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三分钟玩转PDB与Pubchem数据库的API链接
liyq@dp.tech
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三分钟玩转PDB与Pubchem数据库的API链接
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作者：李亚奇 liyq@dp.tech
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你有没有过如下烦恼？
——在研究课题中需要下载一系列的PDB结构，数量太多了用鼠标点击太麻烦。
——已知某分子的smiles，想搜索相似结构并下载下来，但是数量太多了下载不下来。
——……
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阅读完本notebook，你就能掌握“偷懒”的办法，让你的鼠标愉快的摸鱼
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PDB数据库相关连接
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双击即可修改
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PDB数据库的结构相关链接可以分为：
https://files.rcsb.org/download/ PDB ID(-assembly<可选>).(文件格式)
根据任务需求，获取PDB结构可能为pdb文件格式或者mmcif文件格式。
此时，只需要将文件格式部分指定为.pdb或者.cif即可
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因此，定义一个pyhon函数get_structure，这个函数有三个输入参数 ID, all_assembly, str_format:
ID: 即指定需要下载的PDB ID
all_assembly: <True/False> 指定是否需要下载所有的assembly部分, True: 下载所有的assembly, False: 仅下载assembly-1部分
str_format: 指定需要下载的文件格式，pdb或cif
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[28]
import os
import requests
import urllib.request
def get_structure(ID, all_assembly=True, str_format='pdb'):
pdb_id = ID
dir_name = ID
work_path = f"./{dir_name}"
print(f'>>>download {pdb_id} from RCSB')
if str_format == 'cif':
if all_assembly:
assembly_id = 1
while True:
url = f'https://files.rcsb.org/download/{pdb_id}-assembly{assembly_id}.cif'
response = requests.get(url)
if response.status_code == 200:
assembly_folder = os.path.join(work_path, f'assembly_{assembly_id}')
if not os.path.exists(assembly_folder):
os.makedirs(assembly_folder)
print(f'Downloaded biological assembly-{assembly_id}')
urllib.request.urlretrieve(url, os.path.join(assembly_folder, f'{pdb_id}.cif'))
assembly_id += 1
elif response.status_code == 404:
if assembly_id == 1:
print(f'No biological assembly-{assembly_id} found for {pdb_id}')
break
else:
print(f'Warning: {response.status_code} for {pdb_id} assembly-{assembly_id}')
break
else:
if not os.path.exists(work_path):
os.makedirs(work_path)
cif_file = os.path.join(work_path,f'{pdb_id}.cif')
url = f'https://files.rcsb.org/download/{pdb_id}.cif'
urllib.request.urlretrieve(url, cif_file)
elif str_format == 'pdb':
if all_assembly:
assembly_id = 1
while True:
url = f'https://files.rcsb.org/download/{pdb_id}.pdb{assembly_id}'
response = requests.get(url)
if response.status_code == 200:
assembly_folder = os.path.join(work_path, f'assembly_{assembly_id}')
if not os.path.exists(assembly_folder):
os.makedirs(assembly_folder)
print(f'Downloaded biological assembly-{assembly_id}')
urllib.request.urlretrieve(url, os.path.join(assembly_folder, f'{pdb_id}.pdb'))
assembly_id += 1
elif response.status_code == 404:
if assembly_id == 1:
print(f'No biological assembly-{assembly_id} found for {pdb_id}')
break
else:
print(f'Warning: {response.status_code} for {pdb_id} assembly-{assembly_id}')
break
else:
if not os.path.exists(work_path):
os.makedirs(work_path)
pdb_file = os.path.join(work_path,f'{pdb_id}.pdb')
url = f'https://files.rcsb.org/download/{pdb_id}.pdb'
urllib.request.urlretrieve(url, pdb_file)
print('>>>Done')
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根据上述函数，假如需要下载 10gs 结构的pdb文件我们只需要运行如下代码：
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[30]
get_structure(ID='10gs', all_assembly= False, str_format= 'pdb')
>>>download 10gs from RCSB >>>Done
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[24]
!cat 10gs/10gs.pdb
HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-AUG-97 10GS TITLE HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE P1-1; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: GSTP1-1; COMPND 5 EC: 2.5.1.18; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 ORGAN: PLACENTA; SOURCE 6 CELLULAR_LOCATION: CYTOPLASM; SOURCE 7 GENE: GTP_HUMAN; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DETOXIFYING ENZYME, TER117, TLK117, RP298, TELINTRA, EZATIOSTAT HCL, KEYWDS 2 MYELODYSPLASTIC SYNDROME, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.OAKLEY,M.PARKER REVDAT 6 02-AUG-23 10GS 1 REMARK REVDAT 5 13-FEB-13 10GS 1 KEYWDS REVDAT 4 13-JUL-11 10GS 1 VERSN REVDAT 3 24-FEB-09 10GS 1 VERSN REVDAT 2 01-APR-03 10GS 1 JRNL REVDAT 1 16-SEP-98 10GS 0 JRNL AUTH A.J.OAKLEY,M.L.BELLO,A.BATTISTONI,G.RICCI,J.ROSSJOHN, JRNL AUTH 2 H.O.VILLAR,M.W.PARKER JRNL TITL THE STRUCTURES OF HUMAN GLUTATHIONE TRANSFERASE P1-1 IN JRNL TITL 2 COMPLEX WITH GLUTATHIONE AND VARIOUS INHIBITORS AT HIGH JRNL TITL 3 RESOLUTION. JRNL REF J.MOL.BIOL. V. 274 84 1997 JRNL REFN ISSN 0022-2836 JRNL PMID 9398518 JRNL DOI 10.1006/JMBI.1997.1364 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.REINEMER,H.W.DIRR,R.LADENSTEIN,R.HUBER,M.LO BELLO, REMARK 1 AUTH 2 G.FEDERICI,M.W.PARKER REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE REMARK 1 TITL 2 S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH REMARK 1 TITL 3 S-HEXYLGLUTATHIONE AT 2.8 A RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 227 214 1992 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.2 REMARK 3 NUMBER OF REFLECTIONS : 18704 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.176 REMARK 3 FREE R VALUE : 0.214 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.380 REMARK 3 FREE R VALUE TEST SET COUNT : 949 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.40 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2401 REMARK 3 BIN R VALUE (WORKING SET) : 0.2329 REMARK 3 BIN FREE R VALUE : 0.2945 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.75 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 116 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3262 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 169 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.300 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.100 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 10GS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000170026. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-APR-96 REMARK 200 TEMPERATURE (KELVIN) : 288 REMARK 200 PH : 5.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE(002) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27006 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 83.0 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07900 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.17800 REMARK 200 <I/SIGMA(I)> FOR SHELL : 17.80 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: PDB ENTRY 1GSS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.8 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 39.86150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.23000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.86150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.23000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4410 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO A 1 REMARK 465 PRO B 1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 64 111.49 76.75 REMARK 500 ASN A 110 67.97 -155.80 REMARK 500 THR A 141 -115.50 -113.73 REMARK 500 GLN B 64 111.19 76.76 REMARK 500 ASN B 110 68.01 -155.72 REMARK 500 THR B 141 -115.38 -113.63 REMARK 500 REMARK 500 REMARK: NULL REMARK 630 REMARK 630 MOLECULE TYPE: NULL REMARK 630 MOLECULE NAME: L-GAMMA-GLUTAMYL-S-BENZYL-N-[(S)-CARBOXY(PHENYL) REMARK 630 METHYL]-L-CYSTEINAMIDE REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 630 REMARK 630 M RES C SSSEQI REMARK 630 VWW A 210 REMARK 630 VWW B 210 REMARK 630 SOURCE: NULL REMARK 630 TAXONOMY: NULL REMARK 630 SUBCOMP: GGL BCS PG9 REMARK 630 DETAILS: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VWW A 210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VWW B 210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 211 DBREF 10GS A 1 209 UNP P09211 GTP_HUMAN 1 209 DBREF 10GS B 1 209 UNP P09211 GTP_HUMAN 1 209 SEQRES 1 A 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG SEQRES 2 A 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN SEQRES 3 A 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN SEQRES 4 A 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU SEQRES 5 A 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER SEQRES 6 A 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU SEQRES 7 A 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET SEQRES 8 A 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE SEQRES 9 A 209 SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP SEQRES 10 A 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU SEQRES 11 A 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE SEQRES 12 A 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU SEQRES 13 A 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS SEQRES 14 A 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG SEQRES 15 A 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER SEQRES 16 A 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS SEQRES 17 A 209 GLN SEQRES 1 B 209 PRO PRO TYR THR VAL VAL TYR PHE PRO VAL ARG GLY ARG SEQRES 2 B 209 CYS ALA ALA LEU ARG MET LEU LEU ALA ASP GLN GLY GLN SEQRES 3 B 209 SER TRP LYS GLU GLU VAL VAL THR VAL GLU THR TRP GLN SEQRES 4 B 209 GLU GLY SER LEU LYS ALA SER CYS LEU TYR GLY GLN LEU SEQRES 5 B 209 PRO LYS PHE GLN ASP GLY ASP LEU THR LEU TYR GLN SER SEQRES 6 B 209 ASN THR ILE LEU ARG HIS LEU GLY ARG THR LEU GLY LEU SEQRES 7 B 209 TYR GLY LYS ASP GLN GLN GLU ALA ALA LEU VAL ASP MET SEQRES 8 B 209 VAL ASN ASP GLY VAL GLU ASP LEU ARG CYS LYS TYR ILE SEQRES 9 B 209 SER LEU ILE TYR THR ASN TYR GLU ALA GLY LYS ASP ASP SEQRES 10 B 209 TYR VAL LYS ALA LEU PRO GLY GLN LEU LYS PRO PHE GLU SEQRES 11 B 209 THR LEU LEU SER GLN ASN GLN GLY GLY LYS THR PHE ILE SEQRES 12 B 209 VAL GLY ASP GLN ILE SER PHE ALA ASP TYR ASN LEU LEU SEQRES 13 B 209 ASP LEU LEU LEU ILE HIS GLU VAL LEU ALA PRO GLY CYS SEQRES 14 B 209 LEU ASP ALA PHE PRO LEU LEU SER ALA TYR VAL GLY ARG SEQRES 15 B 209 LEU SER ALA ARG PRO LYS LEU LYS ALA PHE LEU ALA SER SEQRES 16 B 209 PRO GLU TYR VAL ASN LEU PRO ILE ASN GLY ASN GLY LYS SEQRES 17 B 209 GLN HET VWW A 210 33 HET MES A 211 12 HET VWW B 210 33 HET MES B 211 12 HETNAM VWW L-GAMMA-GLUTAMYL-S-BENZYL-N-[(S)-CARBOXY(PHENYL) HETNAM 2 VWW METHYL]-L-CYSTEINAMIDE HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID FORMUL 3 VWW 2(C23 H27 N3 O6 S) FORMUL 4 MES 2(C6 H13 N O4 S) FORMUL 7 HOH *169(H2 O) HELIX 1 1 GLY A 12 ASP A 23 5 12 HELIX 2 2 VAL A 35 GLU A 40 1 6 HELIX 3 3 SER A 42 SER A 46 1 5 HELIX 4 4 SER A 65 LEU A 76 1 12 HELIX 5 5 GLN A 83 THR A 109 1 27 HELIX 6 6 TYR A 111 SER A 134 1 24 HELIX 7 7 GLN A 137 GLY A 139 5 3 HELIX 8 8 PHE A 150 LEU A 165 1 16 HELIX 9 9 PRO A 174 ALA A 185 1 12 HELIX 10 10 PRO A 187 ALA A 194 1 8 HELIX 11 11 PRO A 196 VAL A 199 1 4 HELIX 12 12 GLY B 12 ASP B 23 5 12 HELIX 13 13 VAL B 35 GLU B 40 1 6 HELIX 14 14 SER B 42 SER B 46 1 5 HELIX 15 15 SER B 65 LEU B 76 1 12 HELIX 16 16 GLN B 83 THR B 109 1 27 HELIX 17 17 TYR B 111 SER B 134 1 24 HELIX 18 18 GLN B 137 GLY B 139 5 3 HELIX 19 19 PHE B 150 LEU B 165 1 16 HELIX 20 20 PRO B 174 ALA B 185 1 12 HELIX 21 21 PRO B 187 ALA B 194 1 8 HELIX 22 22 PRO B 196 VAL B 199 1 4 SHEET 1 A 4 TRP A 28 VAL A 33 0 SHEET 2 A 4 TYR A 3 PHE A 8 1 N TYR A 3 O LYS A 29 SHEET 3 A 4 LYS A 54 ASP A 57 -1 N GLN A 56 O THR A 4 SHEET 4 A 4 LEU A 60 TYR A 63 -1 N LEU A 62 O PHE A 55 SHEET 1 B 4 TRP B 28 VAL B 33 0 SHEET 2 B 4 TYR B 3 PHE B 8 1 N TYR B 3 O LYS B 29 SHEET 3 B 4 LYS B 54 ASP B 57 -1 N GLN B 56 O THR B 4 SHEET 4 B 4 LEU B 60 TYR B 63 -1 N LEU B 62 O PHE B 55 CISPEP 1 LEU A 52 PRO A 53 0 0.61 CISPEP 2 LEU B 52 PRO B 53 0 0.53 SITE 1 AC1 15 TYR A 7 PHE A 8 ARG A 13 TRP A 38 SITE 2 AC1 15 LYS A 44 GLY A 50 GLN A 51 LEU A 52 SITE 3 AC1 15 PRO A 53 GLN A 64 SER A 65 TYR A 108 SITE 4 AC1 15 HOH A 229 HOH A 303 ASP B 98 SITE 1 AC2 15 ASP A 98 TYR B 7 PHE B 8 ARG B 13 SITE 2 AC2 15 TRP B 38 LYS B 44 GLY B 50 GLN B 51 SITE 3 AC2 15 LEU B 52 PRO B 53 GLN B 64 SER B 65 SITE 4 AC2 15 TYR B 108 HOH B 224 HOH B 287 SITE 1 AC3 5 ALA A 22 TRP A 28 GLU A 30 GLU A 197 SITE 2 AC3 5 ASP B 171 SITE 1 AC4 6 ASP A 171 HOH A 246 ALA B 22 TRP B 28 SITE 2 AC4 6 GLU B 30 GLU B 197 CRYST1 79.723 90.460 69.404 90.00 98.19 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012543 0.000000 0.001805 0.00000 SCALE2 0.000000 0.011055 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014557 0.00000 MTRIX1 1 0.945333 0.099229 0.310644 -5.48795 1 MTRIX2 1 0.099832 -0.994906 0.013998 21.83043 1 MTRIX3 1 0.310451 0.017779 -0.950423 27.67516 1 ATOM 1 N PRO A 2 31.242 3.064 39.284 1.00 39.90 N ATOM 2 CA PRO A 2 31.195 2.392 37.963 1.00 31.96 C ATOM 3 C PRO A 2 29.975 2.923 37.197 1.00 30.23 C ATOM 4 O PRO A 2 29.727 4.132 37.181 1.00 27.03 O ATOM 5 CB PRO A 2 31.063 0.905 38.251 1.00 36.57 C ATOM 6 CG PRO A 2 30.276 0.947 39.549 1.00 35.11 C ATOM 7 CD PRO A 2 30.829 2.121 40.343 1.00 42.06 C ATOM 8 N TYR A 3 29.189 2.020 36.613 1.00 22.83 N ATOM 9 CA TYR A 3 28.011 2.405 35.850 1.00 18.42 C ATOM 10 C TYR A 3 26.711 1.995 36.517 1.00 19.46 C ATOM 11 O TYR A 3 26.629 0.949 37.161 1.00 24.89 O ATOM 12 CB TYR A 3 28.055 1.772 34.459 1.00 17.73 C ATOM 13 CG TYR A 3 29.318 2.059 33.684 1.00 17.23 C ATOM 14 CD1 TYR A 3 29.678 3.366 33.355 1.00 19.19 C ATOM 15 CD2 TYR A 3 30.149 1.023 33.267 1.00 16.84 C ATOM 16 CE1 TYR A 3 30.835 3.633 32.629 1.00 18.79 C ATOM 17 CE2 TYR A 3 31.308 1.279 32.539 1.00 20.85 C ATOM 18 CZ TYR A 3 31.645 2.584 32.226 1.00 20.77 C ATOM 19 OH TYR A 3 32.803 2.828 31.528 1.00 22.24 O ATOM 20 N THR A 4 25.683 2.804 36.297 1.00 13.22 N ATOM 21 CA THR A 4 24.361 2.547 36.835 1.00 19.34 C ATOM 22 C THR A 4 23.337 2.985 35.797 1.00 20.48 C ATOM 23 O THR A 4 23.374 4.124 35.335 1.00 22.30 O ATOM 24 CB THR A 4 24.097 3.357 38.132 1.00 18.80 C ATOM 25 OG1 THR A 4 25.094 3.042 39.110 1.00 19.60 O ATOM 26 CG2 THR A 4 22.713 3.031 38.699 1.00 12.79 C ATOM 27 N VAL A 5 22.463 2.071 35.385 1.00 18.58 N ATOM 28 CA VAL A 5 21.420 2.437 34.438 1.00 17.96 C ATOM 29 C VAL A 5 20.078 2.369 35.160 1.00 19.40 C ATOM 30 O VAL A 5 19.743 1.367 35.790 1.00 22.04 O ATOM 31 CB VAL A 5 21.436 1.582 33.113 1.00 17.57 C ATOM 32 CG1 VAL A 5 22.717 0.779 32.989 1.00 12.49 C ATOM 33 CG2 VAL A 5 20.204 0.704 32.988 1.00 22.38 C ATOM 34 N VAL A 6 19.366 3.488 35.149 1.00 19.86 N ATOM 35 CA VAL A 6 18.059 3.585 35.781 1.00 19.18 C ATOM 36 C VAL A 6 17.049 3.522 34.638 1.00 21.26 C ATOM 37 O VAL A 6 17.045 4.385 33.752 1.00 18.67 O ATOM 38 CB VAL A 6 17.906 4.919 36.550 1.00 19.15 C ATOM 39 CG1 VAL A 6 16.592 4.937 37.304 1.00 13.21 C ATOM 40 CG2 VAL A 6 19.084 5.122 37.497 1.00 16.31 C ATOM 41 N TYR A 7 16.196 2.504 34.657 1.00 16.48 N ATOM 42 CA TYR A 7 15.226 2.331 33.585 1.00 17.51 C ATOM 43 C TYR A 7 14.067 1.427 33.993 1.00 15.22 C ATOM 44 O TYR A 7 14.097 0.789 35.042 1.00 21.57 O ATOM 45 CB TYR A 7 15.954 1.735 32.372 1.00 17.21 C ATOM 46 CG TYR A 7 15.202 1.810 31.064 1.00 19.24 C ATOM 47 CD1 TYR A 7 14.713 3.025 30.580 1.00 23.22 C ATOM 48 CD2 TYR A 7 14.995 0.665 30.297 1.00 18.29 C ATOM 49 CE1 TYR A 7 14.036 3.095 29.363 1.00 18.22 C ATOM 50 CE2 TYR A 7 14.323 0.723 29.083 1.00 19.10 C ATOM 51 CZ TYR A 7 13.846 1.938 28.621 1.00 21.78 C ATOM 52 OH TYR A 7 13.180 1.997 27.419 1.00 19.49 O ATOM 53 N PHE A 8 13.041 1.388 33.152 1.00 17.17 N ATOM 54 CA PHE A 8 11.870 0.551 33.384 1.00 20.97 C ATOM 55 C PHE A 8 12.265 -0.902 33.111 1.00 23.22 C ATOM 56 O PHE A 8 13.297 -1.157 32.496 1.00 22.12 O ATOM 57 CB PHE A 8 10.742 0.990 32.454 1.00 20.14 C ATOM 58 CG PHE A 8 10.344 2.426 32.635 1.00 26.86 C ATOM 59 CD1 PHE A 8 9.655 2.833 33.777 1.00 28.34 C ATOM 60 CD2 PHE A 8 10.680 3.380 31.679 1.00 25.81 C ATOM 61 CE1 PHE A 8 9.306 4.171 33.966 1.00 26.11 C ATOM 62 CE2 PHE A 8 10.337 4.724 31.856 1.00 27.24 C ATOM 63 CZ PHE A 8 9.649 5.120 33.002 1.00 31.55 C ATOM 64 N PRO A 9 11.475 -1.874 33.599 1.00 22.45 N ATOM 65 CA PRO A 9 11.810 -3.285 33.365 1.00 25.63 C ATOM 66 C PRO A 9 11.527 -3.784 31.939 1.00 23.89 C ATOM 67 O PRO A 9 10.777 -4.740 31.743 1.00 27.87 O ATOM 68 CB PRO A 9 10.955 -4.005 34.409 1.00 26.37 C ATOM 69 CG PRO A 9 9.724 -3.141 34.473 1.00 23.87 C ATOM 70 CD PRO A 9 10.312 -1.748 34.496 1.00 24.97 C ATOM 71 N VAL A 10 12.125 -3.123 30.949 1.00 23.67 N ATOM 72 CA VAL A 10 11.969 -3.489 29.541 1.00 19.23 C ATOM 73 C VAL A 10 13.312 -3.289 28.850 1.00 20.13 C ATOM 74 O VAL A 10 14.214 -2.661 29.407 1.00 21.70 O ATOM 75 CB VAL A 10 10.906 -2.613 28.810 1.00 22.15 C ATOM 76 CG1 VAL A 10 9.550 -2.724 29.493 1.00 20.17 C ATOM 77 CG2 VAL A 10 11.359 -1.160 28.743 1.00 22.63 C ATOM 78 N ARG A 11 13.460 -3.848 27.653 1.00 18.71 N ATOM 79 CA ARG A 11 14.701 -3.694 26.898 1.00 18.17 C ATOM 80 C ARG A 11 14.738 -2.278 26.338 1.00 15.50 C ATOM 81 O ARG A 11 15.679 -1.529 26.597 1.00 14.31 O ATOM 82 CB ARG A 11 14.773 -4.713 25.762 1.00 18.01 C ATOM 83 CG ARG A 11 14.797 -6.150 26.244 1.00 27.60 C ATOM 84 CD ARG A 11 14.943 -7.120 25.092 1.00 27.61 C ATOM 85 NE ARG A 11 14.609 -8.476 25.509 1.00 37.28 N ATOM 86 CZ ARG A 11 14.246 -9.448 24.679 1.00 34.90 C ATOM 87 NH1 ARG A 11 14.176 -9.219 23.375 1.00 34.05 N ATOM 88 NH2 ARG A 11 13.917 -10.638 25.163 1.00 34.82 N ATOM 89 N GLY A 12 13.692 -1.933 25.585 1.00 16.37 N ATOM 90 CA GLY A 12 13.546 -0.612 24.995 1.00 15.31 C ATOM 91 C GLY A 12 14.805 0.095 24.539 1.00 16.39 C ATOM 92 O GLY A 12 15.615 -0.464 23.794 1.00 12.85 O ATOM 93 N ARG A 13 14.993 1.315 25.032 1.00 15.58 N ATOM 94 CA ARG A 13 16.152 2.121 24.667 1.00 18.28 C ATOM 95 C ARG A 13 17.452 1.819 25.406 1.00 17.33 C ATOM 96 O ARG A 13 18.432 2.551 25.256 1.00 17.22 O ATOM 97 CB ARG A 13 15.815 3.611 24.771 1.00 20.29 C ATOM 98 CG ARG A 13 14.896 4.098 23.662 1.00 17.00 C ATOM 99 CD ARG A 13 14.694 5.596 23.736 1.00 15.27 C ATOM 100 NE ARG A 13 13.987 6.117 22.568 1.00 18.44 N ATOM 101 CZ ARG A 13 14.584 6.502 21.444 1.00 16.41 C ATOM 102 NH1 ARG A 13 15.904 6.417 21.320 1.00 13.14 N ATOM 103 NH2 ARG A 13 13.856 6.965 20.438 1.00 10.51 N ATOM 104 N CYS A 14 17.470 0.750 26.199 1.00 14.56 N ATOM 105 CA CYS A 14 18.685 0.383 26.927 1.00 11.34 C ATOM 106 C CYS A 14 19.309 -0.901 26.413 1.00 11.79 C ATOM 107 O CYS A 14 20.429 -1.250 26.795 1.00 10.40 O ATOM 108 CB CYS A 14 18.411 0.265 28.428 1.00 13.29 C ATOM 109 SG CYS A 14 18.129 1.852 29.221 1.00 17.53 S ATOM 110 N ALA A 15 18.591 -1.590 25.530 1.00 10.15 N ATOM 111 CA ALA A 15 19.059 -2.847 24.959 1.00 13.24 C ATOM 112 C ALA A 15 20.445 -2.728 24.332 1.00 13.21 C ATOM 113 O ALA A 15 21.353 -3.490 24.667 1.00 18.26 O ATOM 114 CB ALA A 15 18.048 -3.362 23.935 1.00 11.30 C ATOM 115 N ALA A 16 20.620 -1.732 23.470 1.00 16.63 N ATOM 116 CA ALA A 16 21.892 -1.515 22.794 1.00 10.39 C ATOM 117 C ALA A 16 23.036 -1.185 23.745 1.00 15.32 C ATOM 118 O ALA A 16 24.125 -1.760 23.631 1.00 17.28 O ATOM 119 CB ALA A 16 21.747 -0.433 21.742 1.00 14.07 C ATOM 120 N LEU A 17 22.792 -0.282 24.694 1.00 15.12 N ATOM 121 CA LEU A 17 23.834 0.100 25.648 1.00 17.17 C ATOM 122 C LEU A 17 24.190 -1.056 26.589 1.00 15.48 C ATOM 123 O LEU A 17 25.335 -1.168 27.035 1.00 17.10 O ATOM 124 CB LEU A 17 23.454 1.381 26.416 1.00 19.50 C ATOM 125 CG LEU A 17 22.302 1.445 27.420 1.00 23.29 C ATOM 126 CD1 LEU A 17 22.845 1.235 28.820 1.00 21.79 C ATOM 127 CD2 LEU A 17 21.617 2.808 27.334 1.00 20.62 C ATOM 128 N ARG A 18 23.223 -1.931 26.859 1.00 10.96 N ATOM 129 CA ARG A 18 23.468 -3.096 27.707 1.00 15.98 C ATOM 130 C ARG A 18 24.332 -4.104 26.951 1.00 17.26 C ATOM 131 O ARG A 18 25.273 -4.670 27.516 1.00 17.70 O ATOM 132 CB ARG A 18 22.155 -3.748 28.125 1.00 15.83 C ATOM 133 CG ARG A 18 21.408 -2.979 29.195 1.00 13.17 C ATOM 134 CD ARG A 18 19.985 -3.478 29.308 1.00 14.43 C ATOM 135 NE ARG A 18 19.289 -2.858 30.426 1.00 11.87 N ATOM 136 CZ ARG A 18 17.970 -2.717 30.505 1.00 15.61 C ATOM 137 NH1 ARG A 18 17.188 -3.148 29.523 1.00 15.54 N ATOM 138 NH2 ARG A 18 17.430 -2.148 31.577 1.00 13.98 N ATOM 139 N MET A 19 24.019 -4.313 25.671 1.00 16.80 N ATOM 140 CA MET A 19 24.787 -5.237 24.834 1.00 15.14 C ATOM 141 C MET A 19 26.219 -4.743 24.714 1.00 17.68 C ATOM 142 O MET A 19 27.158 -5.536 24.713 1.00 20.00 O ATOM 143 CB MET A 19 24.185 -5.341 23.433 1.00 19.56 C ATOM 144 CG MET A 19 22.786 -5.920 23.379 1.00 21.18 C ATOM 145 SD MET A 19 22.261 -6.218 21.687 1.00 31.83 S ATOM 146 CE MET A 19 22.032 -4.592 21.115 1.00 33.49 C ATOM 147 N LEU A 20 26.374 -3.425 24.611 1.00 14.60 N ATOM 148 CA LEU A 20 27.689 -2.804 24.493 1.00 16.07 C ATOM 149 C LEU A 20 28.521 -3.068 25.751 1.00 19.64 C ATOM 150 O LEU A 20 29.675 -3.501 25.665 1.00 15.82 O ATOM 151 CB LEU A 20 27.529 -1.296 24.252 1.00 17.09 C ATOM 152 CG LEU A 20 28.749 -0.433 23.902 1.00 21.27 C ATOM 153 CD1 LEU A 20 28.275 0.862 23.265 1.00 19.18 C ATOM 154 CD2 LEU A 20 29.615 -0.147 25.128 1.00 16.96 C ATOM 155 N LEU A 21 27.932 -2.792 26.914 1.00 19.49 N ATOM 156 CA LEU A 21 28.607 -3.002 28.192 1.00 18.96 C ATOM 157 C LEU A 21 28.966 -4.472 28.388 1.00 17.46 C ATOM 158 O LEU A 21 30.093 -4.793 28.748 1.00 18.27 O ATOM 159 CB LEU A 21 27.728 -2.518 29.350 1.00 14.89 C ATOM 160 CG LEU A 21 27.585 -1.001 29.494 1.00 14.97 C ATOM 161 CD1 LEU A 21 26.521 -0.668 30.522 1.00 13.48 C ATOM 162 CD2 LEU A 21 28.925 -0.394 29.884 1.00 13.27 C ATOM 163 N ALA A 22 28.013 -5.356 28.115 1.00 16.24 N ATOM 164 CA ALA A 22 28.224 -6.793 28.258 1.00 17.75 C ATOM 165 C ALA A 22 29.358 -7.280 27.364 1.00 18.70 C ATOM 166 O ALA A 22 30.309 -7.909 27.836 1.00 24.16 O ATOM 167 CB ALA A 22 26.946 -7.539 27.928 1.00 16.02 C ATOM 168 N ASP A 23 29.276 -6.943 26.081 1.00 19.77 N ATOM 169 CA ASP A 23 30.281 -7.348 25.105 1.00 20.00 C ATOM 170 C ASP A 23 31.676 -6.787 25.386 1.00 20.89 C ATOM 171 O ASP A 23 32.681 -7.407 25.036 1.00 23.31 O ATOM 172 CB ASP A 23 29.836 -6.954 23.693 1.00 24.93 C ATOM 173 CG ASP A 23 30.595 -7.706 22.612 1.00 28.30 C ATOM 174 OD1 ASP A 23 30.503 -8.949 22.578 1.00 29.29 O ATOM 175 OD2 ASP A 23 31.316 -7.074 21.815 1.00 26.02 O ATOM 176 N GLN A 24 31.738 -5.613 26.006 1.00 24.47 N ATOM 177 CA GLN A 24 33.020 -4.987 26.329 1.00 23.19 C ATOM 178 C GLN A 24 33.566 -5.446 27.673 1.00 22.46 C ATOM 179 O GLN A 24 34.592 -4.950 28.133 1.00 29.52 O ATOM 180 CB GLN A 24 32.897 -3.461 26.306 1.00 19.66 C ATOM 181 CG GLN A 24 32.696 -2.884 24.907 1.00 17.35 C ATOM 182 CD GLN A 24 33.820 -3.268 23.968 1.00 20.22 C ATOM 183 OE1 GLN A 24 34.994 -3.138 24.317 1.00 19.83 O ATOM 184 NE2 GLN A 24 33.472 -3.759 22.785 1.00 13.55 N ATOM 185 N GLY A 25 32.870 -6.391 28.298 1.00 23.76 N ATOM 186 CA GLY A 25 33.295 -6.918 29.582 1.00 23.57 C ATOM 187 C GLY A 25 33.165 -5.936 30.730 1.00 22.99 C ATOM 188 O GLY A 25 33.950 -5.973 31.667 1.00 26.83 O ATOM 189 N GLN A 26 32.171 -5.058 30.658 1.00 26.31 N ATOM 190 CA GLN A 26 31.943 -4.060 31.700 1.00 28.99 C ATOM 191 C GLN A 26 30.861 -4.495 32.677 1.00 27.54 C ATOM 192 O GLN A 26 29.915 -5.189 32.306 1.00 30.40 O ATOM 193 CB GLN A 26 31.540 -2.719 31.078 1.00 31.87 C ATOM 194 CG GLN A 26 32.541 -2.161 30.083 1.00 32.88 C ATOM 195 CD GLN A 26 33.901 -1.926 30.700 1.00 33.03 C ATOM 196 OE1 GLN A 26 34.008 -1.498 31.850 1.00 28.41 O ATOM 197 NE2 GLN A 26 34.953 -2.229 29.948 1.00 38.94 N ATOM 198 N SER A 27 31.007 -4.064 33.926 1.00 28.74 N ATOM 199 CA SER A 27 30.052 -4.378 34.983 1.00 26.82 C ATOM 200 C SER A 27 29.194 -3.143 35.206 1.00 25.69 C ATOM 201 O SER A 27 29.686 -2.018 35.124 1.00 27.06 O ATOM 202 CB SER A 27 30.786 -4.692 36.291 1.00 29.20 C ATOM 203 OG SER A 27 31.909 -5.523 36.071 1.00 41.28 O ATOM 204 N TRP A 28 27.915 -3.345 35.493 1.00 21.96 N ATOM 205 CA TRP A 28 27.033 -2.220 35.755 1.00 24.43 C ATOM 206 C TRP A 28 25.903 -2.616 36.697 1.00 26.77 C ATOM 207 O TRP A 28 25.584 -3.795 36.841 1.00 25.34 O ATOM 208 CB TRP A 28 26.472 -1.638 34.453 1.00 21.55 C ATOM 209 CG TRP A 28 25.449 -2.498 33.757 1.00 14.67 C ATOM 210 CD1 TRP A 28 24.090 -2.375 33.830 1.00 9.31 C ATOM 211 CD2 TRP A 28 25.709 -3.566 32.833 1.00 12.15 C ATOM 212 NE1 TRP A 28 23.491 -3.293 33.002 1.00 11.46 N ATOM 213 CE2 TRP A 28 24.457 -4.035 32.378 1.00 10.63 C ATOM 214 CE3 TRP A 28 26.877 -4.171 32.344 1.00 12.67 C ATOM 215 CZ2 TRP A 28 24.341 -5.078 31.453 1.00 9.14 C ATOM 216 CZ3 TRP A 28 26.759 -5.209 31.426 1.00 13.30 C ATOM 217 CH2 TRP A 28 25.497 -5.650 30.991 1.00 9.78 C ATOM 218 N LYS A 29 25.311 -1.615 37.337 1.00 24.24 N ATOM 219 CA LYS A 29 24.219 -1.817 38.272 1.00 22.87 C ATOM 220 C LYS A 29 22.915 -1.406 37.610 1.00 23.70 C ATOM 221 O LYS A 29 22.855 -0.391 36.920 1.00 25.40 O ATOM 222 CB LYS A 29 24.465 -0.976 39.529 1.00 29.03 C ATOM 223 CG LYS A 29 23.266 -0.813 40.449 1.00 39.95 C ATOM 224 CD LYS A 29 22.942 -2.085 41.219 1.00 51.60 C ATOM 225 CE LYS A 29 21.690 -1.893 42.070 1.00 57.02 C ATOM 226 NZ LYS A 29 21.792 -0.670 42.925 1.00 61.59 N ATOM 227 N GLU A 30 21.883 -2.220 37.792 1.00 25.07 N ATOM 228 CA GLU A 30 20.575 -1.930 37.229 1.00 27.49 C ATOM 229 C GLU A 30 19.651 -1.439 38.332 1.00 30.70 C ATOM 230 O GLU A 30 19.456 -2.119 39.339 1.00 35.30 O ATOM 231 CB GLU A 30 19.971 -3.182 36.581 1.00 25.50 C ATOM 232 CG GLU A 30 20.635 -3.620 35.278 1.00 28.34 C ATOM 233 CD GLU A 30 20.113 -2.894 34.036 1.00 30.13 C ATOM 234 OE1 GLU A 30 19.166 -2.081 34.132 1.00 26.14 O ATOM 235 OE2 GLU A 30 20.642 -3.166 32.940 1.00 25.20 O ATOM 236 N GLU A 31 19.141 -0.226 38.162 1.00 30.04 N ATOM 237 CA GLU A 31 18.212 0.369 39.109 1.00 25.07 C ATOM 238 C GLU A 31 16.875 0.323 38.411 1.00 23.26 C ATOM 239 O GLU A 31 16.590 1.143 37.543 1.00 29.50 O ATOM 240 CB GLU A 31 18.600 1.815 39.412 1.00 34.10 C ATOM 241 CG GLU A 31 19.672 1.960 40.474 1.00 50.28 C ATOM 242 CD GLU A 31 19.149 1.662 41.865 1.00 60.18 C ATOM 243 OE1 GLU A 31 19.103 0.473 42.253 1.00 64.38 O ATOM 244 OE2 GLU A 31 18.780 2.623 42.572 1.00 67.09 O ATOM 245 N VAL A 32 16.074 -0.675 38.753 1.00 23.05 N ATOM 246 CA VAL A 32 14.771 -0.841 38.132 1.00 20.87 C ATOM 247 C VAL A 32 13.711 0.081 38.711 1.00 23.88 C ATOM 248 O VAL A 32 13.533 0.168 39.922 1.00 29.17 O ATOM 249 CB VAL A 32 14.290 -2.303 38.222 1.00 18.51 C ATOM 250 CG1 VAL A 32 12.968 -2.469 37.496 1.00 11.00 C ATOM 251 CG2 VAL A 32 15.342 -3.230 37.632 1.00 19.20 C ATOM 252 N VAL A 33 13.021 0.782 37.821 1.00 26.92 N ATOM 253 CA VAL A 33 11.956 1.693 38.197 1.00 20.59 C ATOM 254 C VAL A 33 10.673 1.115 37.629 1.00 27.61 C ATOM 255 O VAL A 33 10.568 0.885 36.422 1.00 28.93 O ATOM 256 CB VAL A 33 12.180 3.106 37.603 1.00 21.72 C ATOM 257 CG1 VAL A 33 10.984 4.002 37.892 1.00 15.74 C ATOM 258 CG2 VAL A 33 13.446 3.720 38.172 1.00 15.51 C ATOM 259 N THR A 34 9.713 0.850 38.506 1.00 31.68 N ATOM 260 CA THR A 34 8.429 0.298 38.090 1.00 36.01 C ATOM 261 C THR A 34 7.491 1.426 37.669 1.00 38.72 C ATOM 262 O THR A 34 7.734 2.591 37.983 1.00 41.66 O ATOM 263 CB THR A 34 7.770 -0.500 39.231 1.00 36.94 C ATOM 264 OG1 THR A 34 7.449 0.386 40.311 1.00 39.11 O ATOM 265 CG2 THR A 34 8.716 -1.576 39.739 1.00 37.02 C ATOM 266 N VAL A 35 6.421 1.072 36.961 1.00 45.54 N ATOM 267 CA VAL A 35 5.430 2.046 36.503 1.00 49.15 C ATOM 268 C VAL A 35 4.763 2.744 37.696 1.00 50.88 C ATOM 269 O VAL A 35 4.352 3.900 37.599 1.00 50.67 O ATOM 270 CB VAL A 35 4.345 1.367 35.624 1.00 54.47 C ATOM 271 CG1 VAL A 35 3.464 0.436 36.471 1.00 59.75 C ATOM 272 CG2 VAL A 35 3.508 2.415 34.905 1.00 54.91 C ATOM 273 N GLU A 36 4.677 2.035 38.820 1.00 52.65 N ATOM 274 CA GLU A 36 4.078 2.572 40.039 1.00 52.64 C ATOM 275 C GLU A 36 4.960 3.681 40.599 1.00 50.05 C ATOM 276 O GLU A 36 4.495 4.800 40.823 1.00 53.84 O ATOM 277 CB GLU A 36 3.948 1.473 41.092 1.00 61.16 C ATOM 278 CG GLU A 36 3.445 0.142 40.565 1.00 69.73 C ATOM 279 CD GLU A 36 4.198 -1.038 41.164 1.00 76.39 C ATOM 280 OE1 GLU A 36 4.757 -0.902 42.277 1.00 77.39 O ATOM 281 OE2 GLU A 36 4.238 -2.105 40.518 1.00 77.77 O ATOM 282 N THR A 37 6.232 3.355 40.828 1.00 44.55 N ATOM 283 CA THR A 37 7.204 4.305 41.364 1.00 42.71 C ATOM 284 C THR A 37 7.276 5.562 40.490 1.00 42.44 C ATOM 285 O THR A 37 7.340 6.681 41.003 1.00 42.10 O ATOM 286 CB THR A 37 8.615 3.672 41.447 1.00 44.66 C ATOM 287 OG1 THR A 37 8.528 2.371 42.040 1.00 46.34 O ATOM 288 CG2 THR A 37 9.544 4.536 42.290 1.00 41.79 C ATOM 289 N TRP A 38 7.239 5.364 39.172 1.00 42.16 N ATOM 290 CA TRP A 38 7.305 6.459 38.203 1.00 39.46 C ATOM 291 C TRP A 38 6.096 7.393 38.300 1.00 42.03 C ATOM 292 O TRP A 38 6.249 8.617 38.278 1.00 41.15 O ATOM 293 CB TRP A 38 7.428 5.896 36.780 1.00 32.30 C ATOM 294 CG TRP A 38 7.661 6.931 35.701 1.00 24.31 C ATOM 295 CD1 TRP A 38 6.790 7.298 34.715 1.00 18.18 C ATOM 296 CD2 TRP A 38 8.859 7.693 35.485 1.00 16.86 C ATOM 297 NE1 TRP A 38 7.369 8.235 33.897 1.00 19.40 N ATOM 298 CE2 TRP A 38 8.638 8.498 34.344 1.00 19.29 C ATOM 299 CE3 TRP A 38 10.097 7.773 36.138 1.00 22.01 C ATOM 300 CZ2 TRP A 38 9.611 9.372 33.842 1.00 14.35 C ATOM 301 CZ3 TRP A 38 11.065 8.641 35.639 1.00 17.86 C ATOM 302 CH2 TRP A 38 10.813 9.429 34.501 1.00 17.91 C ATOM 303 N GLN A 39 4.902 6.813 38.421 1.00 42.44 N ATOM 304 CA GLN A 39 3.676 7.599 38.523 1.00 44.49 C ATOM 305 C GLN A 39 3.551 8.367 39.836 1.00 46.94 C ATOM 306 O GLN A 39 2.690 9.236 39.972 1.00 47.20 O ATOM 307 CB GLN A 39 2.456 6.715 38.288 1.00 44.40 C ATOM 308 CG GLN A 39 2.354 6.233 36.850 1.00 53.16 C ATOM 309 CD GLN A 39 1.292 5.173 36.648 1.00 59.98 C ATOM 310 OE1 GLN A 39 0.797 4.578 37.607 1.00 67.08 O ATOM 311 NE2 GLN A 39 0.943 4.922 35.392 1.00 59.24 N ATOM 312 N GLU A 40 4.421 8.053 40.795 1.00 49.96 N ATOM 313 CA GLU A 40 4.428 8.743 42.080 1.00 52.49 C ATOM 314 C GLU A 40 4.853 10.200 41.834 1.00 52.77 C ATOM 315 O GLU A 40 4.470 11.100 42.581 1.00 54.24 O ATOM 316 CB GLU A 40 5.373 8.031 43.054 1.00 53.55 C ATOM 317 CG GLU A 40 5.412 8.617 44.451 1.00 59.79 C ATOM 318 CD GLU A 40 6.628 9.486 44.674 1.00 66.11 C ATOM 319 OE1 GLU A 40 7.700 8.924 44.984 1.00 70.23 O ATOM 320 OE2 GLU A 40 6.517 10.723 44.528 1.00 69.73 O ATOM 321 N GLY A 41 5.649 10.415 40.783 1.00 50.64 N ATOM 322 CA GLY A 41 6.069 11.757 40.415 1.00 44.43 C ATOM 323 C GLY A 41 7.438 12.310 40.773 1.00 42.61 C ATOM 324 O GLY A 41 8.028 13.035 39.974 1.00 43.64 O ATOM 325 N SER A 42 7.949 11.983 41.955 1.00 42.42 N ATOM 326 CA SER A 42 9.241 12.506 42.405 1.00 44.32 C ATOM 327 C SER A 42 10.445 12.287 41.484 1.00 41.57 C ATOM 328 O SER A 42 11.182 13.233 41.205 1.00 44.27 O ATOM 329 CB SER A 42 9.560 12.000 43.812 1.00 41.72 C ATOM 330 OG SER A 42 9.633 10.588 43.833 1.00 54.29 O ATOM 331 N LEU A 43 10.649 11.053 41.023 1.00 39.95 N ATOM 332 CA LEU A 43 11.777 10.738 40.141 1.00 34.67 C ATOM 333 C LEU A 43 11.672 11.474 38.803 1.00 31.40 C ATOM 334 O LEU A 43 12.646 12.074 38.344 1.00 30.49 O ATOM 335 CB LEU A 43 11.865 9.229 39.883 1.00 31.59 C ATOM 336 CG LEU A 43 13.242 8.567 39.694 1.00 30.92 C ATOM 337 CD1 LEU A 43 13.109 7.457 38.677 1.00 27.88 C ATOM 338 CD2 LEU A 43 14.315 9.549 39.246 1.00 29.03 C ATOM 339 N LYS A 44 10.494 11.415 38.184 1.00 24.34 N ATOM 340 CA LYS A 44 10.247 12.071 36.901 1.00 27.16 C ATOM 341 C LYS A 44 10.612 13.551 36.969 1.00 31.60 C ATOM 342 O LYS A 44 11.250 14.086 36.062 1.00 33.78 O ATOM 343 CB LYS A 44 8.775 11.939 36.516 1.00 24.51 C ATOM 344 CG LYS A 44 8.460 12.409 35.105 1.00 25.49 C ATOM 345 CD LYS A 44 6.964 12.558 34.887 1.00 25.65 C ATOM 346 CE LYS A 44 6.572 12.269 33.444 1.00 27.65 C ATOM 347 NZ LYS A 44 7.455 12.940 32.449 1.00 30.67 N ATOM 348 N ALA A 45 10.226 14.189 38.071 1.00 32.54 N ATOM 349 CA ALA A 45 10.485 15.604 38.295 1.00 27.71 C ATOM 350 C ALA A 45 11.972 15.932 38.382 1.00 29.20 C ATOM 351 O ALA A 45 12.385 17.032 38.017 1.00 35.04 O ATOM 352 CB ALA A 45 9.769 16.070 39.554 1.00 31.87 C ATOM 353 N SER A 46 12.772 14.989 38.874 1.00 25.18 N ATOM 354 CA SER A 46 14.214 15.203 38.996 1.00 27.63 C ATOM 355 C SER A 46 14.982 14.889 37.710 1.00 27.98 C ATOM 356 O SER A 46 16.181 15.164 37.620 1.00 30.37 O ATOM 357 CB SER A 46 14.785 14.382 40.150 1.00 29.21 C ATOM 358 OG SER A 46 14.561 12.999 39.945 1.00 44.20 O ATOM 359 N CYS A 47 14.304 14.271 36.742 1.00 23.03 N ATOM 360 CA CYS A 47 14.919 13.937 35.454 1.00 26.37 C ATOM 361 C CYS A 47 14.912 15.173 34.559 1.00 25.13 C ATOM 362 O CYS A 47 13.866 15.806 34.386 1.00 22.91 O ATOM 363 CB CYS A 47 14.152 12.808 34.760 1.00 23.46 C ATOM 364 SG CYS A 47 14.304 11.197 35.554 1.00 27.54 S ATOM 365 N LEU A 48 16.067 15.487 33.971 1.00 21.04 N ATOM 366 CA LEU A 48 16.221 16.659 33.103 1.00 20.83 C ATOM 367 C LEU A 48 15.094 16.874 32.084 1.00 23.19 C ATOM 368 O LEU A 48 14.545 17.971 31.989 1.00 22.36 O ATOM 369 CB LEU A 48 17.572 16.613 32.388 1.00 21.43 C ATOM 370 CG LEU A 48 17.905 17.809 31.494 1.00 23.36 C ATOM 371 CD1 LEU A 48 17.888 19.098 32.309 1.00 22.48 C ATOM 372 CD2 LEU A 48 19.263 17.598 30.853 1.00 22.00 C ATOM 373 N TYR A 49 14.754 15.834 31.326 1.00 17.93 N ATOM 374 CA TYR A 49 13.688 15.931 30.332 1.00 17.34 C ATOM 375 C TYR A 49 12.441 15.158 30.766 1.00 21.20 C ATOM 376 O TYR A 49 11.530 14.928 29.961 1.00 14.11 O ATOM 377 CB TYR A 49 14.175 15.426 28.970 1.00 17.04 C ATOM 378 CG TYR A 49 15.371 16.179 28.427 1.00 14.10 C ATOM 379 CD1 TYR A 49 15.281 17.531 28.084 1.00 14.26 C ATOM 380 CD2 TYR A 49 16.596 15.538 28.252 1.00 10.28 C ATOM 381 CE1 TYR A 49 16.391 18.223 27.578 1.00 7.64 C ATOM 382 CE2 TYR A 49 17.707 16.215 27.748 1.00 10.99 C ATOM 383 CZ TYR A 49 17.599 17.555 27.413 1.00 14.17 C ATOM 384 OH TYR A 49 18.697 18.217 26.906 1.00 19.78 O ATOM 385 N GLY A 50 12.413 14.771 32.043 1.00 20.57 N ATOM 386 CA GLY A 50 11.288 14.033 32.598 1.00 16.47 C ATOM 387 C GLY A 50 11.147 12.622 32.061 1.00 19.02 C ATOM 388 O GLY A 50 10.043 12.068 32.051 1.00 21.41 O ATOM 389 N GLN A 51 12.254 12.036 31.608 1.00 16.59 N ATOM 390 CA GLN A 51 12.215 10.686 31.059 1.00 15.75 C ATOM 391 C GLN A 51 13.437 9.843 31.405 1.00 18.20 C ATOM 392 O GLN A 51 14.458 10.358 31.865 1.00 15.12 O ATOM 393 CB GLN A 51 12.079 10.738 29.534 1.00 13.21 C ATOM 394 CG GLN A 51 10.789 11.340 29.017 1.00 14.77 C ATOM 395 CD GLN A 51 10.609 11.132 27.529 1.00 15.60 C ATOM 396 OE1 GLN A 51 9.567 10.663 27.080 1.00 16.69 O ATOM 397 NE2 GLN A 51 11.640 11.452 26.758 1.00 14.70 N ATOM 398 N LEU A 52 13.300 8.535 31.194 1.00 18.47 N ATOM 399 CA LEU A 52 14.378 7.575 31.417 1.00 18.09 C ATOM 400 C LEU A 52 14.744 7.029 30.028 1.00 18.83 C ATOM 401 O LEU A 52 13.942 7.114 29.101 1.00 20.56 O ATOM 402 CB LEU A 52 13.906 6.449 32.346 1.00 17.44 C ATOM 403 CG LEU A 52 13.559 6.853 33.787 1.00 18.00 C ATOM 404 CD1 LEU A 52 13.012 5.654 34.554 1.00 13.76 C ATOM 405 CD2 LEU A 52 14.787 7.422 34.491 