  .   ZN ? ? A HIS 63  A ZN  155 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc4  metalc ? ? A HIS 72  ND1 ? ? ? 1_555 L  ZN  .   ZN ? ? A HIS 71  A ZN  155 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc5  metalc ? ? A HIS 81  ND1 ? ? ? 1_555 L  ZN  .   ZN ? ? A HIS 80  A ZN  155 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc6  metalc ? ? A ASP 84  OD1 ? ? ? 1_555 L  ZN  .   ZN ? ? A ASP 83  A ZN  155 1_555 ? ? ? ? ? ? ? 1.900 ? ? 
metalc7  metalc ? ? A HIS 121 NE2 ? ? ? 1_555 K  CU1 .   CU ? ? A HIS 120 A CU1 154 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc8  metalc ? ? B HIS 47  ND1 ? ? ? 1_555 M  CU1 .   CU ? ? B HIS 46  B CU1 154 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc9  metalc ? ? B HIS 49  NE2 ? ? ? 1_555 M  CU1 .   CU ? ? B HIS 48  B CU1 154 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc10 metalc ? ? B HIS 64  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? B HIS 63  B ZN  155 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc11 metalc ? ? B HIS 72  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? B HIS 71  B ZN  155 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc12 metalc ? ? B HIS 81  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? B HIS 80  B ZN  155 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
metalc13 metalc ? ? B ASP 84  OD1 ? ? ? 1_555 N  ZN  .   ZN ? ? B ASP 83  B ZN  155 1_555 ? ? ? ? ? ? ? 1.957 ? ? 
metalc14 metalc ? ? B HIS 121 NE2 ? ? ? 1_555 M  CU1 .   CU ? ? B HIS 120 B CU1 154 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc15 metalc ? ? C HIS 47  ND1 ? ? ? 1_555 O  CU1 .   CU ? ? C HIS 46  C CU1 154 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
metalc16 metalc ? ? C HIS 49  NE2 ? ? ? 1_555 O  CU1 .   CU ? ? C HIS 48  C CU1 154 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc17 metalc ? ? C HIS 64  NE2 ? ? ? 1_555 O  CU1 .   CU ? ? C HIS 63  C CU1 154 1_555 ? ? ? ? ? ? ? 2.664 ? ? 
metalc18 metalc ? ? C HIS 64  ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? C HIS 63  C ZN  155 1_555 ? ? ? ? ? ? ? 2.362 ? ? 
metalc19 metalc ? ? C HIS 72  ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? C HIS 71  C ZN  155 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc20 metalc ? ? C HIS 81  ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? C HIS 80  C ZN  155 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc21 metalc ? ? C ASP 84  OD1 ? ? ? 1_555 P  ZN  .   ZN ? ? C ASP 83  C ZN  155 1_555 ? ? ? ? ? ? ? 1.809 ? ? 
metalc22 metalc ? ? C HIS 121 NE2 ? ? ? 1_555 O  CU1 .   CU ? ? C HIS 120 C CU1 154 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc23 metalc ? ? D HIS 47  ND1 ? ? ? 1_555 Q  CU1 .   CU ? ? D HIS 46  D CU1 154 1_555 ? ? ? ? ? ? ? 2.146 ? ? 
metalc24 metalc ? ? D HIS 49  NE2 ? ? ? 1_555 Q  CU1 .   CU ? ? D HIS 48  D CU1 154 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc25 metalc ? ? D HIS 64  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? D HIS 63  D ZN  155 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
metalc26 metalc ? ? D HIS 72  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? D HIS 71  D ZN  155 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc27 metalc ? ? D HIS 81  ND1 ? ? ? 1_555 R  ZN  .   ZN ? ? D HIS 80  D ZN  155 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc28 metalc ? ? D ASP 84  OD1 ? ? ? 1_555 R  ZN  .   ZN ? ? D ASP 83  D ZN  155 1_555 ? ? ? ? ? ? ? 1.935 ? ? 
metalc29 metalc ? ? D HIS 121 NE2 ? ? ? 1_555 Q  CU1 .   CU ? ? D HIS 120 D CU1 154 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc30 metalc ? ? E HIS 47  ND1 ? ? ? 1_555 T  CU1 .   CU ? ? E HIS 46  E CU1 154 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc31 metalc ? ? E HIS 49  NE2 ? ? ? 1_555 T  CU1 .   CU ? ? E HIS 48  E CU1 154 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc32 metalc ? ? E HIS 64  ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? E HIS 63  E ZN  155 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc33 metalc ? ? E HIS 72  ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? E HIS 71  E ZN  155 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc34 metalc ? ? E HIS 81  ND1 ? ? ? 1_555 U  ZN  .   ZN ? ? E HIS 80  E ZN  155 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc35 metalc ? ? E ASP 84  OD1 ? ? ? 1_555 U  ZN  .   ZN ? ? E ASP 83  E ZN  155 1_555 ? ? ? ? ? ? ? 1.854 ? ? 
metalc36 metalc ? ? E HIS 121 NE2 ? ? ? 1_555 T  CU1 .   CU ? ? E HIS 120 E CU1 154 1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc37 metalc ? ? F HIS 47  ND1 ? ? ? 1_555 V  CU1 .   CU ? ? F HIS 46  F CU1 154 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc38 metalc ? ? F HIS 49  NE2 ? ? ? 1_555 V  CU1 .   CU ? ? F HIS 48  F CU1 154 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc39 metalc ? ? F HIS 64  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? F HIS 63  F ZN  155 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc40 metalc ? ? F HIS 72  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? F HIS 71  F ZN  155 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc41 metalc ? ? F HIS 81  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? F HIS 80  F ZN  155 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc42 metalc ? ? F ASP 84  OD1 ? ? ? 1_555 W  ZN  .   ZN ? ? F ASP 83  F ZN  155 1_555 ? ? ? ? ? ? ? 1.921 ? ? 
metalc43 metalc ? ? F HIS 121 NE2 ? ? ? 1_555 V  CU1 .   CU ? ? F HIS 120 F CU1 154 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc44 metalc ? ? G HIS 47  ND1 ? ? ? 1_555 X  CU1 .   CU ? ? G HIS 46  G CU1 154 1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc45 metalc ? ? G HIS 49  NE2 ? ? ? 1_555 X  CU1 .   CU ? ? G HIS 48  G CU1 154 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc46 metalc ? ? G HIS 64  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G HIS 63  G ZN  155 1_555 ? ? ? ? ? ? ? 2.163 ? ? 
metalc47 metalc ? ? G HIS 72  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G HIS 71  G ZN  155 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc48 metalc ? ? G HIS 81  ND1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G HIS 80  G ZN  155 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc49 metalc ? ? G ASP 84  OD1 ? ? ? 1_555 Y  ZN  .   ZN ? ? G ASP 83  G ZN  155 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
metalc50 metalc ? ? G HIS 121 NE2 ? ? ? 1_555 X  CU1 .   CU ? ? G HIS 120 G CU1 154 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc51 metalc ? ? H HIS 47  ND1 ? ? ? 1_555 Z  CU1 .   CU ? ? H HIS 46  H CU1 154 1_555 ? ? ? ? ? ? ? 2.151 ? ? 
metalc52 metalc ? ? H HIS 49  NE2 ? ? ? 1_555 Z  CU1 .   CU ? ? H HIS 48  H CU1 154 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc53 metalc ? ? H HIS 64  ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? H HIS 63  H ZN  155 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc54 metalc ? ? H HIS 72  ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? H HIS 71  H ZN  155 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc55 metalc ? ? H HIS 81  ND1 ? ? ? 1_555 AA ZN  .   ZN ? ? H HIS 80  H ZN  155 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc56 metalc ? ? H ASP 84  OD1 ? ? ? 1_555 AA ZN  .   ZN ? ? H ASP 83  H ZN  155 1_555 ? ? ? ? ? ? ? 1.918 ? ? 
metalc57 metalc ? ? H HIS 121 NE2 ? ? ? 1_555 Z  CU1 .   CU ? ? H HIS 120 H CU1 154 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc58 metalc ? ? I HIS 47  ND1 ? ? ? 1_555 BA CU1 .   CU ? ? I HIS 46  I CU1 154 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc59 metalc ? ? I HIS 49  NE2 ? ? ? 1_555 BA CU1 .   CU ? ? I HIS 48  I CU1 154 1_555 ? ? ? ? ? ? ? 2.132 ? ? 
metalc60 metalc ? ? I HIS 64  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? I HIS 63  I ZN  155 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
metalc61 metalc ? ? I HIS 72  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? I HIS 71  I ZN  155 1_555 ? ? ? ? ? ? ? 1.969 ? ? 
metalc62 metalc ? ? I HIS 81  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? I HIS 80  I ZN  155 1_555 ? ? ? ? ? ? ? 2.136 ? ? 
metalc63 metalc ? ? I ASP 84  OD1 ? ? ? 1_555 CA ZN  .   ZN ? ? I ASP 83  I ZN  155 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc64 metalc ? ? I HIS 121 NE2 ? ? ? 1_555 BA CU1 .   CU ? ? I HIS 120 I CU1 154 1_555 ? ? ? ? ? ? ? 1.927 ? ? 
metalc65 metalc ? ? J HIS 47  ND1 ? ? ? 1_555 DA CU1 .   CU ? ? J HIS 46  J CU1 154 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc66 metalc ? ? J HIS 49  NE2 ? ? ? 1_555 DA CU1 .   CU ? ? J HIS 48  J CU1 154 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc67 metalc ? ? J HIS 64  ND1 ? ? ? 1_555 EA ZN  .   ZN ? ? J HIS 63  J ZN  155 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc68 metalc ? ? J HIS 72  ND1 ? ? ? 1_555 EA ZN  .   ZN ? ? J HIS 71  J ZN  155 1_555 ? ? ? ? ? ? ? 1.973 ? ? 
metalc69 metalc ? ? J HIS 81  ND1 ? ? ? 1_555 EA ZN  .   ZN ? ? J HIS 80  J ZN  155 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc70 metalc ? ? J ASP 84  OD1 ? ? ? 1_555 EA ZN  .   ZN ? ? J ASP 83  J ZN  155 1_555 ? ? ? ? ? ? ? 1.916 ? ? 
metalc71 metalc ? ? J HIS 121 NE2 ? ? ? 1_555 DA CU1 .   CU ? ? J HIS 120 J CU1 154 1_555 ? ? ? ? ? ? ? 1.924 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
G ? 5 ? 
H ? 4 ? 
I ? 5 ? 
J ? 4 ? 
K ? 5 ? 
L ? 4 ? 
M ? 5 ? 
N ? 4 ? 
O ? 5 ? 
P ? 4 ? 
Q ? 5 ? 
R ? 4 ? 
S ? 5 ? 
T ? 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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
G 4 5 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
K 4 5 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
M 4 5 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
O 4 5 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
Q 4 5 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
S 1 2 ? anti-parallel 
S 2 3 ? anti-parallel 
S 3 4 ? anti-parallel 
S 4 5 ? anti-parallel 
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 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 
A 1 ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
A 2 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
A 3 GLN A 16  ? GLN A 23  ? GLN A 15  GLN A 22  
A 4 LYS A 4   ? LEU A 9   ? LYS A 3   LEU A 8   
A 5 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
B 1 ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
B 2 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
B 3 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
B 4 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
C 1 ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
C 2 VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
C 3 GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
C 4 LYS B 4   ? LYS B 10  ? LYS B 3   LYS B 9   
C 5 GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
D 1 ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
D 2 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
D 3 THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
D 4 ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
E 1 ALA C 96  ? ASP C 102 ? ALA C 95  ASP C 101 
E 2 VAL C 30  ? LYS C 37  ? VAL C 29  LYS C 36  
E 3 GLN C 16  ? GLU C 22  ? GLN C 15  GLU C 21  
E 4 LYS C 4   ? LEU C 9   ? LYS C 3   LEU C 8   
E 5 GLY C 151 ? ILE C 152 ? GLY C 150 ILE C 151 
F 1 ASP C 84  ? ALA C 90  ? ASP C 83  ALA C 89  
F 2 GLY C 42  ? HIS C 49  ? GLY C 41  HIS C 48  
F 3 THR C 117 ? HIS C 121 ? THR C 116 HIS C 120 
F 4 ARG C 144 ? VAL C 149 ? ARG C 143 VAL C 148 
G 1 ALA D 96  ? ASP D 102 ? ALA D 95  ASP D 101 
G 2 VAL D 30  ? LYS D 37  ? VAL D 29  LYS D 36  
G 3 GLN D 16  ? GLU D 22  ? GLN D 15  GLU D 21  
G 4 LYS D 4   ? LEU D 9   ? LYS D 3   LEU D 8   
G 5 GLY D 151 ? ILE D 152 ? GLY D 150 ILE D 151 
H 1 ASP D 84  ? ALA D 90  ? ASP D 83  ALA D 89  
H 2 GLY D 42  ? HIS D 49  ? GLY D 41  HIS D 48  
H 3 THR D 117 ? HIS D 121 ? THR D 116 HIS D 120 
H 4 ARG D 144 ? VAL D 149 ? ARG D 143 VAL D 148 
I 1 ALA E 96  ? ASP E 102 ? ALA E 95  ASP E 101 
I 2 VAL E 30  ? LYS E 37  ? VAL E 29  LYS E 36  
I 3 GLN E 16  ? GLU E 22  ? GLN E 15  GLU E 21  
I 4 LYS E 4   ? LEU E 9   ? LYS E 3   LEU E 8   
I 5 GLY E 151 ? ILE E 152 ? GLY E 150 ILE E 151 
J 1 ASP E 84  ? ALA E 90  ? ASP E 83  ALA E 89  
J 2 GLY E 42  ? HIS E 49  ? GLY E 41  HIS E 48  
J 3 THR E 117 ? HIS E 121 ? THR E 116 HIS E 120 
J 4 ARG E 144 ? VAL E 149 ? ARG E 143 VAL E 148 
K 1 ALA F 96  ? ASP F 102 ? ALA F 95  ASP F 101 
K 2 VAL F 30  ? LYS F 37  ? VAL F 29  LYS F 36  
K 3 GLN F 16  ? GLU F 22  ? GLN F 15  GLU F 21  
K 4 LYS F 4   ? LEU F 9   ? LYS F 3   LEU F 8   
K 5 GLY F 151 ? ILE F 152 ? GLY F 150 ILE F 151 
L 1 ASP F 84  ? ALA F 90  ? ASP F 83  ALA F 89  
L 2 GLY F 42  ? HIS F 49  ? GLY F 41  HIS F 48  
L 3 THR F 117 ? HIS F 121 ? THR F 116 HIS F 120 
L 4 ARG F 144 ? VAL F 149 ? ARG F 143 VAL F 148 
M 1 ALA G 96  ? ASP G 102 ? ALA G 95  ASP G 101 
M 2 VAL G 30  ? LYS G 37  ? VAL G 29  LYS G 36  
M 3 GLN G 16  ? GLU G 22  ? GLN G 15  GLU G 21  
M 4 LYS G 4   ? LEU G 9   ? LYS G 3   LEU G 8   
M 5 GLY G 151 ? ALA G 153 ? GLY G 150 ALA G 152 
N 1 ASP G 84  ? ALA G 90  ? ASP G 83  ALA G 89  
N 2 GLY G 42  ? HIS G 49  ? GLY G 41  HIS G 48  
N 3 THR G 117 ? HIS G 121 ? THR G 116 HIS G 120 
N 4 ARG G 144 ? VAL G 149 ? ARG G 143 VAL G 148 
O 1 ALA H 96  ? ASP H 102 ? ALA H 95  ASP H 101 
O 2 VAL H 30  ? LYS H 37  ? VAL H 29  LYS H 36  
O 3 GLN H 16  ? GLU H 22  ? GLN H 15  GLU H 21  
O 4 LYS H 4   ? LEU H 9   ? LYS H 3   LEU H 8   
O 5 GLY H 151 ? GLN H 154 ? GLY H 150 GLN H 153 
P 1 ASP H 84  ? ALA H 90  ? ASP H 83  ALA H 89  
P 2 GLY H 42  ? HIS H 49  ? GLY H 41  HIS H 48  
P 3 THR H 117 ? HIS H 121 ? THR H 116 HIS H 120 
P 4 ARG H 144 ? VAL H 149 ? ARG H 143 VAL H 148 
Q 1 ALA I 96  ? ASP I 102 ? ALA I 95  ASP I 101 
Q 2 VAL I 30  ? LYS I 37  ? VAL I 29  LYS I 36  
Q 3 GLN I 16  ? GLN I 23  ? GLN I 15  GLN I 22  
Q 4 LYS I 4   ? LEU I 9   ? LYS I 3   LEU I 8   
Q 5 GLY I 151 ? ALA I 153 ? GLY I 150 ALA I 152 
R 1 ASP I 84  ? ALA I 90  ? ASP I 83  ALA I 89  
R 2 GLY I 42  ? HIS I 49  ? GLY I 41  HIS I 48  
R 3 THR I 117 ? HIS I 121 ? THR I 116 HIS I 120 
R 4 ARG I 144 ? VAL I 149 ? ARG I 143 VAL I 148 
S 1 ALA J 96  ? ASP J 102 ? ALA J 95  ASP J 101 
S 2 VAL J 30  ? LYS J 37  ? VAL J 29  LYS J 36  
S 3 GLN J 16  ? GLU J 22  ? GLN J 15  GLU J 21  
S 4 LYS J 4   ? LEU J 9   ? LYS J 3   LEU J 8   
S 5 GLY J 151 ? ILE J 152 ? GLY J 150 ILE J 151 
T 1 ASP J 84  ? ALA J 90  ? ASP J 83  ALA J 89  
T 2 GLY J 42  ? HIS J 49  ? GLY J 41  HIS J 48  
T 3 THR J 117 ? HIS J 121 ? THR J 116 HIS J 120 
T 4 ARG J 144 ? VAL J 149 ? ARG J 143 VAL J 148 
# 
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 
A 1 2 O ILE A 100 ? O ILE A 99  N VAL A 32  ? N VAL A 31  
A 2 3 O TRP A 33  ? O TRP A 32  N ASN A 20  ? N ASN A 19  
A 3 4 O PHE A 21  ? O PHE A 20  N ALA A 5   ? N ALA A 4   
A 4 5 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
B 1 2 O ALA A 90  ? O ALA A 89  N GLY A 42  ? N GLY A 41  
B 2 3 N HIS A 49  ? N HIS A 48  O THR A 117 ? O THR A 116 
B 3 4 N LEU A 118 ? N LEU A 117 O GLY A 148 ? O GLY A 147 
C 1 2 O ILE B 100 ? O ILE B 99  N VAL B 32  ? N VAL B 31  
C 2 3 O TRP B 33  ? O TRP B 32  N ASN B 20  ? N ASN B 19  
C 3 4 O GLY B 17  ? O GLY B 16  N LEU B 9   ? N LEU B 8   
C 4 5 N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
D 1 2 O ALA B 90  ? O ALA B 89  N GLY B 42  ? N GLY B 41  
D 2 3 N HIS B 49  ? N HIS B 48  O THR B 117 ? O THR B 116 
D 3 4 N LEU B 118 ? N LEU B 117 O GLY B 148 ? O GLY B 147 
E 1 2 O ILE C 100 ? O ILE C 99  N VAL C 32  ? N VAL C 31  
E 2 3 O TRP C 33  ? O TRP C 32  N ASN C 20  ? N ASN C 19  
E 3 4 O ILE C 19  ? O ILE C 18  N ALA C 7   ? N ALA C 6   
E 4 5 N VAL C 6   ? N VAL C 5   O GLY C 151 ? O GLY C 150 
F 1 2 O ALA C 90  ? O ALA C 89  N GLY C 42  ? N GLY C 41  
F 2 3 N HIS C 49  ? N HIS C 48  O THR C 117 ? O THR C 116 
F 3 4 N LEU C 118 ? N LEU C 117 O GLY C 148 ? O GLY C 147 
G 1 2 O ASP D 102 ? O ASP D 101 N VAL D 30  ? N VAL D 29  
G 2 3 O TRP D 33  ? O TRP D 32  N ASN D 20  ? N ASN D 19  
G 3 4 O PHE D 21  ? O PHE D 20  N ALA D 5   ? N ALA D 4   
G 4 5 N VAL D 6   ? N VAL D 5   O GLY D 151 ? O GLY D 150 
H 1 2 O ALA D 90  ? O ALA D 89  N GLY D 42  ? N GLY D 41  
H 2 3 N HIS D 49  ? N HIS D 48  O THR D 117 ? O THR D 116 
H 3 4 N LEU D 118 ? N LEU D 117 O GLY D 148 ? O GLY D 147 
I 1 2 O ILE E 100 ? O ILE E 99  N VAL E 32  ? N VAL E 31  
I 2 3 O TRP E 33  ? O TRP E 32  N ASN E 20  ? N ASN E 19  
I 3 4 O GLY E 17  ? O GLY E 16  N LEU E 9   ? N LEU E 8   
I 4 5 N VAL E 6   ? N VAL E 5   O GLY E 151 ? O GLY E 150 
J 1 2 O ALA E 90  ? O ALA E 89  N GLY E 42  ? N GLY E 41  
J 2 3 N HIS E 49  ? N HIS E 48  O THR E 117 ? O THR E 116 
J 3 4 N LEU E 118 ? N LEU E 117 O GLY E 148 ? O GLY E 147 
K 1 2 O ILE F 100 ? O ILE F 99  N VAL F 32  ? N VAL F 31  
K 2 3 O TRP F 33  ? O TRP F 32  N ASN F 20  ? N ASN F 19  
K 3 4 O ILE F 19  ? O ILE F 18  N ALA F 7   ? N ALA F 6   
K 4 5 N VAL F 6   ? N VAL F 5   O GLY F 151 ? O GLY F 150 
L 1 2 O ALA F 90  ? O ALA F 89  N GLY F 42  ? N GLY F 41  
L 2 3 N HIS F 49  ? N HIS F 48  O THR F 117 ? O THR F 116 
L 3 4 N LEU F 118 ? N LEU F 117 O GLY F 148 ? O GLY F 147 
M 1 2 O ILE G 100 ? O ILE G 99  N VAL G 32  ? N VAL G 31  
M 2 3 O TRP G 33  ? O TRP G 32  N ASN G 20  ? N ASN G 19  
M 3 4 O GLY G 17  ? O GLY G 16  N LEU G 9   ? N LEU G 8   
M 4 5 N VAL G 6   ? N VAL G 5   O GLY G 151 ? O GLY G 150 
N 1 2 O ALA G 90  ? O ALA G 89  N GLY G 42  ? N GLY G 41  
N 2 3 N HIS G 49  ? N HIS G 48  O THR G 117 ? O THR G 116 
N 3 4 N VAL G 120 ? N VAL G 119 O ALA G 146 ? O ALA G 145 
O 1 2 O ALA H 96  ? O ALA H 95  N ILE H 36  ? N ILE H 35  
O 2 3 O TRP H 33  ? O TRP H 32  N ASN H 20  ? N ASN H 19  
O 3 4 O GLY H 17  ? O GLY H 16  N LEU H 9   ? N LEU H 8   
O 4 5 N LYS H 4   ? N LYS H 3   O ALA H 153 ? O ALA H 152 
P 1 2 O ALA H 90  ? O ALA H 89  N GLY H 42  ? N GLY H 41  
P 2 3 N HIS H 49  ? N HIS H 48  O THR H 117 ? O THR H 116 
P 3 4 N LEU H 118 ? N LEU H 117 O GLY H 148 ? O GLY H 147 
Q 1 2 O ILE I 100 ? O ILE I 99  N VAL I 32  ? N VAL I 31  
Q 2 3 O TRP I 33  ? O TRP I 32  N ASN I 20  ? N ASN I 19  
Q 3 4 O PHE I 21  ? O PHE I 20  N ALA I 5   ? N ALA I 4   
Q 4 5 N VAL I 6   ? N VAL I 5   O GLY I 151 ? O GLY I 150 
R 1 2 O ALA I 90  ? O ALA I 89  N GLY I 42  ? N GLY I 41  
R 2 3 N HIS I 49  ? N HIS I 48  O THR I 117 ? O THR I 116 
R 3 4 N LEU I 118 ? N LEU I 117 O GLY I 148 ? O GLY I 147 
S 1 2 O ILE J 100 ? O ILE J 99  N VAL J 32  ? N VAL J 31  
S 2 3 O TRP J 33  ? O TRP J 32  N ASN J 20  ? N ASN J 19  
S 3 4 O PHE J 21  ? O PHE J 20  N ALA J 5   ? N ALA J 4   
S 4 5 N VAL J 6   ? N VAL J 5   O GLY J 151 ? O GLY J 150 
T 1 2 O ALA J 90  ? O ALA J 89  N GLY J 42  ? N GLY J 41  
T 2 3 N HIS J 49  ? N HIS J 48  O THR J 117 ? O THR J 116 
T 3 4 N LEU J 118 ? N LEU J 117 O GLY J 148 ? O GLY J 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 A 154'  
AC2 Software A ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN A 155'   
AC3 Software B CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 B 154'  
AC4 Software B ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN B 155'   
AC5 Software C CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 C 154'  
AC6 Software C ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN C 155'   
AC7 Software D CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 D 154'  
AC8 Software D ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN D 155'   
AC9 Software E CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 E 154'  
BC1 Software E ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN E 155'   
BC2 Software F CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 F 154'  
BC3 Software F ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN F 155'   
BC4 Software G CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 G 154'  
BC5 Software G ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN G 155'   
BC6 Software H CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 H 154'  
BC7 Software H ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN H 155'   
BC8 Software I CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 I 154'  
BC9 Software I ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN I 155'   
CC1 Software J CU1 154  ? 4 'BINDING SITE FOR RESIDUE CU1 J 154'  
CC2 Software J ZN  155  ? 4 'BINDING SITE FOR RESIDUE ZN J 155'   
CC3 Software D SO4 1400 ? 5 'BINDING SITE FOR RESIDUE SO4 D 1400' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A  47  ? HIS A 46   . ? 1_555 ? 
2  AC1 4 HIS A  49  ? HIS A 48   . ? 1_555 ? 
3  AC1 4 HIS A  64  ? HIS A 63   . ? 1_555 ? 
4  AC1 4 HIS A  121 ? HIS A 120  . ? 1_555 ? 
5  AC2 4 HIS A  64  ? HIS A 63   . ? 1_555 ? 
6  AC2 4 HIS A  72  ? HIS A 71   . ? 1_555 ? 
7  AC2 4 HIS A  81  ? HIS A 80   . ? 1_555 ? 
8  AC2 4 ASP A  84  ? ASP A 83   . ? 1_555 ? 
9  AC3 4 HIS B  47  ? HIS B 46   . ? 1_555 ? 
10 AC3 4 HIS B  49  ? HIS B 48   . ? 1_555 ? 
11 AC3 4 HIS B  64  ? HIS B 63   . ? 1_555 ? 
12 AC3 4 HIS B  121 ? HIS B 120  . ? 1_555 ? 
13 AC4 4 HIS B  64  ? HIS B 63   . ? 1_555 ? 
14 AC4 4 HIS B  72  ? HIS B 71   . ? 1_555 ? 
15 AC4 4 HIS B  81  ? HIS B 80   . ? 1_555 ? 
16 AC4 4 ASP B  84  ? ASP B 83   . ? 1_555 ? 
17 AC5 4 HIS C  47  ? HIS C 46   . ? 1_555 ? 
18 AC5 4 HIS C  49  ? HIS C 48   . ? 1_555 ? 
19 AC5 4 HIS C  64  ? HIS C 63   . ? 1_555 ? 
20 AC5 4 HIS C  121 ? HIS C 120  . ? 1_555 ? 
21 AC6 4 HIS C  64  ? HIS C 63   . ? 1_555 ? 
22 AC6 4 HIS C  72  ? HIS C 71   . ? 1_555 ? 
23 AC6 4 HIS C  81  ? HIS C 80   . ? 1_555 ? 
24 AC6 4 ASP C  84  ? ASP C 83   . ? 1_555 ? 
25 AC7 4 HIS D  47  ? HIS D 46   . ? 1_555 ? 
26 AC7 4 HIS D  49  ? HIS D 48   . ? 1_555 ? 
27 AC7 4 HIS D  64  ? HIS D 63   . ? 1_555 ? 
28 AC7 4 HIS D  121 ? HIS D 120  . ? 1_555 ? 
29 AC8 4 HIS D  64  ? HIS D 63   . ? 1_555 ? 
30 AC8 4 HIS D  72  ? HIS D 71   . ? 1_555 ? 
31 AC8 4 HIS D  81  ? HIS D 80   . ? 1_555 ? 
32 AC8 4 ASP D  84  ? ASP D 83   . ? 1_555 ? 
33 AC9 4 HIS E  47  ? HIS E 46   . ? 1_555 ? 
34 AC9 4 HIS E  49  ? HIS E 48   . ? 1_555 ? 
35 AC9 4 HIS E  64  ? HIS E 63   . ? 1_555 ? 
36 AC9 4 HIS E  121 ? HIS E 120  . ? 1_555 ? 
37 BC1 4 HIS E  64  ? HIS E 63   . ? 1_555 ? 
38 BC1 4 HIS E  72  ? HIS E 71   . ? 1_555 ? 
39 BC1 4 HIS E  81  ? HIS E 80   . ? 1_555 ? 
40 BC1 4 ASP E  84  ? ASP E 83   . ? 1_555 ? 
41 BC2 4 HIS F  47  ? HIS F 46   . ? 1_555 ? 
42 BC2 4 HIS F  49  ? HIS F 48   . ? 1_555 ? 
43 BC2 4 HIS F  64  ? HIS F 63   . ? 1_555 ? 
44 BC2 4 HIS F  121 ? HIS F 120  . ? 1_555 ? 
45 BC3 4 HIS F  64  ? HIS F 63   . ? 1_555 ? 
46 BC3 4 HIS F  72  ? HIS F 71   . ? 1_555 ? 
47 BC3 4 HIS F  81  ? HIS F 80   . ? 1_555 ? 
48 BC3 4 ASP F  84  ? ASP F 83   . ? 1_555 ? 
49 BC4 4 HIS G  47  ? HIS G 46   . ? 1_555 ? 
50 BC4 4 HIS G  49  ? HIS G 48   . ? 1_555 ? 
51 BC4 4 HIS G  64  ? HIS G 63   . ? 1_555 ? 
52 BC4 4 HIS G  121 ? HIS G 120  . ? 1_555 ? 
53 BC5 4 HIS G  64  ? HIS G 63   . ? 1_555 ? 
54 BC5 4 HIS G  72  ? HIS G 71   . ? 1_555 ? 
55 BC5 4 HIS G  81  ? HIS G 80   . ? 1_555 ? 
56 BC5 4 ASP G  84  ? ASP G 83   . ? 1_555 ? 
57 BC6 4 HIS H  47  ? HIS H 46   . ? 1_555 ? 
58 BC6 4 HIS H  49  ? HIS H 48   . ? 1_555 ? 
59 BC6 4 HIS H  64  ? HIS H 63   . ? 1_555 ? 
60 BC6 4 HIS H  121 ? HIS H 120  . ? 1_555 ? 
61 BC7 4 HIS H  64  ? HIS H 63   . ? 1_555 ? 
62 BC7 4 HIS H  72  ? HIS H 71   . ? 1_555 ? 
63 BC7 4 HIS H  81  ? HIS H 80   . ? 1_555 ? 
64 BC7 4 ASP H  84  ? ASP H 83   . ? 1_555 ? 
65 BC8 4 HIS I  47  ? HIS I 46   . ? 1_555 ? 
66 BC8 4 HIS I  49  ? HIS I 48   . ? 1_555 ? 
67 BC8 4 HIS I  64  ? HIS I 63   . ? 1_555 ? 
68 BC8 4 HIS I  121 ? HIS I 120  . ? 1_555 ? 
69 BC9 4 HIS I  64  ? HIS I 63   . ? 1_555 ? 
70 BC9 4 HIS I  72  ? HIS I 71   . ? 1_555 ? 
71 BC9 4 HIS I  81  ? HIS I 80   . ? 1_555 ? 
72 BC9 4 ASP I  84  ? ASP I 83   . ? 1_555 ? 
73 CC1 4 HIS J  47  ? HIS J 46   . ? 1_555 ? 
74 CC1 4 HIS J  49  ? HIS J 48   . ? 1_555 ? 
75 CC1 4 HIS J  64  ? HIS J 63   . ? 1_555 ? 
76 CC1 4 HIS J  121 ? HIS J 120  . ? 1_555 ? 
77 CC2 4 HIS J  64  ? HIS J 63   . ? 1_555 ? 
78 CC2 4 HIS J  72  ? HIS J 71   . ? 1_555 ? 
79 CC2 4 HIS J  81  ? HIS J 80   . ? 1_555 ? 
80 CC2 4 ASP J  84  ? ASP J 83   . ? 1_555 ? 
81 CC3 5 LYS B  76  ? LYS B 75   . ? 1_555 ? 
82 CC3 5 LYS D  129 ? LYS D 128  . ? 1_555 ? 
83 CC3 5 HOH IA .   ? HOH D 1429 . ? 1_555 ? 
84 CC3 5 HOH IA .   ? HOH D 1450 . ? 1_555 ? 
85 CC3 5 HOH IA .   ? HOH D 1515 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1N18 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1N18 
_atom_sites.fract_transf_matrix[1][1]   0.004921 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006053 
_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]   0.006930 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
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   . ALA A  1 2   ? 54.426  29.012  7.245  0.00 44.49 ? 1    ALA A N   1 
ATOM   2     C  CA  . ALA A  1 2   ? 53.479  28.563  8.305  0.00 44.46 ? 1    ALA A CA  1 
ATOM   3     C  C   . ALA A  1 2   ? 52.214  29.415  8.300  1.00 43.96 ? 1    ALA A C   1 
ATOM   4     O  O   . ALA A  1 2   ? 52.216  30.540  7.807  1.00 46.21 ? 1    ALA A O   1 
ATOM   5     C  CB  . ALA A  1 2   ? 54.157  28.640  9.669  0.00 44.53 ? 1    ALA A CB  1 
ATOM   6     N  N   . THR A  1 3   ? 51.131  28.873  8.845  1.00 43.03 ? 2    THR A N   1 
ATOM   7     C  CA  . THR A  1 3   ? 49.866  29.597  8.902  1.00 39.77 ? 2    THR A CA  1 
ATOM   8     C  C   . THR A  1 3   ? 49.685  30.194  10.298 1.00 36.11 ? 2    THR A C   1 
ATOM   9     O  O   . THR A  1 3   ? 49.026  31.216  10.462 1.00 32.37 ? 2    THR A O   1 
ATOM   10    C  CB  . THR A  1 3   ? 48.677  28.668  8.592  1.00 41.95 ? 2    THR A CB  1 
ATOM   11    O  OG1 . THR A  1 3   ? 48.896  28.007  7.340  1.00 44.61 ? 2    THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 3   ? 47.396  29.469  8.495  1.00 44.62 ? 2    THR A CG2 1 
ATOM   13    N  N   . LYS A  1 4   ? 50.274  29.540  11.295 1.00 33.77 ? 3    LYS A N   1 
ATOM   14    C  CA  . LYS A  1 4   ? 50.212  29.995  12.682 1.00 31.85 ? 3    LYS A CA  1 
ATOM   15    C  C   . LYS A  1 4   ? 51.608  30.019  13.296 1.00 29.23 ? 3    LYS A C   1 
ATOM   16    O  O   . LYS A  1 4   ? 52.463  29.205  12.952 1.00 26.31 ? 3    LYS A O   1 
ATOM   17    C  CB  . LYS A  1 4   ? 49.319  29.075  13.524 1.00 35.44 ? 3    LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 4   ? 47.829  29.207  13.260 1.00 39.75 ? 3    LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 4   ? 47.022  28.572  14.381 1.00 45.41 ? 3    LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 4   ? 45.531  28.633  14.087 1.00 50.07 ? 3    LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 4   ? 44.722  28.014  15.176 1.00 53.67 ? 3    LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 5   ? 51.826  30.953  14.216 1.00 26.47 ? 4    ALA A N   1 
ATOM   23    C  CA  . ALA A  1 5   ? 53.106  31.078  14.896 1.00 24.77 ? 4    ALA A CA  1 
ATOM   24    C  C   . ALA A  1 5   ? 52.852  31.649  16.284 1.00 25.66 ? 4    ALA A C   1 
ATOM   25    O  O   . ALA A  1 5   ? 51.779  32.195  16.550 1.00 25.99 ? 4    ALA A O   1 
ATOM   26    C  CB  . ALA A  1 5   ? 54.042  31.992  14.104 1.00 24.84 ? 4    ALA A CB  1 
ATOM   27    N  N   . VAL A  1 6   ? 53.837  31.527  17.169 1.00 25.26 ? 5    VAL A N   1 
ATOM   28    C  CA  . VAL A  1 6   ? 53.687  32.029  18.530 1.00 24.94 ? 5    VAL A CA  1 
ATOM   29    C  C   . VAL A  1 6   ? 55.043  32.419  19.109 1.00 25.77 ? 5    VAL A C   1 
ATOM   30    O  O   . VAL A  1 6   ? 56.074  31.861  18.730 1.00 24.98 ? 5    VAL A O   1 
ATOM   31    C  CB  . VAL A  1 6   ? 53.020  30.951  19.440 1.00 25.70 ? 5    VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 6   ? 53.946  29.750  19.596 1.00 26.20 ? 5    VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 6   ? 52.658  31.540  20.801 1.00 26.05 ? 5    VAL A CG2 1 
ATOM   34    N  N   . ALA A  1 7   ? 55.040  33.397  20.008 1.00 23.76 ? 6    ALA A N   1 
ATOM   35    C  CA  . ALA A  1 7   ? 56.265  33.836  20.657 1.00 23.09 ? 6    ALA A CA  1 
ATOM   36    C  C   . ALA A  1 7   ? 55.990  34.010  22.144 1.00 24.02 ? 6    ALA A C   1 
ATOM   37    O  O   . ALA A  1 7   ? 55.005  34.644  22.532 1.00 24.54 ? 6    ALA A O   1 
ATOM   38    C  CB  . ALA A  1 7   ? 56.755  35.158  20.053 1.00 22.55 ? 6    ALA A CB  1 
ATOM   39    N  N   . VAL A  1 8   ? 56.847  33.425  22.971 1.00 22.95 ? 7    VAL A N   1 
ATOM   40    C  CA  . VAL A  1 8   ? 56.705  33.536  24.414 1.00 23.86 ? 7    VAL A CA  1 
ATOM   41    C  C   . VAL A  1 8   ? 57.748  34.541  24.859 1.00 24.35 ? 7    VAL A C   1 
ATOM   42    O  O   . VAL A  1 8   ? 58.947  34.284  24.760 1.00 23.70 ? 7    VAL A O   1 
ATOM   43    C  CB  . VAL A  1 8   ? 56.949  32.182  25.104 1.00 23.71 ? 7    VAL A CB  1 
ATOM   44    C  CG1 . VAL A  1 8   ? 56.877  32.341  26.622 1.00 27.25 ? 7    VAL A CG1 1 
ATOM   45    C  CG2 . VAL A  1 8   ? 55.915  31.177  24.631 1.00 22.57 ? 7    VAL A CG2 1 
ATOM   46    N  N   . LEU A  1 9   ? 57.288  35.693  25.339 1.00 23.47 ? 8    LEU A N   1 
ATOM   47    C  CA  . LEU A  1 9   ? 58.192  36.752  25.769 1.00 24.84 ? 8    LEU A CA  1 
ATOM   48    C  C   . LEU A  1 9   ? 58.685  36.590  27.203 1.00 25.50 ? 8    LEU A C   1 
ATOM   49    O  O   . LEU A  1 9   ? 57.891  36.420  28.129 1.00 24.44 ? 8    LEU A O   1 
ATOM   50    C  CB  . LEU A  1 9   ? 57.500  38.110  25.618 1.00 27.13 ? 8    LEU A CB  1 
ATOM   51    C  CG  . LEU A  1 9   ? 56.896  38.407  24.240 1.00 29.83 ? 8    LEU A CG  1 
ATOM   52    C  CD1 . LEU A  1 9   ? 56.097  39.710  24.286 1.00 30.49 ? 8    LEU A CD1 1 
ATOM   53    C  CD2 . LEU A  1 9   ? 58.006  38.496  23.212 1.00 28.53 ? 8    LEU A CD2 1 
ATOM   54    N  N   . LYS A  1 10  ? 60.003  36.655  27.369 1.00 26.53 ? 9    LYS A N   1 
ATOM   55    C  CA  . LYS A  1 10  ? 60.643  36.543  28.677 1.00 28.64 ? 9    LYS A CA  1 
ATOM   56    C  C   . LYS A  1 10  ? 61.875  37.453  28.707 1.00 28.63 ? 9    LYS A C   1 
ATOM   57    O  O   . LYS A  1 10  ? 62.486  37.722  27.669 1.00 27.30 ? 9    LYS A O   1 
ATOM   58    C  CB  . LYS A  1 10  ? 61.051  35.086  28.948 1.00 31.53 ? 9    LYS A CB  1 
ATOM   59    C  CG  . LYS A  1 10  ? 59.866  34.133  28.967 1.00 35.57 ? 9    LYS A CG  1 
ATOM   60    C  CD  . LYS A  1 10  ? 60.258  32.690  29.252 0.00 37.94 ? 9    LYS A CD  1 
ATOM   61    C  CE  . LYS A  1 10  ? 59.017  31.803  29.334 1.00 40.84 ? 9    LYS A CE  1 
ATOM   62    N  NZ  . LYS A  1 10  ? 59.338  30.362  29.523 1.00 42.81 ? 9    LYS A NZ  1 
ATOM   63    N  N   . GLY A  1 11  ? 62.227  37.932  29.896 1.00 29.31 ? 10   GLY A N   1 
ATOM   64    C  CA  . GLY A  1 11  ? 63.379  38.807  30.040 1.00 31.11 ? 10   GLY A CA  1 
ATOM   65    C  C   . GLY A  1 11  ? 63.989  38.664  31.424 1.00 32.14 ? 10   GLY A C   1 
ATOM   66    O  O   . GLY A  1 11  ? 63.732  37.680  32.111 1.00 33.20 ? 10   GLY A O   1 
ATOM   67    N  N   . ASP A  1 12  ? 64.791  39.638  31.837 1.00 34.08 ? 11   ASP A N   1 
ATOM   68    C  CA  . ASP A  1 12  ? 65.424  39.589  33.152 1.00 37.38 ? 11   ASP A CA  1 
ATOM   69    C  C   . ASP A  1 12  ? 64.523  40.150  34.236 1.00 38.14 ? 11   ASP A C   1 
ATOM   70    O  O   . ASP A  1 12  ? 64.802  39.988  35.423 1.00 40.57 ? 11   ASP A O   1 
ATOM   71    C  CB  . ASP A  1 12  ? 66.732  40.378  33.155 1.00 38.93 ? 11   ASP A CB  1 
ATOM   72    C  CG  . ASP A  1 12  ? 67.743  39.826  32.185 1.00 41.58 ? 11   ASP A CG  1 
ATOM   73    O  OD1 . ASP A  1 12  ? 67.932  38.591  32.173 1.00 42.26 ? 11   ASP A OD1 1 
ATOM   74    O  OD2 . ASP A  1 12  ? 68.351  40.628  31.445 1.00 45.18 ? 11   ASP A OD2 1 
ATOM   75    N  N   . GLY A  1 13  ? 63.448  40.813  33.825 1.00 37.64 ? 12   GLY A N   1 
ATOM   76    C  CA  . GLY A  1 13  ? 62.534  41.401  34.784 1.00 34.10 ? 12   GLY A CA  1 
ATOM   77    C  C   . GLY A  1 13  ? 61.199  40.696  34.877 1.00 32.77 ? 12   GLY A C   1 
ATOM   78    O  O   . GLY A  1 13  ? 61.102  39.501  34.603 1.00 33.22 ? 12   GLY A O   1 
ATOM   79    N  N   . PRO A  1 14  ? 60.139  41.422  35.262 1.00 31.22 ? 13   PRO A N   1 
ATOM   80    C  CA  . PRO A  1 14  ? 58.787  40.883  35.403 1.00 30.07 ? 13   PRO A CA  1 
ATOM   81    C  C   . PRO A  1 14  ? 58.010  40.800  34.094 1.00 27.94 ? 13   PRO A C   1 
ATOM   82    O  O   . PRO A  1 14  ? 56.958  40.169  34.032 1.00 27.89 ? 13   PRO A O   1 
ATOM   83    C  CB  . PRO A  1 14  ? 58.142  41.868  36.368 1.00 29.36 ? 13   PRO A CB  1 
ATOM   84    C  CG  . PRO A  1 14  ? 58.706  43.164  35.879 1.00 29.82 ? 13   PRO A CG  1 
ATOM   85    C  CD  . PRO A  1 14  ? 60.178  42.833  35.690 1.00 30.91 ? 13   PRO A CD  1 
ATOM   86    N  N   . VAL A  1 15  ? 58.521  41.446  33.054 1.00 27.66 ? 14   VAL A N   1 
ATOM   87    C  CA  . VAL A  1 15  ? 57.821  41.462  31.775 1.00 27.37 ? 14   VAL A CA  1 
ATOM   88    C  C   . VAL A  1 15  ? 57.780  40.113  31.077 1.00 28.79 ? 14   VAL A C   1 
ATOM   89    O  O   . VAL A  1 15  ? 58.815  39.519  30.784 1.00 28.11 ? 14   VAL A O   1 
ATOM   90    C  CB  . VAL A  1 15  ? 58.437  42.502  30.824 1.00 26.24 ? 14   VAL A CB  1 
ATOM   91    C  CG1 . VAL A  1 15  ? 57.676  42.520  29.490 1.00 24.95 ? 14   VAL A CG1 1 
ATOM   92    C  CG2 . VAL A  1 15  ? 58.394  43.871  31.476 1.00 27.72 ? 14   VAL A CG2 1 
ATOM   93    N  N   . GLN A  1 16  ? 56.569  39.633  30.817 1.00 29.92 ? 15   GLN A N   1 
ATOM   94    C  CA  . GLN A  1 16  ? 56.382  38.364  30.129 1.00 32.05 ? 15   GLN A CA  1 
ATOM   95    C  C   . GLN A  1 16  ? 55.043  38.360  29.413 1.00 31.20 ? 15   GLN A C   1 
ATOM   96    O  O   . GLN A  1 16  ? 54.160  39.161  29.720 1.00 30.05 ? 15   GLN A O   1 
ATOM   97    C  CB  . GLN A  1 16  ? 56.450  37.195  31.116 1.00 34.83 ? 15   GLN A CB  1 
ATOM   98    C  CG  . GLN A  1 16  ? 55.597  37.371  32.353 1.00 38.76 ? 15   GLN A CG  1 
ATOM   99    C  CD  . GLN A  1 16  ? 55.771  36.232  33.345 1.00 41.11 ? 15   GLN A CD  1 
ATOM   100   O  OE1 . GLN A  1 16  ? 55.176  35.163  33.196 1.00 42.37 ? 15   GLN A OE1 1 
ATOM   101   N  NE2 . GLN A  1 16  ? 56.599  36.455  34.357 1.00 41.62 ? 15   GLN A NE2 1 
ATOM   102   N  N   . GLY A  1 17  ? 54.898  37.460  28.448 1.00 28.69 ? 16   GLY A N   1 
ATOM   103   C  CA  . GLY A  1 17  ? 53.651  37.385  27.717 1.00 29.69 ? 16   GLY A CA  1 
ATOM   104   C  C   . GLY A  1 17  ? 53.671  36.359  26.609 1.00 29.41 ? 16   GLY A C   1 
ATOM   105   O  O   . GLY A  1 17  ? 54.692  35.721  26.347 1.00 28.55 ? 16   GLY A O   1 
ATOM   106   N  N   . ILE A  1 18  ? 52.526  36.206  25.957 1.00 28.34 ? 17   ILE A N   1 
ATOM   107   C  CA  . ILE A  1 18  ? 52.376  35.260  24.866 1.00 29.03 ? 17   ILE A CA  1 
ATOM   108   C  C   . ILE A  1 18  ? 51.724  35.979  23.692 1.00 29.09 ? 17   ILE A C   1 
ATOM   109   O  O   . ILE A  1 18  ? 50.636  36.541  23.831 1.00 29.68 ? 17   ILE A O   1 
ATOM   110   C  CB  . ILE A  1 18  ? 51.493  34.067  25.289 1.00 29.55 ? 17   ILE A CB  1 
ATOM   111   C  CG1 . ILE A  1 18  ? 52.144  33.336  26.465 1.00 29.50 ? 17   ILE A CG1 1 
ATOM   112   C  CG2 . ILE A  1 18  ? 51.281  33.125  24.104 1.00 29.63 ? 17   ILE A CG2 1 
ATOM   113   C  CD1 . ILE A  1 18  ? 51.347  32.148  26.974 1.00 33.31 ? 17   ILE A CD1 1 
ATOM   114   N  N   . ILE A  1 19  ? 52.397  35.972  22.544 1.00 26.76 ? 18   ILE A N   1 
ATOM   115   C  CA  . ILE A  1 19  ? 51.871  36.627  21.350 1.00 25.58 ? 18   ILE A CA  1 
ATOM   116   C  C   . ILE A  1 19  ? 51.647  35.604  20.243 1.00 27.37 ? 18   ILE A C   1 
ATOM   117   O  O   . ILE A  1 19  ? 52.570  34.885  19.858 1.00 26.30 ? 18   ILE A O   1 
ATOM   118   C  CB  . ILE A  1 19  ? 52.843  37.712  20.833 1.00 25.73 ? 18   ILE A CB  1 
ATOM   119   C  CG1 . ILE A  1 19  ? 53.061  38.775  21.907 1.00 23.07 ? 18   ILE A CG1 1 
ATOM   120   C  CG2 . ILE A  1 19  ? 52.291  38.345  19.565 1.00 25.42 ? 18   ILE A CG2 1 
ATOM   121   C  CD1 . ILE A  1 19  ? 51.801  39.543  22.284 1.00 26.49 ? 18   ILE A CD1 1 
ATOM   122   N  N   . ASN A  1 20  ? 50.414  35.544  19.743 1.00 27.23 ? 19   ASN A N   1 
ATOM   123   C  CA  . ASN A  1 20  ? 50.037  34.615  18.684 1.00 27.09 ? 19   ASN A CA  1 
ATOM   124   C  C   . ASN A  1 20  ? 50.053  35.302  17.324 1.00 27.02 ? 19   ASN A C   1 
ATOM   125   O  O   . ASN A  1 20  ? 49.837  36.508  17.229 1.00 26.65 ? 19   ASN A O   1 
ATOM   126   C  CB  . ASN A  1 20  ? 48.638  34.058  18.956 1.00 28.66 ? 19   ASN A CB  1 
ATOM   127   C  CG  . ASN A  1 20  ? 48.533  33.394  20.314 1.00 31.39 ? 19   ASN A CG  1 
ATOM   128   O  OD1 . ASN A  1 20  ? 49.136  32.347  20.552 1.00 32.64 ? 19   ASN A OD1 1 
ATOM   129   N  ND2 . ASN A  1 20  ? 47.768  34.005  21.217 1.00 29.93 ? 19   ASN A ND2 1 
ATOM   130   N  N   . PHE A  1 21  ? 50.322  34.527  16.274 1.00 27.59 ? 20   PHE A N   1 
ATOM   131   C  CA  . PHE A  1 21  ? 50.360  35.045  14.903 1.00 26.69 ? 20   PHE A CA  1 
ATOM   132   C  C   . PHE A  1 21  ? 49.529  34.091  14.052 1.00 28.05 ? 20   PHE A C   1 
ATOM   133   O  O   . PHE A  1 21  ? 49.594  32.872  14.240 1.00 26.61 ? 20   PHE A O   1 
ATOM   134   C  CB  . PHE A  1 21  ? 51.791  35.042  14.332 1.00 25.77 ? 20   PHE A CB  1 
ATOM   135   C  CG  . PHE A  1 21  ? 52.767  35.925  15.065 1.00 26.04 ? 20   PHE A CG  1 
ATOM   136   C  CD1 . PHE A  1 21  ? 53.117  37.172  14.553 1.00 25.11 ? 20   PHE A CD1 1 
ATOM   137   C  CD2 . PHE A  1 21  ? 53.385  35.484  16.236 1.00 26.46 ? 20   PHE A CD2 1 
ATOM   138   C  CE1 . PHE A  1 21  ? 54.071  37.968  15.189 1.00 25.74 ? 20   PHE A CE1 1 
ATOM   139   C  CE2 . PHE A  1 21  ? 54.343  36.269  16.885 1.00 24.18 ? 20   PHE A CE2 1 
ATOM   140   C  CZ  . PHE A  1 21  ? 54.689  37.516  16.358 1.00 25.36 ? 20   PHE A CZ  1 
ATOM   141   N  N   . GLU A  1 22  ? 48.747  34.637  13.127 1.00 29.22 ? 21   GLU A N   1 
ATOM   142   C  CA  . GLU A  1 22  ? 47.945  33.812  12.232 1.00 30.19 ? 21   GLU A CA  1 
ATOM   143   C  C   . GLU A  1 22  ? 47.810  34.499  10.877 1.00 30.44 ? 21   GLU A C   1 
ATOM   144   O  O   . GLU A  1 22  ? 47.488  35.688  10.794 1.00 29.57 ? 21   GLU A O   1 
ATOM   145   C  CB  . GLU A  1 22  ? 46.557  33.529  12.821 1.00 32.67 ? 21   GLU A CB  1 
ATOM   146   C  CG  . GLU A  1 22  ? 45.699  32.646  11.916 1.00 36.07 ? 21   GLU A CG  1 
ATOM   147   C  CD  . GLU A  1 22  ? 44.539  31.979  12.637 1.00 40.27 ? 21   GLU A CD  1 
ATOM   148   O  OE1 . GLU A  1 22  ? 43.772  31.245  11.974 1.00 41.91 ? 21   GLU A OE1 1 
ATOM   149   O  OE2 . GLU A  1 22  ? 44.390  32.177  13.861 1.00 42.35 ? 21   GLU A OE2 1 
ATOM   150   N  N   . GLN A  1 23  ? 48.082  33.742  9.818  1.00 30.15 ? 22   GLN A N   1 
ATOM   151   C  CA  . GLN A  1 23  ? 48.003  34.252  8.455  1.00 30.21 ? 22   GLN A CA  1 
ATOM   152   C  C   . GLN A  1 23  ? 47.148  33.269  7.652  1.00 31.96 ? 22   GLN A C   1 
ATOM   153   O  O   . GLN A  1 23  ? 47.564  32.148  7.365  1.00 31.41 ? 22   GLN A O   1 
ATOM   154   C  CB  . GLN A  1 23  ? 49.416  34.377  7.870  1.00 28.60 ? 22   GLN A CB  1 
ATOM   155   C  CG  . GLN A  1 23  ? 49.502  34.959  6.464  1.00 28.31 ? 22   GLN A CG  1 
ATOM   156   C  CD  . GLN A  1 23  ? 50.937  35.262  6.048  1.00 25.57 ? 22   GLN A CD  1 
ATOM   157   O  OE1 . GLN A  1 23  ? 51.875  34.585  6.472  1.00 23.62 ? 22   GLN A OE1 1 
ATOM   158   N  NE2 . GLN A  1 23  ? 51.111  36.269  5.205  1.00 25.81 ? 22   GLN A NE2 1 
ATOM   159   N  N   . LYS A  1 24  ? 45.939  33.699  7.312  1.00 33.38 ? 23   LYS A N   1 
ATOM   160   C  CA  . LYS A  1 24  ? 45.000  32.861  6.577  1.00 35.34 ? 23   LYS A CA  1 
ATOM   161   C  C   . LYS A  1 24  ? 45.523  32.450  5.200  1.00 33.25 ? 23   LYS A C   1 
ATOM   162   O  O   . LYS A  1 24  ? 45.404  31.291  4.812  1.00 33.67 ? 23   LYS A O   1 
ATOM   163   C  CB  . LYS A  1 24  ? 43.661  33.591  6.437  1.00 38.72 ? 23   LYS A CB  1 
ATOM   164   C  CG  . LYS A  1 24  ? 42.548  32.737  5.862  1.00 44.74 ? 23   LYS A CG  1 
ATOM   165   C  CD  . LYS A  1 24  ? 41.250  33.530  5.745  1.00 49.29 ? 23   LYS A CD  1 
ATOM   166   C  CE  . LYS A  1 24  ? 40.128  32.669  5.183  1.00 51.61 ? 23   LYS A CE  1 
ATOM   167   N  NZ  . LYS A  1 24  ? 38.856  33.434  5.080  1.00 57.07 ? 23   LYS A NZ  1 
ATOM   168   N  N   . GLU A  1 25  ? 46.099  33.397  4.468  1.00 31.94 ? 24   GLU A N   1 
ATOM   169   C  CA  . GLU A  1 25  ? 46.645  33.119  3.141  1.00 33.72 ? 24   GLU A CA  1 
ATOM   170   C  C   . GLU A  1 25  ? 48.071  33.654  3.046  1.00 30.88 ? 24   GLU A C   1 
ATOM   171   O  O   . GLU A  1 25  ? 48.382  34.710  3.600  1.00 29.73 ? 24   GLU A O   1 
ATOM   172   C  CB  . GLU A  1 25  ? 45.767  33.765  2.066  1.00 34.26 ? 24   GLU A CB  1 
ATOM   173   C  CG  . GLU A  1 25  ? 44.320  33.277  2.083  1.00 38.26 ? 24   GLU A CG  1 
ATOM   174   C  CD  . GLU A  1 25  ? 44.189  31.793  1.771  1.00 42.02 ? 24   GLU A CD  1 
ATOM   175   O  OE1 . GLU A  1 25  ? 43.075  31.248  1.924  1.00 43.95 ? 24   GLU A OE1 1 
ATOM   176   O  OE2 . GLU A  1 25  ? 45.194  31.168  1.369  1.00 44.92 ? 24   GLU A OE2 1 
ATOM   177   N  N   . SER A  1 26  ? 48.931  32.926  2.337  1.00 29.83 ? 25   SER A N   1 
ATOM   178   C  CA  . SER A  1 26  ? 50.331  33.316  2.195  1.00 28.70 ? 25   SER A CA  1 
ATOM   179   C  C   . SER A  1 26  ? 50.525  34.738  1.685  1.00 28.34 ? 25   SER A C   1 
ATOM   180   O  O   . SER A  1 26  ? 51.543  35.363  1.971  1.00 28.60 ? 25   SER A O   1 
ATOM   181   C  CB  . SER A  1 26  ? 51.069  32.346  1.269  1.00 28.29 ? 25   SER A CB  1 
ATOM   182   O  OG  . SER A  1 26  ? 50.598  32.454  -0.060 1.00 28.29 ? 25   SER A OG  1 
ATOM   183   N  N   . ASN A  1 27  ? 49.565  35.252  0.922  1.00 26.78 ? 26   ASN A N   1 
ATOM   184   C  CA  . ASN A  1 27  ? 49.692  36.612  0.402  1.00 28.36 ? 26   ASN A CA  1 
ATOM   185   C  C   . ASN A  1 27  ? 48.727  37.540  1.128  1.00 30.49 ? 26   ASN A C   1 
ATOM   186   O  O   . ASN A  1 27  ? 48.465  38.660  0.683  1.00 32.78 ? 26   ASN A O   1 
ATOM   187   C  CB  . ASN A  1 27  ? 49.419  36.639  -1.106 1.00 27.39 ? 26   ASN A CB  1 
ATOM   188   C  CG  . ASN A  1 27  ? 47.984  36.296  -1.446 1.00 27.05 ? 26   ASN A CG  1 
ATOM   189   O  OD1 . ASN A  1 27  ? 47.392  35.388  -0.855 1.00 28.20 ? 26   ASN A OD1 1 
ATOM   190   N  ND2 . ASN A  1 27  ? 47.419  37.010  -2.418 1.00 27.66 ? 26   ASN A ND2 1 
ATOM   191   N  N   . GLY A  1 28  ? 48.206  37.057  2.254  1.00 31.83 ? 27   GLY A N   1 
ATOM   192   C  CA  . GLY A  1 28  ? 47.283  37.839  3.052  1.00 31.49 ? 27   GLY A CA  1 
ATOM   193   C  C   . GLY A  1 28  ? 47.952  38.483  4.256  1.00 31.81 ? 27   GLY A C   1 
ATOM   194   O  O   . GLY A  1 28  ? 49.145  38.281  4.505  1.00 31.29 ? 27   GLY A O   1 
ATOM   195   N  N   . PRO A  1 29  ? 47.198  39.270  5.032  1.00 31.21 ? 28   PRO A N   1 
ATOM   196   C  CA  . PRO A  1 29  ? 47.762  39.933  6.208  1.00 30.72 ? 28   PRO A CA  1 
ATOM   197   C  C   . PRO A  1 29  ? 47.930  38.982  7.385  1.00 29.05 ? 28   PRO A C   1 
ATOM   198   O  O   . PRO A  1 29  ? 47.346  37.897  7.415  1.00 28.56 ? 28   PRO A O   1 
ATOM   199   C  CB  . PRO A  1 29  ? 46.749  41.037  6.488  1.00 31.29 ? 28   PRO A CB  1 
ATOM   200   C  CG  . PRO A  1 29  ? 45.452  40.375  6.125  1.00 33.93 ? 28   PRO A CG  1 
ATOM   201   C  CD  . PRO A  1 29  ? 45.792  39.664  4.824  1.00 30.83 ? 28   PRO A CD  1 
ATOM   202   N  N   . VAL A  1 30  ? 48.739  39.395  8.352  1.00 29.03 ? 29   VAL A N   1 
ATOM   203   C  CA  . VAL A  1 30  ? 48.975  38.586  9.539  1.00 27.19 ? 29   VAL A CA  1 
ATOM   204   C  C   . VAL A  1 30  ? 48.306  39.226  10.753 1.00 28.34 ? 29   VAL A C   1 
ATOM   205   O  O   . VAL A  1 30  ? 48.480  40.418  11.011 1.00 29.26 ? 29   VAL A O   1 
ATOM   206   C  CB  . VAL A  1 30  ? 50.489  38.450  9.840  1.00 26.05 ? 29   VAL A CB  1 
ATOM   207   C  CG1 . VAL A  1 30  ? 50.698  37.735  11.173 1.00 23.01 ? 29   VAL A CG1 1 
ATOM   208   C  CG2 . VAL A  1 30  ? 51.181  37.688  8.718  1.00 24.17 ? 29   VAL A CG2 1 
ATOM   209   N  N   . LYS A  1 31  ? 47.537  38.431  11.488 1.00 28.74 ? 30   LYS A N   1 
ATOM   210   C  CA  . LYS A  1 31  ? 46.888  38.923  12.692 1.00 30.20 ? 30   LYS A CA  1 
ATOM   211   C  C   . LYS A  1 31  ? 47.802  38.591  13.863 1.00 29.84 ? 30   LYS A C   1 
ATOM   212   O  O   . LYS A  1 31  ? 48.302  37.468  13.970 1.00 28.32 ? 30   LYS A O   1 
ATOM   213   C  CB  . LYS A  1 31  ? 45.524  38.262  12.879 1.00 31.95 ? 30   LYS A CB  1 
ATOM   214   C  CG  . LYS A  1 31  ? 44.483  38.735  11.873 1.00 38.89 ? 30   LYS A CG  1 
ATOM   215   C  CD  . LYS A  1 31  ? 43.133  38.070  12.099 1.00 42.94 ? 30   LYS A CD  1 
ATOM   216   C  CE  . LYS A  1 31  ? 42.079  38.638  11.155 1.00 46.06 ? 30   LYS A CE  1 
ATOM   217   N  NZ  . LYS A  1 31  ? 40.758  37.972  11.333 1.00 47.30 ? 30   LYS A NZ  1 
ATOM   218   N  N   . VAL A  1 32  ? 48.024  39.579  14.723 1.00 28.72 ? 31   VAL A N   1 
ATOM   219   C  CA  . VAL A  1 32  ? 48.885  39.435  15.894 1.00 28.68 ? 31   VAL A CA  1 
ATOM   220   C  C   . VAL A  1 32  ? 48.057  39.769  17.136 1.00 29.88 ? 31   VAL A C   1 
ATOM   221   O  O   . VAL A  1 32  ? 47.467  40.847  17.211 1.00 29.83 ? 31   VAL A O   1 
ATOM   222   C  CB  . VAL A  1 32  ? 50.072  40.419  15.820 1.00 27.55 ? 31   VAL A CB  1 
ATOM   223   C  CG1 . VAL A  1 32  ? 51.048  40.158  16.963 1.00 28.49 ? 31   VAL A CG1 1 
ATOM   224   C  CG2 . VAL A  1 32  ? 50.770  40.297  14.471 1.00 29.27 ? 31   VAL A CG2 1 
ATOM   225   N  N   . TRP A  1 33  ? 48.013  38.859  18.105 1.00 27.53 ? 32   TRP A N   1 
ATOM   226   C  CA  . TRP A  1 33  ? 47.237  39.107  19.312 1.00 26.60 ? 32   TRP A CA  1 
ATOM   227   C  C   . TRP A  1 33  ? 47.742  38.319  20.510 1.00 28.12 ? 32   TRP A C   1 
ATOM   228   O  O   . TRP A  1 33  ? 48.349  37.251  20.364 1.00 26.73 ? 32   TRP A O   1 
ATOM   229   C  CB  . TRP A  1 33  ? 45.766  38.766  19.065 1.00 29.96 ? 32   TRP A CB  1 
ATOM   230   C  CG  . TRP A  1 33  ? 45.464  37.304  19.136 1.00 32.36 ? 32   TRP A CG  1 
ATOM   231   C  CD1 . TRP A  1 33  ? 45.005  36.614  20.224 1.00 34.14 ? 32   TRP A CD1 1 
ATOM   232   C  CD2 . TRP A  1 33  ? 45.614  36.344  18.088 1.00 33.68 ? 32   TRP A CD2 1 
ATOM   233   N  NE1 . TRP A  1 33  ? 44.859  35.284  19.916 1.00 34.57 ? 32   TRP A NE1 1 
ATOM   234   C  CE2 . TRP A  1 33  ? 45.228  35.089  18.607 1.00 33.97 ? 32   TRP A CE2 1 
ATOM   235   C  CE3 . TRP A  1 33  ? 46.044  36.419  16.753 1.00 35.09 ? 32   TRP A CE3 1 
ATOM   236   C  CZ2 . TRP A  1 33  ? 45.253  33.917  17.846 1.00 35.02 ? 32   TRP A CZ2 1 
ATOM   237   C  CZ3 . TRP A  1 33  ? 46.070  35.252  15.992 1.00 35.47 ? 32   TRP A CZ3 1 
ATOM   238   C  CH2 . TRP A  1 33  ? 45.677  34.018  16.543 1.00 37.10 ? 32   TRP A CH2 1 
ATOM   239   N  N   . GLY A  1 34  ? 47.471  38.855  21.695 1.00 26.76 ? 33   GLY A N   1 
ATOM   240   C  CA  . GLY A  1 34  ? 47.885  38.216  22.926 1.00 26.65 ? 33   GLY A CA  1 
ATOM   241   C  C   . GLY A  1 34  ? 47.957  39.249  24.035 1.00 29.34 ? 33   GLY A C   1 
ATOM   242   O  O   . GLY A  1 34  ? 47.267  40.270  23.993 1.00 28.13 ? 33   GLY A O   1 
ATOM   243   N  N   . SER A  1 35  ? 48.798  38.999  25.029 1.00 29.50 ? 34   SER A N   1 
ATOM   244   C  CA  . SER A  1 35  ? 48.934  39.938  26.129 1.00 30.43 ? 34   SER A CA  1 
ATOM   245   C  C   . SER A  1 35  ? 50.323  39.882  26.740 1.00 30.77 ? 34   SER A C   1 
ATOM   246   O  O   . SER A  1 35  ? 51.005  38.853  26.687 1.00 30.06 ? 34   SER A O   1 
ATOM   247   C  CB  . SER A  1 35  ? 47.886  39.652  27.205 1.00 32.12 ? 34   SER A CB  1 
ATOM   248   O  OG  . SER A  1 35  ? 48.044  38.347  27.728 1.00 36.52 ? 34   SER A OG  1 
ATOM   249   N  N   . ILE A  1 36  ? 50.728  41.009  27.308 1.00 28.27 ? 35   ILE A N   1 
ATOM   250   C  CA  . ILE A  1 36  ? 52.023  41.153  27.950 1.00 27.72 ? 35   ILE A CA  1 
ATOM   251   C  C   . ILE A  1 36  ? 51.749  41.830  29.290 1.00 29.64 ? 35   ILE A C   1 
ATOM   252   O  O   . ILE A  1 36  ? 50.953  42.772  29.357 1.00 29.37 ? 35   ILE A O   1 
ATOM   253   C  CB  . ILE A  1 36  ? 52.946  42.067  27.134 1.00 25.65 ? 35   ILE A CB  1 
ATOM   254   C  CG1 . ILE A  1 36  ? 53.035  41.567  25.689 1.00 26.89 ? 35   ILE A CG1 1 
ATOM   255   C  CG2 . ILE A  1 36  ? 54.332  42.109  27.766 1.00 23.61 ? 35   ILE A CG2 1 
ATOM   256   C  CD1 . ILE A  1 36  ? 53.825  42.484  24.783 1.00 22.68 ? 35   ILE A CD1 1 
ATOM   257   N  N   . LYS A  1 37  ? 52.388  41.351  30.351 1.00 29.57 ? 36   LYS A N   1 
ATOM   258   C  CA  . LYS A  1 37  ? 52.195  41.944  31.668 1.00 28.68 ? 36   LYS A CA  1 
ATOM   259   C  C   . LYS A  1 37  ? 53.534  42.343  32.271 1.00 27.98 ? 36   LYS A C   1 
ATOM   260   O  O   . LYS A  1 37  ? 54.595  41.976  31.751 1.00 25.25 ? 36   LYS A O   1 
ATOM   261   C  CB  . LYS A  1 37  ? 51.465  40.961  32.589 1.00 30.22 ? 36   LYS A CB  1 
ATOM   262   C  CG  . LYS A  1 37  ? 52.171  39.630  32.784 1.00 32.70 ? 36   LYS A CG  1 
ATOM   263   C  CD  . LYS A  1 37  ? 51.300  38.664  33.572 1.00 33.80 ? 36   LYS A CD  1 
ATOM   264   C  CE  . LYS A  1 37  ? 52.010  37.336  33.791 1.00 33.20 ? 36   LYS A CE  1 
ATOM   265   N  NZ  . LYS A  1 37  ? 51.158  36.367  34.526 1.00 33.27 ? 36   LYS A NZ  1 
ATOM   266   N  N   . GLY A  1 38  ? 53.482  43.109  33.358 1.00 25.34 ? 37   GLY A N   1 
ATOM   267   C  CA  . GLY A  1 38  ? 54.700  43.545  34.019 1.00 23.98 ? 37   GLY A CA  1 
ATOM   268   C  C   . GLY A  1 38  ? 55.282  44.814  33.435 1.00 24.72 ? 37   GLY A C   1 
ATOM   269   O  O   . GLY A  1 38  ? 56.412  45.185  33.745 1.00 25.07 ? 37   GLY A O   1 
ATOM   270   N  N   . LEU A  1 39  ? 54.512  45.489  32.586 1.00 24.75 ? 38   LEU A N   1 
ATOM   271   C  CA  . LEU A  1 39  ? 54.964  46.725  31.957 1.00 24.99 ? 38   LEU A CA  1 
ATOM   272   C  C   . LEU A  1 39  ? 54.503  47.960  32.725 1.00 26.98 ? 38   LEU A C   1 
ATOM   273   O  O   . LEU A  1 39  ? 53.514  47.919  33.456 1.00 28.82 ? 38   LEU A O   1 
ATOM   274   C  CB  . LEU A  1 39  ? 54.409  46.825  30.531 1.00 25.52 ? 38   LEU A CB  1 
ATOM   275   C  CG  . LEU A  1 39  ? 54.855  45.792  29.490 1.00 25.57 ? 38   LEU A CG  1 
ATOM   276   C  CD1 . LEU A  1 39  ? 53.898  45.814  28.316 1.00 22.55 ? 38   LEU A CD1 1 
ATOM   277   C  CD2 . LEU A  1 39  ? 56.278  46.102  29.041 1.00 23.12 ? 38   LEU A CD2 1 
ATOM   278   N  N   . THR A  1 40  ? 55.230  49.057  32.555 1.00 28.42 ? 39   THR A N   1 
ATOM   279   C  CA  . THR A  1 40  ? 54.840  50.309  33.179 1.00 31.63 ? 39   THR A CA  1 
ATOM   280   C  C   . THR A  1 40  ? 53.717  50.828  32.286 1.00 33.14 ? 39   THR A C   1 
ATOM   281   O  O   . THR A  1 40  ? 53.740  50.619  31.070 1.00 29.51 ? 39   THR A O   1 
ATOM   282   C  CB  . THR A  1 40  ? 55.988  51.336  33.182 1.00 31.96 ? 39   THR A CB  1 
ATOM   283   O  OG1 . THR A  1 40  ? 56.479  51.510  31.847 1.00 31.40 ? 39   THR A OG1 1 
ATOM   284   C  CG2 . THR A  1 40  ? 57.122  50.867  34.088 1.00 31.04 ? 39   THR A CG2 1 
ATOM   285   N  N   . GLU A  1 41  ? 52.728  51.483  32.885 1.00 33.42 ? 40   GLU A N   1 
ATOM   286   C  CA  . GLU A  1 41  ? 51.602  52.019  32.129 1.00 33.93 ? 40   GLU A CA  1 
ATOM   287   C  C   . GLU A  1 41  ? 52.085  52.873  30.958 1.00 32.51 ? 40   GLU A C   1 
ATOM   288   O  O   . GLU A  1 41  ? 53.040  53.635  31.092 1.00 32.73 ? 40   GLU A O   1 
ATOM   289   C  CB  . GLU A  1 41  ? 50.715  52.859  33.056 1.00 36.27 ? 40   GLU A CB  1 
ATOM   290   C  CG  . GLU A  1 41  ? 49.488  53.459  32.389 1.00 37.02 ? 40   GLU A CG  1 
ATOM   291   C  CD  . GLU A  1 41  ? 48.652  54.292  33.350 1.00 39.70 ? 40   GLU A CD  1 
ATOM   292   O  OE1 . GLU A  1 41  ? 47.573  54.767  32.938 1.00 40.59 ? 40   GLU A OE1 1 
ATOM   293   O  OE2 . GLU A  1 41  ? 49.074  54.470  34.515 1.00 39.31 ? 40   GLU A OE2 1 
ATOM   294   N  N   . GLY A  1 42  ? 51.438  52.739  29.803 1.00 32.63 ? 41   GLY A N   1 
ATOM   295   C  CA  . GLY A  1 42  ? 51.844  53.537  28.657 1.00 32.34 ? 41   GLY A CA  1 
ATOM   296   C  C   . GLY A  1 42  ? 52.337  52.754  27.453 1.00 32.36 ? 41   GLY A C   1 
ATOM   297   O  O   . GLY A  1 42  ? 52.210  51.530  27.401 1.00 31.56 ? 41   GLY A O   1 
ATOM   298   N  N   . LEU A  1 43  ? 52.921  53.471  26.496 1.00 32.47 ? 42   LEU A N   1 
ATOM   299   C  CA  . LEU A  1 43  ? 53.424  52.880  25.256 1.00 32.38 ? 42   LEU A CA  1 
ATOM   300   C  C   . LEU A  1 43  ? 54.782  52.184  25.358 1.00 30.83 ? 42   LEU A C   1 
ATOM   301   O  O   . LEU A  1 43  ? 55.681  52.635  26.065 1.00 28.18 ? 42   LEU A O   1 
ATOM   302   C  CB  . LEU A  1 43  ? 53.501  53.951  24.159 1.00 34.53 ? 42   LEU A CB  1 
ATOM   303   C  CG  . LEU A  1 43  ? 52.202  54.671  23.770 1.00 37.98 ? 42   LEU A CG  1 
ATOM   304   C  CD1 . LEU A  1 43  ? 52.497  55.647  22.644 1.00 39.18 ? 42   LEU A CD1 1 
ATOM   305   C  CD2 . LEU A  1 43  ? 51.143  53.668  23.338 1.00 39.67 ? 42   LEU A CD2 1 
ATOM   306   N  N   . HIS A  1 44  ? 54.921  51.091  24.612 1.00 29.62 ? 43   HIS A N   1 
ATOM   307   C  CA  . HIS A  1 44  ? 56.150  50.309  24.589 1.00 27.53 ? 43   HIS A CA  1 
ATOM   308   C  C   . HIS A  1 44  ? 56.445  49.796  23.176 1.00 27.15 ? 43   HIS A C   1 
ATOM   309   O  O   . HIS A  1 44  ? 55.573  49.206  22.537 1.00 28.38 ? 43   HIS A O   1 
ATOM   310   C  CB  . HIS A  1 44  ? 56.016  49.125  25.548 1.00 27.33 ? 43   HIS A CB  1 
ATOM   311   C  CG  . HIS A  1 44  ? 55.933  49.522  26.991 1.00 26.56 ? 43   HIS A CG  1 
ATOM   312   N  ND1 . HIS A  1 44  ? 57.037  49.915  27.717 1.00 26.88 ? 43   HIS A ND1 1 
ATOM   313   C  CD2 . HIS A  1 44  ? 54.881  49.595  27.837 1.00 27.04 ? 43   HIS A CD2 1 
ATOM   314   C  CE1 . HIS A  1 44  ? 56.667  50.210  28.951 1.00 26.12 ? 43   HIS A CE1 1 
ATOM   315   N  NE2 . HIS A  1 44  ? 55.364  50.025  29.052 1.00 26.30 ? 43   HIS A NE2 1 
ATOM   316   N  N   . GLY A  1 45  ? 57.670  50.029  22.701 1.00 26.26 ? 44   GLY A N   1 
ATOM   317   C  CA  . GLY A  1 45  ? 58.079  49.568  21.379 1.00 27.03 ? 44   GLY A CA  1 
ATOM   318   C  C   . GLY A  1 45  ? 57.829  48.075  21.220 1.00 27.78 ? 44   GLY A C   1 
ATOM   319   O  O   . GLY A  1 45  ? 57.978  47.313  22.177 1.00 26.63 ? 44   GLY A O   1 
ATOM   320   N  N   . PHE A  1 46  ? 57.483  47.659  20.004 1.00 27.15 ? 45   PHE A N   1 
ATOM   321   C  CA  . PHE A  1 46  ? 57.142  46.271  19.702 1.00 25.02 ? 45   PHE A CA  1 
ATOM   322   C  C   . PHE A  1 46  ? 57.643  45.967  18.281 1.00 27.32 ? 45   PHE A C   1 
ATOM   323   O  O   . PHE A  1 46  ? 57.056  46.443  17.303 1.00 26.43 ? 45   PHE A O   1 
ATOM   324   C  CB  . PHE A  1 46  ? 55.620  46.158  19.774 1.00 25.34 ? 45   PHE A CB  1 
ATOM   325   C  CG  . PHE A  1 46  ? 55.085  44.754  19.798 1.00 25.78 ? 45   PHE A CG  1 
ATOM   326   C  CD1 . PHE A  1 46  ? 55.448  43.867  20.803 1.00 24.99 ? 45   PHE A CD1 1 
ATOM   327   C  CD2 . PHE A  1 46  ? 54.117  44.361  18.879 1.00 26.75 ? 45   PHE A CD2 1 
ATOM   328   C  CE1 . PHE A  1 46  ? 54.847  42.608  20.898 1.00 25.18 ? 45   PHE A CE1 1 
ATOM   329   C  CE2 . PHE A  1 46  ? 53.512  43.108  18.965 1.00 27.88 ? 45   PHE A CE2 1 
ATOM   330   C  CZ  . PHE A  1 46  ? 53.878  42.230  19.983 1.00 27.56 ? 45   PHE A CZ  1 
ATOM   331   N  N   . HIS A  1 47  ? 58.723  45.192  18.158 1.00 25.16 ? 46   HIS A N   1 
ATOM   332   C  CA  . HIS A  1 47  ? 59.271  44.886  16.833 1.00 25.12 ? 46   HIS A CA  1 
ATOM   333   C  C   . HIS A  1 47  ? 59.848  43.493  16.685 1.00 25.97 ? 46   HIS A C   1 
ATOM   334   O  O   . HIS A  1 47  ? 60.150  42.812  17.673 1.00 26.68 ? 46   HIS A O   1 
ATOM   335   C  CB  . HIS A  1 47  ? 60.402  45.853  16.463 1.00 25.74 ? 46   HIS A CB  1 
ATOM   336   C  CG  . HIS A  1 47  ? 60.296  47.201  17.099 1.00 30.78 ? 46   HIS A CG  1 
ATOM   337   N  ND1 . HIS A  1 47  ? 61.127  47.610  18.123 1.00 28.98 ? 46   HIS A ND1 1 
ATOM   338   C  CD2 . HIS A  1 47  ? 59.478  48.250  16.843 1.00 30.86 ? 46   HIS A CD2 1 
ATOM   339   C  CE1 . HIS A  1 47  ? 60.828  48.846  18.464 1.00 30.01 ? 46   HIS A CE1 1 
ATOM   340   N  NE2 . HIS A  1 47  ? 59.828  49.260  17.701 1.00 28.02 ? 46   HIS A NE2 1 
ATOM   341   N  N   . VAL A  1 48  ? 60.014  43.084  15.432 1.00 23.58 ? 47   VAL A N   1 
ATOM   342   C  CA  . VAL A  1 48  ? 60.626  41.806  15.135 1.00 24.07 ? 47   VAL A CA  1 
ATOM   343   C  C   . VAL A  1 48  ? 62.074  42.127  14.794 1.00 24.95 ? 47   VAL A C   1 
ATOM   344   O  O   . VAL A  1 48  ? 62.340  42.886  13.858 1.00 24.73 ? 47   VAL A O   1 
ATOM   345   C  CB  . VAL A  1 48  ? 59.992  41.106  13.911 1.00 22.52 ? 47   VAL A CB  1 
ATOM   346   C  CG1 . VAL A  1 48  ? 60.739  39.802  13.628 1.00 22.88 ? 47   VAL A CG1 1 
ATOM   347   C  CG2 . VAL A  1 48  ? 58.521  40.811  14.173 1.00 21.13 ? 47   VAL A CG2 1 
ATOM   348   N  N   . HIS A  1 49  ? 63.004  41.579  15.569 1.00 24.48 ? 48   HIS A N   1 
ATOM   349   C  CA  . HIS A  1 49  ? 64.417  41.797  15.314 1.00 24.72 ? 48   HIS A CA  1 
ATOM   350   C  C   . HIS A  1 49  ? 64.927  40.658  14.444 1.00 24.47 ? 48   HIS A C   1 
ATOM   351   O  O   . HIS A  1 49  ? 64.407  39.546  14.498 1.00 25.02 ? 48   HIS A O   1 
ATOM   352   C  CB  . HIS A  1 49  ? 65.195  41.889  16.627 1.00 24.46 ? 48   HIS A CB  1 
ATOM   353   C  CG  . HIS A  1 49  ? 64.978  43.180  17.358 1.00 27.39 ? 48   HIS A CG  1 
ATOM   354   N  ND1 . HIS A  1 49  ? 66.015  43.964  17.806 1.00 28.14 ? 48   HIS A ND1 1 
ATOM   355   C  CD2 . HIS A  1 49  ? 63.837  43.831  17.692 1.00 24.81 ? 48   HIS A CD2 1 
ATOM   356   C  CE1 . HIS A  1 49  ? 65.527  45.050  18.385 1.00 27.46 ? 48   HIS A CE1 1 
ATOM   357   N  NE2 . HIS A  1 49  ? 64.208  44.992  18.328 1.00 28.08 ? 48   HIS A NE2 1 
ATOM   358   N  N   . GLU A  1 50  ? 65.948  40.949  13.649 1.00 24.90 ? 49   GLU A N   1 
ATOM   359   C  CA  . GLU A  1 50  ? 66.523  40.003  12.698 1.00 25.20 ? 49   GLU A CA  1 
ATOM   360   C  C   . GLU A  1 50  ? 66.866  38.577  13.134 1.00 24.74 ? 49   GLU A C   1 
ATOM   361   O  O   . GLU A  1 50  ? 66.475  37.626  12.461 1.00 25.63 ? 49   GLU A O   1 
ATOM   362   C  CB  . GLU A  1 50  ? 67.764  40.624  12.039 1.00 27.24 ? 49   GLU A CB  1 
ATOM   363   C  CG  . GLU A  1 50  ? 68.315  39.796  10.884 1.00 28.95 ? 49   GLU A CG  1 
ATOM   364   C  CD  . GLU A  1 50  ? 69.424  40.495  10.120 1.00 31.41 ? 49   GLU A CD  1 
ATOM   365   O  OE1 . GLU A  1 50  ? 69.891  39.929  9.113  1.00 33.51 ? 49   GLU A OE1 1 
ATOM   366   O  OE2 . GLU A  1 50  ? 69.833  41.601  10.523 1.00 32.02 ? 49   GLU A OE2 1 
ATOM   367   N  N   . PHE A  1 51  ? 67.579  38.413  14.243 1.00 23.25 ? 50   PHE A N   1 
ATOM   368   C  CA  . PHE A  1 51  ? 67.980  37.074  14.664 1.00 24.28 ? 50   PHE A CA  1 
ATOM   369   C  C   . PHE A  1 51  ? 67.208  36.408  15.794 1.00 25.26 ? 50   PHE A C   1 
ATOM   370   O  O   . PHE A  1 51  ? 66.859  37.041  16.791 1.00 27.65 ? 50   PHE A O   1 
ATOM   371   C  CB  . PHE A  1 51  ? 69.470  37.087  15.021 1.00 24.30 ? 50   PHE A CB  1 
ATOM   372   C  CG  . PHE A  1 51  ? 70.331  37.703  13.959 1.00 26.90 ? 50   PHE A CG  1 
ATOM   373   C  CD1 . PHE A  1 51  ? 70.421  37.118  12.699 1.00 28.94 ? 50   PHE A CD1 1 
ATOM   374   C  CD2 . PHE A  1 51  ? 71.003  38.901  14.194 1.00 27.76 ? 50   PHE A CD2 1 
ATOM   375   C  CE1 . PHE A  1 51  ? 71.164  37.720  11.683 1.00 28.31 ? 50   PHE A CE1 1 
ATOM   376   C  CE2 . PHE A  1 51  ? 71.750  39.512  13.182 1.00 26.38 ? 50   PHE A CE2 1 
ATOM   377   C  CZ  . PHE A  1 51  ? 71.827  38.920  11.929 1.00 26.96 ? 50   PHE A CZ  1 
ATOM   378   N  N   . GLY A  1 52  ? 66.952  35.114  15.634 1.00 23.76 ? 51   GLY A N   1 
ATOM   379   C  CA  . GLY A  1 52  ? 66.265  34.363  16.672 1.00 22.14 ? 51   GLY A CA  1 
ATOM   380   C  C   . GLY A  1 52  ? 67.344  33.789  17.572 1.00 22.25 ? 51   GLY A C   1 
ATOM   381   O  O   . GLY A  1 52  ? 67.378  32.592  17.852 1.00 21.86 ? 51   GLY A O   1 
ATOM   382   N  N   . ASP A  1 53  ? 68.236  34.665  18.025 1.00 22.05 ? 52   ASP A N   1 
ATOM   383   C  CA  . ASP A  1 53  ? 69.366  34.276  18.865 1.00 20.82 ? 52   ASP A CA  1 
ATOM   384   C  C   . ASP A  1 53  ? 69.206  34.830  20.277 1.00 22.03 ? 52   ASP A C   1 
ATOM   385   O  O   . ASP A  1 53  ? 69.342  36.031  20.513 1.00 21.47 ? 52   ASP A O   1 
ATOM   386   C  CB  . ASP A  1 53  ? 70.651  34.793  18.213 1.00 21.28 ? 52   ASP A CB  1 
ATOM   387   C  CG  . ASP A  1 53  ? 71.901  34.382  18.952 1.00 19.83 ? 52   ASP A CG  1 
ATOM   388   O  OD1 . ASP A  1 53  ? 72.955  34.299  18.288 1.00 25.50 ? 52   ASP A OD1 1 
ATOM   389   O  OD2 . ASP A  1 53  ? 71.847  34.154  20.180 1.00 22.26 ? 52   ASP A OD2 1 
ATOM   390   N  N   . ASN A  1 54  ? 68.920  33.940  21.216 1.00 22.65 ? 53   ASN A N   1 
ATOM   391   C  CA  . ASN A  1 54  ? 68.714  34.334  22.603 1.00 24.95 ? 53   ASN A CA  1 
ATOM   392   C  C   . ASN A  1 54  ? 69.911  33.961  23.486 1.00 24.14 ? 53   ASN A C   1 
ATOM   393   O  O   . ASN A  1 54  ? 69.785  33.927  24.711 1.00 24.84 ? 53   ASN A O   1 
ATOM   394   C  CB  . ASN A  1 54  ? 67.445  33.649  23.127 1.00 25.71 ? 53   ASN A CB  1 
ATOM   395   C  CG  . ASN A  1 54  ? 66.932  34.259  24.418 1.00 29.80 ? 53   ASN A CG  1 
ATOM   396   O  OD1 . ASN A  1 54  ? 66.612  33.545  25.368 1.00 31.19 ? 53   ASN A OD1 1 
ATOM   397   N  ND2 . ASN A  1 54  ? 66.834  35.585  24.452 1.00 31.93 ? 53   ASN A ND2 1 
ATOM   398   N  N   . THR A  1 55  ? 71.069  33.702  22.879 1.00 23.01 ? 54   THR A N   1 
ATOM   399   C  CA  . THR A  1 55  ? 72.249  33.305  23.656 1.00 24.45 ? 54   THR A CA  1 
ATOM   400   C  C   . THR A  1 55  ? 72.697  34.373  24.654 1.00 24.43 ? 54   THR A C   1 
ATOM   401   O  O   . THR A  1 55  ? 73.286  34.063  25.694 1.00 23.66 ? 54   THR A O   1 
ATOM   402   C  CB  . THR A  1 55  ? 73.446  32.913  22.738 1.00 23.49 ? 54   THR A CB  1 
ATOM   403   O  OG1 . THR A  1 55  ? 73.860  34.037  21.956 1.00 23.53 ? 54   THR A OG1 1 
ATOM   404   C  CG2 . THR A  1 55  ? 73.043  31.777  21.803 1.00 23.32 ? 54   THR A CG2 1 
ATOM   405   N  N   . ALA A  1 56  ? 72.414  35.628  24.334 1.00 24.05 ? 55   ALA A N   1 
ATOM   406   C  CA  . ALA A  1 56  ? 72.746  36.747  25.207 1.00 24.33 ? 55   ALA A CA  1 
ATOM   407   C  C   . ALA A  1 56  ? 71.432  37.448  25.566 1.00 26.05 ? 55   ALA A C   1 
ATOM   408   O  O   . ALA A  1 56  ? 71.364  38.676  25.642 1.00 27.07 ? 55   ALA A O   1 
ATOM   409   C  CB  . ALA A  1 56  ? 73.683  37.711  24.486 1.00 23.22 ? 55   ALA A CB  1 
ATOM   410   N  N   . GLY A  1 57  ? 70.384  36.663  25.791 1.00 25.42 ? 56   GLY A N   1 
ATOM   411   C  CA  . GLY A  1 57  ? 69.094  37.254  26.097 1.00 26.00 ? 56   GLY A CA  1 
ATOM   412   C  C   . GLY A  1 57  ? 68.580  37.982  24.862 1.00 26.94 ? 56   GLY A C   1 
ATOM   413   O  O   . GLY A  1 57  ? 68.822  37.541  23.739 1.00 27.03 ? 56   GLY A O   1 
ATOM   414   N  N   . CYS A  1 58  ? 67.884  39.099  25.049 1.00 25.45 ? 57   CYS A N   1 
ATOM   415   C  CA  . CYS A  1 58  ? 67.358  39.852  23.908 1.00 26.19 ? 57   CYS A CA  1 
ATOM   416   C  C   . CYS A  1 58  ? 68.457  40.614  23.172 1.00 25.50 ? 57   CYS A C   1 
ATOM   417   O  O   . CYS A  1 58  ? 68.286  41.031  22.026 1.00 25.15 ? 57   CYS A O   1 
ATOM   418   C  CB  . CYS A  1 58  ? 66.281  40.832  24.380 1.00 26.45 ? 57   CYS A CB  1 
ATOM   419   S  SG  . CYS A  1 58  ? 65.005  39.986  25.352 1.00 28.36 ? 57   CYS A SG  1 
ATOM   420   N  N   . THR A  1 59  ? 69.595  40.773  23.835 1.00 25.94 ? 58   THR A N   1 
ATOM   421   C  CA  . THR A  1 59  ? 70.723  41.498  23.270 1.00 27.46 ? 58   THR A CA  1 
ATOM   422   C  C   . THR A  1 59  ? 71.304  40.889  21.987 1.00 27.46 ? 58   THR A C   1 
ATOM   423   O  O   . THR A  1 59  ? 71.795  41.608  21.121 1.00 29.51 ? 58   THR A O   1 
ATOM   424   C  CB  . THR A  1 59  ? 71.841  41.622  24.322 1.00 29.53 ? 58   THR A CB  1 
ATOM   425   O  OG1 . THR A  1 59  ? 71.288  42.155  25.535 1.00 31.17 ? 58   THR A OG1 1 
ATOM   426   C  CG2 . THR A  1 59  ? 72.932  42.551  23.831 1.00 33.98 ? 58   THR A CG2 1 
ATOM   427   N  N   . SER A  1 60  ? 71.242  39.569  21.857 1.00 24.06 ? 59   SER A N   1 
ATOM   428   C  CA  . SER A  1 60  ? 71.789  38.907  20.675 1.00 23.59 ? 59   SER A CA  1 
ATOM   429   C  C   . SER A  1 60  ? 70.841  38.881  19.478 1.00 23.24 ? 59   SER A C   1 
ATOM   430   O  O   . SER A  1 60  ? 71.202  38.391  18.409 1.00 20.88 ? 59   SER A O   1 
ATOM   431   C  CB  . SER A  1 60  ? 72.208  37.480  21.040 1.00 21.62 ? 59   SER A CB  1 
ATOM   432   O  OG  . SER A  1 60  ? 71.290  36.906  21.956 1.00 24.23 ? 59   SER A OG  1 
ATOM   433   N  N   . ALA A  1 61  ? 69.637  39.422  19.650 1.00 22.67 ? 60   ALA A N   1 
ATOM   434   C  CA  . ALA A  1 61  ? 68.646  39.431  18.573 1.00 23.92 ? 60   ALA A CA  1 
ATOM   435   C  C   . ALA A  1 61  ? 69.028  40.338  17.411 1.00 23.89 ? 60   ALA A C   1 
ATOM   436   O  O   . ALA A  1 61  ? 68.436  40.261  16.334 1.00 23.73 ? 60   ALA A O   1 
ATOM   437   C  CB  . ALA A  1 61  ? 67.281  39.838  19.119 1.00 22.20 ? 60   ALA A CB  1 
ATOM   438   N  N   . GLY A  1 62  ? 70.017  41.196  17.623 1.00 23.44 ? 61   GLY A N   1 
ATOM   439   C  CA  . GLY A  1 62  ? 70.429  42.091  16.562 1.00 23.70 ? 61   GLY A CA  1 
ATOM   440   C  C   . GLY A  1 62  ? 69.449  43.234  16.378 1.00 24.53 ? 61   GLY A C   1 
ATOM   441   O  O   . GLY A  1 62  ? 68.592  43.455  17.235 1.00 26.28 ? 61   GLY A O   1 
ATOM   442   N  N   . PRO A  1 63  ? 69.543  43.977  15.266 1.00 25.01 ? 62   PRO A N   1 
ATOM   443   C  CA  . PRO A  1 63  ? 68.643  45.107  15.001 1.00 24.90 ? 62   PRO A CA  1 
ATOM   444   C  C   . PRO A  1 63  ? 67.276  44.688  14.464 1.00 26.65 ? 62   PRO A C   1 
ATOM   445   O  O   . PRO A  1 63  ? 66.972  43.499  14.362 1.00 25.83 ? 62   PRO A O   1 
ATOM   446   C  CB  . PRO A  1 63  ? 69.433  45.936  13.996 1.00 25.66 ? 62   PRO A CB  1 
ATOM   447   C  CG  . PRO A  1 63  ? 70.108  44.856  13.166 1.00 26.83 ? 62   PRO A CG  1 
ATOM   448   C  CD  . PRO A  1 63  ? 70.573  43.858  14.216 1.00 24.81 ? 62   PRO A CD  1 
ATOM   449   N  N   . HIS A  1 64  ? 66.446  45.673  14.136 1.00 24.89 ? 63   HIS A N   1 
ATOM   450   C  CA  . HIS A  1 64  ? 65.121  45.392  13.603 1.00 24.86 ? 63   HIS A CA  1 
ATOM   451   C  C   . HIS A  1 64  ? 65.261  44.654  12.269 1.00 25.63 ? 63   HIS A C   1 
ATOM   452   O  O   . HIS A  1 64  ? 66.166  44.947  11.484 1.00 24.76 ? 63   HIS A O   1 
ATOM   453   C  CB  . HIS A  1 64  ? 64.345  46.702  13.387 1.00 25.20 ? 63   HIS A CB  1 
ATOM   454   C  CG  . HIS A  1 64  ? 64.085  47.465  14.647 1.00 27.34 ? 63   HIS A CG  1 
ATOM   455   N  ND1 . HIS A  1 64  ? 63.385  48.658  14.666 1.00 28.50 ? 63   HIS A ND1 1 
ATOM   456   C  CD2 . HIS A  1 64  ? 64.434  47.225  15.931 1.00 28.42 ? 63   HIS A CD2 1 
ATOM   457   C  CE1 . HIS A  1 64  ? 63.321  49.111  15.899 1.00 27.98 ? 63   HIS A CE1 1 
ATOM   458   N  NE2 . HIS A  1 64  ? 63.952  48.259  16.693 1.00 31.03 ? 63   HIS A NE2 1 
ATOM   459   N  N   . PHE A  1 65  ? 64.383  43.683  12.029 1.00 25.42 ? 64   PHE A N   1 
ATOM   460   C  CA  . PHE A  1 65  ? 64.404  42.926  10.778 1.00 25.74 ? 64   PHE A CA  1 
ATOM   461   C  C   . PHE A  1 65  ? 64.200  43.958  9.672  1.00 27.54 ? 64   PHE A C   1 
ATOM   462   O  O   . PHE A  1 65  ? 63.162  44.616  9.626  1.00 25.95 ? 64   PHE A O   1 
ATOM   463   C  CB  . PHE A  1 65  ? 63.265  41.913  10.766 1.00 25.93 ? 64   PHE A CB  1 
ATOM   464   C  CG  . PHE A  1 65  ? 63.243  41.032  9.548  1.00 26.30 ? 64   PHE A CG  1 
ATOM   465   C  CD1 . PHE A  1 65  ? 62.030  40.646  8.986  1.00 24.60 ? 64   PHE A CD1 1 
ATOM   466   C  CD2 . PHE A  1 65  ? 64.431  40.576  8.971  1.00 26.47 ? 64   PHE A CD2 1 
ATOM   467   C  CE1 . PHE A  1 65  ? 61.989  39.806  7.870  1.00 27.39 ? 64   PHE A CE1 1 
ATOM   468   C  CE2 . PHE A  1 65  ? 64.404  39.733  7.850  1.00 27.91 ? 64   PHE A CE2 1 
ATOM   469   C  CZ  . PHE A  1 65  ? 63.177  39.352  7.296  1.00 26.84 ? 64   PHE A CZ  1 
ATOM   470   N  N   . ASN A  1 66  ? 65.182  44.086  8.780  1.00 28.58 ? 65   ASN A N   1 
ATOM   471   C  CA  . ASN A  1 66  ? 65.134  45.092  7.720  1.00 30.71 ? 65   ASN A CA  1 
ATOM   472   C  C   . ASN A  1 66  ? 65.707  44.575  6.391  1.00 30.94 ? 65   ASN A C   1 
ATOM   473   O  O   . ASN A  1 66  ? 66.709  45.088  5.890  1.00 29.99 ? 65   ASN A O   1 
ATOM   474   C  CB  . ASN A  1 66  ? 65.916  46.318  8.216  1.00 31.46 ? 65   ASN A CB  1 
ATOM   475   C  CG  . ASN A  1 66  ? 65.868  47.489  7.259  1.00 32.53 ? 65   ASN A CG  1 
ATOM   476   O  OD1 . ASN A  1 66  ? 64.885  47.696  6.552  1.00 33.26 ? 65   ASN A OD1 1 
ATOM   477   N  ND2 . ASN A  1 66  ? 66.931  48.289  7.261  1.00 33.55 ? 65   ASN A ND2 1 
ATOM   478   N  N   . PRO A  1 67  ? 65.060  43.561  5.796  1.00 31.74 ? 66   PRO A N   1 
ATOM   479   C  CA  . PRO A  1 67  ? 65.521  42.986  4.528  1.00 34.30 ? 66   PRO A CA  1 
ATOM   480   C  C   . PRO A  1 67  ? 65.509  43.949  3.341  1.00 35.35 ? 66   PRO A C   1 
ATOM   481   O  O   . PRO A  1 67  ? 66.266  43.768  2.390  1.00 37.62 ? 66   PRO A O   1 
ATOM   482   C  CB  . PRO A  1 67  ? 64.578  41.800  4.328  1.00 33.08 ? 66   PRO A CB  1 
ATOM   483   C  CG  . PRO A  1 67  ? 63.311  42.289  4.937  1.00 32.80 ? 66   PRO A CG  1 
ATOM   484   C  CD  . PRO A  1 67  ? 63.791  42.940  6.216  1.00 31.83 ? 66   PRO A CD  1 
ATOM   485   N  N   . LEU A  1 68  ? 64.663  44.970  3.393  1.00 35.62 ? 67   LEU A N   1 
ATOM   486   C  CA  . LEU A  1 68  ? 64.588  45.932  2.300  1.00 36.95 ? 67   LEU A CA  1 
ATOM   487   C  C   . LEU A  1 68  ? 65.503  47.135  2.512  1.00 38.28 ? 67   LEU A C   1 
ATOM   488   O  O   . LEU A  1 68  ? 65.485  48.086  1.733  1.00 38.67 ? 67   LEU A O   1 
ATOM   489   C  CB  . LEU A  1 68  ? 63.142  46.397  2.110  1.00 38.03 ? 67   LEU A CB  1 
ATOM   490   C  CG  . LEU A  1 68  ? 62.145  45.255  1.882  1.00 38.64 ? 67   LEU A CG  1 
ATOM   491   C  CD1 . LEU A  1 68  ? 60.788  45.831  1.494  1.00 39.50 ? 67   LEU A CD1 1 
ATOM   492   C  CD2 . LEU A  1 68  ? 62.661  44.331  0.793  1.00 37.60 ? 67   LEU A CD2 1 
ATOM   493   N  N   . SER A  1 69  ? 66.305  47.083  3.571  1.00 39.45 ? 68   SER A N   1 
ATOM   494   C  CA  . SER A  1 69  ? 67.244  48.154  3.891  1.00 41.50 ? 68   SER A CA  1 
ATOM   495   C  C   . SER A  1 69  ? 66.620  49.547  3.911  1.00 41.32 ? 68   SER A C   1 
ATOM   496   O  O   . SER A  1 69  ? 67.086  50.453  3.224  1.00 41.62 ? 68   SER A O   1 
ATOM   497   C  CB  . SER A  1 69  ? 68.410  48.140  2.900  1.00 42.31 ? 68   SER A CB  1 
ATOM   498   O  OG  . SER A  1 69  ? 69.140  46.929  2.988  1.00 45.01 ? 68   SER A OG  1 
ATOM   499   N  N   . ARG A  1 70  ? 65.567  49.720  4.700  1.00 41.28 ? 69   ARG A N   1 
ATOM   500   C  CA  . ARG A  1 70  ? 64.916  51.019  4.796  1.00 42.08 ? 69   ARG A CA  1 
ATOM   501   C  C   . ARG A  1 70  ? 65.110  51.606  6.186  1.00 41.68 ? 69   ARG A C   1 
ATOM   502   O  O   . ARG A  1 70  ? 65.676  50.958  7.066  1.00 41.61 ? 69   ARG A O   1 
ATOM   503   C  CB  . ARG A  1 70  ? 63.426  50.887  4.486  1.00 43.51 ? 69   ARG A CB  1 
ATOM   504   C  CG  . ARG A  1 70  ? 63.150  50.483  3.053  1.00 47.58 ? 69   ARG A CG  1 
ATOM   505   C  CD  . ARG A  1 70  ? 61.667  50.463  2.757  1.00 51.29 ? 69   ARG A CD  1 
ATOM   506   N  NE  . ARG A  1 70  ? 61.403  50.093  1.370  1.00 53.53 ? 69   ARG A NE  1 
ATOM   507   C  CZ  . ARG A  1 70  ? 60.190  49.889  0.870  1.00 54.69 ? 69   ARG A CZ  1 
ATOM   508   N  NH1 . ARG A  1 70  ? 60.048  49.552  -0.405 1.00 54.93 ? 69   ARG A NH1 1 
ATOM   509   N  NH2 . ARG A  1 70  ? 59.120  50.023  1.643  1.00 54.81 ? 69   ARG A NH2 1 
ATOM   510   N  N   . LYS A  1 71  ? 64.658  52.839  6.378  1.00 41.26 ? 70   LYS A N   1 
ATOM   511   C  CA  . LYS A  1 71  ? 64.783  53.489  7.676  1.00 41.98 ? 70   LYS A CA  1 
ATOM   512   C  C   . LYS A  1 71  ? 63.630  53.076  8.580  1.00 40.11 ? 70   LYS A C   1 
ATOM   513   O  O   . LYS A  1 71  ? 62.551  52.722  8.101  1.00 38.74 ? 70   LYS A O   1 
ATOM   514   C  CB  . LYS A  1 71  ? 64.793  55.014  7.522  1.00 44.02 ? 70   LYS A CB  1 
ATOM   515   C  CG  . LYS A  1 71  ? 66.047  55.568  6.860  1.00 47.94 ? 70   LYS A CG  1 
ATOM   516   C  CD  . LYS A  1 71  ? 66.086  57.091  6.935  1.00 51.48 ? 70   LYS A CD  1 
ATOM   517   C  CE  . LYS A  1 71  ? 67.377  57.641  6.340  1.00 54.19 ? 70   LYS A CE  1 
ATOM   518   N  NZ  . LYS A  1 71  ? 67.504  59.117  6.531  1.00 56.59 ? 70   LYS A NZ  1 
ATOM   519   N  N   . HIS A  1 72  ? 63.869  53.115  9.888  1.00 38.59 ? 71   HIS A N   1 
ATOM   520   C  CA  . HIS A  1 72  ? 62.846  52.758  10.862 1.00 39.34 ? 71   HIS A CA  1 
ATOM   521   C  C   . HIS A  1 72  ? 61.634  53.667  10.696 1.00 38.30 ? 71   HIS A C   1 
ATOM   522   O  O   . HIS A  1 72  ? 61.770  54.825  10.307 1.00 39.40 ? 71   HIS A O   1 
ATOM   523   C  CB  . HIS A  1 72  ? 63.393  52.903  12.285 1.00 39.16 ? 71   HIS A CB  1 
ATOM   524   C  CG  . HIS A  1 72  ? 62.380  52.621  13.349 1.00 39.28 ? 71   HIS A CG  1 
ATOM   525   N  ND1 . HIS A  1 72  ? 61.880  51.361  13.585 1.00 39.98 ? 71   HIS A ND1 1 
ATOM   526   C  CD2 . HIS A  1 72  ? 61.751  53.448  14.218 1.00 39.66 ? 71   HIS A CD2 1 
ATOM   527   C  CE1 . HIS A  1 72  ? 60.985  51.419  14.556 1.00 40.04 ? 71   HIS A CE1 1 
ATOM   528   N  NE2 . HIS A  1 72  ? 60.887  52.673  14.957 1.00 39.58 ? 71   HIS A NE2 1 
ATOM   529   N  N   . GLY A  1 73  ? 60.453  53.137  10.997 1.00 37.84 ? 72   GLY A N   1 
ATOM   530   C  CA  . GLY A  1 73  ? 59.234  53.914  10.884 1.00 37.15 ? 72   GLY A CA  1 
ATOM   531   C  C   . GLY A  1 73  ? 58.089  53.225  11.603 1.00 37.85 ? 72   GLY A C   1 
ATOM   532   O  O   . GLY A  1 73  ? 58.300  52.250  12.326 1.00 38.12 ? 72   GLY A O   1 
ATOM   533   N  N   . GLY A  1 74  ? 56.876  53.737  11.416 1.00 36.89 ? 73   GLY A N   1 
ATOM   534   C  CA  . GLY A  1 74  ? 55.714  53.138  12.044 1.00 36.26 ? 73   GLY A CA  1 
ATOM   535   C  C   . GLY A  1 74  ? 55.182  52.026  11.160 1.00 36.78 ? 73   GLY A C   1 
ATOM   536   O  O   . GLY A  1 74  ? 55.450  52.019  9.957  1.00 37.46 ? 73   GLY A O   1 
ATOM   537   N  N   . PRO A  1 75  ? 54.418  51.075  11.711 1.00 35.86 ? 74   PRO A N   1 
ATOM   538   C  CA  . PRO A  1 75  ? 53.895  49.988  10.880 1.00 36.71 ? 74   PRO A CA  1 
ATOM   539   C  C   . PRO A  1 75  ? 53.104  50.466  9.662  1.00 39.63 ? 74   PRO A C   1 
ATOM   540   O  O   . PRO A  1 75  ? 53.094  49.806  8.620  1.00 38.49 ? 74   PRO A O   1 
ATOM   541   C  CB  . PRO A  1 75  ? 53.044  49.184  11.862 1.00 34.81 ? 74   PRO A CB  1 
ATOM   542   C  CG  . PRO A  1 75  ? 52.593  50.218  12.849 1.00 34.41 ? 74   PRO A CG  1 
ATOM   543   C  CD  . PRO A  1 75  ? 53.847  51.022  13.068 1.00 36.94 ? 74   PRO A CD  1 
ATOM   544   N  N   . LYS A  1 76  ? 52.459  51.621  9.788  1.00 41.04 ? 75   LYS A N   1 
ATOM   545   C  CA  . LYS A  1 76  ? 51.668  52.160  8.690  1.00 44.45 ? 75   LYS A CA  1 
ATOM   546   C  C   . LYS A  1 76  ? 52.417  53.140  7.790  1.00 45.99 ? 75   LYS A C   1 
ATOM   547   O  O   . LYS A  1 76  ? 51.812  53.802  6.948  1.00 46.68 ? 75   LYS A O   1 
ATOM   548   C  CB  . LYS A  1 76  ? 50.396  52.805  9.240  1.00 44.88 ? 75   LYS A CB  1 
ATOM   549   C  CG  . LYS A  1 76  ? 49.505  51.807  9.957  1.00 45.60 ? 75   LYS A CG  1 
ATOM   550   C  CD  . LYS A  1 76  ? 49.228  50.614  9.052  1.00 47.02 ? 75   LYS A CD  1 
ATOM   551   C  CE  . LYS A  1 76  ? 48.478  49.508  9.771  1.00 47.01 ? 75   LYS A CE  1 
ATOM   552   N  NZ  . LYS A  1 76  ? 48.217  48.354  8.858  1.00 46.62 ? 75   LYS A NZ  1 
ATOM   553   N  N   . ASP A  1 77  ? 53.731  53.230  7.965  1.00 47.50 ? 76   ASP A N   1 
ATOM   554   C  CA  . ASP A  1 77  ? 54.546  54.109  7.135  1.00 49.20 ? 76   ASP A CA  1 
ATOM   555   C  C   . ASP A  1 77  ? 55.053  53.314  5.939  1.00 50.12 ? 76   ASP A C   1 
ATOM   556   O  O   . ASP A  1 77  ? 55.368  52.129  6.058  1.00 49.46 ? 76   ASP A O   1 
ATOM   557   C  CB  . ASP A  1 77  ? 55.747  54.644  7.917  1.00 50.83 ? 76   ASP A CB  1 
ATOM   558   C  CG  . ASP A  1 77  ? 55.350  55.575  9.041  1.00 52.11 ? 76   ASP A CG  1 
ATOM   559   O  OD1 . ASP A  1 77  ? 56.253  56.030  9.776  1.00 53.01 ? 76   ASP A OD1 1 
ATOM   560   O  OD2 . ASP A  1 77  ? 54.141  55.854  9.189  1.00 54.26 ? 76   ASP A OD2 1 
ATOM   561   N  N   . GLU A  1 78  ? 55.129  53.964  4.785  1.00 50.67 ? 77   GLU A N   1 
ATOM   562   C  CA  . GLU A  1 78  ? 55.615  53.298  3.588  1.00 51.86 ? 77   GLU A CA  1 
ATOM   563   C  C   . GLU A  1 78  ? 57.084  52.970  3.843  1.00 50.42 ? 77   GLU A C   1 
ATOM   564   O  O   . GLU A  1 78  ? 57.551  51.869  3.550  1.00 50.41 ? 77   GLU A O   1 
ATOM   565   C  CB  . GLU A  1 78  ? 55.457  54.225  2.376  1.00 54.98 ? 77   GLU A CB  1 
ATOM   566   C  CG  . GLU A  1 78  ? 55.523  53.518  1.028  1.00 59.57 ? 77   GLU A CG  1 
ATOM   567   C  CD  . GLU A  1 78  ? 56.937  53.182  0.604  1.00 62.22 ? 77   GLU A CD  1 
ATOM   568   O  OE1 . GLU A  1 78  ? 57.097  52.418  -0.374 1.00 64.25 ? 77   GLU A OE1 1 
ATOM   569   O  OE2 . GLU A  1 78  ? 57.890  53.688  1.237  1.00 64.52 ? 77   GLU A OE2 1 
ATOM   570   N  N   . GLU A  1 79  ? 57.800  53.934  4.413  1.00 48.62 ? 78   GLU A N   1 
ATOM   571   C  CA  . GLU A  1 79  ? 59.210  53.768  4.740  1.00 47.58 ? 78   GLU A CA  1 
ATOM   572   C  C   . GLU A  1 79  ? 59.326  53.163  6.141  1.00 46.54 ? 78   GLU A C   1 
ATOM   573   O  O   . GLU A  1 79  ? 59.033  53.829  7.137  1.00 45.91 ? 78   GLU A O   1 
ATOM   574   C  CB  . GLU A  1 79  ? 59.917  55.126  4.711  1.00 49.49 ? 78   GLU A CB  1 
ATOM   575   C  CG  . GLU A  1 79  ? 61.406  55.070  5.021  1.00 52.43 ? 78   GLU A CG  1 
ATOM   576   C  CD  . GLU A  1 79  ? 62.207  54.377  3.932  1.00 54.71 ? 78   GLU A CD  1 
ATOM   577   O  OE1 . GLU A  1 79  ? 63.440  54.242  4.093  1.00 53.97 ? 78   GLU A OE1 1 
ATOM   578   O  OE2 . GLU A  1 79  ? 61.606  53.970  2.913  1.00 56.76 ? 78   GLU A OE2 1 
ATOM   579   N  N   . ARG A  1 80  ? 59.744  51.902  6.219  1.00 43.80 ? 79   ARG A N   1 
ATOM   580   C  CA  . ARG A  1 80  ? 59.886  51.236  7.511  1.00 41.53 ? 79   ARG A CA  1 
ATOM   581   C  C   . ARG A  1 80  ? 60.572  49.885  7.409  1.00 40.15 ? 79   ARG A C   1 
ATOM   582   O  O   . ARG A  1 80  ? 60.719  49.328  6.320  1.00 38.45 ? 79   ARG A O   1 
ATOM   583   C  CB  . ARG A  1 80  ? 58.514  51.041  8.160  1.00 41.42 ? 79   ARG A CB  1 
ATOM   584   C  CG  . ARG A  1 80  ? 57.555  50.163  7.359  1.00 42.61 ? 79   ARG A CG  1 
ATOM   585   C  CD  . ARG A  1 80  ? 57.324  48.816  8.029  1.00 42.97 ? 79   ARG A CD  1 
ATOM   586   N  NE  . ARG A  1 80  ? 55.900  48.536  8.195  1.00 42.30 ? 79   ARG A NE  1 
ATOM   587   C  CZ  . ARG A  1 80  ? 55.402  47.424  8.729  1.00 39.36 ? 79   ARG A CZ  1 
ATOM   588   N  NH1 . ARG A  1 80  ? 54.090  47.275  8.831  1.00 37.23 ? 79   ARG A NH1 1 
ATOM   589   N  NH2 . ARG A  1 80  ? 56.207  46.462  9.157  1.00 38.41 ? 79   ARG A NH2 1 
ATOM   590   N  N   . HIS A  1 81  ? 60.992  49.370  8.561  1.00 37.38 ? 80   HIS A N   1 
ATOM   591   C  CA  . HIS A  1 81  ? 61.634  48.066  8.641  1.00 35.56 ? 80   HIS A CA  1 
ATOM   592   C  C   . HIS A  1 81  ? 60.507  47.051  8.599  1.00 33.76 ? 80   HIS A C   1 
ATOM   593   O  O   . HIS A  1 81  ? 59.420  47.311  9.118  1.00 34.41 ? 80   HIS A O   1 
ATOM   594   C  CB  . HIS A  1 81  ? 62.385  47.918  9.968  1.00 33.47 ? 80   HIS A CB  1 
ATOM   595   C  CG  . HIS A  1 81  ? 63.512  48.894  10.147 1.00 33.68 ? 80   HIS A CG  1 
ATOM   596   N  ND1 . HIS A  1 81  ? 63.871  49.390  11.371 1.00 32.15 ? 80   HIS A ND1 1 
ATOM   597   C  CD2 . HIS A  1 81  ? 64.372  49.421  9.243  1.00 31.49 ? 80   HIS A CD2 1 
ATOM   598   C  CE1 . HIS A  1 81  ? 64.920  50.193  11.225 1.00 32.88 ? 80   HIS A CE1 1 
ATOM   599   N  NE2 . HIS A  1 81  ? 65.239  50.225  9.951  1.00 31.92 ? 80   HIS A NE2 1 
ATOM   600   N  N   . VAL A  1 82  ? 60.750  45.898  7.987  1.00 31.78 ? 81   VAL A N   1 
ATOM   601   C  CA  . VAL A  1 82  ? 59.716  44.875  7.934  1.00 28.75 ? 81   VAL A CA  1 
ATOM   602   C  C   . VAL A  1 82  ? 59.281  44.528  9.359  1.00 28.24 ? 81   VAL A C   1 
ATOM   603   O  O   . VAL A  1 82  ? 58.108  44.266  9.606  1.00 29.05 ? 81   VAL A O   1 
ATOM   604   C  CB  . VAL A  1 82  ? 60.224  43.598  7.221  1.00 29.33 ? 81   VAL A CB  1 
ATOM   605   C  CG1 . VAL A  1 82  ? 59.289  42.432  7.495  1.00 26.84 ? 81   VAL A CG1 1 
ATOM   606   C  CG2 . VAL A  1 82  ? 60.309  43.847  5.717  1.00 30.71 ? 81   VAL A CG2 1 
ATOM   607   N  N   . GLY A  1 83  ? 60.228  44.553  10.296 1.00 27.87 ? 82   GLY A N   1 
ATOM   608   C  CA  . GLY A  1 83  ? 59.913  44.221  11.678 1.00 27.77 ? 82   GLY A CA  1 
ATOM   609   C  C   . GLY A  1 83  ? 59.251  45.293  12.539 1.00 29.20 ? 82   GLY A C   1 
ATOM   610   O  O   . GLY A  1 83  ? 58.944  45.039  13.708 1.00 26.69 ? 82   GLY A O   1 
ATOM   611   N  N   . ASP A  1 84  ? 59.008  46.478  11.982 1.00 28.87 ? 83   ASP A N   1 
ATOM   612   C  CA  . ASP A  1 84  ? 58.395  47.563  12.756 1.00 29.27 ? 83   ASP A CA  1 
ATOM   613   C  C   . ASP A  1 84  ? 56.892  47.418  12.994 1.00 29.04 ? 83   ASP A C   1 
ATOM   614   O  O   . ASP A  1 84  ? 56.085  47.675  12.099 1.00 29.14 ? 83   ASP A O   1 
ATOM   615   C  CB  . ASP A  1 84  ? 58.663  48.921  12.090 1.00 27.69 ? 83   ASP A CB  1 
ATOM   616   C  CG  . ASP A  1 84  ? 60.140  49.274  12.045 1.00 30.20 ? 83   ASP A CG  1 
ATOM   617   O  OD1 . ASP A  1 84  ? 60.908  48.808  12.918 1.00 26.68 ? 83   ASP A OD1 1 
ATOM   618   O  OD2 . ASP A  1 84  ? 60.533  50.042  11.140 1.00 31.63 ? 83   ASP A OD2 1 
ATOM   619   N  N   . LEU A  1 85  ? 56.516  47.022  14.208 1.00 28.18 ? 84   LEU A N   1 
ATOM   620   C  CA  . LEU A  1 85  ? 55.108  46.855  14.551 1.00 28.50 ? 84   LEU A CA  1 
ATOM   621   C  C   . LEU A  1 85  ? 54.594  47.927  15.522 1.00 29.27 ? 84   LEU A C   1 
ATOM   622   O  O   . LEU A  1 85  ? 53.570  47.742  16.180 1.00 30.39 ? 84   LEU A O   1 
ATOM   623   C  CB  . LEU A  1 85  ? 54.861  45.453  15.123 1.00 27.39 ? 84   LEU A CB  1 
ATOM   624   C  CG  . LEU A  1 85  ? 55.205  44.298  14.167 1.00 28.84 ? 84   LEU A CG  1 
ATOM   625   C  CD1 . LEU A  1 85  ? 54.940  42.971  14.853 1.00 26.98 ? 84   LEU A CD1 1 
ATOM   626   C  CD2 . LEU A  1 85  ? 54.372  44.407  12.891 1.00 28.00 ? 84   LEU A CD2 1 
ATOM   627   N  N   . GLY A  1 86  ? 55.321  49.038  15.615 1.00 28.81 ? 85   GLY A N   1 
ATOM   628   C  CA  . GLY A  1 86  ? 54.902  50.143  16.462 1.00 30.04 ? 85   GLY A CA  1 
ATOM   629   C  C   . GLY A  1 86  ? 54.969  50.010  17.972 1.00 29.79 ? 85   GLY A C   1 
ATOM   630   O  O   . GLY A  1 86  ? 55.988  49.592  18.523 1.00 30.13 ? 85   GLY A O   1 
ATOM   631   N  N   . ASN A  1 87  ? 53.871  50.378  18.634 1.00 28.64 ? 86   ASN A N   1 
ATOM   632   C  CA  . ASN A  1 87  ? 53.765  50.336  20.093 1.00 30.25 ? 86   ASN A CA  1 
ATOM   633   C  C   . ASN A  1 87  ? 52.578  49.530  20.592 1.00 30.46 ? 86   ASN A C   1 
ATOM   634   O  O   . ASN A  1 87  ? 51.545  49.445  19.928 1.00 30.91 ? 86   ASN A O   1 
ATOM   635   C  CB  . ASN A  1 87  ? 53.588  51.749  20.668 1.00 30.17 ? 86   ASN A CB  1 
ATOM   636   C  CG  . ASN A  1 87  ? 54.811  52.611  20.515 1.00 30.59 ? 86   ASN A CG  1 
ATOM   637   O  OD1 . ASN A  1 87  ? 55.859  52.335  21.098 1.00 31.87 ? 86   ASN A OD1 1 
ATOM   638   N  ND2 . ASN A  1 87  ? 54.684  53.680  19.735 1.00 31.05 ? 86   ASN A ND2 1 
ATOM   639   N  N   . VAL A  1 88  ? 52.734  48.939  21.772 1.00 29.71 ? 87   VAL A N   1 
ATOM   640   C  CA  . VAL A  1 88  ? 51.638  48.225  22.404 1.00 30.05 ? 87   VAL A CA  1 
ATOM   641   C  C   . VAL A  1 88  ? 51.366  49.139  23.598 1.00 30.10 ? 87   VAL A C   1 
ATOM   642   O  O   . VAL A  1 88  ? 52.235  49.923  23.980 1.00 29.61 ? 87   VAL A O   1 
ATOM   643   C  CB  . VAL A  1 88  ? 52.036  46.796  22.871 1.00 30.06 ? 87   VAL A CB  1 
ATOM   644   C  CG1 . VAL A  1 88  ? 52.355  45.930  21.655 1.00 30.39 ? 87   VAL A CG1 1 
ATOM   645   C  CG2 . VAL A  1 88  ? 53.223  46.850  23.818 1.00 29.33 ? 87   VAL A CG2 1 
ATOM   646   N  N   . THR A  1 89  ? 50.173  49.066  24.170 1.00 30.20 ? 88   THR A N   1 
ATOM   647   C  CA  . THR A  1 89  ? 49.832  49.934  25.294 1.00 30.61 ? 88   THR A CA  1 
ATOM   648   C  C   . THR A  1 89  ? 49.501  49.176  26.573 1.00 28.30 ? 88   THR A C   1 
ATOM   649   O  O   . THR A  1 89  ? 48.586  48.359  26.599 1.00 29.16 ? 88   THR A O   1 
ATOM   650   C  CB  . THR A  1 89  ? 48.620  50.833  24.947 1.00 31.96 ? 88   THR A CB  1 
ATOM   651   O  OG1 . THR A  1 89  ? 48.913  51.597  23.773 1.00 32.96 ? 88   THR A OG1 1 
ATOM   652   C  CG2 . THR A  1 89  ? 48.311  51.784  26.104 1.00 33.59 ? 88   THR A CG2 1 
ATOM   653   N  N   . ALA A  1 90  ? 50.250  49.453  27.634 1.00 28.26 ? 89   ALA A N   1 
ATOM   654   C  CA  . ALA A  1 90  ? 50.012  48.804  28.918 1.00 28.18 ? 89   ALA A CA  1 
ATOM   655   C  C   . ALA A  1 90  ? 49.038  49.655  29.733 1.00 28.65 ? 89   ALA A C   1 
ATOM   656   O  O   . ALA A  1 90  ? 49.194  50.873  29.804 1.00 28.18 ? 89   ALA A O   1 
ATOM   657   C  CB  . ALA A  1 90  ? 51.319  48.652  29.674 1.00 26.14 ? 89   ALA A CB  1 
ATOM   658   N  N   . ASP A  1 91  ? 48.043  49.016  30.344 1.00 30.65 ? 90   ASP A N   1 
ATOM   659   C  CA  . ASP A  1 91  ? 47.065  49.737  31.157 1.00 32.79 ? 90   ASP A CA  1 
ATOM   660   C  C   . ASP A  1 91  ? 47.626  50.023  32.554 1.00 34.22 ? 90   ASP A C   1 
ATOM   661   O  O   . ASP A  1 91  ? 48.789  49.726  32.835 1.00 33.96 ? 90   ASP A O   1 
ATOM   662   C  CB  . ASP A  1 91  ? 45.754  48.943  31.254 1.00 32.08 ? 90   ASP A CB  1 
ATOM   663   C  CG  . ASP A  1 91  ? 45.906  47.628  32.004 1.00 33.91 ? 90   ASP A CG  1 
ATOM   664   O  OD1 . ASP A  1 91  ? 44.955  46.814  31.952 1.00 31.61 ? 90   ASP A OD1 1 
ATOM   665   O  OD2 . ASP A  1 91  ? 46.957  47.406  32.650 1.00 33.17 ? 90   ASP A OD2 1 
ATOM   666   N  N   . LYS A  1 92  ? 46.797  50.595  33.424 1.00 33.73 ? 91   LYS A N   1 
ATOM   667   C  CA  . LYS A  1 92  ? 47.226  50.944  34.776 1.00 34.84 ? 91   LYS A CA  1 
ATOM   668   C  C   . LYS A  1 92  ? 47.706  49.739  35.577 1.00 34.18 ? 91   LYS A C   1 
ATOM   669   O  O   . LYS A  1 92  ? 48.489  49.878  36.514 1.00 35.96 ? 91   LYS A O   1 
ATOM   670   C  CB  . LYS A  1 92  ? 46.085  51.639  35.531 1.00 35.48 ? 91   LYS A CB  1 
ATOM   671   C  CG  . LYS A  1 92  ? 44.889  50.743  35.825 1.00 36.76 ? 91   LYS A CG  1 
ATOM   672   C  CD  . LYS A  1 92  ? 43.821  51.492  36.621 1.00 40.31 ? 91   LYS A CD  1 
ATOM   673   C  CE  . LYS A  1 92  ? 42.661  50.582  36.988 0.00 39.52 ? 91   LYS A CE  1 
ATOM   674   N  NZ  . LYS A  1 92  ? 41.639  51.293  37.805 0.00 40.11 ? 91   LYS A NZ  1 
ATOM   675   N  N   . ASP A  1 93  ? 47.226  48.557  35.214 1.00 32.73 ? 92   ASP A N   1 
ATOM   676   C  CA  . ASP A  1 93  ? 47.622  47.342  35.903 1.00 32.69 ? 92   ASP A CA  1 
ATOM   677   C  C   . ASP A  1 93  ? 48.881  46.718  35.297 1.00 31.32 ? 92   ASP A C   1 
ATOM   678   O  O   . ASP A  1 93  ? 49.278  45.617  35.674 1.00 28.43 ? 92   ASP A O   1 
ATOM   679   C  CB  . ASP A  1 93  ? 46.464  46.351  35.887 1.00 36.70 ? 92   ASP A CB  1 
ATOM   680   C  CG  . ASP A  1 93  ? 45.318  46.797  36.774 1.00 41.94 ? 92   ASP A CG  1 
ATOM   681   O  OD1 . ASP A  1 93  ? 44.159  46.432  36.491 1.00 44.62 ? 92   ASP A OD1 1 
ATOM   682   O  OD2 . ASP A  1 93  ? 45.584  47.511  37.766 1.00 44.25 ? 92   ASP A OD2 1 
ATOM   683   N  N   . GLY A  1 94  ? 49.503  47.435  34.365 1.00 29.32 ? 93   GLY A N   1 
ATOM   684   C  CA  . GLY A  1 94  ? 50.720  46.954  33.734 1.00 30.12 ? 93   GLY A CA  1 
ATOM   685   C  C   . GLY A  1 94  ? 50.511  45.900  32.665 1.00 30.15 ? 93   GLY A C   1 
ATOM   686   O  O   . GLY A  1 94  ? 51.457  45.226  32.257 1.00 30.85 ? 93   GLY A O   1 
ATOM   687   N  N   . VAL A  1 95  ? 49.275  45.765  32.201 1.00 28.70 ? 94   VAL A N   1 
ATOM   688   C  CA  . VAL A  1 95  ? 48.937  44.785  31.179 1.00 29.49 ? 94   VAL A CA  1 
ATOM   689   C  C   . VAL A  1 95  ? 48.607  45.433  29.838 1.00 30.11 ? 94   VAL A C   1 
ATOM   690   O  O   . VAL A  1 95  ? 47.801  46.361  29.760 1.00 30.21 ? 94   VAL A O   1 
ATOM   691   C  CB  . VAL A  1 95  ? 47.719  43.940  31.590 1.00 30.29 ? 94   VAL A CB  1 
ATOM   692   C  CG1 . VAL A  1 95  ? 47.352  42.986  30.459 1.00 32.77 ? 94   VAL A CG1 1 
ATOM   693   C  CG2 . VAL A  1 95  ? 48.016  43.174  32.865 1.00 30.93 ? 94   VAL A CG2 1 
ATOM   694   N  N   . ALA A  1 96  ? 49.240  44.938  28.783 1.00 30.22 ? 95   ALA A N   1 
ATOM   695   C  CA  . ALA A  1 96  ? 48.996  45.444  27.443 1.00 30.99 ? 95   ALA A CA  1 
ATOM   696   C  C   . ALA A  1 96  ? 48.343  44.324  26.655 1.00 32.81 ? 95   ALA A C   1 
ATOM   697   O  O   . ALA A  1 96  ? 48.949  43.272  26.442 1.00 34.65 ? 95   ALA A O   1 
ATOM   698   C  CB  . ALA A  1 96  ? 50.303  45.850  26.785 1.00 30.75 ? 95   ALA A CB  1 
ATOM   699   N  N   . ASP A  1 97  ? 47.097  44.528  26.249 1.00 33.93 ? 96   ASP A N   1 
ATOM   700   C  CA  . ASP A  1 97  ? 46.402  43.522  25.460 1.00 35.61 ? 96   ASP A CA  1 
ATOM   701   C  C   . ASP A  1 97  ? 46.667  43.866  24.000 1.00 35.40 ? 96   ASP A C   1 
ATOM   702   O  O   . ASP A  1 97  ? 46.318  44.950  23.528 1.00 34.64 ? 96   ASP A O   1 
ATOM   703   C  CB  . ASP A  1 97  ? 44.910  43.531  25.789 1.00 40.29 ? 96   ASP A CB  1 
ATOM   704   C  CG  . ASP A  1 97  ? 44.619  42.913  27.151 1.00 44.58 ? 96   ASP A CG  1 
ATOM   705   O  OD1 . ASP A  1 97  ? 43.775  43.459  27.894 1.00 48.31 ? 96   ASP A OD1 1 
ATOM   706   O  OD2 . ASP A  1 97  ? 45.235  41.871  27.478 1.00 45.95 ? 96   ASP A OD2 1 
ATOM   707   N  N   . VAL A  1 98  ? 47.309  42.937  23.298 1.00 32.83 ? 97   VAL A N   1 
ATOM   708   C  CA  . VAL A  1 98  ? 47.681  43.143  21.905 1.00 30.67 ? 97   VAL A CA  1 
ATOM   709   C  C   . VAL A  1 98  ? 46.726  42.569  20.863 1.00 30.94 ? 97   VAL A C   1 
ATOM   710   O  O   . VAL A  1 98  ? 46.336  41.403  20.923 1.00 27.98 ? 97   VAL A O   1 
ATOM   711   C  CB  . VAL A  1 98  ? 49.095  42.578  21.646 1.00 31.91 ? 97   VAL A CB  1 
ATOM   712   C  CG1 . VAL A  1 98  ? 49.460  42.721  20.172 1.00 30.82 ? 97   VAL A CG1 1 
ATOM   713   C  CG2 . VAL A  1 98  ? 50.110  43.313  22.521 1.00 31.15 ? 97   VAL A CG2 1 
ATOM   714   N  N   . SER A  1 99  ? 46.361  43.419  19.908 1.00 32.78 ? 98   SER A N   1 
ATOM   715   C  CA  . SER A  1 99  ? 45.479  43.051  18.806 1.00 35.82 ? 98   SER A CA  1 
ATOM   716   C  C   . SER A  1 99  ? 45.925  43.904  17.630 1.00 36.92 ? 98   SER A C   1 
ATOM   717   O  O   . SER A  1 99  ? 45.637  45.101  17.567 1.00 36.51 ? 98   SER A O   1 
ATOM   718   C  CB  . SER A  1 99  ? 44.020  43.350  19.143 1.00 38.41 ? 98   SER A CB  1 
ATOM   719   O  OG  . SER A  1 99  ? 43.178  42.911  18.090 1.00 43.22 ? 98   SER A OG  1 
ATOM   720   N  N   . ILE A  1 100 ? 46.634  43.273  16.702 1.00 35.16 ? 99   ILE A N   1 
ATOM   721   C  CA  . ILE A  1 100 ? 47.186  43.953  15.541 1.00 36.39 ? 99   ILE A CA  1 
ATOM   722   C  C   . ILE A  1 100 ? 46.985  43.142  14.266 1.00 34.30 ? 99   ILE A C   1 
ATOM   723   O  O   . ILE A  1 100 ? 46.825  41.928  14.307 1.00 35.48 ? 99   ILE A O   1 
ATOM   724   C  CB  . ILE A  1 100 ? 48.715  44.164  15.735 1.00 37.46 ? 99   ILE A CB  1 
ATOM   725   C  CG1 . ILE A  1 100 ? 48.969  45.078  16.931 1.00 40.54 ? 99   ILE A CG1 1 
ATOM   726   C  CG2 . ILE A  1 100 ? 49.347  44.737  14.481 1.00 40.39 ? 99   ILE A CG2 1 
ATOM   727   C  CD1 . ILE A  1 100 ? 50.446  45.250  17.266 1.00 39.96 ? 99   ILE A CD1 1 
ATOM   728   N  N   . GLU A  1 101 ? 46.974  43.833  13.137 1.00 34.45 ? 100  GLU A N   1 
ATOM   729   C  CA  . GLU A  1 101 ? 46.871  43.187  11.836 1.00 34.35 ? 100  GLU A CA  1 
ATOM   730   C  C   . GLU A  1 101 ? 47.885  43.942  10.997 1.00 32.30 ? 100  GLU A C   1 
ATOM   731   O  O   . GLU A  1 101 ? 47.877  45.172  10.962 1.00 32.14 ? 100  GLU A O   1 
ATOM   732   C  CB  . GLU A  1 101 ? 45.471  43.318  11.234 1.00 38.58 ? 100  GLU A CB  1 
ATOM   733   C  CG  . GLU A  1 101 ? 45.357  42.602  9.892  1.00 43.54 ? 100  GLU A CG  1 
ATOM   734   C  CD  . GLU A  1 101 ? 43.940  42.530  9.363  1.00 46.05 ? 100  GLU A CD  1 
ATOM   735   O  OE1 . GLU A  1 101 ? 43.080  41.932  10.043 1.00 48.95 ? 100  GLU A OE1 1 
ATOM   736   O  OE2 . GLU A  1 101 ? 43.692  43.066  8.262  1.00 48.08 ? 100  GLU A OE2 1 
ATOM   737   N  N   . ASP A  1 102 ? 48.778  43.209  10.345 1.00 29.51 ? 101  ASP A N   1 
ATOM   738   C  CA  . ASP A  1 102 ? 49.818  43.834  9.547  1.00 29.09 ? 101  ASP A CA  1 
ATOM   739   C  C   . ASP A  1 102 ? 49.972  43.084  8.227  1.00 29.45 ? 101  ASP A C   1 
ATOM   740   O  O   . ASP A  1 102 ? 49.897  41.858  8.187  1.00 29.32 ? 101  ASP A O   1 
ATOM   741   C  CB  . ASP A  1 102 ? 51.130  43.830  10.341 1.00 27.24 ? 101  ASP A CB  1 
ATOM   742   C  CG  . ASP A  1 102 ? 52.202  44.683  9.707  1.00 27.77 ? 101  ASP A CG  1 
ATOM   743   O  OD1 . ASP A  1 102 ? 53.037  44.147  8.947  1.00 29.16 ? 101  ASP A OD1 1 
ATOM   744   O  OD2 . ASP A  1 102 ? 52.213  45.901  9.968  1.00 29.29 ? 101  ASP A OD2 1 
ATOM   745   N  N   . SER A  1 103 ? 50.183  43.828  7.148  1.00 30.44 ? 102  SER A N   1 
ATOM   746   C  CA  . SER A  1 103 ? 50.309  43.219  5.832  1.00 32.40 ? 102  SER A CA  1 
ATOM   747   C  C   . SER A  1 103 ? 51.712  43.344  5.263  1.00 33.22 ? 102  SER A C   1 
ATOM   748   O  O   . SER A  1 103 ? 51.924  43.151  4.064  1.00 34.38 ? 102  SER A O   1 
ATOM   749   C  CB  . SER A  1 103 ? 49.290  43.843  4.869  1.00 33.10 ? 102  SER A CB  1 
ATOM   750   O  OG  . SER A  1 103 ? 49.491  45.241  4.756  1.00 34.51 ? 102  SER A OG  1 
ATOM   751   N  N   . VAL A  1 104 ? 52.672  43.670  6.123  1.00 31.05 ? 103  VAL A N   1 
ATOM   752   C  CA  . VAL A  1 104 ? 54.056  43.796  5.693  1.00 30.77 ? 103  VAL A CA  1 
ATOM   753   C  C   . VAL A  1 104 ? 54.815  42.555  6.141  1.00 30.32 ? 103  VAL A C   1 
ATOM   754   O  O   . VAL A  1 104 ? 55.577  41.968  5.370  1.00 29.75 ? 103  VAL A O   1 
ATOM   755   C  CB  . VAL A  1 104 ? 54.720  45.055  6.282  1.00 31.81 ? 103  VAL A CB  1 
ATOM   756   C  CG1 . VAL A  1 104 ? 56.198  45.092  5.913  1.00 32.27 ? 103  VAL A CG1 1 
ATOM   757   C  CG2 . VAL A  1 104 ? 54.018  46.296  5.750  1.00 35.66 ? 103  VAL A CG2 1 
ATOM   758   N  N   . ILE A  1 105 ? 54.605  42.154  7.391  1.00 28.58 ? 104  ILE A N   1 
ATOM   759   C  CA  . ILE A  1 105 ? 55.253  40.959  7.908  1.00 27.37 ? 104  ILE A CA  1 
ATOM   760   C  C   . ILE A  1 105 ? 54.538  39.743  7.319  1.00 27.58 ? 104  ILE A C   1 
ATOM   761   O  O   . ILE A  1 105 ? 53.371  39.823  6.934  1.00 27.34 ? 104  ILE A O   1 
ATOM   762   C  CB  . ILE A  1 105 ? 55.157  40.876  9.454  1.00 28.98 ? 104  ILE A CB  1 
ATOM   763   C  CG1 . ILE A  1 105 ? 53.687  40.886  9.891  1.00 25.99 ? 104  ILE A CG1 1 
ATOM   764   C  CG2 . ILE A  1 105 ? 55.908  42.038  10.086 1.00 29.53 ? 104  ILE A CG2 1 
ATOM   765   C  CD1 . ILE A  1 105 ? 53.479  40.592  11.371 1.00 26.74 ? 104  ILE A CD1 1 
ATOM   766   N  N   . SER A  1 106 ? 55.238  38.620  7.239  1.00 26.36 ? 105  SER A N   1 
ATOM   767   C  CA  . SER A  1 106 ? 54.634  37.399  6.725  1.00 26.03 ? 105  SER A CA  1 
ATOM   768   C  C   . SER A  1 106 ? 55.189  36.203  7.493  1.00 24.97 ? 105  SER A C   1 
ATOM   769   O  O   . SER A  1 106 ? 56.271  36.285  8.068  1.00 25.22 ? 105  SER A O   1 
ATOM   770   C  CB  . SER A  1 106 ? 54.925  37.240  5.228  1.00 24.06 ? 105  SER A CB  1 
ATOM   771   O  OG  . SER A  1 106 ? 54.172  36.165  4.691  1.00 21.63 ? 105  SER A OG  1 
ATOM   772   N  N   . LEU A  1 107 ? 54.446  35.099  7.501  1.00 24.69 ? 106  LEU A N   1 
ATOM   773   C  CA  . LEU A  1 107 ? 54.874  33.894  8.196  1.00 24.69 ? 106  LEU A CA  1 
ATOM   774   C  C   . LEU A  1 107 ? 55.438  32.855  7.229  1.00 26.05 ? 106  LEU A C   1 
ATOM   775   O  O   . LEU A  1 107 ? 55.611  31.691  7.581  1.00 23.41 ? 106  LEU A O   1 
ATOM   776   C  CB  . LEU A  1 107 ? 53.703  33.291  8.979  1.00 25.21 ? 106  LEU A CB  1 
ATOM   777   C  CG  . LEU A  1 107 ? 53.033  34.205  10.011 1.00 25.10 ? 106  LEU A CG  1 
ATOM   778   C  CD1 . LEU A  1 107 ? 51.947  33.424  10.754 1.00 25.70 ? 106  LEU A CD1 1 
ATOM   779   C  CD2 . LEU A  1 107 ? 54.082  34.732  10.988 1.00 23.63 ? 106  LEU A CD2 1 
ATOM   780   N  N   . SER A  1 108 ? 55.718  33.284  6.006  1.00 26.96 ? 107  SER A N   1 
ATOM   781   C  CA  . SER A  1 108 ? 56.272  32.393  4.995  1.00 27.60 ? 107  SER A CA  1 
ATOM   782   C  C   . SER A  1 108 ? 56.903  33.245  3.909  1.00 27.97 ? 107  SER A C   1 
ATOM   783   O  O   . SER A  1 108 ? 56.757  34.470  3.900  1.00 24.34 ? 107  SER A O   1 
ATOM   784   C  CB  . SER A  1 108 ? 55.176  31.504  4.393  1.00 27.91 ? 107  SER A CB  1 
ATOM   785   O  OG  . SER A  1 108 ? 54.253  32.272  3.644  1.00 27.55 ? 107  SER A OG  1 
ATOM   786   N  N   . GLY A  1 109 ? 57.602  32.597  2.984  1.00 29.67 ? 108  GLY A N   1 
ATOM   787   C  CA  . GLY A  1 109 ? 58.247  33.345  1.929  1.00 31.09 ? 108  GLY A CA  1 
ATOM   788   C  C   . GLY A  1 109 ? 59.653  33.723  2.346  1.00 34.55 ? 108  GLY A C   1 
ATOM   789   O  O   . GLY A  1 109 ? 60.011  33.654  3.527  1.00 34.29 ? 108  GLY A O   1 
ATOM   790   N  N   . ASP A  1 110 ? 60.441  34.142  1.364  1.00 36.66 ? 109  ASP A N   1 
ATOM   791   C  CA  . ASP A  1 110 ? 61.832  34.520  1.561  1.00 39.48 ? 109  ASP A CA  1 
ATOM   792   C  C   . ASP A  1 110 ? 62.074  35.493  2.715  1.00 38.63 ? 109  ASP A C   1 
ATOM   793   O  O   . ASP A  1 110 ? 63.168  35.528  3.277  1.00 39.00 ? 109  ASP A O   1 
ATOM   794   C  CB  . ASP A  1 110 ? 62.375  35.117  0.259  1.00 44.30 ? 109  ASP A CB  1 
ATOM   795   C  CG  . ASP A  1 110 ? 63.850  34.858  0.072  1.00 48.82 ? 109  ASP A CG  1 
ATOM   796   O  OD1 . ASP A  1 110 ? 64.662  35.416  0.842  1.00 52.40 ? 109  ASP A OD1 1 
ATOM   797   O  OD2 . ASP A  1 110 ? 64.198  34.085  -0.846 1.00 53.14 ? 109  ASP A OD2 1 
ATOM   798   N  N   . HIS A  1 111 ? 61.060  36.272  3.076  1.00 37.59 ? 110  HIS A N   1 
ATOM   799   C  CA  . HIS A  1 111 ? 61.211  37.245  4.154  1.00 34.99 ? 110  HIS A CA  1 
ATOM   800   C  C   . HIS A  1 111 ? 60.331  36.962  5.376  1.00 34.50 ? 110  HIS A C   1 
ATOM   801   O  O   . HIS A  1 111 ? 59.905  37.883  6.069  1.00 34.81 ? 110  HIS A O   1 
ATOM   802   C  CB  . HIS A  1 111 ? 60.920  38.649  3.621  1.00 36.38 ? 110  HIS A CB  1 
ATOM   803   C  CG  . HIS A  1 111 ? 61.935  39.149  2.644  1.00 38.71 ? 110  HIS A CG  1 
ATOM   804   N  ND1 . HIS A  1 111 ? 61.742  40.279  1.876  1.00 39.93 ? 110  HIS A ND1 1 
ATOM   805   C  CD2 . HIS A  1 111 ? 63.169  38.684  2.312  1.00 41.90 ? 110  HIS A CD2 1 
ATOM   806   C  CE1 . HIS A  1 111 ? 62.803  40.487  1.119  1.00 39.89 ? 110  HIS A CE1 1 
ATOM   807   N  NE2 . HIS A  1 111 ? 63.684  39.533  1.365  1.00 39.44 ? 110  HIS A NE2 1 
ATOM   808   N  N   . SER A  1 112 ? 60.066  35.687  5.639  1.00 30.80 ? 111  SER A N   1 
ATOM   809   C  CA  . SER A  1 112 ? 59.249  35.285  6.785  1.00 28.30 ? 111  SER A CA  1 
ATOM   810   C  C   . SER A  1 112 ? 59.879  35.709  8.119  1.00 28.03 ? 111  SER A C   1 
ATOM   811   O  O   . SER A  1 112 ? 61.104  35.794  8.239  1.00 26.46 ? 111  SER A O   1 
ATOM   812   C  CB  . SER A  1 112 ? 59.068  33.766  6.771  1.00 27.11 ? 111  SER A CB  1 
ATOM   813   O  OG  . SER A  1 112 ? 58.417  33.306  7.940  1.00 27.57 ? 111  SER A OG  1 
ATOM   814   N  N   . ILE A  1 113 ? 59.043  35.973  9.121  1.00 27.06 ? 112  ILE A N   1 
ATOM   815   C  CA  . ILE A  1 113 ? 59.549  36.364  10.432 1.00 26.48 ? 112  ILE A CA  1 
ATOM   816   C  C   . ILE A  1 113 ? 59.682  35.133  11.322 1.00 25.51 ? 112  ILE A C   1 
ATOM   817   O  O   . ILE A  1 113 ? 60.054  35.234  12.491 1.00 24.81 ? 112  ILE A O   1 
ATOM   818   C  CB  . ILE A  1 113 ? 58.623  37.390  11.136 1.00 26.94 ? 112  ILE A CB  1 
ATOM   819   C  CG1 . ILE A  1 113 ? 57.247  36.774  11.392 1.00 25.59 ? 112  ILE A CG1 1 
ATOM   820   C  CG2 . ILE A  1 113 ? 58.526  38.653  10.296 1.00 27.01 ? 112  ILE A CG2 1 
ATOM   821   C  CD1 . ILE A  1 113 ? 56.299  37.683  12.182 1.00 27.44 ? 112  ILE A CD1 1 
ATOM   822   N  N   . ILE A  1 114 ? 59.357  33.970  10.766 1.00 24.68 ? 113  ILE A N   1 
ATOM   823   C  CA  . ILE A  1 114 ? 59.469  32.727  11.510 1.00 23.42 ? 113  ILE A CA  1 
ATOM   824   C  C   . ILE A  1 114 ? 60.949  32.540  11.847 1.00 23.99 ? 113  ILE A C   1 
ATOM   825   O  O   . ILE A  1 114 ? 61.810  32.707  10.985 1.00 22.63 ? 113  ILE A O   1 
ATOM   826   C  CB  . ILE A  1 114 ? 58.990  31.515  10.663 1.00 24.17 ? 113  ILE A CB  1 
ATOM   827   C  CG1 . ILE A  1 114 ? 57.475  31.587  10.434 1.00 23.56 ? 113  ILE A CG1 1 
ATOM   828   C  CG2 . ILE A  1 114 ? 59.360  30.208  11.357 1.00 23.01 ? 113  ILE A CG2 1 
ATOM   829   C  CD1 . ILE A  1 114 ? 56.655  31.467  11.695 1.00 24.49 ? 113  ILE A CD1 1 
ATOM   830   N  N   . GLY A  1 115 ? 61.242  32.216  13.101 1.00 21.79 ? 114  GLY A N   1 
ATOM   831   C  CA  . GLY A  1 115 ? 62.626  32.004  13.494 1.00 23.46 ? 114  GLY A CA  1 
ATOM   832   C  C   . GLY A  1 115 ? 63.387  33.262  13.876 1.00 22.89 ? 114  GLY A C   1 
ATOM   833   O  O   . GLY A  1 115 ? 64.593  33.214  14.134 1.00 22.87 ? 114  GLY A O   1 
ATOM   834   N  N   . ARG A  1 116 ? 62.694  34.393  13.897 1.00 20.91 ? 115  ARG A N   1 
ATOM   835   C  CA  . ARG A  1 116 ? 63.324  35.644  14.284 1.00 21.46 ? 115  ARG A CA  1 
ATOM   836   C  C   . ARG A  1 116 ? 62.808  35.986  15.683 1.00 23.15 ? 115  ARG A C   1 
ATOM   837   O  O   . ARG A  1 116 ? 62.082  35.184  16.276 1.00 25.55 ? 115  ARG A O   1 
ATOM   838   C  CB  . ARG A  1 116 ? 63.027  36.733  13.242 1.00 20.94 ? 115  ARG A CB  1 
ATOM   839   C  CG  . ARG A  1 116 ? 63.625  36.363  11.872 1.00 18.90 ? 115  ARG A CG  1 
ATOM   840   C  CD  . ARG A  1 116 ? 63.445  37.427  10.797 1.00 22.77 ? 115  ARG A CD  1 
ATOM   841   N  NE  . ARG A  1 116 ? 63.816  36.925  9.469  1.00 24.68 ? 115  ARG A NE  1 
ATOM   842   C  CZ  . ARG A  1 116 ? 65.064  36.747  9.034  1.00 27.25 ? 115  ARG A CZ  1 
ATOM   843   N  NH1 . ARG A  1 116 ? 65.274  36.279  7.807  1.00 28.01 ? 115  ARG A NH1 1 
ATOM   844   N  NH2 . ARG A  1 116 ? 66.107  37.047  9.803  1.00 24.94 ? 115  ARG A NH2 1 
ATOM   845   N  N   . THR A  1 117 ? 63.170  37.154  16.213 1.00 23.52 ? 116  THR A N   1 
ATOM   846   C  CA  . THR A  1 117 ? 62.793  37.522  17.581 1.00 22.48 ? 116  THR A CA  1 
ATOM   847   C  C   . THR A  1 117 ? 61.813  38.680  17.742 1.00 22.30 ? 116  THR A C   1 
ATOM   848   O  O   . THR A  1 117 ? 61.994  39.745  17.156 1.00 22.77 ? 116  THR A O   1 
ATOM   849   C  CB  . THR A  1 117 ? 64.065  37.870  18.417 1.00 23.10 ? 116  THR A CB  1 
ATOM   850   O  OG1 . THR A  1 117 ? 64.925  36.727  18.480 1.00 22.36 ? 116  THR A OG1 1 
ATOM   851   C  CG2 . THR A  1 117 ? 63.690  38.302  19.852 1.00 21.67 ? 116  THR A CG2 1 
ATOM   852   N  N   . LEU A  1 118 ? 60.778  38.460  18.546 1.00 21.30 ? 117  LEU A N   1 
ATOM   853   C  CA  . LEU A  1 118 ? 59.789  39.497  18.829 1.00 21.86 ? 117  LEU A CA  1 
ATOM   854   C  C   . LEU A  1 118 ? 60.267  40.166  20.117 1.00 22.61 ? 117  LEU A C   1 
ATOM   855   O  O   . LEU A  1 118 ? 60.547  39.484  21.102 1.00 23.39 ? 117  LEU A O   1 
ATOM   856   C  CB  . LEU A  1 118 ? 58.405  38.887  19.043 1.00 20.52 ? 117  LEU A CB  1 
ATOM   857   C  CG  . LEU A  1 118 ? 57.304  39.887  19.408 1.00 20.84 ? 117  LEU A CG  1 
ATOM   858   C  CD1 . LEU A  1 118 ? 57.151  40.908  18.278 1.00 20.14 ? 117  LEU A CD1 1 
ATOM   859   C  CD2 . LEU A  1 118 ? 55.994  39.150  19.654 1.00 18.32 ? 117  LEU A CD2 1 
ATOM   860   N  N   . VAL A  1 119 ? 60.357  41.491  20.107 1.00 23.75 ? 118  VAL A N   1 
ATOM   861   C  CA  . VAL A  1 119 ? 60.841  42.241  21.269 1.00 25.28 ? 118  VAL A CA  1 
ATOM   862   C  C   . VAL A  1 119 ? 59.895  43.351  21.740 1.00 25.89 ? 118  VAL A C   1 
ATOM   863   O  O   . VAL A  1 119 ? 59.318  44.074  20.922 1.00 25.44 ? 118  VAL A O   1 
ATOM   864   C  CB  . VAL A  1 119 ? 62.206  42.905  20.946 1.00 25.52 ? 118  VAL A CB  1 
ATOM   865   C  CG1 . VAL A  1 119 ? 62.689  43.735  22.131 1.00 23.73 ? 118  VAL A CG1 1 
ATOM   866   C  CG2 . VAL A  1 119 ? 63.235  41.838  20.579 1.00 26.16 ? 118  VAL A CG2 1 
ATOM   867   N  N   . VAL A  1 120 ? 59.734  43.477  23.058 1.00 26.42 ? 119  VAL A N   1 
ATOM   868   C  CA  . VAL A  1 120 ? 58.911  44.544  23.632 1.00 24.09 ? 119  VAL A CA  1 
ATOM   869   C  C   . VAL A  1 120 ? 59.890  45.454  24.387 1.00 25.06 ? 119  VAL A C   1 
ATOM   870   O  O   . VAL A  1 120 ? 60.722  44.979  25.166 1.00 24.60 ? 119  VAL A O   1 
ATOM   871   C  CB  . VAL A  1 120 ? 57.806  43.990  24.580 1.00 25.21 ? 119  VAL A CB  1 
ATOM   872   C  CG1 . VAL A  1 120 ? 58.419  43.301  25.774 1.00 25.74 ? 119  VAL A CG1 1 
ATOM   873   C  CG2 . VAL A  1 120 ? 56.887  45.125  25.026 1.00 25.90 ? 119  VAL A CG2 1 
ATOM   874   N  N   . HIS A  1 121 ? 59.788  46.758  24.148 1.00 24.67 ? 120  HIS A N   1 
ATOM   875   C  CA  . HIS A  1 121 ? 60.701  47.740  24.726 1.00 26.36 ? 120  HIS A CA  1 
ATOM   876   C  C   . HIS A  1 121 ? 60.332  48.517  25.989 1.00 27.16 ? 120  HIS A C   1 
ATOM   877   O  O   . HIS A  1 121 ? 59.177  48.591  26.400 1.00 26.82 ? 120  HIS A O   1 
ATOM   878   C  CB  . HIS A  1 121 ? 61.084  48.755  23.648 1.00 26.00 ? 120  HIS A CB  1 
ATOM   879   C  CG  . HIS A  1 121 ? 61.998  48.205  22.604 1.00 27.61 ? 120  HIS A CG  1 
ATOM   880   N  ND1 . HIS A  1 121 ? 63.372  48.279  22.706 1.00 26.41 ? 120  HIS A ND1 1 
ATOM   881   C  CD2 . HIS A  1 121 ? 61.742  47.554  21.446 1.00 27.80 ? 120  HIS A CD2 1 
ATOM   882   C  CE1 . HIS A  1 121 ? 63.919  47.699  21.656 1.00 27.94 ? 120  HIS A CE1 1 
ATOM   883   N  NE2 . HIS A  1 121 ? 62.953  47.248  20.874 1.00 27.58 ? 120  HIS A NE2 1 
ATOM   884   N  N   . GLU A  1 122 ? 61.370  49.108  26.570 1.00 29.32 ? 121  GLU A N   1 
ATOM   885   C  CA  . GLU A  1 122 ? 61.293  49.919  27.778 1.00 31.95 ? 121  GLU A CA  1 
ATOM   886   C  C   . GLU A  1 122 ? 60.461  51.178  27.548 1.00 32.56 ? 121  GLU A C   1 
ATOM   887   O  O   . GLU A  1 122 ? 59.516  51.455  28.290 1.00 33.26 ? 121  GLU A O   1 
ATOM   888   C  CB  . GLU A  1 122 ? 62.708  50.328  28.189 1.00 34.61 ? 121  GLU A CB  1 
ATOM   889   C  CG  . GLU A  1 122 ? 62.800  51.337  29.330 1.00 37.74 ? 121  GLU A CG  1 
ATOM   890   C  CD  . GLU A  1 122 ? 64.147  52.054  29.355 1.00 40.46 ? 121  GLU A CD  1 
ATOM   891   O  OE1 . GLU A  1 122 ? 64.471  52.678  30.387 1.00 42.01 ? 121  GLU A OE1 1 
ATOM   892   O  OE2 . GLU A  1 122 ? 64.879  52.004  28.338 1.00 39.93 ? 121  GLU A OE2 1 
ATOM   893   N  N   . LYS A  1 123 ? 60.828  51.930  26.513 1.00 32.89 ? 122  LYS A N   1 
ATOM   894   C  CA  . LYS A  1 123 ? 60.154  53.179  26.178 1.00 36.40 ? 122  LYS A CA  1 
ATOM   895   C  C   . LYS A  1 123 ? 59.293  53.081  24.925 1.00 36.65 ? 122  LYS A C   1 
ATOM   896   O  O   . LYS A  1 123 ? 59.216  52.028  24.284 1.00 34.68 ? 122  LYS A O   1 
ATOM   897   C  CB  . LYS A  1 123 ? 61.189  54.295  25.992 1.00 39.06 ? 122  LYS A CB  1 
ATOM   898   C  CG  . LYS A  1 123 ? 62.072  54.528  27.207 1.00 42.61 ? 122  LYS A CG  1 
ATOM   899   C  CD  . LYS A  1 123 ? 62.946  55.768  27.047 1.00 47.20 ? 122  LYS A CD  1 
ATOM   900   C  CE  . LYS A  1 123 ? 63.955  55.616  25.917 1.00 50.64 ? 122  LYS A CE  1 
ATOM   901   N  NZ  . LYS A  1 123 ? 64.789  56.843  25.739 1.00 52.04 ? 122  LYS A NZ  1 
ATOM   902   N  N   . ALA A  1 124 ? 58.648  54.191  24.580 1.00 35.87 ? 123  ALA A N   1 
ATOM   903   C  CA  . ALA A  1 124 ? 57.791  54.236  23.406 1.00 35.06 ? 123  ALA A CA  1 
ATOM   904   C  C   . ALA A  1 124 ? 58.591  54.412  22.126 1.00 35.20 ? 123  ALA A C   1 
ATOM   905   O  O   . ALA A  1 124 ? 59.658  55.026  22.112 1.00 36.07 ? 123  ALA A O   1 
ATOM   906   C  CB  . ALA A  1 124 ? 56.771  55.367  23.539 1.00 35.24 ? 123  ALA A CB  1 
ATOM   907   N  N   . ASP A  1 125 ? 58.064  53.852  21.047 1.00 35.45 ? 124  ASP A N   1 
ATOM   908   C  CA  . ASP A  1 125 ? 58.688  53.953  19.740 1.00 35.52 ? 124  ASP A CA  1 
ATOM   909   C  C   . ASP A  1 125 ? 58.183  55.270  19.139 1.00 35.46 ? 124  ASP A C   1 
ATOM   910   O  O   . ASP A  1 125 ? 56.978  55.456  18.993 1.00 33.32 ? 124  ASP A O   1 
ATOM   911   C  CB  . ASP A  1 125 ? 58.246  52.757  18.886 1.00 35.71 ? 124  ASP A CB  1 
ATOM   912   C  CG  . ASP A  1 125 ? 58.904  52.724  17.521 1.00 34.57 ? 124  ASP A CG  1 
ATOM   913   O  OD1 . ASP A  1 125 ? 58.849  51.656  16.870 1.00 33.61 ? 124  ASP A OD1 1 
ATOM   914   O  OD2 . ASP A  1 125 ? 59.463  53.754  17.093 1.00 34.86 ? 124  ASP A OD2 1 
ATOM   915   N  N   . ASP A  1 126 ? 59.093  56.183  18.811 1.00 36.98 ? 125  ASP A N   1 
ATOM   916   C  CA  . ASP A  1 126 ? 58.685  57.464  18.235 1.00 39.73 ? 125  ASP A CA  1 
ATOM   917   C  C   . ASP A  1 126 ? 58.384  57.319  16.746 1.00 41.40 ? 125  ASP A C   1 
ATOM   918   O  O   . ASP A  1 126 ? 58.270  58.306  16.017 1.00 41.48 ? 125  ASP A O   1 
ATOM   919   C  CB  . ASP A  1 126 ? 59.758  58.537  18.472 1.00 39.28 ? 125  ASP A CB  1 
ATOM   920   C  CG  . ASP A  1 126 ? 61.035  58.284  17.698 1.00 41.27 ? 125  ASP A CG  1 
ATOM   921   O  OD1 . ASP A  1 126 ? 62.065  58.893  18.058 1.00 41.29 ? 125  ASP A OD1 1 
ATOM   922   O  OD2 . ASP A  1 126 ? 61.016  57.495  16.730 1.00 41.32 ? 125  ASP A OD2 1 
ATOM   923   N  N   . LEU A  1 127 ? 58.263  56.069  16.312 1.00 41.49 ? 126  LEU A N   1 
ATOM   924   C  CA  . LEU A  1 127 ? 57.950  55.729  14.931 1.00 42.34 ? 126  LEU A CA  1 
ATOM   925   C  C   . LEU A  1 127 ? 58.833  56.414  13.893 1.00 43.36 ? 126  LEU A C   1 
ATOM   926   O  O   . LEU A  1 127 ? 58.401  56.675  12.770 1.00 43.82 ? 126  LEU A O   1 
ATOM   927   C  CB  . LEU A  1 127 ? 56.472  56.023  14.662 1.00 42.00 ? 126  LEU A CB  1 
ATOM   928   C  CG  . LEU A  1 127 ? 55.530  55.379  15.688 1.00 42.52 ? 126  LEU A CG  1 
ATOM   929   C  CD1 . LEU A  1 127 ? 54.083  55.717  15.364 1.00 41.42 ? 126  LEU A CD1 1 
ATOM   930   C  CD2 . LEU A  1 127 ? 55.740  53.867  15.698 1.00 42.66 ? 126  LEU A CD2 1 
ATOM   931   N  N   . GLY A  1 128 ? 60.073  56.698  14.277 1.00 45.08 ? 127  GLY A N   1 
ATOM   932   C  CA  . GLY A  1 128 ? 61.016  57.326  13.370 1.00 47.02 ? 127  GLY A CA  1 
ATOM   933   C  C   . GLY A  1 128 ? 60.792  58.796  13.066 1.00 49.37 ? 127  GLY A C   1 
ATOM   934   O  O   . GLY A  1 128 ? 61.191  59.272  12.000 1.00 47.54 ? 127  GLY A O   1 
ATOM   935   N  N   . LYS A  1 129 ? 60.159  59.519  13.988 1.00 50.31 ? 128  LYS A N   1 
ATOM   936   C  CA  . LYS A  1 129 ? 59.905  60.944  13.788 1.00 52.90 ? 128  LYS A CA  1 
ATOM   937   C  C   . LYS A  1 129 ? 60.628  61.772  14.840 1.00 54.09 ? 128  LYS A C   1 
ATOM   938   O  O   . LYS A  1 129 ? 60.442  62.986  14.923 1.00 55.07 ? 128  LYS A O   1 
ATOM   939   C  CB  . LYS A  1 129 ? 58.405  61.244  13.855 1.00 53.16 ? 128  LYS A CB  1 
ATOM   940   C  CG  . LYS A  1 129 ? 57.534  60.420  12.909 1.00 54.88 ? 128  LYS A CG  1 
ATOM   941   C  CD  . LYS A  1 129 ? 58.322  59.877  11.725 1.00 54.84 ? 128  LYS A CD  1 
ATOM   942   C  CE  . LYS A  1 129 ? 57.410  59.327  10.647 1.00 54.52 ? 128  LYS A CE  1 
ATOM   943   N  NZ  . LYS A  1 129 ? 56.341  58.464  11.211 1.00 53.05 ? 128  LYS A NZ  1 
ATOM   944   N  N   . GLY A  1 130 ? 61.461  61.105  15.632 1.00 55.01 ? 129  GLY A N   1 
ATOM   945   C  CA  . GLY A  1 130 ? 62.201  61.776  16.687 1.00 56.08 ? 129  GLY A CA  1 
ATOM   946   C  C   . GLY A  1 130 ? 63.124  62.902  16.258 1.00 56.56 ? 129  GLY A C   1 
ATOM   947   O  O   . GLY A  1 130 ? 63.536  63.714  17.085 1.00 57.41 ? 129  GLY A O   1 
ATOM   948   N  N   . GLY A  1 131 ? 63.466  62.953  14.976 1.00 57.18 ? 130  GLY A N   1 
ATOM   949   C  CA  . GLY A  1 131 ? 64.338  64.011  14.500 1.00 57.57 ? 130  GLY A CA  1 
ATOM   950   C  C   . GLY A  1 131 ? 65.824  63.736  14.651 1.00 58.20 ? 130  GLY A C   1 
ATOM   951   O  O   . GLY A  1 131 ? 66.650  64.524  14.188 1.00 58.93 ? 130  GLY A O   1 
ATOM   952   N  N   . ASN A  1 132 ? 66.175  62.631  15.301 1.00 57.27 ? 131  ASN A N   1 
ATOM   953   C  CA  . ASN A  1 132 ? 67.581  62.281  15.483 1.00 56.27 ? 131  ASN A CA  1 
ATOM   954   C  C   . ASN A  1 132 ? 67.907  60.962  14.787 1.00 55.79 ? 131  ASN A C   1 
ATOM   955   O  O   . ASN A  1 132 ? 67.010  60.195  14.433 1.00 54.88 ? 131  ASN A O   1 
ATOM   956   C  CB  . ASN A  1 132 ? 67.925  62.196  16.973 1.00 56.57 ? 131  ASN A CB  1 
ATOM   957   C  CG  . ASN A  1 132 ? 67.012  61.258  17.731 1.00 56.94 ? 131  ASN A CG  1 
ATOM   958   O  OD1 . ASN A  1 132 ? 66.951  60.062  17.443 1.00 55.96 ? 131  ASN A OD1 1 
ATOM   959   N  ND2 . ASN A  1 132 ? 66.293  61.797  18.707 1.00 57.48 ? 131  ASN A ND2 1 
ATOM   960   N  N   . GLU A  1 133 ? 69.196  60.705  14.596 1.00 55.22 ? 132  GLU A N   1 
ATOM   961   C  CA  . GLU A  1 133 ? 69.645  59.494  13.920 1.00 54.95 ? 132  GLU A CA  1 
ATOM   962   C  C   . GLU A  1 133 ? 69.154  58.214  14.596 1.00 53.89 ? 132  GLU A C   1 
ATOM   963   O  O   . GLU A  1 133 ? 68.819  57.238  13.923 1.00 53.88 ? 132  GLU A O   1 
ATOM   964   C  CB  . GLU A  1 133 ? 71.174  59.488  13.829 1.00 55.68 ? 132  GLU A CB  1 
ATOM   965   C  CG  . GLU A  1 133 ? 71.717  58.547  12.771 1.00 57.15 ? 132  GLU A CG  1 
ATOM   966   C  CD  . GLU A  1 133 ? 73.206  58.699  12.553 0.00 56.86 ? 132  GLU A CD  1 
ATOM   967   O  OE1 . GLU A  1 133 ? 73.739  58.024  11.649 0.00 57.05 ? 132  GLU A OE1 1 
ATOM   968   O  OE2 . GLU A  1 133 ? 73.842  59.490  13.280 0.00 57.04 ? 132  GLU A OE2 1 
ATOM   969   N  N   . GLU A  1 134 ? 69.105  58.221  15.923 1.00 52.55 ? 133  GLU A N   1 
ATOM   970   C  CA  . GLU A  1 134 ? 68.651  57.053  16.669 1.00 50.89 ? 133  GLU A CA  1 
ATOM   971   C  C   . GLU A  1 134 ? 67.184  56.753  16.362 1.00 49.76 ? 133  GLU A C   1 
ATOM   972   O  O   . GLU A  1 134 ? 66.753  55.597  16.389 1.00 48.70 ? 133  GLU A O   1 
ATOM   973   C  CB  . GLU A  1 134 ? 68.829  57.286  18.171 1.00 51.47 ? 133  GLU A CB  1 
ATOM   974   C  CG  . GLU A  1 134 ? 68.538  56.070  19.034 1.00 51.85 ? 133  GLU A CG  1 
ATOM   975   C  CD  . GLU A  1 134 ? 69.544  54.948  18.832 1.00 53.61 ? 133  GLU A CD  1 
ATOM   976   O  OE1 . GLU A  1 134 ? 69.374  53.883  19.462 1.00 54.94 ? 133  GLU A OE1 1 
ATOM   977   O  OE2 . GLU A  1 134 ? 70.503  55.128  18.051 1.00 54.13 ? 133  GLU A OE2 1 
ATOM   978   N  N   . SER A  1 135 ? 66.418  57.797  16.064 1.00 48.26 ? 134  SER A N   1 
ATOM   979   C  CA  . SER A  1 135 ? 65.004  57.631  15.758 1.00 47.27 ? 134  SER A CA  1 
ATOM   980   C  C   . SER A  1 135 ? 64.798  56.855  14.463 1.00 47.19 ? 134  SER A C   1 
ATOM   981   O  O   . SER A  1 135 ? 63.826  56.112  14.324 1.00 46.41 ? 134  SER A O   1 
ATOM   982   C  CB  . SER A  1 135 ? 64.319  58.994  15.648 1.00 47.37 ? 134  SER A CB  1 
ATOM   983   O  OG  . SER A  1 135 ? 62.947  58.846  15.321 1.00 45.58 ? 134  SER A OG  1 
ATOM   984   N  N   . THR A  1 136 ? 65.717  57.028  13.519 1.00 47.03 ? 135  THR A N   1 
ATOM   985   C  CA  . THR A  1 136 ? 65.623  56.350  12.229 1.00 47.65 ? 135  THR A CA  1 
ATOM   986   C  C   . THR A  1 136 ? 66.193  54.936  12.277 1.00 47.31 ? 135  THR A C   1 
ATOM   987   O  O   . THR A  1 136 ? 66.240  54.247  11.257 1.00 47.76 ? 135  THR A O   1 
ATOM   988   C  CB  . THR A  1 136 ? 66.376  57.127  11.130 1.00 47.91 ? 135  THR A CB  1 
ATOM   989   O  OG1 . THR A  1 136 ? 67.781  57.107  11.410 1.00 48.37 ? 135  THR A OG1 1 
ATOM   990   C  CG2 . THR A  1 136 ? 65.897  58.567  11.071 1.00 48.66 ? 135  THR A CG2 1 
ATOM   991   N  N   . LYS A  1 137 ? 66.626  54.510  13.460 1.00 46.10 ? 136  LYS A N   1 
ATOM   992   C  CA  . LYS A  1 137 ? 67.198  53.177  13.638 1.00 45.17 ? 136  LYS A CA  1 
ATOM   993   C  C   . LYS A  1 137 ? 66.334  52.311  14.554 1.00 43.38 ? 136  LYS A C   1 
ATOM   994   O  O   . LYS A  1 137 ? 65.907  51.220  14.180 1.00 42.35 ? 136  LYS A O   1 
ATOM   995   C  CB  . LYS A  1 137 ? 68.598  53.280  14.248 1.00 46.61 ? 136  LYS A CB  1 
ATOM   996   C  CG  . LYS A  1 137 ? 69.588  54.110  13.449 1.00 49.39 ? 136  LYS A CG  1 
ATOM   997   C  CD  . LYS A  1 137 ? 70.828  54.403  14.282 0.00 51.59 ? 136  LYS A CD  1 
ATOM   998   C  CE  . LYS A  1 137 ? 71.802  55.301  13.542 1.00 54.11 ? 136  LYS A CE  1 
ATOM   999   N  NZ  . LYS A  1 137 ? 72.916  55.763  14.421 1.00 55.21 ? 136  LYS A NZ  1 
ATOM   1000  N  N   . THR A  1 138 ? 66.083  52.816  15.757 1.00 41.09 ? 137  THR A N   1 
ATOM   1001  C  CA  . THR A  1 138 ? 65.306  52.098  16.759 1.00 39.46 ? 137  THR A CA  1 
ATOM   1002  C  C   . THR A  1 138 ? 64.036  52.829  17.176 1.00 38.52 ? 137  THR A C   1 
ATOM   1003  O  O   . THR A  1 138 ? 63.161  52.246  17.814 1.00 37.71 ? 137  THR A O   1 
ATOM   1004  C  CB  . THR A  1 138 ? 66.139  51.890  18.030 1.00 39.44 ? 137  THR A CB  1 
ATOM   1005  O  OG1 . THR A  1 138 ? 66.431  53.169  18.614 1.00 36.66 ? 137  THR A OG1 1 
ATOM   1006  C  CG2 . THR A  1 138 ? 67.447  51.178  17.705 1.00 38.62 ? 137  THR A CG2 1 
ATOM   1007  N  N   . GLY A  1 139 ? 63.939  54.106  16.825 1.00 39.06 ? 138  GLY A N   1 
ATOM   1008  C  CA  . GLY A  1 139 ? 62.775  54.881  17.218 1.00 37.90 ? 138  GLY A CA  1 
ATOM   1009  C  C   . GLY A  1 139 ? 62.860  55.255  18.689 1.00 36.65 ? 138  GLY A C   1 
ATOM   1010  O  O   . GLY A  1 139 ? 61.843  55.535  19.326 1.00 37.73 ? 138  GLY A O   1 
ATOM   1011  N  N   . ASN A  1 140 ? 64.079  55.250  19.230 1.00 37.28 ? 139  ASN A N   1 
ATOM   1012  C  CA  . ASN A  1 140 ? 64.323  55.589  20.635 1.00 36.27 ? 139  ASN A CA  1 
ATOM   1013  C  C   . ASN A  1 140 ? 63.451  54.789  21.608 1.00 36.17 ? 139  ASN A C   1 
ATOM   1014  O  O   . ASN A  1 140 ? 62.978  55.323  22.617 1.00 34.91 ? 139  ASN A O   1 
ATOM   1015  C  CB  . ASN A  1 140 ? 64.091  57.090  20.858 1.00 37.56 ? 139  ASN A CB  1 
ATOM   1016  C  CG  . ASN A  1 140 ? 65.070  57.956  20.082 1.00 39.34 ? 139  ASN A CG  1 
ATOM   1017  O  OD1 . ASN A  1 140 ? 66.274  57.940  20.341 1.00 40.66 ? 139  ASN A OD1 1 
ATOM   1018  N  ND2 . ASN A  1 140 ? 64.556  58.714  19.121 1.00 40.05 ? 139  ASN A ND2 1 
ATOM   1019  N  N   . ALA A  1 141 ? 63.253  53.505  21.323 1.00 34.07 ? 140  ALA A N   1 
ATOM   1020  C  CA  . ALA A  1 141 ? 62.424  52.662  22.179 1.00 34.48 ? 140  ALA A CA  1 
ATOM   1021  C  C   . ALA A  1 141 ? 63.124  52.179  23.457 1.00 34.14 ? 140  ALA A C   1 
ATOM   1022  O  O   . ALA A  1 141 ? 62.503  51.543  24.308 1.00 34.74 ? 140  ALA A O   1 
ATOM   1023  C  CB  . ALA A  1 141 ? 61.904  51.465  21.379 1.00 34.08 ? 140  ALA A CB  1 
ATOM   1024  N  N   . GLY A  1 142 ? 64.413  52.465  23.586 1.00 34.57 ? 141  GLY A N   1 
ATOM   1025  C  CA  . GLY A  1 142 ? 65.130  52.055  24.782 1.00 34.95 ? 141  GLY A CA  1 
ATOM   1026  C  C   . GLY A  1 142 ? 65.525  50.590  24.849 1.00 35.21 ? 141  GLY A C   1 
ATOM   1027  O  O   . GLY A  1 142 ? 65.589  49.906  23.825 1.00 36.19 ? 141  GLY A O   1 
ATOM   1028  N  N   . SER A  1 143 ? 65.775  50.103  26.062 1.00 32.89 ? 142  SER A N   1 
ATOM   1029  C  CA  . SER A  1 143 ? 66.200  48.723  26.271 1.00 32.04 ? 142  SER A CA  1 
ATOM   1030  C  C   . SER A  1 143 ? 65.143  47.672  25.943 1.00 30.72 ? 142  SER A C   1 
ATOM   1031  O  O   . SER A  1 143 ? 63.956  47.972  25.800 1.00 28.79 ? 142  SER A O   1 
ATOM   1032  C  CB  . SER A  1 143 ? 66.693  48.527  27.715 1.00 31.57 ? 142  SER A CB  1 
ATOM   1033  O  OG  . SER A  1 143 ? 65.621  48.541  28.641 1.00 35.08 ? 142  SER A OG  1 
ATOM   1034  N  N   . ARG A  1 144 ? 65.597  46.429  25.827 1.00 29.48 ? 143  ARG A N   1 
ATOM   1035  C  CA  . ARG A  1 144 ? 64.721  45.312  25.507 1.00 28.21 ? 143  ARG A CA  1 
ATOM   1036  C  C   . ARG A  1 144 ? 64.320  44.616  26.802 1.00 28.19 ? 143  ARG A C   1 
ATOM   1037  O  O   . ARG A  1 144 ? 65.131  43.937  27.422 1.00 28.02 ? 143  ARG A O   1 
ATOM   1038  C  CB  . ARG A  1 144 ? 65.461  44.360  24.565 1.00 27.52 ? 143  ARG A CB  1 
ATOM   1039  C  CG  . ARG A  1 144 ? 66.077  45.105  23.384 1.00 27.77 ? 143  ARG A CG  1 
ATOM   1040  C  CD  . ARG A  1 144 ? 66.924  44.230  22.467 1.00 27.58 ? 143  ARG A CD  1 
ATOM   1041  N  NE  . ARG A  1 144 ? 67.526  45.057  21.426 1.00 25.19 ? 143  ARG A NE  1 
ATOM   1042  C  CZ  . ARG A  1 144 ? 68.288  44.612  20.433 1.00 27.30 ? 143  ARG A CZ  1 
ATOM   1043  N  NH1 . ARG A  1 144 ? 68.779  45.476  19.552 1.00 25.03 ? 143  ARG A NH1 1 
ATOM   1044  N  NH2 . ARG A  1 144 ? 68.555  43.315  20.311 1.00 25.11 ? 143  ARG A NH2 1 
ATOM   1045  N  N   . LEU A  1 145 ? 63.061  44.784  27.198 1.00 27.42 ? 144  LEU A N   1 
ATOM   1046  C  CA  . LEU A  1 145 ? 62.556  44.205  28.440 1.00 27.39 ? 144  LEU A CA  1 
ATOM   1047  C  C   . LEU A  1 145 ? 62.238  42.717  28.389 1.00 27.19 ? 144  LEU A C   1 
ATOM   1048  O  O   . LEU A  1 145 ? 62.460  41.997  29.363 1.00 25.86 ? 144  LEU A O   1 
ATOM   1049  C  CB  . LEU A  1 145 ? 61.310  44.969  28.899 1.00 29.54 ? 144  LEU A CB  1 
ATOM   1050  C  CG  . LEU A  1 145 ? 61.466  46.478  29.124 1.00 31.82 ? 144  LEU A CG  1 
ATOM   1051  C  CD1 . LEU A  1 145 ? 60.160  47.033  29.674 1.00 34.57 ? 144  LEU A CD1 1 
ATOM   1052  C  CD2 . LEU A  1 145 ? 62.611  46.749  30.095 1.00 33.08 ? 144  LEU A CD2 1 
ATOM   1053  N  N   . ALA A  1 146 ? 61.700  42.255  27.266 1.00 25.82 ? 145  ALA A N   1 
ATOM   1054  C  CA  . ALA A  1 146 ? 61.361  40.843  27.116 1.00 24.28 ? 145  ALA A CA  1 
ATOM   1055  C  C   . ALA A  1 146 ? 61.321  40.494  25.632 1.00 24.33 ? 145  ALA A C   1 
ATOM   1056  O  O   . ALA A  1 146 ? 61.061  41.360  24.792 1.00 23.16 ? 145  ALA A O   1 
ATOM   1057  C  CB  . ALA A  1 146 ? 60.022  40.553  27.762 1.00 24.58 ? 145  ALA A CB  1 
ATOM   1058  N  N   . CYS A  1 147 ? 61.575  39.230  25.311 1.00 22.81 ? 146  CYS A N   1 
ATOM   1059  C  CA  . CYS A  1 147 ? 61.589  38.807  23.914 1.00 23.11 ? 146  CYS A CA  1 
ATOM   1060  C  C   . CYS A  1 147 ? 61.430  37.299  23.817 1.00 23.15 ? 146  CYS A C   1 
ATOM   1061  O  O   . CYS A  1 147 ? 61.558  36.580  24.813 1.00 22.52 ? 146  CYS A O   1 
ATOM   1062  C  CB  . CYS A  1 147 ? 62.913  39.233  23.258 1.00 22.46 ? 146  CYS A CB  1 
ATOM   1063  S  SG  . CYS A  1 147 ? 64.371  38.510  24.086 1.00 24.26 ? 146  CYS A SG  1 
ATOM   1064  N  N   . GLY A  1 148 ? 61.154  36.826  22.607 1.00 23.44 ? 147  GLY A N   1 
ATOM   1065  C  CA  . GLY A  1 148 ? 60.987  35.399  22.389 1.00 22.56 ? 147  GLY A CA  1 
ATOM   1066  C  C   . GLY A  1 148 ? 61.137  35.068  20.920 1.00 22.27 ? 147  GLY A C   1 
ATOM   1067  O  O   . GLY A  1 148 ? 60.813  35.898  20.064 1.00 21.38 ? 147  GLY A O   1 
ATOM   1068  N  N   . VAL A  1 149 ? 61.640  33.875  20.616 1.00 23.00 ? 148  VAL A N   1 
ATOM   1069  C  CA  . VAL A  1 149 ? 61.800  33.462  19.224 1.00 21.74 ? 148  VAL A CA  1 
ATOM   1070  C  C   . VAL A  1 149 ? 60.425  33.113  18.669 1.00 22.32 ? 148  VAL A C   1 
ATOM   1071  O  O   . VAL A  1 149 ? 59.616  32.454  19.336 1.00 23.06 ? 148  VAL A O   1 
ATOM   1072  C  CB  . VAL A  1 149 ? 62.728  32.227  19.095 1.00 22.37 ? 148  VAL A CB  1 
ATOM   1073  C  CG1 . VAL A  1 149 ? 62.922  31.867  17.618 1.00 18.91 ? 148  VAL A CG1 1 
ATOM   1074  C  CG2 . VAL A  1 149 ? 64.074  32.521  19.747 1.00 20.35 ? 148  VAL A CG2 1 
ATOM   1075  N  N   . ILE A  1 150 ? 60.153  33.572  17.455 1.00 22.61 ? 149  ILE A N   1 
ATOM   1076  C  CA  . ILE A  1 150 ? 58.872  33.315  16.812 1.00 23.76 ? 149  ILE A CA  1 
ATOM   1077  C  C   . ILE A  1 150 ? 58.876  31.902  16.239 1.00 25.15 ? 149  ILE A C   1 
ATOM   1078  O  O   . ILE A  1 150 ? 59.589  31.620  15.273 1.00 23.90 ? 149  ILE A O   1 
ATOM   1079  C  CB  . ILE A  1 150 ? 58.629  34.328  15.682 1.00 25.28 ? 149  ILE A CB  1 
ATOM   1080  C  CG1 . ILE A  1 150 ? 58.614  35.745  16.267 1.00 26.94 ? 149  ILE A CG1 1 
ATOM   1081  C  CG2 . ILE A  1 150 ? 57.313  34.018  14.973 1.00 23.89 ? 149  ILE A CG2 1 
ATOM   1082  C  CD1 . ILE A  1 150 ? 58.703  36.853  15.226 1.00 26.77 ? 149  ILE A CD1 1 
ATOM   1083  N  N   . GLY A  1 151 ? 58.083  31.015  16.836 1.00 24.10 ? 150  GLY A N   1 
ATOM   1084  C  CA  . GLY A  1 151 ? 58.042  29.639  16.375 1.00 24.58 ? 150  GLY A CA  1 
ATOM   1085  C  C   . GLY A  1 151 ? 56.743  29.194  15.723 1.00 25.40 ? 150  GLY A C   1 
ATOM   1086  O  O   . GLY A  1 151 ? 55.672  29.752  15.972 1.00 25.10 ? 150  GLY A O   1 
ATOM   1087  N  N   . ILE A  1 152 ? 56.839  28.174  14.878 1.00 24.73 ? 151  ILE A N   1 
ATOM   1088  C  CA  . ILE A  1 152 ? 55.668  27.640  14.191 1.00 26.20 ? 151  ILE A CA  1 
ATOM   1089  C  C   . ILE A  1 152 ? 54.729  27.028  15.228 1.00 25.75 ? 151  ILE A C   1 
ATOM   1090  O  O   . ILE A  1 152 ? 55.178  26.326  16.123 1.00 24.95 ? 151  ILE A O   1 
ATOM   1091  C  CB  . ILE A  1 152 ? 56.081  26.549  13.178 1.00 25.76 ? 151  ILE A CB  1 
ATOM   1092  C  CG1 . ILE A  1 152 ? 56.964  27.169  12.092 1.00 25.00 ? 151  ILE A CG1 1 
ATOM   1093  C  CG2 . ILE A  1 152 ? 54.844  25.883  12.588 1.00 23.92 ? 151  ILE A CG2 1 
ATOM   1094  C  CD1 . ILE A  1 152 ? 57.651  26.149  11.193 1.00 28.31 ? 151  ILE A CD1 1 
ATOM   1095  N  N   . ALA A  1 153 ? 53.434  27.300  15.110 1.00 25.33 ? 152  ALA A N   1 
ATOM   1096  C  CA  . ALA A  1 153 ? 52.465  26.759  16.057 1.00 28.24 ? 152  ALA A CA  1 
ATOM   1097  C  C   . ALA A  1 153 ? 51.407  25.902  15.369 1.00 28.63 ? 152  ALA A C   1 
ATOM   1098  O  O   . ALA A  1 153 ? 51.185  26.016  14.165 1.00 28.63 ? 152  ALA A O   1 
ATOM   1099  C  CB  . ALA A  1 153 ? 51.796  27.895  16.826 1.00 28.37 ? 152  ALA A CB  1 
ATOM   1100  N  N   . GLN A  1 154 ? 50.751  25.046  16.144 1.00 31.48 ? 153  GLN A N   1 
ATOM   1101  C  CA  . GLN A  1 154 ? 49.720  24.172  15.602 1.00 34.11 ? 153  GLN A CA  1 
ATOM   1102  C  C   . GLN A  1 154 ? 48.469  24.973  15.269 1.00 37.14 ? 153  GLN A C   1 
ATOM   1103  O  O   . GLN A  1 154 ? 47.965  24.820  14.136 1.00 39.15 ? 153  GLN A O   1 
ATOM   1104  C  CB  . GLN A  1 154 ? 49.367  23.077  16.607 1.00 36.24 ? 153  GLN A CB  1 
ATOM   1105  C  CG  . GLN A  1 154 ? 48.605  21.912  15.990 1.00 39.22 ? 153  GLN A CG  1 
ATOM   1106  C  CD  . GLN A  1 154 ? 48.156  20.895  17.020 1.00 40.90 ? 153  GLN A CD  1 
ATOM   1107  O  OE1 . GLN A  1 154 ? 47.973  19.718  16.706 1.00 42.57 ? 153  GLN A OE1 1 
ATOM   1108  N  NE2 . GLN A  1 154 ? 47.962  21.346  18.253 1.00 40.29 ? 153  GLN A NE2 1 
ATOM   1109  O  OXT . GLN A  1 154 ? 48.007  25.736  16.149 1.00 37.46 ? 153  GLN A OXT 1 
ATOM   1110  N  N   . ALA B  1 2   ? 68.132  30.004  5.874  0.00 44.64 ? 1    ALA B N   1 
ATOM   1111  C  CA  . ALA B  1 2   ? 69.306  30.577  6.592  0.00 44.59 ? 1    ALA B CA  1 
ATOM   1112  C  C   . ALA B  1 2   ? 70.522  29.670  6.447  1.00 44.34 ? 1    ALA B C   1 
ATOM   1113  O  O   . ALA B  1 2   ? 70.407  28.524  6.021  1.00 46.87 ? 1    ALA B O   1 
ATOM   1114  C  CB  . ALA B  1 2   ? 68.970  30.767  8.065  0.00 44.67 ? 1    ALA B CB  1 
ATOM   1115  N  N   . THR B  1 3   ? 71.691  30.190  6.798  1.00 42.16 ? 2    THR B N   1 
ATOM   1116  C  CA  . THR B  1 3   ? 72.916  29.414  6.705  1.00 39.12 ? 2    THR B CA  1 
ATOM   1117  C  C   . THR B  1 3   ? 73.399  29.059  8.117  1.00 34.22 ? 2    THR B C   1 
ATOM   1118  O  O   . THR B  1 3   ? 74.180  28.126  8.297  1.00 29.84 ? 2    THR B O   1 
ATOM   1119  C  CB  . THR B  1 3   ? 73.997  30.197  5.926  1.00 40.26 ? 2    THR B CB  1 
ATOM   1120  O  OG1 . THR B  1 3   ? 75.112  29.345  5.664  1.00 45.41 ? 2    THR B OG1 1 
ATOM   1121  C  CG2 . THR B  1 3   ? 74.461  31.399  6.711  1.00 44.76 ? 2    THR B CG2 1 
ATOM   1122  N  N   . LYS B  1 4   ? 72.911  29.803  9.111  1.00 29.53 ? 3    LYS B N   1 
ATOM   1123  C  CA  . LYS B  1 4   ? 73.250  29.559  10.514 1.00 27.50 ? 3    LYS B CA  1 
ATOM   1124  C  C   . LYS B  1 4   ? 71.968  29.630  11.348 1.00 25.91 ? 3    LYS B C   1 
ATOM   1125  O  O   . LYS B  1 4   ? 71.053  30.394  11.039 1.00 22.90 ? 3    LYS B O   1 
ATOM   1126  C  CB  . LYS B  1 4   ? 74.235  30.612  11.047 1.00 30.63 ? 3    LYS B CB  1 
ATOM   1127  C  CG  . LYS B  1 4   ? 75.642  30.611  10.424 1.00 33.67 ? 3    LYS B CG  1 
ATOM   1128  C  CD  . LYS B  1 4   ? 76.650  29.794  11.233 1.00 37.22 ? 3    LYS B CD  1 
ATOM   1129  C  CE  . LYS B  1 4   ? 76.892  30.349  12.650 1.00 34.90 ? 3    LYS B CE  1 
ATOM   1130  N  NZ  . LYS B  1 4   ? 77.655  31.635  12.709 1.00 35.04 ? 3    LYS B NZ  1 
ATOM   1131  N  N   . ALA B  1 5   ? 71.910  28.828  12.402 1.00 22.30 ? 4    ALA B N   1 
ATOM   1132  C  CA  . ALA B  1 5   ? 70.761  28.820  13.298 1.00 22.82 ? 4    ALA B CA  1 
ATOM   1133  C  C   . ALA B  1 5   ? 71.284  28.501  14.691 1.00 20.49 ? 4    ALA B C   1 
ATOM   1134  O  O   . ALA B  1 5   ? 72.434  28.082  14.844 1.00 20.04 ? 4    ALA B O   1 
ATOM   1135  C  CB  . ALA B  1 5   ? 69.738  27.772  12.860 1.00 20.93 ? 4    ALA B CB  1 
ATOM   1136  N  N   . VAL B  1 6   ? 70.449  28.708  15.704 1.00 20.56 ? 5    VAL B N   1 
ATOM   1137  C  CA  . VAL B  1 6   ? 70.857  28.438  17.074 1.00 18.90 ? 5    VAL B CA  1 
ATOM   1138  C  C   . VAL B  1 6   ? 69.638  28.217  17.967 1.00 21.31 ? 5    VAL B C   1 
ATOM   1139  O  O   . VAL B  1 6   ? 68.549  28.726  17.698 1.00 19.85 ? 5    VAL B O   1 
ATOM   1140  C  CB  . VAL B  1 6   ? 71.697  29.617  17.633 1.00 20.93 ? 5    VAL B CB  1 
ATOM   1141  C  CG1 . VAL B  1 6   ? 70.819  30.865  17.766 1.00 20.09 ? 5    VAL B CG1 1 
ATOM   1142  C  CG2 . VAL B  1 6   ? 72.328  29.232  18.972 1.00 21.10 ? 5    VAL B CG2 1 
ATOM   1143  N  N   . ALA B  1 7   ? 69.822  27.431  19.020 1.00 22.29 ? 6    ALA B N   1 
ATOM   1144  C  CA  . ALA B  1 7   ? 68.743  27.181  19.956 1.00 22.72 ? 6    ALA B CA  1 
ATOM   1145  C  C   . ALA B  1 7   ? 69.311  27.178  21.365 1.00 22.91 ? 6    ALA B C   1 
ATOM   1146  O  O   . ALA B  1 7   ? 70.328  26.538  21.636 1.00 22.82 ? 6    ALA B O   1 
ATOM   1147  C  CB  . ALA B  1 7   ? 68.068  25.840  19.659 1.00 21.39 ? 6    ALA B CB  1 
ATOM   1148  N  N   . VAL B  1 8   ? 68.651  27.903  22.259 1.00 21.87 ? 7    VAL B N   1 
ATOM   1149  C  CA  . VAL B  1 8   ? 69.077  27.959  23.649 1.00 22.44 ? 7    VAL B CA  1 
ATOM   1150  C  C   . VAL B  1 8   ? 68.181  26.982  24.390 1.00 21.52 ? 7    VAL B C   1 
ATOM   1151  O  O   . VAL B  1 8   ? 66.965  27.152  24.421 1.00 20.14 ? 7    VAL B O   1 
ATOM   1152  C  CB  . VAL B  1 8   ? 68.902  29.379  24.228 1.00 21.34 ? 7    VAL B CB  1 
ATOM   1153  C  CG1 . VAL B  1 8   ? 69.281  29.392  25.702 1.00 22.23 ? 7    VAL B CG1 1 
ATOM   1154  C  CG2 . VAL B  1 8   ? 69.772  30.352  23.455 1.00 23.39 ? 7    VAL B CG2 1 
ATOM   1155  N  N   . LEU B  1 9   ? 68.786  25.947  24.959 1.00 22.80 ? 8    LEU B N   1 
ATOM   1156  C  CA  . LEU B  1 9   ? 68.043  24.919  25.672 1.00 21.68 ? 8    LEU B CA  1 
ATOM   1157  C  C   . LEU B  1 9   ? 67.824  25.244  27.145 1.00 23.19 ? 8    LEU B C   1 
ATOM   1158  O  O   . LEU B  1 9   ? 68.767  25.551  27.870 1.00 22.76 ? 8    LEU B O   1 
ATOM   1159  C  CB  . LEU B  1 9   ? 68.773  23.579  25.550 1.00 23.33 ? 8    LEU B CB  1 
ATOM   1160  C  CG  . LEU B  1 9   ? 69.005  23.103  24.107 1.00 24.36 ? 8    LEU B CG  1 
ATOM   1161  C  CD1 . LEU B  1 9   ? 69.725  21.769  24.097 1.00 24.20 ? 8    LEU B CD1 1 
ATOM   1162  C  CD2 . LEU B  1 9   ? 67.662  22.981  23.398 1.00 26.48 ? 8    LEU B CD2 1 
ATOM   1163  N  N   . LYS B  1 10  ? 66.568  25.168  27.572 1.00 24.89 ? 9    LYS B N   1 
ATOM   1164  C  CA  . LYS B  1 10  ? 66.191  25.420  28.960 1.00 29.00 ? 9    LYS B CA  1 
ATOM   1165  C  C   . LYS B  1 10  ? 65.014  24.521  29.327 1.00 29.83 ? 9    LYS B C   1 
ATOM   1166  O  O   . LYS B  1 10  ? 64.181  24.200  28.479 1.00 28.61 ? 9    LYS B O   1 
ATOM   1167  C  CB  . LYS B  1 10  ? 65.800  26.889  29.157 1.00 30.28 ? 9    LYS B CB  1 
ATOM   1168  C  CG  . LYS B  1 10  ? 66.987  27.829  29.094 1.00 37.69 ? 9    LYS B CG  1 
ATOM   1169  C  CD  . LYS B  1 10  ? 66.574  29.293  29.103 1.00 41.96 ? 9    LYS B CD  1 
ATOM   1170  C  CE  . LYS B  1 10  ? 67.796  30.193  28.951 1.00 42.18 ? 9    LYS B CE  1 
ATOM   1171  N  NZ  . LYS B  1 10  ? 67.412  31.595  28.635 1.00 44.11 ? 9    LYS B NZ  1 
ATOM   1172  N  N   . GLY B  1 11  ? 64.963  24.113  30.591 1.00 30.85 ? 10   GLY B N   1 
ATOM   1173  C  CA  . GLY B  1 11  ? 63.886  23.263  31.064 1.00 33.46 ? 10   GLY B CA  1 
ATOM   1174  C  C   . GLY B  1 11  ? 63.575  23.562  32.521 1.00 36.28 ? 10   GLY B C   1 
ATOM   1175  O  O   . GLY B  1 11  ? 64.028  24.570  33.059 1.00 36.33 ? 10   GLY B O   1 
ATOM   1176  N  N   . ASP B  1 12  ? 62.811  22.691  33.166 1.00 38.07 ? 11   ASP B N   1 
ATOM   1177  C  CA  . ASP B  1 12  ? 62.462  22.899  34.566 1.00 41.70 ? 11   ASP B CA  1 
ATOM   1178  C  C   . ASP B  1 12  ? 63.583  22.478  35.508 1.00 41.72 ? 11   ASP B C   1 
ATOM   1179  O  O   . ASP B  1 12  ? 63.627  22.913  36.659 1.00 44.97 ? 11   ASP B O   1 
ATOM   1180  C  CB  . ASP B  1 12  ? 61.185  22.135  34.913 1.00 44.76 ? 11   ASP B CB  1 
ATOM   1181  C  CG  . ASP B  1 12  ? 59.997  22.592  34.094 1.00 47.77 ? 11   ASP B CG  1 
ATOM   1182  O  OD1 . ASP B  1 12  ? 59.758  23.817  34.028 1.00 49.83 ? 11   ASP B OD1 1 
ATOM   1183  O  OD2 . ASP B  1 12  ? 59.300  21.729  33.519 1.00 50.04 ? 11   ASP B OD2 1 
ATOM   1184  N  N   . GLY B  1 13  ? 64.484  21.631  35.020 1.00 38.87 ? 12   GLY B N   1 
ATOM   1185  C  CA  . GLY B  1 13  ? 65.593  21.176  35.838 1.00 34.82 ? 12   GLY B CA  1 
ATOM   1186  C  C   . GLY B  1 13  ? 66.876  21.925  35.529 1.00 32.53 ? 12   GLY B C   1 
ATOM   1187  O  O   . GLY B  1 13  ? 66.830  23.059  35.064 1.00 32.50 ? 12   GLY B O   1 
ATOM   1188  N  N   . PRO B  1 14  ? 68.042  21.309  35.768 1.00 31.33 ? 13   PRO B N   1 
ATOM   1189  C  CA  . PRO B  1 14  ? 69.358  21.908  35.524 1.00 31.86 ? 13   PRO B CA  1 
ATOM   1190  C  C   . PRO B  1 14  ? 69.880  21.833  34.084 1.00 31.59 ? 13   PRO B C   1 
ATOM   1191  O  O   . PRO B  1 14  ? 70.898  22.446  33.757 1.00 31.87 ? 13   PRO B O   1 
ATOM   1192  C  CB  . PRO B  1 14  ? 70.255  21.136  36.482 1.00 31.65 ? 13   PRO B CB  1 
ATOM   1193  C  CG  . PRO B  1 14  ? 69.678  19.756  36.377 1.00 32.75 ? 13   PRO B CG  1 
ATOM   1194  C  CD  . PRO B  1 14  ? 68.182  20.014  36.456 1.00 30.73 ? 13   PRO B CD  1 
ATOM   1195  N  N   . VAL B  1 15  ? 69.203  21.084  33.225 1.00 29.01 ? 14   VAL B N   1 
ATOM   1196  C  CA  . VAL B  1 15  ? 69.672  20.956  31.849 1.00 27.43 ? 14   VAL B CA  1 
ATOM   1197  C  C   . VAL B  1 15  ? 69.594  22.259  31.073 1.00 25.82 ? 14   VAL B C   1 
ATOM   1198  O  O   . VAL B  1 15  ? 68.529  22.850  30.938 1.00 26.36 ? 14   VAL B O   1 
ATOM   1199  C  CB  . VAL B  1 15  ? 68.878  19.889  31.078 1.00 25.50 ? 14   VAL B CB  1 
ATOM   1200  C  CG1 . VAL B  1 15  ? 69.437  19.754  29.666 1.00 24.33 ? 14   VAL B CG1 1 
ATOM   1201  C  CG2 . VAL B  1 15  ? 68.957  18.565  31.808 1.00 26.42 ? 14   VAL B CG2 1 
ATOM   1202  N  N   . GLN B  1 16  ? 70.733  22.705  30.560 1.00 27.49 ? 15   GLN B N   1 
ATOM   1203  C  CA  . GLN B  1 16  ? 70.778  23.937  29.785 1.00 28.36 ? 15   GLN B CA  1 
ATOM   1204  C  C   . GLN B  1 16  ? 71.975  23.946  28.851 1.00 26.49 ? 15   GLN B C   1 
ATOM   1205  O  O   . GLN B  1 16  ? 72.991  23.291  29.110 1.00 24.75 ? 15   GLN B O   1 
ATOM   1206  C  CB  . GLN B  1 16  ? 70.831  25.156  30.716 1.00 33.26 ? 15   GLN B CB  1 
ATOM   1207  C  CG  . GLN B  1 16  ? 71.897  25.073  31.785 1.00 38.24 ? 15   GLN B CG  1 
ATOM   1208  C  CD  . GLN B  1 16  ? 71.854  26.254  32.740 1.00 44.35 ? 15   GLN B CD  1 
ATOM   1209  O  OE1 . GLN B  1 16  ? 72.076  27.398  32.342 1.00 45.69 ? 15   GLN B OE1 1 
ATOM   1210  N  NE2 . GLN B  1 16  ? 71.563  25.980  34.010 1.00 46.15 ? 15   GLN B NE2 1 
ATOM   1211  N  N   . GLY B  1 17  ? 71.855  24.694  27.759 1.00 23.74 ? 16   GLY B N   1 
ATOM   1212  C  CA  . GLY B  1 17  ? 72.947  24.759  26.812 1.00 24.11 ? 16   GLY B CA  1 
ATOM   1213  C  C   . GLY B  1 17  ? 72.598  25.489  25.536 1.00 22.56 ? 16   GLY B C   1 
ATOM   1214  O  O   . GLY B  1 17  ? 71.458  25.895  25.328 1.00 24.24 ? 16   GLY B O   1 
ATOM   1215  N  N   . ILE B  1 18  ? 73.598  25.654  24.681 1.00 21.47 ? 17   ILE B N   1 
ATOM   1216  C  CA  . ILE B  1 18  ? 73.423  26.341  23.410 1.00 21.49 ? 17   ILE B CA  1 
ATOM   1217  C  C   . ILE B  1 18  ? 73.853  25.428  22.267 1.00 20.87 ? 17   ILE B C   1 
ATOM   1218  O  O   . ILE B  1 18  ? 74.983  24.941  22.239 1.00 20.68 ? 17   ILE B O   1 
ATOM   1219  C  CB  . ILE B  1 18  ? 74.282  27.624  23.348 1.00 21.81 ? 17   ILE B CB  1 
ATOM   1220  C  CG1 . ILE B  1 18  ? 73.823  28.613  24.425 1.00 23.28 ? 17   ILE B CG1 1 
ATOM   1221  C  CG2 . ILE B  1 18  ? 74.189  28.238  21.947 1.00 23.04 ? 17   ILE B CG2 1 
ATOM   1222  C  CD1 . ILE B  1 18  ? 74.778  29.781  24.646 1.00 25.05 ? 17   ILE B CD1 1 
ATOM   1223  N  N   . ILE B  1 19  ? 72.959  25.212  21.313 1.00 21.02 ? 18   ILE B N   1 
ATOM   1224  C  CA  . ILE B  1 19  ? 73.287  24.361  20.179 1.00 19.46 ? 18   ILE B CA  1 
ATOM   1225  C  C   . ILE B  1 19  ? 73.287  25.209  18.920 1.00 21.60 ? 18   ILE B C   1 
ATOM   1226  O  O   . ILE B  1 19  ? 72.338  25.958  18.664 1.00 21.54 ? 18   ILE B O   1 
ATOM   1227  C  CB  . ILE B  1 19  ? 72.263  23.197  20.038 1.00 18.90 ? 18   ILE B CB  1 
ATOM   1228  C  CG1 . ILE B  1 19  ? 72.368  22.268  21.246 1.00 15.07 ? 18   ILE B CG1 1 
ATOM   1229  C  CG2 . ILE B  1 19  ? 72.519  22.420  18.756 1.00 16.21 ? 18   ILE B CG2 1 
ATOM   1230  C  CD1 . ILE B  1 19  ? 73.733  21.580  21.390 1.00 14.89 ? 18   ILE B CD1 1 
ATOM   1231  N  N   . ASN B  1 20  ? 74.362  25.099  18.144 1.00 20.96 ? 19   ASN B N   1 
ATOM   1232  C  CA  . ASN B  1 20  ? 74.493  25.852  16.899 1.00 20.98 ? 19   ASN B CA  1 
ATOM   1233  C  C   . ASN B  1 20  ? 74.278  24.928  15.706 1.00 20.99 ? 19   ASN B C   1 
ATOM   1234  O  O   . ASN B  1 20  ? 74.590  23.736  15.765 1.00 20.37 ? 19   ASN B O   1 
ATOM   1235  C  CB  . ASN B  1 20  ? 75.896  26.474  16.793 1.00 22.36 ? 19   ASN B CB  1 
ATOM   1236  C  CG  . ASN B  1 20  ? 76.279  27.284  18.024 1.00 22.87 ? 19   ASN B CG  1 
ATOM   1237  O  OD1 . ASN B  1 20  ? 75.823  28.405  18.206 1.00 23.62 ? 19   ASN B OD1 1 
ATOM   1238  N  ND2 . ASN B  1 20  ? 77.115  26.705  18.879 1.00 21.85 ? 19   ASN B ND2 1 
ATOM   1239  N  N   . PHE B  1 21  ? 73.755  25.495  14.622 1.00 22.31 ? 20   PHE B N   1 
ATOM   1240  C  CA  . PHE B  1 21  ? 73.506  24.757  13.388 1.00 21.74 ? 20   PHE B CA  1 
ATOM   1241  C  C   . PHE B  1 21  ? 74.126  25.569  12.256 1.00 22.55 ? 20   PHE B C   1 
ATOM   1242  O  O   . PHE B  1 21  ? 73.974  26.790  12.210 1.00 19.50 ? 20   PHE B O   1 
ATOM   1243  C  CB  . PHE B  1 21  ? 72.007  24.640  13.101 1.00 19.88 ? 20   PHE B CB  1 
ATOM   1244  C  CG  . PHE B  1 21  ? 71.228  23.917  14.159 1.00 21.42 ? 20   PHE B CG  1 
ATOM   1245  C  CD1 . PHE B  1 21  ? 70.851  22.592  13.976 1.00 19.91 ? 20   PHE B CD1 1 
ATOM   1246  C  CD2 . PHE B  1 21  ? 70.805  24.585  15.310 1.00 20.48 ? 20   PHE B CD2 1 
ATOM   1247  C  CE1 . PHE B  1 21  ? 70.057  21.938  14.914 1.00 20.14 ? 20   PHE B CE1 1 
ATOM   1248  C  CE2 . PHE B  1 21  ? 70.011  23.940  16.258 1.00 21.01 ? 20   PHE B CE2 1 
ATOM   1249  C  CZ  . PHE B  1 21  ? 69.632  22.613  16.057 1.00 20.25 ? 20   PHE B CZ  1 
ATOM   1250  N  N   . GLU B  1 22  ? 74.824  24.900  11.347 1.00 21.54 ? 21   GLU B N   1 
ATOM   1251  C  CA  . GLU B  1 22  ? 75.408  25.601  10.213 1.00 23.96 ? 21   GLU B CA  1 
ATOM   1252  C  C   . GLU B  1 22  ? 75.283  24.775  8.946  1.00 23.81 ? 21   GLU B C   1 
ATOM   1253  O  O   . GLU B  1 22  ? 75.645  23.595  8.918  1.00 23.91 ? 21   GLU B O   1 
ATOM   1254  C  CB  . GLU B  1 22  ? 76.876  25.945  10.460 1.00 25.91 ? 21   GLU B CB  1 
ATOM   1255  C  CG  . GLU B  1 22  ? 77.481  26.715  9.284  1.00 34.78 ? 21   GLU B CG  1 
ATOM   1256  C  CD  . GLU B  1 22  ? 78.747  27.454  9.652  1.00 40.65 ? 21   GLU B CD  1 
ATOM   1257  O  OE1 . GLU B  1 22  ? 79.410  27.989  8.736  1.00 43.33 ? 21   GLU B OE1 1 
ATOM   1258  O  OE2 . GLU B  1 22  ? 79.076  27.505  10.856 1.00 42.71 ? 21   GLU B OE2 1 
ATOM   1259  N  N   . GLN B  1 23  ? 74.763  25.405  7.900  1.00 23.89 ? 22   GLN B N   1 
ATOM   1260  C  CA  . GLN B  1 23  ? 74.572  24.744  6.621  1.00 26.13 ? 22   GLN B CA  1 
ATOM   1261  C  C   . GLN B  1 23  ? 75.341  25.530  5.550  1.00 28.56 ? 22   GLN B C   1 
ATOM   1262  O  O   . GLN B  1 23  ? 74.923  26.612  5.139  1.00 27.36 ? 22   GLN B O   1 
ATOM   1263  C  CB  . GLN B  1 23  ? 73.073  24.691  6.308  1.00 26.54 ? 22   GLN B CB  1 
ATOM   1264  C  CG  . GLN B  1 23  ? 72.698  23.915  5.057  1.00 27.53 ? 22   GLN B CG  1 
ATOM   1265  C  CD  . GLN B  1 23  ? 71.196  23.721  4.931  1.00 26.91 ? 22   GLN B CD  1 
ATOM   1266  O  OE1 . GLN B  1 23  ? 70.413  24.600  5.296  1.00 28.58 ? 22   GLN B OE1 1 
ATOM   1267  N  NE2 . GLN B  1 23  ? 70.786  22.572  4.398  1.00 28.86 ? 22   GLN B NE2 1 
ATOM   1268  N  N   . LYS B  1 24  ? 76.473  24.981  5.120  1.00 30.71 ? 23   LYS B N   1 
ATOM   1269  C  CA  . LYS B  1 24  ? 77.323  25.629  4.117  1.00 35.44 ? 23   LYS B CA  1 
ATOM   1270  C  C   . LYS B  1 24  ? 76.612  25.875  2.784  1.00 36.55 ? 23   LYS B C   1 
ATOM   1271  O  O   . LYS B  1 24  ? 76.727  26.960  2.218  1.00 36.77 ? 23   LYS B O   1 
ATOM   1272  C  CB  . LYS B  1 24  ? 78.587  24.794  3.894  1.00 39.33 ? 23   LYS B CB  1 
ATOM   1273  C  CG  . LYS B  1 24  ? 79.570  25.375  2.881  1.00 43.81 ? 23   LYS B CG  1 
ATOM   1274  C  CD  . LYS B  1 24  ? 80.816  24.502  2.778  1.00 46.79 ? 23   LYS B CD  1 
ATOM   1275  C  CE  . LYS B  1 24  ? 81.751  24.981  1.675  1.00 49.35 ? 23   LYS B CE  1 
ATOM   1276  N  NZ  . LYS B  1 24  ? 82.962  24.122  1.560  0.00 48.73 ? 23   LYS B NZ  1 
ATOM   1277  N  N   . GLU B  1 25  ? 75.884  24.875  2.290  1.00 37.10 ? 24   GLU B N   1 
ATOM   1278  C  CA  . GLU B  1 25  ? 75.143  24.990  1.029  1.00 40.75 ? 24   GLU B CA  1 
ATOM   1279  C  C   . GLU B  1 25  ? 73.648  24.747  1.278  1.00 41.50 ? 24   GLU B C   1 
ATOM   1280  O  O   . GLU B  1 25  ? 73.280  23.843  2.026  1.00 39.71 ? 24   GLU B O   1 
ATOM   1281  C  CB  . GLU B  1 25  ? 75.689  23.987  0.004  1.00 42.71 ? 24   GLU B CB  1 
ATOM   1282  C  CG  . GLU B  1 25  ? 77.186  24.129  -0.268 1.00 47.80 ? 24   GLU B CG  1 
ATOM   1283  C  CD  . GLU B  1 25  ? 77.583  25.540  -0.675 1.00 51.32 ? 24   GLU B CD  1 
ATOM   1284  O  OE1 . GLU B  1 25  ? 76.921  26.119  -1.567 1.00 52.15 ? 24   GLU B OE1 1 
ATOM   1285  O  OE2 . GLU B  1 25  ? 78.563  26.068  -0.106 1.00 53.77 ? 24   GLU B OE2 1 
ATOM   1286  N  N   . SER B  1 26  ? 72.807  25.561  0.639  1.00 43.07 ? 25   SER B N   1 
ATOM   1287  C  CA  . SER B  1 26  ? 71.338  25.524  0.776  1.00 46.62 ? 25   SER B CA  1 
ATOM   1288  C  C   . SER B  1 26  ? 70.646  24.174  0.762  1.00 48.07 ? 25   SER B C   1 
ATOM   1289  O  O   . SER B  1 26  ? 69.445  24.080  0.902  1.00 50.50 ? 25   SER B O   1 
ATOM   1290  C  CB  . SER B  1 26  ? 70.692  26.364  -0.333 1.00 46.45 ? 25   SER B CB  1 
ATOM   1291  O  OG  . SER B  1 26  ? 70.941  25.792  -1.609 1.00 48.35 ? 25   SER B OG  1 
ATOM   1292  N  N   . ASN B  1 27  ? 71.417  23.124  0.608  1.00 48.35 ? 26   ASN B N   1 
ATOM   1293  C  CA  . ASN B  1 27  ? 70.864  21.797  0.484  1.00 48.17 ? 26   ASN B CA  1 
ATOM   1294  C  C   . ASN B  1 27  ? 71.798  20.782  1.104  1.00 46.12 ? 26   ASN B C   1 
ATOM   1295  O  O   . ASN B  1 27  ? 71.418  19.654  1.386  1.00 47.35 ? 26   ASN B O   1 
ATOM   1296  C  CB  . ASN B  1 27  ? 70.736  21.541  -0.997 1.00 52.24 ? 26   ASN B CB  1 
ATOM   1297  C  CG  . ASN B  1 27  ? 71.953  22.012  -1.731 1.00 55.14 ? 26   ASN B CG  1 
ATOM   1298  O  OD1 . ASN B  1 27  ? 72.773  21.207  -2.162 1.00 56.54 ? 26   ASN B OD1 1 
ATOM   1299  N  ND2 . ASN B  1 27  ? 72.113  23.332  -1.832 1.00 56.26 ? 26   ASN B ND2 1 
ATOM   1300  N  N   . GLY B  1 28  ? 73.026  21.221  1.311  1.00 41.57 ? 27   GLY B N   1 
ATOM   1301  C  CA  . GLY B  1 28  ? 74.039  20.360  1.873  1.00 36.46 ? 27   GLY B CA  1 
ATOM   1302  C  C   . GLY B  1 28  ? 73.740  19.953  3.294  1.00 32.49 ? 27   GLY B C   1 
ATOM   1303  O  O   . GLY B  1 28  ? 72.717  20.329  3.867  1.00 30.38 ? 27   GLY B O   1 
ATOM   1304  N  N   . PRO B  1 29  ? 74.637  19.169  3.893  1.00 31.82 ? 28   PRO B N   1 
ATOM   1305  C  CA  . PRO B  1 29  ? 74.467  18.704  5.268  1.00 29.63 ? 28   PRO B CA  1 
ATOM   1306  C  C   . PRO B  1 29  ? 74.467  19.865  6.256  1.00 27.04 ? 28   PRO B C   1 
ATOM   1307  O  O   . PRO B  1 29  ? 74.970  20.949  5.958  1.00 23.94 ? 28   PRO B O   1 
ATOM   1308  C  CB  . PRO B  1 29  ? 75.667  17.786  5.467  1.00 30.61 ? 28   PRO B CB  1 
ATOM   1309  C  CG  . PRO B  1 29  ? 76.715  18.437  4.613  1.00 33.89 ? 28   PRO B CG  1 
ATOM   1310  C  CD  . PRO B  1 29  ? 75.937  18.737  3.353  1.00 33.65 ? 28   PRO B CD  1 
ATOM   1311  N  N   . VAL B  1 30  ? 73.896  19.628  7.430  1.00 23.88 ? 29   VAL B N   1 
ATOM   1312  C  CA  . VAL B  1 30  ? 73.849  20.639  8.474  1.00 22.82 ? 29   VAL B CA  1 
ATOM   1313  C  C   . VAL B  1 30  ? 74.735  20.160  9.607  1.00 22.83 ? 29   VAL B C   1 
ATOM   1314  O  O   . VAL B  1 30  ? 74.604  19.028  10.071 1.00 23.08 ? 29   VAL B O   1 
ATOM   1315  C  CB  . VAL B  1 30  ? 72.416  20.838  9.016  1.00 21.43 ? 29   VAL B CB  1 
ATOM   1316  C  CG1 . VAL B  1 30  ? 72.429  21.832  10.171 1.00 18.74 ? 29   VAL B CG1 1 
ATOM   1317  C  CG2 . VAL B  1 30  ? 71.499  21.331  7.897  1.00 19.64 ? 29   VAL B CG2 1 
ATOM   1318  N  N   . LYS B  1 31  ? 75.661  21.007  10.032 1.00 23.42 ? 30   LYS B N   1 
ATOM   1319  C  CA  . LYS B  1 31  ? 76.536  20.646  11.134 1.00 23.39 ? 30   LYS B CA  1 
ATOM   1320  C  C   . LYS B  1 31  ? 75.872  21.168  12.395 1.00 22.45 ? 30   LYS B C   1 
ATOM   1321  O  O   . LYS B  1 31  ? 75.362  22.294  12.416 1.00 22.84 ? 30   LYS B O   1 
ATOM   1322  C  CB  . LYS B  1 31  ? 77.920  21.277  10.954 1.00 24.26 ? 30   LYS B CB  1 
ATOM   1323  C  CG  . LYS B  1 31  ? 78.718  20.691  9.796  1.00 32.23 ? 30   LYS B CG  1 
ATOM   1324  C  CD  . LYS B  1 31  ? 80.106  21.320  9.712  1.00 38.30 ? 30   LYS B CD  1 
ATOM   1325  C  CE  . LYS B  1 31  ? 81.017  20.549  8.761  1.00 41.42 ? 30   LYS B CE  1 
ATOM   1326  N  NZ  . LYS B  1 31  ? 82.416  21.085  8.788  1.00 47.78 ? 30   LYS B NZ  1 
ATOM   1327  N  N   . VAL B  1 32  ? 75.862  20.345  13.436 1.00 21.37 ? 31   VAL B N   1 
ATOM   1328  C  CA  . VAL B  1 32  ? 75.241  20.706  14.709 1.00 20.76 ? 31   VAL B CA  1 
ATOM   1329  C  C   . VAL B  1 32  ? 76.284  20.555  15.813 1.00 21.66 ? 31   VAL B C   1 
ATOM   1330  O  O   . VAL B  1 32  ? 76.894  19.494  15.954 1.00 22.62 ? 31   VAL B O   1 
ATOM   1331  C  CB  . VAL B  1 32  ? 74.025  19.778  15.005 1.00 20.00 ? 31   VAL B CB  1 
ATOM   1332  C  CG1 . VAL B  1 32  ? 73.275  20.251  16.240 1.00 18.51 ? 31   VAL B CG1 1 
ATOM   1333  C  CG2 . VAL B  1 32  ? 73.088  19.750  13.805 1.00 19.50 ? 31   VAL B CG2 1 
ATOM   1334  N  N   . TRP B  1 33  ? 76.508  21.616  16.585 1.00 21.29 ? 32   TRP B N   1 
ATOM   1335  C  CA  . TRP B  1 33  ? 77.494  21.554  17.661 1.00 21.48 ? 32   TRP B CA  1 
ATOM   1336  C  C   . TRP B  1 33  ? 77.168  22.527  18.780 1.00 22.94 ? 32   TRP B C   1 
ATOM   1337  O  O   . TRP B  1 33  ? 76.503  23.536  18.569 1.00 23.69 ? 32   TRP B O   1 
ATOM   1338  C  CB  . TRP B  1 33  ? 78.895  21.850  17.124 1.00 23.34 ? 32   TRP B CB  1 
ATOM   1339  C  CG  . TRP B  1 33  ? 79.204  23.310  16.987 1.00 26.49 ? 32   TRP B CG  1 
ATOM   1340  C  CD1 . TRP B  1 33  ? 79.877  24.098  17.883 1.00 27.17 ? 32   TRP B CD1 1 
ATOM   1341  C  CD2 . TRP B  1 33  ? 78.853  24.160  15.894 1.00 28.29 ? 32   TRP B CD2 1 
ATOM   1342  N  NE1 . TRP B  1 33  ? 79.968  25.386  17.409 1.00 28.47 ? 32   TRP B NE1 1 
ATOM   1343  C  CE2 . TRP B  1 33  ? 79.343  25.453  16.187 1.00 28.66 ? 32   TRP B CE2 1 
ATOM   1344  C  CE3 . TRP B  1 33  ? 78.160  23.957  14.689 1.00 30.39 ? 32   TRP B CE3 1 
ATOM   1345  C  CZ2 . TRP B  1 33  ? 79.176  26.538  15.322 1.00 28.85 ? 32   TRP B CZ2 1 
ATOM   1346  C  CZ3 . TRP B  1 33  ? 77.991  25.037  13.824 1.00 32.18 ? 32   TRP B CZ3 1 
ATOM   1347  C  CH2 . TRP B  1 33  ? 78.497  26.314  14.149 1.00 32.67 ? 32   TRP B CH2 1 
ATOM   1348  N  N   . GLY B  1 34  ? 77.646  22.210  19.975 1.00 23.54 ? 33   GLY B N   1 
ATOM   1349  C  CA  . GLY B  1 34  ? 77.394  23.060  21.119 1.00 24.15 ? 33   GLY B CA  1 
ATOM   1350  C  C   . GLY B  1 34  ? 77.642  22.277  22.386 1.00 24.98 ? 33   GLY B C   1 
ATOM   1351  O  O   . GLY B  1 34  ? 78.144  21.157  22.346 1.00 27.18 ? 33   GLY B O   1 
ATOM   1352  N  N   . SER B  1 35  ? 77.283  22.858  23.518 1.00 25.74 ? 34   SER B N   1 
ATOM   1353  C  CA  . SER B  1 35  ? 77.487  22.190  24.783 1.00 26.36 ? 34   SER B CA  1 
ATOM   1354  C  C   . SER B  1 35  ? 76.209  22.208  25.612 1.00 27.08 ? 34   SER B C   1 
ATOM   1355  O  O   . SER B  1 35  ? 75.502  23.217  25.661 1.00 27.29 ? 34   SER B O   1 
ATOM   1356  C  CB  . SER B  1 35  ? 78.620  22.883  25.546 1.00 29.02 ? 34   SER B CB  1 
ATOM   1357  O  OG  . SER B  1 35  ? 78.944  22.172  26.723 1.00 33.59 ? 34   SER B OG  1 
ATOM   1358  N  N   . ILE B  1 36  ? 75.906  21.077  26.242 1.00 24.05 ? 35   ILE B N   1 
ATOM   1359  C  CA  . ILE B  1 36  ? 74.731  20.960  27.096 1.00 22.12 ? 35   ILE B CA  1 
ATOM   1360  C  C   . ILE B  1 36  ? 75.250  20.430  28.425 1.00 23.97 ? 35   ILE B C   1 
ATOM   1361  O  O   . ILE B  1 36  ? 75.989  19.442  28.451 1.00 23.70 ? 35   ILE B O   1 
ATOM   1362  C  CB  . ILE B  1 36  ? 73.701  19.949  26.557 1.00 21.82 ? 35   ILE B CB  1 
ATOM   1363  C  CG1 . ILE B  1 36  ? 73.352  20.260  25.098 1.00 23.08 ? 35   ILE B CG1 1 
ATOM   1364  C  CG2 . ILE B  1 36  ? 72.442  19.996  27.424 1.00 20.91 ? 35   ILE B CG2 1 
ATOM   1365  C  CD1 . ILE B  1 36  ? 72.397  19.250  24.467 1.00 24.23 ? 35   ILE B CD1 1 
ATOM   1366  N  N   . LYS B  1 37  ? 74.866  21.080  29.520 1.00 24.60 ? 36   LYS B N   1 
ATOM   1367  C  CA  . LYS B  1 37  ? 75.309  20.667  30.849 1.00 25.41 ? 36   LYS B CA  1 
ATOM   1368  C  C   . LYS B  1 37  ? 74.125  20.310  31.735 1.00 24.43 ? 36   LYS B C   1 
ATOM   1369  O  O   . LYS B  1 37  ? 72.972  20.586  31.393 1.00 24.64 ? 36   LYS B O   1 
ATOM   1370  C  CB  . LYS B  1 37  ? 76.105  21.792  31.516 1.00 30.23 ? 36   LYS B CB  1 
ATOM   1371  C  CG  . LYS B  1 37  ? 75.245  23.000  31.873 1.00 35.26 ? 36   LYS B CG  1 
ATOM   1372  C  CD  . LYS B  1 37  ? 76.026  24.036  32.670 1.00 41.52 ? 36   LYS B CD  1 
ATOM   1373  C  CE  . LYS B  1 37  ? 75.145  25.234  33.020 1.00 43.12 ? 36   LYS B CE  1 
ATOM   1374  N  NZ  . LYS B  1 37  ? 75.920  26.314  33.697 1.00 47.27 ? 36   LYS B NZ  1 
ATOM   1375  N  N   . GLY B  1 38  ? 74.416  19.692  32.878 1.00 24.81 ? 37   GLY B N   1 
ATOM   1376  C  CA  . GLY B  1 38  ? 73.366  19.318  33.813 1.00 22.73 ? 37   GLY B CA  1 
ATOM   1377  C  C   . GLY B  1 38  ? 72.670  18.007  33.498 1.00 23.60 ? 37   GLY B C   1 
ATOM   1378  O  O   . GLY B  1 38  ? 71.629  17.702  34.076 1.00 23.97 ? 37   GLY B O   1 
ATOM   1379  N  N   . LEU B  1 39  ? 73.248  17.220  32.597 1.00 24.31 ? 38   LEU B N   1 
ATOM   1380  C  CA  . LEU B  1 39  ? 72.669  15.935  32.204 1.00 23.66 ? 38   LEU B CA  1 
ATOM   1381  C  C   . LEU B  1 39  ? 73.275  14.769  32.965 1.00 24.06 ? 38   LEU B C   1 
ATOM   1382  O  O   . LEU B  1 39  ? 74.379  14.868  33.479 1.00 24.00 ? 38   LEU B O   1 
ATOM   1383  C  CB  . LEU B  1 39  ? 72.906  15.690  30.714 1.00 23.38 ? 38   LEU B CB  1 
ATOM   1384  C  CG  . LEU B  1 39  ? 72.220  16.616  29.713 1.00 23.27 ? 38   LEU B CG  1 
ATOM   1385  C  CD1 . LEU B  1 39  ? 72.937  16.536  28.363 1.00 22.41 ? 38   LEU B CD1 1 
ATOM   1386  C  CD2 . LEU B  1 39  ? 70.750  16.217  29.595 1.00 21.82 ? 38   LEU B CD2 1 
ATOM   1387  N  N   . THR B  1 40  ? 72.546  13.658  33.032 1.00 25.60 ? 39   THR B N   1 
ATOM   1388  C  CA  . THR B  1 40  ? 73.072  12.463  33.678 1.00 27.44 ? 39   THR B CA  1 
ATOM   1389  C  C   . THR B  1 40  ? 74.031  11.847  32.658 1.00 28.48 ? 39   THR B C   1 
ATOM   1390  O  O   . THR B  1 40  ? 73.832  11.983  31.445 1.00 26.73 ? 39   THR B O   1 
ATOM   1391  C  CB  . THR B  1 40  ? 71.966  11.440  33.980 1.00 27.76 ? 39   THR B CB  1 
ATOM   1392  O  OG1 . THR B  1 40  ? 71.251  11.146  32.773 1.00 29.78 ? 39   THR B OG1 1 
ATOM   1393  C  CG2 . THR B  1 40  ? 70.996  11.987  35.022 1.00 28.41 ? 39   THR B CG2 1 
ATOM   1394  N  N   . GLU B  1 41  ? 75.069  11.177  33.142 1.00 26.94 ? 40   GLU B N   1 
ATOM   1395  C  CA  . GLU B  1 41  ? 76.048  10.559  32.256 1.00 27.17 ? 40   GLU B CA  1 
ATOM   1396  C  C   . GLU B  1 41  ? 75.386  9.539   31.324 1.00 26.19 ? 40   GLU B C   1 
ATOM   1397  O  O   . GLU B  1 41  ? 74.528  8.769   31.744 1.00 23.69 ? 40   GLU B O   1 
ATOM   1398  C  CB  . GLU B  1 41  ? 77.135  9.871   33.090 1.00 28.67 ? 40   GLU B CB  1 
ATOM   1399  C  CG  . GLU B  1 41  ? 78.298  9.314   32.288 1.00 30.61 ? 40   GLU B CG  1 
ATOM   1400  C  CD  . GLU B  1 41  ? 79.313  8.601   33.167 1.00 36.07 ? 40   GLU B CD  1 
ATOM   1401  O  OE1 . GLU B  1 41  ? 80.354  8.153   32.638 1.00 38.62 ? 40   GLU B OE1 1 
ATOM   1402  O  OE2 . GLU B  1 41  ? 79.068  8.486   34.387 1.00 36.85 ? 40   GLU B OE2 1 
ATOM   1403  N  N   . GLY B  1 42  ? 75.783  9.542   30.055 1.00 24.99 ? 41   GLY B N   1 
ATOM   1404  C  CA  . GLY B  1 42  ? 75.211  8.590   29.116 1.00 25.15 ? 41   GLY B CA  1 
ATOM   1405  C  C   . GLY B  1 42  ? 74.403  9.181   27.969 1.00 23.42 ? 41   GLY B C   1 
ATOM   1406  O  O   . GLY B  1 42  ? 74.455  10.379  27.704 1.00 21.49 ? 41   GLY B O   1 
ATOM   1407  N  N   . LEU B  1 43  ? 73.641  8.321   27.297 1.00 23.73 ? 42   LEU B N   1 
ATOM   1408  C  CA  . LEU B  1 43  ? 72.824  8.712   26.147 1.00 23.27 ? 42   LEU B CA  1 
ATOM   1409  C  C   . LEU B  1 43  ? 71.547  9.478   26.462 1.00 22.01 ? 42   LEU B C   1 
ATOM   1410  O  O   . LEU B  1 43  ? 70.855  9.194   27.440 1.00 22.57 ? 42   LEU B O   1 
ATOM   1411  C  CB  . LEU B  1 43  ? 72.462  7.466   25.334 1.00 24.06 ? 42   LEU B CB  1 
ATOM   1412  C  CG  . LEU B  1 43  ? 73.627  6.698   24.712 1.00 26.03 ? 42   LEU B CG  1 
ATOM   1413  C  CD1 . LEU B  1 43  ? 73.137  5.345   24.207 1.00 24.09 ? 42   LEU B CD1 1 
ATOM   1414  C  CD2 . LEU B  1 43  ? 74.230  7.523   23.575 1.00 24.17 ? 42   LEU B CD2 1 
ATOM   1415  N  N   . HIS B  1 44  ? 71.226  10.436  25.598 1.00 20.09 ? 43   HIS B N   1 
ATOM   1416  C  CA  . HIS B  1 44  ? 70.024  11.247  25.741 1.00 18.96 ? 43   HIS B CA  1 
ATOM   1417  C  C   . HIS B  1 44  ? 69.408  11.542  24.378 1.00 20.18 ? 43   HIS B C   1 
ATOM   1418  O  O   . HIS B  1 44  ? 70.088  12.072  23.499 1.00 18.15 ? 43   HIS B O   1 
ATOM   1419  C  CB  . HIS B  1 44  ? 70.361  12.569  26.433 1.00 19.97 ? 43   HIS B CB  1 
ATOM   1420  C  CG  . HIS B  1 44  ? 70.736  12.408  27.873 1.00 21.02 ? 43   HIS B CG  1 
ATOM   1421  N  ND1 . HIS B  1 44  ? 69.799  12.275  28.873 1.00 21.44 ? 43   HIS B ND1 1 
ATOM   1422  C  CD2 . HIS B  1 44  ? 71.947  12.290  28.470 1.00 20.86 ? 43   HIS B CD2 1 
ATOM   1423  C  CE1 . HIS B  1 44  ? 70.415  12.080  30.026 1.00 23.67 ? 43   HIS B CE1 1 
ATOM   1424  N  NE2 . HIS B  1 44  ? 71.715  12.083  29.810 1.00 22.09 ? 43   HIS B NE2 1 
ATOM   1425  N  N   . GLY B  1 45  ? 68.129  11.203  24.213 1.00 18.68 ? 44   GLY B N   1 
ATOM   1426  C  CA  . GLY B  1 45  ? 67.429  11.467  22.963 1.00 20.11 ? 44   GLY B CA  1 
ATOM   1427  C  C   . GLY B  1 45  ? 67.620  12.919  22.555 1.00 19.67 ? 44   GLY B C   1 
ATOM   1428  O  O   . GLY B  1 45  ? 67.664  13.801  23.408 1.00 19.71 ? 44   GLY B O   1 
ATOM   1429  N  N   . PHE B  1 46  ? 67.692  13.178  21.254 1.00 19.06 ? 45   PHE B N   1 
ATOM   1430  C  CA  . PHE B  1 46  ? 67.952  14.529  20.746 1.00 19.09 ? 45   PHE B CA  1 
ATOM   1431  C  C   . PHE B  1 46  ? 67.208  14.670  19.415 1.00 19.18 ? 45   PHE B C   1 
ATOM   1432  O  O   . PHE B  1 46  ? 67.625  14.094  18.416 1.00 19.54 ? 45   PHE B O   1 
ATOM   1433  C  CB  . PHE B  1 46  ? 69.463  14.637  20.535 1.00 19.83 ? 45   PHE B CB  1 
ATOM   1434  C  CG  . PHE B  1 46  ? 69.966  16.020  20.257 1.00 19.11 ? 45   PHE B CG  1 
ATOM   1435  C  CD1 . PHE B  1 46  ? 69.867  17.018  21.217 1.00 19.41 ? 45   PHE B CD1 1 
ATOM   1436  C  CD2 . PHE B  1 46  ? 70.652  16.290  19.072 1.00 20.78 ? 45   PHE B CD2 1 
ATOM   1437  C  CE1 . PHE B  1 46  ? 70.455  18.272  21.010 1.00 17.74 ? 45   PHE B CE1 1 
ATOM   1438  C  CE2 . PHE B  1 46  ? 71.242  17.541  18.854 1.00 20.18 ? 45   PHE B CE2 1 
ATOM   1439  C  CZ  . PHE B  1 46  ? 71.143  18.530  19.832 1.00 18.51 ? 45   PHE B CZ  1 
ATOM   1440  N  N   . HIS B  1 47  ? 66.112  15.422  19.400 1.00 16.71 ? 46   HIS B N   1 
ATOM   1441  C  CA  . HIS B  1 47  ? 65.317  15.566  18.179 1.00 18.11 ? 46   HIS B CA  1 
ATOM   1442  C  C   . HIS B  1 47  ? 64.770  16.960  17.970 1.00 18.59 ? 46   HIS B C   1 
ATOM   1443  O  O   . HIS B  1 47  ? 64.725  17.770  18.896 1.00 18.41 ? 46   HIS B O   1 
ATOM   1444  C  CB  . HIS B  1 47  ? 64.088  14.640  18.214 1.00 16.78 ? 46   HIS B CB  1 
ATOM   1445  C  CG  . HIS B  1 47  ? 64.286  13.383  18.993 1.00 18.26 ? 46   HIS B CG  1 
ATOM   1446  N  ND1 . HIS B  1 47  ? 63.640  13.134  20.193 1.00 20.90 ? 46   HIS B ND1 1 
ATOM   1447  C  CD2 . HIS B  1 47  ? 65.031  12.281  18.744 1.00 17.71 ? 46   HIS B CD2 1 
ATOM   1448  C  CE1 . HIS B  1 47  ? 63.979  11.947  20.636 1.00 19.85 ? 46   HIS B CE1 1 
ATOM   1449  N  NE2 . HIS B  1 47  ? 64.826  11.400  19.775 1.00 20.76 ? 46   HIS B NE2 1 
ATOM   1450  N  N   . VAL B  1 48  ? 64.328  17.217  16.743 1.00 16.84 ? 47   VAL B N   1 
ATOM   1451  C  CA  . VAL B  1 48  ? 63.687  18.474  16.420 1.00 18.58 ? 47   VAL B CA  1 
ATOM   1452  C  C   . VAL B  1 48  ? 62.206  18.130  16.437 1.00 20.90 ? 47   VAL B C   1 
ATOM   1453  O  O   . VAL B  1 48  ? 61.777  17.193  15.752 1.00 18.95 ? 47   VAL B O   1 
ATOM   1454  C  CB  . VAL B  1 48  ? 64.045  18.983  15.009 1.00 18.20 ? 47   VAL B CB  1 
ATOM   1455  C  CG1 . VAL B  1 48  ? 63.168  20.181  14.662 1.00 19.47 ? 47   VAL B CG1 1 
ATOM   1456  C  CG2 . VAL B  1 48  ? 65.522  19.371  14.951 1.00 17.82 ? 47   VAL B CG2 1 
ATOM   1457  N  N   . HIS B  1 49  ? 61.434  18.862  17.238 1.00 20.29 ? 48   HIS B N   1 
ATOM   1458  C  CA  . HIS B  1 49  ? 60.000  18.633  17.319 1.00 21.27 ? 48   HIS B CA  1 
ATOM   1459  C  C   . HIS B  1 49  ? 59.274  19.631  16.427 1.00 21.76 ? 48   HIS B C   1 
ATOM   1460  O  O   . HIS B  1 49  ? 59.787  20.713  16.124 1.00 21.71 ? 48   HIS B O   1 
ATOM   1461  C  CB  . HIS B  1 49  ? 59.520  18.699  18.779 1.00 19.90 ? 48   HIS B CB  1 
ATOM   1462  C  CG  . HIS B  1 49  ? 59.941  17.514  19.594 1.00 19.45 ? 48   HIS B CG  1 
ATOM   1463  N  ND1 . HIS B  1 49  ? 59.054  16.770  20.351 1.00 19.88 ? 48   HIS B ND1 1 
ATOM   1464  C  CD2 . HIS B  1 49  ? 61.150  16.925  19.757 1.00 19.73 ? 48   HIS B CD2 1 
ATOM   1465  C  CE1 . HIS B  1 49  ? 59.699  15.781  20.939 1.00 17.88 ? 48   HIS B CE1 1 
ATOM   1466  N  NE2 . HIS B  1 49  ? 60.978  15.852  20.597 1.00 18.74 ? 48   HIS B NE2 1 
ATOM   1467  N  N   . GLU B  1 50  ? 58.079  19.248  16.002 1.00 22.66 ? 49   GLU B N   1 
ATOM   1468  C  CA  . GLU B  1 50  ? 57.286  20.036  15.072 1.00 21.95 ? 49   GLU B CA  1 
ATOM   1469  C  C   . GLU B  1 50  ? 56.998  21.505  15.357 1.00 21.49 ? 49   GLU B C   1 
ATOM   1470  O  O   . GLU B  1 50  ? 57.182  22.340  14.482 1.00 22.95 ? 49   GLU B O   1 
ATOM   1471  C  CB  . GLU B  1 50  ? 55.959  19.316  14.798 1.00 22.84 ? 49   GLU B CB  1 
ATOM   1472  C  CG  . GLU B  1 50  ? 55.153  19.921  13.655 1.00 22.27 ? 49   GLU B CG  1 
ATOM   1473  C  CD  . GLU B  1 50  ? 53.869  19.160  13.379 1.00 26.69 ? 49   GLU B CD  1 
ATOM   1474  O  OE1 . GLU B  1 50  ? 53.146  19.543  12.434 1.00 27.81 ? 49   GLU B OE1 1 
ATOM   1475  O  OE2 . GLU B  1 50  ? 53.583  18.185  14.108 1.00 26.05 ? 49   GLU B OE2 1 
ATOM   1476  N  N   . PHE B  1 51  ? 56.548  21.829  16.561 1.00 22.60 ? 50   PHE B N   1 
ATOM   1477  C  CA  . PHE B  1 51  ? 56.195  23.213  16.870 1.00 24.50 ? 50   PHE B CA  1 
ATOM   1478  C  C   . PHE B  1 51  ? 57.180  24.009  17.721 1.00 25.02 ? 50   PHE B C   1 
ATOM   1479  O  O   . PHE B  1 51  ? 57.762  23.482  18.667 1.00 24.00 ? 50   PHE B O   1 
ATOM   1480  C  CB  . PHE B  1 51  ? 54.817  23.231  17.533 1.00 25.08 ? 50   PHE B CB  1 
ATOM   1481  C  CG  . PHE B  1 51  ? 53.764  22.512  16.738 1.00 26.05 ? 50   PHE B CG  1 
ATOM   1482  C  CD1 . PHE B  1 51  ? 53.424  22.948  15.464 1.00 26.18 ? 50   PHE B CD1 1 
ATOM   1483  C  CD2 . PHE B  1 51  ? 53.135  21.379  17.251 1.00 27.36 ? 50   PHE B CD2 1 
ATOM   1484  C  CE1 . PHE B  1 51  ? 52.478  22.267  14.705 1.00 26.76 ? 50   PHE B CE1 1 
ATOM   1485  C  CE2 . PHE B  1 51  ? 52.186  20.689  16.500 1.00 26.13 ? 50   PHE B CE2 1 
ATOM   1486  C  CZ  . PHE B  1 51  ? 51.857  21.135  15.227 1.00 26.27 ? 50   PHE B CZ  1 
ATOM   1487  N  N   . GLY B  1 52  ? 57.354  25.283  17.367 1.00 24.59 ? 51   GLY B N   1 
ATOM   1488  C  CA  . GLY B  1 52  ? 58.240  26.165  18.111 1.00 24.51 ? 51   GLY B CA  1 
ATOM   1489  C  C   . GLY B  1 52  ? 57.394  26.893  19.140 1.00 26.08 ? 51   GLY B C   1 
ATOM   1490  O  O   . GLY B  1 52  ? 57.500  28.103  19.326 1.00 27.35 ? 51   GLY B O   1 
ATOM   1491  N  N   . ASP B  1 53  ? 56.551  26.123  19.818 1.00 26.60 ? 52   ASP B N   1 