1.00 13.17 C ATOM 406 N PRO A 53 15.916 6.393 29.879 1.00 19.09 N ATOM 407 CA PRO A 53 16.958 6.104 30.868 1.00 19.90 C ATOM 408 C PRO A 53 17.741 7.269 31.463 1.00 19.01 C ATOM 409 O PRO A 53 17.821 8.365 30.900 1.00 19.10 O ATOM 410 CB PRO A 53 17.899 5.173 30.101 1.00 14.57 C ATOM 411 CG PRO A 53 17.827 5.716 28.710 1.00 15.00 C ATOM 412 CD PRO A 53 16.329 5.916 28.543 1.00 15.74 C ATOM 413 N LYS A 54 18.298 6.988 32.634 1.00 18.09 N ATOM 414 CA LYS A 54 19.153 7.896 33.370 1.00 15.15 C ATOM 415 C LYS A 54 20.388 7.017 33.525 1.00 14.00 C ATOM 416 O LYS A 54 20.275 5.817 33.763 1.00 14.38 O ATOM 417 CB LYS A 54 18.557 8.225 34.736 1.00 20.85 C ATOM 418 CG LYS A 54 19.461 9.088 35.602 1.00 22.60 C ATOM 419 CD LYS A 54 18.866 9.289 36.976 1.00 24.68 C ATOM 420 CE LYS A 54 19.861 9.935 37.918 1.00 28.90 C ATOM 421 NZ LYS A 54 19.290 10.038 39.285 1.00 35.09 N ATOM 422 N PHE A 55 21.564 7.600 33.378 1.00 15.39 N ATOM 423 CA PHE A 55 22.793 6.830 33.465 1.00 15.69 C ATOM 424 C PHE A 55 23.797 7.525 34.363 1.00 16.50 C ATOM 425 O PHE A 55 23.813 8.746 34.460 1.00 22.85 O ATOM 426 CB PHE A 55 23.367 6.672 32.056 1.00 15.26 C ATOM 427 CG PHE A 55 24.585 5.793 31.971 1.00 15.55 C ATOM 428 CD1 PHE A 55 24.465 4.407 31.997 1.00 14.64 C ATOM 429 CD2 PHE A 55 25.848 6.352 31.796 1.00 17.14 C ATOM 430 CE1 PHE A 55 25.585 3.590 31.845 1.00 17.76 C ATOM 431 CE2 PHE A 55 26.974 5.543 31.643 1.00 22.44 C ATOM 432 CZ PHE A 55 26.840 4.160 31.667 1.00 19.74 C ATOM 433 N GLN A 56 24.620 6.739 35.041 1.00 19.92 N ATOM 434 CA GLN A 56 25.636 7.294 35.912 1.00 18.05 C ATOM 435 C GLN A 56 26.976 6.626 35.693 1.00 15.01 C ATOM 436 O GLN A 56 27.080 5.402 35.614 1.00 22.29 O ATOM 437 CB GLN A 56 25.212 7.189 37.379 1.00 23.86 C ATOM 438 CG GLN A 56 24.110 8.162 37.756 1.00 28.42 C ATOM 439 CD GLN A 56 23.567 7.936 39.146 1.00 39.11 C ATOM 440 OE1 GLN A 56 23.592 6.820 39.662 1.00 41.93 O ATOM 441 NE2 GLN A 56 23.039 8.992 39.750 1.00 46.95 N ATOM 442 N ASP A 57 27.985 7.462 35.507 1.00 13.98 N ATOM 443 CA ASP A 57 29.354 7.026 35.324 1.00 19.23 C ATOM 444 C ASP A 57 30.075 7.835 36.396 1.00 21.08 C ATOM 445 O ASP A 57 30.418 8.994 36.180 1.00 22.39 O ATOM 446 CB ASP A 57 29.844 7.403 33.925 1.00 19.42 C ATOM 447 CG ASP A 57 31.292 7.016 33.683 1.00 26.39 C ATOM 448 OD1 ASP A 57 31.934 6.448 34.592 1.00 30.68 O ATOM 449 OD2 ASP A 57 31.802 7.305 32.583 1.00 28.67 O ATOM 450 N GLY A 58 30.265 7.231 37.565 1.00 21.95 N ATOM 451 CA GLY A 58 30.895 7.942 38.660 1.00 21.98 C ATOM 452 C GLY A 58 29.869 8.974 39.091 1.00 24.46 C ATOM 453 O GLY A 58 28.704 8.631 39.307 1.00 25.96 O ATOM 454 N ASP A 59 30.265 10.240 39.167 1.00 27.61 N ATOM 455 CA ASP A 59 29.319 11.280 39.556 1.00 32.20 C ATOM 456 C ASP A 59 28.710 11.998 38.347 1.00 33.47 C ATOM 457 O ASP A 59 27.966 12.967 38.505 1.00 33.57 O ATOM 458 CB ASP A 59 29.950 12.273 40.545 1.00 33.78 C ATOM 459 CG ASP A 59 30.968 13.201 39.901 1.00 38.79 C ATOM 460 OD1 ASP A 59 31.544 12.862 38.847 1.00 43.22 O ATOM 461 OD2 ASP A 59 31.192 14.287 40.472 1.00 40.49 O ATOM 462 N LEU A 60 29.027 11.512 37.145 1.00 29.38 N ATOM 463 CA LEU A 60 28.494 12.085 35.913 1.00 22.30 C ATOM 464 C LEU A 60 27.126 11.457 35.671 1.00 22.13 C ATOM 465 O LEU A 60 27.011 10.243 35.526 1.00 20.79 O ATOM 466 CB LEU A 60 29.409 11.766 34.728 1.00 23.91 C ATOM 467 CG LEU A 60 29.465 12.720 33.524 1.00 26.34 C ATOM 468 CD1 LEU A 60 29.646 11.916 32.249 1.00 18.46 C ATOM 469 CD2 LEU A 60 28.221 13.580 33.425 1.00 19.40 C ATOM 470 N THR A 61 26.090 12.288 35.654 1.00 21.76 N ATOM 471 CA THR A 61 24.728 11.824 35.426 1.00 20.59 C ATOM 472 C THR A 61 24.315 12.239 34.018 1.00 22.88 C ATOM 473 O THR A 61 24.400 13.412 33.662 1.00 26.82 O ATOM 474 CB THR A 61 23.750 12.425 36.458 1.00 19.20 C ATOM 475 OG1 THR A 61 24.142 12.018 37.774 1.00 23.37 O ATOM 476 CG2 THR A 61 22.324 11.965 36.189 1.00 14.22 C ATOM 477 N LEU A 62 23.876 11.266 33.226 1.00 20.75 N ATOM 478 CA LEU A 62 23.472 11.496 31.843 1.00 20.15 C ATOM 479 C LEU A 62 22.042 11.063 31.553 1.00 16.48 C ATOM 480 O LEU A 62 21.476 10.226 32.251 1.00 19.11 O ATOM 481 CB LEU A 62 24.410 10.730 30.899 1.00 17.43 C ATOM 482 CG LEU A 62 25.628 11.376 30.228 1.00 20.64 C ATOM 483 CD1 LEU A 62 25.999 12.710 30.841 1.00 16.69 C ATOM 484 CD2 LEU A 62 26.794 10.404 30.272 1.00 13.52 C ATOM 485 N TYR A 63 21.458 11.681 30.536 1.00 15.84 N ATOM 486 CA TYR A 63 20.116 11.356 30.068 1.00 15.90 C ATOM 487 C TYR A 63 20.251 11.221 28.550 1.00 18.36 C ATOM 488 O TYR A 63 21.303 11.560 27.995 1.00 14.60 O ATOM 489 CB TYR A 63 19.116 12.453 30.432 1.00 14.13 C ATOM 490 CG TYR A 63 18.897 12.591 31.921 1.00 25.28 C ATOM 491 CD1 TYR A 63 17.919 11.843 32.579 1.00 23.89 C ATOM 492 CD2 TYR A 63 19.688 13.453 32.682 1.00 23.41 C ATOM 493 CE1 TYR A 63 17.741 11.951 33.961 1.00 26.69 C ATOM 494 CE2 TYR A 63 19.519 13.567 34.054 1.00 25.36 C ATOM 495 CZ TYR A 63 18.548 12.814 34.688 1.00 29.54 C ATOM 496 OH TYR A 63 18.403 12.911 36.051 1.00 30.00 O ATOM 497 N GLN A 64 19.210 10.705 27.893 1.00 18.04 N ATOM 498 CA GLN A 64 19.207 10.506 26.440 1.00 13.42 C ATOM 499 C GLN A 64 20.039 9.271 26.079 1.00 10.82 C ATOM 500 O GLN A 64 21.266 9.262 26.226 1.00 8.81 O ATOM 501 CB GLN A 64 19.732 11.757 25.718 1.00 14.07 C ATOM 502 CG GLN A 64 18.864 12.999 25.915 1.00 13.48 C ATOM 503 CD GLN A 64 17.596 12.954 25.091 1.00 13.00 C ATOM 504 OE1 GLN A 64 17.369 12.010 24.339 1.00 15.01 O ATOM 505 NE2 GLN A 64 16.786 13.992 25.195 1.00 16.67 N ATOM 506 N SER A 65 19.354 8.232 25.607 1.00 9.18 N ATOM 507 CA SER A 65 19.990 6.965 25.253 1.00 11.06 C ATOM 508 C SER A 65 21.186 7.099 24.315 1.00 14.01 C ATOM 509 O SER A 65 22.228 6.480 24.552 1.00 13.57 O ATOM 510 CB SER A 65 18.962 6.000 24.665 1.00 9.51 C ATOM 511 OG SER A 65 18.347 6.550 23.517 1.00 13.08 O ATOM 512 N ASN A 66 21.050 7.922 23.273 1.00 13.94 N ATOM 513 CA ASN A 66 22.142 8.122 22.315 1.00 8.62 C ATOM 514 C ASN A 66 23.332 8.882 22.895 1.00 9.76 C ATOM 515 O ASN A 66 24.466 8.685 22.462 1.00 12.73 O ATOM 516 CB ASN A 66 21.634 8.801 21.040 1.00 11.38 C ATOM 517 CG ASN A 66 20.720 7.895 20.233 1.00 13.25 C ATOM 518 OD1 ASN A 66 21.144 6.837 19.781 1.00 17.17 O ATOM 519 ND2 ASN A 66 19.475 8.304 20.046 1.00 6.17 N ATOM 520 N THR A 67 23.081 9.762 23.862 1.00 9.23 N ATOM 521 CA THR A 67 24.164 10.497 24.511 1.00 11.51 C ATOM 522 C THR A 67 24.961 9.464 25.313 1.00 13.47 C ATOM 523 O THR A 67 26.188 9.489 25.338 1.00 14.69 O ATOM 524 CB THR A 67 23.628 11.586 25.453 1.00 11.68 C ATOM 525 OG1 THR A 67 23.059 12.638 24.674 1.00 12.63 O ATOM 526 CG2 THR A 67 24.737 12.150 26.313 1.00 10.29 C ATOM 527 N ILE A 68 24.243 8.537 25.943 1.00 14.73 N ATOM 528 CA ILE A 68 24.864 7.475 26.724 1.00 14.48 C ATOM 529 C ILE A 68 25.715 6.613 25.791 1.00 11.25 C ATOM 530 O ILE A 68 26.866 6.311 26.106 1.00 9.56 O ATOM 531 CB ILE A 68 23.793 6.616 27.436 1.00 12.79 C ATOM 532 CG1 ILE A 68 22.972 7.505 28.374 1.00 9.13 C ATOM 533 CG2 ILE A 68 24.449 5.488 28.217 1.00 9.82 C ATOM 534 CD1 ILE A 68 21.649 6.904 28.789 1.00 13.17 C ATOM 535 N LEU A 69 25.160 6.244 24.636 1.00 13.07 N ATOM 536 CA LEU A 69 25.890 5.439 23.655 1.00 12.02 C ATOM 537 C LEU A 69 27.159 6.151 23.193 1.00 15.87 C ATOM 538 O LEU A 69 28.242 5.555 23.182 1.00 12.15 O ATOM 539 CB LEU A 69 25.009 5.117 22.444 1.00 12.58 C ATOM 540 CG LEU A 69 24.017 3.967 22.607 1.00 12.17 C ATOM 541 CD1 LEU A 69 23.139 3.859 21.380 1.00 19.20 C ATOM 542 CD2 LEU A 69 24.776 2.669 22.825 1.00 15.60 C ATOM 543 N ARG A 70 27.034 7.436 22.857 1.00 13.86 N ATOM 544 CA ARG A 70 28.183 8.215 22.397 1.00 15.49 C ATOM 545 C ARG A 70 29.235 8.388 23.479 1.00 12.74 C ATOM 546 O ARG A 70 30.434 8.364 23.196 1.00 17.08 O ATOM 547 CB ARG A 70 27.743 9.572 21.846 1.00 15.49 C ATOM 548 CG ARG A 70 27.052 9.453 20.506 1.00 14.53 C ATOM 549 CD ARG A 70 26.774 10.795 19.854 1.00 16.53 C ATOM 550 NE ARG A 70 26.441 10.597 18.447 1.00 14.43 N ATOM 551 CZ ARG A 70 25.205 10.484 17.969 1.00 20.23 C ATOM 552 NH1 ARG A 70 24.159 10.568 18.784 1.00 16.25 N ATOM 553 NH2 ARG A 70 25.016 10.217 16.680 1.00 18.14 N ATOM 554 N HIS A 71 28.782 8.527 24.721 1.00 13.52 N ATOM 555 CA HIS A 71 29.689 8.682 25.850 1.00 16.67 C ATOM 556 C HIS A 71 30.530 7.419 26.031 1.00 17.31 C ATOM 557 O HIS A 71 31.750 7.487 26.199 1.00 22.38 O ATOM 558 CB HIS A 71 28.904 8.974 27.125 1.00 13.99 C ATOM 559 CG HIS A 71 29.754 8.985 28.353 1.00 18.15 C ATOM 560 ND1 HIS A 71 30.773 9.893 28.542 1.00 19.19 N ATOM 561 CD2 HIS A 71 29.774 8.167 29.431 1.00 17.73 C ATOM 562 CE1 HIS A 71 31.389 9.633 29.681 1.00 18.15 C ATOM 563 NE2 HIS A 71 30.800 8.591 30.241 1.00 21.88 N ATOM 564 N LEU A 72 29.861 6.269 26.017 1.00 21.14 N ATOM 565 CA LEU A 72 30.529 4.976 26.151 1.00 17.46 C ATOM 566 C LEU A 72 31.444 4.720 24.950 1.00 16.31 C ATOM 567 O LEU A 72 32.557 4.215 25.109 1.00 18.77 O ATOM 568 CB LEU A 72 29.487 3.858 26.274 1.00 14.33 C ATOM 569 CG LEU A 72 29.079 3.354 27.668 1.00 18.13 C ATOM 570 CD1 LEU A 72 29.458 4.336 28.757 1.00 20.50 C ATOM 571 CD2 LEU A 72 27.586 3.061 27.692 1.00 13.42 C ATOM 572 N GLY A 73 30.986 5.098 23.757 1.00 13.56 N ATOM 573 CA GLY A 73 31.785 4.909 22.557 1.00 10.32 C ATOM 574 C GLY A 73 33.052 5.737 22.606 1.00 14.46 C ATOM 575 O GLY A 73 34.115 5.308 22.169 1.00 17.30 O ATOM 576 N ARG A 74 32.946 6.915 23.200 1.00 19.09 N ATOM 577 CA ARG A 74 34.077 7.821 23.322 1.00 22.29 C ATOM 578 C ARG A 74 35.078 7.358 24.384 1.00 22.87 C ATOM 579 O ARG A 74 36.281 7.313 24.130 1.00 23.07 O ATOM 580 CB ARG A 74 33.551 9.217 23.650 1.00 22.22 C ATOM 581 CG ARG A 74 34.495 10.364 23.359 1.00 24.79 C ATOM 582 CD ARG A 74 33.688 11.611 22.990 1.00 22.08 C ATOM 583 NE ARG A 74 32.500 11.712 23.828 1.00 20.83 N ATOM 584 CZ ARG A 74 31.296 12.067 23.399 1.00 19.72 C ATOM 585 NH1 ARG A 74 31.099 12.383 22.127 1.00 15.61 N ATOM 586 NH2 ARG A 74 30.266 12.022 24.234 1.00 13.95 N ATOM 587 N THR A 75 34.578 6.983 25.560 1.00 23.78 N ATOM 588 CA THR A 75 35.441 6.542 26.658 1.00 22.93 C ATOM 589 C THR A 75 36.019 5.137 26.492 1.00 25.60 C ATOM 590 O THR A 75 37.124 4.858 26.957 1.00 26.22 O ATOM 591 CB THR A 75 34.714 6.627 28.022 1.00 23.97 C ATOM 592 OG1 THR A 75 33.496 5.877 27.965 1.00 21.64 O ATOM 593 CG2 THR A 75 34.388 8.079 28.374 1.00 23.63 C ATOM 594 N LEU A 76 35.275 4.258 25.826 1.00 23.96 N ATOM 595 CA LEU A 76 35.714 2.880 25.608 1.00 21.23 C ATOM 596 C LEU A 76 36.415 2.637 24.270 1.00 20.61 C ATOM 597 O LEU A 76 36.886 1.531 24.008 1.00 22.38 O ATOM 598 CB LEU A 76 34.533 1.921 25.761 1.00 22.16 C ATOM 599 CG LEU A 76 34.257 1.322 27.141 1.00 25.44 C ATOM 600 CD1 LEU A 76 34.700 2.254 28.253 1.00 21.65 C ATOM 601 CD2 LEU A 76 32.779 0.986 27.255 1.00 19.89 C ATOM 602 N GLY A 77 36.477 3.663 23.426 1.00 19.21 N ATOM 603 CA GLY A 77 37.136 3.529 22.136 1.00 19.25 C ATOM 604 C GLY A 77 36.347 2.799 21.057 1.00 21.37 C ATOM 605 O GLY A 77 36.911 2.017 20.290 1.00 22.06 O ATOM 606 N LEU A 78 35.043 3.050 21.004 1.00 21.08 N ATOM 607 CA LEU A 78 34.157 2.437 20.017 1.00 20.30 C ATOM 608 C LEU A 78 33.549 3.548 19.152 1.00 21.27 C ATOM 609 O LEU A 78 32.349 3.542 18.875 1.00 20.83 O ATOM 610 CB LEU A 78 33.033 1.677 20.731 1.00 19.64 C ATOM 611 CG LEU A 78 33.385 0.763 21.909 1.00 20.25 C ATOM 612 CD1 LEU A 78 32.114 0.167 22.472 1.00 22.57 C ATOM 613 CD2 LEU A 78 34.336 -0.335 21.467 1.00 16.31 C ATOM 614 N TYR A 79 34.393 4.469 18.693 1.00 21.06 N ATOM 615 CA TYR A 79 33.939 5.612 17.899 1.00 22.29 C ATOM 616 C TYR A 79 34.769 5.849 16.627 1.00 20.37 C ATOM 617 O TYR A 79 34.968 6.994 16.214 1.00 27.12 O ATOM 618 CB TYR A 79 33.999 6.862 18.789 1.00 20.87 C ATOM 619 CG TYR A 79 32.852 7.830 18.629 1.00 18.26 C ATOM 620 CD1 TYR A 79 32.340 8.145 17.368 1.00 16.41 C ATOM 621 CD2 TYR A 79 32.280 8.442 19.746 1.00 17.98 C ATOM 622 CE1 TYR A 79 31.290 9.044 17.220 1.00 11.88 C ATOM 623 CE2 TYR A 79 31.227 9.342 19.613 1.00 14.70 C ATOM 624 CZ TYR A 79 30.737 9.636 18.348 1.00 20.42 C ATOM 625 OH TYR A 79 29.678 10.501 18.215 1.00 19.40 O ATOM 626 N GLY A 80 35.227 4.770 15.998 1.00 18.70 N ATOM 627 CA GLY A 80 36.034 4.887 14.792 1.00 16.59 C ATOM 628 C GLY A 80 37.505 5.119 15.093 1.00 19.71 C ATOM 629 O GLY A 80 37.863 5.471 16.216 1.00 22.37 O ATOM 630 N LYS A 81 38.362 4.948 14.091 1.00 25.55 N ATOM 631 CA LYS A 81 39.796 5.138 14.284 1.00 26.60 C ATOM 632 C LYS A 81 40.212 6.598 14.102 1.00 29.26 C ATOM 633 O LYS A 81 41.284 7.003 14.552 1.00 31.28 O ATOM 634 CB LYS A 81 40.596 4.233 13.342 1.00 31.07 C ATOM 635 CG LYS A 81 40.530 4.637 11.884 1.00 41.33 C ATOM 636 CD LYS A 81 41.422 3.755 11.026 1.00 48.82 C ATOM 637 CE LYS A 81 41.602 4.351 9.636 1.00 49.83 C ATOM 638 NZ LYS A 81 40.302 4.551 8.932 1.00 56.81 N ATOM 639 N ASP A 82 39.365 7.385 13.440 1.00 28.30 N ATOM 640 CA ASP A 82 39.653 8.801 13.217 1.00 25.32 C ATOM 641 C ASP A 82 38.375 9.620 13.058 1.00 22.03 C ATOM 642 O ASP A 82 37.273 9.077 13.162 1.00 28.02 O ATOM 643 CB ASP A 82 40.592 8.991 12.014 1.00 24.51 C ATOM 644 CG ASP A 82 40.061 8.359 10.727 1.00 32.40 C ATOM 645 OD1 ASP A 82 38.830 8.305 10.521 1.00 34.79 O ATOM 646 OD2 ASP A 82 40.893 7.928 9.899 1.00 39.16 O ATOM 647 N GLN A 83 38.520 10.916 12.787 1.00 21.04 N ATOM 648 CA GLN A 83 37.363 11.800 12.634 1.00 23.73 C ATOM 649 C GLN A 83 36.439 11.419 11.493 1.00 21.99 C ATOM 650 O GLN A 83 35.218 11.519 11.621 1.00 21.68 O ATOM 651 CB GLN A 83 37.800 13.254 12.480 1.00 27.64 C ATOM 652 CG GLN A 83 38.391 13.863 13.739 1.00 32.38 C ATOM 653 CD GLN A 83 38.797 15.314 13.549 1.00 39.94 C ATOM 654 OE1 GLN A 83 38.739 16.112 14.488 1.00 41.54 O ATOM 655 NE2 GLN A 83 39.201 15.667 12.330 1.00 41.00 N ATOM 656 N GLN A 84 37.017 10.983 10.379 1.00 23.16 N ATOM 657 CA GLN A 84 36.213 10.583 9.231 1.00 27.70 C ATOM 658 C GLN A 84 35.293 9.425 9.614 1.00 24.54 C ATOM 659 O GLN A 84 34.089 9.466 9.338 1.00 20.97 O ATOM 660 CB GLN A 84 37.102 10.188 8.048 1.00 36.18 C ATOM 661 CG GLN A 84 36.307 9.704 6.836 1.00 50.12 C ATOM 662 CD GLN A 84 37.162 9.503 5.597 1.00 58.08 C ATOM 663 OE1 GLN A 84 37.992 10.348 5.256 1.00 57.17 O ATOM 664 NE2 GLN A 84 36.938 8.392 4.895 1.00 62.96 N ATOM 665 N GLU A 85 35.860 8.413 10.273 1.00 21.12 N ATOM 666 CA GLU A 85 35.083 7.255 10.709 1.00 20.98 C ATOM 667 C GLU A 85 34.068 7.668 11.764 1.00 18.69 C ATOM 668 O GLU A 85 32.944 7.169 11.765 1.00 23.76 O ATOM 669 CB GLU A 85 35.984 6.148 11.258 1.00 19.30 C ATOM 670 CG GLU A 85 36.903 5.533 10.221 1.00 27.09 C ATOM 671 CD GLU A 85 37.334 4.115 10.564 1.00 31.89 C ATOM 672 OE1 GLU A 85 37.249 3.715 11.744 1.00 24.91 O ATOM 673 OE2 GLU A 85 37.768 3.393 9.641 1.00 35.97 O ATOM 674 N ALA A 86 34.461 8.591 12.644 1.00 15.73 N ATOM 675 CA ALA A 86 33.578 9.090 13.699 1.00 12.91 C ATOM 676 C ALA A 86 32.331 9.705 13.078 1.00 13.59 C ATOM 677 O ALA A 86 31.220 9.502 13.569 1.00 18.91 O ATOM 678 CB ALA A 86 34.301 10.118 14.548 1.00 8.01 C ATOM 679 N ALA A 87 32.518 10.435 11.981 1.00 14.25 N ATOM 680 CA ALA A 87 31.406 11.066 11.279 1.00 16.97 C ATOM 681 C ALA A 87 30.487 10.006 10.668 1.00 17.71 C ATOM 682 O ALA A 87 29.262 10.136 10.708 1.00 19.60 O ATOM 683 CB ALA A 87 31.933 12.003 10.194 1.00 19.44 C ATOM 684 N LEU A 88 31.083 8.946 10.124 1.00 19.06 N ATOM 685 CA LEU A 88 30.315 7.861 9.512 1.00 18.23 C ATOM 686 C LEU A 88 29.525 7.075 10.557 1.00 15.42 C ATOM 687 O LEU A 88 28.387 6.674 10.309 1.00 16.23 O ATOM 688 CB LEU A 88 31.240 6.935 8.717 1.00 18.52 C ATOM 689 CG LEU A 88 32.029 7.627 7.600 1.00 22.88 C ATOM 690 CD1 LEU A 88 32.885 6.613 6.851 1.00 22.76 C ATOM 691 CD2 LEU A 88 31.075 8.333 6.647 1.00 19.08 C ATOM 692 N VAL A 89 30.125 6.884 11.732 1.00 14.71 N ATOM 693 CA VAL A 89 29.477 6.172 12.837 1.00 14.76 C ATOM 694 C VAL A 89 28.221 6.938 13.260 1.00 12.99 C ATOM 695 O VAL A 89 27.168 6.338 13.491 1.00 13.64 O ATOM 696 CB VAL A 89 30.437 6.024 14.048 1.00 19.85 C ATOM 697 CG1 VAL A 89 29.708 5.422 15.235 1.00 18.51 C ATOM 698 CG2 VAL A 89 31.630 5.154 13.674 1.00 14.51 C ATOM 699 N ASP A 90 28.345 8.264 13.344 1.00 14.29 N ATOM 700 CA ASP A 90 27.232 9.141 13.709 1.00 11.39 C ATOM 701 C ASP A 90 26.126 9.050 12.666 1.00 11.60 C ATOM 702 O ASP A 90 24.947 8.987 13.006 1.00 11.04 O ATOM 703 CB ASP A 90 27.698 10.603 13.812 1.00 11.00 C ATOM 704 CG ASP A 90 28.359 10.920 15.140 1.00 16.99 C ATOM 705 OD1 ASP A 90 28.036 10.253 16.145 1.00 21.77 O ATOM 706 OD2 ASP A 90 29.183 11.856 15.204 1.00 16.30 O ATOM 707 N MET A 91 26.515 9.064 11.393 1.00 12.69 N ATOM 708 CA MET A 91 25.559 8.986 10.294 1.00 11.58 C ATOM 709 C MET A 91 24.767 7.687 10.358 1.00 11.44 C ATOM 710 O MET A 91 23.562 7.672 10.086 1.00 11.56 O ATOM 711 CB MET A 91 26.285 9.112 8.953 1.00 13.28 C ATOM 712 CG MET A 91 25.365 9.077 7.742 1.00 19.12 C ATOM 713 SD MET A 91 26.261 9.399 6.211 1.00 20.72 S ATOM 714 CE MET A 91 27.389 7.993 6.160 1.00 19.81 C ATOM 715 N VAL A 92 25.448 6.598 10.717 1.00 13.48 N ATOM 716 CA VAL A 92 24.790 5.297 10.848 1.00 16.12 C ATOM 717 C VAL A 92 23.827 5.340 12.037 1.00 13.38 C ATOM 718 O VAL A 92 22.655 4.994 11.902 1.00 15.39 O ATOM 719 CB VAL A 92 25.821 4.145 11.051 1.00 16.05 C ATOM 720 CG1 VAL A 92 25.096 2.839 11.354 1.00 12.02 C ATOM 721 CG2 VAL A 92 26.686 3.980 9.802 1.00 10.91 C ATOM 722 N ASN A 93 24.307 5.821 13.183 1.00 12.98 N ATOM 723 CA ASN A 93 23.479 5.900 14.382 1.00 9.74 C ATOM 724 C ASN A 93 22.250 6.778 14.203 1.00 8.46 C ATOM 725 O ASN A 93 21.165 6.419 14.666 1.00 17.18 O ATOM 726 CB ASN A 93 24.288 6.373 15.595 1.00 13.20 C ATOM 727 CG ASN A 93 23.665 5.908 16.906 1.00 19.58 C ATOM 728 OD1 ASN A 93 23.627 4.712 17.178 1.00 17.40 O ATOM 729 ND2 ASN A 93 23.154 6.841 17.703 1.00 12.48 N ATOM 730 N ASP A 94 22.415 7.919 13.535 1.00 9.64 N ATOM 731 CA ASP A 94 21.289 8.824 13.290 1.00 12.35 C ATOM 732 C ASP A 94 20.267 8.122 12.411 1.00 11.61 C ATOM 733 O ASP A 94 19.061 8.323 12.564 1.00 17.27 O ATOM 734 CB ASP A 94 21.763 10.119 12.621 1.00 16.96 C ATOM 735 CG ASP A 94 22.494 11.048 13.581 1.00 23.49 C ATOM 736 OD1 ASP A 94 22.683 10.691 14.766 1.00 19.71 O ATOM 737 OD2 ASP A 94 22.859 12.161 13.148 1.00 23.12 O ATOM 738 N GLY A 95 20.761 7.293 11.493 1.00 13.22 N ATOM 739 CA GLY A 95 19.880 6.538 10.619 1.00 10.03 C ATOM 740 C GLY A 95 19.112 5.525 11.445 1.00 11.14 C ATOM 741 O GLY A 95 17.902 5.384 11.295 1.00 7.80 O ATOM 742 N VAL A 96 19.814 4.835 12.341 1.00 12.14 N ATOM 743 CA VAL A 96 19.182 3.849 13.216 1.00 15.54 C ATOM 744 C VAL A 96 18.107 4.531 14.072 1.00 16.58 C ATOM 745 O VAL A 96 16.984 4.041 14.176 1.00 17.30 O ATOM 746 CB VAL A 96 20.220 3.177 14.144 1.00 14.32 C ATOM 747 CG1 VAL A 96 19.522 2.296 15.178 1.00 16.11 C ATOM 748 CG2 VAL A 96 21.207 2.364 13.320 1.00 11.14 C ATOM 749 N GLU A 97 18.453 5.686 14.638 1.00 18.63 N ATOM 750 CA GLU A 97 17.539 6.455 15.481 1.00 16.85 C ATOM 751 C GLU A 97 16.254 6.851 14.748 1.00 18.25 C ATOM 752 O GLU A 97 15.164 6.790 15.326 1.00 18.70 O ATOM 753 CB GLU A 97 18.257 7.692 16.042 1.00 17.30 C ATOM 754 CG GLU A 97 17.372 8.657 16.838 1.00 23.07 C ATOM 755 CD GLU A 97 16.645 8.001 18.012 1.00 25.82 C ATOM 756 OE1 GLU A 97 17.222 7.119 18.680 1.00 22.62 O ATOM 757 OE2 GLU A 97 15.485 8.377 18.267 1.00 25.38 O ATOM 758 N ASP A 98 16.381 7.249 13.481 1.00 20.78 N ATOM 759 CA ASP A 98 15.216 7.630 12.677 1.00 17.53 C ATOM 760 C ASP A 98 14.257 6.455 12.514 1.00 17.65 C ATOM 761 O ASP A 98 13.046 6.599 12.700 1.00 15.70 O ATOM 762 CB ASP A 98 15.640 8.139 11.293 1.00 23.36 C ATOM 763 CG ASP A 98 16.111 9.590 11.309 1.00 26.68 C ATOM 764 OD1 ASP A 98 15.894 10.294 12.320 1.00 29.04 O ATOM 765 OD2 ASP A 98 16.676 10.041 10.291 1.00 25.14 O ATOM 766 N LEU A 99 14.799 5.290 12.166 1.00 16.91 N ATOM 767 CA LEU A 99 13.960 4.108 12.000 1.00 19.92 C ATOM 768 C LEU A 99 13.397 3.643 13.346 1.00 13.19 C ATOM 769 O LEU A 99 12.263 3.173 13.420 1.00 18.49 O ATOM 770 CB LEU A 99 14.729 2.982 11.302 1.00 18.14 C ATOM 771 CG LEU A 99 13.939 1.700 11.014 1.00 17.66 C ATOM 772 CD1 LEU A 99 12.600 2.021 10.370 1.00 13.77 C ATOM 773 CD2 LEU A 99 14.759 0.792 10.119 1.00 16.06 C ATOM 774 N ARG A 100 14.170 3.824 14.415 1.00 14.47 N ATOM 775 CA ARG A 100 13.717 3.435 15.748 1.00 15.31 C ATOM 776 C ARG A 100 12.487 4.256 16.153 1.00 17.03 C ATOM 777 O ARG A 100 11.551 3.710 16.735 1.00 19.64 O ATOM 778 CB ARG A 100 14.836 3.593 16.786 1.00 10.73 C ATOM 779 CG ARG A 100 14.465 3.035 18.156 1.00 10.42 C ATOM 780 CD ARG A 100 15.599 3.165 19.162 1.00 11.98 C ATOM 781 NE ARG A 100 16.748 2.327 18.828 1.00 11.76 N ATOM 782 CZ ARG A 100 16.822 1.019 19.057 1.00 15.85 C ATOM 783 NH1 ARG A 100 15.807 0.373 19.621 1.00 11.89 N ATOM 784 NH2 ARG A 100 17.923 0.354 18.732 1.00 15.06 N ATOM 785 N CYS A 101 12.479 5.550 15.820 1.00 14.20 N ATOM 786 CA CYS A 101 11.343 6.417 16.136 1.00 17.83 C ATOM 787 C CYS A 101 10.089 5.953 15.421 1.00 19.55 C ATOM 788 O CYS A 101 8.996 5.993 15.985 1.00 22.33 O ATOM 789 CB CYS A 101 11.628 7.871 15.765 1.00 19.32 C ATOM 790 SG CYS A 101 12.723 8.699 16.921 1.00 32.81 S ATOM 791 N LYS A 102 10.247 5.518 14.175 1.00 19.38 N ATOM 792 CA LYS A 102 9.113 5.028 13.400 1.00 20.61 C ATOM 793 C LYS A 102 8.593 3.749 14.042 1.00 18.02 C ATOM 794 O LYS A 102 7.386 3.549 14.152 1.00 19.13 O ATOM 795 CB LYS A 102 9.528 4.764 11.956 1.00 22.86 C ATOM 796 CG LYS A 102 9.926 6.019 11.212 1.00 30.03 C ATOM 797 CD LYS A 102 10.355 5.710 9.800 1.00 32.90 C ATOM 798 CE LYS A 102 10.687 6.985 9.057 1.00 35.78 C ATOM 799 NZ LYS A 102 11.177 6.693 7.686 1.00 40.87 N ATOM 800 N TYR A 103 9.520 2.900 14.485 1.00 20.01 N ATOM 801 CA TYR A 103 9.180 1.640 15.140 1.00 21.91 C ATOM 802 C TYR A 103 8.402 1.933 16.422 1.00 22.68 C ATOM 803 O TYR A 103 7.340 1.360 16.665 1.00 21.81 O ATOM 804 CB TYR A 103 10.458 0.853 15.466 1.00 23.90 C ATOM 805 CG TYR A 103 10.249 -0.354 16.367 1.00 26.18 C ATOM 806 CD1 TYR A 103 9.838 -1.583 15.845 1.00 25.52 C ATOM 807 CD2 TYR A 103 10.462 -0.265 17.745 1.00 25.90 C ATOM 808 CE1 TYR A 103 9.645 -2.694 16.681 1.00 27.92 C ATOM 809 CE2 TYR A 103 10.273 -1.363 18.585 1.00 25.72 C ATOM 810 CZ TYR A 103 9.865 -2.573 18.050 1.00 31.25 C ATOM 811 OH TYR A 103 9.681 -3.656 18.882 1.00 22.76 O ATOM 812 N ILE A 104 8.935 2.846 17.228 1.00 23.14 N ATOM 813 CA ILE A 104 8.312 3.237 18.486 1.00 24.08 C ATOM 814 C ILE A 104 6.922 3.823 18.249 1.00 24.55 C ATOM 815 O ILE A 104 5.977 3.516 18.973 1.00 23.23 O ATOM 816 CB ILE A 104 9.210 4.239 19.250 1.00 22.12 C ATOM 817 CG1 ILE A 104 10.470 3.521 19.736 1.00 18.44 C ATOM 818 CG2 ILE A 104 8.458 4.863 20.423 1.00 18.42 C ATOM 819 CD1 ILE A 104 11.541 4.448 20.257 1.00 17.78 C ATOM 820 N SER A 105 6.796 4.638 17.208 1.00 28.06 N ATOM 821 CA SER A 105 5.517 5.246 16.876 1.00 27.79 C ATOM 822 C SER A 105 4.501 4.156 16.555 1.00 30.25 C ATOM 823 O SER A 105 3.354 4.239 16.973 1.00 30.82 O ATOM 824 CB SER A 105 5.665 6.190 15.684 1.00 28.66 C ATOM 825 OG SER A 105 4.436 6.833 15.401 1.00 34.23 O ATOM 826 N LEU A 106 4.929 3.128 15.827 1.00 27.81 N ATOM 827 CA LEU A 106 4.042 2.021 15.472 1.00 25.38 C ATOM 828 C LEU A 106 3.581 1.263 16.716 1.00 26.48 C ATOM 829 O LEU A 106 2.384 1.084 16.937 1.00 25.64 O ATOM 830 CB LEU A 106 4.752 1.049 14.524 1.00 23.69 C ATOM 831 CG LEU A 106 4.014 -0.266 14.255 1.00 24.87 C ATOM 832 CD1 LEU A 106 2.744 -0.010 13.457 1.00 22.06 C ATOM 833 CD2 LEU A 106 4.920 -1.225 13.515 1.00 21.05 C ATOM 834 N ILE A 107 4.549 0.831 17.521 1.00 25.21 N ATOM 835 CA ILE A 107 4.295 0.075 18.745 1.00 25.72 C ATOM 836 C ILE A 107 3.351 0.758 19.738 1.00 29.40 C ATOM 837 O ILE A 107 2.390 0.149 20.212 1.00 30.38 O ATOM 838 CB ILE A 107 5.625 -0.253 19.465 1.00 24.29 C ATOM 839 CG1 ILE A 107 6.497 -1.148 18.582 1.00 22.58 C ATOM 840 CG2 ILE A 107 5.364 -0.923 20.802 1.00 23.25 C ATOM 841 CD1 ILE A 107 5.864 -2.479 18.228 1.00 25.00 C ATOM 842 N TYR A 108 3.608 2.031 20.018 1.00 30.44 N ATOM 843 CA TYR A 108 2.807 2.785 20.975 1.00 30.83 C ATOM 844 C TYR A 108 1.609 3.571 20.439 1.00 30.90 C ATOM 845 O TYR A 108 0.682 3.856 21.189 1.00 34.64 O ATOM 846 CB TYR A 108 3.722 3.715 21.775 1.00 28.66 C ATOM 847 CG TYR A 108 4.720 2.979 22.647 1.00 25.90 C ATOM 848 CD1 TYR A 108 4.365 2.515 23.915 1.00 26.12 C ATOM 849 CD2 TYR A 108 6.025 2.749 22.208 1.00 24.41 C ATOM 850 CE1 TYR A 108 5.295 1.837 24.731 1.00 26.04 C ATOM 851 CE2 TYR A 108 6.956 2.076 23.008 1.00 24.30 C ATOM 852 CZ TYR A 108 6.587 1.623 24.267 1.00 26.98 C ATOM 853 OH TYR A 108 7.520 0.967 25.041 1.00 21.61 O ATOM 854 N THR A 109 1.610 3.901 19.151 1.00 38.71 N ATOM 855 CA THR A 109 0.519 4.686 18.568 1.00 37.68 C ATOM 856 C THR A 109 -0.558 3.908 17.809 1.00 40.73 C ATOM 857 O THR A 109 -1.747 4.110 18.057 1.00 45.84 O ATOM 858 CB THR A 109 1.076 5.835 17.695 1.00 38.41 C ATOM 859 OG1 THR A 109 1.792 6.750 18.533 1.00 42.97 O ATOM 860 CG2 THR A 109 -0.035 6.575 16.966 1.00 42.51 C ATOM 861 N ASN A 110 -0.163 3.025 16.896 1.00 37.79 N ATOM 862 CA ASN A 110 -1.148 2.257 16.138 1.00 38.19 C ATOM 863 C ASN A 110 -0.610 0.938 15.594 1.00 34.78 C ATOM 864 O ASN A 110 -0.471 0.748 14.385 1.00 33.68 O ATOM 865 CB ASN A 110 -1.760 3.113 15.016 1.00 40.98 C ATOM 866 CG ASN A 110 -0.760 3.483 13.932 1.00 47.50 C ATOM 867 OD1 ASN A 110 -1.130 3.620 12.768 1.00 47.36 O ATOM 868 ND2 ASN A 110 0.509 3.639 14.305 1.00 51.99 N ATOM 869 N TYR A 111 -0.326 0.020 16.510 1.00 34.51 N ATOM 870 CA TYR A 111 0.192 -1.292 16.159 1.00 34.67 C ATOM 871 C TYR A 111 -0.764 -2.088 15.271 1.00 35.97 C ATOM 872 O TYR A 111 -0.399 -2.504 14.174 1.00 36.36 O ATOM 873 CB TYR A 111 0.503 -2.084 17.431 1.00 33.29 C ATOM 874 CG TYR A 111 1.084 -3.453 17.167 1.00 36.30 C ATOM 875 CD1 TYR A 111 2.460 -3.631 17.026 1.00 35.63 C ATOM 876 CD2 TYR A 111 0.257 -4.569 17.042 1.00 35.82 C ATOM 877 CE1 TYR A 111 2.999 -4.888 16.764 1.00 38.80 C ATOM 878 CE2 TYR A 111 0.784 -5.827 16.779 1.00 42.59 C ATOM 879 CZ TYR A 111 2.156 -5.980 16.640 1.00 41.19 C ATOM 880 OH TYR A 111 2.677 -7.224 16.363 1.00 47.64 O ATOM 881 N GLU A 112 -1.989 -2.281 15.752 1.00 39.49 N ATOM 882 CA GLU A 112 -3.007 -3.045 15.032 1.00 42.50 C ATOM 883 C GLU A 112 -3.254 -2.534 13.627 1.00 41.35 C ATOM 884 O GLU A 112 -3.144 -3.283 12.656 1.00 40.61 O ATOM 885 CB GLU A 112 -4.331 -3.045 15.803 1.00 45.99 C ATOM 886 CG GLU A 112 -4.324 -3.861 17.094 1.00 54.63 C ATOM 887 CD GLU A 112 -3.417 -3.281 18.172 1.00 59.58 C ATOM 888 OE1 GLU A 112 -3.449 -2.047 18.386 1.00 58.39 O ATOM 889 OE2 GLU A 112 -2.683 -4.065 18.813 1.00 60.37 O ATOM 890 N ALA A 113 -3.564 -1.247 13.528 1.00 41.54 N ATOM 891 CA ALA A 113 -3.849 -0.616 12.250 1.00 41.20 C ATOM 892 C ALA A 113 -2.657 -0.486 11.305 1.00 42.16 C ATOM 893 O ALA A 113 -2.724 -0.928 10.161 1.00 48.91 O ATOM 894 CB ALA A 113 -4.485 0.746 12.478 1.00 37.49 C ATOM 895 N GLY A 114 -1.558 0.080 11.794 1.00 41.37 N ATOM 896 CA GLY A 114 -0.394 0.294 10.949 1.00 37.31 C ATOM 897 C GLY A 114 0.639 -0.795 10.719 1.00 37.83 C ATOM 898 O GLY A 114 1.560 -0.588 9.924 1.00 37.80 O ATOM 899 N LYS A 115 0.492 -1.949 11.366 1.00 35.61 N ATOM 900 CA LYS A 115 1.468 -3.033 11.221 1.00 36.68 C ATOM 901 C LYS A 115 1.736 -3.496 9.788 1.00 34.47 C ATOM 902 O LYS A 115 2.882 -3.750 9.422 1.00 32.43 O ATOM 903 CB LYS A 115 1.077 -4.233 12.091 1.00 36.74 C ATOM 904 CG LYS A 115 2.133 -5.332 12.151 1.00 35.81 C ATOM 905 CD LYS A 115 1.627 -6.547 12.921 1.00 43.03 C ATOM 906 CE LYS A 115 2.602 -7.713 12.839 1.00 41.39 C ATOM 907 NZ LYS A 115 3.915 -7.402 13.469 1.00 51.56 N ATOM 908 N ASP A 116 0.689 -3.584 8.975 1.00 36.82 N ATOM 909 CA ASP A 116 0.837 -4.035 7.594 1.00 40.04 C ATOM 910 C ASP A 116 1.599 -3.073 6.686 1.00 38.48 C ATOM 911 O ASP A 116 2.517 -3.485 5.975 1.00 34.17 O ATOM 912 CB ASP A 116 -0.528 -4.380 6.997 1.00 46.19 C ATOM 913 CG ASP A 116 -1.194 -5.549 7.707 1.00 52.56 C ATOM 914 OD1 ASP A 116 -0.476 -6.491 8.114 1.00 49.30 O ATOM 915 OD2 ASP A 116 -2.436 -5.529 7.847 1.00 54.99 O ATOM 916 N ASP A 117 1.230 -1.796 6.721 1.00 36.15 N ATOM 917 CA ASP A 117 1.897 -0.788 5.903 1.00 35.75 C ATOM 918 C ASP A 117 3.364 -0.656 6.285 1.00 35.68 C ATOM 919 O ASP A 117 4.231 -0.529 5.417 1.00 36.69 O ATOM 920 CB ASP A 117 1.202 0.567 6.045 1.00 39.41 C ATOM 921 CG ASP A 117 -0.170 0.596 5.394 1.00 46.88 C ATOM 922 OD1 ASP A 117 -0.525 -0.364 4.671 1.00 47.91 O ATOM 923 OD2 ASP A 117 -0.900 1.586 5.612 1.00 46.96 O ATOM 924 N TYR A 118 3.631 -0.700 7.589 1.00 31.28 N ATOM 925 CA TYR A 118 4.987 -0.593 8.117 1.00 30.67 C ATOM 926 C TYR A 118 5.884 -1.718 7.598 1.00 29.93 C ATOM 927 O TYR A 118 7.026 -1.475 7.198 1.00 28.34 O ATOM 928 CB TYR A 118 4.959 -0.608 9.653 1.00 27.14 C ATOM 929 CG TYR A 118 6.302 -0.352 10.304 1.00 26.38 C ATOM 930 CD1 TYR A 118 7.217 -1.384 10.486 1.00 19.86 C ATOM 931 CD2 TYR A 118 6.659 0.928 10.732 1.00 26.08 C ATOM 932 CE1 TYR A 118 8.453 -1.151 11.075 1.00 29.45 C ATOM 933 CE2 TYR A 118 7.891 1.172 11.324 1.00 24.22 C ATOM 934 CZ TYR A 118 8.785 0.128 11.492 1.00 25.80 C ATOM 935 OH TYR A 118 10.010 0.352 12.079 1.00 24.95 O ATOM 936 N VAL A 119 5.376 -2.948 7.625 1.00 29.06 N ATOM 937 CA VAL A 119 6.144 -4.098 7.151 1.00 33.03 C ATOM 938 C VAL A 119 6.403 -4.022 5.637 1.00 34.40 C ATOM 939 O VAL A 119 7.460 -4.445 5.164 1.00 34.05 O ATOM 940 CB VAL A 119 5.451 -5.433 7.529 1.00 30.33 C ATOM 941 CG1 VAL A 119 6.251 -6.620 7.013 1.00 29.73 C ATOM 942 CG2 VAL A 119 5.314 -5.532 9.037 1.00 31.80 C ATOM 943 N LYS A 120 5.452 -3.460 4.890 1.00 35.61 N ATOM 944 CA LYS A 120 5.590 -3.309 3.439 1.00 38.35 C ATOM 945 C LYS A 120 6.695 -2.307 3.108 1.00 35.33 C ATOM 946 O LYS A 120 7.451 -2.494 2.155 1.00 32.78 O ATOM 947 CB LYS A 120 4.279 -2.819 2.816 1.00 42.82 C ATOM 948 CG LYS A 120 3.118 -3.784 2.943 1.00 52.09 C ATOM 949 CD LYS A 120 1.806 -3.093 2.601 1.00 58.43 C ATOM 950 CE LYS A 120 0.608 -3.969 2.947 1.00 62.88 C ATOM 951 NZ LYS A 120 -0.678 -3.221 2.833 1.00 66.35 N ATOM 952 N ALA A 121 6.782 -1.247 3.910 1.00 33.79 N ATOM 953 CA ALA A 121 7.782 -0.198 3.716 1.00 30.02 C ATOM 954 C ALA A 121 9.154 -0.551 4.280 1.00 25.90 C ATOM 955 O ALA A 121 10.148 0.101 3.956 1.00 31.21 O ATOM 956 CB ALA A 121 7.291 1.108 4.326 1.00 28.93 C ATOM 957 N LEU A 122 9.210 -1.591 5.107 1.00 23.28 N ATOM 958 CA LEU A 122 10.460 -2.020 5.727 1.00 22.18 C ATOM 959 C LEU A 122 11.676 -2.186 4.810 1.00 22.91 C ATOM 960 O LEU A 122 12.755 -1.693 5.130 1.00 25.90 O ATOM 961 CB LEU A 122 10.252 -3.306 6.526 1.00 23.32 C ATOM 962 CG LEU A 122 10.454 -3.225 8.038 1.00 27.19 C ATOM 963 CD1 LEU A 122 10.569 -4.640 8.584 1.00 23.58 C ATOM 964 CD2 LEU A 122 11.711 -2.429 8.373 1.00 16.96 C ATOM 965 N PRO A 123 11.527 -2.896 3.672 1.00 22.26 N ATOM 966 CA PRO A 123 12.660 -3.094 2.756 1.00 18.74 C ATOM 967 C PRO A 123 13.358 -1.797 2.365 1.00 16.63 C ATOM 968 O PRO A 123 14.588 -1.730 2.334 1.00 17.65 O ATOM 969 CB PRO A 123 12.003 -3.767 1.553 1.00 19.28 C ATOM 970 CG PRO A 123 10.920 -4.574 2.181 1.00 19.49 C ATOM 971 CD PRO A 123 10.332 -3.600 3.176 1.00 21.84 C ATOM 972 N GLY A 124 12.568 -0.762 2.095 1.00 22.67 N ATOM 973 CA GLY A 124 13.130 0.523 1.720 1.00 19.75 C ATOM 974 C GLY A 124 13.902 1.143 2.865 1.00 20.52 C ATOM 975 O GLY A 124 14.898 1.830 2.645 1.00 22.10 O ATOM 976 N GLN A 125 13.438 0.890 4.087 1.00 20.90 N ATOM 977 CA GLN A 125 14.077 1.403 5.297 1.00 22.94 C ATOM 978 C GLN A 125 15.373 0.672 5.632 1.00 20.70 C ATOM 979 O GLN A 125 16.293 1.260 6.191 1.00 23.81 O ATOM 980 CB GLN A 125 13.127 1.286 6.491 1.00 21.63 C ATOM 981 CG GLN A 125 11.857 2.102 6.356 1.00 30.39 C ATOM 982 CD GLN A 125 12.147 3.573 6.155 1.00 35.70 C ATOM 983 OE1 GLN A 125 12.847 4.187 6.960 1.00 40.10 O ATOM 984 NE2 GLN A 125 11.607 4.148 5.093 1.00 41.34 N ATOM 985 N LEU A 126 15.438 -0.613 5.295 1.00 22.14 N ATOM 986 CA LEU A 126 16.622 -1.423 5.577 1.00 21.23 C ATOM 987 C LEU A 126 17.730 -1.341 4.530 1.00 21.20 C ATOM 988 O LEU A 126 18.905 -1.537 4.860 1.00 21.15 O ATOM 989 CB LEU A 126 16.220 -2.884 5.801 1.00 21.21 C ATOM 990 CG LEU A 126 15.309 -3.130 7.005 1.00 24.35 C ATOM 991 CD1 LEU A 126 14.871 -4.588 7.049 1.00 19.36 C ATOM 992 CD2 LEU A 126 16.036 -2.735 8.285 1.00 18.94 C ATOM 993 N LYS A 127 17.365 -1.054 3.278 1.00 22.93 N ATOM 994 CA LYS A 127 18.350 -0.955 2.193 1.00 26.44 C ATOM 995 C LYS A 127 19.580 -0.097 2.486 1.00 20.06 C ATOM 996 O LYS A 127 20.699 -0.511 2.187 1.00 22.94 O ATOM 997 CB LYS A 127 17.693 -0.504 0.886 1.00 33.61 C ATOM 998 CG LYS A 127 17.200 -1.656 0.044 1.00 47.30 C ATOM 999 CD LYS A 127 16.323 -1.193 -1.104 1.00 56.32 C ATOM 1000 CE LYS A 127 15.743 -2.395 -1.838 1.00 58.09 C ATOM 1001 NZ LYS A 127 14.710 -2.002 -2.834 1.00 63.23 N ATOM 1002 N PRO A 128 19.397 1.102 3.079 1.00 19.14 N ATOM 1003 CA PRO A 128 20.549 1.958 3.381 1.00 15.28 C ATOM 1004 C PRO A 128 21.665 1.260 4.167 1.00 18.17 C ATOM 1005 O PRO A 128 22.847 1.484 3.901 1.00 21.95 O ATOM 1006 CB PRO A 128 19.920 3.089 4.189 1.00 12.31 C ATOM 1007 CG PRO A 128 18.589 3.241 3.542 1.00 14.29 C ATOM 1008 CD PRO A 128 18.137 1.804 3.401 1.00 15.76 C ATOM 1009 N PHE A 129 21.293 0.394 5.109 1.00 13.72 N ATOM 1010 CA PHE A 129 22.279 -0.313 5.927 1.00 20.85 C ATOM 1011 C PHE A 129 22.978 -1.442 5.168 1.00 19.98 C ATOM 1012 O PHE A 129 24.153 -1.729 5.413 1.00 18.84 O ATOM 1013 CB PHE A 129 21.631 -0.804 7.226 1.00 20.05 C ATOM 1014 CG PHE A 129 20.973 0.300 8.017 1.00 20.02 C ATOM 1015 CD1 PHE A 129 21.740 1.275 8.652 1.00 22.94 C ATOM 1016 CD2 PHE A 129 19.587 0.396 8.084 1.00 22.16 C ATOM 1017 CE1 PHE A 129 21.133 2.330 9.337 1.00 19.18 C ATOM 1018 CE2 PHE A 129 18.972 1.448 8.767 1.00 18.57 C ATOM 1019 CZ PHE A 129 19.748 2.415 9.393 1.00 14.53 C ATOM 1020 N GLU A 130 22.251 -2.068 4.243 1.00 19.42 N ATOM 1021 CA GLU A 130 22.800 -3.126 3.398 1.00 18.85 C ATOM 1022 C GLU A 130 23.848 -2.466 2.493 1.00 21.85 C ATOM 1023 O GLU A 130 24.926 -3.018 2.255 1.00 20.87 O ATOM 1024 CB GLU A 130 21.680 -3.743 2.545 1.00 21.87 C ATOM 1025 CG GLU A 130 22.118 -4.851 1.575 1.00 27.47 C ATOM 1026 CD GLU A 130 22.396 -6.192 2.248 1.00 29.84 C ATOM 1027 OE1 GLU A 130 22.104 -6.336 3.453 1.00 29.88 O ATOM 1028 OE2 GLU A 130 22.898 -7.111 1.564 1.00 32.39 O ATOM 1029 N THR A 131 23.527 -1.256 2.031 1.00 22.30 N ATOM 1030 CA THR A 131 24.407 -0.468 1.167 1.00 21.34 C ATOM 1031 C THR A 131 25.690 -0.079 1.897 1.00 20.14 C ATOM 1032 O THR A 131 26.787 -0.218 1.359 1.00 19.79 O ATOM 1033 CB THR A 131 23.704 0.819 0.699 1.00 26.14 C ATOM 1034 OG1 THR A 131 22.470 0.483 0.053 1.00 25.68 O ATOM 1035 CG2 THR A 131 24.588 1.592 -0.269 1.00 23.33 C ATOM 1036 N LEU A 132 25.540 0.438 3.115 1.00 22.42 N ATOM 1037 CA LEU A 132 26.688 0.833 3.930 1.00 24.35 C ATOM 1038 C LEU A 132 27.625 -0.360 4.110 1.00 24.17 C ATOM 1039 O LEU A 132 28.840 -0.242 3.954 1.00 23.15 O ATOM 1040 CB LEU A 132 26.218 1.335 5.299 1.00 25.57 C ATOM 1041 CG LEU A 132 25.560 2.719 5.320 1.00 29.69 C ATOM 1042 CD1 LEU A 132 24.784 2.930 6.608 1.00 24.66 C ATOM 1043 CD2 LEU A 132 26.627 3.786 5.148 1.00 20.42 C ATOM 1044 N LEU A 133 27.034 -1.515 4.398 1.00 25.87 N ATOM 1045 CA LEU A 133 27.771 -2.755 4.595 1.00 23.23 C ATOM 1046 C LEU A 133 28.514 -3.154 3.316 1.00 25.78 C ATOM 1047 O LEU A 133 29.706 -3.472 3.360 1.00 18.93 O ATOM 1048 CB LEU A 133 26.793 -3.856 5.021 1.00 24.05 C ATOM 1049 CG LEU A 133 27.066 -4.681 6.283 1.00 26.72 C ATOM 1050 CD1 LEU A 133 27.859 -3.901 7.312 1.00 23.16 C ATOM 1051 CD2 LEU A 133 25.739 -5.146 6.861 1.00 24.18 C ATOM 1052 N SER A 134 27.832 -3.081 2.172 1.00 23.49 N ATOM 1053 CA SER A 134 28.447 -3.445 0.893 1.00 29.74 C ATOM 1054 C SER A 134 29.633 -2.564 0.505 1.00 30.07 C ATOM 1055 O SER A 134 30.515 -3.003 -0.237 1.00 36.18 O ATOM 1056 CB SER A 134 27.407 -3.459 -0.236 1.00 27.59 C ATOM 1057 OG SER A 134 26.940 -2.158 -0.544 1.00 32.05 O ATOM 1058 N GLN A 135 29.666 -1.334 1.013 1.00 28.62 N ATOM 1059 CA GLN A 135 30.760 -0.412 0.713 1.00 27.90 C ATOM 1060 C GLN A 135 31.928 -0.516 1.688 1.00 30.39 C ATOM 1061 O GLN A 135 32.943 0.159 1.517 1.00 31.64 O ATOM 1062 CB GLN A 135 30.241 1.019 0.685 1.00 32.68 C ATOM 1063 CG GLN A 135 29.215 1.262 -0.393 1.00 39.38 C ATOM 1064 CD GLN A 135 28.499 2.581 -0.212 1.00 45.11 C ATOM 1065 OE1 GLN A 135 28.712 3.293 0.775 1.00 46.94 O ATOM 1066 NE2 GLN A 135 27.625 2.907 -1.154 1.00 45.99 N ATOM 1067 N ASN A 136 31.780 -1.335 2.724 1.00 27.75 N ATOM 1068 CA ASN A 136 32.832 -1.515 3.709 1.00 28.91 C ATOM 1069 C ASN A 136 33.346 -2.952 3.680 1.00 29.42 C ATOM 1070 O ASN A 136 32.749 -3.841 4.281 1.00 28.45 O ATOM 1071 CB ASN A 136 32.329 -1.150 5.113 1.00 27.76 C ATOM 1072 CG ASN A 136 33.410 -1.294 6.176 1.00 28.46 C ATOM 1073 OD1 ASN A 136 34.596 -1.124 5.895 1.00 30.75 O ATOM 1074 ND2 ASN A 136 33.001 -1.620 7.393 1.00 24.24 N ATOM 1075 N GLN A 137 34.448 -3.170 2.956 1.00 36.91 N ATOM 1076 CA GLN A 137 35.068 -4.498 2.828 1.00 38.50 C ATOM 1077 C GLN A 137 34.067 -5.603 2.494 1.00 37.08 C ATOM 1078 O GLN A 137 34.145 -6.708 3.036 1.00 37.53 O ATOM 1079 CB GLN A 137 35.820 -4.858 4.109 1.00 42.36 C ATOM 1080 CG GLN A 137 37.003 -3.968 4.421 1.00 49.91 C ATOM 1081 CD GLN A 137 37.478 -4.127 5.853 1.00 59.50 C ATOM 1082 OE1 GLN A 137 38.189 -5.084 6.172 1.00 59.71 O ATOM 1083 NE2 GLN A 137 37.096 -3.193 6.717 1.00 62.55 N ATOM 1084 N GLY A 138 33.109 -5.283 1.628 1.00 34.54 N ATOM 1085 CA GLY A 138 32.106 -6.255 1.223 1.00 33.64 C ATOM 1086 C GLY A 138 31.214 -6.793 2.328 1.00 35.93 C ATOM 1087 O GLY A 138 30.678 -7.895 2.206 1.00 40.71 O ATOM 1088 N GLY A 139 31.047 -6.021 3.399 1.00 33.49 N ATOM 1089 CA GLY A 139 30.209 -6.447 4.509 1.00 33.25 C ATOM 1090 C GLY A 139 30.785 -7.588 5.326 1.00 32.97 C ATOM 1091 O GLY A 139 30.050 -8.282 6.024 1.00 35.18 O ATOM 1092 N LYS A 140 32.102 -7.761 5.266 1.00 35.47 N ATOM 1093 CA LYS A 140 32.778 -8.833 5.990 1.00 36.91 C ATOM 1094 C LYS A 140 33.083 -8.498 7.449 1.00 34.37 C ATOM 1095 O LYS A 140 33.253 -9.404 8.263 1.00 35.42 O ATOM 1096 CB LYS A 140 34.074 -9.228 5.266 1.00 39.70 C ATOM 1097 CG LYS A 140 33.871 -9.767 3.849 1.00 48.70 C ATOM 1098 CD LYS A 140 33.284 -11.175 3.843 1.00 55.06 C ATOM 1099 CE LYS A 140 34.358 -12.227 4.096 1.00 64.02 C ATOM 1100 NZ LYS A 140 33.805 -13.614 4.138 1.00 62.77 N ATOM 1101 N THR A 141 33.139 -7.207 7.778 1.00 32.83 N ATOM 1102 CA THR A 141 33.442 -6.773 9.144 1.00 31.17 C ATOM 1103 C THR A 141 32.293 -6.063 9.875 1.00 31.32 C ATOM 1104 O THR A 141 31.255 -6.671 10.135 1.00 32.43 O ATOM 1105 CB THR A 141 34.715 -5.896 9.192 1.00 28.55 C ATOM 1106 OG1 THR A 141 34.603 -4.835 8.235 1.00 28.25 O ATOM 1107 CG2 THR A 141 35.956 -6.726 8.901 1.00 31.43 C ATOM 1108 N PHE A 142 32.481 -4.782 10.200 1.00 26.40 N ATOM 1109 CA PHE A 142 31.481 -4.007 10.924 1.00 19.15 C ATOM 1110 C PHE A 142 30.814 -2.954 10.043 1.00 21.96 C ATOM 1111 O PHE A 142 31.162 -2.817 8.872 1.00 24.65 O ATOM 1112 CB PHE A 142 32.131 -3.388 12.158 1.00 19.57 C ATOM 1113 CG PHE A 142 32.807 -4.402 13.044 1.00 18.76 C ATOM 1114 CD1 PHE A 142 32.062 -5.181 13.928 1.00 20.46 C ATOM 1115 CD2 PHE A 142 34.182 -4.604 12.971 1.00 19.75 C ATOM 1116 CE1 PHE A 142 32.677 -6.150 14.720 1.00 18.82 C ATOM 1117 CE2 PHE A 142 34.807 -5.570 13.757 1.00 18.62 C ATOM 1118 CZ PHE A 142 34.053 -6.343 14.634 1.00 19.03 C ATOM 1119 N ILE A 143 29.845 -2.224 10.590 1.00 18.32 N ATOM 1120 CA ILE A 143 29.126 -1.227 9.802 1.00 19.44 C ATOM 1121 C ILE A 143 30.020 -0.086 9.302 1.00 21.45 C ATOM 1122 O ILE A 143 29.805 0.444 8.211 1.00 21.50 O ATOM 1123 CB ILE A 143 27.875 -0.687 10.560 1.00 20.67 C ATOM 1124 CG1 ILE A 143 26.946 0.047 9.593 1.00 19.72 C ATOM 1125 CG2 ILE A 143 28.281 0.224 11.719 1.00 18.85 C ATOM 1126 CD1 ILE A 143 26.301 -0.847 8.546 1.00 12.02 C ATOM 1127 N VAL A 144 31.032 0.266 10.093 1.00 21.38 N ATOM 1128 CA VAL A 144 31.981 1.325 9.743 1.00 20.03 C ATOM 1129 C VAL A 144 33.383 0.903 10.171 1.00 19.62 C ATOM 1130 O VAL A 144 33.608 0.590 11.341 1.00 21.10 O ATOM 1131 CB VAL A 144 31.644 2.669 10.449 1.00 16.54 C ATOM 1132 CG1 VAL A 144 32.764 3.681 10.217 1.00 16.44 C ATOM 1133 CG2 VAL A 144 30.329 3.228 9.931 1.00 16.31 C ATOM 1134 N GLY A 145 34.316 0.884 9.223 1.00 18.27 N ATOM 1135 CA GLY A 145 35.686 0.504 9.534 1.00 19.01 C ATOM 1136 C GLY A 145 35.887 -0.978 9.801 1.00 25.00 C ATOM 1137 O GLY A 145 35.046 -1.803 9.438 1.00 24.24 O ATOM 1138 N ASP A 146 36.995 -1.316 10.456 1.00 27.91 N ATOM 1139 CA ASP A 146 37.312 -2.709 10.761 1.00 34.30 C ATOM 1140 C ASP A 146 37.306 -3.027 12.257 1.00 35.84 C ATOM 1141 O ASP A 146 37.840 -4.051 12.687 1.00 35.68 O ATOM 1142 CB ASP A 146 38.657 -3.102 10.132 1.00 42.87 C ATOM 1143 CG ASP A 146 39.828 -2.277 10.659 1.00 52.43 C ATOM 1144 OD1 ASP A 146 39.608 -1.262 11.360 1.00 54.33 O ATOM 1145 OD2 ASP A 146 40.984 -2.651 10.357 1.00 57.94 O ATOM 1146 N GLN A 147 36.707 -2.136 13.042 1.00 34.42 N ATOM 1147 CA GLN A 147 36.601 -2.303 14.488 1.00 30.30 C ATOM 1148 C GLN A 147 35.160 -1.956 14.863 1.00 30.17 C ATOM 1149 O GLN A 147 34.537 -1.092 14.236 1.00 28.56 O ATOM 1150 CB GLN A 147 37.592 -1.388 15.220 1.00 33.96 C ATOM 1151 CG GLN A 147 37.435 0.091 14.880 1.00 50.43 C ATOM 1152 CD GLN A 147 38.307 0.998 15.731 1.00 55.59 C ATOM 1153 OE1 GLN A 147 39.418 1.354 15.340 1.00 58.58 O ATOM 1154 NE2 GLN A 147 37.796 1.390 16.897 1.00 54.63 N ATOM 1155 N ILE A 148 34.617 -2.658 15.855 1.00 25.06 N ATOM 1156 CA ILE A 148 33.241 -2.435 16.296 1.00 19.11 C ATOM 1157 C ILE A 148 33.045 -1.043 16.919 1.00 18.93 C ATOM 1158 O ILE A 148 33.955 -0.495 17.541 1.00 17.85 O ATOM 1159 CB ILE A 148 32.792 -3.554 17.276 1.00 15.67 C ATOM 1160 CG1 ILE A 148 31.267 -3.653 17.308 1.00 18.87 C ATOM 1161 CG2 ILE A 148 33.347 -3.305 18.673 1.00 14.46 C ATOM 1162 CD1 ILE A 148 30.755 -4.966 17.868 1.00 13.44 C ATOM 1163 N SER A 149 31.867 -0.463 16.710 1.00 14.56 N ATOM 1164 CA SER A 149 31.556 0.859 17.245 1.00 15.61 C ATOM 1165 C SER A 149 30.213 0.784 17.956 1.00 12.88 C ATOM 1166 O SER A 149 29.525 -0.232 17.867 1.00 12.22 O ATOM 1167 CB SER A 149 31.488 1.894 16.116 1.00 10.55 C ATOM 1168 OG SER A 149 30.349 1.690 15.295 1.00 13.07 O ATOM 1169 N PHE A 150 29.833 1.860 18.645 1.00 14.89 N ATOM 1170 CA PHE A 150 28.557 1.881 19.357 1.00 15.23 C ATOM 1171 C PHE A 150 27.379 1.783 18.396 1.00 9.66 C ATOM 1172 O PHE A 150 26.310 1.299 18.765 1.00 19.65 O ATOM 1173 CB PHE A 150 28.435 3.119 20.270 1.00 14.25 C ATOM 1174 CG PHE A 150 28.325 4.432 19.531 1.00 8.22 C ATOM 1175 CD1 PHE A 150 27.084 4.915 19.129 1.00 2.64 C ATOM 1176 CD2 PHE A 150 29.461 5.184 19.246 1.00 6.27 C ATOM 1177 CE1 PHE A 150 26.974 6.130 18.449 1.00 11.07 C ATOM 1178 CE2 PHE A 150 29.363 6.401 18.566 1.00 10.05 C ATOM 1179 CZ PHE A 150 28.115 6.875 18.167 1.00 7.03 C ATOM 1180 N ALA A 151 27.588 2.222 17.156 1.00 16.82 N ATOM 1181 CA ALA A 151 26.545 2.170 16.130 1.00 17.83 C ATOM 1182 C ALA A 151 26.207 0.716 15.793 1.00 13.16 C ATOM 1183 O ALA A 151 25.063 0.395 15.466 1.00 11.09 O ATOM 1184 CB ALA A 151 26.991 2.923 14.873 1.00 17.78 C ATOM 1185 N ASP A 152 27.206 -0.157 15.888 1.00 8.88 N ATOM 1186 CA ASP A 152 27.009 -1.575 15.618 1.00 15.04 C ATOM 1187 C ASP A 152 26.000 -2.181 16.578 1.00 17.03 C ATOM 1188 O ASP A 152 25.059 -2.856 16.148 1.00 15.36 O ATOM 1189 CB ASP A 152 28.335 -2.330 15.726 1.00 16.98 C ATOM 1190 CG ASP A 152 29.198 -2.166 14.497 1.00 16.02 C ATOM 1191 OD1 ASP A 152 28.763 -2.584 13.411 1.00 16.20 O ATOM 1192 OD2 ASP A 152 30.310 -1.622 14.614 1.00 19.68 O ATOM 1193 N TYR A 153 26.177 -1.910 17.873 1.00 16.69 N ATOM 1194 CA TYR A 153 25.273 -2.436 18.901 1.00 14.36 C ATOM 1195 C TYR A 153 23.861 -1.912 18.711 1.00 13.55 C ATOM 1196 O TYR A 153 22.898 -2.654 18.843 1.00 12.86 O ATOM 1197 CB TYR A 153 25.778 -2.085 20.309 1.00 12.46 C ATOM 1198 CG TYR A 153 27.110 -2.701 20.625 1.00 8.60 C ATOM 1199 CD1 TYR A 153 27.225 -4.070 20.886 1.00 12.19 C ATOM 1200 CD2 TYR A 153 28.269 -1.929 20.612 1.00 12.86 C ATOM 1201 CE1 TYR A 153 28.472 -4.652 21.122 1.00 6.65 C ATOM 1202 CE2 TYR A 153 29.514 -2.500 20.844 1.00 9.42 C ATOM 1203 CZ TYR A 153 29.607 -3.859 21.097 1.00 9.97 C ATOM 1204 OH TYR A 153 30.840 -4.419 21.320 1.00 15.89 O ATOM 1205 N ASN A 154 23.740 -0.634 18.361 1.00 14.34 N ATOM 1206 CA ASN A 154 22.441 -0.022 18.163 1.00 10.38 C ATOM 1207 C ASN A 154 21.757 -0.575 16.909 1.00 11.97 C ATOM 1208 O ASN A 154 20.550 -0.830 16.913 1.00 16.19 O ATOM 1209 CB ASN A 154 22.570 1.500 18.093 1.00 9.39 C ATOM 1210 CG ASN A 154 21.255 2.204 18.378 1.00 14.97 C ATOM 1211 OD1 ASN A 154 20.266 1.567 18.750 1.00 13.26 O ATOM 1212 ND2 ASN A 154 21.250 3.517 18.239 1.00 16.92 N ATOM 1213 N LEU A 155 22.531 -0.765 15.844 1.00 19.22 N ATOM 1214 CA LEU A 155 21.980 -1.296 14.597 1.00 14.98 C ATOM 1215 C LEU A 155 21.551 -2.744 14.831 1.00 15.25 C ATOM 1216 O LEU A 155 20.461 -3.144 14.420 1.00 12.96 O ATOM 1217 CB LEU A 155 23.015 -1.219 13.467 1.00 14.29 C ATOM 1218 CG LEU A 155 22.609 -1.888 12.144 1.00 11.29 C ATOM 1219 CD1 LEU A 155 21.292 -1.328 11.634 1.00 11.27 C ATOM 1220 CD2 LEU A 155 23.708 -1.695 11.117 1.00 11.69 C ATOM 1221 N LEU A 156 22.394 -3.507 15.529 1.00 11.39 N ATOM 1222 CA LEU A 156 22.099 -4.907 15.840 1.00 15.34 C ATOM 1223 C LEU A 156 20.770 -5.011 16.575 1.00 16.71 C ATOM 1224 O LEU A 156 19.918 -5.822 16.208 1.00 15.34 O ATOM 1225 CB LEU A 156 23.206 -5.517 16.699 1.00 15.98 C ATOM 1226 CG LEU A 156 23.016 -6.998 17.041 1.00 20.69 C ATOM 1227 CD1 LEU A 156 22.962 -7.831 15.764 1.00 16.39 C ATOM 1228 CD2 LEU A 156 24.150 -7.473 17.933 1.00 17.86 C ATOM 1229 N ASP A 157 20.591 -4.182 17.605 1.00 14.16 N ATOM 1230 CA ASP A 157 19.346 -4.187 18.362 1.00 12.86 C ATOM 1231 C ASP A 157 18.166 -3.885 17.443 1.00 15.32 C ATOM 1232 O ASP A 157 17.145 -4.577 17.482 1.00 17.32 O ATOM 1233 CB ASP A 157 19.381 -3.161 19.500 1.00 15.85 C ATOM 1234 CG ASP A 157 18.058 -3.075 20.232 1.00 17.29 C ATOM 1235 OD1 ASP A 157 17.627 -4.101 20.788 1.00 18.97 O ATOM 1236 OD2 ASP A 157 17.401 -2.015 20.187 1.00 21.13 O ATOM 1237 N LEU A 158 18.311 -2.853 16.615 1.00 17.19 N ATOM 1238 CA LEU A 158 17.254 -2.470 15.687 1.00 16.57 C ATOM 1239 C LEU A 158 16.878 -3.653 14.781 1.00 16.21 C ATOM 1240 O LEU A 158 15.698 -3.948 14.591 1.00 16.75 O ATOM 1241 CB LEU A 158 17.690 -1.268 14.840 1.00 18.13 C ATOM 1242 CG LEU A 158 16.608 -0.654 13.942 1.00 17.58 C ATOM 1243 CD1 LEU A 158 15.533 0.000 14.795 1.00 16.39 C ATOM 1244 CD2 LEU A 158 17.224 0.367 13.005 1.00 20.43 C ATOM 1245 N LEU A 159 17.882 -4.359 14.271 1.00 15.78 N ATOM 1246 CA LEU A 159 17.638 -5.507 13.394 1.00 16.75 C ATOM 1247 C LEU A 159 16.930 -6.650 14.124 1.00 17.74 C ATOM 1248 O LEU A 159 15.953 -7.204 13.618 1.00 18.77 O ATOM 1249 CB LEU A 159 18.955 -5.991 12.774 1.00 10.89 C ATOM 1250 CG LEU A 159 19.658 -4.948 11.901 1.00 13.04 C ATOM 1251 CD1 LEU A 159 21.008 -5.451 11.432 1.00 13.47 C ATOM 1252 CD2 LEU A 159 18.776 -4.591 10.721 1.00 12.50 C ATOM 1253 N LEU A 160 17.400 -6.968 15.330 1.00 21.94 N ATOM 1254 CA LEU A 160 16.811 -8.035 16.136 1.00 18.20 C ATOM 1255 C LEU A 160 15.341 -7.806 16.466 1.00 15.43 C ATOM 1256 O LEU A 160 14.534 -8.729 16.347 1.00 18.09 O ATOM 1257 CB LEU A 160 17.607 -8.239 17.430 1.00 13.38 C ATOM 1258 CG LEU A 160 19.042 -8.755 17.277 1.00 12.46 C ATOM 1259 CD1 LEU A 160 19.712 -8.790 18.626 1.00 11.30 C ATOM 1260 CD2 LEU A 160 19.050 -10.140 16.648 1.00 13.65 C ATOM 1261 N ILE A 161 14.978 -6.586 16.863 1.00 16.94 N ATOM 1262 CA ILE A 161 13.579 -6.313 17.201 1.00 16.79 C ATOM 1263 C ILE A 161 12.678 -6.332 15.971 1.00 20.31 C ATOM 1264 O ILE A 161 11.464 -6.527 16.090 1.00 18.59 O ATOM 1265 CB ILE A 161 13.388 -4.988 17.990 1.00 18.55 C ATOM 1266 CG1 ILE A 161 13.787 -3.775 17.144 1.00 17.34 C ATOM 1267 CG2 ILE A 161 14.181 -5.037 19.285 1.00 17.38 C ATOM 1268 CD1 ILE A 161 13.656 -2.450 17.877 1.00 17.09 C ATOM 1269 N HIS A 162 13.264 -6.118 14.793 1.00 20.06 N ATOM 1270 CA HIS A 162 12.488 -6.155 13.556 1.00 21.37 C ATOM 1271 C HIS A 162 12.280 -7.595 13.104 1.00 23.90 C ATOM 1272 O HIS A 162 11.306 -7.896 12.420 1.00 25.36 O ATOM 1273 CB HIS A 162 13.137 -5.315 12.459 1.00 21.13 C ATOM 1274 CG HIS A 162 12.784 -3.864 12.537 1.00 19.46 C ATOM 1275 ND1 HIS A 162 13.518 -2.955 13.265 1.00 17.03 N ATOM 1276 CD2 HIS A 162 11.745 -3.170 12.012 1.00 17.18 C ATOM 1277 CE1 HIS A 162 12.948 -1.765 13.191 1.00 19.49 C ATOM 1278 NE2 HIS A 162 11.871 -1.872 12.435 1.00 16.66 N ATOM 1279 N GLU A 163 13.209 -8.473 13.480 1.00 22.19 N ATOM 1280 CA GLU A 163 13.102 -9.892 13.166 1.00 25.77 C ATOM 1281 C GLU A 163 11.895 -10.415 13.937 1.00 25.49 C ATOM 1282 O GLU A 163 11.157 -11.269 13.452 1.00 29.64 O ATOM 1283 CB GLU A 163 14.359 -10.638 13.620 1.00 31.23 C ATOM 1284 CG GLU A 163 15.385 -10.879 12.527 1.00 41.95 C ATOM 1285 CD GLU A 163 14.896 -11.866 11.476 1.00 54.94 C ATOM 1286 OE1 GLU A 163 14.238 -12.862 11.851 1.00 58.13 O ATOM 1287 OE2 GLU A 163 15.162 -11.646 10.272 1.00 59.34 O ATOM 1288 N VAL A 164 11.693 -9.871 15.134 1.00 22.87 N ATOM 1289 CA VAL A 164 10.575 -10.255 15.984 1.00 20.92 C ATOM 1290 C VAL A 164 9.273 -9.677 15.424 1.00 28.41 C ATOM 1291 O VAL A 164 8.242 -10.350 15.417 1.00 29.35 O ATOM 1292 CB VAL A 164 10.775 -9.754 17.440 1.00 19.90 C ATOM 1293 CG1 VAL A 164 9.558 -10.094 18.297 1.00 16.40 C ATOM 1294 CG2 VAL A 164 12.035 -10.365 18.041 1.00 14.12 C ATOM 1295 N LEU A 165 9.330 -8.435 14.946 1.00 27.12 N ATOM 1296 CA LEU A 165 8.154 -7.767 14.389 1.00 26.84 C ATOM 1297 C LEU A 165 7.706 -8.388 13.066 1.00 30.90 C ATOM 1298 O LEU A 165 6.535 -8.718 12.887 1.00 30.74 O ATOM 1299 CB LEU A 165 8.443 -6.278 14.180 1.00 26.41 C ATOM 1300 CG LEU A 165 7.319 -5.438 13.569 1.00 26.41 C ATOM 1301 CD1 LEU A 165 6.193 -5.259 14.570 1.00 25.87 C ATOM 1302 CD2 LEU A 165 7.861 -4.090 13.140 1.00 27.12 C ATOM 1303 N ALA A 166 8.649 -8.520 12.142 1.00 31.46 N ATOM 1304 CA ALA A 166 8.392 -9.085 10.823 1.00 30.90 C ATOM 1305 C ALA A 166 9.403 -10.199 10.566 1.00 28.84 C ATOM 1306 O ALA A 166 10.457 -9.967 9.973 1.00 26.85 O ATOM 1307 CB ALA A 166 8.519 -7.999 9.758 1.00 24.89 C ATOM 1308 N PRO A 167 9.104 -11.420 11.045 1.00 28.75 N ATOM 1309 CA PRO A 167 9.986 -12.581 10.873 1.00 28.20 C ATOM 1310 C PRO A 167 10.393 -12.789 9.417 1.00 27.27 C ATOM 1311 O PRO A 167 9.550 -12.802 8.519 1.00 31.49 O ATOM 1312 CB PRO A 167 9.124 -13.733 11.389 1.00 28.10 C ATOM 1313 CG PRO A 167 8.316 -13.082 12.462 1.00 26.81 C ATOM 1314 CD PRO A 167 7.894 -11.792 11.798 1.00 26.71 C ATOM 1315 N GLY A 168 11.696 -12.906 9.190 1.00 26.50 N ATOM 1316 CA GLY A 168 12.200 -13.110 7.847 1.00 25.10 C ATOM 1317 C GLY A 168 12.401 -11.847 7.030 1.00 30.53 C ATOM 1318 O GLY A 168 12.748 -11.929 5.855 1.00 29.45 O ATOM 1319 N CYS A 169 12.193 -10.679 7.636 1.00 29.85 N ATOM 1320 CA CYS A 169 12.371 -9.410 6.925 1.00 29.39 C ATOM 1321 C CYS A 169 13.805 -9.218 6.419 1.00 25.88 C ATOM 1322 O CYS A 169 14.038 -8.450 5.489 1.00 33.52 O ATOM 1323 CB CYS A 169 11.966 -8.223 7.813 1.00 30.10 C ATOM 1324 SG CYS A 169 12.993 -7.986 9.287 1.00 22.23 S ATOM 1325 N LEU A 170 14.758 -9.917 7.035 1.00 27.50 N ATOM 1326 CA LEU A 170 16.168 -9.838 6.645 1.00 25.42 C ATOM 1327 C LEU A 170 16.587 -10.837 5.561 1.00 27.18 C ATOM 1328 O LEU A 170 17.747 -10.845 5.142 1.00 24.27 O ATOM 1329 CB LEU A 170 17.069 -10.023 7.868 1.00 24.92 C ATOM 1330 CG LEU A 170 17.552 -8.773 8.608 1.00 29.22 C ATOM 1331 CD1 LEU A 170 16.385 -7.864 8.965 1.00 26.39 C ATOM 1332 CD2 LEU A 170 18.319 -9.194 9.853 1.00 25.70 C ATOM 1333 N ASP A 171 15.654 -11.679 5.119 1.00 29.82 N ATOM 1334 CA ASP A 171 15.938 -12.684 4.091 1.00 30.23 C ATOM 1335 C ASP A 171 16.437 -12.059 2.796 1.00 29.49 C ATOM 1336 O ASP A 171 17.368 -12.568 2.170 1.00 30.95 O ATOM 1337 CB ASP A 171 14.692 -13.525 3.797 1.00 31.47 C ATOM 1338 CG ASP A 171 14.366 -14.510 4.906 1.00 34.37 C ATOM 1339 OD1 ASP A 171 15.242 -14.771 5.762 1.00 36.67 O ATOM 1340 OD2 ASP A 171 13.229 -15.034 4.910 1.00 30.92 O ATOM 1341 N ALA A 172 15.827 -10.941 2.416 1.00 28.00 N ATOM 1342 CA ALA A 172 16.192 -10.225 1.198 1.00 27.15 C ATOM 1343 C ALA A 172 17.515 -9.465 1.289 1.00 25.27 C ATOM 1344 O ALA A 172 17.976 -8.899 0.298 1.00 29.11 O ATOM 1345 CB ALA A 172 15.073 -9.267 0.816 1.00 30.36 C ATOM 1346 N PHE A 173 18.133 -9.461 2.469 1.00 25.07 N ATOM 1347 CA PHE A 173 19.388 -8.742 2.672 1.00 20.75 C ATOM 1348 C PHE A 173 20.503 -9.646 3.186 1.00 25.58 C ATOM 1349 O PHE A 173 20.754 -9.716 4.389 1.00 30.09 O ATOM 1350 CB PHE A 173 19.161 -7.575 3.639 1.00 20.04 C ATOM 1351 CG PHE A 173 18.082 -6.626 3.198 1.00 21.17 C ATOM 1352 CD1 PHE A 173 18.353 -5.626 2.270 1.00 22.04 C ATOM 1353 CD2 PHE A 173 16.783 -6.759 3.681 1.00 20.44 C ATOM 1354 CE1 PHE A 173 17.346 -4.768 1.829 1.00 20.70 C ATOM 1355 CE2 PHE A 173 15.767 -5.907 3.247 1.00 24.35 C ATOM 1356 CZ PHE A 173 16.050 -4.911 2.317 1.00 22.90 C ATOM 1357 N PRO A 174 21.226 -10.308 2.266 1.00 26.61 N ATOM 1358 CA PRO A 174 22.326 -11.221 2.597 1.00 24.56 C ATOM 1359 C PRO A 174 23.421 -10.678 3.514 1.00 23.65 C ATOM 1360 O PRO A 174 23.911 -11.401 4.380 1.00 27.88 O ATOM 1361 CB PRO A 174 22.867 -11.624 1.221 1.00 23.89 C ATOM 1362 CG PRO A 174 22.428 -10.507 0.318 1.00 25.80 C ATOM 1363 CD PRO A 174 21.052 -10.214 0.808 1.00 25.20 C ATOM 1364 N LEU A 175 23.812 -9.421 3.320 1.00 24.36 N ATOM 1365 CA LEU A 175 24.853 -8.810 4.147 1.00 21.66 C ATOM 1366 C LEU A 175 24.374 -8.521 5.573 1.00 22.29 C ATOM 1367 O LEU A 175 25.099 -8.764 6.536 1.00 14.38 O ATOM 1368 CB LEU A 175 25.387 -7.538 3.486 1.00 23.93 C ATOM 1369 CG LEU A 175 26.597 -7.654 2.549 1.00 25.32 C ATOM 1370 CD1 LEU A 175 26.691 -9.025 1.906 1.00 24.32 C ATOM 1371 CD2 LEU A 175 26.524 -6.570 1.501 1.00 20.24 C ATOM 1372 N LEU A 176 23.151 -8.015 5.706 1.00 19.43 N ATOM 1373 CA LEU A 176 22.601 -7.726 7.025 1.00 20.80 C ATOM 1374 C LEU A 176 22.419 -9.024 7.810 1.00 26.52 C ATOM 1375 O LEU A 176 22.737 -9.080 8.997 1.00 26.72 O ATOM 1376 CB LEU A 176 21.270 -6.976 6.917 1.00 15.04 C ATOM 1377 CG LEU A 176 21.346 -5.504 6.497 1.00 15.49 C ATOM 1378 CD1 LEU A 176 19.948 -4.931 6.360 1.00 16.94 C ATOM 1379 CD2 LEU A 176 22.152 -4.707 7.510 1.00 19.22 C ATOM 1380 N SER A 177 21.942 -10.070 7.134 1.00 22.83 N ATOM 1381 CA SER A 177 21.735 -11.376 7.763 1.00 21.26 C ATOM 1382 C SER A 177 23.046 -11.955 8.289 1.00 23.19 C ATOM 1383 O SER A 177 23.110 -12.438 9.423 1.00 21.54 O ATOM 1384 CB SER A 177 21.107 -12.356 6.773 1.00 23.24 C ATOM 1385 OG SER A 177 19.812 -11.933 6.397 1.00 22.38 O ATOM 1386 N ALA A 178 24.087 -11.909 7.462 1.00 10.68 N ATOM 1387 CA ALA A 178 25.392 -12.423 7.865 1.00 15.92 C ATOM 1388 C ALA A 178 25.938 -11.572 9.010 1.00 22.27 C ATOM 1389 O ALA A 178 26.549 -12.088 9.946 1.00 25.04 O ATOM 1390 CB ALA A 178 26.355 -12.398 6.684 1.00 8.34 C ATOM 1391 N TYR A 179 25.713 -10.262 8.912 1.00 27.13 N ATOM 1392 CA TYR A 179 26.153 -9.289 9.909 1.00 22.12 C ATOM 1393 C TYR A 179 25.547 -9.630 11.271 1.00 17.98 C ATOM 1394 O TYR A 179 26.266 -9.713 12.269 1.00 21.41 O ATOM 1395 CB TYR A 179 25.733 -7.889 9.447 1.00 21.29 C ATOM 1396 CG TYR A 179 25.950 -6.759 10.430 1.00 17.70 C ATOM 1397 CD1 TYR A 179 27.218 -6.215 10.639 1.00 16.63 C ATOM 1398 CD2 TYR A 179 24.871 -6.191 11.106 1.00 19.36 C ATOM 1399 CE1 TYR A 179 27.401 -5.124 11.495 1.00 18.66 C ATOM 1400 CE2 TYR A 179 25.043 -5.108 11.961 1.00 17.79 C ATOM 1401 CZ TYR A 179 26.306 -4.578 12.151 1.00 19.82 C ATOM 1402 OH TYR A 179 26.461 -3.498 12.990 1.00 20.41 O ATOM 1403 N VAL A 180 24.236 -9.866 11.291 1.00 13.07 N ATOM 1404 CA VAL A 180 23.515 -10.225 12.511 1.00 19.19 C ATOM 1405 C VAL A 180 24.049 -11.533 13.104 1.00 24.64 C ATOM 1406 O VAL A 180 24.326 -11.605 14.299 1.00 27.93 O ATOM 1407 CB VAL A 180 21.992 -10.363 12.249 1.00 18.03 C ATOM 1408 CG1 VAL A 180 21.289 -10.990 13.449 1.00 19.19 C ATOM 1409 CG2 VAL A 180 21.395 -9.008 11.960 1.00 18.40 C ATOM 1410 N GLY A 181 24.214 -12.554 12.263 1.00 26.02 N ATOM 1411 CA GLY A 181 24.720 -13.831 12.737 1.00 17.35 C ATOM 1412 C GLY A 181 26.131 -13.720 13.288 1.00 22.26 C ATOM 1413 O GLY A 181 26.453 -14.290 14.331 1.00 22.16 O ATOM 1414 N ARG A 182 26.963 -12.951 12.596 1.00 17.36 N ATOM 1415 CA ARG A 182 28.350 -12.743 12.981 1.00 19.45 C ATOM 1416 C ARG A 182 28.482 -12.033 14.334 1.00 24.92 C ATOM 1417 O ARG A 182 29.239 -12.474 15.204 1.00 25.69 O ATOM 1418 CB ARG A 182 29.061 -11.936 11.895 1.00 17.30 C ATOM 1419 CG ARG A 182 30.575 -11.862 12.029 1.00 20.82 C ATOM 1420 CD ARG A 182 31.154 -10.905 10.993 1.00 22.91 C ATOM 1421 NE ARG A 182 30.577 -11.137 9.675 1.00 30.38 N ATOM 1422 CZ ARG A 182 29.982 -10.204 8.938 1.00 32.33 C ATOM 1423 NH1 ARG A 182 29.886 -8.954 9.369 1.00 29.87 N ATOM 1424 NH2 ARG A 182 29.424 -10.540 7.786 1.00 33.52 N ATOM 1425 N LEU A 183 27.754 -10.931 14.507 1.00 25.45 N ATOM 1426 CA LEU A 183 27.813 -10.182 15.762 1.00 25.98 C ATOM 1427 C LEU A 183 27.200 -10.962 16.926 1.00 27.07 C ATOM 1428 O LEU A 183 27.736 -10.949 18.032 1.00 26.87 O ATOM 1429 CB LEU A 183 27.141 -8.813 15.621 1.00 22.10 C ATOM 1430 CG LEU A 183 27.844 -7.758 14.758 1.00 24.72 C ATOM 1431 CD1 LEU A 183 27.252 -6.391 15.057 1.00 24.76 C ATOM 1432 CD2 LEU A 183 29.336 -7.732 15.045 1.00 25.15 C ATOM 1433 N SER A 184 26.090 -11.650 16.661 1.00 26.24 N ATOM 1434 CA SER A 184 25.405 -12.458 17.666 1.00 24.33 C ATOM 1435 C SER A 184 26.284 -13.607 18.155 1.00 29.02 C ATOM 1436 O SER A 184 25.998 -14.209 19.194 1.00 33.54 O ATOM 1437 CB SER A 184 24.118 -13.055 17.089 1.00 20.98 C ATOM 1438 OG SER A 184 23.195 -12.052 16.720 1.00 28.40 O ATOM 1439 N ALA A 185 27.334 -13.917 17.395 1.00 24.81 N ATOM 1440 CA ALA A 185 28.244 -15.008 17.733 1.00 27.24 C ATOM 1441 C ALA A 185 29.406 -14.603 18.636 1.00 27.33 C ATOM 1442 O ALA A 185 30.141 -15.462 19.126 1.00 31.32 O ATOM 1443 CB ALA A 185 28.772 -15.663 16.461 1.00 26.67 C ATOM 1444 N ARG A 186 29.591 -13.302 18.841 1.00 26.43 N ATOM 1445 CA ARG A 186 30.670 -12.824 19.702 1.00 21.21 C ATOM 1446 C ARG A 186 30.437 -13.421 21.092 1.00 24.23 C ATOM 1447 O ARG A 186 29.338 -13.329 21.632 1.00 20.12 O ATOM 1448 CB ARG A 186 30.678 -11.294 19.734 1.00 17.88 C ATOM 1449 CG ARG A 186 30.950 -10.678 18.362 1.00 22.26 C ATOM 1450 CD ARG A 186 30.751 -9.165 18.340 1.00 18.35 C ATOM 1451 NE ARG A 186 31.630 -8.475 19.278 1.00 13.60 N ATOM 1452 CZ ARG A 186 32.867 -8.070 19.000 1.00 16.80 C ATOM 1453 NH1 ARG A 186 33.390 -8.268 17.797 1.00 14.21 N ATOM 1454 NH2 ARG A 186 33.580 -7.452 19.929 1.00 12.32 N ATOM 1455 N PRO A 187 31.467 -14.067 21.668 1.00 24.49 N ATOM 1456 CA PRO A 187 31.462 -14.723 22.984 1.00 25.34 C ATOM 1457 C PRO A 187 30.621 -14.082 24.097 1.00 25.65 C ATOM 1458 O PRO A 187 29.605 -14.650 24.519 1.00 21.08 O ATOM 1459 CB PRO A 187 32.944 -14.761 23.339 1.00 26.35 C ATOM 1460 CG PRO A 187 33.573 -15.001 22.018 1.00 27.47 C ATOM 1461 CD PRO A 187 32.836 -14.028 21.121 1.00 23.82 C ATOM 1462 N LYS A 188 31.047 -12.910 24.567 1.00 24.65 N ATOM 1463 CA LYS A 188 30.346 -12.198 25.636 1.00 23.53 C ATOM 1464 C LYS A 188 28.930 -11.764 25.267 1.00 22.47 C ATOM 1465 O LYS A 188 28.028 -11.812 26.105 1.00 27.00 O ATOM 1466 CB LYS A 188 31.165 -10.994 26.095 1.00 23.44 C ATOM 1467 CG LYS A 188 32.523 -11.372 26.653 1.00 25.87 C ATOM 1468 CD LYS A 188 33.392 -10.154 26.897 1.00 36.57 C ATOM 1469 CE LYS A 188 34.796 -10.565 27.302 1.00 42.81 C ATOM 1470 NZ LYS A 188 34.766 -11.441 28.509 1.00 55.19 N ATOM 1471 N LEU A 189 28.733 -11.367 24.012 1.00 24.60 N ATOM 1472 CA LEU A 189 27.420 -10.930 23.537 1.00 21.70 C ATOM 1473 C LEU A 189 26.445 -12.096 23.449 1.00 20.13 C ATOM 1474 O LEU A 189 25.268 -11.956 23.786 1.00 25.43 O ATOM 1475 CB LEU A 189 27.535 -10.271 22.160 1.00 23.48 C ATOM 1476 CG LEU A 189 26.811 -8.942 21.938 1.00 24.03 C ATOM 1477 CD1 LEU A 189 26.780 -8.646 20.451 1.00 23.32 C ATOM 1478 CD2 LEU A 189 25.402 -8.982 22.493 1.00 22.64 C ATOM 1479 N LYS A 190 26.941 -13.238 22.976 1.00 19.82 N ATOM 1480 CA LYS A 190 26.128 -14.445 22.838 1.00 23.37 C ATOM 1481 C LYS A 190 25.623 -14.899 24.203 1.00 19.46 C ATOM 1482 O LYS A 190 24.449 -15.241 24.355 1.00 20.67 O ATOM 1483 CB LYS A 190 26.936 -15.569 22.187 1.00 22.74 C ATOM 1484 CG LYS A 190 26.124 -16.825 21.959 1.00 27.44 C ATOM 1485 CD LYS A 190 26.974 -17.943 21.419 1.00 35.89 C ATOM 1486 CE LYS A 190 26.130 -19.186 21.199 1.00 44.62 C ATOM 1487 NZ LYS A 190 26.952 -20.310 20.677 1.00 50.83 N ATOM 1488 N ALA A 191 26.522 -14.886 25.187 1.00 18.54 N ATOM 1489 CA ALA A 191 26.197 -15.275 26.558 1.00 21.86 C ATOM 1490 C ALA A 191 25.126 -14.342 27.125 1.00 23.54 C ATOM 1491 O ALA A 191 24.137 -14.797 27.704 1.00 28.98 O ATOM 1492 CB ALA A 191 27.451 -15.229 27.418 1.00 14.77 C ATOM 1493 N PHE A 192 25.310 -13.040 26.913 1.00 25.87 N ATOM 1494 CA PHE A 192 24.362 -12.033 27.392 1.00 23.23 C ATOM 1495 C PHE A 192 22.983 -12.159 26.746 1.00 18.39 C ATOM 1496 O PHE A 192 21.969 -12.084 27.434 1.00 20.40 O ATOM 1497 CB PHE A 192 24.919 -10.616 27.172 1.00 24.89 C ATOM 1498 CG PHE A 192 23.961 -9.517 27.558 1.00 22.37 C ATOM 1499 CD1 PHE A 192 23.748 -9.200 28.897 1.00 20.87 C ATOM 1500 CD2 PHE A 192 23.250 -8.820 26.584 1.00 20.65 C ATOM 1501 CE1 PHE A 192 22.840 -8.208 29.261 1.00 20.15 C ATOM 1502 CE2 PHE A 192 22.339 -7.826 26.937 1.00 21.20 C ATOM 1503 CZ PHE A 192 22.133 -7.520 28.280 1.00 20.41 C ATOM 1504 N LEU A 193 22.946 -12.350 25.430 1.00 20.75 N ATOM 1505 CA LEU A 193 21.676 -12.472 24.714 1.00 20.80 C ATOM 1506 C LEU A 193 20.875 -13.703 25.121 1.00 19.55 C ATOM 1507 O LEU A 193 19.658 -13.741 24.947 1.00 18.50 O ATOM 1508 CB LEU A 193 21.903 -12.477 23.198 1.00 21.35 C ATOM 1509 CG LEU A 193 22.401 -11.172 22.576 1.00 22.49 C ATOM 1510 CD1 LEU A 193 22.690 -11.381 21.100 1.00 24.89 C ATOM 1511 CD2 LEU A 193 21.369 -10.074 22.768 1.00 20.59 C ATOM 1512 N ALA A 194 21.557 -14.699 25.676 1.00 21.46 N ATOM 1513 CA ALA A 194 20.897 -15.928 26.099 1.00 24.95 C ATOM 1514 C ALA A 194 20.485 -15.922 27.572 1.00 25.86 C ATOM 1515 O ALA A 194 19.689 -16.761 27.993 1.00 26.94 O ATOM 1516 CB ALA A 194 21.795 -17.124 25.811 1.00 19.38 C ATOM 1517 N SER A 195 21.010 -14.967 28.339 1.00 27.60 N ATOM 1518 CA SER A 195 20.725 -14.857 29.776 1.00 24.45 C ATOM 1519 C SER A 195 19.299 -14.406 30.112 1.00 26.28 C ATOM 1520 O SER A 195 18.633 -13.767 29.298 1.00 30.32 O ATOM 1521 CB SER A 195 21.724 -13.899 30.429 1.00 26.01 C ATOM 1522 OG SER A 195 21.421 -12.548 30.115 1.00 25.65 O ATOM 1523 N PRO A 196 18.820 -14.733 31.332 1.00 24.59 N ATOM 1524 CA PRO A 196 17.472 -14.362 31.795 1.00 24.19 C ATOM 1525 C PRO A 196 17.343 -12.843 31.883 1.00 24.62 C ATOM 1526 O PRO A 196 16.266 -12.277 31.687 1.00 26.10 O ATOM 1527 CB PRO A 196 17.414 -14.980 33.196 1.00 24.24 C ATOM 1528 CG PRO A 196 18.372 -16.125 33.115 1.00 27.98 C ATOM 1529 CD PRO A 196 19.517 -15.528 32.353 1.00 24.65 C ATOM 1530 N GLU A 197 18.467 -12.206 32.196 1.00 19.70 N ATOM 1531 CA GLU A 197 18.591 -10.759 32.328 1.00 23.50 C ATOM 1532 C GLU A 197 18.065 -10.048 31.080 1.00 24.13 C ATOM 1533 O GLU A 197 17.408 -9.007 31.169 1.00 26.91 O ATOM 1534 CB GLU A 197 20.067 -10.439 32.517 1.00 22.94 C ATOM 1535 CG GLU A 197 20.387 -9.061 33.008 1.00 31.92 C ATOM 1536 CD GLU A 197 21.879 -8.869 33.215 1.00 31.00 C ATOM 1537 OE1 GLU A 197 22.582 -9.848 33.558 1.00 33.33 O ATOM 1538 OE2 GLU A 197 22.359 -7.736 33.025 1.00 37.43 O ATOM 1539 N TYR A 198 18.368 -10.627 29.921 1.00 25.29 N ATOM 1540 CA TYR A 198 17.945 -10.092 28.634 1.00 18.96 C ATOM 1541 C TYR A 198 16.641 -10.738 28.163 1.00 20.57 C ATOM 1542 O TYR A 198 15.644 -10.053 27.929 1.00 22.66 O ATOM 1543 CB TYR A 198 19.059 -10.318 27.595 1.00 22.12 C ATOM 1544 CG TYR A 198 18.697 -9.913 26.178 1.00 26.53 C ATOM 1545 CD1 TYR A 198 18.924 -8.613 25.720 1.00 28.57 C ATOM 1546 CD2 TYR A 198 18.109 -10.826 25.300 1.00 25.80 C ATOM 1547 CE1 TYR A 198 18.567 -8.233 24.423 1.00 29.22 C ATOM 1548 CE2 TYR A 198 17.752 -10.459 24.010 1.00 28.53 C ATOM 1549 CZ TYR A 198 17.981 -9.163 23.577 1.00 29.40 C ATOM 1550 OH TYR A 198 17.608 -8.801 22.305 1.00 31.79 O ATOM 1551 N VAL A 199 16.660 -12.063 28.048 1.00 24.03 N ATOM 1552 CA VAL A 199 15.518 -12.845 27.577 1.00 17.51 C ATOM 1553 C VAL A 199 14.191 -12.642 28.301 1.00 16.40 C ATOM 1554 O VAL A 199 13.144 -12.566 27.661 1.00 20.26 O ATOM 1555 CB VAL A 199 15.863 -14.360 27.559 1.00 18.17 C ATOM 1556 CG1 VAL A 199 14.647 -15.186 27.192 1.00 13.57 C ATOM 1557 CG2 VAL A 199 16.992 -14.625 26.577 1.00 13.24 C ATOM 1558 N ASN A 200 14.224 -12.534 29.626 1.00 20.36 N ATOM 1559 CA ASN A 200 12.987 -12.388 30.396 1.00 24.71 C ATOM 1560 C ASN A 200 12.413 -10.980 30.533 1.00 24.30 C ATOM 1561 O ASN A 200 11.457 -10.756 31.277 1.00 26.01 O ATOM 1562 CB ASN A 200 13.130 -13.064 31.760 1.00 23.91 C ATOM 1563 CG ASN A 200 13.303 -14.563 31.640 1.00 24.69 C ATOM 1564 OD1 ASN A 200 12.738 -15.191 30.744 1.00 27.46 O ATOM 1565 ND2 ASN A 200 14.106 -15.140 32.523 1.00 19.32 N ATOM 1566 N LEU A 201 12.986 -10.043 29.790 1.00 25.32 N ATOM 1567 CA LEU A 201 12.527 -8.663 29.793 1.00 21.92 C ATOM 1568 C LEU A 201 11.732 -8.437 28.512 1.00 19.52 C ATOM 1569 O LEU A 201 12.146 -8.880 27.439 1.00 19.36 O ATOM 1570 CB LEU A 201 13.734 -7.730 29.805 1.00 19.53 C ATOM 1571 CG LEU A 201 13.899 -6.754 30.964 1.00 23.03 C ATOM 1572 CD1 LEU A 201 13.669 -7.450 32.294 1.00 12.43 C ATOM 1573 CD2 LEU A 201 15.289 -6.146 30.895 1.00 20.31 C ATOM 1574 N PRO A 202 10.548 -7.811 28.609 1.00 20.25 N ATOM 1575 CA PRO A 202 9.763 -7.568 27.393 1.00 20.74 C ATOM 1576 C PRO A 202 10.473 -6.499 26.554 1.00 21.47 C ATOM 1577 O PRO A 202 11.210 -5.676 27.097 1.00 19.63 O ATOM 1578 CB PRO A 202 8.428 -7.063 27.944 1.00 19.86 C ATOM 1579 CG PRO A 202 8.824 -6.373 29.207 1.00 18.81 C ATOM 1580 CD PRO A 202 9.831 -7.328 29.804 1.00 16.60 C ATOM 1581 N ILE A 203 10.291 -6.535 25.238 1.00 22.14 N ATOM 1582 CA ILE A 203 10.942 -5.559 24.363 1.00 21.07 C ATOM 1583 C ILE A 203 10.426 -4.145 24.631 1.00 20.67 C ATOM 1584 O ILE A 203 11.210 -3.218 24.854 1.00 20.99 O ATOM 1585 CB ILE A 203 10.748 -5.911 22.858 1.00 19.42 C ATOM 1586 CG1 ILE A 203 11.470 -7.222 22.533 1.00 21.91 C ATOM 1587 CG2 ILE A 203 11.290 -4.792 21.975 1.00 16.48 C ATOM 1588 CD1 ILE A 203 11.310 -7.677 21.095 1.00 23.11 C ATOM 1589 N ASN A 204 9.104 -4.005 24.642 1.00 18.80 N ATOM 1590 CA ASN A 204 8.464 -2.718 24.868 1.00 22.71 C ATOM 1591 C ASN A 204 7.588 -2.685 26.121 1.00 24.23 C ATOM 1592 O ASN A 204 7.205 -3.725 26.660 1.00 21.79 O ATOM 1593 CB ASN A 204 7.649 -2.329 23.628 1.00 24.47 C ATOM 1594 CG ASN A 204 8.483 -2.377 22.354 1.00 24.50 C ATOM 1595 OD1 ASN A 204 9.494 -1.685 22.239 1.00 18.23 O ATOM 1596 ND2 ASN A 204 8.087 -3.225 21.414 1.00 21.47 N ATOM 1597 N GLY A 205 7.276 -1.473 26.569 1.00 26.71 N ATOM 1598 CA GLY A 205 6.467 -1.289 27.758 1.00 25.69 C ATOM 1599 C GLY A 205 4.988 -1.609 27.656 1.00 29.15 C ATOM 1600 O GLY A 205 4.303 -1.633 28.676 1.00 34.75 O ATOM 1601 N ASN A 206 4.477 -1.855 26.453 1.00 27.42 N ATOM 1602 CA ASN A 206 3.057 -2.164 26.303 1.00 27.33 C ATOM 1603 C ASN A 206 2.778 -3.617 25.911 1.00 31.61 C ATOM 1604 O ASN A 206 1.663 -3.958 25.508 1.00 32.48 O ATOM 1605 CB ASN A 206 2.381 -1.197 25.319 1.00 27.41 C ATOM 1606 CG ASN A 206 2.868 -1.369 23.887 1.00 26.48 C ATOM 1607 OD1 ASN A 206 3.888 -2.011 23.635 1.00 25.11 O ATOM 1608 ND2 ASN A 206 2.133 -0.798 22.943 1.00 22.41 N ATOM 1609 N GLY A 207 3.797 -4.466 26.018 1.00 33.03 N ATOM 1610 CA GLY A 207 3.631 -5.870 25.685 1.00 37.73 C ATOM 1611 C GLY A 207 3.508 -6.198 24.208 1.00 40.19 C ATOM 1612 O GLY A 207 3.250 -7.348 23.847 1.00 44.39 O ATOM 1613 N LYS A 208 3.653 -5.195 23.349 1.00 38.77 N ATOM 1614 CA LYS A 208 3.575 -5.423 21.910 1.00 32.12 C ATOM 1615 C LYS A 208 4.988 -5.553 21.353 1.00 28.26 C ATOM 1616 O LYS A 208 5.931 -5.001 21.911 1.00 30.78 O ATOM 1617 CB LYS A 208 2.811 -4.289 21.225 1.00 31.16 C ATOM 1618 CG LYS A 208 1.361 -4.209 21.667 1.00 32.20 C ATOM 1619 CD LYS A 208 0.615 -3.101 20.964 1.00 32.83 C ATOM 1620 CE LYS A 208 -0.821 -3.047 21.443 1.00 39.68 C ATOM 1621 NZ LYS A 208 -1.594 -1.975 20.764 1.00 46.46 N ATOM 1622 N GLN A 209 5.132 -6.327 20.283 1.00 28.94 N ATOM 1623 CA GLN A 209 6.428 -6.558 19.650 1.00 28.11 C ATOM 1624 C GLN A 209 6.266 -7.178 18.260 1.00 30.09 C ATOM 1625 O GLN A 209 7.299 -7.477 17.618 1.00 30.42 O ATOM 1626 CB GLN A 209 7.263 -7.493 20.517 1.00 30.55 C ATOM 1627 CG GLN A 209 6.518 -8.755 20.919 1.00 32.09 C ATOM 1628 CD GLN A 209 7.415 -9.783 21.547 1.00 37.68 C ATOM 1629 OE1 GLN A 209 8.145 -9.501 22.493 1.00 40.65 O ATOM 1630 NE2 GLN A 209 7.366 -11.004 21.011 1.00 36.70 N ATOM 1631 OXT GLN A 209 5.111 -7.365 17.827 1.00 28.35 O TER 1632 GLN A 209 ATOM 1633 N PRO B 2 36.456 22.522 0.112 1.00 44.99 N ATOM 1634 CA PRO B 2 35.928 23.163 1.346 1.00 38.33 C ATOM 1635 C PRO B 2 34.592 22.500 1.704 1.00 31.55 C ATOM 1636 O PRO B 2 34.476 21.270 1.661 1.00 27.29 O ATOM 1637 CB PRO B 2 35.742 24.637 1.013 1.00 39.93 C ATOM 1638 CG PRO B 2 35.408 24.539 -0.468 1.00 41.50 C ATOM 1639 CD PRO B 2 36.297 23.435 -1.037 1.00 46.22 C ATOM 1640 N TYR B 3 33.580 23.312 2.002 1.00 23.35 N ATOM 1641 CA TYR B 3 32.265 22.800 2.366 1.00 21.38 C ATOM 1642 C TYR B 3 31.201 23.090 1.321 1.00 22.19 C ATOM 1643 O TYR B 3 31.216 