ATOM   1492  C  CA  . ASP B  1 53  ? 55.618  26.640  20.813 1.00 24.81 ? 52   ASP B CA  1 
ATOM   1493  C  C   . ASP B  1 53  ? 56.043  26.251  22.223 1.00 25.36 ? 52   ASP B C   1 
ATOM   1494  O  O   . ASP B  1 53  ? 56.015  25.074  22.596 1.00 24.85 ? 52   ASP B O   1 
ATOM   1495  C  CB  . ASP B  1 53  ? 54.229  26.081  20.482 1.00 26.27 ? 52   ASP B CB  1 
ATOM   1496  C  CG  . ASP B  1 53  ? 53.138  26.578  21.409 1.00 27.25 ? 52   ASP B CG  1 
ATOM   1497  O  OD1 . ASP B  1 53  ? 51.963  26.474  20.998 1.00 29.55 ? 52   ASP B OD1 1 
ATOM   1498  O  OD2 . ASP B  1 53  ? 53.427  27.048  22.529 1.00 26.52 ? 52   ASP B OD2 1 
ATOM   1499  N  N   . ASN B  1 54  ? 56.441  27.247  23.003 1.00 24.89 ? 53   ASN B N   1 
ATOM   1500  C  CA  . ASN B  1 54  ? 56.873  27.006  24.373 1.00 28.07 ? 53   ASN B CA  1 
ATOM   1501  C  C   . ASN B  1 54  ? 55.837  27.507  25.392 1.00 28.46 ? 53   ASN B C   1 
ATOM   1502  O  O   . ASN B  1 54  ? 56.185  27.792  26.526 1.00 28.12 ? 53   ASN B O   1 
ATOM   1503  C  CB  . ASN B  1 54  ? 58.211  27.708  24.625 1.00 28.93 ? 53   ASN B CB  1 
ATOM   1504  C  CG  . ASN B  1 54  ? 58.893  27.228  25.894 1.00 34.28 ? 53   ASN B CG  1 
ATOM   1505  O  OD1 . ASN B  1 54  ? 59.491  28.016  26.625 1.00 36.12 ? 53   ASN B OD1 1 
ATOM   1506  N  ND2 . ASN B  1 54  ? 58.816  25.926  26.155 1.00 36.54 ? 53   ASN B ND2 1 
ATOM   1507  N  N   . THR B  1 55  ? 54.570  27.597  24.997 1.00 30.45 ? 54   THR B N   1 
ATOM   1508  C  CA  . THR B  1 55  ? 53.532  28.089  25.912 1.00 31.28 ? 54   THR B CA  1 
ATOM   1509  C  C   . THR B  1 55  ? 53.293  27.195  27.126 1.00 32.79 ? 54   THR B C   1 
ATOM   1510  O  O   . THR B  1 55  ? 52.839  27.664  28.169 1.00 32.56 ? 54   THR B O   1 
ATOM   1511  C  CB  . THR B  1 55  ? 52.186  28.311  25.183 1.00 30.85 ? 54   THR B CB  1 
ATOM   1512  O  OG1 . THR B  1 55  ? 51.767  27.097  24.548 1.00 30.19 ? 54   THR B OG1 1 
ATOM   1513  C  CG2 . THR B  1 55  ? 52.328  29.412  24.137 1.00 28.45 ? 54   THR B CG2 1 
ATOM   1514  N  N   . ALA B  1 56  ? 53.597  25.910  26.992 1.00 32.44 ? 55   ALA B N   1 
ATOM   1515  C  CA  . ALA B  1 56  ? 53.426  24.974  28.093 1.00 33.49 ? 55   ALA B CA  1 
ATOM   1516  C  C   . ALA B  1 56  ? 54.715  24.183  28.260 1.00 34.01 ? 55   ALA B C   1 
ATOM   1517  O  O   . ALA B  1 56  ? 54.699  22.954  28.296 1.00 36.69 ? 55   ALA B O   1 
ATOM   1518  C  CB  . ALA B  1 56  ? 52.263  24.030  27.804 1.00 35.07 ? 55   ALA B CB  1 
ATOM   1519  N  N   . GLY B  1 57  ? 55.833  24.893  28.359 1.00 33.34 ? 56   GLY B N   1 
ATOM   1520  C  CA  . GLY B  1 57  ? 57.110  24.221  28.495 1.00 33.28 ? 56   GLY B CA  1 
ATOM   1521  C  C   . GLY B  1 57  ? 57.414  23.443  27.226 1.00 31.91 ? 56   GLY B C   1 
ATOM   1522  O  O   . GLY B  1 57  ? 56.904  23.772  26.156 1.00 33.06 ? 56   GLY B O   1 
ATOM   1523  N  N   . CYS B  1 58  ? 58.231  22.403  27.341 1.00 30.66 ? 57   CYS B N   1 
ATOM   1524  C  CA  . CYS B  1 58  ? 58.593  21.588  26.186 1.00 29.96 ? 57   CYS B CA  1 
ATOM   1525  C  C   . CYS B  1 58  ? 57.433  20.726  25.691 1.00 29.94 ? 57   CYS B C   1 
ATOM   1526  O  O   . CYS B  1 58  ? 57.468  20.213  24.575 1.00 28.64 ? 57   CYS B O   1 
ATOM   1527  C  CB  . CYS B  1 58  ? 59.779  20.691  26.540 1.00 28.62 ? 57   CYS B CB  1 
ATOM   1528  S  SG  . CYS B  1 58  ? 61.222  21.638  27.117 1.00 28.61 ? 57   CYS B SG  1 
ATOM   1529  N  N   . THR B  1 59  ? 56.408  20.572  26.522 1.00 28.90 ? 58   THR B N   1 
ATOM   1530  C  CA  . THR B  1 59  ? 55.254  19.754  26.165 1.00 30.14 ? 58   THR B CA  1 
ATOM   1531  C  C   . THR B  1 59  ? 54.493  20.256  24.937 1.00 28.89 ? 58   THR B C   1 
ATOM   1532  O  O   . THR B  1 59  ? 54.010  19.458  24.135 1.00 28.59 ? 58   THR B O   1 
ATOM   1533  C  CB  . THR B  1 59  ? 54.265  19.649  27.346 1.00 33.70 ? 58   THR B CB  1 
ATOM   1534  O  OG1 . THR B  1 59  ? 54.960  19.182  28.509 1.00 33.62 ? 58   THR B OG1 1 
ATOM   1535  C  CG2 . THR B  1 59  ? 53.136  18.676  27.013 1.00 34.33 ? 58   THR B CG2 1 
ATOM   1536  N  N   . SER B  1 60  ? 54.396  21.571  24.780 1.00 27.23 ? 59   SER B N   1 
ATOM   1537  C  CA  . SER B  1 60  ? 53.675  22.137  23.643 1.00 27.63 ? 59   SER B CA  1 
ATOM   1538  C  C   . SER B  1 60  ? 54.446  22.106  22.316 1.00 27.72 ? 59   SER B C   1 
ATOM   1539  O  O   . SER B  1 60  ? 53.937  22.560  21.286 1.00 27.41 ? 59   SER B O   1 
ATOM   1540  C  CB  . SER B  1 60  ? 53.234  23.569  23.974 1.00 26.75 ? 59   SER B CB  1 
ATOM   1541  O  OG  . SER B  1 60  ? 54.275  24.296  24.600 1.00 28.75 ? 59   SER B OG  1 
ATOM   1542  N  N   . ALA B  1 61  ? 55.660  21.559  22.330 1.00 25.63 ? 60   ALA B N   1 
ATOM   1543  C  CA  . ALA B  1 61  ? 56.461  21.475  21.108 1.00 25.48 ? 60   ALA B CA  1 
ATOM   1544  C  C   . ALA B  1 61  ? 55.895  20.399  20.187 1.00 25.98 ? 60   ALA B C   1 
ATOM   1545  O  O   . ALA B  1 61  ? 56.274  20.297  19.018 1.00 24.98 ? 60   ALA B O   1 
ATOM   1546  C  CB  . ALA B  1 61  ? 57.915  21.161  21.445 1.00 25.58 ? 60   ALA B CB  1 
ATOM   1547  N  N   . GLY B  1 62  ? 54.991  19.585  20.721 1.00 24.66 ? 61   GLY B N   1 
ATOM   1548  C  CA  . GLY B  1 62  ? 54.394  18.538  19.914 1.00 24.14 ? 61   GLY B CA  1 
ATOM   1549  C  C   . GLY B  1 62  ? 55.294  17.341  19.658 1.00 24.87 ? 61   GLY B C   1 
ATOM   1550  O  O   . GLY B  1 62  ? 56.291  17.138  20.353 1.00 23.45 ? 61   GLY B O   1 
ATOM   1551  N  N   . PRO B  1 63  ? 54.963  16.526  18.645 1.00 24.53 ? 62   PRO B N   1 
ATOM   1552  C  CA  . PRO B  1 63  ? 55.740  15.337  18.297 1.00 24.16 ? 62   PRO B CA  1 
ATOM   1553  C  C   . PRO B  1 63  ? 56.989  15.680  17.482 1.00 23.11 ? 62   PRO B C   1 
ATOM   1554  O  O   . PRO B  1 63  ? 57.296  16.850  17.260 1.00 23.90 ? 62   PRO B O   1 
ATOM   1555  C  CB  . PRO B  1 63  ? 54.739  14.512  17.499 1.00 23.05 ? 62   PRO B CB  1 
ATOM   1556  C  CG  . PRO B  1 63  ? 54.021  15.574  16.719 1.00 22.81 ? 62   PRO B CG  1 
ATOM   1557  C  CD  . PRO B  1 63  ? 53.788  16.664  17.760 1.00 23.61 ? 62   PRO B CD  1 
ATOM   1558  N  N   . HIS B  1 64  ? 57.706  14.652  17.046 1.00 23.40 ? 63   HIS B N   1 
ATOM   1559  C  CA  . HIS B  1 64  ? 58.905  14.855  16.242 1.00 23.64 ? 63   HIS B CA  1 
ATOM   1560  C  C   . HIS B  1 64  ? 58.498  15.430  14.898 1.00 23.24 ? 63   HIS B C   1 
ATOM   1561  O  O   . HIS B  1 64  ? 57.447  15.074  14.368 1.00 23.25 ? 63   HIS B O   1 
ATOM   1562  C  CB  . HIS B  1 64  ? 59.625  13.529  16.009 1.00 22.15 ? 63   HIS B CB  1 
ATOM   1563  C  CG  . HIS B  1 64  ? 60.166  12.907  17.251 1.00 21.30 ? 63   HIS B CG  1 
ATOM   1564  N  ND1 . HIS B  1 64  ? 60.853  11.713  17.246 1.00 19.60 ? 63   HIS B ND1 1 
ATOM   1565  C  CD2 . HIS B  1 64  ? 60.123  13.313  18.547 1.00 20.96 ? 63   HIS B CD2 1 
ATOM   1566  C  CE1 . HIS B  1 64  ? 61.209  11.407  18.482 1.00 19.52 ? 63   HIS B CE1 1 
ATOM   1567  N  NE2 . HIS B  1 64  ? 60.778  12.362  19.288 1.00 22.06 ? 63   HIS B NE2 1 
ATOM   1568  N  N   . PHE B  1 65  ? 59.329  16.318  14.359 1.00 21.83 ? 64   PHE B N   1 
ATOM   1569  C  CA  . PHE B  1 65  ? 59.078  16.944  13.062 1.00 20.93 ? 64   PHE B CA  1 
ATOM   1570  C  C   . PHE B  1 65  ? 59.072  15.803  12.051 1.00 23.15 ? 64   PHE B C   1 
ATOM   1571  O  O   . PHE B  1 65  ? 60.096  15.158  11.838 1.00 20.75 ? 64   PHE B O   1 
ATOM   1572  C  CB  . PHE B  1 65  ? 60.198  17.932  12.744 1.00 20.06 ? 64   PHE B CB  1 
ATOM   1573  C  CG  . PHE B  1 65  ? 60.011  18.671  11.449 1.00 21.20 ? 64   PHE B CG  1 
ATOM   1574  C  CD1 . PHE B  1 65  ? 61.112  19.006  10.667 1.00 21.48 ? 64   PHE B CD1 1 
ATOM   1575  C  CD2 . PHE B  1 65  ? 58.740  19.058  11.023 1.00 21.92 ? 64   PHE B CD2 1 
ATOM   1576  C  CE1 . PHE B  1 65  ? 60.956  19.720  9.478  1.00 22.57 ? 64   PHE B CE1 1 
ATOM   1577  C  CE2 . PHE B  1 65  ? 58.570  19.771  9.840  1.00 22.92 ? 64   PHE B CE2 1 
ATOM   1578  C  CZ  . PHE B  1 65  ? 59.682  20.102  9.064  1.00 23.87 ? 64   PHE B CZ  1 
ATOM   1579  N  N   . ASN B  1 66  ? 57.924  15.564  11.424 1.00 24.67 ? 65   ASN B N   1 
ATOM   1580  C  CA  . ASN B  1 66  ? 57.782  14.434  10.508 1.00 26.17 ? 65   ASN B CA  1 
ATOM   1581  C  C   . ASN B  1 66  ? 56.957  14.788  9.268  1.00 28.93 ? 65   ASN B C   1 
ATOM   1582  O  O   . ASN B  1 66  ? 55.883  14.228  9.044  1.00 29.43 ? 65   ASN B O   1 
ATOM   1583  C  CB  . ASN B  1 66  ? 57.126  13.301  11.308 1.00 24.82 ? 65   ASN B CB  1 
ATOM   1584  C  CG  . ASN B  1 66  ? 56.934  12.030  10.514 1.00 24.21 ? 65   ASN B CG  1 
ATOM   1585  O  OD1 . ASN B  1 66  ? 57.708  11.708  9.612  1.00 23.51 ? 65   ASN B OD1 1 
ATOM   1586  N  ND2 . ASN B  1 66  ? 55.907  11.272  10.879 1.00 25.16 ? 65   ASN B ND2 1 
ATOM   1587  N  N   . PRO B  1 67  ? 57.462  15.714  8.437  1.00 28.77 ? 66   PRO B N   1 
ATOM   1588  C  CA  . PRO B  1 67  ? 56.741  16.125  7.226  1.00 30.14 ? 66   PRO B CA  1 
ATOM   1589  C  C   . PRO B  1 67  ? 56.491  15.028  6.192  1.00 32.87 ? 66   PRO B C   1 
ATOM   1590  O  O   . PRO B  1 67  ? 55.575  15.147  5.379  1.00 33.17 ? 66   PRO B O   1 
ATOM   1591  C  CB  . PRO B  1 67  ? 57.604  17.262  6.678  1.00 29.91 ? 66   PRO B CB  1 
ATOM   1592  C  CG  . PRO B  1 67  ? 58.991  16.867  7.107  1.00 28.38 ? 66   PRO B CG  1 
ATOM   1593  C  CD  . PRO B  1 67  ? 58.775  16.382  8.525  1.00 27.20 ? 66   PRO B CD  1 
ATOM   1594  N  N   . LEU B  1 68  ? 57.293  13.966  6.215  1.00 31.93 ? 67   LEU B N   1 
ATOM   1595  C  CA  . LEU B  1 68  ? 57.115  12.877  5.258  1.00 33.82 ? 67   LEU B CA  1 
ATOM   1596  C  C   . LEU B  1 68  ? 56.298  11.729  5.849  1.00 32.88 ? 67   LEU B C   1 
ATOM   1597  O  O   . LEU B  1 68  ? 56.195  10.658  5.252  1.00 32.96 ? 67   LEU B O   1 
ATOM   1598  C  CB  . LEU B  1 68  ? 58.477  12.360  4.776  1.00 34.78 ? 67   LEU B CB  1 
ATOM   1599  C  CG  . LEU B  1 68  ? 59.392  13.403  4.119  1.00 37.50 ? 67   LEU B CG  1 
ATOM   1600  C  CD1 . LEU B  1 68  ? 60.644  12.725  3.588  1.00 37.18 ? 67   LEU B CD1 1 
ATOM   1601  C  CD2 . LEU B  1 68  ? 58.653  14.106  2.990  1.00 37.27 ? 67   LEU B CD2 1 
ATOM   1602  N  N   . SER B  1 69  ? 55.726  11.967  7.026  1.00 32.55 ? 68   SER B N   1 
ATOM   1603  C  CA  . SER B  1 69  ? 54.896  10.985  7.722  1.00 31.77 ? 68   SER B CA  1 
ATOM   1604  C  C   . SER B  1 69  ? 55.481  9.577   7.779  1.00 31.03 ? 68   SER B C   1 
ATOM   1605  O  O   . SER B  1 69  ? 54.825  8.609   7.394  1.00 30.07 ? 68   SER B O   1 
ATOM   1606  C  CB  . SER B  1 69  ? 53.504  10.927  7.078  1.00 33.30 ? 68   SER B CB  1 
ATOM   1607  O  OG  . SER B  1 69  ? 52.809  12.151  7.243  1.00 33.91 ? 68   SER B OG  1 
ATOM   1608  N  N   . ARG B  1 70  ? 56.712  9.460   8.263  1.00 28.79 ? 69   ARG B N   1 
ATOM   1609  C  CA  . ARG B  1 70  ? 57.356  8.159   8.376  1.00 27.75 ? 69   ARG B CA  1 
ATOM   1610  C  C   . ARG B  1 70  ? 57.435  7.735   9.841  1.00 27.39 ? 69   ARG B C   1 
ATOM   1611  O  O   . ARG B  1 70  ? 56.990  8.466   10.731 1.00 25.94 ? 69   ARG B O   1 
ATOM   1612  C  CB  . ARG B  1 70  ? 58.758  8.209   7.761  1.00 30.74 ? 69   ARG B CB  1 
ATOM   1613  C  CG  . ARG B  1 70  ? 58.749  8.441   6.248  1.00 38.23 ? 69   ARG B CG  1 
ATOM   1614  C  CD  . ARG B  1 70  ? 60.136  8.268   5.647  1.00 42.97 ? 69   ARG B CD  1 
ATOM   1615  N  NE  . ARG B  1 70  ? 60.166  8.628   4.231  1.00 46.11 ? 69   ARG B NE  1 
ATOM   1616  C  CZ  . ARG B  1 70  ? 61.264  8.633   3.481  1.00 47.78 ? 69   ARG B CZ  1 
ATOM   1617  N  NH1 . ARG B  1 70  ? 61.195  8.979   2.200  1.00 48.79 ? 69   ARG B NH1 1 
ATOM   1618  N  NH2 . ARG B  1 70  ? 62.433  8.291   4.006  1.00 48.25 ? 69   ARG B NH2 1 
ATOM   1619  N  N   . LYS B  1 71  ? 57.982  6.547   10.083 1.00 26.26 ? 70   LYS B N   1 
ATOM   1620  C  CA  . LYS B  1 71  ? 58.135  6.028   11.438 1.00 25.93 ? 70   LYS B CA  1 
ATOM   1621  C  C   . LYS B  1 71  ? 59.448  6.532   12.033 1.00 24.63 ? 70   LYS B C   1 
ATOM   1622  O  O   . LYS B  1 71  ? 60.374  6.898   11.298 1.00 22.77 ? 70   LYS B O   1 
ATOM   1623  C  CB  . LYS B  1 71  ? 58.147  4.496   11.428 1.00 28.91 ? 70   LYS B CB  1 
ATOM   1624  C  CG  . LYS B  1 71  ? 56.842  3.852   10.960 1.00 35.36 ? 70   LYS B CG  1 
ATOM   1625  C  CD  . LYS B  1 71  ? 55.718  4.078   11.958 1.00 39.54 ? 70   LYS B CD  1 
ATOM   1626  C  CE  . LYS B  1 71  ? 54.412  3.440   11.484 1.00 43.14 ? 70   LYS B CE  1 
ATOM   1627  N  NZ  . LYS B  1 71  ? 54.554  1.970   11.279 1.00 43.98 ? 70   LYS B NZ  1 
ATOM   1628  N  N   . HIS B  1 72  ? 59.527  6.535   13.360 1.00 21.88 ? 71   HIS B N   1 
ATOM   1629  C  CA  . HIS B  1 72  ? 60.729  6.994   14.054 1.00 22.40 ? 71   HIS B CA  1 
ATOM   1630  C  C   . HIS B  1 72  ? 61.906  6.075   13.764 1.00 22.19 ? 71   HIS B C   1 
ATOM   1631  O  O   . HIS B  1 72  ? 61.744  4.859   13.654 1.00 23.67 ? 71   HIS B O   1 
ATOM   1632  C  CB  . HIS B  1 72  ? 60.491  7.027   15.565 1.00 21.65 ? 71   HIS B CB  1 
ATOM   1633  C  CG  . HIS B  1 72  ? 61.682  7.491   16.350 1.00 21.65 ? 71   HIS B CG  1 
ATOM   1634  N  ND1 . HIS B  1 72  ? 62.026  8.814   16.465 1.00 17.72 ? 71   HIS B ND1 1 
ATOM   1635  C  CD2 . HIS B  1 72  ? 62.616  6.787   17.038 1.00 19.60 ? 71   HIS B CD2 1 
ATOM   1636  C  CE1 . HIS B  1 72  ? 63.128  8.917   17.197 1.00 20.81 ? 71   HIS B CE1 1 
ATOM   1637  N  NE2 . HIS B  1 72  ? 63.502  7.704   17.553 1.00 18.06 ? 71   HIS B NE2 1 
ATOM   1638  N  N   . GLY B  1 73  ? 63.091  6.659   13.640 1.00 19.75 ? 72   GLY B N   1 
ATOM   1639  C  CA  . GLY B  1 73  ? 64.277  5.869   13.380 1.00 17.14 ? 72   GLY B CA  1 
ATOM   1640  C  C   . GLY B  1 73  ? 65.508  6.586   13.891 1.00 21.45 ? 72   GLY B C   1 
ATOM   1641  O  O   . GLY B  1 73  ? 65.397  7.606   14.575 1.00 19.00 ? 72   GLY B O   1 
ATOM   1642  N  N   . GLY B  1 74  ? 66.682  6.038   13.588 1.00 20.16 ? 73   GLY B N   1 
ATOM   1643  C  CA  . GLY B  1 74  ? 67.919  6.679   13.989 1.00 21.26 ? 73   GLY B CA  1 
ATOM   1644  C  C   . GLY B  1 74  ? 68.307  7.580   12.824 1.00 21.68 ? 73   GLY B C   1 
ATOM   1645  O  O   . GLY B  1 74  ? 67.799  7.384   11.720 1.00 22.91 ? 73   GLY B O   1 
ATOM   1646  N  N   . PRO B  1 75  ? 69.195  8.565   13.019 1.00 21.28 ? 74   PRO B N   1 
ATOM   1647  C  CA  . PRO B  1 75  ? 69.589  9.456   11.918 1.00 21.10 ? 74   PRO B CA  1 
ATOM   1648  C  C   . PRO B  1 75  ? 70.176  8.779   10.673 1.00 23.64 ? 74   PRO B C   1 
ATOM   1649  O  O   . PRO B  1 75  ? 70.086  9.321   9.571  1.00 23.86 ? 74   PRO B O   1 
ATOM   1650  C  CB  . PRO B  1 75  ? 70.575  10.419  12.583 1.00 20.83 ? 74   PRO B CB  1 
ATOM   1651  C  CG  . PRO B  1 75  ? 71.138  9.612   13.734 1.00 21.99 ? 74   PRO B CG  1 
ATOM   1652  C  CD  . PRO B  1 75  ? 69.919  8.898   14.260 1.00 19.93 ? 74   PRO B CD  1 
ATOM   1653  N  N   . LYS B  1 76  ? 70.766  7.600   10.842 1.00 23.03 ? 75   LYS B N   1 
ATOM   1654  C  CA  . LYS B  1 76  ? 71.360  6.886   9.712  1.00 25.79 ? 75   LYS B CA  1 
ATOM   1655  C  C   . LYS B  1 76  ? 70.331  6.106   8.895  1.00 25.64 ? 75   LYS B C   1 
ATOM   1656  O  O   . LYS B  1 76  ? 70.623  5.670   7.787  1.00 25.44 ? 75   LYS B O   1 
ATOM   1657  C  CB  . LYS B  1 76  ? 72.448  5.927   10.211 1.00 26.30 ? 75   LYS B CB  1 
ATOM   1658  C  CG  . LYS B  1 76  ? 73.566  6.609   10.984 1.00 28.55 ? 75   LYS B CG  1 
ATOM   1659  C  CD  . LYS B  1 76  ? 74.413  5.609   11.771 1.00 32.47 ? 75   LYS B CD  1 
ATOM   1660  C  CE  . LYS B  1 76  ? 75.218  4.686   10.861 1.00 33.70 ? 75   LYS B CE  1 
ATOM   1661  N  NZ  . LYS B  1 76  ? 76.095  3.753   11.636 1.00 33.30 ? 75   LYS B NZ  1 
ATOM   1662  N  N   . ASP B  1 77  ? 69.129  5.938   9.440  1.00 24.62 ? 76   ASP B N   1 
ATOM   1663  C  CA  . ASP B  1 77  ? 68.067  5.194   8.761  1.00 25.48 ? 76   ASP B CA  1 
ATOM   1664  C  C   . ASP B  1 77  ? 67.356  5.972   7.664  1.00 26.99 ? 76   ASP B C   1 
ATOM   1665  O  O   . ASP B  1 77  ? 67.167  7.184   7.769  1.00 23.78 ? 76   ASP B O   1 
ATOM   1666  C  CB  . ASP B  1 77  ? 67.004  4.753   9.768  1.00 25.08 ? 76   ASP B CB  1 
ATOM   1667  C  CG  . ASP B  1 77  ? 67.523  3.752   10.766 1.00 25.95 ? 76   ASP B CG  1 
ATOM   1668  O  OD1 . ASP B  1 77  ? 66.973  3.711   11.885 1.00 26.21 ? 76   ASP B OD1 1 
ATOM   1669  O  OD2 . ASP B  1 77  ? 68.465  3.004   10.430 1.00 25.40 ? 76   ASP B OD2 1 
ATOM   1670  N  N   . GLU B  1 78  ? 66.942  5.263   6.618  1.00 26.68 ? 77   GLU B N   1 
ATOM   1671  C  CA  . GLU B  1 78  ? 66.202  5.898   5.537  1.00 27.68 ? 77   GLU B CA  1 
ATOM   1672  C  C   . GLU B  1 78  ? 64.800  6.149   6.091  1.00 25.97 ? 77   GLU B C   1 
ATOM   1673  O  O   . GLU B  1 78  ? 64.190  7.182   5.825  1.00 26.26 ? 77   GLU B O   1 
ATOM   1674  C  CB  . GLU B  1 78  ? 66.115  4.981   4.313  1.00 31.91 ? 77   GLU B CB  1 
ATOM   1675  C  CG  . GLU B  1 78  ? 65.404  5.637   3.137  1.00 40.15 ? 77   GLU B CG  1 
ATOM   1676  C  CD  . GLU B  1 78  ? 65.146  4.684   1.979  1.00 45.00 ? 77   GLU B CD  1 
ATOM   1677  O  OE1 . GLU B  1 78  ? 64.622  5.147   0.943  1.00 47.99 ? 77   GLU B OE1 1 
ATOM   1678  O  OE2 . GLU B  1 78  ? 65.458  3.477   2.099  1.00 47.75 ? 77   GLU B OE2 1 
ATOM   1679  N  N   . GLU B  1 79  ? 64.296  5.195   6.868  1.00 23.48 ? 78   GLU B N   1 
ATOM   1680  C  CA  . GLU B  1 79  ? 62.980  5.339   7.479  1.00 24.50 ? 78   GLU B CA  1 
ATOM   1681  C  C   . GLU B  1 79  ? 63.153  6.060   8.814  1.00 22.33 ? 78   GLU B C   1 
ATOM   1682  O  O   . GLU B  1 79  ? 63.592  5.472   9.800  1.00 20.44 ? 78   GLU B O   1 
ATOM   1683  C  CB  . GLU B  1 79  ? 62.334  3.970   7.703  1.00 25.12 ? 78   GLU B CB  1 
ATOM   1684  C  CG  . GLU B  1 79  ? 60.931  4.028   8.310  1.00 30.20 ? 78   GLU B CG  1 
ATOM   1685  C  CD  . GLU B  1 79  ? 59.888  4.619   7.368  1.00 31.74 ? 78   GLU B CD  1 
ATOM   1686  O  OE1 . GLU B  1 79  ? 58.749  4.871   7.821  1.00 33.32 ? 78   GLU B OE1 1 
ATOM   1687  O  OE2 . GLU B  1 79  ? 60.196  4.824   6.175  1.00 35.12 ? 78   GLU B OE2 1 
ATOM   1688  N  N   . ARG B  1 80  ? 62.816  7.344   8.834  1.00 21.87 ? 79   ARG B N   1 
ATOM   1689  C  CA  . ARG B  1 80  ? 62.938  8.143   10.045 1.00 22.81 ? 79   ARG B CA  1 
ATOM   1690  C  C   . ARG B  1 80  ? 62.163  9.438   9.893  1.00 23.06 ? 79   ARG B C   1 
ATOM   1691  O  O   . ARG B  1 80  ? 61.706  9.780   8.800  1.00 21.11 ? 79   ARG B O   1 
ATOM   1692  C  CB  . ARG B  1 80  ? 64.414  8.471   10.316 1.00 22.98 ? 79   ARG B CB  1 
ATOM   1693  C  CG  . ARG B  1 80  ? 65.086  9.255   9.190  1.00 24.02 ? 79   ARG B CG  1 
ATOM   1694  C  CD  . ARG B  1 80  ? 65.544  10.630  9.648  1.00 29.01 ? 79   ARG B CD  1 
ATOM   1695  N  NE  . ARG B  1 80  ? 66.985  10.760  9.560  1.00 27.80 ? 79   ARG B NE  1 
ATOM   1696  C  CZ  . ARG B  1 80  ? 67.674  11.864  9.837  1.00 25.30 ? 79   ARG B CZ  1 
ATOM   1697  N  NH1 . ARG B  1 80  ? 68.985  11.844  9.711  1.00 21.18 ? 79   ARG B NH1 1 
ATOM   1698  N  NH2 . ARG B  1 80  ? 67.074  12.979  10.234 1.00 22.88 ? 79   ARG B NH2 1 
ATOM   1699  N  N   . HIS B  1 81  ? 62.012  10.147  11.006 1.00 21.46 ? 80   HIS B N   1 
ATOM   1700  C  CA  . HIS B  1 81  ? 61.346  11.438  11.018 1.00 21.23 ? 80   HIS B CA  1 
ATOM   1701  C  C   . HIS B  1 81  ? 62.448  12.413  10.612 1.00 21.80 ? 80   HIS B C   1 
ATOM   1702  O  O   . HIS B  1 81  ? 63.626  12.146  10.855 1.00 20.75 ? 80   HIS B O   1 
ATOM   1703  C  CB  . HIS B  1 81  ? 60.877  11.768  12.433 1.00 20.40 ? 80   HIS B CB  1 
ATOM   1704  C  CG  . HIS B  1 81  ? 59.839  10.832  12.961 1.00 21.39 ? 80   HIS B CG  1 
ATOM   1705  N  ND1 . HIS B  1 81  ? 59.694  10.572  14.311 1.00 22.81 ? 80   HIS B ND1 1 
ATOM   1706  C  CD2 . HIS B  1 81  ? 58.839  10.161  12.343 1.00 21.52 ? 80   HIS B CD2 1 
ATOM   1707  C  CE1 . HIS B  1 81  ? 58.648  9.788   14.496 1.00 23.20 ? 80   HIS B CE1 1 
ATOM   1708  N  NE2 . HIS B  1 81  ? 58.109  9.524   13.316 1.00 21.21 ? 80   HIS B NE2 1 
ATOM   1709  N  N   . VAL B  1 82  ? 62.093  13.531  9.993  1.00 20.56 ? 81   VAL B N   1 
ATOM   1710  C  CA  . VAL B  1 82  ? 63.127  14.492  9.613  1.00 20.23 ? 81   VAL B CA  1 
ATOM   1711  C  C   . VAL B  1 82  ? 63.876  14.958  10.868 1.00 20.34 ? 81   VAL B C   1 
ATOM   1712  O  O   . VAL B  1 82  ? 65.093  15.115  10.852 1.00 21.76 ? 81   VAL B O   1 
ATOM   1713  C  CB  . VAL B  1 82  ? 62.522  15.719  8.884  1.00 18.95 ? 81   VAL B CB  1 
ATOM   1714  C  CG1 . VAL B  1 82  ? 63.545  16.868  8.836  1.00 19.80 ? 81   VAL B CG1 1 
ATOM   1715  C  CG2 . VAL B  1 82  ? 62.127  15.327  7.461  1.00 18.33 ? 81   VAL B CG2 1 
ATOM   1716  N  N   . GLY B  1 83  ? 63.145  15.138  11.965 1.00 21.05 ? 82   GLY B N   1 
ATOM   1717  C  CA  . GLY B  1 83  ? 63.763  15.605  13.201 1.00 19.38 ? 82   GLY B CA  1 
ATOM   1718  C  C   . GLY B  1 83  ? 64.549  14.608  14.040 1.00 20.15 ? 82   GLY B C   1 
ATOM   1719  O  O   . GLY B  1 83  ? 65.039  14.967  15.116 1.00 18.30 ? 82   GLY B O   1 
ATOM   1720  N  N   . ASP B  1 84  ? 64.696  13.374  13.563 1.00 19.28 ? 83   ASP B N   1 
ATOM   1721  C  CA  . ASP B  1 84  ? 65.421  12.353  14.320 1.00 19.65 ? 83   ASP B CA  1 
ATOM   1722  C  C   . ASP B  1 84  ? 66.936  12.507  14.260 1.00 21.96 ? 83   ASP B C   1 
ATOM   1723  O  O   . ASP B  1 84  ? 67.574  12.040  13.318 1.00 21.58 ? 83   ASP B O   1 
ATOM   1724  C  CB  . ASP B  1 84  ? 65.048  10.948  13.828 1.00 20.90 ? 83   ASP B CB  1 
ATOM   1725  C  CG  . ASP B  1 84  ? 63.615  10.572  14.149 1.00 23.87 ? 83   ASP B CG  1 
ATOM   1726  O  OD1 . ASP B  1 84  ? 63.010  11.228  15.029 1.00 21.52 ? 83   ASP B OD1 1 
ATOM   1727  O  OD2 . ASP B  1 84  ? 63.097  9.609   13.534 1.00 22.56 ? 83   ASP B OD2 1 
ATOM   1728  N  N   . LEU B  1 85  ? 67.515  13.146  15.273 1.00 19.45 ? 84   LEU B N   1 
ATOM   1729  C  CA  . LEU B  1 85  ? 68.954  13.332  15.306 1.00 19.71 ? 84   LEU B CA  1 
ATOM   1730  C  C   . LEU B  1 85  ? 69.664  12.315  16.206 1.00 18.37 ? 84   LEU B C   1 
ATOM   1731  O  O   . LEU B  1 85  ? 70.848  12.450  16.495 1.00 20.44 ? 84   LEU B O   1 
ATOM   1732  C  CB  . LEU B  1 85  ? 69.278  14.771  15.736 1.00 17.02 ? 84   LEU B CB  1 
ATOM   1733  C  CG  . LEU B  1 85  ? 68.782  15.816  14.723 1.00 20.13 ? 84   LEU B CG  1 
ATOM   1734  C  CD1 . LEU B  1 85  ? 68.990  17.227  15.258 1.00 16.22 ? 84   LEU B CD1 1 
ATOM   1735  C  CD2 . LEU B  1 85  ? 69.517  15.624  13.402 1.00 20.13 ? 84   LEU B CD2 1 
ATOM   1736  N  N   . GLY B  1 86  ? 68.933  11.300  16.658 1.00 18.92 ? 85   GLY B N   1 
ATOM   1737  C  CA  . GLY B  1 86  ? 69.541  10.266  17.483 1.00 16.86 ? 85   GLY B CA  1 
ATOM   1738  C  C   . GLY B  1 86  ? 69.757  10.622  18.939 1.00 18.02 ? 85   GLY B C   1 
ATOM   1739  O  O   . GLY B  1 86  ? 68.845  11.114  19.610 1.00 17.03 ? 85   GLY B O   1 
ATOM   1740  N  N   . ASN B  1 87  ? 70.974  10.369  19.418 1.00 16.50 ? 86   ASN B N   1 
ATOM   1741  C  CA  . ASN B  1 87  ? 71.362  10.647  20.800 1.00 18.33 ? 86   ASN B CA  1 
ATOM   1742  C  C   . ASN B  1 87  ? 72.585  11.556  20.877 1.00 19.60 ? 86   ASN B C   1 
ATOM   1743  O  O   . ASN B  1 87  ? 73.328  11.707  19.900 1.00 17.22 ? 86   ASN B O   1 
ATOM   1744  C  CB  . ASN B  1 87  ? 71.763  9.351   21.514 1.00 17.02 ? 86   ASN B CB  1 
ATOM   1745  C  CG  . ASN B  1 87  ? 70.592  8.444   21.801 1.00 20.66 ? 86   ASN B CG  1 
ATOM   1746  O  OD1 . ASN B  1 87  ? 69.702  8.795   22.570 1.00 17.76 ? 86   ASN B OD1 1 
ATOM   1747  N  ND2 . ASN B  1 87  ? 70.593  7.263   21.189 1.00 18.51 ? 86   ASN B ND2 1 
ATOM   1748  N  N   . VAL B  1 88  ? 72.780  12.148  22.053 1.00 16.98 ? 87   VAL B N   1 
ATOM   1749  C  CA  . VAL B  1 88  ? 73.973  12.943  22.347 1.00 19.14 ? 87   VAL B CA  1 
ATOM   1750  C  C   . VAL B  1 88  ? 74.458  12.286  23.640 1.00 21.09 ? 87   VAL B C   1 
ATOM   1751  O  O   . VAL B  1 88  ? 73.647  11.745  24.406 1.00 19.72 ? 87   VAL B O   1 
ATOM   1752  C  CB  . VAL B  1 88  ? 73.682  14.448  22.580 1.00 18.24 ? 87   VAL B CB  1 
ATOM   1753  C  CG1 . VAL B  1 88  ? 73.269  15.102  21.265 1.00 15.25 ? 87   VAL B CG1 1 
ATOM   1754  C  CG2 . VAL B  1 88  ? 72.617  14.629  23.642 1.00 18.96 ? 87   VAL B CG2 1 
ATOM   1755  N  N   . THR B  1 89  ? 75.764  12.310  23.876 1.00 18.88 ? 88   THR B N   1 
ATOM   1756  C  CA  . THR B  1 89  ? 76.338  11.668  25.052 1.00 19.94 ? 88   THR B CA  1 
ATOM   1757  C  C   . THR B  1 89  ? 76.917  12.646  26.071 1.00 21.44 ? 88   THR B C   1 
ATOM   1758  O  O   . THR B  1 89  ? 77.766  13.478  25.739 1.00 20.04 ? 88   THR B O   1 
ATOM   1759  C  CB  . THR B  1 89  ? 77.455  10.670  24.625 1.00 19.51 ? 88   THR B CB  1 
ATOM   1760  O  OG1 . THR B  1 89  ? 76.895  9.654   23.776 1.00 21.18 ? 88   THR B OG1 1 
ATOM   1761  C  CG2 . THR B  1 89  ? 78.098  10.014  25.838 1.00 18.64 ? 88   THR B CG2 1 
ATOM   1762  N  N   . ALA B  1 90  ? 76.443  12.545  27.311 1.00 20.55 ? 89   ALA B N   1 
ATOM   1763  C  CA  . ALA B  1 90  ? 76.934  13.394  28.394 1.00 21.88 ? 89   ALA B CA  1 
ATOM   1764  C  C   . ALA B  1 90  ? 78.070  12.647  29.097 1.00 21.40 ? 89   ALA B C   1 
ATOM   1765  O  O   . ALA B  1 90  ? 77.977  11.439  29.322 1.00 22.02 ? 89   ALA B O   1 
ATOM   1766  C  CB  . ALA B  1 90  ? 75.813  13.691  29.390 1.00 21.58 ? 89   ALA B CB  1 
ATOM   1767  N  N   . ASP B  1 91  ? 79.139  13.361  29.438 1.00 21.98 ? 90   ASP B N   1 
ATOM   1768  C  CA  . ASP B  1 91  ? 80.271  12.740  30.109 1.00 22.89 ? 90   ASP B CA  1 
ATOM   1769  C  C   . ASP B  1 91  ? 80.027  12.607  31.613 1.00 25.41 ? 90   ASP B C   1 
ATOM   1770  O  O   . ASP B  1 91  ? 78.938  12.909  32.101 1.00 22.16 ? 90   ASP B O   1 
ATOM   1771  C  CB  . ASP B  1 91  ? 81.566  13.528  29.823 1.00 23.73 ? 90   ASP B CB  1 
ATOM   1772  C  CG  . ASP B  1 91  ? 81.538  14.952  30.363 1.00 23.71 ? 90   ASP B CG  1 
ATOM   1773  O  OD1 . ASP B  1 91  ? 82.302  15.786  29.832 1.00 27.68 ? 90   ASP B OD1 1 
ATOM   1774  O  OD2 . ASP B  1 91  ? 80.779  15.250  31.311 1.00 23.85 ? 90   ASP B OD2 1 
ATOM   1775  N  N   . LYS B  1 92  ? 81.041  12.133  32.333 1.00 27.12 ? 91   LYS B N   1 
ATOM   1776  C  CA  . LYS B  1 92  ? 80.959  11.935  33.775 1.00 30.78 ? 91   LYS B CA  1 
ATOM   1777  C  C   . LYS B  1 92  ? 80.598  13.212  34.527 1.00 29.90 ? 91   LYS B C   1 
ATOM   1778  O  O   . LYS B  1 92  ? 80.067  13.155  35.635 1.00 30.25 ? 91   LYS B O   1 
ATOM   1779  C  CB  . LYS B  1 92  ? 82.296  11.391  34.294 1.00 34.24 ? 91   LYS B CB  1 
ATOM   1780  C  CG  . LYS B  1 92  ? 83.502  12.226  33.868 1.00 39.12 ? 91   LYS B CG  1 
ATOM   1781  C  CD  . LYS B  1 92  ? 84.829  11.506  34.115 1.00 42.52 ? 91   LYS B CD  1 
ATOM   1782  C  CE  . LYS B  1 92  ? 85.101  11.310  35.600 1.00 44.13 ? 91   LYS B CE  1 
ATOM   1783  N  NZ  . LYS B  1 92  ? 86.410  10.644  35.845 0.00 43.87 ? 91   LYS B NZ  1 
ATOM   1784  N  N   . ASP B  1 93  ? 80.884  14.359  33.924 1.00 29.18 ? 92   ASP B N   1 
ATOM   1785  C  CA  . ASP B  1 93  ? 80.591  15.641  34.554 1.00 29.79 ? 92   ASP B CA  1 
ATOM   1786  C  C   . ASP B  1 93  ? 79.231  16.195  34.145 1.00 28.65 ? 92   ASP B C   1 
ATOM   1787  O  O   . ASP B  1 93  ? 78.885  17.324  34.498 1.00 27.34 ? 92   ASP B O   1 
ATOM   1788  C  CB  . ASP B  1 93  ? 81.696  16.644  34.212 1.00 32.59 ? 92   ASP B CB  1 
ATOM   1789  C  CG  . ASP B  1 93  ? 83.026  16.277  34.851 1.00 35.98 ? 92   ASP B CG  1 
ATOM   1790  O  OD1 . ASP B  1 93  ? 84.079  16.574  34.250 1.00 36.94 ? 92   ASP B OD1 1 
ATOM   1791  O  OD2 . ASP B  1 93  ? 83.014  15.695  35.960 1.00 34.23 ? 92   ASP B OD2 1 
ATOM   1792  N  N   . GLY B  1 94  ? 78.468  15.398  33.399 1.00 26.36 ? 93   GLY B N   1 
ATOM   1793  C  CA  . GLY B  1 94  ? 77.142  15.816  32.968 1.00 25.53 ? 93   GLY B CA  1 
ATOM   1794  C  C   . GLY B  1 94  ? 77.131  16.734  31.757 1.00 24.04 ? 93   GLY B C   1 
ATOM   1795  O  O   . GLY B  1 94  ? 76.125  17.388  31.468 1.00 23.72 ? 93   GLY B O   1 
ATOM   1796  N  N   . VAL B  1 95  ? 78.247  16.774  31.039 1.00 24.38 ? 94   VAL B N   1 
ATOM   1797  C  CA  . VAL B  1 95  ? 78.364  17.627  29.869 1.00 23.43 ? 94   VAL B CA  1 
ATOM   1798  C  C   . VAL B  1 95  ? 78.353  16.869  28.544 1.00 23.01 ? 94   VAL B C   1 
ATOM   1799  O  O   . VAL B  1 95  ? 79.088  15.896  28.354 1.00 24.32 ? 94   VAL B O   1 
ATOM   1800  C  CB  . VAL B  1 95  ? 79.657  18.472  29.937 1.00 23.87 ? 94   VAL B CB  1 
ATOM   1801  C  CG1 . VAL B  1 95  ? 79.861  19.229  28.634 1.00 23.08 ? 94   VAL B CG1 1 
ATOM   1802  C  CG2 . VAL B  1 95  ? 79.580  19.444  31.110 1.00 25.03 ? 94   VAL B CG2 1 
ATOM   1803  N  N   . ALA B  1 96  ? 77.510  17.333  27.629 1.00 22.81 ? 95   ALA B N   1 
ATOM   1804  C  CA  . ALA B  1 96  ? 77.417  16.742  26.305 1.00 21.92 ? 95   ALA B CA  1 
ATOM   1805  C  C   . ALA B  1 96  ? 77.999  17.738  25.309 1.00 22.35 ? 95   ALA B C   1 
ATOM   1806  O  O   . ALA B  1 96  ? 77.404  18.787  25.055 1.00 23.24 ? 95   ALA B O   1 
ATOM   1807  C  CB  . ALA B  1 96  ? 75.953  16.441  25.954 1.00 22.58 ? 95   ALA B CB  1 
ATOM   1808  N  N   . ASP B  1 97  ? 79.177  17.426  24.777 1.00 21.32 ? 96   ASP B N   1 
ATOM   1809  C  CA  . ASP B  1 97  ? 79.821  18.284  23.789 1.00 22.18 ? 96   ASP B CA  1 
ATOM   1810  C  C   . ASP B  1 97  ? 79.336  17.780  22.442 1.00 20.08 ? 96   ASP B C   1 
ATOM   1811  O  O   . ASP B  1 97  ? 80.007  16.995  21.777 1.00 21.67 ? 96   ASP B O   1 
ATOM   1812  C  CB  . ASP B  1 97  ? 81.346  18.177  23.907 1.00 22.17 ? 96   ASP B CB  1 
ATOM   1813  C  CG  . ASP B  1 97  ? 81.883  18.924  25.117 1.00 26.74 ? 96   ASP B CG  1 
ATOM   1814  O  OD1 . ASP B  1 97  ? 82.683  18.345  25.886 1.00 26.66 ? 96   ASP B OD1 1 
ATOM   1815  O  OD2 . ASP B  1 97  ? 81.494  20.099  25.295 1.00 27.76 ? 96   ASP B OD2 1 
ATOM   1816  N  N   . VAL B  1 98  ? 78.155  18.248  22.057 1.00 21.62 ? 97   VAL B N   1 
ATOM   1817  C  CA  . VAL B  1 98  ? 77.498  17.830  20.829 1.00 20.85 ? 97   VAL B CA  1 
ATOM   1818  C  C   . VAL B  1 98  ? 78.238  18.097  19.527 1.00 22.58 ? 97   VAL B C   1 
ATOM   1819  O  O   . VAL B  1 98  ? 78.766  19.191  19.294 1.00 21.11 ? 97   VAL B O   1 
ATOM   1820  C  CB  . VAL B  1 98  ? 76.088  18.457  20.729 1.00 20.52 ? 97   VAL B CB  1 
ATOM   1821  C  CG1 . VAL B  1 98  ? 75.362  17.922  19.499 1.00 18.84 ? 97   VAL B CG1 1 
ATOM   1822  C  CG2 . VAL B  1 98  ? 75.282  18.139  21.993 1.00 19.45 ? 97   VAL B CG2 1 
ATOM   1823  N  N   . SER B  1 99  ? 78.272  17.074  18.680 1.00 21.24 ? 98   SER B N   1 
ATOM   1824  C  CA  . SER B  1 99  ? 78.902  17.181  17.372 1.00 23.61 ? 98   SER B CA  1 
ATOM   1825  C  C   . SER B  1 99  ? 78.206  16.204  16.439 1.00 22.81 ? 98   SER B C   1 
ATOM   1826  O  O   . SER B  1 99  ? 78.515  15.010  16.415 1.00 24.97 ? 98   SER B O   1 
ATOM   1827  C  CB  . SER B  1 99  ? 80.394  16.855  17.442 1.00 24.27 ? 98   SER B CB  1 
ATOM   1828  O  OG  . SER B  1 99  ? 80.965  16.967  16.150 1.00 28.90 ? 98   SER B OG  1 
ATOM   1829  N  N   . ILE B  1 100 ? 77.263  16.726  15.673 1.00 21.19 ? 99   ILE B N   1 
ATOM   1830  C  CA  . ILE B  1 100 ? 76.478  15.922  14.749 1.00 23.07 ? 99   ILE B CA  1 
ATOM   1831  C  C   . ILE B  1 100 ? 76.436  16.570  13.373 1.00 23.98 ? 99   ILE B C   1 
ATOM   1832  O  O   . ILE B  1 100 ? 76.502  17.795  13.250 1.00 23.42 ? 99   ILE B O   1 
ATOM   1833  C  CB  . ILE B  1 100 ? 75.020  15.782  15.267 1.00 21.58 ? 99   ILE B CB  1 
ATOM   1834  C  CG1 . ILE B  1 100 ? 74.985  14.840  16.472 1.00 23.89 ? 99   ILE B CG1 1 
ATOM   1835  C  CG2 . ILE B  1 100 ? 74.093  15.297  14.153 1.00 24.95 ? 99   ILE B CG2 1 
ATOM   1836  C  CD1 . ILE B  1 100 ? 73.619  14.752  17.147 1.00 24.86 ? 99   ILE B CD1 1 
ATOM   1837  N  N   . GLU B  1 101 ? 76.342  15.737  12.344 1.00 22.59 ? 100  GLU B N   1 
ATOM   1838  C  CA  . GLU B  1 101 ? 76.225  16.219  10.979 1.00 23.70 ? 100  GLU B CA  1 
ATOM   1839  C  C   . GLU B  1 101 ? 75.069  15.415  10.402 1.00 22.35 ? 100  GLU B C   1 
ATOM   1840  O  O   . GLU B  1 101 ? 75.041  14.190  10.502 1.00 22.77 ? 100  GLU B O   1 
ATOM   1841  C  CB  . GLU B  1 101 ? 77.518  15.982  10.191 1.00 26.73 ? 100  GLU B CB  1 
ATOM   1842  C  CG  . GLU B  1 101 ? 77.520  16.663  8.836  1.00 33.67 ? 100  GLU B CG  1 
ATOM   1843  C  CD  . GLU B  1 101 ? 78.902  16.724  8.195  1.00 40.12 ? 100  GLU B CD  1 
ATOM   1844  O  OE1 . GLU B  1 101 ? 79.008  17.267  7.075  1.00 42.55 ? 100  GLU B OE1 1 
ATOM   1845  O  OE2 . GLU B  1 101 ? 79.880  16.239  8.806  1.00 43.54 ? 100  GLU B OE2 1 
ATOM   1846  N  N   . ASP B  1 102 ? 74.097  16.102  9.820  1.00 22.05 ? 101  ASP B N   1 
ATOM   1847  C  CA  . ASP B  1 102 ? 72.934  15.418  9.277  1.00 23.56 ? 101  ASP B CA  1 
ATOM   1848  C  C   . ASP B  1 102 ? 72.540  16.013  7.934  1.00 26.33 ? 101  ASP B C   1 
ATOM   1849  O  O   . ASP B  1 102 ? 72.579  17.233  7.753  1.00 24.22 ? 101  ASP B O   1 
ATOM   1850  C  CB  . ASP B  1 102 ? 71.765  15.530  10.257 1.00 21.27 ? 101  ASP B CB  1 
ATOM   1851  C  CG  . ASP B  1 102 ? 70.636  14.582  9.925  1.00 20.40 ? 101  ASP B CG  1 
ATOM   1852  O  OD1 . ASP B  1 102 ? 69.600  15.034  9.394  1.00 19.50 ? 101  ASP B OD1 1 
ATOM   1853  O  OD2 . ASP B  1 102 ? 70.797  13.374  10.188 1.00 22.24 ? 101  ASP B OD2 1 
ATOM   1854  N  N   . SER B  1 103 ? 72.144  15.146  7.006  1.00 24.37 ? 102  SER B N   1 
ATOM   1855  C  CA  . SER B  1 103 ? 71.764  15.572  5.669  1.00 26.60 ? 102  SER B CA  1 
ATOM   1856  C  C   . SER B  1 103 ? 70.267  15.584  5.413  1.00 26.23 ? 102  SER B C   1 
ATOM   1857  O  O   . SER B  1 103 ? 69.838  15.872  4.296  1.00 26.48 ? 102  SER B O   1 
ATOM   1858  C  CB  . SER B  1 103 ? 72.436  14.672  4.631  1.00 27.94 ? 102  SER B CB  1 
ATOM   1859  O  OG  . SER B  1 103 ? 73.845  14.762  4.734  1.00 36.15 ? 102  SER B OG  1 
ATOM   1860  N  N   . VAL B  1 104 ? 69.473  15.274  6.435  1.00 24.42 ? 103  VAL B N   1 
ATOM   1861  C  CA  . VAL B  1 104 ? 68.020  15.254  6.283  1.00 22.69 ? 103  VAL B CA  1 
ATOM   1862  C  C   . VAL B  1 104 ? 67.379  16.552  6.769  1.00 23.52 ? 103  VAL B C   1 
ATOM   1863  O  O   . VAL B  1 104 ? 66.470  17.084  6.127  1.00 21.72 ? 103  VAL B O   1 
ATOM   1864  C  CB  . VAL B  1 104 ? 67.404  14.039  7.026  1.00 24.30 ? 103  VAL B CB  1 
ATOM   1865  C  CG1 . VAL B  1 104 ? 65.887  14.113  6.989  1.00 22.97 ? 103  VAL B CG1 1 
ATOM   1866  C  CG2 . VAL B  1 104 ? 67.875  12.747  6.359  1.00 24.93 ? 103  VAL B CG2 1 
ATOM   1867  N  N   . ILE B  1 105 ? 67.826  17.061  7.913  1.00 22.11 ? 104  ILE B N   1 
ATOM   1868  C  CA  . ILE B  1 105 ? 67.287  18.331  8.383  1.00 21.16 ? 104  ILE B CA  1 
ATOM   1869  C  C   . ILE B  1 105 ? 67.905  19.400  7.484  1.00 20.49 ? 104  ILE B C   1 
ATOM   1870  O  O   . ILE B  1 105 ? 68.940  19.170  6.864  1.00 20.24 ? 104  ILE B O   1 
ATOM   1871  C  CB  . ILE B  1 105 ? 67.710  18.653  9.832  1.00 20.82 ? 104  ILE B CB  1 
ATOM   1872  C  CG1 . ILE B  1 105 ? 69.237  18.569  9.955  1.00 19.03 ? 104  ILE B CG1 1 
ATOM   1873  C  CG2 . ILE B  1 105 ? 66.992  17.728  10.806 1.00 20.89 ? 104  ILE B CG2 1 
ATOM   1874  C  CD1 . ILE B  1 105 ? 69.791  19.132  11.268 1.00 18.51 ? 104  ILE B CD1 1 
ATOM   1875  N  N   . SER B  1 106 ? 67.275  20.561  7.415  1.00 21.16 ? 105  SER B N   1 
ATOM   1876  C  CA  . SER B  1 106 ? 67.800  21.655  6.610  1.00 22.20 ? 105  SER B CA  1 
ATOM   1877  C  C   . SER B  1 106 ? 67.458  22.967  7.302  1.00 22.25 ? 105  SER B C   1 
ATOM   1878  O  O   . SER B  1 106 ? 66.620  22.989  8.198  1.00 23.74 ? 105  SER B O   1 
ATOM   1879  C  CB  . SER B  1 106 ? 67.178  21.633  5.214  1.00 22.06 ? 105  SER B CB  1 
ATOM   1880  O  OG  . SER B  1 106 ? 67.753  22.636  4.404  1.00 21.43 ? 105  SER B OG  1 
ATOM   1881  N  N   . LEU B  1 107 ? 68.104  24.056  6.894  1.00 23.89 ? 106  LEU B N   1 
ATOM   1882  C  CA  . LEU B  1 107 ? 67.817  25.358  7.482  1.00 24.37 ? 106  LEU B CA  1 
ATOM   1883  C  C   . LEU B  1 107 ? 66.963  26.195  6.532  1.00 26.67 ? 106  LEU B C   1 
ATOM   1884  O  O   . LEU B  1 107 ? 66.796  27.398  6.729  1.00 25.16 ? 106  LEU B O   1 
ATOM   1885  C  CB  . LEU B  1 107 ? 69.113  26.099  7.834  1.00 24.26 ? 106  LEU B CB  1 
ATOM   1886  C  CG  . LEU B  1 107 ? 69.994  25.416  8.894  1.00 23.77 ? 106  LEU B CG  1 
ATOM   1887  C  CD1 . LEU B  1 107 ? 71.084  26.383  9.346  1.00 22.46 ? 106  LEU B CD1 1 
ATOM   1888  C  CD2 . LEU B  1 107 ? 69.146  24.986  10.097 1.00 21.44 ? 106  LEU B CD2 1 
ATOM   1889  N  N   . SER B  1 108 ? 66.426  25.542  5.502  1.00 25.76 ? 107  SER B N   1 
ATOM   1890  C  CA  . SER B  1 108 ? 65.547  26.192  4.533  1.00 27.91 ? 107  SER B CA  1 
ATOM   1891  C  C   . SER B  1 108 ? 64.737  25.135  3.774  1.00 27.68 ? 107  SER B C   1 
ATOM   1892  O  O   . SER B  1 108 ? 65.072  23.948  3.791  1.00 25.13 ? 107  SER B O   1 
ATOM   1893  C  CB  . SER B  1 108 ? 66.355  27.029  3.537  1.00 31.65 ? 107  SER B CB  1 
ATOM   1894  O  OG  . SER B  1 108 ? 67.020  26.203  2.603  1.00 32.67 ? 107  SER B OG  1 
ATOM   1895  N  N   . GLY B  1 109 ? 63.660  25.567  3.126  1.00 28.16 ? 108  GLY B N   1 
ATOM   1896  C  CA  . GLY B  1 109 ? 62.835  24.638  2.372  1.00 29.59 ? 108  GLY B CA  1 
ATOM   1897  C  C   . GLY B  1 109 ? 61.825  23.879  3.214  1.00 31.21 ? 108  GLY B C   1 
ATOM   1898  O  O   . GLY B  1 109 ? 61.559  24.239  4.363  1.00 30.78 ? 108  GLY B O   1 
ATOM   1899  N  N   . ASP B  1 110 ? 61.277  22.814  2.632  1.00 31.59 ? 109  ASP B N   1 
ATOM   1900  C  CA  . ASP B  1 110 ? 60.271  21.963  3.271  1.00 32.17 ? 109  ASP B CA  1 
ATOM   1901  C  C   . ASP B  1 110 ? 60.736  21.249  4.528  1.00 29.47 ? 109  ASP B C   1 
ATOM   1902  O  O   . ASP B  1 110 ? 59.936  20.965  5.415  1.00 29.83 ? 109  ASP B O   1 
ATOM   1903  C  CB  . ASP B  1 110 ? 59.779  20.896  2.286  1.00 34.33 ? 109  ASP B CB  1 
ATOM   1904  C  CG  . ASP B  1 110 ? 58.929  21.472  1.180  1.00 39.92 ? 109  ASP B CG  1 
ATOM   1905  O  OD1 . ASP B  1 110 ? 58.492  20.695  0.307  1.00 40.39 ? 109  ASP B OD1 1 
ATOM   1906  O  OD2 . ASP B  1 110 ? 58.692  22.700  1.186  1.00 43.26 ? 109  ASP B OD2 1 
ATOM   1907  N  N   . HIS B  1 111 ? 62.018  20.922  4.590  1.00 28.03 ? 110  HIS B N   1 
ATOM   1908  C  CA  . HIS B  1 111 ? 62.536  20.220  5.750  1.00 28.26 ? 110  HIS B CA  1 
ATOM   1909  C  C   . HIS B  1 111 ? 63.274  21.147  6.703  1.00 25.68 ? 110  HIS B C   1 
ATOM   1910  O  O   . HIS B  1 111 ? 64.075  20.691  7.520  1.00 24.47 ? 110  HIS B O   1 
ATOM   1911  C  CB  . HIS B  1 111 ? 63.443  19.079  5.297  1.00 30.10 ? 110  HIS B CB  1 
ATOM   1912  C  CG  . HIS B  1 111 ? 62.744  18.061  4.460  1.00 33.19 ? 110  HIS B CG  1 
ATOM   1913  N  ND1 . HIS B  1 111 ? 63.400  17.008  3.854  1.00 34.66 ? 110  HIS B ND1 1 
ATOM   1914  C  CD2 . HIS B  1 111 ? 61.437  17.924  4.119  1.00 35.96 ? 110  HIS B CD2 1 
ATOM   1915  C  CE1 . HIS B  1 111 ? 62.537  16.277  3.182  1.00 36.38 ? 110  HIS B CE1 1 
ATOM   1916  N  NE2 . HIS B  1 111 ? 61.333  16.812  3.327  1.00 35.50 ? 110  HIS B NE2 1 
ATOM   1917  N  N   . SER B  1 112 ? 62.985  22.443  6.610  1.00 22.88 ? 111  SER B N   1 
ATOM   1918  C  CA  . SER B  1 112 ? 63.638  23.413  7.478  1.00 24.01 ? 111  SER B CA  1 
ATOM   1919  C  C   . SER B  1 112 ? 63.208  23.248  8.923  1.00 21.12 ? 111  SER B C   1 
ATOM   1920  O  O   . SER B  1 112 ? 62.032  23.051  9.211  1.00 19.84 ? 111  SER B O   1 
ATOM   1921  C  CB  . SER B  1 112 ? 63.333  24.846  7.041  1.00 24.27 ? 111  SER B CB  1 
ATOM   1922  O  OG  . SER B  1 112 ? 63.960  25.755  7.933  1.00 22.87 ? 111  SER B OG  1 
ATOM   1923  N  N   . ILE B  1 113 ? 64.168  23.343  9.831  1.00 20.80 ? 112  ILE B N   1 
ATOM   1924  C  CA  . ILE B  1 113 ? 63.881  23.216  11.252 1.00 20.17 ? 112  ILE B CA  1 
ATOM   1925  C  C   . ILE B  1 113 ? 63.792  24.595  11.910 1.00 20.95 ? 112  ILE B C   1 
ATOM   1926  O  O   . ILE B  1 113 ? 63.631  24.707  13.128 1.00 19.58 ? 112  ILE B O   1 
ATOM   1927  C  CB  . ILE B  1 113 ? 64.964  22.369  11.954 1.00 22.15 ? 112  ILE B CB  1 
ATOM   1928  C  CG1 . ILE B  1 113 ? 66.352  22.957  11.683 1.00 21.83 ? 112  ILE B CG1 1 
ATOM   1929  C  CG2 . ILE B  1 113 ? 64.901  20.927  11.436 1.00 22.19 ? 112  ILE B CG2 1 
ATOM   1930  C  CD1 . ILE B  1 113 ? 67.468  22.318  12.509 1.00 21.62 ? 112  ILE B CD1 1 
ATOM   1931  N  N   . ILE B  1 114 ? 63.894  25.646  11.099 1.00 22.04 ? 113  ILE B N   1 
ATOM   1932  C  CA  . ILE B  1 114 ? 63.811  27.009  11.623 1.00 21.90 ? 113  ILE B CA  1 
ATOM   1933  C  C   . ILE B  1 114 ? 62.408  27.229  12.187 1.00 22.04 ? 113  ILE B C   1 
ATOM   1934  O  O   . ILE B  1 114 ? 61.416  26.903  11.539 1.00 22.65 ? 113  ILE B O   1 
ATOM   1935  C  CB  . ILE B  1 114 ? 64.052  28.059  10.516 1.00 22.21 ? 113  ILE B CB  1 
ATOM   1936  C  CG1 . ILE B  1 114 ? 65.461  27.900  9.923  1.00 21.80 ? 113  ILE B CG1 1 
ATOM   1937  C  CG2 . ILE B  1 114 ? 63.835  29.460  11.082 1.00 20.73 ? 113  ILE B CG2 1 
ATOM   1938  C  CD1 . ILE B  1 114 ? 66.583  28.228  10.877 1.00 23.12 ? 113  ILE B CD1 1 
ATOM   1939  N  N   . GLY B  1 115 ? 62.323  27.765  13.399 1.00 22.20 ? 114  GLY B N   1 
ATOM   1940  C  CA  . GLY B  1 115 ? 61.018  28.006  13.991 1.00 21.09 ? 114  GLY B CA  1 
ATOM   1941  C  C   . GLY B  1 115 ? 60.426  26.790  14.681 1.00 22.71 ? 114  GLY B C   1 
ATOM   1942  O  O   . GLY B  1 115 ? 59.308  26.848  15.189 1.00 21.92 ? 114  GLY B O   1 
ATOM   1943  N  N   . ARG B  1 116 ? 61.165  25.684  14.695 1.00 19.53 ? 115  ARG B N   1 
ATOM   1944  C  CA  . ARG B  1 116 ? 60.688  24.476  15.357 1.00 22.50 ? 115  ARG B CA  1 
ATOM   1945  C  C   . ARG B  1 116 ? 61.455  24.333  16.675 1.00 21.36 ? 115  ARG B C   1 
ATOM   1946  O  O   . ARG B  1 116 ? 62.242  25.210  17.025 1.00 23.95 ? 115  ARG B O   1 
ATOM   1947  C  CB  . ARG B  1 116 ? 60.844  23.263  14.416 1.00 19.90 ? 115  ARG B CB  1 
ATOM   1948  C  CG  . ARG B  1 116 ? 60.096  23.512  13.081 1.00 22.07 ? 115  ARG B CG  1 
ATOM   1949  C  CD  . ARG B  1 116 ? 59.915  22.282  12.204 1.00 23.31 ? 115  ARG B CD  1 
ATOM   1950  N  NE  . ARG B  1 116 ? 59.293  22.629  10.922 1.00 22.26 ? 115  ARG B NE  1 
ATOM   1951  C  CZ  . ARG B  1 116 ? 57.984  22.778  10.725 1.00 22.84 ? 115  ARG B CZ  1 
ATOM   1952  N  NH1 . ARG B  1 116 ? 57.532  23.099  9.518  1.00 21.68 ? 115  ARG B NH1 1 
ATOM   1953  N  NH2 . ARG B  1 116 ? 57.120  22.583  11.720 1.00 22.40 ? 115  ARG B NH2 1 
ATOM   1954  N  N   . THR B  1 117 ? 61.228  23.258  17.416 1.00 21.89 ? 116  THR B N   1 
ATOM   1955  C  CA  . THR B  1 117 ? 61.874  23.107  18.720 1.00 19.18 ? 116  THR B CA  1 
ATOM   1956  C  C   . THR B  1 117 ? 62.884  21.971  18.857 1.00 20.93 ? 116  THR B C   1 
ATOM   1957  O  O   . THR B  1 117 ? 62.592  20.823  18.503 1.00 21.29 ? 116  THR B O   1 
ATOM   1958  C  CB  . THR B  1 117 ? 60.792  22.926  19.831 1.00 19.02 ? 116  THR B CB  1 
ATOM   1959  O  OG1 . THR B  1 117 ? 59.918  24.071  19.857 1.00 20.45 ? 116  THR B OG1 1 
ATOM   1960  C  CG2 . THR B  1 117 ? 61.437  22.757  21.197 1.00 15.55 ? 116  THR B CG2 1 
ATOM   1961  N  N   . LEU B  1 118 ? 64.069  22.297  19.377 1.00 18.70 ? 117  LEU B N   1 
ATOM   1962  C  CA  . LEU B  1 118 ? 65.108  21.298  19.625 1.00 18.26 ? 117  LEU B CA  1 
ATOM   1963  C  C   . LEU B  1 118 ? 64.866  20.803  21.058 1.00 20.05 ? 117  LEU B C   1 
ATOM   1964  O  O   . LEU B  1 118 ? 64.710  21.606  21.982 1.00 20.08 ? 117  LEU B O   1 
ATOM   1965  C  CB  . LEU B  1 118 ? 66.509  21.913  19.528 1.00 15.40 ? 117  LEU B CB  1 
ATOM   1966  C  CG  . LEU B  1 118 ? 67.658  20.916  19.748 1.00 17.81 ? 117  LEU B CG  1 
ATOM   1967  C  CD1 . LEU B  1 118 ? 67.653  19.873  18.628 1.00 17.00 ? 117  LEU B CD1 1 
ATOM   1968  C  CD2 . LEU B  1 118 ? 68.996  21.648  19.786 1.00 18.01 ? 117  LEU B CD2 1 
ATOM   1969  N  N   . VAL B  1 119 ? 64.848  19.489  21.241 1.00 19.40 ? 118  VAL B N   1 
ATOM   1970  C  CA  . VAL B  1 119 ? 64.582  18.894  22.550 1.00 19.53 ? 118  VAL B CA  1 
ATOM   1971  C  C   . VAL B  1 119 ? 65.635  17.858  22.951 1.00 20.21 ? 118  VAL B C   1 
ATOM   1972  O  O   . VAL B  1 119 ? 66.071  17.049  22.129 1.00 18.06 ? 118  VAL B O   1 
ATOM   1973  C  CB  . VAL B  1 119 ? 63.200  18.173  22.544 1.00 19.30 ? 118  VAL B CB  1 
ATOM   1974  C  CG1 . VAL B  1 119 ? 62.920  17.557  23.910 1.00 18.78 ? 118  VAL B CG1 1 
ATOM   1975  C  CG2 . VAL B  1 119 ? 62.087  19.149  22.131 1.00 17.31 ? 118  VAL B CG2 1 
ATOM   1976  N  N   . VAL B  1 120 ? 66.059  17.886  24.210 1.00 19.88 ? 119  VAL B N   1 
ATOM   1977  C  CA  . VAL B  1 120 ? 67.000  16.884  24.681 1.00 18.88 ? 119  VAL B CA  1 
ATOM   1978  C  C   . VAL B  1 120 ? 66.215  16.116  25.743 1.00 20.13 ? 119  VAL B C   1 
ATOM   1979  O  O   . VAL B  1 120 ? 65.593  16.719  26.630 1.00 18.84 ? 119  VAL B O   1 
ATOM   1980  C  CB  . VAL B  1 120 ? 68.306  17.513  25.244 1.00 20.66 ? 119  VAL B CB  1 
ATOM   1981  C  CG1 . VAL B  1 120 ? 68.009  18.416  26.428 1.00 18.25 ? 119  VAL B CG1 1 
ATOM   1982  C  CG2 . VAL B  1 120 ? 69.278  16.399  25.622 1.00 18.72 ? 119  VAL B CG2 1 
ATOM   1983  N  N   . HIS B  1 121 ? 66.239  14.788  25.637 1.00 19.60 ? 120  HIS B N   1 
ATOM   1984  C  CA  . HIS B  1 121 ? 65.466  13.906  26.511 1.00 20.87 ? 120  HIS B CA  1 
ATOM   1985  C  C   . HIS B  1 121 ? 66.082  13.294  27.757 1.00 22.55 ? 120  HIS B C   1 
ATOM   1986  O  O   . HIS B  1 121 ? 67.295  13.294  27.960 1.00 24.06 ? 120  HIS B O   1 
ATOM   1987  C  CB  . HIS B  1 121 ? 64.886  12.763  25.679 1.00 19.18 ? 120  HIS B CB  1 
ATOM   1988  C  CG  . HIS B  1 121 ? 63.837  13.200  24.702 1.00 20.04 ? 120  HIS B CG  1 
ATOM   1989  N  ND1 . HIS B  1 121 ? 62.494  13.132  24.976 1.00 18.93 ? 120  HIS B ND1 1 
ATOM   1990  C  CD2 . HIS B  1 121 ? 63.954  13.733  23.462 1.00 18.91 ? 120  HIS B CD2 1 
ATOM   1991  C  CE1 . HIS B  1 121 ? 61.814  13.603  23.941 1.00 18.19 ? 120  HIS B CE1 1 
ATOM   1992  N  NE2 . HIS B  1 121 ? 62.674  13.974  23.014 1.00 20.32 ? 120  HIS B NE2 1 
ATOM   1993  N  N   . GLU B  1 122 ? 65.189  12.733  28.564 1.00 24.79 ? 121  GLU B N   1 
ATOM   1994  C  CA  . GLU B  1 122 ? 65.517  12.067  29.817 1.00 24.24 ? 121  GLU B CA  1 
ATOM   1995  C  C   . GLU B  1 122 ? 66.351  10.807  29.614 1.00 23.69 ? 121  GLU B C   1 
ATOM   1996  O  O   . GLU B  1 122 ? 67.330  10.585  30.322 1.00 24.44 ? 121  GLU B O   1 
ATOM   1997  C  CB  . GLU B  1 122 ? 64.217  11.693  30.538 1.00 24.86 ? 121  GLU B CB  1 
ATOM   1998  C  CG  . GLU B  1 122 ? 64.415  10.888  31.809 1.00 30.32 ? 121  GLU B CG  1 
ATOM   1999  C  CD  . GLU B  1 122 ? 63.126  10.248  32.309 1.00 31.05 ? 121  GLU B CD  1 
ATOM   2000  O  OE1 . GLU B  1 122 ? 63.149  9.692   33.422 1.00 34.67 ? 121  GLU B OE1 1 
ATOM   2001  O  OE2 . GLU B  1 122 ? 62.101  10.290  31.592 1.00 30.95 ? 121  GLU B OE2 1 
ATOM   2002  N  N   . LYS B  1 123 ? 65.962  9.989   28.639 1.00 24.23 ? 122  LYS B N   1 
ATOM   2003  C  CA  . LYS B  1 123 ? 66.653  8.726   28.375 1.00 24.94 ? 122  LYS B CA  1 
ATOM   2004  C  C   . LYS B  1 123 ? 67.190  8.587   26.956 1.00 21.52 ? 122  LYS B C   1 
ATOM   2005  O  O   . LYS B  1 123 ? 67.015  9.465   26.117 1.00 19.92 ? 122  LYS B O   1 
ATOM   2006  C  CB  . LYS B  1 123 ? 65.701  7.550   28.641 1.00 29.40 ? 122  LYS B CB  1 
ATOM   2007  C  CG  . LYS B  1 123 ? 64.971  7.623   29.968 1.00 35.55 ? 122  LYS B CG  1 
ATOM   2008  C  CD  . LYS B  1 123 ? 64.224  6.336   30.267 1.00 40.37 ? 122  LYS B CD  1 
ATOM   2009  C  CE  . LYS B  1 123 ? 63.101  6.081   29.275 1.00 42.85 ? 122  LYS B CE  1 
ATOM   2010  N  NZ  . LYS B  1 123 ? 62.303  4.874   29.663 1.00 45.27 ? 122  LYS B NZ  1 
ATOM   2011  N  N   . ALA B  1 124 ? 67.828  7.453   26.695 1.00 21.54 ? 123  ALA B N   1 
ATOM   2012  C  CA  . ALA B  1 124 ? 68.372  7.170   25.372 1.00 22.73 ? 123  ALA B CA  1 
ATOM   2013  C  C   . ALA B  1 124 ? 67.249  6.926   24.372 1.00 23.44 ? 123  ALA B C   1 
ATOM   2014  O  O   . ALA B  1 124 ? 66.150  6.485   24.733 1.00 21.21 ? 123  ALA B O   1 
ATOM   2015  C  CB  . ALA B  1 124 ? 69.284  5.945   25.427 1.00 21.79 ? 123  ALA B CB  1 
ATOM   2016  N  N   . ASP B  1 125 ? 67.529  7.236   23.113 1.00 21.66 ? 124  ASP B N   1 
ATOM   2017  C  CA  . ASP B  1 125 ? 66.578  7.021   22.031 1.00 23.26 ? 124  ASP B CA  1 
ATOM   2018  C  C   . ASP B  1 125 ? 66.972  5.637   21.521 1.00 23.70 ? 124  ASP B C   1 
ATOM   2019  O  O   . ASP B  1 125 ? 68.141  5.418   21.204 1.00 22.49 ? 124  ASP B O   1 
ATOM   2020  C  CB  . ASP B  1 125 ? 66.789  8.105   20.963 1.00 21.56 ? 124  ASP B CB  1 
ATOM   2021  C  CG  . ASP B  1 125 ? 65.888  7.936   19.749 1.00 22.65 ? 124  ASP B CG  1 
ATOM   2022  O  OD1 . ASP B  1 125 ? 65.705  8.935   19.022 1.00 19.96 ? 124  ASP B OD1 1 
ATOM   2023  O  OD2 . ASP B  1 125 ? 65.382  6.820   19.506 1.00 22.14 ? 124  ASP B OD2 1 
ATOM   2024  N  N   . ASP B  1 126 ? 66.024  4.695   21.470 1.00 24.31 ? 125  ASP B N   1 
ATOM   2025  C  CA  . ASP B  1 126 ? 66.352  3.342   21.012 1.00 23.23 ? 125  ASP B CA  1 
ATOM   2026  C  C   . ASP B  1 126 ? 66.440  3.237   19.499 1.00 23.61 ? 125  ASP B C   1 
ATOM   2027  O  O   . ASP B  1 126 ? 66.584  2.149   18.943 1.00 22.96 ? 125  ASP B O   1 
ATOM   2028  C  CB  . ASP B  1 126 ? 65.364  2.301   21.583 1.00 25.63 ? 125  ASP B CB  1 
ATOM   2029  C  CG  . ASP B  1 126 ? 63.948  2.425   21.022 1.00 27.26 ? 125  ASP B CG  1 
ATOM   2030  O  OD1 . ASP B  1 126 ? 63.033  1.861   21.664 1.00 24.84 ? 125  ASP B OD1 1 
ATOM   2031  O  OD2 . ASP B  1 126 ? 63.739  3.049   19.957 1.00 25.03 ? 125  ASP B OD2 1 
ATOM   2032  N  N   . LEU B  1 127 ? 66.355  4.390   18.843 1.00 22.39 ? 126  LEU B N   1 
ATOM   2033  C  CA  . LEU B  1 127 ? 66.466  4.484   17.398 1.00 20.47 ? 126  LEU B CA  1 
ATOM   2034  C  C   . LEU B  1 127 ? 65.466  3.611   16.641 1.00 21.50 ? 126  LEU B C   1 
ATOM   2035  O  O   . LEU B  1 127 ? 65.733  3.181   15.515 1.00 19.89 ? 126  LEU B O   1 
ATOM   2036  C  CB  . LEU B  1 127 ? 67.902  4.145   16.986 1.00 19.56 ? 126  LEU B CB  1 
ATOM   2037  C  CG  . LEU B  1 127 ? 68.965  4.838   17.861 1.00 21.14 ? 126  LEU B CG  1 
ATOM   2038  C  CD1 . LEU B  1 127 ? 70.357  4.521   17.349 1.00 17.52 ? 126  LEU B CD1 1 
ATOM   2039  C  CD2 . LEU B  1 127 ? 68.734  6.346   17.863 1.00 14.55 ? 126  LEU B CD2 1 
ATOM   2040  N  N   . GLY B  1 128 ? 64.319  3.363   17.268 1.00 22.47 ? 127  GLY B N   1 
ATOM   2041  C  CA  . GLY B  1 128 ? 63.268  2.571   16.645 1.00 22.40 ? 127  GLY B CA  1 
ATOM   2042  C  C   . GLY B  1 128 ? 63.476  1.070   16.662 1.00 24.79 ? 127  GLY B C   1 
ATOM   2043  O  O   . GLY B  1 128 ? 62.770  0.330   15.970 1.00 25.44 ? 127  GLY B O   1 
ATOM   2044  N  N   . LYS B  1 129 ? 64.424  0.611   17.467 1.00 23.62 ? 128  LYS B N   1 
ATOM   2045  C  CA  . LYS B  1 129 ? 64.729  -0.811  17.545 1.00 25.22 ? 128  LYS B CA  1 
ATOM   2046  C  C   . LYS B  1 129 ? 64.244  -1.447  18.843 1.00 23.26 ? 128  LYS B C   1 
ATOM   2047  O  O   . LYS B  1 129 ? 64.751  -2.490  19.250 1.00 27.41 ? 128  LYS B O   1 
ATOM   2048  C  CB  . LYS B  1 129 ? 66.244  -1.000  17.380 1.00 23.27 ? 128  LYS B CB  1 
ATOM   2049  C  CG  . LYS B  1 129 ? 66.754  -0.412  16.066 1.00 26.05 ? 128  LYS B CG  1 
ATOM   2050  C  CD  . LYS B  1 129 ? 68.273  -0.363  15.960 1.00 31.65 ? 128  LYS B CD  1 
ATOM   2051  C  CE  . LYS B  1 129 ? 68.888  -1.735  15.747 1.00 35.12 ? 128  LYS B CE  1 
ATOM   2052  N  NZ  . LYS B  1 129 ? 70.375  -1.640  15.575 1.00 38.34 ? 128  LYS B NZ  1 
ATOM   2053  N  N   . GLY B  1 130 ? 63.245  -0.825  19.465 1.00 23.06 ? 129  GLY B N   1 
ATOM   2054  C  CA  . GLY B  1 130 ? 62.699  -1.315  20.724 1.00 23.09 ? 129  GLY B CA  1 
ATOM   2055  C  C   . GLY B  1 130 ? 61.595  -2.369  20.674 1.00 25.37 ? 129  GLY B C   1 
ATOM   2056  O  O   . GLY B  1 130 ? 61.255  -2.951  21.706 1.00 25.05 ? 129  GLY B O   1 
ATOM   2057  N  N   . GLY B  1 131 ? 61.014  -2.605  19.500 1.00 25.82 ? 130  GLY B N   1 
ATOM   2058  C  CA  . GLY B  1 131 ? 59.978  -3.622  19.391 1.00 26.49 ? 130  GLY B CA  1 
ATOM   2059  C  C   . GLY B  1 131 ? 58.564  -3.279  19.836 1.00 28.31 ? 130  GLY B C   1 
ATOM   2060  O  O   . GLY B  1 131 ? 57.687  -4.141  19.784 1.00 28.84 ? 130  GLY B O   1 
ATOM   2061  N  N   . ASN B  1 132 ? 58.326  -2.050  20.286 1.00 27.65 ? 131  ASN B N   1 
ATOM   2062  C  CA  . ASN B  1 132 ? 56.979  -1.656  20.688 1.00 28.02 ? 131  ASN B CA  1 
ATOM   2063  C  C   . ASN B  1 132 ? 56.519  -0.458  19.864 1.00 29.23 ? 131  ASN B C   1 
ATOM   2064  O  O   . ASN B  1 132 ? 57.308  0.134   19.123 1.00 28.86 ? 131  ASN B O   1 
ATOM   2065  C  CB  . ASN B  1 132 ? 56.903  -1.353  22.195 1.00 30.19 ? 131  ASN B CB  1 
ATOM   2066  C  CG  . ASN B  1 132 ? 57.909  -0.313  22.648 1.00 31.44 ? 131  ASN B CG  1 
ATOM   2067  O  OD1 . ASN B  1 132 ? 58.366  0.515   21.864 1.00 30.20 ? 131  ASN B OD1 1 
ATOM   2068  N  ND2 . ASN B  1 132 ? 58.243  -0.343  23.931 1.00 31.62 ? 131  ASN B ND2 1 
ATOM   2069  N  N   . GLU B  1 133 ? 55.244  -0.101  19.978 1.00 29.84 ? 132  GLU B N   1 
ATOM   2070  C  CA  . GLU B  1 133 ? 54.709  1.008   19.200 1.00 31.83 ? 132  GLU B CA  1 
ATOM   2071  C  C   . GLU B  1 133 ? 55.379  2.333   19.544 1.00 31.42 ? 132  GLU B C   1 
ATOM   2072  O  O   . GLU B  1 133 ? 55.585  3.179   18.673 1.00 31.31 ? 132  GLU B O   1 
ATOM   2073  C  CB  . GLU B  1 133 ? 53.193  1.119   19.406 1.00 36.76 ? 132  GLU B CB  1 
ATOM   2074  C  CG  . GLU B  1 133 ? 52.521  2.131   18.489 1.00 43.68 ? 132  GLU B CG  1 
ATOM   2075  C  CD  . GLU B  1 133 ? 51.003  2.128   18.610 1.00 48.78 ? 132  GLU B CD  1 
ATOM   2076  O  OE1 . GLU B  1 133 ? 50.350  2.935   17.909 1.00 50.26 ? 132  GLU B OE1 1 
ATOM   2077  O  OE2 . GLU B  1 133 ? 50.466  1.320   19.402 1.00 51.01 ? 132  GLU B OE2 1 
ATOM   2078  N  N   . GLU B  1 134 ? 55.724  2.506   20.815 1.00 30.32 ? 133  GLU B N   1 
ATOM   2079  C  CA  . GLU B  1 134 ? 56.366  3.731   21.267 1.00 29.96 ? 133  GLU B CA  1 
ATOM   2080  C  C   . GLU B  1 134 ? 57.736  3.919   20.608 1.00 27.66 ? 133  GLU B C   1 
ATOM   2081  O  O   . GLU B  1 134 ? 58.135  5.041   20.305 1.00 26.49 ? 133  GLU B O   1 
ATOM   2082  C  CB  . GLU B  1 134 ? 56.514  3.716   22.793 1.00 32.91 ? 133  GLU B CB  1 
ATOM   2083  C  CG  . GLU B  1 134 ? 57.045  5.018   23.370 1.00 38.90 ? 133  GLU B CG  1 
ATOM   2084  C  CD  . GLU B  1 134 ? 56.097  6.184   23.155 1.00 41.98 ? 133  GLU B CD  1 
ATOM   2085  O  OE1 . GLU B  1 134 ? 56.497  7.334   23.427 1.00 46.54 ? 133  GLU B OE1 1 
ATOM   2086  O  OE2 . GLU B  1 134 ? 54.948  5.959   22.723 1.00 45.69 ? 133  GLU B OE2 1 
ATOM   2087  N  N   . SER B  1 135 ? 58.449  2.821   20.379 1.00 23.99 ? 134  SER B N   1 
ATOM   2088  C  CA  . SER B  1 135 ? 59.768  2.895   19.754 1.00 24.12 ? 134  SER B CA  1 
ATOM   2089  C  C   . SER B  1 135 ? 59.688  3.509   18.358 1.00 25.49 ? 134  SER B C   1 
ATOM   2090  O  O   . SER B  1 135 ? 60.562  4.291   17.963 1.00 25.36 ? 134  SER B O   1 
ATOM   2091  C  CB  . SER B  1 135 ? 60.389  1.499   19.669 1.00 22.61 ? 134  SER B CB  1 
ATOM   2092  O  OG  . SER B  1 135 ? 61.627  1.526   18.982 1.00 22.31 ? 134  SER B OG  1 
ATOM   2093  N  N   . THR B  1 136 ? 58.630  3.159   17.627 1.00 25.07 ? 135  THR B N   1 
ATOM   2094  C  CA  . THR B  1 136 ? 58.405  3.651   16.268 1.00 27.03 ? 135  THR B CA  1 
ATOM   2095  C  C   . THR B  1 136 ? 57.817  5.054   16.258 1.00 25.28 ? 135  THR B C   1 
ATOM   2096  O  O   . THR B  1 136 ? 57.504  5.594   15.195 1.00 26.45 ? 135  THR B O   1 
ATOM   2097  C  CB  . THR B  1 136 ? 57.429  2.735   15.483 1.00 29.53 ? 135  THR B CB  1 
ATOM   2098  O  OG1 . THR B  1 136 ? 56.088  2.955   15.943 1.00 35.50 ? 135  THR B OG1 1 
ATOM   2099  C  CG2 . THR B  1 136 ? 57.782  1.286   15.689 1.00 33.00 ? 135  THR B CG2 1 
ATOM   2100  N  N   . LYS B  1 137 ? 57.652  5.641   17.437 1.00 25.86 ? 136  LYS B N   1 
ATOM   2101  C  CA  . LYS B  1 137 ? 57.114  6.994   17.525 1.00 27.75 ? 136  LYS B CA  1 
ATOM   2102  C  C   . LYS B  1 137 ? 58.069  7.982   18.189 1.00 26.56 ? 136  LYS B C   1 
ATOM   2103  O  O   . LYS B  1 137 ? 58.327  9.062   17.651 1.00 26.92 ? 136  LYS B O   1 
ATOM   2104  C  CB  . LYS B  1 137 ? 55.782  7.002   18.286 1.00 31.55 ? 136  LYS B CB  1 
ATOM   2105  C  CG  . LYS B  1 137 ? 54.632  6.359   17.534 1.00 37.27 ? 136  LYS B CG  1 
ATOM   2106  C  CD  . LYS B  1 137 ? 53.316  6.571   18.270 1.00 43.65 ? 136  LYS B CD  1 
ATOM   2107  C  CE  . LYS B  1 137 ? 52.142  6.002   17.485 1.00 46.31 ? 136  LYS B CE  1 
ATOM   2108  N  NZ  . LYS B  1 137 ? 50.842  6.277   18.166 1.00 50.50 ? 136  LYS B NZ  1 
ATOM   2109  N  N   . THR B  1 138 ? 58.603  7.608   19.349 1.00 25.89 ? 137  THR B N   1 
ATOM   2110  C  CA  . THR B  1 138 ? 59.497  8.492   20.094 1.00 24.96 ? 137  THR B CA  1 
ATOM   2111  C  C   . THR B  1 138 ? 60.857  7.886   20.406 1.00 24.55 ? 137  THR B C   1 
ATOM   2112  O  O   . THR B  1 138 ? 61.749  8.579   20.892 1.00 25.54 ? 137  THR B O   1 
ATOM   2113  C  CB  . THR B  1 138 ? 58.878  8.882   21.446 1.00 24.30 ? 137  THR B CB  1 
ATOM   2114  O  OG1 . THR B  1 138 ? 58.802  7.716   22.273 1.00 26.06 ? 137  THR B OG1 1 
ATOM   2115  C  CG2 . THR B  1 138 ? 57.479  9.454   21.263 1.00 25.68 ? 137  THR B CG2 1 
ATOM   2116  N  N   . GLY B  1 139 ? 61.019  6.597   20.142 1.00 21.50 ? 138  GLY B N   1 
ATOM   2117  C  CA  . GLY B  1 139 ? 62.276  5.954   20.458 1.00 21.42 ? 138  GLY B CA  1 
ATOM   2118  C  C   . GLY B  1 139 ? 62.348  5.655   21.952 1.00 22.79 ? 138  GLY B C   1 
ATOM   2119  O  O   . GLY B  1 139 ? 63.394  5.250   22.457 1.00 22.33 ? 138  GLY B O   1 
ATOM   2120  N  N   . ASN B  1 140 ? 61.239  5.858   22.663 1.00 23.93 ? 139  ASN B N   1 
ATOM   2121  C  CA  . ASN B  1 140 ? 61.195  5.598   24.106 1.00 25.16 ? 139  ASN B CA  1 
ATOM   2122  C  C   . ASN B  1 140 ? 62.232  6.445   24.849 1.00 24.36 ? 139  ASN B C   1 
ATOM   2123  O  O   . ASN B  1 140 ? 62.833  5.978   25.813 1.00 22.20 ? 139  ASN B O   1 
ATOM   2124  C  CB  . ASN B  1 140 ? 61.481  4.115   24.386 1.00 26.75 ? 139  ASN B CB  1 
ATOM   2125  C  CG  . ASN B  1 140 ? 60.310  3.210   24.029 1.00 29.77 ? 139  ASN B CG  1 
ATOM   2126  O  OD1 . ASN B  1 140 ? 59.233  3.319   24.612 1.00 31.85 ? 139  ASN B OD1 1 
ATOM   2127  N  ND2 . ASN B  1 140 ? 60.518  2.315   23.070 1.00 26.86 ? 139  ASN B ND2 1 
ATOM   2128  N  N   . ALA B  1 141 ? 62.426  7.687   24.407 1.00 22.04 ? 140  ALA B N   1 
ATOM   2129  C  CA  . ALA B  1 141 ? 63.426  8.569   25.011 1.00 23.26 ? 140  ALA B CA  1 
ATOM   2130  C  C   . ALA B  1 141 ? 62.989  9.250   26.303 1.00 23.20 ? 140  ALA B C   1 
ATOM   2131  O  O   . ALA B  1 141 ? 63.756  9.998   26.907 1.00 24.69 ? 140  ALA B O   1 
ATOM   2132  C  CB  . ALA B  1 141 ? 63.875  9.626   23.988 1.00 20.15 ? 140  ALA B CB  1 
ATOM   2133  N  N   . GLY B  1 142 ? 61.753  9.009   26.721 1.00 25.91 ? 141  GLY B N   1 
ATOM   2134  C  CA  . GLY B  1 142 ? 61.286  9.610   27.957 1.00 25.74 ? 141  GLY B CA  1 
ATOM   2135  C  C   . GLY B  1 142 ? 60.931  11.082  27.897 1.00 25.45 ? 141  GLY B C   1 
ATOM   2136  O  O   . GLY B  1 142 ? 60.710  11.645  26.825 1.00 26.08 ? 141  GLY B O   1 
ATOM   2137  N  N   . SER B  1 143 ? 60.884  11.709  29.069 1.00 25.66 ? 142  SER B N   1 
ATOM   2138  C  CA  . SER B  1 143 ? 60.517  13.112  29.182 1.00 23.26 ? 142  SER B CA  1 
ATOM   2139  C  C   . SER B  1 143 ? 61.471  14.092  28.509 1.00 22.39 ? 142  SER B C   1 
ATOM   2140  O  O   . SER B  1 143 ? 62.613  13.768  28.183 1.00 20.73 ? 142  SER B O   1 
ATOM   2141  C  CB  . SER B  1 143 ? 60.353  13.493  30.658 1.00 26.58 ? 142  SER B CB  1 
ATOM   2142  O  OG  . SER B  1 143 ? 61.594  13.423  31.335 1.00 30.03 ? 142  SER B OG  1 
ATOM   2143  N  N   . ARG B  1 144 ? 60.969  15.302  28.306 1.00 22.29 ? 143  ARG B N   1 
ATOM   2144  C  CA  . ARG B  1 144 ? 61.717  16.374  27.676 1.00 24.50 ? 143  ARG B CA  1 
ATOM   2145  C  C   . ARG B  1 144 ? 62.355  17.197  28.795 1.00 26.41 ? 143  ARG B C   1 
ATOM   2146  O  O   . ARG B  1 144 ? 61.659  17.901  29.529 1.00 25.96 ? 143  ARG B O   1 
ATOM   2147  C  CB  . ARG B  1 144 ? 60.743  17.208  26.839 1.00 23.51 ? 143  ARG B CB  1 
ATOM   2148  C  CG  . ARG B  1 144 ? 59.842  16.309  25.967 1.00 22.19 ? 143  ARG B CG  1 
ATOM   2149  C  CD  . ARG B  1 144 ? 58.854  17.073  25.095 1.00 24.28 ? 143  ARG B CD  1 
ATOM   2150  N  NE  . ARG B  1 144 ? 58.077  16.145  24.274 1.00 23.91 ? 143  ARG B NE  1 
ATOM   2151  C  CZ  . ARG B  1 144 ? 57.175  16.501  23.364 1.00 26.25 ? 143  ARG B CZ  1 
ATOM   2152  N  NH1 . ARG B  1 144 ? 56.529  15.562  22.681 1.00 26.73 ? 143  ARG B NH1 1 
ATOM   2153  N  NH2 . ARG B  1 144 ? 56.918  17.785  23.129 1.00 21.76 ? 143  ARG B NH2 1 
ATOM   2154  N  N   . LEU B  1 145 ? 63.676  17.093  28.932 1.00 25.93 ? 144  LEU B N   1 
ATOM   2155  C  CA  . LEU B  1 145 ? 64.393  17.807  29.989 1.00 25.27 ? 144  LEU B CA  1 
ATOM   2156  C  C   . LEU B  1 145 ? 64.652  19.275  29.689 1.00 25.10 ? 144  LEU B C   1 
ATOM   2157  O  O   . LEU B  1 145 ? 64.652  20.113  30.592 1.00 24.94 ? 144  LEU B O   1 
ATOM   2158  C  CB  . LEU B  1 145 ? 65.716  17.099  30.290 1.00 25.35 ? 144  LEU B CB  1 
ATOM   2159  C  CG  . LEU B  1 145 ? 65.584  15.639  30.733 1.00 27.51 ? 144  LEU B CG  1 
ATOM   2160  C  CD1 . LEU B  1 145 ? 66.956  15.054  30.981 1.00 29.23 ? 144  LEU B CD1 1 
ATOM   2161  C  CD2 . LEU B  1 145 ? 64.728  15.550  31.990 1.00 30.80 ? 144  LEU B CD2 1 
ATOM   2162  N  N   . ALA B  1 146 ? 64.883  19.593  28.422 1.00 22.99 ? 145  ALA B N   1 
ATOM   2163  C  CA  . ALA B  1 146 ? 65.139  20.971  28.035 1.00 20.63 ? 145  ALA B CA  1 
ATOM   2164  C  C   . ALA B  1 146 ? 64.849  21.129  26.552 1.00 20.65 ? 145  ALA B C   1 
ATOM   2165  O  O   . ALA B  1 146 ? 64.970  20.176  25.780 1.00 21.57 ? 145  ALA B O   1 
ATOM   2166  C  CB  . ALA B  1 146 ? 66.590  21.348  28.343 1.00 20.30 ? 145  ALA B CB  1 
ATOM   2167  N  N   . CYS B  1 147 ? 64.462  22.333  26.156 1.00 20.33 ? 146  CYS B N   1 
ATOM   2168  C  CA  . CYS B  1 147 ? 64.138  22.597  24.766 1.00 21.35 ? 146  CYS B CA  1 
ATOM   2169  C  C   . CYS B  1 147 ? 64.301  24.075  24.465 1.00 22.36 ? 146  CYS B C   1 
ATOM   2170  O  O   . CYS B  1 147 ? 64.460  24.893  25.369 1.00 22.94 ? 146  CYS B O   1 
ATOM   2171  C  CB  . CYS B  1 147 ? 62.691  22.175  24.489 1.00 24.26 ? 146  CYS B CB  1 
ATOM   2172  S  SG  . CYS B  1 147 ? 61.508  22.985  25.612 1.00 27.58 ? 146  CYS B SG  1 
ATOM   2173  N  N   . GLY B  1 148 ? 64.261  24.409  23.182 1.00 23.03 ? 147  GLY B N   1 
ATOM   2174  C  CA  . GLY B  1 148 ? 64.396  25.789  22.766 1.00 21.86 ? 147  GLY B CA  1 
ATOM   2175  C  C   . GLY B  1 148 ? 63.981  25.919  21.318 1.00 22.76 ? 147  GLY B C   1 
ATOM   2176  O  O   . GLY B  1 148 ? 64.139  24.975  20.526 1.00 20.63 ? 147  GLY B O   1 
ATOM   2177  N  N   . VAL B  1 149 ? 63.426  27.073  20.969 1.00 21.85 ? 148  VAL B N   1 
ATOM   2178  C  CA  . VAL B  1 149 ? 63.008  27.322  19.599 1.00 21.73 ? 148  VAL B CA  1 
ATOM   2179  C  C   . VAL B  1 149 ? 64.239  27.601  18.737 1.00 23.89 ? 148  VAL B C   1 
ATOM   2180  O  O   . VAL B  1 149 ? 65.124  28.370  19.124 1.00 23.14 ? 148  VAL B O   1 
ATOM   2181  C  CB  . VAL B  1 149 ? 62.053  28.524  19.521 1.00 23.69 ? 148  VAL B CB  1 
ATOM   2182  C  CG1 . VAL B  1 149 ? 61.642  28.780  18.077 1.00 19.62 ? 148  VAL B CG1 1 
ATOM   2183  C  CG2 . VAL B  1 149 ? 60.828  28.257  20.377 1.00 25.08 ? 148  VAL B CG2 1 
ATOM   2184  N  N   . ILE B  1 150 ? 64.291  26.968  17.570 1.00 22.47 ? 149  ILE B N   1 
ATOM   2185  C  CA  . ILE B  1 150 ? 65.410  27.135  16.656 1.00 22.67 ? 149  ILE B CA  1 
ATOM   2186  C  C   . ILE B  1 150 ? 65.266  28.441  15.882 1.00 23.31 ? 149  ILE B C   1 
ATOM   2187  O  O   . ILE B  1 150 ? 64.340  28.610  15.083 1.00 23.47 ? 149  ILE B O   1 
ATOM   2188  C  CB  . ILE B  1 150 ? 65.485  25.946  15.684 1.00 22.30 ? 149  ILE B CB  1 
ATOM   2189  C  CG1 . ILE B  1 150 ? 65.632  24.649  16.495 1.00 21.15 ? 149  ILE B CG1 1 
ATOM   2190  C  CG2 . ILE B  1 150 ? 66.657  26.131  14.724 1.00 20.70 ? 149  ILE B CG2 1 
ATOM   2191  C  CD1 . ILE B  1 150 ? 65.379  23.364  15.716 1.00 21.95 ? 149  ILE B CD1 1 
ATOM   2192  N  N   . GLY B  1 151 ? 66.191  29.365  16.121 1.00 21.70 ? 150  GLY B N   1 
ATOM   2193  C  CA  . GLY B  1 151 ? 66.119  30.653  15.458 1.00 20.57 ? 150  GLY B CA  1 
ATOM   2194  C  C   . GLY B  1 151 ? 67.238  30.961  14.488 1.00 20.73 ? 150  GLY B C   1 
ATOM   2195  O  O   . GLY B  1 151 ? 68.312  30.361  14.532 1.00 21.12 ? 150  GLY B O   1 
ATOM   2196  N  N   . ILE B  1 152 ? 66.970  31.910  13.601 1.00 20.83 ? 151  ILE B N   1 
ATOM   2197  C  CA  . ILE B  1 152 ? 67.937  32.334  12.605 1.00 21.74 ? 151  ILE B CA  1 
ATOM   2198  C  C   . ILE B  1 152 ? 69.087  33.054  13.300 1.00 23.50 ? 151  ILE B C   1 
ATOM   2199  O  O   . ILE B  1 152 ? 68.862  33.913  14.155 1.00 23.80 ? 151  ILE B O   1 
ATOM   2200  C  CB  . ILE B  1 152 ? 67.281  33.286  11.587 1.00 23.55 ? 151  ILE B CB  1 
ATOM   2201  C  CG1 . ILE B  1 152 ? 66.126  32.563  10.883 1.00 24.28 ? 151  ILE B CG1 1 
ATOM   2202  C  CG2 . ILE B  1 152 ? 68.317  33.774  10.588 1.00 22.79 ? 151  ILE B CG2 1 
ATOM   2203  C  CD1 . ILE B  1 152 ? 65.305  33.452  9.968  1.00 25.59 ? 151  ILE B CD1 1 
ATOM   2204  N  N   . ALA B  1 153 ? 70.316  32.704  12.930 1.00 22.32 ? 152  ALA B N   1 
ATOM   2205  C  CA  . ALA B  1 153 ? 71.494  33.318  13.530 1.00 24.60 ? 152  ALA B CA  1 
ATOM   2206  C  C   . ALA B  1 153 ? 72.461  33.813  12.466 1.00 27.17 ? 152  ALA B C   1 
ATOM   2207  O  O   . ALA B  1 153 ? 72.234  33.616  11.274 1.00 25.08 ? 152  ALA B O   1 
ATOM   2208  C  CB  . ALA B  1 153 ? 72.199  32.314  14.448 1.00 26.96 ? 152  ALA B CB  1 
ATOM   2209  N  N   . GLN B  1 154 ? 73.547  34.445  12.911 1.00 29.17 ? 153  GLN B N   1 
ATOM   2210  C  CA  . GLN B  1 154 ? 74.571  34.970  12.009 1.00 33.90 ? 153  GLN B CA  1 
ATOM   2211  C  C   . GLN B  1 154 ? 75.966  34.491  12.429 1.00 36.05 ? 153  GLN B C   1 
ATOM   2212  O  O   . GLN B  1 154 ? 76.090  33.912  13.531 1.00 36.79 ? 153  GLN B O   1 
ATOM   2213  C  CB  . GLN B  1 154 ? 74.544  36.498  12.020 1.00 35.22 ? 153  GLN B CB  1 
ATOM   2214  C  CG  . GLN B  1 154 ? 74.923  37.101  13.366 1.00 36.97 ? 153  GLN B CG  1 
ATOM   2215  C  CD  . GLN B  1 154 ? 75.134  38.603  13.294 1.00 38.41 ? 153  GLN B CD  1 
ATOM   2216  O  OE1 . GLN B  1 154 ? 75.784  39.100  12.376 1.00 38.68 ? 153  GLN B OE1 1 
ATOM   2217  N  NE2 . GLN B  1 154 ? 74.598  39.330  14.273 1.00 36.64 ? 153  GLN B NE2 1 
ATOM   2218  O  OXT . GLN B  1 154 ? 76.926  34.712  11.657 1.00 37.29 ? 153  GLN B OXT 1 
ATOM   2219  N  N   . ALA C  1 2   ? 107.528 1.426   8.450  0.00 48.22 ? 1    ALA C N   1 
ATOM   2220  C  CA  . ALA C  1 2   ? 107.631 2.742   7.759  0.00 48.21 ? 1    ALA C CA  1 
ATOM   2221  C  C   . ALA C  1 2   ? 109.062 3.266   7.822  1.00 47.71 ? 1    ALA C C   1 
ATOM   2222  O  O   . ALA C  1 2   ? 109.997 2.595   7.392  1.00 49.01 ? 1    ALA C O   1 
ATOM   2223  C  CB  . ALA C  1 2   ? 106.676 3.740   8.403  0.00 48.25 ? 1    ALA C CB  1 
ATOM   2224  N  N   . THR C  1 3   ? 109.229 4.471   8.354  1.00 47.71 ? 2    THR C N   1 
ATOM   2225  C  CA  . THR C  1 3   ? 110.551 5.069   8.475  1.00 46.16 ? 2    THR C CA  1 
ATOM   2226  C  C   . THR C  1 3   ? 111.102 4.929   9.893  1.00 43.79 ? 2    THR C C   1 
ATOM   2227  O  O   . THR C  1 3   ? 112.316 4.858   10.081 1.00 42.21 ? 2    THR C O   1 
ATOM   2228  C  CB  . THR C  1 3   ? 110.532 6.562   8.078  1.00 48.08 ? 2    THR C CB  1 
ATOM   2229  O  OG1 . THR C  1 3   ? 109.315 7.166   8.531  1.00 50.55 ? 2    THR C OG1 1 
ATOM   2230  C  CG2 . THR C  1 3   ? 110.638 6.714   6.573  1.00 50.04 ? 2    THR C CG2 1 
ATOM   2231  N  N   . LYS C  1 4   ? 110.214 4.887   10.884 1.00 40.40 ? 3    LYS C N   1 
ATOM   2232  C  CA  . LYS C  1 4   ? 110.631 4.740   12.278 1.00 37.30 ? 3    LYS C CA  1 
ATOM   2233  C  C   . LYS C  1 4   ? 109.937 3.573   12.972 1.00 35.94 ? 3    LYS C C   1 
ATOM   2234  O  O   . LYS C  1 4   ? 108.761 3.298   12.729 1.00 33.40 ? 3    LYS C O   1 
ATOM   2235  C  CB  . LYS C  1 4   ? 110.357 6.023   13.067 1.00 39.71 ? 3    LYS C CB  1 
ATOM   2236  C  CG  . LYS C  1 4   ? 111.243 7.199   12.681 1.00 41.38 ? 3    LYS C CG  1 
ATOM   2237  C  CD  . LYS C  1 4   ? 110.947 8.414   13.540 1.00 42.85 ? 3    LYS C CD  1 
ATOM   2238  C  CE  . LYS C  1 4   ? 111.841 9.585   13.160 1.00 47.04 ? 3    LYS C CE  1 
ATOM   2239  N  NZ  . LYS C  1 4   ? 111.668 10.747  14.077 1.00 47.89 ? 3    LYS C NZ  1 
ATOM   2240  N  N   . ALA C  1 5   ? 110.677 2.895   13.842 1.00 33.62 ? 4    ALA C N   1 
ATOM   2241  C  CA  . ALA C  1 5   ? 110.148 1.760   14.589 1.00 31.83 ? 4    ALA C CA  1 
ATOM   2242  C  C   . ALA C  1 5   ? 110.697 1.774   16.013 1.00 31.42 ? 4    ALA C C   1 
ATOM   2243  O  O   . ALA C  1 5   ? 111.584 2.568   16.342 1.00 30.33 ? 4    ALA C O   1 
ATOM   2244  C  CB  . ALA C  1 5   ? 110.523 0.461   13.899 1.00 29.48 ? 4    ALA C CB  1 
ATOM   2245  N  N   . VAL C  1 6   ? 110.157 0.904   16.858 1.00 31.18 ? 5    VAL C N   1 
ATOM   2246  C  CA  . VAL C  1 6   ? 110.597 0.813   18.244 1.00 30.59 ? 5    VAL C CA  1 
ATOM   2247  C  C   . VAL C  1 6   ? 110.318 -0.579  18.788 1.00 31.92 ? 5    VAL C C   1 
ATOM   2248  O  O   . VAL C  1 6   ? 109.379 -1.252  18.358 1.00 30.82 ? 5    VAL C O   1 
ATOM   2249  C  CB  . VAL C  1 6   ? 109.880 1.862   19.141 1.00 32.09 ? 5    VAL C CB  1 
ATOM   2250  C  CG1 . VAL C  1 6   ? 108.369 1.611   19.149 1.00 31.50 ? 5    VAL C CG1 1 
ATOM   2251  C  CG2 . VAL C  1 6   ? 110.435 1.800   20.561 1.00 29.41 ? 5    VAL C CG2 1 
ATOM   2252  N  N   . ALA C  1 7   ? 111.158 -1.018  19.717 1.00 31.46 ? 6    ALA C N   1 
ATOM   2253  C  CA  . ALA C  1 7   ? 110.988 -2.320  20.339 1.00 31.52 ? 6    ALA C CA  1 
ATOM   2254  C  C   . ALA C  1 7   ? 111.250 -2.179  21.836 1.00 32.42 ? 6    ALA C C   1 
ATOM   2255  O  O   . ALA C  1 7   ? 112.310 -1.694  22.245 1.00 31.90 ? 6    ALA C O   1 
ATOM   2256  C  CB  . ALA C  1 7   ? 111.945 -3.331  19.727 1.00 29.13 ? 6    ALA C CB  1 
ATOM   2257  N  N   . VAL C  1 8   ? 110.272 -2.579  22.643 1.00 31.14 ? 7    VAL C N   1 
ATOM   2258  C  CA  . VAL C  1 8   ? 110.395 -2.517  24.097 1.00 30.12 ? 7    VAL C CA  1 
ATOM   2259  C  C   . VAL C  1 8   ? 110.749 -3.917  24.566 1.00 30.29 ? 7    VAL C C   1 
ATOM   2260  O  O   . VAL C  1 8   ? 109.927 -4.828  24.501 1.00 30.88 ? 7    VAL C O   1 
ATOM   2261  C  CB  . VAL C  1 8   ? 109.073 -2.050  24.744 1.00 30.85 ? 7    VAL C CB  1 
ATOM   2262  C  CG1 . VAL C  1 8   ? 109.189 -2.064  26.270 1.00 31.14 ? 7    VAL C CG1 1 
ATOM   2263  C  CG2 . VAL C  1 8   ? 108.744 -0.648  24.253 1.00 29.80 ? 7    VAL C CG2 1 
ATOM   2264  N  N   . LEU C  1 9   ? 111.988 -4.088  25.015 1.00 30.46 ? 8    LEU C N   1 
ATOM   2265  C  CA  . LEU C  1 9   ? 112.475 -5.385  25.466 1.00 30.36 ? 8    LEU C CA  1 
ATOM   2266  C  C   . LEU C  1 9   ? 112.045 -5.736  26.889 1.00 30.92 ? 8    LEU C C   1 
ATOM   2267  O  O   . LEU C  1 9   ? 112.211 -4.944  27.812 1.00 32.01 ? 8    LEU C O   1 
ATOM   2268  C  CB  . LEU C  1 9   ? 114.003 -5.424  25.372 1.00 31.53 ? 8    LEU C CB  1 
ATOM   2269  C  CG  . LEU C  1 9   ? 114.597 -5.054  24.006 1.00 34.20 ? 8    LEU C CG  1 
ATOM   2270  C  CD1 . LEU C  1 9   ? 116.120 -5.039  24.088 1.00 34.70 ? 8    LEU C CD1 1 
ATOM   2271  C  CD2 . LEU C  1 9   ? 114.130 -6.049  22.956 1.00 33.15 ? 8    LEU C CD2 1 
ATOM   2272  N  N   . LYS C  1 10  ? 111.492 -6.933  27.050 1.00 32.17 ? 9    LYS C N   1 
ATOM   2273  C  CA  . LYS C  1 10  ? 111.050 -7.421  28.351 1.00 33.83 ? 9    LYS C CA  1 
ATOM   2274  C  C   . LYS C  1 10  ? 111.213 -8.927  28.386 1.00 34.08 ? 9    LYS C C   1 
ATOM   2275  O  O   . LYS C  1 10  ? 111.182 -9.592  27.349 1.00 32.96 ? 9    LYS C O   1 
ATOM   2276  C  CB  . LYS C  1 10  ? 109.578 -7.067  28.606 1.00 35.65 ? 9    LYS C CB  1 
ATOM   2277  C  CG  . LYS C  1 10  ? 109.294 -5.579  28.693 1.00 37.99 ? 9    LYS C CG  1 
ATOM   2278  C  CD  . LYS C  1 10  ? 107.836 -5.315  29.045 1.00 42.86 ? 9    LYS C CD  1 
ATOM   2279  C  CE  . LYS C  1 10  ? 107.565 -3.825  29.170 1.00 43.05 ? 9    LYS C CE  1 
ATOM   2280  N  NZ  . LYS C  1 10  ? 106.162 -3.557  29.571 1.00 45.51 ? 9    LYS C NZ  1 
ATOM   2281  N  N   . GLY C  1 11  ? 111.390 -9.459  29.590 1.00 34.97 ? 10   GLY C N   1 
ATOM   2282  C  CA  . GLY C  1 11  ? 111.546 -10.890 29.761 1.00 37.17 ? 10   GLY C CA  1 
ATOM   2283  C  C   . GLY C  1 11  ? 111.144 -11.282 31.172 1.00 39.57 ? 10   GLY C C   1 
ATOM   2284  O  O   . GLY C  1 11  ? 110.457 -10.523 31.860 1.00 38.10 ? 10   GLY C O   1 
ATOM   2285  N  N   . ASP C  1 12  ? 111.571 -12.462 31.606 1.00 41.10 ? 11   ASP C N   1 
ATOM   2286  C  CA  . ASP C  1 12  ? 111.244 -12.938 32.942 1.00 43.82 ? 11   ASP C CA  1 
ATOM   2287  C  C   . ASP C  1 12  ? 112.187 -12.335 33.975 1.00 43.50 ? 11   ASP C C   1 
ATOM   2288  O  O   . ASP C  1 12  ? 111.768 -11.988 35.083 1.00 45.26 ? 11   ASP C O   1 
ATOM   2289  C  CB  . ASP C  1 12  ? 111.324 -14.462 32.986 1.00 47.37 ? 11   ASP C CB  1 
ATOM   2290  C  CG  . ASP C  1 12  ? 110.363 -15.119 32.013 1.00 51.08 ? 11   ASP C CG  1 
ATOM   2291  O  OD1 . ASP C  1 12  ? 109.155 -14.801 32.070 1.00 52.91 ? 11   ASP C OD1 1 
ATOM   2292  O  OD2 . ASP C  1 12  ? 110.811 -15.952 31.194 1.00 52.45 ? 11   ASP C OD2 1 
ATOM   2293  N  N   . GLY C  1 13  ? 113.456 -12.208 33.599 1.00 40.63 ? 12   GLY C N   1 
ATOM   2294  C  CA  . GLY C  1 13  ? 114.455 -11.645 34.489 1.00 37.24 ? 12   GLY C CA  1 
ATOM   2295  C  C   . GLY C  1 13  ? 114.424 -10.128 34.578 1.00 35.15 ? 12   GLY C C   1 
ATOM   2296  O  O   . GLY C  1 13  ? 113.405 -9.512  34.285 1.00 34.54 ? 12   GLY C O   1 
ATOM   2297  N  N   . PRO C  1 14  ? 115.544 -9.495  34.969 1.00 34.06 ? 13   PRO C N   1 
ATOM   2298  C  CA  . PRO C  1 14  ? 115.674 -8.043  35.112 1.00 33.19 ? 13   PRO C CA  1 
ATOM   2299  C  C   . PRO C  1 14  ? 116.024 -7.282  33.834 1.00 33.93 ? 13   PRO C C   1 
ATOM   2300  O  O   . PRO C  1 14  ? 116.016 -6.054  33.817 1.00 34.05 ? 13   PRO C O   1 
ATOM   2301  C  CB  . PRO C  1 14  ? 116.775 -7.919  36.148 1.00 34.31 ? 13   PRO C CB  1 
ATOM   2302  C  CG  . PRO C  1 14  ? 117.719 -9.000  35.705 1.00 33.60 ? 13   PRO C CG  1 
ATOM   2303  C  CD  . PRO C  1 14  ? 116.783 -10.170 35.404 1.00 35.01 ? 13   PRO C CD  1 
ATOM   2304  N  N   . VAL C  1 15  ? 116.337 -8.001  32.767 1.00 35.37 ? 14   VAL C N   1 
ATOM   2305  C  CA  . VAL C  1 15  ? 116.713 -7.343  31.518 1.00 38.13 ? 14   VAL C CA  1 
ATOM   2306  C  C   . VAL C  1 15  ? 115.581 -6.594  30.836 1.00 38.91 ? 14   VAL C C   1 
ATOM   2307  O  O   . VAL C  1 15  ? 114.623 -7.201  30.370 1.00 38.95 ? 14   VAL C O   1 
ATOM   2308  C  CB  . VAL C  1 15  ? 117.268 -8.347  30.482 1.00 36.48 ? 14   VAL C CB  1 
ATOM   2309  C  CG1 . VAL C  1 15  ? 117.755 -7.596  29.242 1.00 39.08 ? 14   VAL C CG1 1 
ATOM   2310  C  CG2 . VAL C  1 15  ? 118.409 -9.148  31.080 1.00 38.83 ? 14   VAL C CG2 1 
ATOM   2311  N  N   . GLN C  1 16  ? 115.696 -5.277  30.763 1.00 39.34 ? 15   GLN C N   1 
ATOM   2312  C  CA  . GLN C  1 16  ? 114.671 -4.506  30.088 1.00 41.60 ? 15   GLN C CA  1 
ATOM   2313  C  C   . GLN C  1 16  ? 115.291 -3.322  29.352 1.00 41.68 ? 15   GLN C C   1 
ATOM   2314  O  O   . GLN C  1 16  ? 116.322 -2.775  29.770 1.00 40.34 ? 15   GLN C O   1 
ATOM   2315  C  CB  . GLN C  1 16  ? 113.579 -4.070  31.082 1.00 44.22 ? 15   GLN C CB  1 
ATOM   2316  C  CG  . GLN C  1 16  ? 114.036 -3.287  32.310 1.00 47.21 ? 15   GLN C CG  1 
ATOM   2317  C  CD  . GLN C  1 16  ? 112.911 -3.121  33.336 1.00 49.44 ? 15   GLN C CD  1 
ATOM   2318  O  OE1 . GLN C  1 16  ? 111.785 -2.755  32.987 1.00 50.48 ? 15   GLN C OE1 1 
ATOM   2319  N  NE2 . GLN C  1 16  ? 113.216 -3.387  34.601 1.00 50.33 ? 15   GLN C NE2 1 
ATOM   2320  N  N   . GLY C  1 17  ? 114.692 -2.972  28.216 1.00 41.26 ? 16   GLY C N   1 
ATOM   2321  C  CA  . GLY C  1 17  ? 115.196 -1.854  27.446 1.00 41.34 ? 16   GLY C CA  1 
ATOM   2322  C  C   . GLY C  1 17  ? 114.281 -1.340  26.346 1.00 42.05 ? 16   GLY C C   1 
ATOM   2323  O  O   . GLY C  1 17  ? 113.222 -1.901  26.062 1.00 41.97 ? 16   GLY C O   1 
ATOM   2324  N  N   . ILE C  1 18  ? 114.709 -0.240  25.739 1.00 40.20 ? 17   ILE C N   1 
ATOM   2325  C  CA  . ILE C  1 18  ? 113.971 0.416   24.673 1.00 39.48 ? 17   ILE C CA  1 
ATOM   2326  C  C   . ILE C  1 18  ? 114.918 0.675   23.508 1.00 39.26 ? 17   ILE C C   1 
ATOM   2327  O  O   . ILE C  1 18  ? 115.905 1.394   23.661 1.00 37.99 ? 17   ILE C O   1 
ATOM   2328  C  CB  . ILE C  1 18  ? 113.408 1.760   25.158 1.00 39.52 ? 17   ILE C CB  1 
ATOM   2329  C  CG1 . ILE C  1 18  ? 112.405 1.522   26.287 1.00 39.83 ? 17   ILE C CG1 1 
ATOM   2330  C  CG2 . ILE C  1 18  ? 112.758 2.499   23.996 1.00 39.91 ? 17   ILE C CG2 1 
ATOM   2331  C  CD1 . ILE C  1 18  ? 111.825 2.803   26.859 1.00 40.41 ? 17   ILE C CD1 1 
ATOM   2332  N  N   . ILE C  1 19  ? 114.619 0.089   22.351 1.00 37.55 ? 18   ILE C N   1 
ATOM   2333  C  CA  . ILE C  1 19  ? 115.457 0.263   21.168 1.00 36.23 ? 18   ILE C CA  1 
ATOM   2334  C  C   . ILE C  1 19  ? 114.687 0.906   20.015 1.00 37.44 ? 18   ILE C C   1 
ATOM   2335  O  O   . ILE C  1 19  ? 113.638 0.402   19.593 1.00 34.29 ? 18   ILE C O   1 
ATOM   2336  C  CB  . ILE C  1 19  ? 116.032 -1.084  20.690 1.00 34.55 ? 18   ILE C CB  1 
ATOM   2337  C  CG1 . ILE C  1 19  ? 116.883 -1.713  21.798 1.00 36.07 ? 18   ILE C CG1 1 
ATOM   2338  C  CG2 . ILE C  1 19  ? 116.854 -0.879  19.430 1.00 33.65 ? 18   ILE C CG2 1 
ATOM   2339  C  CD1 . ILE C  1 19  ? 118.065 -0.859  22.246 1.00 36.33 ? 18   ILE C CD1 1 
ATOM   2340  N  N   . ASN C  1 20  ? 115.225 2.018   19.513 1.00 37.07 ? 19   ASN C N   1 
ATOM   2341  C  CA  . ASN C  1 20  ? 114.626 2.769   18.413 1.00 36.61 ? 19   ASN C CA  1 
ATOM   2342  C  C   . ASN C  1 20  ? 115.214 2.377   17.055 1.00 37.59 ? 19   ASN C C   1 
ATOM   2343  O  O   . ASN C  1 20  ? 116.341 1.881   16.968 1.00 36.89 ? 19   ASN C O   1 
ATOM   2344  C  CB  . ASN C  1 20  ? 114.842 4.268   18.628 1.00 38.07 ? 19   ASN C CB  1 
ATOM   2345  C  CG  . ASN C  1 20  ? 114.311 4.755   19.961 1.00 40.69 ? 19   ASN C CG  1 
ATOM   2346  O  OD1 . ASN C  1 20  ? 113.100 4.833   20.174 1.00 39.75 ? 19   ASN C OD1 1 
ATOM   2347  N  ND2 . ASN C  1 20  ? 115.221 5.085   20.873 1.00 42.02 ? 19   ASN C ND2 1 
ATOM   2348  N  N   . PHE C  1 21  ? 114.435 2.610   15.999 1.00 37.23 ? 20   PHE C N   1 
ATOM   2349  C  CA  . PHE C  1 21  ? 114.838 2.315   14.623 1.00 37.74 ? 20   PHE C CA  1 
ATOM   2350  C  C   . PHE C  1 21  ? 114.459 3.513   13.756 1.00 39.01 ? 20   PHE C C   1 
ATOM   2351  O  O   . PHE C  1 21  ? 113.397 4.107   13.943 1.00 37.02 ? 20   PHE C O   1 
ATOM   2352  C  CB  . PHE C  1 21  ? 114.096 1.091   14.078 1.00 37.31 ? 20   PHE C CB  1 
ATOM   2353  C  CG  . PHE C  1 21  ? 114.465 -0.206  14.740 1.00 34.97 ? 20   PHE C CG  1 
ATOM   2354  C  CD1 . PHE C  1 21  ? 115.424 -1.039  14.180 1.00 35.23 ? 20   PHE C CD1 1 
ATOM   2355  C  CD2 . PHE C  1 21  ? 113.824 -0.613  15.907 1.00 35.12 ? 20   PHE C CD2 1 
ATOM   2356  C  CE1 . PHE C  1 21  ? 115.741 -2.265  14.768 1.00 35.91 ? 20   PHE C CE1 1 
ATOM   2357  C  CE2 . PHE C  1 21  ? 114.131 -1.839  16.507 1.00 34.41 ? 20   PHE C CE2 1 
ATOM   2358  C  CZ  . PHE C  1 21  ? 115.092 -2.667  15.936 1.00 34.49 ? 20   PHE C CZ  1 
ATOM   2359  N  N   . GLU C  1 22  ? 115.325 3.870   12.814 1.00 41.40 ? 21   GLU C N   1 
ATOM   2360  C  CA  . GLU C  1 22  ? 115.045 4.982   11.912 1.00 42.56 ? 21   GLU C CA  1 
ATOM   2361  C  C   . GLU C  1 22  ? 115.718 4.746   10.567 1.00 43.77 ? 21   GLU C C   1 
ATOM   2362  O  O   . GLU C  1 22  ? 116.913 4.444   10.498 1.00 42.96 ? 21   GLU C O   1 
ATOM   2363  C  CB  . GLU C  1 22  ? 115.509 6.311   12.513 1.00 45.54 ? 21   GLU C CB  1 
ATOM   2364  C  CG  . GLU C  1 22  ? 115.242 7.504   11.606 1.00 49.27 ? 21   GLU C CG  1 
ATOM   2365  C  CD  . GLU C  1 22  ? 115.310 8.833   12.336 1.00 53.60 ? 21   GLU C CD  1 
ATOM   2366  O  OE1 . GLU C  1 22  ? 115.250 9.883   11.660 1.00 54.18 ? 21   GLU C OE1 1 
ATOM   2367  O  OE2 . GLU C  1 22  ? 115.413 8.830   13.582 1.00 55.79 ? 21   GLU C OE2 1 
ATOM   2368  N  N   . GLN C  1 23  ? 114.932 4.873   9.501  1.00 43.16 ? 22   GLN C N   1 
ATOM   2369  C  CA  . GLN C  1 23  ? 115.419 4.657   8.145  1.00 43.66 ? 22   GLN C CA  1 
ATOM   2370  C  C   . GLN C  1 23  ? 114.950 5.779   7.219  1.00 44.71 ? 22   GLN C C   1 
ATOM   2371  O  O   . GLN C  1 23  ? 113.798 5.804   6.786  1.00 44.36 ? 22   GLN C O   1 
ATOM   2372  C  CB  . GLN C  1 23  ? 114.927 3.300   7.644  1.00 41.45 ? 22   GLN C CB  1 
ATOM   2373  C  CG  . GLN C  1 23  ? 115.182 3.028   6.180  1.00 40.22 ? 22   GLN C CG  1 
ATOM   2374  C  CD  . GLN C  1 23  ? 114.841 1.606   5.796  1.00 37.94 ? 22   GLN C CD  1 
ATOM   2375  O  OE1 . GLN C  1 23  ? 113.864 1.034   6.285  1.00 37.80 ? 22   GLN C OE1 1 
ATOM   2376  N  NE2 . GLN C  1 23  ? 115.637 1.028   4.908  1.00 38.03 ? 22   GLN C NE2 1 
ATOM   2377  N  N   . LYS C  1 24  ? 115.862 6.702   6.923  1.00 44.59 ? 23   LYS C N   1 
ATOM   2378  C  CA  . LYS C  1 24  ? 115.575 7.856   6.076  1.00 44.35 ? 23   LYS C CA  1 
ATOM   2379  C  C   . LYS C  1 24  ? 115.056 7.528   4.679  1.00 43.24 ? 23   LYS C C   1 
ATOM   2380  O  O   . LYS C  1 24  ? 114.135 8.177   4.193  1.00 43.43 ? 23   LYS C O   1 
ATOM   2381  C  CB  . LYS C  1 24  ? 116.821 8.740   5.964  1.00 43.52 ? 23   LYS C CB  1 
ATOM   2382  C  CG  . LYS C  1 24  ? 117.241 9.367   7.283  1.00 45.73 ? 23   LYS C CG  1 
ATOM   2383  C  CD  . LYS C  1 24  ? 118.465 10.252  7.116  0.00 45.84 ? 23   LYS C CD  1 
ATOM   2384  C  CE  . LYS C  1 24  ? 118.871 10.883  8.438  0.00 46.34 ? 23   LYS C CE  1 
ATOM   2385  N  NZ  . LYS C  1 24  ? 120.067 11.759  8.294  0.00 46.58 ? 23   LYS C NZ  1 
ATOM   2386  N  N   . GLU C  1 25  ? 115.645 6.532   4.032  1.00 43.79 ? 24   GLU C N   1 
ATOM   2387  C  CA  . GLU C  1 25  ? 115.216 6.157   2.691  1.00 44.78 ? 24   GLU C CA  1 
ATOM   2388  C  C   . GLU C  1 25  ? 114.966 4.661   2.620  1.00 44.05 ? 24   GLU C C   1 
ATOM   2389  O  O   . GLU C  1 25  ? 115.718 3.875   3.196  1.00 43.93 ? 24   GLU C O   1 
ATOM   2390  C  CB  . GLU C  1 25  ? 116.275 6.569   1.664  1.00 46.97 ? 24   GLU C CB  1 
ATOM   2391  C  CG  . GLU C  1 25  ? 116.603 8.061   1.686  1.00 50.02 ? 24   GLU C CG  1 
ATOM   2392  C  CD  . GLU C  1 25  ? 115.388 8.945   1.429  1.00 52.52 ? 24   GLU C CD  1 
ATOM   2393  O  OE1 . GLU C  1 25  ? 115.515 10.181  1.550  1.00 52.92 ? 24   GLU C OE1 1 
ATOM   2394  O  OE2 . GLU C  1 25  ? 114.307 8.409   1.106  1.00 55.70 ? 24   GLU C OE2 1 
ATOM   2395  N  N   . SER C  1 26  ? 113.908 4.276   1.911  1.00 41.83 ? 25   SER C N   1 
ATOM   2396  C  CA  . SER C  1 26  ? 113.536 2.874   1.785  1.00 40.93 ? 25   SER C CA  1 
ATOM   2397  C  C   . SER C  1 26  ? 114.646 2.000   1.229  1.00 41.07 ? 25   SER C C   1 
ATOM   2398  O  O   . SER C  1 26  ? 114.656 0.793   1.463  1.00 41.84 ? 25   SER C O   1 
ATOM   2399  C  CB  . SER C  1 26  ? 112.278 2.725   0.921  1.00 41.53 ? 25   SER C CB  1 
ATOM   2400  O  OG  . SER C  1 26  ? 112.534 3.031   -0.438 1.00 40.02 ? 25   SER C OG  1 
ATOM   2401  N  N   . ASN C  1 27  ? 115.575 2.590   0.482  1.00 40.75 ? 26   ASN C N   1 
ATOM   2402  C  CA  . ASN C  1 27  ? 116.678 1.803   -0.061 1.00 41.94 ? 26   ASN C CA  1 
ATOM   2403  C  C   . ASN C  1 27  ? 117.988 2.196   0.626  1.00 42.68 ? 26   ASN C C   1 
ATOM   2404  O  O   . ASN C  1 27  ? 119.078 1.901   0.136  1.00 43.99 ? 26   ASN C O   1 
ATOM   2405  C  CB  . ASN C  1 27  ? 116.768 1.967   -1.594 1.00 40.46 ? 26   ASN C CB  1 
ATOM   2406  C  CG  . ASN C  1 27  ? 117.379 3.290   -2.024 1.00 38.82 ? 26   ASN C CG  1 
ATOM   2407  O  OD1 . ASN C  1 27  ? 117.103 4.341   -1.444 1.00 36.79 ? 26   ASN C OD1 1 
ATOM   2408  N  ND2 . ASN C  1 27  ? 118.206 3.242   -3.074 1.00 38.14 ? 26   ASN C ND2 1 
ATOM   2409  N  N   . GLY C  1 28  ? 117.857 2.846   1.782  1.00 43.35 ? 27   GLY C N   1 
ATOM   2410  C  CA  . GLY C  1 28  ? 119.012 3.274   2.556  1.00 44.63 ? 27   GLY C CA  1 
ATOM   2411  C  C   . GLY C  1 28  ? 119.193 2.472   3.840  1.00 45.47 ? 27   GLY C C   1 
ATOM   2412  O  O   . GLY C  1 28  ? 118.442 1.525   4.085  1.00 45.08 ? 27   GLY C O   1 
ATOM   2413  N  N   . PRO C  1 29  ? 120.181 2.824   4.684  1.00 45.24 ? 28   PRO C N   1 
ATOM   2414  C  CA  . PRO C  1 29  ? 120.443 2.117   5.943  1.00 44.15 ? 28   PRO C CA  1 
ATOM   2415  C  C   . PRO C  1 29  ? 119.499 2.473   7.094  1.00 41.74 ? 28   PRO C C   1 
ATOM   2416  O  O   . PRO C  1 29  ? 118.781 3.474   7.050  1.00 40.51 ? 28   PRO C O   1 
ATOM   2417  C  CB  . PRO C  1 29  ? 121.884 2.501   6.251  1.00 45.13 ? 28   PRO C CB  1 
ATOM   2418  C  CG  . PRO C  1 29  ? 121.928 3.921   5.785  1.00 46.13 ? 28   PRO C CG  1 
ATOM   2419  C  CD  . PRO C  1 29  ? 121.216 3.846   4.441  1.00 45.30 ? 28   PRO C CD  1 
ATOM   2420  N  N   . VAL C  1 30  ? 119.534 1.647   8.134  1.00 40.52 ? 29   VAL C N   1 
ATOM   2421  C  CA  . VAL C  1 30  ? 118.698 1.834   9.313  1.00 38.09 ? 29   VAL C CA  1 
ATOM   2422  C  C   . VAL C  1 30  ? 119.536 2.090   10.567 1.00 37.57 ? 29   VAL C C   1 
ATOM   2423  O  O   . VAL C  1 30  ? 120.442 1.322   10.883 1.00 37.25 ? 29   VAL C O   1 
ATOM   2424  C  CB  . VAL C  1 30  ? 117.824 0.582   9.549  1.00 37.75 ? 29   VAL C CB  1 
ATOM   2425  C  CG1 . VAL C  1 30  ? 116.962 0.762   10.789 1.00 36.55 ? 29   VAL C CG1 1 
ATOM   2426  C  CG2 . VAL C  1 30  ? 116.960 0.322   8.333  1.00 36.05 ? 29   VAL C CG2 1 
ATOM   2427  N  N   . LYS C  1 31  ? 119.242 3.178   11.269 1.00 37.62 ? 30   LYS C N   1 
ATOM   2428  C  CA  . LYS C  1 31  ? 119.956 3.500   12.498 1.00 38.68 ? 30   LYS C CA  1 
ATOM   2429  C  C   . LYS C  1 31  ? 119.245 2.782   13.645 1.00 39.28 ? 30   LYS C C   1 
ATOM   2430  O  O   . LYS C  1 31  ? 118.014 2.772   13.708 1.00 37.65 ? 30   LYS C O   1 
ATOM   2431  C  CB  . LYS C  1 31  ? 119.953 5.013   12.744 1.00 40.90 ? 30   LYS C CB  1 
ATOM   2432  C  CG  . LYS C  1 31  ? 120.782 5.802   11.744 1.00 44.03 ? 30   LYS C CG  1 
ATOM   2433  C  CD  . LYS C  1 31  ? 120.626 7.301   11.935 0.00 46.79 ? 30   LYS C CD  1 
ATOM   2434  C  CE  . LYS C  1 31  ? 121.415 8.068   10.886 1.00 49.60 ? 30   LYS C CE  1 
ATOM   2435  N  NZ  . LYS C  1 31  ? 121.149 9.533   10.939 1.00 51.92 ? 30   LYS C NZ  1 
ATOM   2436  N  N   . VAL C  1 32  ? 120.024 2.181   14.542 1.00 39.02 ? 31   VAL C N   1 
ATOM   2437  C  CA  . VAL C  1 32  ? 119.482 1.442   15.683 1.00 38.76 ? 31   VAL C CA  1 
ATOM   2438  C  C   . VAL C  1 32  ? 120.122 1.925   16.979 1.00 40.75 ? 31   VAL C C   1 
ATOM   2439  O  O   . VAL C  1 32  ? 121.324 1.754   17.181 1.00 41.37 ? 31   VAL C O   1 
ATOM   2440  C  CB  . VAL C  1 32  ? 119.765 -0.063  15.544 1.00 37.57 ? 31   VAL C CB  1 
ATOM   2441  C  CG1 . VAL C  1 32  ? 119.084 -0.825  16.666 1.00 36.47 ? 31   VAL C CG1 1 
ATOM   2442  C  CG2 . VAL C  1 32  ? 119.294 -0.559  14.193 1.00 36.60 ? 31   VAL C CG2 1 
ATOM   2443  N  N   . TRP C  1 33  ? 119.329 2.518   17.865 1.00 40.26 ? 32   TRP C N   1 
ATOM   2444  C  CA  . TRP C  1 33  ? 119.883 3.013   19.116 1.00 41.52 ? 32   TRP C CA  1 
ATOM   2445  C  C   . TRP C  1 33  ? 118.911 2.948   20.282 1.00 42.76 ? 32   TRP C C   1 
ATOM   2446  O  O   . TRP C  1 33  ? 117.693 2.868   20.099 1.00 42.09 ? 32   TRP C O   1 
ATOM   2447  C  CB  . TRP C  1 33  ? 120.363 4.457   18.943 1.00 40.37 ? 32   TRP C CB  1 
ATOM   2448  C  CG  . TRP C  1 33  ? 119.259 5.462   18.922 1.00 40.65 ? 32   TRP C CG  1 
ATOM   2449  C  CD1 . TRP C  1 33  ? 118.885 6.292   19.941 1.00 41.41 ? 32   TRP C CD1 1 
ATOM   2450  C  CD2 . TRP C  1 33  ? 118.369 5.734   17.836 1.00 40.80 ? 32   TRP C CD2 1 
ATOM   2451  N  NE1 . TRP C  1 33  ? 117.817 7.066   19.555 1.00 42.84 ? 32   TRP C NE1 1 
ATOM   2452  C  CE2 . TRP C  1 33  ? 117.479 6.742   18.264 1.00 41.78 ? 32   TRP C CE2 1 
ATOM   2453  C  CE3 . TRP C  1 33  ? 118.237 5.222   16.538 1.00 40.72 ? 32   TRP C CE3 1 
ATOM   2454  C  CZ2 . TRP C  1 33  ? 116.467 7.252   17.443 1.00 42.37 ? 32   TRP C CZ2 1 
ATOM   2455  C  CZ3 . TRP C  1 33  ? 117.230 5.727   15.719 1.00 42.79 ? 32   TRP C CZ3 1 
ATOM   2456  C  CH2 . TRP C  1 33  ? 116.360 6.734   16.177 1.00 42.57 ? 32   TRP C CH2 1 
ATOM   2457  N  N   . GLY C  1 34  ? 119.471 3.002   21.485 1.00 42.42 ? 33   GLY C N   1 
ATOM   2458  C  CA  . GLY C  1 34  ? 118.668 2.957   22.691 1.00 44.39 ? 33   GLY C CA  1 
ATOM   2459  C  C   . GLY C  1 34  ? 119.511 2.490   23.857 1.00 44.66 ? 33   GLY C C   1 
ATOM   2460  O  O   . GLY C  1 34  ? 120.731 2.650   23.850 1.00 45.03 ? 33   GLY C O   1 
ATOM   2461  N  N   . SER C  1 35  ? 118.863 1.906   24.857 1.00 44.99 ? 34   SER C N   1 
ATOM   2462  C  CA  . SER C  1 35  ? 119.563 1.412   26.033 1.00 45.07 ? 34   SER C CA  1 
ATOM   2463  C  C   . SER C  1 35  ? 118.933 0.131   26.555 1.00 44.59 ? 34   SER C C   1 
ATOM   2464  O  O   . SER C  1 35  ? 117.742 -0.115  26.353 1.00 45.01 ? 34   SER C O   1 
ATOM   2465  C  CB  . SER C  1 35  ? 119.548 2.468   27.136 1.00 46.10 ? 34   SER C CB  1 
ATOM   2466  O  OG  . SER C  1 35  ? 120.133 1.963   28.323 1.00 50.63 ? 34   SER C OG  1 
ATOM   2467  N  N   . ILE C  1 36  ? 119.744 -0.686  27.219 1.00 43.51 ? 35   ILE C N   1 
ATOM   2468  C  CA  . ILE C  1 36  ? 119.287 -1.945  27.801 1.00 42.65 ? 35   ILE C CA  1 
ATOM   2469  C  C   . ILE C  1 36  ? 119.979 -2.132  29.151 1.00 43.97 ? 35   ILE C C   1 
ATOM   2470  O  O   . ILE C  1 36  ? 121.206 -2.059  29.236 1.00 43.97 ? 35   ILE C O   1 
ATOM   2471  C  CB  . ILE C  1 36  ? 119.652 -3.150  26.920 1.00 40.33 ? 35   ILE C CB  1 
ATOM   2472  C  CG1 . ILE C  1 36  ? 119.145 -2.939  25.494 1.00 40.90 ? 35   ILE C CG1 1 
ATOM   2473  C  CG2 . ILE C  1 36  ? 119.054 -4.419  27.513 1.00 41.28 ? 35   ILE C CG2 1 
ATOM   2474  C  CD1 . ILE C  1 36  ? 119.447 -4.101  24.569 1.00 37.08 ? 35   ILE C CD1 1 
ATOM   2475  N  N   . LYS C  1 37  ? 119.199 -2.369  30.203 1.00 43.43 ? 36   LYS C N   1 
ATOM   2476  C  CA  . LYS C  1 37  ? 119.773 -2.569  31.528 1.00 44.13 ? 36   LYS C CA  1 
ATOM   2477  C  C   . LYS C  1 37  ? 119.475 -3.952  32.104 1.00 43.36 ? 36   LYS C C   1 
ATOM   2478  O  O   . LYS C  1 37  ? 118.727 -4.737  31.513 1.00 43.43 ? 36   LYS C O   1 
ATOM   2479  C  CB  . LYS C  1 37  ? 119.297 -1.470  32.488 1.00 45.97 ? 36   LYS C CB  1 
ATOM   2480  C  CG  . LYS C  1 37  ? 117.809 -1.150  32.426 1.00 49.71 ? 36   LYS C CG  1 
ATOM   2481  C  CD  . LYS C  1 37  ? 117.497 0.110   33.226 0.00 51.13 ? 36   LYS C CD  1 
ATOM   2482  C  CE  . LYS C  1 37  ? 116.041 0.527   33.079 1.00 53.46 ? 36   LYS C CE  1 
ATOM   2483  N  NZ  . LYS C  1 37  ? 115.723 1.764   33.858 1.00 54.02 ? 36   LYS C NZ  1 
ATOM   2484  N  N   . GLY C  1 38  ? 120.087 -4.252  33.248 1.00 40.46 ? 37   GLY C N   1 
ATOM   2485  C  CA  . GLY C  1 38  ? 119.883 -5.536  33.892 1.00 37.28 ? 37   GLY C CA  1 
ATOM   2486  C  C   . GLY C  1 38  ? 120.699 -6.650  33.276 1.00 36.71 ? 37   GLY C C   1 
ATOM   2487  O  O   . GLY C  1 38  ? 120.443 -7.828  33.529 1.00 34.69 ? 37   GLY C O   1 
ATOM   2488  N  N   . LEU C  1 39  ? 121.691 -6.280  32.469 1.00 36.44 ? 38   LEU C N   1 
ATOM   2489  C  CA  . LEU C  1 39  ? 122.546 -7.255  31.802 1.00 36.82 ? 38   LEU C CA  1 
ATOM   2490  C  C   . LEU C  1 39  ? 123.844 -7.500  32.565 1.00 38.59 ? 38   LEU C C   1 
ATOM   2491  O  O   . LEU C  1 39  ? 124.342 -6.618  33.263 1.00 37.44 ? 38   LEU C O   1 
ATOM   2492  C  CB  . LEU C  1 39  ? 122.900 -6.766  30.392 1.00 37.94 ? 38   LEU C CB  1 
ATOM   2493  C  CG  . LEU C  1 39  ? 121.783 -6.622  29.354 1.00 36.97 ? 38   LEU C CG  1 
ATOM   2494  C  CD1 . LEU C  1 39  ? 122.282 -5.804  28.165 1.00 36.41 ? 38   LEU C CD1 1 
ATOM   2495  C  CD2 . LEU C  1 39  ? 121.329 -7.998  28.909 1.00 35.84 ? 38   LEU C CD2 1 
ATOM   2496  N  N   . THR C  1 40  ? 124.386 -8.705  32.431 1.00 41.49 ? 39   THR C N   1 
ATOM   2497  C  CA  . THR C  1 40  ? 125.648 -9.034  33.072 1.00 44.58 ? 39   THR C CA  1 
ATOM   2498  C  C   . THR C  1 40  ? 126.706 -8.274  32.274 1.00 46.24 ? 39   THR C C   1 
ATOM   2499  O  O   . THR C  1 40  ? 126.718 -8.343  31.043 1.00 45.74 ? 39   THR C O   1 
ATOM   2500  C  CB  . THR C  1 40  ? 125.941 -10.540 32.993 1.00 45.93 ? 39   THR C CB  1 
ATOM   2501  O  OG1 . THR C  1 40  ? 125.897 -10.967 31.626 1.00 46.08 ? 39   THR C OG1 1 
ATOM   2502  C  CG2 . THR C  1 40  ? 124.915 -11.326 33.805 1.00 46.74 ? 39   THR C CG2 1 
ATOM   2503  N  N   . GLU C  1 41  ? 127.574 -7.543  32.970 1.00 46.88 ? 40   GLU C N   1 
ATOM   2504  C  CA  . GLU C  1 41  ? 128.622 -6.756  32.318 1.00 47.40 ? 40   GLU C CA  1 
ATOM   2505  C  C   . GLU C  1 41  ? 129.293 -7.551  31.205 1.00 45.94 ? 40   GLU C C   1 
ATOM   2506  O  O   . GLU C  1 41  ? 129.689 -8.697  31.405 1.00 46.47 ? 40   GLU C O   1 
ATOM   2507  C  CB  . GLU C  1 41  ? 129.674 -6.314  33.341 1.00 49.41 ? 40   GLU C CB  1 
ATOM   2508  C  CG  . GLU C  1 41  ? 130.678 -5.302  32.798 1.00 52.96 ? 40   GLU C CG  1 
ATOM   2509  C  CD  . GLU C  1 41  ? 131.720 -4.890  33.824 1.00 54.43 ? 40   GLU C CD  1 
ATOM   2510  O  OE1 . GLU C  1 41  ? 132.535 -3.997  33.515 1.00 55.88 ? 40   GLU C OE1 1 
ATOM   2511  O  OE2 . GLU C  1 41  ? 131.728 -5.459  34.936 1.00 55.92 ? 40   GLU C OE2 1 
ATOM   2512  N  N   . GLY C  1 42  ? 129.412 -6.946  30.029 1.00 45.00 ? 41   GLY C N   1 
ATOM   2513  C  CA  . GLY C  1 42  ? 130.037 -7.641  28.919 1.00 43.05 ? 41   GLY C CA  1 
ATOM   2514  C  C   . GLY C  1 42  ? 129.222 -7.628  27.637 1.00 41.66 ? 41   GLY C C   1 
ATOM   2515  O  O   . GLY C  1 42  ? 128.322 -6.803  27.465 1.00 40.02 ? 41   GLY C O   1 
ATOM   2516  N  N   . LEU C  1 43  ? 129.537 -8.560  26.743 1.00 41.82 ? 42   LEU C N   1 
ATOM   2517  C  CA  . LEU C  1 43  ? 128.864 -8.658  25.454 1.00 42.02 ? 42   LEU C CA  1 
ATOM   2518  C  C   . LEU C  1 43  ? 127.622 -9.551  25.463 1.00 41.41 ? 42   LEU C C   1 
ATOM   2519  O  O   . LEU C  1 43  ? 127.565 -10.554 26.173 1.00 41.08 ? 42   LEU C O   1 
ATOM   2520  C  CB  . LEU C  1 43  ? 129.844 -9.171  24.400 1.00 42.55 ? 42   LEU C CB  1 
ATOM   2521  C  CG  . LEU C  1 43  ? 131.184 -8.438  24.294 1.00 45.13 ? 42   LEU C CG  1 
ATOM   2522  C  CD1 . LEU C  1 43  ? 131.932 -8.966  23.073 1.00 44.40 ? 42   LEU C CD1 1 
ATOM   2523  C  CD2 . LEU C  1 43  ? 130.966 -6.929  24.180 1.00 45.19 ? 42   LEU C CD2 1 
ATOM   2524  N  N   . HIS C  1 44  ? 126.638 -9.180  24.649 1.00 38.88 ? 43   HIS C N   1 
ATOM   2525  C  CA  . HIS C  1 44  ? 125.392 -9.933  24.547 1.00 37.62 ? 43   HIS C CA  1 
ATOM   2526  C  C   . HIS C  1 44  ? 124.870 -9.946  23.113 1.00 35.60 ? 43   HIS C C   1 
ATOM   2527  O  O   . HIS C  1 44  ? 124.786 -8.894  22.472 1.00 34.36 ? 43   HIS C O   1 
ATOM   2528  C  CB  . HIS C  1 44  ? 124.335 -9.308  25.460 1.00 37.42 ? 43   HIS C CB  1 
ATOM   2529  C  CG  . HIS C  1 44  ? 124.642 -9.435  26.919 1.00 39.47 ? 43   HIS C CG  1 
ATOM   2530  N  ND1 . HIS C  1 44  ? 124.604 -10.640 27.585 1.00 39.72 ? 43   HIS C ND1 1 
ATOM   2531  C  CD2 . HIS C  1 44  ? 124.993 -8.507  27.844 1.00 41.20 ? 43   HIS C CD2 1 
ATOM   2532  C  CE1 . HIS C  1 44  ? 124.917 -10.452 28.854 1.00 41.63 ? 43   HIS C CE1 1 
ATOM   2533  N  NE2 . HIS C  1 44  ? 125.157 -9.164  29.037 1.00 41.57 ? 43   HIS C NE2 1 
ATOM   2534  N  N   . GLY C  1 45  ? 124.525 -11.134 22.618 1.00 32.81 ? 44   GLY C N   1 
ATOM   2535  C  CA  . GLY C  1 45  ? 123.993 -11.259 21.271 1.00 33.37 ? 44   GLY C CA  1 
ATOM   2536  C  C   . GLY C  1 45  ? 122.792 -10.342 21.101 1.00 33.51 ? 44   GLY C C   1 
ATOM   2537  O  O   . GLY C  1 45  ? 122.038 -10.128 22.054 1.00 33.16 ? 44   GLY C O   1 
ATOM   2538  N  N   . PHE C  1 46  ? 122.601 -9.823  19.890 1.00 33.23 ? 45   PHE C N   1 
ATOM   2539  C  CA  . PHE C  1 46  ? 121.520 -8.885  19.594 1.00 33.90 ? 45   PHE C CA  1 
ATOM   2540  C  C   . PHE C  1 46  ? 121.009 -9.176  18.184 1.00 35.32 ? 45   PHE C C   1 
ATOM   2541  O  O   . PHE C  1 46  ? 121.680 -8.839  17.202 1.00 34.85 ? 45   PHE C O   1 
ATOM   2542  C  CB  . PHE C  1 46  ? 122.091 -7.465  19.680 1.00 33.84 ? 45   PHE C CB  1 
ATOM   2543  C  CG  . PHE C  1 46  ? 121.060 -6.374  19.725 1.00 33.44 ? 45   PHE C CG  1 
ATOM   2544  C  CD1 . PHE C  1 46  ? 120.118 -6.325  20.746 1.00 34.54 ? 45   PHE C CD1 1 
ATOM   2545  C  CD2 . PHE C  1 46  ? 121.091 -5.342  18.792 1.00 32.94 ? 45   PHE C CD2 1 
ATOM   2546  C  CE1 . PHE C  1 46  ? 119.223 -5.259  20.843 1.00 35.03 ? 45   PHE C CE1 1 
ATOM   2547  C  CE2 . PHE C  1 46  ? 120.204 -4.274  18.879 1.00 34.90 ? 45   PHE C CE2 1 
ATOM   2548  C  CZ  . PHE C  1 46  ? 119.268 -4.231  19.909 1.00 35.76 ? 45   PHE C CZ  1 
ATOM   2549  N  N   . HIS C  1 47  ? 119.834 -9.805  18.080 1.00 35.25 ? 46   HIS C N   1 
ATOM   2550  C  CA  . HIS C  1 47  ? 119.278 -10.152 16.768 1.00 35.87 ? 46   HIS C CA  1 
ATOM   2551  C  C   . HIS C  1 47  ? 117.777 -9.973  16.581 1.00 35.40 ? 46   HIS C C   1 
ATOM   2552  O  O   . HIS C  1 47  ? 117.013 -9.892  17.547 1.00 34.18 ? 46   HIS C O   1 
ATOM   2553  C  CB  . HIS C  1 47  ? 119.565 -11.611 16.431 1.00 39.21 ? 46   HIS C CB  1 
ATOM   2554  C  CG  . HIS C  1 47  ? 120.793 -12.156 17.083 1.00 43.08 ? 46   HIS C CG  1 
ATOM   2555  N  ND1 . HIS C  1 47  ? 120.742 -13.041 18.135 1.00 45.30 ? 46   HIS C ND1 1 
ATOM   2556  C  CD2 . HIS C  1 47  ? 122.105 -11.917 16.847 1.00 44.72 ? 46   HIS C CD2 1 
ATOM   2557  C  CE1 . HIS C  1 47  ? 121.977 -13.327 18.524 1.00 45.65 ? 46   HIS C CE1 1 
ATOM   2558  N  NE2 . HIS C  1 47  ? 122.816 -12.660 17.761 1.00 44.79 ? 46   HIS C NE2 1 
ATOM   2559  N  N   . VAL C  1 48  ? 117.370 -9.950  15.314 1.00 32.97 ? 47   VAL C N   1 
ATOM   2560  C  CA  . VAL C  1 48  ? 115.960 -9.854  14.951 1.00 32.39 ? 47   VAL C CA  1 
ATOM   2561  C  C   . VAL C  1 48  ? 115.540 -11.280 14.639 1.00 31.12 ? 47   VAL C C   1 
ATOM   2562  O  O   . VAL C  1 48  ? 116.138 -11.925 13.778 1.00 32.52 ? 47   VAL C O   1 
ATOM   2563  C  CB  . VAL C  1 48  ? 115.741 -9.012  13.678 1.00 29.76 ? 47   VAL C CB  1 
ATOM   2564  C  CG1 . VAL C  1 48  ? 114.278 -9.089  13.259 1.00 28.44 ? 47   VAL C CG1 1 
ATOM   2565  C  CG2 . VAL C  1 48  ? 116.159 -7.573  13.927 1.00 28.27 ? 47   VAL C CG2 1 
ATOM   2566  N  N   . HIS C  1 49  ? 114.541 -11.786 15.354 1.00 30.63 ? 48   HIS C N   1 
ATOM   2567  C  CA  . HIS C  1 49  ? 114.059 -13.140 15.111 1.00 28.90 ? 48   HIS C CA  1 
ATOM   2568  C  C   . HIS C  1 49  ? 112.819 -13.096 14.224 1.00 30.48 ? 48   HIS C C   1 
ATOM   2569  O  O   . HIS C  1 49  ? 112.118 -12.085 14.164 1.00 31.04 ? 48   HIS C O   1 
ATOM   2570  C  CB  . HIS C  1 49  ? 113.762 -13.857 16.436 1.00 30.02 ? 48   HIS C CB  1 
ATOM   2571  C  CG  . HIS C  1 49  ? 114.991 -14.278 17.180 1.00 29.47 ? 48   HIS C CG  1 
ATOM   2572  N  ND1 . HIS C  1 49  ? 115.193 -15.576 17.616 1.00 28.74 ? 48   HIS C ND1 1 
ATOM   2573  C  CD2 . HIS C  1 49  ? 116.089 -13.585 17.569 1.00 28.12 ? 48   HIS C CD2 1 
ATOM   2574  C  CE1 . HIS C  1 49  ? 116.353 -15.656 18.235 1.00 29.04 ? 48   HIS C CE1 1 
ATOM   2575  N  NE2 . HIS C  1 49  ? 116.920 -14.461 18.222 1.00 29.46 ? 48   HIS C NE2 1 
ATOM   2576  N  N   . GLU C  1 50  ? 112.551 -14.206 13.549 1.00 30.90 ? 49   GLU C N   1 
ATOM   2577  C  CA  . GLU C  1 50  ? 111.447 -14.312 12.608 1.00 33.54 ? 49   GLU C CA  1 
ATOM   2578  C  C   . GLU C  1 50  ? 110.039 -13.910 13.049 1.00 34.49 ? 49   GLU C C   1 
ATOM   2579  O  O   . GLU C  1 50  ? 109.414 -13.060 12.413 1.00 33.34 ? 49   GLU C O   1 
ATOM   2580  C  CB  . GLU C  1 50  ? 111.403 -15.728 12.036 1.00 34.00 ? 49   GLU C CB  1 
ATOM   2581  C  CG  . GLU C  1 50  ? 110.463 -15.891 10.852 1.00 37.39 ? 49   GLU C CG  1 
ATOM   2582  C  CD  . GLU C  1 50  ? 110.482 -17.296 10.275 1.00 38.15 ? 49   GLU C CD  1 
ATOM   2583  O  OE1 . GLU C  1 50  ? 109.747 -17.554 9.298  1.00 40.39 ? 49   GLU C OE1 1 
ATOM   2584  O  OE2 . GLU C  1 50  ? 111.229 -18.146 10.799 1.00 39.45 ? 49   GLU C OE2 1 
ATOM   2585  N  N   . PHE C  1 51  ? 109.535 -14.507 14.126 1.00 33.89 ? 50   PHE C N   1 
ATOM   2586  C  CA  . PHE C  1 51  ? 108.172 -14.210 14.564 1.00 32.75 ? 50   PHE C CA  1 
ATOM   2587  C  C   . PHE C  1 51  ? 108.001 -13.218 15.712 1.00 30.71 ? 50   PHE C C   1 
ATOM   2588  O  O   . PHE C  1 51  ? 108.747 -13.238 16.691 1.00 30.96 ? 50   PHE C O   1 
ATOM   2589  C  CB  . PHE C  1 51  ? 107.466 -15.520 14.925 1.00 34.58 ? 50   PHE C CB  1 
ATOM   2590  C  CG  . PHE C  1 51  ? 107.595 -16.582 13.876 1.00 35.47 ? 50   PHE C CG  1 
ATOM   2591  C  CD1 . PHE C  1 51  ? 107.122 -16.365 12.588 1.00 36.96 ? 50   PHE C CD1 1 
ATOM   2592  C  CD2 . PHE C  1 51  ? 108.223 -17.787 14.166 1.00 35.70 ? 50   PHE C CD2 1 
ATOM   2593  C  CE1 . PHE C  1 51  ? 107.267 -17.338 11.602 1.00 37.06 ? 50   PHE C CE1 1 
ATOM   2594  C  CE2 . PHE C  1 51  ? 108.373 -18.762 13.192 1.00 36.32 ? 50   PHE C CE2 1 
ATOM   2595  C  CZ  . PHE C  1 51  ? 107.897 -18.535 11.904 1.00 37.88 ? 50   PHE C CZ  1 
ATOM   2596  N  N   . GLY C  1 52  ? 106.999 -12.354 15.581 1.00 27.61 ? 51   GLY C N   1 
ATOM   2597  C  CA  . GLY C  1 52  ? 106.706 -11.387 16.623 1.00 27.06 ? 51   GLY C CA  1 
ATOM   2598  C  C   . GLY C  1 52  ? 105.680 -12.021 17.546 1.00 28.09 ? 51   GLY C C   1 
ATOM   2599  O  O   . GLY C  1 52  ? 104.702 -11.390 17.942 1.00 27.82 ? 51   GLY C O   1 
ATOM   2600  N  N   . ASP C  1 53  ? 105.914 -13.287 17.879 1.00 28.66 ? 52   ASP C N   1 
ATOM   2601  C  CA  . ASP C  1 53  ? 105.013 -14.058 18.727 1.00 29.77 ? 52   ASP C CA  1 
ATOM   2602  C  C   . ASP C  1 53  ? 105.596 -14.232 20.124 1.00 32.22 ? 52   ASP C C   1 
ATOM   2603  O  O   . ASP C  1 53  ? 106.631 -14.881 20.304 1.00 32.05 ? 52   ASP C O   1 
ATOM   2604  C  CB  . ASP C  1 53  ? 104.763 -15.415 18.070 1.00 29.58 ? 52   ASP C CB  1 
ATOM   2605  C  CG  . ASP C  1 53  ? 103.762 -16.266 18.824 1.00 31.44 ? 52   ASP C CG  1 
ATOM   2606  O  OD1 . ASP C  1 53  ? 103.213 -17.194 18.199 1.00 31.63 ? 52   ASP C OD1 1 
ATOM   2607  O  OD2 . ASP C  1 53  ? 103.529 -16.023 20.027 1.00 31.94 ? 52   ASP C OD2 1 
ATOM   2608  N  N   . ASN C  1 54  ? 104.921 -13.656 21.113 1.00 31.86 ? 53   ASN C N   1 
ATOM   2609  C  CA  . ASN C  1 54  ? 105.388 -13.731 22.489 1.00 33.31 ? 53   ASN C CA  1 
ATOM   2610  C  C   . ASN C  1 54  ? 104.452 -14.565 23.369 1.00 34.04 ? 53   ASN C C   1 
ATOM   2611  O  O   . ASN C  1 54  ? 104.466 -14.432 24.590 1.00 33.91 ? 53   ASN C O   1 
ATOM   2612  C  CB  . ASN C  1 54  ? 105.502 -12.318 23.062 1.00 33.32 ? 53   ASN C CB  1 
ATOM   2613  C  CG  . ASN C  1 54  ? 106.324 -12.269 24.329 1.00 37.34 ? 53   ASN C CG  1 
ATOM   2614  O  OD1 . ASN C  1 54  ? 105.969 -11.580 25.287 1.00 37.32 ? 53   ASN C OD1 1 
ATOM   2615  N  ND2 . ASN C  1 54  ? 107.440 -12.995 24.338 1.00 36.40 ? 53   ASN C ND2 1 
ATOM   2616  N  N   . THR C  1 55  ? 103.653 -15.427 22.746 1.00 34.42 ? 54   THR C N   1 
ATOM   2617  C  CA  . THR C  1 55  ? 102.699 -16.261 23.474 1.00 35.38 ? 54   THR C CA  1 
ATOM   2618  C  C   . THR C  1 55  ? 103.344 -17.192 24.491 1.00 37.28 ? 54   THR C C   1 
ATOM   2619  O  O   . THR C  1 55  ? 102.718 -17.570 25.480 1.00 37.02 ? 54   THR C O   1 
ATOM   2620  C  CB  . THR C  1 55  ? 101.857 -17.114 22.513 1.00 35.09 ? 54   THR C CB  1 
ATOM   2621  O  OG1 . THR C  1 55  ? 102.716 -17.959 21.739 1.00 35.51 ? 54   THR C OG1 1 
ATOM   2622  C  CG2 . THR C  1 55  ? 101.047 -16.226 21.586 1.00 33.69 ? 54   THR C CG2 1 
ATOM   2623  N  N   . ALA C  1 56  ? 104.594 -17.566 24.247 1.00 38.50 ? 55   ALA C N   1 
ATOM   2624  C  CA  . ALA C  1 56  ? 105.309 -18.450 25.156 1.00 39.17 ? 55   ALA C CA  1 
ATOM   2625  C  C   . ALA C  1 56  ? 106.675 -17.862 25.474 1.00 39.38 ? 55   ALA C C   1 
ATOM   2626  O  O   . ALA C  1 56  ? 107.682 -18.563 25.433 1.00 40.88 ? 55   ALA C O   1 
ATOM   2627  C  CB  . ALA C  1 56  ? 105.466 -19.828 24.528 1.00 40.49 ? 55   ALA C CB  1 
ATOM   2628  N  N   . GLY C  1 57  ? 106.704 -16.572 25.792 1.00 40.05 ? 56   GLY C N   1 
ATOM   2629  C  CA  . GLY C  1 57  ? 107.965 -15.920 26.094 1.00 39.52 ? 56   GLY C CA  1 
ATOM   2630  C  C   . GLY C  1 57  ? 108.757 -15.710 24.816 1.00 39.73 ? 56   GLY C C   1 
ATOM   2631  O  O   . GLY C  1 57  ? 108.226 -15.883 23.721 1.00 38.02 ? 56   GLY C O   1 
ATOM   2632  N  N   . CYS C  1 58  ? 110.027 -15.344 24.947 1.00 40.25 ? 57   CYS C N   1 
ATOM   2633  C  CA  . CYS C  1 58  ? 110.866 -15.114 23.778 1.00 40.38 ? 57   CYS C CA  1 
ATOM   2634  C  C   . CYS C  1 58  ? 111.109 -16.394 23.004 1.00 40.75 ? 57   CYS C C   1 
ATOM   2635  O  O   . CYS C  1 58  ? 111.684 -16.370 21.920 1.00 41.54 ? 57   CYS C O   1 
ATOM   2636  C  CB  . CYS C  1 58  ? 112.202 -14.505 24.200 1.00 39.07 ? 57   CYS C CB  1 
ATOM   2637  S  SG  . CYS C  1 58  ? 111.979 -12.967 25.130 1.00 38.02 ? 57   CYS C SG  1 
ATOM   2638  N  N   . THR C  1 59  ? 110.657 -17.512 23.559 1.00 40.91 ? 58   THR C N   1 
ATOM   2639  C  CA  . THR C  1 59  ? 110.834 -18.804 22.915 1.00 41.33 ? 58   THR C CA  1 
ATOM   2640  C  C   . THR C  1 59  ? 110.019 -18.937 21.635 1.00 40.62 ? 58   THR C C   1 
ATOM   2641  O  O   . THR C  1 59  ? 110.472 -19.543 20.666 1.00 42.05 ? 58   THR C O   1 
ATOM   2642  C  CB  . THR C  1 59  ? 110.446 -19.955 23.868 1.00 43.64 ? 58   THR C CB  1 
ATOM   2643  O  OG1 . THR C  1 59  ? 111.321 -19.950 25.004 1.00 45.54 ? 58   THR C OG1 1 
ATOM   2644  C  CG2 . THR C  1 59  ? 110.556 -21.300 23.157 1.00 43.97 ? 58   THR C CG2 1 
ATOM   2645  N  N   . SER C  1 60  ? 108.818 -18.374 21.626 1.00 38.72 ? 59   SER C N   1 
ATOM   2646  C  CA  . SER C  1 60  ? 107.966 -18.475 20.448 1.00 38.33 ? 59   SER C CA  1 
ATOM   2647  C  C   . SER C  1 60  ? 108.328 -17.509 19.315 1.00 36.62 ? 59   SER C C   1 
ATOM   2648  O  O   . SER C  1 60  ? 107.647 -17.464 18.293 1.00 36.84 ? 59   SER C O   1 
ATOM   2649  C  CB  . SER C  1 60  ? 106.494 -18.313 20.852 1.00 38.81 ? 59   SER C CB  1 
ATOM   2650  O  OG  . SER C  1 60  ? 106.327 -17.307 21.836 1.00 41.64 ? 59   SER C OG  1 
ATOM   2651  N  N   . ALA C  1 61  ? 109.406 -16.751 19.492 1.00 36.16 ? 60   ALA C N   1 
ATOM   2652  C  CA  . ALA C  1 61  ? 109.850 -15.808 18.467 1.00 34.33 ? 60   ALA C CA  1 
ATOM   2653  C  C   . ALA C  1 61  ? 110.518 -16.558 17.316 1.00 35.29 ? 60   ALA C C   1 
ATOM   2654  O  O   . ALA C  1 61  ? 110.776 -15.990 16.254 1.00 35.19 ? 60   ALA C O   1 
ATOM   2655  C  CB  . ALA C  1 61  ? 110.818 -14.813 19.061 1.00 32.24 ? 60   ALA C CB  1 
ATOM   2656  N  N   . GLY C  1 62  ? 110.803 -17.836 17.536 1.00 35.41 ? 61   GLY C N   1 
ATOM   2657  C  CA  . GLY C  1 62  ? 111.434 -18.638 16.504 1.00 36.92 ? 61   GLY C CA  1 
ATOM   2658  C  C   . GLY C  1 62  ? 112.899 -18.299 16.283 1.00 37.35 ? 61   GLY C C   1 
ATOM   2659  O  O   . GLY C  1 62  ? 113.506 -17.601 17.094 1.00 36.44 ? 61   GLY C O   1 
ATOM   2660  N  N   . PRO C  1 63  ? 113.492 -18.773 15.173 1.00 38.51 ? 62   PRO C N   1 
ATOM   2661  C  CA  . PRO C  1 63  ? 114.898 -18.537 14.822 1.00 38.53 ? 62   PRO C CA  1 
ATOM   2662  C  C   . PRO C  1 63  ? 115.227 -17.107 14.394 1.00 38.87 ? 62   PRO C C   1 
ATOM   2663  O  O   . PRO C  1 63  ? 114.361 -16.229 14.367 1.00 36.91 ? 62   PRO C O   1 
ATOM   2664  C  CB  . PRO C  1 63  ? 115.136 -19.539 13.702 1.00 38.65 ? 62   PRO C CB  1 
ATOM   2665  C  CG  . PRO C  1 63  ? 113.817 -19.554 13.002 1.00 40.90 ? 62   PRO C CG  1 
ATOM   2666  C  CD  . PRO C  1 63  ? 112.834 -19.612 14.156 1.00 38.55 ? 62   PRO C CD  1 
ATOM   2667  N  N   . HIS C  1 64  ? 116.494 -16.874 14.072 1.00 38.67 ? 63   HIS C N   1 
ATOM   2668  C  CA  . HIS C  1 64  ? 116.922 -15.556 13.628 1.00 38.35 ? 63   HIS C CA  1 
ATOM   2669  C  C   . HIS C  1 64  ? 116.240 -15.293 12.280 1.00 37.18 ? 63   HIS C C   1 
ATOM   2670  O  O   . HIS C  1 64  ? 116.070 -16.217 11.481 1.00 34.74 ? 63   HIS C O   1 
ATOM   2671  C  CB  . HIS C  1 64  ? 118.458 -15.519 13.496 1.00 41.69 ? 63   HIS C CB  1 
ATOM   2672  C  CG  . HIS C  1 64  ? 119.182 -15.545 14.812 1.00 44.51 ? 63   HIS C CG  1 
ATOM   2673  N  ND1 . HIS C  1 64  ? 120.556 -15.639 14.911 1.00 44.52 ? 63   HIS C ND1 1 
ATOM   2674  C  CD2 . HIS C  1 64  ? 118.724 -15.461 16.085 1.00 46.95 ? 63   HIS C CD2 1 
ATOM   2675  C  CE1 . HIS C  1 64  ? 120.909 -15.609 16.182 1.00 47.12 ? 63   HIS C CE1 1 
ATOM   2676  N  NE2 . HIS C  1 64  ? 119.817 -15.501 16.919 1.00 47.01 ? 63   HIS C NE2 1 
ATOM   2677  N  N   . PHE C  1 65  ? 115.820 -14.051 12.042 1.00 35.60 ? 64   PHE C N   1 
ATOM   2678  C  CA  . PHE C  1 65  ? 115.161 -13.716 10.780 1.00 35.75 ? 64   PHE C CA  1 
ATOM   2679  C  C   . PHE C  1 65  ? 116.138 -14.028 9.650  1.00 36.88 ? 64   PHE C C   1 
ATOM   2680  O  O   . PHE C  1 65  ? 117.193 -13.391 9.534  1.00 36.56 ? 64   PHE C O   1 
ATOM   2681  C  CB  . PHE C  1 65  ? 114.785 -12.234 10.731 1.00 33.44 ? 64   PHE C CB  1 
ATOM   2682  C  CG  . PHE C  1 65  ? 114.011 -11.849 9.495  1.00 33.72 ? 64   PHE C CG  1 
ATOM   2683  C  CD1 . PHE C  1 65  ? 114.135 -10.576 8.950  1.00 32.16 ? 64   PHE C CD1 1 
ATOM   2684  C  CD2 . PHE C  1 65  ? 113.149 -12.759 8.886  1.00 31.19 ? 64   PHE C CD2 1 
ATOM   2685  C  CE1 . PHE C  1 65  ? 113.413 -10.212 7.815  1.00 32.53 ? 64   PHE C CE1 1 
ATOM   2686  C  CE2 . PHE C  1 65  ? 112.421 -12.404 7.748  1.00 32.97 ? 64   PHE C CE2 1 
ATOM   2687  C  CZ  . PHE C  1 65  ? 112.554 -11.129 7.214  1.00 30.96 ? 64   PHE C CZ  1 
ATOM   2688  N  N   . ASN C  1 66  ? 115.778 -14.996 8.816  1.00 37.24 ? 65   ASN C N   1 
ATOM   2689  C  CA  . ASN C  1 66  ? 116.648 -15.416 7.730  1.00 40.42 ? 65   ASN C CA  1 
ATOM   2690  C  C   . ASN C  1 66  ? 115.902 -15.719 6.424  1.00 40.02 ? 65   ASN C C   1 
ATOM   2691  O  O   . ASN C  1 66  ? 115.803 -16.871 6.003  1.00 40.57 ? 65   ASN C O   1 
ATOM   2692  C  CB  . ASN C  1 66  ? 117.435 -16.645 8.196  1.00 41.18 ? 65   ASN C CB  1 
ATOM   2693  C  CG  . ASN C  1 66  ? 118.490 -17.078 7.204  1.00 43.90 ? 65   ASN C CG  1 
ATOM   2694  O  OD1 . ASN C  1 66  ? 119.324 -16.278 6.778  1.00 43.08 ? 65   ASN C OD1 1 
ATOM   2695  N  ND2 . ASN C  1 66  ? 118.467 -18.355 6.838  1.00 44.17 ? 65   ASN C ND2 1 
ATOM   2696  N  N   . PRO C  1 67  ? 115.373 -14.679 5.761  1.00 40.20 ? 66   PRO C N   1 
ATOM   2697  C  CA  . PRO C  1 67  ? 114.645 -14.869 4.502  1.00 41.65 ? 66   PRO C CA  1 
ATOM   2698  C  C   . PRO C  1 67  ? 115.552 -15.327 3.351  1.00 43.51 ? 66   PRO C C   1 
ATOM   2699  O  O   . PRO C  1 67  ? 115.111 -16.044 2.457  1.00 42.32 ? 66   PRO C O   1 
ATOM   2700  C  CB  . PRO C  1 67  ? 114.040 -13.494 4.252  1.00 41.66 ? 66   PRO C CB  1 
ATOM   2701  C  CG  . PRO C  1 67  ? 115.085 -12.577 4.815  1.00 41.35 ? 66   PRO C CG  1 
ATOM   2702  C  CD  . PRO C  1 67  ? 115.439 -13.252 6.120  1.00 40.13 ? 66   PRO C CD  1 
ATOM   2703  N  N   . LEU C  1 68  ? 116.816 -14.910 3.386  1.00 46.31 ? 67   LEU C N   1 
ATOM   2704  C  CA  . LEU C  1 68  ? 117.788 -15.275 2.354  1.00 49.84 ? 67   LEU C CA  1 
ATOM   2705  C  C   . LEU C  1 68  ? 118.381 -16.668 2.552  1.00 51.02 ? 67   LEU C C   1 
ATOM   2706  O  O   . LEU C  1 68  ? 119.152 -17.144 1.718  1.00 51.84 ? 67   LEU C O   1 
ATOM   2707  C  CB  . LEU C  1 68  ? 118.918 -14.244 2.303  1.00 51.49 ? 67   LEU C CB  1 
ATOM   2708  C  CG  . LEU C  1 68  ? 118.781 -13.091 1.305  1.00 52.02 ? 67   LEU C CG  1 
ATOM   2709  C  CD1 . LEU C  1 68  ? 117.386 -12.497 1.365  1.00 53.79 ? 67   LEU C CD1 1 
ATOM   2710  C  CD2 . LEU C  1 68  ? 119.841 -12.037 1.613  1.00 53.57 ? 67   LEU C CD2 1 
ATOM   2711  N  N   . SER C  1 69  ? 118.036 -17.309 3.663  1.00 51.79 ? 68   SER C N   1 
ATOM   2712  C  CA  . SER C  1 69  ? 118.507 -18.661 3.954  1.00 51.81 ? 68   SER C CA  1 
ATOM   2713  C  C   . SER C  1 69  ? 120.024 -18.792 4.020  1.00 52.46 ? 68   SER C C   1 
ATOM   2714  O  O   . SER C  1 69  ? 120.599 -19.745 3.497  1.00 52.77 ? 68   SER C O   1 
ATOM   2715  C  CB  . SER C  1 69  ? 117.966 -19.624 2.903  1.00 51.13 ? 68   SER C CB  1 
ATOM   2716  O  OG  . SER C  1 69  ? 116.605 -19.350 2.651  1.00 48.08 ? 68   SER C OG  1 
ATOM   2717  N  N   . ARG C  1 70  ? 120.674 -17.836 4.666  1.00 52.63 ? 69   ARG C N   1 
ATOM   2718  C  CA  . ARG C  1 70  ? 122.121 -17.884 4.795  1.00 52.47 ? 69   ARG C CA  1 
ATOM   2719  C  C   . ARG C  1 70  ? 122.520 -18.323 6.200  1.00 51.41 ? 69   ARG C C   1 
ATOM   2720  O  O   . ARG C  1 70  ? 121.679 -18.398 7.093  1.00 50.60 ? 69   ARG C O   1 
ATOM   2721  C  CB  . ARG C  1 70  ? 122.715 -16.516 4.499  0.00 54.27 ? 69   ARG C CB  1 
ATOM   2722  C  CG  . ARG C  1 70  ? 122.490 -16.049 3.081  0.00 56.72 ? 69   ARG C CG  1 
ATOM   2723  C  CD  . ARG C  1 70  ? 123.142 -14.707 2.844  1.00 59.49 ? 69   ARG C CD  1 
ATOM   2724  N  NE  . ARG C  1 70  ? 122.876 -14.201 1.501  1.00 61.35 ? 69   ARG C NE  1 
ATOM   2725  C  CZ  . ARG C  1 70  ? 123.292 -13.021 1.055  1.00 62.76 ? 69   ARG C CZ  1 
ATOM   2726  N  NH1 . ARG C  1 70  ? 123.004 -12.637 -0.182 1.00 63.36 ? 69   ARG C NH1 1 
ATOM   2727  N  NH2 . ARG C  1 70  ? 123.997 -12.221 1.848  1.00 62.51 ? 69   ARG C NH2 1 
ATOM   2728  N  N   . LYS C  1 71  ? 123.801 -18.613 6.393  1.00 49.48 ? 70   LYS C N   1 
ATOM   2729  C  CA  . LYS C  1 71  ? 124.280 -19.037 7.698  1.00 48.59 ? 70   LYS C CA  1 
ATOM   2730  C  C   . LYS C  1 71  ? 124.458 -17.826 8.598  1.00 48.45 ? 70   LYS C C   1 
ATOM   2731  O  O   . LYS C  1 71  ? 124.524 -16.697 8.125  1.00 48.35 ? 70   LYS C O   1 
ATOM   2732  C  CB  . LYS C  1 71  ? 125.593 -19.813 7.551  1.00 50.71 ? 70   LYS C CB  1 
ATOM   2733  C  CG  . LYS C  1 71  ? 125.386 -21.283 7.224  1.00 52.45 ? 70   LYS C CG  1 
ATOM   2734  C  CD  . LYS C  1 71  ? 124.580 -21.463 5.948  1.00 55.64 ? 70   LYS C CD  1 
ATOM   2735  C  CE  . LYS C  1 71  ? 124.377 -22.936 5.633  1.00 56.90 ? 70   LYS C CE  1 
ATOM   2736  N  NZ  . LYS C  1 71  ? 123.625 -23.627 6.716  1.00 57.92 ? 70   LYS C NZ  1 
ATOM   2737  N  N   . HIS C  1 72  ? 124.509 -18.066 9.894  1.00 44.36 ? 71   HIS C N   1 
ATOM   2738  C  CA  . HIS C  1 72  ? 124.660 -17.002 10.851 1.00 43.36 ? 71   HIS C CA  1 
ATOM   2739  C  C   . HIS C  1 72  ? 125.986 -16.226 10.698 1.00 43.46 ? 71   HIS C C   1 
ATOM   2740  O  O   . HIS C  1 72  ? 126.971 -16.730 10.135 1.00 43.10 ? 71   HIS C O   1 
ATOM   2741  C  CB  . HIS C  1 72  ? 124.533 -17.611 12.241 1.00 41.48 ? 71   HIS C CB  1 
ATOM   2742  C  CG  . HIS C  1 72  ? 124.656 -16.615 13.340 1.00 41.54 ? 71   HIS C CG  1 
ATOM   2743  N  ND1 . HIS C  1 72  ? 123.713 -15.642 13.572 1.00 41.44 ? 71   HIS C ND1 1 
ATOM   2744  C  CD2 . HIS C  1 72  ? 125.665 -16.387 14.216 1.00 41.09 ? 71   HIS C CD2 1 
ATOM   2745  C  CE1 . HIS C  1 72  ? 124.138 -14.846 14.545 1.00 41.90 ? 71   HIS C CE1 1 
ATOM   2746  N  NE2 . HIS C  1 72  ? 125.312 -15.277 14.947 1.00 41.14 ? 71   HIS C NE2 1 
ATOM   2747  N  N   . GLY C  1 73  ? 125.997 -14.986 11.187 1.00 42.38 ? 72   GLY C N   1 
ATOM   2748  C  CA  . GLY C  1 73  ? 127.205 -14.179 11.103 1.00 42.51 ? 72   GLY C CA  1 
ATOM   2749  C  C   . GLY C  1 73  ? 127.165 -12.848 11.842 1.00 42.98 ? 72   GLY C C   1 
ATOM   2750  O  O   . GLY C  1 73  ? 126.243 -12.583 12.611 1.00 41.95 ? 72   GLY C O   1 
ATOM   2751  N  N   . GLY C  1 74  ? 128.175 -12.010 11.617 1.00 43.14 ? 73   GLY C N   1 
ATOM   2752  C  CA  . GLY C  1 74  ? 128.216 -10.704 12.261 1.00 42.83 ? 73   GLY C CA  1 
ATOM   2753  C  C   . GLY C  1 74  ? 127.581 -9.669  11.348 1.00 43.40 ? 73   GLY C C   1 
ATOM   2754  O  O   . GLY C  1 74  ? 127.399 -9.946  10.164 1.00 41.20 ? 73   GLY C O   1 
ATOM   2755  N  N   . PRO C  1 75  ? 127.230 -8.471  11.852 1.00 44.34 ? 74   PRO C N   1 
ATOM   2756  C  CA  . PRO C  1 75  ? 126.614 -7.463  10.981 1.00 45.26 ? 74   PRO C CA  1 
ATOM   2757  C  C   . PRO C  1 75  ? 127.517 -7.033  9.825  1.00 46.35 ? 74   PRO C C   1 
ATOM   2758  O  O   . PRO C  1 75  ? 127.027 -6.655  8.761  1.00 46.64 ? 74   PRO C O   1 
ATOM   2759  C  CB  . PRO C  1 75  ? 126.293 -6.319  11.943 1.00 45.30 ? 74   PRO C CB  1 
ATOM   2760  C  CG  . PRO C  1 75  ? 127.352 -6.453  12.999 1.00 45.89 ? 74   PRO C CG  1 
ATOM   2761  C  CD  . PRO C  1 75  ? 127.410 -7.949  13.218 1.00 45.11 ? 74   PRO C CD  1 
ATOM   2762  N  N   . LYS C  1 76  ? 128.831 -7.106  10.035 1.00 46.20 ? 75   LYS C N   1 
ATOM   2763  C  CA  . LYS C  1 76  ? 129.804 -6.734  9.006  1.00 47.58 ? 75   LYS C CA  1 
ATOM   2764  C  C   . LYS C  1 76  ? 129.965 -7.784  7.901  1.00 48.18 ? 75   LYS C C   1 
ATOM   2765  O  O   . LYS C  1 76  ? 130.350 -7.449  6.785  1.00 47.95 ? 75   LYS C O   1 
ATOM   2766  C  CB  . LYS C  1 76  ? 131.179 -6.475  9.636  1.00 47.99 ? 75   LYS C CB  1 
ATOM   2767  C  CG  . LYS C  1 76  ? 131.251 -5.299  10.603 1.00 49.78 ? 75   LYS C CG  1 
ATOM   2768  C  CD  . LYS C  1 76  ? 132.671 -5.147  11.142 1.00 49.70 ? 75   LYS C CD  1 
ATOM   2769  C  CE  . LYS C  1 76  ? 132.809 -3.917  12.026 1.00 50.32 ? 75   LYS C CE  1 
ATOM   2770  N  NZ  . LYS C  1 76  ? 134.223 -3.712  12.436 1.00 49.63 ? 75   LYS C NZ  1 
ATOM   2771  N  N   . ASP C  1 77  ? 129.676 -9.046  8.211  1.00 48.56 ? 76   ASP C N   1 
ATOM   2772  C  CA  . ASP C  1 77  ? 129.811 -10.139 7.246  1.00 49.57 ? 76   ASP C CA  1 
ATOM   2773  C  C   . ASP C  1 77  ? 128.745 -10.150 6.153  1.00 51.06 ? 76   ASP C C   1 
ATOM   2774  O  O   . ASP C  1 77  ? 127.616 -9.687  6.365  1.00 51.80 ? 76   ASP C O   1 
ATOM   2775  C  CB  . ASP C  1 77  ? 129.770 -11.479 7.975  1.00 50.24 ? 76   ASP C CB  1 
ATOM   2776  C  CG  . ASP C  1 77  ? 130.985 -11.710 8.850  0.00 50.49 ? 76   ASP C CG  1 
ATOM   2777  O  OD1 . ASP C  1 77  ? 130.936 -12.668 9.639  0.00 50.71 ? 76   ASP C OD1 1 
ATOM   2778  O  OD2 . ASP C  1 77  ? 131.982 -10.960 8.753  0.00 50.72 ? 76   ASP C OD2 1 
ATOM   2779  N  N   . GLU C  1 78  ? 129.097 -10.682 4.982  1.00 51.71 ? 77   GLU C N   1 
ATOM   2780  C  CA  . GLU C  1 78  ? 128.140 -10.771 3.875  1.00 52.56 ? 77   GLU C CA  1 
ATOM   2781  C  C   . GLU C  1 78  ? 127.277 -12.013 4.123  1.00 51.03 ? 77   GLU C C   1 
ATOM   2782  O  O   . GLU C  1 78  ? 126.051 -11.992 3.925  1.00 51.17 ? 77   GLU C O   1 
ATOM   2783  C  CB  . GLU C  1 78  ? 128.853 -10.924 2.523  1.00 55.60 ? 77   GLU C CB  1 
ATOM   2784  C  CG  . GLU C  1 78  ? 129.787 -9.776  2.134  1.00 59.18 ? 77   GLU C CG  1 
ATOM   2785  C  CD  . GLU C  1 78  ? 130.561 -10.041 0.844  1.00 61.30 ? 77   GLU C CD  1 
ATOM   2786  O  OE1 . GLU C  1 78  ? 131.488 -9.259  0.542  1.00 64.15 ? 77   GLU C OE1 1 
ATOM   2787  O  OE2 . GLU C  1 78  ? 130.246 -11.020 0.130  1.00 62.60 ? 77   GLU C OE2 1 
ATOM   2788  N  N   . GLU C  1 79  ? 127.939 -13.097 4.530  1.00 49.45 ? 78   GLU C N   1 
ATOM   2789  C  CA  . GLU C  1 79  ? 127.259 -14.352 4.842  1.00 49.16 ? 78   GLU C CA  1 
ATOM   2790  C  C   . GLU C  1 79  ? 126.661 -14.198 6.236  1.00 47.45 ? 78   GLU C C   1 
ATOM   2791  O  O   . GLU C  1 79  ? 127.351 -14.362 7.247  1.00 45.52 ? 78   GLU C O   1 
ATOM   2792  C  CB  . GLU C  1 79  ? 128.248 -15.530 4.820  1.00 50.44 ? 78   GLU C CB  1 
ATOM   2793  C  CG  . GLU C  1 79  ? 127.654 -16.936 5.142  1.00 52.72 ? 78   GLU C CG  1 
ATOM   2794  C  CD  . GLU C  1 79  ? 126.636 -17.427 4.112  1.00 52.95 ? 78   GLU C CD  1 
ATOM   2795  O  OE1 . GLU C  1 79  ? 126.189 -18.594 4.208  1.00 53.44 ? 78   GLU C OE1 1 
ATOM   2796  O  OE2 . GLU C  1 79  ? 126.282 -16.638 3.213  1.00 52.49 ? 78   GLU C OE2 1 
ATOM   2797  N  N   . ARG C  1 80  ? 125.371 -13.880 6.278  1.00 45.75 ? 79   ARG C N   1 
ATOM   2798  C  CA  . ARG C  1 80  ? 124.685 -13.703 7.544  1.00 43.75 ? 79   ARG C CA  1 
ATOM   2799  C  C   . ARG C  1 80  ? 123.183 -13.670 7.382  1.00 42.40 ? 79   ARG C C   1 
ATOM   2800  O  O   . ARG C  1 80  ? 122.667 -13.552 6.274  1.00 42.88 ? 79   ARG C O   1 
ATOM   2801  C  CB  . ARG C  1 80  ? 125.140 -12.404 8.199  0.00 44.16 ? 79   ARG C CB  1 
ATOM   2802  C  CG  . ARG C  1 80  ? 124.879 -11.179 7.337  1.00 44.12 ? 79   ARG C CG  1 
ATOM   2803  C  CD  . ARG C  1 80  ? 123.793 -10.282 7.902  1.00 45.95 ? 79   ARG C CD  1 
ATOM   2804  N  NE  . ARG C  1 80  ? 124.258 -8.905  8.043  1.00 45.65 ? 79   ARG C NE  1 
ATOM   2805  C  CZ  . ARG C  1 80  ? 123.539 -7.925  8.580  1.00 45.98 ? 79   ARG C CZ  1 
ATOM   2806  N  NH1 . ARG C  1 80  ? 124.040 -6.698  8.672  1.00 43.33 ? 79   ARG C NH1 1 
ATOM   2807  N  NH2 . ARG C  1 80  ? 122.311 -8.166  9.012  1.00 48.03 ? 79   ARG C NH2 1 
ATOM   2808  N  N   . HIS C  1 81  ? 122.510 -13.774 8.523  1.00 39.92 ? 80   HIS C N   1 
ATOM   2809  C  CA  . HIS C  1 81  ? 121.061 -13.728 8.613  1.00 36.45 ? 80   HIS C CA  1 
ATOM   2810  C  C   . HIS C  1 81  ? 120.728 -12.255 8.565  1.00 35.08 ? 80   HIS C C   1 
ATOM   2811  O  O   . HIS C  1 81  ? 121.492 -11.430 9.067  1.00 35.16 ? 80   HIS C O   1 
ATOM   2812  C  CB  . HIS C  1 81  ? 120.599 -14.282 9.968  1.00 34.92 ? 80   HIS C CB  1 
ATOM   2813  C  CG  . HIS C  1 81  ? 120.903 -15.734 10.167 1.00 36.85 ? 80   HIS C CG  1 
ATOM   2814  N  ND1 . HIS C  1 81  ? 121.071 -16.303 11.424 1.00 31.93 ? 80   HIS C ND1 1 
ATOM   2815  C  CD2 . HIS C  1 81  ? 121.010 -16.748 9.279  1.00 34.51 ? 80   HIS C CD2 1 
ATOM   2816  C  CE1 . HIS C  1 81  ? 121.260 -17.603 11.284 1.00 32.41 ? 80   HIS C CE1 1 
ATOM   2817  N  NE2 . HIS C  1 81  ? 121.228 -17.899 9.998  1.00 34.73 ? 80   HIS C NE2 1 
ATOM   2818  N  N   . VAL C  1 82  ? 119.593 -11.922 7.968  1.00 34.77 ? 81   VAL C N   1 
ATOM   2819  C  CA  . VAL C  1 82  ? 119.174 -10.540 7.894  1.00 34.35 ? 81   VAL C CA  1 
ATOM   2820  C  C   . VAL C  1 82  ? 119.105 -9.931  9.291  1.00 34.71 ? 81   VAL C C   1 
ATOM   2821  O  O   . VAL C  1 82  ? 119.446 -8.759  9.483  1.00 35.25 ? 81   VAL C O   1 
ATOM   2822  C  CB  . VAL C  1 82  ? 117.800 -10.427 7.221  1.00 37.35 ? 81   VAL C CB  1 
ATOM   2823  C  CG1 . VAL C  1 82  ? 117.296 -9.005  7.328  1.00 34.15 ? 81   VAL C CG1 1 
ATOM   2824  C  CG2 . VAL C  1 82  ? 117.910 -10.853 5.762  1.00 36.66 ? 81   VAL C CG2 1 
ATOM   2825  N  N   . GLY C  1 83  ? 118.690 -10.738 10.265 1.00 34.37 ? 82   GLY C N   1 
ATOM   2826  C  CA  . GLY C  1 83  ? 118.572 -10.260 11.634 1.00 35.29 ? 82   GLY C CA  1 
ATOM   2827  C  C   . GLY C  1 83  ? 119.815 -10.261 12.515 1.00 35.29 ? 82   GLY C C   1 
ATOM   2828  O  O   . GLY C  1 83  ? 119.713 -9.962  13.707 1.00 34.83 ? 82   GLY C O   1 
ATOM   2829  N  N   . ASP C  1 84  ? 120.980 -10.574 11.951 1.00 35.17 ? 83   ASP C N   1 
ATOM   2830  C  CA  . ASP C  1 84  ? 122.212 -10.622 12.738 1.00 34.19 ? 83   ASP C CA  1 
ATOM   2831  C  C   . ASP C  1 84  ? 122.801 -9.248  13.018 1.00 34.98 ? 83   ASP C C   1 
ATOM   2832  O  O   . ASP C  1 84  ? 123.544 -8.694  12.200 1.00 35.91 ? 83   ASP C O   1 
ATOM   2833  C  CB  . ASP C  1 84  ? 123.258 -11.482 12.034 1.00 35.02 ? 83   ASP C CB  1 
ATOM   2834  C  CG  . ASP C  1 84  ? 122.871 -12.945 11.984 1.00 35.53 ? 83   ASP C CG  1 
ATOM   2835  O  OD1 . ASP C  1 84  ? 122.050 -13.363 12.828 1.00 39.00 ? 83   ASP C OD1 1 
ATOM   2836  O  OD2 . ASP C  1 84  ? 123.403 -13.677 11.117 1.00 34.73 ? 83   ASP C OD2 1 
ATOM   2837  N  N   . LEU C  1 85  ? 122.470 -8.697  14.179 1.00 32.23 ? 84   LEU C N   1 
ATOM   2838  C  CA  . LEU C  1 85  ? 122.968 -7.385  14.557 1.00 33.87 ? 84   LEU C CA  1 
ATOM   2839  C  C   . LEU C  1 85  ? 124.164 -7.399  15.511 1.00 35.26 ? 84   LEU C C   1 
ATOM   2840  O  O   . LEU C  1 85  ? 124.492 -6.380  16.116 1.00 35.64 ? 84   LEU C O   1 
ATOM   2841  C  CB  . LEU C  1 85  ? 121.827 -6.536  15.133 1.00 34.13 ? 84   LEU C CB  1 
ATOM   2842  C  CG  . LEU C  1 85  ? 120.652 -6.329  14.165 1.00 34.56 ? 84   LEU C CG  1 
ATOM   2843  C  CD1 . LEU C  1 85  ? 119.659 -5.350  14.775 1.00 33.82 ? 84   LEU C CD1 1 
ATOM   2844  C  CD2 . LEU C  1 85  ? 121.168 -5.803  12.828 1.00 32.31 ? 84   LEU C CD2 1 
ATOM   2845  N  N   . GLY C  1 86  ? 124.813 -8.552  15.639 1.00 34.28 ? 85   GLY C N   1 
ATOM   2846  C  CA  . GLY C  1 86  ? 125.994 -8.657  16.486 1.00 35.85 ? 85   GLY C CA  1 
ATOM   2847  C  C   . GLY C  1 86  ? 125.882 -8.644  18.009 1.00 36.83 ? 85   GLY C C   1 
ATOM   2848  O  O   . GLY C  1 86  ? 125.066 -9.370  18.601 1.00 38.01 ? 85   GLY C O   1 
ATOM   2849  N  N   . ASN C  1 87  ? 126.714 -7.808  18.637 1.00 35.51 ? 86   ASN C N   1 
ATOM   2850  C  CA  . ASN C  1 87  ? 126.774 -7.699  20.094 1.00 35.42 ? 86   ASN C CA  1 
ATOM   2851  C  C   . ASN C  1 87  ? 126.638 -6.290  20.667 1.00 34.36 ? 86   ASN C C   1 
ATOM   2852  O  O   . ASN C  1 87  ? 127.173 -5.329  20.113 1.00 35.06 ? 86   ASN C O   1 
ATOM   2853  C  CB  . ASN C  1 87  ? 128.112 -8.250  20.593 1.00 37.64 ? 86   ASN C CB  1 
ATOM   2854  C  CG  . ASN C  1 87  ? 128.208 -9.752  20.495 1.00 39.14 ? 86   ASN C CG  1 
ATOM   2855  O  OD1 . ASN C  1 87  ? 127.589 -10.474 21.275 1.00 38.57 ? 86   ASN C OD1 1 
ATOM   2856  N  ND2 . ASN C  1 87  ? 128.996 -10.236 19.540 1.00 39.72 ? 86   ASN C ND2 1 
ATOM   2857  N  N   . VAL C  1 88  ? 125.946 -6.181  21.799 1.00 33.46 ? 87   VAL C N   1 
ATOM   2858  C  CA  . VAL C  1 88  ? 125.804 -4.901  22.489 1.00 34.64 ? 87   VAL C CA  1 
ATOM   2859  C  C   . VAL C  1 88  ? 126.676 -5.016  23.747 1.00 34.65 ? 87   VAL C C   1 
ATOM   2860  O  O   . VAL C  1 88  ? 126.937 -6.120  24.220 1.00 33.69 ? 87   VAL C O   1 
ATOM   2861  C  CB  . VAL C  1 88  ? 124.328 -4.605  22.858 1.00 35.50 ? 87   VAL C CB  1 
ATOM   2862  C  CG1 . VAL C  1 88  ? 123.541 -4.262  21.583 1.00 34.61 ? 87   VAL C CG1 1 
ATOM   2863  C  CG2 . VAL C  1 88  ? 123.702 -5.810  23.550 1.00 34.57 ? 87   VAL C CG2 1 
ATOM   2864  N  N   . THR C  1 89  ? 127.128 -3.890  24.286 1.00 36.29 ? 88   THR C N   1 
ATOM   2865  C  CA  . THR C  1 89  ? 128.010 -3.923  25.448 1.00 36.97 ? 88   THR C CA  1 
ATOM   2866  C  C   . THR C  1 89  ? 127.438 -3.346  26.733 1.00 38.95 ? 88   THR C C   1 
ATOM   2867  O  O   . THR C  1 89  ? 127.080 -2.167  26.797 1.00 39.92 ? 88   THR C O   1 
ATOM   2868  C  CB  . THR C  1 89  ? 129.331 -3.188  25.127 1.00 38.37 ? 88   THR C CB  1 
ATOM   2869  O  OG1 . THR C  1 89  ? 129.943 -3.804  23.988 1.00 33.73 ? 88   THR C OG1 1 
ATOM   2870  C  CG2 . THR C  1 89  ? 130.288 -3.237  26.323 1.00 38.76 ? 88   THR C CG2 1 
ATOM   2871  N  N   . ALA C  1 90  ? 127.369 -4.183  27.764 1.00 40.12 ? 89   ALA C N   1 
ATOM   2872  C  CA  . ALA C  1 90  ? 126.859 -3.747  29.057 1.00 41.95 ? 89   ALA C CA  1 
ATOM   2873  C  C   . ALA C  1 90  ? 128.030 -3.359  29.951 1.00 42.51 ? 89   ALA C C   1 
ATOM   2874  O  O   . ALA C  1 90  ? 128.983 -4.125  30.111 1.00 41.74 ? 89   ALA C O   1 
ATOM   2875  C  CB  . ALA C  1 90  ? 126.045 -4.858  29.707 1.00 40.55 ? 89   ALA C CB  1 
ATOM   2876  N  N   . ASP C  1 91  ? 127.952 -2.163  30.524 1.00 44.95 ? 90   ASP C N   1 
ATOM   2877  C  CA  . ASP C  1 91  ? 128.996 -1.662  31.404 1.00 47.17 ? 90   ASP C CA  1 
ATOM   2878  C  C   . ASP C  1 91  ? 128.910 -2.328  32.777 1.00 49.06 ? 90   ASP C C   1 
ATOM   2879  O  O   . ASP C  1 91  ? 128.064 -3.197  33.002 1.00 47.87 ? 90   ASP C O   1 
ATOM   2880  C  CB  . ASP C  1 91  ? 128.886 -0.138  31.536 1.00 46.46 ? 90   ASP C CB  1 
ATOM   2881  C  CG  . ASP C  1 91  ? 127.600 0.304   32.207 1.00 45.78 ? 90   ASP C CG  1 
ATOM   2882  O  OD1 . ASP C  1 91  ? 127.298 1.515   32.165 1.00 44.69 ? 90   ASP C OD1 1 
ATOM   2883  O  OD2 . ASP C  1 91  ? 126.895 -0.548  32.785 1.00 46.66 ? 90   ASP C OD2 1 
ATOM   2884  N  N   . LYS C  1 92  ? 129.785 -1.918  33.691 1.00 50.44 ? 91   LYS C N   1 
ATOM   2885  C  CA  . LYS C  1 92  ? 129.810 -2.499  35.028 1.00 52.90 ? 91   LYS C CA  1 
ATOM   2886  C  C   . LYS C  1 92  ? 128.448 -2.434  35.711 1.00 54.03 ? 91   LYS C C   1 
ATOM   2887  O  O   . LYS C  1 92  ? 128.082 -3.334  36.470 1.00 54.53 ? 91   LYS C O   1 
ATOM   2888  C  CB  . LYS C  1 92  ? 130.860 -1.797  35.898 1.00 53.24 ? 91   LYS C CB  1 
ATOM   2889  C  CG  . LYS C  1 92  ? 130.538 -0.350  36.235 1.00 53.77 ? 91   LYS C CG  1 
ATOM   2890  C  CD  . LYS C  1 92  ? 131.537 0.212   37.232 0.00 53.90 ? 91   LYS C CD  1 
ATOM   2891  C  CE  . LYS C  1 92  ? 131.171 1.627   37.647 0.00 54.05 ? 91   LYS C CE  1 
ATOM   2892  N  NZ  . LYS C  1 92  ? 132.113 2.165   38.668 0.00 54.14 ? 91   LYS C NZ  1 
ATOM   2893  N  N   . ASP C  1 93  ? 127.698 -1.372  35.434 1.00 54.77 ? 92   ASP C N   1 
ATOM   2894  C  CA  . ASP C  1 93  ? 126.380 -1.199  36.030 1.00 55.25 ? 92   ASP C CA  1 
ATOM   2895  C  C   . ASP C  1 93  ? 125.297 -1.998  35.306 1.00 54.55 ? 92   ASP C C   1 
ATOM   2896  O  O   . ASP C  1 93  ? 124.118 -1.909  35.652 1.00 54.79 ? 92   ASP C O   1 
ATOM   2897  C  CB  . ASP C  1 93  ? 126.005 0.285   36.054 1.00 57.35 ? 92   ASP C CB  1 
ATOM   2898  C  CG  . ASP C  1 93  ? 126.964 1.115   36.892 1.00 59.60 ? 92   ASP C CG  1 
ATOM   2899  O  OD1 . ASP C  1 93  ? 127.252 0.713   38.040 1.00 59.60 ? 92   ASP C OD1 1 
ATOM   2900  O  OD2 . ASP C  1 93  ? 127.425 2.171   36.408 1.00 61.00 ? 92   ASP C OD2 1 
ATOM   2901  N  N   . GLY C  1 94  ? 125.700 -2.779  34.307 1.00 52.12 ? 93   GLY C N   1 
ATOM   2902  C  CA  . GLY C  1 94  ? 124.751 -3.587  33.560 1.00 50.87 ? 93   GLY C CA  1 
ATOM   2903  C  C   . GLY C  1 94  ? 123.979 -2.825  32.496 1.00 50.20 ? 93   GLY C C   1 
ATOM   2904  O  O   . GLY C  1 94  ? 122.988 -3.328  31.962 1.00 48.99 ? 93   GLY C O   1 
ATOM   2905  N  N   . VAL C  1 95  ? 124.433 -1.616  32.179 1.00 48.46 ? 94   VAL C N   1 
ATOM   2906  C  CA  . VAL C  1 95  ? 123.768 -0.790  31.177 1.00 47.84 ? 94   VAL C CA  1 
ATOM   2907  C  C   . VAL C  1 95  ? 124.501 -0.789  29.835 1.00 48.93 ? 94   VAL C C   1 
ATOM   2908  O  O   . VAL C  1 95  ? 125.718 -0.589  29.770 1.00 47.65 ? 94   VAL C O   1 
ATOM   2909  C  CB  . VAL C  1 95  ? 123.625 0.664   31.674 1.00 47.72 ? 94   VAL C CB  1 
ATOM   2910  C  CG1 . VAL C  1 95  ? 122.941 1.518   30.617 1.00 46.93 ? 94   VAL C CG1 1 
ATOM   2911  C  CG2 . VAL C  1 95  ? 122.830 0.685   32.972 1.00 46.23 ? 94   VAL C CG2 1 
ATOM   2912  N  N   . ALA C  1 96  ? 123.745 -1.019  28.766 1.00 48.45 ? 95   ALA C N   1 
ATOM   2913  C  CA  . ALA C  1 96  ? 124.301 -1.051  27.420 1.00 48.18 ? 95   ALA C CA  1 
ATOM   2914  C  C   . ALA C  1 96  ? 123.725 0.074   26.566 1.00 48.94 ? 95   ALA C C   1 
ATOM   2915  O  O   . ALA C  1 96  ? 122.513 0.137   26.342 1.00 48.13 ? 95   ALA C O   1 
ATOM   2916  C  CB  . ALA C  1 96  ? 124.010 -2.399  26.769 1.00 47.16 ? 95   ALA C CB  1 
ATOM   2917  N  N   . ASP C  1 97  ? 124.597 0.966   26.103 1.00 48.51 ? 96   ASP C N   1 
ATOM   2918  C  CA  . ASP C  1 97  ? 124.187 2.083   25.256 1.00 49.59 ? 96   ASP C CA  1 
ATOM   2919  C  C   . ASP C  1 97  ? 124.298 1.635   23.801 1.00 49.62 ? 96   ASP C C   1 
ATOM   2920  O  O   . ASP C  1 97  ? 125.390 1.617   23.229 1.00 49.50 ? 96   ASP C O   1 
ATOM   2921  C  CB  . ASP C  1 97  ? 125.087 3.296   25.499 1.00 52.16 ? 96   ASP C CB  1 
ATOM   2922  C  CG  . ASP C  1 97  ? 124.861 3.930   26.865 1.00 56.37 ? 96   ASP C CG  1 
ATOM   2923  O  OD1 . ASP C  1 97  ? 125.650 4.825   27.244 1.00 58.49 ? 96   ASP C OD1 1 
ATOM   2924  O  OD2 . ASP C  1 97  ? 123.893 3.544   27.557 1.00 58.31 ? 96   ASP C OD2 1 
ATOM   2925  N  N   . VAL C  1 98  ? 123.165 1.269   23.209 1.00 47.09 ? 97   VAL C N   1 
ATOM   2926  C  CA  . VAL C  1 98  ? 123.142 0.794   21.830 1.00 44.77 ? 97   VAL C CA  1 
ATOM   2927  C  C   . VAL C  1 98  ? 123.153 1.924   20.805 1.00 43.24 ? 97   VAL C C   1 
ATOM   2928  O  O   . VAL C  1 98  ? 122.415 2.902   20.925 1.00 41.20 ? 97   VAL C O   1 
ATOM   2929  C  CB  . VAL C  1 98  ? 121.899 -0.088  21.570 1.00 46.27 ? 97   VAL C CB  1 
ATOM   2930  C  CG1 . VAL C  1 98  ? 121.973 -0.689  20.175 1.00 44.26 ? 97   VAL C CG1 1 
ATOM   2931  C  CG2 . VAL C  1 98  ? 121.804 -1.183  22.626 1.00 45.08 ? 97   VAL C CG2 1 
ATOM   2932  N  N   . SER C  1 99  ? 124.001 1.777   19.795 1.00 42.70 ? 98   SER C N   1 
ATOM   2933  C  CA  . SER C  1 99  ? 124.112 2.766   18.729 1.00 42.80 ? 98   SER C CA  1 
ATOM   2934  C  C   . SER C  1 99  ? 124.725 2.069   17.528 1.00 42.79 ? 98   SER C C   1 
ATOM   2935  O  O   . SER C  1 99  ? 125.946 2.004   17.381 1.00 41.53 ? 98   SER C O   1 
ATOM   2936  C  CB  . SER C  1 99  ? 124.990 3.939   19.161 1.00 43.18 ? 98   SER C CB  1 
ATOM   2937  O  OG  . SER C  1 99  ? 125.003 4.940   18.157 1.00 45.57 ? 98   SER C OG  1 
ATOM   2938  N  N   . ILE C  1 100 ? 123.852 1.548   16.677 1.00 42.25 ? 99   ILE C N   1 
ATOM   2939  C  CA  . ILE C  1 100 ? 124.247 0.809   15.489 1.00 41.15 ? 99   ILE C CA  1 
ATOM   2940  C  C   . ILE C  1 100 ? 123.675 1.443   14.228 1.00 41.38 ? 99   ILE C C   1 
ATOM   2941  O  O   . ILE C  1 100 ? 122.741 2.251   14.282 1.00 38.18 ? 99   ILE C O   1 
ATOM   2942  C  CB  . ILE C  1 100 ? 123.720 -0.643  15.564 1.00 41.79 ? 99   ILE C CB  1 
ATOM   2943  C  CG1 . ILE C  1 100 ? 124.234 -1.317  16.835 1.00 43.36 ? 99   ILE C CG1 1 
ATOM   2944  C  CG2 . ILE C  1 100 ? 124.140 -1.431  14.333 1.00 42.73 ? 99   ILE C CG2 1 
ATOM   2945  C  CD1 . ILE C  1 100 ? 123.626 -2.682  17.082 1.00 43.68 ? 99   ILE C CD1 1 
ATOM   2946  N  N   . GLU C  1 101 ? 124.264 1.072   13.096 1.00 41.62 ? 100  GLU C N   1 
ATOM   2947  C  CA  . GLU C  1 101 ? 123.822 1.522   11.785 1.00 42.25 ? 100  GLU C CA  1 
ATOM   2948  C  C   . GLU C  1 101 ? 123.966 0.271   10.945 1.00 39.51 ? 100  GLU C C   1 
ATOM   2949  O  O   . GLU C  1 101 ? 125.030 -0.336  10.918 1.00 39.21 ? 100  GLU C O   1 
ATOM   2950  C  CB  . GLU C  1 101 ? 124.714 2.640   11.237 1.00 45.16 ? 100  GLU C CB  1 
ATOM   2951  C  CG  . GLU C  1 101 ? 124.174 3.246   9.950  1.00 49.41 ? 100  GLU C CG  1 
ATOM   2952  C  CD  . GLU C  1 101 ? 124.883 4.526   9.553  1.00 53.19 ? 100  GLU C CD  1 
ATOM   2953  O  OE1 . GLU C  1 101 ? 124.437 5.170   8.579  1.00 53.79 ? 100  GLU C OE1 1 
ATOM   2954  O  OE2 . GLU C  1 101 ? 125.883 4.889   10.211 1.00 54.65 ? 100  GLU C OE2 1 
ATOM   2955  N  N   . ASP C  1 102 ? 122.889 -0.130  10.283 1.00 37.83 ? 101  ASP C N   1 
ATOM   2956  C  CA  . ASP C  1 102 ? 122.916 -1.342  9.476  1.00 36.99 ? 101  ASP C CA  1 
ATOM   2957  C  C   . ASP C  1 102 ? 122.222 -1.138  8.131  1.00 38.78 ? 101  ASP C C   1 
ATOM   2958  O  O   . ASP C  1 102 ? 121.195 -0.462  8.046  1.00 38.30 ? 101  ASP C O   1 
ATOM   2959  C  CB  . ASP C  1 102 ? 122.243 -2.470  10.259 1.00 34.62 ? 101  ASP C CB  1 
ATOM   2960  C  CG  . ASP C  1 102 ? 122.465 -3.826  9.637  1.00 31.04 ? 101  ASP C CG  1 
ATOM   2961  O  OD1 . ASP C  1 102 ? 121.586 -4.289  8.885  1.00 31.43 ? 101  ASP C OD1 1 
ATOM   2962  O  OD2 . ASP C  1 102 ? 123.526 -4.426  9.906  1.00 30.22 ? 101  ASP C OD2 1 
ATOM   2963  N  N   . SER C  1 103 ? 122.788 -1.737  7.089  1.00 40.72 ? 102  SER C N   1 
ATOM   2964  C  CA  . SER C  1 103 ? 122.249 -1.616  5.739  1.00 42.70 ? 102  SER C CA  1 
ATOM   2965  C  C   . SER C  1 103 ? 121.681 -2.914  5.182  1.00 41.60 ? 102  SER C C   1 
ATOM   2966  O  O   . SER C  1 103 ? 121.472 -3.029  3.980  1.00 41.82 ? 102  SER C O   1 
ATOM   2967  C  CB  . SER C  1 103 ? 123.332 -1.103  4.783  1.00 44.33 ? 102  SER C CB  1 
ATOM   2968  O  OG  . SER C  1 103 ? 123.706 0.226   5.100  1.00 50.72 ? 102  SER C OG  1 
ATOM   2969  N  N   . VAL C  1 104 ? 121.437 -3.895  6.043  1.00 40.97 ? 103  VAL C N   1 
ATOM   2970  C  CA  . VAL C  1 104 ? 120.885 -5.162  5.575  1.00 38.42 ? 103  VAL C CA  1 
ATOM   2971  C  C   . VAL C  1 104 ? 119.439 -5.302  6.029  1.00 39.54 ? 103  VAL C C   1 
ATOM   2972  O  O   . VAL C  1 104 ? 118.605 -5.868  5.317  1.00 40.55 ? 103  VAL C O   1 
ATOM   2973  C  CB  . VAL C  1 104 ? 121.696 -6.354  6.097  1.00 38.36 ? 103  VAL C CB  1 
ATOM   2974  C  CG1 . VAL C  1 104 ? 121.085 -7.660  5.595  1.00 36.75 ? 103  VAL C CG1 1 
ATOM   2975  C  CG2 . VAL C  1 104 ? 123.135 -6.232  5.629  1.00 37.69 ? 103  VAL C CG2 1 
ATOM   2976  N  N   . ILE C  1 105 ? 119.141 -4.804  7.225  1.00 37.42 ? 104  ILE C N   1 
ATOM   2977  C  CA  . ILE C  1 105 ? 117.773 -4.864  7.719  1.00 37.25 ? 104  ILE C CA  1 
ATOM   2978  C  C   . ILE C  1 105 ? 117.054 -3.654  7.149  1.00 36.56 ? 104  ILE C C   1 
ATOM   2979  O  O   . ILE C  1 105 ? 117.680 -2.644  6.837  1.00 34.56 ? 104  ILE C O   1 
ATOM   2980  C  CB  . ILE C  1 105 ? 117.680 -4.771  9.263  1.00 36.76 ? 104  ILE C CB  1 
ATOM   2981  C  CG1 . ILE C  1 105 ? 118.368 -3.495  9.749  1.00 38.68 ? 104  ILE C CG1 1 
ATOM   2982  C  CG2 . ILE C  1 105 ? 118.262 -6.007  9.897  1.00 38.13 ? 104  ILE C CG2 1 
ATOM   2983  C  CD1 . ILE C  1 105 ? 118.224 -3.254  11.240 1.00 36.56 ? 104  ILE C CD1 1 
ATOM   2984  N  N   . SER C  1 106 ? 115.738 -3.758  7.021  1.00 34.85 ? 105  SER C N   1 
ATOM   2985  C  CA  . SER C  1 106 ? 114.944 -2.657  6.514  1.00 33.45 ? 105  SER C CA  1 
ATOM   2986  C  C   . SER C  1 106 ? 113.615 -2.602  7.243  1.00 31.31 ? 105  SER C C   1 
ATOM   2987  O  O   . SER C  1 106 ? 113.165 -3.601  7.803  1.00 32.57 ? 105  SER C O   1 
ATOM   2988  C  CB  . SER C  1 106 ? 114.721 -2.783  5.002  1.00 34.10 ? 105  SER C CB  1 
ATOM   2989  O  OG  . SER C  1 106 ? 114.121 -1.588  4.522  1.00 34.75 ? 105  SER C OG  1 
ATOM   2990  N  N   . LEU C  1 107 ? 113.015 -1.417  7.250  1.00 31.52 ? 106  LEU C N   1 
ATOM   2991  C  CA  . LEU C  1 107 ? 111.745 -1.200  7.914  1.00 31.40 ? 106  LEU C CA  1 
ATOM   2992  C  C   . LEU C  1 107 ? 110.588 -1.229  6.921  1.00 33.24 ? 106  LEU C C   1 
ATOM   2993  O  O   . LEU C  1 107 ? 109.453 -0.921  7.273  1.00 34.29 ? 106  LEU C O   1 
ATOM   2994  C  CB  . LEU C  1 107 ? 111.760 0.140   8.655  1.00 29.24 ? 106  LEU C CB  1 
ATOM   2995  C  CG  . LEU C  1 107 ? 112.844 0.362   9.720  1.00 29.24 ? 106  LEU C CG  1 
ATOM   2996  C  CD1 . LEU C  1 107 ? 112.549 1.642   10.489 1.00 26.39 ? 106  LEU C CD1 1 
ATOM   2997  C  CD2 . LEU C  1 107 ? 112.885 -0.815  10.678 1.00 27.20 ? 106  LEU C CD2 1 
ATOM   2998  N  N   . SER C  1 108 ? 110.877 -1.589  5.676  1.00 35.43 ? 107  SER C N   1 
ATOM   2999  C  CA  . SER C  1 108 ? 109.840 -1.664  4.654  1.00 37.08 ? 107  SER C CA  1 
ATOM   3000  C  C   . SER C  1 108 ? 110.257 -2.670  3.606  1.00 37.63 ? 107  SER C C   1 
ATOM   3001  O  O   . SER C  1 108 ? 111.342 -3.249  3.681  1.00 35.77 ? 107  SER C O   1 
ATOM   3002  C  CB  . SER C  1 108 ? 109.620 -0.298  3.992  1.00 37.40 ? 107  SER C CB  1 
ATOM   3003  O  OG  . SER C  1 108 ? 110.753 0.101   3.241  1.00 40.44 ? 107  SER C OG  1 
ATOM   3004  N  N   . GLY C  1 109 ? 109.384 -2.881  2.630  1.00 38.08 ? 108  GLY C N   1 
ATOM   3005  C  CA  . GLY C  1 109 ? 109.692 -3.823  1.579  1.00 40.23 ? 108  GLY C CA  1 
ATOM   3006  C  C   . GLY C  1 109 ? 109.267 -5.230  1.937  1.00 41.55 ? 108  GLY C C   1 
ATOM   3007  O  O   . GLY C  1 109 ? 108.770 -5.494  3.034  1.00 42.58 ? 108  GLY C O   1 
ATOM   3008  N  N   . ASP C  1 110 ? 109.483 -6.140  1.001  1.00 42.99 ? 109  ASP C N   1 
ATOM   3009  C  CA  . ASP C  1 110 ? 109.113 -7.533  1.164  1.00 44.96 ? 109  ASP C CA  1 
ATOM   3010  C  C   . ASP C  1 110 ? 109.804 -8.210  2.369  1.00 45.00 ? 109  ASP C C   1 
ATOM   3011  O  O   . ASP C  1 110 ? 109.271 -9.185  2.911  1.00 45.18 ? 109  ASP C O   1 
ATOM   3012  C  CB  . ASP C  1 110 ? 109.447 -8.286  -0.128 1.00 49.31 ? 109  ASP C CB  1 
ATOM   3013  C  CG  . ASP C  1 110 ? 108.650 -9.559  -0.288 1.00 52.37 ? 109  ASP C CG  1 
ATOM   3014  O  OD1 . ASP C  1 110 ? 109.061 -10.413 -1.103 1.00 56.16 ? 109  ASP C OD1 1 
ATOM   3015  O  OD2 . ASP C  1 110 ? 107.610 -9.708  0.388  1.00 54.35 ? 109  ASP C OD2 1 
ATOM   3016  N  N   . HIS C  1 111 ? 110.964 -7.698  2.797  1.00 43.68 ? 110  HIS C N   1 
ATOM   3017  C  CA  . HIS C  1 111 ? 111.705 -8.290  3.922  1.00 41.85 ? 110  HIS C CA  1 
ATOM   3018  C  C   . HIS C  1 111 ? 111.855 -7.377  5.150  1.00 40.16 ? 110  HIS C C   1 
ATOM   3019  O  O   . HIS C  1 111 ? 112.910 -7.363  5.803  1.00 40.18 ? 110  HIS C O   1 
ATOM   3020  C  CB  . HIS C  1 111 ? 113.086 -8.714  3.430  1.00 43.53 ? 110  HIS C CB  1 
ATOM   3021  C  CG  . HIS C  1 111 ? 113.045 -9.838  2.450  1.00 45.91 ? 110  HIS C CG  1 
ATOM   3022  N  ND1 . HIS C  1 111 ? 114.130 -10.198 1.668  1.00 46.45 ? 110  HIS C ND1 1 
ATOM   3023  C  CD2 . HIS C  1 111 ? 112.039 -10.667 2.090  1.00 47.69 ? 110  HIS C CD2 1 
ATOM   3024  C  CE1 . HIS C  1 111 ? 113.785 -11.185 0.876  1.00 47.34 ? 110  HIS C CE1 1 
ATOM   3025  N  NE2 . HIS C  1 111 ? 112.522 -11.497 1.103  1.00 47.26 ? 110  HIS C NE2 1 
ATOM   3026  N  N   . SER C  1 112 ? 110.814 -6.604  5.443  1.00 36.55 ? 111  SER C N   1 
ATOM   3027  C  CA  . SER C  1 112 ? 110.824 -5.699  6.584  1.00 34.47 ? 111  SER C CA  1 
ATOM   3028  C  C   . SER C  1 112 ? 110.904 -6.497  7.887  1.00 32.33 ? 111  SER C C   1 
ATOM   3029  O  O   . SER C  1 112 ? 110.444 -7.641  7.958  1.00 29.92 ? 111  SER C O   1 
ATOM   3030  C  CB  . SER C  1 112 ? 109.537 -4.887  6.572  1.00 33.03 ? 111  SER C CB  1 
ATOM   3031  O  OG  . SER C  1 112 ? 109.468 -3.975  7.645  1.00 31.63 ? 111  SER C OG  1 
ATOM   3032  N  N   . ILE C  1 113 ? 111.480 -5.882  8.914  1.00 31.19 ? 112  ILE C N   1 
ATOM   3033  C  CA  . ILE C  1 113 ? 111.587 -6.527  10.214 1.00 32.39 ? 112  ILE C CA  1 
ATOM   3034  C  C   . ILE C  1 113 ? 110.415 -6.089  11.091 1.00 31.08 ? 112  ILE C C   1 
ATOM   3035  O  O   . ILE C  1 113 ? 110.305 -6.506  12.243 1.00 30.49 ? 112  ILE C O   1 
ATOM   3036  C  CB  . ILE C  1 113 ? 112.908 -6.167  10.917 1.00 30.43 ? 112  ILE C CB  1 
ATOM   3037  C  CG1 . ILE C  1 113 ? 113.035 -4.652  11.058 1.00 32.86 ? 112  ILE C CG1 1 
ATOM   3038  C  CG2 . ILE C  1 113 ? 114.087 -6.736  10.128 1.00 32.73 ? 112  ILE C CG2 1 
ATOM   3039  C  CD1 . ILE C  1 113 ? 114.296 -4.217  11.791 1.00 32.65 ? 112  ILE C CD1 1 
ATOM   3040  N  N   . ILE C  1 114 ? 109.552 -5.236  10.540 1.00 29.95 ? 113  ILE C N   1 
ATOM   3041  C  CA  . ILE C  1 114 ? 108.382 -4.760  11.269 1.00 28.07 ? 113  ILE C CA  1 
ATOM   3042  C  C   . ILE C  1 114 ? 107.505 -5.962  11.602 1.00 26.19 ? 113  ILE C C   1 
ATOM   3043  O  O   . ILE C  1 114 ? 107.218 -6.791  10.736 1.00 23.22 ? 113  ILE C O   1 
ATOM   3044  C  CB  . ILE C  1 114 ? 107.554 -3.767  10.426 1.00 29.83 ? 113  ILE C CB  1 
ATOM   3045  C  CG1 . ILE C  1 114 ? 108.383 -2.517  10.118 1.00 30.69 ? 113  ILE C CG1 1 
ATOM   3046  C  CG2 . ILE C  1 114 ? 106.287 -3.365  11.183 1.00 29.93 ? 113  ILE C CG2 1 
ATOM   3047  C  CD1 . ILE C  1 114 ? 108.744 -1.705  11.339 1.00 32.19 ? 113  ILE C CD1 1 
ATOM   3048  N  N   . GLY C  1 115 ? 107.094 -6.063  12.861 1.00 25.52 ? 114  GLY C N   1 
ATOM   3049  C  CA  . GLY C  1 115 ? 106.246 -7.168  13.266 1.00 23.59 ? 114  GLY C CA  1 
ATOM   3050  C  C   . GLY C  1 115 ? 107.019 -8.400  13.676 1.00 25.44 ? 114  GLY C C   1 
ATOM   3051  O  O   . GLY C  1 115 ? 106.430 -9.424  14.020 1.00 25.72 ? 114  GLY C O   1 
ATOM   3052  N  N   . ARG C  1 116 ? 108.342 -8.317  13.624 1.00 25.12 ? 115  ARG C N   1 
ATOM   3053  C  CA  . ARG C  1 116 ? 109.167 -9.449  14.020 1.00 26.00 ? 115  ARG C CA  1 
ATOM   3054  C  C   . ARG C  1 116 ? 109.690 -9.160  15.427 1.00 25.41 ? 115  ARG C C   1 
ATOM   3055  O  O   . ARG C  1 116 ? 109.261 -8.185  16.047 1.00 25.56 ? 115  ARG C O   1 
ATOM   3056  C  CB  . ARG C  1 116 ? 110.282 -9.668  12.987 1.00 26.20 ? 115  ARG C CB  1 
ATOM   3057  C  CG  . ARG C  1 116 ? 109.682 -9.926  11.588 1.00 28.10 ? 115  ARG C CG  1 
ATOM   3058  C  CD  . ARG C  1 116 ? 110.695 -10.318 10.512 1.00 29.95 ? 115  ARG C CD  1 
ATOM   3059  N  NE  . ARG C  1 116 ? 110.043 -10.495 9.209  1.00 27.37 ? 115  ARG C NE  1 
ATOM   3060  C  CZ  . ARG C  1 116 ? 109.255 -11.520 8.886  1.00 27.85 ? 115  ARG C CZ  1 
ATOM   3061  N  NH1 . ARG C  1 116 ? 108.705 -11.583 7.682  1.00 29.72 ? 115  ARG C NH1 1 
ATOM   3062  N  NH2 . ARG C  1 116 ? 109.022 -12.495 9.753  1.00 30.05 ? 115  ARG C NH2 1 
ATOM   3063  N  N   . THR C  1 117 ? 110.597 -9.986  15.940 1.00 26.47 ? 116  THR C N   1 
ATOM   3064  C  CA  . THR C  1 117 ? 111.086 -9.801  17.310 1.00 27.92 ? 116  THR C CA  1 
ATOM   3065  C  C   . THR C  1 117 ? 112.572 -9.492  17.499 1.00 29.12 ? 116  THR C C   1 
ATOM   3066  O  O   . THR C  1 117 ? 113.431 -10.171 16.939 1.00 29.07 ? 116  THR C O   1 
ATOM   3067  C  CB  . THR C  1 117 ? 110.760 -11.056 18.168 1.00 28.92 ? 116  THR C CB  1 
ATOM   3068  O  OG1 . THR C  1 117 ? 109.339 -11.259 18.202 1.00 28.18 ? 116  THR C OG1 1 
ATOM   3069  C  CG2 . THR C  1 117 ? 111.284 -10.893 19.602 1.00 28.56 ? 116  THR C CG2 1 
ATOM   3070  N  N   . LEU C  1 118 ? 112.859 -8.465  18.297 1.00 28.87 ? 117  LEU C N   1 
ATOM   3071  C  CA  . LEU C  1 118 ? 114.239 -8.096  18.613 1.00 29.47 ? 117  LEU C CA  1 
ATOM   3072  C  C   . LEU C  1 118 ? 114.554 -8.817  19.917 1.00 32.60 ? 117  LEU C C   1 
ATOM   3073  O  O   . LEU C  1 118 ? 113.780 -8.729  20.880 1.00 29.46 ? 117  LEU C O   1 
ATOM   3074  C  CB  . LEU C  1 118 ? 114.382 -6.591  18.823 1.00 27.80 ? 117  LEU C CB  1 
ATOM   3075  C  CG  . LEU C  1 118 ? 115.811 -6.151  19.165 1.00 28.61 ? 117  LEU C CG  1 
ATOM   3076  C  CD1 . LEU C  1 118 ? 116.761 -6.545  18.034 1.00 25.29 ? 117  LEU C CD1 1 
ATOM   3077  C  CD2 . LEU C  1 118 ? 115.844 -4.655  19.401 1.00 26.85 ? 117  LEU C CD2 1 
ATOM   3078  N  N   . VAL C  1 119 ? 115.684 -9.521  19.943 1.00 33.69 ? 118  VAL C N   1 
ATOM   3079  C  CA  . VAL C  1 119 ? 116.098 -10.293 21.111 1.00 35.06 ? 118  VAL C CA  1 
ATOM   3080  C  C   . VAL C  1 119 ? 117.526 -10.013 21.587 1.00 37.06 ? 118  VAL C C   1 
ATOM   3081  O  O   . VAL C  1 119 ? 118.456 -9.942  20.780 1.00 35.85 ? 118  VAL C O   1 
ATOM   3082  C  CB  . VAL C  1 119 ? 116.007 -11.806 20.812 1.00 35.91 ? 118  VAL C CB  1 
ATOM   3083  C  CG1 . VAL C  1 119 ? 116.449 -12.606 22.030 1.00 36.17 ? 118  VAL C CG1 1 
ATOM   3084  C  CG2 . VAL C  1 119 ? 114.590 -12.174 20.402 1.00 35.10 ? 118  VAL C CG2 1 
ATOM   3085  N  N   . VAL C  1 120 ? 117.689 -9.857  22.900 1.00 37.63 ? 119  VAL C N   1 
ATOM   3086  C  CA  . VAL C  1 120 ? 119.005 -9.645  23.493 1.00 38.15 ? 119  VAL C CA  1 
ATOM   3087  C  C   . VAL C  1 120 ? 119.310 -10.933 24.254 1.00 39.06 ? 119  VAL C C   1 
ATOM   3088  O  O   . VAL C  1 120 ? 118.488 -11.420 25.032 1.00 39.07 ? 119  VAL C O   1 
ATOM   3089  C  CB  . VAL C  1 120 ? 119.028 -8.434  24.444 1.00 37.78 ? 119  VAL C CB  1 
ATOM   3090  C  CG1 . VAL C  1 120 ? 118.055 -8.638  25.586 1.00 38.80 ? 119  VAL C CG1 1 
ATOM   3091  C  CG2 . VAL C  1 120 ? 120.443 -8.225  24.968 1.00 38.04 ? 119  VAL C CG2 1 
ATOM   3092  N  N   . HIS C  1 121 ? 120.491 -11.487 24.019 1.00 38.94 ? 120  HIS C N   1 
ATOM   3093  C  CA  . HIS C  1 121 ? 120.864 -12.754 24.626 1.00 38.59 ? 120  HIS C CA  1 
ATOM   3094  C  C   . HIS C  1 121 ? 121.661 -12.793 25.919 1.00 38.90 ? 120  HIS C C   1 
ATOM   3095  O  O   . HIS C  1 121 ? 122.142 -11.778 26.431 1.00 38.07 ? 120  HIS C O   1 
ATOM   3096  C  CB  . HIS C  1 121 ? 121.578 -13.600 23.586 1.00 38.45 ? 120  HIS C CB  1 
ATOM   3097  C  CG  . HIS C  1 121 ? 120.678 -14.096 22.501 1.00 39.71 ? 120  HIS C CG  1 
ATOM   3098  N  ND1 . HIS C  1 121 ? 120.143 -15.363 22.505 1.00 38.81 ? 120  HIS C ND1 1 
ATOM   3099  C  CD2 . HIS C  1 121 ? 120.235 -13.498 21.371 1.00 39.30 ? 120  HIS C CD2 1 
ATOM   3100  C  CE1 . HIS C  1 121 ? 119.410 -15.530 21.416 1.00 38.89 ? 120  HIS C CE1 1 
ATOM   3101  N  NE2 . HIS C  1 121 ? 119.451 -14.414 20.714 1.00 39.38 ? 120  HIS C NE2 1 
ATOM   3102  N  N   . GLU C  1 122 ? 121.770 -14.015 26.428 1.00 39.61 ? 121  GLU C N   1 
ATOM   3103  C  CA  . GLU C  1 122 ? 122.488 -14.326 27.649 1.00 41.69 ? 121  GLU C CA  1 
ATOM   3104  C  C   . GLU C  1 122 ? 123.995 -14.177 27.427 1.00 41.27 ? 121  GLU C C   1 
ATOM   3105  O  O   . GLU C  1 122 ? 124.671 -13.436 28.146 1.00 38.79 ? 121  GLU C O   1 
ATOM   3106  C  CB  . GLU C  1 122 ? 122.186 -15.769 28.044 1.00 45.75 ? 121  GLU C CB  1 
ATOM   3107  C  CG  . GLU C  1 122 ? 122.963 -16.271 29.252 1.00 50.00 ? 121  GLU C CG  1 
ATOM   3108  C  CD  . GLU C  1 122 ? 122.945 -17.789 29.382 1.00 51.53 ? 121  GLU C CD  1 
ATOM   3109  O  OE1 . GLU C  1 122 ? 123.494 -18.309 30.378 1.00 55.75 ? 121  GLU C OE1 1 
ATOM   3110  O  OE2 . GLU C  1 122 ? 122.394 -18.465 28.489 1.00 49.98 ? 121  GLU C OE2 1 
ATOM   3111  N  N   . LYS C  1 123 ? 124.504 -14.895 26.428 1.00 41.40 ? 122  LYS C N   1 
ATOM   3112  C  CA  . LYS C  1 123 ? 125.928 -14.885 26.112 1.00 42.59 ? 122  LYS C CA  1 
ATOM   3113  C  C   . LYS C  1 123 ? 126.266 -13.965 24.944 1.00 43.70 ? 122  LYS C C   1 
ATOM   3114  O  O   . LYS C  1 123 ? 125.381 -13.421 24.272 1.00 41.52 ? 122  LYS C O   1 
ATOM   3115  C  CB  . LYS C  1 123 ? 126.384 -16.305 25.770 1.00 43.31 ? 122  LYS C CB  1 
ATOM   3116  C  CG  . LYS C  1 123 ? 126.085 -17.328 26.859 1.00 46.02 ? 122  LYS C CG  1 
ATOM   3117  C  CD  . LYS C  1 123 ? 126.749 -18.683 26.595 1.00 47.20 ? 122  LYS C CD  1 
ATOM   3118  C  CE  . LYS C  1 123 ? 125.939 -19.570 25.667 0.00 47.48 ? 122  LYS C CE  1 
ATOM   3119  N  NZ  . LYS C  1 123 ? 126.541 -20.933 25.568 0.00 47.86 ? 122  LYS C NZ  1 
ATOM   3120  N  N   . ALA C  1 124 ? 127.562 -13.810 24.703 1.00 43.13 ? 123  ALA C N   1 
ATOM   3121  C  CA  . ALA C  1 124 ? 128.040 -12.986 23.607 1.00 42.72 ? 123  ALA C CA  1 
ATOM   3122  C  C   . ALA C  1 124 ? 127.860 -13.786 22.324 1.00 41.65 ? 123  ALA C C   1 
ATOM   3123  O  O   . ALA C  1 124 ? 127.831 -15.018 22.354 1.00 40.27 ? 123  ALA C O   1 
ATOM   3124  C  CB  . ALA C  1 124 ? 129.515 -12.639 23.815 1.00 43.07 ? 123  ALA C CB  1 
ATOM   3125  N  N   . ASP C  1 125 ? 127.716 -13.074 21.210 1.00 40.70 ? 124  ASP C N   1 
ATOM   3126  C  CA  . ASP C  1 125 ? 127.553 -13.688 19.898 1.00 40.48 ? 124  ASP C CA  1 
ATOM   3127  C  C   . ASP C  1 125 ? 128.961 -13.881 19.322 1.00 39.94 ? 124  ASP C C   1 
ATOM   3128  O  O   . ASP C  1 125 ? 129.733 -12.920 19.239 1.00 37.47 ? 124  ASP C O   1 
ATOM   3129  C  CB  . ASP C  1 125 ? 126.720 -12.755 19.007 1.00 42.56 ? 124  ASP C CB  1 
ATOM   3130  C  CG  . ASP C  1 125 ? 126.394 -13.359 17.653 1.00 43.55 ? 124  ASP C CG  1 
ATOM   3131  O  OD1 . ASP C  1 125 ? 125.517 -12.796 16.961 1.00 43.81 ? 124  ASP C OD1 1 
ATOM   3132  O  OD2 . ASP C  1 125 ? 127.008 -14.381 17.276 1.00 43.89 ? 124  ASP C OD2 1 
ATOM   3133  N  N   . ASP C  1 126 ? 129.293 -15.116 18.943 1.00 38.87 ? 125  ASP C N   1 
ATOM   3134  C  CA  . ASP C  1 126 ? 130.617 -15.423 18.398 1.00 40.51 ? 125  ASP C CA  1 
ATOM   3135  C  C   . ASP C  1 126 ? 130.692 -15.090 16.920 1.00 40.81 ? 125  ASP C C   1 
ATOM   3136  O  O   . ASP C  1 126 ? 131.685 -15.397 16.241 1.00 42.29 ? 125  ASP C O   1 
ATOM   3137  C  CB  . ASP C  1 126 ? 130.958 -16.902 18.625 1.00 39.70 ? 125  ASP C CB  1 
ATOM   3138  C  CG  . ASP C  1 126 ? 130.157 -17.836 17.737 1.00 39.38 ? 125  ASP C CG  1 
ATOM   3139  O  OD1 . ASP C  1 126 ? 130.182 -19.056 18.000 1.00 40.99 ? 125  ASP C OD1 1 
ATOM   3140  O  OD2 . ASP C  1 126 ? 129.512 -17.368 16.776 1.00 38.53 ? 125  ASP C OD2 1 
ATOM   3141  N  N   . LEU C  1 127 ? 129.620 -14.478 16.428 1.00 39.29 ? 126  LEU C N   1 
ATOM   3142  C  CA  . LEU C  1 127 ? 129.526 -14.065 15.038 1.00 39.03 ? 126  LEU C CA  1 
ATOM   3143  C  C   . LEU C  1 127 ? 129.630 -15.203 14.034 1.00 39.61 ? 126  LEU C C   1 
ATOM   3144  O  O   . LEU C  1 127 ? 130.085 -14.999 12.930 1.00 38.51 ? 126  LEU C O   1 
ATOM   3145  C  CB  . LEU C  1 127 ? 130.604 -13.018 14.731 1.00 38.05 ? 126  LEU C CB  1 
ATOM   3146  C  CG  . LEU C  1 127 ? 130.774 -11.919 15.790 1.00 39.06 ? 126  LEU C CG  1 
ATOM   3147  C  CD1 . LEU C  1 127 ? 131.684 -10.828 15.243 1.00 37.49 ? 126  LEU C CD1 1 
ATOM   3148  C  CD2 . LEU C  1 127 ? 129.409 -11.330 16.182 1.00 40.10 ? 126  LEU C CD2 1 
ATOM   3149  N  N   . GLY C  1 128 ? 129.207 -16.401 14.415 1.00 40.41 ? 127  GLY C N   1 
ATOM   3150  C  CA  . GLY C  1 128 ? 129.250 -17.537 13.503 1.00 43.29 ? 127  GLY C CA  1 
ATOM   3151  C  C   . GLY C  1 128 ? 130.621 -18.139 13.224 1.00 46.50 ? 127  GLY C C   1 
ATOM   3152  O  O   . GLY C  1 128 ? 130.774 -18.928 12.290 1.00 46.34 ? 127  GLY C O   1 
ATOM   3153  N  N   . LYS C  1 129 ? 131.625 -17.769 14.014 1.00 48.87 ? 128  LYS C N   1 
ATOM   3154  C  CA  . LYS C  1 129 ? 132.974 -18.309 13.828 1.00 51.67 ? 128  LYS C CA  1 
ATOM   3155  C  C   . LYS C  1 129 ? 133.418 -19.067 15.077 1.00 53.24 ? 128  LYS C C   1 
ATOM   3156  O  O   . LYS C  1 129 ? 134.566 -18.955 15.515 1.00 52.87 ? 128  LYS C O   1 
ATOM   3157  C  CB  . LYS C  1 129 ? 133.969 -17.182 13.519 1.00 52.18 ? 128  LYS C CB  1 
ATOM   3158  C  CG  . LYS C  1 129 ? 133.691 -16.464 12.206 1.00 52.84 ? 128  LYS C CG  1 
ATOM   3159  C  CD  . LYS C  1 129 ? 133.926 -17.386 11.014 1.00 54.54 ? 128  LYS C CD  1 
ATOM   3160  C  CE  . LYS C  1 129 ? 133.370 -16.799 9.723  1.00 55.28 ? 128  LYS C CE  1 
ATOM   3161  N  NZ  . LYS C  1 129 ? 132.610 -15.536 9.953  1.00 56.51 ? 128  LYS C NZ  1 
ATOM   3162  N  N   . GLY C  1 130 ? 132.496 -19.841 15.646 1.00 54.97 ? 129  GLY C N   1 
ATOM   3163  C  CA  . GLY C  1 130 ? 132.803 -20.611 16.839 1.00 55.57 ? 129  GLY C CA  1 
ATOM   3164  C  C   . GLY C  1 130 ? 133.465 -21.935 16.514 1.00 56.52 ? 129  GLY C C   1 
ATOM   3165  O  O   . GLY C  1 130 ? 134.235 -22.462 17.317 1.00 57.43 ? 129  GLY C O   1 
ATOM   3166  N  N   . GLY C  1 131 ? 133.166 -22.475 15.336 1.00 57.01 ? 130  GLY C N   1 
ATOM   3167  C  CA  . GLY C  1 131 ? 133.753 -23.741 14.937 1.00 58.04 ? 130  GLY C CA  1 
ATOM   3168  C  C   . GLY C  1 131 ? 132.824 -24.927 15.119 1.00 59.01 ? 130  GLY C C   1 
ATOM   3169  O  O   . GLY C  1 131 ? 133.223 -26.072 14.911 1.00 58.45 ? 130  GLY C O   1 
ATOM   3170  N  N   . ASN C  1 132 ? 131.585 -24.657 15.513 1.00 60.31 ? 131  ASN C N   1 
ATOM   3171  C  CA  . ASN C  1 132 ? 130.596 -25.714 15.712 1.00 61.71 ? 131  ASN C CA  1 
ATOM   3172  C  C   . ASN C  1 132 ? 129.298 -25.375 14.982 1.00 62.16 ? 131  ASN C C   1 
ATOM   3173  O  O   . ASN C  1 132 ? 129.092 -24.235 14.561 1.00 62.90 ? 131  ASN C O   1 
ATOM   3174  C  CB  . ASN C  1 132 ? 130.320 -25.909 17.205 1.00 61.25 ? 131  ASN C CB  1 
ATOM   3175  C  CG  . ASN C  1 132 ? 129.953 -24.617 17.903 1.00 61.63 ? 131  ASN C CG  1 
ATOM   3176  O  OD1 . ASN C  1 132 ? 128.976 -23.957 17.545 1.00 61.37 ? 131  ASN C OD1 1 
ATOM   3177  N  ND2 . ASN C  1 132 ? 130.737 -24.248 18.908 1.00 61.52 ? 131  ASN C ND2 1 
ATOM   3178  N  N   . GLU C  1 133 ? 128.424 -26.366 14.835 1.00 62.00 ? 132  GLU C N   1 
ATOM   3179  C  CA  . GLU C  1 133 ? 127.157 -26.162 14.144 1.00 61.42 ? 132  GLU C CA  1 
ATOM   3180  C  C   . GLU C  1 133 ? 126.279 -25.111 14.826 1.00 60.93 ? 132  GLU C C   1 
ATOM   3181  O  O   . GLU C  1 133 ? 125.588 -24.340 14.160 1.00 61.23 ? 132  GLU C O   1 
ATOM   3182  C  CB  . GLU C  1 133 ? 126.401 -27.488 14.043 1.00 62.16 ? 132  GLU C CB  1 
ATOM   3183  C  CG  . GLU C  1 133 ? 125.106 -27.401 13.257 1.00 63.84 ? 132  GLU C CG  1 
ATOM   3184  C  CD  . GLU C  1 133 ? 124.536 -28.766 12.925 1.00 64.96 ? 132  GLU C CD  1 
ATOM   3185  O  OE1 . GLU C  1 133 ? 124.252 -29.541 13.863 1.00 65.27 ? 132  GLU C OE1 1 
ATOM   3186  O  OE2 . GLU C  1 133 ? 124.374 -29.066 11.723 1.00 66.10 ? 132  GLU C OE2 1 
ATOM   3187  N  N   . GLU C  1 134 ? 126.313 -25.073 16.151 1.00 60.03 ? 133  GLU C N   1 
ATOM   3188  C  CA  . GLU C  1 134 ? 125.508 -24.112 16.895 1.00 59.31 ? 133  GLU C CA  1 
ATOM   3189  C  C   . GLU C  1 134 ? 125.899 -22.666 16.579 1.00 57.79 ? 133  GLU C C   1 
ATOM   3190  O  O   . GLU C  1 134 ? 125.059 -21.762 16.618 1.00 57.20 ? 133  GLU C O   1 
ATOM   3191  C  CB  . GLU C  1 134 ? 125.644 -24.366 18.398 1.00 59.74 ? 133  GLU C CB  1 
ATOM   3192  C  CG  . GLU C  1 134 ? 124.721 -23.513 19.255 1.00 61.75 ? 133  GLU C CG  1 
ATOM   3193  C  CD  . GLU C  1 134 ? 123.250 -23.758 18.965 1.00 63.27 ? 133  GLU C CD  1 
ATOM   3194  O  OE1 . GLU C  1 134 ? 122.406 -23.083 19.590 1.00 65.15 ? 133  GLU C OE1 1 
ATOM   3195  O  OE2 . GLU C  1 134 ? 122.934 -24.622 18.117 1.00 64.44 ? 133  GLU C OE2 1 
ATOM   3196  N  N   . SER C  1 135 ? 127.172 -22.450 16.265 1.00 55.41 ? 134  SER C N   1 
ATOM   3197  C  CA  . SER C  1 135 ? 127.653 -21.110 15.950 1.00 53.58 ? 134  SER C CA  1 
ATOM   3198  C  C   . SER C  1 135 ? 127.108 -20.628 14.615 1.00 52.92 ? 134  SER C C   1 
ATOM   3199  O  O   . SER C  1 135 ? 126.892 -19.433 14.424 1.00 52.74 ? 134  SER C O   1 
ATOM   3200  C  CB  . SER C  1 135 ? 129.182 -21.080 15.909 1.00 52.59 ? 134  SER C CB  1 
ATOM   3201  O  OG  . SER C  1 135 ? 129.647 -19.792 15.546 1.00 48.49 ? 134  SER C OG  1 
ATOM   3202  N  N   . THR C  1 136 ? 126.887 -21.564 13.699 1.00 50.93 ? 135  THR C N   1 
ATOM   3203  C  CA  . THR C  1 136 ? 126.375 -21.236 12.377 1.00 51.03 ? 135  THR C CA  1 
ATOM   3204  C  C   . THR C  1 136 ? 124.884 -20.928 12.411 1.00 51.10 ? 135  THR C C   1 
ATOM   3205  O  O   . THR C  1 136 ? 124.327 -20.413 11.439 1.00 50.45 ? 135  THR C O   1 
ATOM   3206  C  CB  . THR C  1 136 ? 126.598 -22.393 11.395 1.00 51.69 ? 135  THR C CB  1 
ATOM   3207  O  OG1 . THR C  1 136 ? 125.778 -23.504 11.778 1.00 51.02 ? 135  THR C OG1 1 
ATOM   3208  C  CG2 . THR C  1 136 ? 128.060 -22.821 11.402 1.00 51.87 ? 135  THR C CG2 1 
ATOM   3209  N  N   . LYS C  1 137 ? 124.238 -21.245 13.530 1.00 50.07 ? 136  LYS C N   1 
ATOM   3210  C  CA  . LYS C  1 137 ? 122.808 -20.999 13.665 1.00 49.60 ? 136  LYS C CA  1 
ATOM   3211  C  C   . LYS C  1 137 ? 122.471 -19.880 14.644 1.00 48.77 ? 136  LYS C C   1 
ATOM   3212  O  O   . LYS C  1 137 ? 121.704 -18.973 14.316 1.00 46.91 ? 136  LYS C O   1 
ATOM   3213  C  CB  . LYS C  1 137 ? 122.088 -22.280 14.092 1.00 49.43 ? 136  LYS C CB  1 
ATOM   3214  C  CG  . LYS C  1 137 ? 122.145 -23.395 13.064 1.00 50.49 ? 136  LYS C CG  1 
ATOM   3215  C  CD  . LYS C  1 137 ? 121.316 -24.594 13.502 1.00 51.72 ? 136  LYS C CD  1 
ATOM   3216  C  CE  . LYS C  1 137 ? 121.372 -25.712 12.473 0.00 51.58 ? 136  LYS C CE  1 
ATOM   3217  N  NZ  . LYS C  1 137 ? 120.566 -26.891 12.891 0.00 51.84 ? 136  LYS C NZ  1 
ATOM   3218  N  N   . THR C  1 138 ? 123.050 -19.932 15.839 1.00 47.34 ? 137  THR C N   1 
ATOM   3219  C  CA  . THR C  1 138 ? 122.758 -18.920 16.845 1.00 46.96 ? 137  THR C CA  1 
ATOM   3220  C  C   . THR C  1 138 ? 123.969 -18.118 17.297 1.00 46.85 ? 137  THR C C   1 
ATOM   3221  O  O   . THR C  1 138 ? 123.832 -17.153 18.056 1.00 45.82 ? 137  THR C O   1 
ATOM   3222  C  CB  . THR C  1 138 ? 122.118 -19.560 18.087 1.00 48.39 ? 137  THR C CB  1 
ATOM   3223  O  OG1 . THR C  1 138 ? 123.089 -20.367 18.763 1.00 48.45 ? 137  THR C OG1 1 
ATOM   3224  C  CG2 . THR C  1 138 ? 120.939 -20.439 17.683 1.00 48.50 ? 137  THR C CG2 1 
ATOM   3225  N  N   . GLY C  1 139 ? 125.150 -18.506 16.828 1.00 46.34 ? 138  GLY C N   1 
ATOM   3226  C  CA  . GLY C  1 139 ? 126.355 -17.807 17.234 1.00 46.11 ? 138  GLY C CA  1 
ATOM   3227  C  C   . GLY C  1 139 ? 126.633 -18.099 18.698 1.00 45.46 ? 138  GLY C C   1 
ATOM   3228  O  O   . GLY C  1 139 ? 127.410 -17.398 19.351 1.00 44.72 ? 138  GLY C O   1 
ATOM   3229  N  N   . ASN C  1 140 ? 125.985 -19.144 19.209 1.00 45.17 ? 139  ASN C N   1 
ATOM   3230  C  CA  . ASN C  1 140 ? 126.130 -19.555 20.602 1.00 45.58 ? 139  ASN C CA  1 
ATOM   3231  C  C   . ASN C  1 140 ? 125.823 -18.408 21.566 1.00 45.82 ? 139  ASN C C   1 
ATOM   3232  O  O   . ASN C  1 140 ? 126.495 -18.243 22.584 1.00 44.98 ? 139  ASN C O   1 
ATOM   3233  C  CB  . ASN C  1 140 ? 127.547 -20.087 20.849 1.00 46.45 ? 139  ASN C CB  1 
ATOM   3234  C  CG  . ASN C  1 140 ? 127.846 -21.342 20.045 1.00 47.93 ? 139  ASN C CG  1 
ATOM   3235  O  OD1 . ASN C  1 140 ? 127.180 -22.364 20.200 1.00 49.16 ? 139  ASN C OD1 1 
ATOM   3236  N  ND2 . ASN C  1 140 ? 128.847 -21.267 19.176 1.00 49.72 ? 139  ASN C ND2 1 
ATOM   3237  N  N   . ALA C  1 141 ? 124.801 -17.620 21.239 1.00 44.64 ? 140  ALA C N   1 
ATOM   3238  C  CA  . ALA C  1 141 ? 124.398 -16.493 22.075 1.00 44.90 ? 140  ALA C CA  1 
ATOM   3239  C  C   . ALA C  1 141 ? 123.649 -17.002 23.306 1.00 44.34 ? 140  ALA C C   1 
ATOM   3240  O  O   . ALA C  1 141 ? 123.482 -16.282 24.289 1.00 42.95 ? 140  ALA C O   1 
ATOM   3241  C  CB  . ALA C  1 141 ? 123.515 -15.539 21.277 1.00 45.34 ? 140  ALA C CB  1 
ATOM   3242  N  N   . GLY C  1 142 ? 123.186 -18.244 23.232 1.00 44.78 ? 141  GLY C N   1 
ATOM   3243  C  CA  . GLY C  1 142 ? 122.486 -18.840 24.353 1.00 46.97 ? 141  GLY C CA  1 
ATOM   3244  C  C   . GLY C  1 142 ? 121.048 -18.415 24.585 1.00 48.02 ? 141  GLY C C   1 
ATOM   3245  O  O   . GLY C  1 142 ? 120.286 -18.170 23.649 1.00 47.91 ? 141  GLY C O   1 
ATOM   3246  N  N   . SER C  1 143 ? 120.692 -18.327 25.862 1.00 47.14 ? 142  SER C N   1 
ATOM   3247  C  CA  . SER C  1 143 ? 119.350 -17.966 26.298 1.00 46.91 ? 142  SER C CA  1 
ATOM   3248  C  C   . SER C  1 143 ? 118.866 -16.574 25.880 1.00 45.70 ? 142  SER C C   1 
ATOM   3249  O  O   . SER C  1 143 ? 119.654 -15.642 25.728 1.00 45.27 ? 142  SER C O   1 
ATOM   3250  C  CB  . SER C  1 143 ? 119.272 -18.100 27.822 1.00 46.46 ? 142  SER C CB  1 
ATOM   3251  O  OG  . SER C  1 143 ? 117.993 -17.743 28.304 1.00 50.02 ? 142  SER C OG  1 
ATOM   3252  N  N   . ARG C  1 144 ? 117.552 -16.450 25.708 1.00 44.23 ? 143  ARG C N   1 
ATOM   3253  C  CA  . ARG C  1 144 ? 116.931 -15.184 25.328 1.00 42.29 ? 143  ARG C CA  1 
ATOM   3254  C  C   . ARG C  1 144 ? 116.470 -14.489 26.610 1.00 40.93 ? 143  ARG C C   1 