24.134 0.668 1.00 22.43 O ATOM 1644 CB TYR B 3 31.815 23.414 3.689 1.00 21.29 C ATOM 1645 CG TYR B 3 32.793 23.230 4.822 1.00 20.74 C ATOM 1646 CD1 TYR B 3 33.159 21.957 5.265 1.00 21.60 C ATOM 1647 CD2 TYR B 3 33.345 24.335 5.464 1.00 19.73 C ATOM 1648 CE1 TYR B 3 34.056 21.799 6.325 1.00 20.76 C ATOM 1649 CE2 TYR B 3 34.236 24.189 6.519 1.00 21.65 C ATOM 1650 CZ TYR B 3 34.590 22.926 6.945 1.00 21.17 C ATOM 1651 OH TYR B 3 35.492 22.800 7.974 1.00 24.95 O ATOM 1652 N THR B 4 30.243 22.177 1.221 1.00 19.47 N ATOM 1653 CA THR B 4 29.132 22.312 0.292 1.00 20.33 C ATOM 1654 C THR B 4 27.886 21.755 0.964 1.00 21.18 C ATOM 1655 O THR B 4 27.889 20.616 1.428 1.00 27.50 O ATOM 1656 CB THR B 4 29.367 21.502 -1.009 1.00 17.61 C ATOM 1657 OG1 THR B 4 30.582 21.927 -1.632 1.00 19.50 O ATOM 1658 CG2 THR B 4 28.206 21.693 -1.981 1.00 10.34 C ATOM 1659 N VAL B 5 26.843 22.569 1.075 1.00 16.83 N ATOM 1660 CA VAL B 5 25.602 22.085 1.658 1.00 18.93 C ATOM 1661 C VAL B 5 24.546 22.032 0.554 1.00 22.66 C ATOM 1662 O VAL B 5 24.322 23.009 -0.162 1.00 23.75 O ATOM 1663 CB VAL B 5 25.117 22.916 2.909 1.00 19.36 C ATOM 1664 CG1 VAL B 5 26.209 23.841 3.418 1.00 16.06 C ATOM 1665 CG2 VAL B 5 23.828 23.664 2.633 1.00 20.46 C ATOM 1666 N VAL B 6 23.985 20.847 0.357 1.00 21.03 N ATOM 1667 CA VAL B 6 22.953 20.631 -0.646 1.00 16.98 C ATOM 1668 C VAL B 6 21.639 20.575 0.123 1.00 20.71 C ATOM 1669 O VAL B 6 21.448 19.706 0.982 1.00 20.99 O ATOM 1670 CB VAL B 6 23.181 19.306 -1.404 1.00 19.05 C ATOM 1671 CG1 VAL B 6 22.174 19.168 -2.528 1.00 15.74 C ATOM 1672 CG2 VAL B 6 24.608 19.241 -1.941 1.00 12.93 C ATOM 1673 N TYR B 7 20.735 21.503 -0.175 1.00 18.95 N ATOM 1674 CA TYR B 7 19.470 21.558 0.543 1.00 17.11 C ATOM 1675 C TYR B 7 18.410 22.353 -0.216 1.00 20.00 C ATOM 1676 O TYR B 7 18.700 23.009 -1.215 1.00 28.30 O ATOM 1677 CB TYR B 7 19.725 22.197 1.918 1.00 15.53 C ATOM 1678 CG TYR B 7 18.614 22.036 2.927 1.00 15.81 C ATOM 1679 CD1 TYR B 7 18.124 20.773 3.254 1.00 20.70 C ATOM 1680 CD2 TYR B 7 18.064 23.143 3.573 1.00 17.41 C ATOM 1681 CE1 TYR B 7 17.114 20.610 4.195 1.00 15.62 C ATOM 1682 CE2 TYR B 7 17.053 22.993 4.520 1.00 13.96 C ATOM 1683 CZ TYR B 7 16.583 21.719 4.826 1.00 19.69 C ATOM 1684 OH TYR B 7 15.580 21.549 5.754 1.00 16.01 O ATOM 1685 N PHE B 8 17.173 22.278 0.265 1.00 21.14 N ATOM 1686 CA PHE B 8 16.055 22.997 -0.330 1.00 23.27 C ATOM 1687 C PHE B 8 16.196 24.474 0.033 1.00 24.52 C ATOM 1688 O PHE B 8 16.954 24.816 0.937 1.00 23.06 O ATOM 1689 CB PHE B 8 14.742 22.431 0.206 1.00 20.81 C ATOM 1690 CG PHE B 8 14.568 20.966 -0.067 1.00 28.53 C ATOM 1691 CD1 PHE B 8 14.313 20.511 -1.363 1.00 27.87 C ATOM 1692 CD2 PHE B 8 14.682 20.033 0.961 1.00 24.47 C ATOM 1693 CE1 PHE B 8 14.175 19.149 -1.630 1.00 26.60 C ATOM 1694 CE2 PHE B 8 14.546 18.664 0.705 1.00 28.36 C ATOM 1695 CZ PHE B 8 14.293 18.222 -0.594 1.00 30.39 C ATOM 1696 N PRO B 9 15.506 25.373 -0.688 1.00 26.31 N ATOM 1697 CA PRO B 9 15.608 26.806 -0.384 1.00 25.99 C ATOM 1698 C PRO B 9 14.846 27.247 0.875 1.00 23.56 C ATOM 1699 O PRO B 9 13.976 28.112 0.811 1.00 23.36 O ATOM 1700 CB PRO B 9 15.055 27.456 -1.650 1.00 24.89 C ATOM 1701 CG PRO B 9 13.996 26.473 -2.082 1.00 23.72 C ATOM 1702 CD PRO B 9 14.698 25.148 -1.904 1.00 26.50 C ATOM 1703 N VAL B 10 15.171 26.631 2.009 1.00 25.41 N ATOM 1704 CA VAL B 10 14.550 26.952 3.295 1.00 21.42 C ATOM 1705 C VAL B 10 15.627 26.876 4.372 1.00 21.85 C ATOM 1706 O VAL B 10 16.718 26.351 4.129 1.00 24.62 O ATOM 1707 CB VAL B 10 13.411 25.962 3.669 1.00 18.04 C ATOM 1708 CG1 VAL B 10 12.331 25.954 2.601 1.00 24.91 C ATOM 1709 CG2 VAL B 10 13.962 24.564 3.887 1.00 22.55 C ATOM 1710 N ARG B 11 15.338 27.424 5.548 1.00 19.09 N ATOM 1711 CA ARG B 11 16.292 27.384 6.653 1.00 22.10 C ATOM 1712 C ARG B 11 16.294 25.967 7.214 1.00 20.11 C ATOM 1713 O ARG B 11 17.339 25.313 7.264 1.00 17.99 O ATOM 1714 CB ARG B 11 15.905 28.386 7.740 1.00 21.02 C ATOM 1715 CG ARG B 11 15.934 29.825 7.269 1.00 24.47 C ATOM 1716 CD ARG B 11 15.615 30.782 8.394 1.00 27.24 C ATOM 1717 NE ARG B 11 15.297 32.107 7.876 1.00 35.99 N ATOM 1718 CZ ARG B 11 14.600 33.022 8.539 1.00 35.08 C ATOM 1719 NH1 ARG B 11 14.150 32.762 9.762 1.00 34.23 N ATOM 1720 NH2 ARG B 11 14.322 34.185 7.961 1.00 33.00 N ATOM 1721 N GLY B 12 15.107 25.510 7.614 1.00 17.29 N ATOM 1722 CA GLY B 12 14.919 24.170 8.147 1.00 19.03 C ATOM 1723 C GLY B 12 16.043 23.580 8.979 1.00 21.68 C ATOM 1724 O GLY B 12 16.525 24.201 9.930 1.00 19.53 O ATOM 1725 N ARG B 13 16.494 22.393 8.587 1.00 18.60 N ATOM 1726 CA ARG B 13 17.557 21.700 9.303 1.00 16.78 C ATOM 1727 C ARG B 13 18.984 22.143 8.997 1.00 17.85 C ATOM 1728 O ARG B 13 19.941 21.511 9.453 1.00 14.77 O ATOM 1729 CB ARG B 13 17.419 20.189 9.123 1.00 17.91 C ATOM 1730 CG ARG B 13 16.250 19.595 9.896 1.00 16.36 C ATOM 1731 CD ARG B 13 16.233 18.086 9.786 1.00 17.76 C ATOM 1732 NE ARG B 13 15.255 17.479 10.688 1.00 16.09 N ATOM 1733 CZ ARG B 13 15.511 17.133 11.947 1.00 14.76 C ATOM 1734 NH1 ARG B 13 16.715 17.344 12.474 1.00 9.54 N ATOM 1735 NH2 ARG B 13 14.558 16.583 12.686 1.00 12.19 N ATOM 1736 N CYS B 14 19.137 23.223 8.234 1.00 13.59 N ATOM 1737 CA CYS B 14 20.473 23.722 7.915 1.00 12.78 C ATOM 1738 C CYS B 14 20.777 25.056 8.583 1.00 14.39 C ATOM 1739 O CYS B 14 21.923 25.518 8.566 1.00 17.05 O ATOM 1740 CB CYS B 14 20.666 23.837 6.404 1.00 11.20 C ATOM 1741 SG CYS B 14 20.802 22.248 5.584 1.00 18.79 S ATOM 1742 N ALA B 15 19.754 25.658 9.187 1.00 12.33 N ATOM 1743 CA ALA B 15 19.894 26.944 9.860 1.00 11.57 C ATOM 1744 C ALA B 15 21.024 26.948 10.892 1.00 15.07 C ATOM 1745 O ALA B 15 21.909 27.802 10.851 1.00 19.37 O ATOM 1746 CB ALA B 15 18.577 27.330 10.509 1.00 12.32 C ATOM 1747 N ALA B 16 21.022 25.956 11.777 1.00 18.57 N ATOM 1748 CA ALA B 16 22.038 25.856 12.816 1.00 12.94 C ATOM 1749 C ALA B 16 23.447 25.658 12.272 1.00 14.92 C ATOM 1750 O ALA B 16 24.385 26.332 12.714 1.00 20.76 O ATOM 1751 CB ALA B 16 21.683 24.747 13.791 1.00 14.79 C ATOM 1752 N LEU B 17 23.600 24.755 11.305 1.00 14.18 N ATOM 1753 CA LEU B 17 24.920 24.494 10.730 1.00 16.72 C ATOM 1754 C LEU B 17 25.433 25.696 9.934 1.00 12.67 C ATOM 1755 O LEU B 17 26.639 25.927 9.860 1.00 16.54 O ATOM 1756 CB LEU B 17 24.928 23.195 9.900 1.00 18.29 C ATOM 1757 CG LEU B 17 24.156 23.036 8.588 1.00 21.35 C ATOM 1758 CD1 LEU B 17 25.082 23.325 7.424 1.00 16.63 C ATOM 1759 CD2 LEU B 17 23.615 21.612 8.473 1.00 20.25 C ATOM 1760 N ARG B 18 24.515 26.476 9.367 1.00 12.74 N ATOM 1761 CA ARG B 18 24.891 27.674 8.618 1.00 18.88 C ATOM 1762 C ARG B 18 25.375 28.751 9.588 1.00 16.51 C ATOM 1763 O ARG B 18 26.380 29.416 9.331 1.00 13.17 O ATOM 1764 CB ARG B 18 23.710 28.195 7.804 1.00 15.29 C ATOM 1765 CG ARG B 18 23.418 27.381 6.566 1.00 8.72 C ATOM 1766 CD ARG B 18 22.061 27.743 6.005 1.00 15.71 C ATOM 1767 NE ARG B 18 21.810 27.073 4.734 1.00 15.01 N ATOM 1768 CZ ARG B 18 20.604 26.797 4.254 1.00 12.98 C ATOM 1769 NH1 ARG B 18 19.517 27.128 4.940 1.00 13.28 N ATOM 1770 NH2 ARG B 18 20.486 26.195 3.078 1.00 20.09 N ATOM 1771 N MET B 19 24.661 28.905 10.706 1.00 15.95 N ATOM 1772 CA MET B 19 25.034 29.882 11.728 1.00 15.28 C ATOM 1773 C MET B 19 26.402 29.532 12.294 1.00 17.96 C ATOM 1774 O MET B 19 27.211 30.411 12.574 1.00 19.34 O ATOM 1775 CB MET B 19 24.021 29.901 12.870 1.00 18.95 C ATOM 1776 CG MET B 19 22.626 30.337 12.477 1.00 24.87 C ATOM 1777 SD MET B 19 21.554 30.545 13.921 1.00 34.59 S ATOM 1778 CE MET B 19 21.340 28.900 14.412 1.00 33.63 C ATOM 1779 N LEU B 20 26.648 28.236 12.459 1.00 18.78 N ATOM 1780 CA LEU B 20 27.916 27.744 12.985 1.00 17.18 C ATOM 1781 C LEU B 20 29.064 28.113 12.046 1.00 20.02 C ATOM 1782 O LEU B 20 30.083 28.655 12.485 1.00 16.87 O ATOM 1783 CB LEU B 20 27.842 26.223 13.179 1.00 13.92 C ATOM 1784 CG LEU B 20 28.971 25.482 13.907 1.00 19.86 C ATOM 1785 CD1 LEU B 20 28.451 24.135 14.389 1.00 18.43 C ATOM 1786 CD2 LEU B 20 30.198 25.303 13.017 1.00 13.99 C ATOM 1787 N LEU B 21 28.897 27.801 10.760 1.00 19.50 N ATOM 1788 CA LEU B 21 29.910 28.096 9.752 1.00 19.18 C ATOM 1789 C LEU B 21 30.167 29.596 9.656 1.00 17.53 C ATOM 1790 O LEU B 21 31.316 30.031 9.662 1.00 15.83 O ATOM 1791 CB LEU B 21 29.484 27.549 8.389 1.00 15.49 C ATOM 1792 CG LEU B 21 29.547 26.030 8.229 1.00 15.85 C ATOM 1793 CD1 LEU B 21 28.894 25.612 6.926 1.00 13.39 C ATOM 1794 CD2 LEU B 21 30.993 25.564 8.281 1.00 12.67 C ATOM 1795 N ALA B 22 29.092 30.378 9.604 1.00 15.69 N ATOM 1796 CA ALA B 22 29.191 31.831 9.515 1.00 16.05 C ATOM 1797 C ALA B 22 29.941 32.414 10.711 1.00 19.44 C ATOM 1798 O ALA B 22 30.927 33.135 10.548 1.00 23.53 O ATOM 1799 CB ALA B 22 27.809 32.436 9.426 1.00 13.27 C ATOM 1800 N ASP B 23 29.500 32.051 11.912 1.00 19.70 N ATOM 1801 CA ASP B 23 30.104 32.536 13.145 1.00 16.42 C ATOM 1802 C ASP B 23 31.563 32.119 13.318 1.00 20.57 C ATOM 1803 O ASP B 23 32.342 32.832 13.950 1.00 27.27 O ATOM 1804 CB ASP B 23 29.277 32.073 14.346 1.00 26.04 C ATOM 1805 CG ASP B 23 29.571 32.867 15.601 1.00 27.38 C ATOM 1806 OD1 ASP B 23 29.380 34.102 15.590 1.00 28.68 O ATOM 1807 OD2 ASP B 23 29.966 32.245 16.603 1.00 29.14 O ATOM 1808 N GLN B 24 31.932 30.967 12.767 1.00 22.55 N ATOM 1809 CA GLN B 24 33.307 30.478 12.868 1.00 19.78 C ATOM 1810 C GLN B 24 34.195 31.012 11.754 1.00 23.29 C ATOM 1811 O GLN B 24 35.357 30.622 11.644 1.00 26.51 O ATOM 1812 CB GLN B 24 33.336 28.948 12.871 1.00 21.07 C ATOM 1813 CG GLN B 24 32.766 28.331 14.147 1.00 17.57 C ATOM 1814 CD GLN B 24 33.505 28.794 15.389 1.00 22.26 C ATOM 1815 OE1 GLN B 24 34.736 28.741 15.443 1.00 23.87 O ATOM 1816 NE2 GLN B 24 32.764 29.221 16.399 1.00 22.26 N ATOM 1817 N GLY B 25 33.635 31.896 10.930 1.00 23.55 N ATOM 1818 CA GLY B 25 34.382 32.486 9.833 1.00 26.33 C ATOM 1819 C GLY B 25 34.715 31.517 8.716 1.00 25.96 C ATOM 1820 O GLY B 25 35.752 31.648 8.071 1.00 32.53 O ATOM 1821 N GLN B 26 33.841 30.542 8.488 1.00 27.12 N ATOM 1822 CA GLN B 26 34.048 29.544 7.443 1.00 30.01 C ATOM 1823 C GLN B 26 33.286 29.887 6.169 1.00 29.99 C ATOM 1824 O GLN B 26 32.208 30.479 6.217 1.00 31.54 O ATOM 1825 CB GLN B 26 33.609 28.161 7.928 1.00 32.12 C ATOM 1826 CG GLN B 26 34.300 27.689 9.194 1.00 31.02 C ATOM 1827 CD GLN B 26 35.796 27.590 9.039 1.00 30.45 C ATOM 1828 OE1 GLN B 26 36.293 27.116 8.021 1.00 33.98 O ATOM 1829 NE2 GLN B 26 36.525 28.013 10.064 1.00 34.96 N ATOM 1830 N SER B 27 33.853 29.491 5.033 1.00 29.11 N ATOM 1831 CA SER B 27 33.250 29.730 3.726 1.00 28.11 C ATOM 1832 C SER B 27 32.634 28.421 3.262 1.00 26.42 C ATOM 1833 O SER B 27 33.189 27.350 3.506 1.00 28.32 O ATOM 1834 CB SER B 27 34.319 30.144 2.709 1.00 29.93 C ATOM 1835 OG SER B 27 35.229 31.082 3.255 1.00 40.28 O ATOM 1836 N TRP B 28 31.494 28.501 2.591 1.00 22.19 N ATOM 1837 CA TRP B 28 30.849 27.300 2.083 1.00 24.92 C ATOM 1838 C TRP B 28 30.034 27.599 0.834 1.00 25.73 C ATOM 1839 O TRP B 28 29.657 28.740 0.582 1.00 25.19 O ATOM 1840 CB TRP B 28 29.971 26.643 3.156 1.00 22.29 C ATOM 1841 CG TRP B 28 28.704 27.382 3.489 1.00 15.52 C ATOM 1842 CD1 TRP B 28 27.455 27.126 3.001 1.00 13.84 C ATOM 1843 CD2 TRP B 28 28.560 28.458 4.431 1.00 10.54 C ATOM 1844 NE1 TRP B 28 26.539 27.967 3.587 1.00 15.10 N ATOM 1845 CE2 TRP B 28 27.186 28.790 4.467 1.00 12.21 C ATOM 1846 CE3 TRP B 28 29.449 29.163 5.250 1.00 14.96 C ATOM 1847 CZ2 TRP B 28 26.685 29.803 5.294 1.00 14.12 C ATOM 1848 CZ3 TRP B 28 28.949 30.168 6.071 1.00 12.06 C ATOM 1849 CH2 TRP B 28 27.577 30.476 6.086 1.00 11.62 C ATOM 1850 N LYS B 29 29.774 26.556 0.057 1.00 29.57 N ATOM 1851 CA LYS B 29 29.012 26.663 -1.175 1.00 25.01 C ATOM 1852 C LYS B 29 27.614 26.114 -0.941 1.00 26.43 C ATOM 1853 O LYS B 29 27.443 25.087 -0.286 1.00 27.83 O ATOM 1854 CB LYS B 29 29.717 25.869 -2.280 1.00 29.33 C ATOM 1855 CG LYS B 29 28.887 25.607 -3.523 1.00 38.61 C ATOM 1856 CD LYS B 29 28.694 26.854 -4.373 1.00 50.41 C ATOM 1857 CE LYS B 29 27.795 26.555 -5.569 1.00 57.90 C ATOM 1858 NZ LYS B 29 28.278 25.361 -6.331 1.00 62.68 N ATOM 1859 N GLU B 30 26.614 26.825 -1.446 1.00 26.92 N ATOM 1860 CA GLU B 30 25.232 26.397 -1.314 1.00 27.01 C ATOM 1861 C GLU B 30 24.750 25.834 -2.643 1.00 27.72 C ATOM 1862 O GLU B 30 24.811 26.508 -3.671 1.00 34.02 O ATOM 1863 CB GLU B 30 24.338 27.570 -0.905 1.00 25.94 C ATOM 1864 CG GLU B 30 24.514 28.050 0.532 1.00 29.24 C ATOM 1865 CD GLU B 30 23.715 27.251 1.555 1.00 30.58 C ATOM 1866 OE1 GLU B 30 22.968 26.320 1.174 1.00 25.23 O ATOM 1867 OE2 GLU B 30 23.838 27.564 2.757 1.00 29.25 O ATOM 1868 N GLU B 31 24.337 24.574 -2.623 1.00 28.52 N ATOM 1869 CA GLU B 31 23.813 23.905 -3.803 1.00 25.72 C ATOM 1870 C GLU B 31 22.324 23.805 -3.558 1.00 25.94 C ATOM 1871 O GLU B 31 21.868 22.946 -2.809 1.00 29.29 O ATOM 1872 CB GLU B 31 24.419 22.511 -3.949 1.00 33.03 C ATOM 1873 CG GLU B 31 25.774 22.493 -4.623 1.00 50.55 C ATOM 1874 CD GLU B 31 25.678 22.761 -6.113 1.00 60.19 C ATOM 1875 OE1 GLU B 31 25.642 23.946 -6.515 1.00 63.47 O ATOM 1876 OE2 GLU B 31 25.625 21.779 -6.883 1.00 67.54 O ATOM 1877 N VAL B 32 21.572 24.725 -4.146 1.00 24.92 N ATOM 1878 CA VAL B 32 20.132 24.751 -3.963 1.00 20.60 C ATOM 1879 C VAL B 32 19.401 23.743 -4.828 1.00 22.29 C ATOM 1880 O VAL B 32 19.620 23.663 -6.033 1.00 29.25 O ATOM 1881 CB VAL B 32 19.562 26.158 -4.219 1.00 19.92 C ATOM 1882 CG1 VAL B 32 18.067 26.176 -3.945 1.00 12.11 C ATOM 1883 CG2 VAL B 32 20.279 27.174 -3.342 1.00 14.39 C ATOM 1884 N VAL B 33 18.544 22.962 -4.185 1.00 24.44 N ATOM 1885 CA VAL B 33 17.747 21.954 -4.859 1.00 21.44 C ATOM 1886 C VAL B 33 16.300 22.392 -4.727 1.00 28.87 C ATOM 1887 O VAL B 33 15.805 22.594 -3.617 1.00 27.88 O ATOM 1888 CB VAL B 33 17.915 20.563 -4.207 1.00 17.46 C ATOM 1889 CG1 VAL B 33 16.964 19.562 -4.845 1.00 16.26 C ATOM 1890 CG2 VAL B 33 19.350 20.087 -4.348 1.00 17.19 C ATOM 1891 N THR B 34 15.637 22.574 -5.864 1.00 32.86 N ATOM 1892 CA THR B 34 14.240 22.988 -5.875 1.00 37.55 C ATOM 1893 C THR B 34 13.335 21.766 -5.754 1.00 40.42 C ATOM 1894 O THR B 34 13.777 20.635 -5.960 1.00 43.21 O ATOM 1895 CB THR B 34 13.892 23.739 -7.174 1.00 39.12 C ATOM 1896 OG1 THR B 34 14.013 22.845 -8.287 1.00 42.63 O ATOM 1897 CG2 THR B 34 14.838 24.914 -7.378 1.00 36.51 C ATOM 1898 N VAL B 35 12.069 22.001 -5.418 1.00 47.06 N ATOM 1899 CA VAL B 35 11.088 20.925 -5.277 1.00 51.36 C ATOM 1900 C VAL B 35 10.899 20.185 -6.607 1.00 52.28 C ATOM 1901 O VAL B 35 10.598 18.991 -6.625 1.00 51.27 O ATOM 1902 CB VAL B 35 9.719 21.477 -4.786 1.00 56.08 C ATOM 1903 CG1 VAL B 35 9.053 22.331 -5.876 1.00 61.15 C ATOM 1904 CG2 VAL B 35 8.809 20.338 -4.349 1.00 56.80 C ATOM 1905 N GLU B 36 11.097 20.901 -7.712 1.00 53.52 N ATOM 1906 CA GLU B 36 10.962 20.330 -9.049 1.00 54.84 C ATOM 1907 C GLU B 36 12.079 19.323 -9.294 1.00 50.67 C ATOM 1908 O GLU B 36 11.821 18.167 -9.636 1.00 53.55 O ATOM 1909 CB GLU B 36 11.057 21.429 -10.105 1.00 63.16 C ATOM 1910 CG GLU B 36 10.280 22.693 -9.779 1.00 69.82 C ATOM 1911 CD GLU B 36 11.060 23.952 -10.125 1.00 76.70 C ATOM 1912 OE1 GLU B 36 11.947 23.895 -11.012 1.00 77.80 O ATOM 1913 OE2 GLU B 36 10.796 24.996 -9.492 1.00 77.93 O ATOM 1914 N THR B 37 13.319 19.778 -9.119 1.00 45.47 N ATOM 1915 CA THR B 37 14.498 18.940 -9.312 1.00 44.03 C ATOM 1916 C THR B 37 14.421 17.681 -8.440 1.00 44.83 C ATOM 1917 O THR B 37 14.750 16.582 -8.892 1.00 45.66 O ATOM 1918 CB THR B 37 15.797 19.711 -8.961 1.00 45.59 C ATOM 1919 OG1 THR B 37 15.770 21.007 -9.571 1.00 44.60 O ATOM 1920 CG2 THR B 37 17.022 18.958 -9.462 1.00 41.13 C ATOM 1921 N TRP B 38 13.957 17.852 -7.202 1.00 42.46 N ATOM 1922 CA TRP B 38 13.827 16.750 -6.247 1.00 37.33 C ATOM 1923 C TRP B 38 12.808 15.704 -6.702 1.00 39.59 C ATOM 1924 O TRP B 38 13.067 14.502 -6.616 1.00 39.62 O ATOM 1925 CB TRP B 38 13.447 17.297 -4.864 1.00 33.40 C ATOM 1926 CG TRP B 38 13.438 16.274 -3.751 1.00 25.44 C ATOM 1927 CD1 TRP B 38 12.344 15.804 -3.081 1.00 26.44 C ATOM 1928 CD2 TRP B 38 14.578 15.630 -3.163 1.00 19.69 C ATOM 1929 NE1 TRP B 38 12.732 14.912 -2.109 1.00 26.62 N ATOM 1930 CE2 TRP B 38 14.092 14.785 -2.135 1.00 23.60 C ATOM 1931 CE3 TRP B 38 15.958 15.685 -3.397 1.00 22.42 C ATOM 1932 CZ2 TRP B 38 14.945 14.002 -1.344 1.00 18.02 C ATOM 1933 CZ3 TRP B 38 16.804 14.907 -2.610 1.00 18.65 C ATOM 1934 CH2 TRP B 38 16.291 14.076 -1.595 1.00 16.32 C ATOM 1935 N GLN B 39 11.661 16.164 -7.198 1.00 41.02 N ATOM 1936 CA GLN B 39 10.611 15.261 -7.665 1.00 43.87 C ATOM 1937 C GLN B 39 10.977 14.507 -8.939 1.00 45.67 C ATOM 1938 O GLN B 39 10.292 13.557 -9.322 1.00 46.37 O ATOM 1939 CB GLN B 39 9.294 16.015 -7.833 1.00 43.05 C ATOM 1940 CG GLN B 39 8.703 16.459 -6.503 1.00 53.12 C ATOM 1941 CD GLN B 39 7.534 17.409 -6.652 1.00 59.71 C ATOM 1942 OE1 GLN B 39 7.303 17.975 -7.724 1.00 67.77 O ATOM 1943 NE2 GLN B 39 6.802 17.611 -5.565 1.00 58.04 N ATOM 1944 N GLU B 40 12.064 14.924 -9.586 1.00 49.44 N ATOM 1945 CA GLU B 40 12.539 14.261 -10.795 1.00 52.01 C ATOM 1946 C GLU B 40 13.010 12.849 -10.408 1.00 53.92 C ATOM 1947 O GLU B 40 12.970 11.927 -11.224 1.00 56.56 O ATOM 1948 CB GLU B 40 13.664 15.079 -11.435 1.00 52.61 C ATOM 1949 CG GLU B 40 14.194 14.525 -12.744 1.00 60.77 C ATOM 1950 CD GLU B 40 15.502 13.778 -12.572 1.00 65.52 C ATOM 1951 OE1 GLU B 40 16.568 14.429 -12.577 1.00 70.14 O ATOM 1952 OE2 GLU B 40 15.471 12.538 -12.443 1.00 68.28 O ATOM 1953 N GLY B 41 13.457 12.695 -9.160 1.00 53.26 N ATOM 1954 CA GLY B 41 13.873 11.392 -8.661 1.00 47.13 C ATOM 1955 C GLY B 41 15.333 10.985 -8.568 1.00 45.40 C ATOM 1956 O GLY B 41 15.712 10.304 -7.613 1.00 45.80 O ATOM 1957 N SER B 42 16.152 11.382 -9.537 1.00 43.84 N ATOM 1958 CA SER B 42 17.565 11.000 -9.556 1.00 45.07 C ATOM 1959 C SER B 42 18.397 11.318 -8.310 1.00 42.77 C ATOM 1960 O SER B 42 19.101 10.443 -7.802 1.00 44.63 O ATOM 1961 CB SER B 42 18.254 11.561 -10.802 1.00 45.52 C ATOM 1962 OG SER B 42 18.192 12.975 -10.822 1.00 56.12 O ATOM 1963 N LEU B 43 18.326 12.559 -7.825 1.00 41.45 N ATOM 1964 CA LEU B 43 19.088 12.968 -6.640 1.00 35.47 C ATOM 1965 C LEU B 43 18.646 12.201 -5.389 1.00 33.32 C ATOM 1966 O LEU B 43 19.483 11.691 -4.642 1.00 28.91 O ATOM 1967 CB LEU B 43 18.941 14.473 -6.389 1.00 34.88 C ATOM 1968 CG LEU B 43 20.116 15.266 -5.791 1.00 33.78 C ATOM 1969 CD1 LEU B 43 19.560 16.342 -4.879 1.00 30.86 C ATOM 1970 CD2 LEU B 43 21.086 14.386 -5.015 1.00 31.60 C ATOM 1971 N LYS B 44 17.333 12.136 -5.166 1.00 27.83 N ATOM 1972 CA LYS B 44 16.767 11.434 -4.014 1.00 28.21 C ATOM 1973 C LYS B 44 17.281 10.002 -3.946 1.00 31.60 C ATOM 1974 O LYS B 44 17.657 9.518 -2.880 1.00 32.06 O ATOM 1975 CB LYS B 44 15.241 11.409 -4.106 1.00 26.24 C ATOM 1976 CG LYS B 44 14.554 10.883 -2.859 1.00 22.27 C ATOM 1977 CD LYS B 44 13.084 10.584 -3.116 1.00 23.13 C ATOM 1978 CE LYS B 44 12.238 10.808 -1.871 1.00 28.25 C ATOM 1979 NZ LYS B 44 12.829 10.214 -0.639 1.00 25.33 N ATOM 1980 N ALA B 45 17.320 9.348 -5.105 1.00 35.21 N ATOM 1981 CA ALA B 45 17.777 7.968 -5.217 1.00 32.44 C ATOM 1982 C ALA B 45 19.243 7.792 -4.834 1.00 29.63 C ATOM 1983 O ALA B 45 19.628 6.735 -4.339 1.00 33.70 O ATOM 1984 CB ALA B 45 17.535 7.454 -6.629 1.00 33.51 C ATOM 1985 N SER B 46 20.057 8.818 -5.064 1.00 25.77 N ATOM 1986 CA SER B 46 21.479 8.750 -4.731 1.00 27.32 C ATOM 1987 C SER B 46 21.775 9.115 -3.277 1.00 28.24 C ATOM 1988 O SER B 46 22.907 8.956 -2.817 1.00 29.38 O ATOM 1989 CB SER B 46 22.293 9.644 -5.664 1.00 28.96 C ATOM 1990 OG SER B 46 21.881 10.995 -5.558 1.00 42.89 O ATOM 1991 N CYS B 47 20.774 9.645 -2.575 1.00 26.04 N ATOM 1992 CA CYS B 47 20.923 10.015 -1.166 1.00 24.21 C ATOM 1993 C CYS B 47 20.761 8.769 -0.303 1.00 24.57 C ATOM 1994 O CYS B 47 19.778 8.038 -0.453 1.00 25.43 O ATOM 1995 CB CYS B 47 19.871 11.050 -0.761 1.00 23.70 C ATOM 1996 SG CYS B 47 20.106 12.681 -1.487 1.00 27.60 S ATOM 1997 N LEU B 48 21.702 8.558 0.619 1.00 21.07 N ATOM 1998 CA LEU B 48 21.693 7.396 1.510 1.00 20.15 C ATOM 1999 C LEU B 48 20.336 7.054 2.132 1.00 22.33 C ATOM 2000 O LEU B 48 19.904 5.906 2.072 1.00 28.05 O ATOM 2001 CB LEU B 48 22.740 7.565 2.609 1.00 23.63 C ATOM 2002 CG LEU B 48 22.899 6.392 3.580 1.00 26.35 C ATOM 2003 CD1 LEU B 48 23.265 5.123 2.818 1.00 23.75 C ATOM 2004 CD2 LEU B 48 23.967 6.724 4.606 1.00 23.99 C ATOM 2005 N TYR B 49 19.674 8.041 2.730 1.00 20.96 N ATOM 2006 CA TYR B 49 18.364 7.817 3.347 1.00 19.04 C ATOM 2007 C TYR B 49 17.243 8.473 2.536 1.00 23.06 C ATOM 2008 O TYR B 49 16.103 8.592 3.013 1.00 14.83 O ATOM 2009 CB TYR B 49 18.346 8.338 4.789 1.00 16.45 C ATOM 2010 CG TYR B 49 19.391 7.708 5.687 1.00 15.57 C ATOM 2011 CD1 TYR B 49 19.335 6.349 6.006 1.00 15.62 C ATOM 2012 CD2 TYR B 49 20.433 8.468 6.223 1.00 12.65 C ATOM 2013 CE1 TYR B 49 20.289 5.758 6.835 1.00 9.71 C ATOM 2014 CE2 TYR B 49 21.394 7.887 7.058 1.00 12.31 C ATOM 2015 CZ TYR B 49 21.314 6.531 7.360 1.00 17.11 C ATOM 2016 OH TYR B 49 22.253 5.951 8.189 1.00 16.72 O ATOM 2017 N GLY B 50 17.576 8.877 1.306 1.00 20.59 N ATOM 2018 CA GLY B 50 16.614 9.512 0.418 1.00 15.71 C ATOM 2019 C GLY B 50 16.169 10.891 0.867 1.00 18.57 C ATOM 2020 O GLY B 50 15.067 11.329 0.532 1.00 21.67 O ATOM 2021 N GLN B 51 17.017 11.577 1.633 1.00 20.16 N ATOM 2022 CA GLN B 51 16.677 12.905 2.129 1.00 19.25 C ATOM 2023 C GLN B 51 17.852 13.870 2.166 1.00 20.17 C ATOM 2024 O GLN B 51 19.008 13.467 2.050 1.00 18.88 O ATOM 2025 CB GLN B 51 16.081 12.810 3.538 1.00 14.87 C ATOM 2026 CG GLN B 51 14.756 12.076 3.632 1.00 14.61 C ATOM 2027 CD GLN B 51 14.127 12.226 4.994 1.00 14.77 C ATOM 2028 OE1 GLN B 51 14.752 11.954 6.012 1.00 22.93 O ATOM 2029 NE2 GLN B 51 12.881 12.684 5.021 1.00 16.66 N ATOM 2030 N LEU B 52 17.528 15.153 2.307 1.00 22.03 N ATOM 2031 CA LEU B 52 18.520 16.219 2.414 1.00 22.08 C ATOM 2032 C LEU B 52 18.382 16.774 3.844 1.00 21.71 C ATOM 2033 O LEU B 52 17.341 16.601 4.477 1.00 20.23 O ATOM 2034 CB LEU B 52 18.251 17.310 1.368 1.00 18.06 C ATOM 2035 CG LEU B 52 18.409 16.899 -0.100 1.00 16.20 C ATOM 2036 CD1 LEU B 52 18.006 18.047 -1.017 1.00 13.53 C ATOM 2037 CD2 LEU B 52 19.846 16.468 -0.376 1.00 12.65 C ATOM 2038 N PRO B 53 19.382 17.522 4.340 1.00 20.71 N ATOM 2039 CA PRO B 53 20.643 17.930 3.718 1.00 18.98 C ATOM 2040 C PRO B 53 21.683 16.862 3.415 1.00 21.39 C ATOM 2041 O PRO B 53 21.692 15.771 3.989 1.00 24.37 O ATOM 2042 CB PRO B 53 21.200 18.936 4.724 1.00 17.12 C ATOM 2043 CG PRO B 53 20.752 18.362 6.035 1.00 14.53 C ATOM 2044 CD PRO B 53 19.311 18.013 5.731 1.00 17.11 C ATOM 2045 N LYS B 54 22.544 17.215 2.470 1.00 19.46 N ATOM 2046 CA LYS B 54 23.671 16.408 2.048 1.00 18.15 C ATOM 2047 C LYS B 54 24.800 17.406 2.267 1.00 17.46 C ATOM 2048 O LYS B 54 24.646 18.592 1.984 1.00 19.47 O ATOM 2049 CB LYS B 54 23.562 16.044 0.568 1.00 25.72 C ATOM 2050 CG LYS B 54 24.774 15.291 0.037 1.00 25.89 C ATOM 2051 CD LYS B 54 24.657 15.058 -1.453 1.00 26.27 C ATOM 2052 CE LYS B 54 25.954 14.531 -2.029 1.00 28.22 C ATOM 2053 NZ LYS B 54 25.850 14.396 -3.504 1.00 30.93 N ATOM 2054 N PHE B 55 25.926 16.941 2.780 1.00 17.93 N ATOM 2055 CA PHE B 55 27.038 17.831 3.071 1.00 14.81 C ATOM 2056 C PHE B 55 28.334 17.255 2.542 1.00 16.42 C ATOM 2057 O PHE B 55 28.500 16.045 2.471 1.00 23.75 O ATOM 2058 CB PHE B 55 27.124 18.023 4.588 1.00 17.69 C ATOM 2059 CG PHE B 55 28.160 19.015 5.034 1.00 15.85 C ATOM 2060 CD1 PHE B 55 27.916 20.383 4.952 1.00 13.56 C ATOM 2061 CD2 PHE B 55 29.357 18.578 5.599 1.00 16.92 C ATOM 2062 CE1 PHE B 55 28.848 21.307 5.433 1.00 16.41 C ATOM 2063 CE2 PHE B 55 30.297 19.495 6.085 1.00 23.68 C ATOM 2064 CZ PHE B 55 30.039 20.863 6.001 1.00 18.10 C ATOM 2065 N GLN B 56 29.243 18.132 2.140 1.00 20.41 N ATOM 2066 CA GLN B 56 30.529 17.700 1.635 1.00 20.22 C ATOM 2067 C GLN B 56 31.664 18.498 2.251 1.00 21.92 C ATOM 2068 O GLN B 56 31.611 19.723 2.347 1.00 26.13 O ATOM 2069 CB GLN B 56 30.576 17.789 0.108 1.00 26.34 C ATOM 2070 CG GLN B 56 29.742 16.720 -0.584 1.00 35.71 C ATOM 2071 CD GLN B 56 29.643 16.915 -2.085 1.00 41.57 C ATOM 2072 OE1 GLN B 56 29.760 18.034 -2.593 1.00 41.39 O ATOM 2073 NE2 GLN B 56 29.414 15.824 -2.807 1.00 46.42 N ATOM 2074 N ASP B 57 32.649 17.764 2.746 1.00 19.80 N ATOM 2075 CA ASP B 57 33.839 18.329 3.344 1.00 19.66 C ATOM 2076 C ASP B 57 34.932 17.612 2.565 1.00 24.38 C ATOM 2077 O ASP B 57 35.308 16.486 2.898 1.00 23.76 O ATOM 2078 CB ASP B 57 33.904 17.972 4.832 1.00 21.33 C ATOM 2079 CG ASP B 57 35.151 18.511 5.512 1.00 29.37 C ATOM 2080 OD1 ASP B 57 35.960 19.213 4.863 1.00 31.13 O ATOM 2081 OD2 ASP B 57 35.323 18.240 6.716 1.00 31.27 O ATOM 2082 N GLY B 58 35.412 18.252 1.502 1.00 23.00 N ATOM 2083 CA GLY B 58 36.419 17.622 0.668 1.00 21.06 C ATOM 2084 C GLY B 58 35.688 16.504 -0.049 1.00 22.16 C ATOM 2085 O GLY B 58 34.625 16.734 -0.627 1.00 27.12 O ATOM 2086 N ASP B 59 36.210 15.285 0.025 1.00 28.11 N ATOM 2087 CA ASP B 59 35.540 14.163 -0.624 1.00 35.77 C ATOM 2088 C ASP B 59 34.660 13.365 0.345 1.00 35.78 C ATOM 2089 O ASP B 59 34.103 12.326 -0.021 1.00 37.51 O ATOM 2090 CB ASP B 59 36.545 13.257 -1.356 1.00 42.69 C ATOM 2091 CG ASP B 59 37.405 12.430 -0.414 1.00 50.40 C ATOM 2092 OD1 ASP B 59 37.603 12.835 0.758 1.00 53.57 O ATOM 2093 OD2 ASP B 59 37.898 11.372 -0.869 1.00 54.26 O ATOM 2094 N LEU B 60 34.542 13.859 1.579 1.00 31.06 N ATOM 2095 CA LEU B 60 33.711 13.213 2.591 1.00 25.13 C ATOM 2096 C LEU B 60 32.281 13.697 2.385 1.00 23.57 C ATOM 2097 O LEU B 60 32.010 14.895 2.466 1.00 24.18 O ATOM 2098 CB LEU B 60 34.175 13.600 3.999 1.00 23.83 C ATOM 2099 CG LEU B 60 33.950 12.636 5.174 1.00 23.92 C ATOM 2100 CD1 LEU B 60 33.643 13.432 6.425 1.00 18.58 C ATOM 2101 CD2 LEU B 60 32.828 11.654 4.896 1.00 24.36 C ATOM 2102 N THR B 61 31.378 12.767 2.094 1.00 22.69 N ATOM 2103 CA THR B 61 29.975 13.092 1.882 1.00 19.72 C ATOM 2104 C THR B 61 29.190 12.613 3.100 1.00 25.74 C ATOM 2105 O THR B 61 29.277 11.445 3.483 1.00 28.39 O ATOM 2106 CB THR B 61 29.432 12.417 0.606 1.00 23.67 C ATOM 2107 OG1 THR B 61 30.171 12.885 -0.530 1.00 26.64 O ATOM 2108 CG2 THR B 61 27.949 12.727 0.413 1.00 17.60 C ATOM 2109 N LEU B 62 28.434 13.525 3.704 1.00 22.33 N ATOM 2110 CA LEU B 62 27.642 13.230 4.891 1.00 19.91 C ATOM 2111 C LEU B 62 26.154 13.511 4.715 1.00 18.73 C ATOM 2112 O LEU B 62 25.751 14.300 3.862 1.00 20.87 O ATOM 2113 CB LEU B 62 28.156 14.069 6.068 1.00 16.70 C ATOM 2114 CG LEU B 62 29.161 13.533 7.094 1.00 21.49 C ATOM 2115 CD1 LEU B 62 29.833 12.251 6.641 1.00 17.38 C ATOM 2116 CD2 LEU B 62 30.181 14.617 7.399 1.00 15.96 C ATOM 2117 N TYR B 63 25.348 12.821 5.513 1.00 16.77 N ATOM 2118 CA TYR B 63 23.902 13.007 5.536 1.00 18.08 C ATOM 2119 C TYR B 63 23.547 13.126 7.016 1.00 14.44 C ATOM 2120 O TYR B 63 24.398 12.882 7.872 1.00 19.30 O ATOM 2121 CB TYR B 63 23.171 11.825 4.889 1.00 19.38 C ATOM 2122 CG TYR B 63 23.450 11.685 3.412 1.00 26.32 C ATOM 2123 CD1 TYR B 63 22.657 12.343 2.471 1.00 28.89 C ATOM 2124 CD2 TYR B 63 24.521 10.918 2.952 1.00 23.96 C ATOM 2125 CE1 TYR B 63 22.923 12.250 1.110 1.00 27.77 C ATOM 2126 CE2 TYR B 63 24.797 10.818 1.590 1.00 27.29 C ATOM 2127 CZ TYR B 63 23.994 11.488 0.674 1.00 30.44 C ATOM 2128 OH TYR B 63 24.276 11.412 -0.670 1.00 28.82 O ATOM 2129 N GLN B 64 22.310 13.522 7.310 1.00 14.04 N ATOM 2130 CA GLN B 64 21.836 13.696 8.685 1.00 15.23 C ATOM 2131 C GLN B 64 22.383 15.003 9.270 1.00 12.16 C ATOM 2132 O GLN B 64 23.583 15.137 9.514 1.00 12.06 O ATOM 2133 CB GLN B 64 22.230 12.490 9.551 1.00 16.44 C ATOM 2134 CG GLN B 64 21.594 11.170 9.112 1.00 16.05 C ATOM 2135 CD GLN B 64 20.127 11.068 9.493 1.00 17.17 C ATOM 2136 OE1 GLN B 64 19.565 11.983 10.087 1.00 17.01 O ATOM 2137 NE2 GLN B 64 19.499 9.946 9.151 1.00 17.18 N ATOM 2138 N SER B 65 21.486 15.962 9.485 1.00 11.92 N ATOM 2139 CA SER B 65 21.850 17.276 10.004 1.00 12.45 C ATOM 2140 C SER B 65 22.703 17.242 11.274 1.00 14.60 C ATOM 2141 O SER B 65 23.700 17.964 11.365 1.00 16.80 O ATOM 2142 CB SER B 65 20.598 18.118 10.231 1.00 11.86 C ATOM 2143 OG SER B 65 19.717 17.484 11.140 1.00 15.75 O ATOM 2144 N ASN B 66 22.332 16.392 12.232 1.00 12.08 N ATOM 2145 CA ASN B 66 23.085 16.286 13.484 1.00 12.31 C ATOM 2146 C ASN B 66 24.467 15.659 13.316 1.00 12.87 C ATOM 2147 O ASN B 66 25.384 15.963 14.080 1.00 14.94 O ATOM 2148 CB ASN B 66 22.277 15.536 14.550 1.00 14.74 C ATOM 2149 CG ASN B 66 21.072 16.325 15.011 1.00 15.06 C ATOM 2150 OD1 ASN B 66 21.211 17.435 15.525 1.00 15.55 O ATOM 2151 ND2 ASN B 66 19.884 15.766 14.821 1.00 9.00 N ATOM 2152 N THR B 67 24.619 14.775 12.331 1.00 14.29 N ATOM 2153 CA THR B 67 25.917 14.162 12.058 1.00 11.84 C ATOM 2154 C THR B 67 26.813 15.281 11.531 1.00 13.44 C ATOM 2155 O THR B 67 27.978 15.382 11.898 1.00 13.87 O ATOM 2156 CB THR B 67 25.813 13.043 11.010 1.00 10.79 C ATOM 2157 OG1 THR B 67 25.137 11.924 11.586 1.00 11.75 O ATOM 2158 CG2 THR B 67 27.182 12.605 10.546 1.00 8.81 C ATOM 2159 N ILE B 68 26.239 16.141 10.693 1.00 13.29 N ATOM 2160 CA ILE B 68 26.965 17.275 10.130 1.00 15.73 C ATOM 2161 C ILE B 68 27.392 18.204 11.272 1.00 15.23 C ATOM 2162 O ILE B 68 28.549 18.622 11.333 1.00 14.20 O ATOM 2163 CB ILE B 68 26.089 18.036 9.109 1.00 18.12 C ATOM 2164 CG1 ILE B 68 25.690 17.090 7.972 1.00 12.03 C ATOM 2165 CG2 ILE B 68 26.846 19.242 8.554 1.00 12.44 C ATOM 2166 CD1 ILE B 68 24.511 17.563 7.158 1.00 10.03 C ATOM 2167 N LEU B 69 26.470 18.492 12.192 1.00 10.94 N ATOM 2168 CA LEU B 69 26.774 19.346 13.342 1.00 14.30 C ATOM 2169 C LEU B 69 27.904 18.758 14.187 1.00 16.71 C ATOM 2170 O LEU B 69 28.863 19.456 14.527 1.00 18.11 O ATOM 2171 CB LEU B 69 25.532 19.556 14.215 1.00 10.62 C ATOM 2172 CG LEU B 69 24.531 20.606 13.735 1.00 13.60 C ATOM 2173 CD1 LEU B 69 23.316 20.609 14.632 1.00 17.41 C ATOM 2174 CD2 LEU B 69 25.189 21.984 13.736 1.00 14.10 C ATOM 2175 N ARG B 70 27.813 17.462 14.483 1.00 17.46 N ATOM 2176 CA ARG B 70 28.833 16.794 15.287 1.00 14.70 C ATOM 2177 C ARG B 70 30.183 16.747 14.589 1.00 16.69 C ATOM 2178 O ARG B 70 31.228 16.885 15.230 1.00 15.84 O ATOM 2179 CB ARG B 70 28.378 15.391 15.690 1.00 16.11 C ATOM 2180 CG ARG B 70 27.299 15.417 16.749 1.00 17.77 C ATOM 2181 CD ARG B 70 26.967 14.039 17.299 1.00 17.69 C ATOM 2182 NE ARG B 70 26.195 14.177 18.530 1.00 16.07 N ATOM 2183 CZ ARG B 70 24.867 14.161 18.600 1.00 18.45 C ATOM 2184 NH1 ARG B 70 24.140 13.991 17.503 1.00 16.73 N ATOM 2185 NH2 ARG B 70 24.264 14.389 19.760 1.00 13.69 N ATOM 2186 N HIS B 71 30.154 16.584 13.270 1.00 16.68 N ATOM 2187 CA HIS B 71 31.377 16.538 12.484 1.00 16.33 C ATOM 2188 C HIS B 71 32.098 17.883 12.556 1.00 16.31 C ATOM 2189 O HIS B 71 33.309 17.940 12.777 1.00 23.11 O ATOM 2190 CB HIS B 71 31.061 16.192 11.029 1.00 19.10 C ATOM 2191 CG HIS B 71 32.245 16.289 10.127 1.00 14.31 C ATOM 2192 ND1 HIS B 71 33.357 15.491 10.279 1.00 16.91 N ATOM 2193 CD2 HIS B 71 32.519 17.127 9.101 1.00 19.97 C ATOM 2194 CE1 HIS B 71 34.270 15.836 9.388 1.00 17.30 C ATOM 2195 NE2 HIS B 71 33.786 16.828 8.662 1.00 21.25 N ATOM 2196 N LEU B 72 31.345 18.959 12.349 1.00 19.96 N ATOM 2197 CA LEU B 72 31.890 20.314 12.404 1.00 18.68 C ATOM 2198 C LEU B 72 32.360 20.642 13.825 1.00 20.71 C ATOM 2199 O LEU B 72 33.411 21.261 14.010 1.00 19.88 O ATOM 2200 CB LEU B 72 30.833 21.325 11.944 1.00 15.33 C ATOM 2201 CG LEU B 72 30.828 21.810 10.486 1.00 19.43 C ATOM 2202 CD1 LEU B 72 31.622 20.888 9.583 1.00 25.39 C ATOM 2203 CD2 LEU B 72 29.393 21.953 9.991 1.00 11.24 C ATOM 2204 N GLY B 73 31.594 20.197 14.821 1.00 14.96 N ATOM 2205 CA GLY B 73 31.957 20.446 16.206 1.00 14.21 C ATOM 2206 C GLY B 73 33.255 19.749 16.563 1.00 19.62 C ATOM 2207 O GLY B 73 34.080 20.275 17.301 1.00 25.40 O ATOM 2208 N ARG B 74 33.459 18.575 15.984 1.00 20.36 N ATOM 2209 CA ARG B 74 34.656 17.789 16.232 1.00 22.21 C ATOM 2210 C ARG B 74 35.887 18.368 15.528 1.00 24.14 C ATOM 2211 O ARG B 74 36.944 18.524 16.140 1.00 23.68 O ATOM 2212 CB ARG B 74 34.399 16.351 15.776 1.00 23.20 C ATOM 2213 CG ARG B 74 35.316 15.295 16.361 1.00 25.97 C ATOM 2214 CD ARG B 74 34.562 13.971 16.477 1.00 18.40 C ATOM 2215 NE ARG B 74 33.709 13.769 15.313 1.00 19.99 N ATOM 2216 CZ ARG B 74 32.470 13.288 15.352 1.00 19.18 C ATOM 2217 NH1 ARG B 74 31.919 12.931 16.502 1.00 16.06 N ATOM 2218 NH2 ARG B 74 31.748 13.248 14.242 1.00 14.93 N ATOM 2219 N THR B 75 35.740 18.711 14.250 1.00 24.37 N ATOM 2220 CA THR B 75 36.852 19.252 13.466 1.00 22.93 C ATOM 2221 C THR B 75 37.203 20.705 13.780 1.00 23.45 C ATOM 2222 O THR B 75 38.362 21.099 13.670 1.00 26.31 O ATOM 2223 CB THR B 75 36.596 19.118 11.949 1.00 22.94 C ATOM 2224 OG1 THR B 75 35.351 19.744 11.617 1.00 24.40 O ATOM 2225 CG2 THR B 75 36.543 17.648 11.536 1.00 17.38 C ATOM 2226 N LEU B 76 36.206 21.494 14.171 1.00 21.16 N ATOM 2227 CA LEU B 76 36.416 22.904 14.497 1.00 21.72 C ATOM 2228 C LEU B 76 36.640 23.192 15.986 1.00 22.20 C ATOM 2229 O LEU B 76 36.898 24.333 16.366 1.00 19.86 O ATOM 2230 CB LEU B 76 35.251 23.743 13.971 1.00 21.04 C ATOM 2231 CG LEU B 76 35.359 24.339 12.566 1.00 23.96 C ATOM 2232 CD1 LEU B 76 36.216 23.475 11.659 1.00 23.60 C ATOM 2233 CD2 LEU B 76 33.962 24.527 11.995 1.00 18.34 C ATOM 2234 N GLY B 77 36.537 22.160 16.822 1.00 25.08 N ATOM 2235 CA GLY B 77 36.747 22.332 18.252 1.00 21.49 C ATOM 2236 C GLY B 77 35.595 22.964 19.020 1.00 22.81 C ATOM 2237 O GLY B 77 35.814 23.785 19.912 1.00 26.73 O ATOM 2238 N LEU B 78 34.369 22.585 18.670 1.00 19.13 N ATOM 2239 CA LEU B 78 33.165 23.092 19.325 1.00 17.81 C ATOM 2240 C LEU B 78 32.432 21.911 19.972 1.00 19.78 C ATOM 2241 O LEU B 78 31.208 21.791 19.861 1.00 17.32 O ATOM 2242 CB LEU B 78 32.247 23.751 18.288 1.00 19.37 C ATOM 2243 CG LEU B 78 32.854 24.715 17.265 1.00 21.63 C ATOM 2244 CD1 LEU B 78 31.762 25.193 16.324 1.00 24.18 C ATOM 2245 CD2 LEU B 78 33.512 25.889 17.962 1.00 15.44 C ATOM 2246 N TYR B 79 33.180 21.071 20.686 1.00 19.64 N ATOM 2247 CA TYR B 79 32.618 19.874 21.312 1.00 20.25 C ATOM 2248 C TYR B 79 33.033 19.698 22.782 1.00 21.38 C ATOM 2249 O TYR B 79 33.209 18.571 23.251 1.00 26.49 O ATOM 2250 CB TYR B 79 33.076 18.653 20.502 1.00 22.97 C ATOM 2251 CG TYR B 79 32.037 17.573 20.309 1.00 18.41 C ATOM 2252 CD1 TYR B 79 31.193 17.188 21.353 1.00 13.93 C ATOM 2253 CD2 TYR B 79 31.906 16.929 19.079 1.00 15.23 C ATOM 2254 CE1 TYR B 79 30.243 16.189 21.177 1.00 13.05 C ATOM 2255 CE2 TYR B 79 30.960 15.927 18.891 1.00 17.16 C ATOM 2256 CZ TYR B 79 30.129 15.563 19.946 1.00 19.13 C ATOM 2257 OH TYR B 79 29.176 14.589 19.760 1.00 14.15 O ATOM 2258 N GLY B 80 33.160 20.807 23.508 1.00 19.91 N ATOM 2259 CA GLY B 80 33.561 20.748 24.908 1.00 13.93 C ATOM 2260 C GLY B 80 35.066 20.664 25.082 1.00 18.01 C ATOM 2261 O GLY B 80 35.788 20.366 24.130 1.00 18.02 O ATOM 2262 N LYS B 81 35.547 20.902 26.299 1.00 20.25 N ATOM 2263 CA LYS B 81 36.982 20.858 