ATOM   3255  O  O   . ARG C  1 144 ? 115.457 -14.860 27.198 1.00 41.69 ? 143  ARG C O   1 
ATOM   3256  C  CB  . ARG C  1 144 ? 115.746 -15.453 24.392 1.00 40.94 ? 143  ARG C CB  1 
ATOM   3257  C  CG  . ARG C  1 144 ? 116.107 -16.388 23.242 1.00 40.74 ? 143  ARG C CG  1 
ATOM   3258  C  CD  . ARG C  1 144 ? 114.973 -16.595 22.258 1.00 40.62 ? 143  ARG C CD  1 
ATOM   3259  N  NE  . ARG C  1 144 ? 115.348 -17.566 21.233 1.00 39.23 ? 143  ARG C NE  1 
ATOM   3260  C  CZ  . ARG C  1 144 ? 114.584 -17.912 20.201 1.00 39.65 ? 143  ARG C CZ  1 
ATOM   3261  N  NH1 . ARG C  1 144 ? 115.020 -18.810 19.329 1.00 38.12 ? 143  ARG C NH1 1 
ATOM   3262  N  NH2 . ARG C  1 144 ? 113.390 -17.358 20.034 1.00 38.92 ? 143  ARG C NH2 1 
ATOM   3263  N  N   . LEU C  1 145 ? 117.222 -13.478 27.033 1.00 39.74 ? 144  LEU C N   1 
ATOM   3264  C  CA  . LEU C  1 145 ? 116.931 -12.745 28.262 1.00 37.81 ? 144  LEU C CA  1 
ATOM   3265  C  C   . LEU C  1 145 ? 115.737 -11.805 28.179 1.00 37.35 ? 144  LEU C C   1 
ATOM   3266  O  O   . LEU C  1 145 ? 114.982 -11.670 29.141 1.00 34.98 ? 144  LEU C O   1 
ATOM   3267  C  CB  . LEU C  1 145 ? 118.161 -11.951 28.696 1.00 38.89 ? 144  LEU C CB  1 
ATOM   3268  C  CG  . LEU C  1 145 ? 119.475 -12.731 28.786 1.00 40.57 ? 144  LEU C CG  1 
ATOM   3269  C  CD1 . LEU C  1 145 ? 120.561 -11.805 29.302 1.00 40.87 ? 144  LEU C CD1 1 
ATOM   3270  C  CD2 . LEU C  1 145 ? 119.317 -13.934 29.705 1.00 41.48 ? 144  LEU C CD2 1 
ATOM   3271  N  N   . ALA C  1 146 ? 115.585 -11.136 27.040 1.00 35.10 ? 145  ALA C N   1 
ATOM   3272  C  CA  . ALA C  1 146 ? 114.469 -10.216 26.840 1.00 32.83 ? 145  ALA C CA  1 
ATOM   3273  C  C   . ALA C  1 146 ? 114.204 -10.063 25.349 1.00 31.91 ? 145  ALA C C   1 
ATOM   3274  O  O   . ALA C  1 146 ? 115.090 -10.302 24.521 1.00 29.96 ? 145  ALA C O   1 
ATOM   3275  C  CB  . ALA C  1 146 ? 114.780 -8.854  27.461 1.00 29.92 ? 145  ALA C CB  1 
ATOM   3276  N  N   . CYS C  1 147 ? 112.982 -9.666  25.012 1.00 30.06 ? 146  CYS C N   1 
ATOM   3277  C  CA  . CYS C  1 147 ? 112.604 -9.478  23.622 1.00 30.69 ? 146  CYS C CA  1 
ATOM   3278  C  C   . CYS C  1 147 ? 111.416 -8.534  23.521 1.00 30.85 ? 146  CYS C C   1 
ATOM   3279  O  O   . CYS C  1 147 ? 110.802 -8.173  24.529 1.00 30.69 ? 146  CYS C O   1 
ATOM   3280  C  CB  . CYS C  1 147 ? 112.269 -10.828 22.976 1.00 32.61 ? 146  CYS C CB  1 
ATOM   3281  S  SG  . CYS C  1 147 ? 110.965 -11.767 23.832 1.00 35.49 ? 146  CYS C SG  1 
ATOM   3282  N  N   . GLY C  1 148 ? 111.104 -8.128  22.297 1.00 28.59 ? 147  GLY C N   1 
ATOM   3283  C  CA  . GLY C  1 148 ? 109.992 -7.230  22.073 1.00 28.15 ? 147  GLY C CA  1 
ATOM   3284  C  C   . GLY C  1 148 ? 109.642 -7.206  20.601 1.00 29.40 ? 147  GLY C C   1 
ATOM   3285  O  O   . GLY C  1 148 ? 110.522 -7.347  19.742 1.00 27.90 ? 147  GLY C O   1 
ATOM   3286  N  N   . VAL C  1 149 ? 108.358 -7.042  20.299 1.00 28.96 ? 148  VAL C N   1 
ATOM   3287  C  CA  . VAL C  1 149 ? 107.929 -6.995  18.909 1.00 27.08 ? 148  VAL C CA  1 
ATOM   3288  C  C   . VAL C  1 149 ? 108.359 -5.656  18.323 1.00 26.36 ? 148  VAL C C   1 
ATOM   3289  O  O   . VAL C  1 149 ? 108.217 -4.613  18.965 1.00 27.05 ? 148  VAL C O   1 
ATOM   3290  C  CB  . VAL C  1 149 ? 106.393 -7.135  18.779 1.00 28.68 ? 148  VAL C CB  1 
ATOM   3291  C  CG1 . VAL C  1 149 ? 105.999 -7.168  17.308 1.00 24.58 ? 148  VAL C CG1 1 
ATOM   3292  C  CG2 . VAL C  1 149 ? 105.920 -8.405  19.477 1.00 27.50 ? 148  VAL C CG2 1 
ATOM   3293  N  N   . ILE C  1 150 ? 108.901 -5.687  17.109 1.00 26.41 ? 149  ILE C N   1 
ATOM   3294  C  CA  . ILE C  1 150 ? 109.331 -4.463  16.447 1.00 25.50 ? 149  ILE C CA  1 
ATOM   3295  C  C   . ILE C  1 150 ? 108.093 -3.804  15.861 1.00 26.69 ? 149  ILE C C   1 
ATOM   3296  O  O   . ILE C  1 150 ? 107.513 -4.293  14.885 1.00 27.71 ? 149  ILE C O   1 
ATOM   3297  C  CB  . ILE C  1 150 ? 110.342 -4.769  15.331 1.00 28.73 ? 149  ILE C CB  1 
ATOM   3298  C  CG1 . ILE C  1 150 ? 111.545 -5.513  15.925 1.00 28.79 ? 149  ILE C CG1 1 
ATOM   3299  C  CG2 . ILE C  1 150 ? 110.787 -3.478  14.660 1.00 25.83 ? 149  ILE C CG2 1 
ATOM   3300  C  CD1 . ILE C  1 150 ? 112.595 -5.887  14.914 1.00 28.86 ? 149  ILE C CD1 1 
ATOM   3301  N  N   . GLY C  1 151 ? 107.686 -2.696  16.466 1.00 26.28 ? 150  GLY C N   1 
ATOM   3302  C  CA  . GLY C  1 151 ? 106.497 -2.008  16.015 1.00 27.51 ? 150  GLY C CA  1 
ATOM   3303  C  C   . GLY C  1 151 ? 106.744 -0.686  15.325 1.00 28.76 ? 150  GLY C C   1 
ATOM   3304  O  O   . GLY C  1 151 ? 107.824 -0.095  15.433 1.00 27.24 ? 150  GLY C O   1 
ATOM   3305  N  N   . ILE C  1 152 ? 105.726 -0.228  14.608 1.00 27.87 ? 151  ILE C N   1 
ATOM   3306  C  CA  . ILE C  1 152 ? 105.792 1.034   13.887 1.00 29.65 ? 151  ILE C CA  1 
ATOM   3307  C  C   . ILE C  1 152 ? 105.731 2.182   14.885 1.00 29.03 ? 151  ILE C C   1 
ATOM   3308  O  O   . ILE C  1 152 ? 104.904 2.178   15.798 1.00 28.39 ? 151  ILE C O   1 
ATOM   3309  C  CB  . ILE C  1 152 ? 104.620 1.146   12.884 1.00 29.28 ? 151  ILE C CB  1 
ATOM   3310  C  CG1 . ILE C  1 152 ? 104.681 -0.026  11.903 1.00 28.67 ? 151  ILE C CG1 1 
ATOM   3311  C  CG2 . ILE C  1 152 ? 104.682 2.477   12.149 1.00 29.88 ? 151  ILE C CG2 1 
ATOM   3312  C  CD1 . ILE C  1 152 ? 103.528 -0.074  10.904 1.00 28.46 ? 151  ILE C CD1 1 
ATOM   3313  N  N   . ALA C  1 153 ? 106.616 3.161   14.714 1.00 29.52 ? 152  ALA C N   1 
ATOM   3314  C  CA  . ALA C  1 153 ? 106.673 4.307   15.616 1.00 30.84 ? 152  ALA C CA  1 
ATOM   3315  C  C   . ALA C  1 153 ? 106.384 5.606   14.880 1.00 32.72 ? 152  ALA C C   1 
ATOM   3316  O  O   . ALA C  1 153 ? 106.556 5.694   13.665 1.00 33.24 ? 152  ALA C O   1 
ATOM   3317  C  CB  . ALA C  1 153 ? 108.041 4.376   16.279 1.00 32.97 ? 152  ALA C CB  1 
ATOM   3318  N  N   . GLN C  1 154 ? 105.946 6.616   15.622 1.00 34.35 ? 153  GLN C N   1 
ATOM   3319  C  CA  . GLN C  1 154 ? 105.618 7.900   15.025 1.00 37.28 ? 153  GLN C CA  1 
ATOM   3320  C  C   . GLN C  1 154 ? 106.878 8.646   14.585 1.00 38.88 ? 153  GLN C C   1 
ATOM   3321  O  O   . GLN C  1 154 ? 107.877 8.617   15.337 1.00 38.71 ? 153  GLN C O   1 
ATOM   3322  C  CB  . GLN C  1 154 ? 104.843 8.750   16.028 1.00 37.97 ? 153  GLN C CB  1 
ATOM   3323  C  CG  . GLN C  1 154 ? 104.137 9.939   15.415 1.00 41.54 ? 153  GLN C CG  1 
ATOM   3324  C  CD  . GLN C  1 154 ? 103.510 10.837  16.459 1.00 44.17 ? 153  GLN C CD  1 
ATOM   3325  O  OE1 . GLN C  1 154 ? 102.644 11.656  16.150 1.00 46.46 ? 153  GLN C OE1 1 
ATOM   3326  N  NE2 . GLN C  1 154 ? 103.954 10.697  17.705 1.00 44.67 ? 153  GLN C NE2 1 
ATOM   3327  O  OXT . GLN C  1 154 ? 106.839 9.265   13.499 1.00 40.57 ? 153  GLN C OXT 1 
ATOM   3328  N  N   . ALA D  1 2   ? 101.990 -11.285 5.450  0.00 41.21 ? 1    ALA D N   1 
ATOM   3329  C  CA  . ALA D  1 2   ? 101.879 -12.535 6.255  0.00 40.97 ? 1    ALA D CA  1 
ATOM   3330  C  C   . ALA D  1 2   ? 100.441 -13.038 6.256  1.00 40.94 ? 1    ALA D C   1 
ATOM   3331  O  O   . ALA D  1 2   ? 99.515  -12.290 5.950  1.00 41.17 ? 1    ALA D O   1 
ATOM   3332  C  CB  . ALA D  1 2   ? 102.341 -12.275 7.683  0.00 41.26 ? 1    ALA D CB  1 
ATOM   3333  N  N   . THR D  1 3   ? 100.253 -14.308 6.597  1.00 39.58 ? 2    THR D N   1 
ATOM   3334  C  CA  . THR D  1 3   ? 98.916  -14.876 6.635  1.00 38.72 ? 2    THR D CA  1 
ATOM   3335  C  C   . THR D  1 3   ? 98.437  -15.087 8.069  1.00 35.57 ? 2    THR D C   1 
ATOM   3336  O  O   . THR D  1 3   ? 97.252  -15.323 8.300  1.00 32.15 ? 2    THR D O   1 
ATOM   3337  C  CB  . THR D  1 3   ? 98.846  -16.218 5.875  1.00 41.19 ? 2    THR D CB  1 
ATOM   3338  O  OG1 . THR D  1 3   ? 99.770  -17.148 6.451  1.00 45.30 ? 2    THR D OG1 1 
ATOM   3339  C  CG2 . THR D  1 3   ? 99.185  -16.013 4.404  1.00 43.65 ? 2    THR D CG2 1 
ATOM   3340  N  N   . LYS D  1 4   ? 99.359  -15.009 9.026  1.00 33.26 ? 3    LYS D N   1 
ATOM   3341  C  CA  . LYS D  1 4   ? 99.006  -15.169 10.434 1.00 32.69 ? 3    LYS D CA  1 
ATOM   3342  C  C   . LYS D  1 4   ? 99.720  -14.170 11.329 1.00 30.33 ? 3    LYS D C   1 
ATOM   3343  O  O   . LYS D  1 4   ? 100.852 -13.762 11.054 1.00 29.47 ? 3    LYS D O   1 
ATOM   3344  C  CB  . LYS D  1 4   ? 99.306  -16.587 10.920 1.00 35.30 ? 3    LYS D CB  1 
ATOM   3345  C  CG  . LYS D  1 4   ? 98.335  -17.635 10.409 1.00 39.59 ? 3    LYS D CG  1 
ATOM   3346  C  CD  . LYS D  1 4   ? 98.582  -18.980 11.086 1.00 43.36 ? 3    LYS D CD  1 
ATOM   3347  C  CE  . LYS D  1 4   ? 97.624  -20.044 10.562 1.00 45.81 ? 3    LYS D CE  1 
ATOM   3348  N  NZ  . LYS D  1 4   ? 97.747  -21.333 11.303 1.00 47.88 ? 3    LYS D NZ  1 
ATOM   3349  N  N   . ALA D  1 5   ? 99.048  -13.775 12.405 1.00 26.51 ? 4    ALA D N   1 
ATOM   3350  C  CA  . ALA D  1 5   ? 99.613  -12.824 13.348 1.00 25.56 ? 4    ALA D CA  1 
ATOM   3351  C  C   . ALA D  1 5   ? 99.074  -13.090 14.751 1.00 24.55 ? 4    ALA D C   1 
ATOM   3352  O  O   . ALA D  1 5   ? 98.138  -13.867 14.926 1.00 24.59 ? 4    ALA D O   1 
ATOM   3353  C  CB  . ALA D  1 5   ? 99.277  -11.401 12.918 1.00 23.47 ? 4    ALA D CB  1 
ATOM   3354  N  N   . VAL D  1 6   ? 99.678  -12.446 15.744 1.00 22.62 ? 5    VAL D N   1 
ATOM   3355  C  CA  . VAL D  1 6   ? 99.258  -12.613 17.128 1.00 23.37 ? 5    VAL D CA  1 
ATOM   3356  C  C   . VAL D  1 6   ? 99.609  -11.378 17.949 1.00 23.40 ? 5    VAL D C   1 
ATOM   3357  O  O   . VAL D  1 6   ? 100.550 -10.650 17.632 1.00 22.63 ? 5    VAL D O   1 
ATOM   3358  C  CB  . VAL D  1 6   ? 99.930  -13.857 17.776 1.00 23.78 ? 5    VAL D CB  1 
ATOM   3359  C  CG1 . VAL D  1 6   ? 101.430 -13.668 17.839 1.00 23.82 ? 5    VAL D CG1 1 
ATOM   3360  C  CG2 . VAL D  1 6   ? 99.362  -14.092 19.177 1.00 26.28 ? 5    VAL D CG2 1 
ATOM   3361  N  N   . ALA D  1 7   ? 98.822  -11.136 18.990 1.00 23.17 ? 6    ALA D N   1 
ATOM   3362  C  CA  . ALA D  1 7   ? 99.050  -10.017 19.889 1.00 21.32 ? 6    ALA D CA  1 
ATOM   3363  C  C   . ALA D  1 7   ? 98.774  -10.507 21.309 1.00 24.34 ? 6    ALA D C   1 
ATOM   3364  O  O   . ALA D  1 7   ? 97.739  -11.124 21.572 1.00 21.34 ? 6    ALA D O   1 
ATOM   3365  C  CB  . ALA D  1 7   ? 98.128  -8.856  19.544 1.00 19.86 ? 6    ALA D CB  1 
ATOM   3366  N  N   . VAL D  1 8   ? 99.716  -10.254 22.213 1.00 25.15 ? 7    VAL D N   1 
ATOM   3367  C  CA  . VAL D  1 8   ? 99.561  -10.651 23.609 1.00 26.02 ? 7    VAL D CA  1 
ATOM   3368  C  C   . VAL D  1 8   ? 99.143  -9.395  24.359 1.00 25.85 ? 7    VAL D C   1 
ATOM   3369  O  O   . VAL D  1 8   ? 99.911  -8.444  24.468 1.00 24.56 ? 7    VAL D O   1 
ATOM   3370  C  CB  . VAL D  1 8   ? 100.885 -11.189 24.191 1.00 25.90 ? 7    VAL D CB  1 
ATOM   3371  C  CG1 . VAL D  1 8   ? 100.705 -11.536 25.668 1.00 26.79 ? 7    VAL D CG1 1 
ATOM   3372  C  CG2 . VAL D  1 8   ? 101.326 -12.416 23.414 1.00 25.42 ? 7    VAL D CG2 1 
ATOM   3373  N  N   . LEU D  1 9   ? 97.916  -9.388  24.859 1.00 26.12 ? 8    LEU D N   1 
ATOM   3374  C  CA  . LEU D  1 9   ? 97.402  -8.224  25.563 1.00 26.42 ? 8    LEU D CA  1 
ATOM   3375  C  C   . LEU D  1 9   ? 97.800  -8.196  27.030 1.00 26.73 ? 8    LEU D C   1 
ATOM   3376  O  O   . LEU D  1 9   ? 97.577  -9.151  27.764 1.00 25.23 ? 8    LEU D O   1 
ATOM   3377  C  CB  . LEU D  1 9   ? 95.879  -8.179  25.439 1.00 25.67 ? 8    LEU D CB  1 
ATOM   3378  C  CG  . LEU D  1 9   ? 95.344  -8.196  24.001 1.00 25.70 ? 8    LEU D CG  1 
ATOM   3379  C  CD1 . LEU D  1 9   ? 93.826  -8.127  24.015 1.00 28.00 ? 8    LEU D CD1 1 
ATOM   3380  C  CD2 . LEU D  1 9   ? 95.927  -7.020  23.228 1.00 25.92 ? 8    LEU D CD2 1 
ATOM   3381  N  N   . LYS D  1 10  ? 98.390  -7.084  27.447 1.00 28.87 ? 9    LYS D N   1 
ATOM   3382  C  CA  . LYS D  1 10  ? 98.809  -6.916  28.830 1.00 30.66 ? 9    LYS D CA  1 
ATOM   3383  C  C   . LYS D  1 10  ? 98.576  -5.479  29.255 1.00 30.96 ? 9    LYS D C   1 
ATOM   3384  O  O   . LYS D  1 10  ? 98.586  -4.567  28.428 1.00 30.53 ? 9    LYS D O   1 
ATOM   3385  C  CB  . LYS D  1 10  ? 100.291 -7.264  28.989 1.00 33.23 ? 9    LYS D CB  1 
ATOM   3386  C  CG  . LYS D  1 10  ? 100.618 -8.717  28.700 1.00 37.84 ? 9    LYS D CG  1 
ATOM   3387  C  CD  . LYS D  1 10  ? 102.090 -9.015  28.958 1.00 41.46 ? 9    LYS D CD  1 
ATOM   3388  C  CE  . LYS D  1 10  ? 102.398 -10.490 28.730 1.00 43.84 ? 9    LYS D CE  1 
ATOM   3389  N  NZ  . LYS D  1 10  ? 103.821 -10.820 29.021 1.00 45.82 ? 9    LYS D NZ  1 
ATOM   3390  N  N   . GLY D  1 11  ? 98.372  -5.283  30.552 1.00 31.05 ? 10   GLY D N   1 
ATOM   3391  C  CA  . GLY D  1 11  ? 98.147  -3.951  31.077 1.00 34.51 ? 10   GLY D CA  1 
ATOM   3392  C  C   . GLY D  1 11  ? 98.591  -3.888  32.526 1.00 35.87 ? 10   GLY D C   1 
ATOM   3393  O  O   . GLY D  1 11  ? 99.202  -4.830  33.031 1.00 36.05 ? 10   GLY D O   1 
ATOM   3394  N  N   . ASP D  1 12  ? 98.280  -2.792  33.204 1.00 36.53 ? 11   ASP D N   1 
ATOM   3395  C  CA  . ASP D  1 12  ? 98.672  -2.658  34.601 1.00 38.34 ? 11   ASP D CA  1 
ATOM   3396  C  C   . ASP D  1 12  ? 97.664  -3.284  35.548 1.00 37.11 ? 11   ASP D C   1 
ATOM   3397  O  O   . ASP D  1 12  ? 97.955  -3.466  36.728 1.00 38.48 ? 11   ASP D O   1 
ATOM   3398  C  CB  . ASP D  1 12  ? 98.872  -1.185  34.956 1.00 41.46 ? 11   ASP D CB  1 
ATOM   3399  C  CG  . ASP D  1 12  ? 100.036 -0.568  34.216 1.00 43.74 ? 11   ASP D CG  1 
ATOM   3400  O  OD1 . ASP D  1 12  ? 101.146 -1.139  34.282 1.00 43.93 ? 11   ASP D OD1 1 
ATOM   3401  O  OD2 . ASP D  1 12  ? 99.842  0.483   33.568 1.00 47.55 ? 11   ASP D OD2 1 
ATOM   3402  N  N   . GLY D  1 13  ? 96.487  -3.621  35.026 1.00 35.07 ? 12   GLY D N   1 
ATOM   3403  C  CA  . GLY D  1 13  ? 95.447  -4.224  35.842 1.00 31.73 ? 12   GLY D CA  1 
ATOM   3404  C  C   . GLY D  1 13  ? 95.322  -5.726  35.656 1.00 31.12 ? 12   GLY D C   1 
ATOM   3405  O  O   . GLY D  1 13  ? 96.303  -6.383  35.332 1.00 30.59 ? 12   GLY D O   1 
ATOM   3406  N  N   . PRO D  1 14  ? 94.124  -6.302  35.857 1.00 29.57 ? 13   PRO D N   1 
ATOM   3407  C  CA  . PRO D  1 14  ? 93.914  -7.743  35.703 1.00 29.62 ? 13   PRO D CA  1 
ATOM   3408  C  C   . PRO D  1 14  ? 93.572  -8.184  34.274 1.00 29.23 ? 13   PRO D C   1 
ATOM   3409  O  O   . PRO D  1 14  ? 93.399  -9.371  34.018 1.00 31.68 ? 13   PRO D O   1 
ATOM   3410  C  CB  . PRO D  1 14  ? 92.771  -8.013  36.665 1.00 29.42 ? 13   PRO D CB  1 
ATOM   3411  C  CG  . PRO D  1 14  ? 91.921  -6.802  36.458 1.00 27.88 ? 13   PRO D CG  1 
ATOM   3412  C  CD  . PRO D  1 14  ? 92.928  -5.665  36.437 1.00 28.01 ? 13   PRO D CD  1 
ATOM   3413  N  N   . VAL D  1 15  ? 93.474  -7.237  33.347 1.00 29.47 ? 14   VAL D N   1 
ATOM   3414  C  CA  . VAL D  1 15  ? 93.141  -7.581  31.966 1.00 28.98 ? 14   VAL D CA  1 
ATOM   3415  C  C   . VAL D  1 15  ? 94.339  -8.107  31.181 1.00 27.74 ? 14   VAL D C   1 
ATOM   3416  O  O   . VAL D  1 15  ? 95.387  -7.469  31.116 1.00 27.13 ? 14   VAL D O   1 
ATOM   3417  C  CB  . VAL D  1 15  ? 92.555  -6.369  31.201 1.00 29.15 ? 14   VAL D CB  1 
ATOM   3418  C  CG1 . VAL D  1 15  ? 92.259  -6.763  29.753 1.00 29.06 ? 14   VAL D CG1 1 
ATOM   3419  C  CG2 . VAL D  1 15  ? 91.279  -5.889  31.880 1.00 29.70 ? 14   VAL D CG2 1 
ATOM   3420  N  N   . GLN D  1 16  ? 94.173  -9.284  30.587 1.00 29.14 ? 15   GLN D N   1 
ATOM   3421  C  CA  . GLN D  1 16  ? 95.223  -9.895  29.782 1.00 30.36 ? 15   GLN D CA  1 
ATOM   3422  C  C   . GLN D  1 16  ? 94.632  -10.993 28.900 1.00 28.78 ? 15   GLN D C   1 
ATOM   3423  O  O   . GLN D  1 16  ? 93.570  -11.544 29.199 1.00 25.99 ? 15   GLN D O   1 
ATOM   3424  C  CB  . GLN D  1 16  ? 96.326  -10.477 30.676 1.00 35.00 ? 15   GLN D CB  1 
ATOM   3425  C  CG  . GLN D  1 16  ? 95.858  -11.533 31.660 1.00 41.48 ? 15   GLN D CG  1 
ATOM   3426  C  CD  . GLN D  1 16  ? 96.987  -12.066 32.534 1.00 45.58 ? 15   GLN D CD  1 
ATOM   3427  O  OE1 . GLN D  1 16  ? 97.895  -12.746 32.056 1.00 49.22 ? 15   GLN D OE1 1 
ATOM   3428  N  NE2 . GLN D  1 16  ? 96.934  -11.750 33.822 1.00 47.70 ? 15   GLN D NE2 1 
ATOM   3429  N  N   . GLY D  1 17  ? 95.319  -11.299 27.804 1.00 27.02 ? 16   GLY D N   1 
ATOM   3430  C  CA  . GLY D  1 17  ? 94.839  -12.330 26.903 1.00 27.58 ? 16   GLY D CA  1 
ATOM   3431  C  C   . GLY D  1 17  ? 95.685  -12.457 25.652 1.00 27.38 ? 16   GLY D C   1 
ATOM   3432  O  O   . GLY D  1 17  ? 96.659  -11.730 25.475 1.00 27.68 ? 16   GLY D O   1 
ATOM   3433  N  N   . ILE D  1 18  ? 95.306  -13.389 24.784 1.00 27.31 ? 17   ILE D N   1 
ATOM   3434  C  CA  . ILE D  1 18  ? 96.020  -13.628 23.539 1.00 26.66 ? 17   ILE D CA  1 
ATOM   3435  C  C   . ILE D  1 18  ? 95.037  -13.623 22.375 1.00 26.31 ? 17   ILE D C   1 
ATOM   3436  O  O   . ILE D  1 18  ? 94.035  -14.344 22.387 1.00 24.77 ? 17   ILE D O   1 
ATOM   3437  C  CB  . ILE D  1 18  ? 96.764  -14.976 23.587 1.00 26.53 ? 17   ILE D CB  1 
ATOM   3438  C  CG1 . ILE D  1 18  ? 97.862  -14.910 24.653 1.00 28.72 ? 17   ILE D CG1 1 
ATOM   3439  C  CG2 . ILE D  1 18  ? 97.349  -15.309 22.215 1.00 27.20 ? 17   ILE D CG2 1 
ATOM   3440  C  CD1 . ILE D  1 18  ? 98.611  -16.222 24.852 1.00 31.20 ? 17   ILE D CD1 1 
ATOM   3441  N  N   . ILE D  1 19  ? 95.333  -12.800 21.373 1.00 23.88 ? 18   ILE D N   1 
ATOM   3442  C  CA  . ILE D  1 19  ? 94.476  -12.674 20.203 1.00 22.95 ? 18   ILE D CA  1 
ATOM   3443  C  C   . ILE D  1 19  ? 95.227  -13.081 18.938 1.00 24.20 ? 18   ILE D C   1 
ATOM   3444  O  O   . ILE D  1 19  ? 96.308  -12.569 18.652 1.00 23.21 ? 18   ILE D O   1 
ATOM   3445  C  CB  . ILE D  1 19  ? 93.971  -11.222 20.053 1.00 22.08 ? 18   ILE D CB  1 
ATOM   3446  C  CG1 . ILE D  1 19  ? 93.156  -10.826 21.291 1.00 21.33 ? 18   ILE D CG1 1 
ATOM   3447  C  CG2 . ILE D  1 19  ? 93.133  -11.078 18.768 1.00 20.62 ? 18   ILE D CG2 1 
ATOM   3448  C  CD1 . ILE D  1 19  ? 91.852  -11.637 21.477 1.00 21.84 ? 18   ILE D CD1 1 
ATOM   3449  N  N   . ASN D  1 20  ? 94.635  -14.004 18.186 1.00 24.61 ? 19   ASN D N   1 
ATOM   3450  C  CA  . ASN D  1 20  ? 95.225  -14.508 16.951 1.00 25.74 ? 19   ASN D CA  1 
ATOM   3451  C  C   . ASN D  1 20  ? 94.561  -13.874 15.734 1.00 25.03 ? 19   ASN D C   1 
ATOM   3452  O  O   . ASN D  1 20  ? 93.384  -13.512 15.777 1.00 23.36 ? 19   ASN D O   1 
ATOM   3453  C  CB  . ASN D  1 20  ? 95.045  -16.026 16.862 1.00 25.85 ? 19   ASN D CB  1 
ATOM   3454  C  CG  . ASN D  1 20  ? 95.603  -16.753 18.063 1.00 29.95 ? 19   ASN D CG  1 
ATOM   3455  O  OD1 . ASN D  1 20  ? 96.818  -16.876 18.217 1.00 29.51 ? 19   ASN D OD1 1 
ATOM   3456  N  ND2 . ASN D  1 20  ? 94.714  -17.236 18.932 1.00 29.42 ? 19   ASN D ND2 1 
ATOM   3457  N  N   . PHE D  1 21  ? 95.323  -13.759 14.651 1.00 24.46 ? 20   PHE D N   1 
ATOM   3458  C  CA  . PHE D  1 21  ? 94.828  -13.199 13.395 1.00 24.91 ? 20   PHE D CA  1 
ATOM   3459  C  C   . PHE D  1 21  ? 95.186  -14.162 12.274 1.00 25.68 ? 20   PHE D C   1 
ATOM   3460  O  O   . PHE D  1 21  ? 96.290  -14.713 12.260 1.00 24.08 ? 20   PHE D O   1 
ATOM   3461  C  CB  . PHE D  1 21  ? 95.500  -11.859 13.075 1.00 23.55 ? 20   PHE D CB  1 
ATOM   3462  C  CG  . PHE D  1 21  ? 95.183  -10.766 14.045 1.00 23.15 ? 20   PHE D CG  1 
ATOM   3463  C  CD1 . PHE D  1 21  ? 94.122  -9.900  13.813 1.00 23.63 ? 20   PHE D CD1 1 
ATOM   3464  C  CD2 . PHE D  1 21  ? 95.980  -10.569 15.169 1.00 23.57 ? 20   PHE D CD2 1 
ATOM   3465  C  CE1 . PHE D  1 21  ? 93.849  -8.861  14.691 1.00 21.74 ? 20   PHE D CE1 1 
ATOM   3466  C  CE2 . PHE D  1 21  ? 95.716  -9.532  16.056 1.00 22.62 ? 20   PHE D CE2 1 
ATOM   3467  C  CZ  . PHE D  1 21  ? 94.657  -8.673  15.813 1.00 24.13 ? 20   PHE D CZ  1 
ATOM   3468  N  N   . GLU D  1 22  ? 94.260  -14.366 11.340 1.00 25.09 ? 21   GLU D N   1 
ATOM   3469  C  CA  . GLU D  1 22  ? 94.526  -15.233 10.201 1.00 27.57 ? 21   GLU D CA  1 
ATOM   3470  C  C   . GLU D  1 22  ? 93.841  -14.726 8.940  1.00 26.75 ? 21   GLU D C   1 
ATOM   3471  O  O   . GLU D  1 22  ? 92.645  -14.435 8.931  1.00 23.42 ? 21   GLU D O   1 
ATOM   3472  C  CB  . GLU D  1 22  ? 94.090  -16.676 10.467 1.00 29.55 ? 21   GLU D CB  1 
ATOM   3473  C  CG  . GLU D  1 22  ? 94.568  -17.627 9.370  1.00 37.30 ? 21   GLU D CG  1 
ATOM   3474  C  CD  . GLU D  1 22  ? 94.308  -19.095 9.670  1.00 43.25 ? 21   GLU D CD  1 
ATOM   3475  O  OE1 . GLU D  1 22  ? 94.760  -19.949 8.875  1.00 46.02 ? 21   GLU D OE1 1 
ATOM   3476  O  OE2 . GLU D  1 22  ? 93.655  -19.400 10.691 1.00 47.04 ? 21   GLU D OE2 1 
ATOM   3477  N  N   . GLN D  1 23  ? 94.623  -14.619 7.873  1.00 27.14 ? 22   GLN D N   1 
ATOM   3478  C  CA  . GLN D  1 23  ? 94.123  -14.154 6.590  1.00 27.75 ? 22   GLN D CA  1 
ATOM   3479  C  C   . GLN D  1 23  ? 94.609  -15.111 5.496  1.00 29.02 ? 22   GLN D C   1 
ATOM   3480  O  O   . GLN D  1 23  ? 95.773  -15.087 5.109  1.00 28.47 ? 22   GLN D O   1 
ATOM   3481  C  CB  . GLN D  1 23  ? 94.625  -12.730 6.342  1.00 27.45 ? 22   GLN D CB  1 
ATOM   3482  C  CG  . GLN D  1 23  ? 94.217  -12.122 5.010  1.00 28.71 ? 22   GLN D CG  1 
ATOM   3483  C  CD  . GLN D  1 23  ? 94.720  -10.702 4.872  1.00 28.30 ? 22   GLN D CD  1 
ATOM   3484  O  OE1 . GLN D  1 23  ? 95.843  -10.397 5.273  1.00 30.07 ? 22   GLN D OE1 1 
ATOM   3485  N  NE2 . GLN D  1 23  ? 93.898  -9.826  4.302  1.00 30.57 ? 22   GLN D NE2 1 
ATOM   3486  N  N   . LYS D  1 24  ? 93.703  -15.958 5.017  1.00 31.32 ? 23   LYS D N   1 
ATOM   3487  C  CA  . LYS D  1 24  ? 94.016  -16.940 3.980  1.00 34.70 ? 23   LYS D CA  1 
ATOM   3488  C  C   . LYS D  1 24  ? 94.465  -16.319 2.659  1.00 36.63 ? 23   LYS D C   1 
ATOM   3489  O  O   . LYS D  1 24  ? 95.391  -16.818 2.018  1.00 36.60 ? 23   LYS D O   1 
ATOM   3490  C  CB  . LYS D  1 24  ? 92.804  -17.843 3.725  1.00 36.48 ? 23   LYS D CB  1 
ATOM   3491  C  CG  . LYS D  1 24  ? 92.448  -18.760 4.890  1.00 37.82 ? 23   LYS D CG  1 
ATOM   3492  C  CD  . LYS D  1 24  ? 91.248  -19.635 4.556  0.00 38.26 ? 23   LYS D CD  1 
ATOM   3493  C  CE  . LYS D  1 24  ? 90.902  -20.564 5.709  0.00 38.70 ? 23   LYS D CE  1 
ATOM   3494  N  NZ  . LYS D  1 24  ? 89.723  -21.420 5.401  0.00 38.97 ? 23   LYS D NZ  1 
ATOM   3495  N  N   . GLU D  1 25  ? 93.813  -15.236 2.250  1.00 37.94 ? 24   GLU D N   1 
ATOM   3496  C  CA  . GLU D  1 25  ? 94.160  -14.575 0.996  1.00 41.23 ? 24   GLU D CA  1 
ATOM   3497  C  C   . GLU D  1 25  ? 94.478  -13.099 1.205  1.00 41.87 ? 24   GLU D C   1 
ATOM   3498  O  O   . GLU D  1 25  ? 93.899  -12.447 2.071  1.00 40.28 ? 24   GLU D O   1 
ATOM   3499  C  CB  . GLU D  1 25  ? 93.004  -14.720 0.001  1.00 43.69 ? 24   GLU D CB  1 
ATOM   3500  C  CG  . GLU D  1 25  ? 92.567  -16.159 -0.220 1.00 48.56 ? 24   GLU D CG  1 
ATOM   3501  C  CD  . GLU D  1 25  ? 93.661  -17.018 -0.832 1.00 51.98 ? 24   GLU D CD  1 
ATOM   3502  O  OE1 . GLU D  1 25  ? 93.489  -18.255 -0.879 1.00 54.23 ? 24   GLU D OE1 1 
ATOM   3503  O  OE2 . GLU D  1 25  ? 94.690  -16.458 -1.271 1.00 53.24 ? 24   GLU D OE2 1 
ATOM   3504  N  N   . SER D  1 26  ? 95.394  -12.575 0.396  1.00 42.80 ? 25   SER D N   1 
ATOM   3505  C  CA  . SER D  1 26  ? 95.797  -11.174 0.487  1.00 45.52 ? 25   SER D CA  1 
ATOM   3506  C  C   . SER D  1 26  ? 94.609  -10.224 0.389  1.00 45.59 ? 25   SER D C   1 
ATOM   3507  O  O   . SER D  1 26  ? 94.619  -9.135  0.960  1.00 46.87 ? 25   SER D O   1 
ATOM   3508  C  CB  . SER D  1 26  ? 96.794  -10.841 -0.626 1.00 46.40 ? 25   SER D CB  1 
ATOM   3509  O  OG  . SER D  1 26  ? 97.899  -11.724 -0.595 1.00 50.52 ? 25   SER D OG  1 
ATOM   3510  N  N   . ASN D  1 27  ? 93.585  -10.640 -0.342 1.00 46.09 ? 26   ASN D N   1 
ATOM   3511  C  CA  . ASN D  1 27  ? 92.400  -9.812  -0.523 1.00 47.75 ? 26   ASN D CA  1 
ATOM   3512  C  C   . ASN D  1 27  ? 91.252  -10.239 0.382  1.00 46.43 ? 26   ASN D C   1 
ATOM   3513  O  O   . ASN D  1 27  ? 90.222  -9.570  0.443  1.00 48.05 ? 26   ASN D O   1 
ATOM   3514  C  CB  . ASN D  1 27  ? 91.938  -9.892  -1.979 1.00 49.88 ? 26   ASN D CB  1 
ATOM   3515  C  CG  . ASN D  1 27  ? 91.652  -11.322 -2.421 1.00 53.42 ? 26   ASN D CG  1 
ATOM   3516  O  OD1 . ASN D  1 27  ? 92.521  -12.195 -2.344 1.00 55.32 ? 26   ASN D OD1 1 
ATOM   3517  N  ND2 . ASN D  1 27  ? 90.430  -11.567 -2.885 1.00 54.62 ? 26   ASN D ND2 1 
ATOM   3518  N  N   . GLY D  1 28  ? 91.433  -11.350 1.086  1.00 42.94 ? 27   GLY D N   1 
ATOM   3519  C  CA  . GLY D  1 28  ? 90.373  -11.857 1.936  1.00 39.79 ? 27   GLY D CA  1 
ATOM   3520  C  C   . GLY D  1 28  ? 90.210  -11.242 3.312  1.00 36.08 ? 27   GLY D C   1 
ATOM   3521  O  O   . GLY D  1 28  ? 91.042  -10.457 3.770  1.00 33.66 ? 27   GLY D O   1 
ATOM   3522  N  N   . PRO D  1 29  ? 89.114  -11.586 3.997  1.00 34.15 ? 28   PRO D N   1 
ATOM   3523  C  CA  . PRO D  1 29  ? 88.878  -11.047 5.332  1.00 32.20 ? 28   PRO D CA  1 
ATOM   3524  C  C   . PRO D  1 29  ? 89.853  -11.671 6.323  1.00 29.62 ? 28   PRO D C   1 
ATOM   3525  O  O   . PRO D  1 29  ? 90.457  -12.714 6.052  1.00 27.24 ? 28   PRO D O   1 
ATOM   3526  C  CB  . PRO D  1 29  ? 87.430  -11.439 5.604  1.00 33.55 ? 28   PRO D CB  1 
ATOM   3527  C  CG  . PRO D  1 29  ? 87.311  -12.745 4.904  1.00 35.04 ? 28   PRO D CG  1 
ATOM   3528  C  CD  . PRO D  1 29  ? 88.013  -12.478 3.589  1.00 34.20 ? 28   PRO D CD  1 
ATOM   3529  N  N   . VAL D  1 30  ? 90.010  -11.016 7.463  1.00 27.13 ? 29   VAL D N   1 
ATOM   3530  C  CA  . VAL D  1 30  ? 90.896  -11.499 8.507  1.00 24.84 ? 29   VAL D CA  1 
ATOM   3531  C  C   . VAL D  1 30  ? 90.035  -12.032 9.645  1.00 24.80 ? 29   VAL D C   1 
ATOM   3532  O  O   . VAL D  1 30  ? 89.076  -11.385 10.056 1.00 24.46 ? 29   VAL D O   1 
ATOM   3533  C  CB  . VAL D  1 30  ? 91.776  -10.355 9.059  1.00 23.55 ? 29   VAL D CB  1 
ATOM   3534  C  CG1 . VAL D  1 30  ? 92.666  -10.875 10.185 1.00 18.95 ? 29   VAL D CG1 1 
ATOM   3535  C  CG2 . VAL D  1 30  ? 92.610  -9.749  7.928  1.00 21.59 ? 29   VAL D CG2 1 
ATOM   3536  N  N   . LYS D  1 31  ? 90.366  -13.219 10.134 1.00 24.98 ? 30   LYS D N   1 
ATOM   3537  C  CA  . LYS D  1 31  ? 89.641  -13.801 11.252 1.00 26.68 ? 30   LYS D CA  1 
ATOM   3538  C  C   . LYS D  1 31  ? 90.429  -13.458 12.509 1.00 25.42 ? 30   LYS D C   1 
ATOM   3539  O  O   . LYS D  1 31  ? 91.652  -13.602 12.547 1.00 23.92 ? 30   LYS D O   1 
ATOM   3540  C  CB  . LYS D  1 31  ? 89.520  -15.314 11.096 1.00 28.40 ? 30   LYS D CB  1 
ATOM   3541  C  CG  . LYS D  1 31  ? 88.540  -15.727 10.008 1.00 34.02 ? 30   LYS D CG  1 
ATOM   3542  C  CD  . LYS D  1 31  ? 88.347  -17.235 9.988  1.00 39.01 ? 30   LYS D CD  1 
ATOM   3543  C  CE  . LYS D  1 31  ? 87.336  -17.659 8.929  1.00 41.40 ? 30   LYS D CE  1 
ATOM   3544  N  NZ  . LYS D  1 31  ? 87.213  -19.146 8.869  1.00 44.09 ? 30   LYS D NZ  1 
ATOM   3545  N  N   . VAL D  1 32  ? 89.716  -12.985 13.524 1.00 24.68 ? 31   VAL D N   1 
ATOM   3546  C  CA  . VAL D  1 32  ? 90.322  -12.580 14.782 1.00 23.37 ? 31   VAL D CA  1 
ATOM   3547  C  C   . VAL D  1 32  ? 89.672  -13.402 15.880 1.00 23.91 ? 31   VAL D C   1 
ATOM   3548  O  O   . VAL D  1 32  ? 88.450  -13.442 15.978 1.00 24.68 ? 31   VAL D O   1 
ATOM   3549  C  CB  . VAL D  1 32  ? 90.062  -11.077 15.037 1.00 22.31 ? 31   VAL D CB  1 
ATOM   3550  C  CG1 . VAL D  1 32  ? 90.860  -10.597 16.244 1.00 20.52 ? 31   VAL D CG1 1 
ATOM   3551  C  CG2 . VAL D  1 32  ? 90.429  -10.275 13.792 1.00 22.27 ? 31   VAL D CG2 1 
ATOM   3552  N  N   . TRP D  1 33  ? 90.481  -14.071 16.693 1.00 24.45 ? 32   TRP D N   1 
ATOM   3553  C  CA  . TRP D  1 33  ? 89.933  -14.895 17.759 1.00 25.23 ? 32   TRP D CA  1 
ATOM   3554  C  C   . TRP D  1 33  ? 90.944  -15.111 18.872 1.00 23.70 ? 32   TRP D C   1 
ATOM   3555  O  O   . TRP D  1 33  ? 92.155  -15.043 18.663 1.00 21.52 ? 32   TRP D O   1 
ATOM   3556  C  CB  . TRP D  1 33  ? 89.480  -16.247 17.199 1.00 26.47 ? 32   TRP D CB  1 
ATOM   3557  C  CG  . TRP D  1 33  ? 90.598  -17.218 16.991 1.00 29.35 ? 32   TRP D CG  1 
ATOM   3558  C  CD1 . TRP D  1 33  ? 91.021  -18.185 17.862 1.00 29.24 ? 32   TRP D CD1 1 
ATOM   3559  C  CD2 . TRP D  1 33  ? 91.466  -17.295 15.855 1.00 30.18 ? 32   TRP D CD2 1 
ATOM   3560  N  NE1 . TRP D  1 33  ? 92.098  -18.858 17.335 1.00 32.01 ? 32   TRP D NE1 1 
ATOM   3561  C  CE2 . TRP D  1 33  ? 92.393  -18.331 16.103 1.00 30.90 ? 32   TRP D CE2 1 
ATOM   3562  C  CE3 . TRP D  1 33  ? 91.551  -16.587 14.649 1.00 31.95 ? 32   TRP D CE3 1 
ATOM   3563  C  CZ2 . TRP D  1 33  ? 93.394  -18.679 15.192 1.00 32.29 ? 32   TRP D CZ2 1 
ATOM   3564  C  CZ3 . TRP D  1 33  ? 92.551  -16.934 13.737 1.00 32.39 ? 32   TRP D CZ3 1 
ATOM   3565  C  CH2 . TRP D  1 33  ? 93.457  -17.971 14.017 1.00 31.55 ? 32   TRP D CH2 1 
ATOM   3566  N  N   . GLY D  1 34  ? 90.428  -15.382 20.061 1.00 24.07 ? 33   GLY D N   1 
ATOM   3567  C  CA  . GLY D  1 34  ? 91.289  -15.604 21.200 1.00 24.41 ? 33   GLY D CA  1 
ATOM   3568  C  C   . GLY D  1 34  ? 90.477  -15.416 22.457 1.00 26.64 ? 33   GLY D C   1 
ATOM   3569  O  O   . GLY D  1 34  ? 89.246  -15.449 22.419 1.00 27.15 ? 33   GLY D O   1 
ATOM   3570  N  N   . SER D  1 35  ? 91.155  -15.194 23.573 1.00 27.78 ? 34   SER D N   1 
ATOM   3571  C  CA  . SER D  1 35  ? 90.459  -15.028 24.834 1.00 28.87 ? 34   SER D CA  1 
ATOM   3572  C  C   . SER D  1 35  ? 91.107  -13.963 25.701 1.00 27.83 ? 34   SER D C   1 
ATOM   3573  O  O   . SER D  1 35  ? 92.329  -13.900 25.816 1.00 28.19 ? 34   SER D O   1 
ATOM   3574  C  CB  . SER D  1 35  ? 90.435  -16.362 25.582 1.00 30.00 ? 34   SER D CB  1 
ATOM   3575  O  OG  . SER D  1 35  ? 89.665  -16.269 26.764 1.00 34.74 ? 34   SER D OG  1 
ATOM   3576  N  N   . ILE D  1 36  ? 90.272  -13.122 26.301 1.00 25.19 ? 35   ILE D N   1 
ATOM   3577  C  CA  . ILE D  1 36  ? 90.741  -12.063 27.185 1.00 25.49 ? 35   ILE D CA  1 
ATOM   3578  C  C   . ILE D  1 36  ? 90.002  -12.241 28.511 1.00 26.46 ? 35   ILE D C   1 
ATOM   3579  O  O   . ILE D  1 36  ? 88.783  -12.458 28.524 1.00 26.49 ? 35   ILE D O   1 
ATOM   3580  C  CB  . ILE D  1 36  ? 90.407  -10.665 26.621 1.00 24.63 ? 35   ILE D CB  1 
ATOM   3581  C  CG1 . ILE D  1 36  ? 90.911  -10.542 25.179 1.00 24.61 ? 35   ILE D CG1 1 
ATOM   3582  C  CG2 . ILE D  1 36  ? 91.060  -9.586  27.481 1.00 23.27 ? 35   ILE D CG2 1 
ATOM   3583  C  CD1 . ILE D  1 36  ? 90.472  -9.260  24.493 1.00 26.14 ? 35   ILE D CD1 1 
ATOM   3584  N  N   . LYS D  1 37  ? 90.727  -12.159 29.621 1.00 25.44 ? 36   LYS D N   1 
ATOM   3585  C  CA  . LYS D  1 37  ? 90.095  -12.310 30.932 1.00 27.83 ? 36   LYS D CA  1 
ATOM   3586  C  C   . LYS D  1 37  ? 90.285  -11.051 31.767 1.00 28.87 ? 36   LYS D C   1 
ATOM   3587  O  O   . LYS D  1 37  ? 91.034  -10.147 31.379 1.00 26.67 ? 36   LYS D O   1 
ATOM   3588  C  CB  . LYS D  1 37  ? 90.677  -13.523 31.674 1.00 28.80 ? 36   LYS D CB  1 
ATOM   3589  C  CG  . LYS D  1 37  ? 92.156  -13.404 32.002 1.00 32.09 ? 36   LYS D CG  1 
ATOM   3590  C  CD  . LYS D  1 37  ? 92.643  -14.603 32.805 1.00 36.80 ? 36   LYS D CD  1 
ATOM   3591  C  CE  . LYS D  1 37  ? 94.096  -14.430 33.233 1.00 38.45 ? 36   LYS D CE  1 
ATOM   3592  N  NZ  . LYS D  1 37  ? 94.577  -15.575 34.054 0.00 38.09 ? 36   LYS D NZ  1 
ATOM   3593  N  N   . GLY D  1 38  ? 89.590  -10.991 32.904 1.00 28.07 ? 37   GLY D N   1 
ATOM   3594  C  CA  . GLY D  1 38  ? 89.699  -9.843  33.789 1.00 27.74 ? 37   GLY D CA  1 
ATOM   3595  C  C   . GLY D  1 38  ? 88.887  -8.620  33.404 1.00 27.24 ? 37   GLY D C   1 
ATOM   3596  O  O   . GLY D  1 38  ? 89.127  -7.534  33.928 1.00 26.04 ? 37   GLY D O   1 
ATOM   3597  N  N   . LEU D  1 39  ? 87.911  -8.798  32.516 1.00 26.21 ? 38   LEU D N   1 
ATOM   3598  C  CA  . LEU D  1 39  ? 87.075  -7.696  32.045 1.00 26.03 ? 38   LEU D CA  1 
ATOM   3599  C  C   . LEU D  1 39  ? 85.695  -7.622  32.702 1.00 26.79 ? 38   LEU D C   1 
ATOM   3600  O  O   . LEU D  1 39  ? 85.070  -8.642  32.966 1.00 26.07 ? 38   LEU D O   1 
ATOM   3601  C  CB  . LEU D  1 39  ? 86.874  -7.817  30.531 1.00 23.62 ? 38   LEU D CB  1 
ATOM   3602  C  CG  . LEU D  1 39  ? 88.093  -7.685  29.615 1.00 23.65 ? 38   LEU D CG  1 
ATOM   3603  C  CD1 . LEU D  1 39  ? 87.769  -8.286  28.251 1.00 21.02 ? 38   LEU D CD1 1 
ATOM   3604  C  CD2 . LEU D  1 39  ? 88.482  -6.218  29.491 1.00 22.46 ? 38   LEU D CD2 1 
ATOM   3605  N  N   . THR D  1 40  ? 85.212  -6.411  32.948 1.00 27.83 ? 39   THR D N   1 
ATOM   3606  C  CA  . THR D  1 40  ? 83.888  -6.261  33.541 1.00 29.52 ? 39   THR D CA  1 
ATOM   3607  C  C   . THR D  1 40  ? 82.878  -6.820  32.541 1.00 30.64 ? 39   THR D C   1 
ATOM   3608  O  O   . THR D  1 40  ? 83.078  -6.721  31.324 1.00 29.92 ? 39   THR D O   1 
ATOM   3609  C  CB  . THR D  1 40  ? 83.552  -4.784  33.814 1.00 28.01 ? 39   THR D CB  1 
ATOM   3610  O  OG1 . THR D  1 40  ? 83.623  -4.041  32.589 1.00 27.73 ? 39   THR D OG1 1 
ATOM   3611  C  CG2 . THR D  1 40  ? 84.529  -4.195  34.822 1.00 29.05 ? 39   THR D CG2 1 
ATOM   3612  N  N   . GLU D  1 41  ? 81.799  -7.407  33.045 1.00 29.39 ? 40   GLU D N   1 
ATOM   3613  C  CA  . GLU D  1 41  ? 80.788  -7.989  32.170 1.00 30.44 ? 40   GLU D CA  1 
ATOM   3614  C  C   . GLU D  1 41  ? 80.244  -6.959  31.194 1.00 27.80 ? 40   GLU D C   1 
ATOM   3615  O  O   . GLU D  1 41  ? 79.986  -5.814  31.559 1.00 30.29 ? 40   GLU D O   1 
ATOM   3616  C  CB  . GLU D  1 41  ? 79.635  -8.589  32.992 1.00 31.92 ? 40   GLU D CB  1 
ATOM   3617  C  CG  . GLU D  1 41  ? 78.653  -9.400  32.143 1.00 38.31 ? 40   GLU D CG  1 
ATOM   3618  C  CD  . GLU D  1 41  ? 77.681  -10.236 32.967 1.00 43.31 ? 40   GLU D CD  1 
ATOM   3619  O  OE1 . GLU D  1 41  ? 76.951  -11.063 32.369 1.00 46.23 ? 40   GLU D OE1 1 
ATOM   3620  O  OE2 . GLU D  1 41  ? 77.644  -10.068 34.204 1.00 44.31 ? 40   GLU D OE2 1 
ATOM   3621  N  N   . GLY D  1 42  ? 80.074  -7.365  29.944 1.00 25.91 ? 41   GLY D N   1 
ATOM   3622  C  CA  . GLY D  1 42  ? 79.554  -6.443  28.953 1.00 24.51 ? 41   GLY D CA  1 
ATOM   3623  C  C   . GLY D  1 42  ? 80.520  -6.106  27.829 1.00 24.86 ? 41   GLY D C   1 
ATOM   3624  O  O   . GLY D  1 42  ? 81.529  -6.789  27.623 1.00 24.04 ? 41   GLY D O   1 
ATOM   3625  N  N   . LEU D  1 43  ? 80.204  -5.032  27.111 1.00 23.90 ? 42   LEU D N   1 
ATOM   3626  C  CA  . LEU D  1 43  ? 80.990  -4.579  25.968 1.00 23.47 ? 42   LEU D CA  1 
ATOM   3627  C  C   . LEU D  1 43  ? 82.254  -3.808  26.304 1.00 22.99 ? 42   LEU D C   1 
ATOM   3628  O  O   . LEU D  1 43  ? 82.305  -3.063  27.278 1.00 23.82 ? 42   LEU D O   1 
ATOM   3629  C  CB  . LEU D  1 43  ? 80.120  -3.705  25.062 1.00 22.08 ? 42   LEU D CB  1 
ATOM   3630  C  CG  . LEU D  1 43  ? 78.859  -4.344  24.475 1.00 24.26 ? 42   LEU D CG  1 
ATOM   3631  C  CD1 . LEU D  1 43  ? 77.906  -3.252  24.018 1.00 24.07 ? 42   LEU D CD1 1 
ATOM   3632  C  CD2 . LEU D  1 43  ? 79.230  -5.268  23.318 1.00 23.20 ? 42   LEU D CD2 1 
ATOM   3633  N  N   . HIS D  1 44  ? 83.269  -3.984  25.466 1.00 21.98 ? 43   HIS D N   1 
ATOM   3634  C  CA  . HIS D  1 44  ? 84.541  -3.288  25.619 1.00 21.09 ? 43   HIS D CA  1 
ATOM   3635  C  C   . HIS D  1 44  ? 85.080  -2.958  24.229 1.00 20.95 ? 43   HIS D C   1 
ATOM   3636  O  O   . HIS D  1 44  ? 85.164  -3.844  23.375 1.00 19.15 ? 43   HIS D O   1 
ATOM   3637  C  CB  . HIS D  1 44  ? 85.549  -4.173  26.360 1.00 21.62 ? 43   HIS D CB  1 
ATOM   3638  C  CG  . HIS D  1 44  ? 85.204  -4.402  27.795 1.00 25.00 ? 43   HIS D CG  1 
ATOM   3639  N  ND1 . HIS D  1 44  ? 85.565  -3.521  28.798 1.00 27.68 ? 43   HIS D ND1 1 
ATOM   3640  C  CD2 . HIS D  1 44  ? 84.488  -5.376  28.404 1.00 26.06 ? 43   HIS D CD2 1 
ATOM   3641  C  CE1 . HIS D  1 44  ? 85.087  -3.943  29.950 1.00 26.06 ? 43   HIS D CE1 1 
ATOM   3642  N  NE2 . HIS D  1 44  ? 84.425  -5.072  29.739 1.00 25.45 ? 43   HIS D NE2 1 
ATOM   3643  N  N   . GLY D  1 45  ? 85.428  -1.689  24.013 1.00 19.72 ? 44   GLY D N   1 
ATOM   3644  C  CA  . GLY D  1 45  ? 85.985  -1.266  22.734 1.00 21.18 ? 44   GLY D CA  1 
ATOM   3645  C  C   . GLY D  1 45  ? 87.177  -2.134  22.373 1.00 19.65 ? 44   GLY D C   1 
ATOM   3646  O  O   . GLY D  1 45  ? 87.959  -2.500  23.243 1.00 19.90 ? 44   GLY D O   1 
ATOM   3647  N  N   . PHE D  1 46  ? 87.330  -2.441  21.087 1.00 21.11 ? 45   PHE D N   1 
ATOM   3648  C  CA  . PHE D  1 46  ? 88.401  -3.320  20.601 1.00 19.98 ? 45   PHE D CA  1 
ATOM   3649  C  C   . PHE D  1 46  ? 88.921  -2.726  19.283 1.00 19.87 ? 45   PHE D C   1 
ATOM   3650  O  O   . PHE D  1 46  ? 88.248  -2.814  18.262 1.00 18.14 ? 45   PHE D O   1 
ATOM   3651  C  CB  . PHE D  1 46  ? 87.781  -4.707  20.358 1.00 18.72 ? 45   PHE D CB  1 
ATOM   3652  C  CG  . PHE D  1 46  ? 88.773  -5.822  20.146 1.00 19.45 ? 45   PHE D CG  1 
ATOM   3653  C  CD1 . PHE D  1 46  ? 89.694  -6.156  21.135 1.00 19.70 ? 45   PHE D CD1 1 
ATOM   3654  C  CD2 . PHE D  1 46  ? 88.733  -6.586  18.985 1.00 17.92 ? 45   PHE D CD2 1 
ATOM   3655  C  CE1 . PHE D  1 46  ? 90.542  -7.243  20.982 1.00 18.67 ? 45   PHE D CE1 1 
ATOM   3656  C  CE2 . PHE D  1 46  ? 89.578  -7.677  18.821 1.00 21.23 ? 45   PHE D CE2 1 
ATOM   3657  C  CZ  . PHE D  1 46  ? 90.489  -8.004  19.821 1.00 20.14 ? 45   PHE D CZ  1 
ATOM   3658  N  N   . HIS D  1 47  ? 90.109  -2.126  19.298 1.00 19.32 ? 46   HIS D N   1 
ATOM   3659  C  CA  . HIS D  1 47  ? 90.637  -1.499  18.080 1.00 19.48 ? 46   HIS D CA  1 
ATOM   3660  C  C   . HIS D  1 47  ? 92.127  -1.669  17.846 1.00 18.65 ? 46   HIS D C   1 
ATOM   3661  O  O   . HIS D  1 47  ? 92.900  -1.975  18.757 1.00 20.16 ? 46   HIS D O   1 
ATOM   3662  C  CB  . HIS D  1 47  ? 90.387  0.012   18.092 1.00 19.41 ? 46   HIS D CB  1 
ATOM   3663  C  CG  . HIS D  1 47  ? 89.144  0.430   18.817 1.00 19.17 ? 46   HIS D CG  1 
ATOM   3664  N  ND1 . HIS D  1 47  ? 89.175  1.028   20.053 1.00 19.41 ? 46   HIS D ND1 1 
ATOM   3665  C  CD2 . HIS D  1 47  ? 87.841  0.371   18.455 1.00 19.83 ? 46   HIS D CD2 1 
ATOM   3666  C  CE1 . HIS D  1 47  ? 87.941  1.329   20.427 1.00 19.44 ? 46   HIS D CE1 1 
ATOM   3667  N  NE2 . HIS D  1 47  ? 87.114  0.940   19.476 1.00 20.18 ? 46   HIS D NE2 1 
ATOM   3668  N  N   . VAL D  1 48  ? 92.523  -1.430  16.604 1.00 19.24 ? 47   VAL D N   1 
ATOM   3669  C  CA  . VAL D  1 48  ? 93.926  -1.483  16.231 1.00 18.89 ? 47   VAL D CA  1 
ATOM   3670  C  C   . VAL D  1 48  ? 94.355  -0.020  16.226 1.00 20.41 ? 47   VAL D C   1 
ATOM   3671  O  O   . VAL D  1 48  ? 93.779  0.799   15.495 1.00 19.51 ? 47   VAL D O   1 
ATOM   3672  C  CB  . VAL D  1 48  ? 94.129  -2.060  14.817 1.00 19.33 ? 47   VAL D CB  1 
ATOM   3673  C  CG1 . VAL D  1 48  ? 95.585  -1.858  14.379 1.00 19.73 ? 47   VAL D CG1 1 
ATOM   3674  C  CG2 . VAL D  1 48  ? 93.786  -3.538  14.807 1.00 17.73 ? 47   VAL D CG2 1 
ATOM   3675  N  N   . HIS D  1 49  ? 95.329  0.320   17.063 1.00 20.80 ? 48   HIS D N   1 
ATOM   3676  C  CA  . HIS D  1 49  ? 95.815  1.693   17.114 1.00 21.60 ? 48   HIS D CA  1 
ATOM   3677  C  C   . HIS D  1 49  ? 97.042  1.828   16.217 1.00 21.97 ? 48   HIS D C   1 
ATOM   3678  O  O   . HIS D  1 49  ? 97.763  0.860   15.969 1.00 21.38 ? 48   HIS D O   1 
ATOM   3679  C  CB  . HIS D  1 49  ? 96.124  2.111   18.557 1.00 22.23 ? 48   HIS D CB  1 
ATOM   3680  C  CG  . HIS D  1 49  ? 94.897  2.304   19.399 1.00 22.97 ? 48   HIS D CG  1 
ATOM   3681  N  ND1 . HIS D  1 49  ? 94.635  3.477   20.077 1.00 21.87 ? 48   HIS D ND1 1 
ATOM   3682  C  CD2 . HIS D  1 49  ? 93.856  1.478   19.653 1.00 19.91 ? 48   HIS D CD2 1 
ATOM   3683  C  CE1 . HIS D  1 49  ? 93.480  3.362   20.714 1.00 21.19 ? 48   HIS D CE1 1 
ATOM   3684  N  NE2 . HIS D  1 49  ? 92.988  2.160   20.475 1.00 21.54 ? 48   HIS D NE2 1 
ATOM   3685  N  N   . GLU D  1 50  ? 97.262  3.041   15.732 1.00 23.02 ? 49   GLU D N   1 
ATOM   3686  C  CA  . GLU D  1 50  ? 98.345  3.336   14.807 1.00 23.45 ? 49   GLU D CA  1 
ATOM   3687  C  C   . GLU D  1 50  ? 99.762  2.850   15.119 1.00 23.21 ? 49   GLU D C   1 
ATOM   3688  O  O   . GLU D  1 50  ? 100.374 2.183   14.291 1.00 24.88 ? 49   GLU D O   1 
ATOM   3689  C  CB  . GLU D  1 50  ? 98.392  4.844   14.541 1.00 24.40 ? 49   GLU D CB  1 
ATOM   3690  C  CG  . GLU D  1 50  ? 99.344  5.237   13.419 1.00 24.71 ? 49   GLU D CG  1 
ATOM   3691  C  CD  . GLU D  1 50  ? 99.285  6.713   13.094 1.00 27.73 ? 49   GLU D CD  1 
ATOM   3692  O  OE1 . GLU D  1 50  ? 99.942  7.132   12.123 1.00 29.72 ? 49   GLU D OE1 1 
ATOM   3693  O  OE2 . GLU D  1 50  ? 98.579  7.455   13.807 1.00 29.10 ? 49   GLU D OE2 1 
ATOM   3694  N  N   . PHE D  1 51  ? 100.283 3.165   16.299 1.00 24.91 ? 50   PHE D N   1 
ATOM   3695  C  CA  . PHE D  1 51  ? 101.663 2.789   16.618 1.00 26.40 ? 50   PHE D CA  1 
ATOM   3696  C  C   . PHE D  1 51  ? 101.892 1.567   17.506 1.00 26.36 ? 50   PHE D C   1 
ATOM   3697  O  O   . PHE D  1 51  ? 101.200 1.367   18.501 1.00 27.78 ? 50   PHE D O   1 
ATOM   3698  C  CB  . PHE D  1 51  ? 102.377 3.999   17.237 1.00 25.82 ? 50   PHE D CB  1 
ATOM   3699  C  CG  . PHE D  1 51  ? 102.197 5.272   16.453 1.00 27.71 ? 50   PHE D CG  1 
ATOM   3700  C  CD1 . PHE D  1 51  ? 102.636 5.360   15.138 1.00 29.72 ? 50   PHE D CD1 1 
ATOM   3701  C  CD2 . PHE D  1 51  ? 101.549 6.368   17.015 1.00 28.32 ? 50   PHE D CD2 1 
ATOM   3702  C  CE1 . PHE D  1 51  ? 102.428 6.517   14.391 1.00 31.20 ? 50   PHE D CE1 1 
ATOM   3703  C  CE2 . PHE D  1 51  ? 101.336 7.532   16.274 1.00 28.81 ? 50   PHE D CE2 1 
ATOM   3704  C  CZ  . PHE D  1 51  ? 101.775 7.604   14.961 1.00 28.60 ? 50   PHE D CZ  1 
ATOM   3705  N  N   . GLY D  1 52  ? 102.882 0.759   17.131 1.00 25.06 ? 51   GLY D N   1 
ATOM   3706  C  CA  . GLY D  1 52  ? 103.237 -0.415  17.910 1.00 26.04 ? 51   GLY D CA  1 
ATOM   3707  C  C   . GLY D  1 52  ? 104.321 0.032   18.879 1.00 26.76 ? 51   GLY D C   1 
ATOM   3708  O  O   . GLY D  1 52  ? 105.385 -0.569  18.981 1.00 25.93 ? 51   GLY D O   1 
ATOM   3709  N  N   . ASP D  1 53  ? 104.029 1.112   19.589 1.00 26.98 ? 52   ASP D N   1 
ATOM   3710  C  CA  . ASP D  1 53  ? 104.965 1.713   20.531 1.00 28.39 ? 52   ASP D CA  1 
ATOM   3711  C  C   . ASP D  1 53  ? 104.472 1.548   21.969 1.00 28.73 ? 52   ASP D C   1 
ATOM   3712  O  O   . ASP D  1 53  ? 103.516 2.195   22.387 1.00 28.79 ? 52   ASP D O   1 
ATOM   3713  C  CB  . ASP D  1 53  ? 105.115 3.194   20.166 1.00 27.79 ? 52   ASP D CB  1 
ATOM   3714  C  CG  . ASP D  1 53  ? 106.051 3.949   21.093 1.00 30.46 ? 52   ASP D CG  1 
ATOM   3715  O  OD1 . ASP D  1 53  ? 106.432 5.083   20.732 1.00 29.63 ? 52   ASP D OD1 1 
ATOM   3716  O  OD2 . ASP D  1 53  ? 106.391 3.429   22.174 1.00 30.29 ? 52   ASP D OD2 1 
ATOM   3717  N  N   . ASN D  1 54  ? 105.138 0.678   22.722 1.00 30.61 ? 53   ASN D N   1 
ATOM   3718  C  CA  . ASN D  1 54  ? 104.761 0.418   24.106 1.00 32.92 ? 53   ASN D CA  1 
ATOM   3719  C  C   . ASN D  1 54  ? 105.707 1.100   25.096 1.00 34.26 ? 53   ASN D C   1 
ATOM   3720  O  O   . ASN D  1 54  ? 105.791 0.692   26.252 1.00 34.29 ? 53   ASN D O   1 
ATOM   3721  C  CB  . ASN D  1 54  ? 104.765 -1.092  24.370 1.00 33.92 ? 53   ASN D CB  1 
ATOM   3722  C  CG  . ASN D  1 54  ? 104.081 -1.464  25.680 1.00 37.01 ? 53   ASN D CG  1 
ATOM   3723  O  OD1 . ASN D  1 54  ? 104.439 -2.452  26.318 1.00 39.48 ? 53   ASN D OD1 1 
ATOM   3724  N  ND2 . ASN D  1 54  ? 103.083 -0.683  26.073 1.00 38.05 ? 53   ASN D ND2 1 
ATOM   3725  N  N   . THR D  1 55  ? 106.412 2.136   24.655 1.00 34.84 ? 54   THR D N   1 
ATOM   3726  C  CA  . THR D  1 55  ? 107.345 2.817   25.549 1.00 36.24 ? 54   THR D CA  1 
ATOM   3727  C  C   . THR D  1 55  ? 106.649 3.399   26.771 1.00 36.61 ? 54   THR D C   1 
ATOM   3728  O  O   . THR D  1 55  ? 107.205 3.386   27.867 1.00 37.90 ? 54   THR D O   1 
ATOM   3729  C  CB  . THR D  1 55  ? 108.131 3.937   24.823 1.00 35.16 ? 54   THR D CB  1 
ATOM   3730  O  OG1 . THR D  1 55  ? 107.222 4.890   24.261 1.00 36.63 ? 54   THR D OG1 1 
ATOM   3731  C  CG2 . THR D  1 55  ? 108.986 3.347   23.723 1.00 35.91 ? 54   THR D CG2 1 
ATOM   3732  N  N   . ALA D  1 56  ? 105.433 3.906   26.590 1.00 37.83 ? 55   ALA D N   1 
ATOM   3733  C  CA  . ALA D  1 56  ? 104.674 4.468   27.702 1.00 36.63 ? 55   ALA D CA  1 
ATOM   3734  C  C   . ALA D  1 56  ? 103.345 3.735   27.844 1.00 37.11 ? 55   ALA D C   1 
ATOM   3735  O  O   . ALA D  1 56  ? 102.276 4.342   27.781 1.00 37.29 ? 55   ALA D O   1 
ATOM   3736  C  CB  . ALA D  1 56  ? 104.434 5.962   27.481 1.00 36.90 ? 55   ALA D CB  1 
ATOM   3737  N  N   . GLY D  1 57  ? 103.416 2.423   28.028 1.00 36.94 ? 56   GLY D N   1 
ATOM   3738  C  CA  . GLY D  1 57  ? 102.205 1.638   28.173 1.00 38.02 ? 56   GLY D CA  1 
ATOM   3739  C  C   . GLY D  1 57  ? 101.357 1.659   26.914 1.00 37.51 ? 56   GLY D C   1 
ATOM   3740  O  O   . GLY D  1 57  ? 101.888 1.713   25.805 1.00 38.86 ? 56   GLY D O   1 
ATOM   3741  N  N   . CYS D  1 58  ? 100.040 1.621   27.081 1.00 35.80 ? 57   CYS D N   1 
ATOM   3742  C  CA  . CYS D  1 58  ? 99.128  1.625   25.943 1.00 34.81 ? 57   CYS D CA  1 
ATOM   3743  C  C   . CYS D  1 58  ? 98.895  3.030   25.404 1.00 34.27 ? 57   CYS D C   1 
ATOM   3744  O  O   . CYS D  1 58  ? 98.385  3.202   24.298 1.00 33.76 ? 57   CYS D O   1 
ATOM   3745  C  CB  . CYS D  1 58  ? 97.788  0.995   26.337 1.00 32.24 ? 57   CYS D CB  1 
ATOM   3746  S  SG  . CYS D  1 58  ? 97.954  -0.721  26.914 1.00 30.65 ? 57   CYS D SG  1 
ATOM   3747  N  N   . THR D  1 59  ? 99.287  4.030   26.188 1.00 33.28 ? 58   THR D N   1 
ATOM   3748  C  CA  . THR D  1 59  ? 99.110  5.427   25.806 1.00 32.43 ? 58   THR D CA  1 
ATOM   3749  C  C   . THR D  1 59  ? 99.926  5.828   24.582 1.00 31.14 ? 58   THR D C   1 
ATOM   3750  O  O   . THR D  1 59  ? 99.492  6.659   23.783 1.00 31.88 ? 58   THR D O   1 
ATOM   3751  C  CB  . THR D  1 59  ? 99.489  6.367   26.967 1.00 33.89 ? 58   THR D CB  1 
ATOM   3752  O  OG1 . THR D  1 59  ? 98.725  6.021   28.127 1.00 37.59 ? 58   THR D OG1 1 
ATOM   3753  C  CG2 . THR D  1 59  ? 99.199  7.811   26.600 1.00 34.81 ? 58   THR D CG2 1 
ATOM   3754  N  N   . SER D  1 60  ? 101.106 5.240   24.429 1.00 28.41 ? 59   SER D N   1 
ATOM   3755  C  CA  . SER D  1 60  ? 101.956 5.573   23.296 1.00 28.20 ? 59   SER D CA  1 
ATOM   3756  C  C   . SER D  1 60  ? 101.569 4.888   21.981 1.00 28.08 ? 59   SER D C   1 
ATOM   3757  O  O   . SER D  1 60  ? 102.244 5.066   20.965 1.00 28.48 ? 59   SER D O   1 
ATOM   3758  C  CB  . SER D  1 60  ? 103.428 5.287   23.637 1.00 26.11 ? 59   SER D CB  1 
ATOM   3759  O  OG  . SER D  1 60  ? 103.585 4.046   24.296 1.00 28.37 ? 59   SER D OG  1 
ATOM   3760  N  N   . ALA D  1 61  ? 100.478 4.125   21.988 1.00 26.04 ? 60   ALA D N   1 
ATOM   3761  C  CA  . ALA D  1 61  ? 100.033 3.447   20.766 1.00 24.95 ? 60   ALA D CA  1 
ATOM   3762  C  C   . ALA D  1 61  ? 99.355  4.436   19.824 1.00 25.47 ? 60   ALA D C   1 
ATOM   3763  O  O   . ALA D  1 61  ? 99.050  4.111   18.675 1.00 26.98 ? 60   ALA D O   1 
ATOM   3764  C  CB  . ALA D  1 61  ? 99.067  2.313   21.109 1.00 21.43 ? 60   ALA D CB  1 
ATOM   3765  N  N   . GLY D  1 62  ? 99.109  5.643   20.319 1.00 25.45 ? 61   GLY D N   1 
ATOM   3766  C  CA  . GLY D  1 62  ? 98.467  6.656   19.502 1.00 26.86 ? 61   GLY D CA  1 
ATOM   3767  C  C   . GLY D  1 62  ? 96.973  6.426   19.319 1.00 25.69 ? 61   GLY D C   1 
ATOM   3768  O  O   . GLY D  1 62  ? 96.365  5.656   20.064 1.00 24.35 ? 61   GLY D O   1 
ATOM   3769  N  N   . PRO D  1 63  ? 96.354  7.093   18.335 1.00 25.32 ? 62   PRO D N   1 
ATOM   3770  C  CA  . PRO D  1 63  ? 94.927  6.987   18.023 1.00 24.61 ? 62   PRO D CA  1 
ATOM   3771  C  C   . PRO D  1 63  ? 94.645  5.730   17.203 1.00 23.48 ? 62   PRO D C   1 
ATOM   3772  O  O   . PRO D  1 63  ? 95.546  4.935   16.951 1.00 23.23 ? 62   PRO D O   1 
ATOM   3773  C  CB  . PRO D  1 63  ? 94.668  8.254   17.227 1.00 23.46 ? 62   PRO D CB  1 
ATOM   3774  C  CG  . PRO D  1 63  ? 95.933  8.375   16.430 1.00 25.05 ? 62   PRO D CG  1 
ATOM   3775  C  CD  . PRO D  1 63  ? 97.005  8.084   17.456 1.00 25.41 ? 62   PRO D CD  1 
ATOM   3776  N  N   . HIS D  1 64  ? 93.396  5.556   16.783 1.00 23.99 ? 63   HIS D N   1 
ATOM   3777  C  CA  . HIS D  1 64  ? 93.033  4.385   15.985 1.00 24.25 ? 63   HIS D CA  1 
ATOM   3778  C  C   . HIS D  1 64  ? 93.736  4.456   14.639 1.00 23.82 ? 63   HIS D C   1 
ATOM   3779  O  O   . HIS D  1 64  ? 93.894  5.538   14.081 1.00 22.82 ? 63   HIS D O   1 
ATOM   3780  C  CB  . HIS D  1 64  ? 91.521  4.337   15.750 1.00 23.28 ? 63   HIS D CB  1 
ATOM   3781  C  CG  . HIS D  1 64  ? 90.714  4.235   17.008 1.00 24.42 ? 63   HIS D CG  1 
ATOM   3782  N  ND1 . HIS D  1 64  ? 89.338  4.212   17.008 1.00 23.11 ? 63   HIS D ND1 1 
ATOM   3783  C  CD2 . HIS D  1 64  ? 91.092  4.143   18.306 1.00 25.07 ? 63   HIS D CD2 1 
ATOM   3784  C  CE1 . HIS D  1 64  ? 88.900  4.112   18.253 1.00 23.91 ? 63   HIS D CE1 1 
ATOM   3785  N  NE2 . HIS D  1 64  ? 89.948  4.069   19.057 1.00 27.08 ? 63   HIS D NE2 1 
ATOM   3786  N  N   . PHE D  1 65  ? 94.163  3.303   14.130 1.00 22.22 ? 64   PHE D N   1 
ATOM   3787  C  CA  . PHE D  1 65  ? 94.822  3.229   12.832 1.00 22.68 ? 64   PHE D CA  1 
ATOM   3788  C  C   . PHE D  1 65  ? 93.794  3.809   11.851 1.00 24.27 ? 64   PHE D C   1 
ATOM   3789  O  O   . PHE D  1 65  ? 92.707  3.247   11.686 1.00 22.21 ? 64   PHE D O   1 
ATOM   3790  C  CB  . PHE D  1 65  ? 95.133  1.764   12.502 1.00 21.63 ? 64   PHE D CB  1 
ATOM   3791  C  CG  . PHE D  1 65  ? 95.857  1.563   11.193 1.00 24.88 ? 64   PHE D CG  1 
ATOM   3792  C  CD1 . PHE D  1 65  ? 95.659  0.399   10.454 1.00 23.31 ? 64   PHE D CD1 1 
ATOM   3793  C  CD2 . PHE D  1 65  ? 96.736  2.527   10.702 1.00 24.55 ? 64   PHE D CD2 1 
ATOM   3794  C  CE1 . PHE D  1 65  ? 96.314  0.199   9.238  1.00 26.63 ? 64   PHE D CE1 1 
ATOM   3795  C  CE2 . PHE D  1 65  ? 97.396  2.337   9.488  1.00 25.66 ? 64   PHE D CE2 1 
ATOM   3796  C  CZ  . PHE D  1 65  ? 97.188  1.170   8.757  1.00 26.34 ? 64   PHE D CZ  1 
ATOM   3797  N  N   . ASN D  1 66  ? 94.136  4.925   11.207 1.00 22.75 ? 65   ASN D N   1 
ATOM   3798  C  CA  . ASN D  1 66  ? 93.209  5.603   10.299 1.00 24.80 ? 65   ASN D CA  1 
ATOM   3799  C  C   . ASN D  1 66  ? 93.907  6.200   9.076  1.00 27.67 ? 65   ASN D C   1 
ATOM   3800  O  O   . ASN D  1 66  ? 93.942  7.414   8.896  1.00 27.21 ? 65   ASN D O   1 
ATOM   3801  C  CB  . ASN D  1 66  ? 92.484  6.700   11.088 1.00 23.36 ? 65   ASN D CB  1 
ATOM   3802  C  CG  . ASN D  1 66  ? 91.455  7.442   10.269 1.00 25.37 ? 65   ASN D CG  1 
ATOM   3803  O  OD1 . ASN D  1 66  ? 90.875  6.898   9.331  1.00 26.31 ? 65   ASN D OD1 1 
ATOM   3804  N  ND2 . ASN D  1 66  ? 91.200  8.693   10.641 1.00 26.38 ? 65   ASN D ND2 1 
ATOM   3805  N  N   . PRO D  1 67  ? 94.461  5.344   8.210  1.00 28.07 ? 66   PRO D N   1 
ATOM   3806  C  CA  . PRO D  1 67  ? 95.155  5.823   7.014  1.00 30.42 ? 66   PRO D CA  1 
ATOM   3807  C  C   . PRO D  1 67  ? 94.279  6.572   5.999  1.00 33.90 ? 66   PRO D C   1 
ATOM   3808  O  O   . PRO D  1 67  ? 94.779  7.418   5.256  1.00 33.80 ? 66   PRO D O   1 
ATOM   3809  C  CB  . PRO D  1 67  ? 95.768  4.547   6.443  1.00 29.52 ? 66   PRO D CB  1 
ATOM   3810  C  CG  . PRO D  1 67  ? 94.756  3.504   6.817  1.00 31.16 ? 66   PRO D CG  1 
ATOM   3811  C  CD  . PRO D  1 67  ? 94.408  3.871   8.243  1.00 26.16 ? 66   PRO D CD  1 
ATOM   3812  N  N   . LEU D  1 68  ? 92.980  6.281   5.974  1.00 33.77 ? 67   LEU D N   1 
ATOM   3813  C  CA  . LEU D  1 68  ? 92.084  6.943   5.029  1.00 34.90 ? 67   LEU D CA  1 
ATOM   3814  C  C   . LEU D  1 68  ? 91.480  8.226   5.590  1.00 36.00 ? 67   LEU D C   1 
ATOM   3815  O  O   . LEU D  1 68  ? 90.623  8.846   4.960  1.00 36.64 ? 67   LEU D O   1 
ATOM   3816  C  CB  . LEU D  1 68  ? 90.970  5.985   4.593  1.00 37.52 ? 67   LEU D CB  1 
ATOM   3817  C  CG  . LEU D  1 68  ? 91.438  4.661   3.979  1.00 39.04 ? 67   LEU D CG  1 
ATOM   3818  C  CD1 . LEU D  1 68  ? 90.248  3.894   3.415  1.00 40.12 ? 67   LEU D CD1 1 
ATOM   3819  C  CD2 . LEU D  1 68  ? 92.447  4.944   2.882  1.00 42.36 ? 67   LEU D CD2 1 
ATOM   3820  N  N   . SER D  1 69  ? 91.935  8.613   6.779  1.00 35.29 ? 68   SER D N   1 
ATOM   3821  C  CA  . SER D  1 69  ? 91.477  9.826   7.450  1.00 36.93 ? 68   SER D CA  1 
ATOM   3822  C  C   . SER D  1 69  ? 89.958  9.991   7.512  1.00 37.05 ? 68   SER D C   1 
ATOM   3823  O  O   . SER D  1 69  ? 89.422  11.034  7.132  1.00 35.82 ? 68   SER D O   1 
ATOM   3824  C  CB  . SER D  1 69  ? 92.093  11.059  6.778  1.00 39.24 ? 68   SER D CB  1 
ATOM   3825  O  OG  . SER D  1 69  ? 93.509  11.016  6.827  1.00 41.73 ? 68   SER D OG  1 
ATOM   3826  N  N   . ARG D  1 70  ? 89.265  8.968   8.005  1.00 35.47 ? 69   ARG D N   1 
ATOM   3827  C  CA  . ARG D  1 70  ? 87.813  9.027   8.120  1.00 33.87 ? 69   ARG D CA  1 
ATOM   3828  C  C   . ARG D  1 70  ? 87.417  9.155   9.589  1.00 31.68 ? 69   ARG D C   1 
ATOM   3829  O  O   . ARG D  1 70  ? 88.274  9.161   10.469 1.00 30.65 ? 69   ARG D O   1 
ATOM   3830  C  CB  . ARG D  1 70  ? 87.184  7.769   7.511  1.00 36.24 ? 69   ARG D CB  1 
ATOM   3831  C  CG  . ARG D  1 70  ? 87.476  7.582   6.017  1.00 38.73 ? 69   ARG D CG  1 
ATOM   3832  C  CD  . ARG D  1 70  ? 86.703  6.397   5.437  1.00 43.21 ? 69   ARG D CD  1 
ATOM   3833  N  NE  . ARG D  1 70  ? 87.073  6.108   4.051  1.00 45.72 ? 69   ARG D NE  1 
ATOM   3834  C  CZ  . ARG D  1 70  ? 86.562  5.114   3.326  1.00 47.71 ? 69   ARG D CZ  1 
ATOM   3835  N  NH1 . ARG D  1 70  ? 86.962  4.925   2.075  1.00 47.57 ? 69   ARG D NH1 1 
ATOM   3836  N  NH2 . ARG D  1 70  ? 85.647  4.308   3.846  1.00 49.09 ? 69   ARG D NH2 1 
ATOM   3837  N  N   . LYS D  1 71  ? 86.121  9.267   9.854  1.00 31.53 ? 70   LYS D N   1 
ATOM   3838  C  CA  . LYS D  1 71  ? 85.643  9.380   11.227 1.00 30.35 ? 70   LYS D CA  1 
ATOM   3839  C  C   . LYS D  1 71  ? 85.496  7.987   11.838 1.00 28.76 ? 70   LYS D C   1 
ATOM   3840  O  O   . LYS D  1 71  ? 85.474  6.987   11.117 1.00 26.65 ? 70   LYS D O   1 
ATOM   3841  C  CB  . LYS D  1 71  ? 84.295  10.107  11.264 1.00 32.75 ? 70   LYS D CB  1 
ATOM   3842  C  CG  . LYS D  1 71  ? 84.350  11.565  10.820 1.00 36.34 ? 70   LYS D CG  1 
ATOM   3843  C  CD  . LYS D  1 71  ? 85.200  12.407  11.757 1.00 37.94 ? 70   LYS D CD  1 
ATOM   3844  C  CE  . LYS D  1 71  ? 85.184  13.867  11.337 0.00 37.87 ? 70   LYS D CE  1 
ATOM   3845  N  NZ  . LYS D  1 71  ? 83.792  14.368  11.168 0.00 38.24 ? 70   LYS D NZ  1 
ATOM   3846  N  N   . HIS D  1 72  ? 85.395  7.924   13.165 1.00 25.49 ? 71   HIS D N   1 
ATOM   3847  C  CA  . HIS D  1 72  ? 85.247  6.646   13.861 1.00 23.88 ? 71   HIS D CA  1 
ATOM   3848  C  C   . HIS D  1 72  ? 83.869  6.029   13.595 1.00 24.27 ? 71   HIS D C   1 
ATOM   3849  O  O   . HIS D  1 72  ? 82.872  6.738   13.473 1.00 24.85 ? 71   HIS D O   1 
ATOM   3850  C  CB  . HIS D  1 72  ? 85.422  6.844   15.372 1.00 22.81 ? 71   HIS D CB  1 
ATOM   3851  C  CG  . HIS D  1 72  ? 85.272  5.584   16.169 1.00 22.01 ? 71   HIS D CG  1 
ATOM   3852  N  ND1 . HIS D  1 72  ? 86.293  4.670   16.317 1.00 20.53 ? 71   HIS D ND1 1 
ATOM   3853  C  CD2 . HIS D  1 72  ? 84.210  5.078   16.841 1.00 19.27 ? 71   HIS D CD2 1 
ATOM   3854  C  CE1 . HIS D  1 72  ? 85.866  3.655   17.051 1.00 19.67 ? 71   HIS D CE1 1 
ATOM   3855  N  NE2 . HIS D  1 72  ? 84.608  3.878   17.381 1.00 19.57 ? 71   HIS D NE2 1 
ATOM   3856  N  N   . GLY D  1 73  ? 83.816  4.706   13.511 1.00 23.94 ? 72   GLY D N   1 
ATOM   3857  C  CA  . GLY D  1 73  ? 82.546  4.040   13.282 1.00 22.94 ? 72   GLY D CA  1 
ATOM   3858  C  C   . GLY D  1 73  ? 82.599  2.594   13.728 1.00 23.65 ? 72   GLY D C   1 
ATOM   3859  O  O   . GLY D  1 73  ? 83.563  2.174   14.373 1.00 22.55 ? 72   GLY D O   1 
ATOM   3860  N  N   . GLY D  1 74  ? 81.553  1.836   13.411 1.00 21.40 ? 73   GLY D N   1 
ATOM   3861  C  CA  . GLY D  1 74  ? 81.531  0.428   13.763 1.00 20.94 ? 73   GLY D CA  1 
ATOM   3862  C  C   . GLY D  1 74  ? 82.136  -0.342  12.601 1.00 20.13 ? 73   GLY D C   1 
ATOM   3863  O  O   . GLY D  1 74  ? 82.195  0.187   11.491 1.00 19.93 ? 73   GLY D O   1 
ATOM   3864  N  N   . PRO D  1 75  ? 82.581  -1.593  12.807 1.00 20.86 ? 74   PRO D N   1 
ATOM   3865  C  CA  . PRO D  1 75  ? 83.177  -2.365  11.712 1.00 21.79 ? 74   PRO D CA  1 
ATOM   3866  C  C   . PRO D  1 75  ? 82.310  -2.533  10.455 1.00 25.41 ? 74   PRO D C   1 
ATOM   3867  O  O   . PRO D  1 75  ? 82.840  -2.689  9.350  1.00 24.31 ? 74   PRO D O   1 
ATOM   3868  C  CB  . PRO D  1 75  ? 83.525  -3.702  12.379 1.00 22.73 ? 74   PRO D CB  1 
ATOM   3869  C  CG  . PRO D  1 75  ? 82.538  -3.795  13.522 1.00 22.63 ? 74   PRO D CG  1 
ATOM   3870  C  CD  . PRO D  1 75  ? 82.531  -2.387  14.047 1.00 18.74 ? 74   PRO D CD  1 
ATOM   3871  N  N   . LYS D  1 76  ? 80.990  -2.491  10.618 1.00 25.30 ? 75   LYS D N   1 
ATOM   3872  C  CA  . LYS D  1 76  ? 80.078  -2.652  9.484  1.00 27.20 ? 75   LYS D CA  1 
ATOM   3873  C  C   . LYS D  1 76  ? 79.873  -1.365  8.685  1.00 27.05 ? 75   LYS D C   1 
ATOM   3874  O  O   . LYS D  1 76  ? 79.356  -1.401  7.569  1.00 27.68 ? 75   LYS D O   1 
ATOM   3875  C  CB  . LYS D  1 76  ? 78.719  -3.168  9.976  1.00 29.77 ? 75   LYS D CB  1 
ATOM   3876  C  CG  . LYS D  1 76  ? 78.793  -4.504  10.712 1.00 31.31 ? 75   LYS D CG  1 
ATOM   3877  C  CD  . LYS D  1 76  ? 77.504  -4.798  11.484 1.00 37.18 ? 75   LYS D CD  1 
ATOM   3878  C  CE  . LYS D  1 76  ? 76.305  -4.936  10.552 1.00 38.48 ? 75   LYS D CE  1 
ATOM   3879  N  NZ  . LYS D  1 76  ? 75.069  -5.299  11.297 1.00 43.10 ? 75   LYS D NZ  1 
ATOM   3880  N  N   . ASP D  1 77  ? 80.276  -0.233  9.254  1.00 25.61 ? 76   ASP D N   1 
ATOM   3881  C  CA  . ASP D  1 77  ? 80.131  1.066   8.596  1.00 27.04 ? 76   ASP D CA  1 
ATOM   3882  C  C   . ASP D  1 77  ? 81.172  1.289   7.500  1.00 28.82 ? 76   ASP D C   1 
ATOM   3883  O  O   . ASP D  1 77  ? 82.309  0.844   7.620  1.00 26.06 ? 76   ASP D O   1 
ATOM   3884  C  CB  . ASP D  1 77  ? 80.285  2.196   9.619  1.00 26.74 ? 76   ASP D CB  1 
ATOM   3885  C  CG  . ASP D  1 77  ? 79.185  2.208   10.649 1.00 26.93 ? 76   ASP D CG  1 
ATOM   3886  O  OD1 . ASP D  1 77  ? 79.446  2.662   11.781 1.00 27.13 ? 76   ASP D OD1 1 
ATOM   3887  O  OD2 . ASP D  1 77  ? 78.059  1.782   10.325 1.00 30.62 ? 76   ASP D OD2 1 
ATOM   3888  N  N   . GLU D  1 78  ? 80.790  1.989   6.438  1.00 30.33 ? 77   GLU D N   1 
ATOM   3889  C  CA  . GLU D  1 78  ? 81.755  2.283   5.385  1.00 33.13 ? 77   GLU D CA  1 
ATOM   3890  C  C   . GLU D  1 78  ? 82.641  3.385   5.955  1.00 31.79 ? 77   GLU D C   1 
ATOM   3891  O  O   . GLU D  1 78  ? 83.855  3.389   5.756  1.00 31.60 ? 77   GLU D O   1 
ATOM   3892  C  CB  . GLU D  1 78  ? 81.075  2.785   4.112  1.00 37.22 ? 77   GLU D CB  1 
ATOM   3893  C  CG  . GLU D  1 78  ? 82.078  3.014   2.984  1.00 46.79 ? 77   GLU D CG  1 
ATOM   3894  C  CD  . GLU D  1 78  ? 81.461  3.649   1.757  1.00 50.92 ? 77   GLU D CD  1 
ATOM   3895  O  OE1 . GLU D  1 78  ? 81.039  4.823   1.844  1.00 54.42 ? 77   GLU D OE1 1 
ATOM   3896  O  OE2 . GLU D  1 78  ? 81.400  2.974   0.706  1.00 54.19 ? 77   GLU D OE2 1 
ATOM   3897  N  N   . GLU D  1 79  ? 82.022  4.321   6.670  1.00 28.74 ? 78   GLU D N   1 
ATOM   3898  C  CA  . GLU D  1 79  ? 82.759  5.406   7.299  1.00 28.18 ? 78   GLU D CA  1 
ATOM   3899  C  C   . GLU D  1 79  ? 83.308  4.909   8.641  1.00 27.50 ? 78   GLU D C   1 
ATOM   3900  O  O   . GLU D  1 79  ? 82.597  4.878   9.650  1.00 27.72 ? 78   GLU D O   1 
ATOM   3901  C  CB  . GLU D  1 79  ? 81.846  6.611   7.527  1.00 30.43 ? 78   GLU D CB  1 
ATOM   3902  C  CG  . GLU D  1 79  ? 82.538  7.820   8.153  1.00 33.88 ? 78   GLU D CG  1 
ATOM   3903  C  CD  . GLU D  1 79  ? 83.530  8.502   7.219  1.00 37.81 ? 78   GLU D CD  1 
ATOM   3904  O  OE1 . GLU D  1 79  ? 84.179  9.477   7.659  1.00 34.71 ? 78   GLU D OE1 1 
ATOM   3905  O  OE2 . GLU D  1 79  ? 83.661  8.071   6.049  1.00 40.06 ? 78   GLU D OE2 1 
ATOM   3906  N  N   . ARG D  1 80  ? 84.574  4.511   8.645  1.00 25.21 ? 79   ARG D N   1 
ATOM   3907  C  CA  . ARG D  1 80  ? 85.215  4.023   9.857  1.00 25.51 ? 79   ARG D CA  1 
ATOM   3908  C  C   . ARG D  1 80  ? 86.722  4.089   9.710  1.00 25.60 ? 79   ARG D C   1 
ATOM   3909  O  O   . ARG D  1 80  ? 87.240  4.286   8.607  1.00 24.26 ? 79   ARG D O   1 
ATOM   3910  C  CB  . ARG D  1 80  ? 84.823  2.569   10.120 1.00 23.41 ? 79   ARG D CB  1 
ATOM   3911  C  CG  . ARG D  1 80  ? 85.227  1.614   9.001  1.00 25.68 ? 79   ARG D CG  1 
ATOM   3912  C  CD  . ARG D  1 80  ? 86.226  0.569   9.494  1.00 30.48 ? 79   ARG D CD  1 
ATOM   3913  N  NE  . ARG D  1 80  ? 85.666  -0.764  9.394  1.00 29.07 ? 79   ARG D NE  1 
ATOM   3914  C  CZ  . ARG D  1 80  ? 86.302  -1.891  9.692  1.00 27.62 ? 79   ARG D CZ  1 
ATOM   3915  N  NH1 . ARG D  1 80  ? 85.662  -3.041  9.549  1.00 26.74 ? 79   ARG D NH1 1 
ATOM   3916  N  NH2 . ARG D  1 80  ? 87.557  -1.882  10.130 1.00 23.73 ? 79   ARG D NH2 1 
ATOM   3917  N  N   . HIS D  1 81  ? 87.409  3.927   10.836 1.00 22.90 ? 80   HIS D N   1 
ATOM   3918  C  CA  . HIS D  1 81  ? 88.864  3.902   10.871 1.00 22.98 ? 80   HIS D CA  1 
ATOM   3919  C  C   . HIS D  1 81  ? 89.201  2.480   10.467 1.00 22.74 ? 80   HIS D C   1 
ATOM   3920  O  O   . HIS D  1 81  ? 88.440  1.560   10.771 1.00 20.17 ? 80   HIS D O   1 
ATOM   3921  C  CB  . HIS D  1 81  ? 89.372  4.134   12.300 1.00 22.17 ? 80   HIS D CB  1 
ATOM   3922  C  CG  . HIS D  1 81  ? 89.083  5.496   12.835 1.00 22.15 ? 80   HIS D CG  1 
ATOM   3923  N  ND1 . HIS D  1 81  ? 88.879  5.744   14.178 1.00 22.76 ? 80   HIS D ND1 1 
ATOM   3924  C  CD2 . HIS D  1 81  ? 89.004  6.705   12.222 1.00 21.91 ? 80   HIS D CD2 1 
ATOM   3925  C  CE1 . HIS D  1 81  ? 88.690  7.034   14.368 1.00 22.47 ? 80   HIS D CE1 1 
ATOM   3926  N  NE2 . HIS D  1 81  ? 88.762  7.641   13.191 1.00 23.27 ? 80   HIS D NE2 1 
ATOM   3927  N  N   . VAL D  1 82  ? 90.319  2.281   9.779  1.00 20.77 ? 81   VAL D N   1 
ATOM   3928  C  CA  . VAL D  1 82  ? 90.693  0.926   9.403  1.00 19.44 ? 81   VAL D CA  1 
ATOM   3929  C  C   . VAL D  1 82  ? 90.770  0.050   10.656 1.00 19.45 ? 81   VAL D C   1 
ATOM   3930  O  O   . VAL D  1 82  ? 90.424  -1.131  10.626 1.00 18.18 ? 81   VAL D O   1 
ATOM   3931  C  CB  . VAL D  1 82  ? 92.063  0.900   8.680  1.00 19.11 ? 81   VAL D CB  1 
ATOM   3932  C  CG1 . VAL D  1 82  ? 92.647  -0.501  8.707  1.00 19.08 ? 81   VAL D CG1 1 
ATOM   3933  C  CG2 . VAL D  1 82  ? 91.886  1.357   7.231  1.00 18.15 ? 81   VAL D CG2 1 
ATOM   3934  N  N   . GLY D  1 83  ? 91.211  0.636   11.763 1.00 20.51 ? 82   GLY D N   1 
ATOM   3935  C  CA  . GLY D  1 83  ? 91.338  -0.132  12.991 1.00 20.48 ? 82   GLY D CA  1 
ATOM   3936  C  C   . GLY D  1 83  ? 90.083  -0.364  13.819 1.00 20.41 ? 82   GLY D C   1 
ATOM   3937  O  O   . GLY D  1 83  ? 90.165  -1.009  14.861 1.00 19.00 ? 82   GLY D O   1 
ATOM   3938  N  N   . ASP D  1 84  ? 88.929  0.135   13.373 1.00 21.02 ? 83   ASP D N   1 
ATOM   3939  C  CA  . ASP D  1 84  ? 87.684  -0.031  14.133 1.00 20.74 ? 83   ASP D CA  1 
ATOM   3940  C  C   . ASP D  1 84  ? 87.073  -1.430  14.071 1.00 21.01 ? 83   ASP D C   1 
ATOM   3941  O  O   . ASP D  1 84  ? 86.336  -1.764  13.138 1.00 19.47 ? 83   ASP D O   1 
ATOM   3942  C  CB  . ASP D  1 84  ? 86.643  1.003   13.680 1.00 19.60 ? 83   ASP D CB  1 
ATOM   3943  C  CG  . ASP D  1 84  ? 87.060  2.424   14.000 1.00 18.05 ? 83   ASP D CG  1 
ATOM   3944  O  OD1 . ASP D  1 84  ? 87.928  2.594   14.879 1.00 20.34 ? 83   ASP D OD1 1 
ATOM   3945  O  OD2 . ASP D  1 84  ? 86.521  3.369   13.385 1.00 19.00 ? 83   ASP D OD2 1 
ATOM   3946  N  N   . LEU D  1 85  ? 87.365  -2.244  15.082 1.00 20.84 ? 84   LEU D N   1 
ATOM   3947  C  CA  . LEU D  1 85  ? 86.839  -3.600  15.128 1.00 19.90 ? 84   LEU D CA  1 
ATOM   3948  C  C   . LEU D  1 85  ? 85.611  -3.739  16.035 1.00 21.21 ? 84   LEU D C   1 
ATOM   3949  O  O   . LEU D  1 85  ? 85.144  -4.850  16.293 1.00 22.25 ? 84   LEU D O   1 
ATOM   3950  C  CB  . LEU D  1 85  ? 87.944  -4.570  15.554 1.00 18.63 ? 84   LEU D CB  1 
ATOM   3951  C  CG  . LEU D  1 85  ? 89.088  -4.660  14.537 1.00 20.24 ? 84   LEU D CG  1 
ATOM   3952  C  CD1 . LEU D  1 85  ? 90.188  -5.571  15.069 1.00 20.60 ? 84   LEU D CD1 1 
ATOM   3953  C  CD2 . LEU D  1 85  ? 88.539  -5.185  13.201 1.00 19.82 ? 84   LEU D CD2 1 
ATOM   3954  N  N   . GLY D  1 86  ? 85.091  -2.612  16.512 1.00 19.49 ? 85   GLY D N   1 
ATOM   3955  C  CA  . GLY D  1 86  ? 83.899  -2.641  17.348 1.00 18.54 ? 85   GLY D CA  1 
ATOM   3956  C  C   . GLY D  1 86  ? 84.123  -3.023  18.803 1.00 20.79 ? 85   GLY D C   1 
ATOM   3957  O  O   . GLY D  1 86  ? 85.029  -2.506  19.452 1.00 19.06 ? 85   GLY D O   1 
ATOM   3958  N  N   . ASN D  1 87  ? 83.294  -3.935  19.305 1.00 19.00 ? 86   ASN D N   1 
ATOM   3959  C  CA  . ASN D  1 87  ? 83.376  -4.393  20.692 1.00 19.41 ? 86   ASN D CA  1 
ATOM   3960  C  C   . ASN D  1 87  ? 83.564  -5.896  20.812 1.00 20.98 ? 86   ASN D C   1 
ATOM   3961  O  O   . ASN D  1 87  ? 83.267  -6.651  19.878 1.00 19.13 ? 86   ASN D O   1 
ATOM   3962  C  CB  . ASN D  1 87  ? 82.078  -4.069  21.439 1.00 18.19 ? 86   ASN D CB  1 
ATOM   3963  C  CG  . ASN D  1 87  ? 81.855  -2.596  21.633 1.00 17.23 ? 86   ASN D CG  1 
ATOM   3964  O  OD1 . ASN D  1 87  ? 82.565  -1.946  22.400 1.00 18.20 ? 86   ASN D OD1 1 
ATOM   3965  N  ND2 . ASN D  1 87  ? 80.859  -2.055  20.947 1.00 18.39 ? 86   ASN D ND2 1 
ATOM   3966  N  N   . VAL D  1 88  ? 84.059  -6.316  21.975 1.00 19.60 ? 87   VAL D N   1 
ATOM   3967  C  CA  . VAL D  1 88  ? 84.176  -7.727  22.301 1.00 21.84 ? 87   VAL D CA  1 
ATOM   3968  C  C   . VAL D  1 88  ? 83.318  -7.821  23.566 1.00 22.60 ? 87   VAL D C   1 
ATOM   3969  O  O   . VAL D  1 88  ? 83.144  -6.824  24.275 1.00 21.53 ? 87   VAL D O   1 
ATOM   3970  C  CB  . VAL D  1 88  ? 85.631  -8.180  22.585 1.00 23.16 ? 87   VAL D CB  1 
ATOM   3971  C  CG1 . VAL D  1 88  ? 86.463  -8.066  21.298 1.00 23.23 ? 87   VAL D CG1 1 
ATOM   3972  C  CG2 . VAL D  1 88  ? 86.240  -7.362  23.705 1.00 22.44 ? 87   VAL D CG2 1 
ATOM   3973  N  N   . THR D  1 89  ? 82.768  -8.994  23.845 1.00 21.54 ? 88   THR D N   1 
ATOM   3974  C  CA  . THR D  1 89  ? 81.899  -9.157  25.005 1.00 22.26 ? 88   THR D CA  1 
ATOM   3975  C  C   . THR D  1 89  ? 82.462  -10.102 26.049 1.00 23.59 ? 88   THR D C   1 
ATOM   3976  O  O   . THR D  1 89  ? 82.813  -11.243 25.743 1.00 24.90 ? 88   THR D O   1 
ATOM   3977  C  CB  . THR D  1 89  ? 80.500  -9.675  24.575 1.00 23.50 ? 88   THR D CB  1 
ATOM   3978  O  OG1 . THR D  1 89  ? 79.870  -8.700  23.738 1.00 23.74 ? 88   THR D OG1 1 
ATOM   3979  C  CG2 . THR D  1 89  ? 79.604  -9.935  25.799 1.00 23.08 ? 88   THR D CG2 1 
ATOM   3980  N  N   . ALA D  1 90  ? 82.549  -9.612  27.283 1.00 22.37 ? 89   ALA D N   1 
ATOM   3981  C  CA  . ALA D  1 90  ? 83.040  -10.401 28.402 1.00 24.15 ? 89   ALA D CA  1 
ATOM   3982  C  C   . ALA D  1 90  ? 81.815  -10.949 29.136 1.00 25.55 ? 89   ALA D C   1 
ATOM   3983  O  O   . ALA D  1 90  ? 80.821  -10.230 29.331 1.00 24.21 ? 89   ALA D O   1 
ATOM   3984  C  CB  . ALA D  1 90  ? 83.863  -9.533  29.335 1.00 25.24 ? 89   ALA D CB  1 
ATOM   3985  N  N   . ASP D  1 91  ? 81.891  -12.217 29.529 1.00 26.82 ? 90   ASP D N   1 
ATOM   3986  C  CA  . ASP D  1 91  ? 80.797  -12.885 30.226 1.00 28.40 ? 90   ASP D CA  1 
ATOM   3987  C  C   . ASP D  1 91  ? 80.809  -12.562 31.716 1.00 29.07 ? 90   ASP D C   1 
ATOM   3988  O  O   . ASP D  1 91  ? 81.617  -11.752 32.167 1.00 29.33 ? 90   ASP D O   1 
ATOM   3989  C  CB  . ASP D  1 91  ? 80.883  -14.401 29.990 1.00 28.07 ? 90   ASP D CB  1 
ATOM   3990  C  CG  . ASP D  1 91  ? 82.161  -15.014 30.536 1.00 29.99 ? 90   ASP D CG  1 
ATOM   3991  O  OD1 . ASP D  1 91  ? 82.519  -16.120 30.081 1.00 31.46 ? 90   ASP D OD1 1 
ATOM   3992  O  OD2 . ASP D  1 91  ? 82.801  -14.409 31.424 1.00 32.35 ? 90   ASP D OD2 1 
ATOM   3993  N  N   . LYS D  1 92  ? 79.911  -13.191 32.473 1.00 31.32 ? 91   LYS D N   1 
ATOM   3994  C  CA  . LYS D  1 92  ? 79.798  -12.959 33.914 1.00 33.37 ? 91   LYS D CA  1 
ATOM   3995  C  C   . LYS D  1 92  ? 81.077  -13.285 34.679 1.00 32.17 ? 91   LYS D C   1 
ATOM   3996  O  O   . LYS D  1 92  ? 81.271  -12.819 35.801 1.00 33.18 ? 91   LYS D O   1 
ATOM   3997  C  CB  . LYS D  1 92  ? 78.636  -13.777 34.495 1.00 35.32 ? 91   LYS D CB  1 
ATOM   3998  C  CG  . LYS D  1 92  ? 78.811  -15.283 34.371 1.00 40.37 ? 91   LYS D CG  1 
ATOM   3999  C  CD  . LYS D  1 92  ? 77.605  -16.025 34.934 1.00 43.87 ? 91   LYS D CD  1 
ATOM   4000  C  CE  . LYS D  1 92  ? 77.803  -17.532 34.875 1.00 46.44 ? 91   LYS D CE  1 
ATOM   4001  N  NZ  . LYS D  1 92  ? 78.017  -18.020 33.483 1.00 48.20 ? 91   LYS D NZ  1 
ATOM   4002  N  N   . ASP D  1 93  ? 81.939  -14.095 34.076 1.00 32.42 ? 92   ASP D N   1 
ATOM   4003  C  CA  . ASP D  1 93  ? 83.206  -14.468 34.697 1.00 32.15 ? 92   ASP D CA  1 
ATOM   4004  C  C   . ASP D  1 93  ? 84.300  -13.480 34.307 1.00 31.87 ? 92   ASP D C   1 
ATOM   4005  O  O   . ASP D  1 93  ? 85.438  -13.590 34.762 1.00 31.07 ? 92   ASP D O   1 
ATOM   4006  C  CB  . ASP D  1 93  ? 83.612  -15.872 34.253 1.00 35.30 ? 92   ASP D CB  1 
ATOM   4007  C  CG  . ASP D  1 93  ? 82.704  -16.944 34.820 1.00 39.13 ? 92   ASP D CG  1 
ATOM   4008  O  OD1 . ASP D  1 93  ? 82.502  -17.975 34.140 1.00 40.40 ? 92   ASP D OD1 1 
ATOM   4009  O  OD2 . ASP D  1 93  ? 82.201  -16.757 35.951 1.00 38.48 ? 92   ASP D OD2 1 
ATOM   4010  N  N   . GLY D  1 94  ? 83.953  -12.523 33.452 1.00 29.25 ? 93   GLY D N   1 
ATOM   4011  C  CA  . GLY D  1 94  ? 84.928  -11.538 33.016 1.00 29.57 ? 93   GLY D CA  1 
ATOM   4012  C  C   . GLY D  1 94  ? 85.777  -12.012 31.847 1.00 28.71 ? 93   GLY D C   1 
ATOM   4013  O  O   . GLY D  1 94  ? 86.825  -11.435 31.559 1.00 28.60 ? 93   GLY D O   1 
ATOM   4014  N  N   . VAL D  1 95  ? 85.324  -13.058 31.168 1.00 26.43 ? 94   VAL D N   1 
ATOM   4015  C  CA  . VAL D  1 95  ? 86.061  -13.600 30.037 1.00 26.21 ? 94   VAL D CA  1 
ATOM   4016  C  C   . VAL D  1 95  ? 85.400  -13.318 28.693 1.00 26.14 ? 94   VAL D C   1 
ATOM   4017  O  O   . VAL D  1 95  ? 84.203  -13.563 28.498 1.00 25.34 ? 94   VAL D O   1 
ATOM   4018  C  CB  . VAL D  1 95  ? 86.259  -15.124 30.171 1.00 29.80 ? 94   VAL D CB  1 
ATOM   4019  C  CG1 . VAL D  1 95  ? 86.874  -15.687 28.883 1.00 28.98 ? 94   VAL D CG1 1 
ATOM   4020  C  CG2 . VAL D  1 95  ? 87.170  -15.425 31.358 1.00 29.28 ? 94   VAL D CG2 1 
ATOM   4021  N  N   . ALA D  1 96  ? 86.194  -12.793 27.767 1.00 23.85 ? 95   ALA D N   1 
ATOM   4022  C  CA  . ALA D  1 96  ? 85.705  -12.494 26.430 1.00 25.04 ? 95   ALA D CA  1 
ATOM   4023  C  C   . ALA D  1 96  ? 86.318  -13.484 25.442 1.00 25.60 ? 95   ALA D C   1 
ATOM   4024  O  O   . ALA D  1 96  ? 87.530  -13.502 25.236 1.00 26.64 ? 95   ALA D O   1 
ATOM   4025  C  CB  . ALA D  1 96  ? 86.071  -11.063 26.036 1.00 24.64 ? 95   ALA D CB  1 
ATOM   4026  N  N   . ASP D  1 97  ? 85.483  -14.336 24.865 1.00 25.15 ? 96   ASP D N   1 
ATOM   4027  C  CA  . ASP D  1 97  ? 85.961  -15.288 23.877 1.00 26.31 ? 96   ASP D CA  1 
ATOM   4028  C  C   . ASP D  1 97  ? 85.735  -14.570 22.556 1.00 25.55 ? 96   ASP D C   1 
ATOM   4029  O  O   . ASP D  1 97  ? 84.663  -14.627 21.957 1.00 27.29 ? 96   ASP D O   1 
ATOM   4030  C  CB  . ASP D  1 97  ? 85.172  -16.589 23.967 1.00 28.86 ? 96   ASP D CB  1 
ATOM   4031  C  CG  . ASP D  1 97  ? 85.516  -17.383 25.220 1.00 33.38 ? 96   ASP D CG  1 
ATOM   4032  O  OD1 . ASP D  1 97  ? 84.603  -17.668 26.020 1.00 36.19 ? 96   ASP D OD1 1 
ATOM   4033  O  OD2 . ASP D  1 97  ? 86.710  -17.714 25.405 1.00 35.15 ? 96   ASP D OD2 1 
ATOM   4034  N  N   . VAL D  1 98  ? 86.768  -13.864 22.128 1.00 22.82 ? 97   VAL D N   1 
ATOM   4035  C  CA  . VAL D  1 98  ? 86.708  -13.063 20.918 1.00 22.20 ? 97   VAL D CA  1 
ATOM   4036  C  C   . VAL D  1 98  ? 86.580  -13.855 19.629 1.00 21.46 ? 97   VAL D C   1 
ATOM   4037  O  O   . VAL D  1 98  ? 87.292  -14.831 19.412 1.00 21.57 ? 97   VAL D O   1 
ATOM   4038  C  CB  . VAL D  1 98  ? 87.950  -12.154 20.831 1.00 20.10 ? 97   VAL D CB  1 
ATOM   4039  C  CG1 . VAL D  1 98  ? 87.920  -11.331 19.553 1.00 20.00 ? 97   VAL D CG1 1 
ATOM   4040  C  CG2 . VAL D  1 98  ? 87.995  -11.242 22.056 1.00 21.17 ? 97   VAL D CG2 1 
ATOM   4041  N  N   . SER D  1 99  ? 85.658  -13.425 18.777 1.00 23.10 ? 98   SER D N   1 
ATOM   4042  C  CA  . SER D  1 99  ? 85.468  -14.064 17.483 1.00 25.86 ? 98   SER D CA  1 
ATOM   4043  C  C   . SER D  1 99  ? 84.925  -13.019 16.536 1.00 25.86 ? 98   SER D C   1 
ATOM   4044  O  O   . SER D  1 99  ? 83.741  -12.686 16.555 1.00 28.06 ? 98   SER D O   1 
ATOM   4045  C  CB  . SER D  1 99  ? 84.506  -15.245 17.576 1.00 30.02 ? 98   SER D CB  1 
ATOM   4046  O  OG  . SER D  1 99  ? 84.551  -15.987 16.366 1.00 34.73 ? 98   SER D OG  1 
ATOM   4047  N  N   . ILE D  1 100 ? 85.813  -12.495 15.705 1.00 25.13 ? 99   ILE D N   1 
ATOM   4048  C  CA  . ILE D  1 100 ? 85.459  -11.455 14.758 1.00 24.14 ? 99   ILE D CA  1 
ATOM   4049  C  C   . ILE D  1 100 ? 86.044  -11.778 13.389 1.00 23.09 ? 99   ILE D C   1 
ATOM   4050  O  O   . ILE D  1 100 ? 87.063  -12.457 13.282 1.00 24.31 ? 99   ILE D O   1 
ATOM   4051  C  CB  . ILE D  1 100 ? 86.034  -10.089 15.237 1.00 24.58 ? 99   ILE D CB  1 
ATOM   4052  C  CG1 . ILE D  1 100 ? 85.282  -9.612  16.482 1.00 24.14 ? 99   ILE D CG1 1 
ATOM   4053  C  CG2 . ILE D  1 100 ? 85.976  -9.054  14.112 1.00 25.59 ? 99   ILE D CG2 1 
ATOM   4054  C  CD1 . ILE D  1 100 ? 85.959  -8.435  17.204 1.00 20.47 ? 99   ILE D CD1 1 
ATOM   4055  N  N   . GLU D  1 101 ? 85.378  -11.304 12.345 1.00 24.12 ? 100  GLU D N   1 
ATOM   4056  C  CA  . GLU D  1 101 ? 85.869  -11.474 10.984 1.00 24.65 ? 100  GLU D CA  1 
ATOM   4057  C  C   . GLU D  1 101 ? 85.739  -10.092 10.362 1.00 23.05 ? 100  GLU D C   1 
ATOM   4058  O  O   . GLU D  1 101 ? 84.667  -9.478  10.399 1.00 22.74 ? 100  GLU D O   1 
ATOM   4059  C  CB  . GLU D  1 101 ? 85.047  -12.516 10.211 1.00 27.55 ? 100  GLU D CB  1 
ATOM   4060  C  CG  . GLU D  1 101 ? 85.598  -12.787 8.813  1.00 35.90 ? 100  GLU D CG  1 
ATOM   4061  C  CD  . GLU D  1 101 ? 85.187  -14.144 8.254  1.00 39.29 ? 100  GLU D CD  1 
ATOM   4062  O  OE1 . GLU D  1 101 ? 85.453  -14.397 7.062  1.00 40.79 ? 100  GLU D OE1 1 
ATOM   4063  O  OE2 . GLU D  1 101 ? 84.612  -14.962 9.006  1.00 43.22 ? 100  GLU D OE2 1 
ATOM   4064  N  N   . ASP D  1 102 ? 86.834  -9.588  9.809  1.00 21.39 ? 101  ASP D N   1 
ATOM   4065  C  CA  . ASP D  1 102 ? 86.818  -8.255  9.233  1.00 21.76 ? 101  ASP D CA  1 
ATOM   4066  C  C   . ASP D  1 102 ? 87.533  -8.185  7.889  1.00 21.71 ? 101  ASP D C   1 
ATOM   4067  O  O   . ASP D  1 102 ? 88.608  -8.765  7.716  1.00 20.77 ? 101  ASP D O   1 
ATOM   4068  C  CB  . ASP D  1 102 ? 87.450  -7.275  10.227 1.00 19.64 ? 101  ASP D CB  1 
ATOM   4069  C  CG  . ASP D  1 102 ? 87.202  -5.836  9.858  1.00 21.61 ? 101  ASP D CG  1 
ATOM   4070  O  OD1 . ASP D  1 102 ? 88.074  -5.218  9.215  1.00 21.62 ? 101  ASP D OD1 1 
ATOM   4071  O  OD2 . ASP D  1 102 ? 86.121  -5.325  10.207 1.00 19.29 ? 101  ASP D OD2 1 
ATOM   4072  N  N   . SER D  1 103 ? 86.934  -7.452  6.953  1.00 22.16 ? 102  SER D N   1 
ATOM   4073  C  CA  . SER D  1 103 ? 87.487  -7.308  5.606  1.00 25.13 ? 102  SER D CA  1 
ATOM   4074  C  C   . SER D  1 103 ? 88.148  -5.966  5.331  1.00 24.34 ? 102  SER D C   1 
ATOM   4075  O  O   . SER D  1 103 ? 88.556  -5.697  4.204  1.00 25.05 ? 102  SER D O   1 
ATOM   4076  C  CB  . SER D  1 103 ? 86.392  -7.539  4.563  1.00 27.22 ? 102  SER D CB  1 
ATOM   4077  O  OG  . SER D  1 103 ? 85.882  -8.857  4.661  1.00 34.03 ? 102  SER D OG  1 
ATOM   4078  N  N   . VAL D  1 104 ? 88.243  -5.118  6.348  1.00 22.69 ? 103  VAL D N   1 
ATOM   4079  C  CA  . VAL D  1 104 ? 88.875  -3.818  6.175  1.00 23.01 ? 103  VAL D CA  1 
ATOM   4080  C  C   . VAL D  1 104 ? 90.322  -3.895  6.650  1.00 23.63 ? 103  VAL D C   1 
ATOM   4081  O  O   . VAL D  1 104 ? 91.221  -3.398  5.977  1.00 23.10 ? 103  VAL D O   1 
ATOM   4082  C  CB  . VAL D  1 104 ? 88.101  -2.716  6.930  1.00 23.37 ? 103  VAL D CB  1 
ATOM   4083  C  CG1 . VAL D  1 104 ? 88.875  -1.399  6.903  1.00 23.84 ? 103  VAL D CG1 1 
ATOM   4084  C  CG2 . VAL D  1 104 ? 86.747  -2.524  6.276  1.00 25.63 ? 103  VAL D CG2 1 
ATOM   4085  N  N   . ILE D  1 105 ? 90.561  -4.514  7.804  1.00 20.54 ? 104  ILE D N   1 
ATOM   4086  C  CA  . ILE D  1 105 ? 91.941  -4.659  8.261  1.00 21.57 ? 104  ILE D CA  1 
ATOM   4087  C  C   . ILE D  1 105 ? 92.584  -5.708  7.355  1.00 22.32 ? 104  ILE D C   1 
ATOM   4088  O  O   . ILE D  1 105 ? 91.887  -6.481  6.694  1.00 21.52 ? 104  ILE D O   1 
ATOM   4089  C  CB  . ILE D  1 105 ? 92.047  -5.175  9.716  1.00 21.95 ? 104  ILE D CB  1 
ATOM   4090  C  CG1 . ILE D  1 105 ? 91.302  -6.510  9.853  1.00 21.12 ? 104  ILE D CG1 1 
ATOM   4091  C  CG2 . ILE D  1 105 ? 91.534  -4.123  10.676 1.00 20.41 ? 104  ILE D CG2 1 
ATOM   4092  C  CD1 . ILE D  1 105 ? 91.537  -7.224  11.185 1.00 19.39 ? 104  ILE D CD1 1 
ATOM   4093  N  N   . SER D  1 106 ? 93.909  -5.737  7.323  1.00 22.11 ? 105  SER D N   1 
ATOM   4094  C  CA  . SER D  1 106 ? 94.622  -6.712  6.513  1.00 21.36 ? 105  SER D CA  1 
ATOM   4095  C  C   . SER D  1 106 ? 95.939  -7.049  7.200  1.00 21.86 ? 105  SER D C   1 
ATOM   4096  O  O   . SER D  1 106 ? 96.362  -6.336  8.111  1.00 22.03 ? 105  SER D O   1 
ATOM   4097  C  CB  . SER D  1 106 ? 94.905  -6.148  5.115  1.00 22.99 ? 105  SER D CB  1 
ATOM   4098  O  OG  . SER D  1 106 ? 95.403  -7.165  4.262  1.00 21.21 ? 105  SER D OG  1 
ATOM   4099  N  N   . LEU D  1 107 ? 96.571  -8.144  6.785  1.00 20.22 ? 106  LEU D N   1 
ATOM   4100  C  CA  . LEU D  1 107 ? 97.852  -8.523  7.359  1.00 22.08 ? 106  LEU D CA  1 
ATOM   4101  C  C   . LEU D  1 107 ? 98.985  -8.181  6.381  1.00 24.05 ? 106  LEU D C   1 
ATOM   4102  O  O   . LEU D  1 107 ? 100.131 -8.598  6.567  1.00 22.74 ? 106  LEU D O   1 
ATOM   4103  C  CB  . LEU D  1 107 ? 97.872  -10.016 7.723  1.00 20.13 ? 106  LEU D CB  1 
ATOM   4104  C  CG  . LEU D  1 107 ? 96.861  -10.445 8.806  1.00 22.93 ? 106  LEU D CG  1 
ATOM   4105  C  CD1 . LEU D  1 107 ? 97.157  -11.867 9.256  1.00 21.16 ? 106  LEU D CD1 1 
ATOM   4106  C  CD2 . LEU D  1 107 ? 96.944  -9.500  10.003 1.00 21.59 ? 106  LEU D CD2 1 
ATOM   4107  N  N   . SER D  1 108 ? 98.652  -7.422  5.337  1.00 25.80 ? 107  SER D N   1 
ATOM   4108  C  CA  . SER D  1 108 ? 99.643  -6.981  4.357  1.00 29.05 ? 107  SER D CA  1 
ATOM   4109  C  C   . SER D  1 108 ? 99.120  -5.757  3.610  1.00 30.63 ? 107  SER D C   1 
ATOM   4110  O  O   . SER D  1 108 ? 97.919  -5.478  3.626  1.00 29.40 ? 107  SER D O   1 
ATOM   4111  C  CB  . SER D  1 108 ? 99.974  -8.099  3.359  1.00 30.88 ? 107  SER D CB  1 
ATOM   4112  O  OG  . SER D  1 108 ? 98.928  -8.299  2.429  1.00 34.79 ? 107  SER D OG  1 
ATOM   4113  N  N   . GLY D  1 109 ? 100.031 -5.018  2.978  1.00 30.79 ? 108  GLY D N   1 
ATOM   4114  C  CA  . GLY D  1 109 ? 99.648  -3.834  2.229  1.00 29.88 ? 108  GLY D CA  1 
ATOM   4115  C  C   . GLY D  1 109 ? 99.465  -2.580  3.063  1.00 30.99 ? 108  GLY D C   1 
ATOM   4116  O  O   . GLY D  1 109 ? 99.836  -2.539  4.239  1.00 31.93 ? 108  GLY D O   1 
ATOM   4117  N  N   . ASP D  1 110 ? 98.881  -1.558  2.441  1.00 29.64 ? 109  ASP D N   1 
ATOM   4118  C  CA  . ASP D  1 110 ? 98.617  -0.263  3.076  1.00 30.76 ? 109  ASP D CA  1 
ATOM   4119  C  C   . ASP D  1 110 ? 97.736  -0.324  4.326  1.00 28.48 ? 109  ASP D C   1 
ATOM   4120  O  O   . ASP D  1 110 ? 97.825  0.538   5.193  1.00 27.97 ? 109  ASP D O   1 
ATOM   4121  C  CB  . ASP D  1 110 ? 97.923  0.683   2.087  1.00 32.10 ? 109  ASP D CB  1 
ATOM   4122  C  CG  . ASP D  1 110 ? 98.872  1.281   1.074  1.00 38.32 ? 109  ASP D CG  1 
ATOM   4123  O  OD1 . ASP D  1 110 ? 98.438  2.193   0.336  1.00 38.08 ? 109  ASP D OD1 1 
ATOM   4124  O  OD2 . ASP D  1 110 ? 100.042 0.845   1.014  1.00 38.84 ? 109  ASP D OD2 1 
ATOM   4125  N  N   . HIS D  1 111 ? 96.860  -1.317  4.399  1.00 27.07 ? 110  HIS D N   1 
ATOM   4126  C  CA  . HIS D  1 111 ? 95.958  -1.426  5.538  1.00 27.53 ? 110  HIS D CA  1 
ATOM   4127  C  C   . HIS D  1 111 ? 96.381  -2.500  6.529  1.00 25.26 ? 110  HIS D C   1 
ATOM   4128  O  O   . HIS D  1 111 ? 95.605  -2.899  7.401  1.00 22.87 ? 110  HIS D O   1 
ATOM   4129  C  CB  . HIS D  1 111 ? 94.535  -1.678  5.032  1.00 30.09 ? 110  HIS D CB  1 
ATOM   4130  C  CG  . HIS D  1 111 ? 93.963  -0.527  4.263  1.00 32.92 ? 110  HIS D CG  1 
ATOM   4131  N  ND1 . HIS D  1 111 ? 92.758  -0.597  3.594  1.00 35.69 ? 110  HIS D ND1 1 
ATOM   4132  C  CD2 . HIS D  1 111 ? 94.421  0.735   4.072  1.00 35.69 ? 110  HIS D CD2 1 
ATOM   4133  C  CE1 . HIS D  1 111 ? 92.499  0.566   3.030  1.00 35.71 ? 110  HIS D CE1 1 
ATOM   4134  N  NE2 . HIS D  1 111 ? 93.491  1.395   3.303  1.00 36.53 ? 110  HIS D NE2 1 
ATOM   4135  N  N   . SER D  1 112 ? 97.620  -2.957  6.392  1.00 24.07 ? 111  SER D N   1 
ATOM   4136  C  CA  . SER D  1 112 ? 98.160  -3.982  7.275  1.00 24.17 ? 111  SER D CA  1 
ATOM   4137  C  C   . SER D  1 112 ? 98.229  -3.481  8.713  1.00 23.60 ? 111  SER D C   1 
ATOM   4138  O  O   . SER D  1 112 ? 98.617  -2.339  8.972  1.00 21.12 ? 111  SER D O   1 
ATOM   4139  C  CB  . SER D  1 112 ? 99.566  -4.385  6.830  1.00 23.42 ? 111  SER D CB  1 
ATOM   4140  O  OG  . SER D  1 112 ? 100.105 -5.345  7.716  1.00 27.22 ? 111  SER D OG  1 
ATOM   4141  N  N   . ILE D  1 113 ? 97.851  -4.340  9.650  1.00 20.81 ? 112  ILE D N   1 
ATOM   4142  C  CA  . ILE D  1 113 ? 97.910  -3.973  11.054 1.00 20.42 ? 112  ILE D CA  1 
ATOM   4143  C  C   . ILE D  1 113 ? 99.167  -4.570  11.706 1.00 20.73 ? 112  ILE D C   1 
ATOM   4144  O  O   . ILE D  1 113 ? 99.376  -4.424  12.911 1.00 20.51 ? 112  ILE D O   1 
ATOM   4145  C  CB  . ILE D  1 113 ? 96.649  -4.448  11.805 1.00 18.76 ? 112  ILE D CB  1 
ATOM   4146  C  CG1 . ILE D  1 113 ? 96.498  -5.965  11.685 1.00 18.62 ? 112  ILE D CG1 1 
ATOM   4147  C  CG2 . ILE D  1 113 ? 95.412  -3.757  11.220 1.00 19.89 ? 112  ILE D CG2 1 
ATOM   4148  C  CD1 . ILE D  1 113 ? 95.309  -6.531  12.485 1.00 19.15 ? 112  ILE D CD1 1 
ATOM   4149  N  N   . ILE D  1 114 ? 100.001 -5.236  10.907 1.00 21.36 ? 113  ILE D N   1 
ATOM   4150  C  CA  . ILE D  1 114 ? 101.237 -5.827  11.424 1.00 21.80 ? 113  ILE D CA  1 
ATOM   4151  C  C   . ILE D  1 114 ? 102.134 -4.716  11.977 1.00 22.84 ? 113  ILE D C   1 
ATOM   4152  O  O   . ILE D  1 114 ? 102.348 -3.699  11.324 1.00 22.89 ? 113  ILE D O   1 
ATOM   4153  C  CB  . ILE D  1 114 ? 102.020 -6.584  10.321 1.00 22.88 ? 113  ILE D CB  1 
ATOM   4154  C  CG1 . ILE D  1 114 ? 101.195 -7.759  9.793  1.00 26.65 ? 113  ILE D CG1 1 
ATOM   4155  C  CG2 . ILE D  1 114 ? 103.348 -7.096  10.878 1.00 23.71 ? 113  ILE D CG2 1 
ATOM   4156  C  CD1 . ILE D  1 114 ? 100.911 -8.841  10.824 1.00 26.56 ? 113  ILE D CD1 1 
ATOM   4157  N  N   . GLY D  1 115 ? 102.645 -4.906  13.188 1.00 22.53 ? 114  GLY D N   1 
ATOM   4158  C  CA  . GLY D  1 115 ? 103.509 -3.906  13.785 1.00 21.62 ? 114  GLY D CA  1 
ATOM   4159  C  C   . GLY D  1 115 ? 102.751 -2.772  14.446 1.00 23.10 ? 114  GLY D C   1 
ATOM   4160  O  O   . GLY D  1 115 ? 103.353 -1.784  14.872 1.00 22.61 ? 114  GLY D O   1 
ATOM   4161  N  N   . ARG D  1 116 ? 101.429 -2.890  14.520 1.00 19.67 ? 115  ARG D N   1 
ATOM   4162  C  CA  . ARG D  1 116 ? 100.638 -1.851  15.164 1.00 20.12 ? 115  ARG D CA  1 
ATOM   4163  C  C   . ARG D  1 116 ? 100.130 -2.399  16.500 1.00 19.42 ? 115  ARG D C   1 
ATOM   4164  O  O   . ARG D  1 116 ? 100.527 -3.488  16.895 1.00 23.06 ? 115  ARG D O   1 
ATOM   4165  C  CB  . ARG D  1 116 ? 99.513  -1.391  14.232 1.00 20.16 ? 115  ARG D CB  1 
ATOM   4166  C  CG  . ARG D  1 116 ? 100.085 -0.761  12.949 1.00 22.78 ? 115  ARG D CG  1 
ATOM   4167  C  CD  . ARG D  1 116 ? 99.034  -0.127  12.054 1.00 24.13 ? 115  ARG D CD  1 
ATOM   4168  N  NE  . ARG D  1 116 ? 99.577  0.173   10.727 1.00 25.53 ? 115  ARG D NE  1 
ATOM   4169  C  CZ  . ARG D  1 116 ? 100.278 1.262   10.420 1.00 25.92 ? 115  ARG D CZ  1 
ATOM   4170  N  NH1 . ARG D  1 116 ? 100.729 1.428   9.180  1.00 25.29 ? 115  ARG D NH1 1 
ATOM   4171  N  NH2 . ARG D  1 116 ? 100.505 2.197   11.335 1.00 21.92 ? 115  ARG D NH2 1 
ATOM   4172  N  N   . THR D  1 117 ? 99.275  -1.669  17.206 1.00 21.54 ? 116  THR D N   1 
ATOM   4173  C  CA  . THR D  1 117 ? 98.831  -2.145  18.521 1.00 20.77 ? 116  THR D CA  1 
ATOM   4174  C  C   . THR D  1 117 ? 97.353  -2.472  18.694 1.00 20.19 ? 116  THR D C   1 
ATOM   4175  O  O   . THR D  1 117 ? 96.487  -1.669  18.350 1.00 20.16 ? 116  THR D O   1 
ATOM   4176  C  CB  . THR D  1 117 ? 99.229  -1.128  19.624 1.00 20.78 ? 116  THR D CB  1 
ATOM   4177  O  OG1 . THR D  1 117 ? 100.659 -1.040  19.699 1.00 20.04 ? 116  THR D OG1 1 
ATOM   4178  C  CG2 . THR D  1 117 ? 98.681  -1.560  20.992 1.00 20.07 ? 116  THR D CG2 1 
ATOM   4179  N  N   . LEU D  1 118 ? 97.081  -3.660  19.236 1.00 19.88 ? 117  LEU D N   1 
ATOM   4180  C  CA  . LEU D  1 118 ? 95.715  -4.099  19.503 1.00 18.39 ? 117  LEU D CA  1 
ATOM   4181  C  C   . LEU D  1 118 ? 95.390  -3.634  20.918 1.00 19.90 ? 117  LEU D C   1 
ATOM   4182  O  O   . LEU D  1 118 ? 96.150  -3.912  21.845 1.00 22.68 ? 117  LEU D O   1 
ATOM   4183  C  CB  . LEU D  1 118 ? 95.608  -5.623  19.439 1.00 19.80 ? 117  LEU D CB  1 
ATOM   4184  C  CG  . LEU D  1 118 ? 94.188  -6.144  19.682 1.00 17.40 ? 117  LEU D CG  1 
ATOM   4185  C  CD1 . LEU D  1 118 ? 93.277  -5.609  18.588 1.00 18.73 ? 117  LEU D CD1 1 
ATOM   4186  C  CD2 . LEU D  1 118 ? 94.170  -7.659  19.704 1.00 19.81 ? 117  LEU D CD2 1 
ATOM   4187  N  N   . VAL D  1 119 ? 94.265  -2.945  21.084 1.00 18.67 ? 118  VAL D N   1 
ATOM   4188  C  CA  . VAL D  1 119 ? 93.869  -2.418  22.391 1.00 20.33 ? 118  VAL D CA  1 
ATOM   4189  C  C   . VAL D  1 119 ? 92.456  -2.820  22.823 1.00 21.10 ? 118  VAL D C   1 
ATOM   4190  O  O   . VAL D  1 119 ? 91.527  -2.791  22.013 1.00 19.83 ? 118  VAL D O   1 
ATOM   4191  C  CB  . VAL D  1 119 ? 93.924  -0.868  22.378 1.00 19.99 ? 118  VAL D CB  1 
ATOM   4192  C  CG1 . VAL D  1 119 ? 93.536  -0.301  23.739 1.00 20.90 ? 118  VAL D CG1 1 
ATOM   4193  C  CG2 . VAL D  1 119 ? 95.325  -0.401  21.996 1.00 22.55 ? 118  VAL D CG2 1 
ATOM   4194  N  N   . VAL D  1 120 ? 92.294  -3.210  24.088 1.00 20.95 ? 119  VAL D N   1 
ATOM   4195  C  CA  . VAL D  1 120 ? 90.961  -3.521  24.601 1.00 19.71 ? 119  VAL D CA  1 
ATOM   4196  C  C   . VAL D  1 120 ? 90.648  -2.413  25.621 1.00 21.26 ? 119  VAL D C   1 
ATOM   4197  O  O   . VAL D  1 120 ? 91.488  -2.058  26.463 1.00 20.42 ? 119  VAL D O   1 
ATOM   4198  C  CB  . VAL D  1 120 ? 90.871  -4.949  25.215 1.00 20.32 ? 119  VAL D CB  1 
ATOM   4199  C  CG1 . VAL D  1 120 ? 91.797  -5.102  26.408 1.00 20.40 ? 119  VAL D CG1 1 
ATOM   4200  C  CG2 . VAL D  1 120 ? 89.415  -5.245  25.590 1.00 21.36 ? 119  VAL D CG2 1 
ATOM   4201  N  N   . HIS D  1 121 ? 89.442  -1.858  25.520 1.00 21.57 ? 120  HIS D N   1 
ATOM   4202  C  CA  . HIS D  1 121 ? 89.029  -0.719  26.334 1.00 21.29 ? 120  HIS D CA  1 
ATOM   4203  C  C   . HIS D  1 121 ? 88.192  -0.902  27.586 1.00 22.34 ? 120  HIS D C   1 
ATOM   4204  O  O   . HIS D  1 121 ? 87.572  -1.937  27.819 1.00 21.20 ? 120  HIS D O   1 
ATOM   4205  C  CB  . HIS D  1 121 ? 88.324  0.301   25.436 1.00 20.41 ? 120  HIS D CB  1 
ATOM   4206  C  CG  . HIS D  1 121 ? 89.243  0.993   24.474 1.00 21.31 ? 120  HIS D CG  1 
ATOM   4207  N  ND1 . HIS D  1 121 ? 89.884  2.173   24.775 1.00 20.18 ? 120  HIS D ND1 1 
ATOM   4208  C  CD2 . HIS D  1 121 ? 89.646  0.645   23.229 1.00 19.70 ? 120  HIS D CD2 1 
ATOM   4209  C  CE1 . HIS D  1 121 ? 90.646  2.528   23.754 1.00 20.37 ? 120  HIS D CE1 1 
ATOM   4210  N  NE2 . HIS D  1 121 ? 90.522  1.620   22.806 1.00 19.76 ? 120  HIS D NE2 1 
ATOM   4211  N  N   . GLU D  1 122 ? 88.181  0.167   28.374 1.00 24.47 ? 121  GLU D N   1 
ATOM   4212  C  CA  . GLU D  1 122 ? 87.456  0.244   29.632 1.00 25.12 ? 121  GLU D CA  1 
ATOM   4213  C  C   . GLU D  1 122 ? 85.950  0.196   29.425 1.00 25.21 ? 121  GLU D C   1 
ATOM   4214  O  O   . GLU D  1 122 ? 85.244  -0.505  30.144 1.00 26.22 ? 121  GLU D O   1 
ATOM   4215  C  CB  . GLU D  1 122 ? 87.820  1.553   30.335 1.00 27.27 ? 121  GLU D CB  1 
ATOM   4216  C  CG  . GLU D  1 122 ? 87.102  1.801   31.651 1.00 33.26 ? 121  GLU D CG  1 
ATOM   4217  C  CD  . GLU D  1 122 ? 87.132  3.270   32.060 1.00 37.88 ? 121  GLU D CD  1 
ATOM   4218  O  OE1 . GLU D  1 122 ? 86.904  3.549   33.256 1.00 41.39 ? 121  GLU D OE1 1 
ATOM   4219  O  OE2 . GLU D  1 122 ? 87.372  4.145   31.189 1.00 34.42 ? 121  GLU D OE2 1 
ATOM   4220  N  N   . LYS D  1 123 ? 85.468  0.946   28.437 1.00 24.41 ? 122  LYS D N   1 
ATOM   4221  C  CA  . LYS D  1 123 ? 84.036  1.028   28.157 1.00 25.69 ? 122  LYS D CA  1 
ATOM   4222  C  C   . LYS D  1 123 ? 83.646  0.525   26.773 1.00 23.37 ? 122  LYS D C   1 
ATOM   4223  O  O   . LYS D  1 123 ? 84.495  0.201   25.953 1.00 23.14 ? 122  LYS D O   1 
ATOM   4224  C  CB  . LYS D  1 123 ? 83.577  2.484   28.297 1.00 23.74 ? 122  LYS D CB  1 
ATOM   4225  C  CG  . LYS D  1 123 ? 83.984  3.131   29.624 1.00 29.14 ? 122  LYS D CG  1 
ATOM   4226  C  CD  . LYS D  1 123 ? 83.489  4.571   29.733 1.00 32.86 ? 122  LYS D CD  1 
ATOM   4227  C  CE  . LYS D  1 123 ? 84.103  5.473   28.672 1.00 34.76 ? 122  LYS D CE  1 
ATOM   4228  N  NZ  . LYS D  1 123 ? 83.503  6.857   28.660 1.00 38.43 ? 122  LYS D NZ  1 
ATOM   4229  N  N   . ALA D  1 124 ? 82.342  0.469   26.529 1.00 23.05 ? 123  ALA D N   1 
ATOM   4230  C  CA  . ALA D  1 124 ? 81.820  0.042   25.239 1.00 23.33 ? 123  ALA D CA  1 
ATOM   4231  C  C   . ALA D  1 124 ? 82.102  1.113   24.187 1.00 21.88 ? 123  ALA D C   1 
ATOM   4232  O  O   . ALA D  1 124 ? 82.170  2.304   24.498 1.00 21.59 ? 123  ALA D O   1 
ATOM   4233  C  CB  . ALA D  1 124 ? 80.316  -0.191  25.337 1.00 23.80 ? 123  ALA D CB  1 
ATOM   4234  N  N   . ASP D  1 125 ? 82.270  0.674   22.944 1.00 21.29 ? 124  ASP D N   1 
ATOM   4235  C  CA  . ASP D  1 125 ? 82.495  1.567   21.811 1.00 18.96 ? 124  ASP D CA  1 
ATOM   4236  C  C   . ASP D  1 125 ? 81.082  1.867   21.303 1.00 21.21 ? 124  ASP D C   1 
ATOM   4237  O  O   . ASP D  1 125 ? 80.332  0.939   20.986 1.00 21.82 ? 124  ASP D O   1 
ATOM   4238  C  CB  . ASP D  1 125 ? 83.319  0.822   20.750 1.00 20.29 ? 124  ASP D CB  1 
ATOM   4239  C  CG  . ASP D  1 125 ? 83.613  1.658   19.508 1.00 20.32 ? 124  ASP D CG  1 
ATOM   4240  O  OD1 . ASP D  1 125 ? 84.579  1.305   18.801 1.00 18.99 ? 124  ASP D OD1 1 
ATOM   4241  O  OD2 . ASP D  1 125 ? 82.892  2.640   19.223 1.00 21.02 ? 124  ASP D OD2 1 
ATOM   4242  N  N   . ASP D  1 126 ? 80.696  3.139   21.242 1.00 19.62 ? 125  ASP D N   1 
ATOM   4243  C  CA  . ASP D  1 126 ? 79.347  3.463   20.778 1.00 21.23 ? 125  ASP D CA  1 
ATOM   4244  C  C   . ASP D  1 126 ? 79.244  3.434   19.252 1.00 20.93 ? 125  ASP D C   1 
ATOM   4245  O  O   . ASP D  1 126 ? 78.230  3.823   18.670 1.00 20.50 ? 125  ASP D O   1 
ATOM   4246  C  CB  . ASP D  1 126 ? 78.875  4.814   21.353 1.00 21.76 ? 125  ASP D CB  1 
ATOM   4247  C  CG  . ASP D  1 126 ? 79.644  6.008   20.807 1.00 23.10 ? 125  ASP D CG  1 
ATOM   4248  O  OD1 . ASP D  1 126 ? 79.553  7.092   21.430 1.00 24.57 ? 125  ASP D OD1 1 
ATOM   4249  O  OD2 . ASP D  1 126 ? 80.320  5.883   19.769 1.00 21.18 ? 125  ASP D OD2 1 
ATOM   4250  N  N   . LEU D  1 127 ? 80.314  2.964   18.618 1.00 20.85 ? 126  LEU D N   1 
ATOM   4251  C  CA  . LEU D  1 127 ? 80.363  2.817   17.168 1.00 21.05 ? 126  LEU D CA  1 
ATOM   4252  C  C   . LEU D  1 127 ? 80.093  4.104   16.396 1.00 21.64 ? 126  LEU D C   1 
ATOM   4253  O  O   . LEU D  1 127 ? 79.581  4.072   15.265 1.00 19.80 ? 126  LEU D O   1 
ATOM   4254  C  CB  . LEU D  1 127 ? 79.375  1.724   16.740 1.00 20.81 ? 126  LEU D CB  1 
ATOM   4255  C  CG  . LEU D  1 127 ? 79.416  0.449   17.600 1.00 21.47 ? 126  LEU D CG  1 
ATOM   4256  C  CD1 . LEU D  1 127 ? 78.349  -0.541  17.112 1.00 22.31 ? 126  LEU D CD1 1 
ATOM   4257  C  CD2 . LEU D  1 127 ? 80.803  -0.184  17.526 1.00 21.38 ? 126  LEU D CD2 1 
ATOM   4258  N  N   . GLY D  1 128 ? 80.446  5.234   17.006 1.00 19.80 ? 127  GLY D N   1 
ATOM   4259  C  CA  . GLY D  1 128 ? 80.263  6.519   16.358 1.00 18.68 ? 127  GLY D CA  1 
ATOM   4260  C  C   . GLY D  1 128 ? 78.846  7.062   16.374 1.00 20.26 ? 127  GLY D C   1 
ATOM   4261  O  O   . GLY D  1 128 ? 78.519  7.983   15.623 1.00 20.73 ? 127  GLY D O   1 
ATOM   4262  N  N   . LYS D  1 129 ? 77.999  6.525   17.241 1.00 18.16 ? 128  LYS D N   1 
ATOM   4263  C  CA  . LYS D  1 129 ? 76.623  6.993   17.285 1.00 20.27 ? 128  LYS D CA  1 
ATOM   4264  C  C   . LYS D  1 129 ? 76.296  7.758   18.558 1.00 20.67 ? 128  LYS D C   1 
ATOM   4265  O  O   . LYS D  1 129 ? 75.123  7.960   18.879 1.00 22.30 ? 128  LYS D O   1 
ATOM   4266  C  CB  . LYS D  1 129 ? 75.676  5.799   17.117 1.00 20.80 ? 128  LYS D CB  1 
ATOM   4267  C  CG  . LYS D  1 129 ? 76.079  4.899   15.938 1.00 26.80 ? 128  LYS D CG  1 
ATOM   4268  C  CD  . LYS D  1 129 ? 74.897  4.192   15.292 1.00 33.03 ? 128  LYS D CD  1 
ATOM   4269  C  CE  . LYS D  1 129 ? 74.172  3.278   16.245 1.00 34.39 ? 128  LYS D CE  1 
ATOM   4270  N  NZ  . LYS D  1 129 ? 72.976  2.659   15.594 1.00 37.03 ? 128  LYS D NZ  1 
ATOM   4271  N  N   . GLY D  1 130 ? 77.338  8.188   19.268 1.00 19.45 ? 129  GLY D N   1 
ATOM   4272  C  CA  . GLY D  1 130 ? 77.158  8.916   20.517 1.00 20.70 ? 129  GLY D CA  1 
ATOM   4273  C  C   . GLY D  1 130 ? 76.697  10.366  20.422 1.00 19.77 ? 129  GLY D C   1 
ATOM   4274  O  O   . GLY D  1 130 ? 76.210  10.926  21.406 1.00 20.73 ? 129  GLY D O   1 
ATOM   4275  N  N   . GLY D  1 131 ? 76.866  10.988  19.259 1.00 19.18 ? 130  GLY D N   1 
ATOM   4276  C  CA  . GLY D  1 131 ? 76.428  12.368  19.097 1.00 17.26 ? 130  GLY D CA  1 
ATOM   4277  C  C   . GLY D  1 131 ? 77.342  13.437  19.682 1.00 21.15 ? 130  GLY D C   1 
ATOM   4278  O  O   . GLY D  1 131 ? 77.027  14.627  19.612 1.00 19.65 ? 130  GLY D O   1 
ATOM   4279  N  N   . ASN D  1 132 ? 78.460  13.038  20.282 1.00 21.04 ? 131  ASN D N   1 
ATOM   4280  C  CA  . ASN D  1 132 ? 79.382  14.029  20.826 1.00 22.79 ? 131  ASN D CA  1 
ATOM   4281  C  C   . ASN D  1 132 ? 80.693  13.959  20.057 1.00 23.53 ? 131  ASN D C   1 
ATOM   4282  O  O   . ASN D  1 132 ? 80.889  13.064  19.232 1.00 23.58 ? 131  ASN D O   1 
ATOM   4283  C  CB  . ASN D  1 132 ? 79.608  13.806  22.330 1.00 21.48 ? 131  ASN D CB  1 
ATOM   4284  C  CG  . ASN D  1 132 ? 80.322  12.507  22.639 1.00 25.00 ? 131  ASN D CG  1 
ATOM   4285  O  OD1 . ASN D  1 132 ? 80.361  11.584  21.821 1.00 25.75 ? 131  ASN D OD1 1 
ATOM   4286  N  ND2 . ASN D  1 132 ? 80.882  12.422  23.839 1.00 22.01 ? 131  ASN D ND2 1 
ATOM   4287  N  N   . GLU D  1 133 ? 81.582  14.913  20.308 1.00 26.50 ? 132  GLU D N   1 
ATOM   4288  C  CA  . GLU D  1 133 ? 82.869  14.958  19.615 1.00 26.77 ? 132  GLU D CA  1 
ATOM   4289  C  C   . GLU D  1 133 ? 83.642  13.658  19.739 1.00 25.37 ? 132  GLU D C   1 
ATOM   4290  O  O   . GLU D  1 133 ? 84.144  13.124  18.752 1.00 25.15 ? 132  GLU D O   1 
ATOM   4291  C  CB  . GLU D  1 133 ? 83.740  16.090  20.175 1.00 30.50 ? 132  GLU D CB  1 
ATOM   4292  C  CG  . GLU D  1 133 ? 83.179  17.492  19.992 1.00 36.11 ? 132  GLU D CG  1 
ATOM   4293  C  CD  . GLU D  1 133 ? 84.104  18.569  20.562 1.00 39.28 ? 132  GLU D CD  1 
ATOM   4294  O  OE1 . GLU D  1 133 ? 83.834  19.764  20.332 1.00 41.42 ? 132  GLU D OE1 1 
ATOM   4295  O  OE2 . GLU D  1 133 ? 85.095  18.219  21.241 1.00 41.94 ? 132  GLU D OE2 1 
ATOM   4296  N  N   . GLU D  1 134 ? 83.735  13.162  20.966 1.00 25.28 ? 133  GLU D N   1 
ATOM   4297  C  CA  . GLU D  1 134 ? 84.469  11.942  21.260 1.00 26.80 ? 133  GLU D CA  1 
ATOM   4298  C  C   . GLU D  1 134 ? 83.997  10.704  20.480 1.00 25.89 ? 133  GLU D C   1 
ATOM   4299  O  O   . GLU D  1 134 ? 84.812  9.866   20.097 1.00 23.35 ? 133  GLU D O   1 
ATOM   4300  C  CB  . GLU D  1 134 ? 84.413  11.666  22.767 1.00 28.75 ? 133  GLU D CB  1 
ATOM   4301  C  CG  . GLU D  1 134 ? 85.372  10.588  23.236 1.00 35.21 ? 133  GLU D CG  1 
ATOM   4302  C  CD  . GLU D  1 134 ? 86.832  10.993  23.078 1.00 39.22 ? 133  GLU D CD  1 
ATOM   4303  O  OE1 . GLU D  1 134 ? 87.703  10.105  23.182 1.00 41.03 ? 133  GLU D OE1 1 
ATOM   4304  O  OE2 . GLU D  1 134 ? 87.108  12.193  22.861 1.00 39.22 ? 133  GLU D OE2 1 
ATOM   4305  N  N   . SER D  1 135 ? 82.693  10.589  20.243 1.00 26.38 ? 134  SER D N   1 
ATOM   4306  C  CA  . SER D  1 135 ? 82.154  9.436   19.520 1.00 23.95 ? 134  SER D CA  1 
ATOM   4307  C  C   . SER D  1 135 ? 82.792  9.254   18.144 1.00 24.35 ? 134  SER D C   1 
ATOM   4308  O  O   . SER D  1 135 ? 83.054  8.129   17.716 1.00 24.33 ? 134  SER D O   1 
ATOM   4309  C  CB  . SER D  1 135 ? 80.635  9.566   19.353 1.00 24.53 ? 134  SER D CB  1 
ATOM   4310  O  OG  . SER D  1 135 ? 80.114  8.459   18.626 1.00 23.98 ? 134  SER D OG  1 
ATOM   4311  N  N   . THR D  1 136 ? 83.042  10.369  17.461 1.00 24.58 ? 135  THR D N   1 
ATOM   4312  C  CA  . THR D  1 136 ? 83.630  10.361  16.124 1.00 26.39 ? 135  THR D CA  1 
ATOM   4313  C  C   . THR D  1 136 ? 85.134  10.096  16.129 1.00 25.77 ? 135  THR D C   1 
ATOM   4314  O  O   . THR D  1 136 ? 85.755  9.973   15.068 1.00 25.73 ? 135  THR D O   1 
ATOM   4315  C  CB  . THR D  1 136 ? 83.399  11.710  15.421 1.00 29.97 ? 135  THR D CB  1 
ATOM   4316  O  OG1 . THR D  1 136 ? 84.164  12.725  16.087 1.00 34.77 ? 135  THR D OG1 1 
ATOM   4317  C  CG2 . THR D  1 136 ? 81.931  12.095  15.478 1.00 32.71 ? 135  THR D CG2 1 
ATOM   4318  N  N   . LYS D  1 137 ? 85.718  10.018  17.318 1.00 25.34 ? 136  LYS D N   1 
ATOM   4319  C  CA  . LYS D  1 137 ? 87.148  9.777   17.439 1.00 25.25 ? 136  LYS D CA  1 
ATOM   4320  C  C   . LYS D  1 137 ? 87.483  8.430   18.064 1.00 24.68 ? 136  LYS D C   1 
ATOM   4321  O  O   . LYS D  1 137 ? 88.292  7.671   17.525 1.00 25.23 ? 136  LYS D O   1 
ATOM   4322  C  CB  . LYS D  1 137 ? 87.795  10.886  18.276 1.00 27.71 ? 136  LYS D CB  1 
ATOM   4323  C  CG  . LYS D  1 137 ? 87.708  12.273  17.649 1.00 32.03 ? 136  LYS D CG  1 
ATOM   4324  C  CD  . LYS D  1 137 ? 88.149  13.351  18.636 1.00 35.80 ? 136  LYS D CD  1 
ATOM   4325  C  CE  . LYS D  1 137 ? 88.075  14.736  18.015 0.00 34.94 ? 136  LYS D CE  1 
ATOM   4326  N  NZ  . LYS D  1 137 ? 88.511  15.795  18.967 0.00 35.54 ? 136  LYS D NZ  1 
ATOM   4327  N  N   . THR D  1 138 ? 86.861  8.137   19.202 1.00 23.61 ? 137  THR D N   1 
ATOM   4328  C  CA  . THR D  1 138 ? 87.135  6.899   19.923 1.00 23.18 ? 137  THR D CA  1 
ATOM   4329  C  C   . THR D  1 138 ? 85.899  6.070   20.240 1.00 21.65 ? 137  THR D C   1 
ATOM   4330  O  O   . THR D  1 138 ? 86.013  4.967   20.763 1.00 21.67 ? 137  THR D O   1 
ATOM   4331  C  CB  . THR D  1 138 ? 87.791  7.196   21.260 1.00 23.34 ? 137  THR D CB  1 
ATOM   4332  O  OG1 . THR D  1 138 ? 86.839  7.874   22.091 1.00 24.05 ? 137  THR D OG1 1 
ATOM   4333  C  CG2 . THR D  1 138 ? 89.014  8.083   21.076 1.00 24.85 ? 137  THR D CG2 1 
ATOM   4334  N  N   . GLY D  1 139 ? 84.722  6.604   19.945 1.00 22.18 ? 138  GLY D N   1 
ATOM   4335  C  CA  . GLY D  1 139 ? 83.505  5.885   20.257 1.00 21.37 ? 138  GLY D CA  1 
ATOM   4336  C  C   . GLY D  1 139 ? 83.247  5.916   21.756 1.00 22.64 ? 138  GLY D C   1 
ATOM   4337  O  O   . GLY D  1 139 ? 82.468  5.112   22.267 1.00 20.81 ? 138  GLY D O   1 
ATOM   4338  N  N   . ASN D  1 140 ? 83.902  6.840   22.464 1.00 23.08 ? 139  ASN D N   1 
ATOM   4339  C  CA  . ASN D  1 140 ? 83.739  6.972   23.920 1.00 21.72 ? 139  ASN D CA  1 
ATOM   4340  C  C   . ASN D  1 140 ? 84.131  5.680   24.642 1.00 22.34 ? 139  ASN D C   1 
ATOM   4341  O  O   . ASN D  1 140 ? 83.542  5.324   25.669 1.00 22.42 ? 139  ASN D O   1 
ATOM   4342  C  CB  . ASN D  1 140 ? 82.280  7.324   24.266 1.00 22.94 ? 139  ASN D CB  1 
ATOM   4343  C  CG  . ASN D  1 140 ? 81.904  8.746   23.869 1.00 24.21 ? 139  ASN D CG  1 
ATOM   4344  O  OD1 . ASN D  1 140 ? 82.398  9.711   24.448 1.00 23.84 ? 139  ASN D OD1 1 
ATOM   4345  N  ND2 . ASN D  1 140 ? 81.025  8.881   22.878 1.00 21.65 ? 139  ASN D ND2 1 
ATOM   4346  N  N   . ALA D  1 141 ? 85.131  4.985   24.107 1.00 22.34 ? 140  ALA D N   1 
ATOM   4347  C  CA  . ALA D  1 141 ? 85.585  3.718   24.675 1.00 22.85 ? 140  ALA D CA  1 
ATOM   4348  C  C   . ALA D  1 141 ? 86.363  3.860   25.984 1.00 23.48 ? 140  ALA D C   1 
ATOM   4349  O  O   . ALA D  1 141 ? 86.604  2.871   26.676 1.00 24.27 ? 140  ALA D O   1 
ATOM   4350  C  CB  . ALA D  1 141 ? 86.427  2.967   23.651 1.00 21.63 ? 140  ALA D CB  1 
ATOM   4351  N  N   . GLY D  1 142 ? 86.768  5.081   26.315 1.00 24.37 ? 141  GLY D N   1 
ATOM   4352  C  CA  . GLY D  1 142 ? 87.492  5.291   27.557 1.00 24.49 ? 141  GLY D CA  1 
ATOM   4353  C  C   . GLY D  1 142 ? 88.937  4.820   27.582 1.00 25.57 ? 141  GLY D C   1 
ATOM   4354  O  O   . GLY D  1 142 ? 89.586  4.716   26.543 1.00 25.02 ? 141  GLY D O   1 
ATOM   4355  N  N   . SER D  1 143 ? 89.436  4.517   28.777 1.00 25.83 ? 142  SER D N   1 
ATOM   4356  C  CA  . SER D  1 143 ? 90.823  4.100   28.950 1.00 26.38 ? 142  SER D CA  1 
ATOM   4357  C  C   . SER D  1 143 ? 91.193  2.770   28.304 1.00 27.01 ? 142  SER D C   1 
ATOM   4358  O  O   . SER D  1 143 ? 90.333  1.954   27.965 1.00 27.00 ? 142  SER D O   1 
ATOM   4359  C  CB  . SER D  1 143 ? 91.182  4.058   30.441 1.00 27.67 ? 142  SER D CB  1 
ATOM   4360  O  OG  . SER D  1 143 ? 90.574  2.953   31.081 1.00 35.09 ? 142  SER D OG  1 
ATOM   4361  N  N   . ARG D  1 144 ? 92.497  2.564   28.161 1.00 26.29 ? 143  ARG D N   1 
ATOM   4362  C  CA  . ARG D  1 144 ? 93.051  1.364   27.549 1.00 25.86 ? 143  ARG D CA  1 
ATOM   4363  C  C   . ARG D  1 144 ? 93.476  0.393   28.648 1.00 25.81 ? 143  ARG D C   1 
ATOM   4364  O  O   . ARG D  1 144 ? 94.501  0.587   29.297 1.00 26.22 ? 143  ARG D O   1 
ATOM   4365  C  CB  . ARG D  1 144 ? 94.241  1.780   26.681 1.00 25.30 ? 143  ARG D CB  1 
ATOM   4366  C  CG  . ARG D  1 144 ? 93.906  3.013   25.840 1.00 24.21 ? 143  ARG D CG  1 
ATOM   4367  C  CD  . ARG D  1 144 ? 95.050  3.538   24.994 1.00 26.42 ? 143  ARG D CD  1 
ATOM   4368  N  NE  . ARG D  1 144 ? 94.587  4.647   24.161 1.00 27.38 ? 143  ARG D NE  1 
ATOM   4369  C  CZ  . ARG D  1 144 ? 95.305  5.227   23.204 1.00 29.44 ? 143  ARG D CZ  1 
ATOM   4370  N  NH1 . ARG D  1 144 ? 94.785  6.227   22.503 1.00 27.79 ? 143  ARG D NH1 1 
ATOM   4371  N  NH2 . ARG D  1 144 ? 96.540  4.810   22.943 1.00 27.20 ? 143  ARG D NH2 1 
ATOM   4372  N  N   . LEU D  1 145 ? 92.683  -0.651  28.856 1.00 23.05 ? 144  LEU D N   1 
ATOM   4373  C  CA  . LEU D  1 145 ? 92.980  -1.616  29.903 1.00 23.83 ? 144  LEU D CA  1 
ATOM   4374  C  C   . LEU D  1 145 ? 94.160  -2.527  29.604 1.00 21.95 ? 144  LEU D C   1 
ATOM   4375  O  O   . LEU D  1 145 ? 94.919  -2.876  30.504 1.00 23.18 ? 144  LEU D O   1 
ATOM   4376  C  CB  . LEU D  1 145 ? 91.732  -2.444  30.214 1.00 23.09 ? 144  LEU D CB  1 
ATOM   4377  C  CG  . LEU D  1 145 ? 90.537  -1.567  30.606 1.00 27.54 ? 144  LEU D CG  1 
ATOM   4378  C  CD1 . LEU D  1 145 ? 89.355  -2.442  30.984 1.00 27.69 ? 144  LEU D CD1 1 
ATOM   4379  C  CD2 . LEU D  1 145 ? 90.923  -0.660  31.767 1.00 27.00 ? 144  LEU D CD2 1 
ATOM   4380  N  N   . ALA D  1 146 ? 94.320  -2.911  28.344 1.00 21.82 ? 145  ALA D N   1 
ATOM   4381  C  CA  . ALA D  1 146 ? 95.426  -3.774  27.946 1.00 21.70 ? 145  ALA D CA  1 
ATOM   4382  C  C   . ALA D  1 146 ? 95.679  -3.580  26.458 1.00 23.43 ? 145  ALA D C   1 
ATOM   4383  O  O   . ALA D  1 146 ? 94.787  -3.150  25.718 1.00 23.30 ? 145  ALA D O   1 
ATOM   4384  C  CB  . ALA D  1 146 ? 95.095  -5.238  28.236 1.00 21.00 ? 145  ALA D CB  1 
ATOM   4385  N  N   . CYS D  1 147 ? 96.894  -3.899  26.028 1.00 21.40 ? 146  CYS D N   1 
ATOM   4386  C  CA  . CYS D  1 147 ? 97.273  -3.748  24.630 1.00 23.28 ? 146  CYS D CA  1 
ATOM   4387  C  C   . CYS D  1 147 ? 98.483  -4.616  24.332 1.00 23.48 ? 146  CYS D C   1 
ATOM   4388  O  O   . CYS D  1 147 ? 99.121  -5.144  25.244 1.00 23.45 ? 146  CYS D O   1 
ATOM   4389  C  CB  . CYS D  1 147 ? 97.619  -2.288  24.332 1.00 24.99 ? 146  CYS D CB  1 
ATOM   4390  S  SG  . CYS D  1 147 ? 98.956  -1.636  25.392 1.00 28.17 ? 146  CYS D SG  1 
ATOM   4391  N  N   . GLY D  1 148 ? 98.791  -4.758  23.048 1.00 24.11 ? 147  GLY D N   1 
ATOM   4392  C  CA  . GLY D  1 148 ? 99.932  -5.553  22.642 1.00 22.51 ? 147  GLY D CA  1 
ATOM   4393  C  C   . GLY D  1 148 ? 100.272 -5.300  21.188 1.00 24.33 ? 147  GLY D C   1 
ATOM   4394  O  O   . GLY D  1 148 ? 99.383  -5.024  20.375 1.00 22.64 ? 147  GLY D O   1 
ATOM   4395  N  N   . VAL D  1 149 ? 101.554 -5.392  20.851 1.00 22.69 ? 148  VAL D N   1 
ATOM   4396  C  CA  . VAL D  1 149 ? 101.968 -5.179  19.475 1.00 23.52 ? 148  VAL D CA  1 
ATOM   4397  C  C   . VAL D  1 149 ? 101.639 -6.401  18.622 1.00 22.89 ? 148  VAL D C   1 
ATOM   4398  O  O   . VAL D  1 149 ? 101.924 -7.539  18.997 1.00 24.95 ? 148  VAL D O   1 
ATOM   4399  C  CB  . VAL D  1 149 ? 103.474 -4.890  19.373 1.00 23.83 ? 148  VAL D CB  1 
ATOM   4400  C  CG1 . VAL D  1 149 ? 103.821 -4.522  17.933 1.00 22.50 ? 148  VAL D CG1 1 
ATOM   4401  C  CG2 . VAL D  1 149 ? 103.860 -3.758  20.328 1.00 26.01 ? 148  VAL D CG2 1 
ATOM   4402  N  N   . ILE D  1 150 ? 101.027 -6.155  17.472 1.00 22.73 ? 149  ILE D N   1 
ATOM   4403  C  CA  . ILE D  1 150 ? 100.644 -7.226  16.561 1.00 23.02 ? 149  ILE D CA  1 
ATOM   4404  C  C   . ILE D  1 150 ? 101.875 -7.723  15.814 1.00 23.13 ? 149  ILE D C   1 
ATOM   4405  O  O   . ILE D  1 150 ? 102.439 -7.006  14.991 1.00 22.89 ? 149  ILE D O   1 
ATOM   4406  C  CB  . ILE D  1 150 ? 99.583  -6.723  15.561 1.00 21.68 ? 149  ILE D CB  1 
ATOM   4407  C  CG1 . ILE D  1 150 ? 98.370  -6.196  16.340 1.00 20.89 ? 149  ILE D CG1 1 
ATOM   4408  C  CG2 . ILE D  1 150 ? 99.179  -7.847  14.611 1.00 22.96 ? 149  ILE D CG2 1 
ATOM   4409  C  CD1 . ILE D  1 150 ? 97.364  -5.445  15.509 1.00 20.70 ? 149  ILE D CD1 1 
ATOM   4410  N  N   . GLY D  1 151 ? 102.286 -8.951  16.112 1.00 23.98 ? 150  GLY D N   1 
ATOM   4411  C  CA  . GLY D  1 151 ? 103.457 -9.523  15.471 1.00 25.15 ? 150  GLY D CA  1 
ATOM   4412  C  C   . GLY D  1 151 ? 103.145 -10.660 14.516 1.00 26.60 ? 150  GLY D C   1 
ATOM   4413  O  O   . GLY D  1 151 ? 102.099 -11.307 14.614 1.00 24.97 ? 150  GLY D O   1 
ATOM   4414  N  N   . ILE D  1 152 ? 104.061 -10.901 13.582 1.00 27.17 ? 151  ILE D N   1 
ATOM   4415  C  CA  . ILE D  1 152 ? 103.900 -11.960 12.597 1.00 27.60 ? 151  ILE D CA  1 
ATOM   4416  C  C   . ILE D  1 152 ? 103.981 -13.308 13.292 1.00 29.22 ? 151  ILE D C   1 
ATOM   4417  O  O   . ILE D  1 152 ? 104.880 -13.547 14.104 1.00 30.88 ? 151  ILE D O   1 
ATOM   4418  C  CB  . ILE D  1 152 ? 105.007 -11.896 11.517 1.00 29.51 ? 151  ILE D CB  1 
ATOM   4419  C  CG1 . ILE D  1 152 ? 104.920 -10.570 10.759 1.00 29.56 ? 151  ILE D CG1 1 
ATOM   4420  C  CG2 . ILE D  1 152 ? 104.880 -13.082 10.572 1.00 28.37 ? 151  ILE D CG2 1 
ATOM   4421  C  CD1 . ILE D  1 152 ? 106.030 -10.367 9.735  1.00 31.54 ? 151  ILE D CD1 1 
ATOM   4422  N  N   . ALA D  1 153 ? 103.049 -14.194 12.969 1.00 29.38 ? 152  ALA D N   1 
ATOM   4423  C  CA  . ALA D  1 153 ? 103.030 -15.514 13.582 1.00 32.03 ? 152  ALA D CA  1 
ATOM   4424  C  C   . ALA D  1 153 ? 103.283 -16.603 12.553 1.00 34.65 ? 152  ALA D C   1 
ATOM   4425  O  O   . ALA D  1 153 ? 103.090 -16.401 11.356 1.00 35.17 ? 152  ALA D O   1 
ATOM   4426  C  CB  . ALA D  1 153 ? 101.695 -15.747 14.272 1.00 31.20 ? 152  ALA D CB  1 
ATOM   4427  N  N   . GLN D  1 154 ? 103.719 -17.762 13.030 1.00 37.17 ? 153  GLN D N   1 
ATOM   4428  C  CA  . GLN D  1 154 ? 103.993 -18.887 12.151 1.00 42.30 ? 153  GLN D CA  1 
ATOM   4429  C  C   . GLN D  1 154 ? 102.685 -19.506 11.670 1.00 44.03 ? 153  GLN D C   1 
ATOM   4430  O  O   . GLN D  1 154 ? 101.698 -19.458 12.434 1.00 46.12 ? 153  GLN D O   1 
ATOM   4431  C  CB  . GLN D  1 154 ? 104.829 -19.925 12.900 1.00 43.23 ? 153  GLN D CB  1 
ATOM   4432  C  CG  . GLN D  1 154 ? 104.908 -21.284 12.239 1.00 47.21 ? 153  GLN D CG  1 
ATOM   4433  C  CD  . GLN D  1 154 ? 105.842 -22.222 12.979 1.00 48.06 ? 153  GLN D CD  1 
ATOM   4434  O  OE1 . GLN D  1 154 ? 107.062 -22.110 12.873 1.00 48.89 ? 153  GLN D OE1 1 
ATOM   4435  N  NE2 . GLN D  1 154 ? 105.270 -23.143 13.747 1.00 49.64 ? 153  GLN D NE2 1 
ATOM   4436  O  OXT . GLN D  1 154 ? 102.663 -20.039 10.540 1.00 46.35 ? 153  GLN D OXT 1 
ATOM   4437  N  N   . ALA E  1 2   ? 59.270  -31.028 6.653  0.00 44.91 ? 1    ALA E N   1 
ATOM   4438  C  CA  . ALA E  1 2   ? 57.975  -31.752 6.517  0.00 44.71 ? 1    ALA E CA  1 
ATOM   4439  C  C   . ALA E  1 2   ? 58.202  -33.259 6.547  1.00 44.82 ? 1    ALA E C   1 
ATOM   4440  O  O   . ALA E  1 2   ? 58.033  -33.944 5.538  1.00 45.81 ? 1    ALA E O   1 
ATOM   4441  C  CB  . ALA E  1 2   ? 57.296  -31.353 5.217  0.00 44.94 ? 1    ALA E CB  1 
ATOM   4442  N  N   . THR E  1 3   ? 58.599  -33.772 7.704  1.00 42.42 ? 2    THR E N   1 
ATOM   4443  C  CA  . THR E  1 3   ? 58.849  -35.196 7.838  1.00 38.25 ? 2    THR E CA  1 
ATOM   4444  C  C   . THR E  1 3   ? 58.508  -35.643 9.256  1.00 33.82 ? 2    THR E C   1 
ATOM   4445  O  O   . THR E  1 3   ? 57.972  -36.736 9.450  1.00 30.31 ? 2    THR E O   1 
ATOM   4446  C  CB  . THR E  1 3   ? 60.322  -35.537 7.481  1.00 41.58 ? 2    THR E CB  1 
ATOM   4447  O  OG1 . THR E  1 3   ? 60.448  -36.946 7.268  1.00 44.96 ? 2    THR E OG1 1 
ATOM   4448  C  CG2 . THR E  1 3   ? 61.273  -35.111 8.594  1.00 44.67 ? 2    THR E CG2 1 
ATOM   4449  N  N   . LYS E  1 4   ? 58.796  -34.792 10.240 1.00 28.56 ? 3    LYS E N   1 
ATOM   4450  C  CA  . LYS E  1 4   ? 58.484  -35.103 11.632 1.00 26.26 ? 3    LYS E CA  1 
ATOM   4451  C  C   . LYS E  1 4   ? 57.798  -33.949 12.357 1.00 24.28 ? 3    LYS E C   1 
ATOM   4452  O  O   . LYS E  1 4   ? 58.082  -32.776 12.107 1.00 22.90 ? 3    LYS E O   1 
ATOM   4453  C  CB  . LYS E  1 4   ? 59.745  -35.492 12.403 1.00 28.31 ? 3    LYS E CB  1 
ATOM   4454  C  CG  . LYS E  1 4   ? 60.320  -36.854 12.045 1.00 31.32 ? 3    LYS E CG  1 
ATOM   4455  C  CD  . LYS E  1 4   ? 61.612  -37.105 12.805 1.00 34.87 ? 3    LYS E CD  1 
ATOM   4456  C  CE  . LYS E  1 4   ? 62.177  -38.498 12.523 1.00 38.72 ? 3    LYS E CE  1 
ATOM   4457  N  NZ  . LYS E  1 4   ? 63.289  -38.833 13.455 0.00 37.42 ? 3    LYS E NZ  1 
ATOM   4458  N  N   . ALA E  1 5   ? 56.890  -34.291 13.263 1.00 20.99 ? 4    ALA E N   1 
ATOM   4459  C  CA  . ALA E  1 5   ? 56.184  -33.284 14.042 1.00 19.68 ? 4    ALA E CA  1 
ATOM   4460  C  C   . ALA E  1 5   ? 55.918  -33.823 15.445 1.00 20.04 ? 4    ALA E C   1 
ATOM   4461  O  O   . ALA E  1 5   ? 56.083  -35.015 15.706 1.00 20.08 ? 4    ALA E O   1 
ATOM   4462  C  CB  . ALA E  1 5   ? 54.867  -32.908 13.355 1.00 17.30 ? 4    ALA E CB  1 
ATOM   4463  N  N   . VAL E  1 6   ? 55.518  -32.938 16.347 1.00 18.99 ? 5    VAL E N   1 
ATOM   4464  C  CA  . VAL E  1 6   ? 55.225  -33.338 17.713 1.00 19.21 ? 5    VAL E CA  1 
ATOM   4465  C  C   . VAL E  1 6   ? 54.187  -32.399 18.310 1.00 19.92 ? 5    VAL E C   1 
ATOM   4466  O  O   . VAL E  1 6   ? 54.063  -31.248 17.890 1.00 19.66 ? 5    VAL E O   1 
ATOM   4467  C  CB  . VAL E  1 6   ? 56.500  -33.309 18.587 1.00 21.81 ? 5    VAL E CB  1 
ATOM   4468  C  CG1 . VAL E  1 6   ? 57.019  -31.870 18.707 1.00 19.87 ? 5    VAL E CG1 1 
ATOM   4469  C  CG2 . VAL E  1 6   ? 56.202  -33.904 19.963 1.00 19.82 ? 5    VAL E CG2 1 
ATOM   4470  N  N   . ALA E  1 7   ? 53.417  -32.908 19.264 1.00 19.75 ? 6    ALA E N   1 
ATOM   4471  C  CA  . ALA E  1 7   ? 52.411  -32.106 19.951 1.00 20.76 ? 6    ALA E CA  1 
ATOM   4472  C  C   . ALA E  1 7   ? 52.457  -32.489 21.418 1.00 20.57 ? 6    ALA E C   1 
ATOM   4473  O  O   . ALA E  1 7   ? 52.443  -33.670 21.750 1.00 21.16 ? 6    ALA E O   1 
ATOM   4474  C  CB  . ALA E  1 7   ? 51.013  -32.370 19.380 1.00 17.83 ? 6    ALA E CB  1 
ATOM   4475  N  N   . VAL E  1 8   ? 52.546  -31.488 22.287 1.00 21.72 ? 7    VAL E N   1 
ATOM   4476  C  CA  . VAL E  1 8   ? 52.581  -31.716 23.724 1.00 21.36 ? 7    VAL E CA  1 
ATOM   4477  C  C   . VAL E  1 8   ? 51.184  -31.378 24.216 1.00 20.44 ? 7    VAL E C   1 
ATOM   4478  O  O   . VAL E  1 8   ? 50.741  -30.236 24.103 1.00 19.66 ? 7    VAL E O   1 
ATOM   4479  C  CB  . VAL E  1 8   ? 53.636  -30.812 24.407 1.00 20.55 ? 7    VAL E CB  1 
ATOM   4480  C  CG1 . VAL E  1 8   ? 53.644  -31.042 25.921 1.00 22.43 ? 7    VAL E CG1 1 
ATOM   4481  C  CG2 . VAL E  1 8   ? 55.002  -31.116 23.833 1.00 22.29 ? 7    VAL E CG2 1 
ATOM   4482  N  N   . LEU E  1 9   ? 50.483  -32.380 24.741 1.00 19.65 ? 8    LEU E N   1 
ATOM   4483  C  CA  . LEU E  1 9   ? 49.112  -32.186 25.204 1.00 19.78 ? 8    LEU E CA  1 
ATOM   4484  C  C   . LEU E  1 9   ? 49.023  -31.753 26.662 1.00 19.21 ? 8    LEU E C   1 
ATOM   4485  O  O   . LEU E  1 9   ? 49.615  -32.371 27.540 1.00 18.11 ? 8    LEU E O   1 
ATOM   4486  C  CB  . LEU E  1 9   ? 48.303  -33.477 24.999 1.00 19.37 ? 8    LEU E CB  1 
ATOM   4487  C  CG  . LEU E  1 9   ? 48.358  -34.086 23.591 1.00 20.94 ? 8    LEU E CG  1 
ATOM   4488  C  CD1 . LEU E  1 9   ? 47.674  -35.455 23.579 1.00 22.98 ? 8    LEU E CD1 1 
ATOM   4489  C  CD2 . LEU E  1 9   ? 47.683  -33.136 22.605 1.00 22.12 ? 8    LEU E CD2 1 
ATOM   4490  N  N   . LYS E  1 10  ? 48.266  -30.688 26.902 1.00 20.74 ? 9    LYS E N   1 
ATOM   4491  C  CA  . LYS E  1 10  ? 48.068  -30.158 28.244 1.00 24.58 ? 9    LYS E CA  1 
ATOM   4492  C  C   . LYS E  1 10  ? 46.687  -29.532 28.341 1.00 23.32 ? 9    LYS E C   1 
ATOM   4493  O  O   . LYS E  1 10  ? 46.124  -29.080 27.336 1.00 21.31 ? 9    LYS E O   1 
ATOM   4494  C  CB  . LYS E  1 10  ? 49.134  -29.103 28.565 1.00 27.80 ? 9    LYS E CB  1 
ATOM   4495  C  CG  . LYS E  1 10  ? 50.543  -29.653 28.595 1.00 34.33 ? 9    LYS E CG  1 
ATOM   4496  C  CD  . LYS E  1 10  ? 51.594  -28.563 28.829 1.00 40.03 ? 9    LYS E CD  1 
ATOM   4497  C  CE  . LYS E  1 10  ? 53.007  -29.162 28.815 1.00 40.22 ? 9    LYS E CE  1 
ATOM   4498  N  NZ  . LYS E  1 10  ? 54.086  -28.136 28.901 1.00 44.60 ? 9    LYS E NZ  1 
ATOM   4499  N  N   . GLY E  1 11  ? 46.145  -29.505 29.555 1.00 22.99 ? 10   GLY E N   1 
ATOM   4500  C  CA  . GLY E  1 11  ? 44.833  -28.922 29.775 1.00 24.96 ? 10   GLY E CA  1 
ATOM   4501  C  C   . GLY E  1 11  ? 44.694  -28.442 31.208 1.00 28.21 ? 10   GLY E C   1 
ATOM   4502  O  O   . GLY E  1 11  ? 45.695  -28.251 31.902 1.00 27.76 ? 10   GLY E O   1 
ATOM   4503  N  N   . ASP E  1 12  ? 43.460  -28.261 31.667 1.00 30.90 ? 11   ASP E N   1 
ATOM   4504  C  CA  . ASP E  1 12  ? 43.236  -27.795 33.030 1.00 33.16 ? 11   ASP E CA  1 
ATOM   4505  C  C   . ASP E  1 12  ? 43.166  -28.932 34.036 1.00 33.73 ? 11   ASP E C   1 
ATOM   4506  O  O   . ASP E  1 12  ? 43.122  -28.694 35.245 1.00 33.12 ? 11   ASP E O   1 
ATOM   4507  C  CB  . ASP E  1 12  ? 41.951  -26.974 33.105 1.00 36.80 ? 11   ASP E CB  1 
ATOM   4508  C  CG  . ASP E  1 12  ? 42.001  -25.743 32.230 1.00 40.69 ? 11   ASP E CG  1 
ATOM   4509  O  OD1 . ASP E  1 12  ? 43.018  -25.018 32.286 1.00 41.07 ? 11   ASP E OD1 1 
ATOM   4510  O  OD2 . ASP E  1 12  ? 41.021  -25.499 31.494 1.00 43.93 ? 11   ASP E OD2 1 
ATOM   4511  N  N   . GLY E  1 13  ? 43.155  -30.163 33.535 1.00 31.46 ? 12   GLY E N   1 
ATOM   4512  C  CA  . GLY E  1 13  ? 43.090  -31.318 34.411 1.00 29.60 ? 12   GLY E CA  1 
ATOM   4513  C  C   . GLY E  1 13  ? 44.399  -32.081 34.442 1.00 28.00 ? 12   GLY E C   1 
ATOM   4514  O  O   . GLY E  1 13  ? 45.450  -31.518 34.136 1.00 26.90 ? 12   GLY E O   1 
ATOM   4515  N  N   . PRO E  1 14  ? 44.368  -33.373 34.797 1.00 25.97 ? 13   PRO E N   1 
ATOM   4516  C  CA  . PRO E  1 14  ? 45.569  -34.210 34.868 1.00 26.84 ? 13   PRO E CA  1 
ATOM   4517  C  C   . PRO E  1 14  ? 46.004  -34.840 33.543 1.00 26.37 ? 13   PRO E C   1 
ATOM   4518  O  O   . PRO E  1 14  ? 47.027  -35.517 33.483 1.00 26.80 ? 13   PRO E O   1 
ATOM   4519  C  CB  . PRO E  1 14  ? 45.175  -35.262 35.895 1.00 26.10 ? 13   PRO E CB  1 
ATOM   4520  C  CG  . PRO E  1 14  ? 43.748  -35.507 35.540 1.00 25.64 ? 13   PRO E CG  1 
ATOM   4521  C  CD  . PRO E  1 14  ? 43.194  -34.104 35.310 1.00 27.20 ? 13   PRO E CD  1 
ATOM   4522  N  N   . VAL E  1 15  ? 45.234  -34.620 32.485 1.00 26.57 ? 14   VAL E N   1 
ATOM   4523  C  CA  . VAL E  1 15  ? 45.572  -35.197 31.187 1.00 26.19 ? 14   VAL E CA  1 
ATOM   4524  C  C   . VAL E  1 15  ? 46.751  -34.505 30.502 1.00 26.09 ? 14   VAL E C   1 
ATOM   4525  O  O   . VAL E  1 15  ? 46.730  -33.305 30.261 1.00 25.72 ? 14   VAL E O   1 
ATOM   4526  C  CB  . VAL E  1 15  ? 44.346  -35.172 30.233 1.00 26.28 ? 14   VAL E CB  1 
ATOM   4527  C  CG1 . VAL E  1 15  ? 44.721  -35.740 28.873 1.00 24.01 ? 14   VAL E CG1 1 
ATOM   4528  C  CG2 . VAL E  1 15  ? 43.206  -35.987 30.840 1.00 25.37 ? 14   VAL E CG2 1 
ATOM   4529  N  N   . GLN E  1 16  ? 47.787  -35.275 30.200 1.00 25.55 ? 15   GLN E N   1 
ATOM   4530  C  CA  . GLN E  1 16  ? 48.951  -34.740 29.511 1.00 27.75 ? 15   GLN E CA  1 
ATOM   4531  C  C   . GLN E  1 16  ? 49.654  -35.857 28.760 1.00 26.96 ? 15   GLN E C   1 
ATOM   4532  O  O   . GLN E  1 16  ? 49.545  -37.027 29.120 1.00 27.94 ? 15   GLN E O   1 
ATOM   4533  C  CB  . GLN E  1 16  ? 49.919  -34.083 30.498 1.00 30.42 ? 15   GLN E CB  1 
ATOM   4534  C  CG  . GLN E  1 16  ? 50.469  -35.001 31.566 1.00 35.45 ? 15   GLN E CG  1 
ATOM   4535  C  CD  . GLN E  1 16  ? 51.385  -34.263 32.530 1.00 39.95 ? 15   GLN E CD  1 
ATOM   4536  O  OE1 . GLN E  1 16  ? 52.310  -33.561 32.110 1.00 41.13 ? 15   GLN E OE1 1 
ATOM   4537  N  NE2 . GLN E  1 16  ? 51.135  -34.417 33.825 1.00 37.78 ? 15   GLN E NE2 1 
ATOM   4538  N  N   . GLY E  1 17  ? 50.364  -35.493 27.702 1.00 25.80 ? 16   GLY E N   1 
ATOM   4539  C  CA  . GLY E  1 17  ? 51.076  -36.487 26.928 1.00 24.72 ? 16   GLY E CA  1 
ATOM   4540  C  C   . GLY E  1 17  ? 51.874  -35.856 25.808 1.00 24.33 ? 16   GLY E C   1 
ATOM   4541  O  O   . GLY E  1 17  ? 51.802  -34.646 25.572 1.00 25.46 ? 16   GLY E O   1 
ATOM   4542  N  N   . ILE E  1 18  ? 52.645  -36.689 25.123 1.00 23.37 ? 17   ILE E N   1 
ATOM   4543  C  CA  . ILE E  1 18  ? 53.472  -36.260 24.010 1.00 21.13 ? 17   ILE E CA  1 
ATOM   4544  C  C   . ILE E  1 18  ? 53.147  -37.174 22.841 1.00 22.50 ? 17   ILE E C   1 
ATOM   4545  O  O   . ILE E  1 18  ? 53.260  -38.397 22.953 1.00 21.32 ? 17   ILE E O   1 
ATOM   4546  C  CB  . ILE E  1 18  ? 54.966  -36.398 24.345 1.00 23.48 ? 17   ILE E CB  1 
ATOM   4547  C  CG1 . ILE E  1 18  ? 55.322  -35.470 25.511 1.00 26.58 ? 17   ILE E CG1 1 
ATOM   4548  C  CG2 . ILE E  1 18  ? 55.811  -36.058 23.125 1.00 23.98 ? 17   ILE E CG2 1 
ATOM   4549  C  CD1 . ILE E  1 18  ? 56.740  -35.645 26.006 1.00 27.43 ? 17   ILE E CD1 1 
ATOM   4550  N  N   . ILE E  1 19  ? 52.730  -36.583 21.728 1.00 19.17 ? 18   ILE E N   1 
ATOM   4551  C  CA  . ILE E  1 19  ? 52.394  -37.360 20.545 1.00 19.32 ? 18   ILE E CA  1 
ATOM   4552  C  C   . ILE E  1 19  ? 53.322  -36.987 19.397 1.00 21.33 ? 18   ILE E C   1 
ATOM   4553  O  O   . ILE E  1 19  ? 53.461  -35.809 19.048 1.00 20.18 ? 18   ILE E O   1 
ATOM   4554  C  CB  . ILE E  1 19  ? 50.923  -37.125 20.120 1.00 17.63 ? 18   ILE E CB  1 
ATOM   4555  C  CG1 . ILE E  1 19  ? 49.979  -37.635 21.216 1.00 19.10 ? 18   ILE E CG1 1 
ATOM   4556  C  CG2 . ILE E  1 19  ? 50.642  -37.805 18.788 1.00 18.07 ? 18   ILE E CG2 1 
ATOM   4557  C  CD1 . ILE E  1 19  ? 50.122  -39.124 21.534 1.00 21.05 ? 18   ILE E CD1 1 
ATOM   4558  N  N   . ASN E  1 20  ? 53.954  -38.005 18.822 1.00 19.57 ? 19   ASN E N   1 
ATOM   4559  C  CA  . ASN E  1 20  ? 54.884  -37.838 17.714 1.00 21.97 ? 19   ASN E CA  1 
ATOM   4560  C  C   . ASN E  1 20  ? 54.210  -38.146 16.380 1.00 23.63 ? 19   ASN E C   1 
ATOM   4561  O  O   . ASN E  1 20  ? 53.306  -38.992 16.307 1.00 22.00 ? 19   ASN E O   1 
ATOM   4562  C  CB  . ASN E  1 20  ? 56.078  -38.785 17.887 1.00 23.35 ? 19   ASN E CB  1 
ATOM   4563  C  CG  . ASN E  1 20  ? 56.793  -38.592 19.210 1.00 28.40 ? 19   ASN E CG  1 
ATOM   4564  O  OD1 . ASN E  1 20  ? 57.446  -37.573 19.429 1.00 28.06 ? 19   ASN E OD1 1 
ATOM   4565  N  ND2 . ASN E  1 20  ? 56.668  -39.573 20.104 1.00 27.50 ? 19   ASN E ND2 1 
ATOM   4566  N  N   . PHE E  1 21  ? 54.648  -37.447 15.335 1.00 20.97 ? 20   PHE E N   1 
ATOM   4567  C  CA  . PHE E  1 21  ? 54.141  -37.662 13.983 1.00 22.43 ? 20   PHE E CA  1 
ATOM   4568  C  C   . PHE E  1 21  ? 55.361  -37.850 13.085 1.00 22.72 ? 20   PHE E C   1 
ATOM   4569  O  O   . PHE E  1 21  ? 56.372  -37.152 13.243 1.00 20.36 ? 20   PHE E O   1 
ATOM   4570  C  CB  . PHE E  1 21  ? 53.375  -36.446 13.446 1.00 20.21 ? 20   PHE E CB  1 
ATOM   4571  C  CG  . PHE E  1 21  ? 52.178  -36.057 14.252 1.00 19.25 ? 20   PHE E CG  1 
ATOM   4572  C  CD1 . PHE E  1 21  ? 50.901  -36.410 13.838 1.00 19.60 ? 20   PHE E CD1 1 
ATOM   4573  C  CD2 . PHE E  1 21  ? 52.323  -35.295 15.410 1.00 19.87 ? 20   PHE E CD2 1 
ATOM   4574  C  CE1 . PHE E  1 21  ? 49.776  -36.006 14.566 1.00 19.74 ? 20   PHE E CE1 1 
ATOM   4575  C  CE2 . PHE E  1 21  ? 51.210  -34.886 16.144 1.00 19.70 ? 20   PHE E CE2 1 
ATOM   4576  C  CZ  . PHE E  1 21  ? 49.934  -35.240 15.721 1.00 20.32 ? 20   PHE E CZ  1 
ATOM   4577  N  N   . GLU E  1 22  ? 55.264  -38.777 12.139 1.00 22.54 ? 21   GLU E N   1 
ATOM   4578  C  CA  . GLU E  1 22  ? 56.348  -39.008 11.194 1.00 24.01 ? 21   GLU E CA  1 
ATOM   4579  C  C   . GLU E  1 22  ? 55.793  -39.417 9.834  1.00 24.72 ? 21   GLU E C   1 
ATOM   4580  O  O   . GLU E  1 22  ? 54.941  -40.307 9.730  1.00 24.42 ? 21   GLU E O   1 
ATOM   4581  C  CB  . GLU E  1 22  ? 57.318  -40.070 11.715 1.00 27.81 ? 21   GLU E CB  1 
ATOM   4582  C  CG  . GLU E  1 22  ? 58.498  -40.311 10.781 1.00 35.84 ? 21   GLU E CG  1 
ATOM   4583  C  CD  . GLU E  1 22  ? 59.605  -41.132 11.421 1.00 41.94 ? 21   GLU E CD  1 
ATOM   4584  O  OE1 . GLU E  1 22  ? 60.637  -41.357 10.755 1.00 45.11 ? 21   GLU E OE1 1 
ATOM   4585  O  OE2 . GLU E  1 22  ? 59.446  -41.550 12.587 1.00 45.72 ? 21   GLU E OE2 1 
ATOM   4586  N  N   . GLN E  1 23  ? 56.278  -38.746 8.795  1.00 23.43 ? 22   GLN E N   1 
ATOM   4587  C  CA  . GLN E  1 23  ? 55.852  -39.005 7.426  1.00 24.75 ? 22   GLN E CA  1 
ATOM   4588  C  C   . GLN E  1 23  ? 57.105  -39.193 6.566  1.00 27.42 ? 22   GLN E C   1 
ATOM   4589  O  O   . GLN E  1 23  ? 57.780  -38.226 6.208  1.00 27.43 ? 22   GLN E O   1 
ATOM   4590  C  CB  . GLN E  1 23  ? 55.014  -37.827 6.925  1.00 23.06 ? 22   GLN E CB  1 
ATOM   4591  C  CG  . GLN E  1 23  ? 54.365  -38.042 5.572  1.00 24.08 ? 22   GLN E CG  1 
ATOM   4592  C  CD  . GLN E  1 23  ? 53.430  -36.910 5.205  1.00 24.55 ? 22   GLN E CD  1 
ATOM   4593  O  OE1 . GLN E  1 23  ? 53.551  -35.800 5.723  1.00 25.54 ? 22   GLN E OE1 1 
ATOM   4594  N  NE2 . GLN E  1 23  ? 52.496  -37.180 4.302  1.00 25.30 ? 22   GLN E NE2 1 
ATOM   4595  N  N   . LYS E  1 24  ? 57.413  -40.448 6.252  1.00 27.93 ? 23   LYS E N   1 
ATOM   4596  C  CA  . LYS E  1 24  ? 58.595  -40.783 5.467  1.00 30.77 ? 23   LYS E CA  1 
ATOM   4597  C  C   . LYS E  1 24  ? 58.619  -40.105 4.100  1.00 30.76 ? 23   LYS E C   1 
ATOM   4598  O  O   . LYS E  1 24  ? 59.650  -39.574 3.681  1.00 30.80 ? 23   LYS E O   1 
ATOM   4599  C  CB  . LYS E  1 24  ? 58.697  -42.304 5.300  1.00 32.89 ? 23   LYS E CB  1 
ATOM   4600  C  CG  . LYS E  1 24  ? 60.000  -42.779 4.678  0.00 35.94 ? 23   LYS E CG  1 
ATOM   4601  C  CD  . LYS E  1 24  ? 60.025  -44.293 4.542  0.00 39.32 ? 23   LYS E CD  1 
ATOM   4602  C  CE  . LYS E  1 24  ? 61.330  -44.772 3.930  0.00 41.52 ? 23   LYS E CE  1 
ATOM   4603  N  NZ  . LYS E  1 24  ? 61.356  -46.252 3.777  1.00 47.59 ? 23   LYS E NZ  1 
ATOM   4604  N  N   . GLU E  1 25  ? 57.486  -40.123 3.408  1.00 30.71 ? 24   GLU E N   1 
ATOM   4605  C  CA  . GLU E  1 25  ? 57.387  -39.502 2.091  1.00 31.66 ? 24   GLU E CA  1 
ATOM   4606  C  C   . GLU E  1 25  ? 56.228  -38.517 2.098  1.00 29.89 ? 24   GLU E C   1 
ATOM   4607  O  O   . GLU E  1 25  ? 55.184  -38.777 2.696  1.00 29.80 ? 24   GLU E O   1 
ATOM   4608  C  CB  . GLU E  1 25  ? 57.169  -40.577 1.016  1.00 34.06 ? 24   GLU E CB  1 
ATOM   4609  C  CG  . GLU E  1 25  ? 58.250  -41.655 1.010  1.00 38.78 ? 24   GLU E CG  1 
ATOM   4610  C  CD  . GLU E  1 25  ? 59.634  -41.097 0.730  1.00 42.27 ? 24   GLU E CD  1 
ATOM   4611  O  OE1 . GLU E  1 25  ? 60.630  -41.779 1.051  1.00 45.19 ? 24   GLU E OE1 1 
ATOM   4612  O  OE2 . GLU E  1 25  ? 59.731  -39.979 0.181  1.00 46.90 ? 24   GLU E OE2 1 
ATOM   4613  N  N   . SER E  1 26  ? 56.409  -37.384 1.432  1.00 28.10 ? 25   SER E N   1 
ATOM   4614  C  CA  . SER E  1 26  ? 55.372  -36.367 1.401  1.00 28.25 ? 25   SER E CA  1 
ATOM   4615  C  C   . SER E  1 26  ? 54.037  -36.867 0.848  1.00 28.09 ? 25   SER E C   1 
ATOM   4616  O  O   . SER E  1 26  ? 52.990  -36.288 1.141  1.00 27.67 ? 25   SER E O   1 
ATOM   4617  C  CB  . SER E  1 26  ? 55.852  -35.151 0.603  1.00 27.81 ? 25   SER E CB  1 
ATOM   4618  O  OG  . SER E  1 26  ? 56.238  -35.529 -0.706 1.00 29.50 ? 25   SER E OG  1 
ATOM   4619  N  N   . ASN E  1 27  ? 54.064  -37.936 0.056  1.00 28.22 ? 26   ASN E N   1 
ATOM   4620  C  CA  . ASN E  1 27  ? 52.826  -38.476 -0.507 1.00 29.24 ? 26   ASN E CA  1 
ATOM   4621  C  C   . ASN E  1 27  ? 52.479  -39.797 0.159  1.00 29.18 ? 26   ASN E C   1 
ATOM   4622  O  O   . ASN E  1 27  ? 51.636  -40.552 -0.328 1.00 31.04 ? 26   ASN E O   1 
ATOM   4623  C  CB  . ASN E  1 27  ? 52.954  -38.662 -2.031 1.00 29.27 ? 26   ASN E CB  1 
ATOM   4624  C  CG  . ASN E  1 27  ? 53.934  -39.762 -2.416 1.00 32.19 ? 26   ASN E CG  1 
ATOM   4625  O  OD1 . ASN E  1 27  ? 54.971  -39.939 -1.777 1.00 32.48 ? 26   ASN E OD1 1 
ATOM   4626  N  ND2 . ASN E  1 27  ? 53.614  -40.496 -3.480 1.00 32.64 ? 26   ASN E ND2 1 
ATOM   4627  N  N   . GLY E  1 28  ? 53.131  -40.066 1.283  1.00 27.91 ? 27   GLY E N   1 
ATOM   4628  C  CA  . GLY E  1 28  ? 52.883  -41.298 2.009  1.00 27.97 ? 27   GLY E CA  1 
ATOM   4629  C  C   . GLY E  1 28  ? 52.070  -41.063 3.270  1.00 28.64 ? 27   GLY E C   1 
ATOM   4630  O  O   . GLY E  1 28  ? 51.700  -39.928 3.573  1.00 27.98 ? 27   GLY E O   1 
ATOM   4631  N  N   . PRO E  1 29  ? 51.782  -42.123 4.034  1.00 28.51 ? 28   PRO E N   1 
ATOM   4632  C  CA  . PRO E  1 29  ? 51.004  -42.006 5.266  1.00 28.22 ? 28   PRO E CA  1 
ATOM   4633  C  C   . PRO E  1 29  ? 51.782  -41.403 6.429  1.00 26.89 ? 28   PRO E C   1 
ATOM   4634  O  O   . PRO E  1 29  ? 53.013  -41.385 6.436  1.00 27.03 ? 28   PRO E O   1 
ATOM   4635  C  CB  . PRO E  1 29  ? 50.593  -43.447 5.544  1.00 27.94 ? 28   PRO E CB  1 
ATOM   4636  C  CG  . PRO E  1 29  ? 51.795  -44.206 5.080  1.00 30.86 ? 28   PRO E CG  1 
ATOM   4637  C  CD  . PRO E  1 29  ? 52.115  -43.534 3.758  1.00 28.86 ? 28   PRO E CD  1 
ATOM   4638  N  N   . VAL E  1 30  ? 51.044  -40.914 7.416  1.00 25.32 ? 29   VAL E N   1 
ATOM   4639  C  CA  . VAL E  1 30  ? 51.648  -40.336 8.603  1.00 24.15 ? 29   VAL E CA  1 
ATOM   4640  C  C   . VAL E  1 30  ? 51.458  -41.279 9.784  1.00 24.88 ? 29   VAL E C   1 
ATOM   4641  O  O   . VAL E  1 30  ? 50.334  -41.690 10.074 1.00 24.10 ? 29   VAL E O   1 
ATOM   4642  C  CB  . VAL E  1 30  ? 50.986  -38.995 8.977  1.00 22.02 ? 29   VAL E CB  1 
ATOM   4643  C  CG1 . VAL E  1 30  ? 51.637  -38.432 10.240 1.00 21.62 ? 29   VAL E CG1 1 
ATOM   4644  C  CG2 . VAL E  1 30  ? 51.098  -38.010 7.817  1.00 20.36 ? 29   VAL E CG2 1 
ATOM   4645  N  N   . LYS E  1 31  ? 52.551  -41.631 10.453 1.00 24.12 ? 30   LYS E N   1 
ATOM   4646  C  CA  . LYS E  1 31  ? 52.463  -42.475 11.635 1.00 25.47 ? 30   LYS E CA  1 
ATOM   4647  C  C   . LYS E  1 31  ? 52.357  -41.540 12.840 1.00 25.64 ? 30   LYS E C   1 
ATOM   4648  O  O   . LYS E  1 31  ? 53.093  -40.552 12.941 1.00 25.03 ? 30   LYS E O   1 
ATOM   4649  C  CB  . LYS E  1 31  ? 53.697  -43.370 11.770 1.00 27.71 ? 30   LYS E CB  1 
ATOM   4650  C  CG  . LYS E  1 31  ? 53.742  -44.487 10.740 1.00 35.47 ? 30   LYS E CG  1 
ATOM   4651  C  CD  . LYS E  1 31  ? 54.901  -45.439 10.995 1.00 40.43 ? 30   LYS E CD  1 
ATOM   4652  C  CE  . LYS E  1 31  ? 54.888  -46.580 9.987  1.00 43.23 ? 30   LYS E CE  1 
ATOM   4653  N  NZ  . LYS E  1 31  ? 55.989  -47.549 10.232 1.00 45.84 ? 30   LYS E NZ  1 
ATOM   4654  N  N   . VAL E  1 32  ? 51.431  -41.853 13.739 1.00 23.66 ? 31   VAL E N   1 
ATOM   4655  C  CA  . VAL E  1 32  ? 51.183  -41.058 14.935 1.00 21.91 ? 31   VAL E CA  1 
ATOM   4656  C  C   . VAL E  1 32  ? 51.316  -41.973 16.151 1.00 24.92 ? 31   VAL E C   1 
ATOM   4657  O  O   . VAL E  1 32  ? 50.613  -42.981 16.250 1.00 25.35 ? 31   VAL E O   1 
ATOM   4658  C  CB  . VAL E  1 32  ? 49.755  -40.461 14.900 1.00 21.33 ? 31   VAL E CB  1 
ATOM   4659  C  CG1 . VAL E  1 32  ? 49.524  -39.557 16.108 1.00 20.18 ? 31   VAL E CG1 1 
ATOM   4660  C  CG2 . VAL E  1 32  ? 49.543  -39.692 13.604 1.00 19.91 ? 31   VAL E CG2 1 
ATOM   4661  N  N   . TRP E  1 33  ? 52.221  -41.636 17.067 1.00 23.28 ? 32   TRP E N   1 
ATOM   4662  C  CA  . TRP E  1 33  ? 52.422  -42.458 18.252 1.00 25.82 ? 32   TRP E CA  1 
ATOM   4663  C  C   . TRP E  1 33  ? 52.932  -41.670 19.451 1.00 26.51 ? 32   TRP E C   1 
ATOM   4664  O  O   . TRP E  1 33  ? 53.537  -40.599 19.312 1.00 24.36 ? 32   TRP E O   1 
ATOM   4665  C  CB  . TRP E  1 33  ? 53.402  -43.599 17.950 1.00 26.63 ? 32   TRP E CB  1 
ATOM   4666  C  CG  . TRP E  1 33  ? 54.849  -43.187 17.973 1.00 27.63 ? 32   TRP E CG  1 
ATOM   4667  C  CD1 . TRP E  1 33  ? 55.733  -43.353 19.000 1.00 28.31 ? 32   TRP E CD1 1 
ATOM   4668  C  CD2 . TRP E  1 33  ? 55.572  -42.525 16.924 1.00 29.78 ? 32   TRP E CD2 1 
ATOM   4669  N  NE1 . TRP E  1 33  ? 56.959  -42.834 18.658 1.00 29.91 ? 32   TRP E NE1 1 
ATOM   4670  C  CE2 . TRP E  1 33  ? 56.887  -42.322 17.397 1.00 28.32 ? 32   TRP E CE2 1 
ATOM   4671  C  CE3 . TRP E  1 33  ? 55.228  -42.082 15.641 1.00 30.36 ? 32   TRP E CE3 1 
ATOM   4672  C  CZ2 . TRP E  1 33  ? 57.867  -41.695 16.618 1.00 31.03 ? 32   TRP E CZ2 1 
ATOM   4673  C  CZ3 . TRP E  1 33  ? 56.203  -41.459 14.870 1.00 30.65 ? 32   TRP E CZ3 1 
ATOM   4674  C  CH2 . TRP E  1 33  ? 57.509  -41.269 15.364 1.00 31.97 ? 32   TRP E CH2 1 
ATOM   4675  N  N   . GLY E  1 34  ? 52.687  -42.222 20.631 1.00 25.19 ? 33   GLY E N   1 
ATOM   4676  C  CA  . GLY E  1 34  ? 53.123  -41.579 21.851 1.00 27.55 ? 33   GLY E CA  1 
ATOM   4677  C  C   . GLY E  1 34  ? 52.342  -42.114 23.030 1.00 29.38 ? 33   GLY E C   1 
ATOM   4678  O  O   . GLY E  1 34  ? 51.810  -43.221 22.982 1.00 32.29 ? 33   GLY E O   1 
ATOM   4679  N  N   . SER E  1 35  ? 52.260  -41.326 24.090 1.00 28.18 ? 34   SER E N   1 
ATOM   4680  C  CA  . SER E  1 35  ? 51.544  -41.749 25.276 1.00 28.58 ? 34   SER E CA  1 
ATOM   4681  C  C   . SER E  1 35  ? 50.798  -40.585 25.899 1.00 28.23 ? 34   SER E C   1 
ATOM   4682  O  O   . SER E  1 35  ? 51.295  -39.455 25.926 1.00 29.99 ? 34   SER E O   1 
ATOM   4683  C  CB  . SER E  1 35  ? 52.528  -42.334 26.287 1.00 32.86 ? 34   SER E CB  1 
ATOM   4684  O  OG  . SER E  1 35  ? 51.865  -42.685 27.485 1.00 39.50 ? 34   SER E OG  1 
ATOM   4685  N  N   . ILE E  1 36  ? 49.590  -40.856 26.372 1.00 24.08 ? 35   ILE E N   1 
ATOM   4686  C  CA  . ILE E  1 36  ? 48.777  -39.841 27.026 1.00 23.31 ? 35   ILE E CA  1 
ATOM   4687  C  C   . ILE E  1 36  ? 48.394  -40.450 28.365 1.00 25.74 ? 35   ILE E C   1 
ATOM   4688  O  O   . ILE E  1 36  ? 47.933  -41.593 28.416 1.00 26.65 ? 35   ILE E O   1 
ATOM   4689  C  CB  . ILE E  1 36  ? 47.498  -39.536 26.242 1.00 21.37 ? 35   ILE E CB  1 
ATOM   4690  C  CG1 . ILE E  1 36  ? 47.843  -39.087 24.817 1.00 19.71 ? 35   ILE E CG1 1 
ATOM   4691  C  CG2 . ILE E  1 36  ? 46.691  -38.462 26.969 1.00 18.93 ? 35   ILE E CG2 1 
ATOM   4692  C  CD1 . ILE E  1 36  ? 46.614  -38.806 23.956 1.00 18.64 ? 35   ILE E CD1 1 
ATOM   4693  N  N   . LYS E  1 37  ? 48.595  -39.706 29.445 1.00 24.35 ? 36   LYS E N   1 
ATOM   4694  C  CA  . LYS E  1 37  ? 48.268  -40.216 30.768 1.00 26.44 ? 36   LYS E CA  1 
ATOM   4695  C  C   . LYS E  1 37  ? 47.225  -39.352 31.462 1.00 25.95 ? 36   LYS E C   1 
ATOM   4696  O  O   . LYS E  1 37  ? 46.865  -38.286 30.963 1.00 25.92 ? 36   LYS E O   1 
ATOM   4697  C  CB  . LYS E  1 37  ? 49.540  -40.317 31.615 1.00 28.16 ? 36   LYS E CB  1 
ATOM   4698  C  CG  . LYS E  1 37  ? 50.234  -38.996 31.883 1.00 32.78 ? 36   LYS E CG  1 
ATOM   4699  C  CD  . LYS E  1 37  ? 51.594  -39.237 32.525 1.00 36.04 ? 36   LYS E CD  1 
ATOM   4700  C  CE  . LYS E  1 37  ? 52.320  -37.934 32.808 1.00 38.54 ? 36   LYS E CE  1 
ATOM   4701  N  NZ  . LYS E  1 37  ? 53.723  -38.182 33.258 1.00 39.70 ? 36   LYS E NZ  1 
ATOM   4702  N  N   . GLY E  1 38  ? 46.730  -39.824 32.604 1.00 23.71 ? 37   GLY E N   1 
ATOM   4703  C  CA  . GLY E  1 38  ? 45.718  -39.083 33.338 1.00 22.35 ? 37   GLY E CA  1 
ATOM   4704  C  C   . GLY E  1 38  ? 44.315  -39.237 32.773 1.00 23.05 ? 37   GLY E C   1 
ATOM   4705  O  O   . GLY E  1 38  ? 43.424  -38.433 33.066 1.00 25.64 ? 37   GLY E O   1 
ATOM   4706  N  N   . LEU E  1 39  ? 44.101  -40.276 31.971 1.00 23.35 ? 38   LEU E N   1 
ATOM   4707  C  CA  . LEU E  1 39  ? 42.796  -40.504 31.357 1.00 23.95 ? 38   LEU E CA  1 
ATOM   4708  C  C   . LEU E  1 39  ? 41.972  -41.596 32.020 1.00 26.01 ? 38   LEU E C   1 
ATOM   4709  O  O   . LEU E  1 39  ? 42.520  -42.562 32.552 1.00 28.01 ? 38   LEU E O   1 
ATOM   4710  C  CB  . LEU E  1 39  ? 42.963  -40.890 29.890 1.00 24.32 ? 38   LEU E CB  1 
ATOM   4711  C  CG  . LEU E  1 39  ? 43.491  -39.890 28.866 1.00 22.11 ? 38   LEU E CG  1 
ATOM   4712  C  CD1 . LEU E  1 39  ? 43.886  -40.664 27.608 1.00 22.16 ? 38   LEU E CD1 1 
ATOM   4713  C  CD2 . LEU E  1 39  ? 42.437  -38.833 28.555 1.00 20.03 ? 38   LEU E CD2 1 
ATOM   4714  N  N   . THR E  1 40  ? 40.651  -41.447 31.975 1.00 28.47 ? 39   THR E N   1 
ATOM   4715  C  CA  . THR E  1 40  ? 39.768  -42.469 32.529 1.00 30.88 ? 39   THR E CA  1 
ATOM   4716  C  C   . THR E  1 40  ? 39.880  -43.658 31.571 1.00 31.61 ? 39   THR E C   1 
ATOM   4717  O  O   . THR E  1 40  ? 40.092  -43.474 30.372 1.00 30.15 ? 39   THR E O   1 
ATOM   4718  C  CB  . THR E  1 40  ? 38.294  -42.006 32.559 1.00 31.49 ? 39   THR E CB  1 
ATOM   4719  O  OG1 . THR E  1 40  ? 37.856  -41.716 31.223 1.00 32.68 ? 39   THR E OG1 1 
ATOM   4720  C  CG2 . THR E  1 40  ? 38.135  -40.765 33.429 1.00 31.25 ? 39   THR E CG2 1 
ATOM   4721  N  N   . GLU E  1 41  ? 39.741  -44.871 32.091 1.00 32.57 ? 40   GLU E N   1 
ATOM   4722  C  CA  . GLU E  1 41  ? 39.833  -46.069 31.259 1.00 32.26 ? 40   GLU E CA  1 
ATOM   4723  C  C   . GLU E  1 41  ? 38.814  -46.020 30.117 1.00 30.05 ? 40   GLU E C   1 
ATOM   4724  O  O   . GLU E  1 41  ? 37.695  -45.539 30.291 1.00 30.33 ? 40   GLU E O   1 
ATOM   4725  C  CB  . GLU E  1 41  ? 39.594  -47.322 32.115 1.00 35.27 ? 40   GLU E CB  1 
ATOM   4726  C  CG  . GLU E  1 41  ? 39.739  -48.635 31.360 1.00 39.29 ? 40   GLU E CG  1 
ATOM   4727  C  CD  . GLU E  1 41  ? 39.504  -49.857 32.240 1.00 43.86 ? 40   GLU E CD  1 
ATOM   4728  O  OE1 . GLU E  1 41  ? 39.817  -50.982 31.790 1.00 45.82 ? 40   GLU E OE1 1 
ATOM   4729  O  OE2 . GLU E  1 41  ? 39.004  -49.697 33.376 1.00 43.77 ? 40   GLU E OE2 1 
ATOM   4730  N  N   . GLY E  1 42  ? 39.208  -46.497 28.942 1.00 29.17 ? 41   GLY E N   1 
ATOM   4731  C  CA  . GLY E  1 42  ? 38.283  -46.503 27.819 1.00 28.89 ? 41   GLY E CA  1 
ATOM   4732  C  C   . GLY E  1 42  ? 38.646  -45.638 26.623 1.00 28.76 ? 41   GLY E C   1 
ATOM   4733  O  O   . GLY E  1 42  ? 39.773  -45.158 26.503 1.00 27.26 ? 41   GLY E O   1 
ATOM   4734  N  N   . LEU E  1 43  ? 37.668  -45.432 25.744 1.00 27.57 ? 42   LEU E N   1 
ATOM   4735  C  CA  . LEU E  1 43  ? 37.852  -44.651 24.523 1.00 26.28 ? 42   LEU E CA  1 
ATOM   4736  C  C   . LEU E  1 43  ? 37.763  -43.140 24.721 1.00 23.53 ? 42   LEU E C   1 
ATOM   4737  O  O   . LEU E  1 43  ? 36.965  -42.652 25.518 1.00 21.72 ? 42   LEU E O   1 
ATOM   4738  C  CB  . LEU E  1 43  ? 36.805  -45.057 23.482 1.00 26.26 ? 42   LEU E CB  1 
ATOM   4739  C  CG  . LEU E  1 43  ? 36.780  -46.495 22.961 1.00 29.42 ? 42   LEU E CG  1 
ATOM   4740  C  CD1 . LEU E  1 43  ? 35.509  -46.709 22.137 1.00 29.41 ? 42   LEU E CD1 1 
ATOM   4741  C  CD2 . LEU E  1 43  ? 38.023  -46.765 22.120 1.00 28.15 ? 42   LEU E CD2 1 
ATOM   4742  N  N   . HIS E  1 44  ? 38.568  -42.409 23.952 1.00 19.76 ? 43   HIS E N   1 
ATOM   4743  C  CA  . HIS E  1 44  ? 38.587  -40.953 24.005 1.00 20.81 ? 43   HIS E CA  1 
ATOM   4744  C  C   . HIS E  1 44  ? 38.780  -40.410 22.595 1.00 18.42 ? 43   HIS E C   1 
ATOM   4745  O  O   . HIS E  1 44  ? 39.699  -40.833 21.895 1.00 17.99 ? 43   HIS E O   1 
ATOM   4746  C  CB  . HIS E  1 44  ? 39.742  -40.473 24.892 1.00 20.48 ? 43   HIS E CB  1 
ATOM   4747  C  CG  . HIS E  1 44  ? 39.551  -40.770 26.345 1.00 23.37 ? 43   HIS E CG  1 
ATOM   4748  N  ND1 . HIS E  1 44  ? 38.820  -39.950 27.181 1.00 23.15 ? 43   HIS E ND1 1 
ATOM   4749  C  CD2 . HIS E  1 44  ? 39.985  -41.795 27.112 1.00 23.45 ? 43   HIS E CD2 1 
ATOM   4750  C  CE1 . HIS E  1 44  ? 38.815  -40.456 28.397 1.00 23.42 ? 43   HIS E CE1 1 
ATOM   4751  N  NE2 . HIS E  1 44  ? 39.516  -41.580 28.386 1.00 21.64 ? 43   HIS E NE2 1 
ATOM   4752  N  N   . GLY E  1 45  ? 37.908  -39.489 22.188 1.00 18.88 ? 44   GLY E N   1 
ATOM   4753  C  CA  . GLY E  1 45  ? 38.012  -38.875 20.871 1.00 19.85 ? 44   GLY E CA  1 
ATOM   4754  C  C   . GLY E  1 45  ? 39.417  -38.331 20.688 1.00 21.13 ? 44   GLY E C   1 
ATOM   4755  O  O   . GLY E  1 45  ? 40.038  -37.898 21.659 1.00 21.64 ? 44   GLY E O   1 
ATOM   4756  N  N   . PHE E  1 46  ? 39.901  -38.323 19.449 1.00 20.76 ? 45   PHE E N   1 
ATOM   4757  C  CA  . PHE E  1 46  ? 41.265  -37.890 19.140 1.00 20.53 ? 45   PHE E CA  1 
ATOM   4758  C  C   . PHE E  1 46  ? 41.259  -37.265 17.744 1.00 21.47 ? 45   PHE E C   1 
ATOM   4759  O  O   . PHE E  1 46  ? 41.191  -37.989 16.746 1.00 20.44 ? 45   PHE E O   1 
ATOM   4760  C  CB  . PHE E  1 46  ? 42.152  -39.136 19.164 1.00 19.57 ? 45   PHE E CB  1 
ATOM   4761  C  CG  . PHE E  1 46  ? 43.625  -38.865 19.090 1.00 21.31 ? 45   PHE E CG  1 
ATOM   4762  C  CD1 . PHE E  1 46  ? 44.280  -38.186 20.114 1.00 22.11 ? 45   PHE E CD1 1 
ATOM   4763  C  CD2 . PHE E  1 46  ? 44.382  -39.394 18.045 1.00 20.21 ? 45   PHE E CD2 1 
ATOM   4764  C  CE1 . PHE E  1 46  ? 45.665  -38.046 20.104 1.00 20.44 ? 45   PHE E CE1 1 
ATOM   4765  C  CE2 . PHE E  1 46  ? 45.771  -39.261 18.024 1.00 20.92 ? 45   PHE E CE2 1 
ATOM   4766  C  CZ  . PHE E  1 46  ? 46.413  -38.591 19.056 1.00 21.89 ? 45   PHE E CZ  1 
ATOM   4767  N  N   . HIS E  1 47  ? 41.333  -35.934 17.673 1.00 20.10 ? 46   HIS E N   1 
ATOM   4768  C  CA  . HIS E  1 47  ? 41.290  -35.241 16.382 1.00 19.09 ? 46   HIS E CA  1 
ATOM   4769  C  C   . HIS E  1 47  ? 42.230  -34.051 16.239 1.00 18.58 ? 46   HIS E C   1 
ATOM   4770  O  O   . HIS E  1 47  ? 42.753  -33.515 17.221 1.00 18.37 ? 46   HIS E O   1 
ATOM   4771  C  CB  . HIS E  1 47  ? 39.888  -34.696 16.107 1.00 19.40 ? 46   HIS E CB  1 
ATOM   4772  C  CG  . HIS E  1 47  ? 38.781  -35.519 16.693 1.00 22.56 ? 46   HIS E CG  1 
ATOM   4773  N  ND1 . HIS E  1 47  ? 38.057  -35.109 17.786 1.00 23.41 ? 46   HIS E ND1 1 
ATOM   4774  C  CD2 . HIS E  1 47  ? 38.277  -36.722 16.330 1.00 23.08 ? 46   HIS E CD2 1 
ATOM   4775  C  CE1 . HIS E  1 47  ? 37.146  -36.026 18.078 1.00 23.94 ? 46   HIS E CE1 1 
ATOM   4776  N  NE2 . HIS E  1 47  ? 37.262  -37.012 17.210 1.00 23.63 ? 46   HIS E NE2 1 
ATOM   4777  N  N   . VAL E  1 48  ? 42.408  -33.631 14.992 1.00 17.38 ? 47   VAL E N   1 
ATOM   4778  C  CA  . VAL E  1 48  ? 43.204  -32.456 14.692 1.00 18.62 ? 47   VAL E CA  1 
ATOM   4779  C  C   . VAL E  1 48  ? 42.149  -31.372 14.480 1.00 19.51 ? 47   VAL E C   1 
ATOM   4780  O  O   . VAL E  1 48  ? 41.283  -31.501 13.605 1.00 20.03 ? 47   VAL E O   1 
ATOM   4781  C  CB  . VAL E  1 48  ? 44.015  -32.613 13.382 1.00 17.27 ? 47   VAL E CB  1 
ATOM   4782  C  CG1 . VAL E  1 48  ? 44.724  -31.303 13.052 1.00 19.10 ? 47   VAL E CG1 1 
ATOM   4783  C  CG2 . VAL E  1 48  ? 45.036  -33.731 13.525 1.00 16.73 ? 47   VAL E CG2 1 
ATOM   4784  N  N   . HIS E  1 49  ? 42.189  -30.330 15.301 1.00 18.32 ? 48   HIS E N   1 
ATOM   4785  C  CA  . HIS E  1 49  ? 41.247  -29.237 15.156 1.00 19.38 ? 48   HIS E CA  1 
ATOM   4786  C  C   . HIS E  1 49  ? 41.884  -28.168 14.266 1.00 20.99 ? 48   HIS E C   1 
ATOM   4787  O  O   . HIS E  1 49  ? 43.105  -28.096 14.159 1.00 21.08 ? 48   HIS E O   1 
ATOM   4788  C  CB  . HIS E  1 49  ? 40.855  -28.692 16.529 1.00 18.61 ? 48   HIS E CB  1 
ATOM   4789  C  CG  . HIS E  1 49  ? 39.886  -29.573 17.257 1.00 20.56 ? 48   HIS E CG  1 
ATOM   4790  N  ND1 . HIS E  1 49  ? 38.677  -29.118 17.728 1.00 20.29 ? 48   HIS E ND1 1 
ATOM   4791  C  CD2 . HIS E  1 49  ? 39.940  -30.893 17.565 1.00 18.73 ? 48   HIS E CD2 1 
ATOM   4792  C  CE1 . HIS E  1 49  ? 38.023  -30.120 18.299 1.00 22.65 ? 48   HIS E CE1 1 
ATOM   4793  N  NE2 . HIS E  1 49  ? 38.770  -31.203 18.211 1.00 19.07 ? 48   HIS E NE2 1 
ATOM   4794  N  N   . GLU E  1 50  ? 41.046  -27.351 13.633 1.00 22.17 ? 49   GLU E N   1 
ATOM   4795  C  CA  . GLU E  1 50  ? 41.486  -26.328 12.683 1.00 22.22 ? 49   GLU E CA  1 
ATOM   4796  C  C   . GLU E  1 50  ? 42.572  -25.325 13.071 1.00 20.54 ? 49   GLU E C   1 
ATOM   4797  O  O   . GLU E  1 50  ? 43.535  -25.147 12.326 1.00 19.71 ? 49   GLU E O   1 
ATOM   4798  C  CB  . GLU E  1 50  ? 40.265  -25.549 12.166 1.00 22.56 ? 49   GLU E CB  1 
ATOM   4799  C  CG  . GLU E  1 50  ? 40.558  -24.666 10.951 1.00 23.77 ? 49   GLU E CG  1 
ATOM   4800  C  CD  . GLU E  1 50  ? 39.316  -23.998 10.373 1.00 25.29 ? 49   GLU E CD  1 
ATOM   4801  O  OE1 . GLU E  1 50  ? 39.439  -23.340 9.319  1.00 27.82 ? 49   GLU E OE1 1 
ATOM   4802  O  OE2 . GLU E  1 50  ? 38.222  -24.120 10.966 1.00 26.63 ? 49   GLU E OE2 1 
ATOM   4803  N  N   . PHE E  1 51  ? 42.425  -24.672 14.220 1.00 20.44 ? 50   PHE E N   1 
ATOM   4804  C  CA  . PHE E  1 51  ? 43.382  -23.647 14.635 1.00 21.11 ? 50   PHE E CA  1 
ATOM   4805  C  C   . PHE E  1 51  ? 44.364  -24.007 15.743 1.00 22.31 ? 50   PHE E C   1 
ATOM   4806  O  O   . PHE E  1 51  ? 43.996  -24.656 16.720 1.00 23.60 ? 50   PHE E O   1 
ATOM   4807  C  CB  . PHE E  1 51  ? 42.607  -22.395 15.056 1.00 21.37 ? 50   PHE E CB  1 
ATOM   4808  C  CG  . PHE E  1 51  ? 41.580  -21.963 14.054 1.00 24.38 ? 50   PHE E CG  1 
ATOM   4809  C  CD1 . PHE E  1 51  ? 41.958  -21.610 12.763 1.00 24.73 ? 50   PHE E CD1 1 
ATOM   4810  C  CD2 . PHE E  1 51  ? 40.229  -21.939 14.389 1.00 25.22 ? 50   PHE E CD2 1 
ATOM   4811  C  CE1 . PHE E  1 51  ? 41.004  -21.238 11.818 1.00 25.17 ? 50   PHE E CE1 1 
ATOM   4812  C  CE2 . PHE E  1 51  ? 39.265  -21.566 13.448 1.00 26.30 ? 50   PHE E CE2 1 
ATOM   4813  C  CZ  . PHE E  1 51  ? 39.660  -21.218 12.160 1.00 26.32 ? 50   PHE E CZ  1 
ATOM   4814  N  N   . GLY E  1 52  ? 45.615  -23.566 15.586 1.00 21.24 ? 51   GLY E N   1 
ATOM   4815  C  CA  . GLY E  1 52  ? 46.637  -23.803 16.599 1.00 19.39 ? 51   GLY E CA  1 
ATOM   4816  C  C   . GLY E  1 52  ? 46.601  -22.598 17.528 1.00 23.30 ? 51   GLY E C   1 
ATOM   4817  O  O   . GLY E  1 52  ? 47.612  -21.948 17.803 1.00 23.74 ? 51   GLY E O   1 
ATOM   4818  N  N   . ASP E  1 53  ? 45.404  -22.309 18.016 1.00 23.35 ? 52   ASP E N   1 
ATOM   4819  C  CA  . ASP E  1 53  ? 45.156  -21.166 18.882 1.00 23.40 ? 52   ASP E CA  1 
ATOM   4820  C  C   . ASP E  1 53  ? 44.737  -21.609 20.282 1.00 23.77 ? 52   ASP E C   1 
ATOM   4821  O  O   . ASP E  1 53  ? 43.653  -22.166 20.471 1.00 23.28 ? 52   ASP E O   1 
ATOM   4822  C  CB  . ASP E  1 53  ? 44.071  -20.317 18.221 1.00 23.51 ? 52   ASP E CB  1 
ATOM   4823  C  CG  . ASP E  1 53  ? 43.727  -19.067 19.003 1.00 24.79 ? 52   ASP E CG  1 
ATOM   4824  O  OD1 . ASP E  1 53  ? 43.179  -18.139 18.371 1.00 22.39 ? 52   ASP E OD1 1 
ATOM   4825  O  OD2 . ASP E  1 53  ? 43.979  -19.014 20.225 1.00 25.43 ? 52   ASP E OD2 1 
ATOM   4826  N  N   . ASN E  1 54  ? 45.601  -21.350 21.259 1.00 23.07 ? 53   ASN E N   1 
ATOM   4827  C  CA  . ASN E  1 54  ? 45.345  -21.729 22.642 1.00 24.78 ? 53   ASN E CA  1 
ATOM   4828  C  C   . ASN E  1 54  ? 45.117  -20.506 23.537 1.00 26.29 ? 53   ASN E C   1 
ATOM   4829  O  O   . ASN E  1 54  ? 45.302  -20.577 24.759 1.00 26.03 ? 53   ASN E O   1 
ATOM   4830  C  CB  . ASN E  1 54  ? 46.530  -22.537 23.183 1.00 26.58 ? 53   ASN E CB  1 
ATOM   4831  C  CG  . ASN E  1 54  ? 46.181  -23.322 24.433 1.00 29.85 ? 53   ASN E CG  1 
ATOM   4832  O  OD1 . ASN E  1 54  ? 46.910  -23.293 25.423 1.00 32.59 ? 53   ASN E OD1 1 
ATOM   4833  N  ND2 . ASN E  1 54  ? 45.067  -24.042 24.387 1.00 31.81 ? 53   ASN E ND2 1 
ATOM   4834  N  N   . THR E  1 55  ? 44.715  -19.387 22.941 1.00 26.00 ? 54   THR E N   1 
ATOM   4835  C  CA  . THR E  1 55  ? 44.500  -18.181 23.729 1.00 27.47 ? 54   THR E CA  1 
ATOM   4836  C  C   . THR E  1 55  ? 43.436  -18.391 24.798 1.00 29.34 ? 54   THR E C   1 
ATOM   4837  O  O   . THR E  1 55  ? 43.539  -17.833 25.886 1.00 27.97 ? 54   THR E O   1 
ATOM   4838  C  CB  . THR E  1 55  ? 44.116  -16.980 22.849 1.00 25.40 ? 54   THR E CB  1 
ATOM   4839  O  OG1 . THR E  1 55  ? 42.930  -17.278 22.115 1.00 27.17 ? 54   THR E OG1 1 
ATOM   4840  C  CG2 . THR E  1 55  ? 45.238  -16.662 21.880 1.00 24.64 ? 54   THR E CG2 1 
ATOM   4841  N  N   . ALA E  1 56  ? 42.426  -19.205 24.498 1.00 29.70 ? 55   ALA E N   1 
ATOM   4842  C  CA  . ALA E  1 56  ? 41.372  -19.487 25.468 1.00 31.15 ? 55   ALA E CA  1 
ATOM   4843  C  C   . ALA E  1 56  ? 41.316  -20.984 25.758 1.00 31.63 ? 55   ALA E C   1 
ATOM   4844  O  O   . ALA E  1 56  ? 40.246  -21.584 25.779 1.00 33.58 ? 55   ALA E O   1 
ATOM   4845  C  CB  . ALA E  1 56  ? 40.021  -18.996 24.940 1.00 30.96 ? 55   ALA E CB  1 
ATOM   4846  N  N   . GLY E  1 57  ? 42.475  -21.585 25.992 1.00 30.68 ? 56   GLY E N   1 
ATOM   4847  C  CA  . GLY E  1 57  ? 42.506  -23.011 26.257 1.00 30.81 ? 56   GLY E CA  1 
ATOM   4848  C  C   . GLY E  1 57  ? 42.196  -23.775 24.979 1.00 28.98 ? 56   GLY E C   1 
ATOM   4849  O  O   . GLY E  1 57  ? 42.292  -23.219 23.889 1.00 29.52 ? 56   GLY E O   1 
ATOM   4850  N  N   . CYS E  1 58  ? 41.807  -25.038 25.105 1.00 28.11 ? 57   CYS E N   1 
ATOM   4851  C  CA  . CYS E  1 58  ? 41.501  -25.856 23.932 1.00 26.54 ? 57   CYS E CA  1 
ATOM   4852  C  C   . CYS E  1 58  ? 40.276  -25.391 23.153 1.00 25.81 ? 57   CYS E C   1 
ATOM   4853  O  O   . CYS E  1 58  ? 40.080  -25.776 22.001 1.00 26.33 ? 57   CYS E O   1 
ATOM   4854  C  CB  . CYS E  1 58  ? 41.334  -27.318 24.354 1.00 26.07 ? 57   CYS E CB  1 
ATOM   4855  S  SG  . CYS E  1 58  ? 42.804  -27.965 25.206 1.00 28.35 ? 57   CYS E SG  1 
ATOM   4856  N  N   . THR E  1 59  ? 39.457  -24.551 23.774 1.00 25.02 ? 58   THR E N   1 
ATOM   4857  C  CA  . THR E  1 59  ? 38.255  -24.050 23.123 1.00 25.92 ? 58   THR E CA  1 
ATOM   4858  C  C   . THR E  1 59  ? 38.550  -23.228 21.876 1.00 26.93 ? 58   THR E C   1 
ATOM   4859  O  O   . THR E  1 59  ? 37.805  -23.292 20.900 1.00 26.76 ? 58   THR E O   1 
ATOM   4860  C  CB  . THR E  1 59  ? 37.421  -23.171 24.085 1.00 27.57 ? 58   THR E CB  1 
ATOM   4861  O  OG1 . THR E  1 59  ? 37.020  -23.951 25.216 1.00 31.96 ? 58   THR E OG1 1 
ATOM   4862  C  CG2 . THR E  1 59  ? 36.184  -22.635 23.388 1.00 29.91 ? 58   THR E CG2 1 
ATOM   4863  N  N   . SER E  1 60  ? 39.635  -22.459 21.901 1.00 23.69 ? 59   SER E N   1 
ATOM   4864  C  CA  . SER E  1 60  ? 39.969  -21.613 20.762 1.00 24.63 ? 59   SER E CA  1 
ATOM   4865  C  C   . SER E  1 60  ? 40.526  -22.354 19.546 1.00 23.43 ? 59   SER E C   1 
ATOM   4866  O  O   . SER E  1 60  ? 40.731  -21.758 18.491 1.00 23.04 ? 59   SER E O   1 
ATOM   4867  C  CB  . SER E  1 60  ? 40.923  -20.489 21.204 1.00 24.96 ? 59   SER E CB  1 
ATOM   4868  O  OG  . SER E  1 60  ? 41.904  -20.960 22.113 1.00 28.09 ? 59   SER E OG  1 
ATOM   4869  N  N   . ALA E  1 61  ? 40.755  -23.656 19.681 1.00 22.63 ? 60   ALA E N   1 
ATOM   4870  C  CA  . ALA E  1 61  ? 41.261  -24.438 18.557 1.00 21.90 ? 60   ALA E CA  1 
ATOM   4871  C  C   . ALA E  1 61  ? 40.194  -24.599 17.463 1.00 21.19 ? 60   ALA E C   1 
ATOM   4872  O  O   . ALA E  1 61  ? 40.477  -25.095 16.372 1.00 22.95 ? 60   ALA E O   1 
ATOM   4873  C  CB  . ALA E  1 61  ? 41.730  -25.802 19.039 1.00 19.02 ? 60   ALA E CB  1 
ATOM   4874  N  N   . GLY E  1 62  ? 38.968  -24.178 17.748 1.00 21.62 ? 61   GLY E N   1 
ATOM   4875  C  CA  . GLY E  1 62  ? 37.915  -24.301 16.752 1.00 22.27 ? 61   GLY E CA  1 
ATOM   4876  C  C   . GLY E  1 62  ? 37.441  -25.728 16.511 1.00 22.05 ? 61   GLY E C   1 
ATOM   4877  O  O   . GLY E  1 62  ? 37.698  -26.609 17.323 1.00 23.63 ? 61   GLY E O   1 
ATOM   4878  N  N   . PRO E  1 63  ? 36.743  -25.987 15.393 1.00 24.61 ? 62   PRO E N   1 
ATOM   4879  C  CA  . PRO E  1 63  ? 36.228  -27.319 15.056 1.00 24.50 ? 62   PRO E CA  1 
ATOM   4880  C  C   . PRO E  1 63  ? 37.283  -28.220 14.424 1.00 24.31 ? 62   PRO E C   1 
ATOM   4881  O  O   . PRO E  1 63  ? 38.453  -27.844 14.308 1.00 22.75 ? 62   PRO E O   1 
ATOM   4882  C  CB  . PRO E  1 63  ? 35.096  -27.001 14.092 1.00 25.96 ? 62   PRO E CB  1 
ATOM   4883  C  CG  . PRO E  1 63  ? 35.687  -25.854 13.305 1.00 26.28 ? 62   PRO E CG  1 
ATOM   4884  C  CD  . PRO E  1 63  ? 36.305  -24.990 14.397 1.00 26.01 ? 62   PRO E CD  1 
ATOM   4885  N  N   . HIS E  1 64  ? 36.860  -29.409 14.008 1.00 22.95 ? 63   HIS E N   1 
ATOM   4886  C  CA  . HIS E  1 64  ? 37.770  -30.366 13.381 1.00 22.15 ? 63   HIS E CA  1 
ATOM   4887  C  C   . HIS E  1 64  ? 38.292  -29.825 12.051 1.00 22.04 ? 63   HIS E C   1 
ATOM   4888  O  O   . HIS E  1 64  ? 37.552  -29.188 11.299 1.00 21.93 ? 63   HIS E O   1 
ATOM   4889  C  CB  . HIS E  1 64  ? 37.053  -31.714 13.163 1.00 20.37 ? 63   HIS E CB  1 
ATOM   4890  C  CG  . HIS E  1 64  ? 36.596  -32.360 14.434 1.00 22.12 ? 63   HIS E CG  1 
ATOM   4891  N  ND1 . HIS E  1 64  ? 35.950  -33.584 14.463 1.00 22.94 ? 63   HIS E ND1 1 
ATOM   4892  C  CD2 . HIS E  1 64  ? 36.692  -31.962 15.725 1.00 21.32 ? 63   HIS E CD2 1 
ATOM   4893  C  CE1 . HIS E  1 64  ? 35.674  -33.904 15.713 1.00 18.47 ? 63   HIS E CE1 1 
ATOM   4894  N  NE2 . HIS E  1 64  ? 36.113  -32.936 16.500 1.00 23.14 ? 63   HIS E NE2 1 
ATOM   4895  N  N   . PHE E  1 65  ? 39.576  -30.049 11.780 1.00 23.04 ? 64   PHE E N   1 
ATOM   4896  C  CA  . PHE E  1 65  ? 40.184  -29.592 10.527 1.00 22.29 ? 64   PHE E CA  1 
ATOM   4897  C  C   . PHE E  1 65  ? 39.373  -30.240 9.405  1.00 24.63 ? 64   PHE E C   1 
ATOM   4898  O  O   . PHE E  1 65  ? 39.380  -31.464 9.254  1.00 24.86 ? 64   PHE E O   1 
ATOM   4899  C  CB  . PHE E  1 65  ? 41.649  -30.037 10.448 1.00 21.89 ? 64   PHE E CB  1 
ATOM   4900  C  CG  . PHE E  1 65  ? 42.362  -29.561 9.211  1.00 20.29 ? 64   PHE E CG  1 
ATOM   4901  C  CD1 . PHE E  1 65  ? 43.297  -30.372 8.583  1.00 21.49 ? 64   PHE E CD1 1 
ATOM   4902  C  CD2 . PHE E  1 65  ? 42.104  -28.297 8.679  1.00 22.50 ? 64   PHE E CD2 1 
ATOM   4903  C  CE1 . PHE E  1 65  ? 43.967  -29.943 7.437  1.00 19.28 ? 64   PHE E CE1 1 
ATOM   4904  C  CE2 . PHE E  1 65  ? 42.772  -27.853 7.528  1.00 21.11 ? 64   PHE E CE2 1 
ATOM   4905  C  CZ  . PHE E  1 65  ? 43.702  -28.680 6.911  1.00 21.01 ? 64   PHE E CZ  1 
ATOM   4906  N  N   . ASN E  1 66  ? 38.696  -29.412 8.613  1.00 24.48 ? 65   ASN E N   1 
ATOM   4907  C  CA  . ASN E  1 66  ? 37.811  -29.900 7.556  1.00 25.92 ? 65   ASN E CA  1 
ATOM   4908  C  C   . ASN E  1 66  ? 37.933  -29.105 6.246  1.00 26.36 ? 65   ASN E C   1 
ATOM   4909  O  O   . ASN E  1 66  ? 36.990  -28.434 5.824  1.00 26.46 ? 65   ASN E O   1 
ATOM   4910  C  CB  . ASN E  1 66  ? 36.381  -29.833 8.112  1.00 24.44 ? 65   ASN E CB  1 
ATOM   4911  C  CG  . ASN E  1 66  ? 35.347  -30.476 7.209  1.00 24.85 ? 65   ASN E CG  1 
ATOM   4912  O  OD1 . ASN E  1 66  ? 35.646  -31.376 6.425  1.00 25.82 ? 65   ASN E OD1 1 
ATOM   4913  N  ND2 . ASN E  1 66  ? 34.104  -30.026 7.343  1.00 21.74 ? 65   ASN E ND2 1 
ATOM   4914  N  N   . PRO E  1 67  ? 39.098  -29.183 5.581  1.00 27.07 ? 66   PRO E N   1 
ATOM   4915  C  CA  . PRO E  1 67  ? 39.316  -28.458 4.323  1.00 30.17 ? 66   PRO E CA  1 
ATOM   4916  C  C   . PRO E  1 67  ? 38.435  -28.900 3.154  1.00 33.22 ? 66   PRO E C   1 
ATOM   4917  O  O   . PRO E  1 67  ? 38.215  -28.129 2.225  1.00 35.26 ? 66   PRO E O   1 
ATOM   4918  C  CB  . PRO E  1 67  ? 40.800  -28.685 4.047  1.00 29.65 ? 66   PRO E CB  1 
ATOM   4919  C  CG  . PRO E  1 67  ? 41.038  -30.049 4.640  1.00 27.84 ? 66   PRO E CG  1 
ATOM   4920  C  CD  . PRO E  1 67  ? 40.297  -29.956 5.952  1.00 26.09 ? 66   PRO E CD  1 
ATOM   4921  N  N   . LEU E  1 68  ? 37.937  -30.132 3.193  1.00 34.16 ? 67   LEU E N   1 
ATOM   4922  C  CA  . LEU E  1 68  ? 37.083  -30.629 2.118  1.00 35.91 ? 67   LEU E CA  1 
ATOM   4923  C  C   . LEU E  1 68  ? 35.614  -30.390 2.427  1.00 36.48 ? 67   LEU E C   1 
ATOM   4924  O  O   . LEU E  1 68  ? 34.736  -30.747 1.640  1.00 36.88 ? 67   LEU E O   1 
ATOM   4925  C  CB  . LEU E  1 68  ? 37.329  -32.120 1.884  1.00 37.75 ? 67   LEU E CB  1 
ATOM   4926  C  CG  . LEU E  1 68  ? 38.766  -32.495 1.515  1.00 39.29 ? 67   LEU E CG  1 
ATOM   4927  C  CD1 . LEU E  1 68  ? 38.830  -33.974 1.189  1.00 42.07 ? 67   LEU E CD1 1 
ATOM   4928  C  CD2 . LEU E  1 68  ? 39.235  -31.667 0.324  1.00 41.91 ? 67   LEU E CD2 1 
ATOM   4929  N  N   . SER E  1 69  ? 35.355  -29.785 3.580  1.00 36.07 ? 68   SER E N   1 
ATOM   4930  C  CA  . SER E  1 69  ? 33.998  -29.472 4.006  1.00 36.83 ? 68   SER E CA  1 
ATOM   4931  C  C   . SER E  1 69  ? 33.062  -30.678 4.006  1.00 37.77 ? 68   SER E C   1 
ATOM   4932  O  O   . SER E  1 69  ? 31.994  -30.645 3.394  1.00 38.05 ? 68   SER E O   1 
ATOM   4933  C  CB  . SER E  1 69  ? 33.418  -28.376 3.112  1.00 38.13 ? 68   SER E CB  1 
ATOM   4934  O  OG  . SER E  1 69  ? 34.241  -27.221 3.138  1.00 38.87 ? 68   SER E OG  1 
ATOM   4935  N  N   . ARG E  1 70  ? 33.461  -31.744 4.690  1.00 35.54 ? 69   ARG E N   1 
ATOM   4936  C  CA  . ARG E  1 70  ? 32.630  -32.933 4.766  1.00 35.09 ? 69   ARG E CA  1 
ATOM   4937  C  C   . ARG E  1 70  ? 32.052  -33.081 6.162  1.00 33.80 ? 69   ARG E C   1 
ATOM   4938  O  O   . ARG E  1 70  ? 32.227  -32.204 7.015  1.00 31.33 ? 69   ARG E O   1 
ATOM   4939  C  CB  . ARG E  1 70  ? 33.444  -34.174 4.390  1.00 36.18 ? 69   ARG E CB  1 
ATOM   4940  C  CG  . ARG E  1 70  ? 33.833  -34.193 2.925  1.00 37.75 ? 69   ARG E CG  1 
ATOM   4941  C  CD  . ARG E  1 70  ? 34.565  -35.456 2.525  1.00 40.92 ? 69   ARG E CD  1 
ATOM   4942  N  NE  . ARG E  1 70  ? 34.890  -35.434 1.102  1.00 43.26 ? 69   ARG E NE  1 
ATOM   4943  C  CZ  . ARG E  1 70  ? 35.633  -36.346 0.486  1.00 44.08 ? 69   ARG E CZ  1 
ATOM   4944  N  NH1 . ARG E  1 70  ? 35.873  -36.236 -0.813 1.00 44.76 ? 69   ARG E NH1 1 
ATOM   4945  N  NH2 . ARG E  1 70  ? 36.138  -37.364 1.166  1.00 45.89 ? 69   ARG E NH2 1 
ATOM   4946  N  N   . LYS E  1 71  ? 31.345  -34.185 6.382  1.00 32.79 ? 70   LYS E N   1 
ATOM   4947  C  CA  . LYS E  1 71  ? 30.741  -34.481 7.675  1.00 32.30 ? 70   LYS E CA  1 
ATOM   4948  C  C   . LYS E  1 71  ? 31.728  -35.307 8.494  1.00 29.06 ? 70   LYS E C   1 
ATOM   4949  O  O   . LYS E  1 71  ? 32.633  -35.927 7.938  1.00 29.57 ? 70   LYS E O   1 
ATOM   4950  C  CB  . LYS E  1 71  ? 29.456  -35.288 7.483  1.00 35.09 ? 70   LYS E CB  1 
ATOM   4951  C  CG  . LYS E  1 71  ? 28.373  -34.576 6.691  1.00 39.56 ? 70   LYS E CG  1 
ATOM   4952  C  CD  . LYS E  1 71  ? 27.825  -33.382 7.450  1.00 42.99 ? 70   LYS E CD  1 
ATOM   4953  C  CE  . LYS E  1 71  ? 26.609  -32.788 6.742  1.00 46.67 ? 70   LYS E CE  1 
ATOM   4954  N  NZ  . LYS E  1 71  ? 26.069  -31.603 7.469  1.00 47.74 ? 70   LYS E NZ  1 
ATOM   4955  N  N   . HIS E  1 72  ? 31.540  -35.323 9.807  1.00 27.93 ? 71   HIS E N   1 
ATOM   4956  C  CA  . HIS E  1 72  ? 32.407  -36.082 10.700 1.00 26.87 ? 71   HIS E CA  1 
ATOM   4957  C  C   . HIS E  1 72  ? 32.227  -37.583 10.503 1.00 26.26 ? 71   HIS E C   1 
ATOM   4958  O  O   . HIS E  1 72  ? 31.113  -38.072 10.334 1.00 27.38 ? 71   HIS E O   1 
ATOM   4959  C  CB  . HIS E  1 72  ? 32.100  -35.735 12.162 1.00 25.94 ? 71   HIS E CB  1 
ATOM   4960  C  CG  . HIS E  1 72  ? 32.917  -36.507 13.154 1.00 25.32 ? 71   HIS E CG  1 
ATOM   4961  N  ND1 . HIS E  1 72  ? 34.235  -36.208 13.430 1.00 26.60 ? 71   HIS E ND1 1 
ATOM   4962  C  CD2 . HIS E  1 72  ? 32.606  -37.572 13.932 1.00 25.16 ? 71   HIS E CD2 1 
ATOM   4963  C  CE1 . HIS E  1 72  ? 34.697  -37.051 14.335 1.00 25.41 ? 71   HIS E CE1 1 
ATOM   4964  N  NE2 . HIS E  1 72  ? 33.730  -37.888 14.657 1.00 25.71 ? 71   HIS E NE2 1 
ATOM   4965  N  N   . GLY E  1 73  ? 33.331  -38.313 10.529 1.00 25.09 ? 72   GLY E N   1 
ATOM   4966  C  CA  . GLY E  1 73  ? 33.261  -39.751 10.379 1.00 23.93 ? 72   GLY E CA  1 
ATOM   4967  C  C   . GLY E  1 73  ? 34.423  -40.374 11.118 1.00 24.83 ? 72   GLY E C   1 
ATOM   4968  O  O   . GLY E  1 73  ? 35.109  -39.690 11.881 1.00 24.40 ? 72   GLY E O   1 
ATOM   4969  N  N   . GLY E  1 74  ? 34.631  -41.671 10.911 1.00 23.32 ? 73   GLY E N   1 
ATOM   4970  C  CA  . GLY E  1 74  ? 35.748  -42.356 11.533 1.00 22.83 ? 73   GLY E CA  1 
ATOM   4971  C  C   . GLY E  1 74  ? 36.887  -42.270 10.533 1.00 23.34 ? 73   GLY E C   1 
ATOM   4972  O  O   . GLY E  1 74  ? 36.630  -42.012 9.359  1.00 23.71 ? 73   GLY E O   1 
ATOM   4973  N  N   . PRO E  1 75  ? 38.146  -42.485 10.947 1.00 22.55 ? 74   PRO E N   1 
ATOM   4974  C  CA  . PRO E  1 75  ? 39.277  -42.407 10.015 1.00 24.68 ? 74   PRO E CA  1 
ATOM   4975  C  C   . PRO E  1 75  ? 39.189  -43.295 8.772  1.00 27.24 ? 74   PRO E C   1 
ATOM   4976  O  O   . PRO E  1 75  ? 39.740  -42.961 7.726  1.00 24.27 ? 74   PRO E O   1 
ATOM   4977  C  CB  . PRO E  1 75  ? 40.483  -42.748 10.897 1.00 22.94 ? 74   PRO E CB  1 
ATOM   4978  C  CG  . PRO E  1 75  ? 39.884  -43.556 12.040 1.00 23.22 ? 74   PRO E CG  1 
ATOM   4979  C  CD  . PRO E  1 75  ? 38.602  -42.811 12.308 1.00 22.16 ? 74   PRO E CD  1 
ATOM   4980  N  N   . LYS E  1 76  ? 38.490  -44.417 8.884  1.00 29.23 ? 75   LYS E N   1 
ATOM   4981  C  CA  . LYS E  1 76  ? 38.361  -45.334 7.756  1.00 31.42 ? 75   LYS E CA  1 
ATOM   4982  C  C   . LYS E  1 76  ? 37.234  -44.968 6.789  1.00 31.88 ? 75   LYS E C   1 
ATOM   4983  O  O   . LYS E  1 76  ? 37.119  -45.556 5.715  1.00 31.76 ? 75   LYS E O   1 
ATOM   4984  C  CB  . LYS E  1 76  ? 38.171  -46.754 8.287  1.00 33.74 ? 75   LYS E CB  1 
ATOM   4985  C  CG  . LYS E  1 76  ? 39.377  -47.232 9.088  1.00 35.28 ? 75   LYS E CG  1 
ATOM   4986  C  CD  . LYS E  1 76  ? 39.003  -48.270 10.126 1.00 40.53 ? 75   LYS E CD  1 
ATOM   4987  C  CE  . LYS E  1 76  ? 40.203  -48.616 11.012 1.00 43.61 ? 75   LYS E CE  1 
ATOM   4988  N  NZ  . LYS E  1 76  ? 40.769  -47.452 11.785 1.00 41.30 ? 75   LYS E NZ  1 
ATOM   4989  N  N   . ASP E  1 77  ? 36.408  -43.998 7.164  1.00 30.11 ? 76   ASP E N   1 
ATOM   4990  C  CA  . ASP E  1 77  ? 35.304  -43.569 6.310  1.00 32.11 ? 76   ASP E CA  1 
ATOM   4991  C  C   . ASP E  1 77  ? 35.777  -42.602 5.233  1.00 34.33 ? 76   ASP E C   1 
ATOM   4992  O  O   . ASP E  1 77  ? 36.687  -41.799 5.461  1.00 32.35 ? 76   ASP E O   1 
ATOM   4993  C  CB  . ASP E  1 77  ? 34.232  -42.865 7.134  1.00 31.38 ? 76   ASP E CB  1 
ATOM   4994  C  CG  . ASP E  1 77  ? 33.631  -43.754 8.189  1.00 31.38 ? 76   ASP E CG  1 
ATOM   4995  O  OD1 . ASP E  1 77  ? 33.056  -43.210 9.156  1.00 29.57 ? 76   ASP E OD1 1 
ATOM   4996  O  OD2 . ASP E  1 77  ? 33.728  -44.988 8.043  1.00 31.46 ? 76   ASP E OD2 1 
ATOM   4997  N  N   . GLU E  1 78  ? 35.144  -42.673 4.066  1.00 33.81 ? 77   GLU E N   1 
ATOM   4998  C  CA  . GLU E  1 78  ? 35.478  -41.780 2.965  1.00 35.84 ? 77   GLU E CA  1 
ATOM   4999  C  C   . GLU E  1 78  ? 34.942  -40.401 3.345  1.00 33.59 ? 77   GLU E C   1 
ATOM   5000  O  O   . GLU E  1 78  ? 35.575  -39.378 3.080  1.00 33.90 ? 77   GLU E O   1 
ATOM   5001  C  CB  . GLU E  1 78  ? 34.831  -42.276 1.670  1.00 38.99 ? 77   GLU E CB  1 
ATOM   5002  C  CG  . GLU E  1 78  ? 35.223  -41.491 0.428  1.00 47.77 ? 77   GLU E CG  1 
ATOM   5003  C  CD  . GLU E  1 78  ? 34.292  -40.325 0.145  1.00 52.73 ? 77   GLU E CD  1 
ATOM   5004  O  OE1 . GLU E  1 78  ? 34.554  -39.586 -0.831 1.00 56.08 ? 77   GLU E OE1 1 
ATOM   5005  O  OE2 . GLU E  1 78  ? 33.297  -40.151 0.888  1.00 55.47 ? 77   GLU E OE2 1 
ATOM   5006  N  N   . GLU E  1 79  ? 33.769  -40.386 3.972  1.00 30.69 ? 78   GLU E N   1 
ATOM   5007  C  CA  . GLU E  1 79  ? 33.157  -39.143 4.424  1.00 30.28 ? 78   GLU E CA  1 
ATOM   5008  C  C   . GLU E  1 79  ? 33.660  -38.903 5.846  1.00 29.07 ? 78   GLU E C   1 
ATOM   5009  O  O   . GLU E  1 79  ? 33.168  -39.499 6.808  1.00 26.72 ? 78   GLU E O   1 
ATOM   5010  C  CB  . GLU E  1 79  ? 31.632  -39.254 4.423  1.00 31.64 ? 78   GLU E CB  1 
ATOM   5011  C  CG  . GLU E  1 79  ? 30.902  -37.978 4.852  1.00 34.14 ? 78   GLU E CG  1 
ATOM   5012  C  CD  . GLU E  1 79  ? 30.994  -36.861 3.819  1.00 35.96 ? 78   GLU E CD  1 
ATOM   5013  O  OE1 . GLU E  1 79  ? 30.505  -35.745 4.099  1.00 34.47 ? 78   GLU E OE1 1 
ATOM   5014  O  OE2 . GLU E  1 79  ? 31.551  -37.099 2.726  1.00 39.13 ? 78   GLU E OE2 1 
ATOM   5015  N  N   . ARG E  1 80  ? 34.664  -38.046 5.966  1.00 28.25 ? 79   ARG E N   1 
ATOM   5016  C  CA  . ARG E  1 80  ? 35.244  -37.720 7.260  1.00 26.81 ? 79   ARG E CA  1 
ATOM   5017  C  C   . ARG E  1 80  ? 35.932  -36.369 7.161  1.00 27.81 ? 79   ARG E C   1 