26.564 1.00 24.80 C ATOM 2264 C LYS B 81 37.467 19.447 26.886 1.00 22.49 C ATOM 2265 O LYS B 81 38.660 19.159 26.798 1.00 26.88 O ATOM 2266 CB LYS B 81 37.359 21.824 27.693 1.00 29.28 C ATOM 2267 CG LYS B 81 36.887 21.391 29.062 1.00 40.93 C ATOM 2268 CD LYS B 81 37.378 22.337 30.143 1.00 46.44 C ATOM 2269 CE LYS B 81 37.171 21.740 31.527 1.00 47.73 C ATOM 2270 NZ LYS B 81 35.744 21.403 31.797 1.00 53.48 N ATOM 2271 N ASP B 82 36.541 18.570 27.260 1.00 19.00 N ATOM 2272 CA ASP B 82 36.883 17.188 27.580 1.00 21.26 C ATOM 2273 C ASP B 82 35.704 16.241 27.343 1.00 16.97 C ATOM 2274 O ASP B 82 34.642 16.671 26.892 1.00 18.12 O ATOM 2275 CB ASP B 82 37.418 17.072 29.019 1.00 23.12 C ATOM 2276 CG ASP B 82 36.453 17.617 30.071 1.00 26.23 C ATOM 2277 OD1 ASP B 82 35.220 17.546 29.888 1.00 28.04 O ATOM 2278 OD2 ASP B 82 36.942 18.108 31.108 1.00 32.29 O ATOM 2279 N GLN B 83 35.884 14.960 27.665 1.00 17.70 N ATOM 2280 CA GLN B 83 34.834 13.962 27.465 1.00 21.24 C ATOM 2281 C GLN B 83 33.572 14.230 28.261 1.00 18.81 C ATOM 2282 O GLN B 83 32.466 14.012 27.765 1.00 21.48 O ATOM 2283 CB GLN B 83 35.340 12.555 27.766 1.00 23.61 C ATOM 2284 CG GLN B 83 36.347 12.027 26.760 1.00 30.28 C ATOM 2285 CD GLN B 83 36.828 10.626 27.100 1.00 34.94 C ATOM 2286 OE1 GLN B 83 37.203 9.861 26.217 1.00 35.76 O ATOM 2287 NE2 GLN B 83 36.837 10.292 28.390 1.00 32.08 N ATOM 2288 N GLN B 84 33.729 14.703 29.492 1.00 20.99 N ATOM 2289 CA GLN B 84 32.572 15.001 30.328 1.00 25.50 C ATOM 2290 C GLN B 84 31.706 16.068 29.664 1.00 21.51 C ATOM 2291 O GLN B 84 30.487 15.904 29.555 1.00 19.93 O ATOM 2292 CB GLN B 84 33.003 15.462 31.721 1.00 33.46 C ATOM 2293 CG GLN B 84 31.832 15.842 32.616 1.00 45.68 C ATOM 2294 CD GLN B 84 32.243 16.103 34.049 1.00 53.55 C ATOM 2295 OE1 GLN B 84 33.021 15.347 34.629 1.00 49.34 O ATOM 2296 NE2 GLN B 84 31.713 17.174 34.631 1.00 62.37 N ATOM 2297 N GLU B 85 32.346 17.141 29.197 1.00 17.09 N ATOM 2298 CA GLU B 85 31.629 18.223 28.526 1.00 21.44 C ATOM 2299 C GLU B 85 31.038 17.732 27.213 1.00 19.55 C ATOM 2300 O GLU B 85 29.926 18.118 26.856 1.00 15.23 O ATOM 2301 CB GLU B 85 32.541 19.426 28.269 1.00 21.97 C ATOM 2302 CG GLU B 85 33.034 20.106 29.532 1.00 22.81 C ATOM 2303 CD GLU B 85 33.398 21.567 29.325 1.00 30.73 C ATOM 2304 OE1 GLU B 85 33.661 21.982 28.173 1.00 27.65 O ATOM 2305 OE2 GLU B 85 33.404 22.308 30.332 1.00 32.23 O ATOM 2306 N ALA B 86 31.776 16.866 26.514 1.00 16.11 N ATOM 2307 CA ALA B 86 31.319 16.303 25.245 1.00 13.70 C ATOM 2308 C ALA B 86 30.008 15.557 25.452 1.00 16.13 C ATOM 2309 O ALA B 86 29.086 15.662 24.636 1.00 18.51 O ATOM 2310 CB ALA B 86 32.370 15.372 24.672 1.00 10.98 C ATOM 2311 N ALA B 87 29.919 14.829 26.565 1.00 16.89 N ATOM 2312 CA ALA B 87 28.711 14.078 26.897 1.00 16.48 C ATOM 2313 C ALA B 87 27.547 15.033 27.175 1.00 16.98 C ATOM 2314 O ALA B 87 26.414 14.784 26.757 1.00 15.22 O ATOM 2315 CB ALA B 87 28.963 13.181 28.101 1.00 16.88 C ATOM 2316 N LEU B 88 27.836 16.138 27.862 1.00 19.94 N ATOM 2317 CA LEU B 88 26.813 17.132 28.189 1.00 17.75 C ATOM 2318 C LEU B 88 26.309 17.856 26.939 1.00 15.35 C ATOM 2319 O LEU B 88 25.115 18.135 26.813 1.00 14.44 O ATOM 2320 CB LEU B 88 27.346 18.130 29.221 1.00 17.60 C ATOM 2321 CG LEU B 88 27.814 17.500 30.538 1.00 23.29 C ATOM 2322 CD1 LEU B 88 28.291 18.577 31.499 1.00 18.27 C ATOM 2323 CD2 LEU B 88 26.685 16.686 31.159 1.00 17.93 C ATOM 2324 N VAL B 89 27.222 18.129 26.006 1.00 15.34 N ATOM 2325 CA VAL B 89 26.884 18.790 24.745 1.00 15.99 C ATOM 2326 C VAL B 89 25.902 17.905 23.963 1.00 18.47 C ATOM 2327 O VAL B 89 24.910 18.398 23.412 1.00 14.65 O ATOM 2328 CB VAL B 89 28.152 19.048 23.890 1.00 17.28 C ATOM 2329 CG1 VAL B 89 27.769 19.597 22.529 1.00 18.91 C ATOM 2330 CG2 VAL B 89 29.079 20.024 24.603 1.00 14.77 C ATOM 2331 N ASP B 90 26.182 16.598 23.937 1.00 15.26 N ATOM 2332 CA ASP B 90 25.326 15.624 23.261 1.00 12.80 C ATOM 2333 C ASP B 90 23.949 15.585 23.907 1.00 13.24 C ATOM 2334 O ASP B 90 22.933 15.535 23.218 1.00 13.97 O ATOM 2335 CB ASP B 90 25.940 14.218 23.323 1.00 14.48 C ATOM 2336 CG ASP B 90 27.019 14.002 22.289 1.00 15.65 C ATOM 2337 OD1 ASP B 90 26.959 14.637 21.213 1.00 14.40 O ATOM 2338 OD2 ASP B 90 27.936 13.204 22.566 1.00 17.26 O ATOM 2339 N MET B 91 23.924 15.588 25.238 1.00 14.36 N ATOM 2340 CA MET B 91 22.672 15.555 25.986 1.00 12.69 C ATOM 2341 C MET B 91 21.813 16.771 25.659 1.00 11.09 C ATOM 2342 O MET B 91 20.588 16.663 25.543 1.00 10.93 O ATOM 2343 CB MET B 91 22.956 15.477 27.488 1.00 14.64 C ATOM 2344 CG MET B 91 21.707 15.396 28.351 1.00 19.85 C ATOM 2345 SD MET B 91 22.102 15.155 30.091 1.00 18.21 S ATOM 2346 CE MET B 91 23.017 16.647 30.464 1.00 23.76 C ATOM 2347 N VAL B 92 22.458 17.927 25.515 1.00 10.63 N ATOM 2348 CA VAL B 92 21.746 19.157 25.170 1.00 10.30 C ATOM 2349 C VAL B 92 21.214 19.040 23.741 1.00 11.62 C ATOM 2350 O VAL B 92 20.031 19.262 23.500 1.00 10.63 O ATOM 2351 CB VAL B 92 22.671 20.407 25.281 1.00 14.19 C ATOM 2352 CG1 VAL B 92 21.952 21.644 24.752 1.00 10.37 C ATOM 2353 CG2 VAL B 92 23.086 20.631 26.732 1.00 7.97 C ATOM 2354 N ASN B 93 22.072 18.629 22.808 1.00 14.15 N ATOM 2355 CA ASN B 93 21.668 18.489 21.410 1.00 13.30 C ATOM 2356 C ASN B 93 20.535 17.488 21.208 1.00 13.41 C ATOM 2357 O ASN B 93 19.615 17.745 20.426 1.00 12.03 O ATOM 2358 CB ASN B 93 22.855 18.117 20.516 1.00 14.30 C ATOM 2359 CG ASN B 93 22.628 18.539 19.071 1.00 22.01 C ATOM 2360 OD1 ASN B 93 22.579 19.731 18.777 1.00 19.95 O ATOM 2361 ND2 ASN B 93 22.480 17.570 18.173 1.00 15.93 N ATOM 2362 N ASP B 94 20.599 16.355 21.910 1.00 11.97 N ATOM 2363 CA ASP B 94 19.549 15.339 21.806 1.00 9.81 C ATOM 2364 C ASP B 94 18.238 15.923 22.316 1.00 12.96 C ATOM 2365 O ASP B 94 17.166 15.611 21.793 1.00 17.36 O ATOM 2366 CB ASP B 94 19.918 14.083 22.604 1.00 14.72 C ATOM 2367 CG ASP B 94 21.011 13.259 21.939 1.00 18.65 C ATOM 2368 OD1 ASP B 94 21.498 13.644 20.856 1.00 22.92 O ATOM 2369 OD2 ASP B 94 21.404 12.224 22.509 1.00 24.15 O ATOM 2370 N GLY B 95 18.336 16.778 23.333 1.00 12.02 N ATOM 2371 CA GLY B 95 17.158 17.425 23.879 1.00 9.93 C ATOM 2372 C GLY B 95 16.588 18.374 22.842 1.00 14.76 C ATOM 2373 O GLY B 95 15.378 18.397 22.616 1.00 14.61 O ATOM 2374 N VAL B 96 17.463 19.141 22.190 1.00 14.66 N ATOM 2375 CA VAL B 96 17.038 20.080 21.154 1.00 15.34 C ATOM 2376 C VAL B 96 16.352 19.311 20.018 1.00 20.89 C ATOM 2377 O VAL B 96 15.270 19.694 19.564 1.00 15.99 O ATOM 2378 CB VAL B 96 18.241 20.868 20.583 1.00 16.44 C ATOM 2379 CG1 VAL B 96 17.815 21.698 19.370 1.00 12.22 C ATOM 2380 CG2 VAL B 96 18.839 21.762 21.660 1.00 14.38 C ATOM 2381 N GLU B 97 16.970 18.204 19.602 1.00 22.54 N ATOM 2382 CA GLU B 97 16.447 17.363 18.527 1.00 19.29 C ATOM 2383 C GLU B 97 15.045 16.827 18.829 1.00 17.91 C ATOM 2384 O GLU B 97 14.189 16.795 17.943 1.00 17.10 O ATOM 2385 CB GLU B 97 17.425 16.217 18.231 1.00 16.07 C ATOM 2386 CG GLU B 97 16.930 15.182 17.217 1.00 21.39 C ATOM 2387 CD GLU B 97 16.542 15.782 15.868 1.00 26.63 C ATOM 2388 OE1 GLU B 97 17.213 16.728 15.403 1.00 26.23 O ATOM 2389 OE2 GLU B 97 15.558 15.300 15.270 1.00 26.95 O ATOM 2390 N ASP B 98 14.811 16.422 20.078 1.00 17.96 N ATOM 2391 CA ASP B 98 13.501 15.916 20.485 1.00 14.82 C ATOM 2392 C ASP B 98 12.428 16.985 20.324 1.00 14.91 C ATOM 2393 O ASP B 98 11.354 16.722 19.773 1.00 16.61 O ATOM 2394 CB ASP B 98 13.523 15.428 21.941 1.00 21.11 C ATOM 2395 CG ASP B 98 14.125 14.036 22.094 1.00 25.97 C ATOM 2396 OD1 ASP B 98 14.294 13.323 21.080 1.00 26.80 O ATOM 2397 OD2 ASP B 98 14.436 13.658 23.242 1.00 26.63 O ATOM 2398 N LEU B 99 12.712 18.192 20.808 1.00 16.65 N ATOM 2399 CA LEU B 99 11.748 19.283 20.691 1.00 16.06 C ATOM 2400 C LEU B 99 11.590 19.711 19.229 1.00 12.76 C ATOM 2401 O LEU B 99 10.497 20.071 18.801 1.00 21.60 O ATOM 2402 CB LEU B 99 12.147 20.466 21.576 1.00 18.00 C ATOM 2403 CG LEU B 99 11.181 21.659 21.589 1.00 21.48 C ATOM 2404 CD1 LEU B 99 9.746 21.199 21.787 1.00 15.93 C ATOM 2405 CD2 LEU B 99 11.587 22.628 22.685 1.00 17.55 C ATOM 2406 N ARG B 100 12.669 19.625 18.457 1.00 13.56 N ATOM 2407 CA ARG B 100 12.616 19.991 17.044 1.00 16.04 C ATOM 2408 C ARG B 100 11.662 19.064 16.289 1.00 16.92 C ATOM 2409 O ARG B 100 10.905 19.522 15.438 1.00 19.33 O ATOM 2410 CB ARG B 100 14.010 19.963 16.409 1.00 7.52 C ATOM 2411 CG ARG B 100 14.030 20.509 14.987 1.00 12.34 C ATOM 2412 CD ARG B 100 15.426 20.507 14.384 1.00 10.97 C ATOM 2413 NE ARG B 100 16.329 21.450 15.044 1.00 16.90 N ATOM 2414 CZ ARG B 100 16.341 22.765 14.831 1.00 19.86 C ATOM 2415 NH1 ARG B 100 15.489 23.318 13.972 1.00 16.38 N ATOM 2416 NH2 ARG B 100 17.218 23.530 15.469 1.00 13.57 N ATOM 2417 N CYS B 101 11.678 17.770 16.622 1.00 16.14 N ATOM 2418 CA CYS B 101 10.790 16.800 15.979 1.00 16.98 C ATOM 2419 C CYS B 101 9.335 17.124 16.262 1.00 20.79 C ATOM 2420 O CYS B 101 8.483 16.982 15.386 1.00 25.84 O ATOM 2421 CB CYS B 101 11.092 15.375 16.441 1.00 16.22 C ATOM 2422 SG CYS B 101 12.566 14.679 15.689 1.00 31.13 S ATOM 2423 N LYS B 102 9.052 17.550 17.489 1.00 16.81 N ATOM 2424 CA LYS B 102 7.690 17.910 17.868 1.00 18.43 C ATOM 2425 C LYS B 102 7.270 19.145 17.081 1.00 19.03 C ATOM 2426 O LYS B 102 6.141 19.227 16.605 1.00 20.26 O ATOM 2427 CB LYS B 102 7.607 18.191 19.366 1.00 20.91 C ATOM 2428 CG LYS B 102 7.880 16.969 20.214 1.00 27.44 C ATOM 2429 CD LYS B 102 7.819 17.294 21.684 1.00 32.63 C ATOM 2430 CE LYS B 102 8.025 16.044 22.512 1.00 36.78 C ATOM 2431 NZ LYS B 102 8.034 16.358 23.964 1.00 42.67 N ATOM 2432 N TYR B 103 8.198 20.090 16.935 1.00 19.86 N ATOM 2433 CA TYR B 103 7.954 21.321 16.190 1.00 21.42 C ATOM 2434 C TYR B 103 7.651 20.977 14.733 1.00 22.22 C ATOM 2435 O TYR B 103 6.667 21.450 14.167 1.00 19.68 O ATOM 2436 CB TYR B 103 9.184 22.241 16.271 1.00 26.62 C ATOM 2437 CG TYR B 103 9.153 23.430 15.325 1.00 28.17 C ATOM 2438 CD1 TYR B 103 8.483 24.602 15.671 1.00 26.88 C ATOM 2439 CD2 TYR B 103 9.793 23.384 14.084 1.00 29.97 C ATOM 2440 CE1 TYR B 103 8.447 25.700 14.812 1.00 27.40 C ATOM 2441 CE2 TYR B 103 9.761 24.482 13.213 1.00 27.93 C ATOM 2442 CZ TYR B 103 9.086 25.636 13.587 1.00 29.94 C ATOM 2443 OH TYR B 103 9.052 26.724 12.741 1.00 30.50 O ATOM 2444 N ILE B 104 8.495 20.132 14.145 1.00 24.07 N ATOM 2445 CA ILE B 104 8.338 19.704 12.761 1.00 23.97 C ATOM 2446 C ILE B 104 7.009 18.978 12.564 1.00 26.57 C ATOM 2447 O ILE B 104 6.310 19.200 11.577 1.00 28.55 O ATOM 2448 CB ILE B 104 9.524 18.809 12.332 1.00 22.07 C ATOM 2449 CG1 ILE B 104 10.794 19.659 12.248 1.00 16.09 C ATOM 2450 CG2 ILE B 104 9.239 18.129 10.989 1.00 21.11 C ATOM 2451 CD1 ILE B 104 12.059 18.852 12.096 1.00 18.34 C ATOM 2452 N SER B 105 6.647 18.138 13.528 1.00 27.61 N ATOM 2453 CA SER B 105 5.395 17.401 13.455 1.00 26.28 C ATOM 2454 C SER B 105 4.225 18.376 13.427 1.00 28.13 C ATOM 2455 O SER B 105 3.277 18.187 12.676 1.00 26.69 O ATOM 2456 CB SER B 105 5.260 16.454 14.646 1.00 28.21 C ATOM 2457 OG SER B 105 4.076 15.684 14.542 1.00 37.44 O ATOM 2458 N LEU B 106 4.302 19.428 14.238 1.00 27.67 N ATOM 2459 CA LEU B 106 3.243 20.435 14.283 1.00 27.62 C ATOM 2460 C LEU B 106 3.116 21.168 12.946 1.00 27.00 C ATOM 2461 O LEU B 106 2.035 21.234 12.363 1.00 25.81 O ATOM 2462 CB LEU B 106 3.521 21.456 15.390 1.00 25.45 C ATOM 2463 CG LEU B 106 2.609 22.690 15.396 1.00 24.87 C ATOM 2464 CD1 LEU B 106 1.190 22.296 15.764 1.00 27.15 C ATOM 2465 CD2 LEU B 106 3.136 23.722 16.366 1.00 23.56 C ATOM 2466 N ILE B 107 4.238 21.706 12.475 1.00 25.14 N ATOM 2467 CA ILE B 107 4.301 22.455 11.222 1.00 27.04 C ATOM 2468 C ILE B 107 3.781 21.697 9.996 1.00 28.00 C ATOM 2469 O ILE B 107 2.953 22.214 9.241 1.00 27.57 O ATOM 2470 CB ILE B 107 5.750 22.927 10.947 1.00 23.95 C ATOM 2471 CG1 ILE B 107 6.208 23.887 12.046 1.00 23.85 C ATOM 2472 CG2 ILE B 107 5.851 23.592 9.585 1.00 23.65 C ATOM 2473 CD1 ILE B 107 5.366 25.145 12.168 1.00 24.91 C ATOM 2474 N TYR B 108 4.242 20.464 9.824 1.00 27.63 N ATOM 2475 CA TYR B 108 3.856 19.651 8.679 1.00 29.34 C ATOM 2476 C TYR B 108 2.638 18.741 8.828 1.00 30.46 C ATOM 2477 O TYR B 108 2.021 18.380 7.832 1.00 34.36 O ATOM 2478 CB TYR B 108 5.061 18.830 8.210 1.00 26.16 C ATOM 2479 CG TYR B 108 6.208 19.676 7.688 1.00 26.41 C ATOM 2480 CD1 TYR B 108 6.221 20.125 6.366 1.00 27.77 C ATOM 2481 CD2 TYR B 108 7.282 20.026 8.508 1.00 23.76 C ATOM 2482 CE1 TYR B 108 7.282 20.904 5.867 1.00 28.56 C ATOM 2483 CE2 TYR B 108 8.347 20.806 8.020 1.00 26.85 C ATOM 2484 CZ TYR B 108 8.341 21.240 6.698 1.00 29.26 C ATOM 2485 OH TYR B 108 9.388 22.002 6.214 1.00 25.57 O ATOM 2486 N THR B 109 2.273 18.393 10.056 1.00 36.41 N ATOM 2487 CA THR B 109 1.141 17.493 10.283 1.00 36.88 C ATOM 2488 C THR B 109 -0.188 18.145 10.656 1.00 39.16 C ATOM 2489 O THR B 109 -1.214 17.829 10.052 1.00 45.62 O ATOM 2490 CB THR B 109 1.513 16.391 11.303 1.00 38.45 C ATOM 2491 OG1 THR B 109 2.545 15.570 10.741 1.00 39.55 O ATOM 2492 CG2 THR B 109 0.307 15.529 11.661 1.00 40.13 C ATOM 2493 N ASN B 110 -0.187 19.046 11.634 1.00 37.69 N ATOM 2494 CA ASN B 110 -1.432 19.699 12.038 1.00 39.05 C ATOM 2495 C ASN B 110 -1.225 21.057 12.703 1.00 38.04 C ATOM 2496 O ASN B 110 -1.492 21.239 13.894 1.00 33.79 O ATOM 2497 CB ASN B 110 -2.274 18.769 12.929 1.00 43.62 C ATOM 2498 CG ASN B 110 -1.624 18.477 14.272 1.00 48.97 C ATOM 2499 OD1 ASN B 110 -2.316 18.297 15.273 1.00 47.92 O ATOM 2500 ND2 ASN B 110 -0.291 18.437 14.304 1.00 51.09 N ATOM 2501 N TYR B 111 -0.765 22.016 11.905 1.00 34.78 N ATOM 2502 CA TYR B 111 -0.513 23.365 12.382 1.00 35.81 C ATOM 2503 C TYR B 111 -1.771 24.047 12.921 1.00 38.74 C ATOM 2504 O TYR B 111 -1.804 24.479 14.073 1.00 38.42 O ATOM 2505 CB TYR B 111 0.096 24.206 11.261 1.00 32.89 C ATOM 2506 CG TYR B 111 0.426 25.621 11.673 1.00 36.04 C ATOM 2507 CD1 TYR B 111 1.664 25.932 12.233 1.00 35.00 C ATOM 2508 CD2 TYR B 111 -0.505 26.647 11.520 1.00 35.41 C ATOM 2509 CE1 TYR B 111 1.966 27.231 12.632 1.00 38.24 C ATOM 2510 CE2 TYR B 111 -0.215 27.947 11.918 1.00 37.46 C ATOM 2511 CZ TYR B 111 1.021 28.232 12.473 1.00 40.15 C ATOM 2512 OH TYR B 111 1.304 29.514 12.883 1.00 45.15 O ATOM 2513 N GLU B 112 -2.799 24.128 12.081 1.00 42.24 N ATOM 2514 CA GLU B 112 -4.061 24.774 12.438 1.00 42.80 C ATOM 2515 C GLU B 112 -4.682 24.216 13.704 1.00 39.71 C ATOM 2516 O GLU B 112 -4.957 24.955 14.646 1.00 39.18 O ATOM 2517 CB GLU B 112 -5.072 24.656 11.293 1.00 46.31 C ATOM 2518 CG GLU B 112 -4.747 25.487 10.056 1.00 51.95 C ATOM 2519 CD GLU B 112 -3.492 25.022 9.329 1.00 57.89 C ATOM 2520 OE1 GLU B 112 -3.303 23.796 9.158 1.00 56.58 O ATOM 2521 OE2 GLU B 112 -2.683 25.888 8.932 1.00 59.52 O ATOM 2522 N ALA B 113 -4.875 22.902 13.721 1.00 39.33 N ATOM 2523 CA ALA B 113 -5.482 22.224 14.855 1.00 40.35 C ATOM 2524 C ALA B 113 -4.635 22.194 16.128 1.00 43.21 C ATOM 2525 O ALA B 113 -5.099 22.605 17.190 1.00 49.97 O ATOM 2526 CB ALA B 113 -5.876 20.808 14.455 1.00 37.80 C ATOM 2527 N GLY B 114 -3.386 21.751 16.011 1.00 45.06 N ATOM 2528 CA GLY B 114 -2.527 21.636 17.180 1.00 39.93 C ATOM 2529 C GLY B 114 -1.730 22.819 17.700 1.00 37.84 C ATOM 2530 O GLY B 114 -1.086 22.692 18.743 1.00 38.69 O ATOM 2531 N LYS B 115 -1.782 23.963 17.023 1.00 34.92 N ATOM 2532 CA LYS B 115 -1.015 25.137 17.447 1.00 35.21 C ATOM 2533 C LYS B 115 -1.252 25.599 18.888 1.00 37.65 C ATOM 2534 O LYS B 115 -0.306 25.962 19.589 1.00 33.26 O ATOM 2535 CB LYS B 115 -1.237 26.306 16.482 1.00 33.28 C ATOM 2536 CG LYS B 115 -0.333 27.505 16.738 1.00 34.59 C ATOM 2537 CD LYS B 115 -0.692 28.675 15.835 1.00 42.26 C ATOM 2538 CE LYS B 115 0.090 29.931 16.202 1.00 42.85 C ATOM 2539 NZ LYS B 115 1.560 29.765 16.014 1.00 50.95 N ATOM 2540 N ASP B 116 -2.505 25.568 19.335 1.00 40.00 N ATOM 2541 CA ASP B 116 -2.839 26.006 20.690 1.00 40.24 C ATOM 2542 C ASP B 116 -2.306 25.108 21.802 1.00 39.40 C ATOM 2543 O ASP B 116 -1.699 25.596 22.757 1.00 39.07 O ATOM 2544 CB ASP B 116 -4.348 26.207 20.830 1.00 45.37 C ATOM 2545 CG ASP B 116 -4.876 27.310 19.919 1.00 52.94 C ATOM 2546 OD1 ASP B 116 -4.157 28.310 19.689 1.00 51.62 O ATOM 2547 OD2 ASP B 116 -6.009 27.171 19.413 1.00 57.21 O ATOM 2548 N ASP B 117 -2.517 23.801 21.672 1.00 39.40 N ATOM 2549 CA ASP B 117 -2.039 22.850 22.672 1.00 39.34 C ATOM 2550 C ASP B 117 -0.516 22.871 22.767 1.00 39.16 C ATOM 2551 O ASP B 117 0.047 22.817 23.864 1.00 37.90 O ATOM 2552 CB ASP B 117 -2.518 21.435 22.340 1.00 39.80 C ATOM 2553 CG ASP B 117 -4.015 21.254 22.543 1.00 44.62 C ATOM 2554 OD1 ASP B 117 -4.667 22.136 23.149 1.00 41.27 O ATOM 2555 OD2 ASP B 117 -4.538 20.205 22.115 1.00 46.63 O ATOM 2556 N TYR B 118 0.137 22.965 21.609 1.00 36.72 N ATOM 2557 CA TYR B 118 1.595 23.001 21.529 1.00 33.77 C ATOM 2558 C TYR B 118 2.170 24.200 22.286 1.00 31.74 C ATOM 2559 O TYR B 118 3.147 24.064 23.025 1.00 29.32 O ATOM 2560 CB TYR B 118 2.042 23.040 20.060 1.00 26.76 C ATOM 2561 CG TYR B 118 3.539 22.929 19.861 1.00 27.02 C ATOM 2562 CD1 TYR B 118 4.360 24.052 19.956 1.00 22.08 C ATOM 2563 CD2 TYR B 118 4.137 21.701 19.584 1.00 25.26 C ATOM 2564 CE1 TYR B 118 5.732 23.955 19.784 1.00 21.48 C ATOM 2565 CE2 TYR B 118 5.512 21.594 19.408 1.00 23.74 C ATOM 2566 CZ TYR B 118 6.301 22.725 19.511 1.00 22.53 C ATOM 2567 OH TYR B 118 7.658 22.634 19.341 1.00 22.91 O ATOM 2568 N VAL B 119 1.577 25.374 22.085 1.00 33.54 N ATOM 2569 CA VAL B 119 2.038 26.587 22.758 1.00 34.40 C ATOM 2570 C VAL B 119 1.817 26.511 24.277 1.00 34.73 C ATOM 2571 O VAL B 119 2.627 27.029 25.046 1.00 36.01 O ATOM 2572 CB VAL B 119 1.365 27.853 22.165 1.00 34.26 C ATOM 2573 CG1 VAL B 119 1.844 29.106 22.885 1.00 30.64 C ATOM 2574 CG2 VAL B 119 1.691 27.963 20.684 1.00 32.59 C ATOM 2575 N LYS B 120 0.740 25.844 24.700 1.00 35.93 N ATOM 2576 CA LYS B 120 0.435 25.679 26.125 1.00 36.66 C ATOM 2577 C LYS B 120 1.476 24.785 26.796 1.00 34.60 C ATOM 2578 O LYS B 120 1.872 25.029 27.934 1.00 33.78 O ATOM 2579 CB LYS B 120 -0.946 25.048 26.318 1.00 42.16 C ATOM 2580 CG LYS B 120 -2.102 25.896 25.826 1.00 52.65 C ATOM 2581 CD LYS B 120 -3.379 25.074 25.754 1.00 59.12 C ATOM 2582 CE LYS B 120 -4.491 25.833 25.036 1.00 64.44 C ATOM 2583 NZ LYS B 120 -5.667 24.959 24.755 1.00 66.81 N ATOM 2584 N ALA B 121 1.914 23.754 26.077 1.00 32.64 N ATOM 2585 CA ALA B 121 2.905 22.807 26.586 1.00 29.72 C ATOM 2586 C ALA B 121 4.346 23.304 26.472 1.00 24.52 C ATOM 2587 O ALA B 121 5.249 22.747 27.094 1.00 26.35 O ATOM 2588 CB ALA B 121 2.759 21.470 25.869 1.00 28.02 C ATOM 2589 N LEU B 122 4.552 24.358 25.687 1.00 22.27 N ATOM 2590 CA LEU B 122 5.882 24.921 25.479 1.00 23.68 C ATOM 2591 C LEU B 122 6.729 25.192 26.726 1.00 23.00 C ATOM 2592 O LEU B 122 7.901 24.812 26.762 1.00 27.31 O ATOM 2593 CB LEU B 122 5.803 26.194 24.635 1.00 21.41 C ATOM 2594 CG LEU B 122 6.473 26.159 23.264 1.00 24.97 C ATOM 2595 CD1 LEU B 122 6.605 27.586 22.754 1.00 20.98 C ATOM 2596 CD2 LEU B 122 7.844 25.500 23.355 1.00 12.67 C ATOM 2597 N PRO B 123 6.167 25.863 27.752 1.00 22.31 N ATOM 2598 CA PRO B 123 6.929 26.156 28.972 1.00 21.71 C ATOM 2599 C PRO B 123 7.599 24.929 29.583 1.00 17.26 C ATOM 2600 O PRO B 123 8.756 24.985 29.994 1.00 19.83 O ATOM 2601 CB PRO B 123 5.867 26.739 29.902 1.00 20.24 C ATOM 2602 CG PRO B 123 4.959 27.445 28.956 1.00 16.94 C ATOM 2603 CD PRO B 123 4.808 26.436 27.845 1.00 19.69 C ATOM 2604 N GLY B 124 6.875 23.815 29.603 1.00 22.52 N ATOM 2605 CA GLY B 124 7.418 22.587 30.155 1.00 18.70 C ATOM 2606 C GLY B 124 8.564 22.068 29.314 1.00 19.03 C ATOM 2607 O GLY B 124 9.505 21.477 29.841 1.00 21.95 O ATOM 2608 N GLN B 125 8.479 22.294 28.004 1.00 20.58 N ATOM 2609 CA GLN B 125 9.508 21.868 27.057 1.00 19.34 C ATOM 2610 C GLN B 125 10.764 22.730 27.133 1.00 20.61 C ATOM 2611 O GLN B 125 11.866 22.246 26.898 1.00 22.56 O ATOM 2612 CB GLN B 125 8.965 21.915 25.630 1.00 16.50 C ATOM 2613 CG GLN B 125 7.808 20.974 25.369 1.00 26.69 C ATOM 2614 CD GLN B 125 8.168 19.542 25.677 1.00 32.99 C ATOM 2615 OE1 GLN B 125 9.177 19.035 25.196 1.00 37.77 O ATOM 2616 NE2 GLN B 125 7.359 18.890 26.494 1.00 40.20 N ATOM 2617 N LEU B 126 10.593 24.010 27.454 1.00 20.58 N ATOM 2618 CA LEU B 126 11.720 24.936 27.544 1.00 20.33 C ATOM 2619 C LEU B 126 12.449 24.947 28.888 1.00 22.06 C ATOM 2620 O LEU B 126 13.640 25.263 28.939 1.00 21.85 O ATOM 2621 CB LEU B 126 11.266 26.354 27.186 1.00 23.94 C ATOM 2622 CG LEU B 126 10.754 26.529 25.755 1.00 23.82 C ATOM 2623 CD1 LEU B 126 10.208 27.935 25.556 1.00 22.77 C ATOM 2624 CD2 LEU B 126 11.876 26.229 24.770 1.00 18.90 C ATOM 2625 N LYS B 127 11.745 24.601 29.968 1.00 22.88 N ATOM 2626 CA LYS B 127 12.349 24.580 31.305 1.00 23.56 C ATOM 2627 C LYS B 127 13.688 23.855 31.419 1.00 19.01 C ATOM 2628 O LYS B 127 14.613 24.371 32.047 1.00 18.84 O ATOM 2629 CB LYS B 127 11.369 24.041 32.351 1.00 31.39 C ATOM 2630 CG LYS B 127 10.523 25.123 32.980 1.00 46.72 C ATOM 2631 CD LYS B 127 9.385 24.558 33.803 1.00 55.29 C ATOM 2632 CE LYS B 127 8.489 25.682 34.305 1.00 58.65 C ATOM 2633 NZ LYS B 127 7.241 25.172 34.936 1.00 64.54 N ATOM 2634 N PRO B 128 13.818 22.654 30.814 1.00 18.13 N ATOM 2635 CA PRO B 128 15.087 21.923 30.896 1.00 14.61 C ATOM 2636 C PRO B 128 16.317 22.741 30.488 1.00 18.54 C ATOM 2637 O PRO B 128 17.377 22.628 31.112 1.00 17.61 O ATOM 2638 CB PRO B 128 14.857 20.750 29.950 1.00 10.90 C ATOM 2639 CG PRO B 128 13.409 20.457 30.156 1.00 14.28 C ATOM 2640 CD PRO B 128 12.796 21.837 30.130 1.00 14.32 C ATOM 2641 N PHE B 129 16.171 23.580 29.462 1.00 17.24 N ATOM 2642 CA PHE B 129 17.288 24.398 28.983 1.00 19.39 C ATOM 2643 C PHE B 129 17.600 25.577 29.910 1.00 19.51 C ATOM 2644 O PHE B 129 18.758 25.980 30.047 1.00 17.23 O ATOM 2645 CB PHE B 129 17.031 24.845 27.543 1.00 19.80 C ATOM 2646 CG PHE B 129 16.763 23.697 26.602 1.00 19.75 C ATOM 2647 CD1 PHE B 129 17.783 22.815 26.249 1.00 25.75 C ATOM 2648 CD2 PHE B 129 15.482 23.466 26.109 1.00 21.30 C ATOM 2649 CE1 PHE B 129 17.528 21.716 25.420 1.00 20.32 C ATOM 2650 CE2 PHE B 129 15.218 22.371 25.280 1.00 18.54 C ATOM 2651 CZ PHE B 129 16.242 21.497 24.938 1.00 17.85 C ATOM 2652 N GLU B 130 16.561 26.112 30.552 1.00 19.92 N ATOM 2653 CA GLU B 130 16.712 27.204 31.513 1.00 22.08 C ATOM 2654 C GLU B 130 17.490 26.636 32.711 1.00 25.40 C ATOM 2655 O GLU B 130 18.383 27.287 33.260 1.00 24.97 O ATOM 2656 CB GLU B 130 15.330 27.693 31.965 1.00 20.31 C ATOM 2657 CG GLU B 130 15.334 28.820 33.008 1.00 30.10 C ATOM 2658 CD GLU B 130 15.671 30.204 32.442 1.00 32.54 C ATOM 2659 OE1 GLU B 130 15.761 30.370 31.208 1.00 32.45 O ATOM 2660 OE2 GLU B 130 15.837 31.147 33.245 1.00 31.25 O ATOM 2661 N THR B 131 17.167 25.392 33.066 1.00 23.53 N ATOM 2662 CA THR B 131 17.807 24.682 34.169 1.00 19.38 C ATOM 2663 C THR B 131 19.283 24.438 33.876 1.00 22.04 C ATOM 2664 O THR B 131 20.140 24.674 34.730 1.00 25.02 O ATOM 2665 CB THR B 131 17.126 23.323 34.411 1.00 24.86 C ATOM 2666 OG1 THR B 131 15.725 23.525 34.636 1.00 21.83 O ATOM 2667 CG2 THR B 131 17.738 22.622 35.618 1.00 21.09 C ATOM 2668 N LEU B 132 19.571 23.933 32.679 1.00 22.06 N ATOM 2669 CA LEU B 132 20.947 23.664 32.268 1.00 22.51 C ATOM 2670 C LEU B 132 21.768 24.944 32.373 1.00 21.76 C ATOM 2671 O LEU B 132 22.879 24.943 32.904 1.00 26.98 O ATOM 2672 CB LEU B 132 20.975 23.139 30.830 1.00 25.09 C ATOM 2673 CG LEU B 132 20.498 21.699 30.626 1.00 27.71 C ATOM 2674 CD1 LEU B 132 20.190 21.434 29.163 1.00 27.30 C ATOM 2675 CD2 LEU B 132 21.558 20.739 31.138 1.00 20.21 C ATOM 2676 N LEU B 133 21.183 26.040 31.902 1.00 22.36 N ATOM 2677 CA LEU B 133 21.818 27.349 31.926 1.00 21.87 C ATOM 2678 C LEU B 133 22.087 27.796 33.364 1.00 23.92 C ATOM 2679 O LEU B 133 23.195 28.224 33.686 1.00 22.09 O ATOM 2680 CB LEU B 133 20.918 28.357 31.203 1.00 22.24 C ATOM 2681 CG LEU B 133 21.485 29.226 30.073 1.00 24.50 C ATOM 2682 CD1 LEU B 133 22.629 28.548 29.351 1.00 17.89 C ATOM 2683 CD2 LEU B 133 20.365 29.566 29.107 1.00 20.75 C ATOM 2684 N SER B 134 21.095 27.641 34.239 1.00 23.80 N ATOM 2685 CA SER B 134 21.242 28.038 35.640 1.00 29.27 C ATOM 2686 C SER B 134 22.329 27.268 36.393 1.00 29.55 C ATOM 2687 O SER B 134 22.887 27.773 37.368 1.00 36.82 O ATOM 2688 CB SER B 134 19.904 27.928 36.387 1.00 27.85 C ATOM 2689 OG SER B 134 19.504 26.580 36.554 1.00 36.33 O ATOM 2690 N GLN B 135 22.641 26.059 35.935 1.00 28.71 N ATOM 2691 CA GLN B 135 23.675 25.245 36.573 1.00 29.09 C ATOM 2692 C GLN B 135 25.072 25.482 36.007 1.00 31.52 C ATOM 2693 O GLN B 135 26.046 24.908 36.492 1.00 32.56 O ATOM 2694 CB GLN B 135 23.319 23.768 36.458 1.00 29.48 C ATOM 2695 CG GLN B 135 22.042 23.406 37.169 1.00 36.83 C ATOM 2696 CD GLN B 135 21.561 22.029 36.797 1.00 42.33 C ATOM 2697 OE1 GLN B 135 22.153 21.359 35.951 1.00 46.11 O ATOM 2698 NE2 GLN B 135 20.480 21.596 37.421 1.00 46.26 N ATOM 2699 N ASN B 136 25.172 26.301 34.967 1.00 30.31 N ATOM 2700 CA ASN B 136 26.457 26.599 34.355 1.00 32.37 C ATOM 2701 C ASN B 136 26.792 28.081 34.523 1.00 34.88 C ATOM 2702 O ASN B 136 26.325 28.919 33.754 1.00 39.57 O ATOM 2703 CB ASN B 136 26.450 26.217 32.867 1.00 28.03 C ATOM 2704 CG ASN B 136 27.793 26.461 32.195 1.00 27.27 C ATOM 2705 OD1 ASN B 136 28.839 26.364 32.835 1.00 32.21 O ATOM 2706 ND2 ASN B 136 27.767 26.728 30.901 1.00 24.89 N ATOM 2707 N GLN B 137 27.587 28.395 35.550 1.00 38.39 N ATOM 2708 CA GLN B 137 27.997 29.774 35.843 1.00 38.87 C ATOM 2709 C GLN B 137 26.836 30.769 35.834 1.00 37.46 C ATOM 2710 O GLN B 137 26.969 31.886 35.325 1.00 38.66 O ATOM 2711 CB GLN B 137 29.068 30.230 34.854 1.00 42.50 C ATOM 2712 CG GLN B 137 30.373 29.467 34.937 1.00 49.41 C ATOM 2713 CD GLN B 137 31.245 29.696 33.716 1.00 59.06 C ATOM 2714 OE1 GLN B 137 31.892 30.742 33.593 1.00 59.66 O ATOM 2715 NE2 GLN B 137 31.247 28.736 32.796 1.00 60.93 N ATOM 2716 N GLY B 138 25.692 30.340 36.365 1.00 33.21 N ATOM 2717 CA GLY B 138 24.521 31.201 36.424 1.00 33.94 C ATOM 2718 C GLY B 138 23.967 31.671 35.089 1.00 33.48 C ATOM 2719 O GLY B 138 23.312 32.710 35.024 1.00 33.52 O ATOM 2720 N GLY B 139 24.219 30.904 34.031 1.00 33.09 N ATOM 2721 CA GLY B 139 23.731 31.260 32.708 1.00 35.23 C ATOM 2722 C GLY B 139 24.418 32.467 32.093 1.00 35.89 C ATOM 2723 O GLY B 139 23.871 33.095 31.189 1.00 38.32 O ATOM 2724 N LYS B 140 25.626 32.768 32.560 1.00 34.34 N ATOM 2725 CA LYS B 140 26.386 33.916 32.068 1.00 38.71 C ATOM 2726 C LYS B 140 27.160 33.641 30.781 1.00 35.47 C ATOM 2727 O LYS B 140 27.484 34.575 30.048 1.00 37.05 O ATOM 2728 CB LYS B 140 27.346 34.427 33.154 1.00 38.79 C ATOM 2729 CG LYS B 140 26.660 34.918 34.427 1.00 48.49 C ATOM 2730 CD LYS B 140 25.961 36.260 34.233 1.00 56.54 C ATOM 2731 CE LYS B 140 26.952 37.417 34.311 1.00 64.72 C ATOM 2732 NZ LYS B 140 26.304 38.745 34.084 1.00 65.93 N ATOM 2733 N THR B 141 27.446 32.369 30.503 1.00 34.07 N ATOM 2734 CA THR B 141 28.197 31.993 29.304 1.00 29.17 C ATOM 2735 C THR B 141 27.407 31.185 28.262 1.00 29.06 C ATOM 2736 O THR B 141 26.446 31.689 27.684 1.00 28.74 O ATOM 2737 CB THR B 141 29.500 31.247 29.665 1.00 26.45 C ATOM 2738 OG1 THR B 141 29.203 30.165 30.556 1.00 31.76 O ATOM 2739 CG2 THR B 141 30.499 32.190 30.318 1.00 31.11 C ATOM 2740 N PHE B 142 27.812 29.937 28.030 1.00 25.37 N ATOM 2741 CA PHE B 142 27.169 29.076 27.046 1.00 21.42 C ATOM 2742 C PHE B 142 26.368 27.947 27.688 1.00 19.43 C ATOM 2743 O PHE B 142 26.341 27.826 28.906 1.00 22.06 O ATOM 2744 CB PHE B 142 28.228 28.548 26.083 1.00 20.30 C ATOM 2745 CG PHE B 142 29.040 29.643 25.436 1.00 17.19 C ATOM 2746 CD1 PHE B 142 28.533 30.359 24.353 1.00 16.59 C ATOM 2747 CD2 PHE B 142 30.294 29.981 25.931 1.00 17.17 C ATOM 2748 CE1 PHE B 142 29.261 31.395 23.778 1.00 16.36 C ATOM 2749 CE2 PHE B 142 31.032 31.016 25.363 1.00 13.88 C ATOM 2750 CZ PHE B 142 30.516 31.723 24.285 1.00 16.14 C ATOM 2751 N ILE B 143 25.698 27.134 26.877 1.00 19.33 N ATOM 2752 CA ILE B 143 24.872 26.056 27.414 1.00 23.03 C ATOM 2753 C ILE B 143 25.676 24.999 28.182 1.00 21.83 C ATOM 2754 O ILE B 143 25.188 24.439 29.164 1.00 25.30 O ATOM 2755 CB ILE B 143 23.978 25.410 26.314 1.00 20.01 C ATOM 2756 CG1 ILE B 143 22.872 24.569 26.957 1.00 19.19 C ATOM 2757 CG2 ILE B 143 24.813 24.566 25.352 1.00 18.10 C ATOM 2758 CD1 ILE B 143 21.853 25.373 27.737 1.00 13.87 C ATOM 2759 N VAL B 144 26.912 24.763 27.751 1.00 17.84 N ATOM 2760 CA VAL B 144 27.804 23.798 28.396 1.00 18.31 C ATOM 2761 C VAL B 144 29.220 24.366 28.418 1.00 21.53 C ATOM 2762 O VAL B 144 29.767 24.714 27.373 1.00 23.94 O ATOM 2763 CB VAL B 144 27.842 22.443 27.643 1.00 15.76 C ATOM 2764 CG1 VAL B 144 28.931 21.547 28.228 1.00 12.79 C ATOM 2765 CG2 VAL B 144 26.496 21.745 27.729 1.00 11.21 C ATOM 2766 N GLY B 145 29.805 24.463 29.609 1.00 21.97 N ATOM 2767 CA GLY B 145 31.159 24.983 29.733 1.00 21.16 C ATOM 2768 C GLY B 145 31.284 26.482 29.523 1.00 25.36 C ATOM 2769 O GLY B 145 30.295 27.212 29.599 1.00 24.11 O ATOM 2770 N ASP B 146 32.502 26.938 29.240 1.00 28.44 N ATOM 2771 CA ASP B 146 32.760 28.361 29.029 1.00 35.74 C ATOM 2772 C ASP B 146 33.186 28.702 27.600 1.00 32.93 C ATOM 2773 O ASP B 146 33.714 29.780 27.342 1.00 34.73 O ATOM 2774 CB ASP B 146 33.797 28.872 30.041 1.00 41.62 C ATOM 2775 CG ASP B 146 35.150 28.181 29.909 1.00 50.06 C ATOM 2776 OD1 ASP B 146 35.261 27.160 29.193 1.00 52.39 O ATOM 2777 OD2 ASP B 146 36.118 28.670 30.528 1.00 58.74 O ATOM 2778 N GLN B 147 32.957 27.769 26.682 1.00 34.08 N ATOM 2779 CA GLN B 147 33.286 27.950 25.271 1.00 30.76 C ATOM 2780 C GLN B 147 32.075 27.471 24.470 1.00 27.26 C ATOM 2781 O GLN B 147 31.377 26.544 24.886 1.00 27.27 O ATOM 2782 CB GLN B 147 34.542 27.154 24.896 1.00 35.52 C ATOM 2783 CG GLN B 147 34.436 25.662 25.188 1.00 51.57 C ATOM 2784 CD GLN B 147 35.614 24.854 24.669 1.00 56.61 C ATOM 2785 OE1 GLN B 147 36.563 24.579 25.410 1.00 59.20 O ATOM 2786 NE2 GLN B 147 35.543 24.436 23.402 1.00 54.77 N ATOM 2787 N ILE B 148 31.802 28.130 23.346 1.00 22.04 N ATOM 2788 CA ILE B 148 30.659 27.783 22.506 1.00 20.51 C ATOM 2789 C ILE B 148 30.803 26.389 21.873 1.00 19.28 C ATOM 2790 O ILE B 148 31.912 25.944 21.571 1.00 12.08 O ATOM 2791 CB ILE B 148 30.427 28.874 21.420 1.00 17.72 C ATOM 2792 CG1 ILE B 148 28.986 28.822 20.916 1.00 17.02 C ATOM 2793 CG2 ILE B 148 31.411 28.706 20.270 1.00 16.29 C ATOM 2794 CD1 ILE B 148 28.544 30.080 20.207 1.00 10.84 C ATOM 2795 N SER B 149 29.682 25.690 21.717 1.00 10.71 N ATOM 2796 CA SER B 149 29.687 24.356 21.129 1.00 15.30 C ATOM 2797 C SER B 149 28.632 24.307 20.034 1.00 15.09 C ATOM 2798 O SER B 149 27.846 25.246 19.893 1.00 16.35 O ATOM 2799 CB SER B 149 29.375 23.300 22.194 1.00 11.53 C ATOM 2800 OG SER B 149 28.020 23.373 22.609 1.00 11.96 O ATOM 2801 N PHE B 150 28.598 23.211 19.274 1.00 14.93 N ATOM 2802 CA PHE B 150 27.614 23.076 18.201 1.00 15.07 C ATOM 2803 C PHE B 150 26.188 23.041 18.748 1.00 13.71 C ATOM 2804 O PHE B 150 25.241 23.424 18.059 1.00 21.42 O ATOM 2805 CB PHE B 150 27.908 21.848 17.315 1.00 13.85 C ATOM 2806 CG PHE B 150 27.701 20.518 18.001 1.00 10.83 C ATOM 2807 CD1 PHE B 150 26.448 19.907 18.007 1.00 9.79 C ATOM 2808 CD2 PHE B 150 28.759 19.875 18.632 1.00 9.69 C ATOM 2809 CE1 PHE B 150 26.254 18.678 18.633 1.00 13.21 C ATOM 2810 CE2 PHE B 150 28.576 18.644 19.263 1.00 10.53 C ATOM 2811 CZ PHE B 150 27.321 18.044 19.263 1.00 11.95 C ATOM 2812 N ALA B 151 26.044 22.603 19.998 1.00 16.31 N ATOM 2813 CA ALA B 151 24.736 22.533 20.646 1.00 14.50 C ATOM 2814 C ALA B 151 24.168 23.939 20.838 1.00 12.67 C ATOM 2815 O ALA B 151 22.953 24.136 20.792 1.00 16.19 O ATOM 2816 CB ALA B 151 24.845 21.807 21.992 1.00 16.55 C ATOM 2817 N ASP B 152 25.053 24.911 21.047 1.00 10.04 N ATOM 2818 CA ASP B 152 24.640 26.297 21.227 1.00 13.99 C ATOM 2819 C ASP B 152 23.923 26.818 19.991 1.00 16.09 C ATOM 2820 O ASP B 152 22.832 27.390 20.096 1.00 13.49 O ATOM 2821 CB ASP B 152 25.851 27.184 21.527 1.00 14.41 C ATOM 2822 CG ASP B 152 26.304 27.086 22.967 1.00 14.53 C ATOM 2823 OD1 ASP B 152 25.525 27.460 23.862 1.00 12.69 O ATOM 2824 OD2 ASP B 152 27.447 26.661 23.205 1.00 15.26 O ATOM 2825 N TYR B 153 24.520 26.588 18.819 1.00 13.47 N ATOM 2826 CA TYR B 153 23.932 27.041 17.555 1.00 17.07 C ATOM 2827 C TYR B 153 22.590 26.376 17.306 1.00 12.24 C ATOM 2828 O TYR B 153 21.647 27.022 16.873 1.00 15.63 O ATOM 2829 CB TYR B 153 24.880 26.766 16.377 1.00 11.50 C ATOM 2830 CG TYR B 153 26.180 27.517 16.484 1.00 9.35 C ATOM 2831 CD1 TYR B 153 26.234 28.896 16.252 1.00 10.53 C ATOM 2832 CD2 TYR B 153 27.348 26.864 16.867 1.00 10.73 C ATOM 2833 CE1 TYR B 153 27.424 29.603 16.405 1.00 9.45 C ATOM 2834 CE2 TYR B 153 28.538 27.556 17.024 1.00 10.44 C ATOM 2835 CZ TYR B 153 28.570 28.925 16.793 1.00 14.51 C ATOM 2836 OH TYR B 153 29.750 29.609 16.961 1.00 18.39 O ATOM 2837 N ASN B 154 22.495 25.088 17.612 1.00 14.67 N ATOM 2838 CA ASN B 154 21.266 24.342 17.407 1.00 13.67 C ATOM 2839 C ASN B 154 20.177 24.800 18.383 1.00 12.76 C ATOM 2840 O ASN B 154 19.012 24.933 18.005 1.00 15.87 O ATOM 2841 CB ASN B 154 21.522 22.838 17.535 1.00 9.31 C ATOM 2842 CG ASN B 154 20.439 22.013 16.872 1.00 16.45 C ATOM 2843 OD1 ASN B 154 19.547 22.556 16.218 1.00 18.35 O ATOM 2844 ND2 ASN B 154 20.524 20.701 17.022 1.00 15.86 N ATOM 2845 N LEU B 155 20.563 25.052 19.632 1.00 14.49 N ATOM 2846 CA LEU B 155 19.601 25.502 20.636 1.00 12.89 C ATOM 2847 C LEU B 155 19.122 26.904 20.259 1.00 12.96 C ATOM 2848 O LEU B 155 17.923 27.188 20.308 1.00 14.73 O ATOM 2849 CB LEU B 155 20.234 25.507 22.034 1.00 12.24 C ATOM 2850 CG LEU B 155 19.373 26.105 23.158 1.00 15.93 C ATOM 2851 CD1 LEU B 155 18.026 25.406 23.245 1.00 9.78 C ATOM 2852 CD2 LEU B 155 20.113 26.008 24.481 1.00 17.15 C ATOM 2853 N LEU B 156 20.059 27.758 19.846 1.00 11.38 N ATOM 2854 CA LEU B 156 19.735 29.127 19.442 1.00 14.38 C ATOM 2855 C LEU B 156 18.696 29.113 18.328 1.00 17.22 C ATOM 2856 O LEU B 156 17.695 29.829 18.398 1.00 17.34 O ATOM 2857 CB LEU B 156 20.990 29.861 18.962 1.00 17.64 C ATOM 2858 CG LEU B 156 20.768 31.321 18.555 1.00 19.65 C ATOM 2859 CD1 LEU B 156 20.232 32.127 19.737 1.00 20.09 C ATOM 2860 CD2 LEU B 156 22.068 31.920 18.056 1.00 16.71 C ATOM 2861 N ASP B 157 18.929 28.286 17.308 1.00 12.93 N ATOM 2862 CA ASP B 157 17.987 28.182 16.200 1.00 12.10 C ATOM 2863 C ASP B 157 16.618 27.749 16.712 1.00 15.07 C ATOM 2864 O ASP B 157 15.595 28.339 16.351 1.00 15.21 O ATOM 2865 CB ASP B 157 18.482 27.186 15.150 1.00 13.31 C ATOM 2866 CG ASP B 157 17.480 26.978 14.029 1.00 18.22 C ATOM 2867 OD1 ASP B 157 17.115 27.969 13.360 1.00 16.95 O ATOM 2868 OD2 ASP B 157 17.064 25.823 13.813 1.00 18.97 O ATOM 2869 N LEU B 158 16.605 26.723 17.562 1.00 16.38 N ATOM 2870 CA LEU B 158 15.353 26.222 18.124 1.00 18.41 C ATOM 2871 C LEU B 158 14.596 27.345 18.849 1.00 