ATOM   5018  O  O   . ARG E  1 80  ? 36.112  -35.832 6.068  1.00 26.00 ? 79   ARG E O   1 
ATOM   5019  C  CB  . ARG E  1 80  ? 36.283  -38.771 7.653  1.00 28.40 ? 79   ARG E CB  1 
ATOM   5020  C  CG  . ARG E  1 80  ? 37.481  -38.860 6.696  1.00 26.11 ? 79   ARG E CG  1 
ATOM   5021  C  CD  . ARG E  1 80  ? 38.803  -38.588 7.410  1.00 32.26 ? 79   ARG E CD  1 
ATOM   5022  N  NE  . ARG E  1 80  ? 39.630  -39.781 7.529  1.00 34.13 ? 79   ARG E NE  1 
ATOM   5023  C  CZ  . ARG E  1 80  ? 40.866  -39.799 8.022  1.00 29.78 ? 79   ARG E CZ  1 
ATOM   5024  N  NH1 . ARG E  1 80  ? 41.527  -40.943 8.077  1.00 28.19 ? 79   ARG E NH1 1 
ATOM   5025  N  NH2 . ARG E  1 80  ? 41.443  -38.685 8.461  1.00 29.40 ? 79   ARG E NH2 1 
ATOM   5026  N  N   . HIS E  1 81  ? 36.296  -35.816 8.312  1.00 26.07 ? 80   HIS E N   1 
ATOM   5027  C  CA  . HIS E  1 81  ? 37.022  -34.556 8.353  1.00 24.67 ? 80   HIS E CA  1 
ATOM   5028  C  C   . HIS E  1 81  ? 38.468  -35.015 8.211  1.00 24.46 ? 80   HIS E C   1 
ATOM   5029  O  O   . HIS E  1 81  ? 38.808  -36.121 8.641  1.00 20.16 ? 80   HIS E O   1 
ATOM   5030  C  CB  . HIS E  1 81  ? 36.843  -33.879 9.714  1.00 24.36 ? 80   HIS E CB  1 
ATOM   5031  C  CG  . HIS E  1 81  ? 35.436  -33.454 10.002 1.00 25.59 ? 80   HIS E CG  1 
ATOM   5032  N  ND1 . HIS E  1 81  ? 34.913  -33.436 11.280 1.00 24.76 ? 80   HIS E ND1 1 
ATOM   5033  C  CD2 . HIS E  1 81  ? 34.467  -32.967 9.196  1.00 25.00 ? 80   HIS E CD2 1 
ATOM   5034  C  CE1 . HIS E  1 81  ? 33.687  -32.950 11.244 1.00 25.57 ? 80   HIS E CE1 1 
ATOM   5035  N  NE2 . HIS E  1 81  ? 33.392  -32.656 9.990  1.00 24.83 ? 80   HIS E NE2 1 
ATOM   5036  N  N   . VAL E  1 82  ? 39.321  -34.191 7.606  1.00 22.58 ? 81   VAL E N   1 
ATOM   5037  C  CA  . VAL E  1 82  ? 40.718  -34.569 7.466  1.00 19.48 ? 81   VAL E CA  1 
ATOM   5038  C  C   . VAL E  1 82  ? 41.290  -34.852 8.856  1.00 19.01 ? 81   VAL E C   1 
ATOM   5039  O  O   . VAL E  1 82  ? 42.108  -35.755 9.031  1.00 19.97 ? 81   VAL E O   1 
ATOM   5040  C  CB  . VAL E  1 82  ? 41.545  -33.438 6.783  1.00 21.13 ? 81   VAL E CB  1 
ATOM   5041  C  CG1 . VAL E  1 82  ? 43.040  -33.671 6.983  1.00 18.13 ? 81   VAL E CG1 1 
ATOM   5042  C  CG2 . VAL E  1 82  ? 41.227  -33.402 5.292  1.00 21.52 ? 81   VAL E CG2 1 
ATOM   5043  N  N   . GLY E  1 83  ? 40.835  -34.095 9.851  1.00 18.35 ? 82   GLY E N   1 
ATOM   5044  C  CA  . GLY E  1 83  ? 41.347  -34.280 11.202 1.00 19.27 ? 82   GLY E CA  1 
ATOM   5045  C  C   . GLY E  1 83  ? 40.739  -35.402 12.027 1.00 20.35 ? 82   GLY E C   1 
ATOM   5046  O  O   . GLY E  1 83  ? 41.099  -35.584 13.191 1.00 19.80 ? 82   GLY E O   1 
ATOM   5047  N  N   . ASP E  1 84  ? 39.821  -36.167 11.446 1.00 22.16 ? 83   ASP E N   1 
ATOM   5048  C  CA  . ASP E  1 84  ? 39.189  -37.262 12.189 1.00 22.75 ? 83   ASP E CA  1 
ATOM   5049  C  C   . ASP E  1 84  ? 40.129  -38.454 12.351 1.00 21.98 ? 83   ASP E C   1 
ATOM   5050  O  O   . ASP E  1 84  ? 40.290  -39.244 11.426 1.00 24.51 ? 83   ASP E O   1 
ATOM   5051  C  CB  . ASP E  1 84  ? 37.915  -37.733 11.477 1.00 21.14 ? 83   ASP E CB  1 
ATOM   5052  C  CG  . ASP E  1 84  ? 36.794  -36.717 11.532 1.00 22.96 ? 83   ASP E CG  1 
ATOM   5053  O  OD1 . ASP E  1 84  ? 36.833  -35.814 12.400 1.00 21.68 ? 83   ASP E OD1 1 
ATOM   5054  O  OD2 . ASP E  1 84  ? 35.852  -36.833 10.720 1.00 22.14 ? 83   ASP E OD2 1 
ATOM   5055  N  N   . LEU E  1 85  ? 40.740  -38.603 13.522 1.00 21.26 ? 84   LEU E N   1 
ATOM   5056  C  CA  . LEU E  1 85  ? 41.647  -39.726 13.750 1.00 20.31 ? 84   LEU E CA  1 
ATOM   5057  C  C   . LEU E  1 85  ? 41.030  -40.810 14.648 1.00 20.50 ? 84   LEU E C   1 
ATOM   5058  O  O   . LEU E  1 85  ? 41.729  -41.709 15.125 1.00 21.49 ? 84   LEU E O   1 
ATOM   5059  C  CB  . LEU E  1 85  ? 42.977  -39.232 14.351 1.00 20.19 ? 84   LEU E CB  1 
ATOM   5060  C  CG  . LEU E  1 85  ? 43.818  -38.299 13.459 1.00 20.91 ? 84   LEU E CG  1 
ATOM   5061  C  CD1 . LEU E  1 85  ? 45.121  -37.941 14.175 1.00 21.62 ? 84   LEU E CD1 1 
ATOM   5062  C  CD2 . LEU E  1 85  ? 44.117  -38.981 12.115 1.00 22.43 ? 84   LEU E CD2 1 
ATOM   5063  N  N   . GLY E  1 86  ? 39.726  -40.706 14.891 1.00 21.02 ? 85   GLY E N   1 
ATOM   5064  C  CA  . GLY E  1 86  ? 39.033  -41.703 15.698 1.00 21.56 ? 85   GLY E CA  1 
ATOM   5065  C  C   . GLY E  1 86  ? 39.182  -41.619 17.207 1.00 23.15 ? 85   GLY E C   1 
ATOM   5066  O  O   . GLY E  1 86  ? 39.007  -40.556 17.805 1.00 22.16 ? 85   GLY E O   1 
ATOM   5067  N  N   . ASN E  1 87  ? 39.502  -42.754 17.822 1.00 21.34 ? 86   ASN E N   1 
ATOM   5068  C  CA  . ASN E  1 87  ? 39.673  -42.831 19.269 1.00 23.94 ? 86   ASN E CA  1 
ATOM   5069  C  C   . ASN E  1 87  ? 41.019  -43.414 19.646 1.00 21.52 ? 86   ASN E C   1 
ATOM   5070  O  O   . ASN E  1 87  ? 41.686  -44.053 18.833 1.00 23.19 ? 86   ASN E O   1 
ATOM   5071  C  CB  . ASN E  1 87  ? 38.622  -43.753 19.902 1.00 23.05 ? 86   ASN E CB  1 
ATOM   5072  C  CG  . ASN E  1 87  ? 37.227  -43.205 19.818 1.00 22.96 ? 86   ASN E CG  1 
ATOM   5073  O  OD1 . ASN E  1 87  ? 36.903  -42.194 20.440 1.00 22.07 ? 86   ASN E OD1 1 
ATOM   5074  N  ND2 . ASN E  1 87  ? 36.376  -43.883 19.054 1.00 24.94 ? 86   ASN E ND2 1 
ATOM   5075  N  N   . VAL E  1 88  ? 41.401  -43.181 20.896 1.00 21.82 ? 87   VAL E N   1 
ATOM   5076  C  CA  . VAL E  1 88  ? 42.609  -43.758 21.459 1.00 21.73 ? 87   VAL E CA  1 
ATOM   5077  C  C   . VAL E  1 88  ? 42.060  -44.445 22.701 1.00 22.17 ? 87   VAL E C   1 
ATOM   5078  O  O   . VAL E  1 88  ? 41.047  -44.015 23.260 1.00 21.71 ? 87   VAL E O   1 
ATOM   5079  C  CB  . VAL E  1 88  ? 43.686  -42.701 21.846 1.00 22.35 ? 87   VAL E CB  1 
ATOM   5080  C  CG1 . VAL E  1 88  ? 44.203  -42.026 20.588 1.00 23.58 ? 87   VAL E CG1 1 
ATOM   5081  C  CG2 . VAL E  1 88  ? 43.119  -41.678 22.822 1.00 23.42 ? 87   VAL E CG2 1 
ATOM   5082  N  N   . THR E  1 89  ? 42.717  -45.514 23.124 1.00 22.32 ? 88   THR E N   1 
ATOM   5083  C  CA  . THR E  1 89  ? 42.255  -46.282 24.269 1.00 25.99 ? 88   THR E CA  1 
ATOM   5084  C  C   . THR E  1 89  ? 43.176  -46.181 25.474 1.00 23.96 ? 88   THR E C   1 
ATOM   5085  O  O   . THR E  1 89  ? 44.373  -46.444 25.380 1.00 26.47 ? 88   THR E O   1 
ATOM   5086  C  CB  . THR E  1 89  ? 42.106  -47.771 23.875 1.00 27.85 ? 88   THR E CB  1 
ATOM   5087  O  OG1 . THR E  1 89  ? 41.201  -47.874 22.769 1.00 27.34 ? 88   THR E OG1 1 
ATOM   5088  C  CG2 . THR E  1 89  ? 41.584  -48.594 25.047 1.00 30.29 ? 88   THR E CG2 1 
ATOM   5089  N  N   . ALA E  1 90  ? 42.612  -45.783 26.605 1.00 23.62 ? 89   ALA E N   1 
ATOM   5090  C  CA  . ALA E  1 90  ? 43.388  -45.679 27.830 1.00 27.37 ? 89   ALA E CA  1 
ATOM   5091  C  C   . ALA E  1 90  ? 43.135  -46.952 28.625 1.00 30.48 ? 89   ALA E C   1 
ATOM   5092  O  O   . ALA E  1 90  ? 41.987  -47.379 28.775 1.00 32.37 ? 89   ALA E O   1 
ATOM   5093  C  CB  . ALA E  1 90  ? 42.950  -44.464 28.632 1.00 27.46 ? 89   ALA E CB  1 
ATOM   5094  N  N   . ASP E  1 91  ? 44.203  -47.563 29.123 1.00 32.01 ? 90   ASP E N   1 
ATOM   5095  C  CA  . ASP E  1 91  ? 44.073  -48.790 29.893 1.00 34.39 ? 90   ASP E CA  1 
ATOM   5096  C  C   . ASP E  1 91  ? 43.631  -48.511 31.329 1.00 35.26 ? 90   ASP E C   1 
ATOM   5097  O  O   . ASP E  1 91  ? 43.356  -47.365 31.698 1.00 35.18 ? 90   ASP E O   1 
ATOM   5098  C  CB  . ASP E  1 91  ? 45.396  -49.564 29.868 1.00 35.25 ? 90   ASP E CB  1 
ATOM   5099  C  CG  . ASP E  1 91  ? 46.542  -48.794 30.501 1.00 35.80 ? 90   ASP E CG  1 
ATOM   5100  O  OD1 . ASP E  1 91  ? 47.710  -49.167 30.262 1.00 37.01 ? 90   ASP E OD1 1 
ATOM   5101  O  OD2 . ASP E  1 91  ? 46.282  -47.824 31.243 1.00 37.78 ? 90   ASP E OD2 1 
ATOM   5102  N  N   . LYS E  1 92  ? 43.550  -49.565 32.133 1.00 36.24 ? 91   LYS E N   1 
ATOM   5103  C  CA  . LYS E  1 92  ? 43.130  -49.446 33.527 1.00 37.82 ? 91   LYS E CA  1 
ATOM   5104  C  C   . LYS E  1 92  ? 44.023  -48.498 34.332 1.00 37.31 ? 91   LYS E C   1 
ATOM   5105  O  O   . LYS E  1 92  ? 43.587  -47.921 35.329 1.00 37.37 ? 91   LYS E O   1 
ATOM   5106  C  CB  . LYS E  1 92  ? 43.127  -50.834 34.179 1.00 39.91 ? 91   LYS E CB  1 
ATOM   5107  C  CG  . LYS E  1 92  ? 44.461  -51.562 34.059 1.00 43.59 ? 91   LYS E CG  1 
ATOM   5108  C  CD  . LYS E  1 92  ? 44.375  -53.002 34.553 1.00 46.83 ? 91   LYS E CD  1 
ATOM   5109  C  CE  . LYS E  1 92  ? 45.668  -53.755 34.275 1.00 47.09 ? 91   LYS E CE  1 
ATOM   5110  N  NZ  . LYS E  1 92  ? 45.592  -55.173 34.721 0.00 47.30 ? 91   LYS E NZ  1 
ATOM   5111  N  N   . ASP E  1 93  ? 45.267  -48.338 33.892 1.00 36.56 ? 92   ASP E N   1 
ATOM   5112  C  CA  . ASP E  1 93  ? 46.229  -47.473 34.574 1.00 38.20 ? 92   ASP E CA  1 
ATOM   5113  C  C   . ASP E  1 93  ? 46.130  -45.993 34.193 1.00 36.45 ? 92   ASP E C   1 
ATOM   5114  O  O   . ASP E  1 93  ? 46.913  -45.175 34.675 1.00 36.42 ? 92   ASP E O   1 
ATOM   5115  C  CB  . ASP E  1 93  ? 47.652  -47.971 34.307 1.00 40.89 ? 92   ASP E CB  1 
ATOM   5116  C  CG  . ASP E  1 93  ? 47.994  -49.219 35.102 1.00 47.25 ? 92   ASP E CG  1 
ATOM   5117  O  OD1 . ASP E  1 93  ? 49.001  -49.880 34.766 1.00 51.57 ? 92   ASP E OD1 1 
ATOM   5118  O  OD2 . ASP E  1 93  ? 47.266  -49.534 36.070 1.00 49.09 ? 92   ASP E OD2 1 
ATOM   5119  N  N   . GLY E  1 94  ? 45.179  -45.660 33.326 1.00 34.99 ? 93   GLY E N   1 
ATOM   5120  C  CA  . GLY E  1 94  ? 44.989  -44.281 32.902 1.00 34.06 ? 93   GLY E CA  1 
ATOM   5121  C  C   . GLY E  1 94  ? 45.886  -43.834 31.756 1.00 32.76 ? 93   GLY E C   1 
ATOM   5122  O  O   . GLY E  1 94  ? 45.969  -42.641 31.457 1.00 32.37 ? 93   GLY E O   1 
ATOM   5123  N  N   . VAL E  1 95  ? 46.544  -44.791 31.109 1.00 30.81 ? 94   VAL E N   1 
ATOM   5124  C  CA  . VAL E  1 95  ? 47.460  -44.497 30.016 1.00 29.43 ? 94   VAL E CA  1 
ATOM   5125  C  C   . VAL E  1 95  ? 47.030  -45.037 28.656 1.00 30.42 ? 94   VAL E C   1 
ATOM   5126  O  O   . VAL E  1 95  ? 46.673  -46.208 28.512 1.00 28.81 ? 94   VAL E O   1 
ATOM   5127  C  CB  . VAL E  1 95  ? 48.869  -45.057 30.318 1.00 30.66 ? 94   VAL E CB  1 
ATOM   5128  C  CG1 . VAL E  1 95  ? 49.796  -44.796 29.143 1.00 30.83 ? 94   VAL E CG1 1 
ATOM   5129  C  CG2 . VAL E  1 95  ? 49.425  -44.421 31.594 1.00 30.20 ? 94   VAL E CG2 1 
ATOM   5130  N  N   . ALA E  1 96  ? 47.067  -44.168 27.655 1.00 28.41 ? 95   ALA E N   1 
ATOM   5131  C  CA  . ALA E  1 96  ? 46.725  -44.571 26.304 1.00 29.06 ? 95   ALA E CA  1 
ATOM   5132  C  C   . ALA E  1 96  ? 48.008  -44.530 25.488 1.00 30.28 ? 95   ALA E C   1 
ATOM   5133  O  O   . ALA E  1 96  ? 48.579  -43.453 25.259 1.00 29.82 ? 95   ALA E O   1 
ATOM   5134  C  CB  . ALA E  1 96  ? 45.680  -43.625 25.706 1.00 26.86 ? 95   ALA E CB  1 
ATOM   5135  N  N   . ASP E  1 97  ? 48.488  -45.706 25.092 1.00 30.27 ? 96   ASP E N   1 
ATOM   5136  C  CA  . ASP E  1 97  ? 49.688  -45.799 24.275 1.00 30.92 ? 96   ASP E CA  1 
ATOM   5137  C  C   . ASP E  1 97  ? 49.226  -45.736 22.831 1.00 31.21 ? 96   ASP E C   1 
ATOM   5138  O  O   . ASP E  1 97  ? 48.857  -46.744 22.232 1.00 33.80 ? 96   ASP E O   1 
ATOM   5139  C  CB  . ASP E  1 97  ? 50.424  -47.105 24.542 1.00 33.16 ? 96   ASP E CB  1 
ATOM   5140  C  CG  . ASP E  1 97  ? 51.039  -47.145 25.922 1.00 36.73 ? 96   ASP E CG  1 
ATOM   5141  O  OD1 . ASP E  1 97  ? 50.561  -47.932 26.764 1.00 36.72 ? 96   ASP E OD1 1 
ATOM   5142  O  OD2 . ASP E  1 97  ? 51.995  -46.374 26.165 1.00 37.98 ? 96   ASP E OD2 1 
ATOM   5143  N  N   . VAL E  1 98  ? 49.255  -44.534 22.283 1.00 29.15 ? 97   VAL E N   1 
ATOM   5144  C  CA  . VAL E  1 98  ? 48.806  -44.279 20.927 1.00 27.38 ? 97   VAL E CA  1 
ATOM   5145  C  C   . VAL E  1 98  ? 49.720  -44.808 19.830 1.00 29.09 ? 97   VAL E C   1 
ATOM   5146  O  O   . VAL E  1 98  ? 50.941  -44.666 19.892 1.00 29.60 ? 97   VAL E O   1 
ATOM   5147  C  CB  . VAL E  1 98  ? 48.614  -42.760 20.710 1.00 24.86 ? 97   VAL E CB  1 
ATOM   5148  C  CG1 . VAL E  1 98  ? 47.926  -42.498 19.382 1.00 24.37 ? 97   VAL E CG1 1 
ATOM   5149  C  CG2 . VAL E  1 98  ? 47.811  -42.175 21.856 1.00 24.95 ? 97   VAL E CG2 1 
ATOM   5150  N  N   . SER E  1 99  ? 49.101  -45.418 18.825 1.00 28.73 ? 98   SER E N   1 
ATOM   5151  C  CA  . SER E  1 99  ? 49.796  -45.941 17.658 1.00 31.32 ? 98   SER E CA  1 
ATOM   5152  C  C   . SER E  1 99  ? 48.747  -45.941 16.557 1.00 31.51 ? 98   SER E C   1 
ATOM   5153  O  O   . SER E  1 99  ? 47.844  -46.776 16.542 1.00 33.70 ? 98   SER E O   1 
ATOM   5154  C  CB  . SER E  1 99  ? 50.313  -47.359 17.906 1.00 34.56 ? 98   SER E CB  1 
ATOM   5155  O  OG  . SER E  1 99  ? 51.207  -47.747 16.872 1.00 37.93 ? 98   SER E OG  1 
ATOM   5156  N  N   . ILE E  1 100 ? 48.864  -44.979 15.649 1.00 30.26 ? 99   ILE E N   1 
ATOM   5157  C  CA  . ILE E  1 100 ? 47.918  -44.808 14.554 1.00 29.85 ? 99   ILE E CA  1 
ATOM   5158  C  C   . ILE E  1 100 ? 48.649  -44.452 13.264 1.00 28.51 ? 99   ILE E C   1 
ATOM   5159  O  O   . ILE E  1 100 ? 49.692  -43.801 13.307 1.00 25.71 ? 99   ILE E O   1 
ATOM   5160  C  CB  . ILE E  1 100 ? 46.942  -43.644 14.866 1.00 30.86 ? 99   ILE E CB  1 
ATOM   5161  C  CG1 . ILE E  1 100 ? 46.027  -44.018 16.032 1.00 33.61 ? 99   ILE E CG1 1 
ATOM   5162  C  CG2 . ILE E  1 100 ? 46.138  -43.273 13.625 1.00 33.58 ? 99   ILE E CG2 1 
ATOM   5163  C  CD1 . ILE E  1 100 ? 45.075  -42.900 16.423 1.00 31.03 ? 99   ILE E CD1 1 
ATOM   5164  N  N   . GLU E  1 101 ? 48.098  -44.885 12.130 1.00 27.36 ? 100  GLU E N   1 
ATOM   5165  C  CA  . GLU E  1 101 ? 48.656  -44.559 10.817 1.00 28.17 ? 100  GLU E CA  1 
ATOM   5166  C  C   . GLU E  1 101 ? 47.497  -43.996 10.006 1.00 27.29 ? 100  GLU E C   1 
ATOM   5167  O  O   . GLU E  1 101 ? 46.404  -44.557 10.011 1.00 27.94 ? 100  GLU E O   1 
ATOM   5168  C  CB  . GLU E  1 101 ? 49.236  -45.795 10.116 1.00 31.31 ? 100  GLU E CB  1 
ATOM   5169  C  CG  . GLU E  1 101 ? 50.033  -45.419 8.862  1.00 37.42 ? 100  GLU E CG  1 
ATOM   5170  C  CD  . GLU E  1 101 ? 50.993  -46.505 8.407  1.00 41.22 ? 100  GLU E CD  1 
ATOM   5171  O  OE1 . GLU E  1 101 ? 50.608  -47.330 7.558  1.00 44.64 ? 100  GLU E OE1 1 
ATOM   5172  O  OE2 . GLU E  1 101 ? 52.136  -46.542 8.904  1.00 48.54 ? 100  GLU E OE2 1 
ATOM   5173  N  N   . ASP E  1 102 ? 47.721  -42.884 9.319  1.00 26.93 ? 101  ASP E N   1 
ATOM   5174  C  CA  . ASP E  1 102 ? 46.648  -42.268 8.553  1.00 24.68 ? 101  ASP E CA  1 
ATOM   5175  C  C   . ASP E  1 102 ? 47.155  -41.717 7.227  1.00 26.59 ? 101  ASP E C   1 
ATOM   5176  O  O   . ASP E  1 102 ? 48.249  -41.155 7.159  1.00 25.37 ? 101  ASP E O   1 
ATOM   5177  C  CB  . ASP E  1 102 ? 46.013  -41.154 9.393  1.00 21.80 ? 101  ASP E CB  1 
ATOM   5178  C  CG  . ASP E  1 102 ? 44.695  -40.688 8.842  1.00 22.18 ? 101  ASP E CG  1 
ATOM   5179  O  OD1 . ASP E  1 102 ? 44.667  -39.661 8.129  1.00 22.11 ? 101  ASP E OD1 1 
ATOM   5180  O  OD2 . ASP E  1 102 ? 43.675  -41.356 9.121  1.00 25.20 ? 101  ASP E OD2 1 
ATOM   5181  N  N   . SER E  1 103 ? 46.351  -41.872 6.177  1.00 25.11 ? 102  SER E N   1 
ATOM   5182  C  CA  . SER E  1 103 ? 46.735  -41.404 4.851  1.00 26.96 ? 102  SER E CA  1 
ATOM   5183  C  C   . SER E  1 103 ? 45.974  -40.178 4.398  1.00 25.41 ? 102  SER E C   1 
ATOM   5184  O  O   . SER E  1 103 ? 46.118  -39.741 3.259  1.00 28.66 ? 102  SER E O   1 
ATOM   5185  C  CB  . SER E  1 103 ? 46.538  -42.515 3.819  1.00 30.51 ? 102  SER E CB  1 
ATOM   5186  O  OG  . SER E  1 103 ? 47.529  -43.510 3.968  1.00 37.73 ? 102  SER E OG  1 
ATOM   5187  N  N   . VAL E  1 104 ? 45.155  -39.623 5.278  1.00 23.53 ? 103  VAL E N   1 
ATOM   5188  C  CA  . VAL E  1 104 ? 44.391  -38.442 4.919  1.00 23.78 ? 103  VAL E CA  1 
ATOM   5189  C  C   . VAL E  1 104 ? 45.095  -37.189 5.436  1.00 24.49 ? 103  VAL E C   1 
ATOM   5190  O  O   . VAL E  1 104 ? 45.173  -36.181 4.733  1.00 24.06 ? 103  VAL E O   1 
ATOM   5191  C  CB  . VAL E  1 104 ? 42.963  -38.524 5.478  1.00 23.41 ? 103  VAL E CB  1 
ATOM   5192  C  CG1 . VAL E  1 104 ? 42.188  -37.268 5.108  1.00 22.29 ? 103  VAL E CG1 1 
ATOM   5193  C  CG2 . VAL E  1 104 ? 42.272  -39.770 4.915  1.00 26.10 ? 103  VAL E CG2 1 
ATOM   5194  N  N   . ILE E  1 105 ? 45.604  -37.250 6.663  1.00 22.75 ? 104  ILE E N   1 
ATOM   5195  C  CA  . ILE E  1 105 ? 46.338  -36.113 7.212  1.00 21.47 ? 104  ILE E CA  1 
ATOM   5196  C  C   . ILE E  1 105 ? 47.727  -36.132 6.570  1.00 23.51 ? 104  ILE E C   1 
ATOM   5197  O  O   . ILE E  1 105 ? 48.201  -37.180 6.123  1.00 21.69 ? 104  ILE E O   1 
ATOM   5198  C  CB  . ILE E  1 105 ? 46.529  -36.217 8.751  1.00 20.30 ? 104  ILE E CB  1 
ATOM   5199  C  CG1 . ILE E  1 105 ? 47.219  -37.537 9.103  1.00 19.02 ? 104  ILE E CG1 1 
ATOM   5200  C  CG2 . ILE E  1 105 ? 45.196  -36.077 9.460  1.00 21.45 ? 104  ILE E CG2 1 
ATOM   5201  C  CD1 . ILE E  1 105 ? 47.806  -37.579 10.502 1.00 20.13 ? 104  ILE E CD1 1 
ATOM   5202  N  N   . SER E  1 106 ? 48.376  -34.973 6.523  1.00 23.24 ? 105  SER E N   1 
ATOM   5203  C  CA  . SER E  1 106 ? 49.714  -34.881 5.963  1.00 23.23 ? 105  SER E CA  1 
ATOM   5204  C  C   . SER E  1 106 ? 50.505  -33.863 6.782  1.00 21.50 ? 105  SER E C   1 
ATOM   5205  O  O   . SER E  1 106 ? 49.918  -33.028 7.463  1.00 22.11 ? 105  SER E O   1 
ATOM   5206  C  CB  . SER E  1 106 ? 49.651  -34.437 4.495  1.00 24.74 ? 105  SER E CB  1 
ATOM   5207  O  OG  . SER E  1 106 ? 50.945  -34.447 3.914  1.00 24.76 ? 105  SER E OG  1 
ATOM   5208  N  N   . LEU E  1 107 ? 51.828  -33.941 6.718  1.00 21.13 ? 106  LEU E N   1 
ATOM   5209  C  CA  . LEU E  1 107 ? 52.680  -33.009 7.447  1.00 23.41 ? 106  LEU E CA  1 
ATOM   5210  C  C   . LEU E  1 107 ? 53.222  -31.928 6.523  1.00 26.77 ? 106  LEU E C   1 
ATOM   5211  O  O   . LEU E  1 107 ? 54.155  -31.208 6.872  1.00 27.12 ? 106  LEU E O   1 
ATOM   5212  C  CB  . LEU E  1 107 ? 53.839  -33.753 8.112  1.00 22.39 ? 106  LEU E CB  1 
ATOM   5213  C  CG  . LEU E  1 107 ? 53.425  -34.777 9.174  1.00 21.59 ? 106  LEU E CG  1 
ATOM   5214  C  CD1 . LEU E  1 107 ? 54.671  -35.283 9.882  1.00 22.08 ? 106  LEU E CD1 1 
ATOM   5215  C  CD2 . LEU E  1 107 ? 52.462  -34.139 10.175 1.00 20.88 ? 106  LEU E CD2 1 
ATOM   5216  N  N   . SER E  1 108 ? 52.635  -31.824 5.339  1.00 28.22 ? 107  SER E N   1 
ATOM   5217  C  CA  . SER E  1 108 ? 53.047  -30.815 4.378  1.00 31.54 ? 107  SER E CA  1 
ATOM   5218  C  C   . SER E  1 108 ? 51.995  -30.677 3.305  1.00 33.36 ? 107  SER E C   1 
ATOM   5219  O  O   . SER E  1 108 ? 50.993  -31.391 3.298  1.00 30.40 ? 107  SER E O   1 
ATOM   5220  C  CB  . SER E  1 108 ? 54.386  -31.182 3.726  1.00 32.14 ? 107  SER E CB  1 
ATOM   5221  O  OG  . SER E  1 108 ? 54.293  -32.365 2.949  1.00 32.84 ? 107  SER E OG  1 
ATOM   5222  N  N   . GLY E  1 109 ? 52.230  -29.743 2.398  1.00 36.15 ? 108  GLY E N   1 
ATOM   5223  C  CA  . GLY E  1 109 ? 51.300  -29.538 1.317  1.00 39.73 ? 108  GLY E CA  1 
ATOM   5224  C  C   . GLY E  1 109 ? 50.135  -28.671 1.712  1.00 43.29 ? 108  GLY E C   1 
ATOM   5225  O  O   . GLY E  1 109 ? 49.924  -28.360 2.885  1.00 43.89 ? 108  GLY E O   1 
ATOM   5226  N  N   . ASP E  1 110 ? 49.370  -28.299 0.699  1.00 45.73 ? 109  ASP E N   1 
ATOM   5227  C  CA  . ASP E  1 110 ? 48.203  -27.451 0.836  1.00 48.04 ? 109  ASP E CA  1 
ATOM   5228  C  C   . ASP E  1 110 ? 47.365  -27.686 2.086  1.00 47.02 ? 109  ASP E C   1 
ATOM   5229  O  O   . ASP E  1 110 ? 46.825  -26.740 2.655  1.00 49.08 ? 109  ASP E O   1 
ATOM   5230  C  CB  . ASP E  1 110 ? 47.319  -27.623 -0.400 1.00 50.90 ? 109  ASP E CB  1 
ATOM   5231  C  CG  . ASP E  1 110 ? 46.342  -26.489 -0.577 1.00 52.79 ? 109  ASP E CG  1 
ATOM   5232  O  OD1 . ASP E  1 110 ? 45.431  -26.619 -1.422 1.00 54.98 ? 109  ASP E OD1 1 
ATOM   5233  O  OD2 . ASP E  1 110 ? 46.494  -25.465 0.122  1.00 55.71 ? 109  ASP E OD2 1 
ATOM   5234  N  N   . HIS E  1 111 ? 47.256  -28.937 2.516  1.00 45.90 ? 110  HIS E N   1 
ATOM   5235  C  CA  . HIS E  1 111 ? 46.433  -29.264 3.678  1.00 41.99 ? 110  HIS E CA  1 
ATOM   5236  C  C   . HIS E  1 111 ? 47.145  -29.925 4.864  1.00 38.60 ? 110  HIS E C   1 
ATOM   5237  O  O   . HIS E  1 111 ? 46.612  -30.812 5.523  1.00 37.87 ? 110  HIS E O   1 
ATOM   5238  C  CB  . HIS E  1 111 ? 45.261  -30.126 3.220  1.00 46.74 ? 110  HIS E CB  1 
ATOM   5239  C  CG  . HIS E  1 111 ? 44.346  -29.434 2.253  1.00 50.71 ? 110  HIS E CG  1 
ATOM   5240  N  ND1 . HIS E  1 111 ? 43.451  -30.111 1.464  1.00 52.01 ? 110  HIS E ND1 1 
ATOM   5241  C  CD2 . HIS E  1 111 ? 44.171  -28.113 1.981  1.00 51.15 ? 110  HIS E CD2 1 
ATOM   5242  C  CE1 . HIS E  1 111 ? 42.753  -29.240 0.738  1.00 53.02 ? 110  HIS E CE1 1 
ATOM   5243  N  NE2 . HIS E  1 111 ? 43.178  -28.028 1.041  1.00 51.44 ? 110  HIS E NE2 1 
ATOM   5244  N  N   . SER E  1 112 ? 48.348  -29.460 5.142  1.00 33.42 ? 111  SER E N   1 
ATOM   5245  C  CA  . SER E  1 112 ? 49.152  -29.970 6.247  1.00 27.52 ? 111  SER E CA  1 
ATOM   5246  C  C   . SER E  1 112 ? 48.468  -29.731 7.601  1.00 23.16 ? 111  SER E C   1 
ATOM   5247  O  O   . SER E  1 112 ? 47.620  -28.853 7.722  1.00 23.61 ? 111  SER E O   1 
ATOM   5248  C  CB  . SER E  1 112 ? 50.518  -29.271 6.213  1.00 25.71 ? 111  SER E CB  1 
ATOM   5249  O  OG  . SER E  1 112 ? 51.237  -29.460 7.413  1.00 25.08 ? 111  SER E OG  1 
ATOM   5250  N  N   . ILE E  1 113 ? 48.804  -30.525 8.614  1.00 21.22 ? 112  ILE E N   1 
ATOM   5251  C  CA  . ILE E  1 113 ? 48.227  -30.299 9.940  1.00 19.79 ? 112  ILE E CA  1 
ATOM   5252  C  C   . ILE E  1 113 ? 49.216  -29.508 10.814 1.00 20.33 ? 112  ILE E C   1 
ATOM   5253  O  O   . ILE E  1 113 ? 48.952  -29.231 11.984 1.00 19.29 ? 112  ILE E O   1 
ATOM   5254  C  CB  . ILE E  1 113 ? 47.865  -31.619 10.662 1.00 21.58 ? 112  ILE E CB  1 
ATOM   5255  C  CG1 . ILE E  1 113 ? 49.088  -32.539 10.728 1.00 19.38 ? 112  ILE E CG1 1 
ATOM   5256  C  CG2 . ILE E  1 113 ? 46.681  -32.279 9.965  1.00 23.35 ? 112  ILE E CG2 1 
ATOM   5257  C  CD1 . ILE E  1 113 ? 48.876  -33.782 11.596 1.00 21.15 ? 112  ILE E CD1 1 
ATOM   5258  N  N   . ILE E  1 114 ? 50.361  -29.150 10.237 1.00 20.25 ? 113  ILE E N   1 
ATOM   5259  C  CA  . ILE E  1 114 ? 51.365  -28.372 10.966 1.00 20.98 ? 113  ILE E CA  1 
ATOM   5260  C  C   . ILE E  1 114 ? 50.746  -27.046 11.389 1.00 19.02 ? 113  ILE E C   1 
ATOM   5261  O  O   . ILE E  1 114 ? 50.095  -26.377 10.590 1.00 20.50 ? 113  ILE E O   1 
ATOM   5262  C  CB  . ILE E  1 114 ? 52.592  -28.063 10.085 1.00 20.92 ? 113  ILE E CB  1 
ATOM   5263  C  CG1 . ILE E  1 114 ? 53.269  -29.369 9.651  1.00 21.04 ? 113  ILE E CG1 1 
ATOM   5264  C  CG2 . ILE E  1 114 ? 53.576  -27.167 10.855 1.00 21.41 ? 113  ILE E CG2 1 
ATOM   5265  C  CD1 . ILE E  1 114 ? 53.780  -30.213 10.812 1.00 22.25 ? 113  ILE E CD1 1 
ATOM   5266  N  N   . GLY E  1 115 ? 50.938  -26.671 12.647 1.00 18.03 ? 114  GLY E N   1 
ATOM   5267  C  CA  . GLY E  1 115 ? 50.386  -25.415 13.121 1.00 18.19 ? 114  GLY E CA  1 
ATOM   5268  C  C   . GLY E  1 115 ? 48.938  -25.501 13.554 1.00 18.84 ? 114  GLY E C   1 
ATOM   5269  O  O   . GLY E  1 115 ? 48.331  -24.492 13.922 1.00 17.72 ? 114  GLY E O   1 
ATOM   5270  N  N   . ARG E  1 116 ? 48.367  -26.700 13.498 1.00 19.01 ? 115  ARG E N   1 
ATOM   5271  C  CA  . ARG E  1 116 ? 46.988  -26.882 13.918 1.00 19.31 ? 115  ARG E CA  1 
ATOM   5272  C  C   . ARG E  1 116 ? 47.015  -27.532 15.304 1.00 19.86 ? 115  ARG E C   1 
ATOM   5273  O  O   . ARG E  1 116 ? 48.086  -27.672 15.891 1.00 21.65 ? 115  ARG E O   1 
ATOM   5274  C  CB  . ARG E  1 116 ? 46.228  -27.708 12.868 1.00 19.74 ? 115  ARG E CB  1 
ATOM   5275  C  CG  . ARG E  1 116 ? 46.234  -26.983 11.506 1.00 20.70 ? 115  ARG E CG  1 
ATOM   5276  C  CD  . ARG E  1 116 ? 45.313  -27.593 10.456 1.00 22.50 ? 115  ARG E CD  1 
ATOM   5277  N  NE  . ARG E  1 116 ? 45.470  -26.944 9.150  1.00 22.37 ? 115  ARG E NE  1 
ATOM   5278  C  CZ  . ARG E  1 116 ? 44.930  -25.778 8.804  1.00 23.34 ? 115  ARG E CZ  1 
ATOM   5279  N  NH1 . ARG E  1 116 ? 45.140  -25.284 7.592  1.00 23.71 ? 115  ARG E NH1 1 
ATOM   5280  N  NH2 . ARG E  1 116 ? 44.169  -25.107 9.657  1.00 26.25 ? 115  ARG E NH2 1 
ATOM   5281  N  N   . THR E  1 117 ? 45.866  -27.928 15.836 1.00 20.24 ? 116  THR E N   1 
ATOM   5282  C  CA  . THR E  1 117 ? 45.841  -28.476 17.197 1.00 20.15 ? 116  THR E CA  1 
ATOM   5283  C  C   . THR E  1 117 ? 45.378  -29.914 17.340 1.00 21.26 ? 116  THR E C   1 
ATOM   5284  O  O   . THR E  1 117 ? 44.385  -30.312 16.744 1.00 23.93 ? 116  THR E O   1 
ATOM   5285  C  CB  . THR E  1 117 ? 44.931  -27.611 18.112 1.00 20.35 ? 116  THR E CB  1 
ATOM   5286  O  OG1 . THR E  1 117 ? 45.481  -26.296 18.231 1.00 21.89 ? 116  THR E OG1 1 
ATOM   5287  C  CG2 . THR E  1 117 ? 44.800  -28.226 19.507 1.00 20.59 ? 116  THR E CG2 1 
ATOM   5288  N  N   . LEU E  1 118 ? 46.098  -30.678 18.155 1.00 20.62 ? 117  LEU E N   1 
ATOM   5289  C  CA  . LEU E  1 118 ? 45.741  -32.062 18.434 1.00 19.68 ? 117  LEU E CA  1 
ATOM   5290  C  C   . LEU E  1 118 ? 44.958  -32.004 19.743 1.00 20.53 ? 117  LEU E C   1 
ATOM   5291  O  O   . LEU E  1 118 ? 45.400  -31.375 20.700 1.00 20.08 ? 117  LEU E O   1 
ATOM   5292  C  CB  . LEU E  1 118 ? 46.996  -32.919 18.614 1.00 19.54 ? 117  LEU E CB  1 
ATOM   5293  C  CG  . LEU E  1 118 ? 46.699  -34.399 18.880 1.00 19.70 ? 117  LEU E CG  1 
ATOM   5294  C  CD1 . LEU E  1 118 ? 46.003  -35.007 17.664 1.00 17.39 ? 117  LEU E CD1 1 
ATOM   5295  C  CD2 . LEU E  1 118 ? 47.983  -35.135 19.200 1.00 15.94 ? 117  LEU E CD2 1 
ATOM   5296  N  N   . VAL E  1 119 ? 43.795  -32.648 19.772 1.00 19.81 ? 118  VAL E N   1 
ATOM   5297  C  CA  . VAL E  1 119 ? 42.924  -32.651 20.947 1.00 19.64 ? 118  VAL E CA  1 
ATOM   5298  C  C   . VAL E  1 119 ? 42.500  -34.068 21.351 1.00 20.05 ? 118  VAL E C   1 
ATOM   5299  O  O   . VAL E  1 119 ? 42.173  -34.895 20.489 1.00 19.72 ? 118  VAL E O   1 
ATOM   5300  C  CB  . VAL E  1 119 ? 41.615  -31.838 20.667 1.00 20.80 ? 118  VAL E CB  1 
ATOM   5301  C  CG1 . VAL E  1 119 ? 40.688  -31.883 21.888 1.00 21.41 ? 118  VAL E CG1 1 
ATOM   5302  C  CG2 . VAL E  1 119 ? 41.952  -30.387 20.297 1.00 18.92 ? 118  VAL E CG2 1 
ATOM   5303  N  N   . VAL E  1 120 ? 42.517  -34.346 22.652 1.00 18.78 ? 119  VAL E N   1 
ATOM   5304  C  CA  . VAL E  1 120 ? 42.065  -35.637 23.166 1.00 20.46 ? 119  VAL E CA  1 
ATOM   5305  C  C   . VAL E  1 120 ? 40.827  -35.300 24.007 1.00 22.03 ? 119  VAL E C   1 
ATOM   5306  O  O   . VAL E  1 120 ? 40.868  -34.410 24.862 1.00 21.26 ? 119  VAL E O   1 
ATOM   5307  C  CB  . VAL E  1 120 ? 43.151  -36.346 24.014 1.00 21.11 ? 119  VAL E CB  1 
ATOM   5308  C  CG1 . VAL E  1 120 ? 43.475  -35.539 25.261 1.00 21.47 ? 119  VAL E CG1 1 
ATOM   5309  C  CG2 . VAL E  1 120 ? 42.684  -37.755 24.374 1.00 21.19 ? 119  VAL E CG2 1 
ATOM   5310  N  N   . HIS E  1 121 ? 39.731  -36.012 23.756 1.00 22.12 ? 120  HIS E N   1 
ATOM   5311  C  CA  . HIS E  1 121 ? 38.451  -35.748 24.412 1.00 21.68 ? 120  HIS E CA  1 
ATOM   5312  C  C   . HIS E  1 121 ? 38.030  -36.543 25.644 1.00 21.23 ? 120  HIS E C   1 
ATOM   5313  O  O   . HIS E  1 121 ? 38.587  -37.582 25.987 1.00 22.31 ? 120  HIS E O   1 
ATOM   5314  C  CB  . HIS E  1 121 ? 37.320  -35.851 23.380 1.00 21.43 ? 120  HIS E CB  1 
ATOM   5315  C  CG  . HIS E  1 121 ? 37.387  -34.823 22.297 1.00 20.18 ? 120  HIS E CG  1 
ATOM   5316  N  ND1 . HIS E  1 121 ? 36.580  -33.705 22.282 1.00 21.24 ? 120  HIS E ND1 1 
ATOM   5317  C  CD2 . HIS E  1 121 ? 38.158  -34.745 21.188 1.00 20.84 ? 120  HIS E CD2 1 
ATOM   5318  C  CE1 . HIS E  1 121 ? 36.850  -32.985 21.210 1.00 19.23 ? 120  HIS E CE1 1 
ATOM   5319  N  NE2 . HIS E  1 121 ? 37.805  -33.592 20.529 1.00 21.84 ? 120  HIS E NE2 1 
ATOM   5320  N  N   . GLU E  1 122 ? 37.005  -36.009 26.291 1.00 23.91 ? 121  GLU E N   1 
ATOM   5321  C  CA  . GLU E  1 122 ? 36.410  -36.572 27.492 1.00 26.00 ? 121  GLU E CA  1 
ATOM   5322  C  C   . GLU E  1 122 ? 35.770  -37.935 27.223 1.00 26.39 ? 121  GLU E C   1 
ATOM   5323  O  O   . GLU E  1 122 ? 35.980  -38.892 27.970 1.00 27.35 ? 121  GLU E O   1 
ATOM   5324  C  CB  . GLU E  1 122 ? 35.339  -35.608 28.001 1.00 28.97 ? 121  GLU E CB  1 
ATOM   5325  C  CG  . GLU E  1 122 ? 34.549  -36.091 29.205 1.00 35.10 ? 121  GLU E CG  1 
ATOM   5326  C  CD  . GLU E  1 122 ? 33.250  -35.317 29.391 1.00 39.28 ? 121  GLU E CD  1 
ATOM   5327  O  OE1 . GLU E  1 122 ? 32.554  -35.569 30.394 1.00 41.17 ? 121  GLU E OE1 1 
ATOM   5328  O  OE2 . GLU E  1 122 ? 32.917  -34.465 28.534 1.00 39.85 ? 121  GLU E OE2 1 
ATOM   5329  N  N   . LYS E  1 123 ? 35.005  -38.014 26.139 1.00 25.70 ? 122  LYS E N   1 
ATOM   5330  C  CA  . LYS E  1 123 ? 34.293  -39.235 25.786 1.00 27.68 ? 122  LYS E CA  1 
ATOM   5331  C  C   . LYS E  1 123 ? 34.727  -39.863 24.469 1.00 26.75 ? 122  LYS E C   1 
ATOM   5332  O  O   . LYS E  1 123 ? 35.571  -39.334 23.749 1.00 25.94 ? 122  LYS E O   1 
ATOM   5333  C  CB  . LYS E  1 123 ? 32.791  -38.949 25.712 1.00 28.50 ? 122  LYS E CB  1 
ATOM   5334  C  CG  . LYS E  1 123 ? 32.210  -38.305 26.961 1.00 34.03 ? 122  LYS E CG  1 
ATOM   5335  C  CD  . LYS E  1 123 ? 30.714  -38.083 26.815 1.00 38.32 ? 122  LYS E CD  1 
ATOM   5336  C  CE  . LYS E  1 123 ? 30.405  -37.111 25.686 1.00 41.23 ? 122  LYS E CE  1 
ATOM   5337  N  NZ  . LYS E  1 123 ? 28.948  -37.038 25.387 1.00 43.36 ? 122  LYS E NZ  1 
ATOM   5338  N  N   . ALA E  1 124 ? 34.120  -41.001 24.162 1.00 24.52 ? 123  ALA E N   1 
ATOM   5339  C  CA  . ALA E  1 124 ? 34.410  -41.715 22.934 1.00 23.40 ? 123  ALA E CA  1 
ATOM   5340  C  C   . ALA E  1 124 ? 33.805  -40.984 21.749 1.00 21.67 ? 123  ALA E C   1 
ATOM   5341  O  O   . ALA E  1 124 ? 32.778  -40.313 21.873 1.00 21.01 ? 123  ALA E O   1 
ATOM   5342  C  CB  . ALA E  1 124 ? 33.849  -43.134 23.012 1.00 25.66 ? 123  ALA E CB  1 
ATOM   5343  N  N   . ASP E  1 125 ? 34.472  -41.099 20.606 1.00 20.65 ? 124  ASP E N   1 
ATOM   5344  C  CA  . ASP E  1 125 ? 34.014  -40.510 19.351 1.00 22.24 ? 124  ASP E CA  1 
ATOM   5345  C  C   . ASP E  1 125 ? 33.120  -41.616 18.757 1.00 22.23 ? 124  ASP E C   1 
ATOM   5346  O  O   . ASP E  1 125 ? 33.571  -42.747 18.609 1.00 20.29 ? 124  ASP E O   1 
ATOM   5347  C  CB  . ASP E  1 125 ? 35.236  -40.245 18.458 1.00 23.05 ? 124  ASP E CB  1 
ATOM   5348  C  CG  . ASP E  1 125 ? 34.881  -39.627 17.118 1.00 25.60 ? 124  ASP E CG  1 
ATOM   5349  O  OD1 . ASP E  1 125 ? 35.787  -39.018 16.501 1.00 22.67 ? 124  ASP E OD1 1 
ATOM   5350  O  OD2 . ASP E  1 125 ? 33.723  -39.755 16.669 1.00 22.76 ? 124  ASP E OD2 1 
ATOM   5351  N  N   . ASP E  1 126 ? 31.862  -41.303 18.444 1.00 23.30 ? 125  ASP E N   1 
ATOM   5352  C  CA  . ASP E  1 126 ? 30.955  -42.317 17.896 1.00 25.06 ? 125  ASP E CA  1 
ATOM   5353  C  C   . ASP E  1 126 ? 31.113  -42.511 16.386 1.00 25.18 ? 125  ASP E C   1 
ATOM   5354  O  O   . ASP E  1 126 ? 30.351  -43.246 15.745 1.00 24.77 ? 125  ASP E O   1 
ATOM   5355  C  CB  . ASP E  1 126 ? 29.492  -42.000 18.274 1.00 22.54 ? 125  ASP E CB  1 
ATOM   5356  C  CG  . ASP E  1 126 ? 28.949  -40.739 17.612 1.00 25.41 ? 125  ASP E CG  1 
ATOM   5357  O  OD1 . ASP E  1 126 ? 27.921  -40.241 18.106 1.00 25.79 ? 125  ASP E OD1 1 
ATOM   5358  O  OD2 . ASP E  1 126 ? 29.510  -40.252 16.604 1.00 25.23 ? 125  ASP E OD2 1 
ATOM   5359  N  N   . LEU E  1 127 ? 32.126  -41.849 15.836 1.00 21.69 ? 126  LEU E N   1 
ATOM   5360  C  CA  . LEU E  1 127 ? 32.467  -41.931 14.423 1.00 21.94 ? 126  LEU E CA  1 
ATOM   5361  C  C   . LEU E  1 127 ? 31.345  -41.555 13.464 1.00 22.05 ? 126  LEU E C   1 
ATOM   5362  O  O   . LEU E  1 127 ? 31.304  -42.045 12.338 1.00 22.35 ? 126  LEU E O   1 
ATOM   5363  C  CB  . LEU E  1 127 ? 32.973  -43.341 14.094 1.00 23.10 ? 126  LEU E CB  1 
ATOM   5364  C  CG  . LEU E  1 127 ? 33.916  -43.955 15.130 1.00 25.44 ? 126  LEU E CG  1 
ATOM   5365  C  CD1 . LEU E  1 127 ? 34.261  -45.387 14.732 1.00 26.71 ? 126  LEU E CD1 1 
ATOM   5366  C  CD2 . LEU E  1 127 ? 35.184  -43.105 15.251 1.00 26.93 ? 126  LEU E CD2 1 
ATOM   5367  N  N   . GLY E  1 128 ? 30.451  -40.674 13.904 1.00 21.72 ? 127  GLY E N   1 
ATOM   5368  C  CA  . GLY E  1 128 ? 29.350  -40.238 13.061 1.00 22.90 ? 127  GLY E CA  1 
ATOM   5369  C  C   . GLY E  1 128 ? 28.152  -41.179 13.003 1.00 24.62 ? 127  GLY E C   1 
ATOM   5370  O  O   . GLY E  1 128 ? 27.256  -40.994 12.183 1.00 23.84 ? 127  GLY E O   1 
ATOM   5371  N  N   . LYS E  1 129 ? 28.121  -42.177 13.877 1.00 24.44 ? 128  LYS E N   1 
ATOM   5372  C  CA  . LYS E  1 129 ? 27.015  -43.138 13.880 1.00 28.07 ? 128  LYS E CA  1 
ATOM   5373  C  C   . LYS E  1 129 ? 26.076  -42.949 15.066 1.00 26.76 ? 128  LYS E C   1 
ATOM   5374  O  O   . LYS E  1 129 ? 25.320  -43.856 15.412 1.00 26.98 ? 128  LYS E O   1 
ATOM   5375  C  CB  . LYS E  1 129 ? 27.576  -44.565 13.882 1.00 26.51 ? 128  LYS E CB  1 
ATOM   5376  C  CG  . LYS E  1 129 ? 28.436  -44.873 12.663 1.00 29.74 ? 128  LYS E CG  1 
ATOM   5377  C  CD  . LYS E  1 129 ? 29.296  -46.108 12.870 1.00 34.53 ? 128  LYS E CD  1 
ATOM   5378  C  CE  . LYS E  1 129 ? 28.456  -47.355 13.108 1.00 37.26 ? 128  LYS E CE  1 
ATOM   5379  N  NZ  . LYS E  1 129 ? 29.319  -48.546 13.386 1.00 40.24 ? 128  LYS E NZ  1 
ATOM   5380  N  N   . GLY E  1 130 ? 26.118  -41.764 15.672 1.00 26.88 ? 129  GLY E N   1 
ATOM   5381  C  CA  . GLY E  1 130 ? 25.279  -41.468 16.824 1.00 28.18 ? 129  GLY E CA  1 
ATOM   5382  C  C   . GLY E  1 130 ? 23.819  -41.133 16.544 1.00 29.27 ? 129  GLY E C   1 
ATOM   5383  O  O   . GLY E  1 130 ? 23.011  -41.052 17.468 1.00 29.14 ? 129  GLY E O   1 
ATOM   5384  N  N   . GLY E  1 131 ? 23.476  -40.915 15.282 1.00 29.54 ? 130  GLY E N   1 
ATOM   5385  C  CA  . GLY E  1 131 ? 22.096  -40.614 14.945 1.00 31.48 ? 130  GLY E CA  1 
ATOM   5386  C  C   . GLY E  1 131 ? 21.638  -39.177 15.146 1.00 34.72 ? 130  GLY E C   1 
ATOM   5387  O  O   . GLY E  1 131 ? 20.435  -38.910 15.200 1.00 33.65 ? 130  GLY E O   1 
ATOM   5388  N  N   . ASN E  1 132 ? 22.573  -38.243 15.276 1.00 36.19 ? 131  ASN E N   1 
ATOM   5389  C  CA  . ASN E  1 132 ? 22.173  -36.854 15.430 1.00 38.36 ? 131  ASN E CA  1 
ATOM   5390  C  C   . ASN E  1 132 ? 23.127  -35.829 14.851 1.00 38.47 ? 131  ASN E C   1 
ATOM   5391  O  O   . ASN E  1 132 ? 24.165  -36.154 14.278 1.00 36.70 ? 131  ASN E O   1 
ATOM   5392  C  CB  . ASN E  1 132 ? 21.904  -36.512 16.893 1.00 37.93 ? 131  ASN E CB  1 
ATOM   5393  C  CG  . ASN E  1 132 ? 23.124  -36.659 17.759 1.00 40.74 ? 131  ASN E CG  1 
ATOM   5394  O  OD1 . ASN E  1 132 ? 24.263  -36.587 17.284 1.00 40.35 ? 131  ASN E OD1 1 
ATOM   5395  N  ND2 . ASN E  1 132 ? 22.898  -36.849 19.048 1.00 41.22 ? 131  ASN E ND2 1 
ATOM   5396  N  N   . GLU E  1 133 ? 22.730  -34.578 14.999 1.00 39.59 ? 132  GLU E N   1 
ATOM   5397  C  CA  . GLU E  1 133 ? 23.493  -33.447 14.498 1.00 41.07 ? 132  GLU E CA  1 
ATOM   5398  C  C   . GLU E  1 133 ? 24.923  -33.407 15.059 1.00 36.65 ? 132  GLU E C   1 
ATOM   5399  O  O   . GLU E  1 133 ? 25.888  -33.357 14.309 1.00 37.27 ? 132  GLU E O   1 
ATOM   5400  C  CB  . GLU E  1 133 ? 22.760  -32.158 14.854 1.00 45.06 ? 132  GLU E CB  1 
ATOM   5401  C  CG  . GLU E  1 133 ? 23.034  -31.004 13.901 1.00 51.63 ? 132  GLU E CG  1 
ATOM   5402  C  CD  . GLU E  1 133 ? 22.124  -30.991 12.676 1.00 55.38 ? 132  GLU E CD  1 
ATOM   5403  O  OE1 . GLU E  1 133 ? 22.510  -31.548 11.620 1.00 57.95 ? 132  GLU E OE1 1 
ATOM   5404  O  OE2 . GLU E  1 133 ? 21.018  -30.411 12.775 1.00 55.33 ? 132  GLU E OE2 1 
ATOM   5405  N  N   . GLU E  1 134 ? 25.051  -33.462 16.380 1.00 36.02 ? 133  GLU E N   1 
ATOM   5406  C  CA  . GLU E  1 134 ? 26.354  -33.423 17.038 1.00 33.96 ? 133  GLU E CA  1 
ATOM   5407  C  C   . GLU E  1 134 ? 27.243  -34.575 16.564 1.00 32.54 ? 133  GLU E C   1 
ATOM   5408  O  O   . GLU E  1 134 ? 28.456  -34.417 16.432 1.00 30.61 ? 133  GLU E O   1 
ATOM   5409  C  CB  . GLU E  1 134 ? 26.158  -33.481 18.557 1.00 35.58 ? 133  GLU E CB  1 
ATOM   5410  C  CG  . GLU E  1 134 ? 27.380  -33.106 19.360 1.00 40.94 ? 133  GLU E CG  1 
ATOM   5411  C  CD  . GLU E  1 134 ? 27.793  -31.658 19.164 1.00 43.78 ? 133  GLU E CD  1 
ATOM   5412  O  OE1 . GLU E  1 134 ? 28.823  -31.267 19.742 1.00 48.20 ? 133  GLU E OE1 1 
ATOM   5413  O  OE2 . GLU E  1 134 ? 27.097  -30.912 18.442 1.00 45.14 ? 133  GLU E OE2 1 
ATOM   5414  N  N   . SER E  1 135 ? 26.635  -35.721 16.270 1.00 28.61 ? 134  SER E N   1 
ATOM   5415  C  CA  . SER E  1 135 ? 27.396  -36.885 15.816 1.00 26.79 ? 134  SER E CA  1 
ATOM   5416  C  C   . SER E  1 135 ? 28.153  -36.649 14.511 1.00 26.38 ? 134  SER E C   1 
ATOM   5417  O  O   . SER E  1 135 ? 29.279  -37.119 14.347 1.00 26.27 ? 134  SER E O   1 
ATOM   5418  C  CB  . SER E  1 135 ? 26.472  -38.089 15.638 1.00 29.02 ? 134  SER E CB  1 
ATOM   5419  O  OG  . SER E  1 135 ? 27.175  -39.203 15.121 1.00 26.75 ? 134  SER E OG  1 
ATOM   5420  N  N   . THR E  1 136 ? 27.524  -35.933 13.586 1.00 27.55 ? 135  THR E N   1 
ATOM   5421  C  CA  . THR E  1 136 ? 28.130  -35.636 12.293 1.00 30.69 ? 135  THR E CA  1 
ATOM   5422  C  C   . THR E  1 136 ? 29.032  -34.405 12.342 1.00 29.54 ? 135  THR E C   1 
ATOM   5423  O  O   . THR E  1 136 ? 29.485  -33.923 11.306 1.00 28.07 ? 135  THR E O   1 
ATOM   5424  C  CB  . THR E  1 136 ? 27.056  -35.377 11.238 1.00 34.76 ? 135  THR E CB  1 
ATOM   5425  O  OG1 . THR E  1 136 ? 26.458  -34.092 11.467 1.00 40.59 ? 135  THR E OG1 1 
ATOM   5426  C  CG2 . THR E  1 136 ? 25.994  -36.427 11.324 1.00 37.56 ? 135  THR E CG2 1 
ATOM   5427  N  N   . LYS E  1 137 ? 29.279  -33.908 13.547 1.00 29.37 ? 136  LYS E N   1 
ATOM   5428  C  CA  . LYS E  1 137 ? 30.118  -32.735 13.740 1.00 31.57 ? 136  LYS E CA  1 
ATOM   5429  C  C   . LYS E  1 137 ? 31.315  -33.073 14.611 1.00 28.70 ? 136  LYS E C   1 
ATOM   5430  O  O   . LYS E  1 137 ? 32.456  -32.907 14.197 1.00 27.64 ? 136  LYS E O   1 
ATOM   5431  C  CB  . LYS E  1 137 ? 29.305  -31.615 14.392 1.00 34.65 ? 136  LYS E CB  1 
ATOM   5432  C  CG  . LYS E  1 137 ? 28.229  -31.047 13.489 1.00 39.81 ? 136  LYS E CG  1 
ATOM   5433  C  CD  . LYS E  1 137 ? 27.470  -29.929 14.187 1.00 45.27 ? 136  LYS E CD  1 
ATOM   5434  C  CE  . LYS E  1 137 ? 26.417  -29.315 13.282 0.00 46.43 ? 136  LYS E CE  1 
ATOM   5435  N  NZ  . LYS E  1 137 ? 25.680  -28.218 13.967 1.00 52.87 ? 136  LYS E NZ  1 
ATOM   5436  N  N   . THR E  1 138 ? 31.045  -33.584 15.806 1.00 26.76 ? 137  THR E N   1 
ATOM   5437  C  CA  . THR E  1 138 ? 32.096  -33.917 16.755 1.00 26.11 ? 137  THR E CA  1 
ATOM   5438  C  C   . THR E  1 138 ? 32.159  -35.377 17.166 1.00 25.35 ? 137  THR E C   1 
ATOM   5439  O  O   . THR E  1 138 ? 33.072  -35.773 17.881 1.00 25.06 ? 137  THR E O   1 
ATOM   5440  C  CB  . THR E  1 138 ? 31.923  -33.114 18.040 1.00 28.65 ? 137  THR E CB  1 
ATOM   5441  O  OG1 . THR E  1 138 ? 30.688  -33.500 18.664 1.00 30.90 ? 137  THR E OG1 1 
ATOM   5442  C  CG2 . THR E  1 138 ? 31.892  -31.612 17.737 1.00 28.53 ? 137  THR E CG2 1 
ATOM   5443  N  N   . GLY E  1 139 ? 31.187  -36.177 16.739 1.00 24.86 ? 138  GLY E N   1 
ATOM   5444  C  CA  . GLY E  1 139 ? 31.184  -37.575 17.125 1.00 21.07 ? 138  GLY E CA  1 
ATOM   5445  C  C   . GLY E  1 139 ? 30.775  -37.725 18.580 1.00 23.03 ? 138  GLY E C   1 
ATOM   5446  O  O   . GLY E  1 139 ? 30.946  -38.791 19.176 1.00 21.09 ? 138  GLY E O   1 
ATOM   5447  N  N   . ASN E  1 140 ? 30.225  -36.652 19.150 1.00 24.00 ? 139  ASN E N   1 
ATOM   5448  C  CA  . ASN E  1 140 ? 29.788  -36.641 20.549 1.00 25.85 ? 139  ASN E CA  1 
ATOM   5449  C  C   . ASN E  1 140 ? 30.934  -36.952 21.521 1.00 25.71 ? 139  ASN E C   1 
ATOM   5450  O  O   . ASN E  1 140 ? 30.706  -37.505 22.596 1.00 25.79 ? 139  ASN E O   1 
ATOM   5451  C  CB  . ASN E  1 140 ? 28.645  -37.651 20.759 1.00 26.96 ? 139  ASN E CB  1 
ATOM   5452  C  CG  . ASN E  1 140 ? 27.324  -37.173 20.173 1.00 29.74 ? 139  ASN E CG  1 
ATOM   5453  O  OD1 . ASN E  1 140 ? 26.758  -36.179 20.626 1.00 28.56 ? 139  ASN E OD1 1 
ATOM   5454  N  ND2 . ASN E  1 140 ? 26.828  -37.879 19.160 1.00 26.75 ? 139  ASN E ND2 1 
ATOM   5455  N  N   . ALA E  1 141 ? 32.159  -36.583 21.148 1.00 23.95 ? 140  ALA E N   1 
ATOM   5456  C  CA  . ALA E  1 141 ? 33.337  -36.846 21.983 1.00 24.05 ? 140  ALA E CA  1 
ATOM   5457  C  C   . ALA E  1 141 ? 33.403  -36.009 23.265 1.00 23.08 ? 140  ALA E C   1 
ATOM   5458  O  O   . ALA E  1 141 ? 34.246  -36.248 24.128 1.00 23.99 ? 140  ALA E O   1 
ATOM   5459  C  CB  . ALA E  1 141 ? 34.617  -36.642 21.163 1.00 24.65 ? 140  ALA E CB  1 
ATOM   5460  N  N   . GLY E  1 142 ? 32.526  -35.023 23.388 1.00 24.79 ? 141  GLY E N   1 
ATOM   5461  C  CA  . GLY E  1 142 ? 32.514  -34.219 24.597 1.00 26.45 ? 141  GLY E CA  1 
ATOM   5462  C  C   . GLY E  1 142 ? 33.582  -33.143 24.703 1.00 26.62 ? 141  GLY E C   1 
ATOM   5463  O  O   . GLY E  1 142 ? 34.134  -32.692 23.703 1.00 26.62 ? 141  GLY E O   1 
ATOM   5464  N  N   . SER E  1 143 ? 33.880  -32.742 25.934 1.00 27.43 ? 142  SER E N   1 
ATOM   5465  C  CA  . SER E  1 143 ? 34.851  -31.683 26.187 1.00 28.22 ? 142  SER E CA  1 
ATOM   5466  C  C   . SER E  1 143 ? 36.294  -32.036 25.830 1.00 27.29 ? 142  SER E C   1 
ATOM   5467  O  O   . SER E  1 143 ? 36.669  -33.208 25.699 1.00 24.30 ? 142  SER E O   1 
ATOM   5468  C  CB  . SER E  1 143 ? 34.780  -31.249 27.655 1.00 27.94 ? 142  SER E CB  1 
ATOM   5469  O  OG  . SER E  1 143 ? 35.227  -32.291 28.497 1.00 32.95 ? 142  SER E OG  1 
ATOM   5470  N  N   . ARG E  1 144 ? 37.102  -30.993 25.686 1.00 26.29 ? 143  ARG E N   1 
ATOM   5471  C  CA  . ARG E  1 144 ? 38.503  -31.142 25.332 1.00 24.23 ? 143  ARG E CA  1 
ATOM   5472  C  C   . ARG E  1 144 ? 39.336  -31.200 26.610 1.00 23.14 ? 143  ARG E C   1 
ATOM   5473  O  O   . ARG E  1 144 ? 39.506  -30.193 27.295 1.00 22.56 ? 143  ARG E O   1 
ATOM   5474  C  CB  . ARG E  1 144 ? 38.901  -29.959 24.445 1.00 25.13 ? 143  ARG E CB  1 
ATOM   5475  C  CG  . ARG E  1 144 ? 37.907  -29.771 23.298 1.00 24.35 ? 143  ARG E CG  1 
ATOM   5476  C  CD  . ARG E  1 144 ? 38.109  -28.511 22.460 1.00 24.78 ? 143  ARG E CD  1 
ATOM   5477  N  NE  . ARG E  1 144 ? 37.036  -28.412 21.468 1.00 23.31 ? 143  ARG E NE  1 
ATOM   5478  C  CZ  . ARG E  1 144 ? 37.014  -27.577 20.435 1.00 23.07 ? 143  ARG E CZ  1 
ATOM   5479  N  NH1 . ARG E  1 144 ? 35.980  -27.594 19.603 1.00 21.43 ? 143  ARG E NH1 1 
ATOM   5480  N  NH2 . ARG E  1 144 ? 38.013  -26.726 20.227 1.00 22.47 ? 143  ARG E NH2 1 
ATOM   5481  N  N   . LEU E  1 145 ? 39.850  -32.386 26.922 1.00 20.74 ? 144  LEU E N   1 
ATOM   5482  C  CA  . LEU E  1 145 ? 40.642  -32.601 28.131 1.00 21.43 ? 144  LEU E CA  1 
ATOM   5483  C  C   . LEU E  1 145 ? 42.056  -32.050 28.065 1.00 21.32 ? 144  LEU E C   1 
ATOM   5484  O  O   . LEU E  1 145 ? 42.597  -31.591 29.071 1.00 21.61 ? 144  LEU E O   1 
ATOM   5485  C  CB  . LEU E  1 145 ? 40.713  -34.089 28.451 1.00 22.81 ? 144  LEU E CB  1 
ATOM   5486  C  CG  . LEU E  1 145 ? 39.371  -34.813 28.600 1.00 24.68 ? 144  LEU E CG  1 
ATOM   5487  C  CD1 . LEU E  1 145 ? 39.627  -36.252 28.996 1.00 24.22 ? 144  LEU E CD1 1 
ATOM   5488  C  CD2 . LEU E  1 145 ? 38.516  -34.116 29.645 1.00 27.56 ? 144  LEU E CD2 1 
ATOM   5489  N  N   . ALA E  1 146 ? 42.661  -32.119 26.886 1.00 19.75 ? 145  ALA E N   1 
ATOM   5490  C  CA  . ALA E  1 146 ? 44.018  -31.619 26.701 1.00 19.11 ? 145  ALA E CA  1 
ATOM   5491  C  C   . ALA E  1 146 ? 44.258  -31.404 25.216 1.00 20.49 ? 145  ALA E C   1 
ATOM   5492  O  O   . ALA E  1 146 ? 43.643  -32.067 24.376 1.00 20.12 ? 145  ALA E O   1 
ATOM   5493  C  CB  . ALA E  1 146 ? 45.028  -32.613 27.259 1.00 16.52 ? 145  ALA E CB  1 
ATOM   5494  N  N   . CYS E  1 147 ? 45.145  -30.471 24.892 1.00 19.43 ? 146  CYS E N   1 
ATOM   5495  C  CA  . CYS E  1 147 ? 45.446  -30.185 23.499 1.00 19.94 ? 146  CYS E CA  1 
ATOM   5496  C  C   . CYS E  1 147 ? 46.839  -29.597 23.360 1.00 18.88 ? 146  CYS E C   1 
ATOM   5497  O  O   . CYS E  1 147 ? 47.479  -29.252 24.349 1.00 18.23 ? 146  CYS E O   1 
ATOM   5498  C  CB  . CYS E  1 147 ? 44.410  -29.214 22.935 1.00 21.26 ? 146  CYS E CB  1 
ATOM   5499  S  SG  . CYS E  1 147 ? 44.316  -27.657 23.867 1.00 24.42 ? 146  CYS E SG  1 
ATOM   5500  N  N   . GLY E  1 148 ? 47.312  -29.505 22.127 1.00 19.05 ? 147  GLY E N   1 
ATOM   5501  C  CA  . GLY E  1 148 ? 48.627  -28.947 21.887 1.00 21.32 ? 147  GLY E CA  1 
ATOM   5502  C  C   . GLY E  1 148 ? 48.795  -28.615 20.421 1.00 21.66 ? 147  GLY E C   1 
ATOM   5503  O  O   . GLY E  1 148 ? 48.232  -29.295 19.553 1.00 17.54 ? 147  GLY E O   1 
ATOM   5504  N  N   . VAL E  1 149 ? 49.558  -27.565 20.136 1.00 20.25 ? 148  VAL E N   1 
ATOM   5505  C  CA  . VAL E  1 149 ? 49.800  -27.180 18.752 1.00 18.89 ? 148  VAL E CA  1 
ATOM   5506  C  C   . VAL E  1 149 ? 50.770  -28.185 18.150 1.00 18.56 ? 148  VAL E C   1 
ATOM   5507  O  O   . VAL E  1 149 ? 51.728  -28.605 18.797 1.00 20.33 ? 148  VAL E O   1 
ATOM   5508  C  CB  . VAL E  1 149 ? 50.419  -25.767 18.652 1.00 21.16 ? 148  VAL E CB  1 
ATOM   5509  C  CG1 . VAL E  1 149 ? 50.557  -25.363 17.185 1.00 15.57 ? 148  VAL E CG1 1 
ATOM   5510  C  CG2 . VAL E  1 149 ? 49.542  -24.762 19.400 1.00 20.64 ? 148  VAL E CG2 1 
ATOM   5511  N  N   . ILE E  1 150 ? 50.517  -28.578 16.909 1.00 19.96 ? 149  ILE E N   1 
ATOM   5512  C  CA  . ILE E  1 150 ? 51.373  -29.534 16.227 1.00 18.74 ? 149  ILE E CA  1 
ATOM   5513  C  C   . ILE E  1 150 ? 52.546  -28.773 15.620 1.00 19.20 ? 149  ILE E C   1 
ATOM   5514  O  O   . ILE E  1 150 ? 52.372  -28.000 14.680 1.00 19.76 ? 149  ILE E O   1 
ATOM   5515  C  CB  . ILE E  1 150 ? 50.575  -30.263 15.134 1.00 19.65 ? 149  ILE E CB  1 
ATOM   5516  C  CG1 . ILE E  1 150 ? 49.386  -30.985 15.785 1.00 20.65 ? 149  ILE E CG1 1 
ATOM   5517  C  CG2 . ILE E  1 150 ? 51.471  -31.257 14.398 1.00 20.71 ? 149  ILE E CG2 1 
ATOM   5518  C  CD1 . ILE E  1 150 ? 48.258  -31.305 14.828 1.00 20.40 ? 149  ILE E CD1 1 
ATOM   5519  N  N   . GLY E  1 151 ? 53.739  -28.988 16.165 1.00 18.50 ? 150  GLY E N   1 
ATOM   5520  C  CA  . GLY E  1 151 ? 54.901  -28.279 15.663 1.00 18.51 ? 150  GLY E CA  1 
ATOM   5521  C  C   . GLY E  1 151 ? 55.926  -29.127 14.944 1.00 19.89 ? 150  GLY E C   1 
ATOM   5522  O  O   . GLY E  1 151 ? 56.001  -30.347 15.132 1.00 19.84 ? 150  GLY E O   1 
ATOM   5523  N  N   . ILE E  1 152 ? 56.727  -28.466 14.117 1.00 19.43 ? 151  ILE E N   1 
ATOM   5524  C  CA  . ILE E  1 152 ? 57.780  -29.126 13.353 1.00 19.63 ? 151  ILE E CA  1 
ATOM   5525  C  C   . ILE E  1 152 ? 58.799  -29.682 14.340 1.00 21.34 ? 151  ILE E C   1 
ATOM   5526  O  O   . ILE E  1 152 ? 59.191  -28.997 15.287 1.00 22.85 ? 151  ILE E O   1 
ATOM   5527  C  CB  . ILE E  1 152 ? 58.460  -28.117 12.390 1.00 20.29 ? 151  ILE E CB  1 
ATOM   5528  C  CG1 . ILE E  1 152 ? 57.431  -27.611 11.377 1.00 23.02 ? 151  ILE E CG1 1 
ATOM   5529  C  CG2 . ILE E  1 152 ? 59.656  -28.759 11.693 1.00 22.51 ? 151  ILE E CG2 1 
ATOM   5530  C  CD1 . ILE E  1 152 ? 57.909  -26.449 10.517 1.00 22.65 ? 151  ILE E CD1 1 
ATOM   5531  N  N   . ALA E  1 153 ? 59.215  -30.928 14.134 1.00 21.28 ? 152  ALA E N   1 
ATOM   5532  C  CA  . ALA E  1 153 ? 60.193  -31.553 15.019 1.00 22.08 ? 152  ALA E CA  1 
ATOM   5533  C  C   . ALA E  1 153 ? 61.464  -31.924 14.259 1.00 24.20 ? 152  ALA E C   1 
ATOM   5534  O  O   . ALA E  1 153 ? 61.465  -32.008 13.031 1.00 24.79 ? 152  ALA E O   1 
ATOM   5535  C  CB  . ALA E  1 153 ? 59.598  -32.792 15.677 1.00 24.37 ? 152  ALA E CB  1 
ATOM   5536  N  N   . GLN E  1 154 ? 62.540  -32.146 15.005 1.00 26.75 ? 153  GLN E N   1 
ATOM   5537  C  CA  . GLN E  1 154 ? 63.832  -32.490 14.425 1.00 31.16 ? 153  GLN E CA  1 
ATOM   5538  C  C   . GLN E  1 154 ? 63.830  -33.926 13.904 1.00 32.82 ? 153  GLN E C   1 
ATOM   5539  O  O   . GLN E  1 154 ? 64.218  -34.130 12.733 1.00 33.23 ? 153  GLN E O   1 
ATOM   5540  C  CB  . GLN E  1 154 ? 64.934  -32.323 15.475 1.00 32.59 ? 153  GLN E CB  1 
ATOM   5541  C  CG  . GLN E  1 154 ? 66.332  -32.218 14.890 1.00 38.51 ? 153  GLN E CG  1 
ATOM   5542  C  CD  . GLN E  1 154 ? 67.404  -32.085 15.958 1.00 41.23 ? 153  GLN E CD  1 
ATOM   5543  O  OE1 . GLN E  1 154 ? 68.505  -31.606 15.689 1.00 43.11 ? 153  GLN E OE1 1 
ATOM   5544  N  NE2 . GLN E  1 154 ? 67.089  -32.519 17.176 1.00 42.63 ? 153  GLN E NE2 1 
ATOM   5545  O  OXT . GLN E  1 154 ? 63.446  -34.827 14.681 1.00 32.00 ? 153  GLN E OXT 1 
ATOM   5546  N  N   . ALA F  1 2   ? 48.484  -19.744 5.343  0.00 40.58 ? 1    ALA F N   1 
ATOM   5547  C  CA  . ALA F  1 2   ? 47.787  -19.036 6.454  0.00 40.59 ? 1    ALA F CA  1 
ATOM   5548  C  C   . ALA F  1 2   ? 48.079  -17.542 6.402  1.00 40.18 ? 1    ALA F C   1 
ATOM   5549  O  O   . ALA F  1 2   ? 49.190  -17.133 6.073  1.00 42.45 ? 1    ALA F O   1 
ATOM   5550  C  CB  . ALA F  1 2   ? 48.234  -19.608 7.794  0.00 40.60 ? 1    ALA F CB  1 
ATOM   5551  N  N   . THR F  1 3   ? 47.080  -16.726 6.721  1.00 39.13 ? 2    THR F N   1 
ATOM   5552  C  CA  . THR F  1 3   ? 47.262  -15.285 6.706  1.00 37.26 ? 2    THR F CA  1 
ATOM   5553  C  C   . THR F  1 3   ? 47.310  -14.729 8.126  1.00 32.89 ? 2    THR F C   1 
ATOM   5554  O  O   . THR F  1 3   ? 47.693  -13.577 8.335  1.00 28.89 ? 2    THR F O   1 
ATOM   5555  C  CB  . THR F  1 3   ? 46.143  -14.580 5.910  1.00 38.99 ? 2    THR F CB  1 
ATOM   5556  O  OG1 . THR F  1 3   ? 44.883  -14.783 6.558  1.00 43.19 ? 2    THR F OG1 1 
ATOM   5557  C  CG2 . THR F  1 3   ? 46.076  -15.143 4.497  1.00 42.47 ? 2    THR F CG2 1 
ATOM   5558  N  N   . LYS F  1 4   ? 46.911  -15.550 9.093  1.00 28.84 ? 3    LYS F N   1 
ATOM   5559  C  CA  . LYS F  1 4   ? 46.945  -15.161 10.500 1.00 27.98 ? 3    LYS F CA  1 
ATOM   5560  C  C   . LYS F  1 4   ? 47.463  -16.308 11.360 1.00 26.21 ? 3    LYS F C   1 
ATOM   5561  O  O   . LYS F  1 4   ? 47.246  -17.480 11.046 1.00 22.45 ? 3    LYS F O   1 
ATOM   5562  C  CB  . LYS F  1 4   ? 45.559  -14.734 10.988 1.00 31.89 ? 3    LYS F CB  1 
ATOM   5563  C  CG  . LYS F  1 4   ? 45.079  -13.425 10.387 1.00 36.24 ? 3    LYS F CG  1 
ATOM   5564  C  CD  . LYS F  1 4   ? 43.757  -12.973 10.989 1.00 40.69 ? 3    LYS F CD  1 
ATOM   5565  C  CE  . LYS F  1 4   ? 43.311  -11.651 10.375 1.00 43.53 ? 3    LYS F CE  1 
ATOM   5566  N  NZ  . LYS F  1 4   ? 42.014  -11.169 10.931 1.00 46.21 ? 3    LYS F NZ  1 
ATOM   5567  N  N   . ALA F  1 5   ? 48.156  -15.963 12.440 1.00 22.70 ? 4    ALA F N   1 
ATOM   5568  C  CA  . ALA F  1 5   ? 48.709  -16.956 13.348 1.00 20.82 ? 4    ALA F CA  1 
ATOM   5569  C  C   . ALA F  1 5   ? 48.814  -16.366 14.746 1.00 20.89 ? 4    ALA F C   1 
ATOM   5570  O  O   . ALA F  1 5   ? 48.656  -15.155 14.934 1.00 20.77 ? 4    ALA F O   1 
ATOM   5571  C  CB  . ALA F  1 5   ? 50.084  -17.401 12.864 1.00 19.31 ? 4    ALA F CB  1 
ATOM   5572  N  N   . VAL F  1 6   ? 49.085  -17.222 15.723 1.00 19.13 ? 5    VAL F N   1 
ATOM   5573  C  CA  . VAL F  1 6   ? 49.199  -16.778 17.103 1.00 19.94 ? 5    VAL F CA  1 
ATOM   5574  C  C   . VAL F  1 6   ? 50.111  -17.716 17.887 1.00 20.62 ? 5    VAL F C   1 
ATOM   5575  O  O   . VAL F  1 6   ? 50.270  -18.887 17.534 1.00 18.55 ? 5    VAL F O   1 
ATOM   5576  C  CB  . VAL F  1 6   ? 47.801  -16.726 17.779 1.00 20.83 ? 5    VAL F CB  1 
ATOM   5577  C  CG1 . VAL F  1 6   ? 47.216  -18.131 17.882 1.00 21.13 ? 5    VAL F CG1 1 
ATOM   5578  C  CG2 . VAL F  1 6   ? 47.894  -16.077 19.163 1.00 21.42 ? 5    VAL F CG2 1 
ATOM   5579  N  N   . ALA F  1 7   ? 50.746  -17.178 18.923 1.00 19.84 ? 6    ALA F N   1 
ATOM   5580  C  CA  . ALA F  1 7   ? 51.611  -17.970 19.783 1.00 21.32 ? 6    ALA F CA  1 
ATOM   5581  C  C   . ALA F  1 7   ? 51.300  -17.569 21.219 1.00 21.42 ? 6    ALA F C   1 
ATOM   5582  O  O   . ALA F  1 7   ? 51.235  -16.382 21.532 1.00 22.73 ? 6    ALA F O   1 
ATOM   5583  C  CB  . ALA F  1 7   ? 53.087  -17.703 19.468 1.00 19.04 ? 6    ALA F CB  1 
ATOM   5584  N  N   . VAL F  1 8   ? 51.081  -18.557 22.080 1.00 19.23 ? 7    VAL F N   1 
ATOM   5585  C  CA  . VAL F  1 8   ? 50.802  -18.289 23.485 1.00 19.65 ? 7    VAL F CA  1 
ATOM   5586  C  C   . VAL F  1 8   ? 52.091  -18.640 24.215 1.00 20.44 ? 7    VAL F C   1 
ATOM   5587  O  O   . VAL F  1 8   ? 52.519  -19.790 24.219 1.00 19.02 ? 7    VAL F O   1 
ATOM   5588  C  CB  . VAL F  1 8   ? 49.627  -19.152 23.991 1.00 20.73 ? 7    VAL F CB  1 
ATOM   5589  C  CG1 . VAL F  1 8   ? 49.419  -18.947 25.495 1.00 22.50 ? 7    VAL F CG1 1 
ATOM   5590  C  CG2 . VAL F  1 8   ? 48.361  -18.780 23.223 1.00 20.22 ? 7    VAL F CG2 1 
ATOM   5591  N  N   . LEU F  1 9   ? 52.719  -17.631 24.807 1.00 19.59 ? 8    LEU F N   1 
ATOM   5592  C  CA  . LEU F  1 9   ? 53.983  -17.809 25.505 1.00 19.40 ? 8    LEU F CA  1 
ATOM   5593  C  C   . LEU F  1 9   ? 53.835  -18.185 26.979 1.00 20.56 ? 8    LEU F C   1 
ATOM   5594  O  O   . LEU F  1 9   ? 53.097  -17.548 27.725 1.00 19.65 ? 8    LEU F O   1 
ATOM   5595  C  CB  . LEU F  1 9   ? 54.812  -16.526 25.387 1.00 20.03 ? 8    LEU F CB  1 
ATOM   5596  C  CG  . LEU F  1 9   ? 55.038  -15.958 23.974 1.00 22.48 ? 8    LEU F CG  1 
ATOM   5597  C  CD1 . LEU F  1 9   ? 55.919  -14.712 24.057 1.00 22.63 ? 8    LEU F CD1 1 
ATOM   5598  C  CD2 . LEU F  1 9   ? 55.699  -17.007 23.086 1.00 22.45 ? 8    LEU F CD2 1 
ATOM   5599  N  N   . LYS F  1 10  ? 54.553  -19.227 27.385 1.00 21.52 ? 9    LYS F N   1 
ATOM   5600  C  CA  . LYS F  1 10  ? 54.542  -19.695 28.766 1.00 24.43 ? 9    LYS F CA  1 
ATOM   5601  C  C   . LYS F  1 10  ? 55.911  -20.286 29.053 1.00 23.45 ? 9    LYS F C   1 
ATOM   5602  O  O   . LYS F  1 10  ? 56.623  -20.690 28.132 1.00 20.69 ? 9    LYS F O   1 
ATOM   5603  C  CB  . LYS F  1 10  ? 53.472  -20.772 28.969 1.00 29.27 ? 9    LYS F CB  1 
ATOM   5604  C  CG  . LYS F  1 10  ? 52.052  -20.290 28.722 1.00 35.78 ? 9    LYS F CG  1 
ATOM   5605  C  CD  . LYS F  1 10  ? 51.047  -21.434 28.817 1.00 40.45 ? 9    LYS F CD  1 
ATOM   5606  C  CE  . LYS F  1 10  ? 49.629  -20.942 28.522 1.00 42.60 ? 9    LYS F CE  1 
ATOM   5607  N  NZ  . LYS F  1 10  ? 48.641  -22.057 28.457 1.00 43.65 ? 9    LYS F NZ  1 
ATOM   5608  N  N   . GLY F  1 11  ? 56.275  -20.334 30.329 1.00 23.53 ? 10   GLY F N   1 
ATOM   5609  C  CA  . GLY F  1 11  ? 57.561  -20.887 30.715 1.00 25.12 ? 10   GLY F CA  1 
ATOM   5610  C  C   . GLY F  1 11  ? 57.532  -21.392 32.147 1.00 27.25 ? 10   GLY F C   1 
ATOM   5611  O  O   . GLY F  1 11  ? 56.457  -21.595 32.717 1.00 27.58 ? 10   GLY F O   1 
ATOM   5612  N  N   . ASP F  1 12  ? 58.709  -21.597 32.727 1.00 28.25 ? 11   ASP F N   1 
ATOM   5613  C  CA  . ASP F  1 12  ? 58.814  -22.070 34.103 1.00 31.36 ? 11   ASP F CA  1 
ATOM   5614  C  C   . ASP F  1 12  ? 58.551  -20.955 35.098 1.00 32.07 ? 11   ASP F C   1 
ATOM   5615  O  O   . ASP F  1 12  ? 58.188  -21.215 36.249 1.00 33.04 ? 11   ASP F O   1 
ATOM   5616  C  CB  . ASP F  1 12  ? 60.203  -22.646 34.361 1.00 35.36 ? 11   ASP F CB  1 
ATOM   5617  C  CG  . ASP F  1 12  ? 60.468  -23.886 33.553 1.00 39.02 ? 11   ASP F CG  1 
ATOM   5618  O  OD1 . ASP F  1 12  ? 59.608  -24.789 33.577 1.00 41.03 ? 11   ASP F OD1 1 
ATOM   5619  O  OD2 . ASP F  1 12  ? 61.529  -23.958 32.897 1.00 43.92 ? 11   ASP F OD2 1 
ATOM   5620  N  N   . GLY F  1 13  ? 58.742  -19.717 34.651 1.00 30.51 ? 12   GLY F N   1 
ATOM   5621  C  CA  . GLY F  1 13  ? 58.531  -18.569 35.511 1.00 27.93 ? 12   GLY F CA  1 
ATOM   5622  C  C   . GLY F  1 13  ? 57.217  -17.856 35.265 1.00 28.00 ? 12   GLY F C   1 
ATOM   5623  O  O   . GLY F  1 13  ? 56.280  -18.447 34.731 1.00 27.64 ? 12   GLY F O   1 
ATOM   5624  N  N   . PRO F  1 14  ? 57.127  -16.566 35.623 1.00 26.98 ? 13   PRO F N   1 
ATOM   5625  C  CA  . PRO F  1 14  ? 55.918  -15.758 35.453 1.00 27.93 ? 13   PRO F CA  1 
ATOM   5626  C  C   . PRO F  1 14  ? 55.713  -15.123 34.082 1.00 26.37 ? 13   PRO F C   1 
ATOM   5627  O  O   . PRO F  1 14  ? 54.659  -14.553 33.820 1.00 26.61 ? 13   PRO F O   1 
ATOM   5628  C  CB  . PRO F  1 14  ? 56.076  -14.703 36.534 1.00 26.74 ? 13   PRO F CB  1 
ATOM   5629  C  CG  . PRO F  1 14  ? 57.537  -14.410 36.449 1.00 28.10 ? 13   PRO F CG  1 
ATOM   5630  C  CD  . PRO F  1 14  ? 58.165  -15.796 36.333 1.00 27.89 ? 13   PRO F CD  1 
ATOM   5631  N  N   . VAL F  1 15  ? 56.704  -15.220 33.206 1.00 25.62 ? 14   VAL F N   1 
ATOM   5632  C  CA  . VAL F  1 15  ? 56.586  -14.601 31.890 1.00 24.84 ? 14   VAL F CA  1 
ATOM   5633  C  C   . VAL F  1 15  ? 55.541  -15.276 31.027 1.00 24.84 ? 14   VAL F C   1 
ATOM   5634  O  O   . VAL F  1 15  ? 55.653  -16.454 30.708 1.00 26.53 ? 14   VAL F O   1 
ATOM   5635  C  CB  . VAL F  1 15  ? 57.945  -14.616 31.113 1.00 23.60 ? 14   VAL F CB  1 
ATOM   5636  C  CG1 . VAL F  1 15  ? 57.782  -13.978 29.724 1.00 24.72 ? 14   VAL F CG1 1 
ATOM   5637  C  CG2 . VAL F  1 15  ? 59.007  -13.842 31.895 1.00 25.16 ? 14   VAL F CG2 1 
ATOM   5638  N  N   . GLN F  1 16  ? 54.534  -14.515 30.628 1.00 24.86 ? 15   GLN F N   1 
ATOM   5639  C  CA  . GLN F  1 16  ? 53.490  -15.060 29.784 1.00 26.43 ? 15   GLN F CA  1 
ATOM   5640  C  C   . GLN F  1 16  ? 52.893  -14.006 28.850 1.00 25.36 ? 15   GLN F C   1 
ATOM   5641  O  O   . GLN F  1 16  ? 52.910  -12.797 29.143 1.00 23.97 ? 15   GLN F O   1 
ATOM   5642  C  CB  . GLN F  1 16  ? 52.409  -15.719 30.663 1.00 31.06 ? 15   GLN F CB  1 
ATOM   5643  C  CG  . GLN F  1 16  ? 51.855  -14.862 31.795 1.00 38.82 ? 15   GLN F CG  1 
ATOM   5644  C  CD  . GLN F  1 16  ? 50.918  -15.655 32.706 1.00 44.86 ? 15   GLN F CD  1 
ATOM   5645  O  OE1 . GLN F  1 16  ? 51.154  -15.790 33.907 1.00 49.91 ? 15   GLN F OE1 1 
ATOM   5646  N  NE2 . GLN F  1 16  ? 49.854  -16.192 32.127 1.00 45.17 ? 15   GLN F NE2 1 
ATOM   5647  N  N   . GLY F  1 17  ? 52.409  -14.454 27.697 1.00 22.52 ? 16   GLY F N   1 
ATOM   5648  C  CA  . GLY F  1 17  ? 51.814  -13.516 26.774 1.00 21.54 ? 16   GLY F CA  1 
ATOM   5649  C  C   . GLY F  1 17  ? 51.168  -14.135 25.555 1.00 22.05 ? 16   GLY F C   1 
ATOM   5650  O  O   . GLY F  1 17  ? 51.179  -15.352 25.351 1.00 22.72 ? 16   GLY F O   1 
ATOM   5651  N  N   . ILE F  1 18  ? 50.587  -13.267 24.740 1.00 21.88 ? 17   ILE F N   1 
ATOM   5652  C  CA  . ILE F  1 18  ? 49.920  -13.677 23.521 1.00 22.02 ? 17   ILE F CA  1 
ATOM   5653  C  C   . ILE F  1 18  ? 50.411  -12.812 22.368 1.00 22.08 ? 17   ILE F C   1 
ATOM   5654  O  O   . ILE F  1 18  ? 50.271  -11.589 22.397 1.00 21.88 ? 17   ILE F O   1 
ATOM   5655  C  CB  . ILE F  1 18  ? 48.402  -13.501 23.646 1.00 23.49 ? 17   ILE F CB  1 
ATOM   5656  C  CG1 . ILE F  1 18  ? 47.857  -14.432 24.733 1.00 26.15 ? 17   ILE F CG1 1 
ATOM   5657  C  CG2 . ILE F  1 18  ? 47.741  -13.760 22.292 1.00 26.04 ? 17   ILE F CG2 1 
ATOM   5658  C  CD1 . ILE F  1 18  ? 46.372  -14.207 25.036 1.00 26.57 ? 17   ILE F CD1 1 
ATOM   5659  N  N   . ILE F  1 19  ? 50.971  -13.447 21.345 1.00 20.83 ? 18   ILE F N   1 
ATOM   5660  C  CA  . ILE F  1 19  ? 51.476  -12.713 20.198 1.00 20.98 ? 18   ILE F CA  1 
ATOM   5661  C  C   . ILE F  1 19  ? 50.744  -13.104 18.919 1.00 21.97 ? 18   ILE F C   1 
ATOM   5662  O  O   . ILE F  1 19  ? 50.659  -14.285 18.572 1.00 22.26 ? 18   ILE F O   1 
ATOM   5663  C  CB  . ILE F  1 19  ? 52.984  -12.957 20.005 1.00 19.66 ? 18   ILE F CB  1 
ATOM   5664  C  CG1 . ILE F  1 19  ? 53.756  -12.507 21.252 1.00 21.29 ? 18   ILE F CG1 1 
ATOM   5665  C  CG2 . ILE F  1 19  ? 53.470  -12.205 18.783 1.00 20.37 ? 18   ILE F CG2 1 
ATOM   5666  C  CD1 . ILE F  1 19  ? 53.696  -10.988 21.514 1.00 20.90 ? 18   ILE F CD1 1 
ATOM   5667  N  N   . ASN F  1 20  ? 50.223  -12.096 18.226 1.00 21.70 ? 19   ASN F N   1 
ATOM   5668  C  CA  . ASN F  1 20  ? 49.494  -12.286 16.977 1.00 22.39 ? 19   ASN F CA  1 
ATOM   5669  C  C   . ASN F  1 20  ? 50.379  -11.993 15.772 1.00 23.75 ? 19   ASN F C   1 
ATOM   5670  O  O   . ASN F  1 20  ? 51.319  -11.198 15.850 1.00 24.16 ? 19   ASN F O   1 
ATOM   5671  C  CB  . ASN F  1 20  ? 48.281  -11.356 16.944 1.00 23.33 ? 19   ASN F CB  1 
ATOM   5672  C  CG  . ASN F  1 20  ? 47.394  -11.528 18.153 1.00 25.65 ? 19   ASN F CG  1 
ATOM   5673  O  OD1 . ASN F  1 20  ? 46.674  -12.519 18.270 1.00 24.12 ? 19   ASN F OD1 1 
ATOM   5674  N  ND2 . ASN F  1 20  ? 47.454  -10.572 19.073 1.00 25.29 ? 19   ASN F ND2 1 
ATOM   5675  N  N   . PHE F  1 21  ? 50.064  -12.647 14.659 1.00 22.49 ? 20   PHE F N   1 
ATOM   5676  C  CA  . PHE F  1 21  ? 50.787  -12.473 13.410 1.00 22.04 ? 20   PHE F CA  1 
ATOM   5677  C  C   . PHE F  1 21  ? 49.730  -12.303 12.326 1.00 23.70 ? 20   PHE F C   1 
ATOM   5678  O  O   . PHE F  1 21  ? 48.682  -12.958 12.371 1.00 22.26 ? 20   PHE F O   1 
ATOM   5679  C  CB  . PHE F  1 21  ? 51.619  -13.719 13.069 1.00 21.44 ? 20   PHE F CB  1 
ATOM   5680  C  CG  . PHE F  1 21  ? 52.708  -14.037 14.062 1.00 21.96 ? 20   PHE F CG  1 
ATOM   5681  C  CD1 . PHE F  1 21  ? 54.010  -13.587 13.858 1.00 23.25 ? 20   PHE F CD1 1 
ATOM   5682  C  CD2 . PHE F  1 21  ? 52.440  -14.822 15.180 1.00 22.01 ? 20   PHE F CD2 1 
ATOM   5683  C  CE1 . PHE F  1 21  ? 55.032  -13.920 14.749 1.00 21.34 ? 20   PHE F CE1 1 
ATOM   5684  C  CE2 . PHE F  1 21  ? 53.451  -15.163 16.078 1.00 20.38 ? 20   PHE F CE2 1 
ATOM   5685  C  CZ  . PHE F  1 21  ? 54.752  -14.712 15.860 1.00 20.83 ? 20   PHE F CZ  1 
ATOM   5686  N  N   . GLU F  1 22  ? 49.990  -11.418 11.371 1.00 23.42 ? 21   GLU F N   1 
ATOM   5687  C  CA  . GLU F  1 22  ? 49.078  -11.222 10.254 1.00 26.22 ? 21   GLU F CA  1 
ATOM   5688  C  C   . GLU F  1 22  ? 49.856  -10.853 9.003  1.00 27.57 ? 21   GLU F C   1 
ATOM   5689  O  O   . GLU F  1 22  ? 50.732  -9.982  9.029  1.00 28.24 ? 21   GLU F O   1 
ATOM   5690  C  CB  . GLU F  1 22  ? 48.032  -10.145 10.548 1.00 29.18 ? 21   GLU F CB  1 
ATOM   5691  C  CG  . GLU F  1 22  ? 47.098  -9.915  9.362  1.00 35.38 ? 21   GLU F CG  1 
ATOM   5692  C  CD  . GLU F  1 22  ? 45.793  -9.236  9.733  1.00 40.29 ? 21   GLU F CD  1 
ATOM   5693  O  OE1 . GLU F  1 22  ? 44.993  -8.969  8.812  1.00 44.31 ? 21   GLU F OE1 1 
ATOM   5694  O  OE2 . GLU F  1 22  ? 45.557  -8.972  10.932 1.00 43.00 ? 21   GLU F OE2 1 
ATOM   5695  N  N   . GLN F  1 23  ? 49.534  -11.530 7.908  1.00 26.65 ? 22   GLN F N   1 
ATOM   5696  C  CA  . GLN F  1 23  ? 50.193  -11.298 6.632  1.00 29.02 ? 22   GLN F CA  1 
ATOM   5697  C  C   . GLN F  1 23  ? 49.136  -11.146 5.541  1.00 31.77 ? 22   GLN F C   1 
ATOM   5698  O  O   . GLN F  1 23  ? 48.547  -12.125 5.090  1.00 31.77 ? 22   GLN F O   1 
ATOM   5699  C  CB  . GLN F  1 23  ? 51.132  -12.464 6.325  1.00 27.83 ? 22   GLN F CB  1 
ATOM   5700  C  CG  . GLN F  1 23  ? 51.925  -12.321 5.049  1.00 26.99 ? 22   GLN F CG  1 
ATOM   5701  C  CD  . GLN F  1 23  ? 52.937  -13.430 4.880  1.00 28.07 ? 22   GLN F CD  1 
ATOM   5702  O  OE1 . GLN F  1 23  ? 52.685  -14.574 5.257  1.00 27.22 ? 22   GLN F OE1 1 
ATOM   5703  N  NE2 . GLN F  1 23  ? 54.090  -13.102 4.298  1.00 26.88 ? 22   GLN F NE2 1 
ATOM   5704  N  N   . LYS F  1 24  ? 48.906  -9.904  5.132  1.00 34.66 ? 23   LYS F N   1 
ATOM   5705  C  CA  . LYS F  1 24  ? 47.912  -9.570  4.118  1.00 39.51 ? 23   LYS F CA  1 
ATOM   5706  C  C   . LYS F  1 24  ? 48.164  -10.238 2.769  1.00 39.88 ? 23   LYS F C   1 
ATOM   5707  O  O   . LYS F  1 24  ? 47.227  -10.702 2.123  1.00 41.20 ? 23   LYS F O   1 
ATOM   5708  C  CB  . LYS F  1 24  ? 47.850  -8.047  3.936  1.00 42.56 ? 23   LYS F CB  1 
ATOM   5709  C  CG  . LYS F  1 24  ? 46.716  -7.572  3.038  1.00 48.44 ? 23   LYS F CG  1 
ATOM   5710  C  CD  . LYS F  1 24  ? 46.729  -6.057  2.880  1.00 52.27 ? 23   LYS F CD  1 
ATOM   5711  C  CE  . LYS F  1 24  ? 45.578  -5.578  2.001  1.00 55.74 ? 23   LYS F CE  1 
ATOM   5712  N  NZ  . LYS F  1 24  ? 45.581  -4.093  1.841  1.00 57.43 ? 23   LYS F NZ  1 
ATOM   5713  N  N   . GLU F  1 25  ? 49.423  -10.278 2.345  1.00 40.13 ? 24   GLU F N   1 
ATOM   5714  C  CA  . GLU F  1 25  ? 49.784  -10.889 1.071  1.00 41.36 ? 24   GLU F CA  1 
ATOM   5715  C  C   . GLU F  1 25  ? 50.942  -11.847 1.298  1.00 40.41 ? 24   GLU F C   1 
ATOM   5716  O  O   . GLU F  1 25  ? 51.793  -11.598 2.150  1.00 38.46 ? 24   GLU F O   1 
ATOM   5717  C  CB  . GLU F  1 25  ? 50.202  -9.808  0.070  1.00 44.11 ? 24   GLU F CB  1 
ATOM   5718  C  CG  . GLU F  1 25  ? 49.177  -8.697  -0.104 1.00 49.59 ? 24   GLU F CG  1 
ATOM   5719  C  CD  . GLU F  1 25  ? 47.849  -9.195  -0.656 1.00 53.48 ? 24   GLU F CD  1 
ATOM   5720  O  OE1 . GLU F  1 25  ? 46.907  -8.378  -0.760 1.00 55.31 ? 24   GLU F OE1 1 
ATOM   5721  O  OE2 . GLU F  1 25  ? 47.746  -10.398 -0.988 1.00 54.02 ? 24   GLU F OE2 1 
ATOM   5722  N  N   . SER F  1 26  ? 50.986  -12.933 0.531  1.00 40.63 ? 25   SER F N   1 
ATOM   5723  C  CA  . SER F  1 26  ? 52.056  -13.912 0.693  1.00 41.43 ? 25   SER F CA  1 
ATOM   5724  C  C   . SER F  1 26  ? 53.429  -13.317 0.395  1.00 41.14 ? 25   SER F C   1 
ATOM   5725  O  O   . SER F  1 26  ? 54.444  -13.794 0.901  1.00 40.31 ? 25   SER F O   1 
ATOM   5726  C  CB  . SER F  1 26  ? 51.808  -15.133 -0.202 1.00 43.09 ? 25   SER F CB  1 
ATOM   5727  O  OG  . SER F  1 26  ? 51.840  -14.789 -1.575 1.00 44.45 ? 25   SER F OG  1 
ATOM   5728  N  N   . ASN F  1 27  ? 53.461  -12.269 -0.422 1.00 41.15 ? 26   ASN F N   1 
ATOM   5729  C  CA  . ASN F  1 27  ? 54.727  -11.624 -0.765 1.00 43.29 ? 26   ASN F CA  1 
ATOM   5730  C  C   . ASN F  1 27  ? 54.902  -10.357 0.066  1.00 43.40 ? 26   ASN F C   1 
ATOM   5731  O  O   . ASN F  1 27  ? 55.775  -9.532  -0.218 1.00 45.02 ? 26   ASN F O   1 
ATOM   5732  C  CB  . ASN F  1 27  ? 54.752  -11.266 -2.257 1.00 44.44 ? 26   ASN F CB  1 
ATOM   5733  C  CG  . ASN F  1 27  ? 53.793  -10.131 -2.606 1.00 47.12 ? 26   ASN F CG  1 
ATOM   5734  O  OD1 . ASN F  1 27  ? 52.643  -10.114 -2.164 1.00 47.92 ? 26   ASN F OD1 1 
ATOM   5735  N  ND2 . ASN F  1 27  ? 54.263  -9.184  -3.412 1.00 47.70 ? 26   ASN F ND2 1 
ATOM   5736  N  N   . GLY F  1 28  ? 54.076  -10.209 1.097  1.00 41.06 ? 27   GLY F N   1 
ATOM   5737  C  CA  . GLY F  1 28  ? 54.145  -9.019  1.923  1.00 37.97 ? 27   GLY F CA  1 
ATOM   5738  C  C   . GLY F  1 28  ? 54.676  -9.213  3.327  1.00 35.11 ? 27   GLY F C   1 
ATOM   5739  O  O   . GLY F  1 28  ? 54.910  -10.335 3.770  1.00 33.92 ? 27   GLY F O   1 
ATOM   5740  N  N   . PRO F  1 29  ? 54.873  -8.112  4.060  1.00 33.90 ? 28   PRO F N   1 
ATOM   5741  C  CA  . PRO F  1 29  ? 55.382  -8.180  5.428  1.00 31.79 ? 28   PRO F CA  1 
ATOM   5742  C  C   . PRO F  1 29  ? 54.389  -8.792  6.410  1.00 30.22 ? 28   PRO F C   1 
ATOM   5743  O  O   . PRO F  1 29  ? 53.181  -8.823  6.162  1.00 28.04 ? 28   PRO F O   1 
ATOM   5744  C  CB  . PRO F  1 29  ? 55.688  -6.719  5.753  1.00 33.54 ? 28   PRO F CB  1 
ATOM   5745  C  CG  . PRO F  1 29  ? 54.643  -5.982  4.980  1.00 34.72 ? 28   PRO F CG  1 
ATOM   5746  C  CD  . PRO F  1 29  ? 54.648  -6.713  3.650  1.00 33.06 ? 28   PRO F CD  1 
ATOM   5747  N  N   . VAL F  1 30  ? 54.920  -9.281  7.525  1.00 26.78 ? 29   VAL F N   1 
ATOM   5748  C  CA  . VAL F  1 30  ? 54.111  -9.878  8.570  1.00 24.06 ? 29   VAL F CA  1 
ATOM   5749  C  C   . VAL F  1 30  ? 54.058  -8.905  9.740  1.00 24.21 ? 29   VAL F C   1 
ATOM   5750  O  O   . VAL F  1 30  ? 55.094  -8.421  10.198 1.00 23.35 ? 29   VAL F O   1 
ATOM   5751  C  CB  . VAL F  1 30  ? 54.732  -11.213 9.065  1.00 24.02 ? 29   VAL F CB  1 
ATOM   5752  C  CG1 . VAL F  1 30  ? 53.878  -11.812 10.188 1.00 23.36 ? 29   VAL F CG1 1 
ATOM   5753  C  CG2 . VAL F  1 30  ? 54.848  -12.195 7.908  1.00 23.15 ? 29   VAL F CG2 1 
ATOM   5754  N  N   . LYS F  1 31  ? 52.855  -8.594  10.205 1.00 23.62 ? 30   LYS F N   1 
ATOM   5755  C  CA  . LYS F  1 31  ? 52.713  -7.715  11.354 1.00 24.48 ? 30   LYS F CA  1 
ATOM   5756  C  C   . LYS F  1 31  ? 52.671  -8.617  12.579 1.00 24.73 ? 30   LYS F C   1 
ATOM   5757  O  O   . LYS F  1 31  ? 51.973  -9.635  12.591 1.00 22.57 ? 30   LYS F O   1 
ATOM   5758  C  CB  . LYS F  1 31  ? 51.435  -6.878  11.255 1.00 27.92 ? 30   LYS F CB  1 
ATOM   5759  C  CG  . LYS F  1 31  ? 51.478  -5.857  10.133 1.00 35.53 ? 30   LYS F CG  1 
ATOM   5760  C  CD  . LYS F  1 31  ? 50.341  -4.848  10.215 1.00 40.09 ? 30   LYS F CD  1 
ATOM   5761  C  CE  . LYS F  1 31  ? 50.485  -3.798  9.110  1.00 44.30 ? 30   LYS F CE  1 
ATOM   5762  N  NZ  . LYS F  1 31  ? 49.446  -2.723  9.179  1.00 45.22 ? 30   LYS F NZ  1 
ATOM   5763  N  N   . VAL F  1 32  ? 53.439  -8.245  13.596 1.00 23.10 ? 31   VAL F N   1 
ATOM   5764  C  CA  . VAL F  1 32  ? 53.536  -9.005  14.830 1.00 23.26 ? 31   VAL F CA  1 
ATOM   5765  C  C   . VAL F  1 32  ? 53.198  -8.076  15.985 1.00 24.82 ? 31   VAL F C   1 
ATOM   5766  O  O   . VAL F  1 32  ? 53.884  -7.076  16.198 1.00 24.58 ? 31   VAL F O   1 
ATOM   5767  C  CB  . VAL F  1 32  ? 54.968  -9.528  15.031 1.00 23.45 ? 31   VAL F CB  1 
ATOM   5768  C  CG1 . VAL F  1 32  ? 55.026  -10.440 16.251 1.00 21.89 ? 31   VAL F CG1 1 
ATOM   5769  C  CG2 . VAL F  1 32  ? 55.435  -10.243 13.778 1.00 21.08 ? 31   VAL F CG2 1 
ATOM   5770  N  N   . TRP F  1 33  ? 52.154  -8.405  16.736 1.00 22.56 ? 32   TRP F N   1 
ATOM   5771  C  CA  . TRP F  1 33  ? 51.750  -7.555  17.844 1.00 23.60 ? 32   TRP F CA  1 
ATOM   5772  C  C   . TRP F  1 33  ? 51.088  -8.327  18.968 1.00 24.16 ? 32   TRP F C   1 
ATOM   5773  O  O   . TRP F  1 33  ? 50.500  -9.392  18.761 1.00 24.84 ? 32   TRP F O   1 
ATOM   5774  C  CB  . TRP F  1 33  ? 50.788  -6.480  17.342 1.00 25.35 ? 32   TRP F CB  1 
ATOM   5775  C  CG  . TRP F  1 33  ? 49.391  -6.987  17.130 1.00 26.65 ? 32   TRP F CG  1 
ATOM   5776  C  CD1 . TRP F  1 33  ? 48.338  -6.878  17.997 1.00 28.67 ? 32   TRP F CD1 1 
ATOM   5777  C  CD2 . TRP F  1 33  ? 48.894  -7.688  15.984 1.00 27.20 ? 32   TRP F CD2 1 
ATOM   5778  N  NE1 . TRP F  1 33  ? 47.217  -7.464  17.456 1.00 30.04 ? 32   TRP F NE1 1 
ATOM   5779  C  CE2 . TRP F  1 33  ? 47.533  -7.970  16.219 1.00 27.43 ? 32   TRP F CE2 1 
ATOM   5780  C  CE3 . TRP F  1 33  ? 49.473  -8.105  14.775 1.00 28.09 ? 32   TRP F CE3 1 
ATOM   5781  C  CZ2 . TRP F  1 33  ? 46.733  -8.646  15.294 1.00 29.47 ? 32   TRP F CZ2 1 
ATOM   5782  C  CZ3 . TRP F  1 33  ? 48.676  -8.780  13.851 1.00 29.74 ? 32   TRP F CZ3 1 
ATOM   5783  C  CH2 . TRP F  1 33  ? 47.320  -9.043  14.117 1.00 29.50 ? 32   TRP F CH2 1 
ATOM   5784  N  N   . GLY F  1 34  ? 51.161  -7.762  20.161 1.00 24.39 ? 33   GLY F N   1 
ATOM   5785  C  CA  . GLY F  1 34  ? 50.568  -8.407  21.311 1.00 25.27 ? 33   GLY F CA  1 
ATOM   5786  C  C   . GLY F  1 34  ? 51.166  -7.891  22.598 1.00 26.78 ? 33   GLY F C   1 
ATOM   5787  O  O   . GLY F  1 34  ? 51.779  -6.824  22.633 1.00 28.87 ? 33   GLY F O   1 
ATOM   5788  N  N   . SER F  1 35  ? 50.998  -8.656  23.663 1.00 26.75 ? 34   SER F N   1 
ATOM   5789  C  CA  . SER F  1 35  ? 51.511  -8.250  24.955 1.00 29.07 ? 34   SER F CA  1 
ATOM   5790  C  C   . SER F  1 35  ? 52.174  -9.404  25.696 1.00 27.47 ? 34   SER F C   1 
ATOM   5791  O  O   . SER F  1 35  ? 51.711  -10.541 25.639 1.00 25.56 ? 34   SER F O   1 
ATOM   5792  C  CB  . SER F  1 35  ? 50.363  -7.687  25.795 1.00 30.63 ? 34   SER F CB  1 
ATOM   5793  O  OG  . SER F  1 35  ? 50.783  -7.460  27.121 1.00 37.88 ? 34   SER F OG  1 
ATOM   5794  N  N   . ILE F  1 36  ? 53.272  -9.099  26.375 1.00 24.44 ? 35   ILE F N   1 
ATOM   5795  C  CA  . ILE F  1 36  ? 53.996  -10.085 27.166 1.00 23.43 ? 35   ILE F CA  1 
ATOM   5796  C  C   . ILE F  1 36  ? 54.148  -9.450  28.547 1.00 25.41 ? 35   ILE F C   1 
ATOM   5797  O  O   . ILE F  1 36  ? 54.558  -8.293  28.656 1.00 27.00 ? 35   ILE F O   1 
ATOM   5798  C  CB  . ILE F  1 36  ? 55.397  -10.361 26.599 1.00 20.72 ? 35   ILE F CB  1 
ATOM   5799  C  CG1 . ILE F  1 36  ? 55.303  -10.763 25.127 1.00 20.38 ? 35   ILE F CG1 1 
ATOM   5800  C  CG2 . ILE F  1 36  ? 56.073  -11.448 27.416 1.00 21.29 ? 35   ILE F CG2 1 
ATOM   5801  C  CD1 . ILE F  1 36  ? 56.648  -10.989 24.469 1.00 22.69 ? 35   ILE F CD1 1 
ATOM   5802  N  N   . LYS F  1 37  ? 53.820  -10.196 29.595 1.00 24.85 ? 36   LYS F N   1 
ATOM   5803  C  CA  . LYS F  1 37  ? 53.915  -9.670  30.952 1.00 25.00 ? 36   LYS F CA  1 
ATOM   5804  C  C   . LYS F  1 37  ? 54.860  -10.493 31.817 1.00 23.19 ? 36   LYS F C   1 
ATOM   5805  O  O   . LYS F  1 37  ? 55.315  -11.561 31.407 1.00 23.08 ? 36   LYS F O   1 
ATOM   5806  C  CB  . LYS F  1 37  ? 52.520  -9.630  31.591 1.00 28.73 ? 36   LYS F CB  1 
ATOM   5807  C  CG  . LYS F  1 37  ? 51.906  -10.997 31.815 1.00 34.20 ? 36   LYS F CG  1 
ATOM   5808  C  CD  . LYS F  1 37  ? 50.576  -10.891 32.545 1.00 38.28 ? 36   LYS F CD  1 
ATOM   5809  C  CE  . LYS F  1 37  ? 50.200  -12.215 33.169 1.00 38.88 ? 36   LYS F CE  1 
ATOM   5810  N  NZ  . LYS F  1 37  ? 48.917  -12.077 33.884 0.00 39.12 ? 36   LYS F NZ  1 
ATOM   5811  N  N   . GLY F  1 38  ? 55.149  -9.988  33.017 1.00 22.99 ? 37   GLY F N   1 
ATOM   5812  C  CA  . GLY F  1 38  ? 56.042  -10.679 33.932 1.00 22.30 ? 37   GLY F CA  1 
ATOM   5813  C  C   . GLY F  1 38  ? 57.513  -10.511 33.581 1.00 22.13 ? 37   GLY F C   1 
ATOM   5814  O  O   . GLY F  1 38  ? 58.359  -11.265 34.050 1.00 23.41 ? 37   GLY F O   1 
ATOM   5815  N  N   . LEU F  1 39  ? 57.821  -9.511  32.765 1.00 22.33 ? 38   LEU F N   1 
ATOM   5816  C  CA  . LEU F  1 39  ? 59.199  -9.257  32.342 1.00 22.22 ? 38   LEU F CA  1 
ATOM   5817  C  C   . LEU F  1 39  ? 59.889  -8.159  33.150 1.00 24.93 ? 38   LEU F C   1 
ATOM   5818  O  O   . LEU F  1 39  ? 59.237  -7.245  33.654 1.00 22.21 ? 38   LEU F O   1 
ATOM   5819  C  CB  . LEU F  1 39  ? 59.222  -8.841  30.872 1.00 23.26 ? 38   LEU F CB  1 
ATOM   5820  C  CG  . LEU F  1 39  ? 58.947  -9.868  29.775 1.00 23.39 ? 38   LEU F CG  1 
ATOM   5821  C  CD1 . LEU F  1 39  ? 58.663  -9.153  28.460 1.00 21.88 ? 38   LEU F CD1 1 
ATOM   5822  C  CD2 . LEU F  1 39  ? 60.146  -10.786 29.642 1.00 21.61 ? 38   LEU F CD2 1 
ATOM   5823  N  N   . THR F  1 40  ? 61.208  -8.261  33.275 1.00 25.93 ? 39   THR F N   1 
ATOM   5824  C  CA  . THR F  1 40  ? 61.978  -7.236  33.971 1.00 28.14 ? 39   THR F CA  1 
ATOM   5825  C  C   . THR F  1 40  ? 62.072  -6.074  32.985 1.00 29.42 ? 39   THR F C   1 
ATOM   5826  O  O   . THR F  1 40  ? 62.143  -6.287  31.769 1.00 27.36 ? 39   THR F O   1 
ATOM   5827  C  CB  . THR F  1 40  ? 63.397  -7.723  34.306 1.00 27.54 ? 39   THR F CB  1 
ATOM   5828  O  OG1 . THR F  1 40  ? 64.031  -8.196  33.111 1.00 30.38 ? 39   THR F OG1 1 
ATOM   5829  C  CG2 . THR F  1 40  ? 63.348  -8.850  35.329 1.00 27.54 ? 39   THR F CG2 1 
ATOM   5830  N  N   . GLU F  1 41  ? 62.063  -4.848  33.498 1.00 30.44 ? 40   GLU F N   1 
ATOM   5831  C  CA  . GLU F  1 41  ? 62.128  -3.671  32.638 1.00 31.89 ? 40   GLU F CA  1 
ATOM   5832  C  C   . GLU F  1 41  ? 63.344  -3.728  31.719 1.00 29.54 ? 40   GLU F C   1 
ATOM   5833  O  O   . GLU F  1 41  ? 64.424  -4.136  32.133 1.00 29.85 ? 40   GLU F O   1 
ATOM   5834  C  CB  . GLU F  1 41  ? 62.172  -2.392  33.486 1.00 35.24 ? 40   GLU F CB  1 
ATOM   5835  C  CG  . GLU F  1 41  ? 62.048  -1.112  32.665 1.00 38.17 ? 40   GLU F CG  1 
ATOM   5836  C  CD  . GLU F  1 41  ? 62.007  0.147   33.521 1.00 41.13 ? 40   GLU F CD  1 
ATOM   5837  O  OE1 . GLU F  1 41  ? 61.928  1.252   32.944 1.00 40.88 ? 40   GLU F OE1 1 
ATOM   5838  O  OE2 . GLU F  1 41  ? 62.052  0.031   34.766 1.00 41.47 ? 40   GLU F OE2 1 
ATOM   5839  N  N   . GLY F  1 42  ? 63.163  -3.339  30.463 1.00 29.47 ? 41   GLY F N   1 
ATOM   5840  C  CA  . GLY F  1 42  ? 64.283  -3.356  29.539 1.00 29.45 ? 41   GLY F CA  1 
ATOM   5841  C  C   . GLY F  1 42  ? 64.130  -4.219  28.297 1.00 29.85 ? 41   GLY F C   1 
ATOM   5842  O  O   . GLY F  1 42  ? 63.034  -4.696  27.970 1.00 27.69 ? 41   GLY F O   1 
ATOM   5843  N  N   . LEU F  1 43  ? 65.251  -4.422  27.609 1.00 28.06 ? 42   LEU F N   1 
ATOM   5844  C  CA  . LEU F  1 43  ? 65.289  -5.201  26.374 1.00 25.87 ? 42   LEU F CA  1 
ATOM   5845  C  C   . LEU F  1 43  ? 65.336  -6.705  26.601 1.00 25.79 ? 42   LEU F C   1 
ATOM   5846  O  O   . LEU F  1 43  ? 66.002  -7.180  27.521 1.00 24.01 ? 42   LEU F O   1 
ATOM   5847  C  CB  . LEU F  1 43  ? 66.507  -4.802  25.543 1.00 25.21 ? 42   LEU F CB  1 
ATOM   5848  C  CG  . LEU F  1 43  ? 66.593  -3.374  25.008 1.00 26.65 ? 42   LEU F CG  1 
ATOM   5849  C  CD1 . LEU F  1 43  ? 67.982  -3.136  24.426 1.00 27.57 ? 42   LEU F CD1 1 
ATOM   5850  C  CD2 . LEU F  1 43  ? 65.517  -3.155  23.953 1.00 26.99 ? 42   LEU F CD2 1 
ATOM   5851  N  N   . HIS F  1 44  ? 64.641  -7.444  25.737 1.00 22.88 ? 43   HIS F N   1 
ATOM   5852  C  CA  . HIS F  1 44  ? 64.603  -8.903  25.803 1.00 21.83 ? 43   HIS F CA  1 
ATOM   5853  C  C   . HIS F  1 44  ? 64.640  -9.492  24.391 1.00 18.41 ? 43   HIS F C   1 
ATOM   5854  O  O   . HIS F  1 44  ? 63.835  -9.112  23.541 1.00 19.09 ? 43   HIS F O   1 
ATOM   5855  C  CB  . HIS F  1 44  ? 63.322  -9.366  26.513 1.00 20.73 ? 43   HIS F CB  1 
ATOM   5856  C  CG  . HIS F  1 44  ? 63.304  -9.075  27.987 1.00 21.56 ? 43   HIS F CG  1 
ATOM   5857  N  ND1 . HIS F  1 44  ? 63.864  -9.921  28.914 1.00 22.54 ? 43   HIS F ND1 1 
ATOM   5858  C  CD2 . HIS F  1 44  ? 62.812  -8.018  28.677 1.00 22.66 ? 43   HIS F CD2 1 
ATOM   5859  C  CE1 . HIS F  1 44  ? 63.720  -9.396  30.126 1.00 23.00 ? 43   HIS F CE1 1 
ATOM   5860  N  NE2 . HIS F  1 44  ? 63.086  -8.244  30.005 1.00 20.59 ? 43   HIS F NE2 1 
ATOM   5861  N  N   . GLY F  1 45  ? 65.582  -10.402 24.148 1.00 18.24 ? 44   GLY F N   1 
ATOM   5862  C  CA  . GLY F  1 45  ? 65.683  -11.049 22.842 1.00 20.04 ? 44   GLY F CA  1 
ATOM   5863  C  C   . GLY F  1 45  ? 64.331  -11.637 22.466 1.00 19.62 ? 44   GLY F C   1 
ATOM   5864  O  O   . GLY F  1 45  ? 63.595  -12.099 23.338 1.00 16.94 ? 44   GLY F O   1 
ATOM   5865  N  N   . PHE F  1 46  ? 64.015  -11.636 21.175 1.00 20.10 ? 45   PHE F N   1 
ATOM   5866  C  CA  . PHE F  1 46  ? 62.722  -12.109 20.676 1.00 20.48 ? 45   PHE F CA  1 
ATOM   5867  C  C   . PHE F  1 46  ? 62.974  -12.806 19.334 1.00 20.32 ? 45   PHE F C   1 
ATOM   5868  O  O   . PHE F  1 46  ? 63.273  -12.146 18.342 1.00 19.15 ? 45   PHE F O   1 
ATOM   5869  C  CB  . PHE F  1 46  ? 61.825  -10.873 20.506 1.00 21.45 ? 45   PHE F CB  1 
ATOM   5870  C  CG  . PHE F  1 46  ? 60.374  -11.169 20.225 1.00 22.45 ? 45   PHE F CG  1 
ATOM   5871  C  CD1 . PHE F  1 46  ? 59.599  -11.883 21.134 1.00 23.45 ? 45   PHE F CD1 1 
ATOM   5872  C  CD2 . PHE F  1 46  ? 59.756  -10.629 19.096 1.00 22.49 ? 45   PHE F CD2 1 
ATOM   5873  C  CE1 . PHE F  1 46  ? 58.220  -12.044 20.930 1.00 23.27 ? 45   PHE F CE1 1 
ATOM   5874  C  CE2 . PHE F  1 46  ? 58.384  -10.783 18.880 1.00 23.38 ? 45   PHE F CE2 1 
ATOM   5875  C  CZ  . PHE F  1 46  ? 57.614  -11.491 19.801 1.00 22.96 ? 45   PHE F CZ  1 
ATOM   5876  N  N   . HIS F  1 47  ? 62.869  -14.135 19.299 1.00 18.50 ? 46   HIS F N   1 
ATOM   5877  C  CA  . HIS F  1 47  ? 63.137  -14.859 18.054 1.00 18.53 ? 46   HIS F CA  1 
ATOM   5878  C  C   . HIS F  1 47  ? 62.237  -16.055 17.768 1.00 19.47 ? 46   HIS F C   1 
ATOM   5879  O  O   . HIS F  1 47  ? 61.570  -16.591 18.655 1.00 18.27 ? 46   HIS F O   1 
ATOM   5880  C  CB  . HIS F  1 47  ? 64.570  -15.407 18.029 1.00 18.84 ? 46   HIS F CB  1 
ATOM   5881  C  CG  . HIS F  1 47  ? 65.572  -14.565 18.753 1.00 20.16 ? 46   HIS F CG  1 
ATOM   5882  N  ND1 . HIS F  1 47  ? 66.100  -14.926 19.973 1.00 22.04 ? 46   HIS F ND1 1 
ATOM   5883  C  CD2 . HIS F  1 47  ? 66.159  -13.388 18.425 1.00 20.06 ? 46   HIS F CD2 1 
ATOM   5884  C  CE1 . HIS F  1 47  ? 66.970  -14.010 20.366 1.00 21.52 ? 46   HIS F CE1 1 
ATOM   5885  N  NE2 . HIS F  1 47  ? 67.022  -13.067 19.441 1.00 19.38 ? 46   HIS F NE2 1 
ATOM   5886  N  N   . VAL F  1 48  ? 62.242  -16.475 16.508 1.00 17.28 ? 47   VAL F N   1 
ATOM   5887  C  CA  . VAL F  1 48  ? 61.508  -17.660 16.116 1.00 17.35 ? 47   VAL F CA  1 
ATOM   5888  C  C   . VAL F  1 48  ? 62.581  -18.746 16.074 1.00 18.86 ? 47   VAL F C   1 
ATOM   5889  O  O   . VAL F  1 48  ? 63.579  -18.613 15.359 1.00 19.23 ? 47   VAL F O   1 
ATOM   5890  C  CB  . VAL F  1 48  ? 60.875  -17.530 14.707 1.00 18.06 ? 47   VAL F CB  1 
ATOM   5891  C  CG1 . VAL F  1 48  ? 60.287  -18.882 14.275 1.00 17.56 ? 47   VAL F CG1 1 
ATOM   5892  C  CG2 . VAL F  1 48  ? 59.770  -16.476 14.719 1.00 17.58 ? 47   VAL F CG2 1 
ATOM   5893  N  N   . HIS F  1 49  ? 62.404  -19.795 16.866 1.00 17.00 ? 48   HIS F N   1 
ATOM   5894  C  CA  . HIS F  1 49  ? 63.355  -20.895 16.865 1.00 18.04 ? 48   HIS F CA  1 
ATOM   5895  C  C   . HIS F  1 49  ? 62.833  -21.982 15.936 1.00 20.71 ? 48   HIS F C   1 
ATOM   5896  O  O   . HIS F  1 49  ? 61.629  -22.065 15.673 1.00 21.22 ? 48   HIS F O   1 
ATOM   5897  C  CB  . HIS F  1 49  ? 63.582  -21.421 18.281 1.00 16.29 ? 48   HIS F CB  1 
ATOM   5898  C  CG  . HIS F  1 49  ? 64.387  -20.487 19.135 1.00 18.20 ? 48   HIS F CG  1 
ATOM   5899  N  ND1 . HIS F  1 49  ? 65.527  -20.875 19.791 1.00 18.07 ? 48   HIS F ND1 1 
ATOM   5900  C  CD2 . HIS F  1 49  ? 64.213  -19.171 19.411 1.00 16.21 ? 48   HIS F CD2 1 
ATOM   5901  C  CE1 . HIS F  1 49  ? 66.031  -19.837 20.448 1.00 16.58 ? 48   HIS F CE1 1 
ATOM   5902  N  NE2 . HIS F  1 49  ? 65.250  -18.798 20.233 1.00 17.05 ? 48   HIS F NE2 1 
ATOM   5903  N  N   . GLU F  1 50  ? 63.754  -22.806 15.451 1.00 20.46 ? 49   GLU F N   1 
ATOM   5904  C  CA  . GLU F  1 50  ? 63.475  -23.853 14.477 1.00 21.22 ? 49   GLU F CA  1 
ATOM   5905  C  C   . GLU F  1 50  ? 62.367  -24.877 14.712 1.00 19.84 ? 49   GLU F C   1 
ATOM   5906  O  O   . GLU F  1 50  ? 61.573  -25.135 13.811 1.00 21.89 ? 49   GLU F O   1 
ATOM   5907  C  CB  . GLU F  1 50  ? 64.773  -24.606 14.168 1.00 21.68 ? 49   GLU F CB  1 
ATOM   5908  C  CG  . GLU F  1 50  ? 64.662  -25.535 12.968 1.00 21.34 ? 49   GLU F CG  1 
ATOM   5909  C  CD  . GLU F  1 50  ? 65.976  -26.216 12.630 1.00 23.91 ? 49   GLU F CD  1 
ATOM   5910  O  OE1 . GLU F  1 50  ? 66.033  -26.926 11.608 1.00 25.39 ? 49   GLU F OE1 1 
ATOM   5911  O  OE2 . GLU F  1 50  ? 66.948  -26.048 13.393 1.00 24.31 ? 49   GLU F OE2 1 
ATOM   5912  N  N   . PHE F  1 51  ? 62.315  -25.465 15.900 1.00 20.73 ? 50   PHE F N   1 
ATOM   5913  C  CA  . PHE F  1 51  ? 61.324  -26.500 16.178 1.00 20.70 ? 50   PHE F CA  1 
ATOM   5914  C  C   . PHE F  1 51  ? 60.182  -26.112 17.103 1.00 21.20 ? 50   PHE F C   1 
ATOM   5915  O  O   . PHE F  1 51  ? 60.393  -25.461 18.132 1.00 19.23 ? 50   PHE F O   1 
ATOM   5916  C  CB  . PHE F  1 51  ? 62.036  -27.726 16.753 1.00 22.43 ? 50   PHE F CB  1 
ATOM   5917  C  CG  . PHE F  1 51  ? 63.231  -28.155 15.951 1.00 24.70 ? 50   PHE F CG  1 
ATOM   5918  C  CD1 . PHE F  1 51  ? 63.095  -28.493 14.605 1.00 26.83 ? 50   PHE F CD1 1 
ATOM   5919  C  CD2 . PHE F  1 51  ? 64.495  -28.190 16.530 1.00 24.91 ? 50   PHE F CD2 1 
ATOM   5920  C  CE1 . PHE F  1 51  ? 64.209  -28.860 13.842 1.00 28.97 ? 50   PHE F CE1 1 
ATOM   5921  C  CE2 . PHE F  1 51  ? 65.616  -28.556 15.779 1.00 27.65 ? 50   PHE F CE2 1 
ATOM   5922  C  CZ  . PHE F  1 51  ? 65.472  -28.890 14.432 1.00 28.35 ? 50   PHE F CZ  1 
ATOM   5923  N  N   . GLY F  1 52  ? 58.973  -26.533 16.730 1.00 20.05 ? 51   GLY F N   1 
ATOM   5924  C  CA  . GLY F  1 52  ? 57.796  -26.271 17.544 1.00 19.32 ? 51   GLY F CA  1 
ATOM   5925  C  C   . GLY F  1 52  ? 57.665  -27.466 18.470 1.00 20.54 ? 51   GLY F C   1 
ATOM   5926  O  O   . GLY F  1 52  ? 56.625  -28.127 18.545 1.00 21.25 ? 51   GLY F O   1 
ATOM   5927  N  N   . ASP F  1 53  ? 58.748  -27.737 19.182 1.00 21.45 ? 52   ASP F N   1 
ATOM   5928  C  CA  . ASP F  1 53  ? 58.834  -28.879 20.088 1.00 21.64 ? 52   ASP F CA  1 
ATOM   5929  C  C   . ASP F  1 53  ? 59.030  -28.420 21.519 1.00 22.64 ? 52   ASP F C   1 
ATOM   5930  O  O   . ASP F  1 53  ? 60.083  -27.882 21.873 1.00 20.95 ? 52   ASP F O   1 
ATOM   5931  C  CB  . ASP F  1 53  ? 60.002  -29.759 19.639 1.00 22.48 ? 52   ASP F CB  1 
ATOM   5932  C  CG  . ASP F  1 53  ? 60.216  -30.974 20.522 1.00 23.94 ? 52   ASP F CG  1 
ATOM   5933  O  OD1 . ASP F  1 53  ? 60.909  -31.897 20.051 1.00 25.87 ? 52   ASP F OD1 1 
ATOM   5934  O  OD2 . ASP F  1 53  ? 59.720  -31.011 21.669 1.00 27.14 ? 52   ASP F OD2 1 
ATOM   5935  N  N   . ASN F  1 54  ? 58.018  -28.649 22.344 1.00 22.10 ? 53   ASN F N   1 
ATOM   5936  C  CA  . ASN F  1 54  ? 58.077  -28.247 23.740 1.00 24.17 ? 53   ASN F CA  1 
ATOM   5937  C  C   . ASN F  1 54  ? 58.160  -29.439 24.700 1.00 24.87 ? 53   ASN F C   1 
ATOM   5938  O  O   . ASN F  1 54  ? 57.769  -29.326 25.859 1.00 24.67 ? 53   ASN F O   1 
ATOM   5939  C  CB  . ASN F  1 54  ? 56.845  -27.408 24.073 1.00 25.82 ? 53   ASN F CB  1 
ATOM   5940  C  CG  . ASN F  1 54  ? 57.000  -26.632 25.366 1.00 30.71 ? 53   ASN F CG  1 
ATOM   5941  O  OD1 . ASN F  1 54  ? 56.102  -26.616 26.204 1.00 31.29 ? 53   ASN F OD1 1 
ATOM   5942  N  ND2 . ASN F  1 54  ? 58.140  -25.972 25.526 1.00 30.65 ? 53   ASN F ND2 1 
ATOM   5943  N  N   . THR F  1 55  ? 58.679  -30.572 24.229 1.00 23.74 ? 54   THR F N   1 
ATOM   5944  C  CA  . THR F  1 55  ? 58.773  -31.762 25.079 1.00 26.72 ? 54   THR F CA  1 
ATOM   5945  C  C   . THR F  1 55  ? 59.665  -31.556 26.297 1.00 28.38 ? 54   THR F C   1 
ATOM   5946  O  O   . THR F  1 55  ? 59.461  -32.182 27.332 1.00 27.98 ? 54   THR F O   1 
ATOM   5947  C  CB  . THR F  1 55  ? 59.284  -32.990 24.292 1.00 25.95 ? 54   THR F CB  1 
ATOM   5948  O  OG1 . THR F  1 55  ? 60.533  -32.677 23.676 1.00 27.29 ? 54   THR F OG1 1 
ATOM   5949  C  CG2 . THR F  1 55  ? 58.283  -33.389 23.215 1.00 25.92 ? 54   THR F CG2 1 
ATOM   5950  N  N   . ALA F  1 56  ? 60.658  -30.683 26.174 1.00 28.98 ? 55   ALA F N   1 
ATOM   5951  C  CA  . ALA F  1 56  ? 61.546  -30.400 27.296 1.00 31.33 ? 55   ALA F CA  1 
ATOM   5952  C  C   . ALA F  1 56  ? 61.558  -28.895 27.551 1.00 31.19 ? 55   ALA F C   1 
ATOM   5953  O  O   . ALA F  1 56  ? 62.613  -28.296 27.726 1.00 33.28 ? 55   ALA F O   1 
ATOM   5954  C  CB  . ALA F  1 56  ? 62.957  -30.894 26.991 1.00 30.89 ? 55   ALA F CB  1 
ATOM   5955  N  N   . GLY F  1 57  ? 60.378  -28.289 27.572 1.00 29.99 ? 56   GLY F N   1 
ATOM   5956  C  CA  . GLY F  1 57  ? 60.302  -26.855 27.787 1.00 29.30 ? 56   GLY F CA  1 
ATOM   5957  C  C   . GLY F  1 57  ? 60.829  -26.103 26.572 1.00 28.86 ? 56   GLY F C   1 
ATOM   5958  O  O   . GLY F  1 57  ? 60.899  -26.656 25.473 1.00 29.59 ? 56   GLY F O   1 
ATOM   5959  N  N   . CYS F  1 58  ? 61.225  -24.849 26.766 1.00 27.03 ? 57   CYS F N   1 
ATOM   5960  C  CA  . CYS F  1 58  ? 61.724  -24.039 25.658 1.00 24.91 ? 57   CYS F CA  1 
ATOM   5961  C  C   . CYS F  1 58  ? 63.043  -24.529 25.077 1.00 22.91 ? 57   CYS F C   1 
ATOM   5962  O  O   . CYS F  1 58  ? 63.389  -24.187 23.951 1.00 21.43 ? 57   CYS F O   1 
ATOM   5963  C  CB  . CYS F  1 58  ? 61.847  -22.575 26.097 1.00 22.72 ? 57   CYS F CB  1 
ATOM   5964  S  SG  . CYS F  1 58  ? 60.256  -21.906 26.676 1.00 23.88 ? 57   CYS F SG  1 
ATOM   5965  N  N   . THR F  1 59  ? 63.767  -25.345 25.836 1.00 22.83 ? 58   THR F N   1 
ATOM   5966  C  CA  . THR F  1 59  ? 65.050  -25.872 25.384 1.00 23.84 ? 58   THR F CA  1 
ATOM   5967  C  C   . THR F  1 59  ? 64.939  -26.730 24.123 1.00 23.47 ? 58   THR F C   1 
ATOM   5968  O  O   . THR F  1 59  ? 65.814  -26.685 23.258 1.00 24.45 ? 58   THR F O   1 
ATOM   5969  C  CB  . THR F  1 59  ? 65.725  -26.718 26.492 1.00 27.78 ? 58   THR F CB  1 
ATOM   5970  O  OG1 . THR F  1 59  ? 65.869  -25.926 27.680 1.00 32.72 ? 58   THR F OG1 1 
ATOM   5971  C  CG2 . THR F  1 59  ? 67.100  -27.190 26.041 1.00 27.06 ? 58   THR F CG2 1 
ATOM   5972  N  N   . SER F  1 60  ? 63.869  -27.510 24.008 1.00 22.84 ? 59   SER F N   1 
ATOM   5973  C  CA  . SER F  1 60  ? 63.703  -28.369 22.841 1.00 22.98 ? 59   SER F CA  1 
ATOM   5974  C  C   . SER F  1 60  ? 63.323  -27.654 21.535 1.00 22.69 ? 59   SER F C   1 
ATOM   5975  O  O   . SER F  1 60  ? 63.228  -28.288 20.482 1.00 23.10 ? 59   SER F O   1 
ATOM   5976  C  CB  . SER F  1 60  ? 62.704  -29.495 23.155 1.00 24.77 ? 59   SER F CB  1 
ATOM   5977  O  OG  . SER F  1 60  ? 61.633  -29.036 23.953 1.00 29.75 ? 59   SER F OG  1 
ATOM   5978  N  N   . ALA F  1 61  ? 63.122  -26.340 21.590 1.00 20.21 ? 60   ALA F N   1 
ATOM   5979  C  CA  . ALA F  1 61  ? 62.788  -25.591 20.386 1.00 19.91 ? 60   ALA F CA  1 
ATOM   5980  C  C   . ALA F  1 61  ? 64.007  -25.475 19.459 1.00 21.26 ? 60   ALA F C   1 
ATOM   5981  O  O   . ALA F  1 61  ? 63.894  -25.016 18.327 1.00 19.99 ? 60   ALA F O   1 
ATOM   5982  C  CB  . ALA F  1 61  ? 62.280  -24.205 20.750 1.00 19.85 ? 60   ALA F CB  1 
ATOM   5983  N  N   . GLY F  1 62  ? 65.172  -25.892 19.940 1.00 21.67 ? 61   GLY F N   1 
ATOM   5984  C  CA  . GLY F  1 62  ? 66.366  -25.818 19.115 1.00 23.30 ? 61   GLY F CA  1 
ATOM   5985  C  C   . GLY F  1 62  ? 66.890  -24.402 18.915 1.00 24.47 ? 61   GLY F C   1 
ATOM   5986  O  O   . GLY F  1 62  ? 66.507  -23.482 19.642 1.00 23.78 ? 61   GLY F O   1 
ATOM   5987  N  N   . PRO F  1 63  ? 67.771  -24.197 17.923 1.00 25.57 ? 62   PRO F N   1 
ATOM   5988  C  CA  . PRO F  1 63  ? 68.354  -22.885 17.629 1.00 25.71 ? 62   PRO F CA  1 
ATOM   5989  C  C   . PRO F  1 63  ? 67.416  -21.980 16.844 1.00 24.80 ? 62   PRO F C   1 
ATOM   5990  O  O   . PRO F  1 63  ? 66.276  -22.347 16.556 1.00 24.43 ? 62   PRO F O   1 
ATOM   5991  C  CB  . PRO F  1 63  ? 69.608  -23.246 16.845 1.00 26.52 ? 62   PRO F CB  1 
ATOM   5992  C  CG  . PRO F  1 63  ? 69.132  -24.412 16.024 1.00 27.87 ? 62   PRO F CG  1 
ATOM   5993  C  CD  . PRO F  1 63  ? 68.335  -25.233 17.035 1.00 26.72 ? 62   PRO F CD  1 
ATOM   5994  N  N   . HIS F  1 64  ? 67.895  -20.792 16.499 1.00 22.18 ? 63   HIS F N   1 
ATOM   5995  C  CA  . HIS F  1 64  ? 67.079  -19.859 15.738 1.00 22.18 ? 63   HIS F CA  1 
ATOM   5996  C  C   . HIS F  1 64  ? 66.760  -20.445 14.361 1.00 21.47 ? 63   HIS F C   1 
ATOM   5997  O  O   . HIS F  1 64  ? 67.596  -21.121 13.753 1.00 20.29 ? 63   HIS F O   1 
ATOM   5998  C  CB  . HIS F  1 64  ? 67.806  -18.510 15.583 1.00 22.79 ? 63   HIS F CB  1 
ATOM   5999  C  CG  . HIS F  1 64  ? 68.027  -17.788 16.880 1.00 21.81 ? 63   HIS F CG  1 
ATOM   6000  N  ND1 . HIS F  1 64  ? 68.633  -16.557 16.953 1.00 21.39 ? 63   HIS F ND1 1 
ATOM   6001  C  CD2 . HIS F  1 64  ? 67.719  -18.137 18.155 1.00 23.90 ? 63   HIS F CD2 1 
ATOM   6002  C  CE1 . HIS F  1 64  ? 68.693  -16.172 18.221 1.00 20.07 ? 63   HIS F CE1 1 
ATOM   6003  N  NE2 . HIS F  1 64  ? 68.146  -17.111 18.963 1.00 26.20 ? 63   HIS F NE2 1 
ATOM   6004  N  N   . PHE F  1 65  ? 65.540  -20.206 13.885 1.00 21.72 ? 64   PHE F N   1 
ATOM   6005  C  CA  . PHE F  1 65  ? 65.115  -20.690 12.570 1.00 22.73 ? 64   PHE F CA  1 
ATOM   6006  C  C   . PHE F  1 65  ? 66.095  -20.071 11.570 1.00 25.49 ? 64   PHE F C   1 
ATOM   6007  O  O   . PHE F  1 65  ? 66.106  -18.858 11.376 1.00 24.14 ? 64   PHE F O   1 
ATOM   6008  C  CB  . PHE F  1 65  ? 63.691  -20.216 12.280 1.00 22.06 ? 64   PHE F CB  1 
ATOM   6009  C  CG  . PHE F  1 65  ? 63.154  -20.667 10.950 1.00 20.47 ? 64   PHE F CG  1 
ATOM   6010  C  CD1 . PHE F  1 65  ? 62.299  -19.846 10.224 1.00 23.11 ? 64   PHE F CD1 1 
ATOM   6011  C  CD2 . PHE F  1 65  ? 63.500  -21.908 10.425 1.00 22.88 ? 64   PHE F CD2 1 
ATOM   6012  C  CE1 . PHE F  1 65  ? 61.790  -20.251 8.984  1.00 23.52 ? 64   PHE F CE1 1 
ATOM   6013  C  CE2 . PHE F  1 65  ? 62.999  -22.324 9.191  1.00 22.83 ? 64   PHE F CE2 1 
ATOM   6014  C  CZ  . PHE F  1 65  ? 62.144  -21.491 8.470  1.00 24.94 ? 64   PHE F CZ  1 
ATOM   6015  N  N   . ASN F  1 66  ? 66.904  -20.907 10.931 1.00 27.27 ? 65   ASN F N   1 
ATOM   6016  C  CA  . ASN F  1 66  ? 67.928  -20.412 10.018 1.00 29.14 ? 65   ASN F CA  1 
ATOM   6017  C  C   . ASN F  1 66  ? 68.063  -21.254 8.746  1.00 31.03 ? 65   ASN F C   1 
ATOM   6018  O  O   . ASN F  1 66  ? 69.078  -21.913 8.529  1.00 31.82 ? 65   ASN F O   1 
ATOM   6019  C  CB  . ASN F  1 66  ? 69.255  -20.373 10.793 1.00 26.60 ? 65   ASN F CB  1 
ATOM   6020  C  CG  . ASN F  1 66  ? 70.400  -19.783 9.994  1.00 29.85 ? 65   ASN F CG  1 
ATOM   6021  O  OD1 . ASN F  1 66  ? 70.216  -18.848 9.214  1.00 28.95 ? 65   ASN F OD1 1 
ATOM   6022  N  ND2 . ASN F  1 66  ? 71.603  -20.315 10.210 1.00 28.40 ? 65   ASN F ND2 1 
ATOM   6023  N  N   . PRO F  1 67  ? 67.038  -21.237 7.883  1.00 32.58 ? 66   PRO F N   1 
ATOM   6024  C  CA  . PRO F  1 67  ? 67.104  -22.023 6.650  1.00 35.78 ? 66   PRO F CA  1 
ATOM   6025  C  C   . PRO F  1 67  ? 68.207  -21.608 5.674  1.00 38.67 ? 66   PRO F C   1 
ATOM   6026  O  O   . PRO F  1 67  ? 68.696  -22.435 4.907  1.00 39.24 ? 66   PRO F O   1 
ATOM   6027  C  CB  . PRO F  1 67  ? 65.706  -21.853 6.057  1.00 35.79 ? 66   PRO F CB  1 
ATOM   6028  C  CG  . PRO F  1 67  ? 65.298  -20.498 6.539  1.00 34.49 ? 66   PRO F CG  1 
ATOM   6029  C  CD  . PRO F  1 67  ? 65.754  -20.523 7.981  1.00 31.87 ? 66   PRO F CD  1 
ATOM   6030  N  N   . LEU F  1 68  ? 68.611  -20.341 5.704  1.00 39.10 ? 67   LEU F N   1 
ATOM   6031  C  CA  . LEU F  1 68  ? 69.650  -19.881 4.787  1.00 40.08 ? 67   LEU F CA  1 
ATOM   6032  C  C   . LEU F  1 68  ? 71.056  -20.002 5.364  1.00 40.80 ? 67   LEU F C   1 
ATOM   6033  O  O   . LEU F  1 68  ? 72.011  -19.449 4.818  1.00 41.66 ? 67   LEU F O   1 
ATOM   6034  C  CB  . LEU F  1 68  ? 69.377  -18.438 4.361  1.00 40.50 ? 67   LEU F CB  1 
ATOM   6035  C  CG  . LEU F  1 68  ? 67.985  -18.193 3.765  1.00 41.46 ? 67   LEU F CG  1 
ATOM   6036  C  CD1 . LEU F  1 68  ? 67.912  -16.789 3.203  1.00 42.14 ? 67   LEU F CD1 1 
ATOM   6037  C  CD2 . LEU F  1 68  ? 67.700  -19.206 2.668  1.00 43.76 ? 67   LEU F CD2 1 
ATOM   6038  N  N   . SER F  1 69  ? 71.173  -20.736 6.465  1.00 40.13 ? 68   SER F N   1 
ATOM   6039  C  CA  . SER F  1 69  ? 72.454  -20.961 7.127  1.00 40.86 ? 68   SER F CA  1 
ATOM   6040  C  C   . SER F  1 69  ? 73.333  -19.717 7.226  1.00 40.11 ? 68   SER F C   1 
ATOM   6041  O  O   . SER F  1 69  ? 74.452  -19.698 6.713  1.00 39.23 ? 68   SER F O   1 
ATOM   6042  C  CB  . SER F  1 69  ? 73.226  -22.066 6.402  1.00 41.53 ? 68   SER F CB  1 
ATOM   6043  O  OG  . SER F  1 69  ? 72.517  -23.292 6.432  1.00 44.75 ? 68   SER F OG  1 
ATOM   6044  N  N   . ARG F  1 70  ? 72.835  -18.684 7.894  1.00 38.65 ? 69   ARG F N   1 
ATOM   6045  C  CA  . ARG F  1 70  ? 73.597  -17.454 8.047  1.00 37.65 ? 69   ARG F CA  1 
ATOM   6046  C  C   . ARG F  1 70  ? 73.924  -17.183 9.504  1.00 35.85 ? 69   ARG F C   1 
ATOM   6047  O  O   . ARG F  1 70  ? 73.592  -17.979 10.382 1.00 35.65 ? 69   ARG F O   1 
ATOM   6048  C  CB  . ARG F  1 70  ? 72.825  -16.279 7.450  1.00 38.98 ? 69   ARG F CB  1 
ATOM   6049  C  CG  . ARG F  1 70  ? 72.722  -16.346 5.933  1.00 44.11 ? 69   ARG F CG  1 
ATOM   6050  C  CD  . ARG F  1 70  ? 71.917  -15.192 5.363  1.00 47.21 ? 69   ARG F CD  1 
ATOM   6051  N  NE  . ARG F  1 70  ? 71.905  -15.219 3.903  1.00 50.28 ? 69   ARG F NE  1 
ATOM   6052  C  CZ  . ARG F  1 70  ? 71.206  -14.381 3.143  1.00 52.08 ? 69   ARG F CZ  1 
ATOM   6053  N  NH1 . ARG F  1 70  ? 71.261  -14.485 1.821  1.00 52.69 ? 69   ARG F NH1 1 
ATOM   6054  N  NH2 . ARG F  1 70  ? 70.450  -13.442 3.698  1.00 52.40 ? 69   ARG F NH2 1 
ATOM   6055  N  N   . LYS F  1 71  ? 74.595  -16.065 9.754  1.00 33.50 ? 70   LYS F N   1 
ATOM   6056  C  CA  . LYS F  1 71  ? 74.969  -15.692 11.108 1.00 31.02 ? 70   LYS F CA  1 
ATOM   6057  C  C   . LYS F  1 71  ? 73.836  -14.905 11.741 1.00 27.63 ? 70   LYS F C   1 
ATOM   6058  O  O   . LYS F  1 71  ? 72.990  -14.346 11.045 1.00 24.48 ? 70   LYS F O   1 
ATOM   6059  C  CB  . LYS F  1 71  ? 76.243  -14.838 11.097 1.00 32.76 ? 70   LYS F CB  1 
ATOM   6060  C  CG  . LYS F  1 71  ? 77.500  -15.568 10.634 1.00 36.75 ? 70   LYS F CG  1 
ATOM   6061  C  CD  . LYS F  1 71  ? 77.870  -16.700 11.579 1.00 40.65 ? 70   LYS F CD  1 
ATOM   6062  C  CE  . LYS F  1 71  ? 79.180  -17.364 11.168 1.00 42.41 ? 70   LYS F CE  1 
ATOM   6063  N  NZ  . LYS F  1 71  ? 80.308  -16.393 11.142 0.00 41.95 ? 70   LYS F NZ  1 
ATOM   6064  N  N   . HIS F  1 72  ? 73.826  -14.864 13.068 1.00 27.20 ? 71   HIS F N   1 
ATOM   6065  C  CA  . HIS F  1 72  ? 72.799  -14.130 13.788 1.00 25.17 ? 71   HIS F CA  1 
ATOM   6066  C  C   . HIS F  1 72  ? 72.967  -12.629 13.551 1.00 26.07 ? 71   HIS F C   1 
ATOM   6067  O  O   . HIS F  1 72  ? 74.086  -12.121 13.457 1.00 26.85 ? 71   HIS F O   1 
ATOM   6068  C  CB  . HIS F  1 72  ? 72.900  -14.423 15.283 1.00 20.40 ? 71   HIS F CB  1 
ATOM   6069  C  CG  . HIS F  1 72  ? 71.916  -13.660 16.113 1.00 19.93 ? 71   HIS F CG  1 
ATOM   6070  N  ND1 . HIS F  1 72  ? 70.588  -14.024 16.220 1.00 21.96 ? 71   HIS F ND1 1 
ATOM   6071  C  CD2 . HIS F  1 72  ? 72.057  -12.541 16.862 1.00 19.00 ? 71   HIS F CD2 1 
ATOM   6072  C  CE1 . HIS F  1 72  ? 69.959  -13.163 16.996 1.00 21.17 ? 71   HIS F CE1 1 
ATOM   6073  N  NE2 . HIS F  1 72  ? 70.825  -12.251 17.400 1.00 20.18 ? 71   HIS F NE2 1 
ATOM   6074  N  N   . GLY F  1 73  ? 71.851  -11.920 13.457 1.00 25.42 ? 72   GLY F N   1 
ATOM   6075  C  CA  . GLY F  1 73  ? 71.909  -10.487 13.252 1.00 23.40 ? 72   GLY F CA  1 
ATOM   6076  C  C   . GLY F  1 73  ? 70.650  -9.848  13.788 1.00 24.30 ? 72   GLY F C   1 
ATOM   6077  O  O   . GLY F  1 73  ? 69.880  -10.489 14.505 1.00 22.86 ? 72   GLY F O   1 
ATOM   6078  N  N   . GLY F  1 74  ? 70.443  -8.582  13.453 1.00 22.40 ? 73   GLY F N   1 
ATOM   6079  C  CA  . GLY F  1 74  ? 69.250  -7.892  13.891 1.00 23.05 ? 73   GLY F CA  1 
ATOM   6080  C  C   . GLY F  1 74  ? 68.271  -7.930  12.733 1.00 22.56 ? 73   GLY F C   1 
ATOM   6081  O  O   . GLY F  1 74  ? 68.690  -8.142  11.597 1.00 21.99 ? 73   GLY F O   1 
ATOM   6082  N  N   . PRO F  1 75  ? 66.972  -7.714  12.975 1.00 22.69 ? 74   PRO F N   1 
ATOM   6083  C  CA  . PRO F  1 75  ? 65.984  -7.748  11.891 1.00 24.09 ? 74   PRO F CA  1 
ATOM   6084  C  C   . PRO F  1 75  ? 66.302  -6.885  10.668 1.00 27.06 ? 74   PRO F C   1 
ATOM   6085  O  O   . PRO F  1 75  ? 65.898  -7.215  9.556  1.00 24.04 ? 74   PRO F O   1 
ATOM   6086  C  CB  . PRO F  1 75  ? 64.689  -7.323  12.586 1.00 23.16 ? 74   PRO F CB  1 
ATOM   6087  C  CG  . PRO F  1 75  ? 65.169  -6.484  13.743 1.00 23.67 ? 74   PRO F CG  1 
ATOM   6088  C  CD  . PRO F  1 75  ? 66.356  -7.266  14.235 1.00 22.04 ? 74   PRO F CD  1 
ATOM   6089  N  N   . LYS F  1 76  ? 67.030  -5.790  10.863 1.00 29.83 ? 75   LYS F N   1 
ATOM   6090  C  CA  . LYS F  1 76  ? 67.360  -4.913  9.743  1.00 32.92 ? 75   LYS F CA  1 
ATOM   6091  C  C   . LYS F  1 76  ? 68.561  -5.349  8.907  1.00 33.45 ? 75   LYS F C   1 
ATOM   6092  O  O   . LYS F  1 76  ? 68.756  -4.850  7.801  1.00 33.76 ? 75   LYS F O   1 
ATOM   6093  C  CB  . LYS F  1 76  ? 67.577  -3.483  10.237 1.00 34.97 ? 75   LYS F CB  1 
ATOM   6094  C  CG  . LYS F  1 76  ? 66.335  -2.854  10.844 1.00 37.82 ? 75   LYS F CG  1 
ATOM   6095  C  CD  . LYS F  1 76  ? 66.440  -1.335  10.885 1.00 43.89 ? 75   LYS F CD  1 
ATOM   6096  C  CE  . LYS F  1 76  ? 67.574  -0.860  11.771 1.00 43.96 ? 75   LYS F CE  1 
ATOM   6097  N  NZ  . LYS F  1 76  ? 67.751  0.619   11.667 1.00 43.90 ? 75   LYS F NZ  1 
ATOM   6098  N  N   . ASP F  1 77  ? 69.361  -6.275  9.426  1.00 31.65 ? 76   ASP F N   1 
ATOM   6099  C  CA  . ASP F  1 77  ? 70.537  -6.759  8.703  1.00 32.10 ? 76   ASP F CA  1 
ATOM   6100  C  C   . ASP F  1 77  ? 70.178  -7.708  7.570  1.00 32.53 ? 76   ASP F C   1 
ATOM   6101  O  O   . ASP F  1 77  ? 69.137  -8.363  7.606  1.00 29.84 ? 76   ASP F O   1 
ATOM   6102  C  CB  . ASP F  1 77  ? 71.476  -7.501  9.651  1.00 33.23 ? 76   ASP F CB  1 
ATOM   6103  C  CG  . ASP F  1 77  ? 71.959  -6.636  10.783 1.00 35.76 ? 76   ASP F CG  1 
ATOM   6104  O  OD1 . ASP F  1 77  ? 72.413  -7.201  11.799 1.00 35.46 ? 76   ASP F OD1 1 
ATOM   6105  O  OD2 . ASP F  1 77  ? 71.891  -5.396  10.651 1.00 38.56 ? 76   ASP F OD2 1 
ATOM   6106  N  N   . GLU F  1 78  ? 71.053  -7.789  6.571  1.00 30.66 ? 77   GLU F N   1 
ATOM   6107  C  CA  . GLU F  1 78  ? 70.831  -8.694  5.450  1.00 31.55 ? 77   GLU F CA  1 
ATOM   6108  C  C   . GLU F  1 78  ? 71.353  -10.031 5.957  1.00 30.74 ? 77   GLU F C   1 
ATOM   6109  O  O   . GLU F  1 78  ? 70.790  -11.087 5.671  1.00 32.37 ? 77   GLU F O   1 
ATOM   6110  C  CB  . GLU F  1 78  ? 71.619  -8.234  4.219  1.00 31.98 ? 77   GLU F CB  1 
ATOM   6111  C  CG  . GLU F  1 78  ? 71.005  -8.665  2.888  1.00 36.46 ? 77   GLU F CG  1 
ATOM   6112  C  CD  . GLU F  1 78  ? 71.134  -10.152 2.617  0.00 35.91 ? 77   GLU F CD  1 
ATOM   6113  O  OE1 . GLU F  1 78  ? 70.558  -10.623 1.614  0.00 36.56 ? 77   GLU F OE1 1 
ATOM   6114  O  OE2 . GLU F  1 78  ? 71.813  -10.850 3.397  0.00 36.56 ? 77   GLU F OE2 1 
ATOM   6115  N  N   . GLU F  1 79  ? 72.436  -9.974  6.724  1.00 29.36 ? 78   GLU F N   1 
ATOM   6116  C  CA  . GLU F  1 79  ? 73.009  -11.177 7.310  1.00 30.03 ? 78   GLU F CA  1 
ATOM   6117  C  C   . GLU F  1 79  ? 72.286  -11.401 8.646  1.00 28.47 ? 78   GLU F C   1 
ATOM   6118  O  O   . GLU F  1 79  ? 72.593  -10.757 9.650  1.00 28.30 ? 78   GLU F O   1 
ATOM   6119  C  CB  . GLU F  1 79  ? 74.514  -11.002 7.541  1.00 29.27 ? 78   GLU F CB  1 
ATOM   6120  C  CG  . GLU F  1 79  ? 75.226  -12.245 8.083  1.00 32.51 ? 78   GLU F CG  1 
ATOM   6121  C  CD  . GLU F  1 79  ? 75.298  -13.395 7.079  1.00 35.04 ? 78   GLU F CD  1 
ATOM   6122  O  OE1 . GLU F  1 79  ? 75.772  -14.491 7.459  1.00 34.84 ? 78   GLU F OE1 1 
ATOM   6123  O  OE2 . GLU F  1 79  ? 74.890  -13.208 5.913  1.00 35.36 ? 78   GLU F OE2 1 
ATOM   6124  N  N   . ARG F  1 80  ? 71.315  -12.309 8.645  1.00 27.60 ? 79   ARG F N   1 
ATOM   6125  C  CA  . ARG F  1 80  ? 70.544  -12.613 9.852  1.00 26.65 ? 79   ARG F CA  1 
ATOM   6126  C  C   . ARG F  1 80  ? 69.839  -13.951 9.687  1.00 27.15 ? 79   ARG F C   1 
ATOM   6127  O  O   . ARG F  1 80  ? 69.747  -14.479 8.577  1.00 26.31 ? 79   ARG F O   1 
ATOM   6128  C  CB  . ARG F  1 80  ? 69.477  -11.540 10.084 1.00 27.23 ? 79   ARG F CB  1 
ATOM   6129  C  CG  . ARG F  1 80  ? 68.433  -11.460 8.962  1.00 28.07 ? 79   ARG F CG  1 
ATOM   6130  C  CD  . ARG F  1 80  ? 67.024  -11.770 9.466  1.00 35.25 ? 79   ARG F CD  1 
ATOM   6131  N  NE  . ARG F  1 80  ? 66.176  -10.591 9.440  1.00 31.77 ? 79   ARG F NE  1 
ATOM   6132  C  CZ  . ARG F  1 80  ? 64.890  -10.568 9.768  1.00 29.32 ? 79   ARG F CZ  1 
ATOM   6133  N  NH1 . ARG F  1 80  ? 64.225  -9.421  9.697  1.00 25.53 ? 79   ARG F NH1 1 
ATOM   6134  N  NH2 . ARG F  1 80  ? 64.267  -11.672 10.168 1.00 27.43 ? 79   ARG F NH2 1 
ATOM   6135  N  N   . HIS F  1 81  ? 69.360  -14.501 10.800 1.00 23.99 ? 80   HIS F N   1 
ATOM   6136  C  CA  . HIS F  1 81  ? 68.601  -15.744 10.767 1.00 23.19 ? 80   HIS F CA  1 
ATOM   6137  C  C   . HIS F  1 81  ? 67.202  -15.281 10.391 1.00 22.36 ? 80   HIS F C   1 
ATOM   6138  O  O   . HIS F  1 81  ? 66.806  -14.166 10.743 1.00 21.26 ? 80   HIS F O   1 
ATOM   6139  C  CB  . HIS F  1 81  ? 68.546  -16.388 12.161 1.00 21.48 ? 80   HIS F CB  1 
ATOM   6140  C  CG  . HIS F  1 81  ? 69.872  -16.879 12.661 1.00 22.57 ? 80   HIS F CG  1 
ATOM   6141  N  ND1 . HIS F  1 81  ? 70.199  -16.893 14.000 1.00 21.35 ? 80   HIS F ND1 1 
ATOM   6142  C  CD2 . HIS F  1 81  ? 70.925  -17.418 12.009 1.00 23.14 ? 80   HIS F CD2 1 
ATOM   6143  C  CE1 . HIS F  1 81  ? 71.401  -17.423 14.150 1.00 24.22 ? 80   HIS F CE1 1 
ATOM   6144  N  NE2 . HIS F  1 81  ? 71.863  -17.751 12.955 1.00 23.42 ? 80   HIS F NE2 1 
ATOM   6145  N  N   . VAL F  1 82  ? 66.445  -16.112 9.682  1.00 21.74 ? 81   VAL F N   1 
ATOM   6146  C  CA  . VAL F  1 82  ? 65.083  -15.719 9.326  1.00 20.33 ? 81   VAL F CA  1 
ATOM   6147  C  C   . VAL F  1 82  ? 64.295  -15.418 10.604 1.00 18.58 ? 81   VAL F C   1 
ATOM   6148  O  O   . VAL F  1 82  ? 63.466  -14.513 10.641 1.00 20.09 ? 81   VAL F O   1 
ATOM   6149  C  CB  . VAL F  1 82  ? 64.343  -16.840 8.544  1.00 21.62 ? 81   VAL F CB  1 
ATOM   6150  C  CG1 . VAL F  1 82  ? 62.849  -16.537 8.486  1.00 21.65 ? 81   VAL F CG1 1 
ATOM   6151  C  CG2 . VAL F  1 82  ? 64.901  -16.948 7.128  1.00 21.82 ? 81   VAL F CG2 1 
ATOM   6152  N  N   . GLY F  1 83  ? 64.568  -16.174 11.659 1.00 19.51 ? 82   GLY F N   1 
ATOM   6153  C  CA  . GLY F  1 83  ? 63.852  -15.974 12.908 1.00 19.71 ? 82   GLY F CA  1 
ATOM   6154  C  C   . GLY F  1 83  ? 64.310  -14.819 13.788 1.00 20.77 ? 82   GLY F C   1 
ATOM   6155  O  O   . GLY F  1 83  ? 63.790  -14.655 14.898 1.00 20.13 ? 82   GLY F O   1 
ATOM   6156  N  N   . ASP F  1 84  ? 65.251  -14.006 13.305 1.00 20.26 ? 83   ASP F N   1 
ATOM   6157  C  CA  . ASP F  1 84  ? 65.773  -12.887 14.094 1.00 20.40 ? 83   ASP F CA  1 
ATOM   6158  C  C   . ASP F  1 84  ? 64.876  -11.660 14.100 1.00 20.58 ? 83   ASP F C   1 
ATOM   6159  O  O   . ASP F  1 84  ? 64.926  -10.835 13.184 1.00 23.35 ? 83   ASP F O   1 
ATOM   6160  C  CB  . ASP F  1 84  ? 67.171  -12.474 13.601 1.00 20.62 ? 83   ASP F CB  1 
ATOM   6161  C  CG  . ASP F  1 84  ? 68.243  -13.497 13.929 1.00 21.98 ? 83   ASP F CG  1 
ATOM   6162  O  OD1 . ASP F  1 84  ? 68.012  -14.367 14.801 1.00 21.04 ? 83   ASP F OD1 1 
ATOM   6163  O  OD2 . ASP F  1 84  ? 69.336  -13.429 13.323 1.00 23.18 ? 83   ASP F OD2 1 
ATOM   6164  N  N   . LEU F  1 85  ? 64.079  -11.519 15.153 1.00 18.12 ? 84   LEU F N   1 
ATOM   6165  C  CA  . LEU F  1 85  ? 63.172  -10.388 15.266 1.00 19.09 ? 84   LEU F CA  1 
ATOM   6166  C  C   . LEU F  1 85  ? 63.671  -9.307  16.238 1.00 19.60 ? 84   LEU F C   1 
ATOM   6167  O  O   . LEU F  1 85  ? 62.922  -8.410  16.620 1.00 21.91 ? 84   LEU F O   1 
ATOM   6168  C  CB  . LEU F  1 85  ? 61.783  -10.880 15.682 1.00 15.88 ? 84   LEU F CB  1 
ATOM   6169  C  CG  . LEU F  1 85  ? 61.085  -11.800 14.670 1.00 19.86 ? 84   LEU F CG  1 
ATOM   6170  C  CD1 . LEU F  1 85  ? 59.715  -12.219 15.210 1.00 17.67 ? 84   LEU F CD1 1 
ATOM   6171  C  CD2 . LEU F  1 85  ? 60.916  -11.081 13.341 1.00 18.38 ? 84   LEU F CD2 1 
ATOM   6172  N  N   . GLY F  1 86  ? 64.930  -9.401  16.648 1.00 18.40 ? 85   GLY F N   1 
ATOM   6173  C  CA  . GLY F  1 86  ? 65.479  -8.392  17.540 1.00 19.81 ? 85   GLY F CA  1 
ATOM   6174  C  C   . GLY F  1 86  ? 65.066  -8.446  18.997 1.00 21.41 ? 85   GLY F C   1 
ATOM   6175  O  O   . GLY F  1 86  ? 65.129  -9.506  19.628 1.00 21.03 ? 85   GLY F O   1 
ATOM   6176  N  N   . ASN F  1 87  ? 64.642  -7.297  19.526 1.00 20.51 ? 86   ASN F N   1 
ATOM   6177  C  CA  . ASN F  1 87  ? 64.229  -7.172  20.927 1.00 22.12 ? 86   ASN F CA  1 
ATOM   6178  C  C   . ASN F  1 87  ? 62.847  -6.574  21.101 1.00 20.08 ? 86   ASN F C   1 
ATOM   6179  O  O   . ASN F  1 87  ? 62.334  -5.894  20.221 1.00 22.74 ? 86   ASN F O   1 
ATOM   6180  C  CB  . ASN F  1 87  ? 65.174  -6.235  21.697 1.00 20.18 ? 86   ASN F CB  1 
ATOM   6181  C  CG  . ASN F  1 87  ? 66.555  -6.798  21.869 1.00 20.07 ? 86   ASN F CG  1 
ATOM   6182  O  OD1 . ASN F  1 87  ? 66.767  -7.725  22.649 1.00 21.20 ? 86   ASN F OD1 1 
ATOM   6183  N  ND2 . ASN F  1 87  ? 67.516  -6.233  21.145 1.00 20.28 ? 86   ASN F ND2 1 
ATOM   6184  N  N   . VAL F  1 88  ? 62.261  -6.824  22.262 1.00 20.54 ? 87   VAL F N   1 
ATOM   6185  C  CA  . VAL F  1 88  ? 60.993  -6.216  22.620 1.00 21.02 ? 87   VAL F CA  1 
ATOM   6186  C  C   . VAL F  1 88  ? 61.366  -5.483  23.899 1.00 22.51 ? 87   VAL F C   1 
ATOM   6187  O  O   . VAL F  1 88  ? 62.319  -5.873  24.582 1.00 22.77 ? 87   VAL F O   1 
ATOM   6188  C  CB  . VAL F  1 88  ? 59.877  -7.255  22.877 1.00 22.00 ? 87   VAL F CB  1 
ATOM   6189  C  CG1 . VAL F  1 88  ? 59.470  -7.883  21.554 1.00 20.28 ? 87   VAL F CG1 1 
ATOM   6190  C  CG2 . VAL F  1 88  ? 60.347  -8.317  23.859 1.00 21.91 ? 87   VAL F CG2 1 
ATOM   6191  N  N   . THR F  1 89  ? 60.647  -4.416  24.216 1.00 22.49 ? 88   THR F N   1 
ATOM   6192  C  CA  . THR F  1 89  ? 60.960  -3.638  25.404 1.00 23.88 ? 88   THR F CA  1 
ATOM   6193  C  C   . THR F  1 89  ? 59.856  -3.698  26.445 1.00 24.66 ? 88   THR F C   1 
ATOM   6194  O  O   . THR F  1 89  ? 58.700  -3.402  26.153 1.00 26.75 ? 88   THR F O   1 
ATOM   6195  C  CB  . THR F  1 89  ? 61.216  -2.155  25.035 1.00 23.86 ? 88   THR F CB  1 
ATOM   6196  O  OG1 . THR F  1 89  ? 62.265  -2.078  24.055 1.00 21.17 ? 88   THR F OG1 1 
ATOM   6197  C  CG2 . THR F  1 89  ? 61.608  -1.356  26.273 1.00 21.80 ? 88   THR F CG2 1 
ATOM   6198  N  N   . ALA F  1 90  ? 60.223  -4.091  27.660 1.00 24.93 ? 89   ALA F N   1 
ATOM   6199  C  CA  . ALA F  1 90  ? 59.269  -4.177  28.755 1.00 27.93 ? 89   ALA F CA  1 
ATOM   6200  C  C   . ALA F  1 90  ? 59.348  -2.881  29.544 1.00 28.97 ? 89   ALA F C   1 
ATOM   6201  O  O   . ALA F  1 90  ? 60.443  -2.431  29.891 1.00 27.26 ? 89   ALA F O   1 
ATOM   6202  C  CB  . ALA F  1 90  ? 59.606  -5.355  29.658 1.00 23.49 ? 89   ALA F CB  1 
ATOM   6203  N  N   . ASP F  1 91  ? 58.193  -2.283  29.821 1.00 31.07 ? 90   ASP F N   1 
ATOM   6204  C  CA  . ASP F  1 91  ? 58.149  -1.036  30.576 1.00 34.08 ? 90   ASP F CA  1 
ATOM   6205  C  C   . ASP F  1 91  ? 58.354  -1.306  32.061 1.00 35.68 ? 90   ASP F C   1 
ATOM   6206  O  O   . ASP F  1 91  ? 58.616  -2.439  32.461 1.00 34.47 ? 90   ASP F O   1 
ATOM   6207  C  CB  . ASP F  1 91  ? 56.819  -0.310  30.334 1.00 34.43 ? 90   ASP F CB  1 
ATOM   6208  C  CG  . ASP F  1 91  ? 55.603  -1.117  30.792 1.00 35.70 ? 90   ASP F CG  1 
ATOM   6209  O  OD1 . ASP F  1 91  ? 54.525  -0.948  30.182 1.00 37.42 ? 90   ASP F OD1 1 
ATOM   6210  O  OD2 . ASP F  1 91  ? 55.710  -1.901  31.759 1.00 36.75 ? 90   ASP F OD2 1 
ATOM   6211  N  N   . LYS F  1 92  ? 58.238  -0.260  32.874 1.00 38.34 ? 91   LYS F N   1 
ATOM   6212  C  CA  . LYS F  1 92  ? 58.424  -0.380  34.314 1.00 39.83 ? 91   LYS F CA  1 
ATOM   6213  C  C   . LYS F  1 92  ? 57.383  -1.284  34.966 1.00 38.83 ? 91   LYS F C   1 
ATOM   6214  O  O   . LYS F  1 92  ? 57.612  -1.822  36.046 1.00 37.96 ? 91   LYS F O   1 
ATOM   6215  C  CB  . LYS F  1 92  ? 58.392  1.012   34.958 1.00 44.03 ? 91   LYS F CB  1 
ATOM   6216  C  CG  . LYS F  1 92  ? 57.181  1.845   34.569 1.00 49.27 ? 91   LYS F CG  1 
ATOM   6217  C  CD  . LYS F  1 92  ? 57.249  3.245   35.165 1.00 53.68 ? 91   LYS F CD  1 
ATOM   6218  C  CE  . LYS F  1 92  ? 56.041  4.076   34.758 1.00 55.72 ? 91   LYS F CE  1 
ATOM   6219  N  NZ  . LYS F  1 92  ? 56.123  5.467   35.285 1.00 57.73 ? 91   LYS F NZ  1 
ATOM   6220  N  N   . ASP F  1 93  ? 56.242  -1.449  34.308 1.00 38.30 ? 92   ASP F N   1 
ATOM   6221  C  CA  . ASP F  1 93  ? 55.178  -2.298  34.834 1.00 39.28 ? 92   ASP F CA  1 
ATOM   6222  C  C   . ASP F  1 93  ? 55.432  -3.780  34.545 1.00 37.70 ? 92   ASP F C   1 
ATOM   6223  O  O   . ASP F  1 93  ? 54.650  -4.638  34.956 1.00 35.83 ? 92   ASP F O   1 
ATOM   6224  C  CB  . ASP F  1 93  ? 53.835  -1.879  34.234 1.00 42.80 ? 92   ASP F CB  1 
ATOM   6225  C  CG  . ASP F  1 93  ? 53.392  -0.507  34.701 1.00 48.09 ? 92   ASP F CG  1 
ATOM   6226  O  OD1 . ASP F  1 93  ? 52.419  0.028   34.123 1.00 51.38 ? 92   ASP F OD1 1 
ATOM   6227  O  OD2 . ASP F  1 93  ? 54.009  0.034   35.648 1.00 49.05 ? 92   ASP F OD2 1 
ATOM   6228  N  N   . GLY F  1 94  ? 56.518  -4.071  33.831 1.00 36.32 ? 93   GLY F N   1 
ATOM   6229  C  CA  . GLY F  1 94  ? 56.859  -5.449  33.507 1.00 34.77 ? 93   GLY F CA  1 
ATOM   6230  C  C   . GLY F  1 94  ? 56.155  -5.962  32.262 1.00 33.86 ? 93   GLY F C   1 
ATOM   6231  O  O   . GLY F  1 94  ? 56.114  -7.170  32.002 1.00 34.32 ? 93   GLY F O   1 
ATOM   6232  N  N   . VAL F  1 95  ? 55.621  -5.036  31.476 1.00 30.81 ? 94   VAL F N   1 
ATOM   6233  C  CA  . VAL F  1 95  ? 54.892  -5.383  30.267 1.00 30.70 ? 94   VAL F CA  1 
ATOM   6234  C  C   . VAL F  1 95  ? 55.533  -4.857  28.994 1.00 30.68 ? 94   VAL F C   1 
ATOM   6235  O  O   . VAL F  1 95  ? 55.934  -3.693  28.914 1.00 32.28 ? 94   VAL F O   1 
ATOM   6236  C  CB  . VAL F  1 95  ? 53.450  -4.827  30.324 1.00 31.32 ? 94   VAL F CB  1 
ATOM   6237  C  CG1 . VAL F  1 95  ? 52.690  -5.219  29.067 1.00 31.13 ? 94   VAL F CG1 1 
ATOM   6238  C  CG2 . VAL F  1 95  ? 52.746  -5.329  31.579 1.00 30.71 ? 94   VAL F CG2 1 
ATOM   6239  N  N   . ALA F  1 96  ? 55.628  -5.724  27.992 1.00 29.24 ? 95   ALA F N   1 
ATOM   6240  C  CA  . ALA F  1 96  ? 56.171  -5.329  26.706 1.00 27.94 ? 95   ALA F CA  1 
ATOM   6241  C  C   . ALA F  1 96  ? 55.023  -5.352  25.714 1.00 29.69 ? 95   ALA F C   1 
ATOM   6242  O  O   . ALA F  1 96  ? 54.428  -6.405  25.463 1.00 28.40 ? 95   ALA F O   1 
ATOM   6243  C  CB  . ALA F  1 96  ? 57.272  -6.295  26.257 1.00 27.77 ? 95   ALA F CB  1 
ATOM   6244  N  N   . ASP F  1 97  ? 54.693  -4.185  25.172 1.00 28.76 ? 96   ASP F N   1 
ATOM   6245  C  CA  . ASP F  1 97  ? 53.633  -4.082  24.186 1.00 30.36 ? 96   ASP F CA  1 
ATOM   6246  C  C   . ASP F  1 97  ? 54.283  -4.217  22.822 1.00 30.21 ? 96   ASP F C   1 
ATOM   6247  O  O   . ASP F  1 97  ? 54.769  -3.252  22.241 1.00 33.61 ? 96   ASP F O   1 
ATOM   6248  C  CB  . ASP F  1 97  ? 52.908  -2.751  24.335 1.00 30.56 ? 96   ASP F CB  1 
ATOM   6249  C  CG  . ASP F  1 97  ? 52.076  -2.703  25.599 1.00 34.42 ? 96   ASP F CG  1 
ATOM   6250  O  OD1 . ASP F  1 97  ? 52.328  -1.836  26.462 1.00 35.53 ? 96   ASP F OD1 1 
ATOM   6251  O  OD2 . ASP F  1 97  ? 51.172  -3.558  25.733 1.00 35.89 ? 96   ASP F OD2 1 
ATOM   6252  N  N   . VAL F  1 98  ? 54.281  -5.439  22.317 1.00 28.05 ? 97   VAL F N   1 
ATOM   6253  C  CA  . VAL F  1 98  ? 54.913  -5.740  21.050 1.00 25.34 ? 97   VAL F CA  1 
ATOM   6254  C  C   . VAL F  1 98  ? 54.184  -5.239  19.820 1.00 26.56 ? 97   VAL F C   1 
ATOM   6255  O  O   . VAL F  1 98  ? 52.970  -5.368  19.696 1.00 26.05 ? 97   VAL F O   1 
ATOM   6256  C  CB  . VAL F  1 98  ? 55.138  -7.256  20.919 1.00 24.15 ? 97   VAL F CB  1 
ATOM   6257  C  CG1 . VAL F  1 98  ? 55.930  -7.557  19.669 1.00 20.76 ? 97   VAL F CG1 1 
ATOM   6258  C  CG2 . VAL F  1 98  ? 55.868  -7.776  22.155 1.00 23.27 ? 97   VAL F CG2 1 
ATOM   6259  N  N   . SER F  1 99  ? 54.953  -4.663  18.908 1.00 27.17 ? 98   SER F N   1 
ATOM   6260  C  CA  . SER F  1 99  ? 54.427  -4.158  17.652 1.00 30.04 ? 98   SER F CA  1 
ATOM   6261  C  C   . SER F  1 99  ? 55.621  -4.100  16.721 1.00 29.45 ? 98   SER F C   1 
ATOM   6262  O  O   . SER F  1 99  ? 56.432  -3.175  16.781 1.00 31.37 ? 98   SER F O   1 
ATOM   6263  C  CB  . SER F  1 99  ? 53.818  -2.765  17.824 1.00 31.35 ? 98   SER F CB  1 
ATOM   6264  O  OG  . SER F  1 99  ? 53.146  -2.369  16.638 1.00 34.92 ? 98   SER F OG  1 
ATOM   6265  N  N   . ILE F  1 100 ? 55.718  -5.109  15.869 1.00 28.62 ? 99   ILE F N   1 
ATOM   6266  C  CA  . ILE F  1 100 ? 56.812  -5.251  14.924 1.00 28.80 ? 99   ILE F CA  1 
ATOM   6267  C  C   . ILE F  1 100 ? 56.290  -5.618  13.539 1.00 28.44 ? 99   ILE F C   1 
ATOM   6268  O  O   . ILE F  1 100 ? 55.211  -6.196  13.402 1.00 27.13 ? 99   ILE F O   1 
ATOM   6269  C  CB  . ILE F  1 100 ? 57.770  -6.371  15.398 1.00 30.37 ? 99   ILE F CB  1 
ATOM   6270  C  CG1 . ILE F  1 100 ? 58.495  -5.930  16.671 1.00 31.85 ? 99   ILE F CG1 1 
ATOM   6271  C  CG2 . ILE F  1 100 ? 58.753  -6.738  14.299 1.00 32.85 ? 99   ILE F CG2 1 
ATOM   6272  C  CD1 . ILE F  1 100 ? 59.374  -7.021  17.272 1.00 31.81 ? 99   ILE F CD1 1 
ATOM   6273  N  N   . GLU F  1 101 ? 57.061  -5.268  12.515 1.00 28.51 ? 100  GLU F N   1 
ATOM   6274  C  CA  . GLU F  1 101 ? 56.711  -5.591  11.143 1.00 28.01 ? 100  GLU F CA  1 
ATOM   6275  C  C   . GLU F  1 101 ? 57.988  -6.142  10.526 1.00 26.46 ? 100  GLU F C   1 
ATOM   6276  O  O   . GLU F  1 101 ? 59.053  -5.539  10.639 1.00 25.02 ? 100  GLU F O   1 
ATOM   6277  C  CB  . GLU F  1 101 ? 56.251  -4.341  10.395 1.00 33.02 ? 100  GLU F CB  1 
ATOM   6278  C  CG  . GLU F  1 101 ? 55.266  -4.629  9.289  1.00 37.67 ? 100  GLU F CG  1 
ATOM   6279  C  CD  . GLU F  1 101 ? 54.821  -3.373  8.569  1.00 40.43 ? 100  GLU F CD  1 
ATOM   6280  O  OE1 . GLU F  1 101 ? 55.439  -3.034  7.537  1.00 43.28 ? 100  GLU F OE1 1 
ATOM   6281  O  OE2 . GLU F  1 101 ? 53.866  -2.722  9.047  1.00 42.73 ? 100  GLU F OE2 1 
ATOM   6282  N  N   . ASP F  1 102 ? 57.891  -7.294  9.878  1.00 25.16 ? 101  ASP F N   1 
ATOM   6283  C  CA  . ASP F  1 102 ? 59.070  -7.907  9.293  1.00 24.88 ? 101  ASP F CA  1 
ATOM   6284  C  C   . ASP F  1 102 ? 58.736  -8.567  7.968  1.00 26.83 ? 101  ASP F C   1 
ATOM   6285  O  O   . ASP F  1 102 ? 57.681  -9.184  7.826  1.00 28.27 ? 101  ASP F O   1 
ATOM   6286  C  CB  . ASP F  1 102 ? 59.643  -8.929  10.274 1.00 23.44 ? 101  ASP F CB  1 
ATOM   6287  C  CG  . ASP F  1 102 ? 61.000  -9.421  9.866  1.00 23.47 ? 101  ASP F CG  1 
ATOM   6288  O  OD1 . ASP F  1 102 ? 61.093  -10.519 9.274  1.00 23.90 ? 101  ASP F OD1 1 
ATOM   6289  O  OD2 . ASP F  1 102 ? 61.979  -8.695  10.130 1.00 24.80 ? 101  ASP F OD2 1 
ATOM   6290  N  N   . SER F  1 103 ? 59.640  -8.439  7.002  1.00 26.69 ? 102  SER F N   1 
ATOM   6291  C  CA  . SER F  1 103 ? 59.422  -9.001  5.677  1.00 27.80 ? 102  SER F CA  1 
ATOM   6292  C  C   . SER F  1 103 ? 60.291  -10.210 5.376  1.00 26.80 ? 102  SER F C   1 
ATOM   6293  O  O   . SER F  1 103 ? 60.341  -10.676 4.240  1.00 28.17 ? 102  SER F O   1 
ATOM   6294  C  CB  . SER F  1 103 ? 59.662  -7.923  4.620  1.00 29.49 ? 102  SER F CB  1 
ATOM   6295  O  OG  . SER F  1 103 ? 58.787  -6.834  4.837  1.00 35.92 ? 102  SER F OG  1 
ATOM   6296  N  N   . VAL F  1 104 ? 60.985  -10.717 6.384  1.00 25.13 ? 103  VAL F N   1 
ATOM   6297  C  CA  . VAL F  1 104 ? 61.824  -11.884 6.181  1.00 24.76 ? 103  VAL F CA  1 
ATOM   6298  C  C   . VAL F  1 104 ? 61.071  -13.133 6.646  1.00 26.54 ? 103  VAL F C   1 
ATOM   6299  O  O   . VAL F  1 104 ? 61.108  -14.169 5.979  1.00 24.94 ? 103  VAL F O   1 
ATOM   6300  C  CB  . VAL F  1 104 ? 63.163  -11.742 6.924  1.00 24.79 ? 103  VAL F CB  1 
ATOM   6301  C  CG1 . VAL F  1 104 ? 63.968  -13.031 6.807  1.00 24.21 ? 103  VAL F CG1 1 
ATOM   6302  C  CG2 . VAL F  1 104 ? 63.955  -10.578 6.318  1.00 28.18 ? 103  VAL F CG2 1 
ATOM   6303  N  N   . ILE F  1 105 ? 60.394  -13.044 7.787  1.00 25.11 ? 104  ILE F N   1 
ATOM   6304  C  CA  . ILE F  1 105 ? 59.608  -14.182 8.251  1.00 23.13 ? 104  ILE F CA  1 
ATOM   6305  C  C   . ILE F  1 105 ? 58.368  -14.168 7.366  1.00 23.84 ? 104  ILE F C   1 
ATOM   6306  O  O   . ILE F  1 105 ? 58.046  -13.140 6.762  1.00 24.65 ? 104  ILE F O   1 
ATOM   6307  C  CB  . ILE F  1 105 ? 59.131  -14.038 9.721  1.00 23.03 ? 104  ILE F CB  1 
ATOM   6308  C  CG1 . ILE F  1 105 ? 58.397  -12.710 9.903  1.00 23.67 ? 104  ILE F CG1 1 
ATOM   6309  C  CG2 . ILE F  1 105 ? 60.302  -14.197 10.677 1.00 23.89 ? 104  ILE F CG2 1 
ATOM   6310  C  CD1 . ILE F  1 105 ? 57.729  -12.551 11.266 1.00 24.19 ? 104  ILE F CD1 1 
ATOM   6311  N  N   . SER F  1 106 ? 57.678  -15.302 7.285  1.00 23.06 ? 105  SER F N   1 
ATOM   6312  C  CA  . SER F  1 106 ? 56.462  -15.400 6.491  1.00 21.83 ? 105  SER F CA  1 
ATOM   6313  C  C   . SER F  1 106 ? 55.525  -16.414 7.140  1.00 22.06 ? 105  SER F C   1 
ATOM   6314  O  O   . SER F  1 106 ? 55.952  -17.203 7.983  1.00 21.81 ? 105  SER F O   1 
ATOM   6315  C  CB  . SER F  1 106 ? 56.785  -15.849 5.066  1.00 21.78 ? 105  SER F CB  1 
ATOM   6316  O  OG  . SER F  1 106 ? 55.637  -15.723 4.250  1.00 22.48 ? 105  SER F OG  1 
ATOM   6317  N  N   . LEU F  1 107 ? 54.252  -16.384 6.761  1.00 22.16 ? 106  LEU F N   1 
ATOM   6318  C  CA  . LEU F  1 107 ? 53.287  -17.331 7.308  1.00 23.53 ? 106  LEU F CA  1 
ATOM   6319  C  C   . LEU F  1 107 ? 52.987  -18.445 6.299  1.00 25.87 ? 106  LEU F C   1 
ATOM   6320  O  O   . LEU F  1 107 ? 52.034  -19.208 6.460  1.00 25.32 ? 106  LEU F O   1 
ATOM   6321  C  CB  . LEU F  1 107 ? 51.999  -16.609 7.720  1.00 22.06 ? 106  LEU F CB  1 
ATOM   6322  C  CG  . LEU F  1 107 ? 52.162  -15.536 8.806  1.00 22.95 ? 106  LEU F CG  1 
ATOM   6323  C  CD1 . LEU F  1 107 ? 50.796  -15.067 9.266  1.00 19.88 ? 106  LEU F CD1 1 
ATOM   6324  C  CD2 . LEU F  1 107 ? 52.954  -16.088 9.981  1.00 18.65 ? 106  LEU F CD2 1 
ATOM   6325  N  N   . SER F  1 108 ? 53.808  -18.525 5.253  1.00 26.67 ? 107  SER F N   1 
ATOM   6326  C  CA  . SER F  1 108 ? 53.668  -19.563 4.235  1.00 28.98 ? 107  SER F CA  1 
ATOM   6327  C  C   . SER F  1 108 ? 54.970  -19.669 3.460  1.00 29.50 ? 107  SER F C   1 
ATOM   6328  O  O   . SER F  1 108 ? 55.779  -18.743 3.465  1.00 31.06 ? 107  SER F O   1 
ATOM   6329  C  CB  . SER F  1 108 ? 52.506  -19.258 3.272  1.00 30.75 ? 107  SER F CB  1 
ATOM   6330  O  OG  . SER F  1 108 ? 52.750  -18.105 2.486  1.00 33.21 ? 107  SER F OG  1 
ATOM   6331  N  N   . GLY F  1 109 ? 55.178  -20.808 2.810  1.00 28.71 ? 108  GLY F N   1 
ATOM   6332  C  CA  . GLY F  1 109 ? 56.387  -21.004 2.035  1.00 27.96 ? 108  GLY F CA  1 
ATOM   6333  C  C   . GLY F  1 109 ? 57.571  -21.492 2.849  1.00 27.09 ? 108  GLY F C   1 
ATOM   6334  O  O   . GLY F  1 109 ? 57.425  -21.876 4.008  1.00 26.91 ? 108  GLY F O   1 
ATOM   6335  N  N   . ASP F  1 110 ? 58.746  -21.460 2.228  1.00 26.13 ? 109  ASP F N   1 
ATOM   6336  C  CA  . ASP F  1 110 ? 60.002  -21.897 2.842  1.00 28.95 ? 109  ASP F CA  1 
ATOM   6337  C  C   . ASP F  1 110 ? 60.415  -21.131 4.088  1.00 27.09 ? 109  ASP F C   1 
ATOM   6338  O  O   . ASP F  1 110 ? 61.159  -21.645 4.915  1.00 26.50 ? 109  ASP F O   1 
ATOM   6339  C  CB  . ASP F  1 110 ? 61.145  -21.774 1.839  1.00 32.70 ? 109  ASP F CB  1 
ATOM   6340  C  CG  . ASP F  1 110 ? 61.120  -22.852 0.794  1.00 37.10 ? 109  ASP F CG  1 
ATOM   6341  O  OD1 . ASP F  1 110 ? 62.001  -22.814 -0.086 1.00 37.95 ? 109  ASP F OD1 1 
ATOM   6342  O  OD2 . ASP F  1 110 ? 60.232  -23.732 0.857  1.00 38.24 ? 109  ASP F OD2 1 
ATOM   6343  N  N   . HIS F  1 111 ? 59.971  -19.890 4.199  1.00 26.71 ? 110  HIS F N   1 
ATOM   6344  C  CA  . HIS F  1 111 ? 60.334  -19.081 5.350  1.00 28.15 ? 110  HIS F CA  1 
ATOM   6345  C  C   . HIS F  1 111 ? 59.209  -19.028 6.369  1.00 25.77 ? 110  HIS F C   1 
ATOM   6346  O  O   . HIS F  1 111 ? 59.256  -18.245 7.314  1.00 26.19 ? 110  HIS F O   1 
ATOM   6347  C  CB  . HIS F  1 111 ? 60.708  -17.665 4.899  1.00 28.28 ? 110  HIS F CB  1 
ATOM   6348  C  CG  . HIS F  1 111 ? 61.982  -17.605 4.113  1.00 34.35 ? 110  HIS F CG  1 
ATOM   6349  N  ND1 . HIS F  1 111 ? 62.424  -16.450 3.502  1.00 36.43 ? 110  HIS F ND1 1 
ATOM   6350  C  CD2 . HIS F  1 111 ? 62.916  -18.550 3.850  1.00 36.30 ? 110  HIS F CD2 1 
ATOM   6351  C  CE1 . HIS F  1 111 ? 63.576  -16.690 2.896  1.00 37.28 ? 110  HIS F CE1 1 
ATOM   6352  N  NE2 . HIS F  1 111 ? 63.894  -17.955 3.093  1.00 36.84 ? 110  HIS F NE2 1 
ATOM   6353  N  N   . SER F  1 112 ? 58.206  -19.877 6.186  1.00 24.19 ? 111  SER F N   1 
ATOM   6354  C  CA  . SER F  1 112 ? 57.084  -19.898 7.109  1.00 22.67 ? 111  SER F CA  1 
ATOM   6355  C  C   . SER F  1 112 ? 57.523  -20.217 8.529  1.00 20.12 ? 111  SER F C   1 
ATOM   6356  O  O   . SER F  1 112 ? 58.374  -21.080 8.751  1.00 18.76 ? 111  SER F O   1 
ATOM   6357  C  CB  . SER F  1 112 ? 56.038  -20.922 6.667  1.00 22.01 ? 111  SER F CB  1 
ATOM   6358  O  OG  . SER F  1 112 ? 54.950  -20.923 7.571  1.00 23.51 ? 111  SER F OG  1 
ATOM   6359  N  N   . ILE F  1 113 ? 56.937  -19.511 9.489  1.00 19.22 ? 112  ILE F N   1 
ATOM   6360  C  CA  . ILE F  1 113 ? 57.242  -19.742 10.897 1.00 19.63 ? 112  ILE F CA  1 
ATOM   6361  C  C   . ILE F  1 113 ? 56.119  -20.551 11.560 1.00 19.94 ? 112  ILE F C   1 
ATOM   6362  O  O   . ILE F  1 113 ? 56.148  -20.800 12.767 1.00 18.95 ? 112  ILE F O   1 
ATOM   6363  C  CB  . ILE F  1 113 ? 57.432  -18.411 11.657 1.00 19.59 ? 112  ILE F CB  1 
ATOM   6364  C  CG1 . ILE F  1 113 ? 56.189  -17.536 11.507 1.00 21.37 ? 112  ILE F CG1 1 
ATOM   6365  C  CG2 . ILE F  1 113 ? 58.667  -17.687 11.119 1.00 23.41 ? 112  ILE F CG2 1 
ATOM   6366  C  CD1 . ILE F  1 113 ? 56.256  -16.228 12.279 1.00 22.49 ? 112  ILE F CD1 1 
ATOM   6367  N  N   . ILE F  1 114 ? 55.138  -20.972 10.760 1.00 20.49 ? 113  ILE F N   1 
ATOM   6368  C  CA  . ILE F  1 114 ? 54.022  -21.773 11.266 1.00 20.16 ? 113  ILE F CA  1 
ATOM   6369  C  C   . ILE F  1 114 ? 54.563  -23.116 11.756 1.00 19.48 ? 113  ILE F C   1 
ATOM   6370  O  O   . ILE F  1 114 ? 55.301  -23.790 11.043 1.00 20.06 ? 113  ILE F O   1 
ATOM   6371  C  CB  . ILE F  1 114 ? 52.975  -22.051 10.154 1.00 20.34 ? 113  ILE F CB  1 
ATOM   6372  C  CG1 . ILE F  1 114 ? 52.435  -20.732 9.604  1.00 21.32 ? 113  ILE F CG1 1 
ATOM   6373  C  CG2 . ILE F  1 114 ? 51.827  -22.905 10.710 1.00 18.82 ? 113  ILE F CG2 1 
ATOM   6374  C  CD1 . ILE F  1 114 ? 51.683  -19.912 10.608 1.00 22.35 ? 113  ILE F CD1 1 
ATOM   6375  N  N   . GLY F  1 115 ? 54.210  -23.502 12.974 1.00 19.55 ? 114  GLY F N   1 
ATOM   6376  C  CA  . GLY F  1 115 ? 54.691  -24.775 13.495 1.00 19.31 ? 114  GLY F CA  1 
ATOM   6377  C  C   . GLY F  1 115 ? 56.052  -24.687 14.167 1.00 19.88 ? 114  GLY F C   1 
ATOM   6378  O  O   . GLY F  1 115 ? 56.620  -25.699 14.594 1.00 18.20 ? 114  GLY F O   1 
ATOM   6379  N  N   . ARG F  1 116 ? 56.597  -23.479 14.248 1.00 18.76 ? 115  ARG F N   1 
ATOM   6380  C  CA  . ARG F  1 116 ? 57.894  -23.295 14.888 1.00 18.58 ? 115  ARG F CA  1 
ATOM   6381  C  C   . ARG F  1 116 ? 57.647  -22.627 16.242 1.00 19.30 ? 115  ARG F C   1 
ATOM   6382  O  O   . ARG F  1 116 ? 56.494  -22.472 16.647 1.00 20.32 ? 115  ARG F O   1 
ATOM   6383  C  CB  . ARG F  1 116 ? 58.818  -22.480 13.965 1.00 17.97 ? 115  ARG F CB  1 
ATOM   6384  C  CG  . ARG F  1 116 ? 59.003  -23.189 12.596 1.00 20.35 ? 115  ARG F CG  1 
ATOM   6385  C  CD  . ARG F  1 116 ? 60.138  -22.631 11.733 1.00 21.33 ? 115  ARG F CD  1 
ATOM   6386  N  NE  . ARG F  1 116 ? 60.178  -23.262 10.410 1.00 21.04 ? 115  ARG F NE  1 
ATOM   6387  C  CZ  . ARG F  1 116 ? 60.789  -24.412 10.120 1.00 22.95 ? 115  ARG F CZ  1 
ATOM   6388  N  NH1 . ARG F  1 116 ? 60.748  -24.883 8.879  1.00 22.58 ? 115  ARG F NH1 1 
ATOM   6389  N  NH2 . ARG F  1 116 ? 61.459  -25.085 11.047 1.00 21.75 ? 115  ARG F NH2 1 
ATOM   6390  N  N   . THR F  1 117 ? 58.703  -22.222 16.942 1.00 19.54 ? 116  THR F N   1 
ATOM   6391  C  CA  . THR F  1 117 ? 58.527  -21.643 18.270 1.00 17.27 ? 116  THR F CA  1 
ATOM   6392  C  C   . THR F  1 117 ? 58.986  -20.195 18.461 1.00 20.51 ? 116  THR F C   1 
ATOM   6393  O  O   . THR F  1 117 ? 60.092  -19.821 18.065 1.00 18.46 ? 116  THR F O   1 
ATOM   6394  C  CB  . THR F  1 117 ? 59.245  -22.530 19.316 1.00 17.92 ? 116  THR F CB  1 
ATOM   6395  O  OG1 . THR F  1 117 ? 58.700  -23.857 19.268 1.00 17.94 ? 116  THR F OG1 1 
ATOM   6396  C  CG2 . THR F  1 117 ? 59.080  -21.965 20.726 1.00 15.68 ? 116  THR F CG2 1 
ATOM   6397  N  N   . LEU F  1 118 ? 58.121  -19.385 19.071 1.00 19.58 ? 117  LEU F N   1 
ATOM   6398  C  CA  . LEU F  1 118 ? 58.442  -17.991 19.363 1.00 20.09 ? 117  LEU F CA  1 
ATOM   6399  C  C   . LEU F  1 118 ? 59.018  -18.002 20.773 1.00 20.77 ? 117  LEU F C   1 
ATOM   6400  O  O   . LEU F  1 118 ? 58.446  -18.611 21.684 1.00 18.97 ? 117  LEU F O   1 
ATOM   6401  C  CB  . LEU F  1 118 ? 57.184  -17.114 19.315 1.00 19.09 ? 117  LEU F CB  1 
ATOM   6402  C  CG  . LEU F  1 118 ? 57.422  -15.619 19.559 1.00 18.66 ? 117  LEU F CG  1 
ATOM   6403  C  CD1 . LEU F  1 118 ? 58.301  -15.047 18.439 1.00 18.22 ? 117  LEU F CD1 1 
ATOM   6404  C  CD2 . LEU F  1 118 ? 56.093  -14.888 19.612 1.00 16.01 ? 117  LEU F CD2 1 
ATOM   6405  N  N   . VAL F  1 119 ? 60.158  -17.345 20.954 1.00 18.04 ? 118  VAL F N   1 
ATOM   6406  C  CA  . VAL F  1 119 ? 60.809  -17.321 22.254 1.00 18.32 ? 118  VAL F CA  1 
ATOM   6407  C  C   . VAL F  1 119 ? 61.164  -15.910 22.714 1.00 19.88 ? 118  VAL F C   1 
ATOM   6408  O  O   . VAL F  1 119 ? 61.614  -15.083 21.917 1.00 18.89 ? 118  VAL F O   1 
ATOM   6409  C  CB  . VAL F  1 119 ? 62.127  -18.141 22.229 1.00 18.43 ? 118  VAL F CB  1 
ATOM   6410  C  CG1 . VAL F  1 119 ? 62.817  -18.064 23.604 1.00 16.89 ? 118  VAL F CG1 1 
ATOM   6411  C  CG2 . VAL F  1 119 ? 61.845  -19.597 21.845 1.00 18.32 ? 118  VAL F CG2 1 
ATOM   6412  N  N   . VAL F  1 120 ? 60.947  -15.634 23.996 1.00 19.55 ? 119  VAL F N   1 
ATOM   6413  C  CA  . VAL F  1 120 ? 61.320  -14.339 24.552 1.00 18.69 ? 119  VAL F CA  1 
ATOM   6414  C  C   . VAL F  1 120 ? 62.405  -14.664 25.573 1.00 20.15 ? 119  VAL F C   1 
ATOM   6415  O  O   . VAL F  1 120 ? 62.252  -15.574 26.399 1.00 19.52 ? 119  VAL F O   1 
ATOM   6416  C  CB  . VAL F  1 120 ? 60.131  -13.610 25.204 1.00 19.16 ? 119  VAL F CB  1 
ATOM   6417  C  CG1 . VAL F  1 120 ? 59.583  -14.413 26.383 1.00 16.26 ? 119  VAL F CG1 1 
ATOM   6418  C  CG2 . VAL F  1 120 ? 60.577  -12.209 25.639 1.00 18.76 ? 119  VAL F CG2 1 
ATOM   6419  N  N   . HIS F  1 121 ? 63.499  -13.913 25.505 1.00 19.87 ? 120  HIS F N   1 
ATOM   6420  C  CA  . HIS F  1 121 ? 64.680  -14.148 26.329 1.00 18.99 ? 120  HIS F CA  1 
ATOM   6421  C  C   . HIS F  1 121 ? 64.919  -13.346 27.605 1.00 19.47 ? 120  HIS F C   1 
ATOM   6422  O  O   . HIS F  1 121 ? 64.333  -12.294 27.833 1.00 19.20 ? 120  HIS F O   1 
ATOM   6423  C  CB  . HIS F  1 121 ? 65.919  -14.016 25.440 1.00 19.07 ? 120  HIS F CB  1 
ATOM   6424  C  CG  . HIS F  1 121 ? 66.055  -15.113 24.428 1.00 18.94 ? 120  HIS F CG  1 
ATOM   6425  N  ND1 . HIS F  1 121 ? 66.811  -16.236 24.654 1.00 18.43 ? 120  HIS F ND1 1 
ATOM   6426  C  CD2 . HIS F  1 121 ? 65.517  -15.251 23.193 1.00 19.10 ? 120  HIS F CD2 1 
ATOM   6427  C  CE1 . HIS F  1 121 ? 66.738  -17.032 23.592 1.00 18.47 ? 120  HIS F CE1 1 
ATOM   6428  N  NE2 . HIS F  1 121 ? 65.961  -16.458 22.701 1.00 18.90 ? 120  HIS F NE2 1 
ATOM   6429  N  N   . GLU F  1 122 ? 65.837  -13.875 28.408 1.00 20.19 ? 121  GLU F N   1 
ATOM   6430  C  CA  . GLU F  1 122 ? 66.248  -13.301 29.680 1.00 21.53 ? 121  GLU F CA  1 
ATOM   6431  C  C   . GLU F  1 122 ? 66.922  -11.943 29.501 1.00 22.54 ? 121  GLU F C   1 
ATOM   6432  O  O   . GLU F  1 122 ? 66.619  -10.984 30.216 1.00 21.42 ? 121  GLU F O   1 
ATOM   6433  C  CB  . GLU F  1 122 ? 67.232  -14.255 30.352 1.00 23.43 ? 121  GLU F CB  1 
ATOM   6434  C  CG  . GLU F  1 122 ? 67.746  -13.792 31.704 1.00 29.75 ? 121  GLU F CG  1 
ATOM   6435  C  CD  . GLU F  1 122 ? 68.978  -14.562 32.148 1.00 34.12 ? 121  GLU F CD  1 
ATOM   6436  O  OE1 . GLU F  1 122 ? 69.427  -14.340 33.292 1.00 38.32 ? 121  GLU F OE1 1 
ATOM   6437  O  OE2 . GLU F  1 122 ? 69.506  -15.378 31.356 1.00 35.63 ? 121  GLU F OE2 1 
ATOM   6438  N  N   . LYS F  1 123 ? 67.844  -11.879 28.545 1.00 23.24 ? 122  LYS F N   1 
ATOM   6439  C  CA  . LYS F  1 123 ? 68.599  -10.656 28.276 1.00 25.20 ? 122  LYS F CA  1 
ATOM   6440  C  C   . LYS F  1 123 ? 68.339  -10.049 26.904 1.00 23.64 ? 122  LYS F C   1 
ATOM   6441  O  O   . LYS F  1 123 ? 67.589  -10.593 26.090 1.00 20.55 ? 122  LYS F O   1 
ATOM   6442  C  CB  . LYS F  1 123 ? 70.101  -10.931 28.397 1.00 27.42 ? 122  LYS F CB  1 
ATOM   6443  C  CG  . LYS F  1 123 ? 70.568  -11.309 29.790 1.00 34.36 ? 122  LYS F CG  1 
ATOM   6444  C  CD  . LYS F  1 123 ? 72.092  -11.394 29.856 1.00 38.65 ? 122  LYS F CD  1 
ATOM   6445  C  CE  . LYS F  1 123 ? 72.628  -12.395 28.852 1.00 40.28 ? 122  LYS F CE  1 
ATOM   6446  N  NZ  . LYS F  1 123 ? 74.117  -12.495 28.878 1.00 42.93 ? 122  LYS F NZ  1 
ATOM   6447  N  N   . ALA F  1 124 ? 68.989  -8.917  26.651 1.00 22.76 ? 123  ALA F N   1 
ATOM   6448  C  CA  . ALA F  1 124 ? 68.863  -8.238  25.370 1.00 22.38 ? 123  ALA F CA  1 
ATOM   6449  C  C   . ALA F  1 124 ? 69.683  -8.989  24.330 1.00 21.38 ? 123  ALA F C   1 
ATOM   6450  O  O   . ALA F  1 124 ? 70.677  -9.623  24.656 1.00 20.57 ? 123  ALA F O   1 
ATOM   6451  C  CB  . ALA F  1 124 ? 69.369  -6.798  25.485 1.00 26.18 ? 123  ALA F CB  1 
ATOM   6452  N  N   . ASP F  1 125 ? 69.237  -8.912  23.081 1.00 21.56 ? 124  ASP F N   1 
ATOM   6453  C  CA  . ASP F  1 125 ? 69.895  -9.532  21.939 1.00 20.24 ? 124  ASP F CA  1 
ATOM   6454  C  C   . ASP F  1 125 ? 70.843  -8.432  21.425 1.00 20.35 ? 124  ASP F C   1 
ATOM   6455  O  O   . ASP F  1 125 ? 70.395  -7.319  21.175 1.00 19.81 ? 124  ASP F O   1 
ATOM   6456  C  CB  . ASP F  1 125 ? 68.810  -9.881  20.906 1.00 20.66 ? 124  ASP F CB  1 
ATOM   6457  C  CG  . ASP F  1 125 ? 69.365  -10.442 19.604 1.00 23.55 ? 124  ASP F CG  1 
ATOM   6458  O  OD1 . ASP F  1 125 ? 68.565  -11.041 18.850 1.00 21.82 ? 124  ASP F OD1 1 
ATOM   6459  O  OD2 . ASP F  1 125 ? 70.571  -10.279 19.322 1.00 21.88 ? 124  ASP F OD2 1 
ATOM   6460  N  N   . ASP F  1 126 ? 72.136  -8.727  21.290 1.00 18.85 ? 125  ASP F N   1 
ATOM   6461  C  CA  . ASP F  1 126 ? 73.088  -7.705  20.831 1.00 22.25 ? 125  ASP F CA  1 
ATOM   6462  C  C   . ASP F  1 126 ? 73.141  -7.549  19.313 1.00 21.46 ? 125  ASP F C   1 
ATOM   6463  O  O   . ASP F  1 126 ? 74.020  -6.874  18.757 1.00 21.22 ? 125  ASP F O   1 
ATOM   6464  C  CB  . ASP F  1 126 ? 74.494  -7.964  21.416 1.00 20.22 ? 125  ASP F CB  1 
ATOM   6465  C  CG  . ASP F  1 126 ? 75.159  -9.219  20.873 1.00 23.22 ? 125  ASP F CG  1 
ATOM   6466  O  OD1 . ASP F  1 126 ? 76.128  -9.688  21.516 1.00 21.32 ? 125  ASP F OD1 1 
ATOM   6467  O  OD2 . ASP F  1 126 ? 74.746  -9.731  19.812 1.00 22.96 ? 125  ASP F OD2 1 
ATOM   6468  N  N   . LEU F  1 127 ? 72.174  -8.174  18.655 1.00 20.35 ? 126  LEU F N   1 
ATOM   6469  C  CA  . LEU F  1 127 ? 72.023  -8.112  17.213 1.00 20.66 ? 126  LEU F CA  1 
ATOM   6470  C  C   . LEU F  1 127 ? 73.245  -8.572  16.423 1.00 21.91 ? 126  LEU F C   1 
ATOM   6471  O  O   . LEU F  1 127 ? 73.460  -8.136  15.286 1.00 22.34 ? 126  LEU F O   1 
ATOM   6472  C  CB  . LEU F  1 127 ? 71.611  -6.690  16.813 1.00 22.00 ? 126  LEU F CB  1 
ATOM   6473  C  CG  . LEU F  1 127 ? 70.490  -6.084  17.678 1.00 24.99 ? 126  LEU F CG  1 
ATOM   6474  C  CD1 . LEU F  1 127 ? 70.128  -4.702  17.165 1.00 22.64 ? 126  LEU F CD1 1 
ATOM   6475  C  CD2 . LEU F  1 127 ? 69.256  -6.990  17.665 1.00 26.08 ? 126  LEU F CD2 1 
ATOM   6476  N  N   . GLY F  1 128 ? 74.031  -9.463  17.026 1.00 18.95 ? 127  GLY F N   1 
ATOM   6477  C  CA  . GLY F  1 128 ? 75.207  -10.007 16.361 1.00 20.33 ? 127  GLY F CA  1 
ATOM   6478  C  C   . GLY F  1 128 ? 76.436  -9.116  16.329 1.00 20.90 ? 127  GLY F C   1 
ATOM   6479  O  O   . GLY F  1 128 ? 77.383  -9.377  15.590 1.00 19.61 ? 127  GLY F O   1 
ATOM   6480  N  N   . LYS F  1 129 ? 76.439  -8.079  17.152 1.00 20.95 ? 128  LYS F N   1 
ATOM   6481  C  CA  . LYS F  1 129 ? 77.559  -7.142  17.185 1.00 23.10 ? 128  LYS F CA  1 
ATOM   6482  C  C   . LYS F  1 129 ? 78.354  -7.244  18.473 1.00 22.20 ? 128  LYS F C   1 
ATOM   6483  O  O   . LYS F  1 129 ? 79.029  -6.290  18.862 1.00 24.90 ? 128  LYS F O   1 
ATOM   6484  C  CB  . LYS F  1 129 ? 77.018  -5.724  17.024 1.00 21.86 ? 128  LYS F CB  1 
ATOM   6485  C  CG  . LYS F  1 129 ? 76.215  -5.552  15.738 1.00 26.30 ? 128  LYS F CG  1 
ATOM   6486  C  CD  . LYS F  1 129 ? 75.426  -4.252  15.719 1.00 29.79 ? 128  LYS F CD  1 
ATOM   6487  C  CE  . LYS F  1 129 ? 76.331  -3.039  15.668 1.00 32.08 ? 128  LYS F CE  1 
ATOM   6488  N  NZ  . LYS F  1 129 ? 75.513  -1.790  15.644 1.00 37.79 ? 128  LYS F NZ  1 
ATOM   6489  N  N   . GLY F  1 130 ? 78.284  -8.407  19.116 1.00 21.55 ? 129  GLY F N   1 
ATOM   6490  C  CA  . GLY F  1 130 ? 78.972  -8.615  20.383 1.00 22.48 ? 129  GLY F CA  1 
ATOM   6491  C  C   . GLY F  1 130 ? 80.453  -8.949  20.341 1.00 23.00 ? 129  GLY F C   1 
ATOM   6492  O  O   . GLY F  1 130 ? 81.145  -8.837  21.358 1.00 22.11 ? 129  GLY F O   1 
ATOM   6493  N  N   . GLY F  1 131 ? 80.951  -9.379  19.188 1.00 22.90 ? 130  GLY F N   1 
ATOM   6494  C  CA  . GLY F  1 131 ? 82.368  -9.690  19.089 1.00 22.59 ? 130  GLY F CA  1 
ATOM   6495  C  C   . GLY F  1 131 ? 82.806  -11.056 19.587 1.00 26.77 ? 130  GLY F C   1 
ATOM   6496  O  O   . GLY F  1 131 ? 83.997  -11.371 19.572 1.00 26.40 ? 130  GLY F O   1 
ATOM   6497  N  N   . ASN F  1 132 ? 81.862  -11.864 20.061 1.00 27.98 ? 131  ASN F N   1 
ATOM   6498  C  CA  . ASN F  1 132 ? 82.199  -13.203 20.514 1.00 29.28 ? 131  ASN F CA  1 
ATOM   6499  C  C   . ASN F  1 132 ? 81.379  -14.173 19.669 1.00 31.92 ? 131  ASN F C   1 
ATOM   6500  O  O   . ASN F  1 132 ? 80.430  -13.794 18.998 1.00 30.89 ? 131  ASN F O   1 
ATOM   6501  C  CB  . ASN F  1 132 ? 81.912  -13.402 22.016 1.00 31.20 ? 131  ASN F CB  1 
ATOM   6502  C  CG  . ASN F  1 132 ? 80.428  -13.293 22.368 1.00 32.35 ? 131  ASN F CG  1 
ATOM   6503  O  OD1 . ASN F  1 132 ? 79.578  -13.079 21.500 1.00 33.19 ? 131  ASN F OD1 1 
ATOM   6504  N  ND2 . ASN F  1 132 ? 80.115  -13.443 23.655 1.00 32.25 ? 131  ASN F ND2 1 
ATOM   6505  N  N   . GLU F  1 133 ? 81.766  -15.434 19.691 1.00 33.25 ? 132  GLU F N   1 
ATOM   6506  C  CA  . GLU F  1 133 ? 81.112  -16.475 18.903 1.00 35.18 ? 132  GLU F CA  1 
ATOM   6507  C  C   . GLU F  1 133 ? 79.604  -16.526 19.215 1.00 33.01 ? 132  GLU F C   1 
ATOM   6508  O  O   . GLU F  1 133 ? 78.758  -16.571 18.300 1.00 33.40 ? 132  GLU F O   1 
ATOM   6509  C  CB  . GLU F  1 133 ? 81.765  -17.833 19.217 1.00 40.28 ? 132  GLU F CB  1 
ATOM   6510  C  CG  . GLU F  1 133 ? 81.447  -18.937 18.233 1.00 47.93 ? 132  GLU F CG  1 
ATOM   6511  C  CD  . GLU F  1 133 ? 82.552  -19.118 17.224 1.00 54.12 ? 132  GLU F CD  1 
ATOM   6512  O  OE1 . GLU F  1 133 ? 82.415  -18.605 16.095 1.00 57.18 ? 132  GLU F OE1 1 
ATOM   6513  O  OE2 . GLU F  1 133 ? 83.571  -19.759 17.567 1.00 57.59 ? 132  GLU F OE2 1 
ATOM   6514  N  N   . GLU F  1 134 ? 79.269  -16.508 20.505 1.00 30.86 ? 133  GLU F N   1 
ATOM   6515  C  CA  . GLU F  1 134 ? 77.867  -16.575 20.906 1.00 29.97 ? 133  GLU F CA  1 
ATOM   6516  C  C   . GLU F  1 134 ? 77.013  -15.478 20.281 1.00 27.92 ? 133  GLU F C   1 
ATOM   6517  O  O   . GLU F  1 134 ? 75.826  -15.676 20.027 1.00 24.63 ? 133  GLU F O   1 
ATOM   6518  C  CB  . GLU F  1 134 ? 77.766  -16.484 22.421 1.00 32.57 ? 133  GLU F CB  1 
ATOM   6519  C  CG  . GLU F  1 134 ? 76.353  -16.718 23.026 1.00 38.96 ? 133  GLU F CG  1 
ATOM   6520  C  CD  . GLU F  1 134 ? 75.882  -18.179 22.934 1.00 41.67 ? 133  GLU F CD  1 
ATOM   6521  O  OE1 . GLU F  1 134 ? 74.674  -18.460 23.118 1.00 44.75 ? 133  GLU F OE1 1 
ATOM   6522  O  OE2 . GLU F  1 134 ? 76.734  -19.053 22.683 1.00 41.52 ? 133  GLU F OE2 1 
ATOM   6523  N  N   . SER F  1 135 ? 77.613  -14.311 20.071 1.00 25.19 ? 134  SER F N   1 
ATOM   6524  C  CA  . SER F  1 135 ? 76.894  -13.197 19.475 1.00 24.53 ? 134  SER F CA  1 
ATOM   6525  C  C   . SER F  1 135 ? 76.398  -13.561 18.081 1.00 23.84 ? 134  SER F C   1 
ATOM   6526  O  O   . SER F  1 135 ? 75.279  -13.217 17.708 1.00 24.63 ? 134  SER F O   1 
ATOM   6527  C  CB  . SER F  1 135 ? 77.791  -11.955 19.370 1.00 24.17 ? 134  SER F CB  1 
ATOM   6528  O  OG  . SER F  1 135 ? 77.116  -10.921 18.667 1.00 21.58 ? 134  SER F OG  1 
ATOM   6529  N  N   . THR F  1 136 ? 77.230  -14.254 17.310 1.00 23.85 ? 135  THR F N   1 
ATOM   6530  C  CA  . THR F  1 136 ? 76.863  -14.639 15.948 1.00 26.68 ? 135  THR F CA  1 
ATOM   6531  C  C   . THR F  1 136 ? 75.908  -15.829 15.915 1.00 27.92 ? 135  THR F C   1 
ATOM   6532  O  O   . THR F  1 136 ? 75.512  -16.285 14.840 1.00 27.74 ? 135  THR F O   1 
ATOM   6533  C  CB  . THR F  1 136 ? 78.103  -15.014 15.128 1.00 29.36 ? 135  THR F CB  1 
ATOM   6534  O  OG1 . THR F  1 136 ? 78.721  -16.171 15.707 1.00 35.02 ? 135  THR F OG1 1 
ATOM   6535  C  CG2 . THR F  1 136 ? 79.089  -13.874 15.122 1.00 31.52 ? 135  THR F CG2 1 
ATOM   6536  N  N   . LYS F  1 137 ? 75.552  -16.334 17.091 1.00 27.28 ? 136  LYS F N   1 
ATOM   6537  C  CA  . LYS F  1 137 ? 74.649  -17.472 17.179 1.00 30.12 ? 136  LYS F CA  1 
ATOM   6538  C  C   . LYS F  1 137 ? 73.320  -17.123 17.837 1.00 26.87 ? 136  LYS F C   1 
ATOM   6539  O  O   . LYS F  1 137 ? 72.259  -17.420 17.288 1.00 27.87 ? 136  LYS F O   1 
ATOM   6540  C  CB  . LYS F  1 137 ? 75.308  -18.615 17.958 1.00 33.06 ? 136  LYS F CB  1 
ATOM   6541  C  CG  . LYS F  1 137 ? 76.465  -19.271 17.232 1.00 39.31 ? 136  LYS F CG  1 
ATOM   6542  C  CD  . LYS F  1 137 ? 77.065  -20.406 18.054 1.00 44.66 ? 136  LYS F CD  1 
ATOM   6543  C  CE  . LYS F  1 137 ? 78.229  -21.061 17.320 1.00 48.19 ? 136  LYS F CE  1 
ATOM   6544  N  NZ  . LYS F  1 137 ? 78.832  -22.176 18.113 1.00 51.74 ? 136  LYS F NZ  1 
ATOM   6545  N  N   . THR F  1 138 ? 73.383  -16.492 19.006 1.00 25.55 ? 137  THR F N   1 
ATOM   6546  C  CA  . THR F  1 138 ? 72.177  -16.144 19.751 1.00 25.03 ? 137  THR F CA  1 
ATOM   6547  C  C   . THR F  1 138 ? 72.053  -14.676 20.135 1.00 24.31 ? 137  THR F C   1 
ATOM   6548  O  O   . THR F  1 138 ? 71.024  -14.262 20.665 1.00 21.76 ? 137  THR F O   1 
ATOM   6549  C  CB  . THR F  1 138 ? 72.104  -16.932 21.054 1.00 27.04 ? 137  THR F CB  1 
ATOM   6550  O  OG1 . THR F  1 138 ? 73.173  -16.506 21.908 1.00 25.83 ? 137  THR F OG1 1 
ATOM   6551  C  CG2 . THR F  1 138 ? 72.227  -18.429 20.792 1.00 24.88 ? 137  THR F CG2 1 
ATOM   6552  N  N   . GLY F  1 139 ? 73.094  -13.889 19.889 1.00 22.46 ? 138  GLY F N   1 
ATOM   6553  C  CA  . GLY F  1 139 ? 73.027  -12.489 20.260 1.00 22.15 ? 138  GLY F CA  1 
ATOM   6554  C  C   . GLY F  1 139 ? 73.226  -12.302 21.755 1.00 21.27 ? 138  GLY F C   1 
ATOM   6555  O  O   . GLY F  1 139 ? 72.986  -11.218 22.288 1.00 21.20 ? 138  GLY F O   1 
ATOM   6556  N  N   . ASN F  1 140 ? 73.676  -13.358 22.431 1.00 21.33 ? 139  ASN F N   1 
ATOM   6557  C  CA  . ASN F  1 140 ? 73.912  -13.310 23.872 1.00 21.51 ? 139  ASN F CA  1 
ATOM   6558  C  C   . ASN F  1 140 ? 72.629  -12.958 24.632 1.00 21.29 ? 139  ASN F C   1 
ATOM   6559  O  O   . ASN F  1 140 ? 72.677  -12.288 25.669 1.00 20.75 ? 139  ASN F O   1 
ATOM   6560  C  CB  . ASN F  1 140 ? 75.008  -12.277 24.190 1.00 23.51 ? 139  ASN F CB  1 
ATOM   6561  C  CG  . ASN F  1 140 ? 76.391  -12.734 23.748 1.00 25.98 ? 139  ASN F CG  1 
ATOM   6562  O  OD1 . ASN F  1 140 ? 76.938  -13.694 24.289 1.00 25.46 ? 139  ASN F OD1 1 
ATOM   6563  N  ND2 . ASN F  1 140 ? 76.960  -12.048 22.757 1.00 25.77 ? 139  ASN F ND2 1 
ATOM   6564  N  N   . ALA F  1 141 ? 71.489  -13.426 24.116 1.00 18.35 ? 140  ALA F N   1 
ATOM   6565  C  CA  . ALA F  1 141 ? 70.181  -13.152 24.716 1.00 19.81 ? 140  ALA F CA  1 
ATOM   6566  C  C   . ALA F  1 141 ? 69.886  -13.945 25.994 1.00 21.57 ? 140  ALA F C   1 
ATOM   6567  O  O   . ALA F  1 141 ? 68.860  -13.732 26.643 1.00 22.17 ? 140  ALA F O   1 
ATOM   6568  C  CB  . ALA F  1 141 ? 69.075  -13.401 23.679 1.00 19.22 ? 140  ALA F CB  1 
ATOM   6569  N  N   . GLY F  1 142 ? 70.769  -14.870 26.352 1.00 25.52 ? 141  GLY F N   1 
ATOM   6570  C  CA  . GLY F  1 142 ? 70.556  -15.634 27.572 1.00 24.86 ? 141  GLY F CA  1 
ATOM   6571  C  C   . GLY F  1 142 ? 69.439  -16.668 27.533 1.00 24.75 ? 141  GLY F C   1 
ATOM   6572  O  O   . GLY F  1 142 ? 69.016  -17.105 26.463 1.00 23.36 ? 141  GLY F O   1 
ATOM   6573  N  N   . SER F  1 143 ? 68.950  -17.047 28.711 1.00 24.57 ? 142  SER F N   1 
ATOM   6574  C  CA  . SER F  1 143 ? 67.915  -18.074 28.825 1.00 24.13 ? 142  SER F CA  1 
ATOM   6575  C  C   . SER F  1 143 ? 66.576  -17.761 28.166 1.00 22.93 ? 142  SER F C   1 
ATOM   6576  O  O   . SER F  1 143 ? 66.246  -16.613 27.861 1.00 21.56 ? 142  SER F O   1 
ATOM   6577  C  CB  . SER F  1 143 ? 67.681  -18.433 30.300 1.00 26.09 ? 142  SER F CB  1 
ATOM   6578  O  OG  . SER F  1 143 ? 66.954  -17.415 30.973 1.00 27.39 ? 142  SER F OG  1 
ATOM   6579  N  N   . ARG F  1 144 ? 65.806  -18.820 27.956 1.00 23.28 ? 143  ARG F N   1 
ATOM   6580  C  CA  . ARG F  1 144 ? 64.497  -18.725 27.339 1.00 21.96 ? 143  ARG F CA  1 
ATOM   6581  C  C   . ARG F  1 144 ? 63.473  -18.629 28.466 1.00 21.56 ? 143  ARG F C   1 
ATOM   6582  O  O   . ARG F  1 144 ? 63.211  -19.607 29.162 1.00 22.39 ? 143  ARG F O   1 
ATOM   6583  C  CB  . ARG F  1 144 ? 64.292  -19.971 26.481 1.00 21.04 ? 143  ARG F CB  1 
ATOM   6584  C  CG  . ARG F  1 144 ? 65.494  -20.201 25.568 1.00 22.05 ? 143  ARG F CG  1 
ATOM   6585  C  CD  . ARG F  1 144 ? 65.375  -21.398 24.657 1.00 21.82 ? 143  ARG F CD  1 
ATOM   6586  N  NE  . ARG F  1 144 ? 66.589  -21.538 23.856 1.00 22.65 ? 143  ARG F NE  1 
ATOM   6587  C  CZ  . ARG F  1 144 ? 66.748  -22.410 22.865 1.00 23.90 ? 143  ARG F CZ  1 
ATOM   6588  N  NH1 . ARG F  1 144 ? 67.895  -22.451 22.201 1.00 23.34 ? 143  ARG F NH1 1 
ATOM   6589  N  NH2 . ARG F  1 144 ? 65.760  -23.237 22.533 1.00 21.96 ? 143  ARG F NH2 1 
ATOM   6590  N  N   . LEU F  1 145 ? 62.905  -17.442 28.648 1.00 21.94 ? 144  LEU F N   1 
ATOM   6591  C  CA  . LEU F  1 145 ? 61.933  -17.212 29.720 1.00 21.35 ? 144  LEU F CA  1 
ATOM   6592  C  C   . LEU F  1 145 ? 60.553  -17.789 29.432 1.00 20.41 ? 144  LEU F C   1 
ATOM   6593  O  O   . LEU F  1 145 ? 59.876  -18.277 30.334 1.00 18.88 ? 144  LEU F O   1 
ATOM   6594  C  CB  . LEU F  1 145 ? 61.808  -15.715 30.001 1.00 20.08 ? 144  LEU F CB  1 
ATOM   6595  C  CG  . LEU F  1 145 ? 63.091  -14.974 30.398 1.00 22.64 ? 144  LEU F CG  1 
ATOM   6596  C  CD1 . LEU F  1 145 ? 62.735  -13.545 30.789 1.00 22.99 ? 144  LEU F CD1 1 
ATOM   6597  C  CD2 . LEU F  1 145 ? 63.777  -15.681 31.560 1.00 24.71 ? 144  LEU F CD2 1 
ATOM   6598  N  N   . ALA F  1 146 ? 60.131  -17.716 28.178 1.00 19.42 ? 145  ALA F N   1 
ATOM   6599  C  CA  . ALA F  1 146 ? 58.832  -18.245 27.784 1.00 20.48 ? 145  ALA F CA  1 
ATOM   6600  C  C   . ALA F  1 146 ? 58.837  -18.494 26.283 1.00 20.62 ? 145  ALA F C   1 
ATOM   6601  O  O   . ALA F  1 146 ? 59.580  -17.854 25.536 1.00 20.66 ? 145  ALA F O   1 
ATOM   6602  C  CB  . ALA F  1 146 ? 57.720  -17.263 28.153 1.00 22.27 ? 145  ALA F CB  1 
ATOM   6603  N  N   . CYS F  1 147 ? 57.996  -19.421 25.848 1.00 17.50 ? 146  CYS F N   1 
ATOM   6604  C  CA  . CYS F  1 147 ? 57.919  -19.775 24.446 1.00 18.06 ? 146  CYS F CA  1 
ATOM   6605  C  C   . CYS F  1 147 ? 56.560  -20.383 24.141 1.00 18.80 ? 146  CYS F C   1 
ATOM   6606  O  O   . CYS F  1 147 ? 55.792  -20.725 25.050 1.00 16.60 ? 146  CYS F O   1 
ATOM   6607  C  CB  . CYS F  1 147 ? 59.029  -20.782 24.106 1.00 18.63 ? 146  CYS F CB  1 
ATOM   6608  S  SG  . CYS F  1 147 ? 58.983  -22.294 25.130 1.00 22.86 ? 146  CYS F SG  1 
ATOM   6609  N  N   . GLY F  1 148 ? 56.271  -20.509 22.852 1.00 16.99 ? 147  GLY F N   1 
ATOM   6610  C  CA  . GLY F  1 148 ? 55.010  -21.086 22.425 1.00 18.04 ? 147  GLY F CA  1 
ATOM   6611  C  C   . GLY F  1 148 ? 55.079  -21.450 20.957 1.00 19.54 ? 147  GLY F C   1 
ATOM   6612  O  O   . GLY F  1 148 ? 55.763  -20.777 20.173 1.00 16.48 ? 147  GLY F O   1 
ATOM   6613  N  N   . VAL F  1 149 ? 54.396  -22.527 20.580 1.00 17.57 ? 148  VAL F N   1 
ATOM   6614  C  CA  . VAL F  1 149 ? 54.379  -22.937 19.187 1.00 16.86 ? 148  VAL F CA  1 
ATOM   6615  C  C   . VAL F  1 149 ? 53.477  -21.975 18.421 1.00 17.70 ? 148  VAL F C   1 
ATOM   6616  O  O   . VAL F  1 149 ? 52.401  -21.601 18.887 1.00 18.88 ? 148  VAL F O   1 
ATOM   6617  C  CB  . VAL F  1 149 ? 53.861  -24.393 19.034 1.00 18.47 ? 148  VAL F CB  1 
ATOM   6618  C  CG1 . VAL F  1 149 ? 53.869  -24.806 17.555 1.00 15.64 ? 148  VAL F CG1 1 
ATOM   6619  C  CG2 . VAL F  1 149 ? 54.749  -25.336 19.841 1.00 18.27 ? 148  VAL F CG2 1 
ATOM   6620  N  N   . ILE F  1 150 ? 53.931  -21.562 17.245 1.00 17.92 ? 149  ILE F N   1 
ATOM   6621  C  CA  . ILE F  1 150 ? 53.174  -20.632 16.423 1.00 19.20 ? 149  ILE F CA  1 
ATOM   6622  C  C   . ILE F  1 150 ? 52.135  -21.419 15.622 1.00 20.44 ? 149  ILE F C   1 
ATOM   6623  O  O   . ILE F  1 150 ? 52.490  -22.231 14.769 1.00 19.52 ? 149  ILE F O   1 
ATOM   6624  C  CB  . ILE F  1 150 ? 54.128  -19.875 15.479 1.00 19.79 ? 149  ILE F CB  1 
ATOM   6625  C  CG1 . ILE F  1 150 ? 55.175  -19.129 16.322 1.00 18.91 ? 149  ILE F CG1 1 
ATOM   6626  C  CG2 . ILE F  1 150 ? 53.346  -18.903 14.594 1.00 21.38 ? 149  ILE F CG2 1 
ATOM   6627  C  CD1 . ILE F  1 150 ? 56.398  -18.685 15.541 1.00 19.71 ? 149  ILE F CD1 1 
ATOM   6628  N  N   . GLY F  1 151 ? 50.859  -21.181 15.909 1.00 20.03 ? 150  GLY F N   1 
ATOM   6629  C  CA  . GLY F  1 151 ? 49.807  -21.905 15.214 1.00 21.60 ? 150  GLY F CA  1 
ATOM   6630  C  C   . GLY F  1 151 ? 48.927  -21.064 14.312 1.00 21.94 ? 150  GLY F C   1 
ATOM   6631  O  O   . GLY F  1 151 ? 48.912  -19.836 14.410 1.00 20.21 ? 150  GLY F O   1 
ATOM   6632  N  N   . ILE F  1 152 ? 48.200  -21.735 13.421 1.00 21.04 ? 151  ILE F N   1 
ATOM   6633  C  CA  . ILE F  1 152 ? 47.293  -21.073 12.491 1.00 20.97 ? 151  ILE F CA  1 
ATOM   6634  C  C   . ILE F  1 152 ? 46.109  -20.488 13.257 1.00 22.89 ? 151  ILE F C   1 
ATOM   6635  O  O   . ILE F  1 152 ? 45.500  -21.170 14.084 1.00 22.17 ? 151  ILE F O   1 
ATOM   6636  C  CB  . ILE F  1 152 ? 46.772  -22.074 11.424 1.00 20.91 ? 151  ILE F CB  1 
ATOM   6637  C  CG1 . ILE F  1 152 ? 47.939  -22.576 10.573 1.00 20.49 ? 151  ILE F CG1 1 
ATOM   6638  C  CG2 . ILE F  1 152 ? 45.707  -21.411 10.556 1.00 22.49 ? 151  ILE F CG2 1 
ATOM   6639  C  CD1 . ILE F  1 152 ? 47.581  -23.733 9.642  1.00 23.38 ? 151  ILE F CD1 1 
ATOM   6640  N  N   . ALA F  1 153 ? 45.781  -19.226 12.983 1.00 22.49 ? 152  ALA F N   1 
ATOM   6641  C  CA  . ALA F  1 153 ? 44.675  -18.573 13.674 1.00 25.13 ? 152  ALA F CA  1 
ATOM   6642  C  C   . ALA F  1 153 ? 43.557  -18.188 12.719 1.00 26.32 ? 152  ALA F C   1 
ATOM   6643  O  O   . ALA F  1 153 ? 43.781  -18.035 11.520 1.00 24.38 ? 152  ALA F O   1 
ATOM   6644  C  CB  . ALA F  1 153 ? 45.173  -17.341 14.417 1.00 24.79 ? 152  ALA F CB  1 
ATOM   6645  N  N   . GLN F  1 154 ? 42.353  -18.032 13.260 1.00 28.31 ? 153  GLN F N   1 
ATOM   6646  C  CA  . GLN F  1 154 ? 41.198  -17.670 12.452 1.00 33.86 ? 153  GLN F CA  1 
ATOM   6647  C  C   . GLN F  1 154 ? 41.251  -16.191 12.075 1.00 35.38 ? 153  GLN F C   1 
ATOM   6648  O  O   . GLN F  1 154 ? 41.715  -15.388 12.912 1.00 37.50 ? 153  GLN F O   1 
ATOM   6649  C  CB  . GLN F  1 154 ? 39.910  -17.954 13.226 1.00 33.81 ? 153  GLN F CB  1 
ATOM   6650  C  CG  . GLN F  1 154 ? 38.649  -17.844 12.386 1.00 38.72 ? 153  GLN F CG  1 
ATOM   6651  C  CD  . GLN F  1 154 ? 37.390  -18.104 13.191 1.00 40.28 ? 153  GLN F CD  1 
ATOM   6652  O  OE1 . GLN F  1 154 ? 36.403  -18.614 12.666 1.00 44.62 ? 153  GLN F OE1 1 
ATOM   6653  N  NE2 . GLN F  1 154 ? 37.417  -17.746 14.468 1.00 40.35 ? 153  GLN F NE2 1 
ATOM   6654  O  OXT . GLN F  1 154 ? 40.812  -15.855 10.955 1.00 37.96 ? 153  GLN F OXT 1 
ATOM   6655  N  N   . ALA G  1 2   ? 153.983 3.887   8.426  0.00 51.94 ? 1    ALA G N   1 
ATOM   6656  C  CA  . ALA G  1 2   ? 155.187 4.687   8.790  0.00 51.73 ? 1    ALA G CA  1 
ATOM   6657  C  C   . ALA G  1 2   ? 156.359 3.770   9.122  1.00 51.78 ? 1    ALA G C   1 
ATOM   6658  O  O   . ALA G  1 2   ? 156.418 2.633   8.656  1.00 52.11 ? 1    ALA G O   1 
ATOM   6659  C  CB  . ALA G  1 2   ? 154.873 5.587   9.980  0.00 51.97 ? 1    ALA G CB  1 
ATOM   6660  N  N   . THR G  1 3   ? 157.291 4.271   9.928  1.00 50.19 ? 2    THR G N   1 
ATOM   6661  C  CA  . THR G  1 3   ? 158.459 3.493   10.321 1.00 49.14 ? 2    THR G CA  1 
ATOM   6662  C  C   . THR G  1 3   ? 158.247 2.837   11.680 1.00 46.08 ? 2    THR G C   1 
ATOM   6663  O  O   . THR G  1 3   ? 158.764 1.752   11.936 1.00 44.21 ? 2    THR G O   1 
ATOM   6664  C  CB  . THR G  1 3   ? 159.723 4.374   10.405 1.00 50.04 ? 2    THR G CB  1 
ATOM   6665  O  OG1 . THR G  1 3   ? 160.015 4.916   9.114  1.00 53.82 ? 2    THR G OG1 1 
ATOM   6666  C  CG2 . THR G  1 3   ? 160.915 3.553   10.881 1.00 52.00 ? 2    THR G CG2 1 
ATOM   6667  N  N   . LYS G  1 4   ? 157.488 3.501   12.547 1.00 44.03 ? 3    LYS G N   1 
ATOM   6668  C  CA  . LYS G  1 4   ? 157.220 2.976   13.882 1.00 42.65 ? 3    LYS G CA  1 
ATOM   6669  C  C   . LYS G  1 4   ? 155.732 2.921   14.205 1.00 40.07 ? 3    LYS G C   1 
ATOM   6670  O  O   . LYS G  1 4   ? 154.941 3.722   13.707 1.00 39.19 ? 3    LYS G O   1 
ATOM   6671  C  CB  . LYS G  1 4   ? 157.937 3.820   14.940 1.00 43.71 ? 3    LYS G CB  1 
ATOM   6672  C  CG  . LYS G  1 4   ? 159.449 3.714   14.906 1.00 46.59 ? 3    LYS G CG  1 
ATOM   6673  C  CD  . LYS G  1 4   ? 160.079 4.571   15.992 0.00 49.00 ? 3    LYS G CD  1 
ATOM   6674  C  CE  . LYS G  1 4   ? 161.591 4.458   15.970 1.00 52.46 ? 3    LYS G CE  1 
ATOM   6675  N  NZ  . LYS G  1 4   ? 162.229 5.300   17.026 1.00 55.25 ? 3    LYS G NZ  1 
ATOM   6676  N  N   . ALA G  1 5   ? 155.359 1.964   15.045 1.00 37.29 ? 4    ALA G N   1 
ATOM   6677  C  CA  . ALA G  1 5   ? 153.971 1.794   15.451 1.00 34.92 ? 4    ALA G CA  1 
ATOM   6678  C  C   . ALA G  1 5   ? 153.963 1.210   16.853 1.00 33.46 ? 4    ALA G C   1 
ATOM   6679  O  O   . ALA G  1 5   ? 154.952 0.627   17.290 1.00 33.15 ? 4    ALA G O   1 
ATOM   6680  C  CB  . ALA G  1 5   ? 153.251 0.863   14.484 1.00 35.10 ? 4    ALA G CB  1 
ATOM   6681  N  N   . VAL G  1 6   ? 152.850 1.372   17.558 1.00 32.84 ? 5    VAL G N   1 
ATOM   6682  C  CA  . VAL G  1 6   ? 152.735 0.859   18.914 1.00 31.17 ? 5    VAL G CA  1 
ATOM   6683  C  C   . VAL G  1 6   ? 151.316 0.398   19.211 1.00 31.86 ? 5    VAL G C   1 
ATOM   6684  O  O   . VAL G  1 6   ? 150.349 0.886   18.620 1.00 28.23 ? 5    VAL G O   1 
ATOM   6685  C  CB  . VAL G  1 6   ? 153.134 1.936   19.952 1.00 32.14 ? 5    VAL G CB  1 
ATOM   6686  C  CG1 . VAL G  1 6   ? 152.235 3.156   19.809 1.00 30.57 ? 5    VAL G CG1 1 
ATOM   6687  C  CG2 . VAL G  1 6   ? 153.035 1.365   21.367 1.00 30.81 ? 5    VAL G CG2 1 
ATOM   6688  N  N   . ALA G  1 7   ? 151.196 -0.553  20.129 1.00 32.53 ? 6    ALA G N   1 
ATOM   6689  C  CA  . ALA G  1 7   ? 149.893 -1.060  20.515 1.00 33.54 ? 6    ALA G CA  1 
ATOM   6690  C  C   . ALA G  1 7   ? 149.855 -1.300  22.020 1.00 35.76 ? 6    ALA G C   1 
ATOM   6691  O  O   . ALA G  1 7   ? 150.748 -1.945  22.579 1.00 36.51 ? 6    ALA G O   1 
ATOM   6692  C  CB  . ALA G  1 7   ? 149.588 -2.349  19.765 1.00 34.04 ? 6    ALA G CB  1 
ATOM   6693  N  N   . VAL G  1 8   ? 148.830 -0.759  22.673 1.00 34.56 ? 7    VAL G N   1 
ATOM   6694  C  CA  . VAL G  1 8   ? 148.653 -0.932  24.110 1.00 34.11 ? 7    VAL G CA  1 
ATOM   6695  C  C   . VAL G  1 8   ? 147.555 -1.976  24.289 1.00 34.59 ? 7    VAL G C   1 
ATOM   6696  O  O   . VAL G  1 8   ? 146.423 -1.783  23.843 1.00 32.33 ? 7    VAL G O   1 
ATOM   6697  C  CB  . VAL G  1 8   ? 148.242 0.391   24.783 1.00 34.33 ? 7    VAL G CB  1 
ATOM   6698  C  CG1 . VAL G  1 8   ? 147.894 0.153   26.241 1.00 33.64 ? 7    VAL G CG1 1 
ATOM   6699  C  CG2 . VAL G  1 8   ? 149.378 1.395   24.671 1.00 34.96 ? 7    VAL G CG2 1 
ATOM   6700  N  N   . LEU G  1 9   ? 147.902 -3.085  24.935 1.00 34.96 ? 8    LEU G N   1 
ATOM   6701  C  CA  . LEU G  1 9   ? 146.970 -4.187  25.142 1.00 35.04 ? 8    LEU G CA  1 
ATOM   6702  C  C   . LEU G  1 9   ? 146.205 -4.115  26.460 1.00 36.89 ? 8    LEU G C   1 
ATOM   6703  O  O   . LEU G  1 9   ? 146.795 -3.948  27.530 1.00 36.79 ? 8    LEU G O   1 
ATOM   6704  C  CB  . LEU G  1 9   ? 147.730 -5.515  25.067 1.00 34.99 ? 8    LEU G CB  1 
ATOM   6705  C  CG  . LEU G  1 9   ? 148.599 -5.718  23.815 1.00 36.01 ? 8    LEU G CG  1 
ATOM   6706  C  CD1 . LEU G  1 9   ? 149.476 -6.955  23.978 1.00 35.99 ? 8    LEU G CD1 1 
ATOM   6707  C  CD2 . LEU G  1 9   ? 147.701 -5.854  22.593 1.00 35.04 ? 8    LEU G CD2 1 
ATOM   6708  N  N   . LYS G  1 10  ? 144.885 -4.248  26.366 1.00 38.08 ? 9    LYS G N   1 
ATOM   6709  C  CA  . LYS G  1 10  ? 144.005 -4.225  27.531 1.00 39.69 ? 9    LYS G CA  1 
ATOM   6710  C  C   . LYS G  1 10  ? 142.801 -5.116  27.235 1.00 39.69 ? 9    LYS G C   1 
ATOM   6711  O  O   . LYS G  1 10  ? 142.452 -5.337  26.071 1.00 36.79 ? 9    LYS G O   1 
ATOM   6712  C  CB  . LYS G  1 10  ? 143.542 -2.794  27.830 1.00 41.82 ? 9    LYS G CB  1 
ATOM   6713  C  CG  . LYS G  1 10  ? 144.686 -1.840  28.130 1.00 46.17 ? 9    LYS G CG  1 
ATOM   6714  C  CD  . LYS G  1 10  ? 144.214 -0.414  28.385 1.00 49.74 ? 9    LYS G CD  1 
ATOM   6715  C  CE  . LYS G  1 10  ? 145.404 0.497   28.670 1.00 51.32 ? 9    LYS G CE  1 
ATOM   6716  N  NZ  . LYS G  1 10  ? 145.006 1.892   28.987 1.00 53.95 ? 9    LYS G NZ  1 
ATOM   6717  N  N   . GLY G  1 11  ? 142.179 -5.631  28.290 1.00 38.82 ? 10   GLY G N   1 
ATOM   6718  C  CA  . GLY G  1 11  ? 141.028 -6.497  28.119 1.00 41.23 ? 10   GLY G CA  1 
ATOM   6719  C  C   . GLY G  1 11  ? 140.149 -6.518  29.353 1.00 41.73 ? 10   GLY G C   1 
ATOM   6720  O  O   . GLY G  1 11  ? 140.227 -5.620  30.190 1.00 41.44 ? 10   GLY G O   1 
ATOM   6721  N  N   . ASP G  1 12  ? 139.319 -7.548  29.473 1.00 44.42 ? 11   ASP G N   1 
ATOM   6722  C  CA  . ASP G  1 12  ? 138.410 -7.670  30.607 1.00 47.33 ? 11   ASP G CA  1 
ATOM   6723  C  C   . ASP G  1 12  ? 139.092 -8.217  31.855 1.00 47.72 ? 11   ASP G C   1 
ATOM   6724  O  O   . ASP G  1 12  ? 138.549 -8.128  32.958 1.00 48.32 ? 11   ASP G O   1 
ATOM   6725  C  CB  . ASP G  1 12  ? 137.229 -8.568  30.234 1.00 50.68 ? 11   ASP G CB  1 
ATOM   6726  C  CG  . ASP G  1 12  ? 136.504 -8.083  28.996 1.00 53.36 ? 11   ASP G CG  1 
ATOM   6727  O  OD1 . ASP G  1 12  ? 136.207 -6.871  28.924 1.00 55.72 ? 11   ASP G OD1 1 
ATOM   6728  O  OD2 . ASP G  1 12  ? 136.230 -8.910  28.100 1.00 56.73 ? 11   ASP G OD2 1 
ATOM   6729  N  N   . GLY G  1 13  ? 140.284 -8.777  31.676 1.00 47.98 ? 12   GLY G N   1 
ATOM   6730  C  CA  . GLY G  1 13  ? 141.019 -9.329  32.800 1.00 45.25 ? 12   GLY G CA  1 
ATOM   6731  C  C   . GLY G  1 13  ? 142.218 -8.483  33.188 1.00 44.39 ? 12   GLY G C   1 
ATOM   6732  O  O   . GLY G  1 13  ? 142.221 -7.269  32.968 1.00 43.76 ? 12   GLY G O   1 
ATOM   6733  N  N   . PRO G  1 14  ? 143.259 -9.100  33.772 1.00 42.68 ? 13   PRO G N   1 
ATOM   6734  C  CA  . PRO G  1 14  ? 144.474 -8.400  34.199 1.00 41.77 ? 13   PRO G CA  1 
ATOM   6735  C  C   . PRO G  1 14  ? 145.565 -8.319  33.132 1.00 40.58 ? 13   PRO G C   1 
ATOM   6736  O  O   . PRO G  1 14  ? 146.580 -7.645  33.324 1.00 39.71 ? 13   PRO G O   1 
ATOM   6737  C  CB  . PRO G  1 14  ? 144.923 -9.225  35.394 1.00 41.42 ? 13   PRO G CB  1 
ATOM   6738  C  CG  . PRO G  1 14  ? 144.629 -10.610 34.918 1.00 40.11 ? 13   PRO G CG  1 
ATOM   6739  C  CD  . PRO G  1 14  ? 143.249 -10.480 34.294 1.00 41.69 ? 13   PRO G CD  1 
ATOM   6740  N  N   . VAL G  1 15  ? 145.364 -9.006  32.013 1.00 40.83 ? 14   VAL G N   1 
ATOM   6741  C  CA  . VAL G  1 15  ? 146.364 -9.001  30.948 1.00 40.25 ? 14   VAL G CA  1 
ATOM   6742  C  C   . VAL G  1 15  ? 146.508 -7.626  30.318 1.00 40.82 ? 14   VAL G C   1 
ATOM   6743  O  O   . VAL G  1 15  ? 145.525 -7.008  29.908 1.00 39.65 ? 14   VAL G O   1 
ATOM   6744  C  CB  . VAL G  1 15  ? 146.020 -10.007 29.835 1.00 40.17 ? 14   VAL G CB  1 
ATOM   6745  C  CG1 . VAL G  1 15  ? 147.123 -10.004 28.786 1.00 37.73 ? 14   VAL G CG1 1 
ATOM   6746  C  CG2 . VAL G  1 15  ? 145.844 -11.396 30.424 1.00 39.29 ? 14   VAL G CG2 1 
ATOM   6747  N  N   . GLN G  1 16  ? 147.744 -7.150  30.240 1.00 41.46 ? 15   GLN G N   1 
ATOM   6748  C  CA  . GLN G  1 16  ? 148.009 -5.847  29.655 1.00 42.47 ? 15   GLN G CA  1 
ATOM   6749  C  C   . GLN G  1 16  ? 149.470 -5.759  29.237 1.00 42.56 ? 15   GLN G C   1 
ATOM   6750  O  O   . GLN G  1 16  ? 150.322 -6.489  29.754 1.00 40.98 ? 15   GLN G O   1 
ATOM   6751  C  CB  . GLN G  1 16  ? 147.679 -4.743  30.664 1.00 44.56 ? 15   GLN G CB  1 
ATOM   6752  C  CG  . GLN G  1 16  ? 148.674 -4.600  31.802 1.00 49.07 ? 15   GLN G CG  1 
ATOM   6753  C  CD  . GLN G  1 16  ? 148.167 -3.674  32.898 1.00 52.69 ? 15   GLN G CD  1 
ATOM   6754  O  OE1 . GLN G  1 16  ? 148.950 -3.030  33.601 1.00 53.09 ? 15   GLN G OE1 1 
ATOM   6755  N  NE2 . GLN G  1 16  ? 146.849 -3.617  33.058 1.00 54.25 ? 15   GLN G NE2 1 
ATOM   6756  N  N   . GLY G  1 17  ? 149.757 -4.872  28.292 1.00 41.56 ? 16   GLY G N   1 
ATOM   6757  C  CA  . GLY G  1 17  ? 151.123 -4.724  27.837 1.00 40.47 ? 16   GLY G CA  1 
ATOM   6758  C  C   . GLY G  1 17  ? 151.281 -3.693  26.743 1.00 39.79 ? 16   GLY G C   1 
ATOM   6759  O  O   . GLY G  1 17  ? 150.302 -3.129  26.257 1.00 37.39 ? 16   GLY G O   1 
ATOM   6760  N  N   . ILE G  1 18  ? 152.532 -3.453  26.368 1.00 39.40 ? 17   ILE G N   1 
ATOM   6761  C  CA  . ILE G  1 18  ? 152.884 -2.497  25.329 1.00 40.67 ? 17   ILE G CA  1 
ATOM   6762  C  C   . ILE G  1 18  ? 153.793 -3.193  24.317 1.00 41.12 ? 17   ILE G C   1 
ATOM   6763  O  O   . ILE G  1 18  ? 154.862 -3.685  24.680 1.00 40.64 ? 17   ILE G O   1 
ATOM   6764  C  CB  . ILE G  1 18  ? 153.653 -1.298  25.917 1.00 41.19 ? 17   ILE G CB  1 
ATOM   6765  C  CG1 . ILE G  1 18  ? 152.782 -0.581  26.953 1.00 43.79 ? 17   ILE G CG1 1 
ATOM   6766  C  CG2 . ILE G  1 18  ? 154.065 -0.345  24.799 1.00 41.56 ? 17   ILE G CG2 1 
ATOM   6767  C  CD1 . ILE G  1 18  ? 153.482 0.566   27.649 1.00 43.07 ? 17   ILE G CD1 1 
ATOM   6768  N  N   . ILE G  1 19  ? 153.366 -3.234  23.058 1.00 39.72 ? 18   ILE G N   1 
ATOM   6769  C  CA  . ILE G  1 19  ? 154.155 -3.869  22.007 1.00 39.36 ? 18   ILE G CA  1 
ATOM   6770  C  C   . ILE G  1 19  ? 154.560 -2.834  20.964 1.00 40.34 ? 18   ILE G C   1 
ATOM   6771  O  O   . ILE G  1 19  ? 153.718 -2.096  20.447 1.00 39.80 ? 18   ILE G O   1 
ATOM   6772  C  CB  . ILE G  1 19  ? 153.360 -5.000  21.313 1.00 39.96 ? 18   ILE G CB  1 
ATOM   6773  C  CG1 . ILE G  1 19  ? 152.997 -6.089  22.329 1.00 39.11 ? 18   ILE G CG1 1 
ATOM   6774  C  CG2 . ILE G  1 19  ? 154.187 -5.602  20.191 1.00 37.74 ? 18   ILE G CG2 1 
ATOM   6775  C  CD1 . ILE G  1 19  ? 154.205 -6.788  22.951 1.00 41.08 ? 18   ILE G CD1 1 
ATOM   6776  N  N   . ASN G  1 20  ? 155.853 -2.790  20.658 1.00 40.39 ? 19   ASN G N   1 
ATOM   6777  C  CA  . ASN G  1 20  ? 156.391 -1.840  19.692 1.00 40.33 ? 19   ASN G CA  1 
ATOM   6778  C  C   . ASN G  1 20  ? 156.685 -2.478  18.340 1.00 40.31 ? 19   ASN G C   1 
ATOM   6779  O  O   . ASN G  1 20  ? 157.012 -3.660  18.255 1.00 39.62 ? 19   ASN G O   1 
ATOM   6780  C  CB  . ASN G  1 20  ? 157.668 -1.207  20.241 1.00 40.45 ? 19   ASN G CB  1 
ATOM   6781  C  CG  . ASN G  1 20  ? 157.446 -0.513  21.569 1.00 42.73 ? 19   ASN G CG  1 
ATOM   6782  O  OD1 . ASN G  1 20  ? 156.691 0.455   21.658 1.00 45.34 ? 19   ASN G OD1 1 
ATOM   6783  N  ND2 . ASN G  1 20  ? 158.100 -1.010  22.614 1.00 41.63 ? 19   ASN G ND2 1 
ATOM   6784  N  N   . PHE G  1 21  ? 156.562 -1.678  17.286 1.00 39.96 ? 20   PHE G N   1 
ATOM   6785  C  CA  . PHE G  1 21  ? 156.814 -2.139  15.926 1.00 39.76 ? 20   PHE G CA  1 
ATOM   6786  C  C   . PHE G  1 21  ? 157.737 -1.136  15.240 1.00 41.68 ? 20   PHE G C   1 
ATOM   6787  O  O   . PHE G  1 21  ? 157.580 0.079   15.399 1.00 40.20 ? 20   PHE G O   1 
ATOM   6788  C  CB  . PHE G  1 21  ? 155.513 -2.213  15.122 1.00 37.29 ? 20   PHE G CB  1 
ATOM   6789  C  CG  . PHE G  1 21  ? 154.470 -3.131  15.705 1.00 36.38 ? 20   PHE G CG  1 
ATOM   6790  C  CD1 . PHE G  1 21  ? 154.329 -4.432  15.238 1.00 35.29 ? 20   PHE G CD1 1 
ATOM   6791  C  CD2 . PHE G  1 21  ? 153.604 -2.680  16.699 1.00 35.41 ? 20   PHE G CD2 1 
ATOM   6792  C  CE1 . PHE G  1 21  ? 153.342 -5.273  15.748 1.00 34.36 ? 20   PHE G CE1 1 
ATOM   6793  C  CE2 . PHE G  1 21  ? 152.609 -3.519  17.218 1.00 34.32 ? 20   PHE G CE2 1 
ATOM   6794  C  CZ  . PHE G  1 21  ? 152.481 -4.814  16.738 1.00 33.61 ? 20   PHE G CZ  1 
ATOM   6795  N  N   . GLU G  1 22  ? 158.703 -1.640  14.484 1.00 42.87 ? 21   GLU G N   1 
ATOM   6796  C  CA  . GLU G  1 22  ? 159.603 -0.760  13.754 1.00 45.19 ? 21   GLU G CA  1 
ATOM   6797  C  C   . GLU G  1 22  ? 159.984 -1.404  12.433 1.00 45.21 ? 21   GLU G C   1 
ATOM   6798  O  O   . GLU G  1 22  ? 160.408 -2.559  12.390 1.00 43.99 ? 21   GLU G O   1 
ATOM   6799  C  CB  . GLU G  1 22  ? 160.859 -0.437  14.566 1.00 46.71 ? 21   GLU G CB  1 
ATOM   6800  C  CG  . GLU G  1 22  ? 161.746 0.597   13.881 1.00 50.95 ? 21   GLU G CG  1 
ATOM   6801  C  CD  . GLU G  1 22  ? 162.770 1.224   14.812 1.00 54.02 ? 21   GLU G CD  1 
ATOM   6802  O  OE1 . GLU G  1 22  ? 163.568 2.058   14.335 1.00 55.17 ? 21   GLU G OE1 1 
ATOM   6803  O  OE2 . GLU G  1 22  ? 162.775 0.891   16.016 1.00 55.49 ? 21   GLU G OE2 1 
ATOM   6804  N  N   . GLN G  1 23  ? 159.815 -0.643  11.357 1.00 44.98 ? 22   GLN G N   1 
ATOM   6805  C  CA  . GLN G  1 23  ? 160.121 -1.110  10.014 1.00 47.13 ? 22   GLN G CA  1 
ATOM   6806  C  C   . GLN G  1 23  ? 161.043 -0.095  9.339  1.00 49.15 ? 22   GLN G C   1 
ATOM   6807  O  O   . GLN G  1 23  ? 160.598 0.971   8.905  1.00 48.43 ? 22   GLN G O   1 
ATOM   6808  C  CB  . GLN G  1 23  ? 158.819 -1.264  9.228  1.00 45.33 ? 22   GLN G CB  1 
ATOM   6809  C  CG  . GLN G  1 23  ? 158.977 -1.793  7.818  1.00 45.31 ? 22   GLN G CG  1 
ATOM   6810  C  CD  . GLN G  1 23  ? 157.639 -2.047  7.159  1.00 44.10 ? 22   GLN G CD  1 
ATOM   6811  O  OE1 . GLN G  1 23  ? 156.746 -1.202  7.203  1.00 44.96 ? 22   GLN G OE1 1 
ATOM   6812  N  NE2 . GLN G  1 23  ? 157.493 -3.211  6.538  1.00 44.47 ? 22   GLN G NE2 1 
ATOM   6813  N  N   . LYS G  1 24  ? 162.329 -0.429  9.259  1.00 51.04 ? 23   LYS G N   1 
ATOM   6814  C  CA  . LYS G  1 24  ? 163.316 0.464   8.659  1.00 53.70 ? 23   LYS G CA  1 
ATOM   6815  C  C   . LYS G  1 24  ? 163.158 0.623   7.144  1.00 54.55 ? 23   LYS G C   1 
ATOM   6816  O  O   . LYS G  1 24  ? 163.296 1.729   6.619  1.00 54.73 ? 23   LYS G O   1 
ATOM   6817  C  CB  . LYS G  1 24  ? 164.732 -0.022  8.983  0.00 53.55 ? 23   LYS G CB  1 
ATOM   6818  C  CG  . LYS G  1 24  ? 165.828 0.962   8.596  0.00 53.98 ? 23   LYS G CG  1 
ATOM   6819  C  CD  . LYS G  1 24  ? 167.204 0.420   8.950  0.00 54.16 ? 23   LYS G CD  1 
ATOM   6820  C  CE  . LYS G  1 24  ? 168.303 1.398   8.567  0.00 54.31 ? 23   LYS G CE  1 
ATOM   6821  N  NZ  . LYS G  1 24  ? 169.656 0.873   8.901  0.00 54.41 ? 23   LYS G NZ  1 
ATOM   6822  N  N   . GLU G  1 25  ? 162.872 -0.473  6.444  1.00 55.55 ? 24   GLU G N   1 
ATOM   6823  C  CA  . GLU G  1 25  ? 162.702 -0.425  4.994  1.00 56.36 ? 24   GLU G CA  1 
ATOM   6824  C  C   . GLU G  1 25  ? 161.232 -0.576  4.606  1.00 57.17 ? 24   GLU G C   1 
ATOM   6825  O  O   . GLU G  1 25  ? 160.488 -1.323  5.242  1.00 57.40 ? 24   GLU G O   1 
ATOM   6826  C  CB  . GLU G  1 25  ? 163.531 -1.528  4.326  1.00 55.78 ? 24   GLU G CB  1 
ATOM   6827  C  CG  . GLU G  1 25  ? 165.030 -1.417  4.572  1.00 56.03 ? 24   GLU G CG  1 
ATOM   6828  C  CD  . GLU G  1 25  ? 165.823 -2.494  3.856  0.00 55.86 ? 24   GLU G CD  1 
ATOM   6829  O  OE1 . GLU G  1 25  ? 167.066 -2.499  3.983  0.00 55.85 ? 24   GLU G OE1 1 
ATOM   6830  O  OE2 . GLU G  1 25  ? 165.207 -3.334  3.167  0.00 55.85 ? 24   GLU G OE2 1 
ATOM   6831  N  N   . SER G  1 26  ? 160.825 0.129   3.553  1.00 57.32 ? 25   SER G N   1 
ATOM   6832  C  CA  . SER G  1 26  ? 159.442 0.097   3.080  1.00 58.39 ? 25   SER G CA  1 
ATOM   6833  C  C   . SER G  1 26  ? 158.858 -1.311  2.980  1.00 58.43 ? 25   SER G C   1 
ATOM   6834  O  O   . SER G  1 26  ? 157.821 -1.602  3.574  1.00 59.59 ? 25   SER G O   1 
ATOM   6835  C  CB  . SER G  1 26  ? 159.336 0.795   1.719  1.00 58.99 ? 25   SER G CB  1 
ATOM   6836  O  OG  . SER G  1 26  ? 157.984 0.909   1.304  1.00 59.29 ? 25   SER G OG  1 
ATOM   6837  N  N   . ASN G  1 27  ? 159.513 -2.184  2.224  1.00 58.86 ? 26   ASN G N   1 
ATOM   6838  C  CA  . ASN G  1 27  ? 159.029 -3.553  2.079  1.00 59.65 ? 26   ASN G CA  1 
ATOM   6839  C  C   . ASN G  1 27  ? 159.827 -4.489  2.978  1.00 58.30 ? 26   ASN G C   1 
ATOM   6840  O  O   . ASN G  1 27  ? 159.709 -5.711  2.881  1.00 58.34 ? 26   ASN G O   1 
ATOM   6841  C  CB  . ASN G  1 27  ? 159.152 -4.014  0.622  0.00 61.76 ? 26   ASN G CB  1 
ATOM   6842  C  CG  . ASN G  1 27  ? 160.574 -3.921  0.097  1.00 64.51 ? 26   ASN G CG  1 
ATOM   6843  O  OD1 . ASN G  1 27  ? 161.517 -4.404  0.729  1.00 65.95 ? 26   ASN G OD1 1 
ATOM   6844  N  ND2 . ASN G  1 27  ? 160.734 -3.306  -1.071 1.00 65.32 ? 26   ASN G ND2 1 
ATOM   6845  N  N   . GLY G  1 28  ? 160.634 -3.902  3.858  1.00 56.87 ? 27   GLY G N   1 
ATOM   6846  C  CA  . GLY G  1 28  ? 161.462 -4.689  4.753  1.00 54.82 ? 27   GLY G CA  1 
ATOM   6847  C  C   . GLY G  1 28  ? 160.746 -5.334  5.926  1.00 53.41 ? 27   GLY G C   1 
ATOM   6848  O  O   . GLY G  1 28  ? 159.551 -5.115  6.135  1.00 52.65 ? 27   GLY G O   1 
ATOM   6849  N  N   . PRO G  1 29  ? 161.466 -6.144  6.716  1.00 51.81 ? 28   PRO G N   1 
ATOM   6850  C  CA  . PRO G  1 29  ? 160.907 -6.832  7.882  1.00 50.67 ? 28   PRO G CA  1 
ATOM   6851  C  C   . PRO G  1 29  ? 160.519 -5.863  8.992  1.00 48.98 ? 28   PRO G C   1 
ATOM   6852  O  O   . PRO G  1 29  ? 161.032 -4.744  9.063  1.00 49.55 ? 28   PRO G O   1 
ATOM   6853  C  CB  . PRO G  1 29  ? 162.035 -7.770  8.298  1.00 51.20 ? 28   PRO G CB  1 
ATOM   6854  C  CG  . PRO G  1 29  ? 163.257 -6.988  7.937  1.00 51.34 ? 28   PRO G CG  1 
ATOM   6855  C  CD  . PRO G  1 29  ? 162.901 -6.453  6.569  1.00 51.87 ? 28   PRO G CD  1 
ATOM   6856  N  N   . VAL G  1 30  ? 159.608 -6.300  9.855  1.00 46.42 ? 29   VAL G N   1 
ATOM   6857  C  CA  . VAL G  1 30  ? 159.147 -5.475  10.961 1.00 44.80 ? 29   VAL G CA  1 
ATOM   6858  C  C   . VAL G  1 30  ? 159.571 -6.072  12.294 1.00 44.47 ? 29   VAL G C   1 
ATOM   6859  O  O   . VAL G  1 30  ? 159.282 -7.233  12.586 1.00 42.63 ? 29   VAL G O   1 
ATOM   6860  C  CB  . VAL G  1 30  ? 157.605 -5.340  10.955 1.00 44.26 ? 29   VAL G CB  1 
ATOM   6861  C  CG1 . VAL G  1 30  ? 157.146 -4.527  12.158 1.00 43.04 ? 29   VAL G CG1 1 
ATOM   6862  C  CG2 . VAL G  1 30  ? 157.147 -4.680  9.667  1.00 43.36 ? 29   VAL G CG2 1 
ATOM   6863  N  N   . LYS G  1 31  ? 160.267 -5.277  13.098 1.00 44.87 ? 30   LYS G N   1 
ATOM   6864  C  CA  . LYS G  1 31  ? 160.703 -5.734  14.408 1.00 46.12 ? 30   LYS G CA  1 
ATOM   6865  C  C   . LYS G  1 31  ? 159.573 -5.501  15.402 1.00 46.11 ? 30   LYS G C   1 
ATOM   6866  O  O   . LYS G  1 31  ? 158.971 -4.425  15.433 1.00 46.36 ? 30   LYS G O   1 
ATOM   6867  C  CB  . LYS G  1 31  ? 161.964 -4.985  14.847 1.00 47.71 ? 30   LYS G CB  1 
ATOM   6868  C  CG  . LYS G  1 31  ? 163.179 -5.291  13.977 1.00 50.24 ? 30   LYS G CG  1 
ATOM   6869  C  CD  . LYS G  1 31  ? 164.433 -4.587  14.459 0.00 51.56 ? 30   LYS G CD  1 
ATOM   6870  C  CE  . LYS G  1 31  ? 165.617 -4.952  13.577 0.00 52.69 ? 30   LYS G CE  1 
ATOM   6871  N  NZ  . LYS G  1 31  ? 166.872 -4.280  14.002 1.00 54.66 ? 30   LYS G NZ  1 
ATOM   6872  N  N   . VAL G  1 32  ? 159.281 -6.522  16.201 1.00 45.39 ? 31   VAL G N   1 
ATOM   6873  C  CA  . VAL G  1 32  ? 158.218 -6.448  17.194 1.00 44.16 ? 31   VAL G CA  1 
ATOM   6874  C  C   . VAL G  1 32  ? 158.764 -6.794  18.575 1.00 44.89 ? 31   VAL G C   1 
ATOM   6875  O  O   . VAL G  1 32  ? 159.260 -7.900  18.793 1.00 45.46 ? 31   VAL G O   1 
ATOM   6876  C  CB  . VAL G  1 32  ? 157.086 -7.434  16.853 1.00 43.95 ? 31   VAL G CB  1 
ATOM   6877  C  CG1 . VAL G  1 32  ? 155.884 -7.177  17.745 1.00 42.90 ? 31   VAL G CG1 1 
ATOM   6878  C  CG2 . VAL G  1 32  ? 156.716 -7.313  15.387 1.00 42.01 ? 31   VAL G CG2 1 
ATOM   6879  N  N   . TRP G  1 33  ? 158.671 -5.853  19.508 1.00 45.05 ? 32   TRP G N   1 
ATOM   6880  C  CA  . TRP G  1 33  ? 159.166 -6.091  20.858 1.00 45.76 ? 32   TRP G CA  1 
ATOM   6881  C  C   . TRP G  1 33  ? 158.361 -5.346  21.917 1.00 46.74 ? 32   TRP G C   1 
ATOM   6882  O  O   . TRP G  1 33  ? 157.714 -4.335  21.631 1.00 46.12 ? 32   TRP G O   1 
ATOM   6883  C  CB  . TRP G  1 33  ? 160.634 -5.682  20.954 1.00 47.08 ? 32   TRP G CB  1 
ATOM   6884  C  CG  . TRP G  1 33  ? 160.850 -4.206  20.903 1.00 49.54 ? 32   TRP G CG  1 
ATOM   6885  C  CD1 . TRP G  1 33  ? 161.028 -3.364  21.965 1.00 49.71 ? 32   TRP G CD1 1 
ATOM   6886  C  CD2 . TRP G  1 33  ? 160.894 -3.385  19.728 1.00 50.85 ? 32   TRP G CD2 1 
ATOM   6887  N  NE1 . TRP G  1 33  ? 161.180 -2.071  21.523 1.00 50.48 ? 32   TRP G NE1 1 
ATOM   6888  C  CE2 . TRP G  1 33  ? 161.101 -2.057  20.159 1.00 51.18 ? 32   TRP G CE2 1 
ATOM   6889  C  CE3 . TRP G  1 33  ? 160.775 -3.648  18.357 1.00 52.47 ? 32   TRP G CE3 1 
ATOM   6890  C  CZ2 . TRP G  1 33  ? 161.196 -0.988  19.258 1.00 52.99 ? 32   TRP G CZ2 1 
ATOM   6891  C  CZ3 . TRP G  1 33  ? 160.870 -2.583  17.463 1.00 53.47 ? 32   TRP G CZ3 1 
ATOM   6892  C  CH2 . TRP G  1 33  ? 161.078 -1.269  17.920 1.00 53.18 ? 32   TRP G CH2 1 
ATOM   6893  N  N   . GLY G  1 34  ? 158.416 -5.855  23.144 1.00 47.19 ? 33   GLY G N   1 
ATOM   6894  C  CA  . GLY G  1 34  ? 157.699 -5.241  24.246 1.00 46.55 ? 33   GLY G CA  1 
ATOM   6895  C  C   . GLY G  1 34  ? 157.541 -6.216  25.397 1.00 46.44 ? 33   GLY G C   1 
ATOM   6896  O  O   . GLY G  1 34  ? 158.447 -7.000  25.684 1.00 45.11 ? 33   GLY G O   1 
ATOM   6897  N  N   . SER G  1 35  ? 156.387 -6.174  26.054 1.00 45.90 ? 34   SER G N   1 
ATOM   6898  C  CA  . SER G  1 35  ? 156.116 -7.065  27.174 1.00 45.76 ? 34   SER G CA  1 
ATOM   6899  C  C   . SER G  1 35  ? 154.627 -7.139  27.488 1.00 44.72 ? 34   SER G C   1 
ATOM   6900  O  O   . SER G  1 35  ? 153.885 -6.181  27.270 1.00 43.89 ? 34   SER G O   1 
ATOM   6901  C  CB  . SER G  1 35  ? 156.878 -6.596  28.414 1.00 48.08 ? 34   SER G CB  1 
ATOM   6902  O  OG  . SER G  1 35  ? 156.690 -7.499  29.490 1.00 50.49 ? 34   SER G OG  1 
ATOM   6903  N  N   . ILE G  1 36  ? 154.201 -8.287  28.002 1.00 43.34 ? 35   ILE G N   1 
ATOM   6904  C  CA  . ILE G  1 36  ? 152.806 -8.517  28.359 1.00 41.40 ? 35   ILE G CA  1 
ATOM   6905  C  C   . ILE G  1 36  ? 152.774 -9.201  29.724 1.00 42.34 ? 35   ILE G C   1 
ATOM   6906  O  O   . ILE G  1 36  ? 153.447 -10.212 29.929 1.00 41.57 ? 35   ILE G O   1 
ATOM   6907  C  CB  . ILE G  1 36  ? 152.109 -9.444  27.335 1.00 39.63 ? 35   ILE G CB  1 
ATOM   6908  C  CG1 . ILE G  1 36  ? 152.308 -8.905  25.918 1.00 37.49 ? 35   ILE G CG1 1 
ATOM   6909  C  CG2 . ILE G  1 36  ? 150.619 -9.549  27.648 1.00 37.61 ? 35   ILE G CG2 1 
ATOM   6910  C  CD1 . ILE G  1 36  ? 151.708 -9.787  24.841 1.00 34.07 ? 35   ILE G CD1 1 
ATOM   6911  N  N   . LYS G  1 37  ? 152.003 -8.650  30.658 1.00 41.83 ? 36   LYS G N   1 
ATOM   6912  C  CA  . LYS G  1 37  ? 151.903 -9.237  31.989 1.00 41.36 ? 36   LYS G CA  1 
ATOM   6913  C  C   . LYS G  1 37  ? 150.471 -9.643  32.329 1.00 41.01 ? 36   LYS G C   1 
ATOM   6914  O  O   . LYS G  1 37  ? 149.521 -9.228  31.662 1.00 38.92 ? 36   LYS G O   1 
ATOM   6915  C  CB  . LYS G  1 37  ? 152.443 -8.262  33.040 1.00 41.35 ? 36   LYS G CB  1 
ATOM   6916  C  CG  . LYS G  1 37  ? 151.725 -6.925  33.106 1.00 42.35 ? 36   LYS G CG  1 
ATOM   6917  C  CD  . LYS G  1 37  ? 152.444 -5.990  34.069 1.00 43.56 ? 36   LYS G CD  1 
ATOM   6918  C  CE  . LYS G  1 37  ? 151.813 -4.610  34.088 1.00 44.26 ? 36   LYS G CE  1 
ATOM   6919  N  NZ  . LYS G  1 37  ? 152.617 -3.649  34.898 1.00 42.78 ? 36   LYS G NZ  1 
ATOM   6920  N  N   . GLY G  1 38  ? 150.328 -10.464 33.366 1.00 40.33 ? 37   GLY G N   1 
ATOM   6921  C  CA  . GLY G  1 38  ? 149.011 -10.920 33.775 1.00 40.06 ? 37   GLY G CA  1 
ATOM   6922  C  C   . GLY G  1 38  ? 148.596 -12.203 33.079 1.00 40.41 ? 37   GLY G C   1 
ATOM   6923  O  O   . GLY G  1 38  ? 147.432 -12.601 33.138 1.00 39.67 ? 37   GLY G O   1 
ATOM   6924  N  N   . LEU G  1 39  ? 149.550 -12.853 32.418 1.00 40.14 ? 38   LEU G N   1 
ATOM   6925  C  CA  . LEU G  1 39  ? 149.278 -14.095 31.705 1.00 41.72 ? 38   LEU G CA  1 
ATOM   6926  C  C   . LEU G  1 39  ? 149.644 -15.304 32.549 1.00 42.85 ? 38   LEU G C   1 
ATOM   6927  O  O   . LEU G  1 39  ? 150.424 -15.201 33.493 1.00 43.25 ? 38   LEU G O   1 
ATOM   6928  C  CB  . LEU G  1 39  ? 150.080 -14.148 30.402 1.00 41.64 ? 38   LEU G CB  1 
ATOM   6929  C  CG  . LEU G  1 39  ? 149.677 -13.204 29.268 1.00 42.09 ? 38   LEU G CG  1 
ATOM   6930  C  CD1 . LEU G  1 39  ? 150.820 -13.092 28.266 1.00 41.74 ? 38   LEU G CD1 1 
ATOM   6931  C  CD2 . LEU G  1 39  ? 148.405 -13.718 28.602 1.00 40.50 ? 38   LEU G CD2 1 
ATOM   6932  N  N   . THR G  1 40  ? 149.069 -16.450 32.209 1.00 43.18 ? 39   THR G N   1 
ATOM   6933  C  CA  . THR G  1 40  ? 149.376 -17.677 32.925 1.00 44.39 ? 39   THR G CA  1 
ATOM   6934  C  C   . THR G  1 40  ? 150.637 -18.219 32.269 1.00 44.80 ? 39   THR G C   1 
ATOM   6935  O  O   . THR G  1 40  ? 150.738 -18.240 31.041 1.00 44.55 ? 39   THR G O   1 
ATOM   6936  C  CB  . THR G  1 40  ? 148.259 -18.729 32.773 1.00 44.71 ? 39   THR G CB  1 
ATOM   6937  O  OG1 . THR G  1 40  ? 148.082 -19.035 31.384 1.00 42.66 ? 39   THR G OG1 1 
ATOM   6938  C  CG2 . THR G  1 40  ? 146.945 -18.210 33.354 1.00 44.23 ? 39   THR G CG2 1 
ATOM   6939  N  N   . GLU G  1 41  ? 151.598 -18.638 33.086 1.00 44.75 ? 40   GLU G N   1 
ATOM   6940  C  CA  . GLU G  1 41  ? 152.852 -19.183 32.579 1.00 45.00 ? 40   GLU G CA  1 
ATOM   6941  C  C   . GLU G  1 41  ? 152.560 -20.129 31.420 1.00 43.49 ? 40   GLU G C   1 
ATOM   6942  O  O   . GLU G  1 41  ? 151.678 -20.982 31.514 1.00 42.62 ? 40   GLU G O   1 
ATOM   6943  C  CB  . GLU G  1 41  ? 153.576 -19.938 33.694 1.00 47.63 ? 40   GLU G CB  1 
ATOM   6944  C  CG  . GLU G  1 41  ? 154.912 -20.527 33.289 1.00 51.24 ? 40   GLU G CG  1 
ATOM   6945  C  CD  . GLU G  1 41  ? 155.504 -21.407 34.371 1.00 53.28 ? 40   GLU G CD  1 
ATOM   6946  O  OE1 . GLU G  1 41  ? 154.884 -22.441 34.697 1.00 54.16 ? 40   GLU G OE1 1 
ATOM   6947  O  OE2 . GLU G  1 41  ? 156.583 -21.065 34.900 1.00 55.06 ? 40   GLU G OE2 1 
ATOM   6948  N  N   . GLY G  1 42  ? 153.291 -19.970 30.322 1.00 43.58 ? 41   GLY G N   1 
ATOM   6949  C  CA  . GLY G  1 42  ? 153.074 -20.828 29.170 1.00 42.24 ? 41   GLY G CA  1 
ATOM   6950  C  C   . GLY G  1 42  ? 152.944 -20.065 27.864 1.00 42.33 ? 41   GLY G C   1 
ATOM   6951  O  O   . GLY G  1 42  ? 153.260 -18.874 27.795 1.00 40.87 ? 41   GLY G O   1 
ATOM   6952  N  N   . LEU G  1 43  ? 152.471 -20.756 26.829 1.00 42.08 ? 42   LEU G N   1 
ATOM   6953  C  CA  . LEU G  1 43  ? 152.299 -20.156 25.510 1.00 42.51 ? 42   LEU G CA  1 
ATOM   6954  C  C   . LEU G  1 43  ? 150.938 -19.488 25.353 1.00 42.00 ? 42   LEU G C   1 
ATOM   6955  O  O   . LEU G  1 43  ? 149.954 -19.905 25.965 1.00 40.39 ? 42   LEU G O   1 
ATOM   6956  C  CB  . LEU G  1 43  ? 152.460 -21.215 24.415 1.00 43.66 ? 42   LEU G CB  1 
ATOM   6957  C  CG  . LEU G  1 43  ? 153.784 -21.979 24.319 1.00 45.54 ? 42   LEU G CG  1 
ATOM   6958  C  CD1 . LEU G  1 43  ? 153.736 -22.902 23.108 1.00 44.96 ? 42   LEU G CD1 1 
ATOM   6959  C  CD2 . LEU G  1 43  ? 154.949 -21.008 24.195 1.00 45.44 ? 42   LEU G CD2 1 
ATOM   6960  N  N   . HIS G  1 44  ? 150.893 -18.458 24.511 1.00 41.47 ? 43   HIS G N   1 
ATOM   6961  C  CA  . HIS G  1 44  ? 149.662 -17.714 24.252 1.00 40.46 ? 43   HIS G CA  1 
ATOM   6962  C  C   . HIS G  1 44  ? 149.613 -17.203 22.813 1.00 38.87 ? 43   HIS G C   1 
ATOM   6963  O  O   . HIS G  1 44  ? 150.577 -16.611 22.328 1.00 36.96 ? 43   HIS G O   1 
ATOM   6964  C  CB  . HIS G  1 44  ? 149.557 -16.531 25.220 1.00 39.84 ? 43   HIS G CB  1 
ATOM   6965  C  CG  . HIS G  1 44  ? 149.294 -16.933 26.640 1.00 41.70 ? 43   HIS G CG  1 
ATOM   6966  N  ND1 . HIS G  1 44  ? 148.109 -17.506 27.044 1.00 41.48 ? 43   HIS G ND1 1 
ATOM   6967  C  CD2 . HIS G  1 44  ? 150.066 -16.837 27.750 1.00 41.74 ? 43   HIS G CD2 1 
ATOM   6968  C  CE1 . HIS G  1 44  ? 148.158 -17.747 28.344 1.00 43.00 ? 43   HIS G CE1 1 
ATOM   6969  N  NE2 . HIS G  1 44  ? 149.334 -17.350 28.795 1.00 44.35 ? 43   HIS G NE2 1 
ATOM   6970  N  N   . GLY G  1 45  ? 148.488 -17.439 22.139 1.00 38.72 ? 44   GLY G N   1 
ATOM   6971  C  CA  . GLY G  1 45  ? 148.324 -16.987 20.766 1.00 38.68 ? 44   GLY G CA  1 
ATOM   6972  C  C   . GLY G  1 45  ? 148.599 -15.496 20.646 1.00 38.87 ? 44   GLY G C   1 
ATOM   6973  O  O   . GLY G  1 45  ? 148.251 -14.726 21.542 1.00 37.42 ? 44   GLY G O   1 
ATOM   6974  N  N   . PHE G  1 46  ? 149.205 -15.088 19.533 1.00 37.63 ? 45   PHE G N   1 
ATOM   6975  C  CA  . PHE G  1 46  ? 149.565 -13.690 19.310 1.00 36.71 ? 45   PHE G CA  1 
ATOM   6976  C  C   . PHE G  1 46  ? 149.352 -13.351 17.831 1.00 38.87 ? 45   PHE G C   1 
ATOM   6977  O  O   . PHE G  1 46  ? 150.128 -13.785 16.971 1.00 37.49 ? 45   PHE G O   1 
ATOM   6978  C  CB  . PHE G  1 46  ? 151.038 -13.511 19.698 1.00 37.15 ? 45   PHE G CB  1 
ATOM   6979  C  CG  . PHE G  1 46  ? 151.480 -12.079 19.854 1.00 39.23 ? 45   PHE G CG  1 
ATOM   6980  C  CD1 . PHE G  1 46  ? 150.856 -11.231 20.767 1.00 39.49 ? 45   PHE G CD1 1 
ATOM   6981  C  CD2 . PHE G  1 46  ? 152.577 -11.599 19.138 1.00 37.90 ? 45   PHE G CD2 1 
ATOM   6982  C  CE1 . PHE G  1 46  ? 151.323 -9.921  20.966 1.00 38.54 ? 45   PHE G CE1 1 
ATOM   6983  C  CE2 . PHE G  1 46  ? 153.048 -10.300 19.328 1.00 38.44 ? 45   PHE G CE2 1 
ATOM   6984  C  CZ  . PHE G  1 46  ? 152.421 -9.458  20.246 1.00 37.99 ? 45   PHE G CZ  1 
ATOM   6985  N  N   . HIS G  1 47  ? 148.299 -12.591 17.528 1.00 38.50 ? 46   HIS G N   1 
ATOM   6986  C  CA  . HIS G  1 47  ? 148.025 -12.219 16.139 1.00 38.84 ? 46   HIS G CA  1 
ATOM   6987  C  C   . HIS G  1 47  ? 147.466 -10.814 15.945 1.00 38.63 ? 46   HIS G C   1 
ATOM   6988  O  O   . HIS G  1 47  ? 147.062 -10.134 16.896 1.00 35.77 ? 46   HIS G O   1 
ATOM   6989  C  CB  . HIS G  1 47  ? 147.029 -13.186 15.475 1.00 41.44 ? 46   HIS G CB  1 
ATOM   6990  C  CG  . HIS G  1 47  ? 146.923 -14.524 16.132 1.00 45.06 ? 46   HIS G CG  1 
ATOM   6991  N  ND1 . HIS G  1 47  ? 146.094 -14.765 17.213 1.00 47.38 ? 46   HIS G ND1 1 
ATOM   6992  C  CD2 . HIS G  1 47  ? 147.498 -15.714 15.839 1.00 46.80 ? 46   HIS G CD2 1 
ATOM   6993  C  CE1 . HIS G  1 47  ? 146.163 -16.033 17.548 1.00 47.68 ? 46   HIS G CE1 1 
ATOM   6994  N  NE2 . HIS G  1 47  ? 147.013 -16.640 16.729 1.00 48.83 ? 46   HIS G NE2 1 
ATOM   6995  N  N   . VAL G  1 48  ? 147.438 -10.399 14.682 1.00 37.63 ? 47   VAL G N   1 
ATOM   6996  C  CA  . VAL G  1 48  ? 146.890 -9.113  14.294 1.00 37.67 ? 47   VAL G CA  1 
ATOM   6997  C  C   . VAL G  1 48  ? 145.556 -9.428  13.634 1.00 37.78 ? 47   VAL G C   1 
ATOM   6998  O  O   . VAL G  1 48  ? 145.504 -10.156 12.637 1.00 37.64 ? 47   VAL G O   1 
ATOM   6999  C  CB  . VAL G  1 48  ? 147.789 -8.386  13.265 1.00 38.14 ? 47   VAL G CB  1 
ATOM   7000  C  CG1 . VAL G  1 48  ? 147.063 -7.170  12.710 1.00 39.00 ? 47   VAL G CG1 1 
ATOM   7001  C  CG2 . VAL G  1 48  ? 149.094 -7.965  13.917 1.00 36.75 ? 47   VAL G CG2 1 
ATOM   7002  N  N   . HIS G  1 49  ? 144.476 -8.900  14.198 1.00 35.51 ? 48   HIS G N   1 
ATOM   7003  C  CA  . HIS G  1 49  ? 143.157 -9.132  13.635 1.00 36.00 ? 48   HIS G CA  1 
ATOM   7004  C  C   . HIS G  1 49  ? 142.801 -8.021  12.659 1.00 36.47 ? 48   HIS G C   1 
ATOM   7005  O  O   . HIS G  1 49  ? 143.322 -6.907  12.747 1.00 34.92 ? 48   HIS G O   1 
ATOM   7006  C  CB  . HIS G  1 49  ? 142.114 -9.245  14.748 1.00 35.67 ? 48   HIS G CB  1 
ATOM   7007  C  CG  . HIS G  1 49  ? 142.166 -10.551 15.482 1.00 36.57 ? 48   HIS G CG  1 
ATOM   7008  N  ND1 . HIS G  1 49  ? 141.061 -11.348 15.658 1.00 37.28 ? 48   HIS G ND1 1 
ATOM   7009  C  CD2 . HIS G  1 49  ? 143.203 -11.202 16.064 1.00 34.68 ? 48   HIS G CD2 1 
ATOM   7010  C  CE1 . HIS G  1 49  ? 141.410 -12.442 16.319 1.00 38.11 ? 48   HIS G CE1 1 
ATOM   7011  N  NE2 . HIS G  1 49  ? 142.701 -12.375 16.575 1.00 35.54 ? 48   HIS G NE2 1 
ATOM   7012  N  N   . GLU G  1 50  ? 141.902 -8.337  11.736 1.00 36.83 ? 49   GLU G N   1 
ATOM   7013  C  CA  . GLU G  1 50  ? 141.492 -7.415  10.687 1.00 37.06 ? 49   GLU G CA  1 
ATOM   7014  C  C   . GLU G  1 50  ? 141.023 -6.005  11.041 1.00 36.23 ? 49   GLU G C   1 
ATOM   7015  O  O   . GLU G  1 50  ? 141.519 -5.034  10.472 1.00 34.69 ? 49   GLU G O   1 
ATOM   7016  C  CB  . GLU G  1 50  ? 140.418 -8.071  9.825  1.00 38.73 ? 49   GLU G CB  1 
ATOM   7017  C  CG  . GLU G  1 50  ? 140.048 -7.249  8.604  1.00 41.06 ? 49   GLU G CG  1 
ATOM   7018  C  CD  . GLU G  1 50  ? 139.011 -7.926  7.741  1.00 43.13 ? 49   GLU G CD  1 
ATOM   7019  O  OE1 . GLU G  1 50  ? 138.696 -7.380  6.662  1.00 43.99 ? 49   GLU G OE1 1 
ATOM   7020  O  OE2 . GLU G  1 50  ? 138.510 -9.000  8.142  1.00 42.70 ? 49   GLU G OE2 1 
ATOM   7021  N  N   . PHE G  1 51  ? 140.067 -5.888  11.957 1.00 35.10 ? 50   PHE G N   1 
ATOM   7022  C  CA  . PHE G  1 51  ? 139.519 -4.579  12.300 1.00 36.15 ? 50   PHE G CA  1 
ATOM   7023  C  C   . PHE G  1 51  ? 140.011 -3.940  13.595 1.00 36.29 ? 50   PHE G C   1 
ATOM   7024  O  O   . PHE G  1 51  ? 140.099 -4.595  14.638 1.00 37.42 ? 50   PHE G O   1 
ATOM   7025  C  CB  . PHE G  1 51  ? 137.990 -4.663  12.347 1.00 36.79 ? 50   PHE G CB  1 
ATOM   7026  C  CG  . PHE G  1 51  ? 137.380 -5.347  11.155 1.00 38.53 ? 50   PHE G CG  1 
ATOM   7027  C  CD1 . PHE G  1 51  ? 137.535 -4.825  9.873  1.00 39.69 ? 50   PHE G CD1 1 
ATOM   7028  C  CD2 . PHE G  1 51  ? 136.647 -6.519  11.316 1.00 37.96 ? 50   PHE G CD2 1 
ATOM   7029  C  CE1 . PHE G  1 51  ? 136.967 -5.464  8.768  1.00 40.70 ? 50   PHE G CE1 1 
ATOM   7030  C  CE2 . PHE G  1 51  ? 136.077 -7.164  10.225 1.00 38.63 ? 50   PHE G CE2 1 
ATOM   7031  C  CZ  . PHE G  1 51  ? 136.236 -6.637  8.947  1.00 40.45 ? 50   PHE G CZ  1 
ATOM   7032  N  N   . GLY G  1 52  ? 140.323 -2.650  13.512 1.00 34.96 ? 51   GLY G N   1 
ATOM   7033  C  CA  . GLY G  1 52  ? 140.761 -1.907  14.679 1.00 33.80 ? 51   GLY G CA  1 
ATOM   7034  C  C   . GLY G  1 52  ? 139.506 -1.313  15.295 1.00 33.27 ? 51   GLY G C   1 
ATOM   7035  O  O   . GLY G  1 52  ? 139.423 -0.112  15.544 1.00 34.15 ? 51   GLY G O   1 
ATOM   7036  N  N   . ASP G  1 53  ? 138.522 -2.179  15.522 1.00 31.57 ? 52   ASP G N   1 
ATOM   7037  C  CA  . ASP G  1 53  ? 137.229 -1.804  16.086 1.00 31.35 ? 52   ASP G CA  1 
ATOM   7038  C  C   . ASP G  1 53  ? 137.075 -2.403  17.490 1.00 32.20 ? 52   ASP G C   1 
ATOM   7039  O  O   . ASP G  1 53  ? 136.861 -3.609  17.641 1.00 29.96 ? 52   ASP G O   1 
ATOM   7040  C  CB  . ASP G  1 53  ? 136.128 -2.306  15.142 1.00 32.19 ? 52   ASP G CB  1 
ATOM   7041  C  CG  . ASP G  1 53  ? 134.725 -2.030  15.652 1.00 31.96 ? 52   ASP G CG  1 
ATOM   7042  O  OD1 . ASP G  1 53  ? 133.783 -2.196  14.848 1.00 34.09 ? 52   ASP G OD1 1 
ATOM   7043  O  OD2 . ASP G  1 53  ? 134.553 -1.664  16.835 1.00 31.10 ? 52   ASP G OD2 1 
ATOM   7044  N  N   . ASN G  1 54  ? 137.189 -1.548  18.506 1.00 30.74 ? 53   ASN G N   1 
ATOM   7045  C  CA  . ASN G  1 54  ? 137.089 -1.954  19.914 1.00 30.17 ? 53   ASN G CA  1 
ATOM   7046  C  C   . ASN G  1 54  ? 135.729 -1.583  20.540 1.00 30.99 ? 53   ASN G C   1 
ATOM   7047  O  O   . ASN G  1 54  ? 135.629 -1.402  21.757 1.00 30.86 ? 53   ASN G O   1 
ATOM   7048  C  CB  . ASN G  1 54  ? 138.227 -1.284  20.700 1.00 28.43 ? 53   ASN G CB  1 
ATOM   7049  C  CG  . ASN G  1 54  ? 138.294 -1.723  22.158 1.00 31.62 ? 53   ASN G CG  1 
ATOM   7050  O  OD1 . ASN G  1 54  ? 138.782 -0.981  23.014 1.00 28.20 ? 53   ASN G OD1 1 
ATOM   7051  N  ND2 . ASN G  1 54  ? 137.826 -2.933  22.444 1.00 32.34 ? 53   ASN G ND2 1 
ATOM   7052  N  N   . THR G  1 55  ? 134.683 -1.476  19.723 1.00 30.92 ? 54   THR G N   1 
ATOM   7053  C  CA  . THR G  1 55  ? 133.366 -1.118  20.251 1.00 32.82 ? 54   THR G CA  1 
ATOM   7054  C  C   . THR G  1 55  ? 132.692 -2.264  21.004 1.00 35.86 ? 54   THR G C   1 
ATOM   7055  O  O   . THR G  1 55  ? 131.727 -2.045  21.741 1.00 35.82 ? 54   THR G O   1 
ATOM   7056  C  CB  . THR G  1 55  ? 132.410 -0.628  19.136 1.00 32.26 ? 54   THR G CB  1 
ATOM   7057  O  OG1 . THR G  1 55  ? 132.190 -1.676  18.184 1.00 30.35 ? 54   THR G OG1 1 
ATOM   7058  C  CG2 . THR G  1 55  ? 133.002 0.583   18.429 1.00 31.58 ? 54   THR G CG2 1 
ATOM   7059  N  N   . ALA G  1 56  ? 133.195 -3.483  20.809 1.00 35.39 ? 55   ALA G N   1 
ATOM   7060  C  CA  . ALA G  1 56  ? 132.658 -4.661  21.489 1.00 36.23 ? 55   ALA G CA  1 
ATOM   7061  C  C   . ALA G  1 56  ? 133.821 -5.530  21.955 1.00 37.47 ? 55   ALA G C   1 
ATOM   7062  O  O   . ALA G  1 56  ? 134.096 -6.583  21.372 1.00 38.82 ? 55   ALA G O   1 
ATOM   7063  C  CB  . ALA G  1 56  ? 131.755 -5.452  20.552 1.00 34.97 ? 55   ALA G CB  1 
ATOM   7064  N  N   . GLY G  1 57  ? 134.504 -5.081  23.005 1.00 36.59 ? 56   GLY G N   1 
ATOM   7065  C  CA  . GLY G  1 57  ? 135.639 -5.824  23.521 1.00 36.44 ? 56   GLY G CA  1 
ATOM   7066  C  C   . GLY G  1 57  ? 136.614 -6.131  22.401 1.00 36.01 ? 56   GLY G C   1 
ATOM   7067  O  O   . GLY G  1 57  ? 136.749 -5.354  21.453 1.00 33.36 ? 56   GLY G O   1 
ATOM   7068  N  N   . CYS G  1 58  ? 137.295 -7.267  22.502 1.00 35.72 ? 57   CYS G N   1 
ATOM   7069  C  CA  . CYS G  1 58  ? 138.244 -7.662  21.474 1.00 35.18 ? 57   CYS G CA  1 
ATOM   7070  C  C   . CYS G  1 58  ? 137.528 -8.444  20.381 1.00 34.56 ? 57   CYS G C   1 
ATOM   7071  O  O   . CYS G  1 58  ? 138.127 -8.815  19.375 1.00 35.14 ? 57   CYS G O   1 
ATOM   7072  C  CB  . CYS G  1 58  ? 139.357 -8.514  22.086 1.00 36.39 ? 57   CYS G CB  1 
ATOM   7073  S  SG  . CYS G  1 58  ? 140.333 -7.638  23.348 1.00 37.45 ? 57   CYS G SG  1 
ATOM   7074  N  N   . THR G  1 59  ? 136.235 -8.676  20.574 1.00 34.55 ? 58   THR G N   1 
ATOM   7075  C  CA  . THR G  1 59  ? 135.445 -9.424  19.601 1.00 35.69 ? 58   THR G CA  1 
ATOM   7076  C  C   . THR G  1 59  ? 135.200 -8.688  18.284 1.00 35.53 ? 58   THR G C   1 
ATOM   7077  O  O   . THR G  1 59  ? 135.241 -9.298  17.211 1.00 34.33 ? 58   THR G O   1 
ATOM   7078  C  CB  . THR G  1 59  ? 134.074 -9.831  20.194 1.00 35.93 ? 58   THR G CB  1 
ATOM   7079  O  OG1 . THR G  1 59  ? 134.279 -10.679 21.330 1.00 36.96 ? 58   THR G OG1 1 
ATOM   7080  C  CG2 . THR G  1 59  ? 133.240 -10.575 19.161 1.00 35.32 ? 58   THR G CG2 1 
ATOM   7081  N  N   . SER G  1 60  ? 134.942 -7.385  18.357 1.00 34.70 ? 59   SER G N   1 
ATOM   7082  C  CA  . SER G  1 60  ? 134.670 -6.609  17.150 1.00 33.70 ? 59   SER G CA  1 
ATOM   7083  C  C   . SER G  1 60  ? 135.881 -6.458  16.229 1.00 33.46 ? 59   SER G C   1 
ATOM   7084  O  O   . SER G  1 60  ? 135.784 -5.865  15.156 1.00 34.13 ? 59   SER G O   1 
ATOM   7085  C  CB  . SER G  1 60  ? 134.100 -5.234  17.524 1.00 33.10 ? 59   SER G CB  1 
ATOM   7086  O  OG  . SER G  1 60  ? 134.806 -4.655  18.604 1.00 33.64 ? 59   SER G OG  1 
ATOM   7087  N  N   . ALA G  1 61  ? 137.018 -7.005  16.644 1.00 33.33 ? 60   ALA G N   1 
ATOM   7088  C  CA  . ALA G  1 61  ? 138.230 -6.944  15.831 1.00 33.76 ? 60   ALA G CA  1 
ATOM   7089  C  C   . ALA G  1 61  ? 138.142 -7.945  14.670 1.00 34.45 ? 60   ALA G C   1 
ATOM   7090  O  O   . ALA G  1 61  ? 138.986 -7.952  13.772 1.00 34.65 ? 60   ALA G O   1 
ATOM   7091  C  CB  . ALA G  1 61  ? 139.456 -7.238  16.696 1.00 31.22 ? 60   ALA G CB  1 
ATOM   7092  N  N   . GLY G  1 62  ? 137.114 -8.789  14.692 1.00 35.36 ? 61   GLY G N   1 
ATOM   7093  C  CA  . GLY G  1 62  ? 136.941 -9.763  13.629 1.00 35.62 ? 61   GLY G CA  1 
ATOM   7094  C  C   . GLY G  1 62  ? 137.996 -10.857 13.624 1.00 35.90 ? 61   GLY G C   1 
ATOM   7095  O  O   . GLY G  1 62  ? 138.639 -11.106 14.643 1.00 35.55 ? 61   GLY G O   1 
ATOM   7096  N  N   . PRO G  1 63  ? 138.200 -11.532 12.482 1.00 36.59 ? 62   PRO G N   1 
ATOM   7097  C  CA  . PRO G  1 63  ? 139.192 -12.608 12.372 1.00 37.30 ? 62   PRO G CA  1 
ATOM   7098  C  C   . PRO G  1 63  ? 140.624 -12.098 12.224 1.00 37.23 ? 62   PRO G C   1 
ATOM   7099  O  O   . PRO G  1 63  ? 140.877 -10.897 12.283 1.00 38.17 ? 62   PRO G O   1 
ATOM   7100  C  CB  . PRO G  1 63  ? 138.725 -13.370 11.139 1.00 37.74 ? 62   PRO G CB  1 
ATOM   7101  C  CG  . PRO G  1 63  ? 138.231 -12.253 10.258 1.00 38.10 ? 62   PRO G CG  1 
ATOM   7102  C  CD  . PRO G  1 63  ? 137.440 -11.386 11.226 1.00 36.87 ? 62   PRO G CD  1 
ATOM   7103  N  N   . HIS G  1 64  ? 141.558 -13.024 12.041 1.00 37.82 ? 63   HIS G N   1 
ATOM   7104  C  CA  . HIS G  1 64  ? 142.961 -12.670 11.865 1.00 39.14 ? 63   HIS G CA  1 
ATOM   7105  C  C   . HIS G  1 64  ? 143.090 -11.905 10.545 1.00 38.77 ? 63   HIS G C   1 
ATOM   7106  O  O   . HIS G  1 64  ? 142.341 -12.164 9.600  1.00 37.09 ? 63   HIS G O   1 
ATOM   7107  C  CB  . HIS G  1 64  ? 143.821 -13.941 11.810 1.00 41.36 ? 63   HIS G CB  1 
ATOM   7108  C  CG  . HIS G  1 64  ? 143.759 -14.780 13.053 1.00 43.83 ? 63   HIS G CG  1 
ATOM   7109  N  ND1 . HIS G  1 64  ? 144.326 -16.030 13.134 1.00 43.87 ? 63   HIS G ND1 1 
ATOM   7110  C  CD2 . HIS G  1 64  ? 143.212 -14.534 14.268 1.00 45.51 ? 63   HIS G CD2 1 
ATOM   7111  C  CE1 . HIS G  1 64  ? 144.136 -16.525 14.343 1.00 46.34 ? 63   HIS G CE1 1 
ATOM   7112  N  NE2 . HIS G  1 64  ? 143.461 -15.636 15.053 1.00 48.52 ? 63   HIS G NE2 1 
ATOM   7113  N  N   . PHE G  1 65  ? 144.023 -10.957 10.479 1.00 40.37 ? 64   PHE G N   1 
ATOM   7114  C  CA  . PHE G  1 65  ? 144.221 -10.193 9.248  1.00 42.52 ? 64   PHE G CA  1 
ATOM   7115  C  C   . PHE G  1 65  ? 144.606 -11.203 8.167  1.00 43.25 ? 64   PHE G C   1 
ATOM   7116  O  O   . PHE G  1 65  ? 145.690 -11.785 8.211  1.00 42.92 ? 64   PHE G O   1 
ATOM   7117  C  CB  . PHE G  1 65  ? 145.343 -9.163  9.417  1.00 41.65 ? 64   PHE G CB  1 
ATOM   7118  C  CG  . PHE G  1 65  ? 145.501 -8.238  8.237  1.00 43.49 ? 64   PHE G CG  1 
ATOM   7119  C  CD1 . PHE G  1 65  ? 146.741 -7.678  7.936  1.00 41.64 ? 64   PHE G CD1 1 
ATOM   7120  C  CD2 . PHE G  1 65  ? 144.409 -7.919  7.431  1.00 41.55 ? 64   PHE G CD2 1 
ATOM   7121  C  CE1 . PHE G  1 65  ? 146.892 -6.818  6.848  1.00 42.15 ? 64   PHE G CE1 1 
ATOM   7122  C  CE2 . PHE G  1 65  ? 144.551 -7.058  6.341  1.00 43.00 ? 64   PHE G CE2 1 
ATOM   7123  C  CZ  . PHE G  1 65  ? 145.796 -6.507  6.051  1.00 41.21 ? 64   PHE G CZ  1 
ATOM   7124  N  N   . ASN G  1 66  ? 143.719 -11.407 7.199  1.00 44.73 ? 65   ASN G N   1 
ATOM   7125  C  CA  . ASN G  1 66  ? 143.968 -12.383 6.150  0.00 47.49 ? 65   ASN G CA  1 
ATOM   7126  C  C   . ASN G  1 66  ? 143.590 -11.876 4.759  1.00 48.58 ? 65   ASN G C   1 
ATOM   7127  O  O   . ASN G  1 66  ? 142.615 -12.331 4.163  1.00 47.98 ? 65   ASN G O   1 
ATOM   7128  C  CB  . ASN G  1 66  ? 143.200 -13.664 6.489  0.00 48.75 ? 65   ASN G CB  1 
ATOM   7129  C  CG  . ASN G  1 66  ? 143.367 -14.740 5.449  1.00 50.54 ? 65   ASN G CG  1 
ATOM   7130  O  OD1 . ASN G  1 66  ? 144.475 -15.004 4.983  1.00 51.43 ? 65   ASN G OD1 1 
ATOM   7131  N  ND2 . ASN G  1 66  ? 142.264 -15.386 5.086  1.00 50.45 ? 65   ASN G ND2 1 
ATOM   7132  N  N   . PRO G  1 67  ? 144.371 -10.924 4.222  1.00 49.81 ? 66   PRO G N   1 
ATOM   7133  C  CA  . PRO G  1 67  ? 144.125 -10.346 2.896  1.00 51.75 ? 66   PRO G CA  1 
ATOM   7134  C  C   . PRO G  1 67  ? 144.383 -11.290 1.717  1.00 52.75 ? 66   PRO G C   1 
ATOM   7135  O  O   . PRO G  1 67  ? 143.964 -11.010 0.592  1.00 53.44 ? 66   PRO G O   1 
ATOM   7136  C  CB  . PRO G  1 67  ? 145.043 -9.126  2.880  1.00 51.06 ? 66   PRO G CB  1 
ATOM   7137  C  CG  . PRO G  1 67  ? 146.193 -9.573  3.718  1.00 51.65 ? 66   PRO G CG  1 
ATOM   7138  C  CD  . PRO G  1 67  ? 145.508 -10.255 4.879  1.00 49.86 ? 66   PRO G CD  1 
ATOM   7139  N  N   . LEU G  1 68  ? 145.068 -12.401 1.974  1.00 53.77 ? 67   LEU G N   1 
ATOM   7140  C  CA  . LEU G  1 68  ? 145.368 -13.378 0.927  1.00 54.83 ? 67   LEU G CA  1 
ATOM   7141  C  C   . LEU G  1 68  ? 144.459 -14.603 1.016  1.00 56.21 ? 67   LEU G C   1 
ATOM   7142  O  O   . LEU G  1 68  ? 144.647 -15.579 0.290  1.00 56.58 ? 67   LEU G O   1 
ATOM   7143  C  CB  . LEU G  1 68  ? 146.832 -13.822 1.018  1.00 54.55 ? 67   LEU G CB  1 
ATOM   7144  C  CG  . LEU G  1 68  ? 147.882 -12.735 0.794  0.00 54.64 ? 67   LEU G CG  1 
ATOM   7145  C  CD1 . LEU G  1 68  ? 149.279 -13.326 0.912  0.00 54.62 ? 67   LEU G CD1 1 
ATOM   7146  C  CD2 . LEU G  1 68  ? 147.677 -12.121 -0.577 0.00 54.62 ? 67   LEU G CD2 1 
ATOM   7147  N  N   . SER G  1 69  ? 143.473 -14.541 1.907  1.00 57.18 ? 68   SER G N   1 
ATOM   7148  C  CA  . SER G  1 69  ? 142.529 -15.639 2.105  1.00 57.73 ? 68   SER G CA  1 
ATOM   7149  C  C   . SER G  1 69  ? 143.206 -17.005 2.171  1.00 58.00 ? 68   SER G C   1 
ATOM   7150  O  O   . SER G  1 69  ? 142.782 -17.955 1.512  1.00 58.17 ? 68   SER G O   1 
ATOM   7151  C  CB  . SER G  1 69  ? 141.469 -15.641 0.999  1.00 57.20 ? 68   SER G CB  1 
ATOM   7152  O  OG  . SER G  1 69  ? 140.589 -14.539 1.133  1.00 57.59 ? 68   SER G OG  1 
ATOM   7153  N  N   . ARG G  1 70  ? 144.263 -17.094 2.972  1.00 58.84 ? 69   ARG G N   1 
ATOM   7154  C  CA  . ARG G  1 70  ? 144.997 -18.341 3.151  1.00 59.38 ? 69   ARG G CA  1 
ATOM   7155  C  C   . ARG G  1 70  ? 144.503 -18.948 4.458  1.00 59.35 ? 69   ARG G C   1 
ATOM   7156  O  O   . ARG G  1 70  ? 143.691 -18.341 5.160  1.00 59.06 ? 69   ARG G O   1 
ATOM   7157  C  CB  . ARG G  1 70  ? 146.498 -18.060 3.259  1.00 60.37 ? 69   ARG G CB  1 
ATOM   7158  C  CG  . ARG G  1 70  ? 147.036 -17.098 2.207  1.00 61.94 ? 69   ARG G CG  1 
ATOM   7159  C  CD  . ARG G  1 70  ? 147.343 -17.777 0.882  1.00 63.42 ? 69   ARG G CD  1 
ATOM   7160  N  NE  . ARG G  1 70  ? 148.512 -18.650 0.971  1.00 64.58 ? 69   ARG G NE  1 
ATOM   7161  C  CZ  . ARG G  1 70  ? 148.471 -19.932 1.323  1.00 64.64 ? 69   ARG G CZ  1 
ATOM   7162  N  NH1 . ARG G  1 70  ? 149.592 -20.640 1.380  1.00 64.21 ? 69   ARG G NH1 1 
ATOM   7163  N  NH2 . ARG G  1 70  ? 147.310 -20.510 1.600  1.00 64.90 ? 69   ARG G NH2 1 
ATOM   7164  N  N   . LYS G  1 71  ? 144.988 -20.140 4.788  1.00 59.13 ? 70   LYS G N   1 
ATOM   7165  C  CA  . LYS G  1 71  ? 144.590 -20.792 6.028  1.00 59.09 ? 70   LYS G CA  1 
ATOM   7166  C  C   . LYS G  1 71  ? 145.571 -20.435 7.133  1.00 58.59 ? 70   LYS G C   1 
ATOM   7167  O  O   . LYS G  1 71  ? 146.755 -20.208 6.873  1.00 59.40 ? 70   LYS G O   1 
ATOM   7168  C  CB  . LYS G  1 71  ? 144.538 -22.313 5.850  1.00 59.98 ? 70   LYS G CB  1 
ATOM   7169  C  CG  . LYS G  1 71  ? 143.393 -22.793 4.977  1.00 61.84 ? 70   LYS G CG  1 
ATOM   7170  C  CD  . LYS G  1 71  ? 143.378 -24.307 4.866  1.00 63.21 ? 70   LYS G CD  1 
ATOM   7171  C  CE  . LYS G  1 71  ? 142.224 -24.784 3.997  1.00 64.99 ? 70   LYS G CE  1 
ATOM   7172  N  NZ  . LYS G  1 71  ? 142.204 -26.269 3.870  1.00 65.89 ? 70   LYS G NZ  1 
ATOM   7173  N  N   . HIS G  1 72  ? 145.070 -20.381 8.363  1.00 57.03 ? 71   HIS G N   1 
ATOM   7174  C  CA  . HIS G  1 72  ? 145.895 -20.046 9.517  1.00 55.58 ? 71   HIS G CA  1 
ATOM   7175  C  C   . HIS G  1 72  ? 147.172 -20.883 9.570  1.00 55.74 ? 71   HIS G C   1 
ATOM   7176  O  O   . HIS G  1 72  ? 147.185 -22.041 9.155  1.00 55.94 ? 71   HIS G O   1 
ATOM   7177  C  CB  . HIS G  1 72  ? 145.105 -20.262 10.808 1.00 53.85 ? 71   HIS G CB  1 
ATOM   7178  C  CG  . HIS G  1 72  ? 145.875 -19.930 12.046 1.00 52.99 ? 71   HIS G CG  1 
ATOM   7179  N  ND1 . HIS G  1 72  ? 146.213 -18.638 12.386 1.00 52.08 ? 71   HIS G ND1 1 
ATOM   7180  C  CD2 . HIS G  1 72  ? 146.394 -20.723 13.015 1.00 52.83 ? 71   HIS G CD2 1 
ATOM   7181  C  CE1 . HIS G  1 72  ? 146.906 -18.649 13.513 1.00 53.54 ? 71   HIS G CE1 1 
ATOM   7182  N  NE2 . HIS G  1 72  ? 147.029 -19.902 13.913 1.00 53.96 ? 71   HIS G NE2 1 
ATOM   7183  N  N   . GLY G  1 73  ? 148.240 -20.288 10.090 1.00 55.19 ? 72   GLY G N   1 
ATOM   7184  C  CA  . GLY G  1 73  ? 149.502 -20.993 10.203 1.00 54.69 ? 72   GLY G CA  1 
ATOM   7185  C  C   . GLY G  1 73  ? 150.437 -20.292 11.169 1.00 54.90 ? 72   GLY G C   1 
ATOM   7186  O  O   . GLY G  1 73  ? 150.015 -19.415 11.923 1.00 56.22 ? 72   GLY G O   1 
ATOM   7187  N  N   . GLY G  1 74  ? 151.706 -20.686 11.159 1.00 54.30 ? 73   GLY G N   1 
ATOM   7188  C  CA  . GLY G  1 74  ? 152.680 -20.059 12.032 1.00 53.14 ? 73   GLY G CA  1 
ATOM   7189  C  C   . GLY G  1 74  ? 153.325 -18.890 11.310 1.00 52.56 ? 73   GLY G C   1 
ATOM   7190  O  O   . GLY G  1 74  ? 153.245 -18.809 10.083 1.00 51.90 ? 73   GLY G O   1 
ATOM   7191  N  N   . PRO G  1 75  ? 153.972 -17.965 12.034 1.00 52.40 ? 74   PRO G N   1 
ATOM   7192  C  CA  . PRO G  1 75  ? 154.616 -16.811 11.398 1.00 53.38 ? 74   PRO G CA  1 
ATOM   7193  C  C   . PRO G  1 75  ? 155.699 -17.194 10.388 1.00 55.31 ? 74   PRO G C   1 
ATOM   7194  O  O   . PRO G  1 75  ? 155.833 -16.562 9.336  1.00 54.52 ? 74   PRO G O   1 
ATOM   7195  C  CB  . PRO G  1 75  ? 155.171 -16.026 12.588 1.00 52.38 ? 74   PRO G CB  1 
ATOM   7196  C  CG  . PRO G  1 75  ? 155.432 -17.095 13.609 1.00 51.78 ? 74   PRO G CG  1 
ATOM   7197  C  CD  . PRO G  1 75  ? 154.203 -17.960 13.489 1.00 52.25 ? 74   PRO G CD  1 
ATOM   7198  N  N   . LYS G  1 76  ? 156.465 -18.234 10.708 1.00 55.78 ? 75   LYS G N   1 
ATOM   7199  C  CA  . LYS G  1 76  ? 157.532 -18.691 9.827  1.00 57.52 ? 75   LYS G CA  1 
ATOM   7200  C  C   . LYS G  1 76  ? 157.065 -19.829 8.924  1.00 58.55 ? 75   LYS G C   1 
ATOM   7201  O  O   . LYS G  1 76  ? 157.877 -20.509 8.295  1.00 58.78 ? 75   LYS G O   1 
ATOM   7202  C  CB  . LYS G  1 76  ? 158.744 -19.135 10.655 1.00 56.91 ? 75   LYS G CB  1 
ATOM   7203  C  CG  . LYS G  1 76  ? 159.355 -18.017 11.493 1.00 56.41 ? 75   LYS G CG  1 
ATOM   7204  C  CD  . LYS G  1 76  ? 159.836 -16.875 10.608 0.00 55.86 ? 75   LYS G CD  1 
ATOM   7205  C  CE  . LYS G  1 76  ? 160.289 -15.681 11.431 1.00 55.62 ? 75   LYS G CE  1 
ATOM   7206  N  NZ  . LYS G  1 76  ? 160.837 -14.591 10.570 1.00 54.50 ? 75   LYS G NZ  1 
ATOM   7207  N  N   . ASP G  1 77  ? 155.752 -20.031 8.862  1.00 59.70 ? 76   ASP G N   1 
ATOM   7208  C  CA  . ASP G  1 77  ? 155.187 -21.083 8.025  1.00 60.92 ? 76   ASP G CA  1 
ATOM   7209  C  C   . ASP G  1 77  ? 154.876 -20.551 6.630  1.00 60.66 ? 76   ASP G C   1 
ATOM   7210  O  O   . ASP G  1 77  ? 154.690 -19.350 6.439  1.00 60.00 ? 76   ASP G O   1 
ATOM   7211  C  CB  . ASP G  1 77  ? 153.911 -21.653 8.660  1.00 62.19 ? 76   ASP G CB  1 
ATOM   7212  C  CG  . ASP G  1 77  ? 154.197 -22.519 9.880  1.00 64.81 ? 76   ASP G CG  1 
ATOM   7213  O  OD1 . ASP G  1 77  ? 153.234 -23.049 10.476 1.00 65.18 ? 76   ASP G OD1 1 
ATOM   7214  O  OD2 . ASP G  1 77  ? 155.384 -22.673 10.244 1.00 66.24 ? 76   ASP G OD2 1 
ATOM   7215  N  N   . GLU G  1 78  ? 154.831 -21.458 5.659  1.00 61.23 ? 77   GLU G N   1 
ATOM   7216  C  CA  . GLU G  1 78  ? 154.539 -21.102 4.274  1.00 61.04 ? 77   GLU G CA  1 
ATOM   7217  C  C   . GLU G  1 78  ? 153.125 -20.545 4.171  1.00 60.99 ? 77   GLU G C   1 
ATOM   7218  O  O   . GLU G  1 78  ? 152.933 -19.380 3.824  1.00 61.33 ? 77   GLU G O   1 
ATOM   7219  C  CB  . GLU G  1 78  ? 154.682 -22.337 3.386  0.00 60.60 ? 77   GLU G CB  1 
ATOM   7220  C  CG  . GLU G  1 78  ? 156.088 -22.907 3.366  0.00 60.07 ? 77   GLU G CG  1 
ATOM   7221  C  CD  . GLU G  1 78  ? 156.102 -24.412 3.209  0.00 59.78 ? 77   GLU G CD  1 
ATOM   7222  O  OE1 . GLU G  1 78  ? 155.591 -25.105 4.115  0.00 59.60 ? 77   GLU G OE1 1 
ATOM   7223  O  OE2 . GLU G  1 78  ? 156.620 -24.904 2.186  0.00 59.61 ? 77   GLU G OE2 1 
ATOM   7224  N  N   . GLU G  1 79  ? 152.136 -21.384 4.470  1.00 60.91 ? 78   GLU G N   1 
ATOM   7225  C  CA  . GLU G  1 79  ? 150.743 -20.958 4.426  1.00 60.55 ? 78   GLU G CA  1 
ATOM   7226  C  C   . GLU G  1 79  ? 150.344 -20.363 5.769  1.00 59.51 ? 78   GLU G C   1 
ATOM   7227  O  O   . GLU G  1 79  ? 150.471 -21.009 6.812  1.00 59.52 ? 78   GLU G O   1 
ATOM   7228  C  CB  . GLU G  1 79  ? 149.816 -22.129 4.100  1.00 61.47 ? 78   GLU G CB  1 
ATOM   7229  C  CG  . GLU G  1 79  ? 148.350 -21.722 4.081  1.00 62.79 ? 78   GLU G CG  1 
ATOM   7230  C  CD  . GLU G  1 79  ? 147.431 -22.825 3.605  1.00 63.56 ? 78   GLU G CD  1 
ATOM   7231  O  OE1 . GLU G  1 79  ? 146.230 -22.545 3.414  1.00 64.85 ? 78   GLU G OE1 1 
ATOM   7232  O  OE2 . GLU G  1 79  ? 147.902 -23.967 3.424  1.00 64.84 ? 78   GLU G OE2 1 
ATOM   7233  N  N   . ARG G  1 80  ? 149.852 -19.130 5.735  1.00 57.83 ? 79   ARG G N   1 
ATOM   7234  C  CA  . ARG G  1 80  ? 149.447 -18.443 6.951  1.00 55.40 ? 79   ARG G CA  1 
ATOM   7235  C  C   . ARG G  1 80  ? 148.758 -17.118 6.648  1.00 53.56 ? 79   ARG G C   1 
ATOM   7236  O  O   . ARG G  1 80  ? 148.755 -16.648 5.508  1.00 51.75 ? 79   ARG G O   1 
ATOM   7237  C  CB  . ARG G  1 80  ? 150.675 -18.213 7.839  1.00 56.00 ? 79   ARG G CB  1 
ATOM   7238  C  CG  . ARG G  1 80  ? 151.892 -17.687 7.085  1.00 57.44 ? 79   ARG G CG  1 
ATOM   7239  C  CD  . ARG G  1 80  ? 151.919 -16.172 7.034  1.00 56.84 ? 79   ARG G CD  1 
ATOM   7240  N  NE  . ARG G  1 80  ? 152.639 -15.608 8.173  1.00 58.14 ? 79   ARG G NE  1 
ATOM   7241  C  CZ  . ARG G  1 80  ? 152.656 -14.315 8.480  1.00 58.84 ? 79   ARG G CZ  1 
ATOM   7242  N  NH1 . ARG G  1 80  ? 153.342 -13.886 9.531  1.00 59.54 ? 79   ARG G NH1 1 
ATOM   7243  N  NH2 . ARG G  1 80  ? 151.971 -13.452 7.745  1.00 59.66 ? 79   ARG G NH2 1 
ATOM   7244  N  N   . HIS G  1 81  ? 148.156 -16.536 7.680  1.00 50.55 ? 80   HIS G N   1 
ATOM   7245  C  CA  . HIS G  1 81  ? 147.474 -15.256 7.562  1.00 48.80 ? 80   HIS G CA  1 
ATOM   7246  C  C   . HIS G  1 81  ? 148.537 -14.184 7.756  1.00 46.51 ? 80   HIS G C   1 
ATOM   7247  O  O   . HIS G  1 81  ? 149.519 -14.402 8.466  1.00 46.41 ? 80   HIS G O   1 
ATOM   7248  C  CB  . HIS G  1 81  ? 146.414 -15.118 8.660  1.00 49.12 ? 80   HIS G CB  1 
ATOM   7249  C  CG  . HIS G  1 81  ? 145.338 -16.159 8.604  1.00 49.36 ? 80   HIS G CG  1 
ATOM   7250  N  ND1 . HIS G  1 81  ? 144.633 -16.561 9.721  1.00 47.35 ? 80   HIS G ND1 1 
ATOM   7251  C  CD2 . HIS G  1 81  ? 144.819 -16.854 7.566  1.00 49.23 ? 80   HIS G CD2 1 
ATOM   7252  C  CE1 . HIS G  1 81  ? 143.730 -17.455 9.373  1.00 48.65 ? 80   HIS G CE1 1 
ATOM   7253  N  NE2 . HIS G  1 81  ? 143.819 -17.653 8.066  1.00 49.83 ? 80   HIS G NE2 1 
ATOM   7254  N  N   . VAL G  1 82  ? 148.354 -13.030 7.129  1.00 45.21 ? 81   VAL G N   1 
ATOM   7255  C  CA  . VAL G  1 82  ? 149.321 -11.955 7.291  1.00 43.18 ? 81   VAL G CA  1 
ATOM   7256  C  C   . VAL G  1 82  ? 149.462 -11.614 8.772  1.00 41.91 ? 81   VAL G C   1 
ATOM   7257  O  O   . VAL G  1 82  ? 150.548 -11.268 9.235  1.00 41.73 ? 81   VAL G O   1 
ATOM   7258  C  CB  . VAL G  1 82  ? 148.891 -10.684 6.529  1.00 43.11 ? 81   VAL G CB  1 
ATOM   7259  C  CG1 . VAL G  1 82  ? 149.813 -9.527  6.888  1.00 41.38 ? 81   VAL G CG1 1 
ATOM   7260  C  CG2 . VAL G  1 82  ? 148.928 -10.938 5.028  1.00 42.48 ? 81   VAL G CG2 1 
ATOM   7261  N  N   . GLY G  1 83  ? 148.364 -11.732 9.515  1.00 41.04 ? 82   GLY G N   1 
ATOM   7262  C  CA  . GLY G  1 83  ? 148.393 -11.409 10.932 1.00 40.99 ? 82   GLY G CA  1 
ATOM   7263  C  C   . GLY G  1 83  ? 148.919 -12.477 11.877 1.00 40.74 ? 82   GLY G C   1 
ATOM   7264  O  O   . GLY G  1 83  ? 149.045 -12.229 13.079 1.00 39.38 ? 82   GLY G O   1 
ATOM   7265  N  N   . ASP G  1 84  ? 149.239 -13.656 11.351 1.00 41.66 ? 83   ASP G N   1 
ATOM   7266  C  CA  . ASP G  1 84  ? 149.732 -14.748 12.188 1.00 41.93 ? 83   ASP G CA  1 
ATOM   7267  C  C   . ASP G  1 84  ? 151.139 -14.542 12.740 1.00 42.25 ? 83   ASP G C   1 
ATOM   7268  O  O   . ASP G  1 84  ? 152.131 -14.718 12.029 1.00 43.45 ? 83   ASP G O   1 
ATOM   7269  C  CB  . ASP G  1 84  ? 149.672 -16.073 11.421 1.00 42.01 ? 83   ASP G CB  1 
ATOM   7270  C  CG  . ASP G  1 84  ? 148.249 -16.506 11.123 1.00 42.18 ? 83   ASP G CG  1 
ATOM   7271  O  OD1 . ASP G  1 84  ? 147.340 -16.129 11.898 1.00 42.01 ? 83   ASP G OD1 1 
ATOM   7272  O  OD2 . ASP G  1 84  ? 148.038 -17.234 10.129 1.00 38.82 ? 83   ASP G OD2 1 
ATOM   7273  N  N   . LEU G  1 85  ? 151.220 -14.188 14.020 1.00 41.68 ? 84   LEU G N   1 
ATOM   7274  C  CA  . LEU G  1 85  ? 152.505 -13.964 14.669 1.00 42.28 ? 84   LEU G CA  1 
ATOM   7275  C  C   . LEU G  1 85  ? 152.866 -15.075 15.651 1.00 42.49 ? 84   LEU G C   1 
ATOM   7276  O  O   . LEU G  1 85  ? 153.725 -14.898 16.515 1.00 42.06 ? 84   LEU G O   1 
ATOM   7277  C  CB  . LEU G  1 85  ? 152.510 -12.615 15.388 1.00 42.01 ? 84   LEU G CB  1 
ATOM   7278  C  CG  . LEU G  1 85  ? 152.321 -11.390 14.488 1.00 43.17 ? 84   LEU G CG  1 
ATOM   7279  C  CD1 . LEU G  1 85  ? 152.459 -10.121 15.326 1.00 41.18 ? 84   LEU G CD1 1 
ATOM   7280  C  CD2 . LEU G  1 85  ? 153.350 -11.402 13.362 1.00 40.92 ? 84   LEU G CD2 1 
ATOM   7281  N  N   . GLY G  1 86  ? 152.195 -16.215 15.518 1.00 43.47 ? 85   GLY G N   1 
ATOM   7282  C  CA  . GLY G  1 86  ? 152.479 -17.356 16.373 1.00 44.49 ? 85   GLY G CA  1 
ATOM   7283  C  C   . GLY G  1 86  ? 152.110 -17.244 17.839 1.00 44.83 ? 85   GLY G C   1 
ATOM   7284  O  O   . GLY G  1 86  ? 150.998 -16.849 18.187 1.00 44.68 ? 85   GLY G O   1 
ATOM   7285  N  N   . ASN G  1 87  ? 153.055 -17.609 18.699 1.00 45.09 ? 86   ASN G N   1 
ATOM   7286  C  CA  . ASN G  1 87  ? 152.849 -17.571 20.141 1.00 45.99 ? 86   ASN G CA  1 
ATOM   7287  C  C   . ASN G  1 87  ? 153.909 -16.737 20.835 1.00 45.43 ? 86   ASN G C   1 
ATOM   7288  O  O   . ASN G  1 87  ? 154.971 -16.458 20.279 1.00 45.67 ? 86   ASN G O   1 
ATOM   7289  C  CB  . ASN G  1 87  ? 152.903 -18.988 20.738 1.00 47.71 ? 86   ASN G CB  1 
ATOM   7290  C  CG  . ASN G  1 87  ? 151.731 -19.854 20.323 1.00 49.69 ? 86   ASN G CG  1 
ATOM   7291  O  OD1 . ASN G  1 87  ? 150.579 -19.554 20.642 1.00 50.10 ? 86   ASN G OD1 1 
ATOM   7292  N  ND2 . ASN G  1 87  ? 152.018 -20.941 19.611 1.00 49.62 ? 86   ASN G ND2 1 
ATOM   7293  N  N   . VAL G  1 88  ? 153.601 -16.346 22.065 1.00 44.51 ? 87   VAL G N   1 
ATOM   7294  C  CA  . VAL G  1 88  ? 154.513 -15.588 22.906 1.00 44.03 ? 87   VAL G CA  1 
ATOM   7295  C  C   . VAL G  1 88  ? 154.570 -16.429 24.176 1.00 43.81 ? 87   VAL G C   1 
ATOM   7296  O  O   . VAL G  1 88  ? 153.621 -17.154 24.473 1.00 43.56 ? 87   VAL G O   1 
ATOM   7297  C  CB  . VAL G  1 88  ? 153.966 -14.176 23.218 1.00 45.36 ? 87   VAL G CB  1 
ATOM   7298  C  CG1 . VAL G  1 88  ? 153.927 -13.347 21.945 1.00 44.67 ? 87   VAL G CG1 1 
ATOM   7299  C  CG2 . VAL G  1 88  ? 152.574 -14.271 23.831 1.00 45.03 ? 87   VAL G CG2 1 
ATOM   7300  N  N   . THR G  1 89  ? 155.669 -16.349 24.920 1.00 43.26 ? 88   THR G N   1 
ATOM   7301  C  CA  . THR G  1 89  ? 155.802 -17.154 26.127 1.00 43.66 ? 88   THR G CA  1 
ATOM   7302  C  C   . THR G  1 89  ? 155.815 -16.365 27.427 1.00 43.35 ? 88   THR G C   1 
ATOM   7303  O  O   . THR G  1 89  ? 156.587 -15.420 27.591 1.00 43.41 ? 88   THR G O   1 
ATOM   7304  C  CB  . THR G  1 89  ? 157.077 -18.019 26.072 1.00 44.83 ? 88   THR G CB  1 
ATOM   7305  O  OG1 . THR G  1 89  ? 157.032 -18.855 24.911 1.00 45.45 ? 88   THR G OG1 1 
ATOM   7306  C  CG2 . THR G  1 89  ? 157.185 -18.900 27.320 1.00 44.69 ? 88   THR G CG2 1 
ATOM   7307  N  N   . ALA G  1 90  ? 154.955 -16.776 28.353 1.00 43.36 ? 89   ALA G N   1 
ATOM   7308  C  CA  . ALA G  1 90  ? 154.851 -16.135 29.656 1.00 43.04 ? 89   ALA G CA  1 
ATOM   7309  C  C   . ALA G  1 90  ? 155.648 -16.947 30.673 1.00 42.79 ? 89   ALA G C   1 
ATOM   7310  O  O   . ALA G  1 90  ? 155.471 -18.161 30.780 1.00 41.21 ? 89   ALA G O   1 
ATOM   7311  C  CB  . ALA G  1 90  ? 153.388 -16.049 30.082 1.00 41.90 ? 89   ALA G CB  1 
ATOM   7312  N  N   . ASP G  1 91  ? 156.518 -16.269 31.416 1.00 43.61 ? 90   ASP G N   1 
ATOM   7313  C  CA  . ASP G  1 91  ? 157.352 -16.922 32.420 1.00 45.61 ? 90   ASP G CA  1 
ATOM   7314  C  C   . ASP G  1 91  ? 156.576 -17.261 33.692 1.00 46.65 ? 90   ASP G C   1 
ATOM   7315  O  O   . ASP G  1 91  ? 155.370 -17.026 33.778 1.00 46.71 ? 90   ASP G O   1 
ATOM   7316  C  CB  . ASP G  1 91  ? 158.558 -16.034 32.756 1.00 43.45 ? 90   ASP G CB  1 
ATOM   7317  C  CG  . ASP G  1 91  ? 158.168 -14.737 33.455 1.00 45.65 ? 90   ASP G CG  1 
ATOM   7318  O  OD1 . ASP G  1 91  ? 159.030 -13.836 33.554 1.00 44.82 ? 90   ASP G OD1 1 
ATOM   7319  O  OD2 . ASP G  1 91  ? 157.012 -14.614 33.916 1.00 45.09 ? 90   ASP G OD2 1 
ATOM   7320  N  N   . LYS G  1 92  ? 157.279 -17.812 34.676 1.00 47.84 ? 91   LYS G N   1 
ATOM   7321  C  CA  . LYS G  1 92  ? 156.669 -18.198 35.947 1.00 49.03 ? 91   LYS G CA  1 
ATOM   7322  C  C   . LYS G  1 92  ? 155.994 -17.032 36.667 1.00 48.64 ? 91   LYS G C   1 
ATOM   7323  O  O   . LYS G  1 92  ? 155.159 -17.242 37.543 1.00 49.18 ? 91   LYS G O   1 
ATOM   7324  C  CB  . LYS G  1 92  ? 157.724 -18.821 36.868 1.00 49.35 ? 91   LYS G CB  1 
ATOM   7325  C  CG  . LYS G  1 92  ? 158.878 -17.890 37.203 0.00 50.30 ? 91   LYS G CG  1 
ATOM   7326  C  CD  . LYS G  1 92  ? 159.865 -18.551 38.149 1.00 51.00 ? 91   LYS G CD  1 
ATOM   7327  C  CE  . LYS G  1 92  ? 161.033 -17.632 38.467 0.00 51.24 ? 91   LYS G CE  1 
ATOM   7328  N  NZ  . LYS G  1 92  ? 162.011 -18.281 39.384 0.00 51.51 ? 91   LYS G NZ  1 
ATOM   7329  N  N   . ASP G  1 93  ? 156.359 -15.808 36.303 1.00 48.95 ? 92   ASP G N   1 
ATOM   7330  C  CA  . ASP G  1 93  ? 155.770 -14.628 36.928 1.00 49.10 ? 92   ASP G CA  1 
ATOM   7331  C  C   . ASP G  1 93  ? 154.642 -14.033 36.078 1.00 47.74 ? 92   ASP G C   1 
ATOM   7332  O  O   . ASP G  1 93  ? 154.152 -12.944 36.355 1.00 47.37 ? 92   ASP G O   1 
ATOM   7333  C  CB  . ASP G  1 93  ? 156.851 -13.572 37.187 1.00 51.43 ? 92   ASP G CB  1 
ATOM   7334  C  CG  . ASP G  1 93  ? 157.946 -14.069 38.123 1.00 55.06 ? 92   ASP G CG  1 
ATOM   7335  O  OD1 . ASP G  1 93  ? 158.827 -14.833 37.671 1.00 56.87 ? 92   ASP G OD1 1 
ATOM   7336  O  OD2 . ASP G  1 93  ? 157.918 -13.703 39.318 1.00 56.24 ? 92   ASP G OD2 1 
ATOM   7337  N  N   . GLY G  1 94  ? 154.232 -14.747 35.037 1.00 46.75 ? 93   GLY G N   1 
ATOM   7338  C  CA  . GLY G  1 94  ? 153.156 -14.255 34.193 1.00 46.17 ? 93   GLY G CA  1 
ATOM   7339  C  C   . GLY G  1 94  ? 153.573 -13.184 33.203 1.00 46.46 ? 93   GLY G C   1 
ATOM   7340  O  O   . GLY G  1 94  ? 152.730 -12.551 32.563 1.00 45.33 ? 93   GLY G O   1 
ATOM   7341  N  N   . VAL G  1 95  ? 154.878 -12.986 33.064 1.00 46.55 ? 94   VAL G N   1 
ATOM   7342  C  CA  . VAL G  1 95  ? 155.400 -11.979 32.152 1.00 46.98 ? 94   VAL G CA  1 
ATOM   7343  C  C   . VAL G  1 95  ? 155.931 -12.576 30.852 1.00 48.26 ? 94   VAL G C   1 
ATOM   7344  O  O   . VAL G  1 95  ? 156.737 -13.510 30.861 1.00 47.97 ? 94   VAL G O   1 
ATOM   7345  C  CB  . VAL G  1 95  ? 156.520 -11.159 32.827 1.00 46.63 ? 94   VAL G CB  1 
ATOM   7346  C  CG1 . VAL G  1 95  ? 157.150 -10.197 31.828 1.00 45.60 ? 94   VAL G CG1 1 
ATOM   7347  C  CG2 . VAL G  1 95  ? 155.948 -10.391 34.010 1.00 45.63 ? 94   VAL G CG2 1 
ATOM   7348  N  N   . ALA G  1 96  ? 155.464 -12.029 29.735 1.00 47.67 ? 95   ALA G N   1 
ATOM   7349  C  CA  . ALA G  1 96  ? 155.889 -12.483 28.421 1.00 48.11 ? 95   ALA G CA  1 
ATOM   7350  C  C   . ALA G  1 96  ? 156.714 -11.391 27.753 1.00 49.14 ? 95   ALA G C   1 
ATOM   7351  O  O   . ALA G  1 96  ? 156.196 -10.329 27.402 1.00 48.69 ? 95   ALA G O   1 
ATOM   7352  C  CB  . ALA G  1 96  ? 154.676 -12.824 27.564 1.00 47.04 ? 95   ALA G CB  1 
ATOM   7353  N  N   . ASP G  1 97  ? 158.005 -11.655 27.598 1.00 49.18 ? 96   ASP G N   1 
ATOM   7354  C  CA  . ASP G  1 97  ? 158.916 -10.713 26.965 1.00 50.34 ? 96   ASP G CA  1 
ATOM   7355  C  C   . ASP G  1 97  ? 158.927 -11.004 25.466 1.00 49.78 ? 96   ASP G C   1 
ATOM   7356  O  O   . ASP G  1 97  ? 159.357 -12.073 25.032 1.00 49.23 ? 96   ASP G O   1 
ATOM   7357  C  CB  . ASP G  1 97  ? 160.308 -10.873 27.577 1.00 52.42 ? 96   ASP G CB  1 
ATOM   7358  C  CG  . ASP G  1 97  ? 160.326 -10.538 29.061 1.00 55.17 ? 96   ASP G CG  1 
ATOM   7359  O  OD1 . ASP G  1 97  ? 161.173 -11.088 29.799 1.00 56.92 ? 96   ASP G OD1 1 
ATOM   7360  O  OD2 . ASP G  1 97  ? 159.489 -9.714  29.491 1.00 56.56 ? 96   ASP G OD2 1 
ATOM   7361  N  N   . VAL G  1 98  ? 158.438 -10.046 24.682 1.00 48.04 ? 97   VAL G N   1 
ATOM   7362  C  CA  . VAL G  1 98  ? 158.349 -10.202 23.235 1.00 47.90 ? 97   VAL G CA  1 
ATOM   7363  C  C   . VAL G  1 98  ? 159.515 -9.596  22.455 1.00 48.30 ? 97   VAL G C   1 
ATOM   7364  O  O   . VAL G  1 98  ? 159.951 -8.473  22.715 1.00 47.45 ? 97   VAL G O   1 
ATOM   7365  C  CB  . VAL G  1 98  ? 157.026 -9.596  22.710 1.00 47.24 ? 97   VAL G CB  1 
ATOM   7366  C  CG1 . VAL G  1 98  ? 156.903 -9.818  21.214 1.00 47.51 ? 97   VAL G CG1 1 
ATOM   7367  C  CG2 . VAL G  1 98  ? 155.848 -10.226 23.434 1.00 47.42 ? 97   VAL G CG2 1 
ATOM   7368  N  N   . SER G  1 99  ? 160.008 -10.366 21.494 1.00 49.48 ? 98   SER G N   1 
ATOM   7369  C  CA  . SER G  1 99  ? 161.111 -9.948  20.643 1.00 50.76 ? 98   SER G CA  1 
ATOM   7370  C  C   . SER G  1 99  ? 161.080 -10.816 19.408 1.00 51.20 ? 98   SER G C   1 
ATOM   7371  O  O   . SER G  1 99  ? 161.601 -11.932 19.395 1.00 52.18 ? 98   SER G O   1 
ATOM   7372  C  CB  . SER G  1 99  ? 162.453 -10.129 21.350 1.00 51.65 ? 98   SER G CB  1 
ATOM   7373  O  OG  . SER G  1 99  ? 163.527 -9.800  20.484 0.00 51.49 ? 98   SER G OG  1 
ATOM   7374  N  N   . ILE G  1 100 ? 160.439 -10.318 18.365 1.00 51.11 ? 99   ILE G N   1 
ATOM   7375  C  CA  . ILE G  1 100 ? 160.374 -11.087 17.139 1.00 50.43 ? 99   ILE G CA  1 
ATOM   7376  C  C   . ILE G  1 100 ? 160.511 -10.214 15.922 1.00 50.35 ? 99   ILE G C   1 
ATOM   7377  O  O   . ILE G  1 100 ? 160.447 -8.991  16.004 1.00 49.40 ? 99   ILE G O   1 
ATOM   7378  C  CB  . ILE G  1 100 ? 159.047 -11.850 16.996 1.00 50.63 ? 99   ILE G CB  1 
ATOM   7379  C  CG1 . ILE G  1 100 ? 157.914 -10.876 16.688 1.00 50.04 ? 99   ILE G CG1 1 
ATOM   7380  C  CG2 . ILE G  1 100 ? 158.766 -12.633 18.244 1.00 51.46 ? 99   ILE G CG2 1 
ATOM   7381  C  CD1 . ILE G  1 100 ? 156.566 -11.559 16.507 1.00 52.25 ? 99   ILE G CD1 1 
ATOM   7382  N  N   . GLU G  1 101 ? 160.652 -10.868 14.783 1.00 50.07 ? 100  GLU G N   1 
ATOM   7383  C  CA  . GLU G  1 101 ? 160.789 -10.168 13.535 1.00 50.14 ? 100  GLU G CA  1 
ATOM   7384  C  C   . GLU G  1 101 ? 159.995 -10.964 12.508 1.00 48.64 ? 100  GLU G C   1 
ATOM   7385  O  O   . GLU G  1 101 ? 160.138 -12.189 12.401 1.00 47.44 ? 100  GLU G O   1 
ATOM   7386  C  CB  . GLU G  1 101 ? 162.273 -10.052 13.180 1.00 52.55 ? 100  GLU G CB  1 
ATOM   7387  C  CG  . GLU G  1 101 ? 162.536 -8.985  12.171 1.00 55.77 ? 100  GLU G CG  1 
ATOM   7388  C  CD  . GLU G  1 101 ? 163.972 -8.513  12.165 1.00 58.09 ? 100  GLU G CD  1 
ATOM   7389  O  OE1 . GLU G  1 101 ? 164.419 -8.072  11.089 1.00 58.17 ? 100  GLU G OE1 1 
ATOM   7390  O  OE2 . GLU G  1 101 ? 164.648 -8.560  13.219 1.00 58.72 ? 100  GLU G OE2 1 
ATOM   7391  N  N   . ASP G  1 102 ? 159.105 -10.258 11.813 1.00 48.21 ? 101  ASP G N   1 
ATOM   7392  C  CA  . ASP G  1 102 ? 158.256 -10.865 10.796 1.00 48.66 ? 101  ASP G CA  1 
ATOM   7393  C  C   . ASP G  1 102 ? 158.365 -10.110 9.468  1.00 48.97 ? 101  ASP G C   1 
ATOM   7394  O  O   . ASP G  1 102 ? 158.382 -8.877  9.441  1.00 48.95 ? 101  ASP G O   1 
ATOM   7395  C  CB  . ASP G  1 102 ? 156.796 -10.880 11.265 1.00 47.82 ? 101  ASP G CB  1 
ATOM   7396  C  CG  . ASP G  1 102 ? 155.881 -11.641 10.311 1.00 47.99 ? 101  ASP G CG  1 
ATOM   7397  O  OD1 . ASP G  1 102 ? 155.536 -11.113 9.232  1.00 49.41 ? 101  ASP G OD1 1 
ATOM   7398  O  OD2 . ASP G  1 102 ? 155.509 -12.786 10.638 1.00 50.22 ? 101  ASP G OD2 1 
ATOM   7399  N  N   . SER G  1 103 ? 158.404 -10.858 8.368  1.00 48.84 ? 102  SER G N   1 
ATOM   7400  C  CA  . SER G  1 103 ? 158.535 -10.274 7.032  1.00 49.47 ? 102  SER G CA  1 
ATOM   7401  C  C   . SER G  1 103 ? 157.223 -10.084 6.274  1.00 49.51 ? 102  SER G C   1 
ATOM   7402  O  O   . SER G  1 103 ? 157.175 -9.345  5.286  1.00 48.78 ? 102  SER G O   1 
ATOM   7403  C  CB  . SER G  1 103 ? 159.473 -11.136 6.181  1.00 50.43 ? 102  SER G CB  1 
ATOM   7404  O  OG  . SER G  1 103 ? 160.725 -11.295 6.819  1.00 48.80 ? 102  SER G OG  1 
ATOM   7405  N  N   . VAL G  1 104 ? 156.167 -10.750 6.732  1.00 49.25 ? 103  VAL G N   1 
ATOM   7406  C  CA  . VAL G  1 104 ? 154.867 -10.663 6.077  1.00 48.61 ? 103  VAL G CA  1 
ATOM   7407  C  C   . VAL G  1 104 ? 154.079 -9.410  6.461  1.00 48.51 ? 103  VAL G C   1 
ATOM   7408  O  O   . VAL G  1 104 ? 153.486 -8.759  5.596  1.00 47.99 ? 103  VAL G O   1 
ATOM   7409  C  CB  . VAL G  1 104 ? 154.019 -11.904 6.383  1.00 49.36 ? 103  VAL G CB  1 
ATOM   7410  C  CG1 . VAL G  1 104 ? 152.777 -11.908 5.504  1.00 48.92 ? 103  VAL G CG1 1 
ATOM   7411  C  CG2 . VAL G  1 104 ? 154.847 -13.162 6.154  1.00 49.81 ? 103  VAL G CG2 1 
ATOM   7412  N  N   . ILE G  1 105 ? 154.059 -9.080  7.750  1.00 46.86 ? 104  ILE G N   1 
ATOM   7413  C  CA  . ILE G  1 105 ? 153.355 -7.887  8.205  1.00 44.92 ? 104  ILE G CA  1 
ATOM   7414  C  C   . ILE G  1 105 ? 154.170 -6.687  7.726  1.00 44.88 ? 104  ILE G C   1 
ATOM   7415  O  O   . ILE G  1 105 ? 155.342 -6.825  7.382  1.00 45.03 ? 104  ILE G O   1 
ATOM   7416  C  CB  . ILE G  1 105 ? 153.239 -7.838  9.754  1.00 42.77 ? 104  ILE G CB  1 
ATOM   7417  C  CG1 . ILE G  1 105 ? 154.632 -7.823  10.386 1.00 41.14 ? 104  ILE G CG1 1 
ATOM   7418  C  CG2 . ILE G  1 105 ? 152.443 -9.040  10.258 1.00 42.70 ? 104  ILE G CG2 1 
ATOM   7419  C  CD1 . ILE G  1 105 ? 154.628 -7.576  11.883 1.00 38.52 ? 104  ILE G CD1 1 
ATOM   7420  N  N   . SER G  1 106 ? 153.551 -5.515  7.695  1.00 44.66 ? 105  SER G N   1 
ATOM   7421  C  CA  . SER G  1 106 ? 154.236 -4.306  7.265  1.00 43.71 ? 105  SER G CA  1 
ATOM   7422  C  C   . SER G  1 106 ? 153.529 -3.116  7.896  1.00 43.06 ? 105  SER G C   1 
ATOM   7423  O  O   . SER G  1 106 ? 152.393 -3.228  8.346  1.00 42.13 ? 105  SER G O   1 
ATOM   7424  C  CB  . SER G  1 106 ? 154.199 -4.192  5.740  1.00 43.21 ? 105  SER G CB  1 
ATOM   7425  O  OG  . SER G  1 106 ? 154.958 -3.086  5.284  1.00 44.80 ? 105  SER G OG  1 
ATOM   7426  N  N   . LEU G  1 107 ? 154.206 -1.978  7.958  1.00 42.44 ? 106  LEU G N   1 
ATOM   7427  C  CA  . LEU G  1 107 ? 153.608 -0.786  8.547  1.00 43.08 ? 106  LEU G CA  1 
ATOM   7428  C  C   . LEU G  1 107 ? 153.169 0.193   7.469  1.00 44.91 ? 106  LEU G C   1 
ATOM   7429  O  O   . LEU G  1 107 ? 152.991 1.388   7.720  1.00 44.89 ? 106  LEU G O   1 
ATOM   7430  C  CB  . LEU G  1 107 ? 154.582 -0.119  9.528  1.00 40.90 ? 106  LEU G CB  1 
ATOM   7431  C  CG  . LEU G  1 107 ? 155.128 -1.088  10.586 1.00 40.56 ? 106  LEU G CG  1 
ATOM   7432  C  CD1 . LEU G  1 107 ? 156.025 -0.342  11.561 1.00 40.42 ? 106  LEU G CD1 1 
ATOM   7433  C  CD2 . LEU G  1 107 ? 153.978 -1.763  11.322 1.00 39.07 ? 106  LEU G CD2 1 
ATOM   7434  N  N   . SER G  1 108 ? 152.955 -0.352  6.276  1.00 47.71 ? 107  SER G N   1 
ATOM   7435  C  CA  . SER G  1 108 ? 152.525 0.411   5.116  1.00 50.04 ? 107  SER G CA  1 
ATOM   7436  C  C   . SER G  1 108 ? 152.185 -0.576  4.004  1.00 51.41 ? 107  SER G C   1 
ATOM   7437  O  O   . SER G  1 108 ? 152.636 -1.722  4.026  1.00 50.80 ? 107  SER G O   1 
ATOM   7438  C  CB  . SER G  1 108 ? 153.649 1.335   4.650  1.00 51.67 ? 107  SER G CB  1 
ATOM   7439  O  OG  . SER G  1 108 ? 154.763 0.588   4.183  1.00 53.87 ? 107  SER G OG  1 
ATOM   7440  N  N   . GLY G  1 109 ? 151.395 -0.130  3.032  1.00 52.39 ? 108  GLY G N   1 
ATOM   7441  C  CA  . GLY G  1 109 ? 151.027 -0.999  1.927  1.00 53.32 ? 108  GLY G CA  1 
ATOM   7442  C  C   . GLY G  1 109 ? 149.792 -1.836  2.199  1.00 54.35 ? 108  GLY G C   1 
ATOM   7443  O  O   . GLY G  1 109 ? 149.137 -1.682  3.232  1.00 53.90 ? 108  GLY G O   1 
ATOM   7444  N  N   . ASP G  1 110 ? 149.474 -2.730  1.266  1.00 55.76 ? 109  ASP G N   1 
ATOM   7445  C  CA  . ASP G  1 110 ? 148.308 -3.601  1.394  1.00 55.65 ? 109  ASP G CA  1 
ATOM   7446  C  C   . ASP G  1 110 ? 148.407 -4.528  2.602  1.00 53.72 ? 109  ASP G C   1 
ATOM   7447  O  O   . ASP G  1 110 ? 147.391 -5.022  3.097  1.00 53.48 ? 109  ASP G O   1 
ATOM   7448  C  CB  . ASP G  1 110 ? 148.125 -4.435  0.121  1.00 58.98 ? 109  ASP G CB  1 
ATOM   7449  C  CG  . ASP G  1 110 ? 147.707 -3.594  -1.078 1.00 63.15 ? 109  ASP G CG  1 
ATOM   7450  O  OD1 . ASP G  1 110 ? 147.539 -4.168  -2.178 1.00 65.63 ? 109  ASP G OD1 1 
ATOM   7451  O  OD2 . ASP G  1 110 ? 147.542 -2.363  -0.923 1.00 63.80 ? 109  ASP G OD2 1 
ATOM   7452  N  N   . HIS G  1 111 ? 149.629 -4.771  3.069  1.00 50.67 ? 110  HIS G N   1 
ATOM   7453  C  CA  . HIS G  1 111 ? 149.838 -5.636  4.226  1.00 48.81 ? 110  HIS G CA  1 
ATOM   7454  C  C   . HIS G  1 111 ? 150.056 -4.840  5.509  1.00 46.52 ? 110  HIS G C   1 
ATOM   7455  O  O   . HIS G  1 111 ? 150.519 -5.384  6.515  1.00 45.96 ? 110  HIS G O   1 
ATOM   7456  C  CB  . HIS G  1 111 ? 151.032 -6.567  4.002  1.00 49.20 ? 110  HIS G CB  1 
ATOM   7457  C  CG  . HIS G  1 111 ? 150.758 -7.685  3.044  1.00 51.54 ? 110  HIS G CG  1 
ATOM   7458  N  ND1 . HIS G  1 111 ? 151.637 -8.730  2.852  1.00 52.70 ? 110  HIS G ND1 1 
ATOM   7459  C  CD2 . HIS G  1 111 ? 149.710 -7.921  2.220  1.00 52.35 ? 110  HIS G CD2 1 
ATOM   7460  C  CE1 . HIS G  1 111 ? 151.143 -9.560  1.952  1.00 51.97 ? 110  HIS G CE1 1 
ATOM   7461  N  NE2 . HIS G  1 111 ? 149.973 -9.090  1.551  1.00 52.51 ? 110  HIS G NE2 1 
ATOM   7462  N  N   . SER G  1 112 ? 149.723 -3.553  5.474  1.00 43.85 ? 111  SER G N   1 
ATOM   7463  C  CA  . SER G  1 112 ? 149.890 -2.705  6.650  1.00 42.11 ? 111  SER G CA  1 
ATOM   7464  C  C   . SER G  1 112 ? 148.961 -3.131  7.783  1.00 40.44 ? 111  SER G C   1 
ATOM   7465  O  O   . SER G  1 112 ? 147.781 -3.411  7.561  1.00 39.11 ? 111  SER G O   1 
ATOM   7466  C  CB  . SER G  1 112 ? 149.614 -1.243  6.301  1.00 40.74 ? 111  SER G CB  1 
ATOM   7467  O  OG  . SER G  1 112 ? 149.715 -0.435  7.461  1.00 37.57 ? 111  SER G OG  1 
ATOM   7468  N  N   . ILE G  1 113 ? 149.502 -3.173  8.997  1.00 40.35 ? 112  ILE G N   1 
ATOM   7469  C  CA  . ILE G  1 113 ? 148.724 -3.555  10.170 1.00 38.86 ? 112  ILE G CA  1 
ATOM   7470  C  C   . ILE G  1 113 ? 148.294 -2.320  10.965 1.00 38.83 ? 112  ILE G C   1 
ATOM   7471  O  O   . ILE G  1 113 ? 147.640 -2.428  12.010 1.00 37.61 ? 112  ILE G O   1 
ATOM   7472  C  CB  . ILE G  1 113 ? 149.529 -4.501  11.080 1.00 39.61 ? 112  ILE G CB  1 
ATOM   7473  C  CG1 . ILE G  1 113 ? 150.833 -3.830  11.516 1.00 37.89 ? 112  ILE G CG1 1 
ATOM   7474  C  CG2 . ILE G  1 113 ? 149.825 -5.799  10.336 1.00 38.45 ? 112  ILE G CG2 1 
ATOM   7475  C  CD1 . ILE G  1 113 ? 151.696 -4.704  12.406 1.00 39.37 ? 112  ILE G CD1 1 
ATOM   7476  N  N   . ILE G  1 114 ? 148.670 -1.146  10.459 1.00 37.26 ? 113  ILE G N   1 
ATOM   7477  C  CA  . ILE G  1 114 ? 148.309 0.118   11.091 1.00 34.75 ? 113  ILE G CA  1 
ATOM   7478  C  C   . ILE G  1 114 ? 146.785 0.216   11.100 1.00 34.41 ? 113  ILE G C   1 
ATOM   7479  O  O   . ILE G  1 114 ? 146.137 -0.009  10.078 1.00 33.19 ? 113  ILE G O   1 
ATOM   7480  C  CB  . ILE G  1 114 ? 148.866 1.327   10.294 1.00 36.03 ? 113  ILE G CB  1 
ATOM   7481  C  CG1 . ILE G  1 114 ? 150.399 1.266   10.229 1.00 34.52 ? 113  ILE G CG1 1 
ATOM   7482  C  CG2 . ILE G  1 114 ? 148.397 2.630   10.932 1.00 35.27 ? 113  ILE G CG2 1 
ATOM   7483  C  CD1 . ILE G  1 114 ? 151.083 1.345   11.579 1.00 35.07 ? 113  ILE G CD1 1 
ATOM   7484  N  N   . GLY G  1 115 ? 146.208 0.539   12.251 1.00 33.78 ? 114  GLY G N   1 
ATOM   7485  C  CA  . GLY G  1 115 ? 144.760 0.657   12.314 1.00 33.76 ? 114  GLY G CA  1 
ATOM   7486  C  C   . GLY G  1 115 ? 144.022 -0.655  12.516 1.00 32.06 ? 114  GLY G C   1 
ATOM   7487  O  O   . GLY G  1 115 ? 142.791 -0.684  12.516 1.00 31.20 ? 114  GLY G O   1 
ATOM   7488  N  N   . ARG G  1 116 ? 144.764 -1.745  12.672 1.00 31.87 ? 115  ARG G N   1 
ATOM   7489  C  CA  . ARG G  1 116 ? 144.154 -3.051  12.904 1.00 32.27 ? 115  ARG G CA  1 
ATOM   7490  C  C   . ARG G  1 116 ? 144.373 -3.371  14.382 1.00 32.12 ? 115  ARG G C   1 
ATOM   7491  O  O   . ARG G  1 116 ? 144.911 -2.537  15.104 1.00 32.12 ? 115  ARG G O   1 
ATOM   7492  C  CB  . ARG G  1 116 ? 144.777 -4.100  11.970 1.00 32.88 ? 115  ARG G CB  1 
ATOM   7493  C  CG  . ARG G  1 116 ? 144.446 -3.801  10.496 1.00 32.97 ? 115  ARG G CG  1 
ATOM   7494  C  CD  . ARG G  1 116 ? 145.109 -4.731  9.495  1.00 34.91 ? 115  ARG G CD  1 
ATOM   7495  N  NE  . ARG G  1 116 ? 144.955 -4.231  8.125  1.00 35.69 ? 115  ARG G NE  1 
ATOM   7496  C  CZ  . ARG G  1 116 ? 143.798 -4.153  7.468  1.00 35.60 ? 115  ARG G CZ  1 
ATOM   7497  N  NH1 . ARG G  1 116 ? 143.770 -3.679  6.228  1.00 36.35 ? 115  ARG G NH1 1 
ATOM   7498  N  NH2 . ARG G  1 116 ? 142.670 -4.557  8.035  1.00 30.94 ? 115  ARG G NH2 1 
ATOM   7499  N  N   . THR G  1 117 ? 143.964 -4.548  14.844 1.00 31.49 ? 116  THR G N   1 
ATOM   7500  C  CA  . THR G  1 117 ? 144.106 -4.873  16.267 1.00 32.94 ? 116  THR G CA  1 
ATOM   7501  C  C   . THR G  1 117 ? 145.050 -6.027  16.625 1.00 32.63 ? 116  THR G C   1 
ATOM   7502  O  O   . THR G  1 117 ? 144.951 -7.119  16.069 1.00 32.56 ? 116  THR G O   1 
ATOM   7503  C  CB  . THR G  1 117 ? 142.717 -5.191  16.896 1.00 33.31 ? 116  THR G CB  1 
ATOM   7504  O  OG1 . THR G  1 117 ? 141.826 -4.085  16.700 1.00 32.10 ? 116  THR G OG1 1 
ATOM   7505  C  CG2 . THR G  1 117 ? 142.853 -5.468  18.393 1.00 32.77 ? 116  THR G CG2 1 
ATOM   7506  N  N   . LEU G  1 118 ? 145.963 -5.777  17.560 1.00 32.50 ? 117  LEU G N   1 
ATOM   7507  C  CA  . LEU G  1 118 ? 146.884 -6.814  18.028 1.00 32.93 ? 117  LEU G CA  1 
ATOM   7508  C  C   . LEU G  1 118 ? 146.136 -7.533  19.151 1.00 33.68 ? 117  LEU G C   1 
ATOM   7509  O  O   . LEU G  1 118 ? 145.574 -6.885  20.040 1.00 33.68 ? 117  LEU G O   1 
ATOM   7510  C  CB  . LEU G  1 118 ? 148.178 -6.195  18.573 1.00 30.14 ? 117  LEU G CB  1 
ATOM   7511  C  CG  . LEU G  1 118 ? 149.230 -7.163  19.139 1.00 31.61 ? 117  LEU G CG  1 
ATOM   7512  C  CD1 . LEU G  1 118 ? 149.741 -8.091  18.041 1.00 30.81 ? 117  LEU G CD1 1 
ATOM   7513  C  CD2 . LEU G  1 118 ? 150.380 -6.382  19.744 1.00 30.23 ? 117  LEU G CD2 1 
ATOM   7514  N  N   . VAL G  1 119 ? 146.129 -8.862  19.111 1.00 33.83 ? 118  VAL G N   1 
ATOM   7515  C  CA  . VAL G  1 119 ? 145.418 -9.663  20.109 1.00 34.13 ? 118  VAL G CA  1 
ATOM   7516  C  C   . VAL G  1 119 ? 146.273 -10.756 20.766 1.00 36.25 ? 118  VAL G C   1 
ATOM   7517  O  O   . VAL G  1 119 ? 146.983 -11.499 20.077 1.00 34.94 ? 118  VAL G O   1 
ATOM   7518  C  CB  . VAL G  1 119 ? 144.175 -10.357 19.471 1.00 33.39 ? 118  VAL G CB  1 
ATOM   7519  C  CG1 . VAL G  1 119 ? 143.458 -11.212 20.501 1.00 31.56 ? 118  VAL G CG1 1 
ATOM   7520  C  CG2 . VAL G  1 119 ? 143.223 -9.312  18.891 1.00 32.06 ? 118  VAL G CG2 1 
ATOM   7521  N  N   . VAL G  1 120 ? 146.208 -10.838 22.095 1.00 35.18 ? 119  VAL G N   1 
ATOM   7522  C  CA  . VAL G  1 120 ? 146.930 -11.870 22.838 1.00 37.48 ? 119  VAL G CA  1 
ATOM   7523  C  C   . VAL G  1 120 ? 145.843 -12.837 23.317 1.00 39.06 ? 119  VAL G C   1 
ATOM   7524  O  O   . VAL G  1 120 ? 144.816 -12.413 23.850 1.00 38.33 ? 119  VAL G O   1 
ATOM   7525  C  CB  . VAL G  1 120 ? 147.716 -11.283 24.042 1.00 39.24 ? 119  VAL G CB  1 
ATOM   7526  C  CG1 . VAL G  1 120 ? 146.769 -10.634 25.032 1.00 40.18 ? 119  VAL G CG1 1 
ATOM   7527  C  CG2 . VAL G  1 120 ? 148.534 -12.381 24.710 1.00 39.64 ? 119  VAL G CG2 1 
ATOM   7528  N  N   . HIS G  1 121 ? 146.063 -14.131 23.115 1.00 40.10 ? 120  HIS G N   1 
ATOM   7529  C  CA  . HIS G  1 121 ? 145.067 -15.135 23.468 1.00 41.33 ? 120  HIS G CA  1 
ATOM   7530  C  C   . HIS G  1 121 ? 145.229 -15.916 24.760 1.00 42.73 ? 120  HIS G C   1 
ATOM   7531  O  O   . HIS G  1 121 ? 146.263 -15.863 25.433 1.00 41.90 ? 120  HIS G O   1 
ATOM   7532  C  CB  . HIS G  1 121 ? 144.921 -16.133 22.319 1.00 42.26 ? 120  HIS G CB  1 
ATOM   7533  C  CG  . HIS G  1 121 ? 144.197 -15.585 21.131 1.00 43.00 ? 120  HIS G CG  1 
ATOM   7534  N  ND1 . HIS G  1 121 ? 142.835 -15.711 20.969 1.00 43.74 ? 120  HIS G ND1 1 
ATOM   7535  C  CD2 . HIS G  1 121 ? 144.646 -14.907 20.050 1.00 43.83 ? 120  HIS G CD2 1 
ATOM   7536  C  CE1 . HIS G  1 121 ? 142.475 -15.138 19.831 1.00 44.47 ? 120  HIS G CE1 1 
ATOM   7537  N  NE2 . HIS G  1 121 ? 143.557 -14.644 19.257 1.00 44.20 ? 120  HIS G NE2 1 
ATOM   7538  N  N   . GLU G  1 122 ? 144.166 -16.654 25.066 1.00 44.07 ? 121  GLU G N   1 
ATOM   7539  C  CA  . GLU G  1 122 ? 144.045 -17.501 26.245 1.00 45.89 ? 121  GLU G CA  1 
ATOM   7540  C  C   . GLU G  1 122 ? 144.936 -18.736 26.154 1.00 46.61 ? 121  GLU G C   1 
ATOM   7541  O  O   . GLU G  1 122 ? 145.754 -18.991 27.037 1.00 46.19 ? 121  GLU G O   1 
ATOM   7542  C  CB  . GLU G  1 122 ? 142.589 -17.952 26.387 1.00 47.75 ? 121  GLU G CB  1 
ATOM   7543  C  CG  . GLU G  1 122 ? 142.338 -18.947 27.507 1.00 51.49 ? 121  GLU G CG  1 
ATOM   7544  C  CD  . GLU G  1 122 ? 141.025 -19.696 27.339 1.00 54.13 ? 121  GLU G CD  1 
ATOM   7545  O  OE1 . GLU G  1 122 ? 140.650 -20.453 28.260 1.00 55.14 ? 121  GLU G OE1 1 
ATOM   7546  O  OE2 . GLU G  1 122 ? 140.374 -19.536 26.283 1.00 54.00 ? 121  GLU G OE2 1 
ATOM   7547  N  N   . LYS G  1 123 ? 144.755 -19.506 25.085 1.00 46.70 ? 122  LYS G N   1 
ATOM   7548  C  CA  . LYS G  1 123 ? 145.519 -20.727 24.874 1.00 49.07 ? 122  LYS G CA  1 
ATOM   7549  C  C   . LYS G  1 123 ? 146.663 -20.552 23.883 1.00 50.22 ? 122  LYS G C   1 
ATOM   7550  O  O   . LYS G  1 123 ? 146.870 -19.473 23.325 1.00 48.80 ? 122  LYS G O   1 
ATOM   7551  C  CB  . LYS G  1 123 ? 144.600 -21.848 24.380 1.00 48.99 ? 122  LYS G CB  1 
ATOM   7552  C  CG  . LYS G  1 123 ? 143.616 -22.355 25.418 1.00 51.32 ? 122  LYS G CG  1 
ATOM   7553  C  CD  . LYS G  1 123 ? 142.838 -23.570 24.913 1.00 51.40 ? 122  LYS G CD  1 
ATOM   7554  C  CE  . LYS G  1 123 ? 141.845 -23.199 23.827 0.00 51.35 ? 122  LYS G CE  1 
ATOM   7555  N  NZ  . LYS G  1 123 ? 141.097 -24.390 23.338 0.00 51.36 ? 122  LYS G NZ  1 
ATOM   7556  N  N   . ALA G  1 124 ? 147.408 -21.632 23.673 1.00 50.55 ? 123  ALA G N   1 
ATOM   7557  C  CA  . ALA G  1 124 ? 148.523 -21.613 22.740 1.00 50.80 ? 123  ALA G CA  1 
ATOM   7558  C  C   . ALA G  1 124 ? 147.977 -21.816 21.337 1.00 50.47 ? 123  ALA G C   1 
ATOM   7559  O  O   . ALA G  1 124 ? 146.954 -22.474 21.144 1.00 49.42 ? 123  ALA G O   1 
ATOM   7560  C  CB  . ALA G  1 124 ? 149.517 -22.718 23.082 1.00 51.79 ? 123  ALA G CB  1 
ATOM   7561  N  N   . ASP G  1 125 ? 148.656 -21.227 20.363 1.00 50.56 ? 124  ASP G N   1 
ATOM   7562  C  CA  . ASP G  1 125 ? 148.261 -21.348 18.970 1.00 51.56 ? 124  ASP G CA  1 
ATOM   7563  C  C   . ASP G  1 125 ? 148.939 -22.606 18.422 1.00 51.71 ? 124  ASP G C   1 
ATOM   7564  O  O   . ASP G  1 125 ? 150.161 -22.727 18.476 1.00 50.13 ? 124  ASP G O   1 
ATOM   7565  C  CB  . ASP G  1 125 ? 148.727 -20.106 18.205 1.00 52.84 ? 124  ASP G CB  1 
ATOM   7566  C  CG  . ASP G  1 125 ? 148.305 -20.113 16.752 1.00 53.86 ? 124  ASP G CG  1 
ATOM   7567  O  OD1 . ASP G  1 125 ? 148.523 -19.084 16.077 1.00 54.00 ? 124  ASP G OD1 1 
ATOM   7568  O  OD2 . ASP G  1 125 ? 147.761 -21.137 16.285 1.00 54.70 ? 124  ASP G OD2 1 
ATOM   7569  N  N   . ASP G  1 126 ? 148.149 -23.544 17.908 1.00 53.09 ? 125  ASP G N   1 
ATOM   7570  C  CA  . ASP G  1 126 ? 148.711 -24.779 17.370 1.00 54.78 ? 125  ASP G CA  1 
ATOM   7571  C  C   . ASP G  1 126 ? 149.280 -24.566 15.968 1.00 55.52 ? 125  ASP G C   1 
ATOM   7572  O  O   . ASP G  1 126 ? 149.501 -25.517 15.216 1.00 55.52 ? 125  ASP G O   1 
ATOM   7573  C  CB  . ASP G  1 126 ? 147.654 -25.891 17.366 1.00 53.60 ? 125  ASP G CB  1 
ATOM   7574  C  CG  . ASP G  1 126 ? 146.508 -25.615 16.416 1.00 53.23 ? 125  ASP G CG  1 
ATOM   7575  O  OD1 . ASP G  1 126 ? 145.470 -26.300 16.536 1.00 53.32 ? 125  ASP G OD1 1 
ATOM   7576  O  OD2 . ASP G  1 126 ? 146.642 -24.729 15.546 1.00 52.69 ? 125  ASP G OD2 1 
ATOM   7577  N  N   . LEU G  1 127 ? 149.511 -23.299 15.634 1.00 55.80 ? 126  LEU G N   1 
ATOM   7578  C  CA  . LEU G  1 127 ? 150.070 -22.898 14.347 1.00 55.61 ? 126  LEU G CA  1 
ATOM   7579  C  C   . LEU G  1 127 ? 149.353 -23.485 13.133 1.00 55.55 ? 126  LEU G C   1 
ATOM   7580  O  O   . LEU G  1 127 ? 149.949 -23.639 12.066 1.00 55.30 ? 126  LEU G O   1 
ATOM   7581  C  CB  . LEU G  1 127 ? 151.558 -23.257 14.299 1.00 55.61 ? 126  LEU G CB  1 
ATOM   7582  C  CG  . LEU G  1 127 ? 152.362 -22.767 15.509 1.00 55.84 ? 126  LEU G CG  1 
ATOM   7583  C  CD1 . LEU G  1 127 ? 153.828 -23.121 15.326 1.00 55.84 ? 126  LEU G CD1 1 
ATOM   7584  C  CD2 . LEU G  1 127 ? 152.192 -21.260 15.670 1.00 56.04 ? 126  LEU G CD2 1 
ATOM   7585  N  N   . GLY G  1 128 ? 148.076 -23.809 13.300 1.00 55.25 ? 127  GLY G N   1 
ATOM   7586  C  CA  . GLY G  1 128 ? 147.293 -24.350 12.202 1.00 56.22 ? 127  GLY G CA  1 
ATOM   7587  C  C   . GLY G  1 128 ? 147.607 -25.775 11.788 1.00 57.27 ? 127  GLY G C   1 
ATOM   7588  O  O   . GLY G  1 128 ? 147.389 -26.145 10.635 1.00 56.88 ? 127  GLY G O   1 
ATOM   7589  N  N   . LYS G  1 129 ? 148.109 -26.580 12.720 1.00 58.48 ? 128  LYS G N   1 
ATOM   7590  C  CA  . LYS G  1 129 ? 148.445 -27.972 12.427 1.00 59.67 ? 128  LYS G CA  1 
ATOM   7591  C  C   . LYS G  1 129 ? 147.605 -28.911 13.292 1.00 60.63 ? 128  LYS G C   1 
ATOM   7592  O  O   . LYS G  1 129 ? 147.952 -30.079 13.474 1.00 60.66 ? 128  LYS G O   1 
ATOM   7593  C  CB  . LYS G  1 129 ? 149.928 -28.228 12.706 1.00 59.26 ? 128  LYS G CB  1 
ATOM   7594  C  CG  . LYS G  1 129 ? 150.865 -27.128 12.230 1.00 58.98 ? 128  LYS G CG  1 
ATOM   7595  C  CD  . LYS G  1 129 ? 150.761 -26.890 10.733 1.00 59.79 ? 128  LYS G CD  1 
ATOM   7596  C  CE  . LYS G  1 129 ? 151.731 -25.802 10.287 1.00 59.91 ? 128  LYS G CE  1 
ATOM   7597  N  NZ  . LYS G  1 129 ? 151.635 -25.539 8.825  1.00 60.49 ? 128  LYS G NZ  1 
ATOM   7598  N  N   . GLY G  1 130 ? 146.500 -28.392 13.819 1.00 61.42 ? 129  GLY G N   1 
ATOM   7599  C  CA  . GLY G  1 130 ? 145.633 -29.181 14.679 1.00 62.81 ? 129  GLY G CA  1 
ATOM   7600  C  C   . GLY G  1 130 ? 144.964 -30.384 14.038 1.00 63.27 ? 129  GLY G C   1 
ATOM   7601  O  O   . GLY G  1 130 ? 144.646 -31.357 14.722 1.00 63.31 ? 129  GLY G O   1 
ATOM   7602  N  N   . GLY G  1 131 ? 144.740 -30.323 12.730 1.00 63.44 ? 130  GLY G N   1 
ATOM   7603  C  CA  . GLY G  1 131 ? 144.100 -31.432 12.048 1.00 64.16 ? 130  GLY G CA  1 
ATOM   7604  C  C   . GLY G  1 131 ? 142.601 -31.218 11.952 1.00 64.80 ? 130  GLY G C   1 
ATOM   7605  O  O   . GLY G  1 131 ? 141.894 -31.972 11.275 1.00 65.01 ? 130  GLY G O   1 
ATOM   7606  N  N   . ASN G  1 132 ? 142.111 -30.191 12.643 1.00 64.99 ? 131  ASN G N   1 
ATOM   7607  C  CA  . ASN G  1 132 ? 140.691 -29.863 12.613 1.00 65.06 ? 131  ASN G CA  1 
ATOM   7608  C  C   . ASN G  1 132 ? 140.484 -28.531 11.913 1.00 64.72 ? 131  ASN G C   1 
ATOM   7609  O  O   . ASN G  1 132 ? 141.388 -27.696 11.867 1.00 64.68 ? 131  ASN G O   1 
ATOM   7610  C  CB  . ASN G  1 132 ? 140.116 -29.811 14.028 1.00 65.32 ? 131  ASN G CB  1 
ATOM   7611  C  CG  . ASN G  1 132 ? 140.798 -28.794 14.891 1.00 66.44 ? 131  ASN G CG  1 
ATOM   7612  O  OD1 . ASN G  1 132 ? 140.686 -27.585 14.671 1.00 66.39 ? 131  ASN G OD1 1 
ATOM   7613  N  ND2 . ASN G  1 132 ? 141.527 -29.276 15.882 1.00 66.74 ? 131  ASN G ND2 1 
ATOM   7614  N  N   . GLU G  1 133 ? 139.293 -28.356 11.365 1.00 64.20 ? 132  GLU G N   1 
ATOM   7615  C  CA  . GLU G  1 133 ? 138.965 -27.138 10.650 1.00 63.72 ? 132  GLU G CA  1 
ATOM   7616  C  C   . GLU G  1 133 ? 139.131 -25.858 11.435 1.00 63.20 ? 132  GLU G C   1 
ATOM   7617  O  O   . GLU G  1 133 ? 139.386 -24.812 10.872 1.00 62.76 ? 132  GLU G O   1 
ATOM   7618  C  CB  . GLU G  1 133 ? 137.540 -27.205 10.135 1.00 63.33 ? 132  GLU G CB  1 
ATOM   7619  C  CG  . GLU G  1 133 ? 137.191 -26.000 9.326  1.00 63.11 ? 132  GLU G CG  1 
ATOM   7620  C  CD  . GLU G  1 133 ? 135.792 -26.056 8.812  0.00 62.62 ? 132  GLU G CD  1 
ATOM   7621  O  OE1 . GLU G  1 133 ? 135.047 -26.965 9.228  0.00 62.44 ? 132  GLU G OE1 1 
ATOM   7622  O  OE2 . GLU G  1 133 ? 135.437 -25.185 7.996  0.00 62.44 ? 132  GLU G OE2 1 
ATOM   7623  N  N   . GLU G  1 134 ? 138.982 -25.939 12.746 1.00 62.61 ? 133  GLU G N   1 
ATOM   7624  C  CA  . GLU G  1 134 ? 139.103 -24.754 13.572 1.00 62.39 ? 133  GLU G CA  1 
ATOM   7625  C  C   . GLU G  1 134 ? 140.563 -24.316 13.653 1.00 61.73 ? 133  GLU G C   1 
ATOM   7626  O  O   . GLU G  1 134 ? 140.859 -23.121 13.710 1.00 61.79 ? 133  GLU G O   1 
ATOM   7627  C  CB  . GLU G  1 134 ? 138.507 -25.018 14.964 1.00 62.62 ? 133  GLU G CB  1 
ATOM   7628  C  CG  . GLU G  1 134 ? 138.596 -23.836 15.868 1.00 63.00 ? 133  GLU G CG  1 
ATOM   7629  C  CD  . GLU G  1 134 ? 137.752 -22.673 15.411 1.00 63.58 ? 133  GLU G CD  1 
ATOM   7630  O  OE1 . GLU G  1 134 ? 137.604 -21.753 16.232 1.00 62.54 ? 133  GLU G OE1 1 
ATOM   7631  O  OE2 . GLU G  1 134 ? 137.247 -22.663 14.263 1.00 63.73 ? 133  GLU G OE2 1 
ATOM   7632  N  N   . SER G  1 135 ? 141.473 -25.282 13.573 1.00 60.64 ? 134  SER G N   1 
ATOM   7633  C  CA  . SER G  1 135 ? 142.903 -25.000 13.636 1.00 59.31 ? 134  SER G CA  1 
ATOM   7634  C  C   . SER G  1 135 ? 143.399 -24.192 12.437 1.00 58.28 ? 134  SER G C   1 
ATOM   7635  O  O   . SER G  1 135 ? 144.357 -23.424 12.553 1.00 58.06 ? 134  SER G O   1 
ATOM   7636  C  CB  . SER G  1 135 ? 143.687 -26.312 13.738 1.00 58.65 ? 134  SER G CB  1 
ATOM   7637  O  OG  . SER G  1 135 ? 145.078 -26.078 13.878 1.00 56.84 ? 134  SER G OG  1 
ATOM   7638  N  N   . THR G  1 136 ? 142.736 -24.354 11.297 1.00 57.67 ? 135  THR G N   1 
ATOM   7639  C  CA  . THR G  1 136 ? 143.125 -23.648 10.084 1.00 57.24 ? 135  THR G CA  1 
ATOM   7640  C  C   . THR G  1 136 ? 142.496 -22.263 9.995  1.00 57.06 ? 135  THR G C   1 
ATOM   7641  O  O   . THR G  1 136 ? 142.564 -21.611 8.952  1.00 55.94 ? 135  THR G O   1 
ATOM   7642  C  CB  . THR G  1 136 ? 142.722 -24.437 8.829  1.00 57.68 ? 135  THR G CB  1 
ATOM   7643  O  OG1 . THR G  1 136 ? 141.294 -24.458 8.717  1.00 58.16 ? 135  THR G OG1 1 
ATOM   7644  C  CG2 . THR G  1 136 ? 143.244 -25.868 8.910  1.00 57.75 ? 135  THR G CG2 1 
ATOM   7645  N  N   . LYS G  1 137 ? 141.881 -21.818 11.086 1.00 56.76 ? 136  LYS G N   1 
ATOM   7646  C  CA  . LYS G  1 137 ? 141.256 -20.503 11.110 1.00 56.74 ? 136  LYS G CA  1 
ATOM   7647  C  C   . LYS G  1 137 ? 141.728 -19.677 12.300 1.00 56.39 ? 136  LYS G C   1 
ATOM   7648  O  O   . LYS G  1 137 ? 142.143 -18.527 12.141 1.00 56.48 ? 136  LYS G O   1 
ATOM   7649  C  CB  . LYS G  1 137 ? 139.732 -20.648 11.119 1.00 57.48 ? 136  LYS G CB  1 
ATOM   7650  C  CG  . LYS G  1 137 ? 139.193 -21.240 9.822  1.00 58.12 ? 136  LYS G CG  1 
ATOM   7651  C  CD  . LYS G  1 137 ? 137.676 -21.252 9.770  1.00 58.93 ? 136  LYS G CD  1 
ATOM   7652  C  CE  . LYS G  1 137 ? 137.199 -21.742 8.410  1.00 58.56 ? 136  LYS G CE  1 
ATOM   7653  N  NZ  . LYS G  1 137 ? 135.716 -21.788 8.309  1.00 59.37 ? 136  LYS G NZ  1 
ATOM   7654  N  N   . THR G  1 138 ? 141.686 -20.271 13.488 1.00 55.67 ? 137  THR G N   1 
ATOM   7655  C  CA  . THR G  1 138 ? 142.115 -19.578 14.698 1.00 55.08 ? 137  THR G CA  1 
ATOM   7656  C  C   . THR G  1 138 ? 143.292 -20.293 15.353 1.00 54.64 ? 137  THR G C   1 
ATOM   7657  O  O   . THR G  1 138 ? 144.005 -19.713 16.175 1.00 54.22 ? 137  THR G O   1 
ATOM   7658  C  CB  . THR G  1 138 ? 140.975 -19.498 15.734 1.00 55.23 ? 137  THR G CB  1 
ATOM   7659  O  OG1 . THR G  1 138 ? 140.741 -20.798 16.293 1.00 54.73 ? 137  THR G OG1 1 
ATOM   7660  C  CG2 . THR G  1 138 ? 139.700 -18.996 15.077 1.00 54.60 ? 137  THR G CG2 1 
ATOM   7661  N  N   . GLY G  1 139 ? 143.495 -21.553 14.980 1.00 53.39 ? 138  GLY G N   1 
ATOM   7662  C  CA  . GLY G  1 139 ? 144.574 -22.321 15.568 1.00 52.08 ? 138  GLY G CA  1 
ATOM   7663  C  C   . GLY G  1 139 ? 144.204 -22.719 16.985 1.00 50.68 ? 138  GLY G C   1 
ATOM   7664  O  O   . GLY G  1 139 ? 145.071 -23.021 17.803 1.00 50.35 ? 138  GLY G O   1 
ATOM   7665  N  N   . ASN G  1 140 ? 142.904 -22.709 17.272 1.00 50.48 ? 139  ASN G N   1 
ATOM   7666  C  CA  . ASN G  1 140 ? 142.390 -23.068 18.591 1.00 49.25 ? 139  ASN G CA  1 
ATOM   7667  C  C   . ASN G  1 140 ? 143.115 -22.304 19.702 1.00 47.40 ? 139  ASN G C   1 
ATOM   7668  O  O   . ASN G  1 140 ? 143.410 -22.858 20.762 1.00 46.86 ? 139  ASN G O   1 
ATOM   7669  C  CB  . ASN G  1 140 ? 142.534 -24.580 18.813 1.00 50.86 ? 139  ASN G CB  1 
ATOM   7670  C  CG  . ASN G  1 140 ? 141.869 -25.397 17.718 1.00 52.84 ? 139  ASN G CG  1 
ATOM   7671  O  OD1 . ASN G  1 140 ? 140.657 -25.305 17.505 1.00 52.69 ? 139  ASN G OD1 1 
ATOM   7672  N  ND2 . ASN G  1 140 ? 142.661 -26.201 17.015 1.00 52.98 ? 139  ASN G ND2 1 
ATOM   7673  N  N   . ALA G  1 141 ? 143.389 -21.025 19.458 1.00 45.26 ? 140  ALA G N   1 
ATOM   7674  C  CA  . ALA G  1 141 ? 144.088 -20.188 20.428 1.00 43.38 ? 140  ALA G CA  1 
ATOM   7675  C  C   . ALA G  1 141 ? 143.215 -19.794 21.622 1.00 42.39 ? 140  ALA G C   1 
ATOM   7676  O  O   . ALA G  1 141 ? 143.715 -19.267 22.616 1.00 42.20 ? 140  ALA G O   1 
ATOM   7677  C  CB  . ALA G  1 141 ? 144.624 -18.942 19.739 1.00 43.03 ? 140  ALA G CB  1 
ATOM   7678  N  N   . GLY G  1 142 ? 141.914 -20.040 21.524 1.00 42.55 ? 141  GLY G N   1 
ATOM   7679  C  CA  . GLY G  1 142 ? 141.026 -19.707 22.625 1.00 42.88 ? 141  GLY G CA  1 
ATOM   7680  C  C   . GLY G  1 142 ? 140.485 -18.288 22.615 1.00 42.56 ? 141  GLY G C   1 
ATOM   7681  O  O   . GLY G  1 142 ? 140.450 -17.634 21.573 1.00 41.77 ? 141  GLY G O   1 
ATOM   7682  N  N   . SER G  1 143 ? 140.074 -17.808 23.787 1.00 42.64 ? 142  SER G N   1 
ATOM   7683  C  CA  . SER G  1 143 ? 139.510 -16.467 23.917 1.00 41.93 ? 142  SER G CA  1 
ATOM   7684  C  C   . SER G  1 143 ? 140.557 -15.362 23.830 1.00 40.73 ? 142  SER G C   1 
ATOM   7685  O  O   . SER G  1 143 ? 141.756 -15.607 23.969 1.00 40.04 ? 142  SER G O   1 
ATOM   7686  C  CB  . SER G  1 143 ? 138.746 -16.338 25.241 1.00 41.60 ? 142  SER G CB  1 
ATOM   7687  O  OG  . SER G  1 143 ? 139.633 -16.330 26.344 1.00 42.13 ? 142  SER G OG  1 
ATOM   7688  N  N   . ARG G  1 144 ? 140.079 -14.141 23.608 1.00 38.57 ? 143  ARG G N   1 
ATOM   7689  C  CA  . ARG G  1 144 ? 140.935 -12.968 23.490 1.00 35.97 ? 143  ARG G CA  1 
ATOM   7690  C  C   . ARG G  1 144 ? 141.067 -12.299 24.850 1.00 35.96 ? 143  ARG G C   1 
ATOM   7691  O  O   . ARG G  1 144 ? 140.134 -11.661 25.329 1.00 35.77 ? 143  ARG G O   1 
ATOM   7692  C  CB  . ARG G  1 144 ? 140.325 -12.017 22.456 1.00 36.40 ? 143  ARG G CB  1 
ATOM   7693  C  CG  . ARG G  1 144 ? 140.006 -12.753 21.161 1.00 36.61 ? 143  ARG G CG  1 
ATOM   7694  C  CD  . ARG G  1 144 ? 139.312 -11.923 20.097 1.00 34.82 ? 143  ARG G CD  1 
ATOM   7695  N  NE  . ARG G  1 144 ? 138.989 -12.783 18.960 1.00 35.18 ? 143  ARG G NE  1 
ATOM   7696  C  CZ  . ARG G  1 144 ? 138.505 -12.367 17.794 1.00 35.02 ? 143  ARG G CZ  1 
ATOM   7697  N  NH1 . ARG G  1 144 ? 138.251 -13.250 16.839 1.00 33.37 ? 143  ARG G NH1 1 
ATOM   7698  N  NH2 . ARG G  1 144 ? 138.279 -11.077 17.578 1.00 32.83 ? 143  ARG G NH2 1 
ATOM   7699  N  N   . LEU G  1 145 ? 142.235 -12.447 25.467 1.00 34.51 ? 144  LEU G N   1 
ATOM   7700  C  CA  . LEU G  1 145 ? 142.481 -11.884 26.788 1.00 34.80 ? 144  LEU G CA  1 
ATOM   7701  C  C   . LEU G  1 145 ? 142.715 -10.382 26.806 1.00 34.67 ? 144  LEU G C   1 
ATOM   7702  O  O   . LEU G  1 145 ? 142.263 -9.690  27.717 1.00 34.57 ? 144  LEU G O   1 
ATOM   7703  C  CB  . LEU G  1 145 ? 143.673 -12.585 27.444 1.00 35.89 ? 144  LEU G CB  1 
ATOM   7704  C  CG  . LEU G  1 145 ? 143.532 -14.094 27.671 1.00 34.96 ? 144  LEU G CG  1 
ATOM   7705  C  CD1 . LEU G  1 145 ? 144.743 -14.599 28.435 1.00 35.68 ? 144  LEU G CD1 1 
ATOM   7706  C  CD2 . LEU G  1 145 ? 142.253 -14.390 28.446 1.00 36.86 ? 144  LEU G CD2 1 
ATOM   7707  N  N   . ALA G  1 146 ? 143.436 -9.884  25.809 1.00 34.68 ? 145  ALA G N   1 
ATOM   7708  C  CA  . ALA G  1 146 ? 143.729 -8.458  25.714 1.00 33.02 ? 145  ALA G CA  1 
ATOM   7709  C  C   . ALA G  1 146 ? 144.012 -8.086  24.263 1.00 33.88 ? 145  ALA G C   1 
ATOM   7710  O  O   . ALA G  1 146 ? 144.467 -8.919  23.469 1.00 32.99 ? 145  ALA G O   1 
ATOM   7711  C  CB  . ALA G  1 146 ? 144.925 -8.108  26.588 1.00 33.34 ? 145  ALA G CB  1 
ATOM   7712  N  N   . CYS G  1 147 ? 143.738 -6.832  23.924 1.00 33.24 ? 146  CYS G N   1 
ATOM   7713  C  CA  . CYS G  1 147 ? 143.945 -6.346  22.568 1.00 32.39 ? 146  CYS G CA  1 
ATOM   7714  C  C   . CYS G  1 147 ? 144.192 -4.846  22.560 1.00 32.20 ? 146  CYS G C   1 
ATOM   7715  O  O   . CYS G  1 147 ? 144.018 -4.167  23.572 1.00 30.55 ? 146  CYS G O   1 
ATOM   7716  C  CB  . CYS G  1 147 ? 142.729 -6.681  21.699 1.00 33.04 ? 146  CYS G CB  1 
ATOM   7717  S  SG  . CYS G  1 147 ? 141.133 -6.060  22.326 1.00 37.34 ? 146  CYS G SG  1 
ATOM   7718  N  N   . GLY G  1 148 ? 144.608 -4.332  21.410 1.00 31.72 ? 147  GLY G N   1 
ATOM   7719  C  CA  . GLY G  1 148 ? 144.870 -2.911  21.300 1.00 32.54 ? 147  GLY G CA  1 
ATOM   7720  C  C   . GLY G  1 148 ? 145.015 -2.496  19.851 1.00 33.50 ? 147  GLY G C   1 
ATOM   7721  O  O   . GLY G  1 148 ? 145.615 -3.217  19.049 1.00 32.92 ? 147  GLY G O   1 
ATOM   7722  N  N   . VAL G  1 149 ? 144.451 -1.345  19.502 1.00 32.54 ? 148  VAL G N   1 
ATOM   7723  C  CA  . VAL G  1 149 ? 144.562 -0.865  18.136 1.00 31.91 ? 148  VAL G CA  1 
ATOM   7724  C  C   . VAL G  1 149 ? 146.006 -0.422  17.919 1.00 31.11 ? 148  VAL G C   1 
ATOM   7725  O  O   . VAL G  1 149 ? 146.595 0.263   18.755 1.00 29.68 ? 148  VAL G O   1 
ATOM   7726  C  CB  . VAL G  1 149 ? 143.592 0.313   17.868 1.00 32.72 ? 148  VAL G CB  1 
ATOM   7727  C  CG1 . VAL G  1 149 ? 143.738 0.790   16.431 1.00 31.73 ? 148  VAL G CG1 1 
ATOM   7728  C  CG2 . VAL G  1 149 ? 142.146 -0.135  18.121 1.00 31.86 ? 148  VAL G CG2 1 
ATOM   7729  N  N   . ILE G  1 150 ? 146.581 -0.845  16.802 1.00 31.63 ? 149  ILE G N   1 
ATOM   7730  C  CA  . ILE G  1 150 ? 147.955 -0.503  16.475 1.00 30.52 ? 149  ILE G CA  1 
ATOM   7731  C  C   . ILE G  1 150 ? 147.980 0.899   15.887 1.00 30.40 ? 149  ILE G C   1 
ATOM   7732  O  O   . ILE G  1 150 ? 147.342 1.162   14.867 1.00 29.80 ? 149  ILE G O   1 
ATOM   7733  C  CB  . ILE G  1 150 ? 148.528 -1.502  15.454 1.00 32.25 ? 149  ILE G CB  1 
ATOM   7734  C  CG1 . ILE G  1 150 ? 148.514 -2.912  16.053 1.00 34.04 ? 149  ILE G CG1 1 
ATOM   7735  C  CG2 . ILE G  1 150 ? 149.937 -1.091  15.057 1.00 31.89 ? 149  ILE G CG2 1 
ATOM   7736  C  CD1 . ILE G  1 150 ? 148.941 -4.011  15.085 1.00 38.11 ? 149  ILE G CD1 1 
ATOM   7737  N  N   . GLY G  1 151 ? 148.715 1.796   16.534 1.00 29.89 ? 150  GLY G N   1 
ATOM   7738  C  CA  . GLY G  1 151 ? 148.787 3.160   16.053 1.00 31.39 ? 150  GLY G CA  1 
ATOM   7739  C  C   . GLY G  1 151 ? 150.159 3.587   15.571 1.00 32.19 ? 150  GLY G C   1 
ATOM   7740  O  O   . GLY G  1 151 ? 151.180 3.031   15.977 1.00 30.52 ? 150  GLY G O   1 
ATOM   7741  N  N   . ILE G  1 152 ? 150.177 4.579   14.688 1.00 32.21 ? 151  ILE G N   1 
ATOM   7742  C  CA  . ILE G  1 152 ? 151.424 5.113   14.157 1.00 33.66 ? 151  ILE G CA  1 
ATOM   7743  C  C   . ILE G  1 152 ? 152.170 5.748   15.321 1.00 33.31 ? 151  ILE G C   1 
ATOM   7744  O  O   . ILE G  1 152 ? 151.577 6.475   16.117 1.00 33.39 ? 151  ILE G O   1 
ATOM   7745  C  CB  . ILE G  1 152 ? 151.152 6.191   13.084 1.00 34.26 ? 151  ILE G CB  1 
ATOM   7746  C  CG1 . ILE G  1 152 ? 150.347 5.584   11.936 1.00 33.50 ? 151  ILE G CG1 1 
ATOM   7747  C  CG2 . ILE G  1 152 ? 152.465 6.766   12.569 1.00 35.13 ? 151  ILE G CG2 1 
ATOM   7748  C  CD1 . ILE G  1 152 ? 149.907 6.599   10.895 1.00 36.13 ? 151  ILE G CD1 1 
ATOM   7749  N  N   . ALA G  1 153 ? 153.463 5.470   15.431 1.00 35.14 ? 152  ALA G N   1 
ATOM   7750  C  CA  . ALA G  1 153 ? 154.257 6.026   16.521 1.00 36.22 ? 152  ALA G CA  1 
ATOM   7751  C  C   . ALA G  1 153 ? 155.367 6.937   16.005 1.00 38.61 ? 152  ALA G C   1 
ATOM   7752  O  O   . ALA G  1 153 ? 155.797 6.822   14.859 1.00 36.31 ? 152  ALA G O   1 
ATOM   7753  C  CB  . ALA G  1 153 ? 154.854 4.895   17.361 1.00 37.12 ? 152  ALA G CB  1 
ATOM   7754  N  N   . GLN G  1 154 ? 155.823 7.841   16.867 1.00 40.73 ? 153  GLN G N   1 
ATOM   7755  C  CA  . GLN G  1 154 ? 156.884 8.779   16.518 1.00 45.24 ? 153  GLN G CA  1 
ATOM   7756  C  C   . GLN G  1 154 ? 158.225 8.071   16.322 1.00 47.05 ? 153  GLN G C   1 
ATOM   7757  O  O   . GLN G  1 154 ? 158.731 7.466   17.292 1.00 47.56 ? 153  GLN G O   1 
ATOM   7758  C  CB  . GLN G  1 154 ? 157.003 9.847   17.608 1.00 46.64 ? 153  GLN G CB  1 
ATOM   7759  C  CG  . GLN G  1 154 ? 158.238 10.728  17.506 1.00 50.51 ? 153  GLN G CG  1 
ATOM   7760  C  CD  . GLN G  1 154 ? 158.195 11.893  18.478 1.00 51.93 ? 153  GLN G CD  1 
ATOM   7761  O  OE1 . GLN G  1 154 ? 157.531 12.902  18.229 1.00 53.12 ? 153  GLN G OE1 1 
ATOM   7762  N  NE2 . GLN G  1 154 ? 158.889 11.752  19.600 1.00 52.00 ? 153  GLN G NE2 1 
ATOM   7763  O  OXT . GLN G  1 154 ? 158.752 8.125   15.191 1.00 48.75 ? 153  GLN G OXT 1 
ATOM   7764  N  N   . ALA H  1 2   ? 140.566 2.418   3.802  1.00 43.74 ? 1    ALA H N   1 
ATOM   7765  C  CA  . ALA H  1 2   ? 139.323 1.834   4.384  1.00 43.96 ? 1    ALA H CA  1 
ATOM   7766  C  C   . ALA H  1 2   ? 138.121 2.724   4.082  1.00 43.28 ? 1    ALA H C   1 
ATOM   7767  O  O   . ALA H  1 2   ? 138.280 3.902   3.757  1.00 43.13 ? 1    ALA H O   1 
ATOM   7768  C  CB  . ALA H  1 2   ? 139.486 1.670   5.898  1.00 45.21 ? 1    ALA H CB  1 
ATOM   7769  N  N   . THR H  1 3   ? 136.922 2.156   4.181  1.00 41.91 ? 2    THR H N   1 
ATOM   7770  C  CA  . THR H  1 3   ? 135.705 2.915   3.927  1.00 40.22 ? 2    THR H CA  1 
ATOM   7771  C  C   . THR H  1 3   ? 134.999 3.257   5.236  1.00 38.31 ? 2    THR H C   1 
ATOM   7772  O  O   . THR H  1 3   ? 134.083 4.077   5.253  1.00 37.47 ? 2    THR H O   1 
ATOM   7773  C  CB  . THR H  1 3   ? 134.723 2.140   3.017  1.00 42.55 ? 2    THR H CB  1 
ATOM   7774  O  OG1 . THR H  1 3   ? 134.276 0.953   3.684  1.00 44.02 ? 2    THR H OG1 1 
ATOM   7775  C  CG2 . THR H  1 3   ? 135.402 1.762   1.704  1.00 42.68 ? 2    THR H CG2 1 
ATOM   7776  N  N   . LYS H  1 4   ? 135.427 2.618   6.325  1.00 36.27 ? 3    LYS H N   1 
ATOM   7777  C  CA  . LYS H  1 4   ? 134.859 2.862   7.651  1.00 33.86 ? 3    LYS H CA  1 
ATOM   7778  C  C   . LYS H  1 4   ? 135.925 2.729   8.731  1.00 32.84 ? 3    LYS H C   1 
ATOM   7779  O  O   . LYS H  1 4   ? 136.812 1.881   8.643  1.00 31.85 ? 3    LYS H O   1 
ATOM   7780  C  CB  . LYS H  1 4   ? 133.726 1.879   7.954  1.00 36.17 ? 3    LYS H CB  1 
ATOM   7781  C  CG  . LYS H  1 4   ? 132.448 2.138   7.185  1.00 39.72 ? 3    LYS H CG  1 
ATOM   7782  C  CD  . LYS H  1 4   ? 131.361 1.139   7.546  1.00 40.39 ? 3    LYS H CD  1 
ATOM   7783  C  CE  . LYS H  1 4   ? 130.102 1.410   6.738  1.00 43.29 ? 3    LYS H CE  1 
ATOM   7784  N  NZ  . LYS H  1 4   ? 129.030 0.414   6.997  1.00 45.90 ? 3    LYS H NZ  1 
ATOM   7785  N  N   . ALA H  1 5   ? 135.830 3.573   9.753  1.00 30.89 ? 4    ALA H N   1 
ATOM   7786  C  CA  . ALA H  1 5   ? 136.774 3.547   10.861 1.00 29.81 ? 4    ALA H CA  1 
ATOM   7787  C  C   . ALA H  1 5   ? 136.028 3.887   12.141 1.00 27.56 ? 4    ALA H C   1 
ATOM   7788  O  O   . ALA H  1 5   ? 134.880 4.327   12.099 1.00 28.66 ? 4    ALA H O   1 
ATOM   7789  C  CB  . ALA H  1 5   ? 137.902 4.555   10.625 1.00 27.09 ? 4    ALA H CB  1 
ATOM   7790  N  N   . VAL H  1 6   ? 136.672 3.675   13.281 1.00 28.43 ? 5    VAL H N   1 
ATOM   7791  C  CA  . VAL H  1 6   ? 136.035 3.984   14.550 1.00 27.86 ? 5    VAL H CA  1 
ATOM   7792  C  C   . VAL H  1 6   ? 137.075 4.214   15.631 1.00 28.52 ? 5    VAL H C   1 
ATOM   7793  O  O   . VAL H  1 6   ? 138.188 3.694   15.562 1.00 29.14 ? 5    VAL H O   1 
ATOM   7794  C  CB  . VAL H  1 6   ? 135.072 2.852   14.992 1.00 29.21 ? 5    VAL H CB  1 
ATOM   7795  C  CG1 . VAL H  1 6   ? 135.835 1.539   15.137 1.00 27.62 ? 5    VAL H CG1 1 
ATOM   7796  C  CG2 . VAL H  1 6   ? 134.397 3.226   16.306 1.00 26.25 ? 5    VAL H CG2 1 
ATOM   7797  N  N   . ALA H  1 7   ? 136.704 5.012   16.623 1.00 28.64 ? 6    ALA H N   1 
ATOM   7798  C  CA  . ALA H  1 7   ? 137.595 5.315   17.727 1.00 30.37 ? 6    ALA H CA  1 
ATOM   7799  C  C   . ALA H  1 7   ? 136.828 5.291   19.040 1.00 28.47 ? 6    ALA H C   1 
ATOM   7800  O  O   . ALA H  1 7   ? 135.775 5.917   19.172 1.00 30.03 ? 6    ALA H O   1 
ATOM   7801  C  CB  . ALA H  1 7   ? 138.240 6.688   17.521 1.00 29.31 ? 6    ALA H CB  1 
ATOM   7802  N  N   . VAL H  1 8   ? 137.362 4.559   20.006 1.00 28.02 ? 7    VAL H N   1 
ATOM   7803  C  CA  . VAL H  1 8   ? 136.749 4.462   21.321 1.00 28.87 ? 7    VAL H CA  1 
ATOM   7804  C  C   . VAL H  1 8   ? 137.496 5.453   22.203 1.00 28.30 ? 7    VAL H C   1 
ATOM   7805  O  O   . VAL H  1 8   ? 138.677 5.275   22.469 1.00 25.97 ? 7    VAL H O   1 
ATOM   7806  C  CB  . VAL H  1 8   ? 136.898 3.033   21.897 1.00 29.82 ? 7    VAL H CB  1 
ATOM   7807  C  CG1 . VAL H  1 8   ? 136.216 2.938   23.262 1.00 28.79 ? 7    VAL H CG1 1 
ATOM   7808  C  CG2 . VAL H  1 8   ? 136.285 2.023   20.928 1.00 32.35 ? 7    VAL H CG2 1 
ATOM   7809  N  N   . LEU H  1 9   ? 136.808 6.496   22.651 1.00 29.26 ? 8    LEU H N   1 
ATOM   7810  C  CA  . LEU H  1 9   ? 137.442 7.522   23.475 1.00 31.50 ? 8    LEU H CA  1 
ATOM   7811  C  C   . LEU H  1 9   ? 137.432 7.223   24.970 1.00 32.47 ? 8    LEU H C   1 
ATOM   7812  O  O   . LEU H  1 9   ? 136.381 6.957   25.560 1.00 31.88 ? 8    LEU H O   1 
ATOM   7813  C  CB  . LEU H  1 9   ? 136.776 8.879   23.228 1.00 32.19 ? 8    LEU H CB  1 
ATOM   7814  C  CG  . LEU H  1 9   ? 136.706 9.345   21.767 1.00 34.00 ? 8    LEU H CG  1 
ATOM   7815  C  CD1 . LEU H  1 9   ? 135.996 10.694  21.689 1.00 35.26 ? 8    LEU H CD1 1 
ATOM   7816  C  CD2 . LEU H  1 9   ? 138.111 9.443   21.188 1.00 33.93 ? 8    LEU H CD2 1 
ATOM   7817  N  N   . LYS H  1 10  ? 138.617 7.278   25.569 1.00 32.92 ? 9    LYS H N   1 
ATOM   7818  C  CA  . LYS H  1 10  ? 138.789 7.041   26.996 1.00 36.41 ? 9    LYS H CA  1 
ATOM   7819  C  C   . LYS H  1 10  ? 139.823 8.027   27.520 1.00 36.38 ? 9    LYS H C   1 
ATOM   7820  O  O   . LYS H  1 10  ? 140.609 8.571   26.750 1.00 35.96 ? 9    LYS H O   1 
ATOM   7821  C  CB  . LYS H  1 10  ? 139.282 5.613   27.258 1.00 38.63 ? 9    LYS H CB  1 
ATOM   7822  C  CG  . LYS H  1 10  ? 138.338 4.523   26.788 1.00 42.63 ? 9    LYS H CG  1 
ATOM   7823  C  CD  . LYS H  1 10  ? 138.822 3.149   27.228 1.00 46.56 ? 9    LYS H CD  1 
ATOM   7824  C  CE  . LYS H  1 10  ? 137.845 2.064   26.806 0.00 47.14 ? 9    LYS H CE  1 
ATOM   7825  N  NZ  . LYS H  1 10  ? 138.285 0.711   27.242 1.00 52.12 ? 9    LYS H NZ  1 
ATOM   7826  N  N   . GLY H  1 11  ? 139.814 8.253   28.830 1.00 37.36 ? 10   GLY H N   1 
ATOM   7827  C  CA  . GLY H  1 11  ? 140.764 9.167   29.442 1.00 40.42 ? 10   GLY H CA  1 
ATOM   7828  C  C   . GLY H  1 11  ? 140.915 8.867   30.923 1.00 42.72 ? 10   GLY H C   1 
ATOM   7829  O  O   . GLY H  1 11  ? 140.641 7.750   31.362 1.00 42.87 ? 10   GLY H O   1 
ATOM   7830  N  N   . ASP H  1 12  ? 141.353 9.854   31.699 1.00 45.24 ? 11   ASP H N   1 
ATOM   7831  C  CA  . ASP H  1 12  ? 141.518 9.663   33.136 1.00 46.56 ? 11   ASP H CA  1 
ATOM   7832  C  C   . ASP H  1 12  ? 140.228 9.989   33.879 1.00 46.52 ? 11   ASP H C   1 
ATOM   7833  O  O   . ASP H  1 12  ? 139.992 9.487   34.979 1.00 48.19 ? 11   ASP H O   1 
ATOM   7834  C  CB  . ASP H  1 12  ? 142.647 10.547  33.675 1.00 49.52 ? 11   ASP H CB  1 
ATOM   7835  C  CG  . ASP H  1 12  ? 144.015 10.090  33.216 1.00 52.35 ? 11   ASP H CG  1 
ATOM   7836  O  OD1 . ASP H  1 12  ? 144.308 8.882   33.341 1.00 55.06 ? 11   ASP H OD1 1 
ATOM   7837  O  OD2 . ASP H  1 12  ? 144.799 10.936  32.737 1.00 54.01 ? 11   ASP H OD2 1 
ATOM   7838  N  N   . GLY H  1 13  ? 139.398 10.830  33.272 1.00 44.22 ? 12   GLY H N   1 
ATOM   7839  C  CA  . GLY H  1 13  ? 138.149 11.216  33.899 1.00 41.82 ? 12   GLY H CA  1 
ATOM   7840  C  C   . GLY H  1 13  ? 136.956 10.427  33.395 1.00 40.32 ? 12   GLY H C   1 
ATOM   7841  O  O   . GLY H  1 13  ? 137.110 9.315   32.896 1.00 39.06 ? 12   GLY H O   1 
ATOM   7842  N  N   . PRO H  1 14  ? 135.745 10.992  33.507 1.00 39.15 ? 13   PRO H N   1 
ATOM   7843  C  CA  . PRO H  1 14  ? 134.498 10.356  33.073 1.00 37.83 ? 13   PRO H CA  1 
ATOM   7844  C  C   . PRO H  1 14  ? 134.199 10.407  31.573 1.00 36.70 ? 13   PRO H C   1 
ATOM   7845  O  O   . PRO H  1 14  ? 133.334 9.672   31.088 1.00 36.83 ? 13   PRO H O   1 
ATOM   7846  C  CB  . PRO H  1 14  ? 133.448 11.100  33.882 1.00 38.22 ? 13   PRO H CB  1 
ATOM   7847  C  CG  . PRO H  1 14  ? 133.993 12.494  33.880 1.00 40.03 ? 13   PRO H CG  1 
ATOM   7848  C  CD  . PRO H  1 14  ? 135.466 12.271  34.188 1.00 39.51 ? 13   PRO H CD  1 
ATOM   7849  N  N   . VAL H  1 15  ? 134.910 11.258  30.837 1.00 33.40 ? 14   VAL H N   1 
ATOM   7850  C  CA  . VAL H  1 15  ? 134.662 11.380  29.404 1.00 31.35 ? 14   VAL H CA  1 
ATOM   7851  C  C   . VAL H  1 15  ? 135.006 10.106  28.640 1.00 29.66 ? 14   VAL H C   1 
ATOM   7852  O  O   . VAL H  1 15  ? 136.115 9.590   28.730 1.00 29.35 ? 14   VAL H O   1 
ATOM   7853  C  CB  . VAL H  1 15  ? 135.453 12.559  28.774 1.00 31.33 ? 14   VAL H CB  1 
ATOM   7854  C  CG1 . VAL H  1 15  ? 134.991 12.781  27.333 1.00 28.92 ? 14   VAL H CG1 1 
ATOM   7855  C  CG2 . VAL H  1 15  ? 135.246 13.825  29.590 1.00 30.98 ? 14   VAL H CG2 1 
ATOM   7856  N  N   . GLN H  1 16  ? 134.035 9.605   27.888 1.00 30.17 ? 15   GLN H N   1 
ATOM   7857  C  CA  . GLN H  1 16  ? 134.222 8.397   27.098 1.00 31.49 ? 15   GLN H CA  1 
ATOM   7858  C  C   . GLN H  1 16  ? 133.191 8.407   25.985 1.00 30.37 ? 15   GLN H C   1 
ATOM   7859  O  O   . GLN H  1 16  ? 132.153 9.065   26.092 1.00 30.94 ? 15   GLN H O   1 
ATOM   7860  C  CB  . GLN H  1 16  ? 134.040 7.150   27.974 1.00 35.86 ? 15   GLN H CB  1 
ATOM   7861  C  CG  . GLN H  1 16  ? 132.649 6.994   28.576 1.00 40.37 ? 15   GLN H CG  1 
ATOM   7862  C  CD  . GLN H  1 16  ? 132.608 5.938   29.674 1.00 45.33 ? 15   GLN H CD  1 
ATOM   7863  O  OE1 . GLN H  1 16  ? 133.026 4.799   29.473 1.00 46.97 ? 15   GLN H OE1 1 
ATOM   7864  N  NE2 . GLN H  1 16  ? 132.099 6.316   30.841 1.00 48.29 ? 15   GLN H NE2 1 
ATOM   7865  N  N   . GLY H  1 17  ? 133.469 7.681   24.913 1.00 29.48 ? 16   GLY H N   1 
ATOM   7866  C  CA  . GLY H  1 17  ? 132.522 7.663   23.818 1.00 28.98 ? 16   GLY H CA  1 
ATOM   7867  C  C   . GLY H  1 17  ? 132.996 6.837   22.648 1.00 28.57 ? 16   GLY H C   1 
ATOM   7868  O  O   . GLY H  1 17  ? 134.090 6.277   22.668 1.00 28.59 ? 16   GLY H O   1 
ATOM   7869  N  N   . ILE H  1 18  ? 132.154 6.771   21.625 1.00 27.57 ? 17   ILE H N   1 
ATOM   7870  C  CA  . ILE H  1 18  ? 132.450 6.017   20.417 1.00 28.29 ? 17   ILE H CA  1 
ATOM   7871  C  C   . ILE H  1 18  ? 132.182 6.928   19.221 1.00 27.31 ? 17   ILE H C   1 
ATOM   7872  O  O   . ILE H  1 18  ? 131.085 7.468   19.072 1.00 29.19 ? 17   ILE H O   1 
ATOM   7873  C  CB  . ILE H  1 18  ? 131.563 4.745   20.344 1.00 25.87 ? 17   ILE H CB  1 
ATOM   7874  C  CG1 . ILE H  1 18  ? 131.939 3.802   21.493 1.00 29.12 ? 17   ILE H CG1 1 
ATOM   7875  C  CG2 . ILE H  1 18  ? 131.738 4.041   19.006 1.00 27.54 ? 17   ILE H CG2 1 
ATOM   7876  C  CD1 . ILE H  1 18  ? 131.096 2.534   21.562 1.00 31.26 ? 17   ILE H CD1 1 
ATOM   7877  N  N   . ILE H  1 19  ? 133.195 7.112   18.385 1.00 27.75 ? 18   ILE H N   1 
ATOM   7878  C  CA  . ILE H  1 19  ? 133.062 7.965   17.214 1.00 26.99 ? 18   ILE H CA  1 
ATOM   7879  C  C   . ILE H  1 19  ? 133.285 7.147   15.952 1.00 27.43 ? 18   ILE H C   1 
ATOM   7880  O  O   . ILE H  1 19  ? 134.294 6.454   15.817 1.00 28.89 ? 18   ILE H O   1 
ATOM   7881  C  CB  . ILE H  1 19  ? 134.096 9.126   17.245 1.00 27.29 ? 18   ILE H CB  1 
ATOM   7882  C  CG1 . ILE H  1 19  ? 133.935 9.944   18.528 1.00 28.02 ? 18   ILE H CG1 1 
ATOM   7883  C  CG2 . ILE H  1 19  ? 133.910 10.020  16.024 1.00 26.89 ? 18   ILE H CG2 1 
ATOM   7884  C  CD1 . ILE H  1 19  ? 132.601 10.670  18.644 1.00 27.44 ? 18   ILE H CD1 1 
ATOM   7885  N  N   . ASN H  1 20  ? 132.345 7.247   15.021 1.00 29.19 ? 19   ASN H N   1 
ATOM   7886  C  CA  . ASN H  1 20  ? 132.428 6.525   13.761 1.00 30.85 ? 19   ASN H CA  1 
ATOM   7887  C  C   . ASN H  1 20  ? 132.835 7.442   12.617 1.00 32.11 ? 19   ASN H C   1 
ATOM   7888  O  O   . ASN H  1 20  ? 132.527 8.638   12.622 1.00 33.59 ? 19   ASN H O   1 
ATOM   7889  C  CB  . ASN H  1 20  ? 131.076 5.896   13.436 1.00 30.41 ? 19   ASN H CB  1 
ATOM   7890  C  CG  . ASN H  1 20  ? 130.641 4.894   14.481 1.00 29.99 ? 19   ASN H CG  1 
ATOM   7891  O  OD1 . ASN H  1 20  ? 131.156 3.781   14.537 1.00 28.29 ? 19   ASN H OD1 1 
ATOM   7892  N  ND2 . ASN H  1 20  ? 129.699 5.293   15.327 1.00 29.75 ? 19   ASN H ND2 1 
ATOM   7893  N  N   . PHE H  1 21  ? 133.523 6.864   11.639 1.00 31.99 ? 20   PHE H N   1 
ATOM   7894  C  CA  . PHE H  1 21  ? 133.976 7.587   10.457 1.00 33.10 ? 20   PHE H CA  1 
ATOM   7895  C  C   . PHE H  1 21  ? 133.551 6.760   9.244  1.00 34.17 ? 20   PHE H C   1 
ATOM   7896  O  O   . PHE H  1 21  ? 133.736 5.547   9.221  1.00 32.98 ? 20   PHE H O   1 
ATOM   7897  C  CB  . PHE H  1 21  ? 135.504 7.715   10.457 1.00 33.99 ? 20   PHE H CB  1 
ATOM   7898  C  CG  . PHE H  1 21  ? 136.058 8.533   11.597 1.00 33.55 ? 20   PHE H CG  1 
ATOM   7899  C  CD1 . PHE H  1 21  ? 136.265 9.903   11.453 1.00 35.27 ? 20   PHE H CD1 1 
ATOM   7900  C  CD2 . PHE H  1 21  ? 136.379 7.931   12.811 1.00 33.84 ? 20   PHE H CD2 1 
ATOM   7901  C  CE1 . PHE H  1 21  ? 136.787 10.665  12.505 1.00 33.61 ? 20   PHE H CE1 1 
ATOM   7902  C  CE2 . PHE H  1 21  ? 136.901 8.683   13.870 1.00 33.31 ? 20   PHE H CE2 1 
ATOM   7903  C  CZ  . PHE H  1 21  ? 137.105 10.051  13.713 1.00 33.76 ? 20   PHE H CZ  1 
ATOM   7904  N  N   . GLU H  1 22  ? 132.978 7.408   8.239  1.00 35.59 ? 21   GLU H N   1 
ATOM   7905  C  CA  . GLU H  1 22  ? 132.569 6.696   7.040  1.00 37.96 ? 21   GLU H CA  1 
ATOM   7906  C  C   . GLU H  1 22  ? 132.904 7.530   5.808  1.00 38.46 ? 21   GLU H C   1 
ATOM   7907  O  O   . GLU H  1 22  ? 132.583 8.716   5.741  1.00 38.15 ? 21   GLU H O   1 
ATOM   7908  C  CB  . GLU H  1 22  ? 131.068 6.380   7.083  1.00 38.23 ? 21   GLU H CB  1 
ATOM   7909  C  CG  . GLU H  1 22  ? 130.583 5.622   5.860  1.00 45.66 ? 21   GLU H CG  1 
ATOM   7910  C  CD  . GLU H  1 22  ? 129.116 5.240   5.931  1.00 48.28 ? 21   GLU H CD  1 
ATOM   7911  O  OE1 . GLU H  1 22  ? 128.585 4.766   4.901  1.00 50.15 ? 21   GLU H OE1 1 
ATOM   7912  O  OE2 . GLU H  1 22  ? 128.498 5.408   7.008  1.00 48.44 ? 21   GLU H OE2 1 
ATOM   7913  N  N   . GLN H  1 23  ? 133.564 6.902   4.842  1.00 38.92 ? 22   GLN H N   1 
ATOM   7914  C  CA  . GLN H  1 23  ? 133.954 7.580   3.613  1.00 42.28 ? 22   GLN H CA  1 
ATOM   7915  C  C   . GLN H  1 23  ? 133.707 6.686   2.398  1.00 43.95 ? 22   GLN H C   1 
ATOM   7916  O  O   . GLN H  1 23  ? 134.491 5.784   2.111  1.00 43.54 ? 22   GLN H O   1 
ATOM   7917  C  CB  . GLN H  1 23  ? 135.434 7.976   3.689  1.00 40.21 ? 22   GLN H CB  1 
ATOM   7918  C  CG  . GLN H  1 23  ? 135.996 8.563   2.401  1.00 41.51 ? 22   GLN H CG  1 
ATOM   7919  C  CD  . GLN H  1 23  ? 137.443 9.001   2.534  1.00 40.98 ? 22   GLN H CD  1 
ATOM   7920  O  OE1 . GLN H  1 23  ? 138.287 8.259   3.037  1.00 40.64 ? 22   GLN H OE1 1 
ATOM   7921  N  NE2 . GLN H  1 23  ? 137.740 10.209  2.070  1.00 41.12 ? 22   GLN H NE2 1 
ATOM   7922  N  N   . LYS H  1 24  ? 132.617 6.948   1.683  1.00 47.04 ? 23   LYS H N   1 
ATOM   7923  C  CA  . LYS H  1 24  ? 132.266 6.160   0.505  1.00 50.71 ? 23   LYS H CA  1 
ATOM   7924  C  C   . LYS H  1 24  ? 133.215 6.341   -0.684 1.00 52.23 ? 23   LYS H C   1 
ATOM   7925  O  O   . LYS H  1 24  ? 133.498 5.378   -1.398 1.00 53.28 ? 23   LYS H O   1 
ATOM   7926  C  CB  . LYS H  1 24  ? 130.826 6.466   0.084  1.00 52.20 ? 23   LYS H CB  1 
ATOM   7927  C  CG  . LYS H  1 24  ? 129.797 6.099   1.147  1.00 51.81 ? 23   LYS H CG  1 
ATOM   7928  C  CD  . LYS H  1 24  ? 128.376 6.263   0.635  1.00 53.54 ? 23   LYS H CD  1 
ATOM   7929  C  CE  . LYS H  1 24  ? 127.365 5.823   1.682  0.00 53.17 ? 23   LYS H CE  1 
ATOM   7930  N  NZ  . LYS H  1 24  ? 125.966 5.933   1.185  0.00 53.44 ? 23   LYS H NZ  1 
ATOM   7931  N  N   . GLU H  1 25  ? 133.704 7.561   -0.897 1.00 53.32 ? 24   GLU H N   1 
ATOM   7932  C  CA  . GLU H  1 25  ? 134.634 7.840   -1.996 1.00 54.63 ? 24   GLU H CA  1 
ATOM   7933  C  C   . GLU H  1 25  ? 136.063 7.974   -1.478 1.00 55.22 ? 24   GLU H C   1 
ATOM   7934  O  O   . GLU H  1 25  ? 136.303 8.638   -0.471 1.00 55.94 ? 24   GLU H O   1 
ATOM   7935  C  CB  . GLU H  1 25  ? 134.243 9.131   -2.721 1.00 55.81 ? 24   GLU H CB  1 
ATOM   7936  C  CG  . GLU H  1 25  ? 133.078 8.998   -3.684 1.00 57.66 ? 24   GLU H CG  1 
ATOM   7937  C  CD  . GLU H  1 25  ? 132.649 10.341  -4.253 1.00 59.11 ? 24   GLU H CD  1 
ATOM   7938  O  OE1 . GLU H  1 25  ? 132.087 11.157  -3.491 1.00 59.63 ? 24   GLU H OE1 1 
ATOM   7939  O  OE2 . GLU H  1 25  ? 132.881 10.585  -5.458 1.00 59.45 ? 24   GLU H OE2 1 
ATOM   7940  N  N   . SER H  1 26  ? 137.009 7.357   -2.180 1.00 56.01 ? 25   SER H N   1 
ATOM   7941  C  CA  . SER H  1 26  ? 138.418 7.385   -1.790 1.00 57.22 ? 25   SER H CA  1 
ATOM   7942  C  C   . SER H  1 26  ? 138.922 8.777   -1.421 1.00 57.35 ? 25   SER H C   1 
ATOM   7943  O  O   . SER H  1 26  ? 139.775 8.922   -0.545 1.00 57.74 ? 25   SER H O   1 
ATOM   7944  C  CB  . SER H  1 26  ? 139.291 6.817   -2.913 1.00 58.18 ? 25   SER H CB  1 
ATOM   7945  O  OG  . SER H  1 26  ? 139.256 7.649   -4.059 1.00 59.49 ? 25   SER H OG  1 
ATOM   7946  N  N   . ASN H  1 27  ? 138.398 9.796   -2.091 1.00 57.12 ? 26   ASN H N   1 
ATOM   7947  C  CA  . ASN H  1 27  ? 138.809 11.170  -1.825 1.00 56.78 ? 26   ASN H CA  1 
ATOM   7948  C  C   . ASN H  1 27  ? 137.586 12.032  -1.536 1.00 54.92 ? 26   ASN H C   1 
ATOM   7949  O  O   . ASN H  1 27  ? 137.637 13.258  -1.639 1.00 55.55 ? 26   ASN H O   1 
ATOM   7950  C  CB  . ASN H  1 27  ? 139.570 11.730  -3.031 1.00 58.76 ? 26   ASN H CB  1 
ATOM   7951  C  CG  . ASN H  1 27  ? 138.699 11.851  -4.266 1.00 61.26 ? 26   ASN H CG  1 
ATOM   7952  O  OD1 . ASN H  1 27  ? 137.886 10.970  -4.555 1.00 62.16 ? 26   ASN H OD1 1 
ATOM   7953  N  ND2 . ASN H  1 27  ? 138.873 12.939  -5.009 1.00 62.54 ? 26   ASN H ND2 1 
ATOM   7954  N  N   . GLY H  1 28  ? 136.488 11.378  -1.173 1.00 51.44 ? 27   GLY H N   1 
ATOM   7955  C  CA  . GLY H  1 28  ? 135.265 12.099  -0.880 1.00 47.45 ? 27   GLY H CA  1 
ATOM   7956  C  C   . GLY H  1 28  ? 135.169 12.543  0.566  1.00 44.25 ? 27   GLY H C   1 
ATOM   7957  O  O   . GLY H  1 28  ? 136.089 12.314  1.354  1.00 40.97 ? 27   GLY H O   1 
ATOM   7958  N  N   . PRO H  1 29  ? 134.057 13.186  0.945  1.00 41.93 ? 28   PRO H N   1 
ATOM   7959  C  CA  . PRO H  1 29  ? 133.856 13.660  2.316  1.00 41.00 ? 28   PRO H CA  1 
ATOM   7960  C  C   . PRO H  1 29  ? 133.758 12.523  3.332  1.00 39.23 ? 28   PRO H C   1 
ATOM   7961  O  O   . PRO H  1 29  ? 133.293 11.425  3.016  1.00 38.90 ? 28   PRO H O   1 
ATOM   7962  C  CB  . PRO H  1 29  ? 132.564 14.467  2.212  1.00 41.54 ? 28   PRO H CB  1 
ATOM   7963  C  CG  . PRO H  1 29  ? 131.811 13.741  1.150  1.00 43.36 ? 28   PRO H CG  1 
ATOM   7964  C  CD  . PRO H  1 29  ? 132.881 13.487  0.111  1.00 42.61 ? 28   PRO H CD  1 
ATOM   7965  N  N   . VAL H  1 30  ? 134.207 12.803  4.552  1.00 37.06 ? 29   VAL H N   1 
ATOM   7966  C  CA  . VAL H  1 30  ? 134.178 11.834  5.639  1.00 34.76 ? 29   VAL H CA  1 
ATOM   7967  C  C   . VAL H  1 30  ? 133.098 12.225  6.636  1.00 34.89 ? 29   VAL H C   1 
ATOM   7968  O  O   . VAL H  1 30  ? 133.128 13.327  7.197  1.00 33.43 ? 29   VAL H O   1 
ATOM   7969  C  CB  . VAL H  1 30  ? 135.526 11.787  6.393  1.00 34.52 ? 29   VAL H CB  1 
ATOM   7970  C  CG1 . VAL H  1 30  ? 135.449 10.790  7.546  1.00 32.77 ? 29   VAL H CG1 1 
ATOM   7971  C  CG2 . VAL H  1 30  ? 136.641 11.423  5.439  1.00 32.82 ? 29   VAL H CG2 1 
ATOM   7972  N  N   . LYS H  1 31  ? 132.139 11.330  6.846  1.00 32.61 ? 30   LYS H N   1 
ATOM   7973  C  CA  . LYS H  1 31  ? 131.073 11.593  7.794  1.00 33.70 ? 30   LYS H CA  1 
ATOM   7974  C  C   . LYS H  1 31  ? 131.557 11.139  9.157  1.00 31.78 ? 30   LYS H C   1 
ATOM   7975  O  O   . LYS H  1 31  ? 132.145 10.069  9.281  1.00 31.53 ? 30   LYS H O   1 
ATOM   7976  C  CB  . LYS H  1 31  ? 129.802 10.826  7.411  1.00 36.51 ? 30   LYS H CB  1 
ATOM   7977  C  CG  . LYS H  1 31  ? 129.189 11.263  6.091  1.00 43.42 ? 30   LYS H CG  1 
ATOM   7978  C  CD  . LYS H  1 31  ? 127.852 10.580  5.843  1.00 47.19 ? 30   LYS H CD  1 
ATOM   7979  C  CE  . LYS H  1 31  ? 127.202 11.092  4.562  1.00 49.88 ? 30   LYS H CE  1 
ATOM   7980  N  NZ  . LYS H  1 31  ? 125.869 10.466  4.324  1.00 50.80 ? 30   LYS H NZ  1 
ATOM   7981  N  N   . VAL H  1 32  ? 131.323 11.960  10.172 1.00 30.00 ? 31   VAL H N   1 
ATOM   7982  C  CA  . VAL H  1 32  ? 131.732 11.626  11.527 1.00 29.88 ? 31   VAL H CA  1 
ATOM   7983  C  C   . VAL H  1 32  ? 130.494 11.691  12.409 1.00 31.81 ? 31   VAL H C   1 
ATOM   7984  O  O   . VAL H  1 32  ? 129.847 12.740  12.511 1.00 30.23 ? 31   VAL H O   1 
ATOM   7985  C  CB  . VAL H  1 32  ? 132.791 12.617  12.063 1.00 30.72 ? 31   VAL H CB  1 
ATOM   7986  C  CG1 . VAL H  1 32  ? 133.281 12.170  13.433 1.00 28.06 ? 31   VAL H CG1 1 
ATOM   7987  C  CG2 . VAL H  1 32  ? 133.955 12.713  11.084 1.00 29.87 ? 31   VAL H CG2 1 
ATOM   7988  N  N   . TRP H  1 33  ? 130.160 10.567  13.036 1.00 29.53 ? 32   TRP H N   1 
ATOM   7989  C  CA  . TRP H  1 33  ? 128.987 10.509  13.893 1.00 30.52 ? 32   TRP H CA  1 
ATOM   7990  C  C   . TRP H  1 33  ? 129.217 9.617   15.102 1.00 30.02 ? 32   TRP H C   1 
ATOM   7991  O  O   . TRP H  1 33  ? 129.953 8.635   15.036 1.00 29.11 ? 32   TRP H O   1 
ATOM   7992  C  CB  . TRP H  1 33  ? 127.775 9.995   13.110 1.00 33.15 ? 32   TRP H CB  1 
ATOM   7993  C  CG  . TRP H  1 33  ? 127.895 8.560   12.677 1.00 37.68 ? 32   TRP H CG  1 
ATOM   7994  C  CD1 . TRP H  1 33  ? 128.563 8.084   11.585 1.00 37.79 ? 32   TRP H CD1 1 
ATOM   7995  C  CD2 . TRP H  1 33  ? 127.361 7.416   13.351 1.00 38.44 ? 32   TRP H CD2 1 
ATOM   7996  N  NE1 . TRP H  1 33  ? 128.477 6.711   11.537 1.00 39.22 ? 32   TRP H NE1 1 
ATOM   7997  C  CE2 . TRP H  1 33  ? 127.739 6.273   12.612 1.00 38.81 ? 32   TRP H CE2 1 
ATOM   7998  C  CE3 . TRP H  1 33  ? 126.592 7.239   14.513 1.00 39.22 ? 32   TRP H CE3 1 
ATOM   7999  C  CZ2 . TRP H  1 33  ? 127.388 4.974   12.991 1.00 38.91 ? 32   TRP H CZ2 1 
ATOM   8000  C  CZ3 . TRP H  1 33  ? 126.239 5.944   14.896 1.00 39.25 ? 32   TRP H CZ3 1 
ATOM   8001  C  CH2 . TRP H  1 33  ? 126.636 4.830   14.134 1.00 39.29 ? 32   TRP H CH2 1 
ATOM   8002  N  N   . GLY H  1 34  ? 128.579 9.967   16.211 1.00 29.31 ? 33   GLY H N   1 
ATOM   8003  C  CA  . GLY H  1 34  ? 128.736 9.176   17.412 1.00 30.54 ? 33   GLY H CA  1 
ATOM   8004  C  C   . GLY H  1 34  ? 128.297 9.941   18.636 1.00 31.15 ? 33   GLY H C   1 
ATOM   8005  O  O   . GLY H  1 34  ? 127.631 10.969  18.535 1.00 30.63 ? 33   GLY H O   1 
ATOM   8006  N  N   . SER H  1 35  ? 128.683 9.446   19.802 1.00 33.10 ? 34   SER H N   1 
ATOM   8007  C  CA  . SER H  1 35  ? 128.294 10.088  21.044 1.00 31.29 ? 34   SER H CA  1 
ATOM   8008  C  C   . SER H  1 35  ? 129.432 10.093  22.042 1.00 29.39 ? 34   SER H C   1 
ATOM   8009  O  O   . SER H  1 35  ? 130.222 9.155   22.108 1.00 29.21 ? 34   SER H O   1 
ATOM   8010  C  CB  . SER H  1 35  ? 127.083 9.357   21.637 1.00 35.05 ? 34   SER H CB  1 
ATOM   8011  O  OG  . SER H  1 35  ? 126.646 9.962   22.841 1.00 36.50 ? 34   SER H OG  1 
ATOM   8012  N  N   . ILE H  1 36  ? 129.517 11.167  22.812 1.00 28.12 ? 35   ILE H N   1 
ATOM   8013  C  CA  . ILE H  1 36  ? 130.541 11.300  23.832 1.00 27.45 ? 35   ILE H CA  1 
ATOM   8014  C  C   . ILE H  1 36  ? 129.784 11.802  25.039 1.00 28.51 ? 35   ILE H C   1 
ATOM   8015  O  O   . ILE H  1 36  ? 128.961 12.714  24.924 1.00 29.82 ? 35   ILE H O   1 
ATOM   8016  C  CB  . ILE H  1 36  ? 131.617 12.346  23.447 1.00 28.82 ? 35   ILE H CB  1 
ATOM   8017  C  CG1 . ILE H  1 36  ? 132.228 12.000  22.086 1.00 27.13 ? 35   ILE H CG1 1 
ATOM   8018  C  CG2 . ILE H  1 36  ? 132.718 12.379  24.511 1.00 26.62 ? 35   ILE H CG2 1 
ATOM   8019  C  CD1 . ILE H  1 36  ? 133.202 13.045  21.577 1.00 27.40 ? 35   ILE H CD1 1 
ATOM   8020  N  N   . LYS H  1 37  ? 130.036 11.200  26.192 1.00 28.80 ? 36   LYS H N   1 
ATOM   8021  C  CA  . LYS H  1 37  ? 129.344 11.615  27.403 1.00 29.69 ? 36   LYS H CA  1 
ATOM   8022  C  C   . LYS H  1 37  ? 130.336 11.991  28.492 1.00 28.26 ? 36   LYS H C   1 
ATOM   8023  O  O   . LYS H  1 37  ? 131.544 11.857  28.308 1.00 29.01 ? 36   LYS H O   1 
ATOM   8024  C  CB  . LYS H  1 37  ? 128.424 10.491  27.893 1.00 33.32 ? 36   LYS H CB  1 
ATOM   8025  C  CG  . LYS H  1 37  ? 129.144 9.200   28.249 1.00 36.40 ? 36   LYS H CG  1 
ATOM   8026  C  CD  . LYS H  1 37  ? 128.154 8.127   28.704 1.00 42.16 ? 36   LYS H CD  1 
ATOM   8027  C  CE  . LYS H  1 37  ? 128.864 6.828   29.073 1.00 43.19 ? 36   LYS H CE  1 
ATOM   8028  N  NZ  . LYS H  1 37  ? 127.902 5.787   29.544 1.00 45.63 ? 36   LYS H NZ  1 
ATOM   8029  N  N   . GLY H  1 38  ? 129.814 12.462  29.621 1.00 28.16 ? 37   GLY H N   1 
ATOM   8030  C  CA  . GLY H  1 38  ? 130.659 12.850  30.736 1.00 28.78 ? 37   GLY H CA  1 
ATOM   8031  C  C   . GLY H  1 38  ? 131.339 14.192  30.535 1.00 30.00 ? 37   GLY H C   1 
ATOM   8032  O  O   . GLY H  1 38  ? 132.224 14.564  31.304 1.00 28.07 ? 37   GLY H O   1 
ATOM   8033  N  N   . LEU H  1 39  ? 130.912 14.924  29.508 1.00 30.47 ? 38   LEU H N   1 
ATOM   8034  C  CA  . LEU H  1 39  ? 131.478 16.234  29.186 1.00 31.90 ? 38   LEU H CA  1 
ATOM   8035  C  C   . LEU H  1 39  ? 130.721 17.397  29.818 1.00 32.50 ? 38   LEU H C   1 
ATOM   8036  O  O   . LEU H  1 39  ? 129.517 17.306  30.060 1.00 30.92 ? 38   LEU H O   1 
ATOM   8037  C  CB  . LEU H  1 39  ? 131.486 16.440  27.666 1.00 31.60 ? 38   LEU H CB  1 
ATOM   8038  C  CG  . LEU H  1 39  ? 132.470 15.603  26.852 1.00 30.96 ? 38   LEU H CG  1 
ATOM   8039  C  CD1 . LEU H  1 39  ? 132.091 15.645  25.377 1.00 31.13 ? 38   LEU H CD1 1 
ATOM   8040  C  CD2 . LEU H  1 39  ? 133.876 16.138  27.072 1.00 30.56 ? 38   LEU H CD2 1 
ATOM   8041  N  N   . THR H  1 40  ? 131.433 18.494  30.078 1.00 31.29 ? 39   THR H N   1 
ATOM   8042  C  CA  . THR H  1 40  ? 130.794 19.681  30.635 1.00 31.15 ? 39   THR H CA  1 
ATOM   8043  C  C   . THR H  1 40  ? 129.991 20.284  29.479 1.00 31.53 ? 39   THR H C   1 
ATOM   8044  O  O   . THR H  1 40  ? 130.440 20.267  28.331 1.00 30.02 ? 39   THR H O   1 
ATOM   8045  C  CB  . THR H  1 40  ? 131.827 20.738  31.115 1.00 32.28 ? 39   THR H CB  1 
ATOM   8046  O  OG1 . THR H  1 40  ? 132.642 21.140  30.008 1.00 30.79 ? 39   THR H OG1 1 
ATOM   8047  C  CG2 . THR H  1 40  ? 132.717 20.174  32.225 1.00 29.91 ? 39   THR H CG2 1 
ATOM   8048  N  N   . GLU H  1 41  ? 128.807 20.803  29.781 1.00 30.93 ? 40   GLU H N   1 
ATOM   8049  C  CA  . GLU H  1 41  ? 127.956 21.404  28.763 1.00 32.67 ? 40   GLU H CA  1 
ATOM   8050  C  C   . GLU H  1 41  ? 128.721 22.465  27.970 1.00 32.90 ? 40   GLU H C   1 
ATOM   8051  O  O   . GLU H  1 41  ? 129.496 23.238  28.537 1.00 30.57 ? 40   GLU H O   1 
ATOM   8052  C  CB  . GLU H  1 41  ? 126.726 22.036  29.421 1.00 32.73 ? 40   GLU H CB  1 
ATOM   8053  C  CG  . GLU H  1 41  ? 125.733 22.613  28.429 1.00 36.97 ? 40   GLU H CG  1 
ATOM   8054  C  CD  . GLU H  1 41  ? 124.539 23.269  29.101 1.00 40.50 ? 40   GLU H CD  1 
ATOM   8055  O  OE1 . GLU H  1 41  ? 123.639 23.747  28.376 1.00 43.72 ? 40   GLU H OE1 1 
ATOM   8056  O  OE2 . GLU H  1 41  ? 124.496 23.307  30.350 1.00 41.30 ? 40   GLU H OE2 1 
ATOM   8057  N  N   . GLY H  1 42  ? 128.514 22.491  26.658 1.00 32.20 ? 41   GLY H N   1 
ATOM   8058  C  CA  . GLY H  1 42  ? 129.197 23.479  25.835 1.00 32.62 ? 41   GLY H CA  1 
ATOM   8059  C  C   . GLY H  1 42  ? 130.202 22.950  24.821 1.00 32.37 ? 41   GLY H C   1 
ATOM   8060  O  O   . GLY H  1 42  ? 130.260 21.749  24.542 1.00 31.15 ? 41   GLY H O   1 
ATOM   8061  N  N   . LEU H  1 43  ? 131.008 23.871  24.291 1.00 33.07 ? 42   LEU H N   1 
ATOM   8062  C  CA  . LEU H  1 43  ? 132.024 23.583  23.275 1.00 31.02 ? 42   LEU H CA  1 
ATOM   8063  C  C   . LEU H  1 43  ? 133.249 22.841  23.786 1.00 30.07 ? 42   LEU H C   1 
ATOM   8064  O  O   . LEU H  1 43  ? 133.766 23.142  24.860 1.00 30.32 ? 42   LEU H O   1 
ATOM   8065  C  CB  . LEU H  1 43  ? 132.500 24.891  22.626 1.00 31.68 ? 42   LEU H CB  1 
ATOM   8066  C  CG  . LEU H  1 43  ? 131.486 25.724  21.847 1.00 32.32 ? 42   LEU H CG  1 
ATOM   8067  C  CD1 . LEU H  1 43  ? 132.085 27.089  21.512 1.00 33.21 ? 42   LEU H CD1 1 
ATOM   8068  C  CD2 . LEU H  1 43  ? 131.089 24.977  20.581 1.00 31.00 ? 42   LEU H CD2 1 
ATOM   8069  N  N   . HIS H  1 44  ? 133.722 21.882  22.996 1.00 27.61 ? 43   HIS H N   1 
ATOM   8070  C  CA  . HIS H  1 44  ? 134.911 21.121  23.351 1.00 27.97 ? 43   HIS H CA  1 
ATOM   8071  C  C   . HIS H  1 44  ? 135.779 20.882  22.121 1.00 28.27 ? 43   HIS H C   1 
ATOM   8072  O  O   . HIS H  1 44  ? 135.275 20.435  21.087 1.00 28.03 ? 43   HIS H O   1 
ATOM   8073  C  CB  . HIS H  1 44  ? 134.520 19.776  23.968 1.00 28.61 ? 43   HIS H CB  1 
ATOM   8074  C  CG  . HIS H  1 44  ? 133.949 19.891  25.348 1.00 30.21 ? 43   HIS H CG  1 
ATOM   8075  N  ND1 . HIS H  1 44  ? 134.740 19.934  26.478 1.00 30.29 ? 43   HIS H ND1 1 
ATOM   8076  C  CD2 . HIS H  1 44  ? 132.672 20.010  25.778 1.00 29.22 ? 43   HIS H CD2 1 
ATOM   8077  C  CE1 . HIS H  1 44  ? 133.971 20.073  27.544 1.00 30.32 ? 43   HIS H CE1 1 
ATOM   8078  N  NE2 . HIS H  1 44  ? 132.712 20.122  27.145 1.00 31.64 ? 43   HIS H NE2 1 
ATOM   8079  N  N   . GLY H  1 45  ? 137.072 21.190  22.241 1.00 25.57 ? 44   GLY H N   1 
ATOM   8080  C  CA  . GLY H  1 45  ? 138.008 20.975  21.146 1.00 29.67 ? 44   GLY H CA  1 
ATOM   8081  C  C   . GLY H  1 45  ? 137.917 19.537  20.658 1.00 29.41 ? 44   GLY H C   1 
ATOM   8082  O  O   . GLY H  1 45  ? 137.726 18.621  21.453 1.00 30.10 ? 44   GLY H O   1 
ATOM   8083  N  N   . PHE H  1 46  ? 138.078 19.334  19.357 1.00 29.66 ? 45   PHE H N   1 
ATOM   8084  C  CA  . PHE H  1 46  ? 137.951 18.007  18.761 1.00 27.38 ? 45   PHE H CA  1 
ATOM   8085  C  C   . PHE H  1 46  ? 138.948 17.893  17.606 1.00 26.22 ? 45   PHE H C   1 
ATOM   8086  O  O   . PHE H  1 46  ? 138.729 18.468  16.538 1.00 25.52 ? 45   PHE H O   1 
ATOM   8087  C  CB  . PHE H  1 46  ? 136.513 17.863  18.252 1.00 28.50 ? 45   PHE H CB  1 
ATOM   8088  C  CG  . PHE H  1 46  ? 136.083 16.452  17.959 1.00 30.71 ? 45   PHE H CG  1 
ATOM   8089  C  CD1 . PHE H  1 46  ? 136.054 15.488  18.964 1.00 30.94 ? 45   PHE H CD1 1 
ATOM   8090  C  CD2 . PHE H  1 46  ? 135.625 16.109  16.688 1.00 32.12 ? 45   PHE H CD2 1 
ATOM   8091  C  CE1 . PHE H  1 46  ? 135.569 14.204  18.713 1.00 31.41 ? 45   PHE H CE1 1 
ATOM   8092  C  CE2 . PHE H  1 46  ? 135.135 14.824  16.424 1.00 32.56 ? 45   PHE H CE2 1 
ATOM   8093  C  CZ  . PHE H  1 46  ? 135.107 13.871  17.439 1.00 31.77 ? 45   PHE H CZ  1 
ATOM   8094  N  N   . HIS H  1 47  ? 140.039 17.157  17.813 1.00 25.55 ? 46   HIS H N   1 
ATOM   8095  C  CA  . HIS H  1 47  ? 141.056 17.013  16.768 1.00 25.16 ? 46   HIS H CA  1 
ATOM   8096  C  C   . HIS H  1 47  ? 141.646 15.615  16.642 1.00 25.23 ? 46   HIS H C   1 
ATOM   8097  O  O   . HIS H  1 47  ? 141.573 14.800  17.563 1.00 26.77 ? 46   HIS H O   1 
ATOM   8098  C  CB  . HIS H  1 47  ? 142.237 17.954  17.029 1.00 23.17 ? 46   HIS H CB  1 
ATOM   8099  C  CG  . HIS H  1 47  ? 141.851 19.271  17.625 1.00 23.31 ? 46   HIS H CG  1 
ATOM   8100  N  ND1 . HIS H  1 47  ? 142.255 19.660  18.881 1.00 23.63 ? 46   HIS H ND1 1 
ATOM   8101  C  CD2 . HIS H  1 47  ? 141.119 20.294  17.126 1.00 24.05 ? 46   HIS H CD2 1 
ATOM   8102  C  CE1 . HIS H  1 47  ? 141.789 20.872  19.134 1.00 23.48 ? 46   HIS H CE1 1 
ATOM   8103  N  NE2 . HIS H  1 47  ? 141.097 21.278  18.085 1.00 25.07 ? 46   HIS H NE2 1 
ATOM   8104  N  N   . VAL H  1 48  ? 142.248 15.359  15.489 1.00 24.81 ? 47   VAL H N   1 
ATOM   8105  C  CA  . VAL H  1 48  ? 142.935 14.104  15.242 1.00 23.68 ? 47   VAL H CA  1 
ATOM   8106  C  C   . VAL H  1 48  ? 144.402 14.458  15.400 1.00 25.09 ? 47   VAL H C   1 
ATOM   8107  O  O   . VAL H  1 48  ? 144.923 15.292  14.657 1.00 23.79 ? 47   VAL H O   1 
ATOM   8108  C  CB  . VAL H  1 48  ? 142.741 13.593  13.813 1.00 24.83 ? 47   VAL H CB  1 
ATOM   8109  C  CG1 . VAL H  1 48  ? 143.662 12.380  13.572 1.00 25.71 ? 47   VAL H CG1 1 
ATOM   8110  C  CG2 . VAL H  1 48  ? 141.284 13.209  13.590 1.00 23.96 ? 47   VAL H CG2 1 
ATOM   8111  N  N   . HIS H  1 49  ? 145.061 13.856  16.382 1.00 24.25 ? 48   HIS H N   1 
ATOM   8112  C  CA  . HIS H  1 49  ? 146.469 14.126  16.598 1.00 25.68 ? 48   HIS H CA  1 
ATOM   8113  C  C   . HIS H  1 49  ? 147.312 13.128  15.806 1.00 28.82 ? 48   HIS H C   1 
ATOM   8114  O  O   . HIS H  1 49  ? 146.834 12.059  15.410 1.00 26.78 ? 48   HIS H O   1 
ATOM   8115  C  CB  . HIS H  1 49  ? 146.799 14.114  18.098 1.00 24.51 ? 48   HIS H CB  1 
ATOM   8116  C  CG  . HIS H  1 49  ? 146.214 15.278  18.844 1.00 23.70 ? 48   HIS H CG  1 
ATOM   8117  N  ND1 . HIS H  1 49  ? 146.952 16.050  19.719 1.00 26.18 ? 48   HIS H ND1 1 
ATOM   8118  C  CD2 . HIS H  1 49  ? 144.970 15.814  18.833 1.00 23.71 ? 48   HIS H CD2 1 
ATOM   8119  C  CE1 . HIS H  1 49  ? 146.188 17.010  20.211 1.00 25.25 ? 48   HIS H CE1 1 
ATOM   8120  N  NE2 . HIS H  1 49  ? 144.979 16.890  19.691 1.00 23.91 ? 48   HIS H NE2 1 
ATOM   8121  N  N   . GLU H  1 50  ? 148.562 13.505  15.565 1.00 30.55 ? 49   GLU H N   1 
ATOM   8122  C  CA  . GLU H  1 50  ? 149.495 12.728  14.756 1.00 30.55 ? 49   GLU H CA  1 
ATOM   8123  C  C   . GLU H  1 50  ? 149.777 11.263  15.090 1.00 30.75 ? 49   GLU H C   1 
ATOM   8124  O  O   . GLU H  1 50  ? 149.743 10.412  14.202 1.00 30.65 ? 49   GLU H O   1 
ATOM   8125  C  CB  . GLU H  1 50  ? 150.830 13.480  14.676 1.00 31.39 ? 49   GLU H CB  1 
ATOM   8126  C  CG  . GLU H  1 50  ? 151.770 12.965  13.592 1.00 33.53 ? 49   GLU H CG  1 
ATOM   8127  C  CD  . GLU H  1 50  ? 153.081 13.736  13.517 1.00 34.73 ? 49   GLU H CD  1 
ATOM   8128  O  OE1 . GLU H  1 50  ? 153.880 13.445  12.602 1.00 37.79 ? 49   GLU H OE1 1 
ATOM   8129  O  OE2 . GLU H  1 50  ? 153.320 14.621  14.369 1.00 33.96 ? 49   GLU H OE2 1 
ATOM   8130  N  N   . PHE H  1 51  ? 150.052 10.960  16.353 1.00 31.02 ? 50   PHE H N   1 
ATOM   8131  C  CA  . PHE H  1 51  ? 150.406 9.592   16.718 1.00 31.85 ? 50   PHE H CA  1 
ATOM   8132  C  C   . PHE H  1 51  ? 149.360 8.765   17.455 1.00 31.16 ? 50   PHE H C   1 
ATOM   8133  O  O   . PHE H  1 51  ? 148.678 9.255   18.355 1.00 30.77 ? 50   PHE H O   1 
ATOM   8134  C  CB  . PHE H  1 51  ? 151.697 9.619   17.539 1.00 32.82 ? 50   PHE H CB  1 
ATOM   8135  C  CG  . PHE H  1 51  ? 152.799 10.419  16.902 1.00 34.76 ? 50   PHE H CG  1 
ATOM   8136  C  CD1 . PHE H  1 51  ? 153.355 10.022  15.690 1.00 35.49 ? 50   PHE H CD1 1 
ATOM   8137  C  CD2 . PHE H  1 51  ? 153.264 11.583  17.501 1.00 34.97 ? 50   PHE H CD2 1 
ATOM   8138  C  CE1 . PHE H  1 51  ? 154.358 10.776  15.081 1.00 36.21 ? 50   PHE H CE1 1 
ATOM   8139  C  CE2 . PHE H  1 51  ? 154.267 12.343  16.899 1.00 36.32 ? 50   PHE H CE2 1 
ATOM   8140  C  CZ  . PHE H  1 51  ? 154.812 11.935  15.687 1.00 36.55 ? 50   PHE H CZ  1 
ATOM   8141  N  N   . GLY H  1 52  ? 149.244 7.502   17.053 1.00 31.35 ? 51   GLY H N   1 
ATOM   8142  C  CA  . GLY H  1 52  ? 148.310 6.596   17.692 1.00 32.22 ? 51   GLY H CA  1 
ATOM   8143  C  C   . GLY H  1 52  ? 149.047 5.911   18.828 1.00 33.71 ? 51   GLY H C   1 
ATOM   8144  O  O   . GLY H  1 52  ? 148.992 4.690   18.985 1.00 33.04 ? 51   GLY H O   1 
ATOM   8145  N  N   . ASP H  1 53  ? 149.753 6.719   19.613 1.00 34.86 ? 52   ASP H N   1 
ATOM   8146  C  CA  . ASP H  1 53  ? 150.539 6.239   20.744 1.00 37.29 ? 52   ASP H CA  1 
ATOM   8147  C  C   . ASP H  1 53  ? 149.853 6.600   22.057 1.00 39.04 ? 52   ASP H C   1 
ATOM   8148  O  O   . ASP H  1 53  ? 149.776 7.771   22.430 1.00 39.28 ? 52   ASP H O   1 
ATOM   8149  C  CB  . ASP H  1 53  ? 151.937 6.858   20.687 1.00 37.29 ? 52   ASP H CB  1 
ATOM   8150  C  CG  . ASP H  1 53  ? 152.857 6.335   21.771 1.00 38.68 ? 52   ASP H CG  1 
ATOM   8151  O  OD1 . ASP H  1 53  ? 154.079 6.569   21.668 1.00 39.49 ? 52   ASP H OD1 1 
ATOM   8152  O  OD2 . ASP H  1 53  ? 152.364 5.703   22.728 1.00 38.48 ? 52   ASP H OD2 1 
ATOM   8153  N  N   . ASN H  1 54  ? 149.357 5.582   22.752 1.00 40.08 ? 53   ASN H N   1 
ATOM   8154  C  CA  . ASN H  1 54  ? 148.654 5.769   24.018 1.00 41.02 ? 53   ASN H CA  1 
ATOM   8155  C  C   . ASN H  1 54  ? 149.485 5.251   25.191 1.00 40.97 ? 53   ASN H C   1 
ATOM   8156  O  O   . ASN H  1 54  ? 148.945 4.942   26.252 1.00 39.72 ? 53   ASN H O   1 
ATOM   8157  C  CB  . ASN H  1 54  ? 147.317 5.019   23.966 1.00 43.39 ? 53   ASN H CB  1 
ATOM   8158  C  CG  . ASN H  1 54  ? 146.447 5.276   25.182 1.00 46.09 ? 53   ASN H CG  1 
ATOM   8159  O  OD1 . ASN H  1 54  ? 145.719 4.390   25.632 1.00 46.62 ? 53   ASN H OD1 1 
ATOM   8160  N  ND2 . ASN H  1 54  ? 146.505 6.494   25.711 1.00 48.41 ? 53   ASN H ND2 1 
ATOM   8161  N  N   . THR H  1 55  ? 150.798 5.155   25.002 1.00 41.15 ? 54   THR H N   1 
ATOM   8162  C  CA  . THR H  1 55  ? 151.671 4.656   26.055 1.00 42.19 ? 54   THR H CA  1 
ATOM   8163  C  C   . THR H  1 55  ? 151.692 5.584   27.262 1.00 43.04 ? 54   THR H C   1 
ATOM   8164  O  O   . THR H  1 55  ? 151.909 5.142   28.388 1.00 43.49 ? 54   THR H O   1 
ATOM   8165  C  CB  . THR H  1 55  ? 153.116 4.446   25.546 1.00 43.19 ? 54   THR H CB  1 
ATOM   8166  O  OG1 . THR H  1 55  ? 153.632 5.675   25.020 1.00 42.70 ? 54   THR H OG1 1 
ATOM   8167  C  CG2 . THR H  1 55  ? 153.138 3.382   24.457 1.00 43.38 ? 54   THR H CG2 1 
ATOM   8168  N  N   . ALA H  1 56  ? 151.458 6.870   27.027 1.00 43.45 ? 55   ALA H N   1 
ATOM   8169  C  CA  . ALA H  1 56  ? 151.441 7.846   28.111 1.00 43.52 ? 55   ALA H CA  1 
ATOM   8170  C  C   . ALA H  1 56  ? 150.132 8.627   28.082 1.00 44.25 ? 55   ALA H C   1 
ATOM   8171  O  O   . ALA H  1 56  ? 150.131 9.855   27.958 1.00 46.25 ? 55   ALA H O   1 
ATOM   8172  C  CB  . ALA H  1 56  ? 152.626 8.794   27.980 1.00 43.44 ? 55   ALA H CB  1 
ATOM   8173  N  N   . GLY H  1 57  ? 149.017 7.912   28.192 1.00 43.46 ? 56   GLY H N   1 
ATOM   8174  C  CA  . GLY H  1 57  ? 147.722 8.570   28.168 1.00 42.69 ? 56   GLY H CA  1 
ATOM   8175  C  C   . GLY H  1 57  ? 147.518 9.285   26.845 1.00 41.49 ? 56   GLY H C   1 
ATOM   8176  O  O   . GLY H  1 57  ? 148.036 8.854   25.813 1.00 42.00 ? 56   GLY H O   1 
ATOM   8177  N  N   . CYS H  1 58  ? 146.770 10.381  26.865 1.00 39.52 ? 57   CYS H N   1 
ATOM   8178  C  CA  . CYS H  1 58  ? 146.521 11.132  25.646 1.00 37.85 ? 57   CYS H CA  1 
ATOM   8179  C  C   . CYS H  1 58  ? 147.694 12.053  25.313 1.00 38.28 ? 57   CYS H C   1 
ATOM   8180  O  O   . CYS H  1 58  ? 147.767 12.607  24.218 1.00 37.16 ? 57   CYS H O   1 
ATOM   8181  C  CB  . CYS H  1 58  ? 145.233 11.944  25.785 1.00 36.77 ? 57   CYS H CB  1 
ATOM   8182  S  SG  . CYS H  1 58  ? 143.759 10.908  26.063 1.00 34.33 ? 57   CYS H SG  1 
ATOM   8183  N  N   . THR H  1 59  ? 148.621 12.194  26.254 1.00 38.51 ? 58   THR H N   1 
ATOM   8184  C  CA  . THR H  1 59  ? 149.785 13.056  26.061 1.00 40.51 ? 58   THR H CA  1 
ATOM   8185  C  C   . THR H  1 59  ? 150.700 12.602  24.928 1.00 40.35 ? 58   THR H C   1 
ATOM   8186  O  O   . THR H  1 59  ? 151.243 13.425  24.193 1.00 41.02 ? 58   THR H O   1 
ATOM   8187  C  CB  . THR H  1 59  ? 150.642 13.137  27.347 1.00 41.33 ? 58   THR H CB  1 
ATOM   8188  O  OG1 . THR H  1 59  ? 149.825 13.553  28.449 1.00 42.36 ? 58   THR H OG1 1 
ATOM   8189  C  CG2 . THR H  1 59  ? 151.787 14.131  27.163 1.00 42.46 ? 58   THR H CG2 1 
ATOM   8190  N  N   . SER H  1 60  ? 150.876 11.293  24.789 1.00 40.07 ? 59   SER H N   1 
ATOM   8191  C  CA  . SER H  1 60  ? 151.759 10.757  23.761 1.00 39.81 ? 59   SER H CA  1 
ATOM   8192  C  C   . SER H  1 60  ? 151.201 10.757  22.335 1.00 38.70 ? 59   SER H C   1 
ATOM   8193  O  O   . SER H  1 60  ? 151.867 10.298  21.408 1.00 39.49 ? 59   SER H O   1 
ATOM   8194  C  CB  . SER H  1 60  ? 152.204 9.343   24.151 1.00 40.08 ? 59   SER H CB  1 
ATOM   8195  O  OG  . SER H  1 60  ? 151.098 8.550   24.551 1.00 42.11 ? 59   SER H OG  1 
ATOM   8196  N  N   . ALA H  1 61  ? 149.991 11.273  22.154 1.00 37.48 ? 60   ALA H N   1 
ATOM   8197  C  CA  . ALA H  1 61  ? 149.393 11.328  20.822 1.00 36.96 ? 60   ALA H CA  1 
ATOM   8198  C  C   . ALA H  1 61  ? 150.086 12.402  19.985 1.00 36.93 ? 60   ALA H C   1 
ATOM   8199  O  O   . ALA H  1 61  ? 149.903 12.477  18.768 1.00 37.95 ? 60   ALA H O   1 
ATOM   8200  C  CB  . ALA H  1 61  ? 147.906 11.629  20.925 1.00 37.14 ? 60   ALA H CB  1 
ATOM   8201  N  N   . GLY H  1 62  ? 150.881 13.237  20.647 1.00 35.61 ? 61   GLY H N   1 
ATOM   8202  C  CA  . GLY H  1 62  ? 151.589 14.291  19.943 1.00 34.53 ? 61   GLY H CA  1 
ATOM   8203  C  C   . GLY H  1 62  ? 150.691 15.452  19.557 1.00 34.32 ? 61   GLY H C   1 
ATOM   8204  O  O   . GLY H  1 62  ? 149.610 15.621  20.128 1.00 34.45 ? 61   GLY H O   1 
ATOM   8205  N  N   . PRO H  1 63  ? 151.119 16.278  18.590 1.00 33.70 ? 62   PRO H N   1 
ATOM   8206  C  CA  . PRO H  1 63  ? 150.366 17.441  18.110 1.00 33.07 ? 62   PRO H CA  1 
ATOM   8207  C  C   . PRO H  1 63  ? 149.292 17.093  17.082 1.00 32.55 ? 62   PRO H C   1 
ATOM   8208  O  O   . PRO H  1 63  ? 149.086 15.925  16.739 1.00 31.10 ? 62   PRO H O   1 
ATOM   8209  C  CB  . PRO H  1 63  ? 151.456 18.318  17.510 1.00 34.65 ? 62   PRO H CB  1 
ATOM   8210  C  CG  . PRO H  1 63  ? 152.355 17.294  16.884 1.00 34.33 ? 62   PRO H CG  1 
ATOM   8211  C  CD  . PRO H  1 63  ? 152.466 16.251  17.987 1.00 34.35 ? 62   PRO H CD  1 
ATOM   8212  N  N   . HIS H  1 64  ? 148.614 18.122  16.586 1.00 32.38 ? 63   HIS H N   1 
ATOM   8213  C  CA  . HIS H  1 64  ? 147.572 17.930  15.587 1.00 32.20 ? 63   HIS H CA  1 
ATOM   8214  C  C   . HIS H  1 64  ? 148.164 17.353  14.314 1.00 32.52 ? 63   HIS H C   1 
ATOM   8215  O  O   . HIS H  1 64  ? 149.247 17.756  13.894 1.00 32.41 ? 63   HIS H O   1 
ATOM   8216  C  CB  . HIS H  1 64  ? 146.886 19.258  15.269 1.00 30.70 ? 63   HIS H CB  1 
ATOM   8217  C  CG  . HIS H  1 64  ? 146.154 19.856  16.429 1.00 30.54 ? 63   HIS H CG  1 
ATOM   8218  N  ND1 . HIS H  1 64  ? 145.445 21.026  16.339 1.00 31.26 ? 63   HIS H ND1 1 
ATOM   8219  C  CD2 . HIS H  1 64  ? 146.029 19.429  17.712 1.00 31.34 ? 63   HIS H CD2 1 
ATOM   8220  C  CE1 . HIS H  1 64  ? 144.907 21.305  17.516 1.00 31.04 ? 63   HIS H CE1 1 
ATOM   8221  N  NE2 . HIS H  1 64  ? 145.246 20.355  18.362 1.00 32.60 ? 63   HIS H NE2 1 
ATOM   8222  N  N   . PHE H  1 65  ? 147.457 16.402  13.710 1.00 32.03 ? 64   PHE H N   1 
ATOM   8223  C  CA  . PHE H  1 65  ? 147.912 15.788  12.470 1.00 33.73 ? 64   PHE H CA  1 
ATOM   8224  C  C   . PHE H  1 65  ? 148.019 16.938  11.470 1.00 34.24 ? 64   PHE H C   1 
ATOM   8225  O  O   . PHE H  1 65  ? 147.012 17.549  11.108 1.00 33.79 ? 64   PHE H O   1 
ATOM   8226  C  CB  . PHE H  1 65  ? 146.888 14.761  11.987 1.00 33.31 ? 64   PHE H CB  1 
ATOM   8227  C  CG  . PHE H  1 65  ? 147.312 14.014  10.756 1.00 36.31 ? 64   PHE H CG  1 
ATOM   8228  C  CD1 . PHE H  1 65  ? 146.365 13.592  9.828  1.00 35.20 ? 64   PHE H CD1 1 
ATOM   8229  C  CD2 . PHE H  1 65  ? 148.654 13.722  10.527 1.00 35.44 ? 64   PHE H CD2 1 
ATOM   8230  C  CE1 . PHE H  1 65  ? 146.747 12.893  8.684  1.00 36.72 ? 64   PHE H CE1 1 
ATOM   8231  C  CE2 . PHE H  1 65  ? 149.046 13.025  9.389  1.00 37.69 ? 64   PHE H CE2 1 
ATOM   8232  C  CZ  . PHE H  1 65  ? 148.089 12.609  8.465  1.00 37.89 ? 64   PHE H CZ  1 
ATOM   8233  N  N   . ASN H  1 66  ? 149.237 17.225  11.024 1.00 35.03 ? 65   ASN H N   1 
ATOM   8234  C  CA  . ASN H  1 66  ? 149.474 18.343  10.113 1.00 35.21 ? 65   ASN H CA  1 
ATOM   8235  C  C   . ASN H  1 66  ? 150.521 18.022  9.040  1.00 36.07 ? 65   ASN H C   1 
ATOM   8236  O  O   . ASN H  1 66  ? 151.607 18.597  9.026  1.00 34.99 ? 65   ASN H O   1 
ATOM   8237  C  CB  . ASN H  1 66  ? 149.906 19.548  10.963 1.00 35.96 ? 65   ASN H CB  1 
ATOM   8238  C  CG  . ASN H  1 66  ? 150.227 20.782  10.141 1.00 36.18 ? 65   ASN H CG  1 
ATOM   8239  O  OD1 . ASN H  1 66  ? 149.627 21.031  9.094  1.00 33.39 ? 65   ASN H OD1 1 
ATOM   8240  N  ND2 . ASN H  1 66  ? 151.166 21.582  10.638 1.00 36.47 ? 65   ASN H ND2 1 
ATOM   8241  N  N   . PRO H  1 67  ? 150.195 17.103  8.116  1.00 35.85 ? 66   PRO H N   1 
ATOM   8242  C  CA  . PRO H  1 67  ? 151.127 16.723  7.050  1.00 37.64 ? 66   PRO H CA  1 
ATOM   8243  C  C   . PRO H  1 67  ? 151.498 17.867  6.097  1.00 39.43 ? 66   PRO H C   1 
ATOM   8244  O  O   . PRO H  1 67  ? 152.590 17.875  5.525  1.00 40.03 ? 66   PRO H O   1 
ATOM   8245  C  CB  . PRO H  1 67  ? 150.388 15.589  6.340  1.00 37.65 ? 66   PRO H CB  1 
ATOM   8246  C  CG  . PRO H  1 67  ? 148.953 15.991  6.492  1.00 36.65 ? 66   PRO H CG  1 
ATOM   8247  C  CD  . PRO H  1 67  ? 148.894 16.433  7.936  1.00 35.76 ? 66   PRO H CD  1 
ATOM   8248  N  N   . LEU H  1 68  ? 150.596 18.831  5.933  1.00 39.61 ? 67   LEU H N   1 
ATOM   8249  C  CA  . LEU H  1 68  ? 150.848 19.958  5.043  1.00 40.55 ? 67   LEU H CA  1 
ATOM   8250  C  C   . LEU H  1 68  ? 151.566 21.112  5.744  1.00 41.45 ? 67   LEU H C   1 
ATOM   8251  O  O   . LEU H  1 68  ? 151.708 22.196  5.182  1.00 41.26 ? 67   LEU H O   1 
ATOM   8252  C  CB  . LEU H  1 68  ? 149.531 20.445  4.435  1.00 42.11 ? 67   LEU H CB  1 
ATOM   8253  C  CG  . LEU H  1 68  ? 148.774 19.424  3.578  1.00 43.61 ? 67   LEU H CG  1 
ATOM   8254  C  CD1 . LEU H  1 68  ? 147.473 20.031  3.078  1.00 45.32 ? 67   LEU H CD1 1 
ATOM   8255  C  CD2 . LEU H  1 68  ? 149.643 18.992  2.409  1.00 44.24 ? 67   LEU H CD2 1 
ATOM   8256  N  N   . SER H  1 69  ? 152.011 20.870  6.975  1.00 41.29 ? 68   SER H N   1 
ATOM   8257  C  CA  . SER H  1 69  ? 152.730 21.870  7.764  1.00 41.08 ? 68   SER H CA  1 
ATOM   8258  C  C   . SER H  1 69  ? 152.097 23.254  7.758  1.00 41.78 ? 68   SER H C   1 
ATOM   8259  O  O   . SER H  1 69  ? 152.770 24.247  7.479  1.00 43.10 ? 68   SER H O   1 
ATOM   8260  C  CB  . SER H  1 69  ? 154.177 21.990  7.273  1.00 41.35 ? 68   SER H CB  1 
ATOM   8261  O  OG  . SER H  1 69  ? 154.893 20.787  7.481  1.00 41.65 ? 68   SER H OG  1 
ATOM   8262  N  N   . ARG H  1 70  ? 150.811 23.325  8.075  1.00 40.04 ? 69   ARG H N   1 
ATOM   8263  C  CA  . ARG H  1 70  ? 150.108 24.599  8.104  1.00 39.14 ? 69   ARG H CA  1 
ATOM   8264  C  C   . ARG H  1 70  ? 149.790 24.997  9.540  1.00 37.87 ? 69   ARG H C   1 
ATOM   8265  O  O   . ARG H  1 70  ? 150.121 24.274  10.481 1.00 35.65 ? 69   ARG H O   1 
ATOM   8266  C  CB  . ARG H  1 70  ? 148.817 24.502  7.286  1.00 41.53 ? 69   ARG H CB  1 
ATOM   8267  C  CG  . ARG H  1 70  ? 149.057 24.293  5.795  1.00 44.95 ? 69   ARG H CG  1 
ATOM   8268  C  CD  . ARG H  1 70  ? 147.754 24.205  5.021  1.00 48.29 ? 69   ARG H CD  1 
ATOM   8269  N  NE  . ARG H  1 70  ? 147.983 24.117  3.580  1.00 51.12 ? 69   ARG H NE  1 
ATOM   8270  C  CZ  . ARG H  1 70  ? 147.027 23.917  2.676  1.00 52.63 ? 69   ARG H CZ  1 
ATOM   8271  N  NH1 . ARG H  1 70  ? 147.333 23.854  1.387  1.00 54.26 ? 69   ARG H NH1 1 
ATOM   8272  N  NH2 . ARG H  1 70  ? 145.765 23.775  3.058  1.00 53.39 ? 69   ARG H NH2 1 
ATOM   8273  N  N   . LYS H  1 71  ? 149.164 26.156  9.712  1.00 36.80 ? 70   LYS H N   1 
ATOM   8274  C  CA  . LYS H  1 71  ? 148.801 26.607  11.050 1.00 36.13 ? 70   LYS H CA  1 
ATOM   8275  C  C   . LYS H  1 71  ? 147.394 26.135  11.406 1.00 32.82 ? 70   LYS H C   1 
ATOM   8276  O  O   . LYS H  1 71  ? 146.609 25.785  10.533 1.00 29.87 ? 70   LYS H O   1 
ATOM   8277  C  CB  . LYS H  1 71  ? 148.896 28.131  11.149 1.00 38.60 ? 70   LYS H CB  1 
ATOM   8278  C  CG  . LYS H  1 71  ? 150.330 28.638  11.116 1.00 43.08 ? 70   LYS H CG  1 
ATOM   8279  C  CD  . LYS H  1 71  ? 150.437 30.057  11.648 1.00 47.56 ? 70   LYS H CD  1 
ATOM   8280  C  CE  . LYS H  1 71  ? 151.893 30.453  11.860 1.00 48.30 ? 70   LYS H CE  1 
ATOM   8281  N  NZ  . LYS H  1 71  ? 152.007 31.753  12.584 1.00 51.81 ? 70   LYS H NZ  1 
ATOM   8282  N  N   . HIS H  1 72  ? 147.086 26.129  12.698 1.00 33.53 ? 71   HIS H N   1 
ATOM   8283  C  CA  . HIS H  1 72  ? 145.785 25.681  13.186 1.00 30.74 ? 71   HIS H CA  1 
ATOM   8284  C  C   . HIS H  1 72  ? 144.626 26.594  12.782 1.00 32.55 ? 71   HIS H C   1 
ATOM   8285  O  O   . HIS H  1 72  ? 144.751 27.823  12.788 1.00 31.14 ? 71   HIS H O   1 
ATOM   8286  C  CB  . HIS H  1 72  ? 145.827 25.567  14.707 1.00 28.96 ? 71   HIS H CB  1 
ATOM   8287  C  CG  . HIS H  1 72  ? 144.540 25.105  15.311 1.00 28.75 ? 71   HIS H CG  1 
ATOM   8288  N  ND1 . HIS H  1 72  ? 144.179 23.777  15.378 1.00 25.44 ? 71   HIS H ND1 1 
ATOM   8289  C  CD2 . HIS H  1 72  ? 143.509 25.804  15.844 1.00 27.71 ? 71   HIS H CD2 1 
ATOM   8290  C  CE1 . HIS H  1 72  ? 142.982 23.676  15.924 1.00 25.45 ? 71   HIS H CE1 1 
ATOM   8291  N  NE2 . HIS H  1 72  ? 142.553 24.890  16.216 1.00 26.11 ? 71   HIS H NE2 1 
ATOM   8292  N  N   . GLY H  1 73  ? 143.494 25.981  12.444 1.00 30.99 ? 72   GLY H N   1 
ATOM   8293  C  CA  . GLY H  1 73  ? 142.320 26.740  12.057 1.00 27.94 ? 72   GLY H CA  1 
ATOM   8294  C  C   . GLY H  1 73  ? 141.041 25.956  12.297 1.00 27.41 ? 72   GLY H C   1 
ATOM   8295  O  O   . GLY H  1 73  ? 141.069 24.878  12.892 1.00 25.01 ? 72   GLY H O   1 
ATOM   8296  N  N   . GLY H  1 74  ? 139.917 26.506  11.851 1.00 22.74 ? 73   GLY H N   1 
ATOM   8297  C  CA  . GLY H  1 74  ? 138.645 25.828  12.005 1.00 24.37 ? 73   GLY H CA  1 
ATOM   8298  C  C   . GLY H  1 74  ? 138.472 24.885  10.831 1.00 25.11 ? 73   GLY H C   1 
ATOM   8299  O  O   . GLY H  1 74  ? 139.157 25.038  9.818  1.00 25.13 ? 73   GLY H O   1 
ATOM   8300  N  N   . PRO H  1 75  ? 137.565 23.906  10.921 1.00 26.91 ? 74   PRO H N   1 
ATOM   8301  C  CA  . PRO H  1 75  ? 137.385 22.981  9.800  1.00 29.18 ? 74   PRO H CA  1 
ATOM   8302  C  C   . PRO H  1 75  ? 137.085 23.640  8.455  1.00 31.49 ? 74   PRO H C   1 
ATOM   8303  O  O   . PRO H  1 75  ? 137.505 23.143  7.414  1.00 33.27 ? 74   PRO H O   1 
ATOM   8304  C  CB  . PRO H  1 75  ? 136.253 22.070  10.281 1.00 26.79 ? 74   PRO H CB  1 
ATOM   8305  C  CG  . PRO H  1 75  ? 135.508 22.918  11.255 1.00 28.42 ? 74   PRO H CG  1 
ATOM   8306  C  CD  . PRO H  1 75  ? 136.616 23.608  12.005 1.00 25.39 ? 74   PRO H CD  1 
ATOM   8307  N  N   . LYS H  1 76  ? 136.377 24.765  8.485  1.00 33.93 ? 75   LYS H N   1 
ATOM   8308  C  CA  . LYS H  1 76  ? 136.003 25.482  7.272  1.00 33.58 ? 75   LYS H CA  1 
ATOM   8309  C  C   . LYS H  1 76  ? 137.136 26.312  6.664  1.00 34.01 ? 75   LYS H C   1 
ATOM   8310  O  O   . LYS H  1 76  ? 137.006 26.810  5.547  1.00 32.91 ? 75   LYS H O   1 
ATOM   8311  C  CB  . LYS H  1 76  ? 134.805 26.389  7.571  1.00 37.03 ? 75   LYS H CB  1 
ATOM   8312  C  CG  . LYS H  1 76  ? 133.636 25.663  8.231  1.00 40.40 ? 75   LYS H CG  1 
ATOM   8313  C  CD  . LYS H  1 76  ? 132.651 26.624  8.905  1.00 42.97 ? 75   LYS H CD  1 
ATOM   8314  C  CE  . LYS H  1 76  ? 131.854 27.446  7.898  1.00 45.71 ? 75   LYS H CE  1 
ATOM   8315  N  NZ  . LYS H  1 76  ? 130.823 28.300  8.565  1.00 46.10 ? 75   LYS H NZ  1 
ATOM   8316  N  N   . ASP H  1 77  ? 138.245 26.455  7.386  1.00 34.09 ? 76   ASP H N   1 
ATOM   8317  C  CA  . ASP H  1 77  ? 139.379 27.245  6.894  1.00 34.89 ? 76   ASP H CA  1 
ATOM   8318  C  C   . ASP H  1 77  ? 140.289 26.503  5.928  1.00 36.67 ? 76   ASP H C   1 
ATOM   8319  O  O   . ASP H  1 77  ? 140.556 25.313  6.089  1.00 34.14 ? 76   ASP H O   1 
ATOM   8320  C  CB  . ASP H  1 77  ? 140.240 27.730  8.058  1.00 34.79 ? 76   ASP H CB  1 
ATOM   8321  C  CG  . ASP H  1 77  ? 139.506 28.675  8.975  1.00 35.20 ? 76   ASP H CG  1 
ATOM   8322  O  OD1 . ASP H  1 77  ? 139.892 28.742  10.160 1.00 31.53 ? 76   ASP H OD1 1 
ATOM   8323  O  OD2 . ASP H  1 77  ? 138.557 29.352  8.511  1.00 34.88 ? 76   ASP H OD2 1 
ATOM   8324  N  N   . GLU H  1 78  ? 140.781 27.226  4.929  1.00 37.46 ? 77   GLU H N   1 
ATOM   8325  C  CA  . GLU H  1 78  ? 141.690 26.652  3.955  1.00 39.20 ? 77   GLU H CA  1 
ATOM   8326  C  C   . GLU H  1 78  ? 142.984 26.385  4.726  1.00 37.61 ? 77   GLU H C   1 
ATOM   8327  O  O   . GLU H  1 78  ? 143.602 25.328  4.588  1.00 38.14 ? 77   GLU H O   1 
ATOM   8328  C  CB  . GLU H  1 78  ? 141.933 27.656  2.821  1.00 44.87 ? 77   GLU H CB  1 
ATOM   8329  C  CG  . GLU H  1 78  ? 142.239 27.027  1.471  1.00 52.63 ? 77   GLU H CG  1 
ATOM   8330  C  CD  . GLU H  1 78  ? 143.569 26.307  1.442  1.00 57.20 ? 77   GLU H CD  1 
ATOM   8331  O  OE1 . GLU H  1 78  ? 143.827 25.576  0.460  1.00 61.73 ? 77   GLU H OE1 1 
ATOM   8332  O  OE2 . GLU H  1 78  ? 144.361 26.476  2.392  1.00 59.96 ? 77   GLU H OE2 1 
ATOM   8333  N  N   . GLU H  1 79  ? 143.377 27.353  5.551  1.00 34.41 ? 78   GLU H N   1 
ATOM   8334  C  CA  . GLU H  1 79  ? 144.585 27.242  6.366  1.00 34.70 ? 78   GLU H CA  1 
ATOM   8335  C  C   . GLU H  1 79  ? 144.259 26.533  7.688  1.00 33.77 ? 78   GLU H C   1 
ATOM   8336  O  O   . GLU H  1 79  ? 143.644 27.116  8.588  1.00 32.04 ? 78   GLU H O   1 
ATOM   8337  C  CB  . GLU H  1 79  ? 145.156 28.638  6.657  1.00 35.35 ? 78   GLU H CB  1 
ATOM   8338  C  CG  . GLU H  1 79  ? 146.400 28.650  7.551  1.00 39.04 ? 78   GLU H CG  1 
ATOM   8339  C  CD  . GLU H  1 79  ? 147.655 28.135  6.852  1.00 40.59 ? 78   GLU H CD  1 
ATOM   8340  O  OE1 . GLU H  1 79  ? 148.725 28.104  7.500  1.00 40.77 ? 78   GLU H OE1 1 
ATOM   8341  O  OE2 . GLU H  1 79  ? 147.578 27.765  5.660  1.00 41.31 ? 78   GLU H OE2 1 
ATOM   8342  N  N   . ARG H  1 80  ? 144.676 25.277  7.796  1.00 33.15 ? 79   ARG H N   1 
ATOM   8343  C  CA  . ARG H  1 80  ? 144.431 24.487  8.996  1.00 33.47 ? 79   ARG H CA  1 
ATOM   8344  C  C   . ARG H  1 80  ? 145.206 23.186  8.953  1.00 33.36 ? 79   ARG H C   1 
ATOM   8345  O  O   . ARG H  1 80  ? 145.808 22.838  7.934  1.00 31.64 ? 79   ARG H O   1 
ATOM   8346  C  CB  . ARG H  1 80  ? 142.942 24.160  9.123  1.00 32.24 ? 79   ARG H CB  1 
ATOM   8347  C  CG  . ARG H  1 80  ? 142.372 23.428  7.912  1.00 35.04 ? 79   ARG H CG  1 
ATOM   8348  C  CD  . ARG H  1 80  ? 141.930 22.018  8.258  1.00 36.37 ? 79   ARG H CD  1 
ATOM   8349  N  NE  . ARG H  1 80  ? 140.546 21.797  7.875  1.00 34.62 ? 79   ARG H NE  1 
ATOM   8350  C  CZ  . ARG H  1 80  ? 139.878 20.658  8.035  1.00 33.02 ? 79   ARG H CZ  1 
ATOM   8351  N  NH1 . ARG H  1 80  ? 138.617 20.592  7.642  1.00 31.58 ? 79   ARG H NH1 1 
ATOM   8352  N  NH2 . ARG H  1 80  ? 140.454 19.593  8.574  1.00 31.82 ? 79   ARG H NH2 1 
ATOM   8353  N  N   . HIS H  1 81  ? 145.191 22.475  10.074 1.00 31.77 ? 80   HIS H N   1 
ATOM   8354  C  CA  . HIS H  1 81  ? 145.852 21.184  10.172 1.00 30.93 ? 80   HIS H CA  1 
ATOM   8355  C  C   . HIS H  1 81  ? 144.834 20.210  9.615  1.00 29.87 ? 80   HIS H C   1 
ATOM   8356  O  O   . HIS H  1 81  ? 143.635 20.472  9.677  1.00 30.01 ? 80   HIS H O   1 
ATOM   8357  C  CB  . HIS H  1 81  ? 146.120 20.835  11.631 1.00 31.73 ? 80   HIS H CB  1 
ATOM   8358  C  CG  . HIS H  1 81  ? 146.991 21.821  12.345 1.00 33.00 ? 80   HIS H CG  1 
ATOM   8359  N  ND1 . HIS H  1 81  ? 146.990 21.952  13.709 1.00 34.31 ? 80   HIS H ND1 1 
ATOM   8360  C  CD2 . HIS H  1 81  ? 147.914 22.695  11.872 1.00 33.77 ? 80   HIS H CD2 1 
ATOM   8361  C  CE1 . HIS H  1 81  ? 147.882 22.872  14.062 1.00 34.90 ? 80   HIS H CE1 1 
ATOM   8362  N  NE2 . HIS H  1 81  ? 148.450 23.331  12.968 1.00 35.85 ? 80   HIS H NE2 1 
ATOM   8363  N  N   . VAL H  1 82  ? 145.292 19.089  9.073  1.00 29.82 ? 81   VAL H N   1 
ATOM   8364  C  CA  . VAL H  1 82  ? 144.358 18.105  8.543  1.00 29.30 ? 81   VAL H CA  1 
ATOM   8365  C  C   . VAL H  1 82  ? 143.425 17.588  9.641  1.00 29.33 ? 81   VAL H C   1 
ATOM   8366  O  O   . VAL H  1 82  ? 142.252 17.310  9.389  1.00 30.41 ? 81   VAL H O   1 
ATOM   8367  C  CB  . VAL H  1 82  ? 145.108 16.909  7.908  1.00 30.49 ? 81   VAL H CB  1 
ATOM   8368  C  CG1 . VAL H  1 82  ? 144.120 15.789  7.569  1.00 29.99 ? 81   VAL H CG1 1 
ATOM   8369  C  CG2 . VAL H  1 82  ? 145.829 17.372  6.636  1.00 29.42 ? 81   VAL H CG2 1 
ATOM   8370  N  N   . GLY H  1 83  ? 143.941 17.482  10.862 1.00 29.12 ? 82   GLY H N   1 
ATOM   8371  C  CA  . GLY H  1 83  ? 143.134 16.976  11.963 1.00 28.51 ? 82   GLY H CA  1 
ATOM   8372  C  C   . GLY H  1 83  ? 142.234 17.966  12.686 1.00 27.99 ? 82   GLY H C   1 
ATOM   8373  O  O   . GLY H  1 83  ? 141.625 17.616  13.700 1.00 25.49 ? 82   GLY H O   1 
ATOM   8374  N  N   . ASP H  1 84  ? 142.139 19.193  12.177 1.00 27.56 ? 83   ASP H N   1 
ATOM   8375  C  CA  . ASP H  1 84  ? 141.306 20.214  12.808 1.00 26.97 ? 83   ASP H CA  1 
ATOM   8376  C  C   . ASP H  1 84  ? 139.819 20.025  12.512 1.00 28.54 ? 83   ASP H C   1 
ATOM   8377  O  O   . ASP H  1 84  ? 139.320 20.453  11.465 1.00 27.10 ? 83   ASP H O   1 
ATOM   8378  C  CB  . ASP H  1 84  ? 141.739 21.615  12.360 1.00 27.02 ? 83   ASP H CB  1 
ATOM   8379  C  CG  . ASP H  1 84  ? 143.140 21.966  12.811 1.00 28.51 ? 83   ASP H CG  1 
ATOM   8380  O  OD1 . ASP H  1 84  ? 143.679 21.274  13.706 1.00 27.14 ? 83   ASP H OD1 1 
ATOM   8381  O  OD2 . ASP H  1 84  ? 143.699 22.946  12.279 1.00 26.86 ? 83   ASP H OD2 1 
ATOM   8382  N  N   . LEU H  1 85  ? 139.112 19.398  13.448 1.00 26.74 ? 84   LEU H N   1 
ATOM   8383  C  CA  . LEU H  1 85  ? 137.690 19.152  13.283 1.00 27.21 ? 84   LEU H CA  1 
ATOM   8384  C  C   . LEU H  1 85  ? 136.832 20.147  14.060 1.00 26.87 ? 84   LEU H C   1 
ATOM   8385  O  O   . LEU H  1 85  ? 135.623 19.957  14.205 1.00 26.43 ? 84   LEU H O   1 
ATOM   8386  C  CB  . LEU H  1 85  ? 137.356 17.712  13.701 1.00 27.73 ? 84   LEU H CB  1 
ATOM   8387  C  CG  . LEU H  1 85  ? 137.970 16.646  12.777 1.00 28.43 ? 84   LEU H CG  1 
ATOM   8388  C  CD1 . LEU H  1 85  ? 137.672 15.241  13.298 1.00 31.20 ? 84   LEU H CD1 1 
ATOM   8389  C  CD2 . LEU H  1 85  ? 137.411 16.816  11.370 1.00 29.53 ? 84   LEU H CD2 1 
ATOM   8390  N  N   . GLY H  1 86  ? 137.466 21.205  14.564 1.00 24.34 ? 85   GLY H N   1 
ATOM   8391  C  CA  . GLY H  1 86  ? 136.738 22.225  15.297 1.00 23.83 ? 85   GLY H CA  1 
ATOM   8392  C  C   . GLY H  1 86  ? 136.308 21.858  16.703 1.00 24.37 ? 85   GLY H C   1 
ATOM   8393  O  O   . GLY H  1 86  ? 137.112 21.420  17.527 1.00 25.09 ? 85   GLY H O   1 
ATOM   8394  N  N   . ASN H  1 87  ? 135.026 22.054  16.978 1.00 25.25 ? 86   ASN H N   1 
ATOM   8395  C  CA  . ASN H  1 87  ? 134.454 21.754  18.284 1.00 26.64 ? 86   ASN H CA  1 
ATOM   8396  C  C   . ASN H  1 87  ? 133.277 20.805  18.154 1.00 25.64 ? 86   ASN H C   1 
ATOM   8397  O  O   . ASN H  1 87  ? 132.730 20.616  17.068 1.00 23.72 ? 86   ASN H O   1 
ATOM   8398  C  CB  . ASN H  1 87  ? 133.921 23.025  18.953 1.00 27.20 ? 86   ASN H CB  1 
ATOM   8399  C  CG  . ASN H  1 87  ? 135.013 23.968  19.386 1.00 29.22 ? 86   ASN H CG  1 
ATOM   8400  O  OD1 . ASN H  1 87  ? 135.823 23.640  20.251 1.00 27.37 ? 86   ASN H OD1 1 
ATOM   8401  N  ND2 . ASN H  1 87  ? 135.040 25.155  18.785 1.00 28.18 ? 86   ASN H ND2 1 
ATOM   8402  N  N   . VAL H  1 88  ? 132.913 20.209  19.281 1.00 24.98 ? 87   VAL H N   1 
ATOM   8403  C  CA  . VAL H  1 88  ? 131.743 19.351  19.378 1.00 25.89 ? 87   VAL H CA  1 
ATOM   8404  C  C   . VAL H  1 88  ? 131.040 19.989  20.563 1.00 26.71 ? 87   VAL H C   1 
ATOM   8405  O  O   . VAL H  1 88  ? 131.690 20.602  21.420 1.00 27.04 ? 87   VAL H O   1 
ATOM   8406  C  CB  . VAL H  1 88  ? 132.083 17.860  19.673 1.00 25.58 ? 87   VAL H CB  1 
ATOM   8407  C  CG1 . VAL H  1 88  ? 132.670 17.211  18.417 1.00 27.16 ? 87   VAL H CG1 1 
ATOM   8408  C  CG2 . VAL H  1 88  ? 133.042 17.744  20.838 1.00 23.83 ? 87   VAL H CG2 1 
ATOM   8409  N  N   . THR H  1 89  ? 129.721 19.876  20.606 1.00 27.08 ? 88   THR H N   1 
ATOM   8410  C  CA  . THR H  1 89  ? 128.958 20.495  21.674 1.00 27.94 ? 88   THR H CA  1 
ATOM   8411  C  C   . THR H  1 89  ? 128.201 19.492  22.528 1.00 28.43 ? 88   THR H C   1 
ATOM   8412  O  O   . THR H  1 89  ? 127.474 18.640  22.010 1.00 27.74 ? 88   THR H O   1 
ATOM   8413  C  CB  . THR H  1 89  ? 127.959 21.506  21.093 1.00 27.04 ? 88   THR H CB  1 
ATOM   8414  O  OG1 . THR H  1 89  ? 128.670 22.472  20.310 1.00 28.81 ? 88   THR H OG1 1 
ATOM   8415  C  CG2 . THR H  1 89  ? 127.188 22.210  22.211 1.00 28.95 ? 88   THR H CG2 1 
ATOM   8416  N  N   . ALA H  1 90  ? 128.378 19.608  23.841 1.00 28.57 ? 89   ALA H N   1 
ATOM   8417  C  CA  . ALA H  1 90  ? 127.713 18.735  24.797 1.00 28.37 ? 89   ALA H CA  1 
ATOM   8418  C  C   . ALA H  1 90  ? 126.497 19.467  25.354 1.00 30.47 ? 89   ALA H C   1 
ATOM   8419  O  O   . ALA H  1 90  ? 126.556 20.673  25.612 1.00 31.16 ? 89   ALA H O   1 
ATOM   8420  C  CB  . ALA H  1 90  ? 128.672 18.371  25.926 1.00 28.60 ? 89   ALA H CB  1 
ATOM   8421  N  N   . ASP H  1 91  ? 125.394 18.744  25.531 1.00 30.91 ? 90   ASP H N   1 
ATOM   8422  C  CA  . ASP H  1 91  ? 124.171 19.342  26.054 1.00 32.31 ? 90   ASP H CA  1 
ATOM   8423  C  C   . ASP H  1 91  ? 124.228 19.420  27.580 1.00 33.48 ? 90   ASP H C   1 
ATOM   8424  O  O   . ASP H  1 91  ? 125.249 19.085  28.181 1.00 34.13 ? 90   ASP H O   1 
ATOM   8425  C  CB  . ASP H  1 91  ? 122.947 18.538  25.584 1.00 33.28 ? 90   ASP H CB  1 
ATOM   8426  C  CG  . ASP H  1 91  ? 122.947 17.105  26.095 1.00 32.63 ? 90   ASP H CG  1 
ATOM   8427  O  OD1 . ASP H  1 91  ? 122.239 16.265  25.497 1.00 31.99 ? 90   ASP H OD1 1 
ATOM   8428  O  OD2 . ASP H  1 91  ? 123.638 16.821  27.096 1.00 30.13 ? 90   ASP H OD2 1 
ATOM   8429  N  N   . LYS H  1 92  ? 123.139 19.862  28.205 1.00 35.70 ? 91   LYS H N   1 
ATOM   8430  C  CA  . LYS H  1 92  ? 123.107 20.003  29.660 1.00 37.03 ? 91   LYS H CA  1 
ATOM   8431  C  C   . LYS H  1 92  ? 123.309 18.693  30.412 1.00 36.91 ? 91   LYS H C   1 
ATOM   8432  O  O   . LYS H  1 92  ? 123.625 18.696  31.601 1.00 37.18 ? 91   LYS H O   1 
ATOM   8433  C  CB  . LYS H  1 92  ? 121.798 20.661  30.108 1.00 40.25 ? 91   LYS H CB  1 
ATOM   8434  C  CG  . LYS H  1 92  ? 120.544 19.864  29.812 1.00 43.11 ? 91   LYS H CG  1 
ATOM   8435  C  CD  . LYS H  1 92  ? 119.326 20.585  30.357 0.00 44.63 ? 91   LYS H CD  1 
ATOM   8436  C  CE  . LYS H  1 92  ? 118.054 19.799  30.117 0.00 45.97 ? 91   LYS H CE  1 
ATOM   8437  N  NZ  . LYS H  1 92  ? 116.884 20.513  30.691 1.00 48.81 ? 91   LYS H NZ  1 
ATOM   8438  N  N   . ASP H  1 93  ? 123.127 17.574  29.720 1.00 36.32 ? 92   ASP H N   1 
ATOM   8439  C  CA  . ASP H  1 93  ? 123.312 16.268  30.333 1.00 35.97 ? 92   ASP H CA  1 
ATOM   8440  C  C   . ASP H  1 93  ? 124.731 15.765  30.115 1.00 33.40 ? 92   ASP H C   1 
ATOM   8441  O  O   . ASP H  1 93  ? 125.049 14.627  30.451 1.00 32.31 ? 92   ASP H O   1 
ATOM   8442  C  CB  . ASP H  1 93  ? 122.302 15.273  29.767 1.00 37.12 ? 92   ASP H CB  1 
ATOM   8443  C  CG  . ASP H  1 93  ? 120.901 15.526  30.277 1.00 38.91 ? 92   ASP H CG  1 
ATOM   8444  O  OD1 . ASP H  1 93  ? 119.946 14.947  29.723 1.00 43.10 ? 92   ASP H OD1 1 
ATOM   8445  O  OD2 . ASP H  1 93  ? 120.756 16.302  31.244 1.00 40.40 ? 92   ASP H OD2 1 
ATOM   8446  N  N   . GLY H  1 94  ? 125.578 16.623  29.550 1.00 29.82 ? 93   GLY H N   1 
ATOM   8447  C  CA  . GLY H  1 94  ? 126.960 16.248  29.308 1.00 28.49 ? 93   GLY H CA  1 
ATOM   8448  C  C   . GLY H  1 94  ? 127.181 15.341  28.110 1.00 27.92 ? 93   GLY H C   1 
ATOM   8449  O  O   . GLY H  1 94  ? 128.242 14.730  27.981 1.00 28.51 ? 93   GLY H O   1 
ATOM   8450  N  N   . VAL H  1 95  ? 126.192 15.255  27.225 1.00 27.71 ? 94   VAL H N   1 
ATOM   8451  C  CA  . VAL H  1 95  ? 126.314 14.408  26.046 1.00 25.79 ? 94   VAL H CA  1 
ATOM   8452  C  C   . VAL H  1 95  ? 126.509 15.177  24.740 1.00 26.08 ? 94   VAL H C   1 
ATOM   8453  O  O   . VAL H  1 95  ? 125.781 16.127  24.440 1.00 26.86 ? 94   VAL H O   1 
ATOM   8454  C  CB  . VAL H  1 95  ? 125.079 13.496  25.893 1.00 28.51 ? 94   VAL H CB  1 
ATOM   8455  C  CG1 . VAL H  1 95  ? 125.163 12.706  24.577 1.00 26.64 ? 94   VAL H CG1 1 
ATOM   8456  C  CG2 . VAL H  1 95  ? 124.995 12.538  27.089 1.00 24.40 ? 94   VAL H CG2 1 
ATOM   8457  N  N   . ALA H  1 96  ? 127.501 14.757  23.965 1.00 26.32 ? 95   ALA H N   1 
ATOM   8458  C  CA  . ALA H  1 96  ? 127.775 15.377  22.678 1.00 26.68 ? 95   ALA H CA  1 
ATOM   8459  C  C   . ALA H  1 96  ? 127.380 14.416  21.555 1.00 28.83 ? 95   ALA H C   1 
ATOM   8460  O  O   . ALA H  1 96  ? 128.059 13.411  21.319 1.00 29.56 ? 95   ALA H O   1 
ATOM   8461  C  CB  . ALA H  1 96  ? 129.253 15.724  22.565 1.00 28.08 ? 95   ALA H CB  1 
ATOM   8462  N  N   . ASP H  1 97  ? 126.277 14.714  20.877 1.00 28.69 ? 96   ASP H N   1 
ATOM   8463  C  CA  . ASP H  1 97  ? 125.835 13.884  19.762 1.00 31.29 ? 96   ASP H CA  1 
ATOM   8464  C  C   . ASP H  1 97  ? 126.536 14.406  18.516 1.00 29.77 ? 96   ASP H C   1 
ATOM   8465  O  O   . ASP H  1 97  ? 125.991 15.213  17.762 1.00 30.47 ? 96   ASP H O   1 
ATOM   8466  C  CB  . ASP H  1 97  ? 124.316 13.962  19.614 1.00 34.40 ? 96   ASP H CB  1 
ATOM   8467  C  CG  . ASP H  1 97  ? 123.594 13.075  20.616 1.00 37.22 ? 96   ASP H CG  1 
ATOM   8468  O  OD1 . ASP H  1 97  ? 122.445 13.401  20.985 1.00 39.78 ? 96   ASP H OD1 1 
ATOM   8469  O  OD2 . ASP H  1 97  ? 124.179 12.044  21.022 1.00 37.06 ? 96   ASP H OD2 1 
ATOM   8470  N  N   . VAL H  1 98  ? 127.754 13.919  18.314 1.00 30.68 ? 97   VAL H N   1 
ATOM   8471  C  CA  . VAL H  1 98  ? 128.599 14.335  17.207 1.00 30.93 ? 97   VAL H CA  1 
ATOM   8472  C  C   . VAL H  1 98  ? 128.068 14.082  15.804 1.00 32.71 ? 97   VAL H C   1 
ATOM   8473  O  O   . VAL H  1 98  ? 127.656 12.970  15.449 1.00 29.44 ? 97   VAL H O   1 
ATOM   8474  C  CB  . VAL H  1 98  ? 130.001 13.693  17.327 1.00 31.93 ? 97   VAL H CB  1 
ATOM   8475  C  CG1 . VAL H  1 98  ? 130.876 14.122  16.160 1.00 33.69 ? 97   VAL H CG1 1 
ATOM   8476  C  CG2 . VAL H  1 98  ? 130.646 14.105  18.649 1.00 29.25 ? 97   VAL H CG2 1 
ATOM   8477  N  N   . SER H  1 99  ? 128.089 15.137  15.001 1.00 33.36 ? 98   SER H N   1 
ATOM   8478  C  CA  . SER H  1 99  ? 127.644 15.046  13.624 1.00 36.15 ? 98   SER H CA  1 
ATOM   8479  C  C   . SER H  1 99  ? 128.465 16.053  12.841 1.00 37.47 ? 98   SER H C   1 
ATOM   8480  O  O   . SER H  1 99  ? 128.205 17.257  12.888 1.00 38.81 ? 98   SER H O   1 
ATOM   8481  C  CB  . SER H  1 99  ? 126.154 15.362  13.512 1.00 37.76 ? 98   SER H CB  1 
ATOM   8482  O  OG  . SER H  1 99  ? 125.688 15.095  12.202 1.00 40.85 ? 98   SER H OG  1 
ATOM   8483  N  N   . ILE H  1 100 ? 129.467 15.547  12.132 1.00 35.66 ? 99   ILE H N   1 
ATOM   8484  C  CA  . ILE H  1 100 ? 130.362 16.385  11.351 1.00 36.73 ? 99   ILE H CA  1 
ATOM   8485  C  C   . ILE H  1 100 ? 130.659 15.741  10.009 1.00 36.91 ? 99   ILE H C   1 
ATOM   8486  O  O   . ILE H  1 100 ? 130.643 14.518  9.880  1.00 37.10 ? 99   ILE H O   1 
ATOM   8487  C  CB  . ILE H  1 100 ? 131.711 16.576  12.089 1.00 37.15 ? 99   ILE H CB  1 
ATOM   8488  C  CG1 . ILE H  1 100 ? 131.481 17.255  13.440 1.00 37.21 ? 99   ILE H CG1 1 
ATOM   8489  C  CG2 . ILE H  1 100 ? 132.674 17.390  11.231 1.00 39.04 ? 99   ILE H CG2 1 
ATOM   8490  C  CD1 . ILE H  1 100 ? 132.724 17.307  14.308 1.00 38.14 ? 99   ILE H CD1 1 
ATOM   8491  N  N   . GLU H  1 101 ? 130.914 16.571  9.007  1.00 35.98 ? 100  GLU H N   1 
ATOM   8492  C  CA  . GLU H  1 101 ? 131.276 16.082  7.685  1.00 36.24 ? 100  GLU H CA  1 
ATOM   8493  C  C   . GLU H  1 101 ? 132.490 16.915  7.310  1.00 35.42 ? 100  GLU H C   1 
ATOM   8494  O  O   . GLU H  1 101 ? 132.425 18.148  7.296  1.00 34.49 ? 100  GLU H O   1 
ATOM   8495  C  CB  . GLU H  1 101 ? 130.143 16.288  6.677  1.00 38.15 ? 100  GLU H CB  1 
ATOM   8496  C  CG  . GLU H  1 101 ? 130.457 15.716  5.300  1.00 43.80 ? 100  GLU H CG  1 
ATOM   8497  C  CD  . GLU H  1 101 ? 129.280 15.786  4.342  1.00 48.54 ? 100  GLU H CD  1 
ATOM   8498  O  OE1 . GLU H  1 101 ? 128.263 15.099  4.595  1.00 48.67 ? 100  GLU H OE1 1 
ATOM   8499  O  OE2 . GLU H  1 101 ? 129.372 16.532  3.338  1.00 49.52 ? 100  GLU H OE2 1 
ATOM   8500  N  N   . ASP H  1 102 ? 133.604 16.246  7.039  1.00 31.66 ? 101  ASP H N   1 
ATOM   8501  C  CA  . ASP H  1 102 ? 134.838 16.939  6.704  1.00 32.24 ? 101  ASP H CA  1 
ATOM   8502  C  C   . ASP H  1 102 ? 135.440 16.362  5.430  1.00 33.81 ? 101  ASP H C   1 
ATOM   8503  O  O   . ASP H  1 102 ? 135.476 15.143  5.247  1.00 32.57 ? 101  ASP H O   1 
ATOM   8504  C  CB  . ASP H  1 102 ? 135.825 16.822  7.874  1.00 29.37 ? 101  ASP H CB  1 
ATOM   8505  C  CG  . ASP H  1 102 ? 136.993 17.781  7.751  1.00 30.05 ? 101  ASP H CG  1 
ATOM   8506  O  OD1 . ASP H  1 102 ? 138.046 17.384  7.206  1.00 27.23 ? 101  ASP H OD1 1 
ATOM   8507  O  OD2 . ASP H  1 102 ? 136.846 18.940  8.194  1.00 27.64 ? 101  ASP H OD2 1 
ATOM   8508  N  N   . SER H  1 103 ? 135.909 17.243  4.550  1.00 33.80 ? 102  SER H N   1 
ATOM   8509  C  CA  . SER H  1 103 ? 136.484 16.812  3.283  1.00 36.25 ? 102  SER H CA  1 
ATOM   8510  C  C   . SER H  1 103 ? 138.002 16.933  3.230  1.00 35.99 ? 102  SER H C   1 
ATOM   8511  O  O   . SER H  1 103 ? 138.599 16.794  2.160  1.00 36.99 ? 102  SER H O   1 
ATOM   8512  C  CB  . SER H  1 103 ? 135.874 17.620  2.136  1.00 37.68 ? 102  SER H CB  1 
ATOM   8513  O  OG  . SER H  1 103 ? 136.286 18.975  2.210  1.00 44.03 ? 102  SER H OG  1 
ATOM   8514  N  N   . VAL H  1 104 ? 138.624 17.201  4.374  1.00 35.03 ? 103  VAL H N   1 
ATOM   8515  C  CA  . VAL H  1 104 ? 140.076 17.328  4.431  1.00 35.07 ? 103  VAL H CA  1 
ATOM   8516  C  C   . VAL H  1 104 ? 140.692 16.045  4.987  1.00 35.51 ? 103  VAL H C   1 
ATOM   8517  O  O   . VAL H  1 104 ? 141.717 15.575  4.488  1.00 34.61 ? 103  VAL H O   1 
ATOM   8518  C  CB  . VAL H  1 104 ? 140.511 18.536  5.297  1.00 35.69 ? 103  VAL H CB  1 
ATOM   8519  C  CG1 . VAL H  1 104 ? 142.032 18.586  5.401  1.00 34.80 ? 103  VAL H CG1 1 
ATOM   8520  C  CG2 . VAL H  1 104 ? 139.994 19.830  4.671  1.00 36.94 ? 103  VAL H CG2 1 
ATOM   8521  N  N   . ILE H  1 105 ? 140.075 15.481  6.023  1.00 34.02 ? 104  ILE H N   1 
ATOM   8522  C  CA  . ILE H  1 105 ? 140.581 14.234  6.578  1.00 32.40 ? 104  ILE H CA  1 
ATOM   8523  C  C   . ILE H  1 105 ? 140.184 13.127  5.609  1.00 33.15 ? 104  ILE H C   1 
ATOM   8524  O  O   . ILE H  1 105 ? 139.266 13.300  4.802  1.00 31.80 ? 104  ILE H O   1 
ATOM   8525  C  CB  . ILE H  1 105 ? 139.970 13.905  7.965  1.00 30.97 ? 104  ILE H CB  1 
ATOM   8526  C  CG1 . ILE H  1 105 ? 138.445 13.815  7.869  1.00 28.69 ? 104  ILE H CG1 1 
ATOM   8527  C  CG2 . ILE H  1 105 ? 140.393 14.947  8.984  1.00 29.22 ? 104  ILE H CG2 1 
ATOM   8528  C  CD1 . ILE H  1 105 ? 137.779 13.372  9.180  1.00 29.28 ? 104  ILE H CD1 1 
ATOM   8529  N  N   . SER H  1 106 ? 140.883 12.001  5.683  1.00 33.74 ? 105  SER H N   1 
ATOM   8530  C  CA  . SER H  1 106 ? 140.594 10.857  4.827  1.00 35.61 ? 105  SER H CA  1 
ATOM   8531  C  C   . SER H  1 106 ? 140.889 9.558   5.578  1.00 36.39 ? 105  SER H C   1 
ATOM   8532  O  O   . SER H  1 106 ? 141.581 9.566   6.602  1.00 36.21 ? 105  SER H O   1 
ATOM   8533  C  CB  . SER H  1 106 ? 141.441 10.919  3.553  1.00 36.49 ? 105  SER H CB  1 
ATOM   8534  O  OG  . SER H  1 106 ? 141.155 9.826   2.693  1.00 35.07 ? 105  SER H OG  1 
ATOM   8535  N  N   . LEU H  1 107 ? 140.359 8.449   5.067  1.00 36.06 ? 106  LEU H N   1 
ATOM   8536  C  CA  . LEU H  1 107 ? 140.575 7.144   5.679  1.00 37.48 ? 106  LEU H CA  1 
ATOM   8537  C  C   . LEU H  1 107 ? 141.525 6.322   4.814  1.00 39.85 ? 106  LEU H C   1 
ATOM   8538  O  O   . LEU H  1 107 ? 141.540 5.091   4.872  1.00 39.33 ? 106  LEU H O   1 
ATOM   8539  C  CB  . LEU H  1 107 ? 139.240 6.408   5.865  1.00 35.11 ? 106  LEU H CB  1 
ATOM   8540  C  CG  . LEU H  1 107 ? 138.178 7.164   6.677  1.00 33.99 ? 106  LEU H CG  1 
ATOM   8541  C  CD1 . LEU H  1 107 ? 136.983 6.263   6.932  1.00 32.12 ? 106  LEU H CD1 1 
ATOM   8542  C  CD2 . LEU H  1 107 ? 138.771 7.643   7.995  1.00 30.28 ? 106  LEU H CD2 1 
ATOM   8543  N  N   . SER H  1 108 ? 142.322 7.028   4.019  1.00 42.09 ? 107  SER H N   1 