15.26 C ATOM 2872 O LEU B 158 13.394 27.518 18.658 1.00 17.12 O ATOM 2873 CB LEU B 158 15.622 25.057 19.084 1.00 15.64 C ATOM 2874 CG LEU B 158 14.379 24.318 19.605 1.00 19.50 C ATOM 2875 CD1 LEU B 158 13.689 23.577 18.466 1.00 17.37 C ATOM 2876 CD2 LEU B 158 14.768 23.344 20.698 1.00 16.11 C ATOM 2877 N LEU B 159 15.316 28.139 19.635 1.00 14.85 N ATOM 2878 CA LEU B 159 14.698 29.241 20.375 1.00 15.96 C ATOM 2879 C LEU B 159 14.142 30.323 19.446 1.00 15.59 C ATOM 2880 O LEU B 159 13.007 30.769 19.615 1.00 17.40 O ATOM 2881 CB LEU B 159 15.702 29.839 21.364 1.00 16.12 C ATOM 2882 CG LEU B 159 16.201 28.856 22.431 1.00 16.52 C ATOM 2883 CD1 LEU B 159 17.284 29.483 23.291 1.00 13.09 C ATOM 2884 CD2 LEU B 159 15.033 28.394 23.284 1.00 11.26 C ATOM 2885 N LEU B 160 14.929 30.707 18.443 1.00 20.00 N ATOM 2886 CA LEU B 160 14.516 31.723 17.477 1.00 16.53 C ATOM 2887 C LEU B 160 13.251 31.351 16.709 1.00 18.82 C ATOM 2888 O LEU B 160 12.353 32.186 16.562 1.00 23.62 O ATOM 2889 CB LEU B 160 15.648 32.025 16.493 1.00 10.59 C ATOM 2890 CG LEU B 160 16.904 32.675 17.080 1.00 9.52 C ATOM 2891 CD1 LEU B 160 17.960 32.798 16.002 1.00 11.92 C ATOM 2892 CD2 LEU B 160 16.577 34.042 17.657 1.00 13.66 C ATOM 2893 N ILE B 161 13.153 30.108 16.236 1.00 16.27 N ATOM 2894 CA ILE B 161 11.962 29.704 15.484 1.00 16.31 C ATOM 2895 C ILE B 161 10.726 29.613 16.370 1.00 20.48 C ATOM 2896 O ILE B 161 9.599 29.691 15.876 1.00 17.32 O ATOM 2897 CB ILE B 161 12.159 28.382 14.692 1.00 20.84 C ATOM 2898 CG1 ILE B 161 12.388 27.200 15.636 1.00 20.14 C ATOM 2899 CG2 ILE B 161 13.312 28.530 13.712 1.00 17.48 C ATOM 2900 CD1 ILE B 161 12.634 25.887 14.913 1.00 22.07 C ATOM 2901 N HIS B 162 10.935 29.438 17.676 1.00 20.52 N ATOM 2902 CA HIS B 162 9.816 29.376 18.612 1.00 21.87 C ATOM 2903 C HIS B 162 9.335 30.778 18.957 1.00 21.47 C ATOM 2904 O HIS B 162 8.171 30.970 19.300 1.00 19.89 O ATOM 2905 CB HIS B 162 10.176 28.583 19.871 1.00 20.72 C ATOM 2906 CG HIS B 162 10.007 27.104 19.709 1.00 19.31 C ATOM 2907 ND1 HIS B 162 11.021 26.287 19.255 1.00 17.48 N ATOM 2908 CD2 HIS B 162 8.932 26.305 19.886 1.00 18.21 C ATOM 2909 CE1 HIS B 162 10.573 25.049 19.153 1.00 14.12 C ATOM 2910 NE2 HIS B 162 9.309 25.031 19.529 1.00 15.10 N ATOM 2911 N GLU B 163 10.245 31.749 18.880 1.00 22.78 N ATOM 2912 CA GLU B 163 9.905 33.148 19.121 1.00 24.84 C ATOM 2913 C GLU B 163 8.949 33.560 18.006 1.00 23.79 C ATOM 2914 O GLU B 163 8.013 34.322 18.223 1.00 30.64 O ATOM 2915 CB GLU B 163 11.157 34.021 19.066 1.00 30.78 C ATOM 2916 CG GLU B 163 11.764 34.343 20.422 1.00 43.50 C ATOM 2917 CD GLU B 163 10.884 35.262 21.257 1.00 55.98 C ATOM 2918 OE1 GLU B 163 10.274 36.192 20.684 1.00 60.36 O ATOM 2919 OE2 GLU B 163 10.814 35.064 22.491 1.00 61.63 O ATOM 2920 N VAL B 164 9.188 33.024 16.812 1.00 25.34 N ATOM 2921 CA VAL B 164 8.352 33.307 15.651 1.00 24.08 C ATOM 2922 C VAL B 164 7.006 32.593 15.788 1.00 29.96 C ATOM 2923 O VAL B 164 5.963 33.160 15.465 1.00 34.15 O ATOM 2924 CB VAL B 164 9.043 32.854 14.337 1.00 22.81 C ATOM 2925 CG1 VAL B 164 8.125 33.090 13.140 1.00 20.40 C ATOM 2926 CG2 VAL B 164 10.359 33.598 14.150 1.00 17.22 C ATOM 2927 N LEU B 165 7.035 31.355 16.276 1.00 29.54 N ATOM 2928 CA LEU B 165 5.817 30.565 16.453 1.00 27.52 C ATOM 2929 C LEU B 165 4.922 31.116 17.560 1.00 31.18 C ATOM 2930 O LEU B 165 3.726 31.327 17.360 1.00 30.02 O ATOM 2931 CB LEU B 165 6.174 29.111 16.768 1.00 27.36 C ATOM 2932 CG LEU B 165 5.005 28.153 17.012 1.00 24.81 C ATOM 2933 CD1 LEU B 165 4.270 27.880 15.707 1.00 28.26 C ATOM 2934 CD2 LEU B 165 5.521 26.859 17.605 1.00 25.85 C ATOM 2935 N ALA B 166 5.516 31.325 18.731 1.00 32.61 N ATOM 2936 CA ALA B 166 4.808 31.837 19.896 1.00 28.03 C ATOM 2937 C ALA B 166 5.573 33.037 20.436 1.00 29.47 C ATOM 2938 O ALA B 166 6.410 32.898 21.328 1.00 27.43 O ATOM 2939 CB ALA B 166 4.706 30.753 20.961 1.00 24.54 C ATOM 2940 N PRO B 167 5.316 34.232 19.875 1.00 29.66 N ATOM 2941 CA PRO B 167 5.978 35.472 20.294 1.00 26.74 C ATOM 2942 C PRO B 167 5.890 35.695 21.801 1.00 26.93 C ATOM 2943 O PRO B 167 4.812 35.612 22.392 1.00 28.15 O ATOM 2944 CB PRO B 167 5.208 36.542 19.521 1.00 27.68 C ATOM 2945 CG PRO B 167 4.843 35.834 18.259 1.00 27.80 C ATOM 2946 CD PRO B 167 4.365 34.497 18.778 1.00 27.30 C ATOM 2947 N GLY B 168 7.040 35.938 22.419 1.00 28.32 N ATOM 2948 CA GLY B 168 7.082 36.167 23.850 1.00 28.39 C ATOM 2949 C GLY B 168 7.144 34.914 24.707 1.00 31.42 C ATOM 2950 O GLY B 168 7.100 35.012 25.931 1.00 32.53 O ATOM 2951 N CYS B 169 7.250 33.741 24.083 1.00 27.03 N ATOM 2952 CA CYS B 169 7.323 32.484 24.830 1.00 26.35 C ATOM 2953 C CYS B 169 8.541 32.426 25.758 1.00 26.61 C ATOM 2954 O CYS B 169 8.551 31.667 26.724 1.00 34.29 O ATOM 2955 CB CYS B 169 7.335 31.282 23.877 1.00 25.43 C ATOM 2956 SG CYS B 169 8.792 31.171 22.808 1.00 25.37 S ATOM 2957 N LEU B 170 9.561 33.229 25.461 1.00 28.46 N ATOM 2958 CA LEU B 170 10.781 33.282 26.271 1.00 26.87 C ATOM 2959 C LEU B 170 10.742 34.301 27.416 1.00 29.62 C ATOM 2960 O LEU B 170 11.709 34.420 28.173 1.00 25.36 O ATOM 2961 CB LEU B 170 11.992 33.575 25.384 1.00 25.97 C ATOM 2962 CG LEU B 170 12.803 32.394 24.848 1.00 28.21 C ATOM 2963 CD1 LEU B 170 11.902 31.383 24.160 1.00 26.98 C ATOM 2964 CD2 LEU B 170 13.872 32.913 23.900 1.00 22.98 C ATOM 2965 N ASP B 171 9.640 35.040 27.532 1.00 30.40 N ATOM 2966 CA ASP B 171 9.488 36.048 28.585 1.00 32.42 C ATOM 2967 C ASP B 171 9.623 35.456 29.982 1.00 31.61 C ATOM 2968 O ASP B 171 10.257 36.049 30.855 1.00 29.65 O ATOM 2969 CB ASP B 171 8.133 36.755 28.467 1.00 33.03 C ATOM 2970 CG ASP B 171 8.071 37.724 27.298 1.00 37.32 C ATOM 2971 OD1 ASP B 171 9.138 38.086 26.753 1.00 34.25 O ATOM 2972 OD2 ASP B 171 6.946 38.132 26.930 1.00 34.04 O ATOM 2973 N ALA B 172 9.037 34.277 30.175 1.00 29.44 N ATOM 2974 CA ALA B 172 9.076 33.582 31.458 1.00 26.95 C ATOM 2975 C ALA B 172 10.435 32.960 31.791 1.00 25.40 C ATOM 2976 O ALA B 172 10.623 32.432 32.886 1.00 28.29 O ATOM 2977 CB ALA B 172 7.992 32.508 31.491 1.00 29.79 C ATOM 2978 N PHE B 173 11.381 33.032 30.859 1.00 24.25 N ATOM 2979 CA PHE B 173 12.701 32.443 31.066 1.00 21.71 C ATOM 2980 C PHE B 173 13.825 33.463 30.910 1.00 23.67 C ATOM 2981 O PHE B 173 14.427 33.581 29.844 1.00 30.17 O ATOM 2982 CB PHE B 173 12.902 31.277 30.094 1.00 24.75 C ATOM 2983 CG PHE B 173 11.837 30.219 30.191 1.00 22.15 C ATOM 2984 CD1 PHE B 173 11.906 29.234 31.171 1.00 20.75 C ATOM 2985 CD2 PHE B 173 10.749 30.229 29.323 1.00 18.88 C ATOM 2986 CE1 PHE B 173 10.904 28.276 31.290 1.00 21.32 C ATOM 2987 CE2 PHE B 173 9.740 29.275 29.432 1.00 22.97 C ATOM 2988 CZ PHE B 173 9.818 28.296 30.419 1.00 22.28 C ATOM 2989 N PRO B 174 14.159 34.175 31.998 1.00 26.80 N ATOM 2990 CA PRO B 174 15.211 35.196 32.015 1.00 25.62 C ATOM 2991 C PRO B 174 16.584 34.781 31.492 1.00 25.00 C ATOM 2992 O PRO B 174 17.246 35.562 30.809 1.00 31.27 O ATOM 2993 CB PRO B 174 15.255 35.625 33.487 1.00 22.08 C ATOM 2994 CG PRO B 174 14.677 34.453 34.223 1.00 22.18 C ATOM 2995 CD PRO B 174 13.551 34.038 33.333 1.00 24.14 C ATOM 2996 N LEU B 175 17.018 33.566 31.814 1.00 24.34 N ATOM 2997 CA LEU B 175 18.320 33.078 31.359 1.00 20.62 C ATOM 2998 C LEU B 175 18.340 32.767 29.861 1.00 22.51 C ATOM 2999 O LEU B 175 19.303 33.096 29.170 1.00 17.17 O ATOM 3000 CB LEU B 175 18.747 31.853 32.170 1.00 23.80 C ATOM 3001 CG LEU B 175 19.588 32.073 33.435 1.00 23.93 C ATOM 3002 CD1 LEU B 175 19.345 33.431 34.057 1.00 21.68 C ATOM 3003 CD2 LEU B 175 19.298 30.969 34.420 1.00 20.50 C ATOM 3004 N LEU B 176 17.277 32.143 29.359 1.00 20.38 N ATOM 3005 CA LEU B 176 17.193 31.824 27.939 1.00 22.75 C ATOM 3006 C LEU B 176 17.136 33.113 27.117 1.00 27.36 C ATOM 3007 O LEU B 176 17.803 33.221 26.087 1.00 26.22 O ATOM 3008 CB LEU B 176 15.972 30.946 27.643 1.00 17.98 C ATOM 3009 CG LEU B 176 16.059 29.481 28.085 1.00 19.14 C ATOM 3010 CD1 LEU B 176 14.751 28.769 27.786 1.00 13.79 C ATOM 3011 CD2 LEU B 176 17.216 28.783 27.379 1.00 20.71 C ATOM 3012 N SER B 177 16.373 34.095 27.598 1.00 22.20 N ATOM 3013 CA SER B 177 16.242 35.385 26.919 1.00 22.70 C ATOM 3014 C SER B 177 17.585 36.099 26.816 1.00 20.12 C ATOM 3015 O SER B 177 17.950 36.600 25.751 1.00 16.16 O ATOM 3016 CB SER B 177 15.242 36.279 27.653 1.00 25.67 C ATOM 3017 OG SER B 177 13.941 35.722 27.614 1.00 27.61 O ATOM 3018 N ALA B 178 18.318 36.141 27.924 1.00 12.08 N ATOM 3019 CA ALA B 178 19.623 36.786 27.942 1.00 12.63 C ATOM 3020 C ALA B 178 20.579 36.019 27.036 1.00 20.42 C ATOM 3021 O ALA B 178 21.392 36.614 26.325 1.00 24.13 O ATOM 3022 CB ALA B 178 20.168 36.831 29.363 1.00 10.47 C ATOM 3023 N TYR B 179 20.468 34.693 27.079 1.00 26.21 N ATOM 3024 CA TYR B 179 21.291 33.784 26.279 1.00 21.36 C ATOM 3025 C TYR B 179 21.106 34.087 24.790 1.00 16.25 C ATOM 3026 O TYR B 179 22.082 34.258 24.061 1.00 17.66 O ATOM 3027 CB TYR B 179 20.892 32.339 26.609 1.00 22.39 C ATOM 3028 CG TYR B 179 21.514 31.257 25.759 1.00 17.96 C ATOM 3029 CD1 TYR B 179 22.831 30.842 25.963 1.00 16.55 C ATOM 3030 CD2 TYR B 179 20.759 30.598 24.786 1.00 22.96 C ATOM 3031 CE1 TYR B 179 23.378 29.792 25.222 1.00 13.49 C ATOM 3032 CE2 TYR B 179 21.295 29.549 24.041 1.00 16.87 C ATOM 3033 CZ TYR B 179 22.598 29.151 24.264 1.00 19.04 C ATOM 3034 OH TYR B 179 23.110 28.108 23.527 1.00 22.39 O ATOM 3035 N VAL B 180 19.850 34.194 24.362 1.00 14.69 N ATOM 3036 CA VAL B 180 19.513 34.500 22.973 1.00 19.93 C ATOM 3037 C VAL B 180 20.072 35.863 22.559 1.00 23.03 C ATOM 3038 O VAL B 180 20.697 35.980 21.510 1.00 27.98 O ATOM 3039 CB VAL B 180 17.978 34.484 22.745 1.00 20.59 C ATOM 3040 CG1 VAL B 180 17.625 35.055 21.374 1.00 17.36 C ATOM 3041 CG2 VAL B 180 17.452 33.068 22.856 1.00 24.86 C ATOM 3042 N GLY B 181 19.865 36.879 23.395 1.00 25.76 N ATOM 3043 CA GLY B 181 20.361 38.210 23.083 1.00 19.47 C ATOM 3044 C GLY B 181 21.875 38.254 22.999 1.00 23.23 C ATOM 3045 O GLY B 181 22.445 38.877 22.102 1.00 25.56 O ATOM 3046 N ARG B 182 22.522 37.554 23.923 1.00 20.89 N ATOM 3047 CA ARG B 182 23.978 37.496 23.994 1.00 21.36 C ATOM 3048 C ARG B 182 24.591 36.826 22.759 1.00 25.10 C ATOM 3049 O ARG B 182 25.530 37.356 22.162 1.00 25.87 O ATOM 3050 CB ARG B 182 24.393 36.743 25.260 1.00 16.90 C ATOM 3051 CG ARG B 182 25.872 36.818 25.602 1.00 24.25 C ATOM 3052 CD ARG B 182 26.198 35.901 26.779 1.00 25.43 C ATOM 3053 NE ARG B 182 25.217 36.053 27.848 1.00 33.34 N ATOM 3054 CZ ARG B 182 24.516 35.055 28.377 1.00 33.74 C ATOM 3055 NH1 ARG B 182 24.685 33.808 27.956 1.00 30.68 N ATOM 3056 NH2 ARG B 182 23.594 35.315 29.291 1.00 33.52 N ATOM 3057 N LEU B 183 24.069 35.659 22.384 1.00 24.67 N ATOM 3058 CA LEU B 183 24.586 34.942 21.220 1.00 25.51 C ATOM 3059 C LEU B 183 24.290 35.679 19.910 1.00 25.86 C ATOM 3060 O LEU B 183 25.139 35.736 19.024 1.00 21.11 O ATOM 3061 CB LEU B 183 24.045 33.510 21.165 1.00 19.82 C ATOM 3062 CG LEU B 183 24.545 32.516 22.220 1.00 22.88 C ATOM 3063 CD1 LEU B 183 24.214 31.104 21.769 1.00 23.82 C ATOM 3064 CD2 LEU B 183 26.046 32.644 22.408 1.00 23.87 C ATOM 3065 N SER B 184 23.088 36.246 19.806 1.00 25.81 N ATOM 3066 CA SER B 184 22.673 37.002 18.627 1.00 23.93 C ATOM 3067 C SER B 184 23.539 38.243 18.419 1.00 28.11 C ATOM 3068 O SER B 184 23.526 38.835 17.337 1.00 31.16 O ATOM 3069 CB SER B 184 21.222 37.457 18.768 1.00 14.90 C ATOM 3070 OG SER B 184 20.335 36.362 18.844 1.00 30.76 O ATOM 3071 N ALA B 185 24.266 38.642 19.462 1.00 26.80 N ATOM 3072 CA ALA B 185 25.122 39.823 19.411 1.00 27.09 C ATOM 3073 C ALA B 185 26.542 39.550 18.918 1.00 28.52 C ATOM 3074 O ALA B 185 27.303 40.486 18.666 1.00 30.61 O ATOM 3075 CB ALA B 185 25.160 40.503 20.777 1.00 21.64 C ATOM 3076 N ARG B 186 26.911 38.278 18.801 1.00 25.71 N ATOM 3077 CA ARG B 186 28.247 37.925 18.324 1.00 23.55 C ATOM 3078 C ARG B 186 28.400 38.520 16.923 1.00 22.21 C ATOM 3079 O ARG B 186 27.537 38.330 16.069 1.00 23.51 O ATOM 3080 CB ARG B 186 28.419 36.402 18.319 1.00 19.99 C ATOM 3081 CG ARG B 186 28.309 35.792 19.719 1.00 21.64 C ATOM 3082 CD ARG B 186 28.265 34.267 19.701 1.00 16.75 C ATOM 3083 NE ARG B 186 29.456 33.685 19.091 1.00 11.01 N ATOM 3084 CZ ARG B 186 30.578 33.396 19.744 1.00 17.73 C ATOM 3085 NH1 ARG B 186 30.676 33.621 21.050 1.00 17.95 N ATOM 3086 NH2 ARG B 186 31.604 32.869 19.090 1.00 10.28 N ATOM 3087 N PRO B 187 29.488 39.274 16.686 1.00 22.42 N ATOM 3088 CA PRO B 187 29.827 39.950 15.425 1.00 24.57 C ATOM 3089 C PRO B 187 29.441 39.247 14.115 1.00 26.00 C ATOM 3090 O PRO B 187 28.553 39.717 13.390 1.00 25.25 O ATOM 3091 CB PRO B 187 31.335 40.139 15.548 1.00 24.22 C ATOM 3092 CG PRO B 187 31.496 40.416 16.994 1.00 27.95 C ATOM 3093 CD PRO B 187 30.617 39.361 17.630 1.00 23.17 C ATOM 3094 N LYS B 188 30.106 38.132 13.817 1.00 23.67 N ATOM 3095 CA LYS B 188 29.845 37.374 12.593 1.00 23.78 C ATOM 3096 C LYS B 188 28.436 36.797 12.510 1.00 20.64 C ATOM 3097 O LYS B 188 27.838 36.774 11.434 1.00 25.30 O ATOM 3098 CB LYS B 188 30.881 36.265 12.427 1.00 20.40 C ATOM 3099 CG LYS B 188 32.297 36.785 12.316 1.00 24.48 C ATOM 3100 CD LYS B 188 33.317 35.663 12.365 1.00 36.35 C ATOM 3101 CE LYS B 188 34.731 36.219 12.413 1.00 43.75 C ATOM 3102 NZ LYS B 188 34.991 37.115 11.248 1.00 55.43 N ATOM 3103 N LEU B 189 27.900 36.357 13.647 1.00 23.46 N ATOM 3104 CA LEU B 189 26.554 35.785 13.697 1.00 21.09 C ATOM 3105 C LEU B 189 25.487 36.847 13.462 1.00 21.58 C ATOM 3106 O LEU B 189 24.491 36.594 12.780 1.00 23.91 O ATOM 3107 CB LEU B 189 26.301 35.116 15.050 1.00 22.39 C ATOM 3108 CG LEU B 189 25.680 33.717 15.053 1.00 21.83 C ATOM 3109 CD1 LEU B 189 25.217 33.395 16.463 1.00 25.64 C ATOM 3110 CD2 LEU B 189 24.513 33.625 14.092 1.00 18.77 C ATOM 3111 N LYS B 190 25.695 38.025 14.049 1.00 21.42 N ATOM 3112 CA LYS B 190 24.762 39.142 13.912 1.00 24.54 C ATOM 3113 C LYS B 190 24.663 39.571 12.448 1.00 22.51 C ATOM 3114 O LYS B 190 23.568 39.802 11.932 1.00 18.33 O ATOM 3115 CB LYS B 190 25.213 40.329 14.764 1.00 23.82 C ATOM 3116 CG LYS B 190 24.250 41.493 14.713 1.00 30.28 C ATOM 3117 CD LYS B 190 24.779 42.685 15.469 1.00 34.82 C ATOM 3118 CE LYS B 190 23.784 43.830 15.405 1.00 40.28 C ATOM 3119 NZ LYS B 190 24.286 45.018 16.141 1.00 49.70 N ATOM 3120 N ALA B 191 25.819 39.665 11.794 1.00 19.36 N ATOM 3121 CA ALA B 191 25.898 40.042 10.385 1.00 23.33 C ATOM 3122 C ALA B 191 25.154 39.015 9.527 1.00 24.35 C ATOM 3123 O ALA B 191 24.355 39.377 8.661 1.00 27.15 O ATOM 3124 CB ALA B 191 27.357 40.133 9.957 1.00 16.25 C ATOM 3125 N PHE B 192 25.393 37.733 9.803 1.00 26.56 N ATOM 3126 CA PHE B 192 24.747 36.647 9.071 1.00 23.56 C ATOM 3127 C PHE B 192 23.232 36.623 9.256 1.00 20.20 C ATOM 3128 O PHE B 192 22.489 36.459 8.290 1.00 22.15 O ATOM 3129 CB PHE B 192 25.346 35.292 9.473 1.00 24.14 C ATOM 3130 CG PHE B 192 24.670 34.111 8.822 1.00 24.70 C ATOM 3131 CD1 PHE B 192 24.921 33.794 7.488 1.00 25.11 C ATOM 3132 CD2 PHE B 192 23.762 33.329 9.536 1.00 20.51 C ATOM 3133 CE1 PHE B 192 24.274 32.721 6.871 1.00 22.20 C ATOM 3134 CE2 PHE B 192 23.110 32.256 8.930 1.00 22.34 C ATOM 3135 CZ PHE B 192 23.367 31.951 7.593 1.00 19.70 C ATOM 3136 N LEU B 193 22.773 36.789 10.492 1.00 19.04 N ATOM 3137 CA LEU B 193 21.336 36.771 10.775 1.00 21.91 C ATOM 3138 C LEU B 193 20.581 37.923 10.123 1.00 23.67 C ATOM 3139 O LEU B 193 19.370 37.834 9.914 1.00 24.03 O ATOM 3140 CB LEU B 193 21.076 36.772 12.286 1.00 17.76 C ATOM 3141 CG LEU B 193 21.483 35.511 13.052 1.00 24.07 C ATOM 3142 CD1 LEU B 193 21.284 35.724 14.541 1.00 23.33 C ATOM 3143 CD2 LEU B 193 20.676 34.320 12.567 1.00 19.04 C ATOM 3144 N ALA B 194 21.300 38.993 9.790 1.00 22.81 N ATOM 3145 CA ALA B 194 20.686 40.157 9.166 1.00 22.80 C ATOM 3146 C ALA B 194 20.754 40.134 7.639 1.00 25.52 C ATOM 3147 O ALA B 194 20.049 40.896 6.977 1.00 29.76 O ATOM 3148 CB ALA B 194 21.328 41.430 9.699 1.00 19.44 C ATOM 3149 N SER B 195 21.581 39.247 7.087 1.00 26.56 N ATOM 3150 CA SER B 195 21.767 39.134 5.634 1.00 25.66 C ATOM 3151 C SER B 195 20.570 38.551 4.875 1.00 26.69 C ATOM 3152 O SER B 195 19.751 37.834 5.450 1.00 28.26 O ATOM 3153 CB SER B 195 23.009 38.296 5.336 1.00 23.10 C ATOM 3154 OG SER B 195 22.754 36.920 5.553 1.00 29.46 O ATOM 3155 N PRO B 196 20.459 38.850 3.566 1.00 26.01 N ATOM 3156 CA PRO B 196 19.368 38.363 2.712 1.00 24.55 C ATOM 3157 C PRO B 196 19.424 36.837 2.613 1.00 24.15 C ATOM 3158 O PRO B 196 18.404 36.167 2.472 1.00 22.73 O ATOM 3159 CB PRO B 196 19.684 38.997 1.354 1.00 23.65 C ATOM 3160 CG PRO B 196 20.451 40.225 1.711 1.00 26.05 C ATOM 3161 CD PRO B 196 21.359 39.731 2.794 1.00 24.65 C ATOM 3162 N GLU B 197 20.648 36.319 2.669 1.00 20.70 N ATOM 3163 CA GLU B 197 20.949 34.893 2.601 1.00 22.38 C ATOM 3164 C GLU B 197 20.135 34.114 3.635 1.00 26.67 C ATOM 3165 O GLU B 197 19.642 33.013 3.363 1.00 25.57 O ATOM 3166 CB GLU B 197 22.436 34.720 2.888 1.00 26.03 C ATOM 3167 CG GLU B 197 23.027 33.392 2.540 1.00 28.07 C ATOM 3168 CD GLU B 197 24.517 33.359 2.798 1.00 31.05 C ATOM 3169 OE1 GLU B 197 25.173 34.412 2.628 1.00 34.49 O ATOM 3170 OE2 GLU B 197 25.031 32.280 3.159 1.00 38.12 O ATOM 3171 N TYR B 198 20.005 34.702 4.823 1.00 25.70 N ATOM 3172 CA TYR B 198 19.261 34.105 5.923 1.00 19.98 C ATOM 3173 C TYR B 198 17.818 34.610 5.957 1.00 21.34 C ATOM 3174 O TYR B 198 16.867 33.826 5.883 1.00 24.11 O ATOM 3175 CB TYR B 198 19.967 34.420 7.254 1.00 19.33 C ATOM 3176 CG TYR B 198 19.226 33.955 8.490 1.00 24.19 C ATOM 3177 CD1 TYR B 198 19.427 32.677 9.012 1.00 28.61 C ATOM 3178 CD2 TYR B 198 18.309 34.789 9.127 1.00 22.65 C ATOM 3179 CE1 TYR B 198 18.727 32.239 10.140 1.00 29.02 C ATOM 3180 CE2 TYR B 198 17.608 34.367 10.249 1.00 28.33 C ATOM 3181 CZ TYR B 198 17.817 33.092 10.750 1.00 30.29 C ATOM 3182 OH TYR B 198 17.103 32.675 11.849 1.00 29.25 O ATOM 3183 N VAL B 199 17.670 35.927 6.049 1.00 20.52 N ATOM 3184 CA VAL B 199 16.366 36.582 6.134 1.00 18.57 C ATOM 3185 C VAL B 199 15.352 36.264 5.038 1.00 19.49 C ATOM 3186 O VAL B 199 14.171 36.078 5.326 1.00 20.62 O ATOM 3187 CB VAL B 199 16.534 38.123 6.238 1.00 20.57 C ATOM 3188 CG1 VAL B 199 15.184 38.817 6.206 1.00 16.74 C ATOM 3189 CG2 VAL B 199 17.271 38.484 7.512 1.00 15.97 C ATOM 3190 N ASN B 200 15.803 36.184 3.790 1.00 22.85 N ATOM 3191 CA ASN B 200 14.886 35.928 2.675 1.00 24.75 C ATOM 3192 C ASN B 200 14.529 34.473 2.387 1.00 24.89 C ATOM 3193 O ASN B 200 13.881 34.168 1.385 1.00 27.66 O ATOM 3194 CB ASN B 200 15.377 36.642 1.412 1.00 25.85 C ATOM 3195 CG ASN B 200 15.353 38.154 1.561 1.00 27.06 C ATOM 3196 OD1 ASN B 200 14.457 38.706 2.201 1.00 25.98 O ATOM 3197 ND2 ASN B 200 16.351 38.828 1.000 1.00 24.47 N ATOM 3198 N LEU B 201 14.936 33.584 3.283 1.00 24.34 N ATOM 3199 CA LEU B 201 14.641 32.164 3.155 1.00 25.53 C ATOM 3200 C LEU B 201 13.515 31.839 4.129 1.00 23.67 C ATOM 3201 O LEU B 201 13.528 32.304 5.271 1.00 24.51 O ATOM 3202 CB LEU B 201 15.881 31.355 3.532 1.00 23.76 C ATOM 3203 CG LEU B 201 16.493 30.419 2.496 1.00 25.37 C ATOM 3204 CD1 LEU B 201 16.619 31.110 1.151 1.00 14.82 C ATOM 3205 CD2 LEU B 201 17.848 29.953 3.002 1.00 24.74 C ATOM 3206 N PRO B 202 12.488 31.097 3.676 1.00 24.64 N ATOM 3207 CA PRO B 202 11.390 30.756 4.594 1.00 24.48 C ATOM 3208 C PRO B 202 11.907 29.747 5.625 1.00 25.08 C ATOM 3209 O PRO B 202 12.851 29.003 5.345 1.00 24.30 O ATOM 3210 CB PRO B 202 10.350 30.134 3.662 1.00 19.43 C ATOM 3211 CG PRO B 202 11.187 29.505 2.596 1.00 18.26 C ATOM 3212 CD PRO B 202 12.232 30.566 2.328 1.00 19.55 C ATOM 3213 N ILE B 203 11.325 29.746 6.822 1.00 21.21 N ATOM 3214 CA ILE B 203 11.769 28.824 7.865 1.00 25.05 C ATOM 3215 C ILE B 203 11.506 27.368 7.468 1.00 23.81 C ATOM 3216 O ILE B 203 12.410 26.528 7.505 1.00 19.68 O ATOM 3217 CB ILE B 203 11.087 29.126 9.234 1.00 24.97 C ATOM 3218 CG1 ILE B 203 11.539 30.496 9.751 1.00 21.90 C ATOM 3219 CG2 ILE B 203 11.443 28.047 10.257 1.00 17.71 C ATOM 3220 CD1 ILE B 203 10.893 30.904 11.060 1.00 28.08 C ATOM 3221 N ASN B 204 10.273 27.098 7.053 1.00 21.16 N ATOM 3222 CA ASN B 204 9.868 25.757 6.658 1.00 25.06 C ATOM 3223 C ASN B 204 9.429 25.659 5.195 1.00 27.97 C ATOM 3224 O ASN B 204 9.132 26.666 4.548 1.00 23.05 O ATOM 3225 CB ASN B 204 8.749 25.268 7.586 1.00 23.58 C ATOM 3226 CG ASN B 204 9.135 25.365 9.053 1.00 25.14 C ATOM 3227 OD1 ASN B 204 10.094 24.730 9.492 1.00 17.03 O ATOM 3228 ND2 ASN B 204 8.392 26.159 9.813 1.00 23.78 N ATOM 3229 N GLY B 205 9.396 24.430 4.688 1.00 30.19 N ATOM 3230 CA GLY B 205 9.018 24.184 3.311 1.00 26.72 C ATOM 3231 C GLY B 205 7.556 24.355 2.944 1.00 30.67 C ATOM 3232 O GLY B 205 7.223 24.334 1.761 1.00 36.72 O ATOM 3233 N ASN B 206 6.676 24.527 3.925 1.00 28.40 N ATOM 3234 CA ASN B 206 5.256 24.695 3.624 1.00 26.69 C ATOM 3235 C ASN B 206 4.724 26.105 3.889 1.00 31.27 C ATOM 3236 O ASN B 206 3.511 26.327 3.918 1.00 30.68 O ATOM 3237 CB ASN B 206 4.406 23.646 4.359 1.00 27.24 C ATOM 3238 CG ASN B 206 4.395 23.837 5.869 1.00 30.67 C ATOM 3239 OD1 ASN B 206 5.209 24.572 6.426 1.00 30.77 O ATOM 3240 ND2 ASN B 206 3.457 23.173 6.537 1.00 27.18 N ATOM 3241 N GLY B 207 5.634 27.054 4.089 1.00 33.79 N ATOM 3242 CA GLY B 207 5.230 28.428 4.331 1.00 39.51 C ATOM 3243 C GLY B 207 4.623 28.715 5.693 1.00 42.29 C ATOM 3244 O GLY B 207 4.155 29.828 5.936 1.00 45.87 O ATOM 3245 N LYS B 208 4.597 27.717 6.571 1.00 38.26 N ATOM 3246 CA LYS B 208 4.056 27.909 7.911 1.00 33.75 C ATOM 3247 C LYS B 208 5.206 28.170 8.878 1.00 32.71 C ATOM 3248 O LYS B 208 6.328 27.720 8.647 1.00 30.30 O ATOM 3249 CB LYS B 208 3.233 26.695 8.341 1.00 34.70 C ATOM 3250 CG LYS B 208 2.007 26.480 7.474 1.00 34.73 C ATOM 3251 CD LYS B 208 1.195 25.291 7.926 1.00 36.87 C ATOM 3252 CE LYS B 208 -0.012 25.107 7.027 1.00 37.22 C ATOM 3253 NZ LYS B 208 -0.843 23.951 7.447 1.00 41.92 N ATOM 3254 N GLN B 209 4.930 28.935 9.932 1.00 31.28 N ATOM 3255 CA GLN B 209 5.937 29.288 10.932 1.00 30.34 C ATOM 3256 C GLN B 209 5.293 29.857 12.198 1.00 32.42 C ATOM 3257 O GLN B 209 6.039 30.248 13.126 1.00 30.09 O ATOM 3258 CB GLN B 209 6.903 30.317 10.352 1.00 29.10 C ATOM 3259 CG GLN B 209 6.206 31.505 9.726 1.00 31.66 C ATOM 3260 CD GLN B 209 7.146 32.636 9.396 1.00 37.34 C ATOM 3261 OE1 GLN B 209 6.914 33.780 9.783 1.00 42.45 O ATOM 3262 NE2 GLN B 209 8.237 32.319 8.697 1.00 35.16 N ATOM 3263 OXT GLN B 209 4.045 29.916 12.245 1.00 32.94 O TER 3264 GLN B 209 HETATM 3265 N VWW A 210 15.088 10.798 23.547 1.00 14.90 N HETATM 3266 CA VWW A 210 15.010 9.987 24.792 1.00 20.92 C HETATM 3267 C VWW A 210 16.115 8.924 24.830 1.00 21.55 C HETATM 3268 O VWW A 210 16.520 8.515 25.940 1.00 17.16 O HETATM 3269 CB VWW A 210 13.635 9.327 24.908 1.00 14.23 C HETATM 3270 CG VWW A 210 13.394 8.708 26.271 1.00 18.34 C HETATM 3271 CD VWW A 210 12.045 8.046 26.402 1.00 18.27 C HETATM 3272 OE1 VWW A 210 11.293 7.936 25.435 1.00 19.98 O HETATM 3273 OXT VWW A 210 16.578 8.524 23.744 1.00 21.48 O HETATM 3274 N1 VWW A 210 11.726 7.642 27.628 1.00 23.67 N HETATM 3275 CA1 VWW A 210 10.472 6.967 27.934 1.00 24.20 C HETATM 3276 CB1 VWW A 210 10.726 5.484 28.206 1.00 26.79 C HETATM 3277 SG VWW A 210 11.291 4.524 26.810 1.00 31.02 S HETATM 3278 CD1 VWW A 210 9.729 3.804 26.262 1.00 32.02 C HETATM 3279 CE VWW A 210 8.930 3.171 27.370 1.00 33.22 C HETATM 3280 CZ1 VWW A 210 7.640 3.614 27.650 1.00 35.26 C HETATM 3281 CZ2 VWW A 210 9.464 2.135 28.133 1.00 31.51 C HETATM 3282 CT1 VWW A 210 6.893 3.037 28.673 1.00 35.56 C HETATM 3283 CT2 VWW A 210 8.723 1.550 29.161 1.00 27.28 C HETATM 3284 CH VWW A 210 7.437 2.001 29.430 1.00 30.54 C HETATM 3285 C1 VWW A 210 9.834 7.550 29.180 1.00 22.41 C HETATM 3286 O1 VWW A 210 10.522 8.023 30.084 1.00 21.77 O HETATM 3287 N2 VWW A 210 8.512 7.468 29.229 1.00 21.35 N HETATM 3288 CA2 VWW A 210 7.740 7.933 30.366 1.00 24.25 C HETATM 3289 CB2 VWW A 210 6.555 7.062 30.633 1.00 24.94 C HETATM 3290 CG1 VWW A 210 5.330 7.315 30.027 1.00 25.47 C HETATM 3291 CD11 VWW A 210 4.250 6.459 30.220 1.00 26.21 C HETATM 3292 CE1 VWW A 210 4.392 5.339 31.027 1.00 24.08 C HETATM 3293 CD2 VWW A 210 5.611 5.081 31.640 1.00 25.33 C HETATM 3294 CG2 VWW A 210 6.683 5.941 31.441 1.00 26.11 C HETATM 3295 C2 VWW A 210 7.452 9.433 30.354 1.00 29.42 C HETATM 3296 O2 VWW A 210 7.116 9.957 31.433 1.00 30.71 O HETATM 3297 OXT1 VWW A 210 7.569 10.068 29.284 1.00 29.96 O HETATM 3298 O1 MES A 211 22.426 -6.667 36.176 1.00 47.79 O HETATM 3299 C2 MES A 211 22.801 -7.743 37.079 1.00 46.49 C HETATM 3300 C3 MES A 211 23.908 -8.618 36.449 1.00 45.47 C HETATM 3301 N4 MES A 211 24.406 -8.004 35.114 1.00 49.73 N HETATM 3302 C5 MES A 211 24.696 -6.484 35.214 1.00 41.90 C HETATM 3303 C6 MES A 211 23.492 -5.734 35.827 1.00 45.08 C HETATM 3304 C7 MES A 211 25.584 -8.790 34.500 1.00 49.89 C HETATM 3305 C8 MES A 211 25.740 -8.580 32.981 1.00 55.35 C HETATM 3306 S MES A 211 26.952 -9.695 32.274 1.00 57.16 S HETATM 3307 O1S MES A 211 27.719 -9.006 31.068 1.00 60.43 O HETATM 3308 O2S MES A 211 26.255 -11.032 31.776 1.00 58.34 O HETATM 3309 O3S MES A 211 28.102 -10.124 33.414 1.00 56.85 O HETATM 3310 N VWW B 210 17.077 12.945 10.162 1.00 16.89 N HETATM 3311 CA VWW B 210 17.306 13.763 8.940 1.00 21.84 C HETATM 3312 C VWW B 210 18.253 14.931 9.229 1.00 24.69 C HETATM 3313 O VWW B 210 18.940 15.391 8.288 1.00 19.58 O HETATM 3314 CB VWW B 210 15.973 14.285 8.391 1.00 21.52 C HETATM 3315 CG VWW B 210 16.106 14.903 7.011 1.00 21.74 C HETATM 3316 CD VWW B 210 14.805 15.431 6.460 1.00 19.99 C HETATM 3317 OE1 VWW B 210 13.783 15.449 7.146 1.00 22.91 O HETATM 3318 OXT VWW B 210 18.308 15.365 10.399 1.00 24.44 O HETATM 3319 N1 VWW B 210 14.842 15.822 5.191 1.00 19.67 N HETATM 3320 CA1 VWW B 210 13.684 16.374 4.504 1.00 22.40 C HETATM 3321 CB1 VWW B 210 13.860 17.880 4.304 1.00 25.98 C HETATM 3322 SG VWW B 210 13.864 18.870 5.795 1.00 35.19 S HETATM 3323 CD1 VWW B 210 12.146 19.418 5.816 1.00 31.95 C HETATM 3324 CE VWW B 210 11.671 19.986 4.505 1.00 31.48 C HETATM 3325 CZ1 VWW B 210 10.584 19.426 3.847 1.00 31.71 C HETATM 3326 CZ2 VWW B 210 12.309 21.081 3.929 1.00 30.47 C HETATM 3327 CT1 VWW B 210 10.137 19.946 2.637 1.00 34.94 C HETATM 3328 CT2 VWW B 210 11.868 21.609 2.717 1.00 29.43 C HETATM 3329 CH VWW B 210 10.781 21.040 2.071 1.00 29.23 C HETATM 3330 C1 VWW B 210 13.527 15.754 3.130 1.00 22.49 C HETATM 3331 O1 VWW B 210 14.506 15.367 2.491 1.00 21.23 O HETATM 3332 N2 VWW B 210 12.284 15.705 2.672 1.00 24.26 N HETATM 3333 CA2 VWW B 210 11.953 15.187 1.357 1.00 26.47 C HETATM 3334 CB2 VWW B 210 10.828 15.943 0.724 1.00 27.64 C HETATM 3335 CG1 VWW B 210 9.506 15.556 0.922 1.00 28.67 C HETATM 3336 CD11 VWW B 210 8.460 16.304 0.392 1.00 26.56 C HETATM 3337 CE1 VWW B 210 8.734 17.449 -0.345 1.00 24.74 C HETATM 3338 CD2 VWW B 210 10.051 17.840 -0.551 1.00 27.11 C HETATM 3339 CG2 VWW B 210 11.088 17.086 -0.019 1.00 27.10 C HETATM 3340 C2 VWW B 210 11.827 13.665 1.299 1.00 32.59 C HETATM 3341 O2 VWW B 210 11.904 13.131 0.176 1.00 37.14 O HETATM 3342 OXT1 VWW B 210 11.666 13.022 2.358 1.00 31.09 O HETATM 3343 O1 MES B 211 26.183 31.272 0.193 1.00 47.12 O HETATM 3344 C2 MES B 211 26.710 32.396 -0.566 1.00 47.61 C HETATM 3345 C3 MES B 211 27.473 33.366 0.366 1.00 47.56 C HETATM 3346 N4 MES B 211 27.589 32.781 1.797 1.00 49.71 N HETATM 3347 C5 MES B 211 28.048 31.299 1.811 1.00 44.05 C HETATM 3348 C6 MES B 211 27.174 30.444 0.869 1.00 43.80 C HETATM 3349 C7 MES B 211 28.433 33.671 2.737 1.00 50.84 C HETATM 3350 C8 MES B 211 28.128 33.451 4.233 1.00 55.09 C HETATM 3351 S MES B 211 28.942 34.670 5.266 1.00 57.55 S HETATM 3352 O1S MES B 211 29.363 34.038 6.659 1.00 62.19 O HETATM 3353 O2S MES B 211 28.000 35.922 5.502 1.00 57.67 O HETATM 3354 O3S MES B 211 30.342 35.231 4.534 1.00 60.73 O HETATM 3355 O HOH A 212 16.856 5.713 8.800 1.00 16.93 O HETATM 3356 O HOH A 213 24.864 12.790 14.954 1.00 15.27 O HETATM 3357 O HOH A 214 19.222 10.125 22.641 1.00 14.60 O HETATM 3358 O HOH A 215 17.994 -5.269 27.742 1.00 26.25 O HETATM 3359 O HOH A 216 14.836 11.499 17.763 1.00 45.60 O HETATM 3360 O HOH A 217 12.296 -1.485 21.696 1.00 22.48 O HETATM 3361 O HOH A 218 18.264 -0.347 22.604 1.00 24.01 O HETATM 3362 O HOH A 219 18.984 -6.819 30.132 1.00 24.49 O HETATM 3363 O HOH A 220 8.846 0.722 7.703 1.00 38.31 O HETATM 3364 O HOH A 221 15.392 13.020 31.056 1.00 15.92 O HETATM 3365 O HOH A 222 32.502 -9.851 15.386 1.00 39.94 O HETATM 3366 O HOH A 223 15.654 -5.183 22.314 1.00 19.30 O HETATM 3367 O HOH A 224 20.867 1.758 24.123 1.00 14.59 O HETATM 3368 O HOH A 225 15.898 12.316 28.420 1.00 22.41 O HETATM 3369 O HOH A 226 20.408 -5.887 32.343 1.00 22.92 O HETATM 3370 O HOH A 227 27.482 -9.504 6.105 1.00 28.92 O HETATM 3371 O HOH A 228 20.742 13.852 12.295 1.00 9.82 O HETATM 3372 O HOH A 229 11.227 5.784 23.411 1.00 34.16 O HETATM 3373 O HOH A 230 32.290 -8.743 12.401 1.00 27.08 O HETATM 3374 O HOH A 231 31.990 11.506 26.647 1.00 12.76 O HETATM 3375 O HOH A 232 14.962 -2.529 21.860 1.00 18.34 O HETATM 3376 O HOH A 233 16.967 8.325 7.992 1.00 24.06 O HETATM 3377 O HOH A 234 15.543 -2.258 33.685 1.00 25.16 O HETATM 3378 O HOH A 235 17.114 -0.678 35.263 1.00 19.58 O HETATM 3379 O HOH A 236 8.791 9.465 39.334 1.00 37.60 O HETATM 3380 O HOH A 237 34.310 14.016 12.452 1.00 12.67 O HETATM 3381 O HOH A 238 13.969 12.616 26.601 1.00 21.95 O HETATM 3382 O HOH A 239 10.160 0.310 24.282 1.00 20.56 O HETATM 3383 O HOH A 240 19.312 2.039 21.582 1.00 18.05 O HETATM 3384 O HOH A 241 10.029 -8.816 33.060 1.00 39.55 O HETATM 3385 O HOH A 242 35.056 1.807 16.312 1.00 32.72 O HETATM 3386 O HOH A 243 13.779 5.993 9.092 1.00 28.71 O HETATM 3387 O HOH A 244 18.411 4.734 18.522 1.00 18.23 O HETATM 3388 O HOH A 245 18.955 4.897 21.430 1.00 34.55 O HETATM 3389 O HOH A 246 12.692 -15.663 2.165 1.00 27.14 O HETATM 3390 O HOH A 247 9.528 -6.057 17.702 1.00 30.61 O HETATM 3391 O HOH A 248 27.848 11.658 24.970 1.00 22.35 O HETATM 3392 O HOH A 249 7.063 -5.964 24.445 1.00 25.56 O HETATM 3393 O HOH A 250 31.718 -4.759 6.672 1.00 25.20 O HETATM 3394 O HOH A 251 37.235 5.300 19.246 1.00 28.68 O HETATM 3395 O HOH A 252 22.335 -4.853 39.078 1.00 31.25 O HETATM 3396 O HOH A 253 11.924 9.200 12.190 1.00 27.02 O HETATM 3397 O HOH A 254 22.634 -16.179 22.533 1.00 23.30 O HETATM 3398 O HOH A 255 23.228 -14.875 19.924 1.00 29.84 O HETATM 3399 O HOH A 256 16.518 4.011 6.773 1.00 26.05 O HETATM 3400 O HOH A 257 17.155 11.725 38.434 1.00 29.61 O HETATM 3401 O HOH A 258 19.367 -6.248 21.908 1.00 41.40 O HETATM 3402 O HOH A 259 13.105 11.178 13.974 1.00 35.34 O HETATM 3403 O HOH A 260 23.943 -14.188 3.426 1.00 35.78 O HETATM 3404 O HOH A 261 18.267 11.003 14.044 1.00 24.26 O HETATM 3405 O HOH A 262 32.513 -10.999 23.068 1.00 30.58 O HETATM 3406 O HOH A 263 16.471 -1.866 41.441 1.00 32.83 O HETATM 3407 O HOH A 264 10.393 2.476 2.672 1.00 43.77 O HETATM 3408 O HOH A 265 26.084 15.089 36.221 1.00 33.85 O HETATM 3409 O HOH A 266 11.074 16.591 34.671 1.00 26.74 O HETATM 3410 O HOH A 267 16.029 -5.074 34.430 1.00 29.28 O HETATM 3411 O HOH A 268 33.504 14.579 37.879 1.00 37.22 O HETATM 3412 O HOH A 269 20.015 14.786 37.509 1.00 31.57 O HETATM 3413 O HOH A 270 9.850 -0.734 0.799 1.00 44.55 O HETATM 3414 O HOH A 271 18.006 7.436 40.198 1.00 40.60 O HETATM 3415 O HOH A 272 5.802 14.337 37.928 1.00 47.63 O HETATM 3416 O HOH A 273 17.859 -6.963 33.405 1.00 37.00 O HETATM 3417 O HOH A 274 6.322 16.122 35.511 1.00 28.36 O HETATM 3418 O HOH A 275 11.584 2.588 23.272 1.00 23.29 O HETATM 3419 O HOH A 276 9.668 -6.831 4.979 1.00 37.46 O HETATM 3420 O HOH A 277 15.345 -11.632 16.617 1.00 35.47 O HETATM 3421 O HOH A 278 21.967 9.383 17.161 1.00 11.59 O HETATM 3422 O HOH A 279 33.769 2.278 6.604 1.00 31.81 O HETATM 3423 O HOH A 280 12.853 1.052 20.658 1.00 33.35 O HETATM 3424 O HOH A 281 27.322 -14.924 9.874 1.00 39.84 O HETATM 3425 O HOH A 282 5.859 4.345 12.095 1.00 46.01 O HETATM 3426 O HOH A 283 36.569 -0.737 18.630 1.00 34.35 O HETATM 3427 O HOH A 284 10.770 15.081 27.119 1.00 36.53 O HETATM 3428 O HOH A 285 -1.304 -1.156 7.791 1.00 42.24 O HETATM 3429 O HOH A 286 12.014 18.258 32.649 1.00 30.71 O HETATM 3430 O HOH A 287 35.197 -9.125 12.192 1.00 44.56 O HETATM 3431 O HOH A 288 5.317 -9.782 15.687 1.00 42.83 O HETATM 3432 O HOH A 289 17.900 -13.931 22.827 1.00 31.70 O HETATM 3433 O HOH A 290 30.457 1.930 5.937 1.00 34.51 O HETATM 3434 O HOH A 291 0.159 1.325 24.052 1.00 33.35 O HETATM 3435 O HOH A 292 27.422 4.747 39.020 1.00 28.33 O HETATM 3436 O HOH A 293 8.527 -6.033 32.765 1.00 28.41 O HETATM 3437 O HOH A 294 12.675 -10.466 3.337 1.00 33.14 O HETATM 3438 O HOH A 295 33.330 5.562 30.933 1.00 28.38 O HETATM 3439 O HOH A 296 11.028 12.083 23.872 1.00 38.22 O HETATM 3440 O HOH A 297 37.257 -1.627 32.977 1.00 49.09 O HETATM 3441 O HOH A 298 36.471 -4.552 17.071 1.00 24.34 O HETATM 3442 O HOH A 299 3.874 1.565 28.811 1.00 42.87 O HETATM 3443 O HOH A 300 8.600 7.749 17.971 1.00 29.12 O HETATM 3444 O HOH A 301 41.584 12.051 12.322 1.00 33.56 O HETATM 3445 O HOH A 302 31.419 0.293 13.055 1.00 23.07 O HETATM 3446 O HOH A 303 16.415 9.458 28.524 1.00 17.32 O HETATM 3447 O HOH A 304 7.037 7.219 26.157 1.00 22.76 O HETATM 3448 O HOH B 212 13.454 17.756 24.597 1.00 11.01 O HETATM 3449 O HOH B 213 18.085 19.167 15.835 1.00 20.98 O HETATM 3450 O HOH B 214 28.073 24.985 25.071 1.00 20.71 O HETATM 3451 O HOH B 215 8.484 29.206 13.621 1.00 22.56 O HETATM 3452 O HOH B 216 21.680 22.641 11.177 1.00 20.63 O HETATM 3453 O HOH B 217 12.796 19.616 26.586 1.00 22.96 O HETATM 3454 O HOH B 218 23.867 11.810 21.308 1.00 14.20 O HETATM 3455 O HOH B 219 28.411 23.073 31.892 1.00 38.20 O HETATM 3456 O HOH B 220 13.508 15.158 25.523 1.00 21.69 O HETATM 3457 O HOH B 221 32.876 23.696 23.150 1.00 31.35 O HETATM 3458 O HOH B 222 19.426 29.201 7.021 1.00 29.18 O HETATM 3459 O HOH B 223 21.360 24.690 -0.419 1.00 18.00 O HETATM 3460 O HOH B 224 20.012 14.460 5.832 1.00 16.04 O HETATM 3461 O HOH B 225 36.423 28.055 4.818 1.00 43.31 O HETATM 3462 O HOH B 226 19.814 10.908 2.980 1.00 28.43 O HETATM 3463 O HOH B 227 12.712 24.833 10.939 1.00 23.65 O HETATM 3464 O HOH B 228 19.813 21.921 13.343 1.00 14.31 O HETATM 3465 O HOH B 229 17.244 11.061 6.881 1.00 12.39 O HETATM 3466 O HOH B 230 15.170 26.190 11.302 1.00 13.73 O HETATM 3467 O HOH B 231 11.046 18.004 27.978 1.00 30.85 O HETATM 3468 O HOH B 232 20.516 31.037 5.021 1.00 25.86 O HETATM 3469 O HOH B 233 5.351 22.274 23.007 1.00 30.70 O HETATM 3470 O HOH B 234 21.403 33.860 30.311 1.00 25.27 O HETATM 3471 O HOH B 235 18.828 24.080 11.817 1.00 23.57 O HETATM 3472 O HOH B 236 15.756 29.068 11.383 1.00 32.38 O HETATM 3473 O HOH B 237 4.305 23.672 30.142 1.00 33.02 O HETATM 3474 O HOH B 238 35.926 20.607 21.381 1.00 34.53 O HETATM 3475 O HOH B 239 13.712 22.115 11.957 1.00 32.52 O HETATM 3476 O HOH B 240 35.901 20.117 8.789 1.00 28.22 O HETATM 3477 O HOH B 241 21.023 40.639 20.260 1.00 39.76 O HETATM 3478 O HOH B 242 26.051 29.906 31.091 1.00 19.51 O HETATM 3479 O HOH B 243 5.040 20.399 28.595 1.00 30.69 O HETATM 3480 O HOH B 244 12.948 20.736 9.025 1.00 32.24 O HETATM 3481 O HOH B 245 19.519 11.655 5.700 1.00 13.35 O HETATM 3482 O HOH B 246 21.185 40.432 13.086 1.00 24.15 O HETATM 3483 O HOH B 247 15.496 27.009 36.045 1.00 38.12 O HETATM 3484 O HOH B 248 8.232 29.139 7.075 1.00 37.92 O HETATM 3485 O HOH B 249 23.635 37.390 2.269 1.00 27.76 O HETATM 3486 O HOH B 250 28.841 37.090 8.825 1.00 33.25 O HETATM 3487 O HOH B 251 17.405 12.665 20.396 1.00 36.33 O HETATM 3488 O HOH B 252 21.360 39.448 26.486 1.00 35.67 O HETATM 3489 O HOH B 253 15.307 5.358 4.523 1.00 41.74 O HETATM 3490 O HOH B 254 19.157 26.110 0.532 1.00 20.88 O HETATM 3491 O HOH B 255 29.444 13.529 12.853 1.00 27.96 O HETATM 3492 O HOH B 256 33.907 30.157 22.715 1.00 35.59 O HETATM 3493 O HOH B 257 18.367 30.578 13.288 1.00 40.73 O HETATM 3494 O HOH B 258 10.744 17.520 23.522 1.00 30.43 O HETATM 3495 O HOH B 259 23.552 12.315 -3.486 1.00 32.43 O HETATM 3496 O HOH B 260 7.831 27.765 2.466 1.00 57.19 O HETATM 3497 O HOH B 261 -0.154 21.656 8.944 1.00 29.55 O HETATM 3498 O HOH B 262 32.082 14.883 -1.225 1.00 39.42 O HETATM 3499 O HOH B 263 15.054 7.963 5.666 1.00 37.56 O HETATM 3500 O HOH B 264 20.953 39.600 15.834 1.00 42.54 O HETATM 3501 O HOH B 265 12.952 32.530 -0.873 1.00 26.67 O HETATM 3502 O HOH B 266 12.340 15.041 11.905 1.00 41.80 O HETATM 3503 O HOH B 267 19.239 28.961 -0.427 1.00 38.64 O HETATM 3504 O HOH B 268 32.271 23.932 26.288 1.00 32.90 O HETATM 3505 O HOH B 269 31.221 36.442 15.893 1.00 36.29 O HETATM 3506 O HOH B 270 8.747 32.091 35.052 1.00 28.20 O HETATM 3507 O HOH B 271 17.008 6.889 -1.756 1.00 30.88 O HETATM 3508 O HOH B 272 22.759 30.393 3.495 1.00 20.28 O HETATM 3509 O HOH B 273 34.578 26.557 21.290 1.00 34.08 O HETATM 3510 O HOH B 274 3.412 32.437 13.821 1.00 51.39 O HETATM 3511 O HOH B 275 11.493 22.916 7.603 1.00 35.42 O HETATM 3512 O HOH B 276 27.933 38.505 22.492 1.00 34.14 O HETATM 3513 O HOH B 277 16.161 35.587 13.217 1.00 45.32 O HETATM 3514 O HOH B 278 38.124 18.161 7.834 1.00 37.78 O HETATM 3515 O HOH B 279 34.808 11.002 19.084 1.00 46.41 O HETATM 3516 O HOH B 280 12.943 34.982 16.348 1.00 31.71 O HETATM 3517 O HOH B 281 33.453 33.293 22.322 1.00 38.86 O HETATM 3518 O HOH B 282 11.583 34.856 4.214 1.00 45.28 O HETATM 3519 O HOH B 283 37.564 10.772 22.960 1.00 45.16 O HETATM 3520 O HOH B 284 26.947 9.801 -1.180 1.00 33.54 O HETATM 3521 O HOH B 285 28.871 12.308 -3.005 1.00 33.00 O HETATM 3522 O HOH B 286 21.585 14.640 18.240 1.00 14.49 O HETATM 3523 O HOH B 287 12.893 16.815 9.297 1.00 40.60 O CONECT 3265 3266 CONECT 3266 3265 3267 3269 CONECT 3267 3266 3268 3273 CONECT 3268 3267 CONECT 3269 3266 3270 CONECT 3270 3269 3271 CONECT 3271 3270 3272 3274 CONECT 3272 3271 CONECT 3273 3267 CONECT 3274 3271 3275 CONECT 3275 3274 3276 3285 CONECT 3276 3275 3277 CONECT 3277 3276 3278 CONECT 3278 3277 3279 CONECT 3279 3278 3280 3281 CONECT 3280 3279 3282 CONECT 3281 3279 3283 CONECT 3282 3280 3284 CONECT 3283 3281 3284 CONECT 3284 3282 3283 CONECT 3285 3275 3286 3287 CONECT 3286 3285 CONECT 3287 3285 3288 CONECT 3288 3287 3289 3295 CONECT 3289 3288 3290 3294 CONECT 3290 3289 3291 CONECT 3291 3290 3292 CONECT 3292 3291 3293 CONECT 3293 3292 3294 CONECT 3294 3289 3293 CONECT 3295 3288 3296 3297 CONECT 3296 3295 CONECT 3297 3295 CONECT 3298 3299 3303 CONECT 3299 3298 3300 CONECT 3300 3299 3301 CONECT 3301 3300 3302 3304 CONECT 3302 3301 3303 CONECT 3303 3298 3302 CONECT 3304 3301 3305 CONECT 3305 3304 3306 CONECT 3306 3305 3307 3308 3309 CONECT 3307 3306 CONECT 3308 3306 CONECT 3309 3306 CONECT 3310 3311 CONECT 3311 3310 3312 3314 CONECT 3312 3311 3313 3318 CONECT 3313 3312 CONECT 3314 3311 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 3319 CONECT 3317 3316 CONECT 3318 3312 CONECT 3319 3316 3320 CONECT 3320 3319 3321 3330 CONECT 3321 3320 3322 CONECT 3322 3321 3323 CONECT 3323 3322 3324 CONECT 3324 3323 3325 3326 CONECT 3325 3324 3327 CONECT 3326 3324 3328 CONECT 3327 3325 3329 CONECT 3328 3326 3329 CONECT 3329 3327 3328 CONECT 3330 3320 3331 3332 CONECT 3331 3330 CONECT 3332 3330 3333 CONECT 3333 3332 3334 3340 CONECT 3334 3333 3335 3339 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3334 3338 CONECT 3340 3333 3341 3342 CONECT 3341 3340 CONECT 3342 3340 CONECT 3343 3344 3348 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3345 3347 3349 CONECT 3347 3346 3348 CONECT 3348 3343 3347 CONECT 3349 3346 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 3353 3354 CONECT 3352 3351 CONECT 3353 3351 CONECT 3354 3351 MASTER 279 0 4 22 8 0 12 9 3521 2 90 34 END