ATOM   8544  C  CA  . SER H  1 108 ? 143.309 6.420   3.134  1.00 44.51 ? 107  SER H CA  1 
ATOM   8545  C  C   . SER H  1 108 ? 144.217 7.531   2.605  1.00 45.28 ? 107  SER H C   1 
ATOM   8546  O  O   . SER H  1 108 ? 143.843 8.701   2.628  1.00 44.39 ? 107  SER H O   1 
ATOM   8547  C  CB  . SER H  1 108 ? 142.611 5.703   1.974  1.00 44.53 ? 107  SER H CB  1 
ATOM   8548  O  OG  . SER H  1 108 ? 141.767 6.593   1.265  1.00 49.02 ? 107  SER H OG  1 
ATOM   8549  N  N   . GLY H  1 109 ? 145.407 7.169   2.137  1.00 47.27 ? 108  GLY H N   1 
ATOM   8550  C  CA  . GLY H  1 109 ? 146.330 8.170   1.625  1.00 49.36 ? 108  GLY H CA  1 
ATOM   8551  C  C   . GLY H  1 109 ? 147.146 8.803   2.741  1.00 51.34 ? 108  GLY H C   1 
ATOM   8552  O  O   . GLY H  1 109 ? 146.988 8.442   3.910  1.00 51.60 ? 108  GLY H O   1 
ATOM   8553  N  N   . ASP H  1 110 ? 148.020 9.747   2.395  1.00 51.77 ? 109  ASP H N   1 
ATOM   8554  C  CA  . ASP H  1 110 ? 148.848 10.404  3.404  1.00 52.26 ? 109  ASP H CA  1 
ATOM   8555  C  C   . ASP H  1 110 ? 148.010 11.223  4.378  1.00 51.68 ? 109  ASP H C   1 
ATOM   8556  O  O   . ASP H  1 110 ? 148.435 11.473  5.505  1.00 53.64 ? 109  ASP H O   1 
ATOM   8557  C  CB  . ASP H  1 110 ? 149.899 11.304  2.749  0.00 52.82 ? 109  ASP H CB  1 
ATOM   8558  C  CG  . ASP H  1 110 ? 150.925 10.520  1.957  0.00 53.44 ? 109  ASP H CG  1 
ATOM   8559  O  OD1 . ASP H  1 110 ? 151.499 9.559   2.510  0.00 53.69 ? 109  ASP H OD1 1 
ATOM   8560  O  OD2 . ASP H  1 110 ? 151.163 10.870  0.784  1.00 54.59 ? 109  ASP H OD2 1 
ATOM   8561  N  N   . HIS H  1 111 ? 146.825 11.644  3.944  1.00 49.93 ? 110  HIS H N   1 
ATOM   8562  C  CA  . HIS H  1 111 ? 145.931 12.421  4.799  1.00 48.45 ? 110  HIS H CA  1 
ATOM   8563  C  C   . HIS H  1 111 ? 145.030 11.501  5.621  1.00 45.75 ? 110  HIS H C   1 
ATOM   8564  O  O   . HIS H  1 111 ? 144.090 11.959  6.277  1.00 43.33 ? 110  HIS H O   1 
ATOM   8565  C  CB  . HIS H  1 111 ? 145.066 13.372  3.961  1.00 50.80 ? 110  HIS H CB  1 
ATOM   8566  C  CG  . HIS H  1 111 ? 145.830 14.495  3.328  1.00 53.65 ? 110  HIS H CG  1 
ATOM   8567  N  ND1 . HIS H  1 111 ? 145.216 15.542  2.681  1.00 54.05 ? 110  HIS H ND1 1 
ATOM   8568  C  CD2 . HIS H  1 111 ? 147.164 14.735  3.248  1.00 54.25 ? 110  HIS H CD2 1 
ATOM   8569  C  CE1 . HIS H  1 111 ? 146.132 16.383  2.230  1.00 54.82 ? 110  HIS H CE1 1 
ATOM   8570  N  NE2 . HIS H  1 111 ? 147.322 15.913  2.563  1.00 55.09 ? 110  HIS H NE2 1 
ATOM   8571  N  N   . SER H  1 112 ? 145.321 10.203  5.583  1.00 42.62 ? 111  SER H N   1 
ATOM   8572  C  CA  . SER H  1 112 ? 144.530 9.227   6.326  1.00 41.00 ? 111  SER H CA  1 
ATOM   8573  C  C   . SER H  1 112 ? 144.712 9.403   7.825  1.00 39.27 ? 111  SER H C   1 
ATOM   8574  O  O   . SER H  1 112 ? 145.818 9.660   8.300  1.00 38.53 ? 111  SER H O   1 
ATOM   8575  C  CB  . SER H  1 112 ? 144.927 7.803   5.938  1.00 41.55 ? 111  SER H CB  1 
ATOM   8576  O  OG  . SER H  1 112 ? 144.177 6.856   6.681  1.00 42.10 ? 111  SER H OG  1 
ATOM   8577  N  N   . ILE H  1 113 ? 143.621 9.261   8.570  1.00 38.07 ? 112  ILE H N   1 
ATOM   8578  C  CA  . ILE H  1 113 ? 143.677 9.403   10.015 1.00 36.27 ? 112  ILE H CA  1 
ATOM   8579  C  C   . ILE H  1 113 ? 143.734 8.032   10.678 1.00 36.55 ? 112  ILE H C   1 
ATOM   8580  O  O   . ILE H  1 113 ? 143.752 7.925   11.905 1.00 35.25 ? 112  ILE H O   1 
ATOM   8581  C  CB  . ILE H  1 113 ? 142.456 10.186  10.545 1.00 36.31 ? 112  ILE H CB  1 
ATOM   8582  C  CG1 . ILE H  1 113 ? 141.162 9.481   10.135 1.00 34.27 ? 112  ILE H CG1 1 
ATOM   8583  C  CG2 . ILE H  1 113 ? 142.483 11.615  9.997  1.00 34.73 ? 112  ILE H CG2 1 
ATOM   8584  C  CD1 . ILE H  1 113 ? 139.915 10.142  10.683 1.00 33.96 ? 112  ILE H CD1 1 
ATOM   8585  N  N   . ILE H  1 114 ? 143.771 6.986   9.856  1.00 35.53 ? 113  ILE H N   1 
ATOM   8586  C  CA  . ILE H  1 114 ? 143.837 5.617   10.364 1.00 33.56 ? 113  ILE H CA  1 
ATOM   8587  C  C   . ILE H  1 114 ? 145.136 5.441   11.144 1.00 32.58 ? 113  ILE H C   1 
ATOM   8588  O  O   . ILE H  1 114 ? 146.211 5.792   10.653 1.00 32.66 ? 113  ILE H O   1 
ATOM   8589  C  CB  . ILE H  1 114 ? 143.828 4.571   9.212  1.00 33.40 ? 113  ILE H CB  1 
ATOM   8590  C  CG1 . ILE H  1 114 ? 142.558 4.712   8.359  1.00 33.57 ? 113  ILE H CG1 1 
ATOM   8591  C  CG2 . ILE H  1 114 ? 143.943 3.160   9.795  1.00 32.76 ? 113  ILE H CG2 1 
ATOM   8592  C  CD1 . ILE H  1 114 ? 141.266 4.388   9.085  1.00 34.76 ? 113  ILE H CD1 1 
ATOM   8593  N  N   . GLY H  1 115 ? 145.035 4.901   12.354 1.00 29.42 ? 114  GLY H N   1 
ATOM   8594  C  CA  . GLY H  1 115 ? 146.220 4.681   13.164 1.00 30.78 ? 114  GLY H CA  1 
ATOM   8595  C  C   . GLY H  1 115 ? 146.675 5.894   13.956 1.00 31.55 ? 114  GLY H C   1 
ATOM   8596  O  O   . GLY H  1 115 ? 147.732 5.873   14.592 1.00 28.89 ? 114  GLY H O   1 
ATOM   8597  N  N   . ARG H  1 116 ? 145.884 6.960   13.914 1.00 29.71 ? 115  ARG H N   1 
ATOM   8598  C  CA  . ARG H  1 116 ? 146.226 8.166   14.649 1.00 29.92 ? 115  ARG H CA  1 
ATOM   8599  C  C   . ARG H  1 116 ? 145.273 8.299   15.833 1.00 30.13 ? 115  ARG H C   1 
ATOM   8600  O  O   . ARG H  1 116 ? 144.458 7.408   16.067 1.00 31.65 ? 115  ARG H O   1 
ATOM   8601  C  CB  . ARG H  1 116 ? 146.182 9.375   13.704 1.00 28.73 ? 115  ARG H CB  1 
ATOM   8602  C  CG  . ARG H  1 116 ? 147.188 9.208   12.558 1.00 31.38 ? 115  ARG H CG  1 
ATOM   8603  C  CD  . ARG H  1 116 ? 147.293 10.409  11.633 1.00 33.00 ? 115  ARG H CD  1 
ATOM   8604  N  NE  . ARG H  1 116 ? 148.144 10.107  10.478 1.00 32.60 ? 115  ARG H NE  1 
ATOM   8605  C  CZ  . ARG H  1 116 ? 149.469 9.980   10.520 1.00 32.11 ? 115  ARG H CZ  1 
ATOM   8606  N  NH1 . ARG H  1 116 ? 150.144 9.698   9.414  1.00 33.21 ? 115  ARG H NH1 1 
ATOM   8607  N  NH2 . ARG H  1 116 ? 150.127 10.152  11.655 1.00 34.23 ? 115  ARG H NH2 1 
ATOM   8608  N  N   . THR H  1 117 ? 145.366 9.388   16.587 1.00 28.93 ? 116  THR H N   1 
ATOM   8609  C  CA  . THR H  1 117 ? 144.519 9.534   17.764 1.00 28.67 ? 116  THR H CA  1 
ATOM   8610  C  C   . THR H  1 117 ? 143.468 10.642  17.721 1.00 29.67 ? 116  THR H C   1 
ATOM   8611  O  O   . THR H  1 117 ? 143.782 11.804  17.468 1.00 29.18 ? 116  THR H O   1 
ATOM   8612  C  CB  . THR H  1 117 ? 145.392 9.741   19.026 1.00 28.19 ? 116  THR H CB  1 
ATOM   8613  O  OG1 . THR H  1 117 ? 146.291 8.636   19.173 1.00 28.67 ? 116  THR H OG1 1 
ATOM   8614  C  CG2 . THR H  1 117 ? 144.528 9.850   20.270 1.00 30.81 ? 116  THR H CG2 1 
ATOM   8615  N  N   . LEU H  1 118 ? 142.215 10.267  17.962 1.00 27.99 ? 117  LEU H N   1 
ATOM   8616  C  CA  . LEU H  1 118 ? 141.128 11.239  18.010 1.00 29.27 ? 117  LEU H CA  1 
ATOM   8617  C  C   . LEU H  1 118 ? 141.113 11.732  19.452 1.00 28.32 ? 117  LEU H C   1 
ATOM   8618  O  O   . LEU H  1 118 ? 141.143 10.928  20.377 1.00 27.83 ? 117  LEU H O   1 
ATOM   8619  C  CB  . LEU H  1 118 ? 139.783 10.581  17.672 1.00 28.47 ? 117  LEU H CB  1 
ATOM   8620  C  CG  . LEU H  1 118 ? 138.573 11.519  17.770 1.00 29.16 ? 117  LEU H CG  1 
ATOM   8621  C  CD1 . LEU H  1 118 ? 138.705 12.630  16.728 1.00 26.27 ? 117  LEU H CD1 1 
ATOM   8622  C  CD2 . LEU H  1 118 ? 137.274 10.733  17.559 1.00 26.98 ? 117  LEU H CD2 1 
ATOM   8623  N  N   . VAL H  1 119 ? 141.072 13.049  19.643 1.00 29.47 ? 118  VAL H N   1 
ATOM   8624  C  CA  . VAL H  1 119 ? 141.081 13.632  20.983 1.00 27.52 ? 118  VAL H CA  1 
ATOM   8625  C  C   . VAL H  1 119 ? 139.961 14.649  21.196 1.00 29.80 ? 118  VAL H C   1 
ATOM   8626  O  O   . VAL H  1 119 ? 139.642 15.429  20.295 1.00 29.13 ? 118  VAL H O   1 
ATOM   8627  C  CB  . VAL H  1 119 ? 142.426 14.367  21.259 1.00 29.10 ? 118  VAL H CB  1 
ATOM   8628  C  CG1 . VAL H  1 119 ? 142.407 15.012  22.646 1.00 26.53 ? 118  VAL H CG1 1 
ATOM   8629  C  CG2 . VAL H  1 119 ? 143.590 13.401  21.134 1.00 26.96 ? 118  VAL H CG2 1 
ATOM   8630  N  N   . VAL H  1 120 ? 139.349 14.620  22.380 1.00 28.69 ? 119  VAL H N   1 
ATOM   8631  C  CA  . VAL H  1 120 ? 138.320 15.594  22.722 1.00 27.41 ? 119  VAL H CA  1 
ATOM   8632  C  C   . VAL H  1 120 ? 138.922 16.388  23.886 1.00 27.57 ? 119  VAL H C   1 
ATOM   8633  O  O   . VAL H  1 120 ? 139.487 15.811  24.817 1.00 26.28 ? 119  VAL H O   1 
ATOM   8634  C  CB  . VAL H  1 120 ? 136.979 14.937  23.122 1.00 27.13 ? 119  VAL H CB  1 
ATOM   8635  C  CG1 . VAL H  1 120 ? 137.142 14.071  24.364 1.00 27.89 ? 119  VAL H CG1 1 
ATOM   8636  C  CG2 . VAL H  1 120 ? 135.937 16.024  23.336 1.00 25.91 ? 119  VAL H CG2 1 
ATOM   8637  N  N   . HIS H  1 121 ? 138.803 17.708  23.813 1.00 28.67 ? 120  HIS H N   1 
ATOM   8638  C  CA  . HIS H  1 121 ? 139.400 18.609  24.797 1.00 29.65 ? 120  HIS H CA  1 
ATOM   8639  C  C   . HIS H  1 121 ? 138.556 19.178  25.926 1.00 31.27 ? 120  HIS H C   1 
ATOM   8640  O  O   . HIS H  1 121 ? 137.322 19.128  25.917 1.00 31.65 ? 120  HIS H O   1 
ATOM   8641  C  CB  . HIS H  1 121 ? 140.054 19.777  24.058 1.00 28.66 ? 120  HIS H CB  1 
ATOM   8642  C  CG  . HIS H  1 121 ? 141.263 19.391  23.273 1.00 28.47 ? 120  HIS H CG  1 
ATOM   8643  N  ND1 . HIS H  1 121 ? 142.547 19.530  23.763 1.00 27.85 ? 120  HIS H ND1 1 
ATOM   8644  C  CD2 . HIS H  1 121 ? 141.390 18.832  22.046 1.00 26.65 ? 120  HIS H CD2 1 
ATOM   8645  C  CE1 . HIS H  1 121 ? 143.406 19.074  22.875 1.00 26.48 ? 120  HIS H CE1 1 
ATOM   8646  N  NE2 . HIS H  1 121 ? 142.730 18.641  21.821 1.00 26.90 ? 120  HIS H NE2 1 
ATOM   8647  N  N   . GLU H  1 122 ? 139.274 19.757  26.883 1.00 32.83 ? 121  GLU H N   1 
ATOM   8648  C  CA  . GLU H  1 122 ? 138.707 20.383  28.066 1.00 32.50 ? 121  GLU H CA  1 
ATOM   8649  C  C   . GLU H  1 122 ? 137.901 21.633  27.719 1.00 32.18 ? 121  GLU H C   1 
ATOM   8650  O  O   . GLU H  1 122 ? 136.775 21.809  28.185 1.00 30.87 ? 121  GLU H O   1 
ATOM   8651  C  CB  . GLU H  1 122 ? 139.849 20.759  29.014 1.00 35.26 ? 121  GLU H CB  1 
ATOM   8652  C  CG  . GLU H  1 122 ? 139.443 21.618  30.198 1.00 40.02 ? 121  GLU H CG  1 
ATOM   8653  C  CD  . GLU H  1 122 ? 140.621 22.361  30.804 1.00 42.55 ? 121  GLU H CD  1 
ATOM   8654  O  OE1 . GLU H  1 122 ? 140.433 22.995  31.864 1.00 45.62 ? 121  GLU H OE1 1 
ATOM   8655  O  OE2 . GLU H  1 122 ? 141.730 22.320  30.220 1.00 42.52 ? 121  GLU H OE2 1 
ATOM   8656  N  N   . LYS H  1 123 ? 138.491 22.496  26.895 1.00 33.33 ? 122  LYS H N   1 
ATOM   8657  C  CA  . LYS H  1 123 ? 137.857 23.750  26.500 1.00 34.52 ? 122  LYS H CA  1 
ATOM   8658  C  C   . LYS H  1 123 ? 137.552 23.826  25.008 1.00 31.87 ? 122  LYS H C   1 
ATOM   8659  O  O   . LYS H  1 123 ? 137.887 22.931  24.231 1.00 31.37 ? 122  LYS H O   1 
ATOM   8660  C  CB  . LYS H  1 123 ? 138.767 24.935  26.846 1.00 37.17 ? 122  LYS H CB  1 
ATOM   8661  C  CG  . LYS H  1 123 ? 139.513 24.821  28.158 1.00 40.70 ? 122  LYS H CG  1 
ATOM   8662  C  CD  . LYS H  1 123 ? 140.484 25.986  28.311 1.00 41.79 ? 122  LYS H CD  1 
ATOM   8663  C  CE  . LYS H  1 123 ? 141.318 25.857  29.572 0.00 41.92 ? 122  LYS H CE  1 
ATOM   8664  N  NZ  . LYS H  1 123 ? 142.311 26.960  29.675 0.00 42.24 ? 122  LYS H NZ  1 
ATOM   8665  N  N   . ALA H  1 124 ? 136.932 24.933  24.620 1.00 31.97 ? 123  ALA H N   1 
ATOM   8666  C  CA  . ALA H  1 124 ? 136.593 25.178  23.230 1.00 31.14 ? 123  ALA H CA  1 
ATOM   8667  C  C   . ALA H  1 124 ? 137.855 25.530  22.438 1.00 31.21 ? 123  ALA H C   1 
ATOM   8668  O  O   . ALA H  1 124 ? 138.829 26.047  22.988 1.00 27.37 ? 123  ALA H O   1 
ATOM   8669  C  CB  . ALA H  1 124 ? 135.583 26.316  23.138 1.00 30.18 ? 123  ALA H CB  1 
ATOM   8670  N  N   . ASP H  1 125 ? 137.822 25.224  21.146 1.00 30.05 ? 124  ASP H N   1 
ATOM   8671  C  CA  . ASP H  1 125 ? 138.917 25.503  20.221 1.00 29.79 ? 124  ASP H CA  1 
ATOM   8672  C  C   . ASP H  1 125 ? 138.588 26.888  19.655 1.00 29.21 ? 124  ASP H C   1 
ATOM   8673  O  O   . ASP H  1 125 ? 137.472 27.099  19.180 1.00 29.21 ? 124  ASP H O   1 
ATOM   8674  C  CB  . ASP H  1 125 ? 138.903 24.429  19.119 1.00 28.39 ? 124  ASP H CB  1 
ATOM   8675  C  CG  . ASP H  1 125 ? 139.965 24.642  18.056 1.00 28.45 ? 124  ASP H CG  1 
ATOM   8676  O  OD1 . ASP H  1 125 ? 140.283 23.656  17.352 1.00 25.07 ? 124  ASP H OD1 1 
ATOM   8677  O  OD2 . ASP H  1 125 ? 140.465 25.778  17.905 1.00 27.51 ? 124  ASP H OD2 1 
ATOM   8678  N  N   . ASP H  1 126 ? 139.530 27.831  19.715 1.00 27.64 ? 125  ASP H N   1 
ATOM   8679  C  CA  . ASP H  1 126 ? 139.247 29.179  19.212 1.00 27.08 ? 125  ASP H CA  1 
ATOM   8680  C  C   . ASP H  1 126 ? 139.385 29.296  17.701 1.00 27.19 ? 125  ASP H C   1 
ATOM   8681  O  O   . ASP H  1 126 ? 139.334 30.394  17.135 1.00 24.28 ? 125  ASP H O   1 
ATOM   8682  C  CB  . ASP H  1 126 ? 140.113 30.233  19.930 1.00 29.24 ? 125  ASP H CB  1 
ATOM   8683  C  CG  . ASP H  1 126 ? 141.597 30.111  19.624 1.00 29.85 ? 125  ASP H CG  1 
ATOM   8684  O  OD1 . ASP H  1 126 ? 142.386 30.729  20.370 1.00 30.72 ? 125  ASP H OD1 1 
ATOM   8685  O  OD2 . ASP H  1 126 ? 141.981 29.423  18.653 1.00 30.20 ? 125  ASP H OD2 1 
ATOM   8686  N  N   . LEU H  1 127 ? 139.547 28.139  17.064 1.00 25.05 ? 126  LEU H N   1 
ATOM   8687  C  CA  . LEU H  1 127 ? 139.658 28.015  15.618 1.00 23.04 ? 126  LEU H CA  1 
ATOM   8688  C  C   . LEU H  1 127 ? 140.755 28.888  15.010 1.00 24.81 ? 126  LEU H C   1 
ATOM   8689  O  O   . LEU H  1 127 ? 140.681 29.279  13.839 1.00 22.40 ? 126  LEU H O   1 
ATOM   8690  C  CB  . LEU H  1 127 ? 138.297 28.311  14.982 1.00 20.70 ? 126  LEU H CB  1 
ATOM   8691  C  CG  . LEU H  1 127 ? 137.112 27.568  15.630 1.00 22.41 ? 126  LEU H CG  1 
ATOM   8692  C  CD1 . LEU H  1 127 ? 135.818 27.872  14.885 1.00 20.69 ? 126  LEU H CD1 1 
ATOM   8693  C  CD2 . LEU H  1 127 ? 137.376 26.069  15.621 1.00 22.12 ? 126  LEU H CD2 1 
ATOM   8694  N  N   . GLY H  1 128 ? 141.779 29.164  15.817 1.00 25.39 ? 127  GLY H N   1 
ATOM   8695  C  CA  . GLY H  1 128 ? 142.917 29.955  15.378 1.00 25.92 ? 127  GLY H CA  1 
ATOM   8696  C  C   . GLY H  1 128 ? 142.704 31.451  15.307 1.00 26.77 ? 127  GLY H C   1 
ATOM   8697  O  O   . GLY H  1 128 ? 143.454 32.158  14.629 1.00 25.70 ? 127  GLY H O   1 
ATOM   8698  N  N   . LYS H  1 129 ? 141.701 31.941  16.025 1.00 26.64 ? 128  LYS H N   1 
ATOM   8699  C  CA  . LYS H  1 129 ? 141.384 33.360  16.014 1.00 28.65 ? 128  LYS H CA  1 
ATOM   8700  C  C   . LYS H  1 129 ? 141.649 34.032  17.358 1.00 28.11 ? 128  LYS H C   1 
ATOM   8701  O  O   . LYS H  1 129 ? 141.082 35.082  17.650 1.00 28.72 ? 128  LYS H O   1 
ATOM   8702  C  CB  . LYS H  1 129 ? 139.917 33.536  15.606 1.00 28.78 ? 128  LYS H CB  1 
ATOM   8703  C  CG  . LYS H  1 129 ? 139.588 32.809  14.300 1.00 32.57 ? 128  LYS H CG  1 
ATOM   8704  C  CD  . LYS H  1 129 ? 138.107 32.846  13.949 1.00 36.53 ? 128  LYS H CD  1 
ATOM   8705  C  CE  . LYS H  1 129 ? 137.666 34.213  13.466 1.00 38.46 ? 128  LYS H CE  1 
ATOM   8706  N  NZ  . LYS H  1 129 ? 136.253 34.176  13.001 1.00 40.67 ? 128  LYS H NZ  1 
ATOM   8707  N  N   . GLY H  1 130 ? 142.528 33.428  18.154 1.00 28.08 ? 129  GLY H N   1 
ATOM   8708  C  CA  . GLY H  1 130 ? 142.852 33.953  19.472 1.00 28.26 ? 129  GLY H CA  1 
ATOM   8709  C  C   . GLY H  1 130 ? 143.932 35.024  19.544 1.00 29.98 ? 129  GLY H C   1 
ATOM   8710  O  O   . GLY H  1 130 ? 144.117 35.650  20.591 1.00 28.73 ? 129  GLY H O   1 
ATOM   8711  N  N   . GLY H  1 131 ? 144.658 35.226  18.449 1.00 30.14 ? 130  GLY H N   1 
ATOM   8712  C  CA  . GLY H  1 131 ? 145.691 36.246  18.431 1.00 31.12 ? 130  GLY H CA  1 
ATOM   8713  C  C   . GLY H  1 131 ? 146.993 35.927  19.147 1.00 33.41 ? 130  GLY H C   1 
ATOM   8714  O  O   . GLY H  1 131 ? 147.868 36.786  19.230 1.00 31.53 ? 130  GLY H O   1 
ATOM   8715  N  N   . ASN H  1 132 ? 147.139 34.717  19.680 1.00 33.75 ? 131  ASN H N   1 
ATOM   8716  C  CA  . ASN H  1 132 ? 148.388 34.360  20.356 1.00 35.86 ? 131  ASN H CA  1 
ATOM   8717  C  C   . ASN H  1 132 ? 149.063 33.183  19.683 1.00 37.38 ? 131  ASN H C   1 
ATOM   8718  O  O   . ASN H  1 132 ? 148.474 32.557  18.791 1.00 35.56 ? 131  ASN H O   1 
ATOM   8719  C  CB  . ASN H  1 132 ? 148.150 34.052  21.835 1.00 36.65 ? 131  ASN H CB  1 
ATOM   8720  C  CG  . ASN H  1 132 ? 147.094 32.991  22.059 1.00 39.81 ? 131  ASN H CG  1 
ATOM   8721  O  OD1 . ASN H  1 132 ? 146.895 32.100  21.233 1.00 37.38 ? 131  ASN H OD1 1 
ATOM   8722  N  ND2 . ASN H  1 132 ? 146.421 33.073  23.197 1.00 40.14 ? 131  ASN H ND2 1 
ATOM   8723  N  N   . GLU H  1 133 ? 150.287 32.866  20.091 1.00 39.43 ? 132  GLU H N   1 
ATOM   8724  C  CA  . GLU H  1 133 ? 150.928 31.754  19.433 1.00 41.87 ? 132  GLU H CA  1 
ATOM   8725  C  C   . GLU H  1 133 ? 150.165 30.463  19.650 1.00 40.70 ? 132  GLU H C   1 
ATOM   8726  O  O   . GLU H  1 133 ? 149.968 29.708  18.721 1.00 39.63 ? 132  GLU H O   1 
ATOM   8727  C  CB  . GLU H  1 133 ? 152.368 31.589  19.888 1.00 45.88 ? 132  GLU H CB  1 
ATOM   8728  C  CG  . GLU H  1 133 ? 153.178 30.773  18.873 1.00 52.33 ? 132  GLU H CG  1 
ATOM   8729  C  CD  . GLU H  1 133 ? 154.556 31.343  18.575 1.00 56.76 ? 132  GLU H CD  1 
ATOM   8730  O  OE1 . GLU H  1 133 ? 155.305 30.713  17.790 1.00 60.15 ? 132  GLU H OE1 1 
ATOM   8731  O  OE2 . GLU H  1 133 ? 154.889 32.415  19.119 1.00 59.14 ? 132  GLU H OE2 1 
ATOM   8732  N  N   . GLU H  1 134 ? 149.713 30.219  20.873 1.00 40.45 ? 133  GLU H N   1 
ATOM   8733  C  CA  . GLU H  1 134 ? 148.968 28.996  21.167 1.00 40.29 ? 133  GLU H CA  1 
ATOM   8734  C  C   . GLU H  1 134 ? 147.767 28.805  20.218 1.00 37.39 ? 133  GLU H C   1 
ATOM   8735  O  O   . GLU H  1 134 ? 147.532 27.698  19.726 1.00 37.12 ? 133  GLU H O   1 
ATOM   8736  C  CB  . GLU H  1 134 ? 148.496 28.980  22.635 1.00 43.03 ? 133  GLU H CB  1 
ATOM   8737  C  CG  . GLU H  1 134 ? 147.971 27.627  23.045 1.00 49.41 ? 133  GLU H CG  1 
ATOM   8738  C  CD  . GLU H  1 134 ? 149.027 26.550  22.963 1.00 52.18 ? 133  GLU H CD  1 
ATOM   8739  O  OE1 . GLU H  1 134 ? 148.692 25.406  23.320 1.00 55.29 ? 133  GLU H OE1 1 
ATOM   8740  O  OE2 . GLU H  1 134 ? 150.176 26.833  22.550 1.00 55.55 ? 133  GLU H OE2 1 
ATOM   8741  N  N   . SER H  1 135 ? 147.031 29.879  19.932 1.00 33.77 ? 134  SER H N   1 
ATOM   8742  C  CA  . SER H  1 135 ? 145.868 29.794  19.044 1.00 32.69 ? 134  SER H CA  1 
ATOM   8743  C  C   . SER H  1 135 ? 146.229 29.161  17.705 1.00 32.67 ? 134  SER H C   1 
ATOM   8744  O  O   . SER H  1 135 ? 145.492 28.315  17.192 1.00 31.63 ? 134  SER H O   1 
ATOM   8745  C  CB  . SER H  1 135 ? 145.267 31.187  18.813 1.00 32.74 ? 134  SER H CB  1 
ATOM   8746  O  OG  . SER H  1 135 ? 144.086 31.129  18.025 1.00 31.45 ? 134  SER H OG  1 
ATOM   8747  N  N   . THR H  1 136 ? 147.377 29.555  17.158 1.00 31.54 ? 135  THR H N   1 
ATOM   8748  C  CA  . THR H  1 136 ? 147.839 29.046  15.870 1.00 33.57 ? 135  THR H CA  1 
ATOM   8749  C  C   . THR H  1 136 ? 148.413 27.635  15.946 1.00 32.15 ? 135  THR H C   1 
ATOM   8750  O  O   . THR H  1 136 ? 148.800 27.061  14.923 1.00 29.83 ? 135  THR H O   1 
ATOM   8751  C  CB  . THR H  1 136 ? 148.925 29.964  15.267 1.00 37.34 ? 135  THR H CB  1 
ATOM   8752  O  OG1 . THR H  1 136 ? 150.104 29.921  16.088 1.00 41.67 ? 135  THR H OG1 1 
ATOM   8753  C  CG2 . THR H  1 136 ? 148.425 31.396  15.190 1.00 38.14 ? 135  THR H CG2 1 
ATOM   8754  N  N   . LYS H  1 137 ? 148.476 27.083  17.153 1.00 31.91 ? 136  LYS H N   1 
ATOM   8755  C  CA  . LYS H  1 137 ? 149.006 25.738  17.341 1.00 34.70 ? 136  LYS H CA  1 
ATOM   8756  C  C   . LYS H  1 137 ? 147.954 24.726  17.798 1.00 34.74 ? 136  LYS H C   1 
ATOM   8757  O  O   . LYS H  1 137 ? 147.818 23.654  17.211 1.00 34.65 ? 136  LYS H O   1 
ATOM   8758  C  CB  . LYS H  1 137 ? 150.164 25.758  18.349 1.00 37.46 ? 136  LYS H CB  1 
ATOM   8759  C  CG  . LYS H  1 137 ? 151.441 26.395  17.815 1.00 41.31 ? 136  LYS H CG  1 
ATOM   8760  C  CD  . LYS H  1 137 ? 152.560 26.443  18.860 1.00 43.88 ? 136  LYS H CD  1 
ATOM   8761  C  CE  . LYS H  1 137 ? 152.314 27.523  19.909 1.00 46.10 ? 136  LYS H CE  1 
ATOM   8762  N  NZ  . LYS H  1 137 ? 153.489 27.721  20.808 1.00 47.55 ? 136  LYS H NZ  1 
ATOM   8763  N  N   . THR H  1 138 ? 147.206 25.072  18.839 1.00 34.90 ? 137  THR H N   1 
ATOM   8764  C  CA  . THR H  1 138 ? 146.200 24.161  19.372 1.00 34.61 ? 137  THR H CA  1 
ATOM   8765  C  C   . THR H  1 138 ? 144.826 24.792  19.472 1.00 33.52 ? 137  THR H C   1 
ATOM   8766  O  O   . THR H  1 138 ? 143.848 24.105  19.757 1.00 33.42 ? 137  THR H O   1 
ATOM   8767  C  CB  . THR H  1 138 ? 146.579 23.697  20.783 1.00 34.89 ? 137  THR H CB  1 
ATOM   8768  O  OG1 . THR H  1 138 ? 146.439 24.798  21.691 1.00 36.57 ? 137  THR H OG1 1 
ATOM   8769  C  CG2 . THR H  1 138 ? 148.016 23.205  20.816 1.00 35.18 ? 137  THR H CG2 1 
ATOM   8770  N  N   . GLY H  1 139 ? 144.753 26.102  19.252 1.00 32.64 ? 138  GLY H N   1 
ATOM   8771  C  CA  . GLY H  1 139 ? 143.479 26.786  19.361 1.00 32.29 ? 138  GLY H CA  1 
ATOM   8772  C  C   . GLY H  1 139 ? 143.098 27.018  20.818 1.00 30.77 ? 138  GLY H C   1 
ATOM   8773  O  O   . GLY H  1 139 ? 141.951 27.345  21.119 1.00 30.87 ? 138  GLY H O   1 
ATOM   8774  N  N   . ASN H  1 140 ? 144.059 26.845  21.725 1.00 31.90 ? 139  ASN H N   1 
ATOM   8775  C  CA  . ASN H  1 140 ? 143.821 27.047  23.157 1.00 31.31 ? 139  ASN H CA  1 
ATOM   8776  C  C   . ASN H  1 140 ? 142.679 26.163  23.685 1.00 30.76 ? 139  ASN H C   1 
ATOM   8777  O  O   . ASN H  1 140 ? 141.889 26.597  24.529 1.00 30.43 ? 139  ASN H O   1 
ATOM   8778  C  CB  . ASN H  1 140 ? 143.491 28.520  23.427 1.00 32.13 ? 139  ASN H CB  1 
ATOM   8779  C  CG  . ASN H  1 140 ? 144.649 29.454  23.093 1.00 37.89 ? 139  ASN H CG  1 
ATOM   8780  O  OD1 . ASN H  1 140 ? 145.753 29.303  23.622 1.00 38.49 ? 139  ASN H OD1 1 
ATOM   8781  N  ND2 . ASN H  1 140 ? 144.399 30.426  22.216 1.00 34.05 ? 139  ASN H ND2 1 
ATOM   8782  N  N   . ALA H  1 141 ? 142.606 24.925  23.198 1.00 28.38 ? 140  ALA H N   1 
ATOM   8783  C  CA  . ALA H  1 141 ? 141.548 23.995  23.602 1.00 31.46 ? 140  ALA H CA  1 
ATOM   8784  C  C   . ALA H  1 141 ? 141.742 23.343  24.975 1.00 33.13 ? 140  ALA H C   1 
ATOM   8785  O  O   . ALA H  1 141 ? 140.847 22.662  25.475 1.00 35.59 ? 140  ALA H O   1 
ATOM   8786  C  CB  . ALA H  1 141 ? 141.374 22.913  22.535 1.00 28.73 ? 140  ALA H CB  1 
ATOM   8787  N  N   . GLY H  1 142 ? 142.910 23.529  25.579 1.00 34.09 ? 141  GLY H N   1 
ATOM   8788  C  CA  . GLY H  1 142 ? 143.139 22.958  26.897 1.00 35.88 ? 141  GLY H CA  1 
ATOM   8789  C  C   . GLY H  1 142 ? 143.597 21.510  26.947 1.00 35.69 ? 141  GLY H C   1 
ATOM   8790  O  O   . GLY H  1 142 ? 144.073 20.957  25.953 1.00 35.03 ? 141  GLY H O   1 
ATOM   8791  N  N   . SER H  1 143 ? 143.445 20.890  28.114 1.00 35.25 ? 142  SER H N   1 
ATOM   8792  C  CA  . SER H  1 143 ? 143.878 19.508  28.301 1.00 34.71 ? 142  SER H CA  1 
ATOM   8793  C  C   . SER H  1 143 ? 143.081 18.521  27.457 1.00 34.16 ? 142  SER H C   1 
ATOM   8794  O  O   . SER H  1 143 ? 142.027 18.856  26.915 1.00 33.49 ? 142  SER H O   1 
ATOM   8795  C  CB  . SER H  1 143 ? 143.790 19.112  29.781 1.00 35.64 ? 142  SER H CB  1 
ATOM   8796  O  OG  . SER H  1 143 ? 142.445 18.998  30.205 1.00 36.42 ? 142  SER H OG  1 
ATOM   8797  N  N   . ARG H  1 144 ? 143.603 17.302  27.361 1.00 33.52 ? 143  ARG H N   1 
ATOM   8798  C  CA  . ARG H  1 144 ? 142.988 16.237  26.581 1.00 35.70 ? 143  ARG H CA  1 
ATOM   8799  C  C   . ARG H  1 144 ? 142.187 15.332  27.523 1.00 35.31 ? 143  ARG H C   1 
ATOM   8800  O  O   . ARG H  1 144 ? 142.752 14.504  28.240 1.00 34.60 ? 143  ARG H O   1 
ATOM   8801  C  CB  . ARG H  1 144 ? 144.099 15.462  25.861 1.00 35.65 ? 143  ARG H CB  1 
ATOM   8802  C  CG  . ARG H  1 144 ? 145.108 16.407  25.189 1.00 37.27 ? 143  ARG H CG  1 
ATOM   8803  C  CD  . ARG H  1 144 ? 146.281 15.704  24.516 1.00 38.35 ? 143  ARG H CD  1 
ATOM   8804  N  NE  . ARG H  1 144 ? 147.205 16.677  23.931 1.00 37.70 ? 143  ARG H NE  1 
ATOM   8805  C  CZ  . ARG H  1 144 ? 148.243 16.369  23.156 1.00 37.51 ? 143  ARG H CZ  1 
ATOM   8806  N  NH1 . ARG H  1 144 ? 149.025 17.332  22.673 1.00 33.54 ? 143  ARG H NH1 1 
ATOM   8807  N  NH2 . ARG H  1 144 ? 148.500 15.104  22.857 1.00 36.25 ? 143  ARG H NH2 1 
ATOM   8808  N  N   . LEU H  1 145 ? 140.868 15.498  27.514 1.00 34.34 ? 144  LEU H N   1 
ATOM   8809  C  CA  . LEU H  1 145 ? 139.999 14.728  28.396 1.00 34.67 ? 144  LEU H CA  1 
ATOM   8810  C  C   . LEU H  1 145 ? 139.905 13.252  28.037 1.00 33.50 ? 144  LEU H C   1 
ATOM   8811  O  O   . LEU H  1 145 ? 139.921 12.395  28.915 1.00 31.98 ? 144  LEU H O   1 
ATOM   8812  C  CB  . LEU H  1 145 ? 138.601 15.358  28.438 1.00 34.31 ? 144  LEU H CB  1 
ATOM   8813  C  CG  . LEU H  1 145 ? 138.576 16.830  28.870 1.00 36.90 ? 144  LEU H CG  1 
ATOM   8814  C  CD1 . LEU H  1 145 ? 137.140 17.308  29.016 1.00 36.40 ? 144  LEU H CD1 1 
ATOM   8815  C  CD2 . LEU H  1 145 ? 139.325 16.995  30.184 1.00 37.93 ? 144  LEU H CD2 1 
ATOM   8816  N  N   . ALA H  1 146 ? 139.812 12.952  26.747 1.00 33.34 ? 145  ALA H N   1 
ATOM   8817  C  CA  . ALA H  1 146 ? 139.726 11.566  26.310 1.00 32.47 ? 145  ALA H CA  1 
ATOM   8818  C  C   . ALA H  1 146 ? 140.266 11.417  24.894 1.00 32.78 ? 145  ALA H C   1 
ATOM   8819  O  O   . ALA H  1 146 ? 140.239 12.361  24.099 1.00 29.02 ? 145  ALA H O   1 
ATOM   8820  C  CB  . ALA H  1 146 ? 138.280 11.078  26.385 1.00 32.76 ? 145  ALA H CB  1 
ATOM   8821  N  N   . CYS H  1 147 ? 140.761 10.224  24.586 1.00 31.28 ? 146  CYS H N   1 
ATOM   8822  C  CA  . CYS H  1 147 ? 141.313 9.954   23.270 1.00 32.84 ? 146  CYS H CA  1 
ATOM   8823  C  C   . CYS H  1 147 ? 141.218 8.469   22.935 1.00 32.63 ? 146  CYS H C   1 
ATOM   8824  O  O   . CYS H  1 147 ? 140.973 7.633   23.807 1.00 33.33 ? 146  CYS H O   1 
ATOM   8825  C  CB  . CYS H  1 147 ? 142.775 10.403  23.227 1.00 32.37 ? 146  CYS H CB  1 
ATOM   8826  S  SG  . CYS H  1 147 ? 143.795 9.602   24.501 1.00 36.84 ? 146  CYS H SG  1 
ATOM   8827  N  N   . GLY H  1 148 ? 141.410 8.148   21.663 1.00 31.88 ? 147  GLY H N   1 
ATOM   8828  C  CA  . GLY H  1 148 ? 141.351 6.768   21.231 1.00 30.87 ? 147  GLY H CA  1 
ATOM   8829  C  C   . GLY H  1 148 ? 141.971 6.636   19.859 1.00 31.51 ? 147  GLY H C   1 
ATOM   8830  O  O   . GLY H  1 148 ? 141.893 7.560   19.038 1.00 30.17 ? 147  GLY H O   1 
ATOM   8831  N  N   . VAL H  1 149 ? 142.592 5.493   19.602 1.00 28.98 ? 148  VAL H N   1 
ATOM   8832  C  CA  . VAL H  1 149 ? 143.222 5.258   18.316 1.00 30.29 ? 148  VAL H CA  1 
ATOM   8833  C  C   . VAL H  1 149 ? 142.155 4.972   17.256 1.00 31.93 ? 148  VAL H C   1 
ATOM   8834  O  O   . VAL H  1 149 ? 141.238 4.168   17.468 1.00 32.05 ? 148  VAL H O   1 
ATOM   8835  C  CB  . VAL H  1 149 ? 144.204 4.076   18.405 1.00 29.57 ? 148  VAL H CB  1 
ATOM   8836  C  CG1 . VAL H  1 149 ? 144.908 3.879   17.082 1.00 28.80 ? 148  VAL H CG1 1 
ATOM   8837  C  CG2 . VAL H  1 149 ? 145.204 4.325   19.521 1.00 29.31 ? 148  VAL H CG2 1 
ATOM   8838  N  N   . ILE H  1 150 ? 142.273 5.643   16.118 1.00 32.03 ? 149  ILE H N   1 
ATOM   8839  C  CA  . ILE H  1 150 ? 141.323 5.470   15.029 1.00 32.76 ? 149  ILE H CA  1 
ATOM   8840  C  C   . ILE H  1 150 ? 141.655 4.186   14.270 1.00 32.37 ? 149  ILE H C   1 
ATOM   8841  O  O   . ILE H  1 150 ? 142.690 4.101   13.608 1.00 31.91 ? 149  ILE H O   1 
ATOM   8842  C  CB  . ILE H  1 150 ? 141.378 6.677   14.075 1.00 32.75 ? 149  ILE H CB  1 
ATOM   8843  C  CG1 . ILE H  1 150 ? 141.160 7.967   14.876 1.00 34.56 ? 149  ILE H CG1 1 
ATOM   8844  C  CG2 . ILE H  1 150 ? 140.321 6.537   12.988 1.00 30.82 ? 149  ILE H CG2 1 
ATOM   8845  C  CD1 . ILE H  1 150 ? 141.369 9.241   14.075 1.00 33.95 ? 149  ILE H CD1 1 
ATOM   8846  N  N   . GLY H  1 151 ? 140.771 3.193   14.373 1.00 31.35 ? 150  GLY H N   1 
ATOM   8847  C  CA  . GLY H  1 151 ? 140.999 1.917   13.712 1.00 30.71 ? 150  GLY H CA  1 
ATOM   8848  C  C   . GLY H  1 151 ? 140.081 1.602   12.540 1.00 30.39 ? 150  GLY H C   1 
ATOM   8849  O  O   . GLY H  1 151 ? 139.001 2.174   12.402 1.00 27.56 ? 150  GLY H O   1 
ATOM   8850  N  N   . ILE H  1 152 ? 140.519 0.677   11.691 1.00 31.61 ? 151  ILE H N   1 
ATOM   8851  C  CA  . ILE H  1 152 ? 139.742 0.278   10.523 1.00 34.18 ? 151  ILE H CA  1 
ATOM   8852  C  C   . ILE H  1 152 ? 138.495 -0.495  10.938 1.00 34.38 ? 151  ILE H C   1 
ATOM   8853  O  O   . ILE H  1 152 ? 138.580 -1.466  11.687 1.00 34.84 ? 151  ILE H O   1 
ATOM   8854  C  CB  . ILE H  1 152 ? 140.584 -0.600  9.574  1.00 35.10 ? 151  ILE H CB  1 
ATOM   8855  C  CG1 . ILE H  1 152 ? 141.780 0.204   9.057  1.00 35.07 ? 151  ILE H CG1 1 
ATOM   8856  C  CG2 . ILE H  1 152 ? 139.726 -1.089  8.411  1.00 35.19 ? 151  ILE H CG2 1 
ATOM   8857  C  CD1 . ILE H  1 152 ? 142.765 -0.612  8.246  1.00 38.37 ? 151  ILE H CD1 1 
ATOM   8858  N  N   . ALA H  1 153 ? 137.340 -0.050  10.454 1.00 34.75 ? 152  ALA H N   1 
ATOM   8859  C  CA  . ALA H  1 153 ? 136.072 -0.699  10.770 1.00 37.75 ? 152  ALA H CA  1 
ATOM   8860  C  C   . ALA H  1 153 ? 135.545 -1.483  9.569  1.00 38.88 ? 152  ALA H C   1 
ATOM   8861  O  O   . ALA H  1 153 ? 134.841 -2.478  9.729  1.00 37.99 ? 152  ALA H O   1 
ATOM   8862  C  CB  . ALA H  1 153 ? 135.043 0.343   11.209 1.00 37.27 ? 152  ALA H CB  1 
ATOM   8863  N  N   . GLN H  1 154 ? 135.885 -1.019  8.370  1.00 41.44 ? 153  GLN H N   1 
ATOM   8864  C  CA  . GLN H  1 154 ? 135.457 -1.673  7.137  1.00 46.61 ? 153  GLN H CA  1 
ATOM   8865  C  C   . GLN H  1 154 ? 136.367 -1.271  5.979  1.00 47.04 ? 153  GLN H C   1 
ATOM   8866  O  O   . GLN H  1 154 ? 136.984 -0.186  6.058  1.00 46.23 ? 153  GLN H O   1 
ATOM   8867  C  CB  . GLN H  1 154 ? 134.013 -1.287  6.797  1.00 49.65 ? 153  GLN H CB  1 
ATOM   8868  C  CG  . GLN H  1 154 ? 133.424 -2.057  5.620  1.00 54.83 ? 153  GLN H CG  1 
ATOM   8869  C  CD  . GLN H  1 154 ? 132.037 -1.571  5.238  1.00 58.85 ? 153  GLN H CD  1 
ATOM   8870  O  OE1 . GLN H  1 154 ? 131.887 -0.578  4.524  1.00 60.36 ? 153  GLN H OE1 1 
ATOM   8871  N  NE2 . GLN H  1 154 ? 131.013 -2.264  5.727  1.00 60.68 ? 153  GLN H NE2 1 
ATOM   8872  O  OXT . GLN H  1 154 ? 136.433 -2.041  4.997  1.00 49.10 ? 153  GLN H OXT 1 
ATOM   8873  N  N   . ALA I  1 2   ? 98.796  30.511  1.060  0.00 57.37 ? 1    ALA I N   1 
ATOM   8874  C  CA  . ALA I  1 2   ? 98.692  29.545  2.191  0.00 57.32 ? 1    ALA I CA  1 
ATOM   8875  C  C   . ALA I  1 2   ? 97.309  28.905  2.226  1.00 57.19 ? 1    ALA I C   1 
ATOM   8876  O  O   . ALA I  1 2   ? 96.356  29.435  1.656  1.00 58.05 ? 1    ALA I O   1 
ATOM   8877  C  CB  . ALA I  1 2   ? 98.972  30.257  3.509  0.00 57.38 ? 1    ALA I CB  1 
ATOM   8878  N  N   . THR I  1 3   ? 97.208  27.760  2.895  1.00 56.53 ? 2    THR I N   1 
ATOM   8879  C  CA  . THR I  1 3   ? 95.943  27.042  3.012  1.00 54.99 ? 2    THR I CA  1 
ATOM   8880  C  C   . THR I  1 3   ? 95.302  27.302  4.371  1.00 52.87 ? 2    THR I C   1 
ATOM   8881  O  O   . THR I  1 3   ? 94.079  27.380  4.483  1.00 52.79 ? 2    THR I O   1 
ATOM   8882  C  CB  . THR I  1 3   ? 96.144  25.519  2.828  1.00 55.82 ? 2    THR I CB  1 
ATOM   8883  O  OG1 . THR I  1 3   ? 96.420  25.240  1.451  1.00 58.08 ? 2    THR I OG1 1 
ATOM   8884  C  CG2 . THR I  1 3   ? 94.901  24.751  3.252  1.00 57.41 ? 2    THR I CG2 1 
ATOM   8885  N  N   . LYS I  1 4   ? 96.134  27.436  5.400  1.00 49.56 ? 3    LYS I N   1 
ATOM   8886  C  CA  . LYS I  1 4   ? 95.639  27.695  6.745  1.00 47.09 ? 3    LYS I CA  1 
ATOM   8887  C  C   . LYS I  1 4   ? 96.330  28.901  7.370  1.00 44.74 ? 3    LYS I C   1 
ATOM   8888  O  O   . LYS I  1 4   ? 97.500  29.175  7.096  1.00 43.49 ? 3    LYS I O   1 
ATOM   8889  C  CB  . LYS I  1 4   ? 95.853  26.472  7.640  1.00 47.73 ? 3    LYS I CB  1 
ATOM   8890  C  CG  . LYS I  1 4   ? 95.122  25.222  7.179  1.00 49.58 ? 3    LYS I CG  1 
ATOM   8891  C  CD  . LYS I  1 4   ? 95.326  24.072  8.157  1.00 51.61 ? 3    LYS I CD  1 
ATOM   8892  C  CE  . LYS I  1 4   ? 94.547  22.832  7.726  1.00 53.25 ? 3    LYS I CE  1 
ATOM   8893  N  NZ  . LYS I  1 4   ? 94.704  21.704  8.689  1.00 53.29 ? 3    LYS I NZ  1 
ATOM   8894  N  N   . ALA I  1 5   ? 95.589  29.616  8.208  1.00 40.55 ? 4    ALA I N   1 
ATOM   8895  C  CA  . ALA I  1 5   ? 96.104  30.787  8.901  1.00 39.37 ? 4    ALA I CA  1 
ATOM   8896  C  C   . ALA I  1 5   ? 95.502  30.809  10.300 1.00 38.43 ? 4    ALA I C   1 
ATOM   8897  O  O   . ALA I  1 5   ? 94.484  30.159  10.554 1.00 36.69 ? 4    ALA I O   1 
ATOM   8898  C  CB  . ALA I  1 5   ? 95.727  32.057  8.144  1.00 38.92 ? 4    ALA I CB  1 
ATOM   8899  N  N   . VAL I  1 6   ? 96.132  31.549  11.208 1.00 37.08 ? 5    VAL I N   1 
ATOM   8900  C  CA  . VAL I  1 6   ? 95.641  31.655  12.576 1.00 36.36 ? 5    VAL I CA  1 
ATOM   8901  C  C   . VAL I  1 6   ? 95.951  33.027  13.162 1.00 36.08 ? 5    VAL I C   1 
ATOM   8902  O  O   . VAL I  1 6   ? 96.924  33.672  12.774 1.00 34.56 ? 5    VAL I O   1 
ATOM   8903  C  CB  . VAL I  1 6   ? 96.273  30.586  13.495 1.00 37.40 ? 5    VAL I CB  1 
ATOM   8904  C  CG1 . VAL I  1 6   ? 97.768  30.849  13.663 1.00 38.66 ? 5    VAL I CG1 1 
ATOM   8905  C  CG2 . VAL I  1 6   ? 95.577  30.589  14.847 1.00 35.66 ? 5    VAL I CG2 1 
ATOM   8906  N  N   . ALA I  1 7   ? 95.119  33.462  14.102 1.00 34.80 ? 6    ALA I N   1 
ATOM   8907  C  CA  . ALA I  1 7   ? 95.308  34.751  14.751 1.00 34.62 ? 6    ALA I CA  1 
ATOM   8908  C  C   . ALA I  1 7   ? 94.932  34.653  16.218 1.00 34.51 ? 6    ALA I C   1 
ATOM   8909  O  O   . ALA I  1 7   ? 93.842  34.188  16.555 1.00 34.92 ? 6    ALA I O   1 
ATOM   8910  C  CB  . ALA I  1 7   ? 94.456  35.807  14.067 1.00 33.81 ? 6    ALA I CB  1 
ATOM   8911  N  N   . VAL I  1 8   ? 95.841  35.075  17.091 1.00 32.11 ? 7    VAL I N   1 
ATOM   8912  C  CA  . VAL I  1 8   ? 95.584  35.055  18.524 1.00 31.08 ? 7    VAL I CA  1 
ATOM   8913  C  C   . VAL I  1 8   ? 95.186  36.468  18.939 1.00 32.70 ? 7    VAL I C   1 
ATOM   8914  O  O   . VAL I  1 8   ? 95.992  37.399  18.864 1.00 32.10 ? 7    VAL I O   1 
ATOM   8915  C  CB  . VAL I  1 8   ? 96.831  34.627  19.314 1.00 30.98 ? 7    VAL I CB  1 
ATOM   8916  C  CG1 . VAL I  1 8   ? 96.538  34.647  20.805 1.00 29.98 ? 7    VAL I CG1 1 
ATOM   8917  C  CG2 . VAL I  1 8   ? 97.262  33.243  18.880 1.00 31.34 ? 7    VAL I CG2 1 
ATOM   8918  N  N   . LEU I  1 9   ? 93.940  36.628  19.373 1.00 31.03 ? 8    LEU I N   1 
ATOM   8919  C  CA  . LEU I  1 9   ? 93.443  37.936  19.775 1.00 31.82 ? 8    LEU I CA  1 
ATOM   8920  C  C   . LEU I  1 9   ? 93.771  38.278  21.222 1.00 32.18 ? 8    LEU I C   1 
ATOM   8921  O  O   . LEU I  1 9   ? 93.501  37.499  22.140 1.00 30.84 ? 8    LEU I O   1 
ATOM   8922  C  CB  . LEU I  1 9   ? 91.926  38.014  19.554 1.00 31.43 ? 8    LEU I CB  1 
ATOM   8923  C  CG  . LEU I  1 9   ? 91.426  37.746  18.130 1.00 30.76 ? 8    LEU I CG  1 
ATOM   8924  C  CD1 . LEU I  1 9   ? 89.913  37.926  18.081 1.00 32.91 ? 8    LEU I CD1 1 
ATOM   8925  C  CD2 . LEU I  1 9   ? 92.097  38.690  17.148 1.00 32.58 ? 8    LEU I CD2 1 
ATOM   8926  N  N   . LYS I  1 10  ? 94.363  39.452  21.411 1.00 33.70 ? 9    LYS I N   1 
ATOM   8927  C  CA  . LYS I  1 10  ? 94.729  39.940  22.733 1.00 36.91 ? 9    LYS I CA  1 
ATOM   8928  C  C   . LYS I  1 10  ? 94.628  41.461  22.753 1.00 37.65 ? 9    LYS I C   1 
ATOM   8929  O  O   . LYS I  1 10  ? 94.739  42.116  21.716 1.00 36.51 ? 9    LYS I O   1 
ATOM   8930  C  CB  . LYS I  1 10  ? 96.160  39.516  23.095 1.00 39.28 ? 9    LYS I CB  1 
ATOM   8931  C  CG  . LYS I  1 10  ? 96.335  38.024  23.332 1.00 41.25 ? 9    LYS I CG  1 
ATOM   8932  C  CD  . LYS I  1 10  ? 97.747  37.694  23.802 0.00 43.62 ? 9    LYS I CD  1 
ATOM   8933  C  CE  . LYS I  1 10  ? 97.918  36.200  24.056 1.00 45.76 ? 9    LYS I CE  1 
ATOM   8934  N  NZ  . LYS I  1 10  ? 99.263  35.867  24.612 1.00 47.67 ? 9    LYS I NZ  1 
ATOM   8935  N  N   . GLY I  1 11  ? 94.412  42.017  23.938 1.00 40.49 ? 10   GLY I N   1 
ATOM   8936  C  CA  . GLY I  1 11  ? 94.303  43.458  24.068 1.00 43.19 ? 10   GLY I CA  1 
ATOM   8937  C  C   . GLY I  1 11  ? 94.690  43.908  25.460 1.00 45.22 ? 10   GLY I C   1 
ATOM   8938  O  O   . GLY I  1 11  ? 95.219  43.124  26.249 1.00 45.26 ? 10   GLY I O   1 
ATOM   8939  N  N   . ASP I  1 12  ? 94.417  45.170  25.767 1.00 47.57 ? 11   ASP I N   1 
ATOM   8940  C  CA  . ASP I  1 12  ? 94.747  45.724  27.072 1.00 50.45 ? 11   ASP I CA  1 
ATOM   8941  C  C   . ASP I  1 12  ? 93.748  45.267  28.127 1.00 51.08 ? 11   ASP I C   1 
ATOM   8942  O  O   . ASP I  1 12  ? 93.995  45.399  29.327 1.00 52.40 ? 11   ASP I O   1 
ATOM   8943  C  CB  . ASP I  1 12  ? 94.764  47.254  27.002 1.00 53.08 ? 11   ASP I CB  1 
ATOM   8944  C  CG  . ASP I  1 12  ? 95.650  47.775  25.882 1.00 55.24 ? 11   ASP I CG  1 
ATOM   8945  O  OD1 . ASP I  1 12  ? 96.835  47.381  25.821 1.00 56.17 ? 11   ASP I OD1 1 
ATOM   8946  O  OD2 . ASP I  1 12  ? 95.162  48.582  25.062 1.00 56.64 ? 11   ASP I OD2 1 
ATOM   8947  N  N   . GLY I  1 13  ? 92.621  44.723  27.673 1.00 49.92 ? 12   GLY I N   1 
ATOM   8948  C  CA  . GLY I  1 13  ? 91.599  44.258  28.592 1.00 47.23 ? 12   GLY I CA  1 
ATOM   8949  C  C   . GLY I  1 13  ? 91.537  42.748  28.737 1.00 45.84 ? 12   GLY I C   1 
ATOM   8950  O  O   . GLY I  1 13  ? 92.513  42.052  28.457 1.00 45.63 ? 12   GLY I O   1 
ATOM   8951  N  N   . PRO I  1 14  ? 90.386  42.210  29.173 1.00 44.74 ? 13   PRO I N   1 
ATOM   8952  C  CA  . PRO I  1 14  ? 90.164  40.774  29.370 1.00 42.92 ? 13   PRO I CA  1 
ATOM   8953  C  C   . PRO I  1 14  ? 89.758  39.997  28.116 1.00 41.44 ? 13   PRO I C   1 
ATOM   8954  O  O   . PRO I  1 14  ? 89.590  38.782  28.168 1.00 42.68 ? 13   PRO I O   1 
ATOM   8955  C  CB  . PRO I  1 14  ? 89.072  40.754  30.425 1.00 43.28 ? 13   PRO I CB  1 
ATOM   8956  C  CG  . PRO I  1 14  ? 88.219  41.904  29.993 1.00 43.60 ? 13   PRO I CG  1 
ATOM   8957  C  CD  . PRO I  1 14  ? 89.238  42.985  29.680 1.00 43.98 ? 13   PRO I CD  1 
ATOM   8958  N  N   . VAL I  1 15  ? 89.598  40.690  26.994 1.00 39.75 ? 14   VAL I N   1 
ATOM   8959  C  CA  . VAL I  1 15  ? 89.200  40.027  25.756 1.00 38.15 ? 14   VAL I CA  1 
ATOM   8960  C  C   . VAL I  1 15  ? 90.342  39.267  25.091 1.00 38.30 ? 14   VAL I C   1 
ATOM   8961  O  O   . VAL I  1 15  ? 91.420  39.813  24.855 1.00 38.16 ? 14   VAL I O   1 
ATOM   8962  C  CB  . VAL I  1 15  ? 88.621  41.034  24.745 1.00 36.19 ? 14   VAL I CB  1 
ATOM   8963  C  CG1 . VAL I  1 15  ? 88.320  40.338  23.428 1.00 35.48 ? 14   VAL I CG1 1 
ATOM   8964  C  CG2 . VAL I  1 15  ? 87.355  41.660  25.311 1.00 36.37 ? 14   VAL I CG2 1 
ATOM   8965  N  N   . GLN I  1 16  ? 90.095  37.999  24.783 1.00 38.04 ? 15   GLN I N   1 
ATOM   8966  C  CA  . GLN I  1 16  ? 91.094  37.161  24.138 1.00 38.05 ? 15   GLN I CA  1 
ATOM   8967  C  C   . GLN I  1 16  ? 90.446  35.968  23.449 1.00 37.43 ? 15   GLN I C   1 
ATOM   8968  O  O   . GLN I  1 16  ? 89.385  35.494  23.863 1.00 35.79 ? 15   GLN I O   1 
ATOM   8969  C  CB  . GLN I  1 16  ? 92.115  36.667  25.164 1.00 39.97 ? 15   GLN I CB  1 
ATOM   8970  C  CG  . GLN I  1 16  ? 91.501  35.977  26.366 1.00 42.77 ? 15   GLN I CG  1 
ATOM   8971  C  CD  . GLN I  1 16  ? 92.548  35.500  27.353 1.00 45.95 ? 15   GLN I CD  1 
ATOM   8972  O  OE1 . GLN I  1 16  ? 93.365  34.636  27.037 1.00 49.03 ? 15   GLN I OE1 1 
ATOM   8973  N  NE2 . GLN I  1 16  ? 92.533  36.065  28.553 1.00 46.71 ? 15   GLN I NE2 1 
ATOM   8974  N  N   . GLY I  1 17  ? 91.094  35.488  22.394 1.00 36.86 ? 16   GLY I N   1 
ATOM   8975  C  CA  . GLY I  1 17  ? 90.574  34.354  21.662 1.00 34.96 ? 16   GLY I CA  1 
ATOM   8976  C  C   . GLY I  1 17  ? 91.543  33.865  20.607 1.00 34.69 ? 16   GLY I C   1 
ATOM   8977  O  O   . GLY I  1 17  ? 92.606  34.455  20.393 1.00 34.18 ? 16   GLY I O   1 
ATOM   8978  N  N   . ILE I  1 18  ? 91.170  32.776  19.947 1.00 33.17 ? 17   ILE I N   1 
ATOM   8979  C  CA  . ILE I  1 18  ? 91.982  32.184  18.898 1.00 31.01 ? 17   ILE I CA  1 
ATOM   8980  C  C   . ILE I  1 18  ? 91.076  31.949  17.701 1.00 31.59 ? 17   ILE I C   1 
ATOM   8981  O  O   . ILE I  1 18  ? 90.066  31.248  17.805 1.00 32.88 ? 17   ILE I O   1 
ATOM   8982  C  CB  . ILE I  1 18  ? 92.595  30.840  19.368 1.00 31.76 ? 17   ILE I CB  1 
ATOM   8983  C  CG1 . ILE I  1 18  ? 93.579  31.095  20.512 1.00 32.70 ? 17   ILE I CG1 1 
ATOM   8984  C  CG2 . ILE I  1 18  ? 93.278  30.137  18.204 1.00 31.53 ? 17   ILE I CG2 1 
ATOM   8985  C  CD1 . ILE I  1 18  ? 94.197  29.833  21.109 1.00 33.17 ? 17   ILE I CD1 1 
ATOM   8986  N  N   . ILE I  1 19  ? 91.431  32.545  16.568 1.00 29.56 ? 18   ILE I N   1 
ATOM   8987  C  CA  . ILE I  1 19  ? 90.645  32.410  15.352 1.00 30.29 ? 18   ILE I CA  1 
ATOM   8988  C  C   . ILE I  1 19  ? 91.433  31.700  14.254 1.00 32.95 ? 18   ILE I C   1 
ATOM   8989  O  O   . ILE I  1 19  ? 92.549  32.103  13.919 1.00 30.95 ? 18   ILE I O   1 
ATOM   8990  C  CB  . ILE I  1 19  ? 90.201  33.798  14.833 1.00 28.75 ? 18   ILE I CB  1 
ATOM   8991  C  CG1 . ILE I  1 19  ? 89.375  34.515  15.906 1.00 31.35 ? 18   ILE I CG1 1 
ATOM   8992  C  CG2 . ILE I  1 19  ? 89.438  33.652  13.534 1.00 29.43 ? 18   ILE I CG2 1 
ATOM   8993  C  CD1 . ILE I  1 19  ? 88.144  33.746  16.375 1.00 31.29 ? 18   ILE I CD1 1 
ATOM   8994  N  N   . ASN I  1 20  ? 90.838  30.651  13.691 1.00 32.65 ? 19   ASN I N   1 
ATOM   8995  C  CA  . ASN I  1 20  ? 91.475  29.875  12.634 1.00 35.01 ? 19   ASN I CA  1 
ATOM   8996  C  C   . ASN I  1 20  ? 90.951  30.237  11.253 1.00 35.91 ? 19   ASN I C   1 
ATOM   8997  O  O   . ASN I  1 20  ? 89.804  30.666  11.100 1.00 36.13 ? 19   ASN I O   1 
ATOM   8998  C  CB  . ASN I  1 20  ? 91.256  28.382  12.881 1.00 37.45 ? 19   ASN I CB  1 
ATOM   8999  C  CG  . ASN I  1 20  ? 91.782  27.937  14.224 1.00 40.85 ? 19   ASN I CG  1 
ATOM   9000  O  OD1 . ASN I  1 20  ? 92.993  27.866  14.438 1.00 41.73 ? 19   ASN I OD1 1 
ATOM   9001  N  ND2 . ASN I  1 20  ? 90.869  27.647  15.151 1.00 42.34 ? 19   ASN I ND2 1 
ATOM   9002  N  N   . PHE I  1 21  ? 91.803  30.058  10.249 1.00 35.86 ? 20   PHE I N   1 
ATOM   9003  C  CA  . PHE I  1 21  ? 91.450  30.348  8.863  1.00 37.98 ? 20   PHE I CA  1 
ATOM   9004  C  C   . PHE I  1 21  ? 91.824  29.148  8.002  1.00 40.01 ? 20   PHE I C   1 
ATOM   9005  O  O   . PHE I  1 21  ? 92.830  28.487  8.256  1.00 39.29 ? 20   PHE I O   1 
ATOM   9006  C  CB  . PHE I  1 21  ? 92.218  31.572  8.358  1.00 38.19 ? 20   PHE I CB  1 
ATOM   9007  C  CG  . PHE I  1 21  ? 91.847  32.854  9.047  1.00 37.40 ? 20   PHE I CG  1 
ATOM   9008  C  CD1 . PHE I  1 21  ? 90.942  33.736  8.462  1.00 36.83 ? 20   PHE I CD1 1 
ATOM   9009  C  CD2 . PHE I  1 21  ? 92.409  33.186  10.274 1.00 36.59 ? 20   PHE I CD2 1 
ATOM   9010  C  CE1 . PHE I  1 21  ? 90.601  34.930  9.093  1.00 36.17 ? 20   PHE I CE1 1 
ATOM   9011  C  CE2 . PHE I  1 21  ? 92.072  34.379  10.912 1.00 35.21 ? 20   PHE I CE2 1 
ATOM   9012  C  CZ  . PHE I  1 21  ? 91.168  35.251  10.318 1.00 34.18 ? 20   PHE I CZ  1 
ATOM   9013  N  N   . GLU I  1 22  ? 91.010  28.863  6.992  1.00 42.10 ? 21   GLU I N   1 
ATOM   9014  C  CA  . GLU I  1 22  ? 91.295  27.754  6.092  1.00 45.72 ? 21   GLU I CA  1 
ATOM   9015  C  C   . GLU I  1 22  ? 90.682  27.998  4.723  1.00 46.84 ? 21   GLU I C   1 
ATOM   9016  O  O   . GLU I  1 22  ? 89.501  28.329  4.604  1.00 46.05 ? 21   GLU I O   1 
ATOM   9017  C  CB  . GLU I  1 22  ? 90.781  26.435  6.672  1.00 47.82 ? 21   GLU I CB  1 
ATOM   9018  C  CG  . GLU I  1 22  ? 91.115  25.225  5.806  1.00 52.52 ? 21   GLU I CG  1 
ATOM   9019  C  CD  . GLU I  1 22  ? 90.847  23.906  6.503  1.00 54.73 ? 21   GLU I CD  1 
ATOM   9020  O  OE1 . GLU I  1 22  ? 91.530  23.607  7.507  1.00 56.00 ? 21   GLU I OE1 1 
ATOM   9021  O  OE2 . GLU I  1 22  ? 89.950  23.168  6.047  1.00 57.39 ? 21   GLU I OE2 1 
ATOM   9022  N  N   . GLN I  1 23  ? 91.504  27.846  3.689  1.00 48.66 ? 22   GLN I N   1 
ATOM   9023  C  CA  . GLN I  1 23  ? 91.063  28.047  2.316  1.00 51.38 ? 22   GLN I CA  1 
ATOM   9024  C  C   . GLN I  1 23  ? 91.466  26.829  1.492  1.00 54.05 ? 22   GLN I C   1 
ATOM   9025  O  O   . GLN I  1 23  ? 92.643  26.629  1.182  1.00 54.42 ? 22   GLN I O   1 
ATOM   9026  C  CB  . GLN I  1 23  ? 91.692  29.321  1.748  1.00 50.79 ? 22   GLN I CB  1 
ATOM   9027  C  CG  . GLN I  1 23  ? 91.257  29.673  0.336  1.00 50.44 ? 22   GLN I CG  1 
ATOM   9028  C  CD  . GLN I  1 23  ? 91.746  31.044  -0.088 1.00 51.60 ? 22   GLN I CD  1 
ATOM   9029  O  OE1 . GLN I  1 23  ? 92.898  31.405  0.155  1.00 53.15 ? 22   GLN I OE1 1 
ATOM   9030  N  NE2 . GLN I  1 23  ? 90.876  31.813  -0.733 1.00 50.58 ? 22   GLN I NE2 1 
ATOM   9031  N  N   . LYS I  1 24  ? 90.473  26.016  1.147  1.00 56.16 ? 23   LYS I N   1 
ATOM   9032  C  CA  . LYS I  1 24  ? 90.693  24.793  0.387  1.00 58.84 ? 23   LYS I CA  1 
ATOM   9033  C  C   . LYS I  1 24  ? 91.225  25.044  -1.019 1.00 59.35 ? 23   LYS I C   1 
ATOM   9034  O  O   . LYS I  1 24  ? 92.127  24.343  -1.477 1.00 59.63 ? 23   LYS I O   1 
ATOM   9035  C  CB  . LYS I  1 24  ? 89.388  23.992  0.310  1.00 60.46 ? 23   LYS I CB  1 
ATOM   9036  C  CG  . LYS I  1 24  ? 89.541  22.605  -0.296 1.00 62.80 ? 23   LYS I CG  1 
ATOM   9037  C  CD  . LYS I  1 24  ? 88.204  21.877  -0.359 1.00 64.41 ? 23   LYS I CD  1 
ATOM   9038  C  CE  . LYS I  1 24  ? 88.358  20.478  -0.950 1.00 65.97 ? 23   LYS I CE  1 
ATOM   9039  N  NZ  . LYS I  1 24  ? 87.054  19.748  -1.016 1.00 66.57 ? 23   LYS I NZ  1 
ATOM   9040  N  N   . GLU I  1 25  ? 90.669  26.044  -1.698 1.00 60.53 ? 24   GLU I N   1 
ATOM   9041  C  CA  . GLU I  1 25  ? 91.080  26.370  -3.059 1.00 61.38 ? 24   GLU I CA  1 
ATOM   9042  C  C   . GLU I  1 25  ? 91.627  27.790  -3.154 1.00 61.09 ? 24   GLU I C   1 
ATOM   9043  O  O   . GLU I  1 25  ? 91.085  28.712  -2.546 1.00 61.36 ? 24   GLU I O   1 
ATOM   9044  C  CB  . GLU I  1 25  ? 89.890  26.207  -4.001 1.00 63.09 ? 24   GLU I CB  1 
ATOM   9045  C  CG  . GLU I  1 25  ? 89.231  24.840  -3.911 1.00 65.82 ? 24   GLU I CG  1 
ATOM   9046  C  CD  . GLU I  1 25  ? 87.905  24.780  -4.645 1.00 68.15 ? 24   GLU I CD  1 
ATOM   9047  O  OE1 . GLU I  1 25  ? 87.266  23.706  -4.629 1.00 70.26 ? 24   GLU I OE1 1 
ATOM   9048  O  OE2 . GLU I  1 25  ? 87.501  25.805  -5.237 1.00 68.82 ? 24   GLU I OE2 1 
ATOM   9049  N  N   . SER I  1 26  ? 92.693  27.953  -3.934 1.00 60.29 ? 25   SER I N   1 
ATOM   9050  C  CA  . SER I  1 26  ? 93.355  29.244  -4.115 1.00 60.52 ? 25   SER I CA  1 
ATOM   9051  C  C   . SER I  1 26  ? 92.431  30.456  -4.037 1.00 60.19 ? 25   SER I C   1 
ATOM   9052  O  O   . SER I  1 26  ? 92.616  31.328  -3.189 1.00 61.28 ? 25   SER I O   1 
ATOM   9053  C  CB  . SER I  1 26  ? 94.105  29.275  -5.451 1.00 61.16 ? 25   SER I CB  1 
ATOM   9054  O  OG  . SER I  1 26  ? 93.206  29.330  -6.545 1.00 63.19 ? 25   SER I OG  1 
ATOM   9055  N  N   . ASN I  1 27  ? 91.443  30.513  -4.923 1.00 59.31 ? 26   ASN I N   1 
ATOM   9056  C  CA  . ASN I  1 27  ? 90.511  31.635  -4.944 1.00 58.13 ? 26   ASN I CA  1 
ATOM   9057  C  C   . ASN I  1 27  ? 89.142  31.246  -4.398 1.00 56.99 ? 26   ASN I C   1 
ATOM   9058  O  O   . ASN I  1 27  ? 88.147  31.927  -4.648 1.00 57.18 ? 26   ASN I O   1 
ATOM   9059  C  CB  . ASN I  1 27  ? 90.366  32.168  -6.372 0.00 57.97 ? 26   ASN I CB  1 
ATOM   9060  C  CG  . ASN I  1 27  ? 89.917  31.100  -7.355 0.00 57.88 ? 26   ASN I CG  1 
ATOM   9061  O  OD1 . ASN I  1 27  ? 89.749  31.369  -8.544 0.00 57.82 ? 26   ASN I OD1 1 
ATOM   9062  N  ND2 . ASN I  1 27  ? 89.723  29.882  -6.862 0.00 57.81 ? 26   ASN I ND2 1 
ATOM   9063  N  N   . GLY I  1 28  ? 89.100  30.152  -3.647 1.00 55.62 ? 27   GLY I N   1 
ATOM   9064  C  CA  . GLY I  1 28  ? 87.843  29.692  -3.086 1.00 53.80 ? 27   GLY I CA  1 
ATOM   9065  C  C   . GLY I  1 28  ? 87.462  30.401  -1.800 1.00 52.27 ? 27   GLY I C   1 
ATOM   9066  O  O   . GLY I  1 28  ? 88.150  31.331  -1.372 1.00 51.12 ? 27   GLY I O   1 
ATOM   9067  N  N   . PRO I  1 29  ? 86.359  29.981  -1.159 1.00 50.62 ? 28   PRO I N   1 
ATOM   9068  C  CA  . PRO I  1 29  ? 85.888  30.583  0.091  1.00 48.47 ? 28   PRO I CA  1 
ATOM   9069  C  C   . PRO I  1 29  ? 86.796  30.236  1.265  1.00 46.13 ? 28   PRO I C   1 
ATOM   9070  O  O   . PRO I  1 29  ? 87.473  29.205  1.257  1.00 45.92 ? 28   PRO I O   1 
ATOM   9071  C  CB  . PRO I  1 29  ? 84.495  29.985  0.249  1.00 49.49 ? 28   PRO I CB  1 
ATOM   9072  C  CG  . PRO I  1 29  ? 84.680  28.607  -0.307 1.00 49.83 ? 28   PRO I CG  1 
ATOM   9073  C  CD  . PRO I  1 29  ? 85.460  28.889  -1.578 1.00 50.68 ? 28   PRO I CD  1 
ATOM   9074  N  N   . VAL I  1 30  ? 86.808  31.103  2.271  1.00 43.57 ? 29   VAL I N   1 
ATOM   9075  C  CA  . VAL I  1 30  ? 87.623  30.882  3.454  1.00 42.69 ? 29   VAL I CA  1 
ATOM   9076  C  C   . VAL I  1 30  ? 86.755  30.578  4.664  1.00 41.98 ? 29   VAL I C   1 
ATOM   9077  O  O   . VAL I  1 30  ? 85.752  31.250  4.911  1.00 41.52 ? 29   VAL I O   1 
ATOM   9078  C  CB  . VAL I  1 30  ? 88.489  32.114  3.786  1.00 42.56 ? 29   VAL I CB  1 
ATOM   9079  C  CG1 . VAL I  1 30  ? 89.251  31.875  5.084  1.00 41.67 ? 29   VAL I CG1 1 
ATOM   9080  C  CG2 . VAL I  1 30  ? 89.453  32.392  2.646  1.00 42.65 ? 29   VAL I CG2 1 
ATOM   9081  N  N   . LYS I  1 31  ? 87.145  29.558  5.415  1.00 41.56 ? 30   LYS I N   1 
ATOM   9082  C  CA  . LYS I  1 31  ? 86.412  29.179  6.610  1.00 40.90 ? 30   LYS I CA  1 
ATOM   9083  C  C   . LYS I  1 31  ? 87.089  29.830  7.811  1.00 40.30 ? 30   LYS I C   1 
ATOM   9084  O  O   . LYS I  1 31  ? 88.290  29.648  8.032  1.00 40.89 ? 30   LYS I O   1 
ATOM   9085  C  CB  . LYS I  1 31  ? 86.409  27.660  6.771  1.00 42.62 ? 30   LYS I CB  1 
ATOM   9086  C  CG  . LYS I  1 31  ? 85.708  27.177  8.024  1.00 44.26 ? 30   LYS I CG  1 
ATOM   9087  C  CD  . LYS I  1 31  ? 85.920  25.690  8.229  1.00 47.12 ? 30   LYS I CD  1 
ATOM   9088  C  CE  . LYS I  1 31  ? 85.329  25.228  9.550  1.00 48.72 ? 30   LYS I CE  1 
ATOM   9089  N  NZ  . LYS I  1 31  ? 85.651  23.796  9.816  1.00 52.55 ? 30   LYS I NZ  1 
ATOM   9090  N  N   . VAL I  1 32  ? 86.314  30.594  8.574  1.00 37.80 ? 31   VAL I N   1 
ATOM   9091  C  CA  . VAL I  1 32  ? 86.825  31.278  9.756  1.00 36.97 ? 31   VAL I CA  1 
ATOM   9092  C  C   . VAL I  1 32  ? 86.065  30.787  10.978 1.00 37.67 ? 31   VAL I C   1 
ATOM   9093  O  O   . VAL I  1 32  ? 84.845  30.943  11.058 1.00 38.31 ? 31   VAL I O   1 
ATOM   9094  C  CB  . VAL I  1 32  ? 86.634  32.807  9.638  1.00 36.11 ? 31   VAL I CB  1 
ATOM   9095  C  CG1 . VAL I  1 32  ? 87.260  33.508  10.832 1.00 34.75 ? 31   VAL I CG1 1 
ATOM   9096  C  CG2 . VAL I  1 32  ? 87.242  33.306  8.341  1.00 35.13 ? 31   VAL I CG2 1 
ATOM   9097  N  N   . TRP I  1 33  ? 86.777  30.197  11.931 1.00 36.69 ? 32   TRP I N   1 
ATOM   9098  C  CA  . TRP I  1 33  ? 86.121  29.693  13.129 1.00 37.26 ? 32   TRP I CA  1 
ATOM   9099  C  C   . TRP I  1 33  ? 87.047  29.733  14.334 1.00 36.67 ? 32   TRP I C   1 
ATOM   9100  O  O   . TRP I  1 33  ? 88.270  29.702  14.198 1.00 36.96 ? 32   TRP I O   1 
ATOM   9101  C  CB  . TRP I  1 33  ? 85.644  28.257  12.902 1.00 37.15 ? 32   TRP I CB  1 
ATOM   9102  C  CG  . TRP I  1 33  ? 86.729  27.247  13.058 1.00 37.19 ? 32   TRP I CG  1 
ATOM   9103  C  CD1 . TRP I  1 33  ? 87.011  26.510  14.173 1.00 38.72 ? 32   TRP I CD1 1 
ATOM   9104  C  CD2 . TRP I  1 33  ? 87.704  26.882  12.078 1.00 37.69 ? 32   TRP I CD2 1 
ATOM   9105  N  NE1 . TRP I  1 33  ? 88.102  25.705  13.947 1.00 38.86 ? 32   TRP I NE1 1 
ATOM   9106  C  CE2 . TRP I  1 33  ? 88.548  25.914  12.666 1.00 38.94 ? 32   TRP I CE2 1 
ATOM   9107  C  CE3 . TRP I  1 33  ? 87.949  27.280  10.757 1.00 38.51 ? 32   TRP I CE3 1 
ATOM   9108  C  CZ2 . TRP I  1 33  ? 89.620  25.334  11.979 1.00 38.83 ? 32   TRP I CZ2 1 
ATOM   9109  C  CZ3 . TRP I  1 33  ? 89.017  26.704  10.071 1.00 39.42 ? 32   TRP I CZ3 1 
ATOM   9110  C  CH2 . TRP I  1 33  ? 89.838  25.740  10.686 1.00 40.54 ? 32   TRP I CH2 1 
ATOM   9111  N  N   . GLY I  1 34  ? 86.449  29.792  15.517 1.00 34.93 ? 33   GLY I N   1 
ATOM   9112  C  CA  . GLY I  1 34  ? 87.226  29.834  16.735 1.00 34.44 ? 33   GLY I CA  1 
ATOM   9113  C  C   . GLY I  1 34  ? 86.381  30.306  17.896 1.00 34.91 ? 33   GLY I C   1 
ATOM   9114  O  O   . GLY I  1 34  ? 85.158  30.175  17.880 1.00 37.02 ? 33   GLY I O   1 
ATOM   9115  N  N   . SER I  1 35  ? 87.034  30.865  18.905 1.00 34.33 ? 34   SER I N   1 
ATOM   9116  C  CA  . SER I  1 35  ? 86.333  31.349  20.082 1.00 34.89 ? 34   SER I CA  1 
ATOM   9117  C  C   . SER I  1 35  ? 86.984  32.605  20.647 1.00 34.34 ? 34   SER I C   1 
ATOM   9118  O  O   . SER I  1 35  ? 88.200  32.793  20.538 1.00 33.82 ? 34   SER I O   1 
ATOM   9119  C  CB  . SER I  1 35  ? 86.315  30.261  21.158 1.00 35.51 ? 34   SER I CB  1 
ATOM   9120  O  OG  . SER I  1 35  ? 85.634  30.701  22.318 1.00 38.36 ? 34   SER I OG  1 
ATOM   9121  N  N   . ILE I  1 36  ? 86.162  33.467  21.237 1.00 31.77 ? 35   ILE I N   1 
ATOM   9122  C  CA  . ILE I  1 36  ? 86.634  34.699  21.859 1.00 31.18 ? 35   ILE I CA  1 
ATOM   9123  C  C   . ILE I  1 36  ? 85.887  34.785  23.181 1.00 31.06 ? 35   ILE I C   1 
ATOM   9124  O  O   . ILE I  1 36  ? 84.684  34.527  23.232 1.00 31.53 ? 35   ILE I O   1 
ATOM   9125  C  CB  . ILE I  1 36  ? 86.295  35.954  21.016 1.00 31.66 ? 35   ILE I CB  1 
ATOM   9126  C  CG1 . ILE I  1 36  ? 86.820  35.797  19.589 1.00 31.14 ? 35   ILE I CG1 1 
ATOM   9127  C  CG2 . ILE I  1 36  ? 86.927  37.194  21.651 1.00 29.64 ? 35   ILE I CG2 1 
ATOM   9128  C  CD1 . ILE I  1 36  ? 86.527  36.997  18.698 1.00 31.50 ? 35   ILE I CD1 1 
ATOM   9129  N  N   . LYS I  1 37  ? 86.594  35.126  24.251 1.00 31.08 ? 36   LYS I N   1 
ATOM   9130  C  CA  . LYS I  1 37  ? 85.970  35.231  25.565 1.00 31.50 ? 36   LYS I CA  1 
ATOM   9131  C  C   . LYS I  1 37  ? 86.252  36.580  26.217 1.00 30.79 ? 36   LYS I C   1 
ATOM   9132  O  O   . LYS I  1 37  ? 87.067  37.356  25.722 1.00 29.72 ? 36   LYS I O   1 
ATOM   9133  C  CB  . LYS I  1 37  ? 86.463  34.103  26.475 1.00 34.32 ? 36   LYS I CB  1 
ATOM   9134  C  CG  . LYS I  1 37  ? 87.963  34.081  26.682 1.00 36.81 ? 36   LYS I CG  1 
ATOM   9135  C  CD  . LYS I  1 37  ? 88.374  32.963  27.631 1.00 39.97 ? 36   LYS I CD  1 
ATOM   9136  C  CE  . LYS I  1 37  ? 89.889  32.927  27.813 1.00 41.97 ? 36   LYS I CE  1 
ATOM   9137  N  NZ  . LYS I  1 37  ? 90.317  31.837  28.740 1.00 44.50 ? 36   LYS I NZ  1 
ATOM   9138  N  N   . GLY I  1 38  ? 85.567  36.849  27.325 1.00 31.78 ? 37   GLY I N   1 
ATOM   9139  C  CA  . GLY I  1 38  ? 85.752  38.101  28.039 1.00 31.17 ? 37   GLY I CA  1 
ATOM   9140  C  C   . GLY I  1 38  ? 85.010  39.277  27.430 1.00 31.36 ? 37   GLY I C   1 
ATOM   9141  O  O   . GLY I  1 38  ? 85.253  40.425  27.800 1.00 32.70 ? 37   GLY I O   1 
ATOM   9142  N  N   . LEU I  1 39  ? 84.100  38.998  26.501 1.00 29.47 ? 38   LEU I N   1 
ATOM   9143  C  CA  . LEU I  1 39  ? 83.330  40.047  25.835 1.00 28.66 ? 38   LEU I CA  1 
ATOM   9144  C  C   . LEU I  1 39  ? 82.027  40.365  26.553 1.00 27.99 ? 38   LEU I C   1 
ATOM   9145  O  O   . LEU I  1 39  ? 81.497  39.534  27.285 1.00 29.66 ? 38   LEU I O   1 
ATOM   9146  C  CB  . LEU I  1 39  ? 82.993  39.614  24.404 1.00 28.89 ? 38   LEU I CB  1 
ATOM   9147  C  CG  . LEU I  1 39  ? 84.144  39.406  23.418 1.00 27.65 ? 38   LEU I CG  1 
ATOM   9148  C  CD1 . LEU I  1 39  ? 83.680  38.538  22.261 1.00 28.74 ? 38   LEU I CD1 1 
ATOM   9149  C  CD2 . LEU I  1 39  ? 84.642  40.755  22.925 1.00 27.77 ? 38   LEU I CD2 1 
ATOM   9150  N  N   . THR I  1 40  ? 81.512  41.575  26.355 1.00 29.15 ? 39   THR I N   1 
ATOM   9151  C  CA  . THR I  1 40  ? 80.225  41.924  26.941 1.00 28.33 ? 39   THR I CA  1 
ATOM   9152  C  C   . THR I  1 40  ? 79.232  41.164  26.055 1.00 27.71 ? 39   THR I C   1 
ATOM   9153  O  O   . THR I  1 40  ? 79.459  41.029  24.851 1.00 26.44 ? 39   THR I O   1 
ATOM   9154  C  CB  . THR I  1 40  ? 79.935  43.438  26.851 1.00 29.55 ? 39   THR I CB  1 
ATOM   9155  O  OG1 . THR I  1 40  ? 80.034  43.869  25.488 1.00 30.53 ? 39   THR I OG1 1 
ATOM   9156  C  CG2 . THR I  1 40  ? 80.925  44.223  27.707 1.00 31.05 ? 39   THR I CG2 1 
ATOM   9157  N  N   . GLU I  1 41  ? 78.150  40.655  26.636 1.00 27.93 ? 40   GLU I N   1 
ATOM   9158  C  CA  . GLU I  1 41  ? 77.179  39.905  25.848 1.00 29.77 ? 40   GLU I CA  1 
ATOM   9159  C  C   . GLU I  1 41  ? 76.639  40.752  24.698 1.00 29.78 ? 40   GLU I C   1 
ATOM   9160  O  O   . GLU I  1 41  ? 76.458  41.959  24.843 1.00 30.23 ? 40   GLU I O   1 
ATOM   9161  C  CB  . GLU I  1 41  ? 76.028  39.420  26.734 1.00 31.97 ? 40   GLU I CB  1 
ATOM   9162  C  CG  . GLU I  1 41  ? 75.117  40.509  27.267 1.00 33.99 ? 40   GLU I CG  1 
ATOM   9163  C  CD  . GLU I  1 41  ? 73.959  39.943  28.072 1.00 37.33 ? 40   GLU I CD  1 
ATOM   9164  O  OE1 . GLU I  1 41  ? 73.136  40.734  28.583 1.00 38.34 ? 40   GLU I OE1 1 
ATOM   9165  O  OE2 . GLU I  1 41  ? 73.869  38.702  28.191 1.00 36.32 ? 40   GLU I OE2 1 
ATOM   9166  N  N   . GLY I  1 42  ? 76.400  40.124  23.549 1.00 28.92 ? 41   GLY I N   1 
ATOM   9167  C  CA  . GLY I  1 42  ? 75.884  40.867  22.409 1.00 28.55 ? 41   GLY I CA  1 
ATOM   9168  C  C   . GLY I  1 42  ? 76.756  40.852  21.164 1.00 28.74 ? 41   GLY I C   1 
ATOM   9169  O  O   . GLY I  1 42  ? 77.714  40.075  21.073 1.00 26.25 ? 41   GLY I O   1 
ATOM   9170  N  N   . LEU I  1 43  ? 76.431  41.720  20.206 1.00 27.64 ? 42   LEU I N   1 
ATOM   9171  C  CA  . LEU I  1 43  ? 77.173  41.785  18.948 1.00 30.30 ? 42   LEU I CA  1 
ATOM   9172  C  C   . LEU I  1 43  ? 78.454  42.619  19.022 1.00 31.03 ? 42   LEU I C   1 
ATOM   9173  O  O   . LEU I  1 43  ? 78.514  43.633  19.716 1.00 30.79 ? 42   LEU I O   1 
ATOM   9174  C  CB  . LEU I  1 43  ? 76.291  42.349  17.827 1.00 30.11 ? 42   LEU I CB  1 
ATOM   9175  C  CG  . LEU I  1 43  ? 74.811  41.978  17.705 1.00 33.13 ? 42   LEU I CG  1 
ATOM   9176  C  CD1 . LEU I  1 43  ? 74.380  42.243  16.271 1.00 31.84 ? 42   LEU I CD1 1 
ATOM   9177  C  CD2 . LEU I  1 43  ? 74.560  40.532  18.075 1.00 31.44 ? 42   LEU I CD2 1 
ATOM   9178  N  N   . HIS I  1 44  ? 79.472  42.190  18.281 1.00 30.03 ? 43   HIS I N   1 
ATOM   9179  C  CA  . HIS I  1 44  ? 80.754  42.891  18.253 1.00 31.14 ? 43   HIS I CA  1 
ATOM   9180  C  C   . HIS I  1 44  ? 81.335  42.903  16.843 1.00 31.04 ? 43   HIS I C   1 
ATOM   9181  O  O   . HIS I  1 44  ? 81.417  41.860  16.189 1.00 31.01 ? 43   HIS I O   1 
ATOM   9182  C  CB  . HIS I  1 44  ? 81.746  42.212  19.201 1.00 27.75 ? 43   HIS I CB  1 
ATOM   9183  C  CG  . HIS I  1 44  ? 81.382  42.332  20.648 1.00 28.47 ? 43   HIS I CG  1 
ATOM   9184  N  ND1 . HIS I  1 44  ? 81.774  43.399  21.429 1.00 27.39 ? 43   HIS I ND1 1 
ATOM   9185  C  CD2 . HIS I  1 44  ? 80.656  41.523  21.455 1.00 28.16 ? 43   HIS I CD2 1 
ATOM   9186  C  CE1 . HIS I  1 44  ? 81.310  43.240  22.655 1.00 27.36 ? 43   HIS I CE1 1 
ATOM   9187  N  NE2 . HIS I  1 44  ? 80.627  42.110  22.699 1.00 29.06 ? 43   HIS I NE2 1 
ATOM   9188  N  N   . GLY I  1 45  ? 81.732  44.088  16.382 1.00 30.80 ? 44   GLY I N   1 
ATOM   9189  C  CA  . GLY I  1 45  ? 82.320  44.219  15.060 1.00 30.39 ? 44   GLY I CA  1 
ATOM   9190  C  C   . GLY I  1 45  ? 83.482  43.259  14.906 1.00 29.15 ? 44   GLY I C   1 
ATOM   9191  O  O   . GLY I  1 45  ? 84.198  43.000  15.868 1.00 29.43 ? 44   GLY I O   1 
ATOM   9192  N  N   . PHE I  1 46  ? 83.682  42.750  13.694 1.00 30.23 ? 45   PHE I N   1 
ATOM   9193  C  CA  . PHE I  1 46  ? 84.738  41.772  13.424 1.00 32.39 ? 45   PHE I CA  1 
ATOM   9194  C  C   . PHE I  1 46  ? 85.312  42.055  12.039 1.00 32.74 ? 45   PHE I C   1 
ATOM   9195  O  O   . PHE I  1 46  ? 84.655  41.780  11.037 1.00 32.81 ? 45   PHE I O   1 
ATOM   9196  C  CB  . PHE I  1 46  ? 84.111  40.366  13.466 1.00 31.06 ? 45   PHE I CB  1 
ATOM   9197  C  CG  . PHE I  1 46  ? 85.104  39.231  13.571 1.00 30.54 ? 45   PHE I CG  1 
ATOM   9198  C  CD1 . PHE I  1 46  ? 85.959  39.129  14.663 1.00 31.50 ? 45   PHE I CD1 1 
ATOM   9199  C  CD2 . PHE I  1 46  ? 85.124  38.222  12.610 1.00 29.45 ? 45   PHE I CD2 1 
ATOM   9200  C  CE1 . PHE I  1 46  ? 86.823  38.031  14.799 1.00 30.88 ? 45   PHE I CE1 1 
ATOM   9201  C  CE2 . PHE I  1 46  ? 85.978  37.126  12.735 1.00 30.77 ? 45   PHE I CE2 1 
ATOM   9202  C  CZ  . PHE I  1 46  ? 86.828  37.031  13.833 1.00 29.27 ? 45   PHE I CZ  1 
ATOM   9203  N  N   . HIS I  1 47  ? 86.524  42.609  11.969 1.00 33.49 ? 46   HIS I N   1 
ATOM   9204  C  CA  . HIS I  1 47  ? 87.120  42.911  10.664 1.00 34.12 ? 46   HIS I CA  1 
ATOM   9205  C  C   . HIS I  1 47  ? 88.617  42.652  10.554 1.00 34.81 ? 46   HIS I C   1 
ATOM   9206  O  O   . HIS I  1 47  ? 89.329  42.528  11.551 1.00 33.28 ? 46   HIS I O   1 
ATOM   9207  C  CB  . HIS I  1 47  ? 86.894  44.379  10.269 1.00 34.62 ? 46   HIS I CB  1 
ATOM   9208  C  CG  . HIS I  1 47  ? 85.657  44.992  10.852 1.00 35.99 ? 46   HIS I CG  1 
ATOM   9209  N  ND1 . HIS I  1 47  ? 85.657  45.650  12.059 1.00 35.29 ? 46   HIS I ND1 1 
ATOM   9210  C  CD2 . HIS I  1 47  ? 84.386  45.034  10.394 1.00 35.97 ? 46   HIS I CD2 1 
ATOM   9211  C  CE1 . HIS I  1 47  ? 84.432  46.075  12.326 1.00 35.65 ? 46   HIS I CE1 1 
ATOM   9212  N  NE2 . HIS I  1 47  ? 83.643  45.712  11.329 1.00 36.39 ? 46   HIS I NE2 1 
ATOM   9213  N  N   . VAL I  1 48  ? 89.082  42.573  9.313  1.00 35.37 ? 47   VAL I N   1 
ATOM   9214  C  CA  . VAL I  1 48  ? 90.498  42.400  9.043  1.00 36.75 ? 47   VAL I CA  1 
ATOM   9215  C  C   . VAL I  1 48  ? 90.987  43.795  8.664  1.00 37.86 ? 47   VAL I C   1 
ATOM   9216  O  O   . VAL I  1 48  ? 90.517  44.378  7.685  1.00 37.29 ? 47   VAL I O   1 
ATOM   9217  C  CB  . VAL I  1 48  ? 90.752  41.448  7.853  1.00 36.75 ? 47   VAL I CB  1 
ATOM   9218  C  CG1 . VAL I  1 48  ? 92.225  41.506  7.449  1.00 35.66 ? 47   VAL I CG1 1 
ATOM   9219  C  CG2 . VAL I  1 48  ? 90.369  40.021  8.231  1.00 36.07 ? 47   VAL I CG2 1 
ATOM   9220  N  N   . HIS I  1 49  ? 91.900  44.345  9.453  1.00 38.91 ? 48   HIS I N   1 
ATOM   9221  C  CA  . HIS I  1 49  ? 92.435  45.665  9.155  1.00 39.39 ? 48   HIS I CA  1 
ATOM   9222  C  C   . HIS I  1 49  ? 93.688  45.559  8.292  1.00 40.48 ? 48   HIS I C   1 
ATOM   9223  O  O   . HIS I  1 49  ? 94.381  44.540  8.294  1.00 40.90 ? 48   HIS I O   1 
ATOM   9224  C  CB  . HIS I  1 49  ? 92.722  46.435  10.443 1.00 39.55 ? 48   HIS I CB  1 
ATOM   9225  C  CG  . HIS I  1 49  ? 91.483  46.834  11.183 1.00 41.08 ? 48   HIS I CG  1 
ATOM   9226  N  ND1 . HIS I  1 49  ? 91.375  48.030  11.864 1.00 42.14 ? 48   HIS I ND1 1 
ATOM   9227  C  CD2 . HIS I  1 49  ? 90.298  46.206  11.337 1.00 41.10 ? 48   HIS I CD2 1 
ATOM   9228  C  CE1 . HIS I  1 49  ? 90.174  48.120  12.400 1.00 41.52 ? 48   HIS I CE1 1 
ATOM   9229  N  NE2 . HIS I  1 49  ? 89.495  47.025  12.097 1.00 43.01 ? 48   HIS I NE2 1 
ATOM   9230  N  N   . GLU I  1 50  ? 93.963  46.629  7.555  1.00 40.84 ? 49   GLU I N   1 
ATOM   9231  C  CA  . GLU I  1 50  ? 95.085  46.699  6.630  1.00 40.97 ? 49   GLU I CA  1 
ATOM   9232  C  C   . GLU I  1 50  ? 96.487  46.298  7.097  1.00 39.56 ? 49   GLU I C   1 
ATOM   9233  O  O   . GLU I  1 50  ? 97.141  45.493  6.438  1.00 39.49 ? 49   GLU I O   1 
ATOM   9234  C  CB  . GLU I  1 50  ? 95.153  48.107  6.025  1.00 42.43 ? 49   GLU I CB  1 
ATOM   9235  C  CG  . GLU I  1 50  ? 96.142  48.235  4.879  1.00 43.57 ? 49   GLU I CG  1 
ATOM   9236  C  CD  . GLU I  1 50  ? 96.092  49.595  4.204  1.00 44.78 ? 49   GLU I CD  1 
ATOM   9237  O  OE1 . GLU I  1 50  ? 96.726  49.747  3.140  1.00 44.52 ? 49   GLU I OE1 1 
ATOM   9238  O  OE2 . GLU I  1 50  ? 95.425  50.508  4.736  1.00 43.81 ? 49   GLU I OE2 1 
ATOM   9239  N  N   . PHE I  1 51  ? 96.954  46.844  8.216  1.00 38.85 ? 50   PHE I N   1 
ATOM   9240  C  CA  . PHE I  1 51  ? 98.315  46.547  8.676  1.00 38.76 ? 50   PHE I CA  1 
ATOM   9241  C  C   . PHE I  1 51  ? 98.473  45.595  9.854  1.00 38.10 ? 50   PHE I C   1 
ATOM   9242  O  O   . PHE I  1 51  ? 97.769  45.707  10.857 1.00 38.24 ? 50   PHE I O   1 
ATOM   9243  C  CB  . PHE I  1 51  ? 99.037  47.854  9.023  1.00 38.86 ? 50   PHE I CB  1 
ATOM   9244  C  CG  . PHE I  1 51  ? 98.897  48.918  7.980  1.00 39.51 ? 50   PHE I CG  1 
ATOM   9245  C  CD1 . PHE I  1 51  ? 99.411  48.730  6.703  1.00 39.29 ? 50   PHE I CD1 1 
ATOM   9246  C  CD2 . PHE I  1 51  ? 98.232  50.104  8.270  1.00 40.12 ? 50   PHE I CD2 1 
ATOM   9247  C  CE1 . PHE I  1 51  ? 99.266  49.708  5.727  1.00 39.72 ? 50   PHE I CE1 1 
ATOM   9248  C  CE2 . PHE I  1 51  ? 98.081  51.090  7.300  1.00 40.55 ? 50   PHE I CE2 1 
ATOM   9249  C  CZ  . PHE I  1 51  ? 98.597  50.890  6.026  1.00 40.60 ? 50   PHE I CZ  1 
ATOM   9250  N  N   . GLY I  1 52  ? 99.422  44.670  9.727  1.00 37.70 ? 51   GLY I N   1 
ATOM   9251  C  CA  . GLY I  1 52  ? 99.699  43.727  10.796 1.00 37.43 ? 51   GLY I CA  1 
ATOM   9252  C  C   . GLY I  1 52  ? 100.725 44.359  11.717 1.00 37.56 ? 51   GLY I C   1 
ATOM   9253  O  O   . GLY I  1 52  ? 101.761 43.765  12.029 1.00 38.77 ? 51   GLY I O   1 
ATOM   9254  N  N   . ASP I  1 53  ? 100.423 45.579  12.151 1.00 39.10 ? 52   ASP I N   1 
ATOM   9255  C  CA  . ASP I  1 53  ? 101.300 46.362  13.016 1.00 37.08 ? 52   ASP I CA  1 
ATOM   9256  C  C   . ASP I  1 53  ? 100.661 46.602  14.376 1.00 36.27 ? 52   ASP I C   1 
ATOM   9257  O  O   . ASP I  1 53  ? 99.651  47.291  14.481 1.00 35.97 ? 52   ASP I O   1 
ATOM   9258  C  CB  . ASP I  1 53  ? 101.607 47.693  12.318 1.00 39.26 ? 52   ASP I CB  1 
ATOM   9259  C  CG  . ASP I  1 53  ? 102.474 48.629  13.152 1.00 39.13 ? 52   ASP I CG  1 
ATOM   9260  O  OD1 . ASP I  1 53  ? 103.063 49.548  12.548 1.00 39.91 ? 52   ASP I OD1 1 
ATOM   9261  O  OD2 . ASP I  1 53  ? 102.561 48.466  14.388 1.00 38.61 ? 52   ASP I OD2 1 
ATOM   9262  N  N   . ASN I  1 54  ? 101.267 46.039  15.416 1.00 36.20 ? 53   ASN I N   1 
ATOM   9263  C  CA  . ASN I  1 54  ? 100.761 46.175  16.778 1.00 37.50 ? 53   ASN I CA  1 
ATOM   9264  C  C   . ASN I  1 54  ? 101.707 47.000  17.662 1.00 38.02 ? 53   ASN I C   1 
ATOM   9265  O  O   . ASN I  1 54  ? 101.651 46.915  18.891 1.00 36.29 ? 53   ASN I O   1 
ATOM   9266  C  CB  . ASN I  1 54  ? 100.573 44.780  17.390 1.00 38.35 ? 53   ASN I CB  1 
ATOM   9267  C  CG  . ASN I  1 54  ? 99.833  44.810  18.715 1.00 40.05 ? 53   ASN I CG  1 
ATOM   9268  O  OD1 . ASN I  1 54  ? 100.201 44.113  19.659 1.00 41.62 ? 53   ASN I OD1 1 
ATOM   9269  N  ND2 . ASN I  1 54  ? 98.773  45.606  18.786 1.00 42.59 ? 53   ASN I ND2 1 
ATOM   9270  N  N   . THR I  1 55  ? 102.572 47.799  17.043 1.00 39.29 ? 54   THR I N   1 
ATOM   9271  C  CA  . THR I  1 55  ? 103.520 48.612  17.807 1.00 42.29 ? 54   THR I CA  1 
ATOM   9272  C  C   . THR I  1 55  ? 102.828 49.423  18.897 1.00 43.24 ? 54   THR I C   1 
ATOM   9273  O  O   . THR I  1 55  ? 103.263 49.427  20.049 1.00 44.40 ? 54   THR I O   1 
ATOM   9274  C  CB  . THR I  1 55  ? 104.291 49.577  16.900 1.00 41.96 ? 54   THR I CB  1 
ATOM   9275  O  OG1 . THR I  1 55  ? 103.366 50.426  16.215 1.00 44.20 ? 54   THR I OG1 1 
ATOM   9276  C  CG2 . THR I  1 55  ? 105.117 48.803  15.884 1.00 40.86 ? 54   THR I CG2 1 
ATOM   9277  N  N   . ALA I  1 56  ? 101.748 50.104  18.532 1.00 44.45 ? 55   ALA I N   1 
ATOM   9278  C  CA  . ALA I  1 56  ? 100.992 50.903  19.489 1.00 45.96 ? 55   ALA I CA  1 
ATOM   9279  C  C   . ALA I  1 56  ? 99.584  50.331  19.647 1.00 46.41 ? 55   ALA I C   1 
ATOM   9280  O  O   . ALA I  1 56  ? 98.598  50.966  19.270 1.00 47.59 ? 55   ALA I O   1 
ATOM   9281  C  CB  . ALA I  1 56  ? 100.921 52.358  19.020 1.00 45.92 ? 55   ALA I CB  1 
ATOM   9282  N  N   . GLY I  1 57  ? 99.496  49.127  20.203 1.00 45.60 ? 56   GLY I N   1 
ATOM   9283  C  CA  . GLY I  1 57  ? 98.199  48.500  20.389 1.00 43.96 ? 56   GLY I CA  1 
ATOM   9284  C  C   . GLY I  1 57  ? 97.504  48.232  19.067 1.00 42.81 ? 56   GLY I C   1 
ATOM   9285  O  O   . GLY I  1 57  ? 98.127  48.305  18.006 1.00 42.41 ? 56   GLY I O   1 
ATOM   9286  N  N   . CYS I  1 58  ? 96.209  47.933  19.125 1.00 41.21 ? 57   CYS I N   1 
ATOM   9287  C  CA  . CYS I  1 58  ? 95.435  47.644  17.921 1.00 40.35 ? 57   CYS I CA  1 
ATOM   9288  C  C   . CYS I  1 58  ? 95.248  48.867  17.028 1.00 39.85 ? 57   CYS I C   1 
ATOM   9289  O  O   . CYS I  1 58  ? 94.839  48.745  15.872 1.00 38.80 ? 57   CYS I O   1 
ATOM   9290  C  CB  . CYS I  1 58  ? 94.069  47.063  18.302 1.00 38.52 ? 57   CYS I CB  1 
ATOM   9291  S  SG  . CYS I  1 58  ? 94.167  45.549  19.315 1.00 39.42 ? 57   CYS I SG  1 
ATOM   9292  N  N   . THR I  1 59  ? 95.559  50.044  17.562 1.00 40.67 ? 58   THR I N   1 
ATOM   9293  C  CA  . THR I  1 59  ? 95.416  51.283  16.806 1.00 40.83 ? 58   THR I CA  1 
ATOM   9294  C  C   . THR I  1 59  ? 96.307  51.281  15.572 1.00 40.83 ? 58   THR I C   1 
ATOM   9295  O  O   . THR I  1 59  ? 95.920  51.779  14.514 1.00 40.92 ? 58   THR I O   1 
ATOM   9296  C  CB  . THR I  1 59  ? 95.783  52.506  17.667 1.00 43.23 ? 58   THR I CB  1 
ATOM   9297  O  OG1 . THR I  1 59  ? 95.033  52.474  18.889 1.00 43.65 ? 58   THR I OG1 1 
ATOM   9298  C  CG2 . THR I  1 59  ? 95.459  53.793  16.923 1.00 42.48 ? 58   THR I CG2 1 
ATOM   9299  N  N   . SER I  1 60  ? 97.494  50.701  15.706 1.00 40.23 ? 59   SER I N   1 
ATOM   9300  C  CA  . SER I  1 60  ? 98.455  50.643  14.608 1.00 39.25 ? 59   SER I CA  1 
ATOM   9301  C  C   . SER I  1 60  ? 97.978  49.800  13.419 1.00 38.44 ? 59   SER I C   1 
ATOM   9302  O  O   . SER I  1 60  ? 98.522  49.903  12.315 1.00 35.48 ? 59   SER I O   1 
ATOM   9303  C  CB  . SER I  1 60  ? 99.787  50.093  15.121 1.00 40.11 ? 59   SER I CB  1 
ATOM   9304  O  OG  . SER I  1 60  ? 100.054 50.560  16.431 1.00 43.69 ? 59   SER I OG  1 
ATOM   9305  N  N   . ALA I  1 61  ? 96.962  48.971  13.643 1.00 37.56 ? 60   ALA I N   1 
ATOM   9306  C  CA  . ALA I  1 61  ? 96.434  48.113  12.588 1.00 36.98 ? 60   ALA I CA  1 
ATOM   9307  C  C   . ALA I  1 61  ? 95.890  48.916  11.413 1.00 37.46 ? 60   ALA I C   1 
ATOM   9308  O  O   . ALA I  1 61  ? 95.732  48.392  10.309 1.00 36.34 ? 60   ALA I O   1 
ATOM   9309  C  CB  . ALA I  1 61  ? 95.345  47.203  13.150 1.00 37.76 ? 60   ALA I CB  1 
ATOM   9310  N  N   . GLY I  1 62  ? 95.612  50.193  11.646 1.00 38.85 ? 61   GLY I N   1 
ATOM   9311  C  CA  . GLY I  1 62  ? 95.086  51.025  10.579 1.00 40.42 ? 61   GLY I CA  1 
ATOM   9312  C  C   . GLY I  1 62  ? 93.602  50.799  10.353 1.00 41.02 ? 61   GLY I C   1 
ATOM   9313  O  O   . GLY I  1 62  ? 92.905  50.321  11.249 1.00 41.60 ? 61   GLY I O   1 
ATOM   9314  N  N   . PRO I  1 63  ? 93.086  51.136  9.161  1.00 41.83 ? 62   PRO I N   1 
ATOM   9315  C  CA  . PRO I  1 63  ? 91.672  50.970  8.821  1.00 42.35 ? 62   PRO I CA  1 
ATOM   9316  C  C   . PRO I  1 63  ? 91.380  49.575  8.279  1.00 42.63 ? 62   PRO I C   1 
ATOM   9317  O  O   . PRO I  1 63  ? 92.278  48.738  8.176  1.00 43.42 ? 62   PRO I O   1 
ATOM   9318  C  CB  . PRO I  1 63  ? 91.460  52.042  7.766  1.00 42.08 ? 62   PRO I CB  1 
ATOM   9319  C  CG  . PRO I  1 63  ? 92.732  51.930  6.981  1.00 42.38 ? 62   PRO I CG  1 
ATOM   9320  C  CD  . PRO I  1 63  ? 93.800  51.828  8.070  1.00 42.15 ? 62   PRO I CD  1 
ATOM   9321  N  N   . HIS I  1 64  ? 90.121  49.341  7.922  1.00 42.19 ? 63   HIS I N   1 
ATOM   9322  C  CA  . HIS I  1 64  ? 89.697  48.055  7.382  1.00 42.18 ? 63   HIS I CA  1 
ATOM   9323  C  C   . HIS I  1 64  ? 90.391  47.784  6.053  1.00 42.89 ? 63   HIS I C   1 
ATOM   9324  O  O   . HIS I  1 64  ? 90.456  48.661  5.191  1.00 43.14 ? 63   HIS I O   1 
ATOM   9325  C  CB  . HIS I  1 64  ? 88.173  48.044  7.170  1.00 41.04 ? 63   HIS I CB  1 
ATOM   9326  C  CG  . HIS I  1 64  ? 87.389  48.274  8.423  1.00 40.12 ? 63   HIS I CG  1 
ATOM   9327  N  ND1 . HIS I  1 64  ? 86.006  48.350  8.436  1.00 39.73 ? 63   HIS I ND1 1 
ATOM   9328  C  CD2 . HIS I  1 64  ? 87.780  48.453  9.705  1.00 39.06 ? 63   HIS I CD2 1 
ATOM   9329  C  CE1 . HIS I  1 64  ? 85.593  48.565  9.666  1.00 39.32 ? 63   HIS I CE1 1 
ATOM   9330  N  NE2 . HIS I  1 64  ? 86.648  48.633  10.461 1.00 40.02 ? 63   HIS I NE2 1 
ATOM   9331  N  N   . PHE I  1 65  ? 90.915  46.574  5.890  1.00 43.59 ? 64   PHE I N   1 
ATOM   9332  C  CA  . PHE I  1 65  ? 91.578  46.211  4.644  1.00 45.16 ? 64   PHE I CA  1 
ATOM   9333  C  C   . PHE I  1 65  ? 90.589  46.495  3.515  1.00 47.13 ? 64   PHE I C   1 
ATOM   9334  O  O   . PHE I  1 65  ? 89.563  45.821  3.397  1.00 46.37 ? 64   PHE I O   1 
ATOM   9335  C  CB  . PHE I  1 65  ? 91.942  44.725  4.644  1.00 43.75 ? 64   PHE I CB  1 
ATOM   9336  C  CG  . PHE I  1 65  ? 92.700  44.284  3.422  1.00 44.49 ? 64   PHE I CG  1 
ATOM   9337  C  CD1 . PHE I  1 65  ? 92.578  42.981  2.947  1.00 43.46 ? 64   PHE I CD1 1 
ATOM   9338  C  CD2 . PHE I  1 65  ? 93.543  45.167  2.747  1.00 44.05 ? 64   PHE I CD2 1 
ATOM   9339  C  CE1 . PHE I  1 65  ? 93.281  42.562  1.818  1.00 44.04 ? 64   PHE I CE1 1 
ATOM   9340  C  CE2 . PHE I  1 65  ? 94.250  44.758  1.619  1.00 42.64 ? 64   PHE I CE2 1 
ATOM   9341  C  CZ  . PHE I  1 65  ? 94.119  43.454  1.154  1.00 43.68 ? 64   PHE I CZ  1 
ATOM   9342  N  N   . ASN I  1 66  ? 90.897  47.493  2.691  1.00 48.69 ? 65   ASN I N   1 
ATOM   9343  C  CA  . ASN I  1 66  ? 90.017  47.875  1.591  1.00 49.98 ? 65   ASN I CA  1 
ATOM   9344  C  C   . ASN I  1 66  ? 90.792  48.149  0.300  1.00 51.69 ? 65   ASN I C   1 
ATOM   9345  O  O   . ASN I  1 66  ? 90.900  49.291  -0.146 1.00 51.68 ? 65   ASN I O   1 
ATOM   9346  C  CB  . ASN I  1 66  ? 89.205  49.109  2.001  1.00 50.13 ? 65   ASN I CB  1 
ATOM   9347  C  CG  . ASN I  1 66  ? 88.264  49.581  0.914  1.00 50.45 ? 65   ASN I CG  1 
ATOM   9348  O  OD1 . ASN I  1 66  ? 87.612  48.779  0.248  1.00 50.29 ? 65   ASN I OD1 1 
ATOM   9349  N  ND2 . ASN I  1 66  ? 88.176  50.894  0.740  1.00 50.64 ? 65   ASN I ND2 1 
ATOM   9350  N  N   . PRO I  1 67  ? 91.332  47.088  -0.322 1.00 52.36 ? 66   PRO I N   1 
ATOM   9351  C  CA  . PRO I  1 67  ? 92.105  47.178  -1.563 1.00 53.22 ? 66   PRO I CA  1 
ATOM   9352  C  C   . PRO I  1 67  ? 91.314  47.610  -2.800 1.00 54.42 ? 66   PRO I C   1 
ATOM   9353  O  O   . PRO I  1 67  ? 91.903  48.025  -3.800 1.00 54.63 ? 66   PRO I O   1 
ATOM   9354  C  CB  . PRO I  1 67  ? 92.677  45.772  -1.708 1.00 52.42 ? 66   PRO I CB  1 
ATOM   9355  C  CG  . PRO I  1 67  ? 91.596  44.923  -1.121 1.00 52.25 ? 66   PRO I CG  1 
ATOM   9356  C  CD  . PRO I  1 67  ? 91.240  45.688  0.131  1.00 51.81 ? 66   PRO I CD  1 
ATOM   9357  N  N   . LEU I  1 68  ? 89.990  47.513  -2.742 1.00 53.61 ? 67   LEU I N   1 
ATOM   9358  C  CA  . LEU I  1 68  ? 89.173  47.906  -3.882 1.00 53.82 ? 67   LEU I CA  1 
ATOM   9359  C  C   . LEU I  1 68  ? 88.549  49.281  -3.684 1.00 53.92 ? 67   LEU I C   1 
ATOM   9360  O  O   . LEU I  1 68  ? 87.731  49.725  -4.489 1.00 54.51 ? 67   LEU I O   1 
ATOM   9361  C  CB  . LEU I  1 68  ? 88.085  46.862  -4.144 1.00 54.43 ? 67   LEU I CB  1 
ATOM   9362  C  CG  . LEU I  1 68  ? 88.591  45.452  -4.470 1.00 55.21 ? 67   LEU I CG  1 
ATOM   9363  C  CD1 . LEU I  1 68  ? 87.406  44.544  -4.760 1.00 54.92 ? 67   LEU I CD1 1 
ATOM   9364  C  CD2 . LEU I  1 68  ? 89.534  45.495  -5.669 1.00 54.93 ? 67   LEU I CD2 1 
ATOM   9365  N  N   . SER I  1 69  ? 88.946  49.952  -2.607 1.00 53.61 ? 68   SER I N   1 
ATOM   9366  C  CA  . SER I  1 69  ? 88.452  51.289  -2.295 1.00 54.29 ? 68   SER I CA  1 
ATOM   9367  C  C   . SER I  1 69  ? 86.936  51.429  -2.381 1.00 54.50 ? 68   SER I C   1 
ATOM   9368  O  O   . SER I  1 69  ? 86.423  52.257  -3.135 1.00 54.06 ? 68   SER I O   1 
ATOM   9369  C  CB  . SER I  1 69  ? 89.103  52.320  -3.225 1.00 54.17 ? 68   SER I CB  1 
ATOM   9370  O  OG  . SER I  1 69  ? 90.514  52.308  -3.098 1.00 55.50 ? 68   SER I OG  1 
ATOM   9371  N  N   . ARG I  1 70  ? 86.220  50.621  -1.606 1.00 54.33 ? 69   ARG I N   1 
ATOM   9372  C  CA  . ARG I  1 70  ? 84.764  50.681  -1.590 1.00 52.94 ? 69   ARG I CA  1 
ATOM   9373  C  C   . ARG I  1 70  ? 84.297  51.137  -0.214 1.00 51.94 ? 69   ARG I C   1 
ATOM   9374  O  O   . ARG I  1 70  ? 85.107  51.312  0.698  1.00 51.22 ? 69   ARG I O   1 
ATOM   9375  C  CB  . ARG I  1 70  ? 84.168  49.312  -1.922 1.00 53.65 ? 69   ARG I CB  1 
ATOM   9376  C  CG  . ARG I  1 70  ? 84.452  48.854  -3.344 1.00 55.88 ? 69   ARG I CG  1 
ATOM   9377  C  CD  . ARG I  1 70  ? 83.812  47.507  -3.636 1.00 57.46 ? 69   ARG I CD  1 
ATOM   9378  N  NE  . ARG I  1 70  ? 84.101  47.052  -4.993 1.00 58.53 ? 69   ARG I NE  1 
ATOM   9379  C  CZ  . ARG I  1 70  ? 83.696  45.890  -5.496 1.00 60.55 ? 69   ARG I CZ  1 
ATOM   9380  N  NH1 . ARG I  1 70  ? 84.009  45.560  -6.743 1.00 61.36 ? 69   ARG I NH1 1 
ATOM   9381  N  NH2 . ARG I  1 70  ? 82.979  45.055  -4.755 1.00 60.77 ? 69   ARG I NH2 1 
ATOM   9382  N  N   . LYS I  1 71  ? 82.993  51.340  -0.067 1.00 50.78 ? 70   LYS I N   1 
ATOM   9383  C  CA  . LYS I  1 71  ? 82.440  51.774  1.207  1.00 50.37 ? 70   LYS I CA  1 
ATOM   9384  C  C   . LYS I  1 71  ? 82.290  50.580  2.142  1.00 48.69 ? 70   LYS I C   1 
ATOM   9385  O  O   . LYS I  1 71  ? 82.330  49.429  1.706  1.00 46.97 ? 70   LYS I O   1 
ATOM   9386  C  CB  . LYS I  1 71  ? 81.077  52.438  0.994  1.00 51.99 ? 70   LYS I CB  1 
ATOM   9387  C  CG  . LYS I  1 71  ? 81.117  53.711  0.158  1.00 54.11 ? 70   LYS I CG  1 
ATOM   9388  C  CD  . LYS I  1 71  ? 81.819  54.838  0.890  0.00 55.76 ? 70   LYS I CD  1 
ATOM   9389  C  CE  . LYS I  1 71  ? 81.815  56.105  0.055  1.00 57.49 ? 70   LYS I CE  1 
ATOM   9390  N  NZ  . LYS I  1 71  ? 82.485  57.234  0.761  1.00 58.78 ? 70   LYS I NZ  1 
ATOM   9391  N  N   . HIS I  1 72  ? 82.122  50.863  3.429  1.00 48.38 ? 71   HIS I N   1 
ATOM   9392  C  CA  . HIS I  1 72  ? 81.961  49.815  4.428  1.00 48.05 ? 71   HIS I CA  1 
ATOM   9393  C  C   . HIS I  1 72  ? 80.587  49.170  4.288  1.00 47.21 ? 71   HIS I C   1 
ATOM   9394  O  O   . HIS I  1 72  ? 79.661  49.769  3.743  1.00 48.34 ? 71   HIS I O   1 
ATOM   9395  C  CB  . HIS I  1 72  ? 82.111  50.401  5.834  1.00 47.35 ? 71   HIS I CB  1 
ATOM   9396  C  CG  . HIS I  1 72  ? 81.951  49.394  6.928  1.00 48.32 ? 71   HIS I CG  1 
ATOM   9397  N  ND1 . HIS I  1 72  ? 82.870  48.389  7.157  1.00 47.69 ? 71   HIS I ND1 1 
ATOM   9398  C  CD2 . HIS I  1 72  ? 80.973  49.223  7.849  1.00 48.05 ? 71   HIS I CD2 1 
ATOM   9399  C  CE1 . HIS I  1 72  ? 82.463  47.648  8.171  1.00 48.36 ? 71   HIS I CE1 1 
ATOM   9400  N  NE2 . HIS I  1 72  ? 81.315  48.131  8.610  1.00 47.75 ? 71   HIS I NE2 1 
ATOM   9401  N  N   . GLY I  1 73  ? 80.464  47.944  4.781  1.00 46.84 ? 72   GLY I N   1 
ATOM   9402  C  CA  . GLY I  1 73  ? 79.199  47.238  4.715  1.00 44.04 ? 72   GLY I CA  1 
ATOM   9403  C  C   . GLY I  1 73  ? 79.301  45.911  5.436  1.00 43.20 ? 72   GLY I C   1 
ATOM   9404  O  O   . GLY I  1 73  ? 80.266  45.670  6.167  1.00 42.67 ? 72   GLY I O   1 
ATOM   9405  N  N   . GLY I  1 74  ? 78.302  45.056  5.241  1.00 41.58 ? 73   GLY I N   1 
ATOM   9406  C  CA  . GLY I  1 74  ? 78.312  43.746  5.863  1.00 39.38 ? 73   GLY I CA  1 
ATOM   9407  C  C   . GLY I  1 74  ? 78.915  42.758  4.887  1.00 39.43 ? 73   GLY I C   1 
ATOM   9408  O  O   . GLY I  1 74  ? 78.958  43.036  3.686  1.00 39.29 ? 73   GLY I O   1 
ATOM   9409  N  N   . PRO I  1 75  ? 79.386  41.594  5.360  1.00 39.02 ? 74   PRO I N   1 
ATOM   9410  C  CA  . PRO I  1 75  ? 79.987  40.596  4.473  1.00 40.37 ? 74   PRO I CA  1 
ATOM   9411  C  C   . PRO I  1 75  ? 79.100  40.142  3.317  1.00 41.90 ? 74   PRO I C   1 
ATOM   9412  O  O   . PRO I  1 75  ? 79.600  39.670  2.297  1.00 42.30 ? 74   PRO I O   1 
ATOM   9413  C  CB  . PRO I  1 75  ? 80.336  39.454  5.428  1.00 39.55 ? 74   PRO I CB  1 
ATOM   9414  C  CG  . PRO I  1 75  ? 79.300  39.588  6.510  1.00 38.71 ? 74   PRO I CG  1 
ATOM   9415  C  CD  . PRO I  1 75  ? 79.283  41.077  6.735  1.00 39.31 ? 74   PRO I CD  1 
ATOM   9416  N  N   . LYS I  1 76  ? 77.789  40.286  3.472  1.00 43.34 ? 75   LYS I N   1 
ATOM   9417  C  CA  . LYS I  1 76  ? 76.858  39.876  2.426  1.00 45.50 ? 75   LYS I CA  1 
ATOM   9418  C  C   . LYS I  1 76  ? 76.632  40.973  1.388  1.00 45.74 ? 75   LYS I C   1 
ATOM   9419  O  O   . LYS I  1 76  ? 76.065  40.725  0.327  1.00 45.53 ? 75   LYS I O   1 
ATOM   9420  C  CB  . LYS I  1 76  ? 75.526  39.460  3.055  1.00 46.11 ? 75   LYS I CB  1 
ATOM   9421  C  CG  . LYS I  1 76  ? 75.624  38.180  3.880  1.00 47.93 ? 75   LYS I CG  1 
ATOM   9422  C  CD  . LYS I  1 76  ? 74.596  38.136  5.011  1.00 49.88 ? 75   LYS I CD  1 
ATOM   9423  C  CE  . LYS I  1 76  ? 73.170  38.149  4.494  1.00 49.01 ? 75   LYS I CE  1 
ATOM   9424  N  NZ  . LYS I  1 76  ? 72.193  38.106  5.615  1.00 49.99 ? 75   LYS I NZ  1 
ATOM   9425  N  N   . ASP I  1 77  ? 77.087  42.183  1.695  1.00 45.86 ? 76   ASP I N   1 
ATOM   9426  C  CA  . ASP I  1 77  ? 76.927  43.315  0.787  1.00 47.37 ? 76   ASP I CA  1 
ATOM   9427  C  C   . ASP I  1 77  ? 77.968  43.330  -0.329 1.00 49.17 ? 76   ASP I C   1 
ATOM   9428  O  O   . ASP I  1 77  ? 79.143  43.031  -0.104 1.00 47.82 ? 76   ASP I O   1 
ATOM   9429  C  CB  . ASP I  1 77  ? 77.021  44.626  1.569  1.00 46.77 ? 76   ASP I CB  1 
ATOM   9430  C  CG  . ASP I  1 77  ? 75.849  44.832  2.500  1.00 46.83 ? 76   ASP I CG  1 
ATOM   9431  O  OD1 . ASP I  1 77  ? 75.987  45.605  3.471  1.00 46.17 ? 76   ASP I OD1 1 
ATOM   9432  O  OD2 . ASP I  1 77  ? 74.786  44.228  2.253  1.00 45.87 ? 76   ASP I OD2 1 
ATOM   9433  N  N   . GLU I  1 78  ? 77.528  43.677  -1.535 1.00 50.64 ? 77   GLU I N   1 
ATOM   9434  C  CA  . GLU I  1 78  ? 78.430  43.764  -2.678 1.00 51.90 ? 77   GLU I CA  1 
ATOM   9435  C  C   . GLU I  1 78  ? 79.421  44.884  -2.381 1.00 51.16 ? 77   GLU I C   1 
ATOM   9436  O  O   . GLU I  1 78  ? 80.636  44.705  -2.481 1.00 51.60 ? 77   GLU I O   1 
ATOM   9437  C  CB  . GLU I  1 78  ? 77.642  44.088  -3.952 1.00 54.93 ? 77   GLU I CB  1 
ATOM   9438  C  CG  . GLU I  1 78  ? 78.498  44.533  -5.130 0.00 58.40 ? 77   GLU I CG  1 
ATOM   9439  C  CD  . GLU I  1 78  ? 79.460  43.462  -5.607 1.00 61.17 ? 77   GLU I CD  1 
ATOM   9440  O  OE1 . GLU I  1 78  ? 80.261  43.751  -6.522 1.00 62.99 ? 77   GLU I OE1 1 
ATOM   9441  O  OE2 . GLU I  1 78  ? 79.414  42.332  -5.073 1.00 62.39 ? 77   GLU I OE2 1 
ATOM   9442  N  N   . GLU I  1 79  ? 78.887  46.039  -2.004 1.00 50.12 ? 78   GLU I N   1 
ATOM   9443  C  CA  . GLU I  1 79  ? 79.712  47.191  -1.677 1.00 49.68 ? 78   GLU I CA  1 
ATOM   9444  C  C   . GLU I  1 79  ? 80.236  47.041  -0.251 1.00 49.19 ? 78   GLU I C   1 
ATOM   9445  O  O   . GLU I  1 79  ? 79.519  47.306  0.717  1.00 47.85 ? 78   GLU I O   1 
ATOM   9446  C  CB  . GLU I  1 79  ? 78.890  48.478  -1.798 1.00 50.54 ? 78   GLU I CB  1 
ATOM   9447  C  CG  . GLU I  1 79  ? 79.664  49.760  -1.513 1.00 53.02 ? 78   GLU I CG  1 
ATOM   9448  C  CD  . GLU I  1 79  ? 80.698  50.079  -2.580 1.00 54.15 ? 78   GLU I CD  1 
ATOM   9449  O  OE1 . GLU I  1 79  ? 81.406  51.098  -2.433 1.00 53.55 ? 78   GLU I OE1 1 
ATOM   9450  O  OE2 . GLU I  1 79  ? 80.802  49.315  -3.566 1.00 55.40 ? 78   GLU I OE2 1 
ATOM   9451  N  N   . ARG I  1 80  ? 81.484  46.605  -0.124 1.00 48.28 ? 79   ARG I N   1 
ATOM   9452  C  CA  . ARG I  1 80  ? 82.089  46.435  1.189  1.00 47.37 ? 79   ARG I CA  1 
ATOM   9453  C  C   . ARG I  1 80  ? 83.598  46.288  1.114  1.00 46.68 ? 79   ARG I C   1 
ATOM   9454  O  O   . ARG I  1 80  ? 84.160  46.053  0.044  1.00 46.47 ? 79   ARG I O   1 
ATOM   9455  C  CB  . ARG I  1 80  ? 81.494  45.213  1.890  1.00 47.56 ? 79   ARG I CB  1 
ATOM   9456  C  CG  . ARG I  1 80  ? 81.708  43.892  1.167  1.00 46.77 ? 79   ARG I CG  1 
ATOM   9457  C  CD  . ARG I  1 80  ? 82.675  42.994  1.928  1.00 47.84 ? 79   ARG I CD  1 
ATOM   9458  N  NE  . ARG I  1 80  ? 82.331  41.583  1.778  1.00 47.58 ? 79   ARG I NE  1 
ATOM   9459  C  CZ  . ARG I  1 80  ? 82.978  40.582  2.367  1.00 47.42 ? 79   ARG I CZ  1 
ATOM   9460  N  NH1 . ARG I  1 80  ? 82.580  39.333  2.169  1.00 46.19 ? 79   ARG I NH1 1 
ATOM   9461  N  NH2 . ARG I  1 80  ? 84.026  40.820  3.145  1.00 45.19 ? 79   ARG I NH2 1 
ATOM   9462  N  N   . HIS I  1 81  ? 84.246  46.438  2.265  1.00 45.38 ? 80   HIS I N   1 
ATOM   9463  C  CA  . HIS I  1 81  ? 85.692  46.303  2.368  1.00 43.45 ? 80   HIS I CA  1 
ATOM   9464  C  C   . HIS I  1 81  ? 85.998  44.814  2.334  1.00 43.90 ? 80   HIS I C   1 
ATOM   9465  O  O   . HIS I  1 81  ? 85.204  44.004  2.814  1.00 44.83 ? 80   HIS I O   1 
ATOM   9466  C  CB  . HIS I  1 81  ? 86.182  46.886  3.696  1.00 42.18 ? 80   HIS I CB  1 
ATOM   9467  C  CG  . HIS I  1 81  ? 85.847  48.331  3.881  1.00 41.52 ? 80   HIS I CG  1 
ATOM   9468  N  ND1 . HIS I  1 81  ? 85.798  48.930  5.126  1.00 40.87 ? 80   HIS I ND1 1 
ATOM   9469  C  CD2 . HIS I  1 81  ? 85.556  49.306  2.989  1.00 40.95 ? 80   HIS I CD2 1 
ATOM   9470  C  CE1 . HIS I  1 81  ? 85.490  50.204  4.988  1.00 40.68 ? 80   HIS I CE1 1 
ATOM   9471  N  NE2 . HIS I  1 81  ? 85.338  50.461  3.699  1.00 41.99 ? 80   HIS I NE2 1 
ATOM   9472  N  N   . VAL I  1 82  ? 87.138  44.443  1.767  1.00 41.82 ? 81   VAL I N   1 
ATOM   9473  C  CA  . VAL I  1 82  ? 87.497  43.036  1.721  1.00 40.84 ? 81   VAL I CA  1 
ATOM   9474  C  C   . VAL I  1 82  ? 87.517  42.470  3.140  1.00 39.70 ? 81   VAL I C   1 
ATOM   9475  O  O   . VAL I  1 82  ? 87.154  41.317  3.359  1.00 39.37 ? 81   VAL I O   1 
ATOM   9476  C  CB  . VAL I  1 82  ? 88.888  42.827  1.071  1.00 41.35 ? 81   VAL I CB  1 
ATOM   9477  C  CG1 . VAL I  1 82  ? 89.336  41.377  1.233  1.00 39.80 ? 81   VAL I CG1 1 
ATOM   9478  C  CG2 . VAL I  1 82  ? 88.824  43.190  -0.403 1.00 41.18 ? 81   VAL I CG2 1 
ATOM   9479  N  N   . GLY I  1 83  ? 87.922  43.297  4.101  1.00 38.42 ? 82   GLY I N   1 
ATOM   9480  C  CA  . GLY I  1 83  ? 88.006  42.854  5.484  1.00 37.50 ? 82   GLY I CA  1 
ATOM   9481  C  C   . GLY I  1 83  ? 86.740  42.920  6.323  1.00 37.54 ? 82   GLY I C   1 
ATOM   9482  O  O   . GLY I  1 83  ? 86.795  42.674  7.530  1.00 36.27 ? 82   GLY I O   1 
ATOM   9483  N  N   . ASP I  1 84  ? 85.604  43.242  5.709  1.00 36.27 ? 83   ASP I N   1 
ATOM   9484  C  CA  . ASP I  1 84  ? 84.348  43.324  6.453  1.00 38.42 ? 83   ASP I CA  1 
ATOM   9485  C  C   . ASP I  1 84  ? 83.739  41.944  6.744  1.00 37.69 ? 83   ASP I C   1 
ATOM   9486  O  O   . ASP I  1 84  ? 83.151  41.315  5.867  1.00 38.77 ? 83   ASP I O   1 
ATOM   9487  C  CB  . ASP I  1 84  ? 83.330  44.189  5.696  1.00 39.14 ? 83   ASP I CB  1 
ATOM   9488  C  CG  . ASP I  1 84  ? 83.746  45.649  5.617  1.00 41.27 ? 83   ASP I CG  1 
ATOM   9489  O  OD1 . ASP I  1 84  ? 84.630  46.062  6.397  1.00 41.68 ? 83   ASP I OD1 1 
ATOM   9490  O  OD2 . ASP I  1 84  ? 83.183  46.389  4.784  1.00 43.79 ? 83   ASP I OD2 1 
ATOM   9491  N  N   . LEU I  1 85  ? 83.871  41.482  7.984  1.00 36.31 ? 84   LEU I N   1 
ATOM   9492  C  CA  . LEU I  1 85  ? 83.331  40.181  8.362  1.00 35.51 ? 84   LEU I CA  1 
ATOM   9493  C  C   . LEU I  1 85  ? 82.130  40.268  9.303  1.00 35.11 ? 84   LEU I C   1 
ATOM   9494  O  O   . LEU I  1 85  ? 81.845  39.325  10.041 1.00 35.89 ? 84   LEU I O   1 
ATOM   9495  C  CB  . LEU I  1 85  ? 84.429  39.316  8.993  1.00 34.24 ? 84   LEU I CB  1 
ATOM   9496  C  CG  . LEU I  1 85  ? 85.594  38.986  8.055  1.00 34.20 ? 84   LEU I CG  1 
ATOM   9497  C  CD1 . LEU I  1 85  ? 86.572  38.062  8.754  1.00 34.75 ? 84   LEU I CD1 1 
ATOM   9498  C  CD2 . LEU I  1 85  ? 85.062  38.332  6.788  1.00 32.96 ? 84   LEU I CD2 1 
ATOM   9499  N  N   . GLY I  1 86  ? 81.438  41.404  9.276  1.00 33.68 ? 85   GLY I N   1 
ATOM   9500  C  CA  . GLY I  1 86  ? 80.257  41.589  10.105 1.00 32.75 ? 85   GLY I CA  1 
ATOM   9501  C  C   . GLY I  1 86  ? 80.405  41.602  11.617 1.00 32.52 ? 85   GLY I C   1 
ATOM   9502  O  O   . GLY I  1 86  ? 81.277  42.276  12.171 1.00 32.74 ? 85   GLY I O   1 
ATOM   9503  N  N   . ASN I  1 87  ? 79.529  40.854  12.285 1.00 31.80 ? 86   ASN I N   1 
ATOM   9504  C  CA  . ASN I  1 87  ? 79.517  40.764  13.742 1.00 28.97 ? 86   ASN I CA  1 
ATOM   9505  C  C   . ASN I  1 87  ? 79.600  39.334  14.249 1.00 29.84 ? 86   ASN I C   1 
ATOM   9506  O  O   . ASN I  1 87  ? 79.165  38.395  13.577 1.00 28.62 ? 86   ASN I O   1 
ATOM   9507  C  CB  . ASN I  1 87  ? 78.219  41.350  14.306 1.00 30.09 ? 86   ASN I CB  1 
ATOM   9508  C  CG  . ASN I  1 87  ? 78.091  42.834  14.077 1.00 31.56 ? 86   ASN I CG  1 
ATOM   9509  O  OD1 . ASN I  1 87  ? 78.753  43.634  14.737 1.00 33.27 ? 86   ASN I OD1 1 
ATOM   9510  N  ND2 . ASN I  1 87  ? 77.231  43.214  13.139 1.00 30.92 ? 86   ASN I ND2 1 
ATOM   9511  N  N   . VAL I  1 88  ? 80.155  39.187  15.447 1.00 28.23 ? 87   VAL I N   1 
ATOM   9512  C  CA  . VAL I  1 88  ? 80.222  37.902  16.117 1.00 28.30 ? 87   VAL I CA  1 
ATOM   9513  C  C   . VAL I  1 88  ? 79.316  38.139  17.322 1.00 28.80 ? 87   VAL I C   1 
ATOM   9514  O  O   . VAL I  1 88  ? 79.106  39.287  17.722 1.00 27.38 ? 87   VAL I O   1 
ATOM   9515  C  CB  . VAL I  1 88  ? 81.656  37.543  16.573 1.00 29.72 ? 87   VAL I CB  1 
ATOM   9516  C  CG1 . VAL I  1 88  ? 82.527  37.266  15.353 1.00 27.55 ? 87   VAL I CG1 1 
ATOM   9517  C  CG2 . VAL I  1 88  ? 82.245  38.669  17.412 1.00 29.96 ? 87   VAL I CG2 1 
ATOM   9518  N  N   . THR I  1 89  ? 78.771  37.073  17.894 1.00 26.81 ? 88   THR I N   1 
ATOM   9519  C  CA  . THR I  1 89  ? 77.862  37.217  19.023 1.00 26.98 ? 88   THR I CA  1 
ATOM   9520  C  C   . THR I  1 89  ? 78.358  36.501  20.273 1.00 27.55 ? 88   THR I C   1 
ATOM   9521  O  O   . THR I  1 89  ? 78.580  35.293  20.255 1.00 25.51 ? 88   THR I O   1 
ATOM   9522  C  CB  . THR I  1 89  ? 76.466  36.668  18.646 1.00 28.07 ? 88   THR I CB  1 
ATOM   9523  O  OG1 . THR I  1 89  ? 76.048  37.259  17.408 1.00 27.86 ? 88   THR I OG1 1 
ATOM   9524  C  CG2 . THR I  1 89  ? 75.443  36.989  19.733 1.00 26.83 ? 88   THR I CG2 1 
ATOM   9525  N  N   . ALA I  1 90  ? 78.538  37.258  21.353 1.00 26.49 ? 89   ALA I N   1 
ATOM   9526  C  CA  . ALA I  1 90  ? 78.996  36.693  22.614 1.00 27.18 ? 89   ALA I CA  1 
ATOM   9527  C  C   . ALA I  1 90  ? 77.766  36.361  23.443 1.00 27.55 ? 89   ALA I C   1 
ATOM   9528  O  O   . ALA I  1 90  ? 76.834  37.162  23.520 1.00 28.80 ? 89   ALA I O   1 
ATOM   9529  C  CB  . ALA I  1 90  ? 79.876  37.700  23.362 1.00 25.75 ? 89   ALA I CB  1 
ATOM   9530  N  N   . ASP I  1 91  ? 77.761  35.186  24.064 1.00 28.04 ? 90   ASP I N   1 
ATOM   9531  C  CA  . ASP I  1 91  ? 76.623  34.782  24.879 1.00 28.26 ? 90   ASP I CA  1 
ATOM   9532  C  C   . ASP I  1 91  ? 76.633  35.444  26.256 1.00 29.62 ? 90   ASP I C   1 
ATOM   9533  O  O   . ASP I  1 91  ? 77.519  36.236  26.571 1.00 26.76 ? 90   ASP I O   1 
ATOM   9534  C  CB  . ASP I  1 91  ? 76.576  33.255  25.013 1.00 28.01 ? 90   ASP I CB  1 
ATOM   9535  C  CG  . ASP I  1 91  ? 77.784  32.678  25.739 1.00 31.38 ? 90   ASP I CG  1 
ATOM   9536  O  OD1 . ASP I  1 91  ? 78.003  31.456  25.613 1.00 33.19 ? 90   ASP I OD1 1 
ATOM   9537  O  OD2 . ASP I  1 91  ? 78.502  33.419  26.440 1.00 28.08 ? 90   ASP I OD2 1 
ATOM   9538  N  N   . LYS I  1 92  ? 75.629  35.117  27.062 1.00 31.02 ? 91   LYS I N   1 
ATOM   9539  C  CA  . LYS I  1 92  ? 75.477  35.668  28.405 1.00 33.00 ? 91   LYS I CA  1 
ATOM   9540  C  C   . LYS I  1 92  ? 76.763  35.629  29.226 1.00 34.06 ? 91   LYS I C   1 
ATOM   9541  O  O   . LYS I  1 92  ? 76.974  36.477  30.096 1.00 33.37 ? 91   LYS I O   1 
ATOM   9542  C  CB  . LYS I  1 92  ? 74.372  34.907  29.145 1.00 34.13 ? 91   LYS I CB  1 
ATOM   9543  C  CG  . LYS I  1 92  ? 74.215  35.275  30.613 1.00 38.00 ? 91   LYS I CG  1 
ATOM   9544  C  CD  . LYS I  1 92  ? 73.153  34.419  31.283 0.00 37.55 ? 91   LYS I CD  1 
ATOM   9545  C  CE  . LYS I  1 92  ? 73.068  34.706  32.774 0.00 38.18 ? 91   LYS I CE  1 
ATOM   9546  N  NZ  . LYS I  1 92  ? 72.737  36.130  33.051 0.00 38.30 ? 91   LYS I NZ  1 
ATOM   9547  N  N   . ASP I  1 93  ? 77.621  34.653  28.943 1.00 33.18 ? 92   ASP I N   1 
ATOM   9548  C  CA  . ASP I  1 93  ? 78.874  34.504  29.677 1.00 35.47 ? 92   ASP I CA  1 
ATOM   9549  C  C   . ASP I  1 93  ? 80.083  35.153  29.021 1.00 34.93 ? 92   ASP I C   1 
ATOM   9550  O  O   . ASP I  1 93  ? 81.223  34.873  29.398 1.00 35.62 ? 92   ASP I O   1 
ATOM   9551  C  CB  . ASP I  1 93  ? 79.156  33.023  29.921 1.00 37.76 ? 92   ASP I CB  1 
ATOM   9552  C  CG  . ASP I  1 93  ? 78.173  32.404  30.888 1.00 41.10 ? 92   ASP I CG  1 
ATOM   9553  O  OD1 . ASP I  1 93  ? 77.938  31.182  30.797 1.00 45.18 ? 92   ASP I OD1 1 
ATOM   9554  O  OD2 . ASP I  1 93  ? 77.640  33.141  31.748 1.00 44.24 ? 92   ASP I OD2 1 
ATOM   9555  N  N   . GLY I  1 94  ? 79.835  36.012  28.038 1.00 32.83 ? 93   GLY I N   1 
ATOM   9556  C  CA  . GLY I  1 94  ? 80.920  36.707  27.369 1.00 30.50 ? 93   GLY I CA  1 
ATOM   9557  C  C   . GLY I  1 94  ? 81.708  35.890  26.370 1.00 31.25 ? 93   GLY I C   1 
ATOM   9558  O  O   . GLY I  1 94  ? 82.808  36.291  25.974 1.00 30.86 ? 93   GLY I O   1 
ATOM   9559  N  N   . VAL I  1 95  ? 81.151  34.757  25.949 1.00 29.24 ? 94   VAL I N   1 
ATOM   9560  C  CA  . VAL I  1 95  ? 81.823  33.890  24.992 1.00 27.50 ? 94   VAL I CA  1 
ATOM   9561  C  C   . VAL I  1 95  ? 81.180  33.906  23.608 1.00 28.62 ? 94   VAL I C   1 
ATOM   9562  O  O   . VAL I  1 95  ? 79.968  33.704  23.462 1.00 25.97 ? 94   VAL I O   1 
ATOM   9563  C  CB  . VAL I  1 95  ? 81.850  32.426  25.480 1.00 28.61 ? 94   VAL I CB  1 
ATOM   9564  C  CG1 . VAL I  1 95  ? 82.526  31.551  24.442 1.00 28.90 ? 94   VAL I CG1 1 
ATOM   9565  C  CG2 . VAL I  1 95  ? 82.577  32.328  26.813 1.00 27.51 ? 94   VAL I CG2 1 
ATOM   9566  N  N   . ALA I  1 96  ? 81.999  34.151  22.592 1.00 27.05 ? 95   ALA I N   1 
ATOM   9567  C  CA  . ALA I  1 96  ? 81.512  34.162  21.227 1.00 29.09 ? 95   ALA I CA  1 
ATOM   9568  C  C   . ALA I  1 96  ? 82.117  32.996  20.457 1.00 30.86 ? 95   ALA I C   1 
ATOM   9569  O  O   . ALA I  1 96  ? 83.339  32.899  20.319 1.00 30.53 ? 95   ALA I O   1 
ATOM   9570  C  CB  . ALA I  1 96  ? 81.870  35.474  20.542 1.00 28.54 ? 95   ALA I CB  1 
ATOM   9571  N  N   . ASP I  1 97  ? 81.254  32.103  19.985 1.00 31.12 ? 96   ASP I N   1 
ATOM   9572  C  CA  . ASP I  1 97  ? 81.677  30.964  19.185 1.00 32.36 ? 96   ASP I CA  1 
ATOM   9573  C  C   . ASP I  1 97  ? 81.644  31.487  17.756 1.00 32.17 ? 96   ASP I C   1 
ATOM   9574  O  O   . ASP I  1 97  ? 80.580  31.832  17.237 1.00 32.81 ? 96   ASP I O   1 
ATOM   9575  C  CB  . ASP I  1 97  ? 80.693  29.806  19.345 1.00 37.17 ? 96   ASP I CB  1 
ATOM   9576  C  CG  . ASP I  1 97  ? 81.001  28.649  18.415 1.00 42.74 ? 96   ASP I CG  1 
ATOM   9577  O  OD1 . ASP I  1 97  ? 80.899  28.824  17.179 1.00 45.38 ? 96   ASP I OD1 1 
ATOM   9578  O  OD2 . ASP I  1 97  ? 81.348  27.561  18.919 1.00 47.33 ? 96   ASP I OD2 1 
ATOM   9579  N  N   . VAL I  1 98  ? 82.807  31.556  17.122 1.00 30.14 ? 97   VAL I N   1 
ATOM   9580  C  CA  . VAL I  1 98  ? 82.890  32.082  15.771 1.00 28.25 ? 97   VAL I CA  1 
ATOM   9581  C  C   . VAL I  1 98  ? 82.869  31.018  14.679 1.00 27.58 ? 97   VAL I C   1 
ATOM   9582  O  O   . VAL I  1 98  ? 83.626  30.054  14.717 1.00 26.82 ? 97   VAL I O   1 
ATOM   9583  C  CB  . VAL I  1 98  ? 84.163  32.948  15.603 1.00 28.95 ? 97   VAL I CB  1 
ATOM   9584  C  CG1 . VAL I  1 98  ? 84.208  33.541  14.200 1.00 27.60 ? 97   VAL I CG1 1 
ATOM   9585  C  CG2 . VAL I  1 98  ? 84.182  34.051  16.658 1.00 28.81 ? 97   VAL I CG2 1 
ATOM   9586  N  N   . SER I  1 99  ? 81.983  31.207  13.711 1.00 28.98 ? 98   SER I N   1 
ATOM   9587  C  CA  . SER I  1 99  ? 81.860  30.292  12.583 1.00 31.20 ? 98   SER I CA  1 
ATOM   9588  C  C   . SER I  1 99  ? 81.385  31.107  11.394 1.00 31.92 ? 98   SER I C   1 
ATOM   9589  O  O   . SER I  1 99  ? 80.205  31.458  11.287 1.00 31.10 ? 98   SER I O   1 
ATOM   9590  C  CB  . SER I  1 99  ? 80.864  29.175  12.883 1.00 30.38 ? 98   SER I CB  1 
ATOM   9591  O  OG  . SER I  1 99  ? 81.043  28.116  11.961 1.00 32.66 ? 98   SER I OG  1 
ATOM   9592  N  N   . ILE I  1 100 ? 82.318  31.396  10.498 1.00 31.99 ? 99   ILE I N   1 
ATOM   9593  C  CA  . ILE I  1 100 ? 82.037  32.211  9.330  1.00 33.15 ? 99   ILE I CA  1 
ATOM   9594  C  C   . ILE I  1 100 ? 82.559  31.602  8.037  1.00 33.91 ? 99   ILE I C   1 
ATOM   9595  O  O   . ILE I  1 100 ? 83.543  30.868  8.026  1.00 31.14 ? 99   ILE I O   1 
ATOM   9596  C  CB  . ILE I  1 100 ? 82.672  33.614  9.503  1.00 32.91 ? 99   ILE I CB  1 
ATOM   9597  C  CG1 . ILE I  1 100 ? 82.005  34.343  10.671 1.00 34.08 ? 99   ILE I CG1 1 
ATOM   9598  C  CG2 . ILE I  1 100 ? 82.558  34.414  8.221  1.00 34.81 ? 99   ILE I CG2 1 
ATOM   9599  C  CD1 . ILE I  1 100 ? 82.653  35.674  11.019 1.00 31.39 ? 99   ILE I CD1 1 
ATOM   9600  N  N   . GLU I  1 101 ? 81.879  31.925  6.945  1.00 36.57 ? 100  GLU I N   1 
ATOM   9601  C  CA  . GLU I  1 101 ? 82.269  31.461  5.626  1.00 38.97 ? 100  GLU I CA  1 
ATOM   9602  C  C   . GLU I  1 101 ? 82.263  32.722  4.772  1.00 39.24 ? 100  GLU I C   1 
ATOM   9603  O  O   . GLU I  1 101 ? 81.236  33.393  4.662  1.00 37.72 ? 100  GLU I O   1 
ATOM   9604  C  CB  . GLU I  1 101 ? 81.248  30.458  5.089  1.00 41.60 ? 100  GLU I CB  1 
ATOM   9605  C  CG  . GLU I  1 101 ? 81.771  29.605  3.952  1.00 47.58 ? 100  GLU I CG  1 
ATOM   9606  C  CD  . GLU I  1 101 ? 82.409  28.311  4.429  1.00 49.60 ? 100  GLU I CD  1 
ATOM   9607  O  OE1 . GLU I  1 101 ? 83.098  27.656  3.618  1.00 50.94 ? 100  GLU I OE1 1 
ATOM   9608  O  OE2 . GLU I  1 101 ? 82.211  27.942  5.606  1.00 50.81 ? 100  GLU I OE2 1 
ATOM   9609  N  N   . ASP I  1 102 ? 83.408  33.063  4.189  1.00 40.34 ? 101  ASP I N   1 
ATOM   9610  C  CA  . ASP I  1 102 ? 83.490  34.264  3.364  1.00 41.36 ? 101  ASP I CA  1 
ATOM   9611  C  C   . ASP I  1 102 ? 84.239  34.001  2.063  1.00 42.47 ? 101  ASP I C   1 
ATOM   9612  O  O   . ASP I  1 102 ? 85.250  33.298  2.048  1.00 41.95 ? 101  ASP I O   1 
ATOM   9613  C  CB  . ASP I  1 102 ? 84.163  35.392  4.152  1.00 40.87 ? 101  ASP I CB  1 
ATOM   9614  C  CG  . ASP I  1 102 ? 83.943  36.753  3.522  1.00 41.23 ? 101  ASP I CG  1 
ATOM   9615  O  OD1 . ASP I  1 102 ? 84.754  37.160  2.663  1.00 42.21 ? 101  ASP I OD1 1 
ATOM   9616  O  OD2 . ASP I  1 102 ? 82.945  37.411  3.880  1.00 39.73 ? 101  ASP I OD2 1 
ATOM   9617  N  N   . SER I  1 103 ? 83.737  34.574  0.973  1.00 43.90 ? 102  SER I N   1 
ATOM   9618  C  CA  . SER I  1 103 ? 84.342  34.384  -0.340 1.00 46.03 ? 102  SER I CA  1 
ATOM   9619  C  C   . SER I  1 103 ? 85.073  35.616  -0.865 1.00 45.90 ? 102  SER I C   1 
ATOM   9620  O  O   . SER I  1 103 ? 85.599  35.598  -1.976 1.00 46.90 ? 102  SER I O   1 
ATOM   9621  C  CB  . SER I  1 103 ? 83.267  33.973  -1.348 1.00 46.93 ? 102  SER I CB  1 
ATOM   9622  O  OG  . SER I  1 103 ? 82.310  35.006  -1.507 1.00 50.35 ? 102  SER I OG  1 
ATOM   9623  N  N   . VAL I  1 104 ? 85.101  36.682  -0.072 1.00 46.04 ? 103  VAL I N   1 
ATOM   9624  C  CA  . VAL I  1 104 ? 85.774  37.908  -0.476 1.00 44.94 ? 103  VAL I CA  1 
ATOM   9625  C  C   . VAL I  1 104 ? 87.212  37.928  0.036  1.00 45.42 ? 103  VAL I C   1 
ATOM   9626  O  O   . VAL I  1 104 ? 88.125  38.334  -0.683 1.00 45.91 ? 103  VAL I O   1 
ATOM   9627  C  CB  . VAL I  1 104 ? 85.013  39.148  0.035  1.00 44.64 ? 103  VAL I CB  1 
ATOM   9628  C  CG1 . VAL I  1 104 ? 85.802  40.415  -0.254 1.00 44.15 ? 103  VAL I CG1 1 
ATOM   9629  C  CG2 . VAL I  1 104 ? 83.656  39.221  -0.641 1.00 45.32 ? 103  VAL I CG2 1 
ATOM   9630  N  N   . ILE I  1 105 ? 87.418  37.494  1.276  1.00 43.70 ? 104  ILE I N   1 
ATOM   9631  C  CA  . ILE I  1 105 ? 88.766  37.452  1.829  1.00 42.91 ? 104  ILE I CA  1 
ATOM   9632  C  C   . ILE I  1 105 ? 89.465  36.244  1.226  1.00 43.12 ? 104  ILE I C   1 
ATOM   9633  O  O   . ILE I  1 105 ? 88.817  35.356  0.672  1.00 43.01 ? 104  ILE I O   1 
ATOM   9634  C  CB  . ILE I  1 105 ? 88.773  37.292  3.371  1.00 42.24 ? 104  ILE I CB  1 
ATOM   9635  C  CG1 . ILE I  1 105 ? 88.072  35.988  3.765  1.00 41.19 ? 104  ILE I CG1 1 
ATOM   9636  C  CG2 . ILE I  1 105 ? 88.112  38.493  4.026  1.00 41.19 ? 104  ILE I CG2 1 
ATOM   9637  C  CD1 . ILE I  1 105 ? 88.151  35.663  5.249  1.00 40.38 ? 104  ILE I CD1 1 
ATOM   9638  N  N   . SER I  1 106 ? 90.788  36.215  1.333  1.00 43.37 ? 105  SER I N   1 
ATOM   9639  C  CA  . SER I  1 106 ? 91.577  35.109  0.808  1.00 42.95 ? 105  SER I CA  1 
ATOM   9640  C  C   . SER I  1 106 ? 92.884  34.998  1.585  1.00 42.99 ? 105  SER I C   1 
ATOM   9641  O  O   . SER I  1 106 ? 93.278  35.931  2.288  1.00 42.50 ? 105  SER I O   1 
ATOM   9642  C  CB  . SER I  1 106 ? 91.874  35.330  -0.678 1.00 42.53 ? 105  SER I CB  1 
ATOM   9643  O  OG  . SER I  1 106 ? 92.613  34.246  -1.212 1.00 43.28 ? 105  SER I OG  1 
ATOM   9644  N  N   . LEU I  1 107 ? 93.544  33.852  1.468  1.00 43.18 ? 106  LEU I N   1 
ATOM   9645  C  CA  . LEU I  1 107 ? 94.812  33.638  2.150  1.00 44.60 ? 106  LEU I CA  1 
ATOM   9646  C  C   . LEU I  1 107 ? 95.958  33.659  1.143  1.00 46.40 ? 106  LEU I C   1 
ATOM   9647  O  O   . LEU I  1 107 ? 97.038  33.125  1.399  1.00 47.06 ? 106  LEU I O   1 
ATOM   9648  C  CB  . LEU I  1 107 ? 94.802  32.302  2.899  1.00 42.64 ? 106  LEU I CB  1 
ATOM   9649  C  CG  . LEU I  1 107 ? 93.745  32.153  3.998  1.00 42.60 ? 106  LEU I CG  1 
ATOM   9650  C  CD1 . LEU I  1 107 ? 93.966  30.837  4.726  1.00 39.61 ? 106  LEU I CD1 1 
ATOM   9651  C  CD2 . LEU I  1 107 ? 93.832  33.323  4.972  1.00 39.23 ? 106  LEU I CD2 1 
ATOM   9652  N  N   . SER I  1 108 ? 95.709  34.279  -0.006 1.00 48.59 ? 107  SER I N   1 
ATOM   9653  C  CA  . SER I  1 108 ? 96.713  34.389  -1.058 1.00 51.01 ? 107  SER I CA  1 
ATOM   9654  C  C   . SER I  1 108 ? 96.271  35.418  -2.089 1.00 51.41 ? 107  SER I C   1 
ATOM   9655  O  O   . SER I  1 108 ? 95.077  35.617  -2.303 1.00 50.65 ? 107  SER I O   1 
ATOM   9656  C  CB  . SER I  1 108 ? 96.920  33.037  -1.741 1.00 52.14 ? 107  SER I CB  1 
ATOM   9657  O  OG  . SER I  1 108 ? 95.725  32.597  -2.360 1.00 56.58 ? 107  SER I OG  1 
ATOM   9658  N  N   . GLY I  1 109 ? 97.239  36.077  -2.719 1.00 52.87 ? 108  GLY I N   1 
ATOM   9659  C  CA  . GLY I  1 109 ? 96.917  37.071  -3.725 1.00 53.14 ? 108  GLY I CA  1 
ATOM   9660  C  C   . GLY I  1 109 ? 96.755  38.477  -3.183 1.00 53.72 ? 108  GLY I C   1 
ATOM   9661  O  O   . GLY I  1 109 ? 97.039  38.743  -2.016 1.00 53.77 ? 108  GLY I O   1 
ATOM   9662  N  N   . ASP I  1 110 ? 96.283  39.374  -4.045 1.00 55.18 ? 109  ASP I N   1 
ATOM   9663  C  CA  . ASP I  1 110 ? 96.075  40.780  -3.706 1.00 56.73 ? 109  ASP I CA  1 
ATOM   9664  C  C   . ASP I  1 110 ? 95.065  41.015  -2.584 1.00 56.95 ? 109  ASP I C   1 
ATOM   9665  O  O   . ASP I  1 110 ? 95.079  42.064  -1.937 1.00 57.34 ? 109  ASP I O   1 
ATOM   9666  C  CB  . ASP I  1 110 ? 95.629  41.544  -4.956 1.00 58.48 ? 109  ASP I CB  1 
ATOM   9667  C  CG  . ASP I  1 110 ? 96.656  41.484  -6.076 1.00 60.20 ? 109  ASP I CG  1 
ATOM   9668  O  OD1 . ASP I  1 110 ? 96.343  41.944  -7.196 1.00 60.91 ? 109  ASP I OD1 1 
ATOM   9669  O  OD2 . ASP I  1 110 ? 97.777  40.982  -5.836 1.00 60.36 ? 109  ASP I OD2 1 
ATOM   9670  N  N   . HIS I  1 111 ? 94.184  40.047  -2.360 1.00 56.38 ? 110  HIS I N   1 
ATOM   9671  C  CA  . HIS I  1 111 ? 93.182  40.172  -1.311 1.00 55.80 ? 110  HIS I CA  1 
ATOM   9672  C  C   . HIS I  1 111 ? 93.536  39.308  -0.109 1.00 54.19 ? 110  HIS I C   1 
ATOM   9673  O  O   . HIS I  1 111 ? 92.687  39.029  0.740  1.00 54.71 ? 110  HIS I O   1 
ATOM   9674  C  CB  . HIS I  1 111 ? 91.802  39.781  -1.845 1.00 57.72 ? 110  HIS I CB  1 
ATOM   9675  C  CG  . HIS I  1 111 ? 91.277  40.708  -2.898 1.00 60.75 ? 110  HIS I CG  1 
ATOM   9676  N  ND1 . HIS I  1 111 ? 89.989  40.633  -3.381 1.00 60.85 ? 110  HIS I ND1 1 
ATOM   9677  C  CD2 . HIS I  1 111 ? 91.868  41.735  -3.556 1.00 61.11 ? 110  HIS I CD2 1 
ATOM   9678  C  CE1 . HIS I  1 111 ? 89.807  41.575  -4.290 1.00 61.36 ? 110  HIS I CE1 1 
ATOM   9679  N  NE2 . HIS I  1 111 ? 90.931  42.257  -4.415 1.00 61.53 ? 110  HIS I NE2 1 
ATOM   9680  N  N   . SER I  1 112 ? 94.796  38.890  -0.040 1.00 50.64 ? 111  SER I N   1 
ATOM   9681  C  CA  . SER I  1 112 ? 95.258  38.055  1.060  1.00 48.00 ? 111  SER I CA  1 
ATOM   9682  C  C   . SER I  1 112 ? 95.292  38.828  2.371  1.00 45.72 ? 111  SER I C   1 
ATOM   9683  O  O   . SER I  1 112 ? 95.733  39.976  2.416  1.00 45.11 ? 111  SER I O   1 
ATOM   9684  C  CB  . SER I  1 112 ? 96.653  37.506  0.761  1.00 47.22 ? 111  SER I CB  1 
ATOM   9685  O  OG  . SER I  1 112 ? 97.129  36.737  1.850  1.00 47.09 ? 111  SER I OG  1 
ATOM   9686  N  N   . ILE I  1 113 ? 94.822  38.195  3.438  1.00 43.17 ? 112  ILE I N   1 
ATOM   9687  C  CA  . ILE I  1 113 ? 94.817  38.834  4.744  1.00 41.57 ? 112  ILE I CA  1 
ATOM   9688  C  C   . ILE I  1 113 ? 96.001  38.341  5.571  1.00 39.64 ? 112  ILE I C   1 
ATOM   9689  O  O   . ILE I  1 113 ? 96.158  38.711  6.733  1.00 39.77 ? 112  ILE I O   1 
ATOM   9690  C  CB  . ILE I  1 113 ? 93.500  38.556  5.504  1.00 41.51 ? 112  ILE I CB  1 
ATOM   9691  C  CG1 . ILE I  1 113 ? 93.319  37.052  5.721  1.00 41.46 ? 112  ILE I CG1 1 
ATOM   9692  C  CG2 . ILE I  1 113 ? 92.326  39.126  4.719  1.00 41.37 ? 112  ILE I CG2 1 
ATOM   9693  C  CD1 . ILE I  1 113 ? 92.077  36.694  6.520  1.00 41.72 ? 112  ILE I CD1 1 
ATOM   9694  N  N   . ILE I  1 114 ? 96.831  37.497  4.964  1.00 39.22 ? 113  ILE I N   1 
ATOM   9695  C  CA  . ILE I  1 114 ? 98.013  36.977  5.642  1.00 37.84 ? 113  ILE I CA  1 
ATOM   9696  C  C   . ILE I  1 114 ? 98.906  38.166  5.979  1.00 38.04 ? 113  ILE I C   1 
ATOM   9697  O  O   . ILE I  1 114 ? 99.210  38.982  5.112  1.00 38.15 ? 113  ILE I O   1 
ATOM   9698  C  CB  . ILE I  1 114 ? 98.821  36.014  4.735  1.00 37.78 ? 113  ILE I CB  1 
ATOM   9699  C  CG1 . ILE I  1 114 ? 97.974  34.796  4.362  1.00 38.21 ? 113  ILE I CG1 1 
ATOM   9700  C  CG2 . ILE I  1 114 ? 100.096 35.572  5.448  1.00 36.96 ? 113  ILE I CG2 1 
ATOM   9701  C  CD1 . ILE I  1 114 ? 97.569  33.938  5.547  1.00 37.11 ? 113  ILE I CD1 1 
ATOM   9702  N  N   . GLY I  1 115 ? 99.311  38.274  7.237  1.00 37.69 ? 114  GLY I N   1 
ATOM   9703  C  CA  . GLY I  1 115 ? 100.173 39.375  7.626  1.00 38.38 ? 114  GLY I CA  1 
ATOM   9704  C  C   . GLY I  1 115 ? 99.433  40.637  8.021  1.00 38.18 ? 114  GLY I C   1 
ATOM   9705  O  O   . GLY I  1 115 ? 100.055 41.642  8.355  1.00 38.43 ? 114  GLY I O   1 
ATOM   9706  N  N   . ARG I  1 116 ? 98.106  40.601  7.978  1.00 36.81 ? 115  ARG I N   1 
ATOM   9707  C  CA  . ARG I  1 116 ? 97.324  41.768  8.363  1.00 36.31 ? 115  ARG I CA  1 
ATOM   9708  C  C   . ARG I  1 116 ? 96.749  41.531  9.755  1.00 35.36 ? 115  ARG I C   1 
ATOM   9709  O  O   . ARG I  1 116 ? 97.117  40.558  10.413 1.00 34.07 ? 115  ARG I O   1 
ATOM   9710  C  CB  . ARG I  1 116 ? 96.236  42.043  7.318  1.00 37.88 ? 115  ARG I CB  1 
ATOM   9711  C  CG  . ARG I  1 116 ? 96.833  42.364  5.941  1.00 39.12 ? 115  ARG I CG  1 
ATOM   9712  C  CD  . ARG I  1 116 ? 95.788  42.731  4.899  1.00 41.21 ? 115  ARG I CD  1 
ATOM   9713  N  NE  . ARG I  1 116 ? 96.358  42.818  3.552  1.00 41.58 ? 115  ARG I NE  1 
ATOM   9714  C  CZ  . ARG I  1 116 ? 97.152  43.797  3.123  1.00 41.77 ? 115  ARG I CZ  1 
ATOM   9715  N  NH1 . ARG I  1 116 ? 97.614  43.773  1.879  1.00 41.52 ? 115  ARG I NH1 1 
ATOM   9716  N  NH2 . ARG I  1 116 ? 97.475  44.804  3.925  1.00 40.48 ? 115  ARG I NH2 1 
ATOM   9717  N  N   . THR I  1 117 ? 95.851  42.398  10.214 1.00 34.03 ? 116  THR I N   1 
ATOM   9718  C  CA  . THR I  1 117 ? 95.320  42.243  11.565 1.00 32.85 ? 116  THR I CA  1 
ATOM   9719  C  C   . THR I  1 117 ? 93.820  41.974  11.689 1.00 33.16 ? 116  THR I C   1 
ATOM   9720  O  O   . THR I  1 117 ? 93.004  42.598  11.008 1.00 32.39 ? 116  THR I O   1 
ATOM   9721  C  CB  . THR I  1 117 ? 95.670  43.489  12.425 1.00 33.52 ? 116  THR I CB  1 
ATOM   9722  O  OG1 . THR I  1 117 ? 97.095  43.665  12.464 1.00 32.79 ? 116  THR I OG1 1 
ATOM   9723  C  CG2 . THR I  1 117 ? 95.153  43.325  13.844 1.00 32.16 ? 116  THR I CG2 1 
ATOM   9724  N  N   . LEU I  1 118 ? 93.469  41.035  12.566 1.00 31.20 ? 117  LEU I N   1 
ATOM   9725  C  CA  . LEU I  1 118 ? 92.069  40.703  12.820 1.00 31.24 ? 117  LEU I CA  1 
ATOM   9726  C  C   . LEU I  1 118 ? 91.681  41.454  14.088 1.00 30.83 ? 117  LEU I C   1 
ATOM   9727  O  O   . LEU I  1 118 ? 92.388  41.390  15.095 1.00 31.79 ? 117  LEU I O   1 
ATOM   9728  C  CB  . LEU I  1 118 ? 91.887  39.192  13.033 1.00 30.20 ? 117  LEU I CB  1 
ATOM   9729  C  CG  . LEU I  1 118 ? 90.462  38.715  13.367 1.00 30.53 ? 117  LEU I CG  1 
ATOM   9730  C  CD1 . LEU I  1 118 ? 89.546  38.948  12.172 1.00 28.23 ? 117  LEU I CD1 1 
ATOM   9731  C  CD2 . LEU I  1 118 ? 90.477  37.230  13.741 1.00 28.51 ? 117  LEU I CD2 1 
ATOM   9732  N  N   . VAL I  1 119 ? 90.561  42.167  14.040 1.00 31.09 ? 118  VAL I N   1 
ATOM   9733  C  CA  . VAL I  1 119 ? 90.111  42.944  15.187 1.00 30.62 ? 118  VAL I CA  1 
ATOM   9734  C  C   . VAL I  1 119 ? 88.671  42.669  15.596 1.00 30.39 ? 118  VAL I C   1 
ATOM   9735  O  O   . VAL I  1 119 ? 87.803  42.495  14.745 1.00 29.88 ? 118  VAL I O   1 
ATOM   9736  C  CB  . VAL I  1 119 ? 90.222  44.456  14.893 1.00 31.86 ? 118  VAL I CB  1 
ATOM   9737  C  CG1 . VAL I  1 119 ? 89.738  45.260  16.093 1.00 30.86 ? 118  VAL I CG1 1 
ATOM   9738  C  CG2 . VAL I  1 119 ? 91.660  44.808  14.540 1.00 32.43 ? 118  VAL I CG2 1 
ATOM   9739  N  N   . VAL I  1 120 ? 88.430  42.623  16.903 1.00 30.92 ? 119  VAL I N   1 
ATOM   9740  C  CA  . VAL I  1 120 ? 87.081  42.434  17.429 1.00 31.37 ? 119  VAL I CA  1 
ATOM   9741  C  C   . VAL I  1 120 ? 86.771  43.734  18.169 1.00 32.62 ? 119  VAL I C   1 
ATOM   9742  O  O   . VAL I  1 120 ? 87.526  44.156  19.052 1.00 32.02 ? 119  VAL I O   1 
ATOM   9743  C  CB  . VAL I  1 120 ? 86.977  41.219  18.393 1.00 30.90 ? 119  VAL I CB  1 
ATOM   9744  C  CG1 . VAL I  1 120 ? 87.949  41.364  19.557 1.00 29.71 ? 119  VAL I CG1 1 
ATOM   9745  C  CG2 . VAL I  1 120 ? 85.546  41.101  18.906 1.00 30.59 ? 119  VAL I CG2 1 
ATOM   9746  N  N   . HIS I  1 121 ? 85.658  44.362  17.799 1.00 32.72 ? 120  HIS I N   1 
ATOM   9747  C  CA  . HIS I  1 121 ? 85.264  45.653  18.355 1.00 32.71 ? 120  HIS I CA  1 
ATOM   9748  C  C   . HIS I  1 121 ? 84.375  45.725  19.591 1.00 33.35 ? 120  HIS I C   1 
ATOM   9749  O  O   . HIS I  1 121 ? 83.716  44.758  19.987 1.00 33.51 ? 120  HIS I O   1 
ATOM   9750  C  CB  . HIS I  1 121 ? 84.633  46.494  17.243 1.00 31.54 ? 120  HIS I CB  1 
ATOM   9751  C  CG  . HIS I  1 121 ? 85.613  46.954  16.205 1.00 31.81 ? 120  HIS I CG  1 
ATOM   9752  N  ND1 . HIS I  1 121 ? 86.254  48.169  16.279 1.00 30.99 ? 120  HIS I ND1 1 
ATOM   9753  C  CD2 . HIS I  1 121 ? 86.059  46.357  15.075 1.00 33.51 ? 120  HIS I CD2 1 
ATOM   9754  C  CE1 . HIS I  1 121 ? 87.054  48.306  15.233 1.00 32.64 ? 120  HIS I CE1 1 
ATOM   9755  N  NE2 . HIS I  1 121 ? 86.954  47.222  14.489 1.00 30.18 ? 120  HIS I NE2 1 
ATOM   9756  N  N   . GLU I  1 122 ? 84.371  46.919  20.176 1.00 33.08 ? 121  GLU I N   1 
ATOM   9757  C  CA  . GLU I  1 122 ? 83.606  47.256  21.368 1.00 33.52 ? 121  GLU I CA  1 
ATOM   9758  C  C   . GLU I  1 122 ? 82.098  47.123  21.175 1.00 33.00 ? 121  GLU I C   1 
ATOM   9759  O  O   . GLU I  1 122 ? 81.387  46.645  22.059 1.00 31.94 ? 121  GLU I O   1 
ATOM   9760  C  CB  . GLU I  1 122 ? 83.918  48.703  21.773 1.00 36.16 ? 121  GLU I CB  1 
ATOM   9761  C  CG  . GLU I  1 122 ? 83.107  49.223  22.956 1.00 39.62 ? 121  GLU I CG  1 
ATOM   9762  C  CD  . GLU I  1 122 ? 83.153  50.742  23.087 1.00 43.42 ? 121  GLU I CD  1 
ATOM   9763  O  OE1 . GLU I  1 122 ? 82.604  51.266  24.081 1.00 46.32 ? 121  GLU I OE1 1 
ATOM   9764  O  OE2 . GLU I  1 122 ? 83.724  51.414  22.199 1.00 42.54 ? 121  GLU I OE2 1 
ATOM   9765  N  N   . LYS I  1 123 ? 81.616  47.554  20.016 1.00 34.03 ? 122  LYS I N   1 
ATOM   9766  C  CA  . LYS I  1 123 ? 80.188  47.524  19.733 1.00 36.45 ? 122  LYS I CA  1 
ATOM   9767  C  C   . LYS I  1 123 ? 79.818  46.820  18.438 1.00 35.85 ? 122  LYS I C   1 
ATOM   9768  O  O   . LYS I  1 123 ? 80.677  46.343  17.696 1.00 35.36 ? 122  LYS I O   1 
ATOM   9769  C  CB  . LYS I  1 123 ? 79.649  48.958  19.701 1.00 37.99 ? 122  LYS I CB  1 
ATOM   9770  C  CG  . LYS I  1 123 ? 79.838  49.708  21.015 1.00 41.88 ? 122  LYS I CG  1 
ATOM   9771  C  CD  . LYS I  1 123 ? 79.348  51.145  20.937 1.00 45.41 ? 122  LYS I CD  1 
ATOM   9772  C  CE  . LYS I  1 123 ? 80.194  51.978  19.986 1.00 48.75 ? 122  LYS I CE  1 
ATOM   9773  N  NZ  . LYS I  1 123 ? 79.795  53.416  20.016 1.00 51.12 ? 122  LYS I NZ  1 
ATOM   9774  N  N   . ALA I  1 124 ? 78.519  46.772  18.174 1.00 34.86 ? 123  ALA I N   1 
ATOM   9775  C  CA  . ALA I  1 124 ? 78.003  46.138  16.975 1.00 35.52 ? 123  ALA I CA  1 
ATOM   9776  C  C   . ALA I  1 124 ? 78.361  46.944  15.730 1.00 36.78 ? 123  ALA I C   1 
ATOM   9777  O  O   . ALA I  1 124 ? 78.472  48.168  15.778 1.00 37.22 ? 123  ALA I O   1 
ATOM   9778  C  CB  . ALA I  1 124 ? 76.492  45.993  17.084 1.00 33.56 ? 123  ALA I CB  1 
ATOM   9779  N  N   . ASP I  1 125 ? 78.555  46.239  14.622 1.00 37.53 ? 124  ASP I N   1 
ATOM   9780  C  CA  . ASP I  1 125 ? 78.868  46.861  13.342 1.00 38.50 ? 124  ASP I CA  1 
ATOM   9781  C  C   . ASP I  1 125 ? 77.512  47.068  12.664 1.00 39.16 ? 124  ASP I C   1 
ATOM   9782  O  O   . ASP I  1 125 ? 76.775  46.105  12.451 1.00 37.40 ? 124  ASP I O   1 
ATOM   9783  C  CB  . ASP I  1 125 ? 79.751  45.914  12.522 1.00 40.35 ? 124  ASP I CB  1 
ATOM   9784  C  CG  . ASP I  1 125 ? 80.100  46.465  11.150 1.00 42.01 ? 124  ASP I CG  1 
ATOM   9785  O  OD1 . ASP I  1 125 ? 80.950  45.847  10.475 1.00 40.32 ? 124  ASP I OD1 1 
ATOM   9786  O  OD2 . ASP I  1 125 ? 79.529  47.500  10.741 1.00 43.04 ? 124  ASP I OD2 1 
ATOM   9787  N  N   . ASP I  1 126 ? 77.173  48.317  12.345 1.00 39.52 ? 125  ASP I N   1 
ATOM   9788  C  CA  . ASP I  1 126 ? 75.887  48.612  11.718 1.00 39.57 ? 125  ASP I CA  1 
ATOM   9789  C  C   . ASP I  1 126 ? 75.837  48.181  10.260 1.00 40.82 ? 125  ASP I C   1 
ATOM   9790  O  O   . ASP I  1 126 ? 74.867  48.454  9.552  1.00 42.16 ? 125  ASP I O   1 
ATOM   9791  C  CB  . ASP I  1 126 ? 75.556  50.104  11.846 1.00 40.09 ? 125  ASP I CB  1 
ATOM   9792  C  CG  . ASP I  1 126 ? 76.496  50.990  11.051 1.00 38.80 ? 125  ASP I CG  1 
ATOM   9793  O  OD1 . ASP I  1 126 ? 76.544  52.198  11.351 1.00 38.91 ? 125  ASP I OD1 1 
ATOM   9794  O  OD2 . ASP I  1 126 ? 77.177  50.494  10.128 1.00 40.25 ? 125  ASP I OD2 1 
ATOM   9795  N  N   . LEU I  1 127 ? 76.895  47.511  9.820  1.00 40.78 ? 126  LEU I N   1 
ATOM   9796  C  CA  . LEU I  1 127 ? 76.988  46.998  8.462  1.00 41.94 ? 126  LEU I CA  1 
ATOM   9797  C  C   . LEU I  1 127 ? 76.903  48.054  7.362  1.00 43.93 ? 126  LEU I C   1 
ATOM   9798  O  O   . LEU I  1 127 ? 76.615  47.733  6.207  1.00 43.28 ? 126  LEU I O   1 
ATOM   9799  C  CB  . LEU I  1 127 ? 75.908  45.934  8.246  1.00 41.30 ? 126  LEU I CB  1 
ATOM   9800  C  CG  . LEU I  1 127 ? 75.845  44.856  9.334  1.00 40.74 ? 126  LEU I CG  1 
ATOM   9801  C  CD1 . LEU I  1 127 ? 74.826  43.792  8.948  1.00 39.62 ? 126  LEU I CD1 1 
ATOM   9802  C  CD2 . LEU I  1 127 ? 77.226  44.236  9.522  1.00 37.92 ? 126  LEU I CD2 1 
ATOM   9803  N  N   . GLY I  1 128 ? 77.155  49.308  7.717  1.00 45.60 ? 127  GLY I N   1 
ATOM   9804  C  CA  . GLY I  1 128 ? 77.117  50.369  6.727  1.00 49.41 ? 127  GLY I CA  1 
ATOM   9805  C  C   . GLY I  1 128 ? 75.768  51.036  6.533  1.00 51.72 ? 127  GLY I C   1 
ATOM   9806  O  O   . GLY I  1 128 ? 75.622  51.880  5.650  1.00 52.32 ? 127  GLY I O   1 
ATOM   9807  N  N   . LYS I  1 129 ? 74.783  50.663  7.345  1.00 53.31 ? 128  LYS I N   1 
ATOM   9808  C  CA  . LYS I  1 129 ? 73.449  51.251  7.250  1.00 55.08 ? 128  LYS I CA  1 
ATOM   9809  C  C   . LYS I  1 129 ? 73.159  52.165  8.435  1.00 55.88 ? 128  LYS I C   1 
ATOM   9810  O  O   . LYS I  1 129 ? 72.003  52.346  8.822  1.00 56.59 ? 128  LYS I O   1 
ATOM   9811  C  CB  . LYS I  1 129 ? 72.372  50.164  7.196  1.00 55.29 ? 128  LYS I CB  1 
ATOM   9812  C  CG  . LYS I  1 129 ? 72.243  49.430  5.878  1.00 55.96 ? 128  LYS I CG  1 
ATOM   9813  C  CD  . LYS I  1 129 ? 73.175  48.245  5.793  1.00 57.57 ? 128  LYS I CD  1 
ATOM   9814  C  CE  . LYS I  1 129 ? 72.548  47.144  4.949  1.00 57.65 ? 128  LYS I CE  1 
ATOM   9815  N  NZ  . LYS I  1 129 ? 73.403  46.736  3.805  1.00 58.10 ? 128  LYS I NZ  1 
ATOM   9816  N  N   . GLY I  1 130 ? 74.210  52.740  9.009  1.00 56.59 ? 129  GLY I N   1 
ATOM   9817  C  CA  . GLY I  1 130 ? 74.039  53.621  10.149 1.00 57.49 ? 129  GLY I CA  1 
ATOM   9818  C  C   . GLY I  1 130 ? 73.391  54.948  9.806  1.00 59.02 ? 129  GLY I C   1 
ATOM   9819  O  O   . GLY I  1 130 ? 72.801  55.597  10.671 1.00 59.49 ? 129  GLY I O   1 
ATOM   9820  N  N   . GLY I  1 131 ? 73.503  55.361  8.548  1.00 59.71 ? 130  GLY I N   1 
ATOM   9821  C  CA  . GLY I  1 131 ? 72.912  56.621  8.134  1.00 60.79 ? 130  GLY I CA  1 
ATOM   9822  C  C   . GLY I  1 131 ? 73.820  57.823  8.328  1.00 60.77 ? 130  GLY I C   1 
ATOM   9823  O  O   . GLY I  1 131 ? 73.355  58.964  8.334  1.00 60.92 ? 130  GLY I O   1 
ATOM   9824  N  N   . ASN I  1 132 ? 75.115  57.574  8.492  1.00 60.18 ? 131  ASN I N   1 
ATOM   9825  C  CA  . ASN I  1 132 ? 76.082  58.650  8.672  1.00 59.43 ? 131  ASN I CA  1 
ATOM   9826  C  C   . ASN I  1 132 ? 77.401  58.307  7.984  1.00 59.24 ? 131  ASN I C   1 
ATOM   9827  O  O   . ASN I  1 132 ? 77.593  57.182  7.522  1.00 58.57 ? 131  ASN I O   1 
ATOM   9828  C  CB  . ASN I  1 132 ? 76.319  58.915  10.163 1.00 59.12 ? 131  ASN I CB  1 
ATOM   9829  C  CG  . ASN I  1 132 ? 76.747  57.673  10.917 1.00 59.68 ? 131  ASN I CG  1 
ATOM   9830  O  OD1 . ASN I  1 132 ? 77.644  56.950  10.487 1.00 58.81 ? 131  ASN I OD1 1 
ATOM   9831  N  ND2 . ASN I  1 132 ? 76.113  57.426  12.058 1.00 58.74 ? 131  ASN I ND2 1 
ATOM   9832  N  N   . GLU I  1 133 ? 78.305  59.280  7.915  1.00 59.14 ? 132  GLU I N   1 
ATOM   9833  C  CA  . GLU I  1 133 ? 79.596  59.070  7.268  1.00 58.97 ? 132  GLU I CA  1 
ATOM   9834  C  C   . GLU I  1 133 ? 80.413  57.990  7.962  1.00 57.65 ? 132  GLU I C   1 
ATOM   9835  O  O   . GLU I  1 133 ? 80.998  57.127  7.308  1.00 57.11 ? 132  GLU I O   1 
ATOM   9836  C  CB  . GLU I  1 133 ? 80.401  60.371  7.241  1.00 60.31 ? 132  GLU I CB  1 
ATOM   9837  C  CG  . GLU I  1 133 ? 81.793  60.202  6.648  1.00 62.77 ? 132  GLU I CG  1 
ATOM   9838  C  CD  . GLU I  1 133 ? 82.587  61.493  6.619  1.00 64.44 ? 132  GLU I CD  1 
ATOM   9839  O  OE1 . GLU I  1 133 ? 82.814  62.083  7.698  1.00 64.96 ? 132  GLU I OE1 1 
ATOM   9840  O  OE2 . GLU I  1 133 ? 82.987  61.916  5.512  1.00 64.87 ? 132  GLU I OE2 1 
ATOM   9841  N  N   . GLU I  1 134 ? 80.454  58.051  9.288  1.00 56.83 ? 133  GLU I N   1 
ATOM   9842  C  CA  . GLU I  1 134 ? 81.200  57.086  10.085 1.00 56.36 ? 133  GLU I CA  1 
ATOM   9843  C  C   . GLU I  1 134 ? 80.797  55.654  9.737  1.00 55.24 ? 133  GLU I C   1 
ATOM   9844  O  O   . GLU I  1 134 ? 81.649  54.780  9.577  1.00 55.00 ? 133  GLU I O   1 
ATOM   9845  C  CB  . GLU I  1 134 ? 80.956  57.348  11.573 1.00 57.26 ? 133  GLU I CB  1 
ATOM   9846  C  CG  . GLU I  1 134 ? 81.755  56.456  12.508 1.00 59.96 ? 133  GLU I CG  1 
ATOM   9847  C  CD  . GLU I  1 134 ? 83.248  56.715  12.438 1.00 61.67 ? 133  GLU I CD  1 
ATOM   9848  O  OE1 . GLU I  1 134 ? 84.000  56.037  13.170 1.00 62.40 ? 133  GLU I OE1 1 
ATOM   9849  O  OE2 . GLU I  1 134 ? 83.671  57.594  11.655 1.00 62.41 ? 133  GLU I OE2 1 
ATOM   9850  N  N   . SER I  1 135 ? 79.493  55.425  9.614  1.00 53.35 ? 134  SER I N   1 
ATOM   9851  C  CA  . SER I  1 135 ? 78.973  54.102  9.291  1.00 51.82 ? 134  SER I CA  1 
ATOM   9852  C  C   . SER I  1 135 ? 79.560  53.558  7.995  1.00 51.43 ? 134  SER I C   1 
ATOM   9853  O  O   . SER I  1 135 ? 79.812  52.358  7.872  1.00 50.41 ? 134  SER I O   1 
ATOM   9854  C  CB  . SER I  1 135 ? 77.448  54.149  9.179  1.00 51.36 ? 134  SER I CB  1 
ATOM   9855  O  OG  . SER I  1 135 ? 76.930  52.895  8.772  1.00 49.60 ? 134  SER I OG  1 
ATOM   9856  N  N   . THR I  1 136 ? 79.778  54.443  7.028  1.00 50.75 ? 135  THR I N   1 
ATOM   9857  C  CA  . THR I  1 136 ? 80.331  54.034  5.744  1.00 50.73 ? 135  THR I CA  1 
ATOM   9858  C  C   . THR I  1 136 ? 81.837  53.813  5.847  1.00 50.04 ? 135  THR I C   1 
ATOM   9859  O  O   . THR I  1 136 ? 82.481  53.408  4.878  1.00 48.51 ? 135  THR I O   1 
ATOM   9860  C  CB  . THR I  1 136 ? 80.059  55.094  4.659  1.00 52.54 ? 135  THR I CB  1 
ATOM   9861  O  OG1 . THR I  1 136 ? 80.777  56.294  4.971  1.00 52.51 ? 135  THR I OG1 1 
ATOM   9862  C  CG2 . THR I  1 136 ? 78.568  55.407  4.586  1.00 51.78 ? 135  THR I CG2 1 
ATOM   9863  N  N   . LYS I  1 137 ? 82.394  54.078  7.024  1.00 49.72 ? 136  LYS I N   1 
ATOM   9864  C  CA  . LYS I  1 137 ? 83.826  53.903  7.237  1.00 50.11 ? 136  LYS I CA  1 
ATOM   9865  C  C   . LYS I  1 137 ? 84.164  52.758  8.185  1.00 49.11 ? 136  LYS I C   1 
ATOM   9866  O  O   . LYS I  1 137 ? 84.961  51.881  7.848  1.00 49.17 ? 136  LYS I O   1 
ATOM   9867  C  CB  . LYS I  1 137 ? 84.452  55.194  7.777  1.00 51.48 ? 136  LYS I CB  1 
ATOM   9868  C  CG  . LYS I  1 137 ? 84.549  56.324  6.767  1.00 53.29 ? 136  LYS I CG  1 
ATOM   9869  C  CD  . LYS I  1 137 ? 85.379  57.475  7.322  1.00 55.38 ? 136  LYS I CD  1 
ATOM   9870  C  CE  . LYS I  1 137 ? 85.558  58.581  6.288  1.00 57.87 ? 136  LYS I CE  1 
ATOM   9871  N  NZ  . LYS I  1 137 ? 86.428  59.685  6.790  1.00 58.51 ? 136  LYS I NZ  1 
ATOM   9872  N  N   . THR I  1 138 ? 83.558  52.767  9.368  1.00 47.58 ? 137  THR I N   1 
ATOM   9873  C  CA  . THR I  1 138 ? 83.833  51.742  10.367 1.00 46.32 ? 137  THR I CA  1 
ATOM   9874  C  C   . THR I  1 138 ? 82.606  50.953  10.805 1.00 45.59 ? 137  THR I C   1 
ATOM   9875  O  O   . THR I  1 138 ? 82.730  49.942  11.500 1.00 43.84 ? 137  THR I O   1 
ATOM   9876  C  CB  . THR I  1 138 ? 84.443  52.366  11.628 1.00 46.30 ? 137  THR I CB  1 
ATOM   9877  O  OG1 . THR I  1 138 ? 83.467  53.208  12.254 1.00 46.52 ? 137  THR I OG1 1 
ATOM   9878  C  CG2 . THR I  1 138 ? 85.668  53.196  11.273 1.00 46.60 ? 137  THR I CG2 1 
ATOM   9879  N  N   . GLY I  1 139 ? 81.425  51.417  10.409 1.00 43.47 ? 138  GLY I N   1 
ATOM   9880  C  CA  . GLY I  1 139 ? 80.207  50.739  10.805 1.00 41.91 ? 138  GLY I CA  1 
ATOM   9881  C  C   . GLY I  1 139 ? 79.861  51.094  12.237 1.00 41.43 ? 138  GLY I C   1 
ATOM   9882  O  O   . GLY I  1 139 ? 79.019  50.445  12.864 1.00 41.18 ? 138  GLY I O   1 
ATOM   9883  N  N   . ASN I  1 140 ? 80.516  52.133  12.754 1.00 40.28 ? 139  ASN I N   1 
ATOM   9884  C  CA  . ASN I  1 140 ? 80.298  52.597  14.121 1.00 39.73 ? 139  ASN I CA  1 
ATOM   9885  C  C   . ASN I  1 140 ? 80.502  51.465  15.129 1.00 39.51 ? 139  ASN I C   1 
ATOM   9886  O  O   . ASN I  1 140 ? 79.789  51.375  16.127 1.00 39.53 ? 139  ASN I O   1 
ATOM   9887  C  CB  . ASN I  1 140 ? 78.885  53.180  14.258 1.00 41.04 ? 139  ASN I CB  1 
ATOM   9888  C  CG  . ASN I  1 140 ? 78.694  54.450  13.437 1.00 42.56 ? 139  ASN I CG  1 
ATOM   9889  O  OD1 . ASN I  1 140 ? 79.276  55.491  13.741 1.00 43.30 ? 139  ASN I OD1 1 
ATOM   9890  N  ND2 . ASN I  1 140 ? 77.885  54.364  12.387 1.00 42.11 ? 139  ASN I ND2 1 
ATOM   9891  N  N   . ALA I  1 141 ? 81.493  50.616  14.866 1.00 40.35 ? 140  ALA I N   1 
ATOM   9892  C  CA  . ALA I  1 141 ? 81.797  49.471  15.726 1.00 39.94 ? 140  ALA I CA  1 
ATOM   9893  C  C   . ALA I  1 141 ? 82.519  49.824  17.026 1.00 40.30 ? 140  ALA I C   1 
ATOM   9894  O  O   . ALA I  1 141 ? 82.708  48.965  17.893 1.00 40.39 ? 140  ALA I O   1 
ATOM   9895  C  CB  . ALA I  1 141 ? 82.610  48.447  14.943 1.00 38.77 ? 140  ALA I CB  1 
ATOM   9896  N  N   . GLY I  1 142 ? 82.930  51.080  17.165 1.00 39.30 ? 141  GLY I N   1 
ATOM   9897  C  CA  . GLY I  1 142 ? 83.610  51.489  18.381 1.00 38.85 ? 141  GLY I CA  1 
ATOM   9898  C  C   . GLY I  1 142 ? 85.076  51.100  18.467 1.00 38.80 ? 141  GLY I C   1 
ATOM   9899  O  O   . GLY I  1 142 ? 85.722  50.823  17.454 1.00 38.23 ? 141  GLY I O   1 
ATOM   9900  N  N   . SER I  1 143 ? 85.598  51.067  19.689 1.00 38.64 ? 142  SER I N   1 
ATOM   9901  C  CA  . SER I  1 143 ? 87.002  50.742  19.919 1.00 39.83 ? 142  SER I CA  1 
ATOM   9902  C  C   . SER I  1 143 ? 87.405  49.315  19.543 1.00 39.99 ? 142  SER I C   1 
ATOM   9903  O  O   . SER I  1 143 ? 86.571  48.476  19.193 1.00 39.90 ? 142  SER I O   1 
ATOM   9904  C  CB  . SER I  1 143 ? 87.368  51.003  21.383 1.00 40.15 ? 142  SER I CB  1 
ATOM   9905  O  OG  . SER I  1 143 ? 86.710  50.095  22.249 1.00 42.74 ? 142  SER I OG  1 
ATOM   9906  N  N   . ARG I  1 144 ? 88.705  49.060  19.622 1.00 39.88 ? 143  ARG I N   1 
ATOM   9907  C  CA  . ARG I  1 144 ? 89.267  47.756  19.296 1.00 39.69 ? 143  ARG I CA  1 
ATOM   9908  C  C   . ARG I  1 144 ? 89.664  47.086  20.602 1.00 38.83 ? 143  ARG I C   1 
ATOM   9909  O  O   . ARG I  1 144 ? 90.679  47.432  21.202 1.00 40.02 ? 143  ARG I O   1 
ATOM   9910  C  CB  . ARG I  1 144 ? 90.476  47.949  18.381 1.00 38.65 ? 143  ARG I CB  1 
ATOM   9911  C  CG  . ARG I  1 144 ? 90.159  48.887  17.232 1.00 39.32 ? 143  ARG I CG  1 
ATOM   9912  C  CD  . ARG I  1 144 ? 91.335  49.195  16.330 1.00 38.68 ? 143  ARG I CD  1 
ATOM   9913  N  NE  . ARG I  1 144 ? 90.906  50.098  15.265 1.00 40.44 ? 143  ARG I NE  1 
ATOM   9914  C  CZ  . ARG I  1 144 ? 91.658  50.480  14.240 1.00 40.05 ? 143  ARG I CZ  1 
ATOM   9915  N  NH1 . ARG I  1 144 ? 91.158  51.306  13.332 1.00 40.52 ? 143  ARG I NH1 1 
ATOM   9916  N  NH2 . ARG I  1 144 ? 92.901  50.038  14.116 1.00 41.33 ? 143  ARG I NH2 1 
ATOM   9917  N  N   . LEU I  1 145 ? 88.844  46.137  21.045 1.00 37.77 ? 144  LEU I N   1 
ATOM   9918  C  CA  . LEU I  1 145 ? 89.080  45.425  22.294 1.00 36.34 ? 144  LEU I CA  1 
ATOM   9919  C  C   . LEU I  1 145 ? 90.295  44.510  22.228 1.00 35.38 ? 144  LEU I C   1 
ATOM   9920  O  O   . LEU I  1 145 ? 91.074  44.429  23.174 1.00 36.54 ? 144  LEU I O   1 
ATOM   9921  C  CB  . LEU I  1 145 ? 87.855  44.588  22.663 1.00 38.73 ? 144  LEU I CB  1 
ATOM   9922  C  CG  . LEU I  1 145 ? 86.503  45.292  22.788 1.00 39.60 ? 144  LEU I CG  1 
ATOM   9923  C  CD1 . LEU I  1 145 ? 85.420  44.246  22.987 1.00 40.02 ? 144  LEU I CD1 1 
ATOM   9924  C  CD2 . LEU I  1 145 ? 86.526  46.275  23.946 1.00 39.76 ? 144  LEU I CD2 1 
ATOM   9925  N  N   . ALA I  1 146 ? 90.445  43.805  21.115 1.00 34.55 ? 145  ALA I N   1 
ATOM   9926  C  CA  . ALA I  1 146 ? 91.564  42.889  20.949 1.00 33.43 ? 145  ALA I CA  1 
ATOM   9927  C  C   . ALA I  1 146 ? 91.847  42.684  19.478 1.00 32.92 ? 145  ALA I C   1 
ATOM   9928  O  O   . ALA I  1 146 ? 90.971  42.876  18.633 1.00 32.99 ? 145  ALA I O   1 
ATOM   9929  C  CB  . ALA I  1 146 ? 91.258  41.547  21.626 1.00 32.21 ? 145  ALA I CB  1 
ATOM   9930  N  N   . CYS I  1 147 ? 93.077  42.286  19.174 1.00 31.27 ? 146  CYS I N   1 
ATOM   9931  C  CA  . CYS I  1 147 ? 93.485  42.070  17.800 1.00 31.24 ? 146  CYS I CA  1 
ATOM   9932  C  C   . CYS I  1 147 ? 94.674  41.121  17.739 1.00 29.92 ? 146  CYS I C   1 
ATOM   9933  O  O   . CYS I  1 147 ? 95.299  40.825  18.757 1.00 30.13 ? 146  CYS I O   1 
ATOM   9934  C  CB  . CYS I  1 147 ? 93.873  43.404  17.170 1.00 34.58 ? 146  CYS I CB  1 
ATOM   9935  S  SG  . CYS I  1 147 ? 95.178  44.249  18.118 1.00 37.04 ? 146  CYS I SG  1 
ATOM   9936  N  N   . GLY I  1 148 ? 94.980  40.656  16.534 1.00 30.69 ? 147  GLY I N   1 
ATOM   9937  C  CA  . GLY I  1 148 ? 96.096  39.752  16.346 1.00 30.59 ? 147  GLY I CA  1 
ATOM   9938  C  C   . GLY I  1 148 ? 96.486  39.687  14.887 1.00 29.06 ? 147  GLY I C   1 
ATOM   9939  O  O   . GLY I  1 148 ? 95.640  39.820  14.004 1.00 30.20 ? 147  GLY I O   1 
ATOM   9940  N  N   . VAL I  1 149 ? 97.772  39.501  14.623 1.00 29.71 ? 148  VAL I N   1 
ATOM   9941  C  CA  . VAL I  1 149 ? 98.236  39.407  13.250 1.00 30.44 ? 148  VAL I CA  1 
ATOM   9942  C  C   . VAL I  1 149 ? 97.896  38.023  12.720 1.00 31.47 ? 148  VAL I C   1 
ATOM   9943  O  O   . VAL I  1 149 ? 98.062  37.026  13.417 1.00 32.71 ? 148  VAL I O   1 
ATOM   9944  C  CB  . VAL I  1 149 ? 99.759  39.617  13.147 1.00 32.87 ? 148  VAL I CB  1 
ATOM   9945  C  CG1 . VAL I  1 149 ? 100.193 39.495  11.701 1.00 31.22 ? 148  VAL I CG1 1 
ATOM   9946  C  CG2 . VAL I  1 149 ? 100.137 40.986  13.708 1.00 32.54 ? 148  VAL I CG2 1 
ATOM   9947  N  N   . ILE I  1 150 ? 97.413  37.969  11.488 1.00 32.27 ? 149  ILE I N   1 
ATOM   9948  C  CA  . ILE I  1 150 ? 97.041  36.707  10.870 1.00 33.79 ? 149  ILE I CA  1 
ATOM   9949  C  C   . ILE I  1 150 ? 98.286  36.015  10.334 1.00 34.62 ? 149  ILE I C   1 
ATOM   9950  O  O   . ILE I  1 150 ? 98.840  36.421  9.315  1.00 35.23 ? 149  ILE I O   1 
ATOM   9951  C  CB  . ILE I  1 150 ? 96.049  36.940  9.717  1.00 34.49 ? 149  ILE I CB  1 
ATOM   9952  C  CG1 . ILE I  1 150 ? 94.841  37.728  10.238 1.00 35.10 ? 149  ILE I CG1 1 
ATOM   9953  C  CG2 . ILE I  1 150 ? 95.603  35.602  9.130  1.00 32.79 ? 149  ILE I CG2 1 
ATOM   9954  C  CD1 . ILE I  1 150 ? 93.884  38.189  9.155  1.00 36.50 ? 149  ILE I CD1 1 
ATOM   9955  N  N   . GLY I  1 151 ? 98.721  34.968  11.027 1.00 34.79 ? 150  GLY I N   1 
ATOM   9956  C  CA  . GLY I  1 151 ? 99.909  34.254  10.603 1.00 35.89 ? 150  GLY I CA  1 
ATOM   9957  C  C   . GLY I  1 151 ? 99.647  32.974  9.835  1.00 37.36 ? 150  GLY I C   1 
ATOM   9958  O  O   . GLY I  1 151 ? 98.590  32.354  9.968  1.00 36.39 ? 150  GLY I O   1 
ATOM   9959  N  N   . ILE I  1 152 ? 100.620 32.584  9.018  1.00 37.44 ? 151  ILE I N   1 
ATOM   9960  C  CA  . ILE I  1 152 ? 100.520 31.361  8.237  1.00 39.06 ? 151  ILE I CA  1 
ATOM   9961  C  C   . ILE I  1 152 ? 100.541 30.198  9.224  1.00 38.82 ? 151  ILE I C   1 
ATOM   9962  O  O   . ILE I  1 152 ? 101.375 30.159  10.128 1.00 39.04 ? 151  ILE I O   1 
ATOM   9963  C  CB  . ILE I  1 152 ? 101.711 31.225  7.267  1.00 38.18 ? 151  ILE I CB  1 
ATOM   9964  C  CG1 . ILE I  1 152 ? 101.704 32.386  6.273  1.00 39.18 ? 151  ILE I CG1 1 
ATOM   9965  C  CG2 . ILE I  1 152 ? 101.638 29.895  6.530  1.00 37.40 ? 151  ILE I CG2 1 
ATOM   9966  C  CD1 . ILE I  1 152 ? 102.911 32.410  5.350  1.00 37.67 ? 151  ILE I CD1 1 
ATOM   9967  N  N   . ALA I  1 153 ? 99.616  29.259  9.056  1.00 39.90 ? 152  ALA I N   1 
ATOM   9968  C  CA  . ALA I  1 153 ? 99.536  28.108  9.949  1.00 41.54 ? 152  ALA I CA  1 
ATOM   9969  C  C   . ALA I  1 153 ? 99.846  26.806  9.220  1.00 42.47 ? 152  ALA I C   1 
ATOM   9970  O  O   . ALA I  1 153 ? 99.730  26.715  7.998  1.00 42.99 ? 152  ALA I O   1 
ATOM   9971  C  CB  . ALA I  1 153 ? 98.152  28.036  10.588 1.00 40.38 ? 152  ALA I CB  1 
ATOM   9972  N  N   . GLN I  1 154 ? 100.237 25.797  9.986  1.00 43.94 ? 153  GLN I N   1 
ATOM   9973  C  CA  . GLN I  1 154 ? 100.574 24.499  9.426  1.00 47.58 ? 153  GLN I CA  1 
ATOM   9974  C  C   . GLN I  1 154 ? 99.326  23.824  8.858  1.00 48.54 ? 153  GLN I C   1 
ATOM   9975  O  O   . GLN I  1 154 ? 98.322  23.738  9.598  1.00 47.60 ? 153  GLN I O   1 
ATOM   9976  C  CB  . GLN I  1 154 ? 101.194 23.624  10.514 1.00 48.68 ? 153  GLN I CB  1 
ATOM   9977  C  CG  . GLN I  1 154 ? 101.932 22.409  9.995  1.00 52.14 ? 153  GLN I CG  1 
ATOM   9978  C  CD  . GLN I  1 154 ? 102.544 21.590  11.114 1.00 53.07 ? 153  GLN I CD  1 
ATOM   9979  O  OE1 . GLN I  1 154 ? 103.400 20.739  10.876 1.00 55.72 ? 153  GLN I OE1 1 
ATOM   9980  N  NE2 . GLN I  1 154 ? 102.103 21.839  12.343 1.00 54.11 ? 153  GLN I NE2 1 
ATOM   9981  O  OXT . GLN I  1 154 ? 99.367  23.387  7.685  1.00 48.72 ? 153  GLN I OXT 1 
ATOM   9982  N  N   . ALA J  1 2   ? 105.064 43.186  0.027  0.00 54.64 ? 1    ALA J N   1 
ATOM   9983  C  CA  . ALA J  1 2   ? 105.150 44.552  0.617  0.00 54.60 ? 1    ALA J CA  1 
ATOM   9984  C  C   . ALA J  1 2   ? 106.604 44.994  0.743  1.00 54.63 ? 1    ALA J C   1 
ATOM   9985  O  O   . ALA J  1 2   ? 107.522 44.185  0.609  1.00 55.17 ? 1    ALA J O   1 
ATOM   9986  C  CB  . ALA J  1 2   ? 104.479 44.570  1.985  0.00 54.65 ? 1    ALA J CB  1 
ATOM   9987  N  N   . THR J  1 3   ? 106.807 46.283  0.995  1.00 53.70 ? 2    THR J N   1 
ATOM   9988  C  CA  . THR J  1 3   ? 108.150 46.825  1.138  1.00 52.00 ? 2    THR J CA  1 
ATOM   9989  C  C   . THR J  1 3   ? 108.500 47.063  2.604  1.00 50.04 ? 2    THR J C   1 
ATOM   9990  O  O   . THR J  1 3   ? 109.663 47.280  2.942  1.00 49.53 ? 2    THR J O   1 
ATOM   9991  C  CB  . THR J  1 3   ? 108.313 48.152  0.356  1.00 53.00 ? 2    THR J CB  1 
ATOM   9992  O  OG1 . THR J  1 3   ? 107.284 49.072  0.741  1.00 53.59 ? 2    THR J OG1 1 
ATOM   9993  C  CG2 . THR J  1 3   ? 108.229 47.899  -1.140 1.00 54.61 ? 2    THR J CG2 1 
ATOM   9994  N  N   . LYS J  1 4   ? 107.494 47.021  3.473  1.00 47.23 ? 3    LYS J N   1 
ATOM   9995  C  CA  . LYS J  1 4   ? 107.725 47.222  4.899  1.00 45.75 ? 3    LYS J CA  1 
ATOM   9996  C  C   . LYS J  1 4   ? 106.932 46.253  5.770  1.00 43.73 ? 3    LYS J C   1 
ATOM   9997  O  O   . LYS J  1 4   ? 105.790 45.906  5.463  1.00 43.15 ? 3    LYS J O   1 
ATOM   9998  C  CB  . LYS J  1 4   ? 107.389 48.659  5.296  1.00 47.40 ? 3    LYS J CB  1 
ATOM   9999  C  CG  . LYS J  1 4   ? 108.342 49.694  4.719  1.00 49.94 ? 3    LYS J CG  1 
ATOM   10000 C  CD  . LYS J  1 4   ? 107.975 51.096  5.186  1.00 51.97 ? 3    LYS J CD  1 
ATOM   10001 C  CE  . LYS J  1 4   ? 108.924 52.143  4.614  1.00 54.26 ? 3    LYS J CE  1 
ATOM   10002 N  NZ  . LYS J  1 4   ? 108.566 53.530  5.042  1.00 55.05 ? 3    LYS J NZ  1 
ATOM   10003 N  N   . ALA J  1 5   ? 107.552 45.823  6.862  1.00 41.33 ? 4    ALA J N   1 
ATOM   10004 C  CA  . ALA J  1 5   ? 106.926 44.897  7.797  1.00 38.30 ? 4    ALA J CA  1 
ATOM   10005 C  C   . ALA J  1 5   ? 107.356 45.226  9.224  1.00 37.20 ? 4    ALA J C   1 
ATOM   10006 O  O   . ALA J  1 5   ? 108.271 46.028  9.440  1.00 36.16 ? 4    ALA J O   1 
ATOM   10007 C  CB  . ALA J  1 5   ? 107.312 43.464  7.444  1.00 36.32 ? 4    ALA J CB  1 
ATOM   10008 N  N   . VAL J  1 6   ? 106.690 44.611  10.197 1.00 34.52 ? 5    VAL J N   1 
ATOM   10009 C  CA  . VAL J  1 6   ? 107.004 44.840  11.599 1.00 33.40 ? 5    VAL J CA  1 
ATOM   10010 C  C   . VAL J  1 6   ? 106.566 43.668  12.472 1.00 34.61 ? 5    VAL J C   1 
ATOM   10011 O  O   . VAL J  1 6   ? 105.587 42.982  12.169 1.00 34.56 ? 5    VAL J O   1 
ATOM   10012 C  CB  . VAL J  1 6   ? 106.316 46.118  12.128 1.00 32.64 ? 5    VAL J CB  1 
ATOM   10013 C  CG1 . VAL J  1 6   ? 104.798 45.966  12.048 1.00 34.68 ? 5    VAL J CG1 1 
ATOM   10014 C  CG2 . VAL J  1 6   ? 106.750 46.384  13.555 1.00 29.58 ? 5    VAL J CG2 1 
ATOM   10015 N  N   . ALA J  1 7   ? 107.299 43.447  13.556 1.00 32.75 ? 6    ALA J N   1 
ATOM   10016 C  CA  . ALA J  1 7   ? 106.988 42.372  14.481 1.00 32.73 ? 6    ALA J CA  1 
ATOM   10017 C  C   . ALA J  1 7   ? 107.193 42.843  15.914 1.00 34.22 ? 6    ALA J C   1 
ATOM   10018 O  O   . ALA J  1 7   ? 108.259 43.358  16.266 1.00 34.99 ? 6    ALA J O   1 
ATOM   10019 C  CB  . ALA J  1 7   ? 107.872 41.153  14.193 1.00 32.30 ? 6    ALA J CB  1 
ATOM   10020 N  N   . VAL J  1 8   ? 106.158 42.684  16.730 1.00 32.99 ? 7    VAL J N   1 
ATOM   10021 C  CA  . VAL J  1 8   ? 106.214 43.063  18.135 1.00 34.99 ? 7    VAL J CA  1 
ATOM   10022 C  C   . VAL J  1 8   ? 106.524 41.779  18.896 1.00 35.64 ? 7    VAL J C   1 
ATOM   10023 O  O   . VAL J  1 8   ? 105.746 40.827  18.857 1.00 35.49 ? 7    VAL J O   1 
ATOM   10024 C  CB  . VAL J  1 8   ? 104.859 43.650  18.600 1.00 35.05 ? 7    VAL J CB  1 
ATOM   10025 C  CG1 . VAL J  1 8   ? 104.884 43.933  20.093 1.00 32.95 ? 7    VAL J CG1 1 
ATOM   10026 C  CG2 . VAL J  1 8   ? 104.565 44.928  17.826 1.00 36.19 ? 7    VAL J CG2 1 
ATOM   10027 N  N   . LEU J  1 9   ? 107.671 41.747  19.567 1.00 35.79 ? 8    LEU J N   1 
ATOM   10028 C  CA  . LEU J  1 9   ? 108.090 40.562  20.303 1.00 36.87 ? 8    LEU J CA  1 
ATOM   10029 C  C   . LEU J  1 9   ? 107.555 40.529  21.727 1.00 36.88 ? 8    LEU J C   1 
ATOM   10030 O  O   . LEU J  1 9   ? 107.741 41.472  22.491 1.00 35.74 ? 8    LEU J O   1 
ATOM   10031 C  CB  . LEU J  1 9   ? 109.621 40.470  20.334 1.00 37.59 ? 8    LEU J CB  1 
ATOM   10032 C  CG  . LEU J  1 9   ? 110.352 40.480  18.987 1.00 38.25 ? 8    LEU J CG  1 
ATOM   10033 C  CD1 . LEU J  1 9   ? 111.852 40.387  19.218 1.00 38.26 ? 8    LEU J CD1 1 
ATOM   10034 C  CD2 . LEU J  1 9   ? 109.875 39.321  18.132 1.00 40.35 ? 8    LEU J CD2 1 
ATOM   10035 N  N   . LYS J  1 10  ? 106.891 39.430  22.070 1.00 37.86 ? 9    LYS J N   1 
ATOM   10036 C  CA  . LYS J  1 10  ? 106.329 39.242  23.404 1.00 39.61 ? 9    LYS J CA  1 
ATOM   10037 C  C   . LYS J  1 10  ? 106.536 37.800  23.849 1.00 40.04 ? 9    LYS J C   1 
ATOM   10038 O  O   . LYS J  1 10  ? 106.628 36.892  23.023 1.00 37.60 ? 9    LYS J O   1 
ATOM   10039 C  CB  . LYS J  1 10  ? 104.828 39.556  23.412 1.00 41.25 ? 9    LYS J CB  1 
ATOM   10040 C  CG  . LYS J  1 10  ? 104.476 40.955  22.940 1.00 44.03 ? 9    LYS J CG  1 
ATOM   10041 C  CD  . LYS J  1 10  ? 103.039 41.310  23.299 1.00 47.57 ? 9    LYS J CD  1 
ATOM   10042 C  CE  . LYS J  1 10  ? 102.692 42.718  22.848 0.00 47.89 ? 9    LYS J CE  1 
ATOM   10043 N  NZ  . LYS J  1 10  ? 101.267 43.055  23.106 1.00 53.28 ? 9    LYS J NZ  1 
ATOM   10044 N  N   . GLY J  1 11  ? 106.609 37.599  25.160 1.00 42.61 ? 10   GLY J N   1 
ATOM   10045 C  CA  . GLY J  1 11  ? 106.790 36.265  25.702 1.00 44.89 ? 10   GLY J CA  1 
ATOM   10046 C  C   . GLY J  1 11  ? 106.174 36.176  27.085 1.00 47.52 ? 10   GLY J C   1 
ATOM   10047 O  O   . GLY J  1 11  ? 105.395 37.048  27.474 1.00 46.78 ? 10   GLY J O   1 
ATOM   10048 N  N   . ASP J  1 12  ? 106.514 35.127  27.829 1.00 49.61 ? 11   ASP J N   1 
ATOM   10049 C  CA  . ASP J  1 12  ? 105.987 34.959  29.179 1.00 51.88 ? 11   ASP J CA  1 
ATOM   10050 C  C   . ASP J  1 12  ? 106.862 35.696  30.179 1.00 52.47 ? 11   ASP J C   1 
ATOM   10051 O  O   . ASP J  1 12  ? 106.452 35.948  31.312 1.00 53.68 ? 11   ASP J O   1 
ATOM   10052 C  CB  . ASP J  1 12  ? 105.932 33.480  29.556 1.00 53.56 ? 11   ASP J CB  1 
ATOM   10053 C  CG  . ASP J  1 12  ? 105.055 32.679  28.624 1.00 54.83 ? 11   ASP J CG  1 
ATOM   10054 O  OD1 . ASP J  1 12  ? 103.911 33.113  28.369 1.00 55.77 ? 11   ASP J OD1 1 
ATOM   10055 O  OD2 . ASP J  1 12  ? 105.508 31.614  28.153 1.00 55.91 ? 11   ASP J OD2 1 
ATOM   10056 N  N   . GLY J  1 13  ? 108.072 36.040  29.751 1.00 51.66 ? 12   GLY J N   1 
ATOM   10057 C  CA  . GLY J  1 13  ? 108.991 36.743  30.622 1.00 50.95 ? 12   GLY J CA  1 
ATOM   10058 C  C   . GLY J  1 13  ? 109.016 38.232  30.346 1.00 50.13 ? 12   GLY J C   1 
ATOM   10059 O  O   . GLY J  1 13  ? 108.109 38.755  29.702 1.00 50.51 ? 12   GLY J O   1 
ATOM   10060 N  N   . PRO J  1 14  ? 110.052 38.943  30.818 1.00 49.77 ? 13   PRO J N   1 
ATOM   10061 C  CA  . PRO J  1 14  ? 110.212 40.387  30.633 1.00 49.33 ? 13   PRO J CA  1 
ATOM   10062 C  C   . PRO J  1 14  ? 110.709 40.791  29.245 1.00 48.71 ? 13   PRO J C   1 
ATOM   10063 O  O   . PRO J  1 14  ? 110.686 41.970  28.888 1.00 49.50 ? 13   PRO J O   1 
ATOM   10064 C  CB  . PRO J  1 14  ? 111.210 40.751  31.723 1.00 50.00 ? 13   PRO J CB  1 
ATOM   10065 C  CG  . PRO J  1 14  ? 112.112 39.561  31.724 1.00 49.18 ? 13   PRO J CG  1 
ATOM   10066 C  CD  . PRO J  1 14  ? 111.126 38.409  31.678 1.00 49.70 ? 13   PRO J CD  1 
ATOM   10067 N  N   . VAL J  1 15  ? 111.154 39.813  28.463 1.00 48.50 ? 14   VAL J N   1 
ATOM   10068 C  CA  . VAL J  1 15  ? 111.667 40.091  27.127 1.00 46.47 ? 14   VAL J CA  1 
ATOM   10069 C  C   . VAL J  1 15  ? 110.588 40.577  26.166 1.00 46.40 ? 14   VAL J C   1 
ATOM   10070 O  O   . VAL J  1 15  ? 109.570 39.916  25.967 1.00 45.94 ? 14   VAL J O   1 
ATOM   10071 C  CB  . VAL J  1 15  ? 112.342 38.840  26.512 1.00 46.55 ? 14   VAL J CB  1 
ATOM   10072 C  CG1 . VAL J  1 15  ? 112.862 39.161  25.118 1.00 44.83 ? 14   VAL J CG1 1 
ATOM   10073 C  CG2 . VAL J  1 15  ? 113.479 38.368  27.403 1.00 45.75 ? 14   VAL J CG2 1 
ATOM   10074 N  N   . GLN J  1 16  ? 110.822 41.741  25.570 1.00 45.62 ? 15   GLN J N   1 
ATOM   10075 C  CA  . GLN J  1 16  ? 109.888 42.305  24.609 1.00 44.59 ? 15   GLN J CA  1 
ATOM   10076 C  C   . GLN J  1 16  ? 110.592 43.345  23.748 1.00 42.60 ? 15   GLN J C   1 
ATOM   10077 O  O   . GLN J  1 16  ? 111.605 43.917  24.157 1.00 41.54 ? 15   GLN J O   1 
ATOM   10078 C  CB  . GLN J  1 16  ? 108.693 42.933  25.331 1.00 47.23 ? 15   GLN J CB  1 
ATOM   10079 C  CG  . GLN J  1 16  ? 109.032 44.115  26.215 1.00 50.27 ? 15   GLN J CG  1 
ATOM   10080 C  CD  . GLN J  1 16  ? 107.827 44.610  26.995 1.00 52.35 ? 15   GLN J CD  1 
ATOM   10081 O  OE1 . GLN J  1 16  ? 106.783 44.918  26.417 1.00 53.76 ? 15   GLN J OE1 1 
ATOM   10082 N  NE2 . GLN J  1 16  ? 107.966 44.688  28.313 1.00 52.32 ? 15   GLN J NE2 1 
ATOM   10083 N  N   . GLY J  1 17  ? 110.057 43.579  22.553 1.00 39.98 ? 16   GLY J N   1 
ATOM   10084 C  CA  . GLY J  1 17  ? 110.653 44.549  21.653 1.00 38.01 ? 16   GLY J CA  1 
ATOM   10085 C  C   . GLY J  1 17  ? 109.874 44.762  20.367 1.00 37.48 ? 16   GLY J C   1 
ATOM   10086 O  O   . GLY J  1 17  ? 108.813 44.174  20.154 1.00 36.04 ? 16   GLY J O   1 
ATOM   10087 N  N   . ILE J  1 18  ? 110.409 45.617  19.504 1.00 36.29 ? 17   ILE J N   1 
ATOM   10088 C  CA  . ILE J  1 18  ? 109.778 45.926  18.232 1.00 35.22 ? 17   ILE J CA  1 
ATOM   10089 C  C   . ILE J  1 18  ? 110.838 45.873  17.141 1.00 35.13 ? 17   ILE J C   1 
ATOM   10090 O  O   . ILE J  1 18  ? 111.886 46.509  17.252 1.00 34.80 ? 17   ILE J O   1 
ATOM   10091 C  CB  . ILE J  1 18  ? 109.147 47.335  18.256 1.00 37.44 ? 17   ILE J CB  1 
ATOM   10092 C  CG1 . ILE J  1 18  ? 108.103 47.420  19.373 1.00 38.29 ? 17   ILE J CG1 1 
ATOM   10093 C  CG2 . ILE J  1 18  ? 108.494 47.639  16.919 1.00 38.02 ? 17   ILE J CG2 1 
ATOM   10094 C  CD1 . ILE J  1 18  ? 107.537 48.818  19.575 1.00 40.88 ? 17   ILE J CD1 1 
ATOM   10095 N  N   . ILE J  1 19  ? 110.566 45.111  16.089 1.00 33.74 ? 18   ILE J N   1 
ATOM   10096 C  CA  . ILE J  1 19  ? 111.510 44.978  14.989 1.00 32.94 ? 18   ILE J CA  1 
ATOM   10097 C  C   . ILE J  1 19  ? 110.866 45.380  13.673 1.00 33.42 ? 18   ILE J C   1 
ATOM   10098 O  O   . ILE J  1 19  ? 109.789 44.896  13.323 1.00 33.24 ? 18   ILE J O   1 
ATOM   10099 C  CB  . ILE J  1 19  ? 112.022 43.530  14.870 1.00 30.62 ? 18   ILE J CB  1 
ATOM   10100 C  CG1 . ILE J  1 19  ? 112.779 43.143  16.141 1.00 31.61 ? 18   ILE J CG1 1 
ATOM   10101 C  CG2 . ILE J  1 19  ? 112.896 43.382  13.632 1.00 30.29 ? 18   ILE J CG2 1 
ATOM   10102 C  CD1 . ILE J  1 19  ? 113.973 44.028  16.452 1.00 35.58 ? 18   ILE J CD1 1 
ATOM   10103 N  N   . ASN J  1 20  ? 111.534 46.266  12.944 1.00 31.67 ? 19   ASN J N   1 
ATOM   10104 C  CA  . ASN J  1 20  ? 111.026 46.738  11.662 1.00 33.24 ? 19   ASN J CA  1 
ATOM   10105 C  C   . ASN J  1 20  ? 111.758 46.058  10.512 1.00 33.27 ? 19   ASN J C   1 
ATOM   10106 O  O   . ASN J  1 20  ? 112.912 45.654  10.649 1.00 33.44 ? 19   ASN J O   1 
ATOM   10107 C  CB  . ASN J  1 20  ? 111.205 48.255  11.557 1.00 33.20 ? 19   ASN J CB  1 
ATOM   10108 C  CG  . ASN J  1 20  ? 110.558 48.998  12.710 1.00 35.22 ? 19   ASN J CG  1 
ATOM   10109 O  OD1 . ASN J  1 20  ? 109.334 49.103  12.787 1.00 36.46 ? 19   ASN J OD1 1 
ATOM   10110 N  ND2 . ASN J  1 20  ? 111.381 49.509  13.624 1.00 35.65 ? 19   ASN J ND2 1 
ATOM   10111 N  N   . PHE J  1 21  ? 111.076 45.935  9.380  1.00 34.47 ? 20   PHE J N   1 
ATOM   10112 C  CA  . PHE J  1 21  ? 111.647 45.324  8.184  1.00 36.39 ? 20   PHE J CA  1 
ATOM   10113 C  C   . PHE J  1 21  ? 111.362 46.247  7.007  1.00 38.22 ? 20   PHE J C   1 
ATOM   10114 O  O   . PHE J  1 21  ? 110.266 46.803  6.905  1.00 38.13 ? 20   PHE J O   1 
ATOM   10115 C  CB  . PHE J  1 21  ? 110.986 43.973  7.886  1.00 35.12 ? 20   PHE J CB  1 
ATOM   10116 C  CG  . PHE J  1 21  ? 111.274 42.899  8.899  1.00 34.34 ? 20   PHE J CG  1 
ATOM   10117 C  CD1 . PHE J  1 21  ? 112.269 41.958  8.668  1.00 33.10 ? 20   PHE J CD1 1 
ATOM   10118 C  CD2 . PHE J  1 21  ? 110.514 42.798  10.060 1.00 34.00 ? 20   PHE J CD2 1 
ATOM   10119 C  CE1 . PHE J  1 21  ? 112.503 40.928  9.576  1.00 32.46 ? 20   PHE J CE1 1 
ATOM   10120 C  CE2 . PHE J  1 21  ? 110.741 41.770  10.975 1.00 34.65 ? 20   PHE J CE2 1 
ATOM   10121 C  CZ  . PHE J  1 21  ? 111.737 40.832  10.729 1.00 32.26 ? 20   PHE J CZ  1 
ATOM   10122 N  N   . GLU J  1 22  ? 112.340 46.410  6.122  1.00 39.65 ? 21   GLU J N   1 
ATOM   10123 C  CA  . GLU J  1 22  ? 112.154 47.233  4.935  1.00 42.61 ? 21   GLU J CA  1 
ATOM   10124 C  C   . GLU J  1 22  ? 112.955 46.673  3.771  1.00 43.36 ? 21   GLU J C   1 
ATOM   10125 O  O   . GLU J  1 22  ? 114.121 46.305  3.920  1.00 43.58 ? 21   GLU J O   1 
ATOM   10126 C  CB  . GLU J  1 22  ? 112.558 48.689  5.185  1.00 44.71 ? 21   GLU J CB  1 
ATOM   10127 C  CG  . GLU J  1 22  ? 112.285 49.573  3.968  1.00 49.44 ? 21   GLU J CG  1 
ATOM   10128 C  CD  . GLU J  1 22  ? 112.460 51.057  4.237  1.00 52.93 ? 21   GLU J CD  1 
ATOM   10129 O  OE1 . GLU J  1 22  ? 112.234 51.851  3.297  1.00 54.83 ? 21   GLU J OE1 1 
ATOM   10130 O  OE2 . GLU J  1 22  ? 112.819 51.433  5.374  1.00 54.33 ? 21   GLU J OE2 1 
ATOM   10131 N  N   . GLN J  1 23  ? 112.311 46.606  2.613  1.00 44.37 ? 22   GLN J N   1 
ATOM   10132 C  CA  . GLN J  1 23  ? 112.927 46.083  1.401  1.00 47.06 ? 22   GLN J CA  1 
ATOM   10133 C  C   . GLN J  1 23  ? 112.500 46.963  0.225  1.00 49.50 ? 22   GLN J C   1 
ATOM   10134 O  O   . GLN J  1 23  ? 111.325 46.990  -0.150 1.00 49.23 ? 22   GLN J O   1 
ATOM   10135 C  CB  . GLN J  1 23  ? 112.474 44.635  1.188  1.00 45.89 ? 22   GLN J CB  1 
ATOM   10136 C  CG  . GLN J  1 23  ? 112.939 43.987  -0.101 1.00 44.98 ? 22   GLN J CG  1 
ATOM   10137 C  CD  . GLN J  1 23  ? 112.427 42.564  -0.237 1.00 43.80 ? 22   GLN J CD  1 
ATOM   10138 O  OE1 . GLN J  1 23  ? 111.278 42.274  0.098  1.00 44.46 ? 22   GLN J OE1 1 
ATOM   10139 N  NE2 . GLN J  1 23  ? 113.271 41.673  -0.740 1.00 42.06 ? 22   GLN J NE2 1 
ATOM   10140 N  N   . LYS J  1 24  ? 113.458 47.690  -0.344 1.00 51.95 ? 23   LYS J N   1 
ATOM   10141 C  CA  . LYS J  1 24  ? 113.177 48.585  -1.463 1.00 54.24 ? 23   LYS J CA  1 
ATOM   10142 C  C   . LYS J  1 24  ? 112.942 47.868  -2.791 1.00 55.24 ? 23   LYS J C   1 
ATOM   10143 O  O   . LYS J  1 24  ? 111.971 48.157  -3.489 1.00 56.09 ? 23   LYS J O   1 
ATOM   10144 C  CB  . LYS J  1 24  ? 114.311 49.600  -1.623 1.00 55.01 ? 23   LYS J CB  1 
ATOM   10145 C  CG  . LYS J  1 24  ? 114.419 50.594  -0.474 1.00 56.22 ? 23   LYS J CG  1 
ATOM   10146 C  CD  . LYS J  1 24  ? 115.561 51.583  -0.704 1.00 56.77 ? 23   LYS J CD  1 
ATOM   10147 C  CE  . LYS J  1 24  ? 115.674 52.584  0.431  0.00 56.50 ? 23   LYS J CE  1 
ATOM   10148 N  NZ  . LYS J  1 24  ? 116.789 53.546  0.213  0.00 56.51 ? 23   LYS J NZ  1 
ATOM   10149 N  N   . GLU J  1 25  ? 113.830 46.946  -3.147 1.00 56.55 ? 24   GLU J N   1 
ATOM   10150 C  CA  . GLU J  1 25  ? 113.694 46.211  -4.402 1.00 57.82 ? 24   GLU J CA  1 
ATOM   10151 C  C   . GLU J  1 25  ? 112.982 44.877  -4.183 1.00 58.10 ? 24   GLU J C   1 
ATOM   10152 O  O   . GLU J  1 25  ? 113.191 44.209  -3.167 1.00 58.52 ? 24   GLU J O   1 
ATOM   10153 C  CB  . GLU J  1 25  ? 115.073 45.967  -5.026 1.00 57.32 ? 24   GLU J CB  1 
ATOM   10154 C  CG  . GLU J  1 25  ? 115.872 47.231  -5.296 0.00 57.61 ? 24   GLU J CG  1 
ATOM   10155 C  CD  . GLU J  1 25  ? 115.171 48.171  -6.256 0.00 57.59 ? 24   GLU J CD  1 
ATOM   10156 O  OE1 . GLU J  1 25  ? 114.874 47.749  -7.393 0.00 57.64 ? 24   GLU J OE1 1 
ATOM   10157 O  OE2 . GLU J  1 25  ? 114.919 49.333  -5.873 0.00 57.64 ? 24   GLU J OE2 1 
ATOM   10158 N  N   . SER J  1 26  ? 112.148 44.496  -5.147 1.00 58.00 ? 25   SER J N   1 
ATOM   10159 C  CA  . SER J  1 26  ? 111.390 43.251  -5.077 1.00 57.64 ? 25   SER J CA  1 
ATOM   10160 C  C   . SER J  1 26  ? 112.208 42.103  -4.494 1.00 57.09 ? 25   SER J C   1 
ATOM   10161 O  O   . SER J  1 26  ? 111.862 41.552  -3.448 0.00 57.09 ? 25   SER J O   1 
ATOM   10162 C  CB  . SER J  1 26  ? 110.883 42.865  -6.470 1.00 57.95 ? 25   SER J CB  1 
ATOM   10163 O  OG  . SER J  1 26  ? 110.043 43.873  -7.005 0.00 57.84 ? 25   SER J OG  1 
ATOM   10164 N  N   . ASN J  1 27  ? 113.292 41.745  -5.174 1.00 56.52 ? 26   ASN J N   1 
ATOM   10165 C  CA  . ASN J  1 27  ? 114.156 40.663  -4.717 1.00 56.37 ? 26   ASN J CA  1 
ATOM   10166 C  C   . ASN J  1 27  ? 115.441 41.206  -4.092 1.00 56.35 ? 26   ASN J C   1 
ATOM   10167 O  O   . ASN J  1 27  ? 116.440 40.493  -3.988 1.00 56.95 ? 26   ASN J O   1 
ATOM   10168 C  CB  . ASN J  1 27  ? 114.502 39.737  -5.887 0.00 56.30 ? 26   ASN J CB  1 
ATOM   10169 C  CG  . ASN J  1 27  ? 115.184 40.466  -7.032 0.00 56.22 ? 26   ASN J CG  1 
ATOM   10170 O  OD1 . ASN J  1 27  ? 115.543 39.859  -8.041 0.00 56.17 ? 26   ASN J OD1 1 
ATOM   10171 N  ND2 . ASN J  1 27  ? 115.366 41.774  -6.882 0.00 56.17 ? 26   ASN J ND2 1 
ATOM   10172 N  N   . GLY J  1 28  ? 115.407 42.469  -3.674 1.00 54.97 ? 27   GLY J N   1 
ATOM   10173 C  CA  . GLY J  1 28  ? 116.580 43.086  -3.075 1.00 52.05 ? 27   GLY J CA  1 
ATOM   10174 C  C   . GLY J  1 28  ? 116.777 42.771  -1.602 1.00 50.53 ? 27   GLY J C   1 
ATOM   10175 O  O   . GLY J  1 28  ? 116.004 42.012  -1.016 1.00 50.23 ? 27   GLY J O   1 
ATOM   10176 N  N   . PRO J  1 29  ? 117.810 43.349  -0.969 1.00 48.60 ? 28   PRO J N   1 
ATOM   10177 C  CA  . PRO J  1 29  ? 118.093 43.115  0.450  1.00 45.85 ? 28   PRO J CA  1 
ATOM   10178 C  C   . PRO J  1 29  ? 117.047 43.711  1.387  1.00 42.85 ? 28   PRO J C   1 
ATOM   10179 O  O   . PRO J  1 29  ? 116.348 44.668  1.040  1.00 42.23 ? 28   PRO J O   1 
ATOM   10180 C  CB  . PRO J  1 29  ? 119.466 43.755  0.632  1.00 46.97 ? 28   PRO J CB  1 
ATOM   10181 C  CG  . PRO J  1 29  ? 119.406 44.912  -0.314 1.00 47.19 ? 28   PRO J CG  1 
ATOM   10182 C  CD  . PRO J  1 29  ? 118.795 44.281  -1.549 1.00 48.46 ? 28   PRO J CD  1 
ATOM   10183 N  N   . VAL J  1 30  ? 116.945 43.130  2.577  1.00 39.35 ? 29   VAL J N   1 
ATOM   10184 C  CA  . VAL J  1 30  ? 115.997 43.585  3.583  1.00 35.42 ? 29   VAL J CA  1 
ATOM   10185 C  C   . VAL J  1 30  ? 116.759 44.097  4.794  1.00 35.47 ? 29   VAL J C   1 
ATOM   10186 O  O   . VAL J  1 30  ? 117.670 43.435  5.291  1.00 34.27 ? 29   VAL J O   1 
ATOM   10187 C  CB  . VAL J  1 30  ? 115.071 42.435  4.057  1.00 34.99 ? 29   VAL J CB  1 
ATOM   10188 C  CG1 . VAL J  1 30  ? 114.098 42.950  5.109  1.00 33.94 ? 29   VAL J CG1 1 
ATOM   10189 C  CG2 . VAL J  1 30  ? 114.324 41.839  2.874  1.00 33.56 ? 29   VAL J CG2 1 
ATOM   10190 N  N   . LYS J  1 31  ? 116.387 45.280  5.265  1.00 35.46 ? 30   LYS J N   1 
ATOM   10191 C  CA  . LYS J  1 31  ? 117.031 45.853  6.431  1.00 36.35 ? 30   LYS J CA  1 
ATOM   10192 C  C   . LYS J  1 31  ? 116.149 45.531  7.622  1.00 35.35 ? 30   LYS J C   1 
ATOM   10193 O  O   . LYS J  1 31  ? 114.926 45.649  7.548  1.00 34.11 ? 30   LYS J O   1 
ATOM   10194 C  CB  . LYS J  1 31  ? 117.194 47.363  6.258  1.00 39.23 ? 30   LYS J CB  1 
ATOM   10195 C  CG  . LYS J  1 31  ? 118.087 47.713  5.069  1.00 44.87 ? 30   LYS J CG  1 
ATOM   10196 C  CD  . LYS J  1 31  ? 118.377 49.200  4.968  1.00 47.57 ? 30   LYS J CD  1 
ATOM   10197 C  CE  . LYS J  1 31  ? 119.302 49.484  3.791  1.00 49.28 ? 30   LYS J CE  1 
ATOM   10198 N  NZ  . LYS J  1 31  ? 119.592 50.937  3.642  1.00 52.15 ? 30   LYS J NZ  1 
ATOM   10199 N  N   . VAL J  1 32  ? 116.779 45.104  8.708  1.00 33.99 ? 31   VAL J N   1 
ATOM   10200 C  CA  . VAL J  1 32  ? 116.070 44.730  9.925  1.00 34.56 ? 31   VAL J CA  1 
ATOM   10201 C  C   . VAL J  1 32  ? 116.619 45.550  11.083 1.00 34.13 ? 31   VAL J C   1 
ATOM   10202 O  O   . VAL J  1 32  ? 117.795 45.438  11.415 1.00 35.66 ? 31   VAL J O   1 
ATOM   10203 C  CB  . VAL J  1 32  ? 116.281 43.231  10.222 1.00 33.78 ? 31   VAL J CB  1 
ATOM   10204 C  CG1 . VAL J  1 32  ? 115.441 42.805  11.411 1.00 33.85 ? 31   VAL J CG1 1 
ATOM   10205 C  CG2 . VAL J  1 32  ? 115.940 42.410  8.983  1.00 33.58 ? 31   VAL J CG2 1 
ATOM   10206 N  N   . TRP J  1 33  ? 115.773 46.364  11.705 1.00 33.58 ? 32   TRP J N   1 
ATOM   10207 C  CA  . TRP J  1 33  ? 116.233 47.198  12.806 1.00 34.95 ? 32   TRP J CA  1 
ATOM   10208 C  C   . TRP J  1 33  ? 115.168 47.435  13.863 1.00 34.76 ? 32   TRP J C   1 
ATOM   10209 O  O   . TRP J  1 33  ? 113.968 47.410  13.579 1.00 36.28 ? 32   TRP J O   1 
ATOM   10210 C  CB  . TRP J  1 33  ? 116.718 48.549  12.266 1.00 34.32 ? 32   TRP J CB  1 
ATOM   10211 C  CG  . TRP J  1 33  ? 115.606 49.496  11.946 1.00 34.41 ? 32   TRP J CG  1 
ATOM   10212 C  CD1 . TRP J  1 33  ? 115.122 50.494  12.745 1.00 33.92 ? 32   TRP J CD1 1 
ATOM   10213 C  CD2 . TRP J  1 33  ? 114.813 49.514  10.755 1.00 34.62 ? 32   TRP J CD2 1 
ATOM   10214 N  NE1 . TRP J  1 33  ? 114.076 51.133  12.123 1.00 35.79 ? 32   TRP J NE1 1 
ATOM   10215 C  CE2 . TRP J  1 33  ? 113.866 50.553  10.900 1.00 35.25 ? 32   TRP J CE2 1 
ATOM   10216 C  CE3 . TRP J  1 33  ? 114.811 48.755  9.577  1.00 36.25 ? 32   TRP J CE3 1 
ATOM   10217 C  CZ2 . TRP J  1 33  ? 112.921 50.850  9.910  1.00 36.89 ? 32   TRP J CZ2 1 
ATOM   10218 C  CZ3 . TRP J  1 33  ? 113.871 49.049  8.592  1.00 37.63 ? 32   TRP J CZ3 1 
ATOM   10219 C  CH2 . TRP J  1 33  ? 112.940 50.091  8.767  1.00 37.39 ? 32   TRP J CH2 1 
ATOM   10220 N  N   . GLY J  1 34  ? 115.623 47.684  15.084 1.00 33.97 ? 33   GLY J N   1 
ATOM   10221 C  CA  . GLY J  1 34  ? 114.711 47.927  16.181 1.00 33.15 ? 33   GLY J CA  1 
ATOM   10222 C  C   . GLY J  1 34  ? 115.411 47.735  17.508 1.00 34.41 ? 33   GLY J C   1 
ATOM   10223 O  O   . GLY J  1 34  ? 116.632 47.852  17.603 1.00 33.09 ? 33   GLY J O   1 
ATOM   10224 N  N   . SER J  1 35  ? 114.637 47.426  18.538 1.00 34.89 ? 34   SER J N   1 
ATOM   10225 C  CA  . SER J  1 35  ? 115.191 47.232  19.862 1.00 35.52 ? 34   SER J CA  1 
ATOM   10226 C  C   . SER J  1 35  ? 114.432 46.148  20.613 1.00 36.90 ? 34   SER J C   1 
ATOM   10227 O  O   . SER J  1 35  ? 113.264 45.874  20.321 1.00 35.10 ? 34   SER J O   1 
ATOM   10228 C  CB  . SER J  1 35  ? 115.128 48.545  20.642 1.00 37.96 ? 34   SER J CB  1 
ATOM   10229 O  OG  . SER J  1 35  ? 115.650 48.390  21.948 1.00 41.96 ? 34   SER J OG  1 
ATOM   10230 N  N   . ILE J  1 36  ? 115.111 45.538  21.578 1.00 36.58 ? 35   ILE J N   1 
ATOM   10231 C  CA  . ILE J  1 36  ? 114.542 44.482  22.406 1.00 38.64 ? 35   ILE J CA  1 
ATOM   10232 C  C   . ILE J  1 36  ? 115.100 44.691  23.806 1.00 40.12 ? 35   ILE J C   1 
ATOM   10233 O  O   . ILE J  1 36  ? 116.273 45.035  23.957 1.00 41.77 ? 35   ILE J O   1 
ATOM   10234 C  CB  . ILE J  1 36  ? 114.975 43.083  21.911 1.00 37.83 ? 35   ILE J CB  1 
ATOM   10235 C  CG1 . ILE J  1 36  ? 114.563 42.894  20.450 1.00 36.75 ? 35   ILE J CG1 1 
ATOM   10236 C  CG2 . ILE J  1 36  ? 114.353 42.005  22.789 1.00 36.81 ? 35   ILE J CG2 1 
ATOM   10237 C  CD1 . ILE J  1 36  ? 115.160 41.659  19.795 1.00 34.47 ? 35   ILE J CD1 1 
ATOM   10238 N  N   . LYS J  1 37  ? 114.269 44.496  24.825 1.00 40.87 ? 36   LYS J N   1 
ATOM   10239 C  CA  . LYS J  1 37  ? 114.714 44.671  26.205 1.00 42.79 ? 36   LYS J CA  1 
ATOM   10240 C  C   . LYS J  1 37  ? 114.319 43.488  27.079 1.00 43.81 ? 36   LYS J C   1 
ATOM   10241 O  O   . LYS J  1 37  ? 113.499 42.655  26.684 1.00 44.51 ? 36   LYS J O   1 
ATOM   10242 C  CB  . LYS J  1 37  ? 114.122 45.952  26.796 1.00 44.56 ? 36   LYS J CB  1 
ATOM   10243 C  CG  . LYS J  1 37  ? 112.606 45.935  26.913 1.00 46.89 ? 36   LYS J CG  1 
ATOM   10244 C  CD  . LYS J  1 37  ? 112.088 47.177  27.630 1.00 48.05 ? 36   LYS J CD  1 
ATOM   10245 C  CE  . LYS J  1 37  ? 110.567 47.172  27.710 1.00 48.99 ? 36   LYS J CE  1 
ATOM   10246 N  NZ  . LYS J  1 37  ? 110.043 48.380  28.404 0.00 49.03 ? 36   LYS J NZ  1 
ATOM   10247 N  N   . GLY J  1 38  ? 114.905 43.427  28.272 1.00 44.06 ? 37   GLY J N   1 
ATOM   10248 C  CA  . GLY J  1 38  ? 114.607 42.351  29.200 1.00 44.32 ? 37   GLY J CA  1 
ATOM   10249 C  C   . GLY J  1 38  ? 115.452 41.117  28.956 1.00 44.56 ? 37   GLY J C   1 
ATOM   10250 O  O   . GLY J  1 38  ? 115.157 40.037  29.470 1.00 43.94 ? 37   GLY J O   1 
ATOM   10251 N  N   . LEU J  1 39  ? 116.511 41.286  28.171 1.00 44.17 ? 38   LEU J N   1 
ATOM   10252 C  CA  . LEU J  1 39  ? 117.417 40.194  27.832 1.00 43.47 ? 38   LEU J CA  1 
ATOM   10253 C  C   . LEU J  1 39  ? 118.648 40.155  28.722 1.00 43.80 ? 38   LEU J C   1 
ATOM   10254 O  O   . LEU J  1 39  ? 119.038 41.165  29.305 1.00 42.59 ? 38   LEU J O   1 
ATOM   10255 C  CB  . LEU J  1 39  ? 117.890 40.334  26.383 1.00 41.74 ? 38   LEU J CB  1 
ATOM   10256 C  CG  . LEU J  1 39  ? 116.897 40.139  25.241 1.00 42.16 ? 38   LEU J CG  1 
ATOM   10257 C  CD1 . LEU J  1 39  ? 117.480 40.731  23.961 1.00 39.84 ? 38   LEU J CD1 1 
ATOM   10258 C  CD2 . LEU J  1 39  ? 116.594 38.657  25.077 1.00 39.76 ? 38   LEU J CD2 1 
ATOM   10259 N  N   . THR J  1 40  ? 119.258 38.978  28.814 1.00 44.19 ? 39   THR J N   1 
ATOM   10260 C  CA  . THR J  1 40  ? 120.479 38.811  29.591 1.00 45.06 ? 39   THR J CA  1 
ATOM   10261 C  C   . THR J  1 40  ? 121.599 39.303  28.679 1.00 44.90 ? 39   THR J C   1 
ATOM   10262 O  O   . THR J  1 40  ? 121.551 39.097  27.465 1.00 45.71 ? 39   THR J O   1 
ATOM   10263 C  CB  . THR J  1 40  ? 120.730 37.335  29.932 1.00 44.88 ? 39   THR J CB  1 
ATOM   10264 O  OG1 . THR J  1 40  ? 120.884 36.584  28.720 1.00 46.38 ? 39   THR J OG1 1 
ATOM   10265 C  CG2 . THR J  1 40  ? 119.562 36.768  30.723 1.00 46.63 ? 39   THR J CG2 1 
ATOM   10266 N  N   . GLU J  1 41  ? 122.600 39.955  29.257 1.00 44.58 ? 40   GLU J N   1 
ATOM   10267 C  CA  . GLU J  1 41  ? 123.714 40.486  28.478 1.00 44.36 ? 40   GLU J CA  1 
ATOM   10268 C  C   . GLU J  1 41  ? 124.357 39.429  27.588 1.00 43.50 ? 40   GLU J C   1 
ATOM   10269 O  O   . GLU J  1 41  ? 124.572 38.291  28.013 1.00 42.26 ? 40   GLU J O   1 
ATOM   10270 C  CB  . GLU J  1 41  ? 124.775 41.071  29.411 1.00 46.01 ? 40   GLU J CB  1 
ATOM   10271 C  CG  . GLU J  1 41  ? 125.926 41.745  28.688 1.00 48.54 ? 40   GLU J CG  1 
ATOM   10272 C  CD  . GLU J  1 41  ? 127.018 42.212  29.633 1.00 50.81 ? 40   GLU J CD  1 
ATOM   10273 O  OE1 . GLU J  1 41  ? 127.969 42.874  29.159 1.00 51.59 ? 40   GLU J OE1 1 
ATOM   10274 O  OE2 . GLU J  1 41  ? 126.931 41.915  30.845 1.00 50.83 ? 40   GLU J OE2 1 
ATOM   10275 N  N   . GLY J  1 42  ? 124.663 39.809  26.351 1.00 41.85 ? 41   GLY J N   1 
ATOM   10276 C  CA  . GLY J  1 42  ? 125.291 38.872  25.438 1.00 40.13 ? 41   GLY J CA  1 
ATOM   10277 C  C   . GLY J  1 42  ? 124.507 38.563  24.176 1.00 39.44 ? 41   GLY J C   1 
ATOM   10278 O  O   . GLY J  1 42  ? 123.550 39.261  23.826 1.00 39.28 ? 41   GLY J O   1 
ATOM   10279 N  N   . LEU J  1 43  ? 124.920 37.500  23.494 1.00 37.21 ? 42   LEU J N   1 
ATOM   10280 C  CA  . LEU J  1 43  ? 124.289 37.079  22.249 1.00 36.73 ? 42   LEU J CA  1 
ATOM   10281 C  C   . LEU J  1 43  ? 122.998 36.296  22.452 1.00 34.97 ? 42   LEU J C   1 
ATOM   10282 O  O   . LEU J  1 43  ? 122.841 35.576  23.432 1.00 34.46 ? 42   LEU J O   1 
ATOM   10283 C  CB  . LEU J  1 43  ? 125.264 36.223  21.436 1.00 35.39 ? 42   LEU J CB  1 
ATOM   10284 C  CG  . LEU J  1 43  ? 126.565 36.875  20.969 1.00 38.23 ? 42   LEU J CG  1 
ATOM   10285 C  CD1 . LEU J  1 43  ? 127.479 35.808  20.370 1.00 39.01 ? 42   LEU J CD1 1 
ATOM   10286 C  CD2 . LEU J  1 43  ? 126.262 37.967  19.948 1.00 38.43 ? 42   LEU J CD2 1 
ATOM   10287 N  N   . HIS J  1 44  ? 122.081 36.438  21.504 1.00 34.75 ? 43   HIS J N   1 
ATOM   10288 C  CA  . HIS J  1 44  ? 120.808 35.730  21.541 1.00 31.91 ? 43   HIS J CA  1 
ATOM   10289 C  C   . HIS J  1 44  ? 120.396 35.369  20.119 1.00 31.61 ? 43   HIS J C   1 
ATOM   10290 O  O   . HIS J  1 44  ? 120.416 36.222  19.231 1.00 29.28 ? 43   HIS J O   1 
ATOM   10291 C  CB  . HIS J  1 44  ? 119.737 36.609  22.193 1.00 33.44 ? 43   HIS J CB  1 
ATOM   10292 C  CG  . HIS J  1 44  ? 119.888 36.745  23.671 1.00 33.57 ? 43   HIS J CG  1 
ATOM   10293 N  ND1 . HIS J  1 44  ? 119.515 35.746  24.556 1.00 35.71 ? 43   HIS J ND1 1 
ATOM   10294 C  CD2 . HIS J  1 44  ? 120.395 37.739  24.437 1.00 34.14 ? 43   HIS J CD2 1 
ATOM   10295 C  CE1 . HIS J  1 44  ? 119.785 36.124  25.786 1.00 35.29 ? 43   HIS J CE1 1 
ATOM   10296 N  NE2 . HIS J  1 44  ? 120.321 37.334  25.745 1.00 35.71 ? 43   HIS J NE2 1 
ATOM   10297 N  N   . GLY J  1 45  ? 120.033 34.105  19.905 1.00 30.58 ? 44   GLY J N   1 
ATOM   10298 C  CA  . GLY J  1 45  ? 119.609 33.658  18.587 1.00 29.26 ? 44   GLY J CA  1 
ATOM   10299 C  C   . GLY J  1 45  ? 118.478 34.529  18.071 1.00 28.46 ? 44   GLY J C   1 
ATOM   10300 O  O   . GLY J  1 45  ? 117.631 34.966  18.845 1.00 30.74 ? 44   GLY J O   1 
ATOM   10301 N  N   . PHE J  1 46  ? 118.454 34.761  16.764 1.00 28.29 ? 45   PHE J N   1 
ATOM   10302 C  CA  . PHE J  1 46  ? 117.458 35.625  16.134 1.00 29.03 ? 45   PHE J CA  1 
ATOM   10303 C  C   . PHE J  1 46  ? 117.089 34.981  14.793 1.00 29.50 ? 45   PHE J C   1 
ATOM   10304 O  O   . PHE J  1 46  ? 117.887 34.997  13.855 1.00 29.03 ? 45   PHE J O   1 
ATOM   10305 C  CB  . PHE J  1 46  ? 118.104 37.007  15.927 1.00 29.96 ? 45   PHE J CB  1 
ATOM   10306 C  CG  . PHE J  1 46  ? 117.136 38.122  15.615 1.00 29.86 ? 45   PHE J CG  1 
ATOM   10307 C  CD1 . PHE J  1 46  ? 116.168 38.508  16.536 1.00 30.21 ? 45   PHE J CD1 1 
ATOM   10308 C  CD2 . PHE J  1 46  ? 117.249 38.837  14.426 1.00 29.60 ? 45   PHE J CD2 1 
ATOM   10309 C  CE1 . PHE J  1 46  ? 115.329 39.595  16.280 1.00 31.44 ? 45   PHE J CE1 1 
ATOM   10310 C  CE2 . PHE J  1 46  ? 116.415 39.926  14.158 1.00 30.14 ? 45   PHE J CE2 1 
ATOM   10311 C  CZ  . PHE J  1 46  ? 115.456 40.307  15.087 1.00 29.63 ? 45   PHE J CZ  1 
ATOM   10312 N  N   . HIS J  1 47  ? 115.891 34.405  14.698 1.00 28.45 ? 46   HIS J N   1 
ATOM   10313 C  CA  . HIS J  1 47  ? 115.484 33.748  13.458 1.00 29.35 ? 46   HIS J CA  1 
ATOM   10314 C  C   . HIS J  1 47  ? 114.021 33.922  13.083 1.00 29.46 ? 46   HIS J C   1 
ATOM   10315 O  O   . HIS J  1 47  ? 113.180 34.280  13.905 1.00 28.51 ? 46   HIS J O   1 
ATOM   10316 C  CB  . HIS J  1 47  ? 115.746 32.233  13.526 1.00 32.24 ? 46   HIS J CB  1 
ATOM   10317 C  CG  . HIS J  1 47  ? 116.966 31.852  14.296 1.00 31.39 ? 46   HIS J CG  1 
ATOM   10318 N  ND1 . HIS J  1 47  ? 116.914 31.400  15.603 1.00 34.10 ? 46   HIS J ND1 1 
ATOM   10319 C  CD2 . HIS J  1 47  ? 118.277 31.841  13.959 1.00 32.05 ? 46   HIS J CD2 1 
ATOM   10320 C  CE1 . HIS J  1 47  ? 118.128 31.132  16.026 1.00 34.30 ? 46   HIS J CE1 1 
ATOM   10321 N  NE2 . HIS J  1 47  ? 118.982 31.391  15.045 1.00 32.83 ? 46   HIS J NE2 1 
ATOM   10322 N  N   . VAL J  1 48  ? 113.729 33.651  11.819 1.00 29.47 ? 47   VAL J N   1 
ATOM   10323 C  CA  . VAL J  1 48  ? 112.364 33.710  11.338 1.00 31.62 ? 47   VAL J CA  1 
ATOM   10324 C  C   . VAL J  1 48  ? 111.911 32.254  11.301 1.00 32.65 ? 47   VAL J C   1 
ATOM   10325 O  O   . VAL J  1 48  ? 112.535 31.423  10.631 1.00 30.30 ? 47   VAL J O   1 
ATOM   10326 C  CB  . VAL J  1 48  ? 112.275 34.303  9.919  1.00 31.85 ? 47   VAL J CB  1 
ATOM   10327 C  CG1 . VAL J  1 48  ? 110.834 34.246  9.423  1.00 33.90 ? 47   VAL J CG1 1 
ATOM   10328 C  CG2 . VAL J  1 48  ? 112.763 35.739  9.929  1.00 32.33 ? 47   VAL J CG2 1 
ATOM   10329 N  N   . HIS J  1 49  ? 110.857 31.938  12.048 1.00 33.56 ? 48   HIS J N   1 
ATOM   10330 C  CA  . HIS J  1 49  ? 110.338 30.577  12.069 1.00 34.90 ? 48   HIS J CA  1 
ATOM   10331 C  C   . HIS J  1 49  ? 109.199 30.418  11.075 1.00 35.10 ? 48   HIS J C   1 
ATOM   10332 O  O   . HIS J  1 49  ? 108.520 31.382  10.717 1.00 35.17 ? 48   HIS J O   1 
ATOM   10333 C  CB  . HIS J  1 49  ? 109.899 30.176  13.480 1.00 33.80 ? 48   HIS J CB  1 
ATOM   10334 C  CG  . HIS J  1 49  ? 111.047 29.935  14.414 1.00 34.47 ? 48   HIS J CG  1 
ATOM   10335 N  ND1 . HIS J  1 49  ? 111.166 28.785  15.166 1.00 33.11 ? 48   HIS J ND1 1 
ATOM   10336 C  CD2 . HIS J  1 49  ? 112.130 30.692  14.705 1.00 33.74 ? 48   HIS J CD2 1 
ATOM   10337 C  CE1 . HIS J  1 49  ? 112.278 28.845  15.881 1.00 31.31 ? 48   HIS J CE1 1 
ATOM   10338 N  NE2 . HIS J  1 49  ? 112.880 29.988  15.622 1.00 32.40 ? 48   HIS J NE2 1 
ATOM   10339 N  N   . GLU J  1 50  ? 109.005 29.182  10.635 1.00 35.77 ? 49   GLU J N   1 
ATOM   10340 C  CA  . GLU J  1 50  ? 108.006 28.842  9.636  1.00 35.69 ? 49   GLU J CA  1 
ATOM   10341 C  C   . GLU J  1 50  ? 106.567 29.322  9.812  1.00 34.17 ? 49   GLU J C   1 
ATOM   10342 O  O   . GLU J  1 50  ? 105.971 29.814  8.856  1.00 35.00 ? 49   GLU J O   1 
ATOM   10343 C  CB  . GLU J  1 50  ? 107.998 27.325  9.433  1.00 36.78 ? 49   GLU J CB  1 
ATOM   10344 C  CG  . GLU J  1 50  ? 107.235 26.874  8.197  1.00 38.16 ? 49   GLU J CG  1 
ATOM   10345 C  CD  . GLU J  1 50  ? 107.298 25.373  7.999  1.00 38.77 ? 49   GLU J CD  1 
ATOM   10346 O  OE1 . GLU J  1 50  ? 106.821 24.895  6.950  1.00 39.67 ? 49   GLU J OE1 1 
ATOM   10347 O  OE2 . GLU J  1 50  ? 107.821 24.676  8.897  1.00 36.48 ? 49   GLU J OE2 1 
ATOM   10348 N  N   . PHE J  1 51  ? 106.010 29.201  11.014 1.00 34.88 ? 50   PHE J N   1 
ATOM   10349 C  CA  . PHE J  1 51  ? 104.607 29.575  11.218 1.00 36.50 ? 50   PHE J CA  1 
ATOM   10350 C  C   . PHE J  1 51  ? 104.286 30.761  12.120 1.00 35.46 ? 50   PHE J C   1 
ATOM   10351 O  O   . PHE J  1 51  ? 104.830 30.890  13.213 1.00 35.19 ? 50   PHE J O   1 
ATOM   10352 C  CB  . PHE J  1 51  ? 103.828 28.362  11.742 1.00 36.91 ? 50   PHE J CB  1 
ATOM   10353 C  CG  . PHE J  1 51  ? 104.094 27.092  10.980 1.00 38.15 ? 50   PHE J CG  1 
ATOM   10354 C  CD1 . PHE J  1 51  ? 103.791 26.998  9.624  1.00 39.00 ? 50   PHE J CD1 1 
ATOM   10355 C  CD2 . PHE J  1 51  ? 104.653 25.990  11.622 1.00 38.99 ? 50   PHE J CD2 1 
ATOM   10356 C  CE1 . PHE J  1 51  ? 104.045 25.821  8.917  1.00 40.72 ? 50   PHE J CE1 1 
ATOM   10357 C  CE2 . PHE J  1 51  ? 104.910 24.811  10.924 1.00 39.89 ? 50   PHE J CE2 1 
ATOM   10358 C  CZ  . PHE J  1 51  ? 104.605 24.727  9.569  1.00 39.41 ? 50   PHE J CZ  1 
ATOM   10359 N  N   . GLY J  1 52  ? 103.367 31.606  11.657 1.00 35.83 ? 51   GLY J N   1 
ATOM   10360 C  CA  . GLY J  1 52  ? 102.942 32.752  12.444 1.00 38.36 ? 51   GLY J CA  1 
ATOM   10361 C  C   . GLY J  1 52  ? 101.796 32.301  13.335 1.00 38.83 ? 51   GLY J C   1 
ATOM   10362 O  O   . GLY J  1 52  ? 100.750 32.947  13.427 1.00 39.32 ? 51   GLY J O   1 
ATOM   10363 N  N   . ASP J  1 53  ? 102.012 31.172  13.999 1.00 39.78 ? 52   ASP J N   1 
ATOM   10364 C  CA  . ASP J  1 53  ? 101.017 30.569  14.877 1.00 39.57 ? 52   ASP J CA  1 
ATOM   10365 C  C   . ASP J  1 53  ? 101.447 30.675  16.332 1.00 39.22 ? 52   ASP J C   1 
ATOM   10366 O  O   . ASP J  1 53  ? 102.385 30.007  16.761 1.00 39.10 ? 52   ASP J O   1 
ATOM   10367 C  CB  . ASP J  1 53  ? 100.831 29.105  14.467 1.00 39.97 ? 52   ASP J CB  1 
ATOM   10368 C  CG  . ASP J  1 53  ? 99.873  28.347  15.367 1.00 40.19 ? 52   ASP J CG  1 
ATOM   10369 O  OD1 . ASP J  1 53  ? 99.452  27.251  14.946 1.00 41.60 ? 52   ASP J OD1 1 
ATOM   10370 O  OD2 . ASP J  1 53  ? 99.553  28.822  16.480 1.00 39.89 ? 52   ASP J OD2 1 
ATOM   10371 N  N   . ASN J  1 54  ? 100.749 31.508  17.093 1.00 38.27 ? 53   ASN J N   1 
ATOM   10372 C  CA  . ASN J  1 54  ? 101.086 31.706  18.494 1.00 39.66 ? 53   ASN J CA  1 
ATOM   10373 C  C   . ASN J  1 54  ? 100.057 31.078  19.435 1.00 40.03 ? 53   ASN J C   1 
ATOM   10374 O  O   . ASN J  1 54  ? 100.046 31.370  20.631 1.00 39.03 ? 53   ASN J O   1 
ATOM   10375 C  CB  . ASN J  1 54  ? 101.197 33.205  18.792 1.00 40.01 ? 53   ASN J CB  1 
ATOM   10376 C  CG  . ASN J  1 54  ? 101.924 33.485  20.086 1.00 41.62 ? 53   ASN J CG  1 
ATOM   10377 O  OD1 . ASN J  1 54  ? 101.489 34.306  20.896 1.00 43.08 ? 53   ASN J OD1 1 
ATOM   10378 N  ND2 . ASN J  1 54  ? 103.050 32.811  20.285 1.00 43.14 ? 53   ASN J ND2 1 
ATOM   10379 N  N   . THR J  1 55  ? 99.199  30.217  18.898 1.00 42.17 ? 54   THR J N   1 
ATOM   10380 C  CA  . THR J  1 55  ? 98.168  29.576  19.710 1.00 45.10 ? 54   THR J CA  1 
ATOM   10381 C  C   . THR J  1 55  ? 98.727  28.964  20.991 1.00 45.57 ? 54   THR J C   1 
ATOM   10382 O  O   . THR J  1 55  ? 98.121  29.081  22.053 1.00 46.35 ? 54   THR J O   1 
ATOM   10383 C  CB  . THR J  1 55  ? 97.428  28.479  18.919 1.00 45.12 ? 54   THR J CB  1 
ATOM   10384 O  OG1 . THR J  1 55  ? 98.367  27.510  18.447 1.00 47.42 ? 54   THR J OG1 1 
ATOM   10385 C  CG2 . THR J  1 55  ? 96.696  29.082  17.733 1.00 46.11 ? 54   THR J CG2 1 
ATOM   10386 N  N   . ALA J  1 56  ? 99.890  28.326  20.892 1.00 46.26 ? 55   ALA J N   1 
ATOM   10387 C  CA  . ALA J  1 56  ? 100.515 27.701  22.053 1.00 47.04 ? 55   ALA J CA  1 
ATOM   10388 C  C   . ALA J  1 56  ? 101.816 28.396  22.440 1.00 47.61 ? 55   ALA J C   1 
ATOM   10389 O  O   . ALA J  1 56  ? 102.751 27.755  22.919 1.00 48.43 ? 55   ALA J O   1 
ATOM   10390 C  CB  . ALA J  1 56  ? 100.783 26.226  21.761 1.00 48.17 ? 55   ALA J CB  1 
ATOM   10391 N  N   . GLY J  1 57  ? 101.874 29.709  22.244 1.00 47.38 ? 56   GLY J N   1 
ATOM   10392 C  CA  . GLY J  1 57  ? 103.089 30.436  22.567 1.00 44.83 ? 56   GLY J CA  1 
ATOM   10393 C  C   . GLY J  1 57  ? 104.040 30.375  21.388 1.00 42.66 ? 56   GLY J C   1 
ATOM   10394 O  O   . GLY J  1 57  ? 103.625 30.057  20.276 1.00 42.52 ? 56   GLY J O   1 
ATOM   10395 N  N   . CYS J  1 58  ? 105.315 30.669  21.618 1.00 42.60 ? 57   CYS J N   1 
ATOM   10396 C  CA  . CYS J  1 58  ? 106.299 30.645  20.538 1.00 40.80 ? 57   CYS J CA  1 
ATOM   10397 C  C   . CYS J  1 58  ? 106.577 29.233  20.025 1.00 39.67 ? 57   CYS J C   1 
ATOM   10398 O  O   . CYS J  1 58  ? 107.044 29.055  18.898 1.00 39.50 ? 57   CYS J O   1 
ATOM   10399 C  CB  . CYS J  1 58  ? 107.604 31.305  21.000 1.00 39.76 ? 57   CYS J CB  1 
ATOM   10400 S  SG  . CYS J  1 58  ? 107.384 33.021  21.576 1.00 40.83 ? 57   CYS J SG  1 
ATOM   10401 N  N   . THR J  1 59  ? 106.271 28.230  20.843 1.00 39.00 ? 58   THR J N   1 
ATOM   10402 C  CA  . THR J  1 59  ? 106.498 26.843  20.455 1.00 38.10 ? 58   THR J CA  1 
ATOM   10403 C  C   . THR J  1 59  ? 105.748 26.477  19.181 1.00 37.60 ? 58   THR J C   1 
ATOM   10404 O  O   . THR J  1 59  ? 106.227 25.670  18.387 1.00 37.84 ? 58   THR J O   1 
ATOM   10405 C  CB  . THR J  1 59  ? 106.057 25.864  21.561 1.00 40.15 ? 58   THR J CB  1 
ATOM   10406 O  OG1 . THR J  1 59  ? 106.739 26.174  22.782 1.00 40.01 ? 58   THR J OG1 1 
ATOM   10407 C  CG2 . THR J  1 59  ? 106.380 24.425  21.155 1.00 40.99 ? 58   THR J CG2 1 
ATOM   10408 N  N   . SER J  1 60  ? 104.573 27.067  18.981 1.00 36.64 ? 59   SER J N   1 
ATOM   10409 C  CA  . SER J  1 60  ? 103.781 26.760  17.797 1.00 36.79 ? 59   SER J CA  1 
ATOM   10410 C  C   . SER J  1 60  ? 104.251 27.439  16.515 1.00 36.18 ? 59   SER J C   1 
ATOM   10411 O  O   . SER J  1 60  ? 103.626 27.286  15.465 1.00 35.96 ? 59   SER J O   1 
ATOM   10412 C  CB  . SER J  1 60  ? 102.295 27.066  18.054 1.00 39.13 ? 59   SER J CB  1 
ATOM   10413 O  OG  . SER J  1 60  ? 102.118 28.243  18.825 1.00 42.59 ? 59   SER J OG  1 
ATOM   10414 N  N   . ALA J  1 61  ? 105.363 28.166  16.591 1.00 36.51 ? 60   ALA J N   1 
ATOM   10415 C  CA  . ALA J  1 61  ? 105.914 28.851  15.422 1.00 35.56 ? 60   ALA J CA  1 
ATOM   10416 C  C   . ALA J  1 61  ? 106.574 27.865  14.464 1.00 34.79 ? 60   ALA J C   1 
ATOM   10417 O  O   . ALA J  1 61  ? 106.817 28.180  13.294 1.00 32.40 ? 60   ALA J O   1 
ATOM   10418 C  CB  . ALA J  1 61  ? 106.928 29.901  15.863 1.00 37.54 ? 60   ALA J CB  1 
ATOM   10419 N  N   . GLY J  1 62  ? 106.864 26.668  14.966 1.00 35.41 ? 61   GLY J N   1 
ATOM   10420 C  CA  . GLY J  1 62  ? 107.491 25.649  14.143 1.00 35.30 ? 61   GLY J CA  1 
ATOM   10421 C  C   . GLY J  1 62  ? 108.999 25.817  14.078 1.00 35.12 ? 61   GLY J C   1 
ATOM   10422 O  O   . GLY J  1 62  ? 109.567 26.564  14.875 1.00 33.72 ? 61   GLY J O   1 
ATOM   10423 N  N   . PRO J  1 63  ? 109.674 25.129  13.142 1.00 34.84 ? 62   PRO J N   1 
ATOM   10424 C  CA  . PRO J  1 63  ? 111.129 25.198  12.965 1.00 34.70 ? 62   PRO J CA  1 
ATOM   10425 C  C   . PRO J  1 63  ? 111.511 26.461  12.193 1.00 33.60 ? 62   PRO J C   1 
ATOM   10426 O  O   . PRO J  1 63  ? 110.645 27.267  11.861 1.00 33.41 ? 62   PRO J O   1 
ATOM   10427 C  CB  . PRO J  1 63  ? 111.425 23.931  12.174 1.00 34.44 ? 62   PRO J CB  1 
ATOM   10428 C  CG  . PRO J  1 63  ? 110.241 23.869  11.254 1.00 35.32 ? 62   PRO J CG  1 
ATOM   10429 C  CD  . PRO J  1 63  ? 109.082 24.166  12.195 1.00 34.68 ? 62   PRO J CD  1 
ATOM   10430 N  N   . HIS J  1 64  ? 112.799 26.630  11.903 1.00 32.85 ? 63   HIS J N   1 
ATOM   10431 C  CA  . HIS J  1 64  ? 113.258 27.805  11.164 1.00 33.07 ? 63   HIS J CA  1 
ATOM   10432 C  C   . HIS J  1 64  ? 112.696 27.770  9.741  1.00 32.77 ? 63   HIS J C   1 
ATOM   10433 O  O   . HIS J  1 64  ? 112.598 26.705  9.136  1.00 32.42 ? 63   HIS J O   1 
ATOM   10434 C  CB  . HIS J  1 64  ? 114.797 27.836  11.102 1.00 32.99 ? 63   HIS J CB  1 
ATOM   10435 C  CG  . HIS J  1 64  ? 115.456 27.986  12.436 1.00 31.52 ? 63   HIS J CG  1 
ATOM   10436 N  ND1 . HIS J  1 64  ? 116.831 28.003  12.593 1.00 34.76 ? 63   HIS J ND1 1 
ATOM   10437 C  CD2 . HIS J  1 64  ? 114.942 28.134  13.681 1.00 33.96 ? 63   HIS J CD2 1 
ATOM   10438 C  CE1 . HIS J  1 64  ? 117.126 28.153  13.871 1.00 32.42 ? 63   HIS J CE1 1 
ATOM   10439 N  NE2 . HIS J  1 64  ? 115.997 28.236  14.552 1.00 32.11 ? 63   HIS J NE2 1 
ATOM   10440 N  N   . PHE J  1 65  ? 112.315 28.928  9.213  1.00 33.60 ? 64   PHE J N   1 
ATOM   10441 C  CA  . PHE J  1 65  ? 111.789 29.002  7.851  1.00 33.67 ? 64   PHE J CA  1 
ATOM   10442 C  C   . PHE J  1 65  ? 112.866 28.401  6.940  1.00 35.02 ? 64   PHE J C   1 
ATOM   10443 O  O   . PHE J  1 65  ? 113.987 28.915  6.872  1.00 33.30 ? 64   PHE J O   1 
ATOM   10444 C  CB  . PHE J  1 65  ? 111.525 30.457  7.470  1.00 33.70 ? 64   PHE J CB  1 
ATOM   10445 C  CG  . PHE J  1 65  ? 110.864 30.626  6.132  1.00 35.05 ? 64   PHE J CG  1 
ATOM   10446 C  CD1 . PHE J  1 65  ? 111.207 31.691  5.308  1.00 34.45 ? 64   PHE J CD1 1 
ATOM   10447 C  CD2 . PHE J  1 65  ? 109.897 29.723  5.695  1.00 34.60 ? 64   PHE J CD2 1 
ATOM   10448 C  CE1 . PHE J  1 65  ? 110.594 31.863  4.067  1.00 35.86 ? 64   PHE J CE1 1 
ATOM   10449 C  CE2 . PHE J  1 65  ? 109.276 29.884  4.457  1.00 34.23 ? 64   PHE J CE2 1 
ATOM   10450 C  CZ  . PHE J  1 65  ? 109.627 30.953  3.639  1.00 37.02 ? 64   PHE J CZ  1 
ATOM   10451 N  N   . ASN J  1 66  ? 112.528 27.324  6.235  1.00 34.40 ? 65   ASN J N   1 
ATOM   10452 C  CA  . ASN J  1 66  ? 113.503 26.642  5.387  1.00 36.17 ? 65   ASN J CA  1 
ATOM   10453 C  C   . ASN J  1 66  ? 112.932 26.119  4.068  1.00 37.34 ? 65   ASN J C   1 
ATOM   10454 O  O   . ASN J  1 66  ? 112.873 24.915  3.840  1.00 38.50 ? 65   ASN J O   1 
ATOM   10455 C  CB  . ASN J  1 66  ? 114.115 25.491  6.194  1.00 35.71 ? 65   ASN J CB  1 
ATOM   10456 C  CG  . ASN J  1 66  ? 115.282 24.830  5.493  1.00 38.23 ? 65   ASN J CG  1 
ATOM   10457 O  OD1 . ASN J  1 66  ? 115.956 25.445  4.668  1.00 35.36 ? 65   ASN J OD1 1 
ATOM   10458 N  ND2 . ASN J  1 66  ? 115.545 23.573  5.844  1.00 37.72 ? 65   ASN J ND2 1 
ATOM   10459 N  N   . PRO J  1 67  ? 112.523 27.024  3.170  1.00 39.11 ? 66   PRO J N   1 
ATOM   10460 C  CA  . PRO J  1 67  ? 111.961 26.606  1.882  1.00 40.39 ? 66   PRO J CA  1 
ATOM   10461 C  C   . PRO J  1 67  ? 112.949 25.927  0.925  1.00 41.99 ? 66   PRO J C   1 
ATOM   10462 O  O   . PRO J  1 67  ? 112.533 25.215  0.009  1.00 42.72 ? 66   PRO J O   1 
ATOM   10463 C  CB  . PRO J  1 67  ? 111.404 27.908  1.315  1.00 39.92 ? 66   PRO J CB  1 
ATOM   10464 C  CG  . PRO J  1 67  ? 112.366 28.925  1.842  1.00 40.93 ? 66   PRO J CG  1 
ATOM   10465 C  CD  . PRO J  1 67  ? 112.539 28.493  3.283  1.00 38.85 ? 66   PRO J CD  1 
ATOM   10466 N  N   . LEU J  1 68  ? 114.248 26.144  1.122  1.00 41.65 ? 67   LEU J N   1 
ATOM   10467 C  CA  . LEU J  1 68  ? 115.242 25.519  0.249  1.00 41.42 ? 67   LEU J CA  1 
ATOM   10468 C  C   . LEU J  1 68  ? 115.705 24.176  0.804  1.00 41.17 ? 67   LEU J C   1 
ATOM   10469 O  O   . LEU J  1 68  ? 116.524 23.491  0.193  1.00 42.07 ? 67   LEU J O   1 
ATOM   10470 C  CB  . LEU J  1 68  ? 116.456 26.433  0.053  1.00 42.07 ? 67   LEU J CB  1 
ATOM   10471 C  CG  . LEU J  1 68  ? 116.246 27.810  -0.585 1.00 43.17 ? 67   LEU J CG  1 
ATOM   10472 C  CD1 . LEU J  1 68  ? 117.604 28.438  -0.833 1.00 44.31 ? 67   LEU J CD1 1 
ATOM   10473 C  CD2 . LEU J  1 68  ? 115.481 27.693  -1.892 1.00 44.03 ? 67   LEU J CD2 1 
ATOM   10474 N  N   . SER J  1 69  ? 115.182 23.805  1.968  1.00 40.72 ? 68   SER J N   1 
ATOM   10475 C  CA  . SER J  1 69  ? 115.540 22.537  2.596  1.00 41.08 ? 68   SER J CA  1 
ATOM   10476 C  C   . SER J  1 69  ? 117.047 22.346  2.763  1.00 40.21 ? 68   SER J C   1 
ATOM   10477 O  O   . SER J  1 69  ? 117.614 21.391  2.237  1.00 39.91 ? 68   SER J O   1 
ATOM   10478 C  CB  . SER J  1 69  ? 114.977 21.371  1.776  1.00 41.42 ? 68   SER J CB  1 
ATOM   10479 O  OG  . SER J  1 69  ? 113.567 21.456  1.676  1.00 43.46 ? 68   SER J OG  1 
ATOM   10480 N  N   . ARG J  1 70  ? 117.694 23.251  3.492  1.00 40.04 ? 69   ARG J N   1 
ATOM   10481 C  CA  . ARG J  1 70  ? 119.134 23.148  3.731  1.00 39.39 ? 69   ARG J CA  1 
ATOM   10482 C  C   . ARG J  1 70  ? 119.400 23.028  5.227  1.00 36.61 ? 69   ARG J C   1 
ATOM   10483 O  O   . ARG J  1 70  ? 118.467 23.010  6.021  1.00 35.01 ? 69   ARG J O   1 
ATOM   10484 C  CB  . ARG J  1 70  ? 119.862 24.371  3.157  1.00 40.02 ? 69   ARG J CB  1 
ATOM   10485 C  CG  . ARG J  1 70  ? 119.888 24.407  1.632  1.00 42.43 ? 69   ARG J CG  1 
ATOM   10486 C  CD  . ARG J  1 70  ? 120.534 25.682  1.097  1.00 45.08 ? 69   ARG J CD  1 
ATOM   10487 N  NE  . ARG J  1 70  ? 120.538 25.705  -0.363 1.00 46.68 ? 69   ARG J NE  1 
ATOM   10488 C  CZ  . ARG J  1 70  ? 120.946 26.734  -1.102 1.00 47.93 ? 69   ARG J CZ  1 
ATOM   10489 N  NH1 . ARG J  1 70  ? 120.912 26.653  -2.425 1.00 47.72 ? 69   ARG J NH1 1 
ATOM   10490 N  NH2 . ARG J  1 70  ? 121.384 27.845  -0.522 1.00 48.11 ? 69   ARG J NH2 1 
ATOM   10491 N  N   . LYS J  1 71  ? 120.670 22.931  5.606  1.00 36.03 ? 70   LYS J N   1 
ATOM   10492 C  CA  . LYS J  1 71  ? 121.040 22.823  7.015  1.00 36.78 ? 70   LYS J CA  1 
ATOM   10493 C  C   . LYS J  1 71  ? 121.148 24.218  7.625  1.00 35.27 ? 70   LYS J C   1 
ATOM   10494 O  O   . LYS J  1 71  ? 121.267 25.207  6.902  1.00 36.10 ? 70   LYS J O   1 
ATOM   10495 C  CB  . LYS J  1 71  ? 122.380 22.099  7.158  1.00 39.40 ? 70   LYS J CB  1 
ATOM   10496 C  CG  . LYS J  1 71  ? 122.378 20.666  6.659  1.00 44.05 ? 70   LYS J CG  1 
ATOM   10497 C  CD  . LYS J  1 71  ? 121.536 19.768  7.550  0.00 46.72 ? 70   LYS J CD  1 
ATOM   10498 C  CE  . LYS J  1 71  ? 121.568 18.326  7.066  1.00 50.62 ? 70   LYS J CE  1 
ATOM   10499 N  NZ  . LYS J  1 71  ? 120.745 17.431  7.937  1.00 53.00 ? 70   LYS J NZ  1 
ATOM   10500 N  N   . HIS J  1 72  ? 121.114 24.289  8.952  1.00 33.57 ? 71   HIS J N   1 
ATOM   10501 C  CA  . HIS J  1 72  ? 121.201 25.562  9.664  1.00 33.24 ? 71   HIS J CA  1 
ATOM   10502 C  C   . HIS J  1 72  ? 122.602 26.170  9.556  1.00 32.44 ? 71   HIS J C   1 
ATOM   10503 O  O   . HIS J  1 72  ? 123.594 25.450  9.477  1.00 31.91 ? 71   HIS J O   1 
ATOM   10504 C  CB  . HIS J  1 72  ? 120.855 25.352  11.143 1.00 32.17 ? 71   HIS J CB  1 
ATOM   10505 C  CG  . HIS J  1 72  ? 120.946 26.596  11.972 1.00 33.00 ? 71   HIS J CG  1 
ATOM   10506 N  ND1 . HIS J  1 72  ? 119.939 27.537  12.023 1.00 34.42 ? 71   HIS J ND1 1 
ATOM   10507 C  CD2 . HIS J  1 72  ? 121.936 27.063  12.771 1.00 32.67 ? 71   HIS J CD2 1 
ATOM   10508 C  CE1 . HIS J  1 72  ? 120.305 28.528  12.817 1.00 33.86 ? 71   HIS J CE1 1 
ATOM   10509 N  NE2 . HIS J  1 72  ? 121.512 28.265  13.284 1.00 31.95 ? 71   HIS J NE2 1 
ATOM   10510 N  N   . GLY J  1 73  ? 122.674 27.498  9.559  1.00 31.45 ? 72   GLY J N   1 
ATOM   10511 C  CA  . GLY J  1 73  ? 123.960 28.168  9.484  1.00 30.85 ? 72   GLY J CA  1 
ATOM   10512 C  C   . GLY J  1 73  ? 123.853 29.628  9.882  1.00 32.00 ? 72   GLY J C   1 
ATOM   10513 O  O   . GLY J  1 73  ? 122.800 30.077  10.343 1.00 31.42 ? 72   GLY J O   1 
ATOM   10514 N  N   . GLY J  1 74  ? 124.948 30.368  9.718  1.00 30.86 ? 73   GLY J N   1 
ATOM   10515 C  CA  . GLY J  1 74  ? 124.947 31.784  10.039 1.00 28.38 ? 73   GLY J CA  1 
ATOM   10516 C  C   . GLY J  1 74  ? 124.411 32.533  8.835  1.00 29.07 ? 73   GLY J C   1 
ATOM   10517 O  O   . GLY J  1 74  ? 124.408 31.986  7.734  1.00 29.59 ? 73   GLY J O   1 
ATOM   10518 N  N   . PRO J  1 75  ? 123.964 33.786  8.994  1.00 29.08 ? 74   PRO J N   1 
ATOM   10519 C  CA  . PRO J  1 75  ? 123.431 34.534  7.854  1.00 30.33 ? 74   PRO J CA  1 
ATOM   10520 C  C   . PRO J  1 75  ? 124.366 34.710  6.656  1.00 32.00 ? 74   PRO J C   1 
ATOM   10521 O  O   . PRO J  1 75  ? 123.905 34.906  5.530  1.00 30.78 ? 74   PRO J O   1 
ATOM   10522 C  CB  . PRO J  1 75  ? 123.008 35.866  8.479  1.00 30.47 ? 74   PRO J CB  1 
ATOM   10523 C  CG  . PRO J  1 75  ? 123.919 36.007  9.658  1.00 30.67 ? 74   PRO J CG  1 
ATOM   10524 C  CD  . PRO J  1 75  ? 123.970 34.610  10.215 1.00 29.45 ? 74   PRO J CD  1 
ATOM   10525 N  N   . LYS J  1 76  ? 125.671 34.622  6.892  1.00 34.55 ? 75   LYS J N   1 
ATOM   10526 C  CA  . LYS J  1 76  ? 126.651 34.793  5.821  1.00 36.27 ? 75   LYS J CA  1 
ATOM   10527 C  C   . LYS J  1 76  ? 126.936 33.504  5.062  1.00 38.42 ? 75   LYS J C   1 
ATOM   10528 O  O   . LYS J  1 76  ? 127.489 33.526  3.962  1.00 38.61 ? 75   LYS J O   1 
ATOM   10529 C  CB  . LYS J  1 76  ? 127.961 35.335  6.392  1.00 36.82 ? 75   LYS J CB  1 
ATOM   10530 C  CG  . LYS J  1 76  ? 127.843 36.706  7.013  1.00 35.67 ? 75   LYS J CG  1 
ATOM   10531 C  CD  . LYS J  1 76  ? 129.184 37.155  7.542  0.00 37.06 ? 75   LYS J CD  1 
ATOM   10532 C  CE  . LYS J  1 76  ? 129.100 38.534  8.149  0.00 37.34 ? 75   LYS J CE  1 
ATOM   10533 N  NZ  . LYS J  1 76  ? 130.432 38.948  8.639  0.00 37.79 ? 75   LYS J NZ  1 
ATOM   10534 N  N   . ASP J  1 77  ? 126.557 32.382  5.655  1.00 39.71 ? 76   ASP J N   1 
ATOM   10535 C  CA  . ASP J  1 77  ? 126.774 31.084  5.039  1.00 41.52 ? 76   ASP J CA  1 
ATOM   10536 C  C   . ASP J  1 77  ? 125.857 30.843  3.848  1.00 43.57 ? 76   ASP J C   1 
ATOM   10537 O  O   . ASP J  1 77  ? 124.728 31.341  3.804  1.00 43.43 ? 76   ASP J O   1 
ATOM   10538 C  CB  . ASP J  1 77  ? 126.560 29.990  6.081  1.00 41.03 ? 76   ASP J CB  1 
ATOM   10539 C  CG  . ASP J  1 77  ? 127.586 30.043  7.185  1.00 40.48 ? 76   ASP J CG  1 
ATOM   10540 O  OD1 . ASP J  1 77  ? 127.317 29.522  8.284  1.00 40.11 ? 76   ASP J OD1 1 
ATOM   10541 O  OD2 . ASP J  1 77  ? 128.671 30.603  6.946  1.00 42.05 ? 76   ASP J OD2 1 
ATOM   10542 N  N   . GLU J  1 78  ? 126.360 30.091  2.874  1.00 44.37 ? 77   GLU J N   1 
ATOM   10543 C  CA  . GLU J  1 78  ? 125.582 29.743  1.693  1.00 45.95 ? 77   GLU J CA  1 
ATOM   10544 C  C   . GLU J  1 78  ? 124.597 28.685  2.162  1.00 44.66 ? 77   GLU J C   1 
ATOM   10545 O  O   . GLU J  1 78  ? 123.420 28.700  1.797  1.00 44.06 ? 77   GLU J O   1 
ATOM   10546 C  CB  . GLU J  1 78  ? 126.492 29.163  0.606  1.00 49.69 ? 77   GLU J CB  1 
ATOM   10547 C  CG  . GLU J  1 78  ? 125.757 28.434  -0.516 1.00 54.87 ? 77   GLU J CG  1 
ATOM   10548 C  CD  . GLU J  1 78  ? 124.879 29.349  -1.355 1.00 58.52 ? 77   GLU J CD  1 
ATOM   10549 O  OE1 . GLU J  1 78  ? 124.166 28.834  -2.244 1.00 61.23 ? 77   GLU J OE1 1 
ATOM   10550 O  OE2 . GLU J  1 78  ? 124.903 30.580  -1.132 1.00 59.80 ? 77   GLU J OE2 1 
ATOM   10551 N  N   . GLU J  1 79  ? 125.100 27.769  2.985  1.00 43.06 ? 78   GLU J N   1 
ATOM   10552 C  CA  . GLU J  1 79  ? 124.295 26.692  3.540  1.00 41.25 ? 78   GLU J CA  1 
ATOM   10553 C  C   . GLU J  1 79  ? 123.645 27.176  4.829  1.00 39.92 ? 78   GLU J C   1 
ATOM   10554 O  O   . GLU J  1 79  ? 124.281 27.225  5.882  1.00 39.23 ? 78   GLU J O   1 
ATOM   10555 C  CB  . GLU J  1 79  ? 125.169 25.470  3.834  1.00 41.53 ? 78   GLU J CB  1 
ATOM   10556 C  CG  . GLU J  1 79  ? 124.404 24.268  4.383  1.00 43.70 ? 78   GLU J CG  1 
ATOM   10557 C  CD  . GLU J  1 79  ? 123.528 23.586  3.340  1.00 44.52 ? 78   GLU J CD  1 
ATOM   10558 O  OE1 . GLU J  1 79  ? 122.804 22.634  3.704  1.00 42.88 ? 78   GLU J OE1 1 
ATOM   10559 O  OE2 . GLU J  1 79  ? 123.565 23.994  2.158  1.00 44.06 ? 78   GLU J OE2 1 
ATOM   10560 N  N   . ARG J  1 80  ? 122.371 27.534  4.739  1.00 39.16 ? 79   ARG J N   1 
ATOM   10561 C  CA  . ARG J  1 80  ? 121.625 28.012  5.894  1.00 38.32 ? 79   ARG J CA  1 
ATOM   10562 C  C   . ARG J  1 80  ? 120.136 28.014  5.587  1.00 36.32 ? 79   ARG J C   1 
ATOM   10563 O  O   . ARG J  1 80  ? 119.725 27.787  4.450  1.00 36.70 ? 79   ARG J O   1 
ATOM   10564 C  CB  . ARG J  1 80  ? 122.065 29.433  6.250  1.00 37.55 ? 79   ARG J CB  1 
ATOM   10565 C  CG  . ARG J  1 80  ? 121.862 30.443  5.129  1.00 39.49 ? 79   ARG J CG  1 
ATOM   10566 C  CD  . ARG J  1 80  ? 120.801 31.473  5.489  1.00 42.25 ? 79   ARG J CD  1 
ATOM   10567 N  NE  . ARG J  1 80  ? 121.252 32.828  5.209  1.00 41.84 ? 79   ARG J NE  1 
ATOM   10568 C  CZ  . ARG J  1 80  ? 120.537 33.928  5.425  1.00 41.84 ? 79   ARG J CZ  1 
ATOM   10569 N  NH1 . ARG J  1 80  ? 121.060 35.110  5.132  1.00 39.38 ? 79   ARG J NH1 1 
ATOM   10570 N  NH2 . ARG J  1 80  ? 119.309 33.857  5.923  1.00 40.50 ? 79   ARG J NH2 1 
ATOM   10571 N  N   . HIS J  1 81  ? 119.334 28.268  6.614  1.00 35.63 ? 80   HIS J N   1 
ATOM   10572 C  CA  . HIS J  1 81  ? 117.883 28.340  6.470  1.00 33.54 ? 80   HIS J CA  1 
ATOM   10573 C  C   . HIS J  1 81  ? 117.577 29.759  6.026  1.00 33.80 ? 80   HIS J C   1 
ATOM   10574 O  O   . HIS J  1 81  ? 118.335 30.674  6.329  1.00 32.38 ? 80   HIS J O   1 
ATOM   10575 C  CB  . HIS J  1 81  ? 117.210 28.096  7.817  1.00 31.35 ? 80   HIS J CB  1 
ATOM   10576 C  CG  . HIS J  1 81  ? 117.489 26.745  8.395  1.00 30.85 ? 80   HIS J CG  1 
ATOM   10577 N  ND1 . HIS J  1 81  ? 117.556 26.520  9.753  1.00 27.98 ? 80   HIS J ND1 1 
ATOM   10578 C  CD2 . HIS J  1 81  ? 117.692 25.546  7.803  1.00 29.53 ? 80   HIS J CD2 1 
ATOM   10579 C  CE1 . HIS J  1 81  ? 117.788 25.237  9.971  1.00 26.86 ? 80   HIS J CE1 1 
ATOM   10580 N  NE2 . HIS J  1 81  ? 117.875 24.625  8.806  1.00 27.46 ? 80   HIS J NE2 1 
ATOM   10581 N  N   . VAL J  1 82  ? 116.477 29.955  5.311  1.00 33.50 ? 81   VAL J N   1 
ATOM   10582 C  CA  . VAL J  1 82  ? 116.132 31.298  4.883  1.00 33.99 ? 81   VAL J CA  1 
ATOM   10583 C  C   . VAL J  1 82  ? 115.923 32.189  6.112  1.00 33.22 ? 81   VAL J C   1 
ATOM   10584 O  O   . VAL J  1 82  ? 116.205 33.385  6.073  1.00 31.99 ? 81   VAL J O   1 
ATOM   10585 C  CB  . VAL J  1 82  ? 114.858 31.298  4.007  1.00 33.08 ? 81   VAL J CB  1 
ATOM   10586 C  CG1 . VAL J  1 82  ? 114.370 32.718  3.785  1.00 34.54 ? 81   VAL J CG1 1 
ATOM   10587 C  CG2 . VAL J  1 82  ? 115.165 30.656  2.661  1.00 34.97 ? 81   VAL J CG2 1 
ATOM   10588 N  N   . GLY J  1 83  ? 115.464 31.594  7.208  1.00 31.70 ? 82   GLY J N   1 
ATOM   10589 C  CA  . GLY J  1 83  ? 115.213 32.365  8.412  1.00 32.08 ? 82   GLY J CA  1 
ATOM   10590 C  C   . GLY J  1 83  ? 116.373 32.583  9.371  1.00 31.56 ? 82   GLY J C   1 
ATOM   10591 O  O   . GLY J  1 83  ? 116.179 33.165  10.435 1.00 31.57 ? 82   GLY J O   1 
ATOM   10592 N  N   . ASP J  1 84  ? 117.573 32.131  9.013  1.00 31.14 ? 83   ASP J N   1 
ATOM   10593 C  CA  . ASP J  1 84  ? 118.734 32.300  9.889  1.00 31.80 ? 83   ASP J CA  1 
ATOM   10594 C  C   . ASP J  1 84  ? 119.298 33.724  9.872  1.00 30.85 ? 83   ASP J C   1 
ATOM   10595 O  O   . ASP J  1 84  ? 119.986 34.112  8.929  1.00 32.61 ? 83   ASP J O   1 
ATOM   10596 C  CB  . ASP J  1 84  ? 119.842 31.310  9.504  1.00 31.91 ? 83   ASP J CB  1 
ATOM   10597 C  CG  . ASP J  1 84  ? 119.434 29.867  9.730  1.00 31.27 ? 83   ASP J CG  1 
ATOM   10598 O  OD1 . ASP J  1 84  ? 118.552 29.645  10.579 1.00 33.80 ? 83   ASP J OD1 1 
ATOM   10599 O  OD2 . ASP J  1 84  ? 119.994 28.958  9.078  1.00 29.62 ? 83   ASP J OD2 1 
ATOM   10600 N  N   . LEU J  1 85  ? 119.015 34.496  10.918 1.00 29.84 ? 84   LEU J N   1 
ATOM   10601 C  CA  . LEU J  1 85  ? 119.513 35.865  10.994 1.00 29.77 ? 84   LEU J CA  1 
ATOM   10602 C  C   . LEU J  1 85  ? 120.613 36.025  12.037 1.00 28.81 ? 84   LEU J C   1 
ATOM   10603 O  O   . LEU J  1 85  ? 120.898 37.134  12.482 1.00 29.58 ? 84   LEU J O   1 
ATOM   10604 C  CB  . LEU J  1 85  ? 118.371 36.838  11.299 1.00 28.50 ? 84   LEU J CB  1 
ATOM   10605 C  CG  . LEU J  1 85  ? 117.257 36.929  10.255 1.00 30.17 ? 84   LEU J CG  1 
ATOM   10606 C  CD1 . LEU J  1 85  ? 116.221 37.951  10.712 1.00 30.06 ? 84   LEU J CD1 1 
ATOM   10607 C  CD2 . LEU J  1 85  ? 117.836 37.319  8.897  1.00 29.00 ? 84   LEU J CD2 1 
ATOM   10608 N  N   . GLY J  1 86  ? 121.216 34.912  12.437 1.00 27.89 ? 85   GLY J N   1 
ATOM   10609 C  CA  . GLY J  1 86  ? 122.299 34.964  13.404 1.00 29.04 ? 85   GLY J CA  1 
ATOM   10610 C  C   . GLY J  1 86  ? 121.938 35.318  14.834 1.00 29.54 ? 85   GLY J C   1 
ATOM   10611 O  O   . GLY J  1 86  ? 121.036 34.712  15.426 1.00 29.71 ? 85   GLY J O   1 
ATOM   10612 N  N   . ASN J  1 87  ? 122.652 36.300  15.386 1.00 27.81 ? 86   ASN J N   1 
ATOM   10613 C  CA  . ASN J  1 87  ? 122.457 36.756  16.759 1.00 27.54 ? 86   ASN J CA  1 
ATOM   10614 C  C   . ASN J  1 87  ? 122.266 38.258  16.888 1.00 30.52 ? 86   ASN J C   1 
ATOM   10615 O  O   . ASN J  1 87  ? 122.655 39.035  16.012 1.00 30.48 ? 86   ASN J O   1 
ATOM   10616 C  CB  . ASN J  1 87  ? 123.676 36.412  17.618 1.00 29.21 ? 86   ASN J CB  1 
ATOM   10617 C  CG  . ASN J  1 87  ? 123.835 34.936  17.858 1.00 31.90 ? 86   ASN J CG  1 
ATOM   10618 O  OD1 . ASN J  1 87  ? 123.037 34.325  18.566 1.00 30.91 ? 86   ASN J OD1 1 
ATOM   10619 N  ND2 . ASN J  1 87  ? 124.876 34.350  17.273 1.00 30.92 ? 86   ASN J ND2 1 
ATOM   10620 N  N   . VAL J  1 88  ? 121.671 38.652  18.009 1.00 30.10 ? 87   VAL J N   1 
ATOM   10621 C  CA  . VAL J  1 88  ? 121.490 40.053  18.345 1.00 30.96 ? 87   VAL J CA  1 
ATOM   10622 C  C   . VAL J  1 88  ? 122.276 40.155  19.646 1.00 31.99 ? 87   VAL J C   1 
ATOM   10623 O  O   . VAL J  1 88  ? 122.466 39.147  20.336 1.00 30.71 ? 87   VAL J O   1 
ATOM   10624 C  CB  . VAL J  1 88  ? 120.015 40.427  18.585 1.00 29.22 ? 87   VAL J CB  1 
ATOM   10625 C  CG1 . VAL J  1 88  ? 119.247 40.364  17.272 1.00 30.70 ? 87   VAL J CG1 1 
ATOM   10626 C  CG2 . VAL J  1 88  ? 119.401 39.505  19.616 1.00 30.44 ? 87   VAL J CG2 1 
ATOM   10627 N  N   . THR J  1 89  ? 122.742 41.353  19.980 1.00 31.68 ? 88   THR J N   1 
ATOM   10628 C  CA  . THR J  1 89  ? 123.534 41.538  21.187 1.00 31.80 ? 88   THR J CA  1 
ATOM   10629 C  C   . THR J  1 89  ? 122.884 42.481  22.190 1.00 33.76 ? 88   THR J C   1 
ATOM   10630 O  O   . THR J  1 89  ? 122.556 43.623  21.864 1.00 32.22 ? 88   THR J O   1 
ATOM   10631 C  CB  . THR J  1 89  ? 124.931 42.088  20.836 1.00 33.47 ? 88   THR J CB  1 
ATOM   10632 O  OG1 . THR J  1 89  ? 125.533 41.255  19.836 1.00 32.46 ? 88   THR J OG1 1 
ATOM   10633 C  CG2 . THR J  1 89  ? 125.821 42.113  22.075 1.00 33.49 ? 88   THR J CG2 1 
ATOM   10634 N  N   . ALA J  1 90  ? 122.703 41.995  23.412 1.00 35.51 ? 89   ALA J N   1 
ATOM   10635 C  CA  . ALA J  1 90  ? 122.107 42.795  24.471 1.00 39.18 ? 89   ALA J CA  1 
ATOM   10636 C  C   . ALA J  1 90  ? 123.220 43.386  25.331 1.00 41.31 ? 89   ALA J C   1 
ATOM   10637 O  O   . ALA J  1 90  ? 124.134 42.675  25.749 1.00 41.07 ? 89   ALA J O   1 
ATOM   10638 C  CB  . ALA J  1 90  ? 121.185 41.933  25.322 1.00 38.42 ? 89   ALA J CB  1 
ATOM   10639 N  N   . ASP J  1 91  ? 123.140 44.686  25.589 1.00 45.03 ? 90   ASP J N   1 
ATOM   10640 C  CA  . ASP J  1 91  ? 124.146 45.364  26.399 1.00 48.31 ? 90   ASP J CA  1 
ATOM   10641 C  C   . ASP J  1 91  ? 123.984 45.028  27.877 1.00 50.25 ? 90   ASP J C   1 
ATOM   10642 O  O   . ASP J  1 91  ? 123.098 44.259  28.255 1.00 49.85 ? 90   ASP J O   1 
ATOM   10643 C  CB  . ASP J  1 91  ? 124.065 46.881  26.179 1.00 48.99 ? 90   ASP J CB  1 
ATOM   10644 C  CG  . ASP J  1 91  ? 122.747 47.479  26.647 1.00 50.95 ? 90   ASP J CG  1 
ATOM   10645 O  OD1 . ASP J  1 91  ? 122.393 48.574  26.156 1.00 51.69 ? 90   ASP J OD1 1 
ATOM   10646 O  OD2 . ASP J  1 91  ? 122.071 46.875  27.509 1.00 51.41 ? 90   ASP J OD2 1 
ATOM   10647 N  N   . LYS J  1 92  ? 124.844 45.605  28.710 1.00 52.60 ? 91   LYS J N   1 
ATOM   10648 C  CA  . LYS J  1 92  ? 124.803 45.357  30.147 1.00 55.05 ? 91   LYS J CA  1 
ATOM   10649 C  C   . LYS J  1 92  ? 123.434 45.645  30.759 1.00 55.19 ? 91   LYS J C   1 
ATOM   10650 O  O   . LYS J  1 92  ? 123.058 45.043  31.763 1.00 55.54 ? 91   LYS J O   1 
ATOM   10651 C  CB  . LYS J  1 92  ? 125.880 46.193  30.853 1.00 56.45 ? 91   LYS J CB  1 
ATOM   10652 C  CG  . LYS J  1 92  ? 125.826 47.682  30.535 1.00 59.61 ? 91   LYS J CG  1 
ATOM   10653 C  CD  . LYS J  1 92  ? 126.960 48.448  31.211 1.00 61.24 ? 91   LYS J CD  1 
ATOM   10654 C  CE  . LYS J  1 92  ? 126.862 48.379  32.731 1.00 63.47 ? 91   LYS J CE  1 
ATOM   10655 N  NZ  . LYS J  1 92  ? 127.964 49.124  33.408 1.00 63.42 ? 91   LYS J NZ  1 
ATOM   10656 N  N   . ASP J  1 93  ? 122.687 46.556  30.145 1.00 55.45 ? 92   ASP J N   1 
ATOM   10657 C  CA  . ASP J  1 93  ? 121.366 46.918  30.648 1.00 55.77 ? 92   ASP J CA  1 
ATOM   10658 C  C   . ASP J  1 93  ? 120.250 46.050  30.077 1.00 54.87 ? 92   ASP J C   1 
ATOM   10659 O  O   . ASP J  1 93  ? 119.071 46.396  30.176 1.00 55.15 ? 92   ASP J O   1 
ATOM   10660 C  CB  . ASP J  1 93  ? 121.087 48.390  30.351 1.00 57.70 ? 92   ASP J CB  1 
ATOM   10661 C  CG  . ASP J  1 93  ? 122.053 49.317  31.064 1.00 59.68 ? 92   ASP J CG  1 
ATOM   10662 O  OD1 . ASP J  1 93  ? 122.018 50.537  30.798 1.00 61.39 ? 92   ASP J OD1 1 
ATOM   10663 O  OD2 . ASP J  1 93  ? 122.846 48.824  31.896 1.00 59.77 ? 92   ASP J OD2 1 
ATOM   10664 N  N   . GLY J  1 94  ? 120.626 44.924  29.480 1.00 52.73 ? 93   GLY J N   1 
ATOM   10665 C  CA  . GLY J  1 94  ? 119.640 44.014  28.923 1.00 50.24 ? 93   GLY J CA  1 
ATOM   10666 C  C   . GLY J  1 94  ? 118.931 44.505  27.677 1.00 48.49 ? 93   GLY J C   1 
ATOM   10667 O  O   . GLY J  1 94  ? 117.960 43.893  27.233 1.00 48.25 ? 93   GLY J O   1 
ATOM   10668 N  N   . VAL J  1 95  ? 119.405 45.608  27.108 1.00 45.92 ? 94   VAL J N   1 
ATOM   10669 C  CA  . VAL J  1 95  ? 118.795 46.151  25.903 1.00 44.30 ? 94   VAL J CA  1 
ATOM   10670 C  C   . VAL J  1 95  ? 119.623 45.817  24.670 1.00 43.56 ? 94   VAL J C   1 
ATOM   10671 O  O   . VAL J  1 95  ? 120.848 45.953  24.672 1.00 44.04 ? 94   VAL J O   1 
ATOM   10672 C  CB  . VAL J  1 95  ? 118.649 47.680  25.981 1.00 44.87 ? 94   VAL J CB  1 
ATOM   10673 C  CG1 . VAL J  1 95  ? 118.060 48.205  24.680 1.00 45.59 ? 94   VAL J CG1 1 
ATOM   10674 C  CG2 . VAL J  1 95  ? 117.763 48.061  27.162 1.00 45.42 ? 94   VAL J CG2 1 
ATOM   10675 N  N   . ALA J  1 96  ? 118.947 45.381  23.614 1.00 41.54 ? 95   ALA J N   1 
ATOM   10676 C  CA  . ALA J  1 96  ? 119.628 45.038  22.378 1.00 38.96 ? 95   ALA J CA  1 
ATOM   10677 C  C   . ALA J  1 96  ? 119.131 45.868  21.210 1.00 38.36 ? 95   ALA J C   1 
ATOM   10678 O  O   . ALA J  1 96  ? 118.003 45.695  20.738 1.00 37.48 ? 95   ALA J O   1 
ATOM   10679 C  CB  . ALA J  1 96  ? 119.446 43.553  22.067 1.00 39.82 ? 95   ALA J CB  1 
ATOM   10680 N  N   . ASP J  1 97  ? 119.968 46.790  20.754 1.00 36.42 ? 96   ASP J N   1 
ATOM   10681 C  CA  . ASP J  1 97  ? 119.617 47.596  19.603 1.00 34.78 ? 96   ASP J CA  1 
ATOM   10682 C  C   . ASP J  1 97  ? 119.923 46.655  18.453 1.00 32.66 ? 96   ASP J C   1 
ATOM   10683 O  O   . ASP J  1 97  ? 120.970 46.013  18.433 1.00 33.46 ? 96   ASP J O   1 
ATOM   10684 C  CB  . ASP J  1 97  ? 120.491 48.845  19.542 1.00 38.46 ? 96   ASP J CB  1 
ATOM   10685 C  CG  . ASP J  1 97  ? 120.135 49.852  20.622 1.00 42.95 ? 96   ASP J CG  1 
ATOM   10686 O  OD1 . ASP J  1 97  ? 121.021 50.639  21.019 1.00 47.01 ? 96   ASP J OD1 1 
ATOM   10687 O  OD2 . ASP J  1 97  ? 118.963 49.864  21.069 1.00 45.26 ? 96   ASP J OD2 1 
ATOM   10688 N  N   . VAL J  1 98  ? 118.999 46.549  17.512 1.00 29.74 ? 97   VAL J N   1 
ATOM   10689 C  CA  . VAL J  1 98  ? 119.176 45.648  16.387 1.00 27.79 ? 97   VAL J CA  1 
ATOM   10690 C  C   . VAL J  1 98  ? 119.284 46.384  15.070 1.00 28.26 ? 97   VAL J C   1 
ATOM   10691 O  O   . VAL J  1 98  ? 118.559 47.342  14.821 1.00 30.10 ? 97   VAL J O   1 
ATOM   10692 C  CB  . VAL J  1 98  ? 117.987 44.655  16.279 1.00 27.35 ? 97   VAL J CB  1 
ATOM   10693 C  CG1 . VAL J  1 98  ? 118.153 43.770  15.052 1.00 27.04 ? 97   VAL J CG1 1 
ATOM   10694 C  CG2 . VAL J  1 98  ? 117.896 43.813  17.536 1.00 26.43 ? 97   VAL J CG2 1 
ATOM   10695 N  N   . SER J  1 99  ? 120.197 45.926  14.227 1.00 28.72 ? 98   SER J N   1 
ATOM   10696 C  CA  . SER J  1 99  ? 120.368 46.506  12.909 1.00 30.85 ? 98   SER J CA  1 
ATOM   10697 C  C   . SER J  1 99  ? 121.087 45.469  12.074 1.00 31.74 ? 98   SER J C   1 
ATOM   10698 O  O   . SER J  1 99  ? 122.293 45.267  12.201 1.00 33.91 ? 98   SER J O   1 
ATOM   10699 C  CB  . SER J  1 99  ? 121.170 47.807  12.969 1.00 32.73 ? 98   SER J CB  1 
ATOM   10700 O  OG  . SER J  1 99  ? 121.119 48.463  11.713 1.00 33.45 ? 98   SER J OG  1 
ATOM   10701 N  N   . ILE J  1 100 ? 120.320 44.801  11.225 1.00 32.43 ? 99   ILE J N   1 
ATOM   10702 C  CA  . ILE J  1 100 ? 120.837 43.749  10.372 1.00 31.71 ? 99   ILE J CA  1 
ATOM   10703 C  C   . ILE J  1 100 ? 120.349 43.978  8.955  1.00 32.34 ? 99   ILE J C   1 
ATOM   10704 O  O   . ILE J  1 100 ? 119.319 44.609  8.740  1.00 33.53 ? 99   ILE J O   1 
ATOM   10705 C  CB  . ILE J  1 100 ? 120.336 42.367  10.878 1.00 33.26 ? 99   ILE J CB  1 
ATOM   10706 C  CG1 . ILE J  1 100 ? 121.032 42.018  12.195 1.00 33.49 ? 99   ILE J CG1 1 
ATOM   10707 C  CG2 . ILE J  1 100 ? 120.564 41.293  9.833  1.00 33.30 ? 99   ILE J CG2 1 
ATOM   10708 C  CD1 . ILE J  1 100 ? 120.475 40.785  12.878 1.00 34.13 ? 99   ILE J CD1 1 
ATOM   10709 N  N   . GLU J  1 101 ? 121.107 43.479  7.990  1.00 32.80 ? 100  GLU J N   1 
ATOM   10710 C  CA  . GLU J  1 101 ? 120.741 43.593  6.589  1.00 34.30 ? 100  GLU J CA  1 
ATOM   10711 C  C   . GLU J  1 101 ? 120.956 42.207  6.013  1.00 33.70 ? 100  GLU J C   1 
ATOM   10712 O  O   . GLU J  1 101 ? 122.036 41.631  6.147  1.00 33.50 ? 100  GLU J O   1 
ATOM   10713 C  CB  . GLU J  1 101 ? 121.627 44.620  5.879  1.00 38.02 ? 100  GLU J CB  1 
ATOM   10714 C  CG  . GLU J  1 101 ? 121.350 44.732  4.391  1.00 45.35 ? 100  GLU J CG  1 
ATOM   10715 C  CD  . GLU J  1 101 ? 121.921 45.999  3.784  1.00 48.72 ? 100  GLU J CD  1 
ATOM   10716 O  OE1 . GLU J  1 101 ? 121.889 46.127  2.543  1.00 50.72 ? 100  GLU J OE1 1 
ATOM   10717 O  OE2 . GLU J  1 101 ? 122.393 46.867  4.551  1.00 50.96 ? 100  GLU J OE2 1 
ATOM   10718 N  N   . ASP J  1 102 ? 119.926 41.662  5.381  1.00 33.47 ? 101  ASP J N   1 
ATOM   10719 C  CA  . ASP J  1 102 ? 120.030 40.319  4.839  1.00 34.32 ? 101  ASP J CA  1 
ATOM   10720 C  C   . ASP J  1 102 ? 119.477 40.238  3.423  1.00 35.99 ? 101  ASP J C   1 
ATOM   10721 O  O   . ASP J  1 102 ? 118.480 40.881  3.098  1.00 36.46 ? 101  ASP J O   1 
ATOM   10722 C  CB  . ASP J  1 102 ? 119.299 39.354  5.780  1.00 33.57 ? 101  ASP J CB  1 
ATOM   10723 C  CG  . ASP J  1 102 ? 119.553 37.906  5.443  1.00 32.23 ? 101  ASP J CG  1 
ATOM   10724 O  OD1 . ASP J  1 102 ? 118.754 37.324  4.684  1.00 31.51 ? 101  ASP J OD1 1 
ATOM   10725 O  OD2 . ASP J  1 102 ? 120.562 37.356  5.933  1.00 32.56 ? 101  ASP J OD2 1 
ATOM   10726 N  N   . SER J  1 103 ? 120.134 39.443  2.584  1.00 38.30 ? 102  SER J N   1 
ATOM   10727 C  CA  . SER J  1 103 ? 119.735 39.289  1.187  1.00 40.77 ? 102  SER J CA  1 
ATOM   10728 C  C   . SER J  1 103 ? 118.923 38.030  0.904  1.00 41.11 ? 102  SER J C   1 
ATOM   10729 O  O   . SER J  1 103 ? 118.357 37.887  -0.183 1.00 40.94 ? 102  SER J O   1 
ATOM   10730 C  CB  . SER J  1 103 ? 120.978 39.274  0.296  1.00 41.66 ? 102  SER J CB  1 
ATOM   10731 O  OG  . SER J  1 103 ? 121.805 40.391  0.564  1.00 46.85 ? 102  SER J OG  1 
ATOM   10732 N  N   . VAL J  1 104 ? 118.875 37.119  1.873  1.00 40.06 ? 103  VAL J N   1 
ATOM   10733 C  CA  . VAL J  1 104 ? 118.146 35.866  1.709  1.00 39.76 ? 103  VAL J CA  1 
ATOM   10734 C  C   . VAL J  1 104 ? 116.653 35.988  2.003  1.00 39.94 ? 103  VAL J C   1 
ATOM   10735 O  O   . VAL J  1 104 ? 115.827 35.590  1.183  1.00 40.02 ? 103  VAL J O   1 
ATOM   10736 C  CB  . VAL J  1 104 ? 118.754 34.755  2.597  1.00 40.49 ? 103  VAL J CB  1 
ATOM   10737 C  CG1 . VAL J  1 104 ? 117.893 33.501  2.536  1.00 40.68 ? 103  VAL J CG1 1 
ATOM   10738 C  CG2 . VAL J  1 104 ? 120.163 34.433  2.119  1.00 40.07 ? 103  VAL J CG2 1 
ATOM   10739 N  N   . ILE J  1 105 ? 116.299 36.522  3.168  1.00 37.99 ? 104  ILE J N   1 
ATOM   10740 C  CA  . ILE J  1 105 ? 114.888 36.679  3.490  1.00 37.27 ? 104  ILE J CA  1 
ATOM   10741 C  C   . ILE J  1 105 ? 114.298 37.687  2.516  1.00 37.95 ? 104  ILE J C   1 
ATOM   10742 O  O   . ILE J  1 105 ? 115.031 38.433  1.866  1.00 36.67 ? 104  ILE J O   1 
ATOM   10743 C  CB  . ILE J  1 105 ? 114.666 37.209  4.931  1.00 35.83 ? 104  ILE J CB  1 
ATOM   10744 C  CG1 . ILE J  1 105 ? 115.365 38.560  5.106  1.00 34.20 ? 104  ILE J CG1 1 
ATOM   10745 C  CG2 . ILE J  1 105 ? 115.163 36.194  5.942  1.00 35.19 ? 104  ILE J CG2 1 
ATOM   10746 C  CD1 . ILE J  1 105 ? 115.122 39.221  6.455  1.00 30.00 ? 104  ILE J CD1 1 
ATOM   10747 N  N   . SER J  1 106 ? 112.976 37.701  2.409  1.00 37.21 ? 105  SER J N   1 
ATOM   10748 C  CA  . SER J  1 106 ? 112.299 38.638  1.528  1.00 38.47 ? 105  SER J CA  1 
ATOM   10749 C  C   . SER J  1 106 ? 110.917 38.955  2.077  1.00 38.72 ? 105  SER J C   1 
ATOM   10750 O  O   . SER J  1 106 ? 110.388 38.217  2.903  1.00 39.40 ? 105  SER J O   1 
ATOM   10751 C  CB  . SER J  1 106 ? 112.170 38.053  0.120  1.00 38.60 ? 105  SER J CB  1 
ATOM   10752 O  OG  . SER J  1 106 ? 111.521 38.974  -0.745 1.00 39.29 ? 105  SER J OG  1 
ATOM   10753 N  N   . LEU J  1 107 ? 110.343 40.062  1.624  1.00 40.32 ? 106  LEU J N   1 
ATOM   10754 C  CA  . LEU J  1 107 ? 109.011 40.457  2.058  1.00 42.68 ? 106  LEU J CA  1 
ATOM   10755 C  C   . LEU J  1 107 ? 108.035 40.241  0.903  1.00 45.09 ? 106  LEU J C   1 
ATOM   10756 O  O   . LEU J  1 107 ? 106.911 40.745  0.917  1.00 46.49 ? 106  LEU J O   1 
ATOM   10757 C  CB  . LEU J  1 107 ? 109.002 41.927  2.495  1.00 41.30 ? 106  LEU J CB  1 
ATOM   10758 C  CG  . LEU J  1 107 ? 109.926 42.316  3.659  1.00 41.17 ? 106  LEU J CG  1 
ATOM   10759 C  CD1 . LEU J  1 107 ? 109.683 43.772  4.031  1.00 39.33 ? 106  LEU J CD1 1 
ATOM   10760 C  CD2 . LEU J  1 107 ? 109.670 41.414  4.867  1.00 39.02 ? 106  LEU J CD2 1 
ATOM   10761 N  N   . SER J  1 108 ? 108.480 39.482  -0.094 1.00 47.74 ? 107  SER J N   1 
ATOM   10762 C  CA  . SER J  1 108 ? 107.672 39.176  -1.269 1.00 50.90 ? 107  SER J CA  1 
ATOM   10763 C  C   . SER J  1 108 ? 108.039 37.807  -1.828 1.00 51.48 ? 107  SER J C   1 
ATOM   10764 O  O   . SER J  1 108 ? 109.151 37.323  -1.628 1.00 50.04 ? 107  SER J O   1 
ATOM   10765 C  CB  . SER J  1 108 ? 107.897 40.226  -2.362 1.00 52.78 ? 107  SER J CB  1 
ATOM   10766 O  OG  . SER J  1 108 ? 107.572 41.527  -1.908 1.00 57.51 ? 107  SER J OG  1 
ATOM   10767 N  N   . GLY J  1 109 ? 107.093 37.190  -2.528 1.00 53.14 ? 108  GLY J N   1 
ATOM   10768 C  CA  . GLY J  1 109 ? 107.336 35.894  -3.137 1.00 54.08 ? 108  GLY J CA  1 
ATOM   10769 C  C   . GLY J  1 109 ? 107.556 34.705  -2.220 1.00 54.80 ? 108  GLY J C   1 
ATOM   10770 O  O   . GLY J  1 109 ? 107.317 34.763  -1.015 1.00 54.63 ? 108  GLY J O   1 
ATOM   10771 N  N   . ASP J  1 110 ? 108.028 33.620  -2.826 1.00 56.10 ? 109  ASP J N   1 
ATOM   10772 C  CA  . ASP J  1 110 ? 108.298 32.355  -2.150 1.00 57.27 ? 109  ASP J CA  1 
ATOM   10773 C  C   . ASP J  1 110 ? 109.070 32.412  -0.834 1.00 56.13 ? 109  ASP J C   1 
ATOM   10774 O  O   . ASP J  1 110 ? 108.809 31.620  0.072  1.00 56.70 ? 109  ASP J O   1 
ATOM   10775 C  CB  . ASP J  1 110 ? 109.020 31.417  -3.122 0.00 60.34 ? 109  ASP J CB  1 
ATOM   10776 C  CG  . ASP J  1 110 ? 110.142 32.109  -3.874 1.00 63.84 ? 109  ASP J CG  1 
ATOM   10777 O  OD1 . ASP J  1 110 ? 111.210 32.349  -3.273 1.00 66.13 ? 109  ASP J OD1 1 
ATOM   10778 O  OD2 . ASP J  1 110 ? 109.950 32.426  -5.068 1.00 65.77 ? 109  ASP J OD2 1 
ATOM   10779 N  N   . HIS J  1 111 ? 110.025 33.328  -0.723 1.00 54.69 ? 110  HIS J N   1 
ATOM   10780 C  CA  . HIS J  1 111 ? 110.810 33.433  0.503  1.00 52.28 ? 110  HIS J CA  1 
ATOM   10781 C  C   . HIS J  1 111 ? 110.281 34.504  1.439  1.00 49.73 ? 110  HIS J C   1 
ATOM   10782 O  O   . HIS J  1 111 ? 110.975 34.929  2.366  1.00 48.18 ? 110  HIS J O   1 
ATOM   10783 C  CB  . HIS J  1 111 ? 112.279 33.722  0.174  1.00 54.55 ? 110  HIS J CB  1 
ATOM   10784 C  CG  . HIS J  1 111 ? 112.975 32.582  -0.491 1.00 57.09 ? 110  HIS J CG  1 
ATOM   10785 N  ND1 . HIS J  1 111 ? 114.289 32.660  -0.931 1.00 58.13 ? 110  HIS J ND1 1 
ATOM   10786 C  CD2 . HIS J  1 111 ? 112.565 31.330  -0.798 1.00 57.70 ? 110  HIS J CD2 1 
ATOM   10787 C  CE1 . HIS J  1 111 ? 114.640 31.516  -1.469 1.00 58.31 ? 110  HIS J CE1 1 
ATOM   10788 N  NE2 . HIS J  1 111 ? 113.608 30.682  -1.403 1.00 58.78 ? 110  HIS J NE2 1 
ATOM   10789 N  N   . SER J  1 112 ? 109.052 34.944  1.198  1.00 47.03 ? 111  SER J N   1 
ATOM   10790 C  CA  . SER J  1 112 ? 108.456 35.971  2.041  1.00 45.16 ? 111  SER J CA  1 
ATOM   10791 C  C   . SER J  1 112 ? 108.329 35.484  3.477  1.00 43.84 ? 111  SER J C   1 
ATOM   10792 O  O   . SER J  1 112 ? 107.984 34.327  3.727  1.00 44.07 ? 111  SER J O   1 
ATOM   10793 C  CB  . SER J  1 112 ? 107.075 36.365  1.518  1.00 43.99 ? 111  SER J CB  1 
ATOM   10794 O  OG  . SER J  1 112 ? 106.496 37.354  2.351  1.00 43.11 ? 111  SER J OG  1 
ATOM   10795 N  N   . ILE J  1 113 ? 108.629 36.369  4.419  1.00 40.96 ? 112  ILE J N   1 
ATOM   10796 C  CA  . ILE J  1 113 ? 108.526 36.036  5.830  1.00 39.40 ? 112  ILE J CA  1 
ATOM   10797 C  C   . ILE J  1 113 ? 107.277 36.698  6.405  1.00 38.17 ? 112  ILE J C   1 
ATOM   10798 O  O   . ILE J  1 113 ? 107.001 36.592  7.598  1.00 37.74 ? 112  ILE J O   1 
ATOM   10799 C  CB  . ILE J  1 113 ? 109.767 36.511  6.616  1.00 39.24 ? 112  ILE J CB  1 
ATOM   10800 C  CG1 . ILE J  1 113 ? 109.918 38.031  6.494  1.00 39.54 ? 112  ILE J CG1 1 
ATOM   10801 C  CG2 . ILE J  1 113 ? 111.009 35.788  6.099  1.00 38.53 ? 112  ILE J CG2 1 
ATOM   10802 C  CD1 . ILE J  1 113 ? 111.078 38.603  7.307  1.00 38.02 ? 112  ILE J CD1 1 
ATOM   10803 N  N   . ILE J  1 114 ? 106.530 37.391  5.548  1.00 37.12 ? 113  ILE J N   1 
ATOM   10804 C  CA  . ILE J  1 114 ? 105.298 38.040  5.974  1.00 36.93 ? 113  ILE J CA  1 
ATOM   10805 C  C   . ILE J  1 114 ? 104.354 36.927  6.419  1.00 37.25 ? 113  ILE J C   1 
ATOM   10806 O  O   . ILE J  1 114 ? 104.166 35.943  5.703  1.00 37.28 ? 113  ILE J O   1 
ATOM   10807 C  CB  . ILE J  1 114 ? 104.621 38.809  4.817  1.00 38.01 ? 113  ILE J CB  1 
ATOM   10808 C  CG1 . ILE J  1 114 ? 105.530 39.939  4.322  1.00 39.53 ? 113  ILE J CG1 1 
ATOM   10809 C  CG2 . ILE J  1 114 ? 103.286 39.377  5.286  1.00 38.23 ? 113  ILE J CG2 1 
ATOM   10810 C  CD1 . ILE J  1 114 ? 105.756 41.042  5.345  1.00 38.83 ? 113  ILE J CD1 1 
ATOM   10811 N  N   . GLY J  1 115 ? 103.771 37.075  7.603  1.00 36.29 ? 114  GLY J N   1 
ATOM   10812 C  CA  . GLY J  1 115 ? 102.859 36.059  8.092  1.00 36.45 ? 114  GLY J CA  1 
ATOM   10813 C  C   . GLY J  1 115 ? 103.566 34.964  8.861  1.00 36.19 ? 114  GLY J C   1 
ATOM   10814 O  O   . GLY J  1 115 ? 102.925 34.043  9.365  1.00 35.09 ? 114  GLY J O   1 
ATOM   10815 N  N   . ARG J  1 116 ? 104.890 35.053  8.948  1.00 34.94 ? 115  ARG J N   1 
ATOM   10816 C  CA  . ARG J  1 116 ? 105.658 34.062  9.687  1.00 34.07 ? 115  ARG J CA  1 
ATOM   10817 C  C   . ARG J  1 116 ? 106.057 34.661  11.033 1.00 32.92 ? 115  ARG J C   1 
ATOM   10818 O  O   . ARG J  1 116 ? 105.611 35.754  11.368 1.00 34.12 ? 115  ARG J O   1 
ATOM   10819 C  CB  . ARG J  1 116 ? 106.862 33.609  8.857  1.00 33.97 ? 115  ARG J CB  1 
ATOM   10820 C  CG  . ARG J  1 116 ? 106.418 33.011  7.521  1.00 36.29 ? 115  ARG J CG  1 
ATOM   10821 C  CD  . ARG J  1 116 ? 107.538 32.348  6.731  1.00 34.71 ? 115  ARG J CD  1 
ATOM   10822 N  NE  . ARG J  1 116 ? 107.075 31.917  5.412  1.00 35.44 ? 115  ARG J NE  1 
ATOM   10823 C  CZ  . ARG J  1 116 ? 106.339 30.831  5.178  1.00 35.51 ? 115  ARG J CZ  1 
ATOM   10824 N  NH1 . ARG J  1 116 ? 105.971 30.539  3.939  1.00 34.00 ? 115  ARG J NH1 1 
ATOM   10825 N  NH2 . ARG J  1 116 ? 105.990 30.024  6.172  1.00 34.70 ? 115  ARG J NH2 1 
ATOM   10826 N  N   . THR J  1 117 ? 106.880 33.962  11.808 1.00 32.51 ? 116  THR J N   1 
ATOM   10827 C  CA  . THR J  1 117 ? 107.248 34.450  13.134 1.00 30.62 ? 116  THR J CA  1 
ATOM   10828 C  C   . THR J  1 117 ? 108.718 34.802  13.356 1.00 31.82 ? 116  THR J C   1 
ATOM   10829 O  O   . THR J  1 117 ? 109.615 34.094  12.898 1.00 32.61 ? 116  THR J O   1 
ATOM   10830 C  CB  . THR J  1 117 ? 106.837 33.416  14.223 1.00 30.99 ? 116  THR J CB  1 
ATOM   10831 O  OG1 . THR J  1 117 ? 105.414 33.223  14.200 1.00 30.48 ? 116  THR J OG1 1 
ATOM   10832 C  CG2 . THR J  1 117 ? 107.249 33.893  15.606 1.00 28.19 ? 116  THR J CG2 1 
ATOM   10833 N  N   . LEU J  1 118 ? 108.951 35.900  14.072 1.00 30.49 ? 117  LEU J N   1 
ATOM   10834 C  CA  . LEU J  1 118 ? 110.307 36.334  14.406 1.00 31.19 ? 117  LEU J CA  1 
ATOM   10835 C  C   . LEU J  1 118 ? 110.540 35.907  15.849 1.00 28.97 ? 117  LEU J C   1 
ATOM   10836 O  O   . LEU J  1 118 ? 109.722 36.187  16.718 1.00 31.58 ? 117  LEU J O   1 
ATOM   10837 C  CB  . LEU J  1 118 ? 110.450 37.857  14.295 1.00 31.08 ? 117  LEU J CB  1 
ATOM   10838 C  CG  . LEU J  1 118 ? 111.829 38.386  14.716 1.00 30.98 ? 117  LEU J CG  1 
ATOM   10839 C  CD1 . LEU J  1 118 ? 112.897 37.824  13.776 1.00 30.53 ? 117  LEU J CD1 1 
ATOM   10840 C  CD2 . LEU J  1 118 ? 111.840 39.909  14.688 1.00 30.27 ? 117  LEU J CD2 1 
ATOM   10841 N  N   . VAL J  1 119 ? 111.653 35.237  16.113 1.00 28.26 ? 118  VAL J N   1 
ATOM   10842 C  CA  . VAL J  1 119 ? 111.934 34.769  17.464 1.00 28.72 ? 118  VAL J CA  1 
ATOM   10843 C  C   . VAL J  1 119 ? 113.304 35.155  18.002 1.00 29.27 ? 118  VAL J C   1 
ATOM   10844 O  O   . VAL J  1 119 ? 114.303 35.102  17.283 1.00 29.54 ? 118  VAL J O   1 
ATOM   10845 C  CB  . VAL J  1 119 ? 111.828 33.222  17.541 1.00 29.91 ? 118  VAL J CB  1 
ATOM   10846 C  CG1 . VAL J  1 119 ? 112.132 32.744  18.954 1.00 29.73 ? 118  VAL J CG1 1 
ATOM   10847 C  CG2 . VAL J  1 119 ? 110.442 32.772  17.111 1.00 30.16 ? 118  VAL J CG2 1 
ATOM   10848 N  N   . VAL J  1 120 ? 113.345 35.557  19.267 1.00 28.90 ? 119  VAL J N   1 
ATOM   10849 C  CA  . VAL J  1 120 ? 114.611 35.881  19.907 1.00 30.99 ? 119  VAL J CA  1 
ATOM   10850 C  C   . VAL J  1 120 ? 114.795 34.798  20.968 1.00 33.07 ? 119  VAL J C   1 
ATOM   10851 O  O   . VAL J  1 120 ? 113.939 34.606  21.838 1.00 32.65 ? 119  VAL J O   1 
ATOM   10852 C  CB  . VAL J  1 120 ? 114.613 37.297  20.543 1.00 30.41 ? 119  VAL J CB  1 
ATOM   10853 C  CG1 . VAL J  1 120 ? 113.540 37.419  21.610 1.00 30.95 ? 119  VAL J CG1 1 
ATOM   10854 C  CG2 . VAL J  1 120 ? 115.990 37.588  21.123 1.00 31.69 ? 119  VAL J CG2 1 
ATOM   10855 N  N   . HIS J  1 121 ? 115.913 34.083  20.877 1.00 33.52 ? 120  HIS J N   1 
ATOM   10856 C  CA  . HIS J  1 121 ? 116.213 32.968  21.769 1.00 32.48 ? 120  HIS J CA  1 
ATOM   10857 C  C   . HIS J  1 121 ? 116.920 33.223  23.086 1.00 34.51 ? 120  HIS J C   1 
ATOM   10858 O  O   . HIS J  1 121 ? 117.491 34.287  23.332 1.00 34.81 ? 120  HIS J O   1 
ATOM   10859 C  CB  . HIS J  1 121 ? 117.010 31.918  21.006 1.00 29.51 ? 120  HIS J CB  1 
ATOM   10860 C  CG  . HIS J  1 121 ? 116.234 31.246  19.925 1.00 27.57 ? 120  HIS J CG  1 
ATOM   10861 N  ND1 . HIS J  1 121 ? 115.515 30.091  20.137 1.00 26.97 ? 120  HIS J ND1 1 
ATOM   10862 C  CD2 . HIS J  1 121 ? 116.044 31.574  18.624 1.00 30.49 ? 120  HIS J CD2 1 
ATOM   10863 C  CE1 . HIS J  1 121 ? 114.916 29.736  19.011 1.00 31.18 ? 120  HIS J CE1 1 
ATOM   10864 N  NE2 . HIS J  1 121 ? 115.221 30.620  18.081 1.00 23.32 ? 120  HIS J NE2 1 
ATOM   10865 N  N   . GLU J  1 122 ? 116.879 32.181  23.913 1.00 37.25 ? 121  GLU J N   1 
ATOM   10866 C  CA  . GLU J  1 122 ? 117.480 32.146  25.237 1.00 39.13 ? 121  GLU J CA  1 
ATOM   10867 C  C   . GLU J  1 122 ? 119.003 32.202  25.170 1.00 39.11 ? 121  GLU J C   1 
ATOM   10868 O  O   . GLU J  1 122 ? 119.642 32.925  25.935 1.00 38.41 ? 121  GLU J O   1 
ATOM   10869 C  CB  . GLU J  1 122 ? 117.052 30.854  25.939 1.00 40.59 ? 121  GLU J CB  1 
ATOM   10870 C  CG  . GLU J  1 122 ? 117.802 30.545  27.223 1.00 45.71 ? 121  GLU J CG  1 
ATOM   10871 C  CD  . GLU J  1 122 ? 117.770 29.063  27.574 1.00 48.52 ? 121  GLU J CD  1 
ATOM   10872 O  OE1 . GLU J  1 122 ? 118.342 28.690  28.619 1.00 50.57 ? 121  GLU J OE1 1 
ATOM   10873 O  OE2 . GLU J  1 122 ? 117.182 28.271  26.804 1.00 48.88 ? 121  GLU J OE2 1 
ATOM   10874 N  N   . LYS J  1 123 ? 119.579 31.431  24.253 1.00 38.82 ? 122  LYS J N   1 
ATOM   10875 C  CA  . LYS J  1 123 ? 121.030 31.376  24.114 1.00 39.44 ? 122  LYS J CA  1 
ATOM   10876 C  C   . LYS J  1 123 ? 121.538 31.829  22.750 1.00 36.66 ? 122  LYS J C   1 
ATOM   10877 O  O   . LYS J  1 123 ? 120.760 32.163  21.856 1.00 35.20 ? 122  LYS J O   1 
ATOM   10878 C  CB  . LYS J  1 123 ? 121.518 29.950  24.391 1.00 40.98 ? 122  LYS J CB  1 
ATOM   10879 C  CG  . LYS J  1 123 ? 121.164 29.444  25.784 1.00 45.64 ? 122  LYS J CG  1 
ATOM   10880 C  CD  . LYS J  1 123 ? 121.668 28.028  26.028 1.00 48.50 ? 122  LYS J CD  1 
ATOM   10881 C  CE  . LYS J  1 123 ? 120.963 27.017  25.138 1.00 50.58 ? 122  LYS J CE  1 
ATOM   10882 N  NZ  . LYS J  1 123 ? 121.406 25.621  25.425 1.00 53.28 ? 122  LYS J NZ  1 
ATOM   10883 N  N   . ALA J  1 124 ? 122.858 31.830  22.603 1.00 34.86 ? 123  ALA J N   1 
ATOM   10884 C  CA  . ALA J  1 124 ? 123.491 32.231  21.357 1.00 33.70 ? 123  ALA J CA  1 
ATOM   10885 C  C   . ALA J  1 124 ? 123.319 31.168  20.285 1.00 32.44 ? 123  ALA J C   1 
ATOM   10886 O  O   . ALA J  1 124 ? 123.248 29.977  20.583 1.00 33.30 ? 123  ALA J O   1 
ATOM   10887 C  CB  . ALA J  1 124 ? 124.976 32.488  21.591 1.00 33.74 ? 123  ALA J CB  1 
ATOM   10888 N  N   . ASP J  1 125 ? 123.226 31.612  19.038 1.00 29.84 ? 124  ASP J N   1 
ATOM   10889 C  CA  . ASP J  1 125 ? 123.117 30.713  17.895 1.00 28.76 ? 124  ASP J CA  1 
ATOM   10890 C  C   . ASP J  1 125 ? 124.580 30.438  17.530 1.00 29.70 ? 124  ASP J C   1 
ATOM   10891 O  O   . ASP J  1 125 ? 125.355 31.382  17.347 1.00 29.01 ? 124  ASP J O   1 
ATOM   10892 C  CB  . ASP J  1 125 ? 122.385 31.436  16.755 1.00 26.68 ? 124  ASP J CB  1 
ATOM   10893 C  CG  . ASP J  1 125 ? 122.286 30.608  15.487 1.00 25.87 ? 124  ASP J CG  1 
ATOM   10894 O  OD1 . ASP J  1 125 ? 121.452 30.952  14.625 1.00 26.00 ? 124  ASP J OD1 1 
ATOM   10895 O  OD2 . ASP J  1 125 ? 123.044 29.629  15.332 1.00 27.11 ? 124  ASP J OD2 1 
ATOM   10896 N  N   . ASP J  1 126 ? 124.974 29.167  17.446 1.00 28.10 ? 125  ASP J N   1 
ATOM   10897 C  CA  . ASP J  1 126 ? 126.370 28.854  17.124 1.00 27.78 ? 125  ASP J CA  1 
ATOM   10898 C  C   . ASP J  1 126 ? 126.658 28.851  15.625 1.00 27.53 ? 125  ASP J C   1 
ATOM   10899 O  O   . ASP J  1 126 ? 127.721 28.421  15.183 1.00 27.65 ? 125  ASP J O   1 
ATOM   10900 C  CB  . ASP J  1 126 ? 126.799 27.521  17.780 1.00 28.48 ? 125  ASP J CB  1 
ATOM   10901 C  CG  . ASP J  1 126 ? 126.142 26.294  17.156 1.00 30.33 ? 125  ASP J CG  1 
ATOM   10902 O  OD1 . ASP J  1 126 ? 126.184 25.221  17.803 1.00 30.80 ? 125  ASP J OD1 1 
ATOM   10903 O  OD2 . ASP J  1 126 ? 125.607 26.380  16.027 1.00 29.96 ? 125  ASP J OD2 1 
ATOM   10904 N  N   . LEU J  1 127 ? 125.695 29.332  14.850 1.00 26.35 ? 126  LEU J N   1 
ATOM   10905 C  CA  . LEU J  1 127 ? 125.836 29.438  13.399 1.00 27.99 ? 126  LEU J CA  1 
ATOM   10906 C  C   . LEU J  1 127 ? 126.192 28.126  12.690 1.00 27.62 ? 126  LEU J C   1 
ATOM   10907 O  O   . LEU J  1 127 ? 126.792 28.139  11.612 1.00 24.97 ? 126  LEU J O   1 
ATOM   10908 C  CB  . LEU J  1 127 ? 126.886 30.514  13.068 1.00 26.65 ? 126  LEU J CB  1 
ATOM   10909 C  CG  . LEU J  1 127 ? 126.794 31.788  13.918 1.00 28.35 ? 126  LEU J CG  1 
ATOM   10910 C  CD1 . LEU J  1 127 ? 127.880 32.780  13.501 1.00 29.73 ? 126  LEU J CD1 1 
ATOM   10911 C  CD2 . LEU J  1 127 ? 125.406 32.412  13.759 1.00 27.18 ? 126  LEU J CD2 1 
ATOM   10912 N  N   . GLY J  1 128 ? 125.817 26.999  13.293 1.00 27.88 ? 127  GLY J N   1 
ATOM   10913 C  CA  . GLY J  1 128 ? 126.086 25.707  12.682 1.00 25.85 ? 127  GLY J CA  1 
ATOM   10914 C  C   . GLY J  1 128 ? 127.495 25.168  12.856 1.00 26.41 ? 127  GLY J C   1 
ATOM   10915 O  O   . GLY J  1 128 ? 127.896 24.229  12.169 1.00 24.71 ? 127  GLY J O   1 
ATOM   10916 N  N   . LYS J  1 129 ? 128.244 25.741  13.788 1.00 24.80 ? 128  LYS J N   1 
ATOM   10917 C  CA  . LYS J  1 129 ? 129.618 25.309  14.023 1.00 27.56 ? 128  LYS J CA  1 
ATOM   10918 C  C   . LYS J  1 129 ? 129.756 24.545  15.339 1.00 26.91 ? 128  LYS J C   1 
ATOM   10919 O  O   . LYS J  1 129 ? 130.863 24.375  15.857 1.00 27.24 ? 128  LYS J O   1 
ATOM   10920 C  CB  . LYS J  1 129 ? 130.534 26.540  14.020 1.00 27.18 ? 128  LYS J CB  1 
ATOM   10921 C  CG  . LYS J  1 129 ? 130.413 27.360  12.730 1.00 29.63 ? 128  LYS J CG  1 
ATOM   10922 C  CD  . LYS J  1 129 ? 131.174 28.679  12.807 1.00 33.11 ? 128  LYS J CD  1 
ATOM   10923 C  CE  . LYS J  1 129 ? 132.676 28.469  12.826 1.00 34.08 ? 128  LYS J CE  1 
ATOM   10924 N  NZ  . LYS J  1 129 ? 133.395 29.770  12.947 1.00 37.58 ? 128  LYS J NZ  1 
ATOM   10925 N  N   . GLY J  1 130 ? 128.626 24.079  15.862 1.00 25.55 ? 129  GLY J N   1 
ATOM   10926 C  CA  . GLY J  1 130 ? 128.619 23.356  17.126 1.00 25.60 ? 129  GLY J CA  1 
ATOM   10927 C  C   . GLY J  1 130 ? 129.141 21.932  17.104 1.00 23.79 ? 129  GLY J C   1 
ATOM   10928 O  O   . GLY J  1 130 ? 129.497 21.389  18.152 1.00 25.14 ? 129  GLY J O   1 
ATOM   10929 N  N   . GLY J  1 131 ? 129.183 21.317  15.926 1.00 24.16 ? 130  GLY J N   1 
ATOM   10930 C  CA  . GLY J  1 131 ? 129.682 19.953  15.828 1.00 25.60 ? 130  GLY J CA  1 
ATOM   10931 C  C   . GLY J  1 131 ? 128.702 18.855  16.223 1.00 27.81 ? 130  GLY J C   1 
ATOM   10932 O  O   . GLY J  1 131 ? 129.038 17.675  16.155 1.00 28.23 ? 130  GLY J O   1 
ATOM   10933 N  N   . ASN J  1 132 ? 127.500 19.222  16.654 1.00 28.84 ? 131  ASN J N   1 
ATOM   10934 C  CA  . ASN J  1 132 ? 126.510 18.212  17.026 1.00 30.97 ? 131  ASN J CA  1 
ATOM   10935 C  C   . ASN J  1 132 ? 125.317 18.336  16.088 1.00 30.85 ? 131  ASN J C   1 
ATOM   10936 O  O   . ASN J  1 132 ? 125.194 19.320  15.358 1.00 30.90 ? 131  ASN J O   1 
ATOM   10937 C  CB  . ASN J  1 132 ? 126.080 18.366  18.500 1.00 29.97 ? 131  ASN J CB  1 
ATOM   10938 C  CG  . ASN J  1 132 ? 125.335 19.661  18.774 1.00 31.83 ? 131  ASN J CG  1 
ATOM   10939 O  OD1 . ASN J  1 132 ? 125.293 20.560  17.935 1.00 32.29 ? 131  ASN J OD1 1 
ATOM   10940 N  ND2 . ASN J  1 132 ? 124.750 19.766  19.969 1.00 30.57 ? 131  ASN J ND2 1 
ATOM   10941 N  N   . GLU J  1 133 ? 124.445 17.335  16.093 1.00 31.74 ? 132  GLU J N   1 
ATOM   10942 C  CA  . GLU J  1 133 ? 123.282 17.341  15.210 1.00 32.85 ? 132  GLU J CA  1 
ATOM   10943 C  C   . GLU J  1 133 ? 122.412 18.585  15.380 1.00 31.31 ? 132  GLU J C   1 
ATOM   10944 O  O   . GLU J  1 133 ? 121.935 19.153  14.398 1.00 29.79 ? 132  GLU J O   1 
ATOM   10945 C  CB  . GLU J  1 133 ? 122.431 16.092  15.450 1.00 37.04 ? 132  GLU J CB  1 
ATOM   10946 C  CG  . GLU J  1 133 ? 121.266 15.946  14.490 0.00 43.81 ? 132  GLU J CG  1 
ATOM   10947 C  CD  . GLU J  1 133 ? 120.303 14.858  14.914 1.00 49.86 ? 132  GLU J CD  1 
ATOM   10948 O  OE1 . GLU J  1 133 ? 119.475 14.435  14.070 1.00 53.18 ? 132  GLU J OE1 1 
ATOM   10949 O  OE2 . GLU J  1 133 ? 120.369 14.436  16.095 1.00 52.17 ? 132  GLU J OE2 1 
ATOM   10950 N  N   . GLU J  1 134 ? 122.210 19.004  16.626 1.00 30.58 ? 133  GLU J N   1 
ATOM   10951 C  CA  . GLU J  1 134 ? 121.385 20.169  16.922 1.00 32.52 ? 133  GLU J CA  1 
ATOM   10952 C  C   . GLU J  1 134 ? 121.921 21.450  16.262 1.00 31.85 ? 133  GLU J C   1 
ATOM   10953 O  O   . GLU J  1 134 ? 121.148 22.285  15.783 1.00 29.52 ? 133  GLU J O   1 
ATOM   10954 C  CB  . GLU J  1 134 ? 121.289 20.360  18.441 1.00 34.80 ? 133  GLU J CB  1 
ATOM   10955 C  CG  . GLU J  1 134 ? 120.271 21.403  18.865 1.00 42.68 ? 133  GLU J CG  1 
ATOM   10956 C  CD  . GLU J  1 134 ? 118.843 21.003  18.527 1.00 46.65 ? 133  GLU J CD  1 
ATOM   10957 O  OE1 . GLU J  1 134 ? 117.982 21.901  18.430 1.00 49.46 ? 133  GLU J OE1 1 
ATOM   10958 O  OE2 . GLU J  1 134 ? 118.578 19.791  18.369 1.00 48.97 ? 133  GLU J OE2 1 
ATOM   10959 N  N   . SER J  1 135 ? 123.244 21.593  16.229 1.00 30.01 ? 134  SER J N   1 
ATOM   10960 C  CA  . SER J  1 135 ? 123.865 22.773  15.636 1.00 29.45 ? 134  SER J CA  1 
ATOM   10961 C  C   . SER J  1 135 ? 123.399 23.003  14.203 1.00 31.07 ? 134  SER J C   1 
ATOM   10962 O  O   . SER J  1 135 ? 123.226 24.145  13.772 1.00 30.89 ? 134  SER J O   1 
ATOM   10963 C  CB  . SER J  1 135 ? 125.389 22.633  15.653 1.00 29.42 ? 134  SER J CB  1 
ATOM   10964 O  OG  . SER J  1 135 ? 126.002 23.762  15.055 1.00 29.01 ? 134  SER J OG  1 
ATOM   10965 N  N   . THR J  1 136 ? 123.191 21.911  13.472 1.00 32.03 ? 135  THR J N   1 
ATOM   10966 C  CA  . THR J  1 136 ? 122.762 21.982  12.080 1.00 34.24 ? 135  THR J CA  1 
ATOM   10967 C  C   . THR J  1 136 ? 121.254 22.158  11.910 1.00 33.69 ? 135  THR J C   1 
ATOM   10968 O  O   . THR J  1 136 ? 120.746 22.135  10.786 1.00 33.31 ? 135  THR J O   1 
ATOM   10969 C  CB  . THR J  1 136 ? 123.177 20.716  11.308 1.00 37.39 ? 135  THR J CB  1 
ATOM   10970 O  OG1 . THR J  1 136 ? 122.410 19.601  11.776 1.00 40.96 ? 135  THR J OG1 1 
ATOM   10971 C  CG2 . THR J  1 136 ? 124.652 20.427  11.525 1.00 38.61 ? 135  THR J CG2 1 
ATOM   10972 N  N   . LYS J  1 137 ? 120.538 22.326  13.016 1.00 33.09 ? 136  LYS J N   1 
ATOM   10973 C  CA  . LYS J  1 137 ? 119.092 22.510  12.943 1.00 33.73 ? 136  LYS J CA  1 
ATOM   10974 C  C   . LYS J  1 137 ? 118.656 23.825  13.588 1.00 32.86 ? 136  LYS J C   1 
ATOM   10975 O  O   . LYS J  1 137 ? 117.890 24.592  12.998 1.00 32.65 ? 136  LYS J O   1 
ATOM   10976 C  CB  . LYS J  1 137 ? 118.367 21.354  13.638 1.00 36.15 ? 136  LYS J CB  1 
ATOM   10977 C  CG  . LYS J  1 137 ? 118.762 19.966  13.157 1.00 40.83 ? 136  LYS J CG  1 
ATOM   10978 C  CD  . LYS J  1 137 ? 118.138 18.904  14.047 1.00 43.11 ? 136  LYS J CD  1 
ATOM   10979 C  CE  . LYS J  1 137 ? 118.643 17.519  13.715 0.00 44.10 ? 136  LYS J CE  1 
ATOM   10980 N  NZ  . LYS J  1 137 ? 118.123 16.528  14.695 1.00 46.80 ? 136  LYS J NZ  1 
ATOM   10981 N  N   . THR J  1 138 ? 119.154 24.085  14.796 1.00 31.34 ? 137  THR J N   1 
ATOM   10982 C  CA  . THR J  1 138 ? 118.782 25.292  15.527 1.00 32.17 ? 137  THR J CA  1 
ATOM   10983 C  C   . THR J  1 138 ? 119.954 26.150  15.999 1.00 31.96 ? 137  THR J C   1 
ATOM   10984 O  O   . THR J  1 138 ? 119.743 27.204  16.595 1.00 31.45 ? 137  THR J O   1 
ATOM   10985 C  CB  . THR J  1 138 ? 117.985 24.939  16.777 1.00 32.38 ? 137  THR J CB  1 
ATOM   10986 O  OG1 . THR J  1 138 ? 118.873 24.352  17.739 1.00 33.29 ? 137  THR J OG1 1 
ATOM   10987 C  CG2 . THR J  1 138 ? 116.863 23.955  16.439 1.00 30.56 ? 137  THR J CG2 1 
ATOM   10988 N  N   . GLY J  1 139 ? 121.180 25.700  15.752 1.00 32.16 ? 138  GLY J N   1 
ATOM   10989 C  CA  . GLY J  1 139 ? 122.332 26.460  16.200 1.00 31.99 ? 138  GLY J CA  1 
ATOM   10990 C  C   . GLY J  1 139 ? 122.483 26.376  17.710 1.00 32.65 ? 138  GLY J C   1 
ATOM   10991 O  O   . GLY J  1 139 ? 123.289 27.093  18.300 1.00 32.82 ? 138  GLY J O   1 
ATOM   10992 N  N   . ASN J  1 140 ? 121.709 25.491  18.339 1.00 32.39 ? 139  ASN J N   1 
ATOM   10993 C  CA  . ASN J  1 140 ? 121.756 25.313  19.794 1.00 31.26 ? 139  ASN J CA  1 
ATOM   10994 C  C   . ASN J  1 140 ? 121.352 26.593  20.527 1.00 31.17 ? 139  ASN J C   1 
ATOM   10995 O  O   . ASN J  1 140 ? 121.825 26.857  21.631 1.00 30.92 ? 139  ASN J O   1 
ATOM   10996 C  CB  . ASN J  1 140 ? 123.167 24.890  20.233 1.00 30.77 ? 139  ASN J CB  1 
ATOM   10997 C  CG  . ASN J  1 140 ? 123.508 23.457  19.832 1.00 32.70 ? 139  ASN J CG  1 
ATOM   10998 O  OD1 . ASN J  1 140 ? 122.959 22.502  20.382 1.00 31.97 ? 139  ASN J OD1 1 
ATOM   10999 N  ND2 . ASN J  1 140 ? 124.413 23.305  18.869 1.00 29.23 ? 139  ASN J ND2 1 
ATOM   11000 N  N   . ALA J  1 141 ? 120.458 27.372  19.920 1.00 30.72 ? 140  ALA J N   1 
ATOM   11001 C  CA  . ALA J  1 141 ? 120.013 28.636  20.511 1.00 33.36 ? 140  ALA J CA  1 
ATOM   11002 C  C   . ALA J  1 141 ? 119.152 28.490  21.763 1.00 35.48 ? 140  ALA J C   1 
ATOM   11003 O  O   . ALA J  1 141 ? 118.930 29.459  22.486 1.00 36.20 ? 140  ALA J O   1 
ATOM   11004 C  CB  . ALA J  1 141 ? 119.269 29.464  19.465 1.00 31.73 ? 140  ALA J CB  1 
ATOM   11005 N  N   . GLY J  1 142 ? 118.653 27.287  22.017 1.00 36.64 ? 141  GLY J N   1 
ATOM   11006 C  CA  . GLY J  1 142 ? 117.839 27.087  23.202 1.00 37.80 ? 141  GLY J CA  1 
ATOM   11007 C  C   . GLY J  1 142 ? 116.376 27.463  23.044 1.00 38.27 ? 141  GLY J C   1 
ATOM   11008 O  O   . GLY J  1 142 ? 115.830 27.421  21.939 1.00 36.83 ? 141  GLY J O   1 
ATOM   11009 N  N   . SER J  1 143 ? 115.748 27.851  24.151 1.00 37.78 ? 142  SER J N   1 
ATOM   11010 C  CA  . SER J  1 143 ? 114.328 28.195  24.155 1.00 39.75 ? 142  SER J CA  1 
ATOM   11011 C  C   . SER J  1 143 ? 113.968 29.515  23.484 1.00 40.45 ? 142  SER J C   1 
ATOM   11012 O  O   . SER J  1 143 ? 114.831 30.337  23.172 1.00 41.45 ? 142  SER J O   1 
ATOM   11013 C  CB  . SER J  1 143 ? 113.789 28.195  25.589 1.00 39.94 ? 142  SER J CB  1 
ATOM   11014 O  OG  . SER J  1 143 ? 114.363 29.240  26.353 1.00 40.26 ? 142  SER J OG  1 
ATOM   11015 N  N   . ARG J  1 144 ? 112.668 29.706  23.286 1.00 39.46 ? 143  ARG J N   1 
ATOM   11016 C  CA  . ARG J  1 144 ? 112.132 30.892  22.643 1.00 39.14 ? 143  ARG J CA  1 
ATOM   11017 C  C   . ARG J  1 144 ? 111.621 31.876  23.697 1.00 40.61 ? 143  ARG J C   1 
ATOM   11018 O  O   . ARG J  1 144 ? 110.527 31.706  24.241 1.00 41.46 ? 143  ARG J O   1 
ATOM   11019 C  CB  . ARG J  1 144 ? 111.012 30.457  21.694 1.00 37.33 ? 143  ARG J CB  1 
ATOM   11020 C  CG  . ARG J  1 144 ? 111.415 29.227  20.884 1.00 36.47 ? 143  ARG J CG  1 
ATOM   11021 C  CD  . ARG J  1 144 ? 110.366 28.763  19.883 1.00 38.12 ? 143  ARG J CD  1 
ATOM   11022 N  NE  . ARG J  1 144 ? 110.874 27.641  19.094 1.00 34.99 ? 143  ARG J NE  1 
ATOM   11023 C  CZ  . ARG J  1 144 ? 110.255 27.106  18.044 1.00 35.22 ? 143  ARG J CZ  1 
ATOM   11024 N  NH1 . ARG J  1 144 ? 110.810 26.089  17.396 1.00 31.87 ? 143  ARG J NH1 1 
ATOM   11025 N  NH2 . ARG J  1 144 ? 109.087 27.585  17.640 1.00 33.57 ? 143  ARG J NH2 1 
ATOM   11026 N  N   . LEU J  1 145 ? 112.420 32.905  23.975 1.00 39.41 ? 144  LEU J N   1 
ATOM   11027 C  CA  . LEU J  1 145 ? 112.081 33.911  24.979 1.00 39.41 ? 144  LEU J CA  1 
ATOM   11028 C  C   . LEU J  1 145 ? 110.951 34.857  24.587 1.00 39.71 ? 144  LEU J C   1 
ATOM   11029 O  O   . LEU J  1 145 ? 110.134 35.246  25.425 1.00 39.39 ? 144  LEU J O   1 
ATOM   11030 C  CB  . LEU J  1 145 ? 113.321 34.736  25.332 1.00 39.22 ? 144  LEU J CB  1 
ATOM   11031 C  CG  . LEU J  1 145 ? 114.536 33.963  25.851 1.00 41.22 ? 144  LEU J CG  1 
ATOM   11032 C  CD1 . LEU J  1 145 ? 115.649 34.943  26.182 1.00 42.29 ? 144  LEU J CD1 1 
ATOM   11033 C  CD2 . LEU J  1 145 ? 114.154 33.158  27.084 1.00 41.88 ? 144  LEU J CD2 1 
ATOM   11034 N  N   . ALA J  1 146 ? 110.912 35.244  23.320 1.00 38.22 ? 145  ALA J N   1 
ATOM   11035 C  CA  . ALA J  1 146 ? 109.874 36.145  22.848 1.00 37.54 ? 145  ALA J CA  1 
ATOM   11036 C  C   . ALA J  1 146 ? 109.752 35.983  21.348 1.00 37.58 ? 145  ALA J C   1 
ATOM   11037 O  O   . ALA J  1 146 ? 110.726 35.648  20.670 1.00 38.11 ? 145  ALA J O   1 
ATOM   11038 C  CB  . ALA J  1 146 ? 110.225 37.587  23.199 1.00 38.33 ? 145  ALA J CB  1 
ATOM   11039 N  N   . CYS J  1 147 ? 108.551 36.215  20.833 1.00 34.83 ? 146  CYS J N   1 
ATOM   11040 C  CA  . CYS J  1 147 ? 108.299 36.087  19.409 1.00 34.33 ? 146  CYS J CA  1 
ATOM   11041 C  C   . CYS J  1 147 ? 107.144 36.981  19.007 1.00 32.31 ? 146  CYS J C   1 
ATOM   11042 O  O   . CYS J  1 147 ? 106.452 37.540  19.853 1.00 32.31 ? 146  CYS J O   1 
ATOM   11043 C  CB  . CYS J  1 147 ? 107.969 34.634  19.059 1.00 37.10 ? 146  CYS J CB  1 
ATOM   11044 S  SG  . CYS J  1 147 ? 106.544 33.964  19.982 1.00 39.15 ? 146  CYS J SG  1 
ATOM   11045 N  N   . GLY J  1 148 ? 106.944 37.116  17.704 1.00 32.49 ? 147  GLY J N   1 
ATOM   11046 C  CA  . GLY J  1 148 ? 105.862 37.939  17.211 1.00 32.55 ? 147  GLY J CA  1 
ATOM   11047 C  C   . GLY J  1 148 ? 105.651 37.643  15.749 1.00 33.15 ? 147  GLY J C   1 
ATOM   11048 O  O   . GLY J  1 148 ? 106.606 37.314  15.041 1.00 33.56 ? 147  GLY J O   1 
ATOM   11049 N  N   . VAL J  1 149 ? 104.407 37.742  15.295 1.00 32.91 ? 148  VAL J N   1 
ATOM   11050 C  CA  . VAL J  1 149 ? 104.097 37.492  13.898 1.00 33.38 ? 148  VAL J CA  1 
ATOM   11051 C  C   . VAL J  1 149 ? 104.570 38.680  13.069 1.00 34.43 ? 148  VAL J C   1 
ATOM   11052 O  O   . VAL J  1 149 ? 104.377 39.838  13.453 1.00 35.06 ? 148  VAL J O   1 
ATOM   11053 C  CB  . VAL J  1 149 ? 102.584 37.306  13.680 1.00 33.84 ? 148  VAL J CB  1 
ATOM   11054 C  CG1 . VAL J  1 149 ? 102.312 36.956  12.225 1.00 33.17 ? 148  VAL J CG1 1 
ATOM   11055 C  CG2 . VAL J  1 149 ? 102.053 36.219  14.607 1.00 33.90 ? 148  VAL J CG2 1 
ATOM   11056 N  N   . ILE J  1 150 ? 105.200 38.390  11.938 1.00 34.06 ? 149  ILE J N   1 
ATOM   11057 C  CA  . ILE J  1 150 ? 105.698 39.435  11.060 1.00 34.48 ? 149  ILE J CA  1 
ATOM   11058 C  C   . ILE J  1 150 ? 104.544 39.936  10.209 1.00 35.93 ? 149  ILE J C   1 
ATOM   11059 O  O   . ILE J  1 150 ? 104.069 39.229  9.314  1.00 35.99 ? 149  ILE J O   1 
ATOM   11060 C  CB  . ILE J  1 150 ? 106.819 38.899  10.154 1.00 34.05 ? 149  ILE J CB  1 
ATOM   11061 C  CG1 . ILE J  1 150 ? 107.981 38.409  11.024 1.00 33.95 ? 149  ILE J CG1 1 
ATOM   11062 C  CG2 . ILE J  1 150 ? 107.266 39.978  9.180  1.00 33.94 ? 149  ILE J CG2 1 
ATOM   11063 C  CD1 . ILE J  1 150 ? 109.061 37.673  10.266 1.00 33.20 ? 149  ILE J CD1 1 
ATOM   11064 N  N   . GLY J  1 151 ? 104.094 41.156  10.496 1.00 35.65 ? 150  GLY J N   1 
ATOM   11065 C  CA  . GLY J  1 151 ? 102.981 41.724  9.758  1.00 36.47 ? 150  GLY J CA  1 
ATOM   11066 C  C   . GLY J  1 151 ? 103.325 42.851  8.805  1.00 38.07 ? 150  GLY J C   1 
ATOM   11067 O  O   . GLY J  1 151 ? 104.361 43.512  8.931  1.00 37.44 ? 150  GLY J O   1 
ATOM   11068 N  N   . ILE J  1 152 ? 102.440 43.066  7.839  1.00 37.45 ? 151  ILE J N   1 
ATOM   11069 C  CA  . ILE J  1 152 ? 102.616 44.116  6.848  1.00 37.51 ? 151  ILE J CA  1 
ATOM   11070 C  C   . ILE J  1 152 ? 102.516 45.468  7.546  1.00 37.74 ? 151  ILE J C   1 
ATOM   11071 O  O   . ILE J  1 152 ? 101.625 45.677  8.368  1.00 37.27 ? 151  ILE J O   1 
ATOM   11072 C  CB  . ILE J  1 152 ? 101.532 44.011  5.762  1.00 36.71 ? 151  ILE J CB  1 
ATOM   11073 C  CG1 . ILE J  1 152 ? 101.678 42.680  5.023  1.00 35.66 ? 151  ILE J CG1 1 
ATOM   11074 C  CG2 . ILE J  1 152 ? 101.633 45.188  4.800  1.00 38.84 ? 151  ILE J CG2 1 
ATOM   11075 C  CD1 . ILE J  1 152 ? 100.585 42.417  3.998  1.00 33.14 ? 151  ILE J CD1 1 
ATOM   11076 N  N   . ALA J  1 153 ? 103.441 46.376  7.236  1.00 38.53 ? 152  ALA J N   1 
ATOM   11077 C  CA  . ALA J  1 153 ? 103.444 47.705  7.849  1.00 38.90 ? 152  ALA J CA  1 
ATOM   11078 C  C   . ALA J  1 153 ? 103.229 48.787  6.796  1.00 39.98 ? 152  ALA J C   1 
ATOM   11079 O  O   . ALA J  1 153 ? 103.484 48.573  5.609  1.00 38.51 ? 152  ALA J O   1 
ATOM   11080 C  CB  . ALA J  1 153 ? 104.759 47.947  8.578  1.00 39.49 ? 152  ALA J CB  1 
ATOM   11081 N  N   . GLN J  1 154 ? 102.762 49.952  7.232  1.00 41.70 ? 153  GLN J N   1 
ATOM   11082 C  CA  . GLN J  1 154 ? 102.518 51.044  6.300  1.00 44.52 ? 153  GLN J CA  1 
ATOM   11083 C  C   . GLN J  1 154 ? 103.842 51.632  5.817  1.00 44.75 ? 153  GLN J C   1 
ATOM   11084 O  O   . GLN J  1 154 ? 104.765 51.781  6.653  1.00 44.82 ? 153  GLN J O   1 
ATOM   11085 C  CB  . GLN J  1 154 ? 101.684 52.141  6.965  1.00 45.69 ? 153  GLN J CB  1 
ATOM   11086 C  CG  . GLN J  1 154 ? 101.096 53.135  5.974  1.00 49.36 ? 153  GLN J CG  1 
ATOM   11087 C  CD  . GLN J  1 154 ? 100.215 54.178  6.637  1.00 50.97 ? 153  GLN J CD  1 
ATOM   11088 O  OE1 . GLN J  1 154 ? 99.345  54.768  5.992  1.00 52.06 ? 153  GLN J OE1 1 
ATOM   11089 N  NE2 . GLN J  1 154 ? 100.443 54.419  7.925  1.00 50.13 ? 153  GLN J NE2 1 
ATOM   11090 O  OXT . GLN J  1 154 ? 103.932 51.939  4.609  1.00 44.23 ? 153  GLN J OXT 1 
HETATM 11091 CU CU  . CU1 K  2 .   ? 62.768  46.471  18.906 1.00 33.35 ? 154  CU1 A CU  1 
HETATM 11092 ZN ZN  . ZN  L  3 .   ? 62.650  49.559  13.021 1.00 33.10 ? 155  ZN  A ZN  1 
HETATM 11093 CU CU  . CU1 M  2 .   ? 62.340  14.438  21.073 1.00 26.77 ? 154  CU1 B CU  1 
HETATM 11094 ZN ZN  . ZN  N  3 .   ? 61.307  10.533  15.696 1.00 22.55 ? 155  ZN  B ZN  1 
HETATM 11095 CU CU  . CU1 O  2 .   ? 118.864 -13.885 18.811 1.00 42.27 ? 154  CU1 C CU  1 
HETATM 11096 ZN ZN  . ZN  P  3 .   ? 121.812 -15.151 12.971 1.00 41.41 ? 155  ZN  C ZN  1 
HETATM 11097 CU CU  . CU1 Q  2 .   ? 91.028  1.746   20.862 1.00 28.39 ? 154  CU1 D CU  1 
HETATM 11098 ZN ZN  . ZN  R  3 .   ? 88.102  4.415   15.510 1.00 22.49 ? 155  ZN  D ZN  1 
HETATM 11099 S  S   . SO4 S  4 .   ? 73.406  1.098   12.162 1.00 68.70 ? 1400 SO4 D S   1 
HETATM 11100 O  O1  . SO4 S  4 .   ? 72.108  1.753   11.913 1.00 69.06 ? 1400 SO4 D O1  1 
HETATM 11101 O  O2  . SO4 S  4 .   ? 74.197  1.100   10.917 1.00 69.07 ? 1400 SO4 D O2  1 
HETATM 11102 O  O3  . SO4 S  4 .   ? 73.179  -0.294  12.601 1.00 68.01 ? 1400 SO4 D O3  1 
HETATM 11103 O  O4  . SO4 S  4 .   ? 74.143  1.835   13.208 1.00 68.23 ? 1400 SO4 D O4  1 
HETATM 11104 CU CU  . CU1 T  2 .   ? 38.312  -33.186 18.665 1.00 26.90 ? 154  CU1 E CU  1 
HETATM 11105 ZN ZN  . ZN  U  3 .   ? 35.452  -34.633 12.768 1.00 24.34 ? 155  ZN  E ZN  1 
HETATM 11106 CU CU  . CU1 V  2 .   ? 65.757  -16.908 20.749 1.00 26.36 ? 154  CU1 F CU  1 
HETATM 11107 ZN ZN  . ZN  W  3 .   ? 69.434  -15.538 15.346 1.00 22.85 ? 155  ZN  F ZN  1 
HETATM 11108 CU CU  . CU1 X  2 .   ? 144.079 -13.831 17.396 1.00 42.01 ? 154  CU1 G CU  1 
HETATM 11109 ZN ZN  . ZN  Y  3 .   ? 145.574 -16.791 11.540 1.00 45.76 ? 155  ZN  G ZN  1 
HETATM 11110 CU CU  . CU1 Z  2 .   ? 143.537 18.307  19.954 1.00 34.19 ? 154  CU1 H CU  1 
HETATM 11111 ZN ZN  . ZN  AA 3 .   ? 145.124 22.081  14.675 1.00 28.66 ? 155  ZN  H ZN  1 
HETATM 11112 CU CU  . CU1 BA 2 .   ? 87.489  46.667  12.723 1.00 41.86 ? 154  CU1 I CU  1 
HETATM 11113 ZN ZN  . ZN  CA 3 .   ? 84.767  48.032  6.767  1.00 40.53 ? 155  ZN  I ZN  1 
HETATM 11114 CU CU  . CU1 DA 2 .   ? 114.796 30.564  16.205 1.00 37.79 ? 154  CU1 J CU  1 
HETATM 11115 ZN ZN  . ZN  EA 3 .   ? 118.206 27.843  11.131 1.00 31.49 ? 155  ZN  J ZN  1 
HETATM 11116 O  O   . HOH FA 5 .   ? 52.165  33.674  -1.658 1.00 25.96 ? 156  HOH A O   1 
HETATM 11117 O  O   . HOH FA 5 .   ? 68.001  31.358  20.263 1.00 21.33 ? 157  HOH A O   1 
HETATM 11118 O  O   . HOH FA 5 .   ? 54.097  34.677  2.380  1.00 27.60 ? 158  HOH A O   1 
HETATM 11119 O  O   . HOH FA 5 .   ? 71.732  45.343  17.581 1.00 21.31 ? 159  HOH A O   1 
HETATM 11120 O  O   . HOH FA 5 .   ? 58.889  31.863  21.898 1.00 20.22 ? 160  HOH A O   1 
HETATM 11121 O  O   . HOH FA 5 .   ? 68.927  37.241  8.395  1.00 33.95 ? 161  HOH A O   1 
HETATM 11122 O  O   . HOH FA 5 .   ? 44.112  51.875  32.502 1.00 35.96 ? 162  HOH A O   1 
HETATM 11123 O  O   . HOH FA 5 .   ? 57.944  48.694  31.653 1.00 27.38 ? 163  HOH A O   1 
HETATM 11124 O  O   . HOH FA 5 .   ? 51.299  24.744  18.842 1.00 29.55 ? 164  HOH A O   1 
HETATM 11125 O  O   . HOH FA 5 .   ? 61.914  31.862  22.760 1.00 31.05 ? 165  HOH A O   1 
HETATM 11126 O  O   . HOH FA 5 .   ? 59.290  30.846  7.226  1.00 31.58 ? 166  HOH A O   1 
HETATM 11127 O  O   . HOH FA 5 .   ? 51.454  51.270  16.622 1.00 33.58 ? 167  HOH A O   1 
HETATM 11128 O  O   . HOH FA 5 .   ? 62.888  46.151  5.615  1.00 30.35 ? 168  HOH A O   1 
HETATM 11129 O  O   . HOH FA 5 .   ? 48.020  46.360  20.190 1.00 30.62 ? 169  HOH A O   1 
HETATM 11130 O  O   . HOH FA 5 .   ? 58.454  46.555  33.387 1.00 28.48 ? 170  HOH A O   1 
HETATM 11131 O  O   . HOH FA 5 .   ? 65.849  50.407  21.156 1.00 33.05 ? 171  HOH A O   1 
HETATM 11132 O  O   . HOH FA 5 .   ? 61.380  42.115  32.217 1.00 29.71 ? 172  HOH A O   1 
HETATM 11133 O  O   . HOH FA 5 .   ? 48.658  40.315  -1.413 1.00 31.56 ? 173  HOH A O   1 
HETATM 11134 O  O   . HOH FA 5 .   ? 54.807  39.700  35.571 1.00 31.59 ? 174  HOH A O   1 
HETATM 11135 O  O   . HOH FA 5 .   ? 73.098  35.305  15.722 1.00 29.88 ? 175  HOH A O   1 
HETATM 11136 O  O   . HOH FA 5 .   ? 59.432  34.048  -1.464 1.00 38.03 ? 176  HOH A O   1 
HETATM 11137 O  O   . HOH FA 5 .   ? 58.092  39.124  6.878  1.00 27.98 ? 177  HOH A O   1 
HETATM 11138 O  O   . HOH FA 5 .   ? 67.785  35.242  6.957  1.00 41.43 ? 178  HOH A O   1 
HETATM 11139 O  O   . HOH FA 5 .   ? 52.767  51.596  35.759 1.00 36.79 ? 179  HOH A O   1 
HETATM 11140 O  O   . HOH FA 5 .   ? 59.614  50.482  31.022 1.00 35.79 ? 180  HOH A O   1 
HETATM 11141 O  O   . HOH FA 5 .   ? 49.646  30.859  18.225 1.00 29.83 ? 181  HOH A O   1 
HETATM 11142 O  O   . HOH FA 5 .   ? 66.620  36.978  21.402 1.00 34.98 ? 182  HOH A O   1 
HETATM 11143 O  O   . HOH FA 5 .   ? 57.633  50.565  14.690 1.00 34.12 ? 183  HOH A O   1 
HETATM 11144 O  O   . HOH FA 5 .   ? 62.058  32.200  8.432  1.00 30.66 ? 184  HOH A O   1 
HETATM 11145 O  O   . HOH FA 5 .   ? 50.993  43.465  34.991 1.00 36.23 ? 185  HOH A O   1 
HETATM 11146 O  O   . HOH FA 5 .   ? 52.073  32.219  5.367  1.00 33.25 ? 186  HOH A O   1 
HETATM 11147 O  O   . HOH FA 5 .   ? 75.232  32.986  18.359 1.00 30.95 ? 187  HOH A O   1 
HETATM 11148 O  O   . HOH FA 5 .   ? 60.912  32.689  25.511 1.00 31.38 ? 188  HOH A O   1 
HETATM 11149 O  O   . HOH FA 5 .   ? 49.573  41.430  35.688 1.00 29.98 ? 189  HOH A O   1 
HETATM 11150 O  O   . HOH FA 5 .   ? 46.031  36.268  5.378  1.00 37.32 ? 190  HOH A O   1 
HETATM 11151 O  O   . HOH FA 5 .   ? 48.287  47.297  22.992 1.00 34.86 ? 191  HOH A O   1 
HETATM 11152 O  O   . HOH FA 5 .   ? 76.413  33.504  20.967 1.00 31.16 ? 192  HOH A O   1 
HETATM 11153 O  O   . HOH FA 5 .   ? 66.540  48.309  19.112 1.00 43.26 ? 193  HOH A O   1 
HETATM 11154 O  O   . HOH FA 5 .   ? 61.655  44.924  33.139 1.00 44.74 ? 194  HOH A O   1 
HETATM 11155 O  O   . HOH FA 5 .   ? 52.285  53.839  11.949 1.00 36.87 ? 195  HOH A O   1 
HETATM 11156 O  O   . HOH FA 5 .   ? 67.165  39.389  27.874 1.00 32.78 ? 196  HOH A O   1 
HETATM 11157 O  O   . HOH FA 5 .   ? 49.493  48.084  18.738 1.00 35.57 ? 197  HOH A O   1 
HETATM 11158 O  O   . HOH FA 5 .   ? 71.165  62.884  15.541 1.00 52.61 ? 198  HOH A O   1 
HETATM 11159 O  O   . HOH FA 5 .   ? 63.947  35.383  26.080 1.00 40.22 ? 199  HOH A O   1 
HETATM 11160 O  O   . HOH FA 5 .   ? 44.471  44.600  33.194 1.00 44.55 ? 200  HOH A O   1 
HETATM 11161 O  O   . HOH FA 5 .   ? 49.268  31.554  5.019  1.00 32.16 ? 201  HOH A O   1 
HETATM 11162 O  O   . HOH FA 5 .   ? 63.182  34.875  6.459  1.00 38.02 ? 202  HOH A O   1 
HETATM 11163 O  O   . HOH FA 5 .   ? 67.130  48.715  14.211 1.00 29.83 ? 203  HOH A O   1 
HETATM 11164 O  O   . HOH FA 5 .   ? 58.144  28.676  8.241  1.00 42.00 ? 204  HOH A O   1 
HETATM 11165 O  O   . HOH FA 5 .   ? 51.800  37.195  37.204 1.00 33.39 ? 205  HOH A O   1 
HETATM 11166 O  O   . HOH FA 5 .   ? 47.002  44.929  7.510  1.00 42.10 ? 206  HOH A O   1 
HETATM 11167 O  O   . HOH FA 5 .   ? 58.022  29.419  3.643  1.00 45.82 ? 207  HOH A O   1 
HETATM 11168 O  O   . HOH FA 5 .   ? 52.993  48.724  35.953 1.00 36.75 ? 208  HOH A O   1 
HETATM 11169 O  O   . HOH FA 5 .   ? 69.832  33.522  7.345  1.00 44.52 ? 209  HOH A O   1 
HETATM 11170 O  O   . HOH FA 5 .   ? 49.311  30.333  22.351 1.00 34.45 ? 210  HOH A O   1 
HETATM 11171 O  O   . HOH FA 5 .   ? 45.049  36.070  8.807  1.00 42.13 ? 211  HOH A O   1 
HETATM 11172 O  O   . HOH FA 5 .   ? 60.660  38.087  32.169 1.00 33.17 ? 212  HOH A O   1 
HETATM 11173 O  O   . HOH FA 5 .   ? 69.698  45.201  24.494 1.00 51.18 ? 213  HOH A O   1 
HETATM 11174 O  O   . HOH FA 5 .   ? 51.833  54.146  18.534 1.00 41.05 ? 214  HOH A O   1 
HETATM 11175 O  O   . HOH FA 5 .   ? 65.326  37.727  4.508  1.00 44.99 ? 215  HOH A O   1 
HETATM 11176 O  O   . HOH FA 5 .   ? 48.358  30.599  24.967 1.00 44.16 ? 216  HOH A O   1 
HETATM 11177 O  O   . HOH FA 5 .   ? 48.011  30.555  0.956  1.00 41.07 ? 217  HOH A O   1 
HETATM 11178 O  O   . HOH FA 5 .   ? 60.682  47.402  4.660  1.00 41.44 ? 218  HOH A O   1 
HETATM 11179 O  O   . HOH FA 5 .   ? 59.379  42.043  2.890  1.00 38.61 ? 219  HOH A O   1 
HETATM 11180 O  O   . HOH FA 5 .   ? 48.062  39.656  34.148 1.00 42.37 ? 220  HOH A O   1 
HETATM 11181 O  O   . HOH FA 5 .   ? 47.406  53.206  28.911 1.00 39.41 ? 221  HOH A O   1 
HETATM 11182 O  O   . HOH FA 5 .   ? 50.439  46.808  7.778  1.00 41.44 ? 222  HOH A O   1 
HETATM 11183 O  O   . HOH FA 5 .   ? 67.717  42.740  8.800  1.00 39.27 ? 223  HOH A O   1 
HETATM 11184 O  O   . HOH FA 5 .   ? 58.308  36.577  2.737  1.00 38.68 ? 224  HOH A O   1 
HETATM 11185 O  O   . HOH FA 5 .   ? 49.883  46.650  11.343 1.00 40.78 ? 225  HOH A O   1 
HETATM 11186 O  O   . HOH FA 5 .   ? 56.212  54.248  28.124 1.00 37.70 ? 226  HOH A O   1 
HETATM 11187 O  O   . HOH FA 5 .   ? 45.968  53.394  31.419 1.00 45.98 ? 227  HOH A O   1 
HETATM 11188 O  O   . HOH FA 5 .   ? 51.075  48.719  15.927 1.00 35.35 ? 228  HOH A O   1 
HETATM 11189 O  O   . HOH FA 5 .   ? 37.770  33.917  3.011  1.00 48.60 ? 229  HOH A O   1 
HETATM 11190 O  O   . HOH FA 5 .   ? 48.968  35.487  32.552 1.00 52.81 ? 230  HOH A O   1 
HETATM 11191 O  O   . HOH FA 5 .   ? 57.162  34.046  29.925 1.00 48.19 ? 231  HOH A O   1 
HETATM 11192 O  O   . HOH FA 5 .   ? 49.537  48.338  13.680 1.00 36.69 ? 232  HOH A O   1 
HETATM 11193 O  O   . HOH FA 5 .   ? 72.968  46.343  15.404 1.00 50.50 ? 233  HOH A O   1 
HETATM 11194 O  O   . HOH FA 5 .   ? 51.230  26.765  11.425 1.00 42.91 ? 234  HOH A O   1 
HETATM 11195 O  O   . HOH FA 5 .   ? 50.799  36.382  30.025 1.00 52.21 ? 235  HOH A O   1 
HETATM 11196 O  O   . HOH FA 5 .   ? 64.938  42.034  30.660 1.00 42.35 ? 236  HOH A O   1 
HETATM 11197 O  O   . HOH FA 5 .   ? 68.059  47.071  10.669 1.00 40.78 ? 237  HOH A O   1 
HETATM 11198 O  O   . HOH FA 5 .   ? 67.899  41.040  6.358  1.00 41.47 ? 238  HOH A O   1 
HETATM 11199 O  O   . HOH FA 5 .   ? 65.591  34.284  3.174  1.00 55.18 ? 239  HOH A O   1 
HETATM 11200 O  O   . HOH FA 5 .   ? 50.363  52.450  36.743 1.00 54.33 ? 240  HOH A O   1 
HETATM 11201 O  O   . HOH FA 5 .   ? 58.017  55.893  27.492 1.00 55.00 ? 241  HOH A O   1 
HETATM 11202 O  O   . HOH FA 5 .   ? 44.377  40.715  22.661 1.00 43.23 ? 242  HOH A O   1 
HETATM 11203 O  O   . HOH FA 5 .   ? 58.057  40.718  4.589  1.00 44.24 ? 243  HOH A O   1 
HETATM 11204 O  O   . HOH FA 5 .   ? 52.934  43.851  36.751 1.00 37.98 ? 244  HOH A O   1 
HETATM 11205 O  O   . HOH FA 5 .   ? 45.085  46.399  28.507 1.00 49.85 ? 245  HOH A O   1 
HETATM 11206 O  O   . HOH FA 5 .   ? 52.955  35.070  30.571 1.00 50.06 ? 246  HOH A O   1 
HETATM 11207 O  O   . HOH FA 5 .   ? 68.860  49.134  12.333 1.00 42.37 ? 247  HOH A O   1 
HETATM 11208 O  O   . HOH FA 5 .   ? 59.012  57.698  26.125 1.00 53.51 ? 248  HOH A O   1 
HETATM 11209 O  O   . HOH FA 5 .   ? 60.320  29.023  2.844  1.00 51.63 ? 249  HOH A O   1 
HETATM 11210 O  O   . HOH FA 5 .   ? 47.270  33.509  23.958 1.00 38.14 ? 250  HOH A O   1 
HETATM 11211 O  O   . HOH FA 5 .   ? 72.861  31.592  27.238 1.00 44.52 ? 251  HOH A O   1 
HETATM 11212 O  O   . HOH FA 5 .   ? 60.201  56.418  8.442  1.00 46.36 ? 252  HOH A O   1 
HETATM 11213 O  O   . HOH FA 5 .   ? 53.332  56.404  26.923 1.00 44.35 ? 253  HOH A O   1 
HETATM 11214 O  O   . HOH FA 5 .   ? 70.050  35.463  28.960 1.00 44.21 ? 254  HOH A O   1 
HETATM 11215 O  O   . HOH FA 5 .   ? 65.833  31.254  26.279 1.00 47.99 ? 255  HOH A O   1 
HETATM 11216 O  O   . HOH FA 5 .   ? 45.204  43.344  35.526 1.00 48.11 ? 256  HOH A O   1 
HETATM 11217 O  O   . HOH FA 5 .   ? 63.845  33.575  23.349 1.00 49.01 ? 257  HOH A O   1 
HETATM 11218 O  O   . HOH FA 5 .   ? 63.901  32.479  27.601 1.00 49.97 ? 258  HOH A O   1 
HETATM 11219 O  O   . HOH FA 5 .   ? 72.493  40.966  8.126  1.00 54.54 ? 259  HOH A O   1 
HETATM 11220 O  O   . HOH FA 5 .   ? 72.104  42.630  10.123 1.00 55.46 ? 260  HOH A O   1 
HETATM 11221 O  O   . HOH FA 5 .   ? 48.883  18.688  13.990 1.00 49.12 ? 261  HOH A O   1 
HETATM 11222 O  O   . HOH FA 5 .   ? 48.267  35.580  25.299 1.00 52.36 ? 262  HOH A O   1 
HETATM 11223 O  O   . HOH FA 5 .   ? 49.701  20.475  12.350 1.00 50.81 ? 263  HOH A O   1 
HETATM 11224 O  O   . HOH FA 5 .   ? 51.516  49.253  5.852  1.00 50.24 ? 264  HOH A O   1 
HETATM 11225 O  O   . HOH FA 5 .   ? 67.591  47.938  16.803 1.00 43.49 ? 265  HOH A O   1 
HETATM 11226 O  O   . HOH FA 5 .   ? 71.565  43.366  19.449 1.00 49.69 ? 266  HOH A O   1 
HETATM 11227 O  O   . HOH FA 5 .   ? 54.104  55.007  33.272 1.00 46.12 ? 267  HOH A O   1 
HETATM 11228 O  O   . HOH FA 5 .   ? 49.431  50.838  21.323 1.00 47.10 ? 268  HOH A O   1 
HETATM 11229 O  O   . HOH FA 5 .   ? 66.875  53.732  22.201 1.00 51.29 ? 269  HOH A O   1 
HETATM 11230 O  O   . HOH FA 5 .   ? 70.660  60.244  17.943 1.00 60.00 ? 270  HOH A O   1 
HETATM 11231 O  O   . HOH FA 5 .   ? 45.298  37.051  25.244 1.00 45.45 ? 271  HOH A O   1 
HETATM 11232 O  O   . HOH FA 5 .   ? 43.585  32.987  21.355 1.00 51.07 ? 272  HOH A O   1 
HETATM 11233 O  O   . HOH FA 5 .   ? 60.044  30.860  4.678  1.00 58.33 ? 273  HOH A O   1 
HETATM 11234 O  O   . HOH FA 5 .   ? 53.153  28.476  4.984  1.00 50.73 ? 274  HOH A O   1 
HETATM 11235 O  O   . HOH FA 5 .   ? 45.646  28.302  6.673  1.00 55.83 ? 275  HOH A O   1 
HETATM 11236 O  O   . HOH FA 5 .   ? 56.813  56.827  5.140  1.00 61.12 ? 276  HOH A O   1 
HETATM 11237 O  O   . HOH FA 5 .   ? 43.611  29.412  5.346  1.00 53.11 ? 277  HOH A O   1 
HETATM 11238 O  O   . HOH FA 5 .   ? 46.367  47.168  25.738 1.00 48.34 ? 278  HOH A O   1 
HETATM 11239 O  O   . HOH FA 5 .   ? 67.244  56.763  23.008 1.00 57.28 ? 279  HOH A O   1 
HETATM 11240 O  O   . HOH FA 5 .   ? 52.836  25.942  9.500  1.00 54.36 ? 280  HOH A O   1 
HETATM 11241 O  O   . HOH FA 5 .   ? 64.168  49.520  18.899 1.00 55.52 ? 281  HOH A O   1 
HETATM 11242 O  O   . HOH FA 5 .   ? 60.992  31.057  1.040  1.00 52.09 ? 282  HOH A O   1 
HETATM 11243 O  O   . HOH FA 5 .   ? 68.111  54.669  25.281 1.00 57.00 ? 283  HOH A O   1 
HETATM 11244 O  O   . HOH FA 5 .   ? 68.494  45.842  26.173 1.00 36.88 ? 284  HOH A O   1 
HETATM 11245 O  O   . HOH FA 5 .   ? 71.072  45.753  22.493 1.00 51.74 ? 285  HOH A O   1 
HETATM 11246 O  O   . HOH GA 5 .   ? 73.704  5.507   28.245 1.00 25.27 ? 156  HOH B O   1 
HETATM 11247 O  O   . HOH GA 5 .   ? 77.886  7.137   23.759 1.00 18.09 ? 157  HOH B O   1 
HETATM 11248 O  O   . HOH GA 5 .   ? 66.503  9.592   16.496 1.00 18.51 ? 158  HOH B O   1 
HETATM 11249 O  O   . HOH GA 5 .   ? 71.250  5.885   13.301 1.00 20.96 ? 159  HOH B O   1 
HETATM 11250 O  O   . HOH GA 5 .   ? 73.330  11.201  17.299 1.00 23.53 ? 160  HOH B O   1 
HETATM 11251 O  O   . HOH GA 5 .   ? 57.160  29.520  21.613 1.00 26.22 ? 161  HOH B O   1 
HETATM 11252 O  O   . HOH GA 5 .   ? 66.509  29.412  21.360 1.00 19.67 ? 162  HOH B O   1 
HETATM 11253 O  O   . HOH GA 5 .   ? 80.188  14.745  25.735 1.00 24.39 ? 163  HOH B O   1 
HETATM 11254 O  O   . HOH GA 5 .   ? 73.078  12.577  11.373 1.00 27.99 ? 164  HOH B O   1 
HETATM 11255 O  O   . HOH GA 5 .   ? 78.220  5.400   12.903 1.00 27.60 ? 165  HOH B O   1 
HETATM 11256 O  O   . HOH GA 5 .   ? 55.719  17.149  11.644 1.00 25.46 ? 166  HOH B O   1 
HETATM 11257 O  O   . HOH GA 5 .   ? 59.450  13.050  8.088  1.00 23.02 ? 167  HOH B O   1 
HETATM 11258 O  O   . HOH GA 5 .   ? 66.188  20.310  33.161 1.00 26.28 ? 168  HOH B O   1 
HETATM 11259 O  O   . HOH GA 5 .   ? 72.213  12.479  7.618  1.00 31.37 ? 169  HOH B O   1 
HETATM 11260 O  O   . HOH GA 5 .   ? 54.113  21.831  10.910 1.00 36.24 ? 170  HOH B O   1 
HETATM 11261 O  O   . HOH GA 5 .   ? 68.160  2.643   13.875 1.00 24.90 ? 171  HOH B O   1 
HETATM 11262 O  O   . HOH GA 5 .   ? 61.093  -1.717  16.778 1.00 26.17 ? 172  HOH B O   1 
HETATM 11263 O  O   . HOH GA 5 .   ? 68.030  12.047  32.745 1.00 23.70 ? 173  HOH B O   1 
HETATM 11264 O  O   . HOH GA 5 .   ? 69.696  13.999  32.664 1.00 25.93 ? 174  HOH B O   1 
HETATM 11265 O  O   . HOH GA 5 .   ? 75.600  14.513  6.671  1.00 31.79 ? 175  HOH B O   1 
HETATM 11266 O  O   . HOH GA 5 .   ? 76.465  12.722  12.964 1.00 24.71 ? 176  HOH B O   1 
HETATM 11267 O  O   . HOH GA 5 .   ? 83.455  10.708  31.021 1.00 33.72 ? 177  HOH B O   1 
HETATM 11268 O  O   . HOH GA 5 .   ? 53.592  15.036  21.407 1.00 34.06 ? 178  HOH B O   1 
HETATM 11269 O  O   . HOH GA 5 .   ? 66.921  -3.796  19.418 1.00 33.08 ? 179  HOH B O   1 
HETATM 11270 O  O   . HOH GA 5 .   ? 75.986  22.217  3.548  1.00 27.49 ? 180  HOH B O   1 
HETATM 11271 O  O   . HOH GA 5 .   ? 73.045  6.976   15.039 1.00 25.33 ? 181  HOH B O   1 
HETATM 11272 O  O   . HOH GA 5 .   ? 75.567  4.271   26.730 1.00 28.33 ? 182  HOH B O   1 
HETATM 11273 O  O   . HOH GA 5 .   ? 81.439  21.698  22.870 1.00 37.40 ? 183  HOH B O   1 
HETATM 11274 O  O   . HOH GA 5 .   ? 76.683  4.861   24.020 1.00 33.55 ? 184  HOH B O   1 
HETATM 11275 O  O   . HOH GA 5 .   ? 58.041  15.740  29.047 1.00 34.29 ? 185  HOH B O   1 
HETATM 11276 O  O   . HOH GA 5 .   ? 82.308  15.850  27.069 1.00 27.52 ? 186  HOH B O   1 
HETATM 11277 O  O   . HOH GA 5 .   ? 70.039  3.588   21.445 1.00 29.83 ? 187  HOH B O   1 
HETATM 11278 O  O   . HOH GA 5 .   ? 57.167  11.649  17.695 1.00 25.52 ? 188  HOH B O   1 
HETATM 11279 O  O   . HOH GA 5 .   ? 79.381  35.789  12.308 1.00 31.77 ? 189  HOH B O   1 
HETATM 11280 O  O   . HOH GA 5 .   ? 63.247  29.179  23.056 1.00 31.55 ? 190  HOH B O   1 
HETATM 11281 O  O   . HOH GA 5 .   ? 59.863  10.725  24.300 1.00 25.81 ? 191  HOH B O   1 
HETATM 11282 O  O   . HOH GA 5 .   ? 67.049  24.160  32.480 1.00 29.81 ? 192  HOH B O   1 
HETATM 11283 O  O   . HOH GA 5 .   ? 79.094  12.584  16.683 1.00 33.20 ? 193  HOH B O   1 
HETATM 11284 O  O   . HOH GA 5 .   ? 65.902  17.943  34.446 1.00 34.63 ? 194  HOH B O   1 
HETATM 11285 O  O   . HOH GA 5 .   ? 79.330  6.441   25.922 1.00 31.87 ? 195  HOH B O   1 
HETATM 11286 O  O   . HOH GA 5 .   ? 77.704  39.099  10.468 1.00 33.83 ? 196  HOH B O   1 
HETATM 11287 O  O   . HOH GA 5 .   ? 65.547  2.400   6.874  1.00 34.37 ? 197  HOH B O   1 
HETATM 11288 O  O   . HOH GA 5 .   ? 68.887  1.184   19.921 1.00 29.03 ? 198  HOH B O   1 
HETATM 11289 O  O   . HOH GA 5 .   ? 55.836  8.123   13.787 1.00 29.15 ? 199  HOH B O   1 
HETATM 11290 O  O   . HOH GA 5 .   ? 63.812  3.249   10.951 1.00 33.24 ? 200  HOH B O   1 
HETATM 11291 O  O   . HOH GA 5 .   ? 64.277  21.468  2.887  1.00 26.03 ? 201  HOH B O   1 
HETATM 11292 O  O   . HOH GA 5 .   ? 77.584  25.696  23.295 1.00 30.46 ? 202  HOH B O   1 
HETATM 11293 O  O   . HOH GA 5 .   ? 60.683  27.138  8.947  1.00 27.51 ? 203  HOH B O   1 
HETATM 11294 O  O   . HOH GA 5 .   ? 71.611  17.359  2.528  1.00 30.78 ? 204  HOH B O   1 
HETATM 11295 O  O   . HOH GA 5 .   ? 59.337  7.466   26.410 1.00 43.97 ? 205  HOH B O   1 
HETATM 11296 O  O   . HOH GA 5 .   ? 77.517  22.560  6.735  1.00 30.11 ? 206  HOH B O   1 
HETATM 11297 O  O   . HOH GA 5 .   ? 70.251  2.621   24.080 1.00 33.80 ? 207  HOH B O   1 
HETATM 11298 O  O   . HOH GA 5 .   ? 57.094  12.987  20.082 1.00 31.30 ? 208  HOH B O   1 
HETATM 11299 O  O   . HOH GA 5 .   ? 58.488  23.752  23.709 1.00 35.62 ? 209  HOH B O   1 
HETATM 11300 O  O   . HOH GA 5 .   ? 51.374  22.447  20.324 1.00 34.41 ? 210  HOH B O   1 
HETATM 11301 O  O   . HOH GA 5 .   ? 59.293  12.643  21.980 1.00 38.95 ? 211  HOH B O   1 
HETATM 11302 O  O   . HOH GA 5 .   ? 53.049  -1.296  21.090 1.00 30.27 ? 212  HOH B O   1 
HETATM 11303 O  O   . HOH GA 5 .   ? 76.934  30.584  4.045  1.00 44.02 ? 213  HOH B O   1 
HETATM 11304 O  O   . HOH GA 5 .   ? 75.497  11.343  35.971 1.00 31.55 ? 214  HOH B O   1 
HETATM 11305 O  O   . HOH GA 5 .   ? 54.449  0.976   23.026 1.00 30.20 ? 215  HOH B O   1 
HETATM 11306 O  O   . HOH GA 5 .   ? 69.855  19.293  4.091  1.00 33.65 ? 216  HOH B O   1 
HETATM 11307 O  O   . HOH GA 5 .   ? 59.868  23.262  7.728  1.00 39.99 ? 217  HOH B O   1 
HETATM 11308 O  O   . HOH GA 5 .   ? 84.817  14.707  29.246 1.00 38.34 ? 218  HOH B O   1 
HETATM 11309 O  O   . HOH GA 5 .   ? 54.463  23.765  9.168  1.00 41.38 ? 219  HOH B O   1 
HETATM 11310 O  O   . HOH GA 5 .   ? 80.777  20.361  20.675 1.00 32.49 ? 220  HOH B O   1 
HETATM 11311 O  O   . HOH GA 5 .   ? 71.104  2.874   26.518 1.00 34.32 ? 221  HOH B O   1 
HETATM 11312 O  O   . HOH GA 5 .   ? 65.394  9.861   5.608  1.00 29.94 ? 222  HOH B O   1 
HETATM 11313 O  O   . HOH GA 5 .   ? 68.019  2.443   5.864  1.00 38.51 ? 223  HOH B O   1 
HETATM 11314 O  O   . HOH GA 5 .   ? 78.515  2.867   24.232 1.00 35.49 ? 224  HOH B O   1 
HETATM 11315 O  O   . HOH GA 5 .   ? 62.637  28.033  7.114  1.00 33.19 ? 225  HOH B O   1 
HETATM 11316 O  O   . HOH GA 5 .   ? 76.931  19.151  34.066 1.00 27.40 ? 226  HOH B O   1 
HETATM 11317 O  O   . HOH GA 5 .   ? 61.399  11.635  6.883  1.00 29.98 ? 227  HOH B O   1 
HETATM 11318 O  O   . HOH GA 5 .   ? 68.728  5.791   28.984 1.00 34.83 ? 228  HOH B O   1 
HETATM 11319 O  O   . HOH GA 5 .   ? 72.002  32.654  8.941  1.00 40.00 ? 229  HOH B O   1 
HETATM 11320 O  O   . HOH GA 5 .   ? 63.762  1.899   26.159 1.00 31.27 ? 230  HOH B O   1 
HETATM 11321 O  O   . HOH GA 5 .   ? 73.373  27.367  3.084  1.00 39.31 ? 231  HOH B O   1 
HETATM 11322 O  O   . HOH GA 5 .   ? 69.106  -2.744  20.575 1.00 39.09 ? 232  HOH B O   1 
HETATM 11323 O  O   . HOH GA 5 .   ? 69.722  16.082  34.721 1.00 35.68 ? 233  HOH B O   1 
HETATM 11324 O  O   . HOH GA 5 .   ? 67.085  3.982   28.465 1.00 34.51 ? 234  HOH B O   1 
HETATM 11325 O  O   . HOH GA 5 .   ? 65.523  3.970   26.108 1.00 30.76 ? 235  HOH B O   1 
HETATM 11326 O  O   . HOH GA 5 .   ? 68.453  -0.525  22.062 1.00 39.09 ? 236  HOH B O   1 
HETATM 11327 O  O   . HOH GA 5 .   ? 57.497  12.817  24.337 1.00 53.22 ? 237  HOH B O   1 
HETATM 11328 O  O   . HOH GA 5 .   ? 76.689  11.548  10.505 1.00 36.70 ? 238  HOH B O   1 
HETATM 11329 O  O   . HOH GA 5 .   ? 63.056  28.441  2.737  1.00 44.39 ? 239  HOH B O   1 
HETATM 11330 O  O   . HOH GA 5 .   ? 59.712  25.384  22.440 1.00 36.83 ? 240  HOH B O   1 
HETATM 11331 O  O   . HOH GA 5 .   ? 61.728  20.379  31.474 1.00 45.42 ? 241  HOH B O   1 
HETATM 11332 O  O   . HOH GA 5 .   ? 63.158  -0.366  12.980 1.00 40.76 ? 242  HOH B O   1 
HETATM 11333 O  O   . HOH GA 5 .   ? 68.626  9.027   6.381  1.00 34.72 ? 243  HOH B O   1 
HETATM 11334 O  O   . HOH GA 5 .   ? 75.042  12.206  7.835  1.00 50.13 ? 244  HOH B O   1 
HETATM 11335 O  O   . HOH GA 5 .   ? 70.641  7.443   29.364 1.00 37.47 ? 245  HOH B O   1 
HETATM 11336 O  O   . HOH GA 5 .   ? 73.257  42.836  12.347 1.00 40.31 ? 246  HOH B O   1 
HETATM 11337 O  O   . HOH GA 5 .   ? 78.910  12.899  13.238 1.00 43.19 ? 247  HOH B O   1 
HETATM 11338 O  O   . HOH GA 5 .   ? 78.805  28.844  2.617  1.00 40.74 ? 248  HOH B O   1 
HETATM 11339 O  O   . HOH GA 5 .   ? 73.841  10.104  11.043 1.00 35.30 ? 249  HOH B O   1 
HETATM 11340 O  O   . HOH GA 5 .   ? 54.336  6.098   9.161  1.00 45.72 ? 250  HOH B O   1 
HETATM 11341 O  O   . HOH GA 5 .   ? 61.756  2.522   12.195 1.00 38.12 ? 251  HOH B O   1 
HETATM 11342 O  O   . HOH GA 5 .   ? 71.072  -3.710  13.541 1.00 43.51 ? 252  HOH B O   1 
HETATM 11343 O  O   . HOH GA 5 .   ? 73.402  11.695  37.746 1.00 40.84 ? 253  HOH B O   1 
HETATM 11344 O  O   . HOH GA 5 .   ? 61.760  -4.019  15.000 1.00 43.07 ? 254  HOH B O   1 
HETATM 11345 O  O   . HOH GA 5 .   ? 72.846  27.665  28.375 1.00 52.50 ? 255  HOH B O   1 
HETATM 11346 O  O   . HOH GA 5 .   ? 67.063  16.718  38.613 1.00 39.06 ? 256  HOH B O   1 
HETATM 11347 O  O   . HOH GA 5 .   ? 56.351  16.458  27.459 1.00 41.80 ? 257  HOH B O   1 
HETATM 11348 O  O   . HOH GA 5 .   ? 78.104  21.330  2.086  1.00 43.60 ? 258  HOH B O   1 
HETATM 11349 O  O   . HOH GA 5 .   ? 63.586  11.696  5.344  1.00 39.09 ? 259  HOH B O   1 
HETATM 11350 O  O   . HOH GA 5 .   ? 60.211  30.454  26.886 1.00 53.78 ? 260  HOH B O   1 
HETATM 11351 O  O   . HOH GA 5 .   ? 69.541  13.401  2.632  1.00 36.04 ? 261  HOH B O   1 
HETATM 11352 O  O   . HOH GA 5 .   ? 51.194  17.069  14.687 1.00 43.13 ? 262  HOH B O   1 
HETATM 11353 O  O   . HOH GA 5 .   ? 82.092  21.688  27.018 1.00 45.77 ? 263  HOH B O   1 
HETATM 11354 O  O   . HOH GA 5 .   ? 61.499  2.099   27.404 1.00 46.46 ? 264  HOH B O   1 
HETATM 11355 O  O   . HOH GA 5 .   ? 83.246  18.125  30.744 1.00 36.40 ? 265  HOH B O   1 
HETATM 11356 O  O   . HOH GA 5 .   ? 65.903  16.492  3.556  1.00 63.14 ? 266  HOH B O   1 
HETATM 11357 O  O   . HOH GA 5 .   ? 62.430  26.189  26.773 1.00 34.60 ? 267  HOH B O   1 
HETATM 11358 O  O   . HOH GA 5 .   ? 75.324  41.469  12.000 1.00 44.19 ? 268  HOH B O   1 
HETATM 11359 O  O   . HOH GA 5 .   ? 71.102  35.449  8.950  1.00 48.22 ? 269  HOH B O   1 
HETATM 11360 O  O   . HOH GA 5 .   ? 74.895  29.330  15.255 1.00 40.03 ? 270  HOH B O   1 
HETATM 11361 O  O   . HOH GA 5 .   ? 67.369  22.352  1.701  1.00 44.75 ? 271  HOH B O   1 
HETATM 11362 O  O   . HOH GA 5 .   ? 59.601  22.891  30.049 1.00 47.31 ? 272  HOH B O   1 
HETATM 11363 O  O   . HOH GA 5 .   ? 78.243  27.771  21.222 1.00 41.60 ? 273  HOH B O   1 
HETATM 11364 O  O   . HOH GA 5 .   ? 59.363  25.691  7.038  1.00 42.71 ? 274  HOH B O   1 
HETATM 11365 O  O   . HOH GA 5 .   ? 62.239  4.719   4.220  1.00 48.95 ? 275  HOH B O   1 
HETATM 11366 O  O   . HOH GA 5 .   ? 60.757  25.521  28.755 1.00 47.52 ? 276  HOH B O   1 
HETATM 11367 O  O   . HOH GA 5 .   ? 74.982  15.651  35.878 1.00 36.97 ? 277  HOH B O   1 
HETATM 11368 O  O   . HOH GA 5 .   ? 73.561  1.991   26.089 1.00 51.61 ? 278  HOH B O   1 
HETATM 11369 O  O   . HOH GA 5 .   ? 62.561  28.949  27.857 1.00 44.04 ? 279  HOH B O   1 
HETATM 11370 O  O   . HOH GA 5 .   ? 53.332  9.394   10.702 1.00 41.17 ? 280  HOH B O   1 
HETATM 11371 O  O   . HOH GA 5 .   ? 82.156  24.456  25.994 1.00 48.75 ? 281  HOH B O   1 
HETATM 11372 O  O   . HOH GA 5 .   ? 54.827  12.671  21.462 1.00 37.46 ? 282  HOH B O   1 
HETATM 11373 O  O   . HOH GA 5 .   ? 82.516  7.379   34.979 1.00 47.41 ? 283  HOH B O   1 
HETATM 11374 O  O   . HOH GA 5 .   ? 54.776  15.218  25.875 1.00 44.96 ? 284  HOH B O   1 
HETATM 11375 O  O   . HOH GA 5 .   ? 74.454  1.595   23.732 1.00 35.51 ? 285  HOH B O   1 
HETATM 11376 O  O   . HOH GA 5 .   ? 65.979  19.312  39.335 1.00 40.21 ? 286  HOH B O   1 
HETATM 11377 O  O   . HOH GA 5 .   ? 75.802  31.372  16.445 1.00 52.63 ? 287  HOH B O   1 
HETATM 11378 O  O   . HOH GA 5 .   ? 48.806  28.527  19.011 1.00 48.83 ? 288  HOH B O   1 
HETATM 11379 O  O   . HOH GA 5 .   ? 56.222  4.491   7.324  1.00 49.66 ? 289  HOH B O   1 
HETATM 11380 O  O   . HOH GA 5 .   ? 58.768  1.026   26.828 1.00 48.62 ? 290  HOH B O   1 
HETATM 11381 O  O   . HOH GA 5 .   ? 70.001  27.901  28.832 1.00 46.37 ? 291  HOH B O   1 
HETATM 11382 O  O   . HOH GA 5 .   ? 53.648  16.833  23.872 1.00 42.69 ? 292  HOH B O   1 
HETATM 11383 O  O   . HOH GA 5 .   ? 55.624  13.210  14.201 1.00 44.47 ? 293  HOH B O   1 
HETATM 11384 O  O   . HOH GA 5 .   ? 71.765  0.316   17.165 1.00 50.68 ? 294  HOH B O   1 
HETATM 11385 O  O   . HOH GA 5 .   ? 57.164  21.258  5.942  1.00 44.63 ? 295  HOH B O   1 
HETATM 11386 O  O   . HOH GA 5 .   ? 79.453  19.415  14.098 1.00 41.58 ? 296  HOH B O   1 
HETATM 11387 O  O   . HOH GA 5 .   ? 76.460  30.498  19.645 1.00 37.50 ? 297  HOH B O   1 
HETATM 11388 O  O   . HOH GA 5 .   ? 57.595  10.098  27.777 1.00 55.08 ? 298  HOH B O   1 
HETATM 11389 O  O   . HOH GA 5 .   ? 58.352  9.887   1.848  1.00 50.83 ? 299  HOH B O   1 
HETATM 11390 O  O   . HOH GA 5 .   ? 76.796  13.932  36.694 1.00 53.86 ? 300  HOH B O   1 
HETATM 11391 O  O   . HOH GA 5 .   ? 65.140  28.782  25.347 1.00 36.33 ? 301  HOH B O   1 
HETATM 11392 O  O   . HOH GA 5 .   ? 84.583  11.112  28.841 1.00 52.36 ? 302  HOH B O   1 
HETATM 11393 O  O   . HOH GA 5 .   ? 55.436  20.459  7.727  1.00 45.31 ? 303  HOH B O   1 
HETATM 11394 O  O   . HOH GA 5 .   ? 73.755  20.947  37.632 1.00 48.30 ? 304  HOH B O   1 
HETATM 11395 O  O   . HOH GA 5 .   ? 81.645  8.549   30.489 1.00 52.62 ? 305  HOH B O   1 
HETATM 11396 O  O   . HOH GA 5 .   ? 64.261  0.443   28.745 1.00 42.44 ? 306  HOH B O   1 
HETATM 11397 O  O   . HOH GA 5 .   ? 80.336  15.089  13.610 1.00 47.35 ? 307  HOH B O   1 
HETATM 11398 O  O   . HOH GA 5 .   ? 63.745  1.921   4.687  1.00 52.56 ? 308  HOH B O   1 
HETATM 11399 O  O   . HOH GA 5 .   ? 79.535  24.184  8.170  1.00 51.76 ? 309  HOH B O   1 
HETATM 11400 O  O   . HOH GA 5 .   ? 80.051  17.672  12.207 1.00 46.63 ? 310  HOH B O   1 
HETATM 11401 O  O   . HOH GA 5 .   ? 82.564  23.219  7.297  1.00 62.40 ? 311  HOH B O   1 
HETATM 11402 O  O   . HOH GA 5 .   ? 62.382  14.527  0.593  1.00 52.57 ? 312  HOH B O   1 
HETATM 11403 O  O   . HOH GA 5 .   ? 56.095  1.443   26.062 1.00 42.83 ? 313  HOH B O   1 
HETATM 11404 O  O   . HOH GA 5 .   ? 64.796  2.633   30.217 1.00 48.46 ? 314  HOH B O   1 
HETATM 11405 O  O   . HOH GA 5 .   ? 77.614  29.026  5.834  1.00 36.26 ? 315  HOH B O   1 
HETATM 11406 O  O   . HOH GA 5 .   ? 58.624  4.953   26.728 1.00 42.11 ? 316  HOH B O   1 
HETATM 11407 O  O   . HOH GA 5 .   ? 65.187  30.954  23.233 1.00 47.50 ? 317  HOH B O   1 
HETATM 11408 O  O   . HOH GA 5 .   ? 85.338  12.289  31.071 1.00 59.68 ? 318  HOH B O   1 
HETATM 11409 O  O   . HOH GA 5 .   ? 49.971  27.963  21.232 1.00 51.61 ? 319  HOH B O   1 
HETATM 11410 O  O   . HOH GA 5 .   ? 54.844  18.540  9.418  1.00 40.77 ? 320  HOH B O   1 
HETATM 11411 O  O   . HOH GA 5 .   ? 79.681  9.157   29.041 1.00 46.10 ? 321  HOH B O   1 
HETATM 11412 O  O   . HOH GA 5 .   ? 53.296  13.203  4.830  1.00 50.77 ? 322  HOH B O   1 
HETATM 11413 O  O   . HOH GA 5 .   ? 60.048  16.093  0.666  1.00 62.58 ? 323  HOH B O   1 
HETATM 11414 O  O   . HOH GA 5 .   ? 65.839  24.302  0.055  1.00 43.52 ? 324  HOH B O   1 
HETATM 11415 O  O   . HOH GA 5 .   ? 69.162  33.040  27.321 1.00 49.46 ? 325  HOH B O   1 
HETATM 11416 O  O   . HOH GA 5 .   ? 62.043  18.542  0.185  1.00 42.20 ? 326  HOH B O   1 
HETATM 11417 O  O   . HOH GA 5 .   ? 67.247  16.051  35.415 1.00 47.58 ? 327  HOH B O   1 
HETATM 11418 O  O   . HOH GA 5 .   ? 51.341  15.436  20.419 1.00 57.81 ? 328  HOH B O   1 
HETATM 11419 O  O   . HOH GA 5 .   ? 75.695  18.165  36.627 1.00 51.64 ? 329  HOH B O   1 
HETATM 11420 O  O   . HOH GA 5 .   ? 53.658  15.236  12.365 1.00 46.11 ? 330  HOH B O   1 
HETATM 11421 O  O   . HOH GA 5 .   ? 65.027  1.280   9.119  1.00 47.98 ? 331  HOH B O   1 
HETATM 11422 O  O   . HOH GA 5 .   ? 81.162  21.330  13.823 1.00 43.19 ? 332  HOH B O   1 
HETATM 11423 O  O   . HOH GA 5 .   ? 69.071  1.595   7.983  1.00 44.29 ? 333  HOH B O   1 
HETATM 11424 O  O   . HOH GA 5 .   ? 73.093  18.552  37.391 1.00 53.16 ? 334  HOH B O   1 
HETATM 11425 O  O   . HOH GA 5 .   ? 68.537  2.036   27.665 1.00 51.34 ? 335  HOH B O   1 
HETATM 11426 O  O   . HOH GA 5 .   ? 61.622  27.943  4.754  1.00 54.74 ? 336  HOH B O   1 
HETATM 11427 O  O   . HOH GA 5 .   ? 70.813  26.937  3.990  1.00 48.80 ? 337  HOH B O   1 
HETATM 11428 O  O   . HOH GA 5 .   ? 61.426  26.681  24.069 1.00 44.97 ? 338  HOH B O   1 
HETATM 11429 O  O   . HOH GA 5 .   ? 50.876  13.253  18.509 1.00 50.69 ? 339  HOH B O   1 
HETATM 11430 O  O   . HOH GA 5 .   ? 51.943  12.404  16.308 1.00 45.28 ? 340  HOH B O   1 
HETATM 11431 O  O   . HOH GA 5 .   ? 58.818  18.354  0.071  1.00 41.77 ? 341  HOH B O   1 
HETATM 11432 O  O   . HOH GA 5 .   ? 65.119  15.665  -0.244 1.00 48.07 ? 342  HOH B O   1 
HETATM 11433 O  O   . HOH GA 5 .   ? 74.233  9.414   8.593  1.00 53.49 ? 343  HOH B O   1 
HETATM 11434 O  O   . HOH GA 5 .   ? 69.149  25.281  2.936  1.00 48.47 ? 344  HOH B O   1 
HETATM 11435 O  O   . HOH GA 5 .   ? 71.413  4.794   28.575 1.00 52.64 ? 345  HOH B O   1 
HETATM 11436 O  O   . HOH GA 5 .   ? 64.299  13.436  2.966  1.00 44.94 ? 346  HOH B O   1 
HETATM 11437 O  O   . HOH GA 5 .   ? 57.938  8.713   25.018 1.00 52.72 ? 347  HOH B O   1 
HETATM 11438 O  O   . HOH HA 5 .   ? 124.942 -11.055 14.840 1.00 31.85 ? 156  HOH C O   1 
HETATM 11439 O  O   . HOH HA 5 .   ? 106.372 -6.209  22.493 1.00 25.96 ? 157  HOH C O   1 
HETATM 11440 O  O   . HOH HA 5 .   ? 107.886 -3.608  21.504 1.00 25.31 ? 158  HOH C O   1 
HETATM 11441 O  O   . HOH HA 5 .   ? 113.052 1.125   -2.032 1.00 35.03 ? 159  HOH C O   1 
HETATM 11442 O  O   . HOH HA 5 .   ? 108.495 -13.424 21.469 1.00 37.31 ? 160  HOH C O   1 
HETATM 11443 O  O   . HOH HA 5 .   ? 118.738 -13.742 5.792  1.00 40.24 ? 161  HOH C O   1 
HETATM 11444 O  O   . HOH HA 5 .   ? 111.631 1.976   4.870  1.00 35.30 ? 162  HOH C O   1 
HETATM 11445 O  O   . HOH HA 5 .   ? 112.080 -2.905  37.557 1.00 41.25 ? 163  HOH C O   1 
HETATM 11446 O  O   . HOH HA 5 .   ? 125.966 -0.700  20.128 1.00 26.54 ? 164  HOH C O   1 
HETATM 11447 O  O   . HOH HA 5 .   ? 131.407 -10.565 27.660 1.00 45.87 ? 165  HOH C O   1 
HETATM 11448 O  O   . HOH HA 5 .   ? 112.392 -8.244  32.115 1.00 33.71 ? 166  HOH C O   1 
HETATM 11449 O  O   . HOH HA 5 .   ? 125.939 7.331   18.806 1.00 33.08 ? 167  HOH C O   1 
HETATM 11450 O  O   . HOH HA 5 .   ? 124.514 -20.187 3.002  1.00 38.33 ? 168  HOH C O   1 
HETATM 11451 O  O   . HOH HA 5 .   ? 107.238 5.181   10.973 1.00 41.63 ? 169  HOH C O   1 
HETATM 11452 O  O   . HOH HA 5 .   ? 106.660 -7.014  8.039  1.00 32.31 ? 170  HOH C O   1 
HETATM 11453 O  O   . HOH HA 5 .   ? 108.131 -10.984 20.717 1.00 31.43 ? 171  HOH C O   1 
HETATM 11454 O  O   . HOH HA 5 .   ? 116.524 -9.064  2.660  1.00 37.50 ? 172  HOH C O   1 
HETATM 11455 O  O   . HOH HA 5 .   ? 130.752 -8.392  12.058 1.00 38.87 ? 173  HOH C O   1 
HETATM 11456 O  O   . HOH HA 5 .   ? 126.641 -1.383  22.715 1.00 44.29 ? 174  HOH C O   1 
HETATM 11457 O  O   . HOH HA 5 .   ? 107.717 -6.050  25.090 1.00 34.74 ? 175  HOH C O   1 
HETATM 11458 O  O   . HOH HA 5 .   ? 126.624 -2.887  18.663 1.00 44.85 ? 176  HOH C O   1 
HETATM 11459 O  O   . HOH HA 5 .   ? 123.070 -20.434 21.540 1.00 48.62 ? 177  HOH C O   1 
HETATM 11460 O  O   . HOH HA 5 .   ? 113.676 -21.415 17.380 1.00 38.10 ? 178  HOH C O   1 
HETATM 11461 O  O   . HOH HA 5 .   ? 103.129 -11.483 20.168 1.00 27.93 ? 179  HOH C O   1 
HETATM 11462 O  O   . HOH HA 5 .   ? 126.481 -7.300  4.927  1.00 37.74 ? 180  HOH C O   1 
HETATM 11463 O  O   . HOH HA 5 .   ? 112.305 -5.414  2.523  1.00 37.78 ? 181  HOH C O   1 
HETATM 11464 O  O   . HOH HA 5 .   ? 106.451 -19.549 16.806 1.00 44.20 ? 182  HOH C O   1 
HETATM 11465 O  O   . HOH HA 5 .   ? 112.643 4.477   4.732  1.00 38.66 ? 183  HOH C O   1 
HETATM 11466 O  O   . HOH HA 5 .   ? 111.533 4.952   18.060 1.00 38.97 ? 184  HOH C O   1 
HETATM 11467 O  O   . HOH HA 5 .   ? 107.328 -9.451  23.008 1.00 36.59 ? 185  HOH C O   1 
HETATM 11468 O  O   . HOH HA 5 .   ? 115.571 -4.099  35.486 1.00 48.55 ? 186  HOH C O   1 
HETATM 11469 O  O   . HOH HA 5 .   ? 125.371 -2.833  11.215 1.00 35.80 ? 187  HOH C O   1 
HETATM 11470 O  O   . HOH HA 5 .   ? 107.202 0.270   6.138  1.00 37.52 ? 188  HOH C O   1 
HETATM 11471 O  O   . HOH HA 5 .   ? 129.559 -14.374 26.862 1.00 41.55 ? 189  HOH C O   1 
HETATM 11472 O  O   . HOH HA 5 .   ? 115.222 -19.084 25.640 1.00 39.14 ? 190  HOH C O   1 
HETATM 11473 O  O   . HOH HA 5 .   ? 115.039 -6.200  6.831  1.00 44.64 ? 191  HOH C O   1 
HETATM 11474 O  O   . HOH HA 5 .   ? 121.599 -2.599  35.104 1.00 43.27 ? 192  HOH C O   1 
HETATM 11475 O  O   . HOH HA 5 .   ? 104.204 -9.622  25.917 1.00 43.72 ? 193  HOH C O   1 
HETATM 11476 O  O   . HOH HA 5 .   ? 112.321 6.582   0.519  1.00 50.00 ? 194  HOH C O   1 
HETATM 11477 O  O   . HOH HA 5 .   ? 113.489 -16.422 8.701  1.00 41.07 ? 195  HOH C O   1 
HETATM 11478 O  O   . HOH HA 5 .   ? 109.257 -5.599  -2.005 1.00 46.71 ? 196  HOH C O   1 
HETATM 11479 O  O   . HOH HA 5 .   ? 107.907 2.600   4.556  1.00 46.06 ? 197  HOH C O   1 
HETATM 11480 O  O   . HOH HA 5 .   ? 111.229 5.869   22.152 1.00 41.64 ? 198  HOH C O   1 
HETATM 11481 O  O   . HOH HA 5 .   ? 108.558 -9.639  25.676 1.00 38.99 ? 199  HOH C O   1 
HETATM 11482 O  O   . HOH HA 5 .   ? 110.280 -18.047 26.498 1.00 52.42 ? 200  HOH C O   1 
HETATM 11483 O  O   . HOH HA 5 .   ? 136.048 -19.946 13.248 1.00 46.40 ? 201  HOH C O   1 
HETATM 11484 O  O   . HOH HA 5 .   ? 127.003 0.146   13.588 1.00 33.69 ? 202  HOH C O   1 
HETATM 11485 O  O   . HOH HA 5 .   ? 122.682 -11.198 31.361 1.00 39.80 ? 203  HOH C O   1 
HETATM 11486 O  O   . HOH HA 5 .   ? 115.390 -10.821 31.861 1.00 39.68 ? 204  HOH C O   1 
HETATM 11487 O  O   . HOH HA 5 .   ? 121.902 -15.054 -0.868 1.00 55.39 ? 205  HOH C O   1 
HETATM 11488 O  O   . HOH HA 5 .   ? 118.858 -0.959  4.738  1.00 37.29 ? 206  HOH C O   1 
HETATM 11489 O  O   . HOH HA 5 .   ? 109.106 -9.155  6.335  1.00 55.79 ? 207  HOH C O   1 
HETATM 11490 O  O   . HOH HA 5 .   ? 116.207 -7.022  4.369  1.00 40.33 ? 208  HOH C O   1 
HETATM 11491 O  O   . HOH HA 5 .   ? 117.939 5.578   5.244  1.00 44.82 ? 209  HOH C O   1 
HETATM 11492 O  O   . HOH HA 5 .   ? 128.210 0.675   11.113 1.00 44.31 ? 210  HOH C O   1 
HETATM 11493 O  O   . HOH HA 5 .   ? 123.641 -13.796 30.623 1.00 62.28 ? 211  HOH C O   1 
HETATM 11494 O  O   . HOH HA 5 .   ? 134.158 -14.398 17.291 1.00 49.62 ? 212  HOH C O   1 
HETATM 11495 O  O   . HOH HA 5 .   ? 118.252 -18.299 18.328 1.00 48.64 ? 213  HOH C O   1 
HETATM 11496 O  O   . HOH HA 5 .   ? 116.387 9.368   21.198 1.00 49.53 ? 214  HOH C O   1 
HETATM 11497 O  O   . HOH HA 5 .   ? 110.735 -20.824 10.651 1.00 57.29 ? 215  HOH C O   1 
HETATM 11498 O  O   . HOH HA 5 .   ? 130.067 -16.669 26.112 1.00 54.76 ? 216  HOH C O   1 
HETATM 11499 O  O   . HOH HA 5 .   ? 127.719 5.316   21.754 1.00 39.92 ? 217  HOH C O   1 
HETATM 11500 O  O   . HOH HA 5 .   ? 107.906 8.361   17.789 1.00 49.57 ? 218  HOH C O   1 
HETATM 11501 O  O   . HOH HA 5 .   ? 129.031 -3.697  21.531 1.00 45.28 ? 219  HOH C O   1 
HETATM 11502 O  O   . HOH HA 5 .   ? 115.182 -21.277 2.201  1.00 44.78 ? 220  HOH C O   1 
HETATM 11503 O  O   . HOH HA 5 .   ? 115.563 4.251   31.890 1.00 53.86 ? 221  HOH C O   1 
HETATM 11504 O  O   . HOH HA 5 .   ? 110.754 -3.012  29.532 1.00 47.68 ? 222  HOH C O   1 
HETATM 11505 O  O   . HOH HA 5 .   ? 122.987 -1.805  38.406 1.00 49.24 ? 223  HOH C O   1 
HETATM 11506 O  O   . HOH HA 5 .   ? 133.394 -9.993  -0.582 1.00 39.64 ? 224  HOH C O   1 
HETATM 11507 O  O   . HOH HA 5 .   ? 128.457 -10.663 30.847 1.00 43.38 ? 225  HOH C O   1 
HETATM 11508 O  O   . HOH HA 5 .   ? 125.282 0.750   7.933  1.00 49.99 ? 226  HOH C O   1 
HETATM 11509 O  O   . HOH HA 5 .   ? 106.838 -3.457  6.933  1.00 41.65 ? 227  HOH C O   1 
HETATM 11510 O  O   . HOH HA 5 .   ? 106.006 -2.444  3.007  1.00 59.12 ? 228  HOH C O   1 
HETATM 11511 O  O   . HOH HA 5 .   ? 113.703 -14.023 30.332 1.00 41.67 ? 229  HOH C O   1 
HETATM 11512 O  O   . HOH HA 5 .   ? 106.464 -4.471  4.342  1.00 53.90 ? 230  HOH C O   1 
HETATM 11513 O  O   . HOH HA 5 .   ? 128.034 -12.129 28.642 1.00 62.77 ? 231  HOH C O   1 
HETATM 11514 O  O   . HOH HA 5 .   ? 122.679 4.968   22.645 1.00 40.86 ? 232  HOH C O   1 
HETATM 11515 O  O   . HOH HA 5 .   ? 108.238 -14.744 8.447  1.00 53.93 ? 233  HOH C O   1 
HETATM 11516 O  O   . HOH HA 5 .   ? 105.381 -1.231  7.977  1.00 47.35 ? 234  HOH C O   1 
HETATM 11517 O  O   . HOH HA 5 .   ? 126.902 -2.479  13.769 1.00 49.81 ? 235  HOH C O   1 
HETATM 11518 O  O   . HOH HA 5 .   ? 126.571 -4.322  16.290 1.00 47.36 ? 236  HOH C O   1 
HETATM 11519 O  O   . HOH HA 5 .   ? 118.299 7.369   10.095 1.00 50.35 ? 237  HOH C O   1 
HETATM 11520 O  O   . HOH HA 5 .   ? 128.653 -19.171 10.876 1.00 65.17 ? 238  HOH C O   1 
HETATM 11521 O  O   . HOH HA 5 .   ? 122.994 4.898   15.897 1.00 47.68 ? 239  HOH C O   1 
HETATM 11522 O  O   . HOH HA 5 .   ? 106.572 -8.208  26.774 1.00 43.20 ? 240  HOH C O   1 
HETATM 11523 O  O   . HOH HA 5 .   ? 120.875 -18.430 20.985 1.00 48.09 ? 241  HOH C O   1 
HETATM 11524 O  O   . HOH HA 5 .   ? 116.260 4.107   24.813 1.00 43.71 ? 242  HOH C O   1 
HETATM 11525 O  O   . HOH HA 5 .   ? 131.762 -13.287 11.435 1.00 48.45 ? 243  HOH C O   1 
HETATM 11526 O  O   . HOH HA 5 .   ? 116.424 -1.223  35.613 1.00 52.05 ? 244  HOH C O   1 
HETATM 11527 O  O   . HOH HA 5 .   ? 129.847 -28.736 16.012 1.00 63.14 ? 245  HOH C O   1 
HETATM 11528 O  O   . HOH HA 5 .   ? 127.531 2.711   22.079 1.00 45.11 ? 246  HOH C O   1 
HETATM 11529 O  O   . HOH HA 5 .   ? 127.360 0.220   25.934 1.00 42.62 ? 247  HOH C O   1 
HETATM 11530 O  O   . HOH HA 5 .   ? 121.661 -7.128  36.160 1.00 44.89 ? 248  HOH C O   1 
HETATM 11531 O  O   . HOH HA 5 .   ? 128.984 1.801   18.185 1.00 43.96 ? 249  HOH C O   1 
HETATM 11532 O  O   . HOH HA 5 .   ? 128.295 0.628   20.493 1.00 56.09 ? 250  HOH C O   1 
HETATM 11533 O  O   . HOH HA 5 .   ? 120.753 -10.167 33.350 1.00 43.45 ? 251  HOH C O   1 
HETATM 11534 O  O   . HOH HA 5 .   ? 131.019 -6.823  4.076  1.00 63.52 ? 252  HOH C O   1 
HETATM 11535 O  O   . HOH HA 5 .   ? 115.527 -15.541 31.607 1.00 51.47 ? 253  HOH C O   1 
HETATM 11536 O  O   . HOH HA 5 .   ? 133.495 -9.685  11.623 1.00 48.85 ? 254  HOH C O   1 
HETATM 11537 O  O   . HOH HA 5 .   ? 133.949 -12.172 12.002 1.00 50.86 ? 255  HOH C O   1 
HETATM 11538 O  O   . HOH HA 5 .   ? 124.568 -6.407  35.951 1.00 48.70 ? 256  HOH C O   1 
HETATM 11539 O  O   . HOH HA 5 .   ? 120.762 0.096   -2.234 1.00 52.14 ? 257  HOH C O   1 
HETATM 11540 O  O   . HOH HA 5 .   ? 127.949 -8.877  35.749 1.00 45.66 ? 258  HOH C O   1 
HETATM 11541 O  O   . HOH HA 5 .   ? 124.994 -16.212 5.921  1.00 61.83 ? 259  HOH C O   1 
HETATM 11542 O  O   . HOH HA 5 .   ? 118.473 -20.134 13.729 1.00 51.78 ? 260  HOH C O   1 
HETATM 11543 O  O   . HOH HA 5 .   ? 124.944 -25.248 10.235 1.00 51.09 ? 261  HOH C O   1 
HETATM 11544 O  O   . HOH HA 5 .   ? 134.632 -26.272 12.804 1.00 61.58 ? 262  HOH C O   1 
HETATM 11545 O  O   . HOH HA 5 .   ? 126.144 -14.079 2.307  1.00 62.43 ? 263  HOH C O   1 
HETATM 11546 O  O   . HOH IA 5 .   ? 79.257  -2.090  13.239 1.00 18.64 ? 1401 HOH D O   1 
HETATM 11547 O  O   . HOH IA 5 .   ? 102.221 -9.107  21.317 1.00 22.34 ? 1402 HOH D O   1 
HETATM 11548 O  O   . HOH IA 5 .   ? 72.923  6.407   19.518 1.00 26.13 ? 1403 HOH D O   1 
HETATM 11549 O  O   . HOH IA 5 .   ? 103.494 -5.965  23.100 1.00 31.26 ? 1404 HOH D O   1 
HETATM 11550 O  O   . HOH IA 5 .   ? 83.033  -6.493  17.144 1.00 22.25 ? 1405 HOH D O   1 
HETATM 11551 O  O   . HOH IA 5 .   ? 102.762 -3.148  8.696  1.00 27.81 ? 1406 HOH D O   1 
HETATM 11552 O  O   . HOH IA 5 .   ? 84.714  0.247   16.354 1.00 22.64 ? 1407 HOH D O   1 
HETATM 11553 O  O   . HOH IA 5 .   ? 77.481  10.486  16.548 1.00 21.27 ? 1408 HOH D O   1 
HETATM 11554 O  O   . HOH IA 5 .   ? 96.070  8.942   21.098 1.00 28.29 ? 1409 HOH D O   1 
HETATM 11555 O  O   . HOH IA 5 .   ? 77.566  -15.145 30.919 1.00 38.24 ? 1410 HOH D O   1 
HETATM 11556 O  O   . HOH IA 5 .   ? 96.109  -3.459  2.724  1.00 27.93 ? 1411 HOH D O   1 
HETATM 11557 O  O   . HOH IA 5 .   ? 88.900  3.686   6.769  1.00 24.71 ? 1412 HOH D O   1 
HETATM 11558 O  O   . HOH IA 5 .   ? 77.857  -3.610  28.005 1.00 28.39 ? 1413 HOH D O   1 
HETATM 11559 O  O   . HOH IA 5 .   ? 76.062  2.281   19.749 1.00 32.08 ? 1414 HOH D O   1 
HETATM 11560 O  O   . HOH IA 5 .   ? 96.646  6.150   11.314 1.00 30.44 ? 1415 HOH D O   1 
HETATM 11561 O  O   . HOH IA 5 .   ? 88.139  -12.804 34.228 1.00 29.88 ? 1416 HOH D O   1 
HETATM 11562 O  O   . HOH IA 5 .   ? 72.631  8.644   17.252 1.00 30.19 ? 1417 HOH D O   1 
HETATM 11563 O  O   . HOH IA 5 .   ? 80.556  4.036   25.945 1.00 29.25 ? 1418 HOH D O   1 
HETATM 11564 O  O   . HOH IA 5 .   ? 90.704  4.918   21.736 1.00 29.71 ? 1419 HOH D O   1 
HETATM 11565 O  O   . HOH IA 5 .   ? 91.151  4.741   7.961  1.00 23.30 ? 1420 HOH D O   1 
HETATM 11566 O  O   . HOH IA 5 .   ? 75.309  11.056  15.221 1.00 28.45 ? 1421 HOH D O   1 
HETATM 11567 O  O   . HOH IA 5 .   ? 82.971  14.639  23.278 1.00 25.09 ? 1422 HOH D O   1 
HETATM 11568 O  O   . HOH IA 5 .   ? 84.636  -9.934  6.752  1.00 32.93 ? 1423 HOH D O   1 
HETATM 11569 O  O   . HOH IA 5 .   ? 89.236  5.810   24.102 1.00 26.66 ? 1424 HOH D O   1 
HETATM 11570 O  O   . HOH IA 5 .   ? 88.868  -4.809  34.297 1.00 30.16 ? 1425 HOH D O   1 
HETATM 11571 O  O   . HOH IA 5 .   ? 106.886 -1.204  21.299 1.00 26.09 ? 1426 HOH D O   1 
HETATM 11572 O  O   . HOH IA 5 .   ? 82.674  -13.996 25.569 1.00 26.04 ? 1427 HOH D O   1 
HETATM 11573 O  O   . HOH IA 5 .   ? 103.521 7.215   19.944 1.00 36.09 ? 1428 HOH D O   1 
HETATM 11574 O  O   . HOH IA 5 .   ? 70.560  -0.353  12.263 1.00 45.58 ? 1429 HOH D O   1 
HETATM 11575 O  O   . HOH IA 5 .   ? 79.210  -4.109  14.906 1.00 31.71 ? 1430 HOH D O   1 
HETATM 11576 O  O   . HOH IA 5 .   ? 94.408  4.823   28.886 1.00 36.14 ? 1431 HOH D O   1 
HETATM 11577 O  O   . HOH IA 5 .   ? 81.840  -7.795  15.264 1.00 33.92 ? 1432 HOH D O   1 
HETATM 11578 O  O   . HOH IA 5 .   ? 84.177  -6.836  11.132 1.00 29.00 ? 1433 HOH D O   1 
HETATM 11579 O  O   . HOH IA 5 .   ? 79.732  3.037   28.406 1.00 37.72 ? 1434 HOH D O   1 
HETATM 11580 O  O   . HOH IA 5 .   ? 77.775  2.306   13.708 1.00 25.95 ? 1435 HOH D O   1 
HETATM 11581 O  O   . HOH IA 5 .   ? 77.738  0.241   21.317 1.00 25.51 ? 1436 HOH D O   1 
HETATM 11582 O  O   . HOH IA 5 .   ? 103.303 -5.751  3.143  1.00 43.86 ? 1437 HOH D O   1 
HETATM 11583 O  O   . HOH IA 5 .   ? 77.069  0.607   23.648 1.00 30.78 ? 1438 HOH D O   1 
HETATM 11584 O  O   . HOH IA 5 .   ? 79.962  -6.334  13.513 1.00 33.79 ? 1439 HOH D O   1 
HETATM 11585 O  O   . HOH IA 5 .   ? 83.387  13.583  25.832 1.00 31.98 ? 1440 HOH D O   1 
HETATM 11586 O  O   . HOH IA 5 .   ? 72.734  4.067   20.341 1.00 37.82 ? 1441 HOH D O   1 
HETATM 11587 O  O   . HOH IA 5 .   ? 91.051  7.585   17.621 1.00 27.25 ? 1442 HOH D O   1 
HETATM 11588 O  O   . HOH IA 5 .   ? 74.844  8.833   13.490 1.00 27.86 ? 1443 HOH D O   1 
HETATM 11589 O  O   . HOH IA 5 .   ? 75.266  3.449   21.908 1.00 40.74 ? 1444 HOH D O   1 
HETATM 11590 O  O   . HOH IA 5 .   ? 98.306  -16.606 16.071 1.00 35.19 ? 1445 HOH D O   1 
HETATM 11591 O  O   . HOH IA 5 .   ? 92.277  6.702   20.244 1.00 28.32 ? 1446 HOH D O   1 
HETATM 11592 O  O   . HOH IA 5 .   ? 78.090  -10.246 29.237 1.00 39.86 ? 1447 HOH D O   1 
HETATM 11593 O  O   . HOH IA 5 .   ? 98.561  -18.042 19.824 1.00 32.24 ? 1448 HOH D O   1 
HETATM 11594 O  O   . HOH IA 5 .   ? 95.827  6.327   27.134 1.00 45.99 ? 1449 HOH D O   1 
HETATM 11595 O  O   . HOH IA 5 .   ? 70.699  3.121   13.895 1.00 33.22 ? 1450 HOH D O   1 
HETATM 11596 O  O   . HOH IA 5 .   ? 87.080  -4.193  32.473 1.00 26.55 ? 1451 HOH D O   1 
HETATM 11597 O  O   . HOH IA 5 .   ? 76.895  -0.251  26.479 1.00 33.63 ? 1452 HOH D O   1 
HETATM 11598 O  O   . HOH IA 5 .   ? 82.707  -10.114 13.000 1.00 26.65 ? 1453 HOH D O   1 
HETATM 11599 O  O   . HOH IA 5 .   ? 97.051  -14.048 3.097  1.00 37.93 ? 1454 HOH D O   1 
HETATM 11600 O  O   . HOH IA 5 .   ? 85.432  1.097   5.427  1.00 40.51 ? 1455 HOH D O   1 
HETATM 11601 O  O   . HOH IA 5 .   ? 104.527 -18.114 15.532 1.00 38.99 ? 1456 HOH D O   1 
HETATM 11602 O  O   . HOH IA 5 .   ? 91.205  -14.420 3.842  1.00 38.31 ? 1457 HOH D O   1 
HETATM 11603 O  O   . HOH IA 5 .   ? 102.659 -5.892  6.812  1.00 29.57 ? 1458 HOH D O   1 
HETATM 11604 O  O   . HOH IA 5 .   ? 93.619  -11.482 35.498 1.00 31.46 ? 1459 HOH D O   1 
HETATM 11605 O  O   . HOH IA 5 .   ? 105.383 6.200   18.385 1.00 37.94 ? 1460 HOH D O   1 
HETATM 11606 O  O   . HOH IA 5 .   ? 87.191  -17.351 20.712 1.00 37.65 ? 1461 HOH D O   1 
HETATM 11607 O  O   . HOH IA 5 .   ? 101.344 5.204   10.833 1.00 33.48 ? 1462 HOH D O   1 
HETATM 11608 O  O   . HOH IA 5 .   ? 92.308  6.213   24.717 1.00 39.39 ? 1463 HOH D O   1 
HETATM 11609 O  O   . HOH IA 5 .   ? 82.625  6.385   3.944  1.00 42.84 ? 1464 HOH D O   1 
HETATM 11610 O  O   . HOH IA 5 .   ? 101.292 1.015   23.346 1.00 34.24 ? 1465 HOH D O   1 
HETATM 11611 O  O   . HOH IA 5 .   ? 82.665  -16.270 27.079 1.00 31.46 ? 1466 HOH D O   1 
HETATM 11612 O  O   . HOH IA 5 .   ? 75.737  -7.384  8.912  1.00 48.74 ? 1467 HOH D O   1 
HETATM 11613 O  O   . HOH IA 5 .   ? 94.307  -4.136  33.021 1.00 43.13 ? 1468 HOH D O   1 
HETATM 11614 O  O   . HOH IA 5 .   ? 93.512  -17.158 23.238 1.00 41.66 ? 1469 HOH D O   1 
HETATM 11615 O  O   . HOH IA 5 .   ? 88.557  10.444  13.673 1.00 38.53 ? 1470 HOH D O   1 
HETATM 11616 O  O   . HOH IA 5 .   ? 90.771  -15.747 6.756  1.00 39.84 ? 1471 HOH D O   1 
HETATM 11617 O  O   . HOH IA 5 .   ? 76.636  2.524   7.841  1.00 45.18 ? 1472 HOH D O   1 
HETATM 11618 O  O   . HOH IA 5 .   ? 80.968  -2.248  29.311 1.00 38.63 ? 1473 HOH D O   1 
HETATM 11619 O  O   . HOH IA 5 .   ? 77.748  1.944   5.559  1.00 43.91 ? 1474 HOH D O   1 
HETATM 11620 O  O   . HOH IA 5 .   ? 78.973  4.524   6.843  1.00 42.50 ? 1475 HOH D O   1 
HETATM 11621 O  O   . HOH IA 5 .   ? 88.109  1.887   5.132  1.00 36.62 ? 1476 HOH D O   1 
HETATM 11622 O  O   . HOH IA 5 .   ? 101.768 -1.290  22.360 1.00 34.76 ? 1477 HOH D O   1 
HETATM 11623 O  O   . HOH IA 5 .   ? 96.297  -1.196  32.197 1.00 44.10 ? 1478 HOH D O   1 
HETATM 11624 O  O   . HOH IA 5 .   ? 81.338  -11.786 16.384 1.00 44.70 ? 1479 HOH D O   1 
HETATM 11625 O  O   . HOH IA 5 .   ? 102.663 -3.784  4.944  1.00 46.72 ? 1480 HOH D O   1 
HETATM 11626 O  O   . HOH IA 5 .   ? 97.029  -17.256 13.741 1.00 44.67 ? 1481 HOH D O   1 
HETATM 11627 O  O   . HOH IA 5 .   ? 77.247  7.878   12.769 1.00 44.87 ? 1482 HOH D O   1 
HETATM 11628 O  O   . HOH IA 5 .   ? 83.988  -12.384 6.328  1.00 51.62 ? 1483 HOH D O   1 
HETATM 11629 O  O   . HOH IA 5 .   ? 83.292  -1.181  6.009  1.00 40.78 ? 1484 HOH D O   1 
HETATM 11630 O  O   . HOH IA 5 .   ? 91.467  -7.820  4.149  1.00 36.69 ? 1485 HOH D O   1 
HETATM 11631 O  O   . HOH IA 5 .   ? 95.802  -6.792  1.659  1.00 38.47 ? 1486 HOH D O   1 
HETATM 11632 O  O   . HOH IA 5 .   ? 84.546  -5.981  7.434  1.00 35.82 ? 1487 HOH D O   1 
HETATM 11633 O  O   . HOH IA 5 .   ? 96.080  8.636   12.007 1.00 50.05 ? 1488 HOH D O   1 
HETATM 11634 O  O   . HOH IA 5 .   ? 102.436 -3.729  24.050 1.00 41.39 ? 1489 HOH D O   1 
HETATM 11635 O  O   . HOH IA 5 .   ? 75.214  -7.706  12.883 1.00 44.65 ? 1490 HOH D O   1 
HETATM 11636 O  O   . HOH IA 5 .   ? 84.716  16.529  23.649 1.00 36.67 ? 1491 HOH D O   1 
HETATM 11637 O  O   . HOH IA 5 .   ? 94.145  -0.462  34.061 1.00 50.51 ? 1492 HOH D O   1 
HETATM 11638 O  O   . HOH IA 5 .   ? 100.005 -0.505  7.568  1.00 44.90 ? 1493 HOH D O   1 
HETATM 11639 O  O   . HOH IA 5 .   ? 73.629  1.930   18.868 1.00 49.95 ? 1494 HOH D O   1 
HETATM 11640 O  O   . HOH IA 5 .   ? 104.394 -8.599  22.961 1.00 53.50 ? 1495 HOH D O   1 
HETATM 11641 O  O   . HOH IA 5 .   ? 86.791  14.767  21.906 1.00 50.24 ? 1496 HOH D O   1 
HETATM 11642 O  O   . HOH IA 5 .   ? 102.571 4.001   9.062  1.00 53.68 ? 1497 HOH D O   1 
HETATM 11643 O  O   . HOH IA 5 .   ? 89.272  -7.829  2.200  1.00 34.76 ? 1498 HOH D O   1 
HETATM 11644 O  O   . HOH IA 5 .   ? 87.134  -15.690 13.923 1.00 37.10 ? 1499 HOH D O   1 
HETATM 11645 O  O   . HOH IA 5 .   ? 99.225  2.634   5.583  1.00 39.57 ? 1500 HOH D O   1 
HETATM 11646 O  O   . HOH IA 5 .   ? 102.353 -7.783  25.294 1.00 39.93 ? 1501 HOH D O   1 
HETATM 11647 O  O   . HOH IA 5 .   ? 98.713  10.017  14.124 1.00 42.80 ? 1502 HOH D O   1 
HETATM 11648 O  O   . HOH IA 5 .   ? 98.714  -12.086 28.418 1.00 39.13 ? 1503 HOH D O   1 
HETATM 11649 O  O   . HOH IA 5 .   ? 78.327  5.851   8.832  1.00 42.59 ? 1504 HOH D O   1 
HETATM 11650 O  O   . HOH IA 5 .   ? 105.593 -4.771  26.160 1.00 44.75 ? 1505 HOH D O   1 
HETATM 11651 O  O   . HOH IA 5 .   ? 101.414 -3.957  26.613 1.00 35.59 ? 1506 HOH D O   1 
HETATM 11652 O  O   . HOH IA 5 .   ? 90.968  10.211  15.945 1.00 45.13 ? 1507 HOH D O   1 
HETATM 11653 O  O   . HOH IA 5 .   ? 99.556  0.165   29.646 1.00 41.98 ? 1508 HOH D O   1 
HETATM 11654 O  O   . HOH IA 5 .   ? 79.710  -17.650 30.098 1.00 57.99 ? 1509 HOH D O   1 
HETATM 11655 O  O   . HOH IA 5 .   ? 88.627  -17.216 5.387  1.00 48.34 ? 1510 HOH D O   1 
HETATM 11656 O  O   . HOH IA 5 .   ? 91.314  -16.015 28.963 1.00 47.53 ? 1511 HOH D O   1 
HETATM 11657 O  O   . HOH IA 5 .   ? 91.016  -19.069 22.809 1.00 50.93 ? 1512 HOH D O   1 
HETATM 11658 O  O   . HOH IA 5 .   ? 97.239  1.128   30.123 1.00 51.91 ? 1513 HOH D O   1 
HETATM 11659 O  O   . HOH IA 5 .   ? 80.588  6.202   11.022 1.00 49.88 ? 1514 HOH D O   1 
HETATM 11660 O  O   . HOH IA 5 .   ? 74.613  -2.497  12.560 1.00 59.95 ? 1515 HOH D O   1 
HETATM 11661 O  O   . HOH IA 5 .   ? 84.541  9.882   3.856  1.00 46.02 ? 1516 HOH D O   1 
HETATM 11662 O  O   . HOH IA 5 .   ? 93.335  8.292   14.100 1.00 44.31 ? 1517 HOH D O   1 
HETATM 11663 O  O   . HOH IA 5 .   ? 80.174  5.152   30.206 1.00 53.59 ? 1518 HOH D O   1 
HETATM 11664 O  O   . HOH IA 5 .   ? 91.078  -17.968 8.635  1.00 49.44 ? 1519 HOH D O   1 
HETATM 11665 O  O   . HOH IA 5 .   ? 103.321 -5.707  27.030 1.00 47.36 ? 1520 HOH D O   1 
HETATM 11666 O  O   . HOH IA 5 .   ? 77.375  2.140   27.868 1.00 57.36 ? 1521 HOH D O   1 
HETATM 11667 O  O   . HOH IA 5 .   ? 99.537  3.918   29.420 1.00 49.32 ? 1522 HOH D O   1 
HETATM 11668 O  O   . HOH IA 5 .   ? 101.318 -1.992  28.930 1.00 42.42 ? 1523 HOH D O   1 
HETATM 11669 O  O   . HOH IA 5 .   ? 78.045  6.523   29.846 1.00 52.48 ? 1524 HOH D O   1 
HETATM 11670 O  O   . HOH IA 5 .   ? 82.150  20.984  18.146 1.00 48.85 ? 1525 HOH D O   1 
HETATM 11671 O  O   . HOH IA 5 .   ? 88.196  -18.692 27.330 1.00 51.82 ? 1526 HOH D O   1 
HETATM 11672 O  O   . HOH IA 5 .   ? 88.073  -18.406 23.117 1.00 48.46 ? 1527 HOH D O   1 
HETATM 11673 O  O   . HOH IA 5 .   ? 89.370  -15.853 2.122  1.00 52.33 ? 1528 HOH D O   1 
HETATM 11674 O  O   . HOH IA 5 .   ? 101.513 10.540  12.456 1.00 49.04 ? 1529 HOH D O   1 
HETATM 11675 O  O   . HOH IA 5 .   ? 81.468  -6.542  10.771 1.00 41.33 ? 1530 HOH D O   1 
HETATM 11676 O  O   . HOH IA 5 .   ? 82.818  -3.564  6.936  1.00 47.52 ? 1531 HOH D O   1 
HETATM 11677 O  O   . HOH IA 5 .   ? 97.880  -6.433  -0.060 1.00 51.46 ? 1532 HOH D O   1 
HETATM 11678 O  O   . HOH IA 5 .   ? 92.096  8.685   24.152 1.00 49.47 ? 1533 HOH D O   1 
HETATM 11679 O  O   . HOH IA 5 .   ? 104.067 2.346   7.719  1.00 49.34 ? 1534 HOH D O   1 
HETATM 11680 O  O   . HOH IA 5 .   ? 80.539  0.751   29.035 1.00 45.38 ? 1535 HOH D O   1 
HETATM 11681 O  O   . HOH IA 5 .   ? 92.748  8.932   21.572 1.00 48.24 ? 1536 HOH D O   1 
HETATM 11682 O  O   . HOH IA 5 .   ? 96.921  3.465   28.740 1.00 59.06 ? 1537 HOH D O   1 
HETATM 11683 O  O   . HOH IA 5 .   ? 80.631  -6.240  8.350  1.00 58.20 ? 1538 HOH D O   1 
HETATM 11684 O  O   . HOH IA 5 .   ? 75.838  -4.830  26.854 1.00 40.82 ? 1539 HOH D O   1 
HETATM 11685 O  O   . HOH IA 5 .   ? 77.180  8.172   9.092  1.00 57.39 ? 1540 HOH D O   1 
HETATM 11686 O  O   . HOH IA 5 .   ? 88.406  8.108   2.219  1.00 56.90 ? 1541 HOH D O   1 
HETATM 11687 O  O   . HOH IA 5 .   ? 103.483 9.036   11.663 1.00 52.85 ? 1542 HOH D O   1 
HETATM 11688 O  O   . HOH IA 5 .   ? 94.031  2.289   32.107 1.00 57.47 ? 1543 HOH D O   1 
HETATM 11689 O  O   . HOH IA 5 .   ? 83.445  23.285  17.455 1.00 59.24 ? 1544 HOH D O   1 
HETATM 11690 O  O   . HOH IA 5 .   ? 93.478  -4.487  1.841  1.00 54.03 ? 1545 HOH D O   1 
HETATM 11691 O  O   . HOH IA 5 .   ? 95.306  9.597   9.250  1.00 46.20 ? 1546 HOH D O   1 
HETATM 11692 O  O   . HOH IA 5 .   ? 94.414  -9.168  -3.257 1.00 58.83 ? 1547 HOH D O   1 
HETATM 11693 O  O   . HOH IA 5 .   ? 74.588  -1.658  26.332 1.00 47.97 ? 1548 HOH D O   1 
HETATM 11694 O  O   . HOH IA 5 .   ? 80.920  -3.451  31.561 1.00 40.34 ? 1549 HOH D O   1 
HETATM 11695 O  O   . HOH IA 5 .   ? 81.674  14.492  9.758  1.00 52.42 ? 1550 HOH D O   1 
HETATM 11696 O  O   . HOH IA 5 .   ? 98.372  6.158   8.729  1.00 47.33 ? 1551 HOH D O   1 
HETATM 11697 O  O   . HOH IA 5 .   ? 81.864  11.343  27.107 1.00 42.10 ? 1552 HOH D O   1 
HETATM 11698 O  O   . HOH IA 5 .   ? 84.315  21.274  22.658 1.00 57.95 ? 1553 HOH D O   1 
HETATM 11699 O  O   . HOH IA 5 .   ? 91.264  10.865  19.947 1.00 43.05 ? 1554 HOH D O   1 
HETATM 11700 O  O   . HOH IA 5 .   ? 79.716  6.662   4.619  1.00 56.91 ? 1555 HOH D O   1 
HETATM 11701 O  O   . HOH IA 5 .   ? 73.402  2.401   8.179  1.00 55.11 ? 1556 HOH D O   1 
HETATM 11702 O  O   . HOH IA 5 .   ? 75.856  -7.328  27.881 1.00 54.75 ? 1557 HOH D O   1 
HETATM 11703 O  O   . HOH IA 5 .   ? 102.015 -15.648 8.852  1.00 40.01 ? 1558 HOH D O   1 
HETATM 11704 O  O   . HOH IA 5 .   ? 100.824 2.721   31.313 1.00 57.07 ? 1559 HOH D O   1 
HETATM 11705 O  O   . HOH IA 5 .   ? 86.362  -18.409 16.514 1.00 49.69 ? 1560 HOH D O   1 
HETATM 11706 O  O   . HOH IA 5 .   ? 79.758  -4.351  34.041 1.00 43.70 ? 1561 HOH D O   1 
HETATM 11707 O  O   . HOH IA 5 .   ? 82.697  -12.666 38.688 1.00 56.49 ? 1562 HOH D O   1 
HETATM 11708 O  O   . HOH IA 5 .   ? 86.146  -1.661  32.587 1.00 37.47 ? 1563 HOH D O   1 
HETATM 11709 O  O   . HOH IA 5 .   ? 103.630 -10.456 31.852 1.00 62.24 ? 1564 HOH D O   1 
HETATM 11710 O  O   . HOH IA 5 .   ? 104.547 -14.136 6.844  1.00 57.63 ? 1565 HOH D O   1 
HETATM 11711 O  O   . HOH IA 5 .   ? 80.870  -10.254 36.659 1.00 46.06 ? 1566 HOH D O   1 
HETATM 11712 O  O   . HOH IA 5 .   ? 94.776  0.709   0.122  1.00 47.87 ? 1567 HOH D O   1 
HETATM 11713 O  O   . HOH IA 5 .   ? 102.449 -1.213  7.123  1.00 55.41 ? 1568 HOH D O   1 
HETATM 11714 O  O   . HOH IA 5 .   ? 85.962  7.960   26.320 1.00 44.45 ? 1569 HOH D O   1 
HETATM 11715 O  O   . HOH IA 5 .   ? 91.467  -2.534  3.592  1.00 38.42 ? 1570 HOH D O   1 
HETATM 11716 O  O   . HOH JA 5 .   ? 51.194  -26.227 22.438 1.00 22.31 ? 156  HOH E O   1 
HETATM 11717 O  O   . HOH JA 5 .   ? 52.789  -28.883 21.274 1.00 19.35 ? 157  HOH E O   1 
HETATM 11718 O  O   . HOH JA 5 .   ? 37.077  -39.540 14.045 1.00 25.41 ? 158  HOH E O   1 
HETATM 11719 O  O   . HOH JA 5 .   ? 34.016  -30.342 14.209 1.00 22.69 ? 159  HOH E O   1 
HETATM 11720 O  O   . HOH JA 5 .   ? 48.321  -20.799 20.253 1.00 24.78 ? 160  HOH E O   1 
HETATM 11721 O  O   . HOH JA 5 .   ? 38.817  -26.685 8.564  1.00 25.40 ? 161  HOH E O   1 
HETATM 11722 O  O   . HOH JA 5 .   ? 38.030  -32.244 5.194  1.00 23.97 ? 162  HOH E O   1 
HETATM 11723 O  O   . HOH JA 5 .   ? 39.488  -38.809 31.237 1.00 26.41 ? 163  HOH E O   1 
HETATM 11724 O  O   . HOH JA 5 .   ? 49.206  -39.097 4.201  1.00 26.15 ? 164  HOH E O   1 
HETATM 11725 O  O   . HOH JA 5 .   ? 36.924  -45.519 11.295 1.00 26.22 ? 165  HOH E O   1 
HETATM 11726 O  O   . HOH JA 5 .   ? 30.380  -33.036 21.624 1.00 36.60 ? 166  HOH E O   1 
HETATM 11727 O  O   . HOH JA 5 .   ? 58.267  -36.104 17.167 1.00 26.60 ? 167  HOH E O   1 
HETATM 11728 O  O   . HOH JA 5 .   ? 34.983  -46.859 26.221 1.00 33.07 ? 168  HOH E O   1 
HETATM 11729 O  O   . HOH JA 5 .   ? 41.915  -44.270 16.066 1.00 33.18 ? 169  HOH E O   1 
HETATM 11730 O  O   . HOH JA 5 .   ? 35.956  -28.036 26.012 1.00 32.22 ? 170  HOH E O   1 
HETATM 11731 O  O   . HOH JA 5 .   ? 41.834  -18.374 16.057 1.00 26.94 ? 171  HOH E O   1 
HETATM 11732 O  O   . HOH JA 5 .   ? 55.413  -34.325 4.361  1.00 34.97 ? 172  HOH E O   1 
HETATM 11733 O  O   . HOH JA 5 .   ? 40.989  -37.373 33.191 1.00 26.09 ? 173  HOH E O   1 
HETATM 11734 O  O   . HOH JA 5 .   ? 34.508  -25.246 17.742 1.00 29.81 ? 174  HOH E O   1 
HETATM 11735 O  O   . HOH JA 5 .   ? 43.907  -43.798 10.333 1.00 25.18 ? 175  HOH E O   1 
HETATM 11736 O  O   . HOH JA 5 .   ? 48.536  -31.578 1.978  1.00 27.33 ? 176  HOH E O   1 
HETATM 11737 O  O   . HOH JA 5 .   ? 43.194  -32.297 31.675 1.00 29.55 ? 177  HOH E O   1 
HETATM 11738 O  O   . HOH JA 5 .   ? 24.498  -40.642 12.615 1.00 29.91 ? 178  HOH E O   1 
HETATM 11739 O  O   . HOH JA 5 .   ? 30.933  -31.243 9.832  1.00 31.78 ? 179  HOH E O   1 
HETATM 11740 O  O   . HOH JA 5 .   ? 30.346  -40.776 22.913 1.00 28.10 ? 180  HOH E O   1 
HETATM 11741 O  O   . HOH JA 5 .   ? 39.752  -19.676 17.215 1.00 32.20 ? 181  HOH E O   1 
HETATM 11742 O  O   . HOH JA 5 .   ? 51.333  -40.112 -5.094 1.00 30.74 ? 182  HOH E O   1 
HETATM 11743 O  O   . HOH JA 5 .   ? 26.815  -41.588 20.297 1.00 27.53 ? 183  HOH E O   1 
HETATM 11744 O  O   . HOH JA 5 .   ? 46.696  -48.001 25.567 1.00 27.21 ? 184  HOH E O   1 
HETATM 11745 O  O   . HOH JA 5 .   ? 45.282  -46.482 12.410 1.00 34.61 ? 185  HOH E O   1 
HETATM 11746 O  O   . HOH JA 5 .   ? 38.659  -46.520 13.319 1.00 42.50 ? 186  HOH E O   1 
HETATM 11747 O  O   . HOH JA 5 .   ? 47.004  -31.127 31.763 1.00 35.52 ? 187  HOH E O   1 
HETATM 11748 O  O   . HOH JA 5 .   ? 32.899  -42.429 26.540 1.00 41.48 ? 188  HOH E O   1 
HETATM 11749 O  O   . HOH JA 5 .   ? 30.713  -42.073 25.415 1.00 37.15 ? 189  HOH E O   1 
HETATM 11750 O  O   . HOH JA 5 .   ? 42.311  -22.827 8.321  1.00 35.48 ? 190  HOH E O   1 
HETATM 11751 O  O   . HOH JA 5 .   ? 55.126  -41.711 4.448  1.00 28.61 ? 191  HOH E O   1 
HETATM 11752 O  O   . HOH JA 5 .   ? 50.333  -25.809 8.008  1.00 25.02 ? 192  HOH E O   1 
HETATM 11753 O  O   . HOH JA 5 .   ? 59.062  -36.418 21.359 1.00 35.81 ? 193  HOH E O   1 
HETATM 11754 O  O   . HOH JA 5 .   ? 48.026  -41.675 34.590 1.00 31.90 ? 194  HOH E O   1 
HETATM 11755 O  O   . HOH JA 5 .   ? 35.099  -31.561 18.872 1.00 35.25 ? 195  HOH E O   1 
HETATM 11756 O  O   . HOH JA 5 .   ? 50.000  -41.117 -2.545 1.00 35.31 ? 196  HOH E O   1 
HETATM 11757 O  O   . HOH JA 5 .   ? 52.835  -27.420 6.501  1.00 28.22 ? 197  HOH E O   1 
HETATM 11758 O  O   . HOH JA 5 .   ? 32.920  -45.322 18.877 1.00 31.33 ? 198  HOH E O   1 
HETATM 11759 O  O   . HOH JA 5 .   ? 43.879  -43.350 6.366  1.00 34.11 ? 199  HOH E O   1 
HETATM 11760 O  O   . HOH JA 5 .   ? 33.264  -45.041 3.422  1.00 45.89 ? 200  HOH E O   1 
HETATM 11761 O  O   . HOH JA 5 .   ? 30.596  -45.747 16.682 1.00 33.46 ? 201  HOH E O   1 
HETATM 11762 O  O   . HOH JA 5 .   ? 62.808  -34.815 17.025 1.00 47.56 ? 202  HOH E O   1 
HETATM 11763 O  O   . HOH JA 5 .   ? 36.900  -38.557 30.544 1.00 28.63 ? 203  HOH E O   1 
HETATM 11764 O  O   . HOH JA 5 .   ? 36.183  -22.587 10.905 1.00 37.43 ? 204  HOH E O   1 
HETATM 11765 O  O   . HOH JA 5 .   ? 38.100  -34.838 4.266  1.00 34.12 ? 205  HOH E O   1 
HETATM 11766 O  O   . HOH JA 5 .   ? 42.206  -25.799 27.738 1.00 36.82 ? 206  HOH E O   1 
HETATM 11767 O  O   . HOH JA 5 .   ? 31.805  -45.599 21.084 1.00 33.59 ? 207  HOH E O   1 
HETATM 11768 O  O   . HOH JA 5 .   ? 39.341  -36.982 3.168  1.00 34.38 ? 208  HOH E O   1 
HETATM 11769 O  O   . HOH JA 5 .   ? 44.557  -22.622 6.595  1.00 45.36 ? 209  HOH E O   1 
HETATM 11770 O  O   . HOH JA 5 .   ? 57.514  -36.304 4.196  1.00 35.91 ? 210  HOH E O   1 
HETATM 11771 O  O   . HOH JA 5 .   ? 46.278  -25.380 20.876 1.00 33.85 ? 211  HOH E O   1 
HETATM 11772 O  O   . HOH JA 5 .   ? 52.589  -45.768 21.497 1.00 36.50 ? 212  HOH E O   1 
HETATM 11773 O  O   . HOH JA 5 .   ? 55.346  -27.008 7.387  1.00 41.04 ? 213  HOH E O   1 
HETATM 11774 O  O   . HOH JA 5 .   ? 39.810  -51.558 11.716 1.00 34.73 ? 214  HOH E O   1 
HETATM 11775 O  O   . HOH JA 5 .   ? 20.106  -33.291 16.169 1.00 32.30 ? 215  HOH E O   1 
HETATM 11776 O  O   . HOH JA 5 .   ? 60.828  -32.606 10.467 1.00 35.54 ? 216  HOH E O   1 
HETATM 11777 O  O   . HOH JA 5 .   ? 34.768  -47.190 18.070 1.00 37.06 ? 217  HOH E O   1 
HETATM 11778 O  O   . HOH JA 5 .   ? 35.465  -24.296 20.288 1.00 34.46 ? 218  HOH E O   1 
HETATM 11779 O  O   . HOH JA 5 .   ? 50.554  -42.671 34.413 1.00 30.94 ? 219  HOH E O   1 
HETATM 11780 O  O   . HOH JA 5 .   ? 46.900  -26.819 6.091  1.00 33.43 ? 220  HOH E O   1 
HETATM 11781 O  O   . HOH JA 5 .   ? 54.900  -31.048 -0.382 1.00 48.41 ? 221  HOH E O   1 
HETATM 11782 O  O   . HOH JA 5 .   ? 48.015  -25.635 22.902 1.00 36.58 ? 222  HOH E O   1 
HETATM 11783 O  O   . HOH JA 5 .   ? 53.560  -45.415 24.000 1.00 45.42 ? 223  HOH E O   1 
HETATM 11784 O  O   . HOH JA 5 .   ? 43.817  -24.718 21.648 1.00 30.06 ? 224  HOH E O   1 
HETATM 11785 O  O   . HOH JA 5 .   ? 32.157  -44.507 11.025 1.00 32.97 ? 225  HOH E O   1 
HETATM 11786 O  O   . HOH JA 5 .   ? 25.088  -46.599 15.721 1.00 34.32 ? 226  HOH E O   1 
HETATM 11787 O  O   . HOH JA 5 .   ? 42.163  -44.531 34.721 1.00 40.19 ? 227  HOH E O   1 
HETATM 11788 O  O   . HOH JA 5 .   ? 36.007  -26.476 24.238 1.00 50.69 ? 228  HOH E O   1 
HETATM 11789 O  O   . HOH JA 5 .   ? 43.291  -32.843 2.005  1.00 39.95 ? 229  HOH E O   1 
HETATM 11790 O  O   . HOH JA 5 .   ? 48.808  -25.357 5.893  1.00 35.61 ? 230  HOH E O   1 
HETATM 11791 O  O   . HOH JA 5 .   ? 33.454  -32.349 21.140 1.00 36.28 ? 231  HOH E O   1 
HETATM 11792 O  O   . HOH JA 5 .   ? 50.902  -27.833 25.092 1.00 36.95 ? 232  HOH E O   1 
HETATM 11793 O  O   . HOH JA 5 .   ? 33.083  -45.340 25.737 1.00 53.68 ? 233  HOH E O   1 
HETATM 11794 O  O   . HOH JA 5 .   ? 49.777  -42.691 1.493  1.00 48.09 ? 234  HOH E O   1 
HETATM 11795 O  O   . HOH JA 5 .   ? 45.093  -25.634 27.314 1.00 43.86 ? 235  HOH E O   1 
HETATM 11796 O  O   . HOH JA 5 .   ? 34.453  -29.785 21.649 1.00 39.08 ? 236  HOH E O   1 
HETATM 11797 O  O   . HOH JA 5 .   ? 53.526  -29.240 -1.328 1.00 40.09 ? 237  HOH E O   1 
HETATM 11798 O  O   . HOH JA 5 .   ? 24.055  -46.387 13.373 1.00 42.78 ? 238  HOH E O   1 
HETATM 11799 O  O   . HOH JA 5 .   ? 35.439  -49.475 19.681 1.00 37.31 ? 239  HOH E O   1 
HETATM 11800 O  O   . HOH JA 5 .   ? 42.146  -51.945 30.797 1.00 60.94 ? 240  HOH E O   1 
HETATM 11801 O  O   . HOH JA 5 .   ? 57.619  -39.870 22.957 1.00 44.67 ? 241  HOH E O   1 
HETATM 11802 O  O   . HOH JA 5 .   ? 58.886  -36.981 0.147  1.00 43.32 ? 242  HOH E O   1 
HETATM 11803 O  O   . HOH JA 5 .   ? 52.573  -42.916 32.440 1.00 37.52 ? 243  HOH E O   1 
HETATM 11804 O  O   . HOH JA 5 .   ? 46.078  -18.255 27.263 1.00 55.38 ? 244  HOH E O   1 
HETATM 11805 O  O   . HOH JA 5 .   ? 40.847  -33.983 32.713 1.00 40.77 ? 245  HOH E O   1 
HETATM 11806 O  O   . HOH JA 5 .   ? 53.248  -24.500 27.283 1.00 42.54 ? 246  HOH E O   1 
HETATM 11807 O  O   . HOH JA 5 .   ? 30.832  -40.354 7.885  1.00 36.18 ? 247  HOH E O   1 
HETATM 11808 O  O   . HOH JA 5 .   ? 31.786  -43.068 3.856  1.00 43.21 ? 248  HOH E O   1 
HETATM 11809 O  O   . HOH JA 5 .   ? 25.751  -46.292 11.377 1.00 42.19 ? 249  HOH E O   1 
HETATM 11810 O  O   . HOH JA 5 .   ? 32.983  -27.525 17.798 1.00 42.39 ? 250  HOH E O   1 
HETATM 11811 O  O   . HOH JA 5 .   ? 62.151  -37.855 5.665  1.00 44.00 ? 251  HOH E O   1 
HETATM 11812 O  O   . HOH JA 5 .   ? 45.223  -33.176 3.781  1.00 56.11 ? 252  HOH E O   1 
HETATM 11813 O  O   . HOH JA 5 .   ? 56.975  -31.701 0.883  1.00 46.43 ? 253  HOH E O   1 
HETATM 11814 O  O   . HOH JA 5 .   ? 41.292  -43.433 4.928  1.00 46.17 ? 254  HOH E O   1 
HETATM 11815 O  O   . HOH JA 5 .   ? 49.573  -22.798 25.894 1.00 48.44 ? 255  HOH E O   1 
HETATM 11816 O  O   . HOH JA 5 .   ? 39.277  -44.912 35.081 1.00 48.70 ? 256  HOH E O   1 
HETATM 11817 O  O   . HOH JA 5 .   ? 34.472  -26.101 22.317 1.00 40.20 ? 257  HOH E O   1 
HETATM 11818 O  O   . HOH JA 5 .   ? 41.194  -29.506 30.301 1.00 35.28 ? 258  HOH E O   1 
HETATM 11819 O  O   . HOH JA 5 .   ? 59.190  -37.951 23.869 1.00 51.40 ? 259  HOH E O   1 
HETATM 11820 O  O   . HOH JA 5 .   ? 34.917  -28.809 10.938 1.00 33.82 ? 260  HOH E O   1 
HETATM 11821 O  O   . HOH JA 5 .   ? 42.344  -50.044 11.900 1.00 51.18 ? 261  HOH E O   1 
HETATM 11822 O  O   . HOH JA 5 .   ? 34.962  -34.020 18.964 1.00 47.61 ? 262  HOH E O   1 
HETATM 11823 O  O   . HOH JA 5 .   ? 39.991  -25.550 6.351  1.00 45.94 ? 263  HOH E O   1 
HETATM 11824 O  O   . HOH JA 5 .   ? 47.470  -41.717 -2.153 1.00 39.88 ? 264  HOH E O   1 
HETATM 11825 O  O   . HOH JA 5 .   ? 54.030  -27.005 3.061  1.00 54.27 ? 265  HOH E O   1 
HETATM 11826 O  O   . HOH JA 5 .   ? 55.734  -42.508 7.605  1.00 40.75 ? 266  HOH E O   1 
HETATM 11827 O  O   . HOH JA 5 .   ? 41.027  -50.150 28.280 1.00 37.40 ? 267  HOH E O   1 
HETATM 11828 O  O   . HOH JA 5 .   ? 51.741  -26.384 4.125  1.00 46.76 ? 268  HOH E O   1 
HETATM 11829 O  O   . HOH JA 5 .   ? 47.387  -26.611 25.599 1.00 37.91 ? 269  HOH E O   1 
HETATM 11830 O  O   . HOH JA 5 .   ? 42.790  -46.114 14.313 1.00 38.67 ? 270  HOH E O   1 
HETATM 11831 O  O   . HOH JA 5 .   ? 45.294  -27.718 37.383 1.00 42.55 ? 271  HOH E O   1 
HETATM 11832 O  O   . HOH JA 5 .   ? 55.168  -39.957 24.022 1.00 39.59 ? 272  HOH E O   1 
HETATM 11833 O  O   . HOH JA 5 .   ? 30.604  -28.203 16.247 1.00 54.06 ? 273  HOH E O   1 
HETATM 11834 O  O   . HOH JA 5 .   ? 31.266  -49.120 10.211 1.00 54.88 ? 274  HOH E O   1 
HETATM 11835 O  O   . HOH JA 5 .   ? 47.248  -45.244 6.316  1.00 38.07 ? 275  HOH E O   1 
HETATM 11836 O  O   . HOH JA 5 .   ? 46.859  -29.439 35.534 1.00 43.09 ? 276  HOH E O   1 
HETATM 11837 O  O   . HOH JA 5 .   ? 22.659  -32.902 17.891 1.00 45.28 ? 277  HOH E O   1 
HETATM 11838 O  O   . HOH JA 5 .   ? 27.015  -40.447 9.572  1.00 46.79 ? 278  HOH E O   1 
HETATM 11839 O  O   . HOH JA 5 .   ? 60.595  -30.335 8.799  1.00 42.30 ? 279  HOH E O   1 
HETATM 11840 O  O   . HOH JA 5 .   ? 32.215  -46.209 23.617 1.00 47.48 ? 280  HOH E O   1 
HETATM 11841 O  O   . HOH JA 5 .   ? 52.178  -45.455 14.456 1.00 46.36 ? 281  HOH E O   1 
HETATM 11842 O  O   . HOH JA 5 .   ? 53.185  -27.258 26.396 1.00 47.26 ? 282  HOH E O   1 
HETATM 11843 O  O   . HOH JA 5 .   ? 34.448  -29.478 17.042 1.00 37.18 ? 283  HOH E O   1 
HETATM 11844 O  O   . HOH JA 5 .   ? 49.710  -25.706 26.477 1.00 46.61 ? 284  HOH E O   1 
HETATM 11845 O  O   . HOH JA 5 .   ? 57.257  -39.241 -2.677 1.00 40.60 ? 285  HOH E O   1 
HETATM 11846 O  O   . HOH JA 5 .   ? 32.314  -29.161 12.539 1.00 54.53 ? 286  HOH E O   1 
HETATM 11847 O  O   . HOH JA 5 .   ? 45.538  -29.025 -2.654 1.00 53.12 ? 287  HOH E O   1 
HETATM 11848 O  O   . HOH JA 5 .   ? 30.390  -35.833 0.478  1.00 54.87 ? 288  HOH E O   1 
HETATM 11849 O  O   . HOH JA 5 .   ? 49.862  -48.448 31.396 1.00 44.29 ? 289  HOH E O   1 
HETATM 11850 O  O   . HOH JA 5 .   ? 56.219  -29.522 7.444  1.00 45.81 ? 290  HOH E O   1 
HETATM 11851 O  O   . HOH JA 5 .   ? 41.376  -36.934 1.563  1.00 44.97 ? 291  HOH E O   1 
HETATM 11852 O  O   . HOH JA 5 .   ? 55.536  -43.173 24.327 1.00 44.49 ? 292  HOH E O   1 
HETATM 11853 O  O   . HOH JA 5 .   ? 54.820  -41.990 33.474 1.00 41.45 ? 293  HOH E O   1 
HETATM 11854 O  O   . HOH JA 5 .   ? 32.842  -49.909 21.063 1.00 47.57 ? 294  HOH E O   1 
HETATM 11855 O  O   . HOH JA 5 .   ? 37.724  -20.724 26.680 1.00 44.28 ? 295  HOH E O   1 
HETATM 11856 O  O   . HOH JA 5 .   ? 54.490  -39.096 27.014 1.00 42.08 ? 296  HOH E O   1 
HETATM 11857 O  O   . HOH JA 5 .   ? 33.488  -33.780 -1.455 1.00 51.31 ? 297  HOH E O   1 
HETATM 11858 O  O   . HOH JA 5 .   ? 40.694  -53.515 33.414 1.00 50.97 ? 298  HOH E O   1 
HETATM 11859 O  O   . HOH JA 5 .   ? 53.359  -33.858 28.435 1.00 41.08 ? 299  HOH E O   1 
HETATM 11860 O  O   . HOH JA 5 .   ? 29.255  -33.538 3.032  1.00 47.09 ? 300  HOH E O   1 
HETATM 11861 O  O   . HOH JA 5 .   ? 40.727  -27.861 28.491 1.00 41.92 ? 301  HOH E O   1 
HETATM 11862 O  O   . HOH JA 5 .   ? 39.201  -41.655 4.294  1.00 41.19 ? 302  HOH E O   1 
HETATM 11863 O  O   . HOH JA 5 .   ? 23.302  -42.818 11.753 1.00 49.25 ? 303  HOH E O   1 
HETATM 11864 O  O   . HOH JA 5 .   ? 42.182  -25.067 4.953  1.00 51.36 ? 304  HOH E O   1 
HETATM 11865 O  O   . HOH JA 5 .   ? 53.799  -36.021 29.621 1.00 43.72 ? 305  HOH E O   1 
HETATM 11866 O  O   . HOH JA 5 .   ? 38.393  -39.417 3.252  1.00 41.05 ? 306  HOH E O   1 
HETATM 11867 O  O   . HOH JA 5 .   ? 43.935  -35.479 2.505  1.00 58.61 ? 307  HOH E O   1 
HETATM 11868 O  O   . HOH JA 5 .   ? 32.608  -28.397 20.630 1.00 52.40 ? 308  HOH E O   1 
HETATM 11869 O  O   . HOH JA 5 .   ? 62.097  -40.513 4.476  1.00 42.08 ? 309  HOH E O   1 
HETATM 11870 O  O   . HOH JA 5 .   ? 32.559  -49.095 23.731 1.00 47.97 ? 310  HOH E O   1 
HETATM 11871 O  O   . HOH JA 5 .   ? 48.302  -49.225 27.334 1.00 42.88 ? 311  HOH E O   1 
HETATM 11872 O  O   . HOH JA 5 .   ? 55.893  -44.061 3.172  1.00 44.92 ? 312  HOH E O   1 
HETATM 11873 O  O   . HOH JA 5 .   ? 35.217  -43.560 27.250 1.00 48.47 ? 313  HOH E O   1 
HETATM 11874 O  O   . HOH JA 5 .   ? 46.652  -48.424 12.523 1.00 44.23 ? 314  HOH E O   1 
HETATM 11875 O  O   . HOH JA 5 .   ? 35.967  -25.709 9.022  1.00 46.35 ? 315  HOH E O   1 
HETATM 11876 O  O   . HOH JA 5 .   ? 59.977  -36.216 3.167  1.00 52.64 ? 316  HOH E O   1 
HETATM 11877 O  O   . HOH JA 5 .   ? 27.094  -47.926 16.718 1.00 40.89 ? 317  HOH E O   1 
HETATM 11878 O  O   . HOH JA 5 .   ? 51.927  -32.121 29.028 1.00 44.67 ? 318  HOH E O   1 
HETATM 11879 O  O   . HOH JA 5 .   ? 68.666  -29.889 12.706 1.00 53.79 ? 319  HOH E O   1 
HETATM 11880 O  O   . HOH JA 5 .   ? 57.306  -43.354 9.511  1.00 39.92 ? 320  HOH E O   1 
HETATM 11881 O  O   . HOH JA 5 .   ? 28.346  -50.490 10.589 1.00 38.69 ? 321  HOH E O   1 
HETATM 11882 O  O   . HOH JA 5 .   ? 60.790  -38.509 19.591 1.00 54.75 ? 322  HOH E O   1 
HETATM 11883 O  O   . HOH JA 5 .   ? 55.674  -40.000 31.386 1.00 59.52 ? 323  HOH E O   1 
HETATM 11884 O  O   . HOH JA 5 .   ? 49.188  -35.960 35.007 1.00 44.38 ? 324  HOH E O   1 
HETATM 11885 O  O   . HOH JA 5 .   ? 45.530  -47.579 9.282  1.00 45.48 ? 325  HOH E O   1 
HETATM 11886 O  O   . HOH JA 5 .   ? 43.728  -15.540 18.332 1.00 38.94 ? 326  HOH E O   1 
HETATM 11887 O  O   . HOH JA 5 .   ? 50.582  -28.907 -2.439 1.00 53.04 ? 327  HOH E O   1 
HETATM 11888 O  O   . HOH JA 5 .   ? 61.258  -39.198 7.845  1.00 38.44 ? 328  HOH E O   1 
HETATM 11889 O  O   . HOH JA 5 .   ? 36.131  -19.340 24.817 1.00 42.86 ? 329  HOH E O   1 
HETATM 11890 O  O   . HOH JA 5 .   ? 48.923  -48.482 38.169 1.00 61.63 ? 330  HOH E O   1 
HETATM 11891 O  O   . HOH JA 5 .   ? 34.456  -39.100 31.991 1.00 42.60 ? 331  HOH E O   1 
HETATM 11892 O  O   . HOH JA 5 .   ? 55.202  -42.602 -1.029 1.00 49.20 ? 332  HOH E O   1 
HETATM 11893 O  O   . HOH JA 5 .   ? 39.017  -23.889 26.776 1.00 53.63 ? 333  HOH E O   1 
HETATM 11894 O  O   . HOH JA 5 .   ? 24.111  -35.895 21.001 1.00 48.18 ? 334  HOH E O   1 
HETATM 11895 O  O   . HOH JA 5 .   ? 54.371  -39.954 35.044 1.00 45.57 ? 335  HOH E O   1 
HETATM 11896 O  O   . HOH JA 5 .   ? 22.884  -33.467 20.317 1.00 50.16 ? 336  HOH E O   1 
HETATM 11897 O  O   . HOH JA 5 .   ? 37.369  -19.509 22.084 1.00 47.40 ? 337  HOH E O   1 
HETATM 11898 O  O   . HOH JA 5 .   ? 46.098  -48.194 15.076 1.00 49.30 ? 338  HOH E O   1 
HETATM 11899 O  O   . HOH JA 5 .   ? 52.899  -42.008 29.981 1.00 47.91 ? 339  HOH E O   1 
HETATM 11900 O  O   . HOH JA 5 .   ? 44.917  -38.964 1.038  1.00 55.12 ? 340  HOH E O   1 
HETATM 11901 O  O   . HOH JA 5 .   ? 46.571  -33.027 6.424  1.00 38.76 ? 341  HOH E O   1 
HETATM 11902 O  O   . HOH JA 5 .   ? 39.196  -26.532 26.865 1.00 53.01 ? 342  HOH E O   1 
HETATM 11903 O  O   . HOH JA 5 .   ? 29.986  -42.141 9.962  1.00 50.17 ? 343  HOH E O   1 
HETATM 11904 O  O   . HOH JA 5 .   ? 44.367  -52.896 31.106 1.00 48.12 ? 344  HOH E O   1 
HETATM 11905 O  O   . HOH JA 5 .   ? 31.493  -51.478 9.370  1.00 48.74 ? 345  HOH E O   1 
HETATM 11906 O  O   . HOH JA 5 .   ? 34.305  -49.949 9.802  1.00 52.69 ? 346  HOH E O   1 
HETATM 11907 O  O   . HOH KA 5 .   ? 50.907  -21.212 21.051 1.00 17.97 ? 156  HOH F O   1 
HETATM 11908 O  O   . HOH KA 5 .   ? 55.539  -29.217 20.964 1.00 21.36 ? 157  HOH F O   1 
HETATM 11909 O  O   . HOH KA 5 .   ? 67.597  -10.692 16.393 1.00 16.71 ? 158  HOH F O   1 
HETATM 11910 O  O   . HOH KA 5 .   ? 52.634  -23.932 22.682 1.00 25.57 ? 159  HOH F O   1 
HETATM 11911 O  O   . HOH KA 5 .   ? 77.146  -8.342  23.649 1.00 23.60 ? 160  HOH F O   1 
HETATM 11912 O  O   . HOH KA 5 .   ? 68.160  -4.523  13.503 1.00 22.58 ? 161  HOH F O   1 
HETATM 11913 O  O   . HOH KA 5 .   ? 72.907  -5.720  13.746 1.00 28.33 ? 162  HOH F O   1 
HETATM 11914 O  O   . HOH KA 5 .   ? 55.191  -18.800 32.340 1.00 28.59 ? 163  HOH F O   1 
HETATM 11915 O  O   . HOH KA 5 .   ? 53.119  -23.274 2.991  1.00 41.67 ? 164  HOH F O   1 
HETATM 11916 O  O   . HOH KA 5 .   ? 55.531  -24.372 8.470  1.00 25.39 ? 165  HOH F O   1 
HETATM 11917 O  O   . HOH KA 5 .   ? 63.244  -27.304 10.186 1.00 30.81 ? 166  HOH F O   1 
HETATM 11918 O  O   . HOH KA 5 .   ? 56.405  -2.063  25.777 1.00 26.55 ? 167  HOH F O   1 
HETATM 11919 O  O   . HOH KA 5 .   ? 62.369  -10.891 32.712 1.00 23.67 ? 168  HOH F O   1 
HETATM 11920 O  O   . HOH KA 5 .   ? 68.900  -18.576 21.476 1.00 27.53 ? 169  HOH F O   1 
HETATM 11921 O  O   . HOH KA 5 .   ? 69.627  -24.951 20.799 1.00 27.63 ? 170  HOH F O   1 
HETATM 11922 O  O   . HOH KA 5 .   ? 53.355  -22.996 6.682  1.00 29.20 ? 171  HOH F O   1 
HETATM 11923 O  O   . HOH KA 5 .   ? 62.541  -31.694 17.929 1.00 34.05 ? 172  HOH F O   1 
HETATM 11924 O  O   . HOH KA 5 .   ? 58.883  -17.292 32.963 1.00 27.68 ? 173  HOH F O   1 
HETATM 11925 O  O   . HOH KA 5 .   ? 55.701  -23.194 26.309 1.00 36.30 ? 174  HOH F O   1 
HETATM 11926 O  O   . HOH KA 5 .   ? 66.821  -21.602 28.626 1.00 33.99 ? 175  HOH F O   1 
HETATM 11927 O  O   . HOH KA 5 .   ? 75.734  -6.060  24.107 1.00 25.56 ? 176  HOH F O   1 
HETATM 11928 O  O   . HOH KA 5 .   ? 75.911  -9.367  25.921 1.00 24.85 ? 177  HOH F O   1 
HETATM 11929 O  O   . HOH KA 5 .   ? 68.200  -18.099 7.646  1.00 26.61 ? 178  HOH F O   1 
HETATM 11930 O  O   . HOH KA 5 .   ? 70.670  -19.877 17.196 1.00 26.79 ? 179  HOH F O   1 
HETATM 11931 O  O   . HOH KA 5 .   ? 65.342  1.291   13.079 1.00 31.26 ? 180  HOH F O   1 
HETATM 11932 O  O   . HOH KA 5 .   ? 62.616  -5.906  17.499 1.00 34.41 ? 181  HOH F O   1 
HETATM 11933 O  O   . HOH KA 5 .   ? 65.234  -11.272 32.534 1.00 28.49 ? 182  HOH F O   1 
HETATM 11934 O  O   . HOH KA 5 .   ? 55.799  -24.093 23.739 1.00 27.45 ? 183  HOH F O   1 
HETATM 11935 O  O   . HOH KA 5 .   ? 63.834  0.198   23.840 1.00 23.64 ? 184  HOH F O   1 
HETATM 11936 O  O   . HOH KA 5 .   ? 60.668  -12.264 34.530 1.00 27.11 ? 185  HOH F O   1 
HETATM 11937 O  O   . HOH KA 5 .   ? 79.969  -9.672  16.378 1.00 25.07 ? 186  HOH F O   1 
HETATM 11938 O  O   . HOH KA 5 .   ? 67.473  -2.792  28.455 1.00 29.37 ? 187  HOH F O   1 
HETATM 11939 O  O   . HOH KA 5 .   ? 71.136  -4.618  21.266 1.00 36.03 ? 188  HOH F O   1 
HETATM 11940 O  O   . HOH KA 5 .   ? 61.141  -16.039 34.238 1.00 33.08 ? 189  HOH F O   1 
HETATM 11941 O  O   . HOH KA 5 .   ? 69.791  -20.384 19.751 1.00 32.70 ? 190  HOH F O   1 
HETATM 11942 O  O   . HOH KA 5 .   ? 73.101  -9.130  26.094 1.00 29.55 ? 191  HOH F O   1 
HETATM 11943 O  O   . HOH KA 5 .   ? 69.161  -20.382 24.308 1.00 39.10 ? 192  HOH F O   1 
HETATM 11944 O  O   . HOH KA 5 .   ? 64.359  -30.356 19.419 1.00 29.99 ? 193  HOH F O   1 
HETATM 11945 O  O   . HOH KA 5 .   ? 81.063  -16.718 23.012 1.00 31.09 ? 194  HOH F O   1 
HETATM 11946 O  O   . HOH KA 5 .   ? 70.185  -17.534 23.931 1.00 29.36 ? 195  HOH F O   1 
HETATM 11947 O  O   . HOH KA 5 .   ? 74.728  -9.897  11.183 1.00 38.24 ? 196  HOH F O   1 
HETATM 11948 O  O   . HOH KA 5 .   ? 66.739  -23.668 10.954 1.00 32.88 ? 197  HOH F O   1 
HETATM 11949 O  O   . HOH KA 5 .   ? 72.499  -7.922  28.412 1.00 37.61 ? 198  HOH F O   1 
HETATM 11950 O  O   . HOH KA 5 .   ? 46.072  -13.777 16.114 1.00 30.00 ? 199  HOH F O   1 
HETATM 11951 O  O   . HOH KA 5 .   ? 76.940  -2.098  20.142 1.00 30.52 ? 200  HOH F O   1 
HETATM 11952 O  O   . HOH KA 5 .   ? 58.445  -18.000 2.548  1.00 26.86 ? 201  HOH F O   1 
HETATM 11953 O  O   . HOH KA 5 .   ? 68.374  -15.583 6.577  1.00 31.42 ? 202  HOH F O   1 
HETATM 11954 O  O   . HOH KA 5 .   ? 66.489  0.361   24.271 1.00 27.29 ? 203  HOH F O   1 
HETATM 11955 O  O   . HOH KA 5 .   ? 53.743  -8.066  34.561 1.00 35.52 ? 204  HOH F O   1 
HETATM 11956 O  O   . HOH KA 5 .   ? 61.576  -6.491  11.404 1.00 27.95 ? 205  HOH F O   1 
HETATM 11957 O  O   . HOH KA 5 .   ? 58.533  -1.552  16.613 1.00 38.37 ? 206  HOH F O   1 
HETATM 11958 O  O   . HOH KA 5 .   ? 80.837  -4.388  17.161 1.00 38.76 ? 207  HOH F O   1 
HETATM 11959 O  O   . HOH KA 5 .   ? 73.971  -11.975 4.016  1.00 42.03 ? 208  HOH F O   1 
HETATM 11960 O  O   . HOH KA 5 .   ? 65.261  -5.048  17.312 1.00 39.61 ? 209  HOH F O   1 
HETATM 11961 O  O   . HOH KA 5 .   ? 50.590  -7.764  6.887  1.00 34.53 ? 210  HOH F O   1 
HETATM 11962 O  O   . HOH KA 5 .   ? 66.216  -3.496  14.958 1.00 44.13 ? 211  HOH F O   1 
HETATM 11963 O  O   . HOH KA 5 .   ? 74.500  -18.947 13.461 1.00 33.78 ? 212  HOH F O   1 
HETATM 11964 O  O   . HOH KA 5 .   ? 69.416  -4.252  28.363 1.00 41.17 ? 213  HOH F O   1 
HETATM 11965 O  O   . HOH KA 5 .   ? 50.894  -22.991 7.291  1.00 38.31 ? 214  HOH F O   1 
HETATM 11966 O  O   . HOH KA 5 .   ? 61.597  0.260   29.509 1.00 33.01 ? 215  HOH F O   1 
HETATM 11967 O  O   . HOH KA 5 .   ? 48.003  -9.852  23.292 1.00 32.45 ? 216  HOH F O   1 
HETATM 11968 O  O   . HOH KA 5 .   ? 58.284  2.621   31.856 1.00 48.41 ? 217  HOH F O   1 
HETATM 11969 O  O   . HOH KA 5 .   ? 67.403  2.709   24.551 1.00 37.02 ? 218  HOH F O   1 
HETATM 11970 O  O   . HOH KA 5 .   ? 78.928  -3.598  19.362 1.00 31.04 ? 219  HOH F O   1 
HETATM 11971 O  O   . HOH KA 5 .   ? 44.762  -17.523 8.846  1.00 35.98 ? 220  HOH F O   1 
HETATM 11972 O  O   . HOH KA 5 .   ? 74.146  -7.288  6.915  1.00 46.83 ? 221  HOH F O   1 
HETATM 11973 O  O   . HOH KA 5 .   ? 59.449  -3.581  13.114 1.00 34.83 ? 222  HOH F O   1 
HETATM 11974 O  O   . HOH KA 5 .   ? 61.561  -4.515  36.227 1.00 36.41 ? 223  HOH F O   1 
HETATM 11975 O  O   . HOH KA 5 .   ? 50.978  -7.095  33.848 1.00 32.40 ? 224  HOH F O   1 
HETATM 11976 O  O   . HOH KA 5 .   ? 70.244  -7.398  28.948 1.00 36.60 ? 225  HOH F O   1 
HETATM 11977 O  O   . HOH KA 5 .   ? 57.689  -24.659 21.808 1.00 31.87 ? 226  HOH F O   1 
HETATM 11978 O  O   . HOH KA 5 .   ? 57.571  -24.202 28.491 1.00 43.19 ? 227  HOH F O   1 
HETATM 11979 O  O   . HOH KA 5 .   ? 77.807  -8.468  12.873 1.00 41.14 ? 228  HOH F O   1 
HETATM 11980 O  O   . HOH KA 5 .   ? 71.110  -3.972  26.389 1.00 37.53 ? 229  HOH F O   1 
HETATM 11981 O  O   . HOH KA 5 .   ? 50.257  -17.785 28.662 1.00 37.29 ? 230  HOH F O   1 
HETATM 11982 O  O   . HOH KA 5 .   ? 59.063  -5.503  35.979 1.00 40.52 ? 231  HOH F O   1 
HETATM 11983 O  O   . HOH KA 5 .   ? 57.116  -12.126 4.286  1.00 33.54 ? 232  HOH F O   1 
HETATM 11984 O  O   . HOH KA 5 .   ? 60.207  -23.974 29.266 1.00 35.62 ? 233  HOH F O   1 
HETATM 11985 O  O   . HOH KA 5 .   ? 44.833  -13.589 19.824 1.00 33.28 ? 234  HOH F O   1 
HETATM 11986 O  O   . HOH KA 5 .   ? 71.927  -4.507  23.800 1.00 33.46 ? 235  HOH F O   1 
HETATM 11987 O  O   . HOH KA 5 .   ? 59.807  -25.344 23.004 1.00 36.03 ? 236  HOH F O   1 
HETATM 11988 O  O   . HOH KA 5 .   ? 76.689  -0.037  13.768 1.00 38.18 ? 237  HOH F O   1 
HETATM 11989 O  O   . HOH KA 5 .   ? 68.256  -25.759 23.170 1.00 35.02 ? 238  HOH F O   1 
HETATM 11990 O  O   . HOH KA 5 .   ? 74.366  0.037   17.041 1.00 45.58 ? 239  HOH F O   1 
HETATM 11991 O  O   . HOH KA 5 .   ? 46.491  -20.740 27.353 1.00 38.26 ? 240  HOH F O   1 
HETATM 11992 O  O   . HOH KA 5 .   ? 62.521  -23.876 5.243  1.00 40.77 ? 241  HOH F O   1 
HETATM 11993 O  O   . HOH KA 5 .   ? 55.566  -16.169 1.693  1.00 33.57 ? 242  HOH F O   1 
HETATM 11994 O  O   . HOH KA 5 .   ? 51.519  -8.730  3.782  1.00 38.69 ? 243  HOH F O   1 
HETATM 11995 O  O   . HOH KA 5 .   ? 70.479  -1.036  26.168 1.00 45.62 ? 244  HOH F O   1 
HETATM 11996 O  O   . HOH KA 5 .   ? 73.092  -6.775  24.338 1.00 34.40 ? 245  HOH F O   1 
HETATM 11997 O  O   . HOH KA 5 .   ? 74.121  -2.733  23.880 1.00 34.92 ? 246  HOH F O   1 
HETATM 11998 O  O   . HOH KA 5 .   ? 69.343  -27.383 13.581 1.00 43.99 ? 247  HOH F O   1 
HETATM 11999 O  O   . HOH KA 5 .   ? 80.202  -16.056 25.600 1.00 52.59 ? 248  HOH F O   1 
HETATM 12000 O  O   . HOH KA 5 .   ? 52.175  -22.263 24.910 1.00 34.24 ? 249  HOH F O   1 
HETATM 12001 O  O   . HOH KA 5 .   ? 52.471  -16.023 35.867 1.00 42.42 ? 250  HOH F O   1 
HETATM 12002 O  O   . HOH KA 5 .   ? 63.492  -25.314 29.071 1.00 52.43 ? 251  HOH F O   1 
HETATM 12003 O  O   . HOH KA 5 .   ? 84.444  -19.545 20.047 1.00 45.94 ? 252  HOH F O   1 
HETATM 12004 O  O   . HOH KA 5 .   ? 67.544  -6.294  29.469 1.00 46.95 ? 253  HOH F O   1 
HETATM 12005 O  O   . HOH KA 5 .   ? 37.121  -20.024 9.642  1.00 46.60 ? 254  HOH F O   1 
HETATM 12006 O  O   . HOH KA 5 .   ? 59.208  -23.163 7.152  1.00 37.99 ? 255  HOH F O   1 
HETATM 12007 O  O   . HOH KA 5 .   ? 56.937  -12.472 1.616  1.00 52.05 ? 256  HOH F O   1 
HETATM 12008 O  O   . HOH KA 5 .   ? 58.463  -5.248  7.010  1.00 38.92 ? 257  HOH F O   1 
HETATM 12009 O  O   . HOH KA 5 .   ? 73.451  -16.177 25.760 1.00 43.64 ? 258  HOH F O   1 
HETATM 12010 O  O   . HOH KA 5 .   ? 70.503  -0.218  23.728 1.00 33.80 ? 259  HOH F O   1 
HETATM 12011 O  O   . HOH KA 5 .   ? 61.282  -14.087 2.947  1.00 41.58 ? 260  HOH F O   1 
HETATM 12012 O  O   . HOH KA 5 .   ? 61.975  -6.856  7.680  1.00 41.10 ? 261  HOH F O   1 
HETATM 12013 O  O   . HOH KA 5 .   ? 71.035  -22.492 20.868 1.00 45.29 ? 262  HOH F O   1 
HETATM 12014 O  O   . HOH KA 5 .   ? 69.307  -24.521 11.555 1.00 43.87 ? 263  HOH F O   1 
HETATM 12015 O  O   . HOH KA 5 .   ? 76.970  -11.529 27.260 1.00 38.03 ? 264  HOH F O   1 
HETATM 12016 O  O   . HOH KA 5 .   ? 45.051  -19.570 7.315  1.00 50.80 ? 265  HOH F O   1 
HETATM 12017 O  O   . HOH KA 5 .   ? 51.090  -4.147  21.000 1.00 38.05 ? 266  HOH F O   1 
HETATM 12018 O  O   . HOH KA 5 .   ? 52.646  -4.612  13.931 1.00 37.96 ? 267  HOH F O   1 
HETATM 12019 O  O   . HOH KA 5 .   ? 49.003  -13.841 3.089  1.00 39.04 ? 268  HOH F O   1 
HETATM 12020 O  O   . HOH KA 5 .   ? 71.218  -21.671 23.394 1.00 54.31 ? 269  HOH F O   1 
HETATM 12021 O  O   . HOH KA 5 .   ? 63.938  -2.859  13.703 1.00 36.25 ? 270  HOH F O   1 
HETATM 12022 O  O   . HOH KA 5 .   ? 73.552  -4.378  19.614 1.00 40.35 ? 271  HOH F O   1 
HETATM 12023 O  O   . HOH KA 5 .   ? 67.849  -0.472  26.677 1.00 42.30 ? 272  HOH F O   1 
HETATM 12024 O  O   . HOH KA 5 .   ? 55.113  -7.062  -5.094 1.00 49.75 ? 273  HOH F O   1 
HETATM 12025 O  O   . HOH KA 5 .   ? 66.045  -24.808 8.660  1.00 48.59 ? 274  HOH F O   1 
HETATM 12026 O  O   . HOH KA 5 .   ? 61.418  -21.781 30.276 1.00 40.10 ? 275  HOH F O   1 
HETATM 12027 O  O   . HOH KA 5 .   ? 78.694  -13.940 27.596 1.00 51.02 ? 276  HOH F O   1 
HETATM 12028 O  O   . HOH KA 5 .   ? 77.292  -16.622 6.967  1.00 52.37 ? 277  HOH F O   1 
HETATM 12029 O  O   . HOH KA 5 .   ? 42.421  -15.813 8.243  1.00 42.56 ? 278  HOH F O   1 
HETATM 12030 O  O   . HOH KA 5 .   ? 44.065  -12.543 22.351 1.00 47.03 ? 279  HOH F O   1 
HETATM 12031 O  O   . HOH KA 5 .   ? 57.255  -24.766 6.646  1.00 44.31 ? 280  HOH F O   1 
HETATM 12032 O  O   . HOH KA 5 .   ? 68.962  -24.059 25.475 1.00 48.65 ? 281  HOH F O   1 
HETATM 12033 O  O   . HOH KA 5 .   ? 45.872  -10.652 21.794 1.00 48.48 ? 282  HOH F O   1 
HETATM 12034 O  O   . HOH KA 5 .   ? 75.873  -9.047  4.548  1.00 50.32 ? 283  HOH F O   1 
HETATM 12035 O  O   . HOH KA 5 .   ? 64.048  -25.269 6.747  1.00 49.30 ? 284  HOH F O   1 
HETATM 12036 O  O   . HOH KA 5 .   ? 47.182  -22.637 5.804  1.00 52.20 ? 285  HOH F O   1 
HETATM 12037 O  O   . HOH KA 5 .   ? 49.126  -6.229  31.847 1.00 43.56 ? 286  HOH F O   1 
HETATM 12038 O  O   . HOH KA 5 .   ? 73.033  -5.171  5.496  1.00 51.10 ? 287  HOH F O   1 
HETATM 12039 O  O   . HOH KA 5 .   ? 74.948  -1.875  18.671 1.00 44.59 ? 288  HOH F O   1 
HETATM 12040 O  O   . HOH KA 5 .   ? 49.637  -4.590  23.168 1.00 39.71 ? 289  HOH F O   1 
HETATM 12041 O  O   . HOH KA 5 .   ? 73.943  -17.306 3.003  1.00 53.58 ? 290  HOH F O   1 
HETATM 12042 O  O   . HOH KA 5 .   ? 44.854  -12.197 4.759  1.00 59.54 ? 291  HOH F O   1 
HETATM 12043 O  O   . HOH KA 5 .   ? 48.966  -11.160 26.495 1.00 44.38 ? 292  HOH F O   1 
HETATM 12044 O  O   . HOH KA 5 .   ? 67.111  -13.794 5.138  1.00 42.83 ? 293  HOH F O   1 
HETATM 12045 O  O   . HOH KA 5 .   ? 62.703  -33.814 24.403 1.00 47.26 ? 294  HOH F O   1 
HETATM 12046 O  O   . HOH KA 5 .   ? 60.091  -2.702  10.462 1.00 44.56 ? 295  HOH F O   1 
HETATM 12047 O  O   . HOH KA 5 .   ? 73.033  -0.472  19.894 1.00 49.68 ? 296  HOH F O   1 
HETATM 12048 O  O   . HOH KA 5 .   ? 72.581  -18.784 24.879 1.00 56.61 ? 297  HOH F O   1 
HETATM 12049 O  O   . HOH KA 5 .   ? 75.474  -4.017  21.903 1.00 47.13 ? 298  HOH F O   1 
HETATM 12050 O  O   . HOH KA 5 .   ? 61.085  -4.427  8.174  1.00 58.32 ? 299  HOH F O   1 
HETATM 12051 O  O   . HOH KA 5 .   ? 50.869  -15.957 3.920  1.00 45.06 ? 300  HOH F O   1 
HETATM 12052 O  O   . HOH KA 5 .   ? 60.595  4.154   34.062 1.00 50.07 ? 301  HOH F O   1 
HETATM 12053 O  O   . HOH KA 5 .   ? 65.748  -6.531  32.052 1.00 46.95 ? 302  HOH F O   1 
HETATM 12054 O  O   . HOH KA 5 .   ? 54.349  1.802   29.364 1.00 50.90 ? 303  HOH F O   1 
HETATM 12055 O  O   . HOH KA 5 .   ? 69.081  -21.668 31.059 1.00 54.19 ? 304  HOH F O   1 
HETATM 12056 O  O   . HOH KA 5 .   ? 60.739  -34.560 20.154 1.00 43.67 ? 305  HOH F O   1 
HETATM 12057 O  O   . HOH KA 5 .   ? 72.850  -0.264  22.387 1.00 45.10 ? 306  HOH F O   1 
HETATM 12058 O  O   . HOH KA 5 .   ? 67.079  -23.460 27.140 1.00 50.13 ? 307  HOH F O   1 
HETATM 12059 O  O   . HOH KA 5 .   ? 60.635  -35.737 17.950 1.00 48.87 ? 308  HOH F O   1 
HETATM 12060 O  O   . HOH KA 5 .   ? 64.370  -31.977 23.425 1.00 49.19 ? 309  HOH F O   1 
HETATM 12061 O  O   . HOH KA 5 .   ? 55.499  -23.968 4.393  1.00 48.00 ? 310  HOH F O   1 
HETATM 12062 O  O   . HOH KA 5 .   ? 64.355  -6.700  6.508  1.00 44.63 ? 311  HOH F O   1 
HETATM 12063 O  O   . HOH KA 5 .   ? 57.407  3.376   29.679 1.00 57.39 ? 312  HOH F O   1 
HETATM 12064 O  O   . HOH KA 5 .   ? 76.850  -11.938 14.257 1.00 45.44 ? 313  HOH F O   1 
HETATM 12065 O  O   . HOH KA 5 .   ? 56.978  -8.151  -3.192 1.00 53.04 ? 314  HOH F O   1 
HETATM 12066 O  O   . HOH KA 5 .   ? 54.487  -14.205 -2.703 1.00 59.61 ? 315  HOH F O   1 
HETATM 12067 O  O   . HOH KA 5 .   ? 67.852  -11.359 5.403  1.00 40.65 ? 316  HOH F O   1 
HETATM 12068 O  O   . HOH KA 5 .   ? 65.946  -30.507 24.804 1.00 47.12 ? 317  HOH F O   1 
HETATM 12069 O  O   . HOH KA 5 .   ? 44.341  -7.957  18.315 1.00 58.33 ? 318  HOH F O   1 