代码
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通过调用函数，我们成功下载了10gs的pdb格式结构文件。
同理，假如需要下载mmcif文件，我们只需要运行：
代码
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[31]
get_structure(ID='10gs', all_assembly= False, str_format= 'cif')
>>>download 10gs from RCSB >>>Done
代码
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[32]
!cat 10gs/10gs.cif
data_10GS # _entry.id 10GS # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.375 _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 10GS pdb_000010gs 10.2210/pdb10gs/pdb WWPDB D_1000170026 ? ? # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 10GS _pdbx_database_status.recvd_initial_deposition_date 1997-08-14 _pdbx_database_status.deposit_site ? _pdbx_database_status.process_site BNL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_nmr_data ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Oakley, A.' 1 'Parker, M.' 2 # 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 'The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution.' J.Mol.Biol. 274 84 100 1997 JMOBAK UK 0022-2836 0070 ? 9398518 10.1006/jmbi.1997.1364 1 ;Three-Dimensional Structure of Class Pi Glutathione S-Transferase from Human Placenta in Complex with S-Hexylglutathione at 2.8 A Resolution ; J.Mol.Biol. 227 214 ? 1992 JMOBAK UK 0022-2836 0070 ? ? ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal _citation_author.identifier_ORCID primary 'Oakley, A.J.' 1 ? primary 'Bello, M.L.' 2 ? primary 'Battistoni, A.' 3 ? primary 'Ricci, G.' 4 ? primary 'Rossjohn, J.' 5 ? primary 'Villar, H.O.' 6 ? primary 'Parker, M.W.' 7 ? 1 'Reinemer, P.' 8 ? 1 'Dirr, H.W.' 9 ? 1 'Ladenstein, R.' 10 ? 1 'Huber, R.' 11 ? 1 'Lo Bello, M.' 12 ? 1 'Federici, G.' 13 ? 1 'Parker, M.W.' 14 ? # _cell.entry_id 10GS _cell.length_a 79.723 _cell.length_b 90.460 _cell.length_c 69.404 _cell.angle_alpha 90.00 _cell.angle_beta 98.19 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 10GS _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 _symmetry.space_group_name_Hall ? # 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 'GLUTATHIONE S-TRANSFERASE P1-1' 23246.570 2 2.5.1.18 ? ? ? 2 non-polymer syn 'L-gamma-glutamyl-S-benzyl-N-[(S)-carboxy(phenyl)methyl]-L-cysteinamide' 473.542 2 ? ? ? ? 3 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237 2 ? ? ? ? 4 water nat water 18.015 169 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 GSTP1-1 2 'TER117, GLU-BCS-PGY' # _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 ;PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYG KDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLL IHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ ; _entity_poly.pdbx_seq_one_letter_code_can ;PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYG KDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLL IHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ ; _entity_poly.pdbx_strand_id A,B _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 PRO n 1 2 PRO n 1 3 TYR n 1 4 THR n 1 5 VAL n 1 6 VAL n 1 7 TYR n 1 8 PHE n 1 9 PRO n 1 10 VAL n 1 11 ARG n 1 12 GLY n 1 13 ARG n 1 14 CYS n 1 15 ALA n 1 16 ALA n 1 17 LEU n 1 18 ARG n 1 19 MET n 1 20 LEU n 1 21 LEU n 1 22 ALA n 1 23 ASP n 1 24 GLN n 1 25 GLY n 1 26 GLN n 1 27 SER n 1 28 TRP n 1 29 LYS n 1 30 GLU n 1 31 GLU n 1 32 VAL n 1 33 VAL n 1 34 THR n 1 35 VAL n 1 36 GLU n 1 37 THR n 1 38 TRP n 1 39 GLN n 1 40 GLU n 1 41 GLY n 1 42 SER n 1 43 LEU n 1 44 LYS n 1 45 ALA n 1 46 SER n 1 47 CYS n 1 48 LEU n 1 49 TYR n 1 50 GLY n 1 51 GLN n 1 52 LEU n 1 53 PRO n 1 54 LYS n 1 55 PHE n 1 56 GLN n 1 57 ASP n 1 58 GLY n 1 59 ASP n 1 60 LEU n 1 61 THR n 1 62 LEU n 1 63 TYR n 1 64 GLN n 1 65 SER n 1 66 ASN n 1 67 THR n 1 68 ILE n 1 69 LEU n 1 70 ARG n 1 71 HIS n 1 72 LEU n 1 73 GLY n 1 74 ARG n 1 75 THR n 1 76 LEU n 1 77 GLY n 1 78 LEU n 1 79 TYR n 1 80 GLY n 1 81 LYS n 1 82 ASP n 1 83 GLN n 1 84 GLN n 1 85 GLU n 1 86 ALA n 1 87 ALA n 1 88 LEU n 1 89 VAL n 1 90 ASP n 1 91 MET n 1 92 VAL n 1 93 ASN n 1 94 ASP n 1 95 GLY n 1 96 VAL n 1 97 GLU n 1 98 ASP n 1 99 LEU n 1 100 ARG n 1 101 CYS n 1 102 LYS n 1 103 TYR n 1 104 ILE n 1 105 SER n 1 106 LEU n 1 107 ILE n 1 108 TYR n 1 109 THR n 1 110 ASN n 1 111 TYR n 1 112 GLU n 1 113 ALA n 1 114 GLY n 1 115 LYS n 1 116 ASP n 1 117 ASP n 1 118 TYR n 1 119 VAL n 1 120 LYS n 1 121 ALA n 1 122 LEU n 1 123 PRO n 1 124 GLY n 1 125 GLN n 1 126 LEU n 1 127 LYS n 1 128 PRO n 1 129 PHE n 1 130 GLU n 1 131 THR n 1 132 LEU n 1 133 LEU n 1 134 SER n 1 135 GLN n 1 136 ASN n 1 137 GLN n 1 138 GLY n 1 139 GLY n 1 140 LYS n 1 141 THR n 1 142 PHE n 1 143 ILE n 1 144 VAL n 1 145 GLY n 1 146 ASP n 1 147 GLN n 1 148 ILE n 1 149 SER n 1 150 PHE n 1 151 ALA n 1 152 ASP n 1 153 TYR n 1 154 ASN n 1 155 LEU n 1 156 LEU n 1 157 ASP n 1 158 LEU n 1 159 LEU n 1 160 LEU n 1 161 ILE n 1 162 HIS n 1 163 GLU n 1 164 VAL n 1 165 LEU n 1 166 ALA n 1 167 PRO n 1 168 GLY n 1 169 CYS n 1 170 LEU n 1 171 ASP n 1 172 ALA n 1 173 PHE n 1 174 PRO n 1 175 LEU n 1 176 LEU n 1 177 SER n 1 178 ALA n 1 179 TYR n 1 180 VAL n 1 181 GLY n 1 182 ARG n 1 183 LEU n 1 184 SER n 1 185 ALA n 1 186 ARG n 1 187 PRO n 1 188 LYS n 1 189 LEU n 1 190 LYS n 1 191 ALA n 1 192 PHE n 1 193 LEU n 1 194 ALA n 1 195 SER n 1 196 PRO n 1 197 GLU n 1 198 TYR n 1 199 VAL n 1 200 ASN n 1 201 LEU n 1 202 PRO n 1 203 ILE n 1 204 ASN n 1 205 GLY n 1 206 ASN n 1 207 GLY n 1 208 LYS n 1 209 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 GTP_HUMAN _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 PLACENTA _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location CYTOPLASM _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 GTP_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P09211 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYG KDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLL IHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ ; _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 10GS A 1 ? 209 ? P09211 1 ? 209 ? 1 209 2 1 10GS B 1 ? 209 ? P09211 1 ? 209 ? 1 209 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MES non-polymer . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ? 'C6 H13 N O4 S' 195.237 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 VWW peptide-like . 'L-gamma-glutamyl-S-benzyl-N-[(S)-carboxy(phenyl)methyl]-L-cysteinamide' ? 'C23 H27 N3 O6 S' 473.542 # _exptl.entry_id 10GS _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.61 _exptl_crystal.density_percent_sol 52.86 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.8 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details 'pH 5.8' # _diffrn.id 1 _diffrn.ambient_temp 288 _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 1996-04-08 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'GRAPHITE(002)' _diffrn_radiation.pdbx_diffrn_protocol ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RUH2R' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 10GS _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.0 _reflns.d_resolution_high 2.20 _reflns.number_obs 27006 _reflns.number_all ? _reflns.percent_possible_obs 83 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.0790000 _reflns.pdbx_netI_over_sigmaI 12.5 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 2.7 _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_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.20 _reflns_shell.d_res_low 2.30 _reflns_shell.percent_possible_all 77 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.1780000 _reflns_shell.meanI_over_sigI_obs 17.8 _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 10GS _refine.ls_number_reflns_obs 18704 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 15.0 _refine.ls_d_res_high 2.20 _refine.ls_percent_reflns_obs 90.18 _refine.ls_R_factor_obs 0.1762000 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1762000 _refine.ls_R_factor_R_free 0.2140000 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.38 _refine.ls_number_reflns_R_free 949 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1GSS' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_redundancy_reflns_obs ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_phase_error ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3262 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 90 _refine_hist.number_atoms_solvent 169 _refine_hist.number_atoms_total 3521 _refine_hist.d_res_high 2.20 _refine_hist.d_res_low 15.0 # 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 x_bond_d 0.006 ? ? ? 'X-RAY DIFFRACTION' ? x_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg 1.3 ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d 22.0 ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d 1.1 ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 8 _refine_ls_shell.d_res_high 2.20 _refine_ls_shell.d_res_low 2.30 _refine_ls_shell.number_reflns_R_work 2401 _refine_ls_shell.R_factor_R_work 0.2329000 _refine_ls_shell.percent_reflns_obs 81.40 _refine_ls_shell.R_factor_R_free 0.2945000 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free 3.75 _refine_ls_shell.number_reflns_R_free 116 _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _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 PARHCSDX.PRO TOPHCSDX.PRO 'X-RAY DIFFRACTION' 2 ? ? 'X-RAY DIFFRACTION' # _struct_ncs_oper.id 1 _struct_ncs_oper.code given _struct_ncs_oper.details ? _struct_ncs_oper.matrix[1][1] 0.945333 _struct_ncs_oper.matrix[1][2] 0.099229 _struct_ncs_oper.matrix[1][3] 0.310644 _struct_ncs_oper.matrix[2][1] 0.099832 _struct_ncs_oper.matrix[2][2] -0.994906 _struct_ncs_oper.matrix[2][3] 0.013998 _struct_ncs_oper.matrix[3][1] 0.310451 _struct_ncs_oper.matrix[3][2] 0.017779 _struct_ncs_oper.matrix[3][3] -0.950423 _struct_ncs_oper.vector[1] -5.48795 _struct_ncs_oper.vector[2] 21.83043 _struct_ncs_oper.vector[3] 27.67516 # _struct.entry_id 10GS _struct.title 'HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 10GS _struct_keywords.pdbx_keywords 'TRANSFERASE/TRANSFERASE INHIBITOR' _struct_keywords.text ;DETOXIFYING ENZYME, TER117, TLK117, RP298, TELINTRA, EZATIOSTAT HCL, MYELODYSPLASTIC SYNDROME, TRANSFERASE-TRANSFERASE INHIBITOR complex ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 3 ? G N N 4 ? H N N 4 ? # _struct_biol.id 1 _struct_biol.details ? # 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 GLY A 12 ? ASP A 23 ? GLY A 12 ASP A 23 5 ? 12 HELX_P HELX_P2 2 VAL A 35 ? GLU A 40 ? VAL A 35 GLU A 40 1 ? 6 HELX_P HELX_P3 3 SER A 42 ? SER A 46 ? SER A 42 SER A 46 1 ? 5 HELX_P HELX_P4 4 SER A 65 ? LEU A 76 ? SER A 65 LEU A 76 1 ? 12 HELX_P HELX_P5 5 GLN A 83 ? THR A 109 ? GLN A 83 THR A 109 1 ? 27 HELX_P HELX_P6 6 TYR A 111 ? SER A 134 ? TYR A 111 SER A 134 1 ? 24 HELX_P HELX_P7 7 GLN A 137 ? GLY A 139 ? GLN A 137 GLY A 139 5 ? 3 HELX_P HELX_P8 8 PHE A 150 ? LEU A 165 ? PHE A 150 LEU A 165 1 ? 16 HELX_P HELX_P9 9 PRO A 174 ? ALA A 185 ? PRO A 174 ALA A 185 1 ? 12 HELX_P HELX_P10 10 PRO A 187 ? ALA A 194 ? PRO A 187 ALA A 194 1 ? 8 HELX_P HELX_P11 11 PRO A 196 ? VAL A 199 ? PRO A 196 VAL A 199 1 ? 4 HELX_P HELX_P12 12 GLY B 12 ? ASP B 23 ? GLY B 12 ASP B 23 5 ? 12 HELX_P HELX_P13 13 VAL B 35 ? GLU B 40 ? VAL B 35 GLU B 40 1 ? 6 HELX_P HELX_P14 14 SER B 42 ? SER B 46 ? SER B 42 SER B 46 1 ? 5 HELX_P HELX_P15 15 SER B 65 ? LEU B 76 ? SER B 65 LEU B 76 1 ? 12 HELX_P HELX_P16 16 GLN B 83 ? THR B 109 ? GLN B 83 THR B 109 1 ? 27 HELX_P HELX_P17 17 TYR B 111 ? SER B 134 ? TYR B 111 SER B 134 1 ? 24 HELX_P HELX_P18 18 GLN B 137 ? GLY B 139 ? GLN B 137 GLY B 139 5 ? 3 HELX_P HELX_P19 19 PHE B 150 ? LEU B 165 ? PHE B 150 LEU B 165 1 ? 16 HELX_P HELX_P20 20 PRO B 174 ? ALA B 185 ? PRO B 174 ALA B 185 1 ? 12 HELX_P HELX_P21 21 PRO B 187 ? ALA B 194 ? PRO B 187 ALA B 194 1 ? 8 HELX_P HELX_P22 22 PRO B 196 ? VAL B 199 ? PRO B 196 VAL B 199 1 ? 4 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 LEU 52 A . ? LEU 52 A PRO 53 A ? PRO 53 A 1 0.61 2 LEU 52 B . ? LEU 52 B PRO 53 B ? PRO 53 B 1 0.53 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 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 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? parallel B 2 3 ? anti-parallel B 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 TRP A 28 ? VAL A 33 ? TRP A 28 VAL A 33 A 2 TYR A 3 ? PHE A 8 ? TYR A 3 PHE A 8 A 3 LYS A 54 ? ASP A 57 ? LYS A 54 ASP A 57 A 4 LEU A 60 ? TYR A 63 ? LEU A 60 TYR A 63 B 1 TRP B 28 ? VAL B 33 ? TRP B 28 VAL B 33 B 2 TYR B 3 ? PHE B 8 ? TYR B 3 PHE B 8 B 3 LYS B 54 ? ASP B 57 ? LYS B 54 ASP B 57 B 4 LEU B 60 ? TYR B 63 ? LEU B 60 TYR B 63 # 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 LYS A 29 ? O LYS A 29 N TYR A 3 ? N TYR A 3 A 2 3 O THR A 4 ? O THR A 4 N GLN A 56 ? N GLN A 56 A 3 4 O PHE A 55 ? O PHE A 55 N LEU A 62 ? N LEU A 62 B 1 2 O LYS B 29 ? O LYS B 29 N TYR B 3 ? N TYR B 3 B 2 3 O THR B 4 ? O THR B 4 N GLN B 56 ? N GLN B 56 B 3 4 O PHE B 55 ? O PHE B 55 N LEU B 62 ? N LEU B 62 # 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 VWW 210 ? 15 'BINDING SITE FOR RESIDUE VWW A 210' AC2 Software B VWW 210 ? 15 'BINDING SITE FOR RESIDUE VWW B 210' AC3 Software A MES 211 ? 5 'BINDING SITE FOR RESIDUE MES A 211' AC4 Software B MES 211 ? 6 'BINDING SITE FOR RESIDUE MES B 211' # 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 15 TYR A 7 ? TYR A 7 . ? 1_555 ? 2 AC1 15 PHE A 8 ? PHE A 8 . ? 1_555 ? 3 AC1 15 ARG A 13 ? ARG A 13 . ? 1_555 ? 4 AC1 15 TRP A 38 ? TRP A 38 . ? 1_555 ? 5 AC1 15 LYS A 44 ? LYS A 44 . ? 1_555 ? 6 AC1 15 GLY A 50 ? GLY A 50 . ? 1_555 ? 7 AC1 15 GLN A 51 ? GLN A 51 . ? 1_555 ? 8 AC1 15 LEU A 52 ? LEU A 52 . ? 1_555 ? 9 AC1 15 PRO A 53 ? PRO A 53 . ? 1_555 ? 10 AC1 15 GLN A 64 ? GLN A 64 . ? 1_555 ? 11 AC1 15 SER A 65 ? SER A 65 . ? 1_555 ? 12 AC1 15 TYR A 108 ? TYR A 108 . ? 1_555 ? 13 AC1 15 HOH G . ? HOH A 229 . ? 1_555 ? 14 AC1 15 HOH G . ? HOH A 303 . ? 1_555 ? 15 AC1 15 ASP B 98 ? ASP B 98 . ? 1_555 ? 16 AC2 15 ASP A 98 ? ASP A 98 . ? 1_555 ? 17 AC2 15 TYR B 7 ? TYR B 7 . ? 1_555 ? 18 AC2 15 PHE B 8 ? PHE B 8 . ? 1_555 ? 19 AC2 15 ARG B 13 ? ARG B 13 . ? 1_555 ? 20 AC2 15 TRP B 38 ? TRP B 38 . ? 1_555 ? 21 AC2 15 LYS B 44 ? LYS B 44 . ? 1_555 ? 22 AC2 15 GLY B 50 ? GLY B 50 . ? 1_555 ? 23 AC2 15 GLN B 51 ? GLN B 51 . ? 1_555 ? 24 AC2 15 LEU B 52 ? LEU B 52 . ? 1_555 ? 25 AC2 15 PRO B 53 ? PRO B 53 . ? 1_555 ? 26 AC2 15 GLN B 64 ? GLN B 64 . ? 1_555 ? 27 AC2 15 SER B 65 ? SER B 65 . ? 1_555 ? 28 AC2 15 TYR B 108 ? TYR B 108 . ? 1_555 ? 29 AC2 15 HOH H . ? HOH B 224 . ? 1_555 ? 30 AC2 15 HOH H . ? HOH B 287 . ? 1_555 ? 31 AC3 5 ALA A 22 ? ALA A 22 . ? 1_555 ? 32 AC3 5 TRP A 28 ? TRP A 28 . ? 1_555 ? 33 AC3 5 GLU A 30 ? GLU A 30 . ? 1_555 ? 34 AC3 5 GLU A 197 ? GLU A 197 . ? 1_555 ? 35 AC3 5 ASP B 171 ? ASP B 171 . ? 4_546 ? 36 AC4 6 ASP A 171 ? ASP A 171 . ? 4_555 ? 37 AC4 6 HOH G . ? HOH A 246 . ? 4_555 ? 38 AC4 6 ALA B 22 ? ALA B 22 . ? 1_555 ? 39 AC4 6 TRP B 28 ? TRP B 28 . ? 1_555 ? 40 AC4 6 GLU B 30 ? GLU B 30 . ? 1_555 ? 41 AC4 6 GLU B 197 ? GLU B 197 . ? 1_555 ? # _database_PDB_matrix.entry_id 10GS _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 10GS _atom_sites.fract_transf_matrix[1][1] 0.012543 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.001805 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011055 _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] 0.014557 _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 N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PRO A 1 2 ? 31.242 3.064 39.284 1.00 39.90 ? 2 PRO A N 1 ATOM 2 C CA . PRO A 1 2 ? 31.195 2.392 37.963 1.00 31.96 ? 2 PRO A CA 1 ATOM 3 C C . PRO A 1 2 ? 29.975 2.923 37.197 1.00 30.23 ? 2 PRO A C 1 ATOM 4 O O . PRO A 1 2 ? 29.727 4.132 37.181 1.00 27.03 ? 2 PRO A O 1 ATOM 5 C CB . PRO A 1 2 ? 31.063 0.905 38.251 1.00 36.57 ? 2 PRO A CB 1 ATOM 6 C CG . PRO A 1 2 ? 30.276 0.947 39.549 1.00 35.11 ? 2 PRO A CG 1 ATOM 7 C CD . PRO A 1 2 ? 30.829 2.121 40.343 1.00 42.06 ? 2 PRO A CD 1 ATOM 8 N N . TYR A 1 3 ? 29.189 2.020 36.613 1.00 22.83 ? 3 TYR A N 1 ATOM 9 C CA . TYR A 1 3 ? 28.011 2.405 35.850 1.00 18.42 ? 3 TYR A CA 1 ATOM 10 C C . TYR A 1 3 ? 26.711 1.995 36.517 1.00 19.46 ? 3 TYR A C 1 ATOM 11 O O . TYR A 1 3 ? 26.629 0.949 37.161 1.00 24.89 ? 3 TYR A O 1 ATOM 12 C CB . TYR A 1 3 ? 28.055 1.772 34.459 1.00 17.73 ? 3 TYR A CB 1 ATOM 13 C CG . TYR A 1 3 ? 29.318 2.059 33.684 1.00 17.23 ? 3 TYR A CG 1 ATOM 14 C CD1 . TYR A 1 3 ? 29.678 3.366 33.355 1.00 19.19 ? 3 TYR A CD1 1 ATOM 15 C CD2 . TYR A 1 3 ? 30.149 1.023 33.267 1.00 16.84 ? 3 TYR A CD2 1 ATOM 16 C CE1 . TYR A 1 3 ? 30.835 3.633 32.629 1.00 18.79 ? 3 TYR A CE1 1 ATOM 17 C CE2 . TYR A 1 3 ? 31.308 1.279 32.539 1.00 20.85 ? 3 TYR A CE2 1 ATOM 18 C CZ . TYR A 1 3 ? 31.645 2.584 32.226 1.00 20.77 ? 3 TYR A CZ 1 ATOM 19 O OH . TYR A 1 3 ? 32.803 2.828 31.528 1.00 22.24 ? 3 TYR A OH 1 ATOM 20 N N . THR A 1 4 ? 25.683 2.804 36.297 1.00 13.22 ? 4 THR A N 1 ATOM 21 C CA . THR A 1 4 ? 24.361 2.547 36.835 1.00 19.34 ? 4 THR A CA 1 ATOM 22 C C . THR A 1 4 ? 23.337 2.985 35.797 1.00 20.48 ? 4 THR A C 1 ATOM 23 O O . THR A 1 4 ? 23.374 4.124 35.335 1.00 22.30 ? 4 THR A O 1 ATOM 24 C CB . THR A 1 4 ? 24.097 3.357 38.132 1.00 18.80 ? 4 THR A CB 1 ATOM 25 O OG1 . THR A 1 4 ? 25.094 3.042 39.110 1.00 19.60 ? 4 THR A OG1 1 ATOM 26 C CG2 . THR A 1 4 ? 22.713 3.031 38.699 1.00 12.79 ? 4 THR A CG2 1 ATOM 27 N N . VAL A 1 5 ? 22.463 2.071 35.385 1.00 18.58 ? 5 VAL A N 1 ATOM 28 C CA . VAL A 1 5 ? 21.420 2.437 34.438 1.00 17.96 ? 5 VAL A CA 1 ATOM 29 C C . VAL A 1 5 ? 20.078 2.369 35.160 1.00 19.40 ? 5 VAL A C 1 ATOM 30 O O . VAL A 1 5 ? 19.743 1.367 35.790 1.00 22.04 ? 5 VAL A O 1 ATOM 31 C CB . VAL A 1 5 ? 21.436 1.582 33.113 1.00 17.57 ? 5 VAL A CB 1 ATOM 32 C CG1 . VAL A 1 5 ? 22.717 0.779 32.989 1.00 12.49 ? 5 VAL A CG1 1 ATOM 33 C CG2 . VAL A 1 5 ? 20.204 0.704 32.988 1.00 22.38 ? 5 VAL A CG2 1 ATOM 34 N N . VAL A 1 6 ? 19.366 3.488 35.149 1.00 19.86 ? 6 VAL A N 1 ATOM 35 C CA . VAL A 1 6 ? 18.059 3.585 35.781 1.00 19.18 ? 6 VAL A CA 1 ATOM 36 C C . VAL A 1 6 ? 17.049 3.522 34.638 1.00 21.26 ? 6 VAL A C 1 ATOM 37 O O . VAL A 1 6 ? 17.045 4.385 33.752 1.00 18.67 ? 6 VAL A O 1 ATOM 38 C CB . VAL A 1 6 ? 17.906 4.919 36.550 1.00 19.15 ? 6 VAL A CB 1 ATOM 39 C CG1 . VAL A 1 6 ? 16.592 4.937 37.304 1.00 13.21 ? 6 VAL A CG1 1 ATOM 40 C CG2 . VAL A 1 6 ? 19.084 5.122 37.497 1.00 16.31 ? 6 VAL A CG2 1 ATOM 41 N N . TYR A 1 7 ? 16.196 2.504 34.657 1.00 16.48 ? 7 TYR A N 1 ATOM 42 C CA . TYR A 1 7 ? 15.226 2.331 33.585 1.00 17.51 ? 7 TYR A CA 1 ATOM 43 C C . TYR A 1 7 ? 14.067 1.427 33.993 1.00 15.22 ? 7 TYR A C 1 ATOM 44 O O . TYR A 1 7 ? 14.097 0.789 35.042 1.00 21.57 ? 7 TYR A O 1 ATOM 45 C CB . TYR A 1 7 ? 15.954 1.735 32.372 1.00 17.21 ? 7 TYR A CB 1 ATOM 46 C CG . TYR A 1 7 ? 15.202 1.810 31.064 1.00 19.24 ? 7 TYR A CG 1 ATOM 47 C CD1 . TYR A 1 7 ? 14.713 3.025 30.580 1.00 23.22 ? 7 TYR A CD1 1 ATOM 48 C CD2 . TYR A 1 7 ? 14.995 0.665 30.297 1.00 18.29 ? 7 TYR A CD2 1 ATOM 49 C CE1 . TYR A 1 7 ? 14.036 3.095 29.363 1.00 18.22 ? 7 TYR A CE1 1 ATOM 50 C CE2 . TYR A 1 7 ? 14.323 0.723 29.083 1.00 19.10 ? 7 TYR A CE2 1 ATOM 51 C CZ . TYR A 1 7 ? 13.846 1.938 28.621 1.00 21.78 ? 7 TYR A CZ 1 ATOM 52 O OH . TYR A 1 7 ? 13.180 1.997 27.419 1.00 19.49 ? 7 TYR A OH 1 ATOM 53 N N . PHE A 1 8 ? 13.041 1.388 33.152 1.00 17.17 ? 8 PHE A N 1 ATOM 54 C CA . PHE A 1 8 ? 11.870 0.551 33.384 1.00 20.97 ? 8 PHE A CA 1 ATOM 55 C C . PHE A 1 8 ? 12.265 -0.902 33.111 1.00 23.22 ? 8 PHE A C 1 ATOM 56 O O . PHE A 1 8 ? 13.297 -1.157 32.496 1.00 22.12 ? 8 PHE A O 1 ATOM 57 C CB . PHE A 1 8 ? 10.742 0.990 32.454 1.00 20.14 ? 8 PHE A CB 1 ATOM 58 C CG . PHE A 1 8 ? 10.344 2.426 32.635 1.00 26.86 ? 8 PHE A CG 1 ATOM 59 C CD1 . PHE A 1 8 ? 9.655 2.833 33.777 1.00 28.34 ? 8 PHE A CD1 1 ATOM 60 C CD2 . PHE A 1 8 ? 10.680 3.380 31.679 1.00 25.81 ? 8 PHE A CD2 1 ATOM 61 C CE1 . PHE A 1 8 ? 9.306 4.171 33.966 1.00 26.11 ? 8 PHE A CE1 1 ATOM 62 C CE2 . PHE A 1 8 ? 10.337 4.724 31.856 1.00 27.24 ? 8 PHE A CE2 1 ATOM 63 C CZ . PHE A 1 8 ? 9.649 5.120 33.002 1.00 31.55 ? 8 PHE A CZ 1 ATOM 64 N N . PRO A 1 9 ? 11.475 -1.874 33.599 1.00 22.45 ? 9 PRO A N 1 ATOM 65 C CA . PRO A 1 9 ? 11.810 -3.285 33.365 1.00 25.63 ? 9 PRO A CA 1 ATOM 66 C C . PRO A 1 9 ? 11.527 -3.784 31.939 1.00 23.89 ? 9 PRO A C 1 ATOM 67 O O . PRO A 1 9 ? 10.777 -4.740 31.743 1.00 27.87 ? 9 PRO A O 1 ATOM 68 C CB . PRO A 1 9 ? 10.955 -4.005 34.409 1.00 26.37 ? 9 PRO A CB 1 ATOM 69 C CG . PRO A 1 9 ? 9.724 -3.141 34.473 1.00 23.87 ? 9 PRO A CG 1 ATOM 70 C CD . PRO A 1 9 ? 10.312 -1.748 34.496 1.00 24.97 ? 9 PRO A CD 1 ATOM 71 N N . VAL A 1 10 ? 12.125 -3.123 30.949 1.00 23.67 ? 10 VAL A N 1 ATOM 72 C CA . VAL A 1 10 ? 11.969 -3.489 29.541 1.00 19.23 ? 10 VAL A CA 1 ATOM 73 C C . VAL A 1 10 ? 13.312 -3.289 28.850 1.00 20.13 ? 10 VAL A C 1 ATOM 74 O O . VAL A 1 10 ? 14.214 -2.661 29.407 1.00 21.70 ? 10 VAL A O 1 ATOM 75 C CB . VAL A 1 10 ? 10.906 -2.613 28.810 1.00 22.15 ? 10 VAL A CB 1 ATOM 76 C CG1 . VAL A 1 10 ? 9.550 -2.724 29.493 1.00 20.17 ? 10 VAL A CG1 1 ATOM 77 C CG2 . VAL A 1 10 ? 11.359 -1.160 28.743 1.00 22.63 ? 10 VAL A CG2 1 ATOM 78 N N . ARG A 1 11 ? 13.460 -3.848 27.653 1.00 18.71 ? 11 ARG A N 1 ATOM 79 C CA . ARG A 1 11 ? 14.701 -3.694 26.898 1.00 18.17 ? 11 ARG A CA 1 ATOM 80 C C . ARG A 1 11 ? 14.738 -2.278 26.338 1.00 15.50 ? 11 ARG A C 1 ATOM 81 O O . ARG A 1 11 ? 15.679 -1.529 26.597 1.00 14.31 ? 11 ARG A O 1 ATOM 82 C CB . ARG A 1 11 ? 14.773 -4.713 25.762 1.00 18.01 ? 11 ARG A CB 1 ATOM 83 C CG . ARG A 1 11 ? 14.797 -6.150 26.244 1.00 27.60 ? 11 ARG A CG 1 ATOM 84 C CD . ARG A 1 11 ? 14.943 -7.120 25.092 1.00 27.61 ? 11 ARG A CD 1 ATOM 85 N NE . ARG A 1 11 ? 14.609 -8.476 25.509 1.00 37.28 ? 11 ARG A NE 1 ATOM 86 C CZ . ARG A 1 11 ? 14.246 -9.448 24.679 1.00 34.90 ? 11 ARG A CZ 1 ATOM 87 N NH1 . ARG A 1 11 ? 14.176 -9.219 23.375 1.00 34.05 ? 11 ARG A NH1 1 ATOM 88 N NH2 . ARG A 1 11 ? 13.917 -10.638 25.163 1.00 34.82 ? 11 ARG A NH2 1 ATOM 89 N N . GLY A 1 12 ? 13.692 -1.933 25.585 1.00 16.37 ? 12 GLY A N 1 ATOM 90 C CA . GLY A 1 12 ? 13.546 -0.612 24.995 1.00 15.31 ? 12 GLY A CA 1 ATOM 91 C C . GLY A 1 12 ? 14.805 0.095 24.539 1.00 16.39 ? 12 GLY A C 1 ATOM 92 O O . GLY A 1 12 ? 15.615 -0.464 23.794 1.00 12.85 ? 12 GLY A O 1 ATOM 93 N N . ARG A 1 13 ? 14.993 1.315 25.032 1.00 15.58 ? 13 ARG A N 1 ATOM 94 C CA . ARG A 1 13 ? 16.152 2.121 24.667 1.00 18.28 ? 13 ARG A CA 1 ATOM 95 C C . ARG A 1 13 ? 17.452 1.819 25.406 1.00 17.33 ? 13 ARG A C 1 ATOM 96 O O . ARG A 1 13 ? 18.432 2.551 25.256 1.00 17.22 ? 13 ARG A O 1 ATOM 97 C CB . ARG A 1 13 ? 15.815 3.611 24.771 1.00 20.29 ? 13 ARG A CB 1 ATOM 98 C CG . ARG A 1 13 ? 14.896 4.098 23.662 1.00 17.00 ? 13 ARG A CG 1 ATOM 99 C CD . ARG A 1 13 ? 14.694 5.596 23.736 1.00 15.27 ? 13 ARG A CD 1 ATOM 100 N NE . ARG A 1 13 ? 13.987 6.117 22.568 1.00 18.44 ? 13 ARG A NE 1 ATOM 101 C CZ . ARG A 1 13 ? 14.584 6.502 21.444 1.00 16.41 ? 13 ARG A CZ 1 ATOM 102 N NH1 . ARG A 1 13 ? 15.904 6.417 21.320 1.00 13.14 ? 13 ARG A NH1 1 ATOM 103 N NH2 . ARG A 1 13 ? 13.856 6.965 20.438 1.00 10.51 ? 13 ARG A NH2 1 ATOM 104 N N . CYS A 1 14 ? 17.470 0.750 26.199 1.00 14.56 ? 14 CYS A N 1 ATOM 105 C CA . CYS A 1 14 ? 18.685 0.383 26.927 1.00 11.34 ? 14 CYS A CA 1 ATOM 106 C C . CYS A 1 14 ? 19.309 -0.901 26.413 1.00 11.79 ? 14 CYS A C 1 ATOM 107 O O . CYS A 1 14 ? 20.429 -1.250 26.795 1.00 10.40 ? 14 CYS A O 1 ATOM 108 C CB . CYS A 1 14 ? 18.411 0.265 28.428 1.00 13.29 ? 14 CYS A CB 1 ATOM 109 S SG . CYS A 1 14 ? 18.129 1.852 29.221 1.00 17.53 ? 14 CYS A SG 1 ATOM 110 N N . ALA A 1 15 ? 18.591 -1.590 25.530 1.00 10.15 ? 15 ALA A N 1 ATOM 111 C CA . ALA A 1 15 ? 19.059 -2.847 24.959 1.00 13.24 ? 15 ALA A CA 1 ATOM 112 C C . ALA A 1 15 ? 20.445 -2.728 24.332 1.00 13.21 ? 15 ALA A C 1 ATOM 113 O O . ALA A 1 15 ? 21.353 -3.490 24.667 1.00 18.26 ? 15 ALA A O 1 ATOM 114 C CB . ALA A 1 15 ? 18.048 -3.362 23.935 1.00 11.30 ? 15 ALA A CB 1 ATOM 115 N N . ALA A 1 16 ? 20.620 -1.732 23.470 1.00 16.63 ? 16 ALA A N 1 ATOM 116 C CA . ALA A 1 16 ? 21.892 -1.515 22.794 1.00 10.39 ? 16 ALA A CA 1 ATOM 117 C C . ALA A 1 16 ? 23.036 -1.185 23.745 1.00 15.32 ? 16 ALA A C 1 ATOM 118 O O . ALA A 1 16 ? 24.125 -1.760 23.631 1.00 17.28 ? 16 ALA A O 1 ATOM 119 C CB . ALA A 1 16 ? 21.747 -0.433 21.742 1.00 14.07 ? 16 ALA A CB 1 ATOM 120 N N . LEU A 1 17 ? 22.792 -0.282 24.694 1.00 15.12 ? 17 LEU A N 1 ATOM 121 C CA . LEU A 1 17 ? 23.834 0.100 25.648 1.00 17.17 ? 17 LEU A CA 1 ATOM 122 C C . LEU A 1 17 ? 24.190 -1.056 26.589 1.00 15.48 ? 17 LEU A C 1 ATOM 123 O O . LEU A 1 17 ? 25.335 -1.168 27.035 1.00 17.10 ? 17 LEU A O 1 ATOM 124 C CB . LEU A 1 17 ? 23.454 1.381 26.416 1.00 19.50 ? 17 LEU A CB 1 ATOM 125 C CG . LEU A 1 17 ? 22.302 1.445 27.420 1.00 23.29 ? 17 LEU A CG 1 ATOM 126 C CD1 . LEU A 1 17 ? 22.845 1.235 28.820 1.00 21.79 ? 17 LEU A CD1 1 ATOM 127 C CD2 . LEU A 1 17 ? 21.617 2.808 27.334 1.00 20.62 ? 17 LEU A CD2 1 ATOM 128 N N . ARG A 1 18 ? 23.223 -1.931 26.859 1.00 10.96 ? 18 ARG A N 1 ATOM 129 C CA . ARG A 1 18 ? 23.468 -3.096 27.707 1.00 15.98 ? 18 ARG A CA 1 ATOM 130 C C . ARG A 1 18 ? 24.332 -4.104 26.951 1.00 17.26 ? 18 ARG A C 1 ATOM 131 O O . ARG A 1 18 ? 25.273 -4.670 27.516 1.00 17.70 ? 18 ARG A O 1 ATOM 132 C CB . ARG A 1 18 ? 22.155 -3.748 28.125 1.00 15.83 ? 18 ARG A CB 1 ATOM 133 C CG . ARG A 1 18 ? 21.408 -2.979 29.195 1.00 13.17 ? 18 ARG A CG 1 ATOM 134 C CD . ARG A 1 18 ? 19.985 -3.478 29.308 1.00 14.43 ? 18 ARG A CD 1 ATOM 135 N NE . ARG A 1 18 ? 19.289 -2.858 30.426 1.00 11.87 ? 18 ARG A NE 1 ATOM 136 C CZ . ARG A 1 18 ? 17.970 -2.717 30.505 1.00 15.61 ? 18 ARG A CZ 1 ATOM 137 N NH1 . ARG A 1 18 ? 17.188 -3.148 29.523 1.00 15.54 ? 18 ARG A NH1 1 ATOM 138 N NH2 . ARG A 1 18 ? 17.430 -2.148 31.577 1.00 13.98 ? 18 ARG A NH2 1 ATOM 139 N N . MET A 1 19 ? 24.019 -4.313 25.671 1.00 16.80 ? 19 MET A N 1 ATOM 140 C CA . MET A 1 19 ? 24.787 -5.237 24.834 1.00 15.14 ? 19 MET A CA 1 ATOM 141 C C . MET A 1 19 ? 26.219 -4.743 24.714 1.00 17.68 ? 19 MET A C 1 ATOM 142 O O . MET A 1 19 ? 27.158 -5.536 24.713 1.00 20.00 ? 19 MET A O 1 ATOM 143 C CB . MET A 1 19 ? 24.185 -5.341 23.433 1.00 19.56 ? 19 MET A CB 1 ATOM 144 C CG . MET A 1 19 ? 22.786 -5.920 23.379 1.00 21.18 ? 19 MET A CG 1 ATOM 145 S SD . MET A 1 19 ? 22.261 -6.218 21.687 1.00 31.83 ? 19 MET A SD 1 ATOM 146 C CE . MET A 1 19 ? 22.032 -4.592 21.115 1.00 33.49 ? 19 MET A CE 1 ATOM 147 N N . LEU A 1 20 ? 26.374 -3.425 24.611 1.00 14.60 ? 20 LEU A N 1 ATOM 148 C CA . LEU A 1 20 ? 27.689 -2.804 24.493 1.00 16.07 ? 20 LEU A CA 1 ATOM 149 C C . LEU A 1 20 ? 28.521 -3.068 25.751 1.00 19.64 ? 20 LEU A C 1 ATOM 150 O O . LEU A 1 20 ? 29.675 -3.501 25.665 1.00 15.82 ? 20 LEU A O 1 ATOM 151 C CB . LEU A 1 20 ? 27.529 -1.296 24.252 1.00 17.09 ? 20 LEU A CB 1 ATOM 152 C CG . LEU A 1 20 ? 28.749 -0.433 23.902 1.00 21.27 ? 20 LEU A CG 1 ATOM 153 C CD1 . LEU A 1 20 ? 28.275 0.862 23.265 1.00 19.18 ? 20 LEU A CD1 1 ATOM 154 C CD2 . LEU A 1 20 ? 29.615 -0.147 25.128 1.00 16.96 ? 20 LEU A CD2 1 ATOM 155 N N . LEU A 1 21 ? 27.932 -2.792 26.914 1.00 19.49 ? 21 LEU A N 1 ATOM 156 C CA . LEU A 1 21 ? 28.607 -3.002 28.192 1.00 18.96 ? 21 LEU A CA 1 ATOM 157 C C . LEU A 1 21 ? 28.966 -4.472 28.388 1.00 17.46 ? 21 LEU A C 1 ATOM 158 O O . LEU A 1 21 ? 30.093 -4.793 28.748 1.00 18.27 ? 21 LEU A O 1 ATOM 159 C CB . LEU A 1 21 ? 27.728 -2.518 29.350 1.00 14.89 ? 21 LEU A CB 1 ATOM 160 C CG . LEU A 1 21 ? 27.585 -1.001 29.494 1.00 14.97 ? 21 LEU A CG 1 ATOM 161 C CD1 . LEU A 1 21 ? 26.521 -0.668 30.522 1.00 13.48 ? 21 LEU A CD1 1 ATOM 162 C CD2 . LEU A 1 21 ? 28.925 -0.394 29.884 1.00 13.27 ? 21 LEU A CD2 1 ATOM 163 N N . ALA A 1 22 ? 28.013 -5.356 28.115 1.00 16.24 ? 22 ALA A N 1 ATOM 164 C CA . ALA A 1 22 ? 28.224 -6.793 28.258 1.00 17.75 ? 22 ALA A CA 1 ATOM 165 C C . ALA A 1 22 ? 29.358 -7.280 27.364 1.00 18.70 ? 22 ALA A C 1 ATOM 166 O O . ALA A 1 22 ? 30.309 -7.909 27.836 1.00 24.16 ? 22 ALA A O 1 ATOM 167 C CB . ALA A 1 22 ? 26.946 -7.539 27.928 1.00 16.02 ? 22 ALA A CB 1 ATOM 168 N N . ASP A 1 23 ? 29.276 -6.943 26.081 1.00 19.77 ? 23 ASP A N 1 ATOM 169 C CA . ASP A 1 23 ? 30.281 -7.348 25.105 1.00 20.00 ? 23 ASP A CA 1 ATOM 170 C C . ASP A 1 23 ? 31.676 -6.787 25.386 1.00 20.89 ? 23 ASP A C 1 ATOM 171 O O . ASP A 1 23 ? 32.681 -7.407 25.036 1.00 23.31 ? 23 ASP A O 1 ATOM 172 C CB . ASP A 1 23 ? 29.836 -6.954 23.693 1.00 24.93 ? 23 ASP A CB 1 ATOM 173 C CG . ASP A 1 23 ? 30.595 -7.706 22.612 1.00 28.30 ? 23 ASP A CG 1 ATOM 174 O OD1 . ASP A 1 23 ? 30.503 -8.949 22.578 1.00 29.29 ? 23 ASP A OD1 1 ATOM 175 O OD2 . ASP A 1 23 ? 31.316 -7.074 21.815 1.00 26.02 ? 23 ASP A OD2 1 ATOM 176 N N . GLN A 1 24 ? 31.738 -5.613 26.006 1.00 24.47 ? 24 GLN A N 1 ATOM 177 C CA . GLN A 1 24 ? 33.020 -4.987 26.329 1.00 23.19 ? 24 GLN A CA 1 ATOM 178 C C . GLN A 1 24 ? 33.566 -5.446 27.673 1.00 22.46 ? 24 GLN A C 1 ATOM 179 O O . GLN A 1 24 ? 34.592 -4.950 28.133 1.00 29.52 ? 24 GLN A O 1 ATOM 180 C CB . GLN A 1 24 ? 32.897 -3.461 26.306 1.00 19.66 ? 24 GLN A CB 1 ATOM 181 C CG . GLN A 1 24 ? 32.696 -2.884 24.907 1.00 17.35 ? 24 GLN A CG 1 ATOM 182 C CD . GLN A 1 24 ? 33.820 -3.268 23.968 1.00 20.22 ? 24 GLN A CD 1 ATOM 183 O OE1 . GLN A 1 24 ? 34.994 -3.138 24.317 1.00 19.83 ? 24 GLN A OE1 1 ATOM 184 N NE2 . GLN A 1 24 ? 33.472 -3.759 22.785 1.00 13.55 ? 24 GLN A NE2 1 ATOM 185 N N . GLY A 1 25 ? 32.870 -6.391 28.298 1.00 23.76 ? 25 GLY A N 1 ATOM 186 C CA . GLY A 1 25 ? 33.295 -6.918 29.582 1.00 23.57 ? 25 GLY A CA 1 ATOM 187 C C . GLY A 1 25 ? 33.165 -5.936 30.730 1.00 22.99 ? 25 GLY A C 1 ATOM 188 O O . GLY A 1 25 ? 33.950 -5.973 31.667 1.00 26.83 ? 25 GLY A O 1 ATOM 189 N N . GLN A 1 26 ? 32.171 -5.058 30.658 1.00 26.31 ? 26 GLN A N 1 ATOM 190 C CA . GLN A 1 26 ? 