HETATM 12070 O  O   . HOH KA 5 .   ? 60.449  -26.229 31.297 1.00 44.39 ? 319  HOH F O   1 
HETATM 12071 O  O   . HOH KA 5 .   ? 58.392  -1.459  13.527 1.00 47.88 ? 320  HOH F O   1 
HETATM 12072 O  O   . HOH KA 5 .   ? 61.660  -27.664 8.162  1.00 52.16 ? 321  HOH F O   1 
HETATM 12073 O  O   . HOH KA 5 .   ? 54.504  -0.979  27.254 1.00 54.28 ? 322  HOH F O   1 
HETATM 12074 O  O   . HOH KA 5 .   ? 43.605  -14.279 16.146 1.00 46.67 ? 323  HOH F O   1 
HETATM 12075 O  O   . HOH KA 5 .   ? 63.985  -21.381 -0.128 1.00 44.07 ? 324  HOH F O   1 
HETATM 12076 O  O   . HOH KA 5 .   ? 56.371  -6.549  -0.061 1.00 49.30 ? 325  HOH F O   1 
HETATM 12077 O  O   . HOH KA 5 .   ? 70.601  -23.851 8.901  1.00 50.42 ? 326  HOH F O   1 
HETATM 12078 O  O   . HOH KA 5 .   ? 60.849  -20.094 31.998 1.00 44.51 ? 327  HOH F O   1 
HETATM 12079 O  O   . HOH KA 5 .   ? 64.798  -13.824 34.469 1.00 49.14 ? 328  HOH F O   1 
HETATM 12080 O  O   . HOH KA 5 .   ? 58.887  -15.367 1.999  1.00 47.89 ? 329  HOH F O   1 
HETATM 12081 O  O   . HOH KA 5 .   ? 58.070  -6.730  1.957  1.00 46.05 ? 330  HOH F O   1 
HETATM 12082 O  O   . HOH KA 5 .   ? 67.750  -8.787  31.507 1.00 52.82 ? 331  HOH F O   1 
HETATM 12083 O  O   . HOH KA 5 .   ? 50.639  -5.170  5.199  1.00 50.78 ? 332  HOH F O   1 
HETATM 12084 O  O   . HOH KA 5 .   ? 65.242  -29.399 29.321 1.00 51.34 ? 333  HOH F O   1 
HETATM 12085 O  O   . HOH KA 5 .   ? 74.957  -12.272 1.303  1.00 60.34 ? 334  HOH F O   1 
HETATM 12086 O  O   . HOH KA 5 .   ? 74.557  -9.534  30.171 1.00 52.14 ? 335  HOH F O   1 
HETATM 12087 O  O   . HOH KA 5 .   ? 49.589  -7.906  29.999 1.00 66.09 ? 336  HOH F O   1 
HETATM 12088 O  O   . HOH KA 5 .   ? 50.998  -6.182  2.665  1.00 49.33 ? 337  HOH F O   1 
HETATM 12089 O  O   . HOH KA 5 .   ? 73.118  -9.881  33.096 1.00 47.35 ? 338  HOH F O   1 
HETATM 12090 O  O   . HOH LA 5 .   ? 138.868 -21.092 19.199 1.00 35.82 ? 156  HOH G O   1 
HETATM 12091 O  O   . HOH LA 5 .   ? 146.668 -16.119 30.822 1.00 38.35 ? 157  HOH G O   1 
HETATM 12092 O  O   . HOH LA 5 .   ? 147.046 0.875   21.094 1.00 38.02 ? 158  HOH G O   1 
HETATM 12093 O  O   . HOH LA 5 .   ? 156.005 -20.480 12.668 1.00 41.67 ? 159  HOH G O   1 
HETATM 12094 O  O   . HOH LA 5 .   ? 141.173 -0.746  25.356 1.00 48.31 ? 160  HOH G O   1 
HETATM 12095 O  O   . HOH LA 5 .   ? 145.600 -14.033 32.351 1.00 35.04 ? 161  HOH G O   1 
HETATM 12096 O  O   . HOH LA 5 .   ? 160.282 -18.683 34.094 1.00 42.42 ? 162  HOH G O   1 
HETATM 12097 O  O   . HOH LA 5 .   ? 142.760 -9.601  30.529 1.00 33.71 ? 163  HOH G O   1 
HETATM 12098 O  O   . HOH LA 5 .   ? 152.656 -10.777 35.334 1.00 34.74 ? 164  HOH G O   1 
HETATM 12099 O  O   . HOH LA 5 .   ? 146.431 -13.334 4.317  1.00 40.02 ? 165  HOH G O   1 
HETATM 12100 O  O   . HOH LA 5 .   ? 142.826 -0.060  21.559 1.00 37.18 ? 166  HOH G O   1 
HETATM 12101 O  O   . HOH LA 5 .   ? 137.371 -13.537 23.513 1.00 38.75 ? 167  HOH G O   1 
HETATM 12102 O  O   . HOH LA 5 .   ? 136.082 -9.211  24.246 1.00 49.07 ? 168  HOH G O   1 
HETATM 12103 O  O   . HOH LA 5 .   ? 138.792 -15.659 18.819 1.00 39.84 ? 169  HOH G O   1 
HETATM 12104 O  O   . HOH LA 5 .   ? 142.734 -12.470 32.037 1.00 47.04 ? 170  HOH G O   1 
HETATM 12105 O  O   . HOH LA 5 .   ? 135.128 -11.928 16.209 1.00 44.26 ? 171  HOH G O   1 
HETATM 12106 O  O   . HOH LA 5 .   ? 138.158 1.056   18.023 1.00 27.94 ? 172  HOH G O   1 
HETATM 12107 O  O   . HOH LA 5 .   ? 156.303 2.655   23.746 1.00 42.84 ? 173  HOH G O   1 
HETATM 12108 O  O   . HOH LA 5 .   ? 143.458 -5.752  30.783 1.00 38.05 ? 174  HOH G O   1 
HETATM 12109 O  O   . HOH LA 5 .   ? 131.607 -0.592  14.486 1.00 38.67 ? 175  HOH G O   1 
HETATM 12110 O  O   . HOH LA 5 .   ? 155.644 -24.117 13.056 1.00 43.63 ? 176  HOH G O   1 
HETATM 12111 O  O   . HOH LA 5 .   ? 148.727 -14.487 3.661  1.00 45.59 ? 177  HOH G O   1 
HETATM 12112 O  O   . HOH LA 5 .   ? 133.955 -0.629  24.255 1.00 39.54 ? 178  HOH G O   1 
HETATM 12113 O  O   . HOH LA 5 .   ? 141.348 -2.575  21.432 1.00 37.75 ? 179  HOH G O   1 
HETATM 12114 O  O   . HOH LA 5 .   ? 138.245 -5.298  19.003 1.00 41.00 ? 180  HOH G O   1 
HETATM 12115 O  O   . HOH LA 5 .   ? 135.500 -13.494 13.760 1.00 41.71 ? 181  HOH G O   1 
HETATM 12116 O  O   . HOH LA 5 .   ? 140.099 -3.431  19.056 1.00 43.69 ? 182  HOH G O   1 
HETATM 12117 O  O   . HOH LA 5 .   ? 140.210 -4.629  5.923  1.00 41.64 ? 183  HOH G O   1 
HETATM 12118 O  O   . HOH LA 5 .   ? 157.497 -14.130 23.959 1.00 45.59 ? 184  HOH G O   1 
HETATM 12119 O  O   . HOH LA 5 .   ? 141.048 -10.005 6.752  1.00 55.88 ? 185  HOH G O   1 
HETATM 12120 O  O   . HOH LA 5 .   ? 158.877 -11.334 35.679 1.00 53.52 ? 186  HOH G O   1 
HETATM 12121 O  O   . HOH LA 5 .   ? 144.010 -0.177  24.188 1.00 36.87 ? 187  HOH G O   1 
HETATM 12122 O  O   . HOH LA 5 .   ? 157.577 -20.241 30.355 1.00 44.71 ? 188  HOH G O   1 
HETATM 12123 O  O   . HOH LA 5 .   ? 152.037 -4.766  37.165 1.00 49.10 ? 189  HOH G O   1 
HETATM 12124 O  O   . HOH LA 5 .   ? 137.108 -15.520 13.999 1.00 37.82 ? 190  HOH G O   1 
HETATM 12125 O  O   . HOH LA 5 .   ? 150.546 2.967   3.625  1.00 48.99 ? 191  HOH G O   1 
HETATM 12126 O  O   . HOH LA 5 .   ? 153.909 -8.712  36.285 1.00 56.16 ? 192  HOH G O   1 
HETATM 12127 O  O   . HOH LA 5 .   ? 146.561 0.663   7.407  1.00 41.16 ? 193  HOH G O   1 
HETATM 12128 O  O   . HOH LA 5 .   ? 130.321 -7.441  17.571 1.00 28.40 ? 194  HOH G O   1 
HETATM 12129 O  O   . HOH LA 5 .   ? 162.532 4.508   8.590  1.00 52.33 ? 195  HOH G O   1 
HETATM 12130 O  O   . HOH LA 5 .   ? 140.041 1.226   21.465 1.00 49.87 ? 196  HOH G O   1 
HETATM 12131 O  O   . HOH LA 5 .   ? 136.127 -24.231 12.205 1.00 55.16 ? 197  HOH G O   1 
HETATM 12132 O  O   . HOH LA 5 .   ? 162.857 -3.233  10.708 1.00 49.58 ? 198  HOH G O   1 
HETATM 12133 O  O   . HOH LA 5 .   ? 139.610 -15.274 14.496 1.00 44.37 ? 199  HOH G O   1 
HETATM 12134 O  O   . HOH LA 5 .   ? 138.202 -9.794  25.932 1.00 49.79 ? 200  HOH G O   1 
HETATM 12135 O  O   . HOH LA 5 .   ? 145.909 -24.284 8.135  1.00 52.11 ? 201  HOH G O   1 
HETATM 12136 O  O   . HOH LA 5 .   ? 150.306 -31.483 13.660 1.00 45.74 ? 202  HOH G O   1 
HETATM 12137 O  O   . HOH LA 5 .   ? 152.358 -29.807 14.260 1.00 48.01 ? 203  HOH G O   1 
HETATM 12138 O  O   . HOH LA 5 .   ? 158.989 -14.639 28.433 1.00 49.66 ? 204  HOH G O   1 
HETATM 12139 O  O   . HOH LA 5 .   ? 145.265 -21.306 0.262  1.00 57.23 ? 205  HOH G O   1 
HETATM 12140 O  O   . HOH LA 5 .   ? 150.073 -17.575 14.380 1.00 41.27 ? 206  HOH G O   1 
HETATM 12141 O  O   . HOH LA 5 .   ? 153.673 -4.105  29.990 1.00 59.93 ? 207  HOH G O   1 
HETATM 12142 O  O   . HOH LA 5 .   ? 136.165 -12.892 20.231 1.00 45.00 ? 208  HOH G O   1 
HETATM 12143 O  O   . HOH LA 5 .   ? 131.208 -7.027  14.714 1.00 43.35 ? 209  HOH G O   1 
HETATM 12144 O  O   . HOH LA 5 .   ? 157.058 1.960   18.749 1.00 45.82 ? 210  HOH G O   1 
HETATM 12145 O  O   . HOH LA 5 .   ? 136.407 -12.546 26.560 1.00 64.27 ? 211  HOH G O   1 
HETATM 12146 O  O   . HOH LA 5 .   ? 152.124 -4.071  2.473  1.00 43.63 ? 212  HOH G O   1 
HETATM 12147 O  O   . HOH LA 5 .   ? 136.902 -0.790  25.129 1.00 49.87 ? 213  HOH G O   1 
HETATM 12148 O  O   . HOH LA 5 .   ? 156.492 -15.560 17.248 1.00 44.00 ? 214  HOH G O   1 
HETATM 12149 O  O   . HOH LA 5 .   ? 147.388 -1.667  29.414 1.00 57.81 ? 215  HOH G O   1 
HETATM 12150 O  O   . HOH LA 5 .   ? 152.652 -2.857  38.724 1.00 47.68 ? 216  HOH G O   1 
HETATM 12151 O  O   . HOH LA 5 .   ? 141.342 -12.599 -0.526 1.00 61.21 ? 217  HOH G O   1 
HETATM 12152 O  O   . HOH LA 5 .   ? 149.814 -1.157  29.438 1.00 45.79 ? 218  HOH G O   1 
HETATM 12153 O  O   . HOH LA 5 .   ? 158.394 -13.372 21.397 1.00 47.70 ? 219  HOH G O   1 
HETATM 12154 O  O   . HOH LA 5 .   ? 157.651 -13.695 11.878 1.00 60.44 ? 220  HOH G O   1 
HETATM 12155 O  O   . HOH LA 5 .   ? 146.528 -2.876  5.162  1.00 47.20 ? 221  HOH G O   1 
HETATM 12156 O  O   . HOH LA 5 .   ? 138.053 -6.923  25.792 1.00 51.23 ? 222  HOH G O   1 
HETATM 12157 O  O   . HOH LA 5 .   ? 160.625 -6.605  27.148 1.00 52.01 ? 223  HOH G O   1 
HETATM 12158 O  O   . HOH LA 5 .   ? 157.349 -15.150 19.624 1.00 47.45 ? 224  HOH G O   1 
HETATM 12159 O  O   . HOH LA 5 .   ? 138.500 -4.493  25.010 1.00 50.57 ? 225  HOH G O   1 
HETATM 12160 O  O   . HOH LA 5 .   ? 155.765 -18.592 17.401 1.00 51.31 ? 226  HOH G O   1 
HETATM 12161 O  O   . HOH LA 5 .   ? 151.553 -3.296  -1.136 1.00 53.16 ? 227  HOH G O   1 
HETATM 12162 O  O   . HOH LA 5 .   ? 140.621 -17.831 18.778 1.00 40.46 ? 228  HOH G O   1 
HETATM 12163 O  O   . HOH LA 5 .   ? 155.710 -9.950  38.218 1.00 43.99 ? 229  HOH G O   1 
HETATM 12164 O  O   . HOH LA 5 .   ? 140.999 -3.294  24.264 1.00 51.29 ? 230  HOH G O   1 
HETATM 12165 O  O   . HOH LA 5 .   ? 150.882 -18.896 36.037 1.00 51.00 ? 231  HOH G O   1 
HETATM 12166 O  O   . HOH LA 5 .   ? 150.228 -10.899 36.667 1.00 47.19 ? 232  HOH G O   1 
HETATM 12167 O  O   . HOH LA 5 .   ? 149.945 4.331   8.075  1.00 45.68 ? 233  HOH G O   1 
HETATM 12168 O  O   . HOH LA 5 .   ? 158.956 -13.261 9.299  1.00 50.31 ? 234  HOH G O   1 
HETATM 12169 O  O   . HOH LA 5 .   ? 155.614 -6.870  34.843 1.00 52.47 ? 235  HOH G O   1 
HETATM 12170 O  O   . HOH LA 5 .   ? 149.143 2.110   6.811  1.00 42.34 ? 236  HOH G O   1 
HETATM 12171 O  O   . HOH LA 5 .   ? 131.479 -4.093  15.177 1.00 53.46 ? 237  HOH G O   1 
HETATM 12172 O  O   . HOH LA 5 .   ? 129.674 -3.331  13.251 1.00 52.29 ? 238  HOH G O   1 
HETATM 12173 O  O   . HOH LA 5 .   ? 140.556 -11.666 30.329 1.00 62.43 ? 239  HOH G O   1 
HETATM 12174 O  O   . HOH LA 5 .   ? 152.198 -26.721 15.064 1.00 51.99 ? 240  HOH G O   1 
HETATM 12175 O  O   . HOH LA 5 .   ? 163.077 -2.287  1.057  1.00 60.81 ? 241  HOH G O   1 
HETATM 12176 O  O   . HOH LA 5 .   ? 140.798 -15.826 16.846 1.00 54.14 ? 242  HOH G O   1 
HETATM 12177 O  O   . HOH LA 5 .   ? 133.091 -3.166  24.503 1.00 45.90 ? 243  HOH G O   1 
HETATM 12178 O  O   . HOH LA 5 .   ? 133.843 -4.642  26.659 1.00 46.07 ? 244  HOH G O   1 
HETATM 12179 O  O   . HOH LA 5 .   ? 140.659 -16.065 11.827 1.00 48.82 ? 245  HOH G O   1 
HETATM 12180 O  O   . HOH MA 5 .   ? 135.398 26.477  10.928 1.00 25.41 ? 156  HOH H O   1 
HETATM 12181 O  O   . HOH MA 5 .   ? 148.141 19.693  7.556  1.00 27.47 ? 157  HOH H O   1 
HETATM 12182 O  O   . HOH MA 5 .   ? 144.925 34.287  15.702 1.00 26.75 ? 158  HOH H O   1 
HETATM 12183 O  O   . HOH MA 5 .   ? 139.625 2.948   19.388 1.00 25.94 ? 159  HOH H O   1 
HETATM 12184 O  O   . HOH MA 5 .   ? 137.793 12.142  31.184 1.00 29.97 ? 160  HOH H O   1 
HETATM 12185 O  O   . HOH MA 5 .   ? 139.891 23.070  14.732 1.00 24.00 ? 161  HOH H O   1 
HETATM 12186 O  O   . HOH MA 5 .   ? 124.983 17.205  21.689 1.00 28.14 ? 162  HOH H O   1 
HETATM 12187 O  O   . HOH MA 5 .   ? 134.390 18.147  30.190 1.00 31.80 ? 163  HOH H O   1 
HETATM 12188 O  O   . HOH MA 5 .   ? 151.570 15.789  11.503 1.00 30.84 ? 164  HOH H O   1 
HETATM 12189 O  O   . HOH MA 5 .   ? 146.216 16.548  28.516 1.00 41.11 ? 165  HOH H O   1 
HETATM 12190 O  O   . HOH MA 5 .   ? 145.924 24.835  24.886 1.00 43.11 ? 166  HOH H O   1 
HETATM 12191 O  O   . HOH MA 5 .   ? 138.396 29.890  11.799 1.00 30.25 ? 167  HOH H O   1 
HETATM 12192 O  O   . HOH MA 5 .   ? 128.282 6.347   19.358 1.00 37.39 ? 168  HOH H O   1 
HETATM 12193 O  O   . HOH MA 5 .   ? 138.742 36.351  17.683 1.00 33.06 ? 169  HOH H O   1 
HETATM 12194 O  O   . HOH MA 5 .   ? 128.260 4.199   17.640 1.00 32.55 ? 170  HOH H O   1 
HETATM 12195 O  O   . HOH MA 5 .   ? 136.765 31.440  17.723 1.00 32.06 ? 171  HOH H O   1 
HETATM 12196 O  O   . HOH MA 5 .   ? 149.006 20.954  17.431 1.00 33.33 ? 172  HOH H O   1 
HETATM 12197 O  O   . HOH MA 5 .   ? 141.031 32.447  22.346 1.00 29.90 ? 173  HOH H O   1 
HETATM 12198 O  O   . HOH MA 5 .   ? 128.015 8.536   25.044 1.00 44.38 ? 174  HOH H O   1 
HETATM 12199 O  O   . HOH MA 5 .   ? 135.470 28.928  19.102 1.00 38.19 ? 175  HOH H O   1 
HETATM 12200 O  O   . HOH MA 5 .   ? 132.350 2.879   12.405 1.00 34.88 ? 176  HOH H O   1 
HETATM 12201 O  O   . HOH MA 5 .   ? 138.381 32.357  22.236 1.00 31.38 ? 177  HOH H O   1 
HETATM 12202 O  O   . HOH MA 5 .   ? 145.792 20.350  21.127 1.00 43.53 ? 178  HOH H O   1 
HETATM 12203 O  O   . HOH MA 5 .   ? 140.933 30.662  24.599 1.00 35.92 ? 179  HOH H O   1 
HETATM 12204 O  O   . HOH MA 5 .   ? 150.555 24.881  13.612 1.00 40.20 ? 180  HOH H O   1 
HETATM 12205 O  O   . HOH MA 5 .   ? 130.701 26.722  25.369 1.00 33.45 ? 181  HOH H O   1 
HETATM 12206 O  O   . HOH MA 5 .   ? 122.794 16.113  22.971 1.00 38.40 ? 182  HOH H O   1 
HETATM 12207 O  O   . HOH MA 5 .   ? 133.148 20.999  14.468 1.00 33.30 ? 183  HOH H O   1 
HETATM 12208 O  O   . HOH MA 5 .   ? 130.394 1.452   15.969 1.00 32.91 ? 184  HOH H O   1 
HETATM 12209 O  O   . HOH MA 5 .   ? 132.888 27.833  25.511 1.00 51.66 ? 185  HOH H O   1 
HETATM 12210 O  O   . HOH MA 5 .   ? 133.195 25.858  16.729 1.00 33.66 ? 186  HOH H O   1 
HETATM 12211 O  O   . HOH MA 5 .   ? 133.383 4.455   24.880 1.00 44.51 ? 187  HOH H O   1 
HETATM 12212 O  O   . HOH MA 5 .   ? 148.973 3.230   21.375 1.00 33.85 ? 188  HOH H O   1 
HETATM 12213 O  O   . HOH MA 5 .   ? 147.319 9.087   23.188 1.00 40.13 ? 189  HOH H O   1 
HETATM 12214 O  O   . HOH MA 5 .   ? 141.950 30.270  5.614  1.00 45.53 ? 190  HOH H O   1 
HETATM 12215 O  O   . HOH MA 5 .   ? 133.380 -3.925  7.971  1.00 61.50 ? 191  HOH H O   1 
HETATM 12216 O  O   . HOH MA 5 .   ? 126.234 17.909  33.101 1.00 49.06 ? 192  HOH H O   1 
HETATM 12217 O  O   . HOH MA 5 .   ? 127.190 19.672  13.316 1.00 39.87 ? 193  HOH H O   1 
HETATM 12218 O  O   . HOH MA 5 .   ? 137.497 29.808  22.280 1.00 39.15 ? 194  HOH H O   1 
HETATM 12219 O  O   . HOH MA 5 .   ? 131.223 9.685   3.155  1.00 44.95 ? 195  HOH H O   1 
HETATM 12220 O  O   . HOH MA 5 .   ? 133.583 25.362  12.183 1.00 32.95 ? 196  HOH H O   1 
HETATM 12221 O  O   . HOH MA 5 .   ? 133.731 16.337  32.322 1.00 41.76 ? 197  HOH H O   1 
HETATM 12222 O  O   . HOH MA 5 .   ? 135.605 36.182  11.281 1.00 46.22 ? 198  HOH H O   1 
HETATM 12223 O  O   . HOH MA 5 .   ? 130.438 19.493  9.572  1.00 33.79 ? 199  HOH H O   1 
HETATM 12224 O  O   . HOH MA 5 .   ? 121.896 18.273  21.698 1.00 48.66 ? 200  HOH H O   1 
HETATM 12225 O  O   . HOH MA 5 .   ? 148.482 20.069  19.863 1.00 43.72 ? 201  HOH H O   1 
HETATM 12226 O  O   . HOH MA 5 .   ? 132.513 17.762  3.757  1.00 41.84 ? 202  HOH H O   1 
HETATM 12227 O  O   . HOH MA 5 .   ? 144.214 7.379   27.484 1.00 52.40 ? 203  HOH H O   1 
HETATM 12228 O  O   . HOH MA 5 .   ? 145.471 4.471   6.111  1.00 42.79 ? 204  HOH H O   1 
HETATM 12229 O  O   . HOH MA 5 .   ? 154.924 8.098   19.690 1.00 38.98 ? 205  HOH H O   1 
HETATM 12230 O  O   . HOH MA 5 .   ? 142.661 15.070  2.215  1.00 58.00 ? 206  HOH H O   1 
HETATM 12231 O  O   . HOH MA 5 .   ? 152.015 17.451  21.514 1.00 47.35 ? 207  HOH H O   1 
HETATM 12232 O  O   . HOH MA 5 .   ? 136.504 34.912  9.190  1.00 64.14 ? 208  HOH H O   1 
HETATM 12233 O  O   . HOH MA 5 .   ? 131.192 0.533   11.922 1.00 40.57 ? 209  HOH H O   1 
HETATM 12234 O  O   . HOH MA 5 .   ? 154.518 10.442  20.806 1.00 46.34 ? 210  HOH H O   1 
HETATM 12235 O  O   . HOH MA 5 .   ? 121.143 13.911  26.368 1.00 43.13 ? 211  HOH H O   1 
HETATM 12236 O  O   . HOH MA 5 .   ? 124.845 23.193  24.949 1.00 40.58 ? 212  HOH H O   1 
HETATM 12237 O  O   . HOH MA 5 .   ? 136.246 -5.035  4.968  1.00 47.95 ? 213  HOH H O   1 
HETATM 12238 O  O   . HOH MA 5 .   ? 144.812 2.314   23.099 1.00 48.88 ? 214  HOH H O   1 
HETATM 12239 O  O   . HOH MA 5 .   ? 127.761 20.750  32.362 1.00 46.25 ? 215  HOH H O   1 
HETATM 12240 O  O   . HOH MA 5 .   ? 135.272 20.152  5.336  1.00 38.74 ? 216  HOH H O   1 
HETATM 12241 O  O   . HOH MA 5 .   ? 139.390 28.375  24.254 1.00 32.96 ? 217  HOH H O   1 
HETATM 12242 O  O   . HOH MA 5 .   ? 119.629 17.503  24.851 1.00 47.04 ? 218  HOH H O   1 
HETATM 12243 O  O   . HOH MA 5 .   ? 142.468 8.661   -0.129 1.00 58.61 ? 219  HOH H O   1 
HETATM 12244 O  O   . HOH MA 5 .   ? 137.314 28.507  26.637 1.00 41.18 ? 220  HOH H O   1 
HETATM 12245 O  O   . HOH MA 5 .   ? 131.984 23.729  10.680 1.00 35.67 ? 221  HOH H O   1 
HETATM 12246 O  O   . HOH MA 5 .   ? 127.927 2.446   9.102  1.00 40.42 ? 222  HOH H O   1 
HETATM 12247 O  O   . HOH MA 5 .   ? 140.571 3.680   23.386 1.00 35.68 ? 223  HOH H O   1 
HETATM 12248 O  O   . HOH MA 5 .   ? 139.678 30.148  4.517  1.00 49.28 ? 224  HOH H O   1 
HETATM 12249 O  O   . HOH MA 5 .   ? 148.638 5.524   30.068 1.00 52.09 ? 225  HOH H O   1 
HETATM 12250 O  O   . HOH MA 5 .   ? 134.223 19.775  8.659  1.00 37.22 ? 226  HOH H O   1 
HETATM 12251 O  O   . HOH MA 5 .   ? 135.938 10.104  37.032 1.00 45.47 ? 227  HOH H O   1 
HETATM 12252 O  O   . HOH MA 5 .   ? 133.456 24.517  26.933 1.00 44.62 ? 228  HOH H O   1 
HETATM 12253 O  O   . HOH MA 5 .   ? 135.951 30.446  25.513 1.00 37.62 ? 229  HOH H O   1 
HETATM 12254 O  O   . HOH MA 5 .   ? 135.941 20.354  30.698 1.00 34.95 ? 230  HOH H O   1 
HETATM 12255 O  O   . HOH MA 5 .   ? 140.721 37.437  15.597 1.00 42.22 ? 231  HOH H O   1 
HETATM 12256 O  O   . HOH MA 5 .   ? 135.156 29.834  21.422 1.00 39.39 ? 232  HOH H O   1 
HETATM 12257 O  O   . HOH MA 5 .   ? 146.266 21.005  6.132  1.00 43.24 ? 233  HOH H O   1 
HETATM 12258 O  O   . HOH MA 5 .   ? 139.555 29.655  28.167 1.00 47.99 ? 234  HOH H O   1 
HETATM 12259 O  O   . HOH MA 5 .   ? 138.313 13.385  2.356  1.00 43.44 ? 235  HOH H O   1 
HETATM 12260 O  O   . HOH MA 5 .   ? 143.548 27.514  31.849 1.00 54.15 ? 236  HOH H O   1 
HETATM 12261 O  O   . HOH MA 5 .   ? 142.374 12.126  30.182 1.00 49.13 ? 237  HOH H O   1 
HETATM 12262 O  O   . HOH MA 5 .   ? 153.451 10.957  11.090 1.00 47.41 ? 238  HOH H O   1 
HETATM 12263 O  O   . HOH MA 5 .   ? 146.440 27.450  3.471  1.00 59.28 ? 239  HOH H O   1 
HETATM 12264 O  O   . HOH MA 5 .   ? 127.301 -0.436  4.219  1.00 59.66 ? 240  HOH H O   1 
HETATM 12265 O  O   . HOH MA 5 .   ? 133.898 29.904  23.823 1.00 49.96 ? 241  HOH H O   1 
HETATM 12266 O  O   . HOH MA 5 .   ? 142.754 3.658   21.862 1.00 40.34 ? 242  HOH H O   1 
HETATM 12267 O  O   . HOH MA 5 .   ? 135.727 22.618  33.102 1.00 46.73 ? 243  HOH H O   1 
HETATM 12268 O  O   . HOH MA 5 .   ? 153.482 35.044  12.677 1.00 48.64 ? 244  HOH H O   1 
HETATM 12269 O  O   . HOH MA 5 .   ? 135.483 3.957   26.415 1.00 49.59 ? 245  HOH H O   1 
HETATM 12270 O  O   . HOH MA 5 .   ? 127.071 12.651  30.236 1.00 36.13 ? 246  HOH H O   1 
HETATM 12271 O  O   . HOH MA 5 .   ? 121.543 11.861  28.265 1.00 47.33 ? 247  HOH H O   1 
HETATM 12272 O  O   . HOH MA 5 .   ? 150.459 20.387  21.600 1.00 43.70 ? 248  HOH H O   1 
HETATM 12273 O  O   . HOH MA 5 .   ? 147.289 5.616   8.203  1.00 41.66 ? 249  HOH H O   1 
HETATM 12274 O  O   . HOH MA 5 .   ? 146.053 7.182   21.662 1.00 46.65 ? 250  HOH H O   1 
HETATM 12275 O  O   . HOH MA 5 .   ? 139.464 31.741  9.474  1.00 53.95 ? 251  HOH H O   1 
HETATM 12276 O  O   . HOH MA 5 .   ? 137.226 8.187   30.461 1.00 38.66 ? 252  HOH H O   1 
HETATM 12277 O  O   . HOH MA 5 .   ? 143.975 5.970   22.982 1.00 51.45 ? 253  HOH H O   1 
HETATM 12278 O  O   . HOH MA 5 .   ? 136.898 22.019  4.396  1.00 44.46 ? 254  HOH H O   1 
HETATM 12279 O  O   . HOH MA 5 .   ? 132.110 23.578  28.897 1.00 48.83 ? 255  HOH H O   1 
HETATM 12280 O  O   . HOH MA 5 .   ? 152.843 34.146  21.699 1.00 57.53 ? 256  HOH H O   1 
HETATM 12281 O  O   . HOH MA 5 .   ? 129.307 6.505   23.599 1.00 44.04 ? 257  HOH H O   1 
HETATM 12282 O  O   . HOH MA 5 .   ? 135.734 26.585  26.706 1.00 52.45 ? 258  HOH H O   1 
HETATM 12283 O  O   . HOH MA 5 .   ? 137.644 14.766  32.734 1.00 44.22 ? 259  HOH H O   1 
HETATM 12284 O  O   . HOH MA 5 .   ? 142.709 6.129   25.527 1.00 43.46 ? 260  HOH H O   1 
HETATM 12285 O  O   . HOH MA 5 .   ? 131.391 -1.766  10.276 1.00 53.06 ? 261  HOH H O   1 
HETATM 12286 O  O   . HOH MA 5 .   ? 145.053 21.682  23.609 1.00 38.90 ? 262  HOH H O   1 
HETATM 12287 O  O   . HOH MA 5 .   ? 136.823 13.225  37.156 1.00 54.71 ? 263  HOH H O   1 
HETATM 12288 O  O   . HOH MA 5 .   ? 141.997 3.536   25.845 1.00 51.26 ? 264  HOH H O   1 
HETATM 12289 O  O   . HOH MA 5 .   ? 125.203 0.517   1.945  1.00 53.01 ? 265  HOH H O   1 
HETATM 12290 O  O   . HOH MA 5 .   ? 137.337 15.442  0.039  1.00 56.30 ? 266  HOH H O   1 
HETATM 12291 O  O   . HOH MA 5 .   ? 139.849 13.211  36.535 1.00 53.15 ? 267  HOH H O   1 
HETATM 12292 O  O   . HOH MA 5 .   ? 143.962 2.143   6.063  1.00 58.13 ? 268  HOH H O   1 
HETATM 12293 O  O   . HOH MA 5 .   ? 150.717 31.678  23.387 1.00 54.58 ? 269  HOH H O   1 
HETATM 12294 O  O   . HOH MA 5 .   ? 128.509 16.838  32.431 1.00 44.57 ? 270  HOH H O   1 
HETATM 12295 O  O   . HOH MA 5 .   ? 128.186 14.269  32.580 1.00 50.41 ? 271  HOH H O   1 
HETATM 12296 O  O   . HOH MA 5 .   ? 151.251 28.482  7.244  1.00 47.05 ? 272  HOH H O   1 
HETATM 12297 O  O   . HOH MA 5 .   ? 133.770 23.129  31.398 1.00 54.04 ? 273  HOH H O   1 
HETATM 12298 O  O   . HOH MA 5 .   ? 151.790 33.533  14.528 1.00 53.78 ? 274  HOH H O   1 
HETATM 12299 O  O   . HOH MA 5 .   ? 150.365 24.321  2.390  1.00 57.82 ? 275  HOH H O   1 
HETATM 12300 O  O   . HOH MA 5 .   ? 123.341 10.165  22.556 1.00 49.87 ? 276  HOH H O   1 
HETATM 12301 O  O   . HOH MA 5 .   ? 134.983 23.503  29.056 1.00 62.07 ? 277  HOH H O   1 
HETATM 12302 O  O   . HOH MA 5 .   ? 155.273 6.537   26.696 1.00 55.25 ? 278  HOH H O   1 
HETATM 12303 O  O   . HOH MA 5 .   ? 146.896 22.924  26.354 1.00 54.03 ? 279  HOH H O   1 
HETATM 12304 O  O   . HOH MA 5 .   ? 125.491 22.250  32.442 1.00 58.77 ? 280  HOH H O   1 
HETATM 12305 O  O   . HOH MA 5 .   ? 129.447 4.614   9.926  1.00 44.87 ? 281  HOH H O   1 
HETATM 12306 O  O   . HOH MA 5 .   ? 153.257 8.953   9.068  1.00 54.63 ? 282  HOH H O   1 
HETATM 12307 O  O   . HOH MA 5 .   ? 127.883 19.790  9.862  1.00 56.77 ? 283  HOH H O   1 
HETATM 12308 O  O   . HOH MA 5 .   ? 149.351 7.134   6.172  1.00 47.82 ? 284  HOH H O   1 
HETATM 12309 O  O   . HOH MA 5 .   ? 130.775 6.878   9.985  1.00 57.27 ? 285  HOH H O   1 
HETATM 12310 O  O   . HOH MA 5 .   ? 138.315 17.986  -1.785 1.00 53.80 ? 286  HOH H O   1 
HETATM 12311 O  O   . HOH MA 5 .   ? 131.810 3.175   9.887  1.00 60.75 ? 287  HOH H O   1 
HETATM 12312 O  O   . HOH MA 5 .   ? 143.379 29.465  9.843  1.00 48.44 ? 288  HOH H O   1 
HETATM 12313 O  O   . HOH MA 5 .   ? 147.969 8.572   7.701  1.00 53.42 ? 289  HOH H O   1 
HETATM 12314 O  O   . HOH MA 5 .   ? 141.613 10.417  -1.642 1.00 66.32 ? 290  HOH H O   1 
HETATM 12315 O  O   . HOH MA 5 .   ? 120.748 21.121  26.768 1.00 54.37 ? 291  HOH H O   1 
HETATM 12316 O  O   . HOH NA 5 .   ? 80.341  33.736  14.002 1.00 26.37 ? 156  HOH I O   1 
HETATM 12317 O  O   . HOH NA 5 .   ? 79.873  37.355  10.165 1.00 32.79 ? 157  HOH I O   1 
HETATM 12318 O  O   . HOH NA 5 .   ? 73.464  37.823  16.565 1.00 27.83 ? 158  HOH I O   1 
HETATM 12319 O  O   . HOH NA 5 .   ? 86.880  31.063  24.582 1.00 48.04 ? 159  HOH I O   1 
HETATM 12320 O  O   . HOH NA 5 .   ? 99.596  38.850  16.995 1.00 36.75 ? 160  HOH I O   1 
HETATM 12321 O  O   . HOH NA 5 .   ? 83.291  43.374  25.307 1.00 31.18 ? 161  HOH I O   1 
HETATM 12322 O  O   . HOH NA 5 .   ? 98.206  36.121  15.994 1.00 32.70 ? 162  HOH I O   1 
HETATM 12323 O  O   . HOH NA 5 .   ? 82.356  45.934  24.388 1.00 35.41 ? 163  HOH I O   1 
HETATM 12324 O  O   . HOH NA 5 .   ? 81.377  44.199  8.421  1.00 36.61 ? 164  HOH I O   1 
HETATM 12325 O  O   . HOH NA 5 .   ? 76.076  41.428  5.919  1.00 31.74 ? 165  HOH I O   1 
HETATM 12326 O  O   . HOH NA 5 .   ? 72.263  47.258  10.615 1.00 47.21 ? 166  HOH I O   1 
HETATM 12327 O  O   . HOH NA 5 .   ? 83.868  35.144  29.049 1.00 39.72 ? 167  HOH I O   1 
HETATM 12328 O  O   . HOH NA 5 .   ? 81.064  35.564  1.227  1.00 41.04 ? 168  HOH I O   1 
HETATM 12329 O  O   . HOH NA 5 .   ? 74.700  43.611  21.208 1.00 31.95 ? 169  HOH I O   1 
HETATM 12330 O  O   . HOH NA 5 .   ? 79.312  35.974  7.570  1.00 34.20 ? 170  HOH I O   1 
HETATM 12331 O  O   . HOH NA 5 .   ? 75.788  39.725  8.011  1.00 42.83 ? 171  HOH I O   1 
HETATM 12332 O  O   . HOH NA 5 .   ? 79.876  29.874  27.390 1.00 37.10 ? 172  HOH I O   1 
HETATM 12333 O  O   . HOH NA 5 .   ? 102.989 43.949  14.668 1.00 29.73 ? 173  HOH I O   1 
HETATM 12334 O  O   . HOH NA 5 .   ? 99.685  51.997  11.115 1.00 43.22 ? 174  HOH I O   1 
HETATM 12335 O  O   . HOH NA 5 .   ? 74.111  45.583  12.789 1.00 29.74 ? 175  HOH I O   1 
HETATM 12336 O  O   . HOH NA 5 .   ? 84.802  43.051  27.726 1.00 33.60 ? 176  HOH I O   1 
HETATM 12337 O  O   . HOH NA 5 .   ? 76.769  36.706  7.058  1.00 43.35 ? 177  HOH I O   1 
HETATM 12338 O  O   . HOH NA 5 .   ? 94.573  26.956  16.362 1.00 33.14 ? 178  HOH I O   1 
HETATM 12339 O  O   . HOH NA 5 .   ? 83.584  53.932  15.368 1.00 47.96 ? 179  HOH I O   1 
HETATM 12340 O  O   . HOH NA 5 .   ? 98.796  47.312  2.592  1.00 49.99 ? 180  HOH I O   1 
HETATM 12341 O  O   . HOH NA 5 .   ? 100.691 25.893  12.515 1.00 45.03 ? 181  HOH I O   1 
HETATM 12342 O  O   . HOH NA 5 .   ? 79.382  33.386  7.075  1.00 46.34 ? 182  HOH I O   1 
HETATM 12343 O  O   . HOH NA 5 .   ? 80.836  35.868  5.105  1.00 36.35 ? 183  HOH I O   1 
HETATM 12344 O  O   . HOH NA 5 .   ? 93.266  40.994  26.191 1.00 47.97 ? 184  HOH I O   1 
HETATM 12345 O  O   . HOH NA 5 .   ? 79.158  34.641  16.448 1.00 33.82 ? 185  HOH I O   1 
HETATM 12346 O  O   . HOH NA 5 .   ? 88.432  27.517  -0.841 1.00 43.52 ? 186  HOH I O   1 
HETATM 12347 O  O   . HOH NA 5 .   ? 78.150  32.957  4.789  1.00 40.84 ? 187  HOH I O   1 
HETATM 12348 O  O   . HOH NA 5 .   ? 88.046  46.387  -0.654 1.00 40.88 ? 188  HOH I O   1 
HETATM 12349 O  O   . HOH NA 5 .   ? 79.474  37.271  31.648 1.00 50.42 ? 189  HOH I O   1 
HETATM 12350 O  O   . HOH NA 5 .   ? 84.432  24.856  5.102  1.00 55.81 ? 190  HOH I O   1 
HETATM 12351 O  O   . HOH NA 5 .   ? 97.406  42.127  19.944 1.00 43.16 ? 191  HOH I O   1 
HETATM 12352 O  O   . HOH NA 5 .   ? 99.903  38.945  2.570  1.00 44.30 ? 192  HOH I O   1 
HETATM 12353 O  O   . HOH NA 5 .   ? 98.711  42.050  17.647 1.00 42.73 ? 193  HOH I O   1 
HETATM 12354 O  O   . HOH NA 5 .   ? 73.006  37.086  8.105  1.00 45.59 ? 194  HOH I O   1 
HETATM 12355 O  O   . HOH NA 5 .   ? 83.166  27.860  16.327 1.00 44.73 ? 195  HOH I O   1 
HETATM 12356 O  O   . HOH NA 5 .   ? 82.631  25.692  13.765 1.00 44.80 ? 196  HOH I O   1 
HETATM 12357 O  O   . HOH NA 5 .   ? 78.281  45.214  21.777 1.00 47.58 ? 197  HOH I O   1 
HETATM 12358 O  O   . HOH NA 5 .   ? 94.515  27.345  12.423 1.00 43.73 ? 198  HOH I O   1 
HETATM 12359 O  O   . HOH NA 5 .   ? 93.354  48.835  2.604  1.00 48.59 ? 199  HOH I O   1 
HETATM 12360 O  O   . HOH NA 5 .   ? 93.240  53.621  14.815 1.00 47.85 ? 200  HOH I O   1 
HETATM 12361 O  O   . HOH NA 5 .   ? 78.617  30.898  15.528 1.00 38.48 ? 201  HOH I O   1 
HETATM 12362 O  O   . HOH NA 5 .   ? 90.972  27.025  17.912 1.00 50.17 ? 202  HOH I O   1 
HETATM 12363 O  O   . HOH NA 5 .   ? 81.163  28.816  1.240  1.00 44.92 ? 203  HOH I O   1 
HETATM 12364 O  O   . HOH NA 5 .   ? 76.281  48.431  19.802 1.00 44.51 ? 204  HOH I O   1 
HETATM 12365 O  O   . HOH NA 5 .   ? 85.727  30.514  27.405 1.00 45.45 ? 205  HOH I O   1 
HETATM 12366 O  O   . HOH NA 5 .   ? 88.877  33.797  -1.604 1.00 57.90 ? 206  HOH I O   1 
HETATM 12367 O  O   . HOH NA 5 .   ? 86.788  45.082  27.735 1.00 42.18 ? 207  HOH I O   1 
HETATM 12368 O  O   . HOH NA 5 .   ? 92.689  53.699  11.332 1.00 39.82 ? 208  HOH I O   1 
HETATM 12369 O  O   . HOH NA 5 .   ? 71.684  37.641  29.154 1.00 42.63 ? 209  HOH I O   1 
HETATM 12370 O  O   . HOH NA 5 .   ? 82.836  29.323  21.669 1.00 39.76 ? 210  HOH I O   1 
HETATM 12371 O  O   . HOH NA 5 .   ? 70.942  59.215  6.355  1.00 59.55 ? 211  HOH I O   1 
HETATM 12372 O  O   . HOH NA 5 .   ? 93.613  26.263  19.123 1.00 51.06 ? 212  HOH I O   1 
HETATM 12373 O  O   . HOH NA 5 .   ? 98.080  38.697  19.675 1.00 39.78 ? 213  HOH I O   1 
HETATM 12374 O  O   . HOH NA 5 .   ? 77.815  41.189  29.685 1.00 40.88 ? 214  HOH I O   1 
HETATM 12375 O  O   . HOH NA 5 .   ? 77.911  44.090  24.062 1.00 39.82 ? 215  HOH I O   1 
HETATM 12376 O  O   . HOH NA 5 .   ? 93.844  37.756  -3.419 1.00 51.30 ? 216  HOH I O   1 
HETATM 12377 O  O   . HOH NA 5 .   ? 80.712  39.178  29.766 1.00 46.16 ? 217  HOH I O   1 
HETATM 12378 O  O   . HOH NA 5 .   ? 90.528  43.454  25.969 1.00 54.36 ? 218  HOH I O   1 
HETATM 12379 O  O   . HOH NA 5 .   ? 76.202  45.997  -1.848 1.00 53.41 ? 219  HOH I O   1 
HETATM 12380 O  O   . HOH NA 5 .   ? 81.778  31.751  1.337  1.00 53.30 ? 220  HOH I O   1 
HETATM 12381 O  O   . HOH NA 5 .   ? 84.572  42.458  -7.481 1.00 58.62 ? 221  HOH I O   1 
HETATM 12382 O  O   . HOH NA 5 .   ? 75.966  39.023  30.543 1.00 45.32 ? 222  HOH I O   1 
HETATM 12383 O  O   . HOH NA 5 .   ? 88.010  26.877  2.286  1.00 44.90 ? 223  HOH I O   1 
HETATM 12384 O  O   . HOH NA 5 .   ? 78.448  30.768  22.832 1.00 55.52 ? 224  HOH I O   1 
HETATM 12385 O  O   . HOH NA 5 .   ? 78.594  52.208  3.585  1.00 53.87 ? 225  HOH I O   1 
HETATM 12386 O  O   . HOH NA 5 .   ? 93.253  26.934  10.144 1.00 62.96 ? 226  HOH I O   1 
HETATM 12387 O  O   . HOH NA 5 .   ? 100.192 35.548  -1.719 1.00 57.14 ? 227  HOH I O   1 
HETATM 12388 O  O   . HOH NA 5 .   ? 96.594  44.303  -1.528 1.00 55.39 ? 228  HOH I O   1 
HETATM 12389 O  O   . HOH NA 5 .   ? 99.822  36.567  1.461  1.00 44.53 ? 229  HOH I O   1 
HETATM 12390 O  O   . HOH NA 5 .   ? 95.032  30.033  -0.925 1.00 58.70 ? 230  HOH I O   1 
HETATM 12391 O  O   . HOH NA 5 .   ? 99.343  40.599  0.428  1.00 58.57 ? 231  HOH I O   1 
HETATM 12392 O  O   . HOH NA 5 .   ? 77.709  48.820  1.948  1.00 54.41 ? 232  HOH I O   1 
HETATM 12393 O  O   . HOH NA 5 .   ? 85.517  51.108  14.977 1.00 44.63 ? 233  HOH I O   1 
HETATM 12394 O  O   . HOH NA 5 .   ? 87.775  50.709  13.102 1.00 52.32 ? 234  HOH I O   1 
HETATM 12395 O  O   . HOH NA 5 .   ? 76.317  34.860  5.024  1.00 47.20 ? 235  HOH I O   1 
HETATM 12396 O  O   . HOH NA 5 .   ? 83.365  43.581  30.301 1.00 52.67 ? 236  HOH I O   1 
HETATM 12397 O  O   . HOH NA 5 .   ? 76.103  42.969  29.732 1.00 57.75 ? 237  HOH I O   1 
HETATM 12398 O  O   . HOH NA 5 .   ? 95.507  47.453  21.625 1.00 49.58 ? 238  HOH I O   1 
HETATM 12399 O  O   . HOH NA 5 .   ? 84.327  49.175  -7.213 1.00 55.02 ? 239  HOH I O   1 
HETATM 12400 O  O   . HOH NA 5 .   ? 98.175  43.958  15.212 1.00 48.52 ? 240  HOH I O   1 
HETATM 12401 O  O   . HOH NA 5 .   ? 97.292  46.213  16.082 1.00 48.10 ? 241  HOH I O   1 
HETATM 12402 O  O   . HOH NA 5 .   ? 96.835  41.405  0.090  1.00 50.49 ? 242  HOH I O   1 
HETATM 12403 O  O   . HOH NA 5 .   ? 95.050  37.629  -6.815 1.00 50.23 ? 243  HOH I O   1 
HETATM 12404 O  O   . HOH NA 5 .   ? 92.148  52.309  18.259 1.00 59.98 ? 244  HOH I O   1 
HETATM 12405 O  O   . HOH NA 5 .   ? 95.889  53.226  4.788  1.00 46.35 ? 245  HOH I O   1 
HETATM 12406 O  O   . HOH NA 5 .   ? 90.885  51.502  20.122 1.00 48.80 ? 246  HOH I O   1 
HETATM 12407 O  O   . HOH OA 5 .   ? 99.053  33.296  15.679 1.00 29.61 ? 156  HOH J O   1 
HETATM 12408 O  O   . HOH OA 5 .   ? 127.478 25.118  20.133 1.00 27.46 ? 157  HOH J O   1 
HETATM 12409 O  O   . HOH OA 5 .   ? 127.185 34.423  9.660  1.00 34.00 ? 158  HOH J O   1 
HETATM 12410 O  O   . HOH OA 5 .   ? 128.705 21.956  13.043 1.00 26.97 ? 159  HOH J O   1 
HETATM 12411 O  O   . HOH OA 5 .   ? 123.831 42.372  8.845  1.00 32.47 ? 160  HOH J O   1 
HETATM 12412 O  O   . HOH OA 5 .   ? 121.625 31.996  12.277 1.00 32.14 ? 161  HOH J O   1 
HETATM 12413 O  O   . HOH OA 5 .   ? 103.842 41.384  15.598 1.00 26.45 ? 162  HOH J O   1 
HETATM 12414 O  O   . HOH OA 5 .   ? 115.035 24.668  12.895 1.00 33.01 ? 163  HOH J O   1 
HETATM 12415 O  O   . HOH OA 5 .   ? 102.496 38.885  17.041 1.00 36.34 ? 164  HOH J O   1 
HETATM 12416 O  O   . HOH OA 5 .   ? 122.636 17.322  19.181 1.00 37.36 ? 165  HOH J O   1 
HETATM 12417 O  O   . HOH OA 5 .   ? 118.183 28.349  2.328  1.00 35.89 ? 166  HOH J O   1 
HETATM 12418 O  O   . HOH OA 5 .   ? 123.451 38.560  13.534 1.00 40.03 ? 167  HOH J O   1 
HETATM 12419 O  O   . HOH OA 5 .   ? 133.352 28.372  17.713 1.00 34.99 ? 168  HOH J O   1 
HETATM 12420 O  O   . HOH OA 5 .   ? 115.723 27.513  3.347  1.00 31.78 ? 169  HOH J O   1 
HETATM 12421 O  O   . HOH OA 5 .   ? 104.305 31.739  17.853 1.00 43.11 ? 170  HOH J O   1 
HETATM 12422 O  O   . HOH OA 5 .   ? 104.893 27.384  5.056  1.00 40.01 ? 171  HOH J O   1 
HETATM 12423 O  O   . HOH OA 5 .   ? 128.708 29.664  10.412 1.00 40.19 ? 172  HOH J O   1 
HETATM 12424 O  O   . HOH OA 5 .   ? 130.689 28.901  18.715 1.00 37.39 ? 173  HOH J O   1 
HETATM 12425 O  O   . HOH OA 5 .   ? 122.445 39.046  7.012  1.00 32.92 ? 174  HOH J O   1 
HETATM 12426 O  O   . HOH OA 5 .   ? 128.016 27.825  3.032  1.00 52.63 ? 175  HOH J O   1 
HETATM 12427 O  O   . HOH OA 5 .   ? 125.840 25.995  7.653  1.00 49.02 ? 176  HOH J O   1 
HETATM 12428 O  O   . HOH OA 5 .   ? 113.446 25.928  20.026 1.00 48.15 ? 177  HOH J O   1 
HETATM 12429 O  O   . HOH OA 5 .   ? 118.421 34.237  28.042 1.00 42.66 ? 178  HOH J O   1 
HETATM 12430 O  O   . HOH OA 5 .   ? 118.895 23.546  -1.521 1.00 41.12 ? 179  HOH J O   1 
HETATM 12431 O  O   . HOH OA 5 .   ? 117.523 36.742  28.174 1.00 39.76 ? 180  HOH J O   1 
HETATM 12432 O  O   . HOH OA 5 .   ? 128.941 26.931  5.129  1.00 47.43 ? 181  HOH J O   1 
HETATM 12433 O  O   . HOH OA 5 .   ? 109.674 23.301  16.191 1.00 39.30 ? 182  HOH J O   1 
HETATM 12434 O  O   . HOH OA 5 .   ? 107.419 50.354  14.414 1.00 42.05 ? 183  HOH J O   1 
HETATM 12435 O  O   . HOH OA 5 .   ? 129.745 29.973  2.578  1.00 47.72 ? 184  HOH J O   1 
HETATM 12436 O  O   . HOH OA 5 .   ? 122.810 46.444  21.464 1.00 34.45 ? 185  HOH J O   1 
HETATM 12437 O  O   . HOH OA 5 .   ? 122.478 39.897  32.246 1.00 47.94 ? 186  HOH J O   1 
HETATM 12438 O  O   . HOH OA 5 .   ? 109.034 34.516  -6.114 1.00 49.09 ? 187  HOH J O   1 
HETATM 12439 O  O   . HOH OA 5 .   ? 118.426 24.328  20.667 1.00 44.75 ? 188  HOH J O   1 
HETATM 12440 O  O   . HOH OA 5 .   ? 133.594 23.664  14.605 1.00 43.57 ? 189  HOH J O   1 
HETATM 12441 O  O   . HOH OA 5 .   ? 127.270 35.670  24.635 1.00 43.96 ? 190  HOH J O   1 
HETATM 12442 O  O   . HOH OA 5 .   ? 135.774 29.765  11.816 1.00 43.26 ? 191  HOH J O   1 
HETATM 12443 O  O   . HOH OA 5 .   ? 119.334 30.548  1.110  1.00 40.74 ? 192  HOH J O   1 
HETATM 12444 O  O   . HOH OA 5 .   ? 103.069 36.064  18.432 1.00 39.84 ? 193  HOH J O   1 
HETATM 12445 O  O   . HOH OA 5 .   ? 124.618 28.306  22.146 1.00 35.07 ? 194  HOH J O   1 
HETATM 12446 O  O   . HOH OA 5 .   ? 121.862 43.193  18.229 1.00 37.81 ? 195  HOH J O   1 
HETATM 12447 O  O   . HOH OA 5 .   ? 131.328 21.294  12.174 1.00 38.70 ? 196  HOH J O   1 
HETATM 12448 O  O   . HOH OA 5 .   ? 115.798 37.524  29.960 1.00 39.69 ? 197  HOH J O   1 
HETATM 12449 O  O   . HOH OA 5 .   ? 129.757 29.987  16.540 1.00 40.76 ? 198  HOH J O   1 
HETATM 12450 O  O   . HOH OA 5 .   ? 122.286 12.805  16.391 1.00 44.02 ? 199  HOH J O   1 
HETATM 12451 O  O   . HOH OA 5 .   ? 104.046 36.056  20.900 1.00 43.03 ? 200  HOH J O   1 
HETATM 12452 O  O   . HOH OA 5 .   ? 125.048 30.096  24.741 1.00 51.66 ? 201  HOH J O   1 
HETATM 12453 O  O   . HOH OA 5 .   ? 121.219 20.496  2.867  1.00 47.92 ? 202  HOH J O   1 
HETATM 12454 O  O   . HOH OA 5 .   ? 113.637 25.590  14.955 1.00 49.45 ? 203  HOH J O   1 
HETATM 12455 O  O   . HOH OA 5 .   ? 124.574 39.627  0.894  1.00 56.39 ? 204  HOH J O   1 
HETATM 12456 O  O   . HOH OA 5 .   ? 101.836 50.308  9.896  1.00 49.25 ? 205  HOH J O   1 
HETATM 12457 O  O   . HOH OA 5 .   ? 125.993 25.669  22.354 1.00 50.96 ? 206  HOH J O   1 
HETATM 12458 O  O   . HOH OA 5 .   ? 110.721 27.282  23.903 1.00 37.46 ? 207  HOH J O   1 
HETATM 12459 O  O   . HOH OA 5 .   ? 114.818 27.353  17.138 1.00 46.16 ? 208  HOH J O   1 
HETATM 12460 O  O   . HOH OA 5 .   ? 122.318 21.845  0.512  1.00 41.86 ? 209  HOH J O   1 
HETATM 12461 O  O   . HOH OA 5 .   ? 127.731 30.159  24.575 1.00 47.75 ? 210  HOH J O   1 
HETATM 12462 O  O   . HOH OA 5 .   ? 122.015 31.258  1.293  1.00 41.03 ? 211  HOH J O   1 
HETATM 12463 O  O   . HOH OA 5 .   ? 99.591  36.590  21.172 1.00 48.43 ? 212  HOH J O   1 
HETATM 12464 O  O   . HOH OA 5 .   ? 116.371 26.606  19.488 1.00 38.98 ? 213  HOH J O   1 
HETATM 12465 O  O   . HOH OA 5 .   ? 112.072 49.724  17.849 1.00 45.94 ? 214  HOH J O   1 
HETATM 12466 O  O   . HOH OA 5 .   ? 127.959 32.113  17.851 1.00 38.58 ? 215  HOH J O   1 
HETATM 12467 O  O   . HOH OA 5 .   ? 110.160 26.039  6.198  1.00 39.21 ? 216  HOH J O   1 
HETATM 12468 O  O   . HOH OA 5 .   ? 118.435 49.836  16.218 1.00 47.05 ? 217  HOH J O   1 
HETATM 12469 O  O   . HOH OA 5 .   ? 119.245 47.699  9.174  1.00 41.12 ? 218  HOH J O   1 
HETATM 12470 O  O   . HOH OA 5 .   ? 115.767 46.092  -1.322 1.00 50.57 ? 219  HOH J O   1 
HETATM 12471 O  O   . HOH OA 5 .   ? 123.858 33.226  2.152  1.00 45.63 ? 220  HOH J O   1 
HETATM 12472 O  O   . HOH OA 5 .   ? 103.472 39.698  19.504 1.00 41.94 ? 221  HOH J O   1 
HETATM 12473 O  O   . HOH OA 5 .   ? 109.565 26.144  22.243 1.00 53.76 ? 222  HOH J O   1 
HETATM 12474 O  O   . HOH OA 5 .   ? 132.669 32.553  19.136 1.00 53.34 ? 223  HOH J O   1 
HETATM 12475 O  O   . HOH OA 5 .   ? 128.391 31.990  20.436 1.00 38.30 ? 224  HOH J O   1 
HETATM 12476 O  O   . HOH OA 5 .   ? 110.572 23.220  7.566  1.00 49.31 ? 225  HOH J O   1 
HETATM 12477 O  O   . HOH OA 5 .   ? 122.384 41.754  2.757  1.00 47.36 ? 226  HOH J O   1 
HETATM 12478 O  O   . HOH OA 5 .   ? 118.388 50.503  9.040  1.00 53.37 ? 227  HOH J O   1 
HETATM 12479 O  O   . HOH OA 5 .   ? 123.930 39.731  9.183  1.00 48.78 ? 228  HOH J O   1 
HETATM 12480 O  O   . HOH OA 5 .   ? 108.537 24.166  18.442 1.00 47.69 ? 229  HOH J O   1 
HETATM 12481 O  O   . HOH OA 5 .   ? 106.634 31.680  -4.638 1.00 58.71 ? 230  HOH J O   1 
HETATM 12482 O  O   . HOH OA 5 .   ? 103.791 35.257  3.144  1.00 43.61 ? 231  HOH J O   1 
HETATM 12483 O  O   . HOH OA 5 .   ? 110.148 24.305  20.557 1.00 45.48 ? 232  HOH J O   1 
HETATM 12484 O  O   . HOH OA 5 .   ? 127.355 47.582  27.807 1.00 51.95 ? 233  HOH J O   1 
HETATM 12485 O  O   . HOH OA 5 .   ? 102.680 24.634  14.488 1.00 52.11 ? 234  HOH J O   1 
HETATM 12486 O  O   . HOH OA 5 .   ? 120.823 49.984  27.999 1.00 64.35 ? 235  HOH J O   1 
HETATM 12487 O  O   . HOH OA 5 .   ? 123.869 36.023  2.490  1.00 47.44 ? 236  HOH J O   1 
HETATM 12488 O  O   . HOH OA 5 .   ? 108.089 49.024  10.706 1.00 52.39 ? 237  HOH J O   1 
HETATM 12489 O  O   . HOH OA 5 .   ? 124.779 43.991  11.442 1.00 47.47 ? 238  HOH J O   1 
HETATM 12490 O  O   . HOH OA 5 .   ? 126.716 38.499  10.020 1.00 53.23 ? 239  HOH J O   1 
HETATM 12491 O  O   . HOH OA 5 .   ? 105.554 32.013  23.995 1.00 46.79 ? 240  HOH J O   1 
HETATM 12492 O  O   . HOH OA 5 .   ? 134.580 31.918  15.052 1.00 52.63 ? 241  HOH J O   1 
HETATM 12493 O  O   . HOH OA 5 .   ? 104.595 47.782  3.294  1.00 56.55 ? 242  HOH J O   1 
HETATM 12494 O  O   . HOH OA 5 .   ? 124.615 49.542  28.580 1.00 54.44 ? 243  HOH J O   1 
HETATM 12495 O  O   . HOH OA 5 .   ? 118.088 47.272  -3.035 1.00 49.85 ? 244  HOH J O   1 
HETATM 12496 O  O   . HOH OA 5 .   ? 109.645 48.852  8.398  1.00 51.33 ? 245  HOH J O   1 
HETATM 12497 O  O   . HOH OA 5 .   ? 104.182 38.063  1.064  1.00 50.72 ? 246  HOH J O   1 
HETATM 12498 O  O   . HOH OA 5 .   ? 132.835 30.331  16.102 1.00 61.10 ? 247  HOH J O   1 
HETATM 12499 O  O   . HOH OA 5 .   ? 131.080 30.996  20.620 1.00 59.80 ? 248  HOH J O   1 
HETATM 12500 O  O   . HOH OA 5 .   ? 117.938 21.952  9.411  1.00 42.70 ? 249  HOH J O   1 
HETATM 12501 O  O   . HOH OA 5 .   ? 128.681 27.473  20.594 1.00 47.66 ? 250  HOH J O   1 
HETATM 12502 O  O   . HOH OA 5 .   ? 104.107 34.347  23.033 1.00 56.52 ? 251  HOH J O   1 
HETATM 12503 O  O   . HOH OA 5 .   ? 110.787 35.319  -2.398 1.00 44.88 ? 252  HOH J O   1 
HETATM 12504 O  O   . HOH OA 5 .   ? 107.135 32.507  2.166  1.00 51.27 ? 253  HOH J O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   ALA 7   6   6   ALA ALA A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 SER 112 111 111 SER SER A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   ALA 5   4   4   ALA ALA B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   ALA 7   6   6   ALA ALA B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 SER 112 111 111 SER SER B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
C 1 1   MET 1   0   ?   ?   ?   C . n 
C 1 2   ALA 2   1   1   ALA ALA C . n 
C 1 3   THR 3   2   2   THR THR C . n 
C 1 4   LYS 4   3   3   LYS LYS C . n 
C 1 5   ALA 5   4   4   ALA ALA C . n 
C 1 6   VAL 6   5   5   VAL VAL C . n 
C 1 7   ALA 7   6   6   ALA ALA C . n 
C 1 8   VAL 8   7   7   VAL VAL C . n 
C 1 9   LEU 9   8   8   LEU LEU C . n 
C 1 10  LYS 10  9   9   LYS LYS C . n 
C 1 11  GLY 11  10  10  GLY GLY C . n 
C 1 12  ASP 12  11  11  ASP ASP C . n 
C 1 13  GLY 13  12  12  GLY GLY C . n 
C 1 14  PRO 14  13  13  PRO PRO C . n 
C 1 15  VAL 15  14  14  VAL VAL C . n 
C 1 16  GLN 16  15  15  GLN GLN C . n 
C 1 17  GLY 17  16  16  GLY GLY C . n 
C 1 18  ILE 18  17  17  ILE ILE C . n 
C 1 19  ILE 19  18  18  ILE ILE C . n 
C 1 20  ASN 20  19  19  ASN ASN C . n 
C 1 21  PHE 21  20  20  PHE PHE C . n 
C 1 22  GLU 22  21  21  GLU GLU C . n 
C 1 23  GLN 23  22  22  GLN GLN C . n 
C 1 24  LYS 24  23  23  LYS LYS C . n 
C 1 25  GLU 25  24  24  GLU GLU C . n 
C 1 26  SER 26  25  25  SER SER C . n 
C 1 27  ASN 27  26  26  ASN ASN C . n 
C 1 28  GLY 28  27  27  GLY GLY C . n 
C 1 29  PRO 29  28  28  PRO PRO C . n 
C 1 30  VAL 30  29  29  VAL VAL C . n 
C 1 31  LYS 31  30  30  LYS LYS C . n 
C 1 32  VAL 32  31  31  VAL VAL C . n 
C 1 33  TRP 33  32  32  TRP TRP C . n 
C 1 34  GLY 34  33  33  GLY GLY C . n 
C 1 35  SER 35  34  34  SER SER C . n 
C 1 36  ILE 36  35  35  ILE ILE C . n 
C 1 37  LYS 37  36  36  LYS LYS C . n 
C 1 38  GLY 38  37  37  GLY GLY C . n 
C 1 39  LEU 39  38  38  LEU LEU C . n 
C 1 40  THR 40  39  39  THR THR C . n 
C 1 41  GLU 41  40  40  GLU GLU C . n 
C 1 42  GLY 42  41  41  GLY GLY C . n 
C 1 43  LEU 43  42  42  LEU LEU C . n 
C 1 44  HIS 44  43  43  HIS HIS C . n 
C 1 45  GLY 45  44  44  GLY GLY C . n 
C 1 46  PHE 46  45  45  PHE PHE C . n 
C 1 47  HIS 47  46  46  HIS HIS C . n 
C 1 48  VAL 48  47  47  VAL VAL C . n 
C 1 49  HIS 49  48  48  HIS HIS C . n 
C 1 50  GLU 50  49  49  GLU GLU C . n 
C 1 51  PHE 51  50  50  PHE PHE C . n 
C 1 52  GLY 52  51  51  GLY GLY C . n 
C 1 53  ASP 53  52  52  ASP ASP C . n 
C 1 54  ASN 54  53  53  ASN ASN C . n 
C 1 55  THR 55  54  54  THR THR C . n 
C 1 56  ALA 56  55  55  ALA ALA C . n 
C 1 57  GLY 57  56  56  GLY GLY C . n 
C 1 58  CYS 58  57  57  CYS CYS C . n 
C 1 59  THR 59  58  58  THR THR C . n 
C 1 60  SER 60  59  59  SER SER C . n 
C 1 61  ALA 61  60  60  ALA ALA C . n 
C 1 62  GLY 62  61  61  GLY GLY C . n 
C 1 63  PRO 63  62  62  PRO PRO C . n 
C 1 64  HIS 64  63  63  HIS HIS C . n 
C 1 65  PHE 65  64  64  PHE PHE C . n 
C 1 66  ASN 66  65  65  ASN ASN C . n 
C 1 67  PRO 67  66  66  PRO PRO C . n 
C 1 68  LEU 68  67  67  LEU LEU C . n 
C 1 69  SER 69  68  68  SER SER C . n 
C 1 70  ARG 70  69  69  ARG ARG C . n 
C 1 71  LYS 71  70  70  LYS LYS C . n 
C 1 72  HIS 72  71  71  HIS HIS C . n 
C 1 73  GLY 73  72  72  GLY GLY C . n 
C 1 74  GLY 74  73  73  GLY GLY C . n 
C 1 75  PRO 75  74  74  PRO PRO C . n 
C 1 76  LYS 76  75  75  LYS LYS C . n 
C 1 77  ASP 77  76  76  ASP ASP C . n 
C 1 78  GLU 78  77  77  GLU GLU C . n 
C 1 79  GLU 79  78  78  GLU GLU C . n 
C 1 80  ARG 80  79  79  ARG ARG C . n 
C 1 81  HIS 81  80  80  HIS HIS C . n 
C 1 82  VAL 82  81  81  VAL VAL C . n 
C 1 83  GLY 83  82  82  GLY GLY C . n 
C 1 84  ASP 84  83  83  ASP ASP C . n 
C 1 85  LEU 85  84  84  LEU LEU C . n 
C 1 86  GLY 86  85  85  GLY GLY C . n 
C 1 87  ASN 87  86  86  ASN ASN C . n 
C 1 88  VAL 88  87  87  VAL VAL C . n 
C 1 89  THR 89  88  88  THR THR C . n 
C 1 90  ALA 90  89  89  ALA ALA C . n 
C 1 91  ASP 91  90  90  ASP ASP C . n 
C 1 92  LYS 92  91  91  LYS LYS C . n 
C 1 93  ASP 93  92  92  ASP ASP C . n 
C 1 94  GLY 94  93  93  GLY GLY C . n 
C 1 95  VAL 95  94  94  VAL VAL C . n 
C 1 96  ALA 96  95  95  ALA ALA C . n 
C 1 97  ASP 97  96  96  ASP ASP C . n 
C 1 98  VAL 98  97  97  VAL VAL C . n 
C 1 99  SER 99  98  98  SER SER C . n 
C 1 100 ILE 100 99  99  ILE ILE C . n 
C 1 101 GLU 101 100 100 GLU GLU C . n 
C 1 102 ASP 102 101 101 ASP ASP C . n 
C 1 103 SER 103 102 102 SER SER C . n 
C 1 104 VAL 104 103 103 VAL VAL C . n 
C 1 105 ILE 105 104 104 ILE ILE C . n 
C 1 106 SER 106 105 105 SER SER C . n 
C 1 107 LEU 107 106 106 LEU LEU C . n 
C 1 108 SER 108 107 107 SER SER C . n 
C 1 109 GLY 109 108 108 GLY GLY C . n 
C 1 110 ASP 110 109 109 ASP ASP C . n 
C 1 111 HIS 111 110 110 HIS HIS C . n 
C 1 112 SER 112 111 111 SER SER C . n 
C 1 113 ILE 113 112 112 ILE ILE C . n 
C 1 114 ILE 114 113 113 ILE ILE C . n 
C 1 115 GLY 115 114 114 GLY GLY C . n 
C 1 116 ARG 116 115 115 ARG ARG C . n 
C 1 117 THR 117 116 116 THR THR C . n 
C 1 118 LEU 118 117 117 LEU LEU C . n 
C 1 119 VAL 119 118 118 VAL VAL C . n 
C 1 120 VAL 120 119 119 VAL VAL C . n 
C 1 121 HIS 121 120 120 HIS HIS C . n 
C 1 122 GLU 122 121 121 GLU GLU C . n 
C 1 123 LYS 123 122 122 LYS LYS C . n 
C 1 124 ALA 124 123 123 ALA ALA C . n 
C 1 125 ASP 125 124 124 ASP ASP C . n 
C 1 126 ASP 126 125 125 ASP ASP C . n 
C 1 127 LEU 127 126 126 LEU LEU C . n 
C 1 128 GLY 128 127 127 GLY GLY C . n 
C 1 129 LYS 129 128 128 LYS LYS C . n 
C 1 130 GLY 130 129 129 GLY GLY C . n 
C 1 131 GLY 131 130 130 GLY GLY C . n 
C 1 132 ASN 132 131 131 ASN ASN C . n 
C 1 133 GLU 133 132 132 GLU GLU C . n 
C 1 134 GLU 134 133 133 GLU GLU C . n 
C 1 135 SER 135 134 134 SER SER C . n 
C 1 136 THR 136 135 135 THR THR C . n 
C 1 137 LYS 137 136 136 LYS LYS C . n 
C 1 138 THR 138 137 137 THR THR C . n 
C 1 139 GLY 139 138 138 GLY GLY C . n 
C 1 140 ASN 140 139 139 ASN ASN C . n 
C 1 141 ALA 141 140 140 ALA ALA C . n 
C 1 142 GLY 142 141 141 GLY GLY C . n 
C 1 143 SER 143 142 142 SER SER C . n 
C 1 144 ARG 144 143 143 ARG ARG C . n 
C 1 145 LEU 145 144 144 LEU LEU C . n 
C 1 146 ALA 146 145 145 ALA ALA C . n 
C 1 147 CYS 147 146 146 CYS CYS C . n 
C 1 148 GLY 148 147 147 GLY GLY C . n 
C 1 149 VAL 149 148 148 VAL VAL C . n 
C 1 150 ILE 150 149 149 ILE ILE C . n 
C 1 151 GLY 151 150 150 GLY GLY C . n 
C 1 152 ILE 152 151 151 ILE ILE C . n 
C 1 153 ALA 153 152 152 ALA ALA C . n 
C 1 154 GLN 154 153 153 GLN GLN C . n 
D 1 1   MET 1   0   ?   ?   ?   D . n 
D 1 2   ALA 2   1   1   ALA ALA D . n 
D 1 3   THR 3   2   2   THR THR D . n 
D 1 4   LYS 4   3   3   LYS LYS D . n 
D 1 5   ALA 5   4   4   ALA ALA D . n 
D 1 6   VAL 6   5   5   VAL VAL D . n 
D 1 7   ALA 7   6   6   ALA ALA D . n 
D 1 8   VAL 8   7   7   VAL VAL D . n 
D 1 9   LEU 9   8   8   LEU LEU D . n 
D 1 10  LYS 10  9   9   LYS LYS D . n 
D 1 11  GLY 11  10  10  GLY GLY D . n 
D 1 12  ASP 12  11  11  ASP ASP D . n 
D 1 13  GLY 13  12  12  GLY GLY D . n 
D 1 14  PRO 14  13  13  PRO PRO D . n 
D 1 15  VAL 15  14  14  VAL VAL D . n 
D 1 16  GLN 16  15  15  GLN GLN D . n 
D 1 17  GLY 17  16  16  GLY GLY D . n 
D 1 18  ILE 18  17  17  ILE ILE D . n 
D 1 19  ILE 19  18  18  ILE ILE D . n 
D 1 20  ASN 20  19  19  ASN ASN D . n 
D 1 21  PHE 21  20  20  PHE PHE D . n 
D 1 22  GLU 22  21  21  GLU GLU D . n 
D 1 23  GLN 23  22  22  GLN GLN D . n 
D 1 24  LYS 24  23  23  LYS LYS D . n 
D 1 25  GLU 25  24  24  GLU GLU D . n 
D 1 26  SER 26  25  25  SER SER D . n 
D 1 27  ASN 27  26  26  ASN ASN D . n 
D 1 28  GLY 28  27  27  GLY GLY D . n 
D 1 29  PRO 29  28  28  PRO PRO D . n 
D 1 30  VAL 30  29  29  VAL VAL D . n 
D 1 31  LYS 31  30  30  LYS LYS D . n 
D 1 32  VAL 32  31  31  VAL VAL D . n 
D 1 33  TRP 33  32  32  TRP TRP D . n 
D 1 34  GLY 34  33  33  GLY GLY D . n 
D 1 35  SER 35  34  34  SER SER D . n 
D 1 36  ILE 36  35  35  ILE ILE D . n 
D 1 37  LYS 37  36  36  LYS LYS D . n 
D 1 38  GLY 38  37  37  GLY GLY D . n 
D 1 39  LEU 39  38  38  LEU LEU D . n 
D 1 40  THR 40  39  39  THR THR D . n 
D 1 41  GLU 41  40  40  GLU GLU D . n 
D 1 42  GLY 42  41  41  GLY GLY D . n 
D 1 43  LEU 43  42  42  LEU LEU D . n 
D 1 44  HIS 44  43  43  HIS HIS D . n 
D 1 45  GLY 45  44  44  GLY GLY D . n 
D 1 46  PHE 46  45  45  PHE PHE D . n 
D 1 47  HIS 47  46  46  HIS HIS D . n 
D 1 48  VAL 48  47  47  VAL VAL D . n 
D 1 49  HIS 49  48  48  HIS HIS D . n 
D 1 50  GLU 50  49  49  GLU GLU D . n 
D 1 51  PHE 51  50  50  PHE PHE D . n 
D 1 52  GLY 52  51  51  GLY GLY D . n 
D 1 53  ASP 53  52  52  ASP ASP D . n 
D 1 54  ASN 54  53  53  ASN ASN D . n 
D 1 55  THR 55  54  54  THR THR D . n 
D 1 56  ALA 56  55  55  ALA ALA D . n 
D 1 57  GLY 57  56  56  GLY GLY D . n 
D 1 58  CYS 58  57  57  CYS CYS D . n 
D 1 59  THR 59  58  58  THR THR D . n 
D 1 60  SER 60  59  59  SER SER D . n 
D 1 61  ALA 61  60  60  ALA ALA D . n 
D 1 62  GLY 62  61  61  GLY GLY D . n 
D 1 63  PRO 63  62  62  PRO PRO D . n 
D 1 64  HIS 64  63  63  HIS HIS D . n 
D 1 65  PHE 65  64  64  PHE PHE D . n 
D 1 66  ASN 66  65  65  ASN ASN D . n 
D 1 67  PRO 67  66  66  PRO PRO D . n 
D 1 68  LEU 68  67  67  LEU LEU D . n 
D 1 69  SER 69  68  68  SER SER D . n 
D 1 70  ARG 70  69  69  ARG ARG D . n 
D 1 71  LYS 71  70  70  LYS LYS D . n 
D 1 72  HIS 72  71  71  HIS HIS D . n 
D 1 73  GLY 73  72  72  GLY GLY D . n 
D 1 74  GLY 74  73  73  GLY GLY D . n 
D 1 75  PRO 75  74  74  PRO PRO D . n 
D 1 76  LYS 76  75  75  LYS LYS D . n 
D 1 77  ASP 77  76  76  ASP ASP D . n 
D 1 78  GLU 78  77  77  GLU GLU D . n 
D 1 79  GLU 79  78  78  GLU GLU D . n 
D 1 80  ARG 80  79  79  ARG ARG D . n 
D 1 81  HIS 81  80  80  HIS HIS D . n 
D 1 82  VAL 82  81  81  VAL VAL D . n 
D 1 83  GLY 83  82  82  GLY GLY D . n 
D 1 84  ASP 84  83  83  ASP ASP D . n 
D 1 85  LEU 85  84  84  LEU LEU D . n 
D 1 86  GLY 86  85  85  GLY GLY D . n 
D 1 87  ASN 87  86  86  ASN ASN D . n 
D 1 88  VAL 88  87  87  VAL VAL D . n 
D 1 89  THR 89  88  88  THR THR D . n 
D 1 90  ALA 90  89  89  ALA ALA D . n 
D 1 91  ASP 91  90  90  ASP ASP D . n 
D 1 92  LYS 92  91  91  LYS LYS D . n 
D 1 93  ASP 93  92  92  ASP ASP D . n 
D 1 94  GLY 94  93  93  GLY GLY D . n 
D 1 95  VAL 95  94  94  VAL VAL D . n 
D 1 96  ALA 96  95  95  ALA ALA D . n 
D 1 97  ASP 97  96  96  ASP ASP D . n 
D 1 98  VAL 98  97  97  VAL VAL D . n 
D 1 99  SER 99  98  98  SER SER D . n 
D 1 100 ILE 100 99  99  ILE ILE D . n 
D 1 101 GLU 101 100 100 GLU GLU D . n 
D 1 102 ASP 102 101 101 ASP ASP D . n 
D 1 103 SER 103 102 102 SER SER D . n 
D 1 104 VAL 104 103 103 VAL VAL D . n 
D 1 105 ILE 105 104 104 ILE ILE D . n 
D 1 106 SER 106 105 105 SER SER D . n 
D 1 107 LEU 107 106 106 LEU LEU D . n 
D 1 108 SER 108 107 107 SER SER D . n 
D 1 109 GLY 109 108 108 GLY GLY D . n 
D 1 110 ASP 110 109 109 ASP ASP D . n 
D 1 111 HIS 111 110 110 HIS HIS D . n 
D 1 112 SER 112 111 111 SER SER D . n 
D 1 113 ILE 113 112 112 ILE ILE D . n 
D 1 114 ILE 114 113 113 ILE ILE D . n 
D 1 115 GLY 115 114 114 GLY GLY D . n 
D 1 116 ARG 116 115 115 ARG ARG D . n 
D 1 117 THR 117 116 116 THR THR D . n 
D 1 118 LEU 118 117 117 LEU LEU D . n 
D 1 119 VAL 119 118 118 VAL VAL D . n 
D 1 120 VAL 120 119 119 VAL VAL D . n 
D 1 121 HIS 121 120 120 HIS HIS D . n 
D 1 122 GLU 122 121 121 GLU GLU D . n 
D 1 123 LYS 123 122 122 LYS LYS D . n 
D 1 124 ALA 124 123 123 ALA ALA D . n 
D 1 125 ASP 125 124 124 ASP ASP D . n 
D 1 126 ASP 126 125 125 ASP ASP D . n 
D 1 127 LEU 127 126 126 LEU LEU D . n 
D 1 128 GLY 128 127 127 GLY GLY D . n 
D 1 129 LYS 129 128 128 LYS LYS D . n 
D 1 130 GLY 130 129 129 GLY GLY D . n 
D 1 131 GLY 131 130 130 GLY GLY D . n 
D 1 132 ASN 132 131 131 ASN ASN D . n 
D 1 133 GLU 133 132 132 GLU GLU D . n 
D 1 134 GLU 134 133 133 GLU GLU D . n 
D 1 135 SER 135 134 134 SER SER D . n 
D 1 136 THR 136 135 135 THR THR D . n 
D 1 137 LYS 137 136 136 LYS LYS D . n 
D 1 138 THR 138 137 137 THR THR D . n 
D 1 139 GLY 139 138 138 GLY GLY D . n 
D 1 140 ASN 140 139 139 ASN ASN D . n 
D 1 141 ALA 141 140 140 ALA ALA D . n 
D 1 142 GLY 142 141 141 GLY GLY D . n 
D 1 143 SER 143 142 142 SER SER D . n 
D 1 144 ARG 144 143 143 ARG ARG D . n 
D 1 145 LEU 145 144 144 LEU LEU D . n 
D 1 146 ALA 146 145 145 ALA ALA D . n 
D 1 147 CYS 147 146 146 CYS CYS D . n 
D 1 148 GLY 148 147 147 GLY GLY D . n 
D 1 149 VAL 149 148 148 VAL VAL D . n 
D 1 150 ILE 150 149 149 ILE ILE D . n 
D 1 151 GLY 151 150 150 GLY GLY D . n 
D 1 152 ILE 152 151 151 ILE ILE D . n 
D 1 153 ALA 153 152 152 ALA ALA D . n 
D 1 154 GLN 154 153 153 GLN GLN D . n 
E 1 1   MET 1   0   ?   ?   ?   E . n 
E 1 2   ALA 2   1   1   ALA ALA E . n 
E 1 3   THR 3   2   2   THR THR E . n 
E 1 4   LYS 4   3   3   LYS LYS E . n 
E 1 5   ALA 5   4   4   ALA ALA E . n 
E 1 6   VAL 6   5   5   VAL VAL E . n 
E 1 7   ALA 7   6   6   ALA ALA E . n 
E 1 8   VAL 8   7   7   VAL VAL E . n 
E 1 9   LEU 9   8   8   LEU LEU E . n 
E 1 10  LYS 10  9   9   LYS LYS E . n 
E 1 11  GLY 11  10  10  GLY GLY E . n 
E 1 12  ASP 12  11  11  ASP ASP E . n 
E 1 13  GLY 13  12  12  GLY GLY E . n 
E 1 14  PRO 14  13  13  PRO PRO E . n 
E 1 15  VAL 15  14  14  VAL VAL E . n 
E 1 16  GLN 16  15  15  GLN GLN E . n 
E 1 17  GLY 17  16  16  GLY GLY E . n 
E 1 18  ILE 18  17  17  ILE ILE E . n 
E 1 19  ILE 19  18  18  ILE ILE E . n 
E 1 20  ASN 20  19  19  ASN ASN E . n 
E 1 21  PHE 21  20  20  PHE PHE E . n 
E 1 22  GLU 22  21  21  GLU GLU E . n 
E 1 23  GLN 23  22  22  GLN GLN E . n 
E 1 24  LYS 24  23  23  LYS LYS E . n 
E 1 25  GLU 25  24  24  GLU GLU E . n 
E 1 26  SER 26  25  25  SER SER E . n 
E 1 27  ASN 27  26  26  ASN ASN E . n 
E 1 28  GLY 28  27  27  GLY GLY E . n 
E 1 29  PRO 29  28  28  PRO PRO E . n 
E 1 30  VAL 30  29  29  VAL VAL E . n 
E 1 31  LYS 31  30  30  LYS LYS E . n 
E 1 32  VAL 32  31  31  VAL VAL E . n 
E 1 33  TRP 33  32  32  TRP TRP E . n 
E 1 34  GLY 34  33  33  GLY GLY E . n 
E 1 35  SER 35  34  34  SER SER E . n 
E 1 36  ILE 36  35  35  ILE ILE E . n 
E 1 37  LYS 37  36  36  LYS LYS E . n 
E 1 38  GLY 38  37  37  GLY GLY E . n 
E 1 39  LEU 39  38  38  LEU LEU E . n 
E 1 40  THR 40  39  39  THR THR E . n 
E 1 41  GLU 41  40  40  GLU GLU E . n 
E 1 42  GLY 42  41  41  GLY GLY E . n 
E 1 43  LEU 43  42  42  LEU LEU E . n 
E 1 44  HIS 44  43  43  HIS HIS E . n 
E 1 45  GLY 45  44  44  GLY GLY E . n 
E 1 46  PHE 46  45  45  PHE PHE E . n 
E 1 47  HIS 47  46  46  HIS HIS E . n 
E 1 48  VAL 48  47  47  VAL VAL E . n 
E 1 49  HIS 49  48  48  HIS HIS E . n 
E 1 50  GLU 50  49  49  GLU GLU E . n 
E 1 51  PHE 51  50  50  PHE PHE E . n 
E 1 52  GLY 52  51  51  GLY GLY E . n 
E 1 53  ASP 53  52  52  ASP ASP E . n 
E 1 54  ASN 54  53  53  ASN ASN E . n 
E 1 55  THR 55  54  54  THR THR E . n 
E 1 56  ALA 56  55  55  ALA ALA E . n 
E 1 57  GLY 57  56  56  GLY GLY E . n 
E 1 58  CYS 58  57  57  CYS CYS E . n 
E 1 59  THR 59  58  58  THR THR E . n 
E 1 60  SER 60  59  59  SER SER E . n 
E 1 61  ALA 61  60  60  ALA ALA E . n 
E 1 62  GLY 62  61  61  GLY GLY E . n 
E 1 63  PRO 63  62  62  PRO PRO E . n 
E 1 64  HIS 64  63  63  HIS HIS E . n 
E 1 65  PHE 65  64  64  PHE PHE E . n 
E 1 66  ASN 66  65  65  ASN ASN E . n 
E 1 67  PRO 67  66  66  PRO PRO E . n 
E 1 68  LEU 68  67  67  LEU LEU E . n 
E 1 69  SER 69  68  68  SER SER E . n 
E 1 70  ARG 70  69  69  ARG ARG E . n 
E 1 71  LYS 71  70  70  LYS LYS E . n 
E 1 72  HIS 72  71  71  HIS HIS E . n 
E 1 73  GLY 73  72  72  GLY GLY E . n 
E 1 74  GLY 74  73  73  GLY GLY E . n 
E 1 75  PRO 75  74  74  PRO PRO E . n 
E 1 76  LYS 76  75  75  LYS LYS E . n 
E 1 77  ASP 77  76  76  ASP ASP E . n 
E 1 78  GLU 78  77  77  GLU GLU E . n 
E 1 79  GLU 79  78  78  GLU GLU E . n 
E 1 80  ARG 80  79  79  ARG ARG E . n 
E 1 81  HIS 81  80  80  HIS HIS E . n 
E 1 82  VAL 82  81  81  VAL VAL E . n 
E 1 83  GLY 83  82  82  GLY GLY E . n 
E 1 84  ASP 84  83  83  ASP ASP E . n 
E 1 85  LEU 85  84  84  LEU LEU E . n 
E 1 86  GLY 86  85  85  GLY GLY E . n 
E 1 87  ASN 87  86  86  ASN ASN E . n 
E 1 88  VAL 88  87  87  VAL VAL E . n 
E 1 89  THR 89  88  88  THR THR E . n 
E 1 90  ALA 90  89  89  ALA ALA E . n 
E 1 91  ASP 91  90  90  ASP ASP E . n 
E 1 92  LYS 92  91  91  LYS LYS E . n 
E 1 93  ASP 93  92  92  ASP ASP E . n 
E 1 94  GLY 94  93  93  GLY GLY E . n 
E 1 95  VAL 95  94  94  VAL VAL E . n 
E 1 96  ALA 96  95  95  ALA ALA E . n 
E 1 97  ASP 97  96  96  ASP ASP E . n 
E 1 98  VAL 98  97  97  VAL VAL E . n 
E 1 99  SER 99  98  98  SER SER E . n 
E 1 100 ILE 100 99  99  ILE ILE E . n 
E 1 101 GLU 101 100 100 GLU GLU E . n 
E 1 102 ASP 102 101 101 ASP ASP E . n 
E 1 103 SER 103 102 102 SER SER E . n 
E 1 104 VAL 104 103 103 VAL VAL E . n 
E 1 105 ILE 105 104 104 ILE ILE E . n 
E 1 106 SER 106 105 105 SER SER E . n 
E 1 107 LEU 107 106 106 LEU LEU E . n 
E 1 108 SER 108 107 107 SER SER E . n 
E 1 109 GLY 109 108 108 GLY GLY E . n 
E 1 110 ASP 110 109 109 ASP ASP E . n 
E 1 111 HIS 111 110 110 HIS HIS E . n 
E 1 112 SER 112 111 111 SER SER E . n 
E 1 113 ILE 113 112 112 ILE ILE E . n 
E 1 114 ILE 114 113 113 ILE ILE E . n 
E 1 115 GLY 115 114 114 GLY GLY E . n 
E 1 116 ARG 116 115 115 ARG ARG E . n 
E 1 117 THR 117 116 116 THR THR E . n 
E 1 118 LEU 118 117 117 LEU LEU E . n 
E 1 119 VAL 119 118 118 VAL VAL E . n 
E 1 120 VAL 120 119 119 VAL VAL E . n 
E 1 121 HIS 121 120 120 HIS HIS E . n 
E 1 122 GLU 122 121 121 GLU GLU E . n 
E 1 123 LYS 123 122 122 LYS LYS E . n 
E 1 124 ALA 124 123 123 ALA ALA E . n 
E 1 125 ASP 125 124 124 ASP ASP E . n 
E 1 126 ASP 126 125 125 ASP ASP E . n 
E 1 127 LEU 127 126 126 LEU LEU E . n 
E 1 128 GLY 128 127 127 GLY GLY E . n 
E 1 129 LYS 129 128 128 LYS LYS E . n 
E 1 130 GLY 130 129 129 GLY GLY E . n 
E 1 131 GLY 131 130 130 GLY GLY E . n 
E 1 132 ASN 132 131 131 ASN ASN E . n 
E 1 133 GLU 133 132 132 GLU GLU E . n 
E 1 134 GLU 134 133 133 GLU GLU E . n 
E 1 135 SER 135 134 134 SER SER E . n 
E 1 136 THR 136 135 135 THR THR E . n 
E 1 137 LYS 137 136 136 LYS LYS E . n 
E 1 138 THR 138 137 137 THR THR E . n 
E 1 139 GLY 139 138 138 GLY GLY E . n 
E 1 140 ASN 140 139 139 ASN ASN E . n 
E 1 141 ALA 141 140 140 ALA ALA E . n 
E 1 142 GLY 142 141 141 GLY GLY E . n 
E 1 143 SER 143 142 142 SER SER E . n 
E 1 144 ARG 144 143 143 ARG ARG E . n 
E 1 145 LEU 145 144 144 LEU LEU E . n 
E 1 146 ALA 146 145 145 ALA ALA E . n 
E 1 147 CYS 147 146 146 CYS CYS E . n 
E 1 148 GLY 148 147 147 GLY GLY E . n 
E 1 149 VAL 149 148 148 VAL VAL E . n 
E 1 150 ILE 150 149 149 ILE ILE E . n 
E 1 151 GLY 151 150 150 GLY GLY E . n 
E 1 152 ILE 152 151 151 ILE ILE E . n 
E 1 153 ALA 153 152 152 ALA ALA E . n 
E 1 154 GLN 154 153 153 GLN GLN E . n 
F 1 1   MET 1   0   ?   ?   ?   F . n 
F 1 2   ALA 2   1   1   ALA ALA F . n 
F 1 3   THR 3   2   2   THR THR F . n 
F 1 4   LYS 4   3   3   LYS LYS F . n 
F 1 5   ALA 5   4   4   ALA ALA F . n 
F 1 6   VAL 6   5   5   VAL VAL F . n 
F 1 7   ALA 7   6   6   ALA ALA F . n 
F 1 8   VAL 8   7   7   VAL VAL F . n 
F 1 9   LEU 9   8   8   LEU LEU F . n 
F 1 10  LYS 10  9   9   LYS LYS F . n 
F 1 11  GLY 11  10  10  GLY GLY F . n 
F 1 12  ASP 12  11  11  ASP ASP F . n 
F 1 13  GLY 13  12  12  GLY GLY F . n 
F 1 14  PRO 14  13  13  PRO PRO F . n 
F 1 15  VAL 15  14  14  VAL VAL F . n 
F 1 16  GLN 16  15  15  GLN GLN F . n 
F 1 17  GLY 17  16  16  GLY GLY F . n 
F 1 18  ILE 18  17  17  ILE ILE F . n 
F 1 19  ILE 19  18  18  ILE ILE F . n 
F 1 20  ASN 20  19  19  ASN ASN F . n 
F 1 21  PHE 21  20  20  PHE PHE F . n 
F 1 22  GLU 22  21  21  GLU GLU F . n 
F 1 23  GLN 23  22  22  GLN GLN F . n 
F 1 24  LYS 24  23  23  LYS LYS F . n 
F 1 25  GLU 25  24  24  GLU GLU F . n 
F 1 26  SER 26  25  25  SER SER F . n 
F 1 27  ASN 27  26  26  ASN ASN F . n 
F 1 28  GLY 28  27  27  GLY GLY F . n 
F 1 29  PRO 29  28  28  PRO PRO F . n 
F 1 30  VAL 30  29  29  VAL VAL F . n 
F 1 31  LYS 31  30  30  LYS LYS F . n 
F 1 32  VAL 32  31  31  VAL VAL F . n 
F 1 33  TRP 33  32  32  TRP TRP F . n 
F 1 34  GLY 34  33  33  GLY GLY F . n 
F 1 35  SER 35  34  34  SER SER F . n 
F 1 36  ILE 36  35  35  ILE ILE F . n 
F 1 37  LYS 37  36  36  LYS LYS F . n 
F 1 38  GLY 38  37  37  GLY GLY F . n 
F 1 39  LEU 39  38  38  LEU LEU F . n 
F 1 40  THR 40  39  39  THR THR F . n 
F 1 41  GLU 41  40  40  GLU GLU F . n 
F 1 42  GLY 42  41  41  GLY GLY F . n 
F 1 43  LEU 43  42  42  LEU LEU F . n 
F 1 44  HIS 44  43  43  HIS HIS F . n 
F 1 45  GLY 45  44  44  GLY GLY F . n 
F 1 46  PHE 46  45  45  PHE PHE F . n 
F 1 47  HIS 47  46  46  HIS HIS F . n 
F 1 48  VAL 48  47  47  VAL VAL F . n 
F 1 49  HIS 49  48  48  HIS HIS F . n 
F 1 50  GLU 50  49  49  GLU GLU F . n 
F 1 51  PHE 51  50  50  PHE PHE F . n 
F 1 52  GLY 52  51  51  GLY GLY F . n 
F 1 53  ASP 53  52  52  ASP ASP F . n 
F 1 54  ASN 54  53  53  ASN ASN F . n 
F 1 55  THR 55  54  54  THR THR F . n 
F 1 56  ALA 56  55  55  ALA ALA F . n 
F 1 57  GLY 57  56  56  GLY GLY F . n 
F 1 58  CYS 58  57  57  CYS CYS F . n 
F 1 59  THR 59  58  58  THR THR F . n 
F 1 60  SER 60  59  59  SER SER F . n 
F 1 61  ALA 61  60  60  ALA ALA F . n 
F 1 62  GLY 62  61  61  GLY GLY F . n 
F 1 63  PRO 63  62  62  PRO PRO F . n 
F 1 64  HIS 64  63  63  HIS HIS F . n 
F 1 65  PHE 65  64  64  PHE PHE F . n 
F 1 66  ASN 66  65  65  ASN ASN F . n 
F 1 67  PRO 67  66  66  PRO PRO F . n 
F 1 68  LEU 68  67  67  LEU LEU F . n 
F 1 69  SER 69  68  68  SER SER F . n 
F 1 70  ARG 70  69  69  ARG ARG F . n 
F 1 71  LYS 71  70  70  LYS LYS F . n 
F 1 72  HIS 72  71  71  HIS HIS F . n 
F 1 73  GLY 73  72  72  GLY GLY F . n 
F 1 74  GLY 74  73  73  GLY GLY F . n 
F 1 75  PRO 75  74  74  PRO PRO F . n 
F 1 76  LYS 76  75  75  LYS LYS F . n 
F 1 77  ASP 77  76  76  ASP ASP F . n 
F 1 78  GLU 78  77  77  GLU GLU F . n 
F 1 79  GLU 79  78  78  GLU GLU F . n 
F 1 80  ARG 80  79  79  ARG ARG F . n 
F 1 81  HIS 81  80  80  HIS HIS F . n 
F 1 82  VAL 82  81  81  VAL VAL F . n 
F 1 83  GLY 83  82  82  GLY GLY F . n 
F 1 84  ASP 84  83  83  ASP ASP F . n 
F 1 85  LEU 85  84  84  LEU LEU F . n 
F 1 86  GLY 86  85  85  GLY GLY F . n 
F 1 87  ASN 87  86  86  ASN ASN F . n 
F 1 88  VAL 88  87  87  VAL VAL F . n 
F 1 89  THR 89  88  88  THR THR F . n 
F 1 90  ALA 90  89  89  ALA ALA F . n 
F 1 91  ASP 91  90  90  ASP ASP F . n 
F 1 92  LYS 92  91  91  LYS LYS F . n 
F 1 93  ASP 93  92  92  ASP ASP F . n 
F 1 94  GLY 94  93  93  GLY GLY F . n 
F 1 95  VAL 95  94  94  VAL VAL F . n 
F 1 96  ALA 96  95  95  ALA ALA F . n 
F 1 97  ASP 97  96  96  ASP ASP F . n 
F 1 98  VAL 98  97  97  VAL VAL F . n 
F 1 99  SER 99  98  98  SER SER F . n 
F 1 100 ILE 100 99  99  ILE ILE F . n 
F 1 101 GLU 101 100 100 GLU GLU F . n 
F 1 102 ASP 102 101 101 ASP ASP F . n 
F 1 103 SER 103 102 102 SER SER F . n 
F 1 104 VAL 104 103 103 VAL VAL F . n 
F 1 105 ILE 105 104 104 ILE ILE F . n 
F 1 106 SER 106 105 105 SER SER F . n 
F 1 107 LEU 107 106 106 LEU LEU F . n 
F 1 108 SER 108 107 107 SER SER F . n 
F 1 109 GLY 109 108 108 GLY GLY F . n 
F 1 110 ASP 110 109 109 ASP ASP F . n 
F 1 111 HIS 111 110 110 HIS HIS F . n 
F 1 112 SER 112 111 111 SER SER F . n 
F 1 113 ILE 113 112 112 ILE ILE F . n 
F 1 114 ILE 114 113 113 ILE ILE F . n 
F 1 115 GLY 115 114 114 GLY GLY F . n 
F 1 116 ARG 116 115 115 ARG ARG F . n 
F 1 117 THR 117 116 116 THR THR F . n 
F 1 118 LEU 118 117 117 LEU LEU F . n 
F 1 119 VAL 119 118 118 VAL VAL F . n 
F 1 120 VAL 120 119 119 VAL VAL F . n 
F 1 121 HIS 121 120 120 HIS HIS F . n 
F 1 122 GLU 122 121 121 GLU GLU F . n 
F 1 123 LYS 123 122 122 LYS LYS F . n 
F 1 124 ALA 124 123 123 ALA ALA F . n 
F 1 125 ASP 125 124 124 ASP ASP F . n 
F 1 126 ASP 126 125 125 ASP ASP F . n 
F 1 127 LEU 127 126 126 LEU LEU F . n 
F 1 128 GLY 128 127 127 GLY GLY F . n 
F 1 129 LYS 129 128 128 LYS LYS F . n 
F 1 130 GLY 130 129 129 GLY GLY F . n 
F 1 131 GLY 131 130 130 GLY GLY F . n 
F 1 132 ASN 132 131 131 ASN ASN F . n 
F 1 133 GLU 133 132 132 GLU GLU F . n 
F 1 134 GLU 134 133 133 GLU GLU F . n 
F 1 135 SER 135 134 134 SER SER F . n 
F 1 136 THR 136 135 135 THR THR F . n 
F 1 137 LYS 137 136 136 LYS LYS F . n 
F 1 138 THR 138 137 137 THR THR F . n 
F 1 139 GLY 139 138 138 GLY GLY F . n 
F 1 140 ASN 140 139 139 ASN ASN F . n 
F 1 141 ALA 141 140 140 ALA ALA F . n 
F 1 142 GLY 142 141 141 GLY GLY F . n 
F 1 143 SER 143 142 142 SER SER F . n 
F 1 144 ARG 144 143 143 ARG ARG F . n 
F 1 145 LEU 145 144 144 LEU LEU F . n 
F 1 146 ALA 146 145 145 ALA ALA F . n 
F 1 147 CYS 147 146 146 CYS CYS F . n 
F 1 148 GLY 148 147 147 GLY GLY F . n 
F 1 149 VAL 149 148 148 VAL VAL F . n 
F 1 150 ILE 150 149 149 ILE ILE F . n 
F 1 151 GLY 151 150 150 GLY GLY F . n 
F 1 152 ILE 152 151 151 ILE ILE F . n 
F 1 153 ALA 153 152 152 ALA ALA F . n 
F 1 154 GLN 154 153 153 GLN GLN F . n 
G 1 1   MET 1   0   ?   ?   ?   G . n 
G 1 2   ALA 2   1   1   ALA ALA G . n 
G 1 3   THR 3   2   2   THR THR G . n 
G 1 4   LYS 4   3   3   LYS LYS G . n 
G 1 5   ALA 5   4   4   ALA ALA G . n 
G 1 6   VAL 6   5   5   VAL VAL G . n 
G 1 7   ALA 7   6   6   ALA ALA G . n 
G 1 8   VAL 8   7   7   VAL VAL G . n 
G 1 9   LEU 9   8   8   LEU LEU G . n 
G 1 10  LYS 10  9   9   LYS LYS G . n 
G 1 11  GLY 11  10  10  GLY GLY G . n 
G 1 12  ASP 12  11  11  ASP ASP G . n 
G 1 13  GLY 13  12  12  GLY GLY G . n 
G 1 14  PRO 14  13  13  PRO PRO G . n 
G 1 15  VAL 15  14  14  VAL VAL G . n 
G 1 16  GLN 16  15  15  GLN GLN G . n 
G 1 17  GLY 17  16  16  GLY GLY G . n 
G 1 18  ILE 18  17  17  ILE ILE G . n 
G 1 19  ILE 19  18  18  ILE ILE G . n 
G 1 20  ASN 20  19  19  ASN ASN G . n 
G 1 21  PHE 21  20  20  PHE PHE G . n 
G 1 22  GLU 22  21  21  GLU GLU G . n 
G 1 23  GLN 23  22  22  GLN GLN G . n 
G 1 24  LYS 24  23  23  LYS LYS G . n 
G 1 25  GLU 25  24  24  GLU GLU G . n 
G 1 26  SER 26  25  25  SER SER G . n 
G 1 27  ASN 27  26  26  ASN ASN G . n 
G 1 28  GLY 28  27  27  GLY GLY G . n 
G 1 29  PRO 29  28  28  PRO PRO G . n 
G 1 30  VAL 30  29  29  VAL VAL G . n 
G 1 31  LYS 31  30  30  LYS LYS G . n 
G 1 32  VAL 32  31  31  VAL VAL G . n 
G 1 33  TRP 33  32  32  TRP TRP G . n 
G 1 34  GLY 34  33  33  GLY GLY G . n 
G 1 35  SER 35  34  34  SER SER G . n 
G 1 36  ILE 36  35  35  ILE ILE G . n 
G 1 37  LYS 37  36  36  LYS LYS G . n 
G 1 38  GLY 38  37  37  GLY GLY G . n 
G 1 39  LEU 39  38  38  LEU LEU G . n 
G 1 40  THR 40  39  39  THR THR G . n 
G 1 41  GLU 41  40  40  GLU GLU G . n 
G 1 42  GLY 42  41  41  GLY GLY G . n 
G 1 43  LEU 43  42  42  LEU LEU G . n 
G 1 44  HIS 44  43  43  HIS HIS G . n 
G 1 45  GLY 45  44  44  GLY GLY G . n 
G 1 46  PHE 46  45  45  PHE PHE G . n 
G 1 47  HIS 47  46  46  HIS HIS G . n 
G 1 48  VAL 48  47  47  VAL VAL G . n 
G 1 49  HIS 49  48  48  HIS HIS G . n 
G 1 50  GLU 50  49  49  GLU GLU G . n 
G 1 51  PHE 51  50  50  PHE PHE G . n 
G 1 52  GLY 52  51  51  GLY GLY G . n 
G 1 53  ASP 53  52  52  ASP ASP G . n 
G 1 54  ASN 54  53  53  ASN ASN G . n 
G 1 55  THR 55  54  54  THR THR G . n 
G 1 56  ALA 56  55  55  ALA ALA G . n 
G 1 57  GLY 57  56  56  GLY GLY G . n 
G 1 58  CYS 58  57  57  CYS CYS G . n 
G 1 59  THR 59  58  58  THR THR G . n 
G 1 60  SER 60  59  59  SER SER G . n 
G 1 61  ALA 61  60  60  ALA ALA G . n 
G 1 62  GLY 62  61  61  GLY GLY G . n 
G 1 63  PRO 63  62  62  PRO PRO G . n 
G 1 64  HIS 64  63  63  HIS HIS G . n 
G 1 65  PHE 65  64  64  PHE PHE G . n 
G 1 66  ASN 66  65  65  ASN ASN G . n 
G 1 67  PRO 67  66  66  PRO PRO G . n 
G 1 68  LEU 68  67  67  LEU LEU G . n 
G 1 69  SER 69  68  68  SER SER G . n 
G 1 70  ARG 70  69  69  ARG ARG G . n 
G 1 71  LYS 71  70  70  LYS LYS G . n 
G 1 72  HIS 72  71  71  HIS HIS G . n 
G 1 73  GLY 73  72  72  GLY GLY G . n 
G 1 74  GLY 74  73  73  GLY GLY G . n 
G 1 75  PRO 75  74  74  PRO PRO G . n 
G 1 76  LYS 76  75  75  LYS LYS G . n 
G 1 77  ASP 77  76  76  ASP ASP G . n 
G 1 78  GLU 78  77  77  GLU GLU G . n 
G 1 79  GLU 79  78  78  GLU GLU G . n 
G 1 80  ARG 80  79  79  ARG ARG G . n 
G 1 81  HIS 81  80  80  HIS HIS G . n 
G 1 82  VAL 82  81  81  VAL VAL G . n 
G 1 83  GLY 83  82  82  GLY GLY G . n 
G 1 84  ASP 84  83  83  ASP ASP G . n 
G 1 85  LEU 85  84  84  LEU LEU G . n 
G 1 86  GLY 86  85  85  GLY GLY G . n 
G 1 87  ASN 87  86  86  ASN ASN G . n 
G 1 88  VAL 88  87  87  VAL VAL G . n 
G 1 89  THR 89  88  88  THR THR G . n 
G 1 90  ALA 90  89  89  ALA ALA G . n 
G 1 91  ASP 91  90  90  ASP ASP G . n 
G 1 92  LYS 92  91  91  LYS LYS G . n 
G 1 93  ASP 93  92  92  ASP ASP G . n 
G 1 94  GLY 94  93  93  GLY GLY G . n 
G 1 95  VAL 95  94  94  VAL VAL G . n 
G 1 96  ALA 96  95  95  ALA ALA G . n 
G 1 97  ASP 97  96  96  ASP ASP G . n 
G 1 98  VAL 98  97  97  VAL VAL G . n 
G 1 99  SER 99  98  98  SER SER G . n 
G 1 100 ILE 100 99  99  ILE ILE G . n 
G 1 101 GLU 101 100 100 GLU GLU G . n 
G 1 102 ASP 102 101 101 ASP ASP G . n 
G 1 103 SER 103 102 102 SER SER G . n 
G 1 104 VAL 104 103 103 VAL VAL G . n 
G 1 105 ILE 105 104 104 ILE ILE G . n 
G 1 106 SER 106 105 105 SER SER G . n 
G 1 107 LEU 107 106 106 LEU LEU G . n 
G 1 108 SER 108 107 107 SER SER G . n 
G 1 109 GLY 109 108 108 GLY GLY G . n 
G 1 110 ASP 110 109 109 ASP ASP G . n 
G 1 111 HIS 111 110 110 HIS HIS G . n 
G 1 112 SER 112 111 111 SER SER G . n 
G 1 113 ILE 113 112 112 ILE ILE G . n 
G 1 114 ILE 114 113 113 ILE ILE G . n 
G 1 115 GLY 115 114 114 GLY GLY G . n 
G 1 116 ARG 116 115 115 ARG ARG G . n 
G 1 117 THR 117 116 116 THR THR G . n 
G 1 118 LEU 118 117 117 LEU LEU G . n 
G 1 119 VAL 119 118 118 VAL VAL G . n 
G 1 120 VAL 120 119 119 VAL VAL G . n 
G 1 121 HIS 121 120 120 HIS HIS G . n 
G 1 122 GLU 122 121 121 GLU GLU G . n 
G 1 123 LYS 123 122 122 LYS LYS G . n 
G 1 124 ALA 124 123 123 ALA ALA G . n 
G 1 125 ASP 125 124 124 ASP ASP G . n 
G 1 126 ASP 126 125 125 ASP ASP G . n 
G 1 127 LEU 127 126 126 LEU LEU G . n 
G 1 128 GLY 128 127 127 GLY GLY G . n 
G 1 129 LYS 129 128 128 LYS LYS G . n 
G 1 130 GLY 130 129 129 GLY GLY G . n 
G 1 131 GLY 131 130 130 GLY GLY G . n 
G 1 132 ASN 132 131 131 ASN ASN G . n 
G 1 133 GLU 133 132 132 GLU GLU G . n 
G 1 134 GLU 134 133 133 GLU GLU G . n 
G 1 135 SER 135 134 134 SER SER G . n 
G 1 136 THR 136 135 135 THR THR G . n 
G 1 137 LYS 137 136 136 LYS LYS G . n 
G 1 138 THR 138 137 137 THR THR G . n 
G 1 139 GLY 139 138 138 GLY GLY G . n 
G 1 140 ASN 140 139 139 ASN ASN G . n 
G 1 141 ALA 141 140 140 ALA ALA G . n 
G 1 142 GLY 142 141 141 GLY GLY G . n 
G 1 143 SER 143 142 142 SER SER G . n 
G 1 144 ARG 144 143 143 ARG ARG G . n 
G 1 145 LEU 145 144 144 LEU LEU G . n 
G 1 146 ALA 146 145 145 ALA ALA G . n 
G 1 147 CYS 147 146 146 CYS CYS G . n 
G 1 148 GLY 148 147 147 GLY GLY G . n 
G 1 149 VAL 149 148 148 VAL VAL G . n 
G 1 150 ILE 150 149 149 ILE ILE G . n 
G 1 151 GLY 151 150 150 GLY GLY G . n 
G 1 152 ILE 152 151 151 ILE ILE G . n 
G 1 153 ALA 153 152 152 ALA ALA G . n 
G 1 154 GLN 154 153 153 GLN GLN G . n 
H 1 1   MET 1   0   ?   ?   ?   H . n 
H 1 2   ALA 2   1   1   ALA ALA H . n 
H 1 3   THR 3   2   2   THR THR H . n 
H 1 4   LYS 4   3   3   LYS LYS H . n 
H 1 5   ALA 5   4   4   ALA ALA H . n 
H 1 6   VAL 6   5   5   VAL VAL H . n 
H 1 7   ALA 7   6   6   ALA ALA H . n 
H 1 8   VAL 8   7   7   VAL VAL H . n 
H 1 9   LEU 9   8   8   LEU LEU H . n 
H 1 10  LYS 10  9   9   LYS LYS H . n 
H 1 11  GLY 11  10  10  GLY GLY H . n 
H 1 12  ASP 12  11  11  ASP ASP H . n 
H 1 13  GLY 13  12  12  GLY GLY H . n 
H 1 14  PRO 14  13  13  PRO PRO H . n 
H 1 15  VAL 15  14  14  VAL VAL H . n 
H 1 16  GLN 16  15  15  GLN GLN H . n 
H 1 17  GLY 17  16  16  GLY GLY H . n 
H 1 18  ILE 18  17  17  ILE ILE H . n 
H 1 19  ILE 19  18  18  ILE ILE H . n 
H 1 20  ASN 20  19  19  ASN ASN H . n 
H 1 21  PHE 21  20  20  PHE PHE H . n 
H 1 22  GLU 22  21  21  GLU GLU H . n 
H 1 23  GLN 23  22  22  GLN GLN H . n 
H 1 24  LYS 24  23  23  LYS LYS H . n 
H 1 25  GLU 25  24  24  GLU GLU H . n 
H 1 26  SER 26  25  25  SER SER H . n 
H 1 27  ASN 27  26  26  ASN ASN H . n 
H 1 28  GLY 28  27  27  GLY GLY H . n 
H 1 29  PRO 29  28  28  PRO PRO H . n 
H 1 30  VAL 30  29  29  VAL VAL H . n 
H 1 31  LYS 31  30  30  LYS LYS H . n 
H 1 32  VAL 32  31  31  VAL VAL H . n 
H 1 33  TRP 33  32  32  TRP TRP H . n 
H 1 34  GLY 34  33  33  GLY GLY H . n 
H 1 35  SER 35  34  34  SER SER H . n 
H 1 36  ILE 36  35  35  ILE ILE H . n 
H 1 37  LYS 37  36  36  LYS LYS H . n 
H 1 38  GLY 38  37  37  GLY GLY H . n 
H 1 39  LEU 39  38  38  LEU LEU H . n 
H 1 40  THR 40  39  39  THR THR H . n 
H 1 41  GLU 41  40  40  GLU GLU H . n 
H 1 42  GLY 42  41  41  GLY GLY H . n 
H 1 43  LEU 43  42  42  LEU LEU H . n 
H 1 44  HIS 44  43  43  HIS HIS H . n 
H 1 45  GLY 45  44  44  GLY GLY H . n 
H 1 46  PHE 46  45  45  PHE PHE H . n 
H 1 47  HIS 47  46  46  HIS HIS H . n 
H 1 48  VAL 48  47  47  VAL VAL H . n 
H 1 49  HIS 49  48  48  HIS HIS H . n 
H 1 50  GLU 50  49  49  GLU GLU H . n 
H 1 51  PHE 51  50  50  PHE PHE H . n 
H 1 52  GLY 52  51  51  GLY GLY H . n 
H 1 53  ASP 53  52  52  ASP ASP H . n 
H 1 54  ASN 54  53  53  ASN ASN H . n 
H 1 55  THR 55  54  54  THR THR H . n 
H 1 56  ALA 56  55  55  ALA ALA H . n 
H 1 57  GLY 57  56  56  GLY GLY H . n 
H 1 58  CYS 58  57  57  CYS CYS H . n 
H 1 59  THR 59  58  58  THR THR H . n 
H 1 60  SER 60  59  59  SER SER H . n 
H 1 61  ALA 61  60  60  ALA ALA H . n 
H 1 62  GLY 62  61  61  GLY GLY H . n 
H 1 63  PRO 63  62  62  PRO PRO H . n 
H 1 64  HIS 64  63  63  HIS HIS H . n 
H 1 65  PHE 65  64  64  PHE PHE H . n 
H 1 66  ASN 66  65  65  ASN ASN H . n 
H 1 67  PRO 67  66  66  PRO PRO H . n 
H 1 68  LEU 68  67  67  LEU LEU H . n 
H 1 69  SER 69  68  68  SER SER H . n 
H 1 70  ARG 70  69  69  ARG ARG H . n 
H 1 71  LYS 71  70  70  LYS LYS H . n 
H 1 72  HIS 72  71  71  HIS HIS H . n 
H 1 73  GLY 73  72  72  GLY GLY H . n 
H 1 74  GLY 74  73  73  GLY GLY H . n 
H 1 75  PRO 75  74  74  PRO PRO H . n 
H 1 76  LYS 76  75  75  LYS LYS H . n 
H 1 77  ASP 77  76  76  ASP ASP H . n 
H 1 78  GLU 78  77  77  GLU GLU H . n 
H 1 79  GLU 79  78  78  GLU GLU H . n 
H 1 80  ARG 80  79  79  ARG ARG H . n 
H 1 81  HIS 81  80  80  HIS HIS H . n 
H 1 82  VAL 82  81  81  VAL VAL H . n 
H 1 83  GLY 83  82  82  GLY GLY H . n 
H 1 84  ASP 84  83  83  ASP ASP H . n 
H 1 85  LEU 85  84  84  LEU LEU H . n 
H 1 86  GLY 86  85  85  GLY GLY H . n 
H 1 87  ASN 87  86  86  ASN ASN H . n 
H 1 88  VAL 88  87  87  VAL VAL H . n 
H 1 89  THR 89  88  88  THR THR H . n 
H 1 90  ALA 90  89  89  ALA ALA H . n 
H 1 91  ASP 91  90  90  ASP ASP H . n 
H 1 92  LYS 92  91  91  LYS LYS H . n 
H 1 93  ASP 93  92  92  ASP ASP H . n 
H 1 94  GLY 94  93  93  GLY GLY H . n 
H 1 95  VAL 95  94  94  VAL VAL H . n 
H 1 96  ALA 96  95  95  ALA ALA H . n 
H 1 97  ASP 97  96  96  ASP ASP H . n 
H 1 98  VAL 98  97  97  VAL VAL H . n 
H 1 99  SER 99  98  98  SER SER H . n 
H 1 100 ILE 100 99  99  ILE ILE H . n 
H 1 101 GLU 101 100 100 GLU GLU H . n 
H 1 102 ASP 102 101 101 ASP ASP H . n 
H 1 103 SER 103 102 102 SER SER H . n 
H 1 104 VAL 104 103 103 VAL VAL H . n 
H 1 105 ILE 105 104 104 ILE ILE H . n 
H 1 106 SER 106 105 105 SER SER H . n 
H 1 107 LEU 107 106 106 LEU LEU H . n 
H 1 108 SER 108 107 107 SER SER H . n 
H 1 109 GLY 109 108 108 GLY GLY H . n 
H 1 110 ASP 110 109 109 ASP ASP H . n 
H 1 111 HIS 111 110 110 HIS HIS H . n 
H 1 112 SER 112 111 111 SER SER H . n 
H 1 113 ILE 113 112 112 ILE ILE H . n 
H 1 114 ILE 114 113 113 ILE ILE H . n 
H 1 115 GLY 115 114 114 GLY GLY H . n 
H 1 116 ARG 116 115 115 ARG ARG H . n 
H 1 117 THR 117 116 116 THR THR H . n 
H 1 118 LEU 118 117 117 LEU LEU H . n 
H 1 119 VAL 119 118 118 VAL VAL H . n 
H 1 120 VAL 120 119 119 VAL VAL H . n 
H 1 121 HIS 121 120 120 HIS HIS H . n 
H 1 122 GLU 122 121 121 GLU GLU H . n 
H 1 123 LYS 123 122 122 LYS LYS H . n 
H 1 124 ALA 124 123 123 ALA ALA H . n 
H 1 125 ASP 125 124 124 ASP ASP H . n 
H 1 126 ASP 126 125 125 ASP ASP H . n 
H 1 127 LEU 127 126 126 LEU LEU H . n 
H 1 128 GLY 128 127 127 GLY GLY H . n 
H 1 129 LYS 129 128 128 LYS LYS H . n 
H 1 130 GLY 130 129 129 GLY GLY H . n 
H 1 131 GLY 131 130 130 GLY GLY H . n 
H 1 132 ASN 132 131 131 ASN ASN H . n 
H 1 133 GLU 133 132 132 GLU GLU H . n 
H 1 134 GLU 134 133 133 GLU GLU H . n 
H 1 135 SER 135 134 134 SER SER H . n 
H 1 136 THR 136 135 135 THR THR H . n 
H 1 137 LYS 137 136 136 LYS LYS H . n 
H 1 138 THR 138 137 137 THR THR H . n 
H 1 139 GLY 139 138 138 GLY GLY H . n 
H 1 140 ASN 140 139 139 ASN ASN H . n 
H 1 141 ALA 141 140 140 ALA ALA H . n 
H 1 142 GLY 142 141 141 GLY GLY H . n 
H 1 143 SER 143 142 142 SER SER H . n 
H 1 144 ARG 144 143 143 ARG ARG H . n 
H 1 145 LEU 145 144 144 LEU LEU H . n 
H 1 146 ALA 146 145 145 ALA ALA H . n 
H 1 147 CYS 147 146 146 CYS CYS H . n 
H 1 148 GLY 148 147 147 GLY GLY H . n 
H 1 149 VAL 149 148 148 VAL VAL H . n 
H 1 150 ILE 150 149 149 ILE ILE H . n 
H 1 151 GLY 151 150 150 GLY GLY H . n 
H 1 152 ILE 152 151 151 ILE ILE H . n 
H 1 153 ALA 153 152 152 ALA ALA H . n 
H 1 154 GLN 154 153 153 GLN GLN H . n 
I 1 1   MET 1   0   ?   ?   ?   I . n 
I 1 2   ALA 2   1   1   ALA ALA I . n 
I 1 3   THR 3   2   2   THR THR I . n 
I 1 4   LYS 4   3   3   LYS LYS I . n 
I 1 5   ALA 5   4   4   ALA ALA I . n 
I 1 6   VAL 6   5   5   VAL VAL I . n 
I 1 7   ALA 7   6   6   ALA ALA I . n 
I 1 8   VAL 8   7   7   VAL VAL I . n 
I 1 9   LEU 9   8   8   LEU LEU I . n 
I 1 10  LYS 10  9   9   LYS LYS I . n 
I 1 11  GLY 11  10  10  GLY GLY I . n 
I 1 12  ASP 12  11  11  ASP ASP I . n 
I 1 13  GLY 13  12  12  GLY GLY I . n 
I 1 14  PRO 14  13  13  PRO PRO I . n 
I 1 15  VAL 15  14  14  VAL VAL I . n 
I 1 16  GLN 16  15  15  GLN GLN I . n 
I 1 17  GLY 17  16  16  GLY GLY I . n 
I 1 18  ILE 18  17  17  ILE ILE I . n 
I 1 19  ILE 19  18  18  ILE ILE I . n 
I 1 20  ASN 20  19  19  ASN ASN I . n 
I 1 21  PHE 21  20  20  PHE PHE I . n 
I 1 22  GLU 22  21  21  GLU GLU I . n 
I 1 23  GLN 23  22  22  GLN GLN I . n 
I 1 24  LYS 24  23  23  LYS LYS I . n 
I 1 25  GLU 25  24  24  GLU GLU I . n 
I 1 26  SER 26  25  25  SER SER I . n 
I 1 27  ASN 27  26  26  ASN ASN I . n 
I 1 28  GLY 28  27  27  GLY GLY I . n 
I 1 29  PRO 29  28  28  PRO PRO I . n 
I 1 30  VAL 30  29  29  VAL VAL I . n 
I 1 31  LYS 31  30  30  LYS LYS I . n 
I 1 32  VAL 32  31  31  VAL VAL I . n 
I 1 33  TRP 33  32  32  TRP TRP I . n 
I 1 34  GLY 34  33  33  GLY GLY I . n 
I 1 35  SER 35  34  34  SER SER I . n 
I 1 36  ILE 36  35  35  ILE ILE I . n 
I 1 37  LYS 37  36  36  LYS LYS I . n 
I 1 38  GLY 38  37  37  GLY GLY I . n 
I 1 39  LEU 39  38  38  LEU LEU I . n 
I 1 40  THR 40  39  39  THR THR I . n 
I 1 41  GLU 41  40  40  GLU GLU I . n 
I 1 42  GLY 42  41  41  GLY GLY I . n 
I 1 43  LEU 43  42  42  LEU LEU I . n 
I 1 44  HIS 44  43  43  HIS HIS I . n 
I 1 45  GLY 45  44  44  GLY GLY I . n 
I 1 46  PHE 46  45  45  PHE PHE I . n 
I 1 47  HIS 47  46  46  HIS HIS I . n 
I 1 48  VAL 48  47  47  VAL VAL I . n 
I 1 49  HIS 49  48  48  HIS HIS I . n 
I 1 50  GLU 50  49  49  GLU GLU I . n 
I 1 51  PHE 51  50  50  PHE PHE I . n 
I 1 52  GLY 52  51  51  GLY GLY I . n 
I 1 53  ASP 53  52  52  ASP ASP I . n 
I 1 54  ASN 54  53  53  ASN ASN I . n 
I 1 55  THR 55  54  54  THR THR I . n 
I 1 56  ALA 56  55  55  ALA ALA I . n 
I 1 57  GLY 57  56  56  GLY GLY I . n 
I 1 58  CYS 58  57  57  CYS CYS I . n 
I 1 59  THR 59  58  58  THR THR I . n 
I 1 60  SER 60  59  59  SER SER I . n 
I 1 61  ALA 61  60  60  ALA ALA I . n 
I 1 62  GLY 62  61  61  GLY GLY I . n 
I 1 63  PRO 63  62  62  PRO PRO I . n 
I 1 64  HIS 64  63  63  HIS HIS I . n 
I 1 65  PHE 65  64  64  PHE PHE I . n 
I 1 66  ASN 66  65  65  ASN ASN I . n 
I 1 67  PRO 67  66  66  PRO PRO I . n 
I 1 68  LEU 68  67  67  LEU LEU I . n 
I 1 69  SER 69  68  68  SER SER I . n 
I 1 70  ARG 70  69  69  ARG ARG I . n 
I 1 71  LYS 71  70  70  LYS LYS I . n 
I 1 72  HIS 72  71  71  HIS HIS I . n 
I 1 73  GLY 73  72  72  GLY GLY I . n 
I 1 74  GLY 74  73  73  GLY GLY I . n 
I 1 75  PRO 75  74  74  PRO PRO I . n 
I 1 76  LYS 76  75  75  LYS LYS I . n 
I 1 77  ASP 77  76  76  ASP ASP I . n 
I 1 78  GLU 78  77  77  GLU GLU I . n 
I 1 79  GLU 79  78  78  GLU GLU I . n 
I 1 80  ARG 80  79  79  ARG ARG I . n 
I 1 81  HIS 81  80  80  HIS HIS I . n 
I 1 82  VAL 82  81  81  VAL VAL I . n 
I 1 83  GLY 83  82  82  GLY GLY I . n 
I 1 84  ASP 84  83  83  ASP ASP I . n 
I 1 85  LEU 85  84  84  LEU LEU I . n 
I 1 86  GLY 86  85  85  GLY GLY I . n 
I 1 87  ASN 87  86  86  ASN ASN I . n 
I 1 88  VAL 88  87  87  VAL VAL I . n 
I 1 89  THR 89  88  88  THR THR I . n 
I 1 90  ALA 90  89  89  ALA ALA I . n 
I 1 91  ASP 91  90  90  ASP ASP I . n 
I 1 92  LYS 92  91  91  LYS LYS I . n 
I 1 93  ASP 93  92  92  ASP ASP I . n 
I 1 94  GLY 94  93  93  GLY GLY I . n 
I 1 95  VAL 95  94  94  VAL VAL I . n 
I 1 96  ALA 96  95  95  ALA ALA I . n 
I 1 97  ASP 97  96  96  ASP ASP I . n 
I 1 98  VAL 98  97  97  VAL VAL I . n 
I 1 99  SER 99  98  98  SER SER I . n 
I 1 100 ILE 100 99  99  ILE ILE I . n 
I 1 101 GLU 101 100 100 GLU GLU I . n 
I 1 102 ASP 102 101 101 ASP ASP I . n 
I 1 103 SER 103 102 102 SER SER I . n 
I 1 104 VAL 104 103 103 VAL VAL I . n 
I 1 105 ILE 105 104 104 ILE ILE I . n 
I 1 106 SER 106 105 105 SER SER I . n 
I 1 107 LEU 107 106 106 LEU LEU I . n 
I 1 108 SER 108 107 107 SER SER I . n 
I 1 109 GLY 109 108 108 GLY GLY I . n 
I 1 110 ASP 110 109 109 ASP ASP I . n 
I 1 111 HIS 111 110 110 HIS HIS I . n 
I 1 112 SER 112 111 111 SER SER I . n 
I 1 113 ILE 113 112 112 ILE ILE I . n 
I 1 114 ILE 114 113 113 ILE ILE I . n 
I 1 115 GLY 115 114 114 GLY GLY I . n 
I 1 116 ARG 116 115 115 ARG ARG I . n 
I 1 117 THR 117 116 116 THR THR I . n 
I 1 118 LEU 118 117 117 LEU LEU I . n 
I 1 119 VAL 119 118 118 VAL VAL I . n 
I 1 120 VAL 120 119 119 VAL VAL I . n 
I 1 121 HIS 121 120 120 HIS HIS I . n 
I 1 122 GLU 122 121 121 GLU GLU I . n 
I 1 123 LYS 123 122 122 LYS LYS I . n 
I 1 124 ALA 124 123 123 ALA ALA I . n 
I 1 125 ASP 125 124 124 ASP ASP I . n 
I 1 126 ASP 126 125 125 ASP ASP I . n 
I 1 127 LEU 127 126 126 LEU LEU I . n 
I 1 128 GLY 128 127 127 GLY GLY I . n 
I 1 129 LYS 129 128 128 LYS LYS I . n 
I 1 130 GLY 130 129 129 GLY GLY I . n 
I 1 131 GLY 131 130 130 GLY GLY I . n 
I 1 132 ASN 132 131 131 ASN ASN I . n 
I 1 133 GLU 133 132 132 GLU GLU I . n 
I 1 134 GLU 134 133 133 GLU GLU I . n 
I 1 135 SER 135 134 134 SER SER I . n 
I 1 136 THR 136 135 135 THR THR I . n 
I 1 137 LYS 137 136 136 LYS LYS I . n 
I 1 138 THR 138 137 137 THR THR I . n 
I 1 139 GLY 139 138 138 GLY GLY I . n 
I 1 140 ASN 140 139 139 ASN ASN I . n 
I 1 141 ALA 141 140 140 ALA ALA I . n 
I 1 142 GLY 142 141 141 GLY GLY I . n 
I 1 143 SER 143 142 142 SER SER I . n 
I 1 144 ARG 144 143 143 ARG ARG I . n 
I 1 145 LEU 145 144 144 LEU LEU I . n 
I 1 146 ALA 146 145 145 ALA ALA I . n 
I 1 147 CYS 147 146 146 CYS CYS I . n 
I 1 148 GLY 148 147 147 GLY GLY I . n 
I 1 149 VAL 149 148 148 VAL VAL I . n 
I 1 150 ILE 150 149 149 ILE ILE I . n 
I 1 151 GLY 151 150 150 GLY GLY I . n 
I 1 152 ILE 152 151 151 ILE ILE I . n 
I 1 153 ALA 153 152 152 ALA ALA I . n 
I 1 154 GLN 154 153 153 GLN GLN I . n 
J 1 1   MET 1   0   ?   ?   ?   J . n 
J 1 2   ALA 2   1   1   ALA ALA J . n 
J 1 3   THR 3   2   2   THR THR J . n 
J 1 4   LYS 4   3   3   LYS LYS J . n 
J 1 5   ALA 5   4   4   ALA ALA J . n 
J 1 6   VAL 6   5   5   VAL VAL J . n 
J 1 7   ALA 7   6   6   ALA ALA J . n 
J 1 8   VAL 8   7   7   VAL VAL J . n 
J 1 9   LEU 9   8   8   LEU LEU J . n 
J 1 10  LYS 10  9   9   LYS LYS J . n 
J 1 11  GLY 11  10  10  GLY GLY J . n 
J 1 12  ASP 12  11  11  ASP ASP J . n 
J 1 13  GLY 13  12  12  GLY GLY J . n 
J 1 14  PRO 14  13  13  PRO PRO J . n 
J 1 15  VAL 15  14  14  VAL VAL J . n 
J 1 16  GLN 16  15  15  GLN GLN J . n 
J 1 17  GLY 17  16  16  GLY GLY J . n 
J 1 18  ILE 18  17  17  ILE ILE J . n 
J 1 19  ILE 19  18  18  ILE ILE J . n 
J 1 20  ASN 20  19  19  ASN ASN J . n 
J 1 21  PHE 21  20  20  PHE PHE J . n 
J 1 22  GLU 22  21  21  GLU GLU J . n 
J 1 23  GLN 23  22  22  GLN GLN J . n 
J 1 24  LYS 24  23  23  LYS LYS J . n 
J 1 25  GLU 25  24  24  GLU GLU J . n 
J 1 26  SER 26  25  25  SER SER J . n 
J 1 27  ASN 27  26  26  ASN ASN J . n 
J 1 28  GLY 28  27  27  GLY GLY J . n 
J 1 29  PRO 29  28  28  PRO PRO J . n 
J 1 30  VAL 30  29  29  VAL VAL J . n 
J 1 31  LYS 31  30  30  LYS LYS J . n 
J 1 32  VAL 32  31  31  VAL VAL J . n 
J 1 33  TRP 33  32  32  TRP TRP J . n 
J 1 34  GLY 34  33  33  GLY GLY J . n 
J 1 35  SER 35  34  34  SER SER J . n 
J 1 36  ILE 36  35  35  ILE ILE J . n 
J 1 37  LYS 37  36  36  LYS LYS J . n 
J 1 38  GLY 38  37  37  GLY GLY J . n 
J 1 39  LEU 39  38  38  LEU LEU J . n 
J 1 40  THR 40  39  39  THR THR J . n 
J 1 41  GLU 41  40  40  GLU GLU J . n 
J 1 42  GLY 42  41  41  GLY GLY J . n 
J 1 43  LEU 43  42  42  LEU LEU J . n 
J 1 44  HIS 44  43  43  HIS HIS J . n 
J 1 45  GLY 45  44  44  GLY GLY J . n 
J 1 46  PHE 46  45  45  PHE PHE J . n 
J 1 47  HIS 47  46  46  HIS HIS J . n 
J 1 48  VAL 48  47  47  VAL VAL J . n 
J 1 49  HIS 49  48  48  HIS HIS J . n 
J 1 50  GLU 50  49  49  GLU GLU J . n 
J 1 51  PHE 51  50  50  PHE PHE J . n 
J 1 52  GLY 52  51  51  GLY GLY J . n 
J 1 53  ASP 53  52  52  ASP ASP J . n 
J 1 54  ASN 54  53  53  ASN ASN J . n 
J 1 55  THR 55  54  54  THR THR J . n 
J 1 56  ALA 56  55  55  ALA ALA J . n 
J 1 57  GLY 57  56  56  GLY GLY J . n 
J 1 58  CYS 58  57  57  CYS CYS J . n 
J 1 59  THR 59  58  58  THR THR J . n 
J 1 60  SER 60  59  59  SER SER J . n 
J 1 61  ALA 61  60  60  ALA ALA J . n 
J 1 62  GLY 62  61  61  GLY GLY J . n 
J 1 63  PRO 63  62  62  PRO PRO J . n 
J 1 64  HIS 64  63  63  HIS HIS J . n 
J 1 65  PHE 65  64  64  PHE PHE J . n 
J 1 66  ASN 66  65  65  ASN ASN J . n 
J 1 67  PRO 67  66  66  PRO PRO J . n 
J 1 68  LEU 68  67  67  LEU LEU J . n 
J 1 69  SER 69  68  68  SER SER J . n 
J 1 70  ARG 70  69  69  ARG ARG J . n 
J 1 71  LYS 71  70  70  LYS LYS J . n 
J 1 72  HIS 72  71  71  HIS HIS J . n 
J 1 73  GLY 73  72  72  GLY GLY J . n 
J 1 74  GLY 74  73  73  GLY GLY J . n 
J 1 75  PRO 75  74  74  PRO PRO J . n 
J 1 76  LYS 76  75  75  LYS LYS J . n 
J 1 77  ASP 77  76  76  ASP ASP J . n 
J 1 78  GLU 78  77  77  GLU GLU J . n 
J 1 79  GLU 79  78  78  GLU GLU J . n 
J 1 80  ARG 80  79  79  ARG ARG J . n 
J 1 81  HIS 81  80  80  HIS HIS J . n 
J 1 82  VAL 82  81  81  VAL VAL J . n 
J 1 83  GLY 83  82  82  GLY GLY J . n 
J 1 84  ASP 84  83  83  ASP ASP J . n 
J 1 85  LEU 85  84  84  LEU LEU J . n 
J 1 86  GLY 86  85  85  GLY GLY J . n 
J 1 87  ASN 87  86  86  ASN ASN J . n 
J 1 88  VAL 88  87  87  VAL VAL J . n 
J 1 89  THR 89  88  88  THR THR J . n 
J 1 90  ALA 90  89  89  ALA ALA J . n 
J 1 91  ASP 91  90  90  ASP ASP J . n 
J 1 92  LYS 92  91  91  LYS LYS J . n 
J 1 93  ASP 93  92  92  ASP ASP J . n 
J 1 94  GLY 94  93  93  GLY GLY J . n 
J 1 95  VAL 95  94  94  VAL VAL J . n 
J 1 96  ALA 96  95  95  ALA ALA J . n 
J 1 97  ASP 97  96  96  ASP ASP J . n 
J 1 98  VAL 98  97  97  VAL VAL J . n 
J 1 99  SER 99  98  98  SER SER J . n 
J 1 100 ILE 100 99  99  ILE ILE J . n 
J 1 101 GLU 101 100 100 GLU GLU J . n 
J 1 102 ASP 102 101 101 ASP ASP J . n 
J 1 103 SER 103 102 102 SER SER J . n 
J 1 104 VAL 104 103 103 VAL VAL J . n 
J 1 105 ILE 105 104 104 ILE ILE J . n 
J 1 106 SER 106 105 105 SER SER J . n 
J 1 107 LEU 107 106 106 LEU LEU J . n 
J 1 108 SER 108 107 107 SER SER J . n 
J 1 109 GLY 109 108 108 GLY GLY J . n 
J 1 110 ASP 110 109 109 ASP ASP J . n 
J 1 111 HIS 111 110 110 HIS HIS J . n 
J 1 112 SER 112 111 111 SER SER J . n 
J 1 113 ILE 113 112 112 ILE ILE J . n 
J 1 114 ILE 114 113 113 ILE ILE J . n 
J 1 115 GLY 115 114 114 GLY GLY J . n 
J 1 116 ARG 116 115 115 ARG ARG J . n 
J 1 117 THR 117 116 116 THR THR J . n 
J 1 118 LEU 118 117 117 LEU LEU J . n 
J 1 119 VAL 119 118 118 VAL VAL J . n 
J 1 120 VAL 120 119 119 VAL VAL J . n 
J 1 121 HIS 121 120 120 HIS HIS J . n 
J 1 122 GLU 122 121 121 GLU GLU J . n 
J 1 123 LYS 123 122 122 LYS LYS J . n 
J 1 124 ALA 124 123 123 ALA ALA J . n 
J 1 125 ASP 125 124 124 ASP ASP J . n 
J 1 126 ASP 126 125 125 ASP ASP J . n 
J 1 127 LEU 127 126 126 LEU LEU J . n 
J 1 128 GLY 128 127 127 GLY GLY J . n 
J 1 129 LYS 129 128 128 LYS LYS J . n 
J 1 130 GLY 130 129 129 GLY GLY J . n 
J 1 131 GLY 131 130 130 GLY GLY J . n 
J 1 132 ASN 132 131 131 ASN ASN J . n 
J 1 133 GLU 133 132 132 GLU GLU J . n 
J 1 134 GLU 134 133 133 GLU GLU J . n 
J 1 135 SER 135 134 134 SER SER J . n 
J 1 136 THR 136 135 135 THR THR J . n 
J 1 137 LYS 137 136 136 LYS LYS J . n 
J 1 138 THR 138 137 137 THR THR J . n 
J 1 139 GLY 139 138 138 GLY GLY J . n 
J 1 140 ASN 140 139 139 ASN ASN J . n 
J 1 141 ALA 141 140 140 ALA ALA J . n 
J 1 142 GLY 142 141 141 GLY GLY J . n 
J 1 143 SER 143 142 142 SER SER J . n 
J 1 144 ARG 144 143 143 ARG ARG J . n 
J 1 145 LEU 145 144 144 LEU LEU J . n 
J 1 146 ALA 146 145 145 ALA ALA J . n 
J 1 147 CYS 147 146 146 CYS CYS J . n 
J 1 148 GLY 148 147 147 GLY GLY J . n 
J 1 149 VAL 149 148 148 VAL VAL J . n 
J 1 150 ILE 150 149 149 ILE ILE J . n 
J 1 151 GLY 151 150 150 GLY GLY J . n 
J 1 152 ILE 152 151 151 ILE ILE J . n 
J 1 153 ALA 153 152 152 ALA ALA J . n 
J 1 154 GLN 154 153 153 GLN GLN J . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
K  2 CU1 1   154  154  CU1 CU1 A . 
L  3 ZN  1   155  155  ZN  ZN2 A . 
M  2 CU1 1   154  154  CU1 CU1 B . 
N  3 ZN  1   155  155  ZN  ZN2 B . 
O  2 CU1 1   154  154  CU1 CU1 C . 
P  3 ZN  1   155  155  ZN  ZN2 C . 
Q  2 CU1 1   154  154  CU1 CU1 D . 
R  3 ZN  1   155  155  ZN  ZN2 D . 
S  4 SO4 1   1400 1    SO4 SO4 D . 
T  2 CU1 1   154  154  CU1 CU1 E . 
U  3 ZN  1   155  155  ZN  ZN2 E . 
V  2 CU1 1   154  154  CU1 CU1 F . 
W  3 ZN  1   155  155  ZN  ZN2 F . 
X  2 CU1 1   154  154  CU1 CU1 G . 
Y  3 ZN  1   155  155  ZN  ZN2 G . 
Z  2 CU1 1   154  154  CU1 CU1 H . 
AA 3 ZN  1   155  155  ZN  ZN2 H . 
BA 2 CU1 1   154  154  CU1 CU1 I . 
CA 3 ZN  1   155  155  ZN  ZN2 I . 
DA 2 CU1 1   154  154  CU1 CU1 J . 
EA 3 ZN  1   155  155  ZN  ZN2 J . 
FA 5 HOH 1   156  6    HOH HOH A . 
FA 5 HOH 2   157  13   HOH HOH A . 
FA 5 HOH 3   158  16   HOH HOH A . 
FA 5 HOH 4   159  18   HOH HOH A . 
FA 5 HOH 5   160  20   HOH HOH A . 
FA 5 HOH 6   161  52   HOH HOH A . 
FA 5 HOH 7   162  71   HOH HOH A . 
FA 5 HOH 8   163  90   HOH HOH A . 
FA 5 HOH 9   164  97   HOH HOH A . 
FA 5 HOH 10  165  105  HOH HOH A . 
FA 5 HOH 11  166  148  HOH HOH A . 
FA 5 HOH 12  167  170  HOH HOH A . 
FA 5 HOH 13  168  177  HOH HOH A . 
FA 5 HOH 14  169  179  HOH HOH A . 
FA 5 HOH 15  170  182  HOH HOH A . 
FA 5 HOH 16  171  187  HOH HOH A . 
FA 5 HOH 17  172  188  HOH HOH A . 
FA 5 HOH 18  173  196  HOH HOH A . 
FA 5 HOH 19  174  200  HOH HOH A . 
FA 5 HOH 20  175  222  HOH HOH A . 
FA 5 HOH 21  176  225  HOH HOH A . 
FA 5 HOH 22  177  229  HOH HOH A . 
FA 5 HOH 23  178  232  HOH HOH A . 
FA 5 HOH 24  179  235  HOH HOH A . 
FA 5 HOH 25  180  238  HOH HOH A . 
FA 5 HOH 26  181  244  HOH HOH A . 
FA 5 HOH 27  182  245  HOH HOH A . 
FA 5 HOH 28  183  251  HOH HOH A . 
FA 5 HOH 29  184  260  HOH HOH A . 
FA 5 HOH 30  185  263  HOH HOH A . 
FA 5 HOH 31  186  281  HOH HOH A . 
FA 5 HOH 32  187  288  HOH HOH A . 
FA 5 HOH 33  188  290  HOH HOH A . 
FA 5 HOH 34  189  322  HOH HOH A . 
FA 5 HOH 35  190  334  HOH HOH A . 
FA 5 HOH 36  191  344  HOH HOH A . 
FA 5 HOH 37  192  345  HOH HOH A . 
FA 5 HOH 38  193  347  HOH HOH A . 
FA 5 HOH 39  194  353  HOH HOH A . 
FA 5 HOH 40  195  354  HOH HOH A . 
FA 5 HOH 41  196  358  HOH HOH A . 
FA 5 HOH 42  197  361  HOH HOH A . 
FA 5 HOH 43  198  372  HOH HOH A . 
FA 5 HOH 44  199  385  HOH HOH A . 
FA 5 HOH 45  200  392  HOH HOH A . 
FA 5 HOH 46  201  395  HOH HOH A . 
FA 5 HOH 47  202  414  HOH HOH A . 
FA 5 HOH 48  203  415  HOH HOH A . 
FA 5 HOH 49  204  416  HOH HOH A . 
FA 5 HOH 50  205  419  HOH HOH A . 
FA 5 HOH 51  206  438  HOH HOH A . 
FA 5 HOH 52  207  441  HOH HOH A . 
FA 5 HOH 53  208  445  HOH HOH A . 
FA 5 HOH 54  209  464  HOH HOH A . 
FA 5 HOH 55  210  482  HOH HOH A . 
FA 5 HOH 56  211  484  HOH HOH A . 
FA 5 HOH 57  212  504  HOH HOH A . 
FA 5 HOH 58  213  514  HOH HOH A . 
FA 5 HOH 59  214  515  HOH HOH A . 
FA 5 HOH 60  215  519  HOH HOH A . 
FA 5 HOH 61  216  547  HOH HOH A . 
FA 5 HOH 62  217  552  HOH HOH A . 
FA 5 HOH 63  218  570  HOH HOH A . 
FA 5 HOH 64  219  578  HOH HOH A . 
FA 5 HOH 65  220  585  HOH HOH A . 
FA 5 HOH 66  221  619  HOH HOH A . 
FA 5 HOH 67  222  630  HOH HOH A . 
FA 5 HOH 68  223  633  HOH HOH A . 
FA 5 HOH 69  224  638  HOH HOH A . 
FA 5 HOH 70  225  647  HOH HOH A . 
FA 5 HOH 71  226  652  HOH HOH A . 
FA 5 HOH 72  227  664  HOH HOH A . 
FA 5 HOH 73  228  692  HOH HOH A . 
FA 5 HOH 74  229  700  HOH HOH A . 
FA 5 HOH 75  230  703  HOH HOH A . 
FA 5 HOH 76  231  725  HOH HOH A . 
FA 5 HOH 77  232  736  HOH HOH A . 
FA 5 HOH 78  233  759  HOH HOH A . 
FA 5 HOH 79  234  794  HOH HOH A . 
FA 5 HOH 80  235  811  HOH HOH A . 
FA 5 HOH 81  236  818  HOH HOH A . 
FA 5 HOH 82  237  863  HOH HOH A . 
FA 5 HOH 83  238  867  HOH HOH A . 
FA 5 HOH 84  239  872  HOH HOH A . 
FA 5 HOH 85  240  884  HOH HOH A . 
FA 5 HOH 86  241  895  HOH HOH A . 
FA 5 HOH 87  242  918  HOH HOH A . 
FA 5 HOH 88  243  942  HOH HOH A . 
FA 5 HOH 89  244  958  HOH HOH A . 
FA 5 HOH 90  245  959  HOH HOH A . 
FA 5 HOH 91  246  966  HOH HOH A . 
FA 5 HOH 92  247  972  HOH HOH A . 
FA 5 HOH 93  248  978  HOH HOH A . 
FA 5 HOH 94  249  982  HOH HOH A . 
FA 5 HOH 95  250  1005 HOH HOH A . 
FA 5 HOH 96  251  1011 HOH HOH A . 
FA 5 HOH 97  252  1015 HOH HOH A . 
FA 5 HOH 98  253  1026 HOH HOH A . 
FA 5 HOH 99  254  1037 HOH HOH A . 
FA 5 HOH 100 255  1067 HOH HOH A . 
FA 5 HOH 101 256  1084 HOH HOH A . 
FA 5 HOH 102 257  1094 HOH HOH A . 
FA 5 HOH 103 258  1107 HOH HOH A . 
FA 5 HOH 104 259  1119 HOH HOH A . 
FA 5 HOH 105 260  1121 HOH HOH A . 
FA 5 HOH 106 261  1128 HOH HOH A . 
FA 5 HOH 107 262  1154 HOH HOH A . 
FA 5 HOH 108 263  1166 HOH HOH A . 
FA 5 HOH 109 264  1189 HOH HOH A . 
FA 5 HOH 110 265  1234 HOH HOH A . 
FA 5 HOH 111 266  1241 HOH HOH A . 
FA 5 HOH 112 267  1242 HOH HOH A . 
FA 5 HOH 113 268  1252 HOH HOH A . 
FA 5 HOH 114 269  1256 HOH HOH A . 
FA 5 HOH 115 270  1288 HOH HOH A . 
FA 5 HOH 116 271  1291 HOH HOH A . 
FA 5 HOH 117 272  1294 HOH HOH A . 
FA 5 HOH 118 273  1325 HOH HOH A . 
FA 5 HOH 119 274  1329 HOH HOH A . 
FA 5 HOH 120 275  1331 HOH HOH A . 
FA 5 HOH 121 276  1337 HOH HOH A . 
FA 5 HOH 122 277  1341 HOH HOH A . 
FA 5 HOH 123 278  1343 HOH HOH A . 
FA 5 HOH 124 279  1345 HOH HOH A . 
FA 5 HOH 125 280  1359 HOH HOH A . 
FA 5 HOH 126 281  1363 HOH HOH A . 
FA 5 HOH 127 282  1373 HOH HOH A . 
FA 5 HOH 128 283  1377 HOH HOH A . 
FA 5 HOH 129 284  1386 HOH HOH A . 
FA 5 HOH 130 285  1387 HOH HOH A . 
GA 5 HOH 1   156  1    HOH HOH B . 
GA 5 HOH 2   157  4    HOH HOH B . 
GA 5 HOH 3   158  11   HOH HOH B . 
GA 5 HOH 4   159  15   HOH HOH B . 
GA 5 HOH 5   160  17   HOH HOH B . 
GA 5 HOH 6   161  19   HOH HOH B . 
GA 5 HOH 7   162  25   HOH HOH B . 
GA 5 HOH 8   163  26   HOH HOH B . 
GA 5 HOH 9   164  33   HOH HOH B . 
GA 5 HOH 10  165  45   HOH HOH B . 
GA 5 HOH 11  166  49   HOH HOH B . 
GA 5 HOH 12  167  57   HOH HOH B . 
GA 5 HOH 13  168  58   HOH HOH B . 
GA 5 HOH 14  169  59   HOH HOH B . 
GA 5 HOH 15  170  64   HOH HOH B . 
GA 5 HOH 16  171  72   HOH HOH B . 
GA 5 HOH 17  172  75   HOH HOH B . 
GA 5 HOH 18  173  78   HOH HOH B . 
GA 5 HOH 19  174  79   HOH HOH B . 
GA 5 HOH 20  175  81   HOH HOH B . 
GA 5 HOH 21  176  83   HOH HOH B . 
GA 5 HOH 22  177  85   HOH HOH B . 
GA 5 HOH 23  178  93   HOH HOH B . 
GA 5 HOH 24  179  106  HOH HOH B . 
GA 5 HOH 25  180  108  HOH HOH B . 
GA 5 HOH 26  181  109  HOH HOH B . 
GA 5 HOH 27  182  111  HOH HOH B . 
GA 5 HOH 28  183  119  HOH HOH B . 
GA 5 HOH 29  184  125  HOH HOH B . 
GA 5 HOH 30  185  127  HOH HOH B . 
GA 5 HOH 31  186  130  HOH HOH B . 
GA 5 HOH 32  187  131  HOH HOH B . 
GA 5 HOH 33  188  142  HOH HOH B . 
GA 5 HOH 34  189  143  HOH HOH B . 
GA 5 HOH 35  190  145  HOH HOH B . 
GA 5 HOH 36  191  155  HOH HOH B . 
GA 5 HOH 37  192  158  HOH HOH B . 
GA 5 HOH 38  193  159  HOH HOH B . 
GA 5 HOH 39  194  180  HOH HOH B . 
GA 5 HOH 40  195  192  HOH HOH B . 
GA 5 HOH 41  196  193  HOH HOH B . 
GA 5 HOH 42  197  194  HOH HOH B . 
GA 5 HOH 43  198  199  HOH HOH B . 
GA 5 HOH 44  199  203  HOH HOH B . 
GA 5 HOH 45  200  212  HOH HOH B . 
GA 5 HOH 46  201  217  HOH HOH B . 
GA 5 HOH 47  202  223  HOH HOH B . 
GA 5 HOH 48  203  230  HOH HOH B . 
GA 5 HOH 49  204  233  HOH HOH B . 
GA 5 HOH 50  205  234  HOH HOH B . 
GA 5 HOH 51  206  236  HOH HOH B . 
GA 5 HOH 52  207  239  HOH HOH B . 
GA 5 HOH 53  208  240  HOH HOH B . 
GA 5 HOH 54  209  259  HOH HOH B . 
GA 5 HOH 55  210  265  HOH HOH B . 
GA 5 HOH 56  211  274  HOH HOH B . 
GA 5 HOH 57  212  283  HOH HOH B . 
GA 5 HOH 58  213  286  HOH HOH B . 
GA 5 HOH 59  214  289  HOH HOH B . 
GA 5 HOH 60  215  293  HOH HOH B . 
GA 5 HOH 61  216  294  HOH HOH B . 
GA 5 HOH 62  217  317  HOH HOH B . 
GA 5 HOH 63  218  320  HOH HOH B . 
GA 5 HOH 64  219  321  HOH HOH B . 
GA 5 HOH 65  220  324  HOH HOH B . 
GA 5 HOH 66  221  325  HOH HOH B . 
GA 5 HOH 67  222  327  HOH HOH B . 
GA 5 HOH 68  223  328  HOH HOH B . 
GA 5 HOH 69  224  330  HOH HOH B . 
GA 5 HOH 70  225  331  HOH HOH B . 
GA 5 HOH 71  226  333  HOH HOH B . 
GA 5 HOH 72  227  367  HOH HOH B . 
GA 5 HOH 73  228  388  HOH HOH B . 
GA 5 HOH 74  229  391  HOH HOH B . 
GA 5 HOH 75  230  393  HOH HOH B . 
GA 5 HOH 76  231  424  HOH HOH B . 
GA 5 HOH 77  232  425  HOH HOH B . 
GA 5 HOH 78  233  426  HOH HOH B . 
GA 5 HOH 79  234  427  HOH HOH B . 
GA 5 HOH 80  235  429  HOH HOH B . 
GA 5 HOH 81  236  434  HOH HOH B . 
GA 5 HOH 82  237  439  HOH HOH B . 
GA 5 HOH 83  238  453  HOH HOH B . 
GA 5 HOH 84  239  454  HOH HOH B . 
GA 5 HOH 85  240  459  HOH HOH B . 
GA 5 HOH 86  241  470  HOH HOH B . 
GA 5 HOH 87  242  485  HOH HOH B . 
GA 5 HOH 88  243  507  HOH HOH B . 
GA 5 HOH 89  244  512  HOH HOH B . 
GA 5 HOH 90  245  527  HOH HOH B . 
GA 5 HOH 91  246  536  HOH HOH B . 
GA 5 HOH 92  247  543  HOH HOH B . 
GA 5 HOH 93  248  546  HOH HOH B . 
GA 5 HOH 94  249  562  HOH HOH B . 
GA 5 HOH 95  250  566  HOH HOH B . 
GA 5 HOH 96  251  567  HOH HOH B . 
GA 5 HOH 97  252  568  HOH HOH B . 
GA 5 HOH 98  253  572  HOH HOH B . 
GA 5 HOH 99  254  579  HOH HOH B . 
GA 5 HOH 100 255  580  HOH HOH B . 
GA 5 HOH 101 256  581  HOH HOH B . 
GA 5 HOH 102 257  589  HOH HOH B . 
GA 5 HOH 103 258  600  HOH HOH B . 
GA 5 HOH 104 259  604  HOH HOH B . 
GA 5 HOH 105 260  605  HOH HOH B . 
GA 5 HOH 106 261  606  HOH HOH B . 
GA 5 HOH 107 262  620  HOH HOH B . 
GA 5 HOH 108 263  624  HOH HOH B . 
GA 5 HOH 109 264  645  HOH HOH B . 
GA 5 HOH 110 265  661  HOH HOH B . 
GA 5 HOH 111 266  666  HOH HOH B . 
GA 5 HOH 112 267  670  HOH HOH B . 
GA 5 HOH 113 268  671  HOH HOH B . 
GA 5 HOH 114 269  686  HOH HOH B . 
GA 5 HOH 115 270  688  HOH HOH B . 
GA 5 HOH 116 271  697  HOH HOH B . 
GA 5 HOH 117 272  735  HOH HOH B . 
GA 5 HOH 118 273  746  HOH HOH B . 
GA 5 HOH 119 274  748  HOH HOH B . 
GA 5 HOH 120 275  758  HOH HOH B . 
GA 5 HOH 121 276  779  HOH HOH B . 
GA 5 HOH 122 277  784  HOH HOH B . 
GA 5 HOH 123 278  786  HOH HOH B . 
GA 5 HOH 124 279  796  HOH HOH B . 
GA 5 HOH 125 280  801  HOH HOH B . 
GA 5 HOH 126 281  808  HOH HOH B . 
GA 5 HOH 127 282  809  HOH HOH B . 
GA 5 HOH 128 283  822  HOH HOH B . 
GA 5 HOH 129 284  835  HOH HOH B . 
GA 5 HOH 130 285  840  HOH HOH B . 
GA 5 HOH 131 286  841  HOH HOH B . 
GA 5 HOH 132 287  844  HOH HOH B . 
GA 5 HOH 133 288  869  HOH HOH B . 
GA 5 HOH 134 289  888  HOH HOH B . 
GA 5 HOH 135 290  889  HOH HOH B . 
GA 5 HOH 136 291  903  HOH HOH B . 
GA 5 HOH 137 292  927  HOH HOH B . 
GA 5 HOH 138 293  932  HOH HOH B . 
GA 5 HOH 139 294  933  HOH HOH B . 
GA 5 HOH 140 295  938  HOH HOH B . 
GA 5 HOH 141 296  946  HOH HOH B . 
GA 5 HOH 142 297  950  HOH HOH B . 
GA 5 HOH 143 298  960  HOH HOH B . 
GA 5 HOH 144 299  961  HOH HOH B . 
GA 5 HOH 145 300  964  HOH HOH B . 
GA 5 HOH 146 301  965  HOH HOH B . 
GA 5 HOH 147 302  969  HOH HOH B . 
GA 5 HOH 148 303  975  HOH HOH B . 
GA 5 HOH 149 304  984  HOH HOH B . 
GA 5 HOH 150 305  985  HOH HOH B . 
GA 5 HOH 151 306  986  HOH HOH B . 
GA 5 HOH 152 307  988  HOH HOH B . 
GA 5 HOH 153 308  1030 HOH HOH B . 
GA 5 HOH 154 309  1044 HOH HOH B . 
GA 5 HOH 155 310  1045 HOH HOH B . 
GA 5 HOH 156 311  1048 HOH HOH B . 
GA 5 HOH 157 312  1058 HOH HOH B . 
GA 5 HOH 158 313  1075 HOH HOH B . 
GA 5 HOH 159 314  1081 HOH HOH B . 
GA 5 HOH 160 315  1089 HOH HOH B . 
GA 5 HOH 161 316  1120 HOH HOH B . 
GA 5 HOH 162 317  1122 HOH HOH B . 
GA 5 HOH 163 318  1137 HOH HOH B . 
GA 5 HOH 164 319  1142 HOH HOH B . 
GA 5 HOH 165 320  1148 HOH HOH B . 
GA 5 HOH 166 321  1149 HOH HOH B . 
GA 5 HOH 167 322  1153 HOH HOH B . 
GA 5 HOH 168 323  1155 HOH HOH B . 
GA 5 HOH 169 324  1161 HOH HOH B . 
GA 5 HOH 170 325  1164 HOH HOH B . 
GA 5 HOH 171 326  1193 HOH HOH B . 
GA 5 HOH 172 327  1195 HOH HOH B . 
GA 5 HOH 173 328  1206 HOH HOH B . 
GA 5 HOH 174 329  1210 HOH HOH B . 
GA 5 HOH 175 330  1218 HOH HOH B . 
GA 5 HOH 176 331  1221 HOH HOH B . 
GA 5 HOH 177 332  1224 HOH HOH B . 
GA 5 HOH 178 333  1237 HOH HOH B . 
GA 5 HOH 179 334  1244 HOH HOH B . 
GA 5 HOH 180 335  1267 HOH HOH B . 
GA 5 HOH 181 336  1273 HOH HOH B . 
GA 5 HOH 182 337  1280 HOH HOH B . 
GA 5 HOH 183 338  1296 HOH HOH B . 
GA 5 HOH 184 339  1303 HOH HOH B . 
GA 5 HOH 185 340  1307 HOH HOH B . 
GA 5 HOH 186 341  1309 HOH HOH B . 
GA 5 HOH 187 342  1315 HOH HOH B . 
GA 5 HOH 188 343  1350 HOH HOH B . 
GA 5 HOH 189 344  1380 HOH HOH B . 
GA 5 HOH 190 345  1382 HOH HOH B . 
GA 5 HOH 191 346  1383 HOH HOH B . 
GA 5 HOH 192 347  1385 HOH HOH B . 
HA 5 HOH 1   156  53   HOH HOH C . 
HA 5 HOH 2   157  87   HOH HOH C . 
HA 5 HOH 3   158  103  HOH HOH C . 
HA 5 HOH 4   159  118  HOH HOH C . 
HA 5 HOH 5   160  133  HOH HOH C . 
HA 5 HOH 6   161  162  HOH HOH C . 
HA 5 HOH 7   162  206  HOH HOH C . 
HA 5 HOH 8   163  211  HOH HOH C . 
HA 5 HOH 9   164  261  HOH HOH C . 
HA 5 HOH 10  165  268  HOH HOH C . 
HA 5 HOH 11  166  269  HOH HOH C . 
HA 5 HOH 12  167  282  HOH HOH C . 
HA 5 HOH 13  168  304  HOH HOH C . 
HA 5 HOH 14  169  356  HOH HOH C . 
HA 5 HOH 15  170  359  HOH HOH C . 
HA 5 HOH 16  171  369  HOH HOH C . 
HA 5 HOH 17  172  373  HOH HOH C . 
HA 5 HOH 18  173  377  HOH HOH C . 
HA 5 HOH 19  174  383  HOH HOH C . 
HA 5 HOH 20  175  386  HOH HOH C . 
HA 5 HOH 21  176  405  HOH HOH C . 
HA 5 HOH 22  177  440  HOH HOH C . 
HA 5 HOH 23  178  442  HOH HOH C . 
HA 5 HOH 24  179  451  HOH HOH C . 
HA 5 HOH 25  180  455  HOH HOH C . 
HA 5 HOH 26  181  458  HOH HOH C . 
HA 5 HOH 27  182  465  HOH HOH C . 
HA 5 HOH 28  183  466  HOH HOH C . 
HA 5 HOH 29  184  468  HOH HOH C . 
HA 5 HOH 30  185  506  HOH HOH C . 
HA 5 HOH 31  186  510  HOH HOH C . 
HA 5 HOH 32  187  513  HOH HOH C . 
HA 5 HOH 33  188  529  HOH HOH C . 
HA 5 HOH 34  189  534  HOH HOH C . 
HA 5 HOH 35  190  553  HOH HOH C . 
HA 5 HOH 36  191  565  HOH HOH C . 
HA 5 HOH 37  192  573  HOH HOH C . 
HA 5 HOH 38  193  577  HOH HOH C . 
HA 5 HOH 39  194  588  HOH HOH C . 
HA 5 HOH 40  195  612  HOH HOH C . 
HA 5 HOH 41  196  636  HOH HOH C . 
HA 5 HOH 42  197  637  HOH HOH C . 
HA 5 HOH 43  198  643  HOH HOH C . 
HA 5 HOH 44  199  650  HOH HOH C . 
HA 5 HOH 45  200  651  HOH HOH C . 
HA 5 HOH 46  201  676  HOH HOH C . 
HA 5 HOH 47  202  678  HOH HOH C . 
HA 5 HOH 48  203  683  HOH HOH C . 
HA 5 HOH 49  204  694  HOH HOH C . 
HA 5 HOH 50  205  699  HOH HOH C . 
HA 5 HOH 51  206  708  HOH HOH C . 
HA 5 HOH 52  207  710  HOH HOH C . 
HA 5 HOH 53  208  722  HOH HOH C . 
HA 5 HOH 54  209  727  HOH HOH C . 
HA 5 HOH 55  210  744  HOH HOH C . 
HA 5 HOH 56  211  783  HOH HOH C . 
HA 5 HOH 57  212  790  HOH HOH C . 
HA 5 HOH 58  213  816  HOH HOH C . 
HA 5 HOH 59  214  824  HOH HOH C . 
HA 5 HOH 60  215  829  HOH HOH C . 
HA 5 HOH 61  216  836  HOH HOH C . 
HA 5 HOH 62  217  855  HOH HOH C . 
HA 5 HOH 63  218  873  HOH HOH C . 
HA 5 HOH 64  219  882  HOH HOH C . 
HA 5 HOH 65  220  905  HOH HOH C . 
HA 5 HOH 66  221  907  HOH HOH C . 
HA 5 HOH 67  222  913  HOH HOH C . 
HA 5 HOH 68  223  929  HOH HOH C . 
HA 5 HOH 69  224  940  HOH HOH C . 
HA 5 HOH 70  225  943  HOH HOH C . 
HA 5 HOH 71  226  987  HOH HOH C . 
HA 5 HOH 72  227  991  HOH HOH C . 
HA 5 HOH 73  228  992  HOH HOH C . 
HA 5 HOH 74  229  1021 HOH HOH C . 
HA 5 HOH 75  230  1068 HOH HOH C . 
HA 5 HOH 76  231  1078 HOH HOH C . 
HA 5 HOH 77  232  1092 HOH HOH C . 
HA 5 HOH 78  233  1093 HOH HOH C . 
HA 5 HOH 79  234  1103 HOH HOH C . 
HA 5 HOH 80  235  1124 HOH HOH C . 
HA 5 HOH 81  236  1150 HOH HOH C . 
HA 5 HOH 82  237  1165 HOH HOH C . 
HA 5 HOH 83  238  1176 HOH HOH C . 
HA 5 HOH 84  239  1182 HOH HOH C . 
HA 5 HOH 85  240  1199 HOH HOH C . 
HA 5 HOH 86  241  1200 HOH HOH C . 
HA 5 HOH 87  242  1213 HOH HOH C . 
HA 5 HOH 88  243  1227 HOH HOH C . 
HA 5 HOH 89  244  1230 HOH HOH C . 
HA 5 HOH 90  245  1236 HOH HOH C . 
HA 5 HOH 91  246  1251 HOH HOH C . 
HA 5 HOH 92  247  1266 HOH HOH C . 
HA 5 HOH 93  248  1269 HOH HOH C . 
HA 5 HOH 94  249  1277 HOH HOH C . 
HA 5 HOH 95  250  1279 HOH HOH C . 
HA 5 HOH 96  251  1286 HOH HOH C . 
HA 5 HOH 97  252  1293 HOH HOH C . 
HA 5 HOH 98  253  1297 HOH HOH C . 
HA 5 HOH 99  254  1305 HOH HOH C . 
HA 5 HOH 100 255  1310 HOH HOH C . 
HA 5 HOH 101 256  1317 HOH HOH C . 
HA 5 HOH 102 257  1319 HOH HOH C . 
HA 5 HOH 103 258  1320 HOH HOH C . 
HA 5 HOH 104 259  1354 HOH HOH C . 
HA 5 HOH 105 260  1356 HOH HOH C . 
HA 5 HOH 106 261  1364 HOH HOH C . 
HA 5 HOH 107 262  1365 HOH HOH C . 
HA 5 HOH 108 263  1366 HOH HOH C . 
IA 5 HOH 1   1401 2    HOH HOH D . 
IA 5 HOH 2   1402 12   HOH HOH D . 
IA 5 HOH 3   1403 23   HOH HOH D . 
IA 5 HOH 4   1404 28   HOH HOH D . 
IA 5 HOH 5   1405 29   HOH HOH D . 
IA 5 HOH 6   1406 31   HOH HOH D . 
IA 5 HOH 7   1407 32   HOH HOH D . 
IA 5 HOH 8   1408 34   HOH HOH D . 
IA 5 HOH 9   1409 37   HOH HOH D . 
IA 5 HOH 10  1410 43   HOH HOH D . 
IA 5 HOH 11  1411 46   HOH HOH D . 
IA 5 HOH 12  1412 50   HOH HOH D . 
IA 5 HOH 13  1413 51   HOH HOH D . 
IA 5 HOH 14  1414 56   HOH HOH D . 
IA 5 HOH 15  1415 61   HOH HOH D . 
IA 5 HOH 16  1416 68   HOH HOH D . 
IA 5 HOH 17  1417 80   HOH HOH D . 
IA 5 HOH 18  1418 92   HOH HOH D . 
IA 5 HOH 19  1419 99   HOH HOH D . 
IA 5 HOH 20  1420 112  HOH HOH D . 
IA 5 HOH 21  1421 114  HOH HOH D . 
IA 5 HOH 22  1422 117  HOH HOH D . 
IA 5 HOH 23  1423 124  HOH HOH D . 
IA 5 HOH 24  1424 137  HOH HOH D . 
IA 5 HOH 25  1425 138  HOH HOH D . 
IA 5 HOH 26  1426 140  HOH HOH D . 
IA 5 HOH 27  1427 149  HOH HOH D . 
IA 5 HOH 28  1428 151  HOH HOH D . 
IA 5 HOH 29  1429 152  HOH HOH D . 
IA 5 HOH 30  1430 153  HOH HOH D . 
IA 5 HOH 31  1431 156  HOH HOH D . 
IA 5 HOH 32  1432 163  HOH HOH D . 
IA 5 HOH 33  1433 167  HOH HOH D . 
IA 5 HOH 34  1434 171  HOH HOH D . 
IA 5 HOH 35  1435 185  HOH HOH D . 
IA 5 HOH 36  1436 186  HOH HOH D . 
IA 5 HOH 37  1437 210  HOH HOH D . 
IA 5 HOH 38  1438 213  HOH HOH D . 
IA 5 HOH 39  1439 214  HOH HOH D . 
IA 5 HOH 40  1440 215  HOH HOH D . 
IA 5 HOH 41  1441 270  HOH HOH D . 
IA 5 HOH 42  1442 277  HOH HOH D . 
IA 5 HOH 43  1443 284  HOH HOH D . 
IA 5 HOH 44  1444 285  HOH HOH D . 
IA 5 HOH 45  1445 287  HOH HOH D . 
IA 5 HOH 46  1446 291  HOH HOH D . 
IA 5 HOH 47  1447 296  HOH HOH D . 
IA 5 HOH 48  1448 299  HOH HOH D . 
IA 5 HOH 49  1449 305  HOH HOH D . 
IA 5 HOH 50  1450 312  HOH HOH D . 
IA 5 HOH 51  1451 323  HOH HOH D . 
IA 5 HOH 52  1452 329  HOH HOH D . 
IA 5 HOH 53  1453 360  HOH HOH D . 
IA 5 HOH 54  1454 364  HOH HOH D . 
IA 5 HOH 55  1455 366  HOH HOH D . 
IA 5 HOH 56  1456 370  HOH HOH D . 
IA 5 HOH 57  1457 378  HOH HOH D . 
IA 5 HOH 58  1458 379  HOH HOH D . 
IA 5 HOH 59  1459 380  HOH HOH D . 
IA 5 HOH 60  1460 402  HOH HOH D . 
IA 5 HOH 61  1461 406  HOH HOH D . 
IA 5 HOH 62  1462 412  HOH HOH D . 
IA 5 HOH 63  1463 413  HOH HOH D . 
IA 5 HOH 64  1464 443  HOH HOH D . 
IA 5 HOH 65  1465 446  HOH HOH D . 
IA 5 HOH 66  1466 449  HOH HOH D . 
IA 5 HOH 67  1467 450  HOH HOH D . 
IA 5 HOH 68  1468 467  HOH HOH D . 
IA 5 HOH 69  1469 475  HOH HOH D . 
IA 5 HOH 70  1470 487  HOH HOH D . 
IA 5 HOH 71  1471 495  HOH HOH D . 
IA 5 HOH 72  1472 516  HOH HOH D . 
IA 5 HOH 73  1473 525  HOH HOH D . 
IA 5 HOH 74  1474 537  HOH HOH D . 
IA 5 HOH 75  1475 544  HOH HOH D . 
IA 5 HOH 76  1476 559  HOH HOH D . 
IA 5 HOH 77  1477 561  HOH HOH D . 
IA 5 HOH 78  1478 569  HOH HOH D . 
IA 5 HOH 79  1479 590  HOH HOH D . 
IA 5 HOH 80  1480 598  HOH HOH D . 
IA 5 HOH 81  1481 607  HOH HOH D . 
IA 5 HOH 82  1482 631  HOH HOH D . 
IA 5 HOH 83  1483 644  HOH HOH D . 
IA 5 HOH 84  1484 653  HOH HOH D . 
IA 5 HOH 85  1485 655  HOH HOH D . 
IA 5 HOH 86  1486 660  HOH HOH D . 
IA 5 HOH 87  1487 663  HOH HOH D . 
IA 5 HOH 88  1488 667  HOH HOH D . 
IA 5 HOH 89  1489 674  HOH HOH D . 
IA 5 HOH 90  1490 702  HOH HOH D . 
IA 5 HOH 91  1491 706  HOH HOH D . 
IA 5 HOH 92  1492 709  HOH HOH D . 
IA 5 HOH 93  1493 714  HOH HOH D . 
IA 5 HOH 94  1494 726  HOH HOH D . 
IA 5 HOH 95  1495 729  HOH HOH D . 
IA 5 HOH 96  1496 731  HOH HOH D . 
IA 5 HOH 97  1497 741  HOH HOH D . 
IA 5 HOH 98  1498 742  HOH HOH D . 
IA 5 HOH 99  1499 752  HOH HOH D . 
IA 5 HOH 100 1500 775  HOH HOH D . 
IA 5 HOH 101 1501 777  HOH HOH D . 
IA 5 HOH 102 1502 781  HOH HOH D . 
IA 5 HOH 103 1503 791  HOH HOH D . 
IA 5 HOH 104 1504 795  HOH HOH D . 
IA 5 HOH 105 1505 798  HOH HOH D . 
IA 5 HOH 106 1506 812  HOH HOH D . 
IA 5 HOH 107 1507 814  HOH HOH D . 
IA 5 HOH 108 1508 815  HOH HOH D . 
IA 5 HOH 109 1509 828  HOH HOH D . 
IA 5 HOH 110 1510 833  HOH HOH D . 
IA 5 HOH 111 1511 834  HOH HOH D . 
IA 5 HOH 112 1512 845  HOH HOH D . 
IA 5 HOH 113 1513 848  HOH HOH D . 
IA 5 HOH 114 1514 862  HOH HOH D . 
IA 5 HOH 115 1515 871  HOH HOH D . 
IA 5 HOH 116 1516 875  HOH HOH D . 
IA 5 HOH 117 1517 878  HOH HOH D . 
IA 5 HOH 118 1518 899  HOH HOH D . 
IA 5 HOH 119 1519 909  HOH HOH D . 
IA 5 HOH 120 1520 916  HOH HOH D . 
IA 5 HOH 121 1521 917  HOH HOH D . 
IA 5 HOH 122 1522 974  HOH HOH D . 
IA 5 HOH 123 1523 981  HOH HOH D . 
IA 5 HOH 124 1524 994  HOH HOH D . 
IA 5 HOH 125 1525 1009 HOH HOH D . 
IA 5 HOH 126 1526 1020 HOH HOH D . 
IA 5 HOH 127 1527 1022 HOH HOH D . 
IA 5 HOH 128 1528 1024 HOH HOH D . 
IA 5 HOH 129 1529 1036 HOH HOH D . 
IA 5 HOH 130 1530 1050 HOH HOH D . 
IA 5 HOH 131 1531 1076 HOH HOH D . 
IA 5 HOH 132 1532 1083 HOH HOH D . 
IA 5 HOH 133 1533 1088 HOH HOH D . 
IA 5 HOH 134 1534 1091 HOH HOH D . 
IA 5 HOH 135 1535 1100 HOH HOH D . 
IA 5 HOH 136 1536 1118 HOH HOH D . 
IA 5 HOH 137 1537 1129 HOH HOH D . 
IA 5 HOH 138 1538 1132 HOH HOH D . 
IA 5 HOH 139 1539 1135 HOH HOH D . 
IA 5 HOH 140 1540 1146 HOH HOH D . 
IA 5 HOH 141 1541 1162 HOH HOH D . 
IA 5 HOH 142 1542 1177 HOH HOH D . 
IA 5 HOH 143 1543 1180 HOH HOH D . 
IA 5 HOH 144 1544 1185 HOH HOH D . 
IA 5 HOH 145 1545 1188 HOH HOH D . 
IA 5 HOH 146 1546 1190 HOH HOH D . 
IA 5 HOH 147 1547 1194 HOH HOH D . 
IA 5 HOH 148 1548 1196 HOH HOH D . 
IA 5 HOH 149 1549 1203 HOH HOH D . 
IA 5 HOH 150 1550 1228 HOH HOH D . 
IA 5 HOH 151 1551 1229 HOH HOH D . 
IA 5 HOH 152 1552 1231 HOH HOH D . 
IA 5 HOH 153 1553 1235 HOH HOH D . 
IA 5 HOH 154 1554 1239 HOH HOH D . 
IA 5 HOH 155 1555 1240 HOH HOH D . 
IA 5 HOH 156 1556 1246 HOH HOH D . 
IA 5 HOH 157 1557 1257 HOH HOH D . 
IA 5 HOH 158 1558 1260 HOH HOH D . 
IA 5 HOH 159 1559 1274 HOH HOH D . 
IA 5 HOH 160 1560 1275 HOH HOH D . 
IA 5 HOH 161 1561 1299 HOH HOH D . 
IA 5 HOH 162 1562 1333 HOH HOH D . 
IA 5 HOH 163 1563 1335 HOH HOH D . 
IA 5 HOH 164 1564 1336 HOH HOH D . 
IA 5 HOH 165 1565 1344 HOH HOH D . 
IA 5 HOH 166 1566 1346 HOH HOH D . 
IA 5 HOH 167 1567 1347 HOH HOH D . 
IA 5 HOH 168 1568 1362 HOH HOH D . 
IA 5 HOH 169 1569 1370 HOH HOH D . 
IA 5 HOH 170 1570 1378 HOH HOH D . 
JA 5 HOH 1   156  5    HOH HOH E . 
JA 5 HOH 2   157  7    HOH HOH E . 
JA 5 HOH 3   158  21   HOH HOH E . 
JA 5 HOH 4   159  22   HOH HOH E . 
JA 5 HOH 5   160  24   HOH HOH E . 
JA 5 HOH 6   161  27   HOH HOH E . 
JA 5 HOH 7   162  30   HOH HOH E . 
JA 5 HOH 8   163  35   HOH HOH E . 
JA 5 HOH 9   164  36   HOH HOH E . 
JA 5 HOH 10  165  38   HOH HOH E . 
JA 5 HOH 11  166  41   HOH HOH E . 
JA 5 HOH 12  167  60   HOH HOH E . 
JA 5 HOH 13  168  67   HOH HOH E . 
JA 5 HOH 14  169  88   HOH HOH E . 
JA 5 HOH 15  170  91   HOH HOH E . 
JA 5 HOH 16  171  98   HOH HOH E . 
JA 5 HOH 17  172  102  HOH HOH E . 
JA 5 HOH 18  173  107  HOH HOH E . 
JA 5 HOH 19  174  120  HOH HOH E . 
JA 5 HOH 20  175  121  HOH HOH E . 
JA 5 HOH 21  176  128  HOH HOH E . 
JA 5 HOH 22  177  168  HOH HOH E . 
JA 5 HOH 23  178  176  HOH HOH E . 
JA 5 HOH 24  179  181  HOH HOH E . 
JA 5 HOH 25  180  184  HOH HOH E . 
JA 5 HOH 26  181  189  HOH HOH E . 
JA 5 HOH 27  182  190  HOH HOH E . 
JA 5 HOH 28  183  195  HOH HOH E . 
JA 5 HOH 29  184  197  HOH HOH E . 
JA 5 HOH 30  185  198  HOH HOH E . 
JA 5 HOH 31  186  201  HOH HOH E . 
JA 5 HOH 32  187  204  HOH HOH E . 
JA 5 HOH 33  188  209  HOH HOH E . 
JA 5 HOH 34  189  218  HOH HOH E . 
JA 5 HOH 35  190  220  HOH HOH E . 
JA 5 HOH 36  191  227  HOH HOH E . 
JA 5 HOH 37  192  228  HOH HOH E . 
JA 5 HOH 38  193  241  HOH HOH E . 
JA 5 HOH 39  194  243  HOH HOH E . 
JA 5 HOH 40  195  246  HOH HOH E . 
JA 5 HOH 41  196  247  HOH HOH E . 
JA 5 HOH 42  197  249  HOH HOH E . 
JA 5 HOH 43  198  250  HOH HOH E . 
JA 5 HOH 44  199  264  HOH HOH E . 
JA 5 HOH 45  200  273  HOH HOH E . 
JA 5 HOH 46  201  276  HOH HOH E . 
JA 5 HOH 47  202  279  HOH HOH E . 
JA 5 HOH 48  203  301  HOH HOH E . 
JA 5 HOH 49  204  302  HOH HOH E . 
JA 5 HOH 50  205  306  HOH HOH E . 
JA 5 HOH 51  206  316  HOH HOH E . 
JA 5 HOH 52  207  326  HOH HOH E . 
JA 5 HOH 53  208  338  HOH HOH E . 
JA 5 HOH 54  209  340  HOH HOH E . 
JA 5 HOH 55  210  342  HOH HOH E . 
JA 5 HOH 56  211  343  HOH HOH E . 
JA 5 HOH 57  212  349  HOH HOH E . 
JA 5 HOH 58  213  350  HOH HOH E . 
JA 5 HOH 59  214  362  HOH HOH E . 
JA 5 HOH 60  215  381  HOH HOH E . 
JA 5 HOH 61  216  390  HOH HOH E . 
JA 5 HOH 62  217  397  HOH HOH E . 
JA 5 HOH 63  218  398  HOH HOH E . 
JA 5 HOH 64  219  403  HOH HOH E . 
JA 5 HOH 65  220  410  HOH HOH E . 
JA 5 HOH 66  221  428  HOH HOH E . 
JA 5 HOH 67  222  431  HOH HOH E . 
JA 5 HOH 68  223  436  HOH HOH E . 
JA 5 HOH 69  224  437  HOH HOH E . 
JA 5 HOH 70  225  463  HOH HOH E . 
JA 5 HOH 71  226  469  HOH HOH E . 
JA 5 HOH 72  227  471  HOH HOH E . 
JA 5 HOH 73  228  476  HOH HOH E . 
JA 5 HOH 74  229  479  HOH HOH E . 
JA 5 HOH 75  230  481  HOH HOH E . 
JA 5 HOH 76  231  483  HOH HOH E . 
JA 5 HOH 77  232  490  HOH HOH E . 
JA 5 HOH 78  233  497  HOH HOH E . 
JA 5 HOH 79  234  503  HOH HOH E . 
JA 5 HOH 80  235  524  HOH HOH E . 
JA 5 HOH 81  236  530  HOH HOH E . 
JA 5 HOH 82  237  535  HOH HOH E . 
JA 5 HOH 83  238  554  HOH HOH E . 
JA 5 HOH 84  239  557  HOH HOH E . 
JA 5 HOH 85  240  564  HOH HOH E . 
JA 5 HOH 86  241  583  HOH HOH E . 
JA 5 HOH 87  242  586  HOH HOH E . 
JA 5 HOH 88  243  591  HOH HOH E . 
JA 5 HOH 89  244  593  HOH HOH E . 
JA 5 HOH 90  245  597  HOH HOH E . 
JA 5 HOH 91  246  602  HOH HOH E . 
JA 5 HOH 92  247  611  HOH HOH E . 
JA 5 HOH 93  248  618  HOH HOH E . 
JA 5 HOH 94  249  635  HOH HOH E . 
JA 5 HOH 95  250  642  HOH HOH E . 
JA 5 HOH 96  251  648  HOH HOH E . 
JA 5 HOH 97  252  654  HOH HOH E . 
JA 5 HOH 98  253  679  HOH HOH E . 
JA 5 HOH 99  254  681  HOH HOH E . 
JA 5 HOH 100 255  685  HOH HOH E . 
JA 5 HOH 101 256  687  HOH HOH E . 
JA 5 HOH 102 257  689  HOH HOH E . 
JA 5 HOH 103 258  693  HOH HOH E . 
JA 5 HOH 104 259  696  HOH HOH E . 
JA 5 HOH 105 260  698  HOH HOH E . 
JA 5 HOH 106 261  711  HOH HOH E . 
JA 5 HOH 107 262  719  HOH HOH E . 
JA 5 HOH 108 263  721  HOH HOH E . 
JA 5 HOH 109 264  732  HOH HOH E . 
JA 5 HOH 110 265  734  HOH HOH E . 
JA 5 HOH 111 266  745  HOH HOH E . 
JA 5 HOH 112 267  750  HOH HOH E . 
JA 5 HOH 113 268  763  HOH HOH E . 
JA 5 HOH 114 269  773  HOH HOH E . 
JA 5 HOH 115 270  788  HOH HOH E . 
JA 5 HOH 116 271  799  HOH HOH E . 
JA 5 HOH 117 272  806  HOH HOH E . 
JA 5 HOH 118 273  807  HOH HOH E . 
JA 5 HOH 119 274  813  HOH HOH E . 
JA 5 HOH 120 275  830  HOH HOH E . 
JA 5 HOH 121 276  842  HOH HOH E . 
JA 5 HOH 122 277  843  HOH HOH E . 
JA 5 HOH 123 278  846  HOH HOH E . 
JA 5 HOH 124 279  853  HOH HOH E . 
JA 5 HOH 125 280  854  HOH HOH E . 
JA 5 HOH 126 281  857  HOH HOH E . 
JA 5 HOH 127 282  859  HOH HOH E . 
JA 5 HOH 128 283  876  HOH HOH E . 
JA 5 HOH 129 284  881  HOH HOH E . 
JA 5 HOH 130 285  890  HOH HOH E . 
JA 5 HOH 131 286  894  HOH HOH E . 
JA 5 HOH 132 287  900  HOH HOH E . 
JA 5 HOH 133 288  901  HOH HOH E . 
JA 5 HOH 134 289  914  HOH HOH E . 
JA 5 HOH 135 290  931  HOH HOH E . 
JA 5 HOH 136 291  952  HOH HOH E . 
JA 5 HOH 137 292  953  HOH HOH E . 
JA 5 HOH 138 293  955  HOH HOH E . 
JA 5 HOH 139 294  962  HOH HOH E . 
JA 5 HOH 140 295  973  HOH HOH E . 
JA 5 HOH 141 296  979  HOH HOH E . 
JA 5 HOH 142 297  980  HOH HOH E . 
JA 5 HOH 143 298  990  HOH HOH E . 
JA 5 HOH 144 299  998  HOH HOH E . 
JA 5 HOH 145 300  1008 HOH HOH E . 
JA 5 HOH 146 301  1012 HOH HOH E . 
JA 5 HOH 147 302  1013 HOH HOH E . 
JA 5 HOH 148 303  1029 HOH HOH E . 
JA 5 HOH 149 304  1032 HOH HOH E . 
JA 5 HOH 150 305  1035 HOH HOH E . 
JA 5 HOH 151 306  1039 HOH HOH E . 
JA 5 HOH 152 307  1043 HOH HOH E . 
JA 5 HOH 153 308  1049 HOH HOH E . 
JA 5 HOH 154 309  1053 HOH HOH E . 
JA 5 HOH 155 310  1064 HOH HOH E . 
JA 5 HOH 156 311  1071 HOH HOH E . 
JA 5 HOH 157 312  1072 HOH HOH E . 
JA 5 HOH 158 313  1074 HOH HOH E . 
JA 5 HOH 159 314  1080 HOH HOH E . 
JA 5 HOH 160 315  1085 HOH HOH E . 
JA 5 HOH 161 316  1098 HOH HOH E . 
JA 5 HOH 162 317  1102 HOH HOH E . 
JA 5 HOH 163 318  1106 HOH HOH E . 
JA 5 HOH 164 319  1111 HOH HOH E . 
JA 5 HOH 165 320  1116 HOH HOH E . 
JA 5 HOH 166 321  1141 HOH HOH E . 
JA 5 HOH 167 322  1171 HOH HOH E . 
JA 5 HOH 168 323  1174 HOH HOH E . 
JA 5 HOH 169 324  1183 HOH HOH E . 
JA 5 HOH 170 325  1186 HOH HOH E . 
JA 5 HOH 171 326  1198 HOH HOH E . 
JA 5 HOH 172 327  1205 HOH HOH E . 
JA 5 HOH 173 328  1214 HOH HOH E . 
JA 5 HOH 174 329  1248 HOH HOH E . 
JA 5 HOH 175 330  1263 HOH HOH E . 
JA 5 HOH 176 331  1264 HOH HOH E . 
JA 5 HOH 177 332  1271 HOH HOH E . 
JA 5 HOH 178 333  1304 HOH HOH E . 
JA 5 HOH 179 334  1321 HOH HOH E . 
JA 5 HOH 180 335  1324 HOH HOH E . 
JA 5 HOH 181 336  1327 HOH HOH E . 
JA 5 HOH 182 337  1328 HOH HOH E . 
JA 5 HOH 183 338  1339 HOH HOH E . 
JA 5 HOH 184 339  1348 HOH HOH E . 
JA 5 HOH 185 340  1351 HOH HOH E . 
JA 5 HOH 186 341  1360 HOH HOH E . 
JA 5 HOH 187 342  1368 HOH HOH E . 
JA 5 HOH 188 343  1379 HOH HOH E . 
JA 5 HOH 189 344  1384 HOH HOH E . 
JA 5 HOH 190 345  1388 HOH HOH E . 
JA 5 HOH 191 346  1389 HOH HOH E . 
KA 5 HOH 1   156  3    HOH HOH F . 
KA 5 HOH 2   157  9    HOH HOH F . 
KA 5 HOH 3   158  10   HOH HOH F . 
KA 5 HOH 4   159  14   HOH HOH F . 
KA 5 HOH 5   160  40   HOH HOH F . 
KA 5 HOH 6   161  42   HOH HOH F . 
KA 5 HOH 7   162  44   HOH HOH F . 
KA 5 HOH 8   163  63   HOH HOH F . 
KA 5 HOH 9   164  65   HOH HOH F . 
KA 5 HOH 10  165  69   HOH HOH F . 
KA 5 HOH 11  166  70   HOH HOH F . 
KA 5 HOH 12  167  74   HOH HOH F . 
KA 5 HOH 13  168  76   HOH HOH F . 
KA 5 HOH 14  169  84   HOH HOH F . 
KA 5 HOH 15  170  89   HOH HOH F . 
KA 5 HOH 16  171  94   HOH HOH F . 
KA 5 HOH 17  172  95   HOH HOH F . 
KA 5 HOH 18  173  100  HOH HOH F . 
KA 5 HOH 19  174  101  HOH HOH F . 
KA 5 HOH 20  175  104  HOH HOH F . 
KA 5 HOH 21  176  110  HOH HOH F . 
KA 5 HOH 22  177  113  HOH HOH F . 
KA 5 HOH 23  178  115  HOH HOH F . 
KA 5 HOH 24  179  123  HOH HOH F . 
KA 5 HOH 25  180  126  HOH HOH F . 
KA 5 HOH 26  181  132  HOH HOH F . 
KA 5 HOH 27  182  134  HOH HOH F . 
KA 5 HOH 28  183  135  HOH HOH F . 
KA 5 HOH 29  184  139  HOH HOH F . 
KA 5 HOH 30  185  141  HOH HOH F . 
KA 5 HOH 31  186  144  HOH HOH F . 
KA 5 HOH 32  187  150  HOH HOH F . 
KA 5 HOH 33  188  157  HOH HOH F . 
KA 5 HOH 34  189  164  HOH HOH F . 
KA 5 HOH 35  190  165  HOH HOH F . 
KA 5 HOH 36  191  166  HOH HOH F . 
KA 5 HOH 37  192  169  HOH HOH F . 
KA 5 HOH 38  193  175  HOH HOH F . 
KA 5 HOH 39  194  183  HOH HOH F . 
KA 5 HOH 40  195  191  HOH HOH F . 
KA 5 HOH 41  196  205  HOH HOH F . 
KA 5 HOH 42  197  207  HOH HOH F . 
KA 5 HOH 43  198  216  HOH HOH F . 
KA 5 HOH 44  199  219  HOH HOH F . 
KA 5 HOH 45  200  221  HOH HOH F . 
KA 5 HOH 46  201  226  HOH HOH F . 
KA 5 HOH 47  202  237  HOH HOH F . 
KA 5 HOH 48  203  242  HOH HOH F . 
KA 5 HOH 49  204  248  HOH HOH F . 
KA 5 HOH 50  205  254  HOH HOH F . 
KA 5 HOH 51  206  255  HOH HOH F . 
KA 5 HOH 52  207  258  HOH HOH F . 
KA 5 HOH 53  208  262  HOH HOH F . 
KA 5 HOH 54  209  271  HOH HOH F . 
KA 5 HOH 55  210  298  HOH HOH F . 
KA 5 HOH 56  211  300  HOH HOH F . 
KA 5 HOH 57  212  308  HOH HOH F . 
KA 5 HOH 58  213  310  HOH HOH F . 
KA 5 HOH 59  214  311  HOH HOH F . 
KA 5 HOH 60  215  313  HOH HOH F . 
KA 5 HOH 61  216  314  HOH HOH F . 
KA 5 HOH 62  217  319  HOH HOH F . 
KA 5 HOH 63  218  335  HOH HOH F . 
KA 5 HOH 64  219  337  HOH HOH F . 
KA 5 HOH 65  220  339  HOH HOH F . 
KA 5 HOH 66  221  341  HOH HOH F . 
KA 5 HOH 67  222  357  HOH HOH F . 
KA 5 HOH 68  223  368  HOH HOH F . 
KA 5 HOH 69  224  371  HOH HOH F . 
KA 5 HOH 70  225  375  HOH HOH F . 
KA 5 HOH 71  226  401  HOH HOH F . 
KA 5 HOH 72  227  409  HOH HOH F . 
KA 5 HOH 73  228  411  HOH HOH F . 
KA 5 HOH 74  229  417  HOH HOH F . 
KA 5 HOH 75  230  420  HOH HOH F . 
KA 5 HOH 76  231  433  HOH HOH F . 
KA 5 HOH 77  232  448  HOH HOH F . 
KA 5 HOH 78  233  456  HOH HOH F . 
KA 5 HOH 79  234  461  HOH HOH F . 
KA 5 HOH 80  235  473  HOH HOH F . 
KA 5 HOH 81  236  477  HOH HOH F . 
KA 5 HOH 82  237  488  HOH HOH F . 
KA 5 HOH 83  238  489  HOH HOH F . 
KA 5 HOH 84  239  493  HOH HOH F . 
KA 5 HOH 85  240  494  HOH HOH F . 
KA 5 HOH 86  241  505  HOH HOH F . 
KA 5 HOH 87  242  520  HOH HOH F . 
KA 5 HOH 88  243  522  HOH HOH F . 
KA 5 HOH 89  244  539  HOH HOH F . 
KA 5 HOH 90  245  540  HOH HOH F . 
KA 5 HOH 91  246  541  HOH HOH F . 
KA 5 HOH 92  247  549  HOH HOH F . 
KA 5 HOH 93  248  550  HOH HOH F . 
KA 5 HOH 94  249  551  HOH HOH F . 
KA 5 HOH 95  250  571  HOH HOH F . 
KA 5 HOH 96  251  584  HOH HOH F . 
KA 5 HOH 97  252  608  HOH HOH F . 
KA 5 HOH 98  253  609  HOH HOH F . 
KA 5 HOH 99  254  610  HOH HOH F . 
KA 5 HOH 100 255  616  HOH HOH F . 
KA 5 HOH 101 256  625  HOH HOH F . 
KA 5 HOH 102 257  627  HOH HOH F . 
KA 5 HOH 103 258  658  HOH HOH F . 
KA 5 HOH 104 259  659  HOH HOH F . 
KA 5 HOH 105 260  669  HOH HOH F . 
KA 5 HOH 106 261  672  HOH HOH F . 
KA 5 HOH 107 262  684  HOH HOH F . 
KA 5 HOH 108 263  715  HOH HOH F . 
KA 5 HOH 109 264  724  HOH HOH F . 
KA 5 HOH 110 265  733  HOH HOH F . 
KA 5 HOH 111 266  764  HOH HOH F . 
KA 5 HOH 112 267  765  HOH HOH F . 
KA 5 HOH 113 268  766  HOH HOH F . 
KA 5 HOH 114 269  768  HOH HOH F . 
KA 5 HOH 115 270  771  HOH HOH F . 
KA 5 HOH 116 271  772  HOH HOH F . 
KA 5 HOH 117 272  787  HOH HOH F . 
KA 5 HOH 118 273  789  HOH HOH F . 
KA 5 HOH 119 274  792  HOH HOH F . 
KA 5 HOH 120 275  793  HOH HOH F . 
KA 5 HOH 121 276  797  HOH HOH F . 
KA 5 HOH 122 277  817  HOH HOH F . 
KA 5 HOH 123 278  819  HOH HOH F . 
KA 5 HOH 124 279  820  HOH HOH F . 
KA 5 HOH 125 280  849  HOH HOH F . 
KA 5 HOH 126 281  851  HOH HOH F . 
KA 5 HOH 127 282  852  HOH HOH F . 
KA 5 HOH 128 283  866  HOH HOH F . 
KA 5 HOH 129 284  870  HOH HOH F . 
KA 5 HOH 130 285  874  HOH HOH F . 
KA 5 HOH 131 286  877  HOH HOH F . 
KA 5 HOH 132 287  880  HOH HOH F . 
KA 5 HOH 133 288  885  HOH HOH F . 
KA 5 HOH 134 289  887  HOH HOH F . 
KA 5 HOH 135 290  893  HOH HOH F . 
KA 5 HOH 136 291  904  HOH HOH F . 
KA 5 HOH 137 292  915  HOH HOH F . 
KA 5 HOH 138 293  924  HOH HOH F . 
KA 5 HOH 139 294  925  HOH HOH F . 
KA 5 HOH 140 295  926  HOH HOH F . 
KA 5 HOH 141 296  947  HOH HOH F . 
KA 5 HOH 142 297  948  HOH HOH F . 
KA 5 HOH 143 298  957  HOH HOH F . 
KA 5 HOH 144 299  993  HOH HOH F . 
KA 5 HOH 145 300  1004 HOH HOH F . 
KA 5 HOH 146 301  1010 HOH HOH F . 
KA 5 HOH 147 302  1014 HOH HOH F . 
KA 5 HOH 148 303  1018 HOH HOH F . 
KA 5 HOH 149 304  1023 HOH HOH F . 
KA 5 HOH 150 305  1034 HOH HOH F . 
KA 5 HOH 151 306  1038 HOH HOH F . 
KA 5 HOH 152 307  1040 HOH HOH F . 
KA 5 HOH 153 308  1056 HOH HOH F . 
KA 5 HOH 154 309  1060 HOH HOH F . 
KA 5 HOH 155 310  1065 HOH HOH F . 
KA 5 HOH 156 311  1079 HOH HOH F . 
KA 5 HOH 157 312  1086 HOH HOH F . 
KA 5 HOH 158 313  1087 HOH HOH F . 
KA 5 HOH 159 314  1097 HOH HOH F . 
KA 5 HOH 160 315  1099 HOH HOH F . 
KA 5 HOH 161 316  1108 HOH HOH F . 
KA 5 HOH 162 317  1112 HOH HOH F . 
KA 5 HOH 163 318  1113 HOH HOH F . 
KA 5 HOH 164 319  1125 HOH HOH F . 
KA 5 HOH 165 320  1126 HOH HOH F . 
KA 5 HOH 166 321  1133 HOH HOH F . 
KA 5 HOH 167 322  1140 HOH HOH F . 
KA 5 HOH 168 323  1156 HOH HOH F . 
KA 5 HOH 169 324  1159 HOH HOH F . 
KA 5 HOH 170 325  1163 HOH HOH F . 
KA 5 HOH 171 326  1169 HOH HOH F . 
KA 5 HOH 172 327  1178 HOH HOH F . 
KA 5 HOH 173 328  1192 HOH HOH F . 
KA 5 HOH 174 329  1201 HOH HOH F . 
KA 5 HOH 175 330  1202 HOH HOH F . 
KA 5 HOH 176 331  1204 HOH HOH F . 
KA 5 HOH 177 332  1270 HOH HOH F . 
KA 5 HOH 178 333  1276 HOH HOH F . 
KA 5 HOH 179 334  1290 HOH HOH F . 
KA 5 HOH 180 335  1295 HOH HOH F . 
KA 5 HOH 181 336  1301 HOH HOH F . 
KA 5 HOH 182 337  1311 HOH HOH F . 
KA 5 HOH 183 338  1313 HOH HOH F . 
LA 5 HOH 1   156  54   HOH HOH G . 
LA 5 HOH 2   157  129  HOH HOH G . 
LA 5 HOH 3   158  172  HOH HOH G . 
LA 5 HOH 4   159  253  HOH HOH G . 
LA 5 HOH 5   160  278  HOH HOH G . 
LA 5 HOH 6   161  295  HOH HOH G . 
LA 5 HOH 7   162  315  HOH HOH G . 
LA 5 HOH 8   163  336  HOH HOH G . 
LA 5 HOH 9   164  363  HOH HOH G . 
LA 5 HOH 10  165  374  HOH HOH G . 
LA 5 HOH 11  166  399  HOH HOH G . 
LA 5 HOH 12  167  400  HOH HOH G . 
LA 5 HOH 13  168  408  HOH HOH G . 
LA 5 HOH 14  169  422  HOH HOH G . 
LA 5 HOH 15  170  430  HOH HOH G . 
LA 5 HOH 16  171  491  HOH HOH G . 
LA 5 HOH 17  172  498  HOH HOH G . 
LA 5 HOH 18  173  502  HOH HOH G . 
LA 5 HOH 19  174  518  HOH HOH G . 
LA 5 HOH 20  175  523  HOH HOH G . 
LA 5 HOH 21  176  533  HOH HOH G . 
LA 5 HOH 22  177  538  HOH HOH G . 
LA 5 HOH 23  178  542  HOH HOH G . 
LA 5 HOH 24  179  592  HOH HOH G . 
LA 5 HOH 25  180  601  HOH HOH G . 
LA 5 HOH 26  181  622  HOH HOH G . 
LA 5 HOH 27  182  634  HOH HOH G . 
LA 5 HOH 28  183  649  HOH HOH G . 
LA 5 HOH 29  184  675  HOH HOH G . 
LA 5 HOH 30  185  695  HOH HOH G . 
LA 5 HOH 31  186  713  HOH HOH G . 
LA 5 HOH 32  187  720  HOH HOH G . 
LA 5 HOH 33  188  780  HOH HOH G . 
LA 5 HOH 34  189  803  HOH HOH G . 
LA 5 HOH 35  190  825  HOH HOH G . 
LA 5 HOH 36  191  826  HOH HOH G . 
LA 5 HOH 37  192  827  HOH HOH G . 
LA 5 HOH 38  193  831  HOH HOH G . 
LA 5 HOH 39  194  864  HOH HOH G . 
LA 5 HOH 40  195  891  HOH HOH G . 
LA 5 HOH 41  196  897  HOH HOH G . 
LA 5 HOH 42  197  908  HOH HOH G . 
LA 5 HOH 43  198  910  HOH HOH G . 
LA 5 HOH 44  199  921  HOH HOH G . 
LA 5 HOH 45  200  937  HOH HOH G . 
LA 5 HOH 46  201  954  HOH HOH G . 
LA 5 HOH 47  202  963  HOH HOH G . 
LA 5 HOH 48  203  970  HOH HOH G . 
LA 5 HOH 49  204  971  HOH HOH G . 
LA 5 HOH 50  205  983  HOH HOH G . 
LA 5 HOH 51  206  997  HOH HOH G . 
LA 5 HOH 52  207  1003 HOH HOH G . 
LA 5 HOH 53  208  1007 HOH HOH G . 
LA 5 HOH 54  209  1016 HOH HOH G . 
LA 5 HOH 55  210  1028 HOH HOH G . 
LA 5 HOH 56  211  1033 HOH HOH G . 
LA 5 HOH 57  212  1051 HOH HOH G . 
LA 5 HOH 58  213  1062 HOH HOH G . 
LA 5 HOH 59  214  1073 HOH HOH G . 
LA 5 HOH 60  215  1077 HOH HOH G . 
LA 5 HOH 61  216  1082 HOH HOH G . 
LA 5 HOH 62  217  1096 HOH HOH G . 
LA 5 HOH 63  218  1110 HOH HOH G . 
LA 5 HOH 64  219  1131 HOH HOH G . 
LA 5 HOH 65  220  1134 HOH HOH G . 
LA 5 HOH 66  221  1136 HOH HOH G . 
LA 5 HOH 67  222  1138 HOH HOH G . 
LA 5 HOH 68  223  1144 HOH HOH G . 
LA 5 HOH 69  224  1147 HOH HOH G . 
LA 5 HOH 70  225  1160 HOH HOH G . 
LA 5 HOH 71  226  1172 HOH HOH G . 
LA 5 HOH 72  227  1184 HOH HOH G . 
LA 5 HOH 73  228  1197 HOH HOH G . 
LA 5 HOH 74  229  1219 HOH HOH G . 
LA 5 HOH 75  230  1222 HOH HOH G . 
LA 5 HOH 76  231  1225 HOH HOH G . 
LA 5 HOH 77  232  1253 HOH HOH G . 
LA 5 HOH 78  233  1258 HOH HOH G . 
LA 5 HOH 79  234  1283 HOH HOH G . 
LA 5 HOH 80  235  1292 HOH HOH G . 
LA 5 HOH 81  236  1316 HOH HOH G . 
LA 5 HOH 82  237  1318 HOH HOH G . 
LA 5 HOH 83  238  1330 HOH HOH G . 
LA 5 HOH 84  239  1332 HOH HOH G . 
LA 5 HOH 85  240  1334 HOH HOH G . 
LA 5 HOH 86  241  1342 HOH HOH G . 
LA 5 HOH 87  242  1352 HOH HOH G . 
LA 5 HOH 88  243  1357 HOH HOH G . 
LA 5 HOH 89  244  1369 HOH HOH G . 
LA 5 HOH 90  245  1376 HOH HOH G . 
MA 5 HOH 1   156  8    HOH HOH H . 
MA 5 HOH 2   157  47   HOH HOH H . 
MA 5 HOH 3   158  48   HOH HOH H . 
MA 5 HOH 4   159  66   HOH HOH H . 
MA 5 HOH 5   160  73   HOH HOH H . 
MA 5 HOH 6   161  82   HOH HOH H . 
MA 5 HOH 7   162  146  HOH HOH H . 
MA 5 HOH 8   163  147  HOH HOH H . 
MA 5 HOH 9   164  154  HOH HOH H . 
MA 5 HOH 10  165  160  HOH HOH H . 
MA 5 HOH 11  166  161  HOH HOH H . 
MA 5 HOH 12  167  173  HOH HOH H . 
MA 5 HOH 13  168  174  HOH HOH H . 
MA 5 HOH 14  169  178  HOH HOH H . 
MA 5 HOH 15  170  202  HOH HOH H . 
MA 5 HOH 16  171  252  HOH HOH H . 
MA 5 HOH 17  172  267  HOH HOH H . 
MA 5 HOH 18  173  275  HOH HOH H . 
MA 5 HOH 19  174  292  HOH HOH H . 
MA 5 HOH 20  175  303  HOH HOH H . 
MA 5 HOH 21  176  307  HOH HOH H . 
MA 5 HOH 22  177  332  HOH HOH H . 
MA 5 HOH 23  178  348  HOH HOH H . 
MA 5 HOH 24  179  355  HOH HOH H . 
MA 5 HOH 25  180  376  HOH HOH H . 
MA 5 HOH 26  181  382  HOH HOH H . 
MA 5 HOH 27  182  384  HOH HOH H . 
MA 5 HOH 28  183  389  HOH HOH H . 
MA 5 HOH 29  184  396  HOH HOH H . 
MA 5 HOH 30  185  432  HOH HOH H . 
MA 5 HOH 31  186  435  HOH HOH H . 
MA 5 HOH 32  187  444  HOH HOH H . 
MA 5 HOH 33  188  447  HOH HOH H . 
MA 5 HOH 34  189  478  HOH HOH H . 
MA 5 HOH 35  190  480  HOH HOH H . 
MA 5 HOH 36  191  486  HOH HOH H . 
MA 5 HOH 37  192  492  HOH HOH H . 
MA 5 HOH 38  193  508  HOH HOH H . 
MA 5 HOH 39  194  509  HOH HOH H . 
MA 5 HOH 40  195  511  HOH HOH H . 
MA 5 HOH 41  196  517  HOH HOH H . 
MA 5 HOH 42  197  521  HOH HOH H . 
MA 5 HOH 43  198  556  HOH HOH H . 
MA 5 HOH 44  199  560  HOH HOH H . 
MA 5 HOH 45  200  596  HOH HOH H . 
MA 5 HOH 46  201  613  HOH HOH H . 
MA 5 HOH 47  202  628  HOH HOH H . 
MA 5 HOH 48  203  632  HOH HOH H . 
MA 5 HOH 49  204  639  HOH HOH H . 
MA 5 HOH 50  205  640  HOH HOH H . 
MA 5 HOH 51  206  665  HOH HOH H . 
MA 5 HOH 52  207  668  HOH HOH H . 
MA 5 HOH 53  208  680  HOH HOH H . 
MA 5 HOH 54  209  682  HOH HOH H . 
MA 5 HOH 55  210  690  HOH HOH H . 
MA 5 HOH 56  211  701  HOH HOH H . 
MA 5 HOH 57  212  704  HOH HOH H . 
MA 5 HOH 58  213  705  HOH HOH H . 
MA 5 HOH 59  214  712  HOH HOH H . 
MA 5 HOH 60  215  716  HOH HOH H . 
MA 5 HOH 61  216  718  HOH HOH H . 
MA 5 HOH 62  217  723  HOH HOH H . 
MA 5 HOH 63  218  730  HOH HOH H . 
MA 5 HOH 64  219  738  HOH HOH H . 
MA 5 HOH 65  220  739  HOH HOH H . 
MA 5 HOH 66  221  740  HOH HOH H . 
MA 5 HOH 67  222  749  HOH HOH H . 
MA 5 HOH 68  223  751  HOH HOH H . 
MA 5 HOH 69  224  762  HOH HOH H . 
MA 5 HOH 70  225  767  HOH HOH H . 
MA 5 HOH 71  226  800  HOH HOH H . 
MA 5 HOH 72  227  821  HOH HOH H . 
MA 5 HOH 73  228  823  HOH HOH H . 
MA 5 HOH 74  229  838  HOH HOH H . 
MA 5 HOH 75  230  839  HOH HOH H . 
MA 5 HOH 76  231  847  HOH HOH H . 
MA 5 HOH 77  232  858  HOH HOH H . 
MA 5 HOH 78  233  865  HOH HOH H . 
MA 5 HOH 79  234  868  HOH HOH H . 
MA 5 HOH 80  235  886  HOH HOH H . 
MA 5 HOH 81  236  902  HOH HOH H . 
MA 5 HOH 82  237  906  HOH HOH H . 
MA 5 HOH 83  238  911  HOH HOH H . 
MA 5 HOH 84  239  912  HOH HOH H . 
MA 5 HOH 85  240  928  HOH HOH H . 
MA 5 HOH 86  241  934  HOH HOH H . 
MA 5 HOH 87  242  936  HOH HOH H . 
MA 5 HOH 88  243  941  HOH HOH H . 
MA 5 HOH 89  244  945  HOH HOH H . 
MA 5 HOH 90  245  949  HOH HOH H . 
MA 5 HOH 91  246  956  HOH HOH H . 
MA 5 HOH 92  247  976  HOH HOH H . 
MA 5 HOH 93  248  995  HOH HOH H . 
MA 5 HOH 94  249  1000 HOH HOH H . 
MA 5 HOH 95  250  1002 HOH HOH H . 
MA 5 HOH 96  251  1054 HOH HOH H . 
MA 5 HOH 97  252  1055 HOH HOH H . 
MA 5 HOH 98  253  1057 HOH HOH H . 
MA 5 HOH 99  254  1061 HOH HOH H . 
MA 5 HOH 100 255  1063 HOH HOH H . 
MA 5 HOH 101 256  1069 HOH HOH H . 
MA 5 HOH 102 257  1104 HOH HOH H . 
MA 5 HOH 103 258  1114 HOH HOH H . 
MA 5 HOH 104 259  1123 HOH HOH H . 
MA 5 HOH 105 260  1127 HOH HOH H . 
MA 5 HOH 106 261  1151 HOH HOH H . 
MA 5 HOH 107 262  1167 HOH HOH H . 
MA 5 HOH 108 263  1170 HOH HOH H . 
MA 5 HOH 109 264  1179 HOH HOH H . 
MA 5 HOH 110 265  1191 HOH HOH H . 
MA 5 HOH 111 266  1207 HOH HOH H . 
MA 5 HOH 112 267  1209 HOH HOH H . 
MA 5 HOH 113 268  1211 HOH HOH H . 
MA 5 HOH 114 269  1215 HOH HOH H . 
MA 5 HOH 115 270  1223 HOH HOH H . 
MA 5 HOH 116 271  1245 HOH HOH H . 
MA 5 HOH 117 272  1249 HOH HOH H . 
MA 5 HOH 118 273  1259 HOH HOH H . 
MA 5 HOH 119 274  1261 HOH HOH H . 
MA 5 HOH 120 275  1268 HOH HOH H . 
MA 5 HOH 121 276  1272 HOH HOH H . 
MA 5 HOH 122 277  1284 HOH HOH H . 
MA 5 HOH 123 278  1298 HOH HOH H . 
MA 5 HOH 124 279  1300 HOH HOH H . 
MA 5 HOH 125 280  1302 HOH HOH H . 
MA 5 HOH 126 281  1312 HOH HOH H . 
MA 5 HOH 127 282  1314 HOH HOH H . 
MA 5 HOH 128 283  1322 HOH HOH H . 
MA 5 HOH 129 284  1323 HOH HOH H . 
MA 5 HOH 130 285  1326 HOH HOH H . 
MA 5 HOH 131 286  1338 HOH HOH H . 
MA 5 HOH 132 287  1355 HOH HOH H . 
MA 5 HOH 133 288  1358 HOH HOH H . 
MA 5 HOH 134 289  1371 HOH HOH H . 
MA 5 HOH 135 290  1374 HOH HOH H . 
MA 5 HOH 136 291  1375 HOH HOH H . 
NA 5 HOH 1   156  62   HOH HOH I . 
NA 5 HOH 2   157  96   HOH HOH I . 
NA 5 HOH 3   158  122  HOH HOH I . 
NA 5 HOH 4   159  231  HOH HOH I . 
NA 5 HOH 5   160  256  HOH HOH I . 
NA 5 HOH 6   161  266  HOH HOH I . 
NA 5 HOH 7   162  297  HOH HOH I . 
NA 5 HOH 8   163  309  HOH HOH I . 
NA 5 HOH 9   164  318  HOH HOH I . 
NA 5 HOH 10  165  365  HOH HOH I . 
NA 5 HOH 11  166  394  HOH HOH I . 
NA 5 HOH 12  167  404  HOH HOH I . 
NA 5 HOH 13  168  407  HOH HOH I . 
NA 5 HOH 14  169  421  HOH HOH I . 
NA 5 HOH 15  170  423  HOH HOH I . 
NA 5 HOH 16  171  457  HOH HOH I . 
NA 5 HOH 17  172  472  HOH HOH I . 
NA 5 HOH 18  173  496  HOH HOH I . 
NA 5 HOH 19  174  500  HOH HOH I . 
NA 5 HOH 20  175  501  HOH HOH I . 
NA 5 HOH 21  176  531  HOH HOH I . 
NA 5 HOH 22  177  558  HOH HOH I . 
NA 5 HOH 23  178  574  HOH HOH I . 
NA 5 HOH 24  179  575  HOH HOH I . 
NA 5 HOH 25  180  576  HOH HOH I . 
NA 5 HOH 26  181  582  HOH HOH I . 
NA 5 HOH 27  182  594  HOH HOH I . 
NA 5 HOH 28  183  599  HOH HOH I . 
NA 5 HOH 29  184  603  HOH HOH I . 
NA 5 HOH 30  185  617  HOH HOH I . 
NA 5 HOH 31  186  646  HOH HOH I . 
NA 5 HOH 32  187  656  HOH HOH I . 
NA 5 HOH 33  188  662  HOH HOH I . 
NA 5 HOH 34  189  673  HOH HOH I . 
NA 5 HOH 35  190  691  HOH HOH I . 
NA 5 HOH 36  191  707  HOH HOH I . 
NA 5 HOH 37  192  717  HOH HOH I . 
NA 5 HOH 38  193  747  HOH HOH I . 
NA 5 HOH 39  194  753  HOH HOH I . 
NA 5 HOH 40  195  756  HOH HOH I . 
NA 5 HOH 41  196  757  HOH HOH I . 
NA 5 HOH 42  197  760  HOH HOH I . 
NA 5 HOH 43  198  770  HOH HOH I . 
NA 5 HOH 44  199  774  HOH HOH I . 
NA 5 HOH 45  200  776  HOH HOH I . 
NA 5 HOH 46  201  778  HOH HOH I . 
NA 5 HOH 47  202  785  HOH HOH I . 
NA 5 HOH 48  203  810  HOH HOH I . 
NA 5 HOH 49  204  850  HOH HOH I . 
NA 5 HOH 50  205  860  HOH HOH I . 
NA 5 HOH 51  206  861  HOH HOH I . 
NA 5 HOH 52  207  879  HOH HOH I . 
NA 5 HOH 53  208  883  HOH HOH I . 
NA 5 HOH 54  209  892  HOH HOH I . 
NA 5 HOH 55  210  896  HOH HOH I . 
NA 5 HOH 56  211  898  HOH HOH I . 
NA 5 HOH 57  212  919  HOH HOH I . 
NA 5 HOH 58  213  923  HOH HOH I . 
NA 5 HOH 59  214  939  HOH HOH I . 
NA 5 HOH 60  215  944  HOH HOH I . 
NA 5 HOH 61  216  968  HOH HOH I . 
NA 5 HOH 62  217  996  HOH HOH I . 
NA 5 HOH 63  218  1001 HOH HOH I . 
NA 5 HOH 64  219  1019 HOH HOH I . 
NA 5 HOH 65  220  1027 HOH HOH I . 
NA 5 HOH 66  221  1101 HOH HOH I . 
NA 5 HOH 67  222  1109 HOH HOH I . 
NA 5 HOH 68  223  1143 HOH HOH I . 
NA 5 HOH 69  224  1145 HOH HOH I . 
NA 5 HOH 70  225  1152 HOH HOH I . 
NA 5 HOH 71  226  1173 HOH HOH I . 
NA 5 HOH 72  227  1175 HOH HOH I . 
NA 5 HOH 73  228  1187 HOH HOH I . 
NA 5 HOH 74  229  1212 HOH HOH I . 
NA 5 HOH 75  230  1217 HOH HOH I . 
NA 5 HOH 76  231  1220 HOH HOH I . 
NA 5 HOH 77  232  1226 HOH HOH I . 
NA 5 HOH 78  233  1232 HOH HOH I . 
NA 5 HOH 79  234  1243 HOH HOH I . 
NA 5 HOH 80  235  1262 HOH HOH I . 
NA 5 HOH 81  236  1265 HOH HOH I . 
NA 5 HOH 82  237  1278 HOH HOH I . 
NA 5 HOH 83  238  1281 HOH HOH I . 
NA 5 HOH 84  239  1285 HOH HOH I . 
NA 5 HOH 85  240  1287 HOH HOH I . 
NA 5 HOH 86  241  1308 HOH HOH I . 
NA 5 HOH 87  242  1340 HOH HOH I . 
NA 5 HOH 88  243  1353 HOH HOH I . 
NA 5 HOH 89  244  1367 HOH HOH I . 
NA 5 HOH 90  245  1372 HOH HOH I . 
NA 5 HOH 91  246  1381 HOH HOH I . 
OA 5 HOH 1   156  39   HOH HOH J . 
OA 5 HOH 2   157  55   HOH HOH J . 
OA 5 HOH 3   158  77   HOH HOH J . 
OA 5 HOH 4   159  86   HOH HOH J . 
OA 5 HOH 5   160  116  HOH HOH J . 
OA 5 HOH 6   161  136  HOH HOH J . 
OA 5 HOH 7   162  208  HOH HOH J . 
OA 5 HOH 8   163  224  HOH HOH J . 
OA 5 HOH 9   164  257  HOH HOH J . 
OA 5 HOH 10  165  272  HOH HOH J . 
OA 5 HOH 11  166  280  HOH HOH J . 
OA 5 HOH 12  167  346  HOH HOH J . 
OA 5 HOH 13  168  351  HOH HOH J . 
OA 5 HOH 14  169  352  HOH HOH J . 
OA 5 HOH 15  170  387  HOH HOH J . 
OA 5 HOH 16  171  418  HOH HOH J . 
OA 5 HOH 17  172  452  HOH HOH J . 
OA 5 HOH 18  173  460  HOH HOH J . 
OA 5 HOH 19  174  462  HOH HOH J . 
OA 5 HOH 20  175  474  HOH HOH J . 
OA 5 HOH 21  176  499  HOH HOH J . 
OA 5 HOH 22  177  526  HOH HOH J . 
OA 5 HOH 23  178  528  HOH HOH J . 
OA 5 HOH 24  179  532  HOH HOH J . 
OA 5 HOH 25  180  545  HOH HOH J . 
OA 5 HOH 26  181  548  HOH HOH J . 
OA 5 HOH 27  182  555  HOH HOH J . 
OA 5 HOH 28  183  563  HOH HOH J . 
OA 5 HOH 29  184  587  HOH HOH J . 
OA 5 HOH 30  185  595  HOH HOH J . 
OA 5 HOH 31  186  614  HOH HOH J . 
OA 5 HOH 32  187  615  HOH HOH J . 
OA 5 HOH 33  188  621  HOH HOH J . 
OA 5 HOH 34  189  623  HOH HOH J . 
OA 5 HOH 35  190  626  HOH HOH J . 
OA 5 HOH 36  191  629  HOH HOH J . 
OA 5 HOH 37  192  641  HOH HOH J . 
OA 5 HOH 38  193  657  HOH HOH J . 
OA 5 HOH 39  194  677  HOH HOH J . 
OA 5 HOH 40  195  728  HOH HOH J . 
OA 5 HOH 41  196  737  HOH HOH J . 
OA 5 HOH 42  197  743  HOH HOH J . 
OA 5 HOH 43  198  754  HOH HOH J . 
OA 5 HOH 44  199  755  HOH HOH J . 
OA 5 HOH 45  200  761  HOH HOH J . 
OA 5 HOH 46  201  769  HOH HOH J . 
OA 5 HOH 47  202  782  HOH HOH J . 
OA 5 HOH 48  203  802  HOH HOH J . 
OA 5 HOH 49  204  804  HOH HOH J . 
OA 5 HOH 50  205  805  HOH HOH J . 
OA 5 HOH 51  206  832  HOH HOH J . 
OA 5 HOH 52  207  837  HOH HOH J . 
OA 5 HOH 53  208  856  HOH HOH J . 
OA 5 HOH 54  209  920  HOH HOH J . 
OA 5 HOH 55  210  922  HOH HOH J . 
OA 5 HOH 56  211  930  HOH HOH J . 
OA 5 HOH 57  212  935  HOH HOH J . 
OA 5 HOH 58  213  951  HOH HOH J . 
OA 5 HOH 59  214  967  HOH HOH J . 
OA 5 HOH 60  215  977  HOH HOH J . 
OA 5 HOH 61  216  989  HOH HOH J . 
OA 5 HOH 62  217  999  HOH HOH J . 
OA 5 HOH 63  218  1006 HOH HOH J . 
OA 5 HOH 64  219  1017 HOH HOH J . 
OA 5 HOH 65  220  1025 HOH HOH J . 
OA 5 HOH 66  221  1031 HOH HOH J . 
OA 5 HOH 67  222  1041 HOH HOH J . 
OA 5 HOH 68  223  1042 HOH HOH J . 
OA 5 HOH 69  224  1046 HOH HOH J . 
OA 5 HOH 70  225  1047 HOH HOH J . 
OA 5 HOH 71  226  1052 HOH HOH J . 
OA 5 HOH 72  227  1059 HOH HOH J . 
OA 5 HOH 73  228  1066 HOH HOH J . 
OA 5 HOH 74  229  1070 HOH HOH J . 
OA 5 HOH 75  230  1090 HOH HOH J . 
OA 5 HOH 76  231  1095 HOH HOH J . 
OA 5 HOH 77  232  1105 HOH HOH J . 
OA 5 HOH 78  233  1115 HOH HOH J . 
OA 5 HOH 79  234  1117 HOH HOH J . 
OA 5 HOH 80  235  1130 HOH HOH J . 
OA 5 HOH 81  236  1139 HOH HOH J . 
OA 5 HOH 82  237  1157 HOH HOH J . 
OA 5 HOH 83  238  1158 HOH HOH J . 
OA 5 HOH 84  239  1168 HOH HOH J . 
OA 5 HOH 85  240  1181 HOH HOH J . 
OA 5 HOH 86  241  1208 HOH HOH J . 
OA 5 HOH 87  242  1216 HOH HOH J . 
OA 5 HOH 88  243  1233 HOH HOH J . 
OA 5 HOH 89  244  1238 HOH HOH J . 
OA 5 HOH 90  245  1247 HOH HOH J . 
OA 5 HOH 91  246  1250 HOH HOH J . 
OA 5 HOH 92  247  1254 HOH HOH J . 
OA 5 HOH 93  248  1255 HOH HOH J . 
OA 5 HOH 94  249  1282 HOH HOH J . 
OA 5 HOH 95  250  1289 HOH HOH J . 
OA 5 HOH 96  251  1306 HOH HOH J . 
OA 5 HOH 97  252  1349 HOH HOH J . 
OA 5 HOH 98  253  1361 HOH HOH J . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_defined_assembly              ?    dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,K,L,M,N,FA,GA     
2 1 C,D,O,P,Q,R,S,HA,IA   
3 1 E,F,T,U,V,W,JA,KA     
4 1 G,H,X,Y,Z,AA,LA,MA    
5 1 I,J,BA,CA,DA,EA,NA,OA 
# 
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)' 1570  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  13920 ? 
2 'ABSA (A^2)' 1410  ? 
2 MORE         -11   ? 
2 'SSA (A^2)'  14040 ? 
3 'ABSA (A^2)' 1420  ? 
3 MORE         -10   ? 
3 'SSA (A^2)'  14020 ? 
5 'ABSA (A^2)' 1420  ? 
5 MORE         -11   ? 
5 'SSA (A^2)'  13880 ? 
# 
_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_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 47 ? A HIS 46 ? 1_555 CU ? K  CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 49  ? A HIS 48  ? 1_555 141.4 ? 
2  ND1 ? A HIS 47 ? A HIS 46 ? 1_555 CU ? K  CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 102.2 ? 
3  NE2 ? A HIS 49 ? A HIS 48 ? 1_555 CU ? K  CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 116.3 ? 
4  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? L  ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 72  ? A HIS 71  ? 1_555 107.9 ? 
5  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? L  ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 113.7 ? 
6  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? L  ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 121.2 ? 
7  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? L  ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 84  ? A ASP 83  ? 1_555 101.7 ? 
8  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? L  ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 84  ? A ASP 83  ? 1_555 91.0  ? 
9  ND1 ? A HIS 81 ? A HIS 80 ? 1_555 ZN ? L  ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 84  ? A ASP 83  ? 1_555 117.9 ? 
10 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 CU ? M  CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 49  ? B HIS 48  ? 1_555 140.8 ? 
11 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 CU ? M  CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 99.3  ? 
12 NE2 ? B HIS 49 ? B HIS 48 ? 1_555 CU ? M  CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 119.9 ? 
13 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? N  ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 72  ? B HIS 71  ? 1_555 106.8 ? 
14 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? N  ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 81  ? B HIS 80  ? 1_555 108.8 ? 
15 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? N  ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 81  ? B HIS 80  ? 1_555 122.3 ? 
16 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? N  ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 84  ? B ASP 83  ? 1_555 104.6 ? 
17 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? N  ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 84  ? B ASP 83  ? 1_555 97.0  ? 
18 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 ZN ? N  ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 84  ? B ASP 83  ? 1_555 115.6 ? 
19 ND1 ? C HIS 47 ? C HIS 46 ? 1_555 CU ? O  CU1 . ? C CU1 154 ? 1_555 NE2 ? C HIS 49  ? C HIS 48  ? 1_555 144.8 ? 
20 ND1 ? C HIS 47 ? C HIS 46 ? 1_555 CU ? O  CU1 . ? C CU1 154 ? 1_555 NE2 ? C HIS 64  ? C HIS 63  ? 1_555 72.8  ? 
21 NE2 ? C HIS 49 ? C HIS 48 ? 1_555 CU ? O  CU1 . ? C CU1 154 ? 1_555 NE2 ? C HIS 64  ? C HIS 63  ? 1_555 88.0  ? 
22 ND1 ? C HIS 47 ? C HIS 46 ? 1_555 CU ? O  CU1 . ? C CU1 154 ? 1_555 NE2 ? C HIS 121 ? C HIS 120 ? 1_555 98.1  ? 
23 NE2 ? C HIS 49 ? C HIS 48 ? 1_555 CU ? O  CU1 . ? C CU1 154 ? 1_555 NE2 ? C HIS 121 ? C HIS 120 ? 1_555 116.7 ? 
24 NE2 ? C HIS 64 ? C HIS 63 ? 1_555 CU ? O  CU1 . ? C CU1 154 ? 1_555 NE2 ? C HIS 121 ? C HIS 120 ? 1_555 113.5 ? 
25 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? P  ZN  . ? C ZN  155 ? 1_555 ND1 ? C HIS 72  ? C HIS 71  ? 1_555 101.7 ? 
26 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? P  ZN  . ? C ZN  155 ? 1_555 ND1 ? C HIS 81  ? C HIS 80  ? 1_555 108.0 ? 
27 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 ZN ? P  ZN  . ? C ZN  155 ? 1_555 ND1 ? C HIS 81  ? C HIS 80  ? 1_555 114.7 ? 
28 ND1 ? C HIS 64 ? C HIS 63 ? 1_555 ZN ? P  ZN  . ? C ZN  155 ? 1_555 OD1 ? C ASP 84  ? C ASP 83  ? 1_555 109.8 ? 
29 ND1 ? C HIS 72 ? C HIS 71 ? 1_555 ZN ? P  ZN  . ? C ZN  155 ? 1_555 OD1 ? C ASP 84  ? C ASP 83  ? 1_555 97.9  ? 
30 ND1 ? C HIS 81 ? C HIS 80 ? 1_555 ZN ? P  ZN  . ? C ZN  155 ? 1_555 OD1 ? C ASP 84  ? C ASP 83  ? 1_555 122.6 ? 
31 ND1 ? D HIS 47 ? D HIS 46 ? 1_555 CU ? Q  CU1 . ? D CU1 154 ? 1_555 NE2 ? D HIS 49  ? D HIS 48  ? 1_555 145.7 ? 
32 ND1 ? D HIS 47 ? D HIS 46 ? 1_555 CU ? Q  CU1 . ? D CU1 154 ? 1_555 NE2 ? D HIS 121 ? D HIS 120 ? 1_555 97.2  ? 
33 NE2 ? D HIS 49 ? D HIS 48 ? 1_555 CU ? Q  CU1 . ? D CU1 154 ? 1_555 NE2 ? D HIS 121 ? D HIS 120 ? 1_555 115.9 ? 
34 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? R  ZN  . ? D ZN  155 ? 1_555 ND1 ? D HIS 72  ? D HIS 71  ? 1_555 106.1 ? 
35 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? R  ZN  . ? D ZN  155 ? 1_555 ND1 ? D HIS 81  ? D HIS 80  ? 1_555 109.2 ? 
36 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? R  ZN  . ? D ZN  155 ? 1_555 ND1 ? D HIS 81  ? D HIS 80  ? 1_555 121.8 ? 
37 ND1 ? D HIS 64 ? D HIS 63 ? 1_555 ZN ? R  ZN  . ? D ZN  155 ? 1_555 OD1 ? D ASP 84  ? D ASP 83  ? 1_555 102.1 ? 
38 ND1 ? D HIS 72 ? D HIS 71 ? 1_555 ZN ? R  ZN  . ? D ZN  155 ? 1_555 OD1 ? D ASP 84  ? D ASP 83  ? 1_555 99.8  ? 
39 ND1 ? D HIS 81 ? D HIS 80 ? 1_555 ZN ? R  ZN  . ? D ZN  155 ? 1_555 OD1 ? D ASP 84  ? D ASP 83  ? 1_555 115.8 ? 
40 ND1 ? E HIS 47 ? E HIS 46 ? 1_555 CU ? T  CU1 . ? E CU1 154 ? 1_555 NE2 ? E HIS 49  ? E HIS 48  ? 1_555 142.7 ? 
41 ND1 ? E HIS 47 ? E HIS 46 ? 1_555 CU ? T  CU1 . ? E CU1 154 ? 1_555 NE2 ? E HIS 121 ? E HIS 120 ? 1_555 100.0 ? 
42 NE2 ? E HIS 49 ? E HIS 48 ? 1_555 CU ? T  CU1 . ? E CU1 154 ? 1_555 NE2 ? E HIS 121 ? E HIS 120 ? 1_555 117.2 ? 
43 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? U  ZN  . ? E ZN  155 ? 1_555 ND1 ? E HIS 72  ? E HIS 71  ? 1_555 105.3 ? 
44 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? U  ZN  . ? E ZN  155 ? 1_555 ND1 ? E HIS 81  ? E HIS 80  ? 1_555 112.1 ? 
45 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? U  ZN  . ? E ZN  155 ? 1_555 ND1 ? E HIS 81  ? E HIS 80  ? 1_555 122.1 ? 
46 ND1 ? E HIS 64 ? E HIS 63 ? 1_555 ZN ? U  ZN  . ? E ZN  155 ? 1_555 OD1 ? E ASP 84  ? E ASP 83  ? 1_555 108.0 ? 
47 ND1 ? E HIS 72 ? E HIS 71 ? 1_555 ZN ? U  ZN  . ? E ZN  155 ? 1_555 OD1 ? E ASP 84  ? E ASP 83  ? 1_555 90.9  ? 
48 ND1 ? E HIS 81 ? E HIS 80 ? 1_555 ZN ? U  ZN  . ? E ZN  155 ? 1_555 OD1 ? E ASP 84  ? E ASP 83  ? 1_555 116.0 ? 
49 ND1 ? F HIS 47 ? F HIS 46 ? 1_555 CU ? V  CU1 . ? F CU1 154 ? 1_555 NE2 ? F HIS 49  ? F HIS 48  ? 1_555 143.8 ? 
50 ND1 ? F HIS 47 ? F HIS 46 ? 1_555 CU ? V  CU1 . ? F CU1 154 ? 1_555 NE2 ? F HIS 121 ? F HIS 120 ? 1_555 97.3  ? 
51 NE2 ? F HIS 49 ? F HIS 48 ? 1_555 CU ? V  CU1 . ? F CU1 154 ? 1_555 NE2 ? F HIS 121 ? F HIS 120 ? 1_555 118.8 ? 
52 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? W  ZN  . ? F ZN  155 ? 1_555 ND1 ? F HIS 72  ? F HIS 71  ? 1_555 104.2 ? 
53 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? W  ZN  . ? F ZN  155 ? 1_555 ND1 ? F HIS 81  ? F HIS 80  ? 1_555 109.2 ? 
54 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? W  ZN  . ? F ZN  155 ? 1_555 ND1 ? F HIS 81  ? F HIS 80  ? 1_555 123.0 ? 
55 ND1 ? F HIS 64 ? F HIS 63 ? 1_555 ZN ? W  ZN  . ? F ZN  155 ? 1_555 OD1 ? F ASP 84  ? F ASP 83  ? 1_555 103.6 ? 
56 ND1 ? F HIS 72 ? F HIS 71 ? 1_555 ZN ? W  ZN  . ? F ZN  155 ? 1_555 OD1 ? F ASP 84  ? F ASP 83  ? 1_555 94.9  ? 
57 ND1 ? F HIS 81 ? F HIS 80 ? 1_555 ZN ? W  ZN  . ? F ZN  155 ? 1_555 OD1 ? F ASP 84  ? F ASP 83  ? 1_555 119.4 ? 
58 ND1 ? G HIS 47 ? G HIS 46 ? 1_555 CU ? X  CU1 . ? G CU1 154 ? 1_555 NE2 ? G HIS 49  ? G HIS 48  ? 1_555 145.7 ? 
59 ND1 ? G HIS 47 ? G HIS 46 ? 1_555 CU ? X  CU1 . ? G CU1 154 ? 1_555 NE2 ? G HIS 121 ? G HIS 120 ? 1_555 97.8  ? 
60 NE2 ? G HIS 49 ? G HIS 48 ? 1_555 CU ? X  CU1 . ? G CU1 154 ? 1_555 NE2 ? G HIS 121 ? G HIS 120 ? 1_555 116.0 ? 
61 ND1 ? G HIS 64 ? G HIS 63 ? 1_555 ZN ? Y  ZN  . ? G ZN  155 ? 1_555 ND1 ? G HIS 72  ? G HIS 71  ? 1_555 100.7 ? 
62 ND1 ? G HIS 64 ? G HIS 63 ? 1_555 ZN ? Y  ZN  . ? G ZN  155 ? 1_555 ND1 ? G HIS 81  ? G HIS 80  ? 1_555 110.4 ? 
63 ND1 ? G HIS 72 ? G HIS 71 ? 1_555 ZN ? Y  ZN  . ? G ZN  155 ? 1_555 ND1 ? G HIS 81  ? G HIS 80  ? 1_555 125.8 ? 
64 ND1 ? G HIS 64 ? G HIS 63 ? 1_555 ZN ? Y  ZN  . ? G ZN  155 ? 1_555 OD1 ? G ASP 84  ? G ASP 83  ? 1_555 105.8 ? 
65 ND1 ? G HIS 72 ? G HIS 71 ? 1_555 ZN ? Y  ZN  . ? G ZN  155 ? 1_555 OD1 ? G ASP 84  ? G ASP 83  ? 1_555 87.1  ? 
66 ND1 ? G HIS 81 ? G HIS 80 ? 1_555 ZN ? Y  ZN  . ? G ZN  155 ? 1_555 OD1 ? G ASP 84  ? G ASP 83  ? 1_555 123.1 ? 
67 ND1 ? H HIS 47 ? H HIS 46 ? 1_555 CU ? Z  CU1 . ? H CU1 154 ? 1_555 NE2 ? H HIS 49  ? H HIS 48  ? 1_555 142.6 ? 
68 ND1 ? H HIS 47 ? H HIS 46 ? 1_555 CU ? Z  CU1 . ? H CU1 154 ? 1_555 NE2 ? H HIS 121 ? H HIS 120 ? 1_555 96.7  ? 
69 NE2 ? H HIS 49 ? H HIS 48 ? 1_555 CU ? Z  CU1 . ? H CU1 154 ? 1_555 NE2 ? H HIS 121 ? H HIS 120 ? 1_555 120.4 ? 
70 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? AA ZN  . ? H ZN  155 ? 1_555 ND1 ? H HIS 72  ? H HIS 71  ? 1_555 102.9 ? 
71 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? AA ZN  . ? H ZN  155 ? 1_555 ND1 ? H HIS 81  ? H HIS 80  ? 1_555 102.0 ? 
72 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 ZN ? AA ZN  . ? H ZN  155 ? 1_555 ND1 ? H HIS 81  ? H HIS 80  ? 1_555 127.8 ? 
73 ND1 ? H HIS 64 ? H HIS 63 ? 1_555 ZN ? AA ZN  . ? H ZN  155 ? 1_555 OD1 ? H ASP 84  ? H ASP 83  ? 1_555 108.7 ? 
74 ND1 ? H HIS 72 ? H HIS 71 ? 1_555 ZN ? AA ZN  . ? H ZN  155 ? 1_555 OD1 ? H ASP 84  ? H ASP 83  ? 1_555 100.0 ? 
75 ND1 ? H HIS 81 ? H HIS 80 ? 1_555 ZN ? AA ZN  . ? H ZN  155 ? 1_555 OD1 ? H ASP 84  ? H ASP 83  ? 1_555 114.2 ? 
76 ND1 ? I HIS 47 ? I HIS 46 ? 1_555 CU ? BA CU1 . ? I CU1 154 ? 1_555 NE2 ? I HIS 49  ? I HIS 48  ? 1_555 140.7 ? 
77 ND1 ? I HIS 47 ? I HIS 46 ? 1_555 CU ? BA CU1 . ? I CU1 154 ? 1_555 NE2 ? I HIS 121 ? I HIS 120 ? 1_555 100.3 ? 
78 NE2 ? I HIS 49 ? I HIS 48 ? 1_555 CU ? BA CU1 . ? I CU1 154 ? 1_555 NE2 ? I HIS 121 ? I HIS 120 ? 1_555 118.8 ? 
79 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? CA ZN  . ? I ZN  155 ? 1_555 ND1 ? I HIS 72  ? I HIS 71  ? 1_555 112.5 ? 
80 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? CA ZN  . ? I ZN  155 ? 1_555 ND1 ? I HIS 81  ? I HIS 80  ? 1_555 105.2 ? 
81 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? CA ZN  . ? I ZN  155 ? 1_555 ND1 ? I HIS 81  ? I HIS 80  ? 1_555 122.7 ? 
82 ND1 ? I HIS 64 ? I HIS 63 ? 1_555 ZN ? CA ZN  . ? I ZN  155 ? 1_555 OD1 ? I ASP 84  ? I ASP 83  ? 1_555 109.5 ? 
83 ND1 ? I HIS 72 ? I HIS 71 ? 1_555 ZN ? CA ZN  . ? I ZN  155 ? 1_555 OD1 ? I ASP 84  ? I ASP 83  ? 1_555 98.5  ? 
84 ND1 ? I HIS 81 ? I HIS 80 ? 1_555 ZN ? CA ZN  . ? I ZN  155 ? 1_555 OD1 ? I ASP 84  ? I ASP 83  ? 1_555 107.7 ? 
85 ND1 ? J HIS 47 ? J HIS 46 ? 1_555 CU ? DA CU1 . ? J CU1 154 ? 1_555 NE2 ? J HIS 49  ? J HIS 48  ? 1_555 148.6 ? 
86 ND1 ? J HIS 47 ? J HIS 46 ? 1_555 CU ? DA CU1 . ? J CU1 154 ? 1_555 NE2 ? J HIS 121 ? J HIS 120 ? 1_555 92.3  ? 
87 NE2 ? J HIS 49 ? J HIS 48 ? 1_555 CU ? DA CU1 . ? J CU1 154 ? 1_555 NE2 ? J HIS 121 ? J HIS 120 ? 1_555 118.9 ? 
88 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? EA ZN  . ? J ZN  155 ? 1_555 ND1 ? J HIS 72  ? J HIS 71  ? 1_555 106.5 ? 
89 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? EA ZN  . ? J ZN  155 ? 1_555 ND1 ? J HIS 81  ? J HIS 80  ? 1_555 109.1 ? 
90 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? EA ZN  . ? J ZN  155 ? 1_555 ND1 ? J HIS 81  ? J HIS 80  ? 1_555 119.3 ? 
91 ND1 ? J HIS 64 ? J HIS 63 ? 1_555 ZN ? EA ZN  . ? J ZN  155 ? 1_555 OD1 ? J ASP 84  ? J ASP 83  ? 1_555 104.9 ? 
92 ND1 ? J HIS 72 ? J HIS 71 ? 1_555 ZN ? EA ZN  . ? J ZN  155 ? 1_555 OD1 ? J ASP 84  ? J ASP 83  ? 1_555 96.7  ? 
93 ND1 ? J HIS 81 ? J HIS 80 ? 1_555 ZN ? EA ZN  . ? J ZN  155 ? 1_555 OD1 ? J ASP 84  ? J ASP 83  ? 1_555 118.6 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2002-11-27 
2 'Structure model' 1 1 2008-04-28 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-10-27 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Database references'       
4 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' database_2             
2 4 'Structure model' pdbx_struct_conn_angle 
3 4 'Structure model' struct_conn            
4 4 'Structure model' struct_ref_seq_dif     
5 4 'Structure model' struct_site            
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_database_2.pdbx_DOI'                        
2  4 'Structure model' '_database_2.pdbx_database_accession'         
3  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
13 4 'Structure model' '_pdbx_struct_conn_angle.value'               
14 4 'Structure model' '_struct_conn.pdbx_dist_value'                
15 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
16 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
17 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
18 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
19 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
20 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
21 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
22 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
23 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
24 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
25 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
26 4 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
27 4 'Structure model' '_struct_ref_seq_dif.details'                 
28 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
29 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
30 4 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' . ? 1 
SCALEPACK 'data scaling'   . ? 2 
CNS       refinement       . ? 3 
CNS       phasing          . ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 C ASP 76  ? ? O C HOH 243 ? ? 2.07 
2 1 O   A HOH 213 ? ? O A HOH 284 ? ? 2.16 
# 
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 O  D HOH 1567 ? ? 1_555 O D HOH 1567 ? ? 4_555 1.44 
2 1 NZ F LYS 36   ? ? 1_555 O G ASP 92   ? ? 3_655 2.10 
# 
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 SER B 25  ? ? -43.96  -0.92  
2 1 ASN B 26  ? ? -147.05 -16.35 
3 1 THR E 2   ? ? -147.92 -36.97 
4 1 ASP E 109 ? ? -37.56  -35.82 
5 1 LYS E 136 ? ? -120.11 -56.52 
6 1 SER G 98  ? ? -160.54 94.78  
7 1 ALA I 55  ? ? -115.98 66.32  
8 1 LEU I 126 ? ? 59.82   19.51  
# 
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 0 A ALA 1   ? N   ? A ALA 2   N   
2   1 Y 0 A ALA 1   ? CA  ? A ALA 2   CA  
3   1 Y 0 A ALA 1   ? CB  ? A ALA 2   CB  
4   1 Y 0 A LYS 9   ? CD  ? A LYS 10  CD  
5   1 Y 0 A LYS 91  ? CE  ? A LYS 92  CE  
6   1 Y 0 A LYS 91  ? NZ  ? A LYS 92  NZ  
7   1 Y 0 A GLU 132 ? CD  ? A GLU 133 CD  
8   1 Y 0 A GLU 132 ? OE1 ? A GLU 133 OE1 
9   1 Y 0 A GLU 132 ? OE2 ? A GLU 133 OE2 
10  1 Y 0 A LYS 136 ? CD  ? A LYS 137 CD  
11  1 Y 0 B ALA 1   ? N   ? B ALA 2   N   
12  1 Y 0 B ALA 1   ? CA  ? B ALA 2   CA  
13  1 Y 0 B ALA 1   ? CB  ? B ALA 2   CB  
14  1 Y 0 B LYS 23  ? NZ  ? B LYS 24  NZ  
15  1 Y 0 B LYS 91  ? NZ  ? B LYS 92  NZ  
16  1 Y 0 C ALA 1   ? N   ? C ALA 2   N   
17  1 Y 0 C ALA 1   ? CA  ? C ALA 2   CA  
18  1 Y 0 C ALA 1   ? CB  ? C ALA 2   CB  
19  1 Y 0 C LYS 23  ? CD  ? C LYS 24  CD  
20  1 Y 0 C LYS 23  ? CE  ? C LYS 24  CE  
21  1 Y 0 C LYS 23  ? NZ  ? C LYS 24  NZ  
22  1 Y 0 C LYS 30  ? CD  ? C LYS 31  CD  
23  1 Y 0 C LYS 36  ? CD  ? C LYS 37  CD  
24  1 Y 0 C ARG 69  ? CB  ? C ARG 70  CB  
25  1 Y 0 C ARG 69  ? CG  ? C ARG 70  CG  
26  1 Y 0 C ASP 76  ? CG  ? C ASP 77  CG  
27  1 Y 0 C ASP 76  ? OD1 ? C ASP 77  OD1 
28  1 Y 0 C ASP 76  ? OD2 ? C ASP 77  OD2 
29  1 Y 0 C ARG 79  ? CB  ? C ARG 80  CB  
30  1 Y 0 C LYS 91  ? CD  ? C LYS 92  CD  
31  1 Y 0 C LYS 91  ? CE  ? C LYS 92  CE  
32  1 Y 0 C LYS 91  ? NZ  ? C LYS 92  NZ  
33  1 Y 0 C LYS 122 ? CE  ? C LYS 123 CE  
34  1 Y 0 C LYS 122 ? NZ  ? C LYS 123 NZ  
35  1 Y 0 C LYS 136 ? CE  ? C LYS 137 CE  
36  1 Y 0 C LYS 136 ? NZ  ? C LYS 137 NZ  
37  1 Y 0 D ALA 1   ? N   ? D ALA 2   N   
38  1 Y 0 D ALA 1   ? CA  ? D ALA 2   CA  
39  1 Y 0 D ALA 1   ? CB  ? D ALA 2   CB  
40  1 Y 0 D LYS 23  ? CD  ? D LYS 24  CD  
41  1 Y 0 D LYS 23  ? CE  ? D LYS 24  CE  
42  1 Y 0 D LYS 23  ? NZ  ? D LYS 24  NZ  
43  1 Y 0 D LYS 36  ? NZ  ? D LYS 37  NZ  
44  1 Y 0 D LYS 70  ? CE  ? D LYS 71  CE  
45  1 Y 0 D LYS 70  ? NZ  ? D LYS 71  NZ  
46  1 Y 0 D LYS 136 ? CE  ? D LYS 137 CE  
47  1 Y 0 D LYS 136 ? NZ  ? D LYS 137 NZ  
48  1 Y 0 E ALA 1   ? N   ? E ALA 2   N   
49  1 Y 0 E ALA 1   ? CA  ? E ALA 2   CA  
50  1 Y 0 E ALA 1   ? CB  ? E ALA 2   CB  
51  1 Y 0 E LYS 3   ? NZ  ? E LYS 4   NZ  
52  1 Y 0 E LYS 23  ? CG  ? E LYS 24  CG  
53  1 Y 0 E LYS 23  ? CD  ? E LYS 24  CD  
54  1 Y 0 E LYS 23  ? CE  ? E LYS 24  CE  
55  1 Y 0 E LYS 91  ? NZ  ? E LYS 92  NZ  
56  1 Y 0 E LYS 136 ? CE  ? E LYS 137 CE  
57  1 Y 0 F ALA 1   ? N   ? F ALA 2   N   
58  1 Y 0 F ALA 1   ? CA  ? F ALA 2   CA  
59  1 Y 0 F ALA 1   ? CB  ? F ALA 2   CB  
60  1 Y 0 F LYS 36  ? NZ  ? F LYS 37  NZ  
61  1 Y 0 F LYS 70  ? NZ  ? F LYS 71  NZ  
62  1 Y 0 F GLU 77  ? CD  ? F GLU 78  CD  
63  1 Y 0 F GLU 77  ? OE1 ? F GLU 78  OE1 
64  1 Y 0 F GLU 77  ? OE2 ? F GLU 78  OE2 
65  1 Y 0 G ALA 1   ? N   ? G ALA 2   N   
66  1 Y 0 G ALA 1   ? CA  ? G ALA 2   CA  
67  1 Y 0 G ALA 1   ? CB  ? G ALA 2   CB  
68  1 Y 0 G LYS 3   ? CD  ? G LYS 4   CD  
69  1 Y 0 G LYS 23  ? CB  ? G LYS 24  CB  
70  1 Y 0 G LYS 23  ? CG  ? G LYS 24  CG  
71  1 Y 0 G LYS 23  ? CD  ? G LYS 24  CD  
72  1 Y 0 G LYS 23  ? CE  ? G LYS 24  CE  
73  1 Y 0 G LYS 23  ? NZ  ? G LYS 24  NZ  
74  1 Y 0 G GLU 24  ? CD  ? G GLU 25  CD  
75  1 Y 0 G GLU 24  ? OE1 ? G GLU 25  OE1 
76  1 Y 0 G GLU 24  ? OE2 ? G GLU 25  OE2 
77  1 Y 0 G ASN 26  ? CB  ? G ASN 27  CB  
78  1 Y 0 G LYS 30  ? CD  ? G LYS 31  CD  
79  1 Y 0 G LYS 30  ? CE  ? G LYS 31  CE  
80  1 Y 0 G ASN 65  ? CA  ? G ASN 66  CA  
81  1 Y 0 G ASN 65  ? CB  ? G ASN 66  CB  
82  1 Y 0 G LEU 67  ? CG  ? G LEU 68  CG  
83  1 Y 0 G LEU 67  ? CD1 ? G LEU 68  CD1 
84  1 Y 0 G LEU 67  ? CD2 ? G LEU 68  CD2 
85  1 Y 0 G LYS 75  ? CD  ? G LYS 76  CD  
86  1 Y 0 G GLU 77  ? CB  ? G GLU 78  CB  
87  1 Y 0 G GLU 77  ? CG  ? G GLU 78  CG  
88  1 Y 0 G GLU 77  ? CD  ? G GLU 78  CD  
89  1 Y 0 G GLU 77  ? OE1 ? G GLU 78  OE1 
90  1 Y 0 G GLU 77  ? OE2 ? G GLU 78  OE2 
91  1 Y 0 G LYS 91  ? CG  ? G LYS 92  CG  
92  1 Y 0 G LYS 91  ? CE  ? G LYS 92  CE  
93  1 Y 0 G LYS 91  ? NZ  ? G LYS 92  NZ  
94  1 Y 0 G SER 98  ? OG  ? G SER 99  OG  
95  1 Y 0 G LYS 122 ? CE  ? G LYS 123 CE  
96  1 Y 0 G LYS 122 ? NZ  ? G LYS 123 NZ  
97  1 Y 0 G GLU 132 ? CD  ? G GLU 133 CD  
98  1 Y 0 G GLU 132 ? OE1 ? G GLU 133 OE1 
99  1 Y 0 G GLU 132 ? OE2 ? G GLU 133 OE2 
100 1 Y 0 H LYS 9   ? CE  ? H LYS 10  CE  
101 1 Y 0 H LYS 23  ? CE  ? H LYS 24  CE  
102 1 Y 0 H LYS 23  ? NZ  ? H LYS 24  NZ  
103 1 Y 0 H LYS 91  ? CD  ? H LYS 92  CD  
104 1 Y 0 H LYS 91  ? CE  ? H LYS 92  CE  
105 1 Y 0 H ASP 109 ? CB  ? H ASP 110 CB  
106 1 Y 0 H ASP 109 ? CG  ? H ASP 110 CG  
107 1 Y 0 H ASP 109 ? OD1 ? H ASP 110 OD1 
108 1 Y 0 H LYS 122 ? CE  ? H LYS 123 CE  
109 1 Y 0 H LYS 122 ? NZ  ? H LYS 123 NZ  
110 1 Y 0 I ALA 1   ? N   ? I ALA 2   N   
111 1 Y 0 I ALA 1   ? CA  ? I ALA 2   CA  
112 1 Y 0 I ALA 1   ? CB  ? I ALA 2   CB  
113 1 Y 0 I LYS 9   ? CD  ? I LYS 10  CD  
114 1 Y 0 I ASN 26  ? CB  ? I ASN 27  CB  
115 1 Y 0 I ASN 26  ? CG  ? I ASN 27  CG  
116 1 Y 0 I ASN 26  ? OD1 ? I ASN 27  OD1 
117 1 Y 0 I ASN 26  ? ND2 ? I ASN 27  ND2 
118 1 Y 0 I LYS 70  ? CD  ? I LYS 71  CD  
119 1 Y 0 I GLU 77  ? CG  ? I GLU 78  CG  
120 1 Y 0 I LYS 91  ? CD  ? I LYS 92  CD  
121 1 Y 0 I LYS 91  ? CE  ? I LYS 92  CE  
122 1 Y 0 I LYS 91  ? NZ  ? I LYS 92  NZ  
123 1 Y 0 J ALA 1   ? N   ? J ALA 2   N   
124 1 Y 0 J ALA 1   ? CA  ? J ALA 2   CA  
125 1 Y 0 J ALA 1   ? CB  ? J ALA 2   CB  
126 1 Y 0 J LYS 9   ? CE  ? J LYS 10  CE  
127 1 Y 0 J LYS 23  ? CE  ? J LYS 24  CE  
128 1 Y 0 J LYS 23  ? NZ  ? J LYS 24  NZ  
129 1 Y 0 J GLU 24  ? CG  ? J GLU 25  CG  
130 1 Y 0 J GLU 24  ? CD  ? J GLU 25  CD  
131 1 Y 0 J GLU 24  ? OE1 ? J GLU 25  OE1 
132 1 Y 0 J GLU 24  ? OE2 ? J GLU 25  OE2 
133 1 Y 0 J SER 25  ? O   ? J SER 26  O   
134 1 Y 0 J SER 25  ? OG  ? J SER 26  OG  
135 1 Y 0 J ASN 26  ? CB  ? J ASN 27  CB  
136 1 Y 0 J ASN 26  ? CG  ? J ASN 27  CG  
137 1 Y 0 J ASN 26  ? OD1 ? J ASN 27  OD1 
138 1 Y 0 J ASN 26  ? ND2 ? J ASN 27  ND2 
139 1 Y 0 J LYS 36  ? NZ  ? J LYS 37  NZ  
140 1 Y 0 J LYS 70  ? CD  ? J LYS 71  CD  
141 1 Y 0 J LYS 75  ? CD  ? J LYS 76  CD  
142 1 Y 0 J LYS 75  ? CE  ? J LYS 76  CE  
143 1 Y 0 J LYS 75  ? NZ  ? J LYS 76  NZ  
144 1 Y 0 J ASP 109 ? CB  ? J ASP 110 CB  
145 1 Y 0 J GLU 132 ? CG  ? J GLU 133 CG  
146 1 Y 0 J LYS 136 ? CE  ? J LYS 137 CE  
# 
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 MET 0 ? A MET 1 
2  1 Y 1 B MET 0 ? B MET 1 
3  1 Y 1 C MET 0 ? C MET 1 
4  1 Y 1 D MET 0 ? D MET 1 
5  1 Y 1 E MET 0 ? E MET 1 
6  1 Y 1 F MET 0 ? F MET 1 
7  1 Y 1 G MET 0 ? G MET 1 
8  1 Y 1 H MET 0 ? H MET 1 
9  1 Y 1 I MET 0 ? I MET 1 
10 1 Y 1 J MET 0 ? J MET 1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (I) ION' CU1 
3 'ZINC ION'       ZN  
4 'SULFATE ION'    SO4 
5 water            HOH 
# 