31.943 -4.060 31.700 1.00 28.99 ? 26 GLN A CA 1 ATOM 191 C C . GLN A 1 26 ? 30.861 -4.495 32.677 1.00 27.54 ? 26 GLN A C 1 ATOM 192 O O . GLN A 1 26 ? 29.915 -5.189 32.306 1.00 30.40 ? 26 GLN A O 1 ATOM 193 C CB . GLN A 1 26 ? 31.540 -2.719 31.078 1.00 31.87 ? 26 GLN A CB 1 ATOM 194 C CG . GLN A 1 26 ? 32.541 -2.161 30.083 1.00 32.88 ? 26 GLN A CG 1 ATOM 195 C CD . GLN A 1 26 ? 33.901 -1.926 30.700 1.00 33.03 ? 26 GLN A CD 1 ATOM 196 O OE1 . GLN A 1 26 ? 34.008 -1.498 31.850 1.00 28.41 ? 26 GLN A OE1 1 ATOM 197 N NE2 . GLN A 1 26 ? 34.953 -2.229 29.948 1.00 38.94 ? 26 GLN A NE2 1 ATOM 198 N N . SER A 1 27 ? 31.007 -4.064 33.926 1.00 28.74 ? 27 SER A N 1 ATOM 199 C CA . SER A 1 27 ? 30.052 -4.378 34.983 1.00 26.82 ? 27 SER A CA 1 ATOM 200 C C . SER A 1 27 ? 29.194 -3.143 35.206 1.00 25.69 ? 27 SER A C 1 ATOM 201 O O . SER A 1 27 ? 29.686 -2.018 35.124 1.00 27.06 ? 27 SER A O 1 ATOM 202 C CB . SER A 1 27 ? 30.786 -4.692 36.291 1.00 29.20 ? 27 SER A CB 1 ATOM 203 O OG . SER A 1 27 ? 31.909 -5.523 36.071 1.00 41.28 ? 27 SER A OG 1 ATOM 204 N N . TRP A 1 28 ? 27.915 -3.345 35.493 1.00 21.96 ? 28 TRP A N 1 ATOM 205 C CA . TRP A 1 28 ? 27.033 -2.220 35.755 1.00 24.43 ? 28 TRP A CA 1 ATOM 206 C C . TRP A 1 28 ? 25.903 -2.616 36.697 1.00 26.77 ? 28 TRP A C 1 ATOM 207 O O . TRP A 1 28 ? 25.584 -3.795 36.841 1.00 25.34 ? 28 TRP A O 1 ATOM 208 C CB . TRP A 1 28 ? 26.472 -1.638 34.453 1.00 21.55 ? 28 TRP A CB 1 ATOM 209 C CG . TRP A 1 28 ? 25.449 -2.498 33.757 1.00 14.67 ? 28 TRP A CG 1 ATOM 210 C CD1 . TRP A 1 28 ? 24.090 -2.375 33.830 1.00 9.31 ? 28 TRP A CD1 1 ATOM 211 C CD2 . TRP A 1 28 ? 25.709 -3.566 32.833 1.00 12.15 ? 28 TRP A CD2 1 ATOM 212 N NE1 . TRP A 1 28 ? 23.491 -3.293 33.002 1.00 11.46 ? 28 TRP A NE1 1 ATOM 213 C CE2 . TRP A 1 28 ? 24.457 -4.035 32.378 1.00 10.63 ? 28 TRP A CE2 1 ATOM 214 C CE3 . TRP A 1 28 ? 26.877 -4.171 32.344 1.00 12.67 ? 28 TRP A CE3 1 ATOM 215 C CZ2 . TRP A 1 28 ? 24.341 -5.078 31.453 1.00 9.14 ? 28 TRP A CZ2 1 ATOM 216 C CZ3 . TRP A 1 28 ? 26.759 -5.209 31.426 1.00 13.30 ? 28 TRP A CZ3 1 ATOM 217 C CH2 . TRP A 1 28 ? 25.497 -5.650 30.991 1.00 9.78 ? 28 TRP A CH2 1 ATOM 218 N N . LYS A 1 29 ? 25.311 -1.615 37.337 1.00 24.24 ? 29 LYS A N 1 ATOM 219 C CA . LYS A 1 29 ? 24.219 -1.817 38.272 1.00 22.87 ? 29 LYS A CA 1 ATOM 220 C C . LYS A 1 29 ? 22.915 -1.406 37.610 1.00 23.70 ? 29 LYS A C 1 ATOM 221 O O . LYS A 1 29 ? 22.855 -0.391 36.920 1.00 25.40 ? 29 LYS A O 1 ATOM 222 C CB . LYS A 1 29 ? 24.465 -0.976 39.529 1.00 29.03 ? 29 LYS A CB 1 ATOM 223 C CG . LYS A 1 29 ? 23.266 -0.813 40.449 1.00 39.95 ? 29 LYS A CG 1 ATOM 224 C CD . LYS A 1 29 ? 22.942 -2.085 41.219 1.00 51.60 ? 29 LYS A CD 1 ATOM 225 C CE . LYS A 1 29 ? 21.690 -1.893 42.070 1.00 57.02 ? 29 LYS A CE 1 ATOM 226 N NZ . LYS A 1 29 ? 21.792 -0.670 42.925 1.00 61.59 ? 29 LYS A NZ 1 ATOM 227 N N . GLU A 1 30 ? 21.883 -2.220 37.792 1.00 25.07 ? 30 GLU A N 1 ATOM 228 C CA . GLU A 1 30 ? 20.575 -1.930 37.229 1.00 27.49 ? 30 GLU A CA 1 ATOM 229 C C . GLU A 1 30 ? 19.651 -1.439 38.332 1.00 30.70 ? 30 GLU A C 1 ATOM 230 O O . GLU A 1 30 ? 19.456 -2.119 39.339 1.00 35.30 ? 30 GLU A O 1 ATOM 231 C CB . GLU A 1 30 ? 19.971 -3.182 36.581 1.00 25.50 ? 30 GLU A CB 1 ATOM 232 C CG . GLU A 1 30 ? 20.635 -3.620 35.278 1.00 28.34 ? 30 GLU A CG 1 ATOM 233 C CD . GLU A 1 30 ? 20.113 -2.894 34.036 1.00 30.13 ? 30 GLU A CD 1 ATOM 234 O OE1 . GLU A 1 30 ? 19.166 -2.081 34.132 1.00 26.14 ? 30 GLU A OE1 1 ATOM 235 O OE2 . GLU A 1 30 ? 20.642 -3.166 32.940 1.00 25.20 ? 30 GLU A OE2 1 ATOM 236 N N . GLU A 1 31 ? 19.141 -0.226 38.162 1.00 30.04 ? 31 GLU A N 1 ATOM 237 C CA . GLU A 1 31 ? 18.212 0.369 39.109 1.00 25.07 ? 31 GLU A CA 1 ATOM 238 C C . GLU A 1 31 ? 16.875 0.323 38.411 1.00 23.26 ? 31 GLU A C 1 ATOM 239 O O . GLU A 1 31 ? 16.590 1.143 37.543 1.00 29.50 ? 31 GLU A O 1 ATOM 240 C CB . GLU A 1 31 ? 18.600 1.815 39.412 1.00 34.10 ? 31 GLU A CB 1 ATOM 241 C CG . GLU A 1 31 ? 19.672 1.960 40.474 1.00 50.28 ? 31 GLU A CG 1 ATOM 242 C CD . GLU A 1 31 ? 19.149 1.662 41.865 1.00 60.18 ? 31 GLU A CD 1 ATOM 243 O OE1 . GLU A 1 31 ? 19.103 0.473 42.253 1.00 64.38 ? 31 GLU A OE1 1 ATOM 244 O OE2 . GLU A 1 31 ? 18.780 2.623 42.572 1.00 67.09 ? 31 GLU A OE2 1 ATOM 245 N N . VAL A 1 32 ? 16.074 -0.675 38.753 1.00 23.05 ? 32 VAL A N 1 ATOM 246 C CA . VAL A 1 32 ? 14.771 -0.841 38.132 1.00 20.87 ? 32 VAL A CA 1 ATOM 247 C C . VAL A 1 32 ? 13.711 0.081 38.711 1.00 23.88 ? 32 VAL A C 1 ATOM 248 O O . VAL A 1 32 ? 13.533 0.168 39.922 1.00 29.17 ? 32 VAL A O 1 ATOM 249 C CB . VAL A 1 32 ? 14.290 -2.303 38.222 1.00 18.51 ? 32 VAL A CB 1 ATOM 250 C CG1 . VAL A 1 32 ? 12.968 -2.469 37.496 1.00 11.00 ? 32 VAL A CG1 1 ATOM 251 C CG2 . VAL A 1 32 ? 15.342 -3.230 37.632 1.00 19.20 ? 32 VAL A CG2 1 ATOM 252 N N . VAL A 1 33 ? 13.021 0.782 37.821 1.00 26.92 ? 33 VAL A N 1 ATOM 253 C CA . VAL A 1 33 ? 11.956 1.693 38.197 1.00 20.59 ? 33 VAL A CA 1 ATOM 254 C C . VAL A 1 33 ? 10.673 1.115 37.629 1.00 27.61 ? 33 VAL A C 1 ATOM 255 O O . VAL A 1 33 ? 10.568 0.885 36.422 1.00 28.93 ? 33 VAL A O 1 ATOM 256 C CB . VAL A 1 33 ? 12.180 3.106 37.603 1.00 21.72 ? 33 VAL A CB 1 ATOM 257 C CG1 . VAL A 1 33 ? 10.984 4.002 37.892 1.00 15.74 ? 33 VAL A CG1 1 ATOM 258 C CG2 . VAL A 1 33 ? 13.446 3.720 38.172 1.00 15.51 ? 33 VAL A CG2 1 ATOM 259 N N . THR A 1 34 ? 9.713 0.850 38.506 1.00 31.68 ? 34 THR A N 1 ATOM 260 C CA . THR A 1 34 ? 8.429 0.298 38.090 1.00 36.01 ? 34 THR A CA 1 ATOM 261 C C . THR A 1 34 ? 7.491 1.426 37.669 1.00 38.72 ? 34 THR A C 1 ATOM 262 O O . THR A 1 34 ? 7.734 2.591 37.983 1.00 41.66 ? 34 THR A O 1 ATOM 263 C CB . THR A 1 34 ? 7.770 -0.500 39.231 1.00 36.94 ? 34 THR A CB 1 ATOM 264 O OG1 . THR A 1 34 ? 7.449 0.386 40.311 1.00 39.11 ? 34 THR A OG1 1 ATOM 265 C CG2 . THR A 1 34 ? 8.716 -1.576 39.739 1.00 37.02 ? 34 THR A CG2 1 ATOM 266 N N . VAL A 1 35 ? 6.421 1.072 36.961 1.00 45.54 ? 35 VAL A N 1 ATOM 267 C CA . VAL A 1 35 ? 5.430 2.046 36.503 1.00 49.15 ? 35 VAL A CA 1 ATOM 268 C C . VAL A 1 35 ? 4.763 2.744 37.696 1.00 50.88 ? 35 VAL A C 1 ATOM 269 O O . VAL A 1 35 ? 4.352 3.900 37.599 1.00 50.67 ? 35 VAL A O 1 ATOM 270 C CB . VAL A 1 35 ? 4.345 1.367 35.624 1.00 54.47 ? 35 VAL A CB 1 ATOM 271 C CG1 . VAL A 1 35 ? 3.464 0.436 36.471 1.00 59.75 ? 35 VAL A CG1 1 ATOM 272 C CG2 . VAL A 1 35 ? 3.508 2.415 34.905 1.00 54.91 ? 35 VAL A CG2 1 ATOM 273 N N . GLU A 1 36 ? 4.677 2.035 38.820 1.00 52.65 ? 36 GLU A N 1 ATOM 274 C CA . GLU A 1 36 ? 4.078 2.572 40.039 1.00 52.64 ? 36 GLU A CA 1 ATOM 275 C C . GLU A 1 36 ? 4.960 3.681 40.599 1.00 50.05 ? 36 GLU A C 1 ATOM 276 O O . GLU A 1 36 ? 4.495 4.800 40.823 1.00 53.84 ? 36 GLU A O 1 ATOM 277 C CB . GLU A 1 36 ? 3.948 1.473 41.092 1.00 61.16 ? 36 GLU A CB 1 ATOM 278 C CG . GLU A 1 36 ? 3.445 0.142 40.565 1.00 69.73 ? 36 GLU A CG 1 ATOM 279 C CD . GLU A 1 36 ? 4.198 -1.038 41.164 1.00 76.39 ? 36 GLU A CD 1 ATOM 280 O OE1 . GLU A 1 36 ? 4.757 -0.902 42.277 1.00 77.39 ? 36 GLU A OE1 1 ATOM 281 O OE2 . GLU A 1 36 ? 4.238 -2.105 40.518 1.00 77.77 ? 36 GLU A OE2 1 ATOM 282 N N . THR A 1 37 ? 6.232 3.355 40.828 1.00 44.55 ? 37 THR A N 1 ATOM 283 C CA . THR A 1 37 ? 7.204 4.305 41.364 1.00 42.71 ? 37 THR A CA 1 ATOM 284 C C . THR A 1 37 ? 7.276 5.562 40.490 1.00 42.44 ? 37 THR A C 1 ATOM 285 O O . THR A 1 37 ? 7.340 6.681 41.003 1.00 42.10 ? 37 THR A O 1 ATOM 286 C CB . THR A 1 37 ? 8.615 3.672 41.447 1.00 44.66 ? 37 THR A CB 1 ATOM 287 O OG1 . THR A 1 37 ? 8.528 2.371 42.040 1.00 46.34 ? 37 THR A OG1 1 ATOM 288 C CG2 . THR A 1 37 ? 9.544 4.536 42.290 1.00 41.79 ? 37 THR A CG2 1 ATOM 289 N N . TRP A 1 38 ? 7.239 5.364 39.172 1.00 42.16 ? 38 TRP A N 1 ATOM 290 C CA . TRP A 1 38 ? 7.305 6.459 38.203 1.00 39.46 ? 38 TRP A CA 1 ATOM 291 C C . TRP A 1 38 ? 6.096 7.393 38.300 1.00 42.03 ? 38 TRP A C 1 ATOM 292 O O . TRP A 1 38 ? 6.249 8.617 38.278 1.00 41.15 ? 38 TRP A O 1 ATOM 293 C CB . TRP A 1 38 ? 7.428 5.896 36.780 1.00 32.30 ? 38 TRP A CB 1 ATOM 294 C CG . TRP A 1 38 ? 7.661 6.931 35.701 1.00 24.31 ? 38 TRP A CG 1 ATOM 295 C CD1 . TRP A 1 38 ? 6.790 7.298 34.715 1.00 18.18 ? 38 TRP A CD1 1 ATOM 296 C CD2 . TRP A 1 38 ? 8.859 7.693 35.485 1.00 16.86 ? 38 TRP A CD2 1 ATOM 297 N NE1 . TRP A 1 38 ? 7.369 8.235 33.897 1.00 19.40 ? 38 TRP A NE1 1 ATOM 298 C CE2 . TRP A 1 38 ? 8.638 8.498 34.344 1.00 19.29 ? 38 TRP A CE2 1 ATOM 299 C CE3 . TRP A 1 38 ? 10.097 7.773 36.138 1.00 22.01 ? 38 TRP A CE3 1 ATOM 300 C CZ2 . TRP A 1 38 ? 9.611 9.372 33.842 1.00 14.35 ? 38 TRP A CZ2 1 ATOM 301 C CZ3 . TRP A 1 38 ? 11.065 8.641 35.639 1.00 17.86 ? 38 TRP A CZ3 1 ATOM 302 C CH2 . TRP A 1 38 ? 10.813 9.429 34.501 1.00 17.91 ? 38 TRP A CH2 1 ATOM 303 N N . GLN A 1 39 ? 4.902 6.813 38.421 1.00 42.44 ? 39 GLN A N 1 ATOM 304 C CA . GLN A 1 39 ? 3.676 7.599 38.523 1.00 44.49 ? 39 GLN A CA 1 ATOM 305 C C . GLN A 1 39 ? 3.551 8.367 39.836 1.00 46.94 ? 39 GLN A C 1 ATOM 306 O O . GLN A 1 39 ? 2.690 9.236 39.972 1.00 47.20 ? 39 GLN A O 1 ATOM 307 C CB . GLN A 1 39 ? 2.456 6.715 38.288 1.00 44.40 ? 39 GLN A CB 1 ATOM 308 C CG . GLN A 1 39 ? 2.354 6.233 36.850 1.00 53.16 ? 39 GLN A CG 1 ATOM 309 C CD . GLN A 1 39 ? 1.292 5.173 36.648 1.00 59.98 ? 39 GLN A CD 1 ATOM 310 O OE1 . GLN A 1 39 ? 0.797 4.578 37.607 1.00 67.08 ? 39 GLN A OE1 1 ATOM 311 N NE2 . GLN A 1 39 ? 0.943 4.922 35.392 1.00 59.24 ? 39 GLN A NE2 1 ATOM 312 N N . GLU A 1 40 ? 4.421 8.053 40.795 1.00 49.96 ? 40 GLU A N 1 ATOM 313 C CA . GLU A 1 40 ? 4.428 8.743 42.080 1.00 52.49 ? 40 GLU A CA 1 ATOM 314 C C . GLU A 1 40 ? 4.853 10.200 41.834 1.00 52.77 ? 40 GLU A C 1 ATOM 315 O O . GLU A 1 40 ? 4.470 11.100 42.581 1.00 54.24 ? 40 GLU A O 1 ATOM 316 C CB . GLU A 1 40 ? 5.373 8.031 43.054 1.00 53.55 ? 40 GLU A CB 1 ATOM 317 C CG . GLU A 1 40 ? 5.412 8.617 44.451 1.00 59.79 ? 40 GLU A CG 1 ATOM 318 C CD . GLU A 1 40 ? 6.628 9.486 44.674 1.00 66.11 ? 40 GLU A CD 1 ATOM 319 O OE1 . GLU A 1 40 ? 7.700 8.924 44.984 1.00 70.23 ? 40 GLU A OE1 1 ATOM 320 O OE2 . GLU A 1 40 ? 6.517 10.723 44.528 1.00 69.73 ? 40 GLU A OE2 1 ATOM 321 N N . GLY A 1 41 ? 5.649 10.415 40.783 1.00 50.64 ? 41 GLY A N 1 ATOM 322 C CA . GLY A 1 41 ? 6.069 11.757 40.415 1.00 44.43 ? 41 GLY A CA 1 ATOM 323 C C . GLY A 1 41 ? 7.438 12.310 40.773 1.00 42.61 ? 41 GLY A C 1 ATOM 324 O O . GLY A 1 41 ? 8.028 13.035 39.974 1.00 43.64 ? 41 GLY A O 1 ATOM 325 N N . SER A 1 42 ? 7.949 11.983 41.955 1.00 42.42 ? 42 SER A N 1 ATOM 326 C CA . SER A 1 42 ? 9.241 12.506 42.405 1.00 44.32 ? 42 SER A CA 1 ATOM 327 C C . SER A 1 42 ? 10.445 12.287 41.484 1.00 41.57 ? 42 SER A C 1 ATOM 328 O O . SER A 1 42 ? 11.182 13.233 41.205 1.00 44.27 ? 42 SER A O 1 ATOM 329 C CB . SER A 1 42 ? 9.560 12.000 43.812 1.00 41.72 ? 42 SER A CB 1 ATOM 330 O OG . SER A 1 42 ? 9.633 10.588 43.833 1.00 54.29 ? 42 SER A OG 1 ATOM 331 N N . LEU A 1 43 ? 10.649 11.053 41.023 1.00 39.95 ? 43 LEU A N 1 ATOM 332 C CA . LEU A 1 43 ? 11.777 10.738 40.141 1.00 34.67 ? 43 LEU A CA 1 ATOM 333 C C . LEU A 1 43 ? 11.672 11.474 38.803 1.00 31.40 ? 43 LEU A C 1 ATOM 334 O O . LEU A 1 43 ? 12.646 12.074 38.344 1.00 30.49 ? 43 LEU A O 1 ATOM 335 C CB . LEU A 1 43 ? 11.865 9.229 39.883 1.00 31.59 ? 43 LEU A CB 1 ATOM 336 C CG . LEU A 1 43 ? 13.242 8.567 39.694 1.00 30.92 ? 43 LEU A CG 1 ATOM 337 C CD1 . LEU A 1 43 ? 13.109 7.457 38.677 1.00 27.88 ? 43 LEU A CD1 1 ATOM 338 C CD2 . LEU A 1 43 ? 14.315 9.549 39.246 1.00 29.03 ? 43 LEU A CD2 1 ATOM 339 N N . LYS A 1 44 ? 10.494 11.415 38.184 1.00 24.34 ? 44 LYS A N 1 ATOM 340 C CA . LYS A 1 44 ? 10.247 12.071 36.901 1.00 27.16 ? 44 LYS A CA 1 ATOM 341 C C . LYS A 1 44 ? 10.612 13.551 36.969 1.00 31.60 ? 44 LYS A C 1 ATOM 342 O O . LYS A 1 44 ? 11.250 14.086 36.062 1.00 33.78 ? 44 LYS A O 1 ATOM 343 C CB . LYS A 1 44 ? 8.775 11.939 36.516 1.00 24.51 ? 44 LYS A CB 1 ATOM 344 C CG . LYS A 1 44 ? 8.460 12.409 35.105 1.00 25.49 ? 44 LYS A CG 1 ATOM 345 C CD . LYS A 1 44 ? 6.964 12.558 34.887 1.00 25.65 ? 44 LYS A CD 1 ATOM 346 C CE . LYS A 1 44 ? 6.572 12.269 33.444 1.00 27.65 ? 44 LYS A CE 1 ATOM 347 N NZ . LYS A 1 44 ? 7.455 12.940 32.449 1.00 30.67 ? 44 LYS A NZ 1 ATOM 348 N N . ALA A 1 45 ? 10.226 14.189 38.071 1.00 32.54 ? 45 ALA A N 1 ATOM 349 C CA . ALA A 1 45 ? 10.485 15.604 38.295 1.00 27.71 ? 45 ALA A CA 1 ATOM 350 C C . ALA A 1 45 ? 11.972 15.932 38.382 1.00 29.20 ? 45 ALA A C 1 ATOM 351 O O . ALA A 1 45 ? 12.385 17.032 38.017 1.00 35.04 ? 45 ALA A O 1 ATOM 352 C CB . ALA A 1 45 ? 9.769 16.070 39.554 1.00 31.87 ? 45 ALA A CB 1 ATOM 353 N N . SER A 1 46 ? 12.772 14.989 38.874 1.00 25.18 ? 46 SER A N 1 ATOM 354 C CA . SER A 1 46 ? 14.214 15.203 38.996 1.00 27.63 ? 46 SER A CA 1 ATOM 355 C C . SER A 1 46 ? 14.982 14.889 37.710 1.00 27.98 ? 46 SER A C 1 ATOM 356 O O . SER A 1 46 ? 16.181 15.164 37.620 1.00 30.37 ? 46 SER A O 1 ATOM 357 C CB . SER A 1 46 ? 14.785 14.382 40.150 1.00 29.21 ? 46 SER A CB 1 ATOM 358 O OG . SER A 1 46 ? 14.561 12.999 39.945 1.00 44.20 ? 46 SER A OG 1 ATOM 359 N N . CYS A 1 47 ? 14.304 14.271 36.742 1.00 23.03 ? 47 CYS A N 1 ATOM 360 C CA . CYS A 1 47 ? 14.919 13.937 35.454 1.00 26.37 ? 47 CYS A CA 1 ATOM 361 C C . CYS A 1 47 ? 14.912 15.173 34.559 1.00 25.13 ? 47 CYS A C 1 ATOM 362 O O . CYS A 1 47 ? 13.866 15.806 34.386 1.00 22.91 ? 47 CYS A O 1 ATOM 363 C CB . CYS A 1 47 ? 14.152 12.808 34.760 1.00 23.46 ? 47 CYS A CB 1 ATOM 364 S SG . CYS A 1 47 ? 14.304 11.197 35.554 1.00 27.54 ? 47 CYS A SG 1 ATOM 365 N N . LEU A 1 48 ? 16.067 15.487 33.971 1.00 21.04 ? 48 LEU A N 1 ATOM 366 C CA . LEU A 1 48 ? 16.221 16.659 33.103 1.00 20.83 ? 48 LEU A CA 1 ATOM 367 C C . LEU A 1 48 ? 15.094 16.874 32.084 1.00 23.19 ? 48 LEU A C 1 ATOM 368 O O . LEU A 1 48 ? 14.545 17.971 31.989 1.00 22.36 ? 48 LEU A O 1 ATOM 369 C CB . LEU A 1 48 ? 17.572 16.613 32.388 1.00 21.43 ? 48 LEU A CB 1 ATOM 370 C CG . LEU A 1 48 ? 17.905 17.809 31.494 1.00 23.36 ? 48 LEU A CG 1 ATOM 371 C CD1 . LEU A 1 48 ? 17.888 19.098 32.309 1.00 22.48 ? 48 LEU A CD1 1 ATOM 372 C CD2 . LEU A 1 48 ? 19.263 17.598 30.853 1.00 22.00 ? 48 LEU A CD2 1 ATOM 373 N N . TYR A 1 49 ? 14.754 15.834 31.326 1.00 17.93 ? 49 TYR A N 1 ATOM 374 C CA . TYR A 1 49 ? 13.688 15.931 30.332 1.00 17.34 ? 49 TYR A CA 1 ATOM 375 C C . TYR A 1 49 ? 12.441 15.158 30.766 1.00 21.20 ? 49 TYR A C 1 ATOM 376 O O . TYR A 1 49 ? 11.530 14.928 29.961 1.00 14.11 ? 49 TYR A O 1 ATOM 377 C CB . TYR A 1 49 ? 14.175 15.426 28.970 1.00 17.04 ? 49 TYR A CB 1 ATOM 378 C CG . TYR A 1 49 ? 15.371 16.179 28.427 1.00 14.10 ? 49 TYR A CG 1 ATOM 379 C CD1 . TYR A 1 49 ? 15.281 17.531 28.084 1.00 14.26 ? 49 TYR A CD1 1 ATOM 380 C CD2 . TYR A 1 49 ? 16.596 15.538 28.252 1.00 10.28 ? 49 TYR A CD2 1 ATOM 381 C CE1 . TYR A 1 49 ? 16.391 18.223 27.578 1.00 7.64 ? 49 TYR A CE1 1 ATOM 382 C CE2 . TYR A 1 49 ? 17.707 16.215 27.748 1.00 10.99 ? 49 TYR A CE2 1 ATOM 383 C CZ . TYR A 1 49 ? 17.599 17.555 27.413 1.00 14.17 ? 49 TYR A CZ 1 ATOM 384 O OH . TYR A 1 49 ? 18.697 18.217 26.906 1.00 19.78 ? 49 TYR A OH 1 ATOM 385 N N . GLY A 1 50 ? 12.413 14.771 32.043 1.00 20.57 ? 50 GLY A N 1 ATOM 386 C CA . GLY A 1 50 ? 11.288 14.033 32.598 1.00 16.47 ? 50 GLY A CA 1 ATOM 387 C C . GLY A 1 50 ? 11.147 12.622 32.061 1.00 19.02 ? 50 GLY A C 1 ATOM 388 O O . GLY A 1 50 ? 10.043 12.068 32.051 1.00 21.41 ? 50 GLY A O 1 ATOM 389 N N . GLN A 1 51 ? 12.254 12.036 31.608 1.00 16.59 ? 51 GLN A N 1 ATOM 390 C CA . GLN A 1 51 ? 12.215 10.686 31.059 1.00 15.75 ? 51 GLN A CA 1 ATOM 391 C C . GLN A 1 51 ? 13.437 9.843 31.405 1.00 18.20 ? 51 GLN A C 1 ATOM 392 O O . GLN A 1 51 ? 14.458 10.358 31.865 1.00 15.12 ? 51 GLN A O 1 ATOM 393 C CB . GLN A 1 51 ? 12.079 10.738 29.534 1.00 13.21 ? 51 GLN A CB 1 ATOM 394 C CG . GLN A 1 51 ? 10.789 11.340 29.017 1.00 14.77 ? 51 GLN A CG 1 ATOM 395 C CD . GLN A 1 51 ? 10.609 11.132 27.529 1.00 15.60 ? 51 GLN A CD 1 ATOM 396 O OE1 . GLN A 1 51 ? 9.567 10.663 27.080 1.00 16.69 ? 51 GLN A OE1 1 ATOM 397 N NE2 . GLN A 1 51 ? 11.640 11.452 26.758 1.00 14.70 ? 51 GLN A NE2 1 ATOM 398 N N . LEU A 1 52 ? 13.300 8.535 31.194 1.00 18.47 ? 52 LEU A N 1 ATOM 399 C CA . LEU A 1 52 ? 14.378 7.575 31.417 1.00 18.09 ? 52 LEU A CA 1 ATOM 400 C C . LEU A 1 52 ? 14.744 7.029 30.028 1.00 18.83 ? 52 LEU A C 1 ATOM 401 O O . LEU A 1 52 ? 13.942 7.114 29.101 1.00 20.56 ? 52 LEU A O 1 ATOM 402 C CB . LEU A 1 52 ? 13.906 6.449 32.346 1.00 17.44 ? 52 LEU A CB 1 ATOM 403 C CG . LEU A 1 52 ? 13.559 6.853 33.787 1.00 18.00 ? 52 LEU A CG 1 ATOM 404 C CD1 . LEU A 1 52 ? 13.012 5.654 34.554 1.00 13.76 ? 52 LEU A CD1 1 ATOM 405 C CD2 . LEU A 1 52 ? 14.787 7.422 34.491 1.00 13.17 ? 52 LEU A CD2 1 ATOM 406 N N . PRO A 1 53 ? 15.916 6.393 29.879 1.00 19.09 ? 53 PRO A N 1 ATOM 407 C CA . PRO A 1 53 ? 16.958 6.104 30.868 1.00 19.90 ? 53 PRO A CA 1 ATOM 408 C C . PRO A 1 53 ? 17.741 7.269 31.463 1.00 19.01 ? 53 PRO A C 1 ATOM 409 O O . PRO A 1 53 ? 17.821 8.365 30.900 1.00 19.10 ? 53 PRO A O 1 ATOM 410 C CB . PRO A 1 53 ? 17.899 5.173 30.101 1.00 14.57 ? 53 PRO A CB 1 ATOM 411 C CG . PRO A 1 53 ? 17.827 5.716 28.710 1.00 15.00 ? 53 PRO A CG 1 ATOM 412 C CD . PRO A 1 53 ? 16.329 5.916 28.543 1.00 15.74 ? 53 PRO A CD 1 ATOM 413 N N . LYS A 1 54 ? 18.298 6.988 32.634 1.00 18.09 ? 54 LYS A N 1 ATOM 414 C CA . LYS A 1 54 ? 19.153 7.896 33.370 1.00 15.15 ? 54 LYS A CA 1 ATOM 415 C C . LYS A 1 54 ? 20.388 7.017 33.525 1.00 14.00 ? 54 LYS A C 1 ATOM 416 O O . LYS A 1 54 ? 20.275 5.817 33.763 1.00 14.38 ? 54 LYS A O 1 ATOM 417 C CB . LYS A 1 54 ? 18.557 8.225 34.736 1.00 20.85 ? 54 LYS A CB 1 ATOM 418 C CG . LYS A 1 54 ? 19.461 9.088 35.602 1.00 22.60 ? 54 LYS A CG 1 ATOM 419 C CD . LYS A 1 54 ? 18.866 9.289 36.976 1.00 24.68 ? 54 LYS A CD 1 ATOM 420 C CE . LYS A 1 54 ? 19.861 9.935 37.918 1.00 28.90 ? 54 LYS A CE 1 ATOM 421 N NZ . LYS A 1 54 ? 19.290 10.038 39.285 1.00 35.09 ? 54 LYS A NZ 1 ATOM 422 N N . PHE A 1 55 ? 21.564 7.600 33.378 1.00 15.39 ? 55 PHE A N 1 ATOM 423 C CA . PHE A 1 55 ? 22.793 6.830 33.465 1.00 15.69 ? 55 PHE A CA 1 ATOM 424 C C . PHE A 1 55 ? 23.797 7.525 34.363 1.00 16.50 ? 55 PHE A C 1 ATOM 425 O O . PHE A 1 55 ? 23.813 8.746 34.460 1.00 22.85 ? 55 PHE A O 1 ATOM 426 C CB . PHE A 1 55 ? 23.367 6.672 32.056 1.00 15.26 ? 55 PHE A CB 1 ATOM 427 C CG . PHE A 1 55 ? 24.585 5.793 31.971 1.00 15.55 ? 55 PHE A CG 1 ATOM 428 C CD1 . PHE A 1 55 ? 24.465 4.407 31.997 1.00 14.64 ? 55 PHE A CD1 1 ATOM 429 C CD2 . PHE A 1 55 ? 25.848 6.352 31.796 1.00 17.14 ? 55 PHE A CD2 1 ATOM 430 C CE1 . PHE A 1 55 ? 25.585 3.590 31.845 1.00 17.76 ? 55 PHE A CE1 1 ATOM 431 C CE2 . PHE A 1 55 ? 26.974 5.543 31.643 1.00 22.44 ? 55 PHE A CE2 1 ATOM 432 C CZ . PHE A 1 55 ? 26.840 4.160 31.667 1.00 19.74 ? 55 PHE A CZ 1 ATOM 433 N N . GLN A 1 56 ? 24.620 6.739 35.041 1.00 19.92 ? 56 GLN A N 1 ATOM 434 C CA . GLN A 1 56 ? 25.636 7.294 35.912 1.00 18.05 ? 56 GLN A CA 1 ATOM 435 C C . GLN A 1 56 ? 26.976 6.626 35.693 1.00 15.01 ? 56 GLN A C 1 ATOM 436 O O . GLN A 1 56 ? 27.080 5.402 35.614 1.00 22.29 ? 56 GLN A O 1 ATOM 437 C CB . GLN A 1 56 ? 25.212 7.189 37.379 1.00 23.86 ? 56 GLN A CB 1 ATOM 438 C CG . GLN A 1 56 ? 24.110 8.162 37.756 1.00 28.42 ? 56 GLN A CG 1 ATOM 439 C CD . GLN A 1 56 ? 23.567 7.936 39.146 1.00 39.11 ? 56 GLN A CD 1 ATOM 440 O OE1 . GLN A 1 56 ? 23.592 6.820 39.662 1.00 41.93 ? 56 GLN A OE1 1 ATOM 441 N NE2 . GLN A 1 56 ? 23.039 8.992 39.750 1.00 46.95 ? 56 GLN A NE2 1 ATOM 442 N N . ASP A 1 57 ? 27.985 7.462 35.507 1.00 13.98 ? 57 ASP A N 1 ATOM 443 C CA . ASP A 1 57 ? 29.354 7.026 35.324 1.00 19.23 ? 57 ASP A CA 1 ATOM 444 C C . ASP A 1 57 ? 30.075 7.835 36.396 1.00 21.08 ? 57 ASP A C 1 ATOM 445 O O . ASP A 1 57 ? 30.418 8.994 36.180 1.00 22.39 ? 57 ASP A O 1 ATOM 446 C CB . ASP A 1 57 ? 29.844 7.403 33.925 1.00 19.42 ? 57 ASP A CB 1 ATOM 447 C CG . ASP A 1 57 ? 31.292 7.016 33.683 1.00 26.39 ? 57 ASP A CG 1 ATOM 448 O OD1 . ASP A 1 57 ? 31.934 6.448 34.592 1.00 30.68 ? 57 ASP A OD1 1 ATOM 449 O OD2 . ASP A 1 57 ? 31.802 7.305 32.583 1.00 28.67 ? 57 ASP A OD2 1 ATOM 450 N N . GLY A 1 58 ? 30.265 7.231 37.565 1.00 21.95 ? 58 GLY A N 1 ATOM 451 C CA . GLY A 1 58 ? 30.895 7.942 38.660 1.00 21.98 ? 58 GLY A CA 1 ATOM 452 C C . GLY A 1 58 ? 29.869 8.974 39.091 1.00 24.46 ? 58 GLY A C 1 ATOM 453 O O . GLY A 1 58 ? 28.704 8.631 39.307 1.00 25.96 ? 58 GLY A O 1 ATOM 454 N N . ASP A 1 59 ? 30.265 10.240 39.167 1.00 27.61 ? 59 ASP A N 1 ATOM 455 C CA . ASP A 1 59 ? 29.319 11.280 39.556 1.00 32.20 ? 59 ASP A CA 1 ATOM 456 C C . ASP A 1 59 ? 28.710 11.998 38.347 1.00 33.47 ? 59 ASP A C 1 ATOM 457 O O . ASP A 1 59 ? 27.966 12.967 38.505 1.00 33.57 ? 59 ASP A O 1 ATOM 458 C CB . ASP A 1 59 ? 29.950 12.273 40.545 1.00 33.78 ? 59 ASP A CB 1 ATOM 459 C CG . ASP A 1 59 ? 30.968 13.201 39.901 1.00 38.79 ? 59 ASP A CG 1 ATOM 460 O OD1 . ASP A 1 59 ? 31.544 12.862 38.847 1.00 43.22 ? 59 ASP A OD1 1 ATOM 461 O OD2 . ASP A 1 59 ? 31.192 14.287 40.472 1.00 40.49 ? 59 ASP A OD2 1 ATOM 462 N N . LEU A 1 60 ? 29.027 11.512 37.145 1.00 29.38 ? 60 LEU A N 1 ATOM 463 C CA . LEU A 1 60 ? 28.494 12.085 35.913 1.00 22.30 ? 60 LEU A CA 1 ATOM 464 C C . LEU A 1 60 ? 27.126 11.457 35.671 1.00 22.13 ? 60 LEU A C 1 ATOM 465 O O . LEU A 1 60 ? 27.011 10.243 35.526 1.00 20.79 ? 60 LEU A O 1 ATOM 466 C CB . LEU A 1 60 ? 29.409 11.766 34.728 1.00 23.91 ? 60 LEU A CB 1 ATOM 467 C CG . LEU A 1 60 ? 29.465 12.720 33.524 1.00 26.34 ? 60 LEU A CG 1 ATOM 468 C CD1 . LEU A 1 60 ? 29.646 11.916 32.249 1.00 18.46 ? 60 LEU A CD1 1 ATOM 469 C CD2 . LEU A 1 60 ? 28.221 13.580 33.425 1.00 19.40 ? 60 LEU A CD2 1 ATOM 470 N N . THR A 1 61 ? 26.090 12.288 35.654 1.00 21.76 ? 61 THR A N 1 ATOM 471 C CA . THR A 1 61 ? 24.728 11.824 35.426 1.00 20.59 ? 61 THR A CA 1 ATOM 472 C C . THR A 1 61 ? 24.315 12.239 34.018 1.00 22.88 ? 61 THR A C 1 ATOM 473 O O . THR A 1 61 ? 24.400 13.412 33.662 1.00 26.82 ? 61 THR A O 1 ATOM 474 C CB . THR A 1 61 ? 23.750 12.425 36.458 1.00 19.20 ? 61 THR A CB 1 ATOM 475 O OG1 . THR A 1 61 ? 24.142 12.018 37.774 1.00 23.37 ? 61 THR A OG1 1 ATOM 476 C CG2 . THR A 1 61 ? 22.324 11.965 36.189 1.00 14.22 ? 61 THR A CG2 1 ATOM 477 N N . LEU A 1 62 ? 23.876 11.266 33.226 1.00 20.75 ? 62 LEU A N 1 ATOM 478 C CA . LEU A 1 62 ? 23.472 11.496 31.843 1.00 20.15 ? 62 LEU A CA 1 ATOM 479 C C . LEU A 1 62 ? 22.042 11.063 31.553 1.00 16.48 ? 62 LEU A C 1 ATOM 480 O O . LEU A 1 62 ? 21.476 10.226 32.251 1.00 19.11 ? 62 LEU A O 1 ATOM 481 C CB . LEU A 1 62 ? 24.410 10.730 30.899 1.00 17.43 ? 62 LEU A CB 1 ATOM 482 C CG . LEU A 1 62 ? 25.628 11.376 30.228 1.00 20.64 ? 62 LEU A CG 1 ATOM 483 C CD1 . LEU A 1 62 ? 25.999 12.710 30.841 1.00 16.69 ? 62 LEU A CD1 1 ATOM 484 C CD2 . LEU A 1 62 ? 26.794 10.404 30.272 1.00 13.52 ? 62 LEU A CD2 1 ATOM 485 N N . TYR A 1 63 ? 21.458 11.681 30.536 1.00 15.84 ? 63 TYR A N 1 ATOM 486 C CA . TYR A 1 63 ? 20.116 11.356 30.068 1.00 15.90 ? 63 TYR A CA 1 ATOM 487 C C . TYR A 1 63 ? 20.251 11.221 28.550 1.00 18.36 ? 63 TYR A C 1 ATOM 488 O O . TYR A 1 63 ? 21.303 11.560 27.995 1.00 14.60 ? 63 TYR A O 1 ATOM 489 C CB . TYR A 1 63 ? 19.116 12.453 30.432 1.00 14.13 ? 63 TYR A CB 1 ATOM 490 C CG . TYR A 1 63 ? 18.897 12.591 31.921 1.00 25.28 ? 63 TYR A CG 1 ATOM 491 C CD1 . TYR A 1 63 ? 17.919 11.843 32.579 1.00 23.89 ? 63 TYR A CD1 1 ATOM 492 C CD2 . TYR A 1 63 ? 19.688 13.453 32.682 1.00 23.41 ? 63 TYR A CD2 1 ATOM 493 C CE1 . TYR A 1 63 ? 17.741 11.951 33.961 1.00 26.69 ? 63 TYR A CE1 1 ATOM 494 C CE2 . TYR A 1 63 ? 19.519 13.567 34.054 1.00 25.36 ? 63 TYR A CE2 1 ATOM 495 C CZ . TYR A 1 63 ? 18.548 12.814 34.688 1.00 29.54 ? 63 TYR A CZ 1 ATOM 496 O OH . TYR A 1 63 ? 18.403 12.911 36.051 1.00 30.00 ? 63 TYR A OH 1 ATOM 497 N N . GLN A 1 64 ? 19.210 10.705 27.893 1.00 18.04 ? 64 GLN A N 1 ATOM 498 C CA . GLN A 1 64 ? 19.207 10.506 26.440 1.00 13.42 ? 64 GLN A CA 1 ATOM 499 C C . GLN A 1 64 ? 20.039 9.271 26.079 1.00 10.82 ? 64 GLN A C 1 ATOM 500 O O . GLN A 1 64 ? 21.266 9.262 26.226 1.00 8.81 ? 64 GLN A O 1 ATOM 501 C CB . GLN A 1 64 ? 19.732 11.757 25.718 1.00 14.07 ? 64 GLN A CB 1 ATOM 502 C CG . GLN A 1 64 ? 18.864 12.999 25.915 1.00 13.48 ? 64 GLN A CG 1 ATOM 503 C CD . GLN A 1 64 ? 17.596 12.954 25.091 1.00 13.00 ? 64 GLN A CD 1 ATOM 504 O OE1 . GLN A 1 64 ? 17.369 12.010 24.339 1.00 15.01 ? 64 GLN A OE1 1 ATOM 505 N NE2 . GLN A 1 64 ? 16.786 13.992 25.195 1.00 16.67 ? 64 GLN A NE2 1 ATOM 506 N N . SER A 1 65 ? 19.354 8.232 25.607 1.00 9.18 ? 65 SER A N 1 ATOM 507 C CA . SER A 1 65 ? 19.990 6.965 25.253 1.00 11.06 ? 65 SER A CA 1 ATOM 508 C C . SER A 1 65 ? 21.186 7.099 24.315 1.00 14.01 ? 65 SER A C 1 ATOM 509 O O . SER A 1 65 ? 22.228 6.480 24.552 1.00 13.57 ? 65 SER A O 1 ATOM 510 C CB . SER A 1 65 ? 18.962 6.000 24.665 1.00 9.51 ? 65 SER A CB 1 ATOM 511 O OG . SER A 1 65 ? 18.347 6.550 23.517 1.00 13.08 ? 65 SER A OG 1 ATOM 512 N N . ASN A 1 66 ? 21.050 7.922 23.273 1.00 13.94 ? 66 ASN A N 1 ATOM 513 C CA . ASN A 1 66 ? 22.142 8.122 22.315 1.00 8.62 ? 66 ASN A CA 1 ATOM 514 C C . ASN A 1 66 ? 23.332 8.882 22.895 1.00 9.76 ? 66 ASN A C 1 ATOM 515 O O . ASN A 1 66 ? 24.466 8.685 22.462 1.00 12.73 ? 66 ASN A O 1 ATOM 516 C CB . ASN A 1 66 ? 21.634 8.801 21.040 1.00 11.38 ? 66 ASN A CB 1 ATOM 517 C CG . ASN A 1 66 ? 20.720 7.895 20.233 1.00 13.25 ? 66 ASN A CG 1 ATOM 518 O OD1 . ASN A 1 66 ? 21.144 6.837 19.781 1.00 17.17 ? 66 ASN A OD1 1 ATOM 519 N ND2 . ASN A 1 66 ? 19.475 8.304 20.046 1.00 6.17 ? 66 ASN A ND2 1 ATOM 520 N N . THR A 1 67 ? 23.081 9.762 23.862 1.00 9.23 ? 67 THR A N 1 ATOM 521 C CA . THR A 1 67 ? 24.164 10.497 24.511 1.00 11.51 ? 67 THR A CA 1 ATOM 522 C C . THR A 1 67 ? 24.961 9.464 25.313 1.00 13.47 ? 67 THR A C 1 ATOM 523 O O . THR A 1 67 ? 26.188 9.489 25.338 1.00 14.69 ? 67 THR A O 1 ATOM 524 C CB . THR A 1 67 ? 23.628 11.586 25.453 1.00 11.68 ? 67 THR A CB 1 ATOM 525 O OG1 . THR A 1 67 ? 23.059 12.638 24.674 1.00 12.63 ? 67 THR A OG1 1 ATOM 526 C CG2 . THR A 1 67 ? 24.737 12.150 26.313 1.00 10.29 ? 67 THR A CG2 1 ATOM 527 N N . ILE A 1 68 ? 24.243 8.537 25.943 1.00 14.73 ? 68 ILE A N 1 ATOM 528 C CA . ILE A 1 68 ? 24.864 7.475 26.724 1.00 14.48 ? 68 ILE A CA 1 ATOM 529 C C . ILE A 1 68 ? 25.715 6.613 25.791 1.00 11.25 ? 68 ILE A C 1 ATOM 530 O O . ILE A 1 68 ? 26.866 6.311 26.106 1.00 9.56 ? 68 ILE A O 1 ATOM 531 C CB . ILE A 1 68 ? 23.793 6.616 27.436 1.00 12.79 ? 68 ILE A CB 1 ATOM 532 C CG1 . ILE A 1 68 ? 22.972 7.505 28.374 1.00 9.13 ? 68 ILE A CG1 1 ATOM 533 C CG2 . ILE A 1 68 ? 24.449 5.488 28.217 1.00 9.82 ? 68 ILE A CG2 1 ATOM 534 C CD1 . ILE A 1 68 ? 21.649 6.904 28.789 1.00 13.17 ? 68 ILE A CD1 1 ATOM 535 N N . LEU A 1 69 ? 25.160 6.244 24.636 1.00 13.07 ? 69 LEU A N 1 ATOM 536 C CA . LEU A 1 69 ? 25.890 5.439 23.655 1.00 12.02 ? 69 LEU A CA 1 ATOM 537 C C . LEU A 1 69 ? 27.159 6.151 23.193 1.00 15.87 ? 69 LEU A C 1 ATOM 538 O O . LEU A 1 69 ? 28.242 5.555 23.182 1.00 12.15 ? 69 LEU A O 1 ATOM 539 C CB . LEU A 1 69 ? 25.009 5.117 22.444 1.00 12.58 ? 69 LEU A CB 1 ATOM 540 C CG . LEU A 1 69 ? 24.017 3.967 22.607 1.00 12.17 ? 69 LEU A CG 1 ATOM 541 C CD1 . LEU A 1 69 ? 23.139 3.859 21.380 1.00 19.20 ? 69 LEU A CD1 1 ATOM 542 C CD2 . LEU A 1 69 ? 24.776 2.669 22.825 1.00 15.60 ? 69 LEU A CD2 1 ATOM 543 N N . ARG A 1 70 ? 27.034 7.436 22.857 1.00 13.86 ? 70 ARG A N 1 ATOM 544 C CA . ARG A 1 70 ? 28.183 8.215 22.397 1.00 15.49 ? 70 ARG A CA 1 ATOM 545 C C . ARG A 1 70 ? 29.235 8.388 23.479 1.00 12.74 ? 70 ARG A C 1 ATOM 546 O O . ARG A 1 70 ? 30.434 8.364 23.196 1.00 17.08 ? 70 ARG A O 1 ATOM 547 C CB . ARG A 1 70 ? 27.743 9.572 21.846 1.00 15.49 ? 70 ARG A CB 1 ATOM 548 C CG . ARG A 1 70 ? 27.052 9.453 20.506 1.00 14.53 ? 70 ARG A CG 1 ATOM 549 C CD . ARG A 1 70 ? 26.774 10.795 19.854 1.00 16.53 ? 70 ARG A CD 1 ATOM 550 N NE . ARG A 1 70 ? 26.441 10.597 18.447 1.00 14.43 ? 70 ARG A NE 1 ATOM 551 C CZ . ARG A 1 70 ? 25.205 10.484 17.969 1.00 20.23 ? 70 ARG A CZ 1 ATOM 552 N NH1 . ARG A 1 70 ? 24.159 10.568 18.784 1.00 16.25 ? 70 ARG A NH1 1 ATOM 553 N NH2 . ARG A 1 70 ? 25.016 10.217 16.680 1.00 18.14 ? 70 ARG A NH2 1 ATOM 554 N N . HIS A 1 71 ? 28.782 8.527 24.721 1.00 13.52 ? 71 HIS A N 1 ATOM 555 C CA . HIS A 1 71 ? 29.689 8.682 25.850 1.00 16.67 ? 71 HIS A CA 1 ATOM 556 C C . HIS A 1 71 ? 30.530 7.419 26.031 1.00 17.31 ? 71 HIS A C 1 ATOM 557 O O . HIS A 1 71 ? 31.750 7.487 26.199 1.00 22.38 ? 71 HIS A O 1 ATOM 558 C CB . HIS A 1 71 ? 28.904 8.974 27.125 1.00 13.99 ? 71 HIS A CB 1 ATOM 559 C CG . HIS A 1 71 ? 29.754 8.985 28.353 1.00 18.15 ? 71 HIS A CG 1 ATOM 560 N ND1 . HIS A 1 71 ? 30.773 9.893 28.542 1.00 19.19 ? 71 HIS A ND1 1 ATOM 561 C CD2 . HIS A 1 71 ? 29.774 8.167 29.431 1.00 17.73 ? 71 HIS A CD2 1 ATOM 562 C CE1 . HIS A 1 71 ? 31.389 9.633 29.681 1.00 18.15 ? 71 HIS A CE1 1 ATOM 563 N NE2 . HIS A 1 71 ? 30.800 8.591 30.241 1.00 21.88 ? 71 HIS A NE2 1 ATOM 564 N N . LEU A 1 72 ? 29.861 6.269 26.017 1.00 21.14 ? 72 LEU A N 1 ATOM 565 C CA . LEU A 1 72 ? 30.529 4.976 26.151 1.00 17.46 ? 72 LEU A CA 1 ATOM 566 C C . LEU A 1 72 ? 31.444 4.720 24.950 1.00 16.31 ? 72 LEU A C 1 ATOM 567 O O . LEU A 1 72 ? 32.557 4.215 25.109 1.00 18.77 ? 72 LEU A O 1 ATOM 568 C CB . LEU A 1 72 ? 29.487 3.858 26.274 1.00 14.33 ? 72 LEU A CB 1 ATOM 569 C CG . LEU A 1 72 ? 29.079 3.354 27.668 1.00 18.13 ? 72 LEU A CG 1 ATOM 570 C CD1 . LEU A 1 72 ? 29.458 4.336 28.757 1.00 20.50 ? 72 LEU A CD1 1 ATOM 571 C CD2 . LEU A 1 72 ? 27.586 3.061 27.692 1.00 13.42 ? 72 LEU A CD2 1 ATOM 572 N N . GLY A 1 73 ? 30.986 5.098 23.757 1.00 13.56 ? 73 GLY A N 1 ATOM 573 C CA . GLY A 1 73 ? 31.785 4.909 22.557 1.00 10.32 ? 73 GLY A CA 1 ATOM 574 C C . GLY A 1 73 ? 33.052 5.737 22.606 1.00 14.46 ? 73 GLY A C 1 ATOM 575 O O . GLY A 1 73 ? 34.115 5.308 22.169 1.00 17.30 ? 73 GLY A O 1 ATOM 576 N N . ARG A 1 74 ? 32.946 6.915 23.200 1.00 19.09 ? 74 ARG A N 1 ATOM 577 C CA . ARG A 1 74 ? 34.077 7.821 23.322 1.00 22.29 ? 74 ARG A CA 1 ATOM 578 C C . ARG A 1 74 ? 35.078 7.358 24.384 1.00 22.87 ? 74 ARG A C 1 ATOM 579 O O . ARG A 1 74 ? 36.281 7.313 24.130 1.00 23.07 ? 74 ARG A O 1 ATOM 580 C CB . ARG A 1 74 ? 33.551 9.217 23.650 1.00 22.22 ? 74 ARG A CB 1 ATOM 581 C CG . ARG A 1 74 ? 34.495 10.364 23.359 1.00 24.79 ? 74 ARG A CG 1 ATOM 582 C CD . ARG A 1 74 ? 33.688 11.611 22.990 1.00 22.08 ? 74 ARG A CD 1 ATOM 583 N NE . ARG A 1 74 ? 32.500 11.712 23.828 1.00 20.83 ? 74 ARG A NE 1 ATOM 584 C CZ . ARG A 1 74 ? 31.296 12.067 23.399 1.00 19.72 ? 74 ARG A CZ 1 ATOM 585 N NH1 . ARG A 1 74 ? 31.099 12.383 22.127 1.00 15.61 ? 74 ARG A NH1 1 ATOM 586 N NH2 . ARG A 1 74 ? 30.266 12.022 24.234 1.00 13.95 ? 74 ARG A NH2 1 ATOM 587 N N . THR A 1 75 ? 34.578 6.983 25.560 1.00 23.78 ? 75 THR A N 1 ATOM 588 C CA . THR A 1 75 ? 35.441 6.542 26.658 1.00 22.93 ? 75 THR A CA 1 ATOM 589 C C . THR A 1 75 ? 36.019 5.137 26.492 1.00 25.60 ? 75 THR A C 1 ATOM 590 O O . THR A 1 75 ? 37.124 4.858 26.957 1.00 26.22 ? 75 THR A O 1 ATOM 591 C CB . THR A 1 75 ? 34.714 6.627 28.022 1.00 23.97 ? 75 THR A CB 1 ATOM 592 O OG1 . THR A 1 75 ? 33.496 5.877 27.965 1.00 21.64 ? 75 THR A OG1 1 ATOM 593 C CG2 . THR A 1 75 ? 34.388 8.079 28.374 1.00 23.63 ? 75 THR A CG2 1 ATOM 594 N N . LEU A 1 76 ? 35.275 4.258 25.826 1.00 23.96 ? 76 LEU A N 1 ATOM 595 C CA . LEU A 1 76 ? 35.714 2.880 25.608 1.00 21.23 ? 76 LEU A CA 1 ATOM 596 C C . LEU A 1 76 ? 36.415 2.637 24.270 1.00 20.61 ? 76 LEU A C 1 ATOM 597 O O . LEU A 1 76 ? 36.886 1.531 24.008 1.00 22.38 ? 76 LEU A O 1 ATOM 598 C CB . LEU A 1 76 ? 34.533 1.921 25.761 1.00 22.16 ? 76 LEU A CB 1 ATOM 599 C CG . LEU A 1 76 ? 34.257 1.322 27.141 1.00 25.44 ? 76 LEU A CG 1 ATOM 600 C CD1 . LEU A 1 76 ? 34.700 2.254 28.253 1.00 21.65 ? 76 LEU A CD1 1 ATOM 601 C CD2 . LEU A 1 76 ? 32.779 0.986 27.255 1.00 19.89 ? 76 LEU A CD2 1 ATOM 602 N N . GLY A 1 77 ? 36.477 3.663 23.426 1.00 19.21 ? 77 GLY A N 1 ATOM 603 C CA . GLY A 1 77 ? 37.136 3.529 22.136 1.00 19.25 ? 77 GLY A CA 1 ATOM 604 C C . GLY A 1 77 ? 36.347 2.799 21.057 1.00 21.37 ? 77 GLY A C 1 ATOM 605 O O . GLY A 1 77 ? 36.911 2.017 20.290 1.00 22.06 ? 77 GLY A O 1 ATOM 606 N N . LEU A 1 78 ? 35.043 3.050 21.004 1.00 21.08 ? 78 LEU A N 1 ATOM 607 C CA . LEU A 1 78 ? 34.157 2.437 20.017 1.00 20.30 ? 78 LEU A CA 1 ATOM 608 C C . LEU A 1 78 ? 33.549 3.548 19.152 1.00 21.27 ? 78 LEU A C 1 ATOM 609 O O . LEU A 1 78 ? 32.349 3.542 18.875 1.00 20.83 ? 78 LEU A O 1 ATOM 610 C CB . LEU A 1 78 ? 33.033 1.677 20.731 1.00 19.64 ? 78 LEU A CB 1 ATOM 611 C CG . LEU A 1 78 ? 33.385 0.763 21.909 1.00 20.25 ? 78 LEU A CG 1 ATOM 612 C CD1 . LEU A 1 78 ? 32.114 0.167 22.472 1.00 22.57 ? 78 LEU A CD1 1 ATOM 613 C CD2 . LEU A 1 78 ? 34.336 -0.335 21.467 1.00 16.31 ? 78 LEU A CD2 1 ATOM 614 N N . TYR A 1 79 ? 34.393 4.469 18.693 1.00 21.06 ? 79 TYR A N 1 ATOM 615 C CA . TYR A 1 79 ? 33.939 5.612 17.899 1.00 22.29 ? 79 TYR A CA 1 ATOM 616 C C . TYR A 1 79 ? 34.769 5.849 16.627 1.00 20.37 ? 79 TYR A C 1 ATOM 617 O O . TYR A 1 79 ? 34.968 6.994 16.214 1.00 27.12 ? 79 TYR A O 1 ATOM 618 C CB . TYR A 1 79 ? 33.999 6.862 18.789 1.00 20.87 ? 79 TYR A CB 1 ATOM 619 C CG . TYR A 1 79 ? 32.852 7.830 18.629 1.00 18.26 ? 79 TYR A CG 1 ATOM 620 C CD1 . TYR A 1 79 ? 32.340 8.145 17.368 1.00 16.41 ? 79 TYR A CD1 1 ATOM 621 C CD2 . TYR A 1 79 ? 32.280 8.442 19.746 1.00 17.98 ? 79 TYR A CD2 1 ATOM 622 C CE1 . TYR A 1 79 ? 31.290 9.044 17.220 1.00 11.88 ? 79 TYR A CE1 1 ATOM 623 C CE2 . TYR A 1 79 ? 31.227 9.342 19.613 1.00 14.70 ? 79 TYR A CE2 1 ATOM 624 C CZ . TYR A 1 79 ? 30.737 9.636 18.348 1.00 20.42 ? 79 TYR A CZ 1 ATOM 625 O OH . TYR A 1 79 ? 29.678 10.501 18.215 1.00 19.40 ? 79 TYR A OH 1 ATOM 626 N N . GLY A 1 80 ? 35.227 4.770 15.998 1.00 18.70 ? 80 GLY A N 1 ATOM 627 C CA . GLY A 1 80 ? 36.034 4.887 14.792 1.00 16.59 ? 80 GLY A CA 1 ATOM 628 C C . GLY A 1 80 ? 37.505 5.119 15.093 1.00 19.71 ? 80 GLY A C 1 ATOM 629 O O . GLY A 1 80 ? 37.863 5.471 16.216 1.00 22.37 ? 80 GLY A O 1 ATOM 630 N N . LYS A 1 81 ? 38.362 4.948 14.091 1.00 25.55 ? 81 LYS A N 1 ATOM 631 C CA . LYS A 1 81 ? 39.796 5.138 14.284 1.00 26.60 ? 81 LYS A CA 1 ATOM 632 C C . LYS A 1 81 ? 40.212 6.598 14.102 1.00 29.26 ? 81 LYS A C 1 ATOM 633 O O . LYS A 1 81 ? 41.284 7.003 14.552 1.00 31.28 ? 81 LYS A O 1 ATOM 634 C CB . LYS A 1 81 ? 40.596 4.233 13.342 1.00 31.07 ? 81 LYS A CB 1 ATOM 635 C CG . LYS A 1 81 ? 40.530 4.637 11.884 1.00 41.33 ? 81 LYS A CG 1 ATOM 636 C CD . LYS A 1 81 ? 41.422 3.755 11.026 1.00 48.82 ? 81 LYS A CD 1 ATOM 637 C CE . LYS A 1 81 ? 41.602 4.351 9.636 1.00 49.83 ? 81 LYS A CE 1 ATOM 638 N NZ . LYS A 1 81 ? 40.302 4.551 8.932 1.00 56.81 ? 81 LYS A NZ 1 ATOM 639 N N . ASP A 1 82 ? 39.365 7.385 13.440 1.00 28.30 ? 82 ASP A N 1 ATOM 640 C CA . ASP A 1 82 ? 39.653 8.801 13.217 1.00 25.32 ? 82 ASP A CA 1 ATOM 641 C C . ASP A 1 82 ? 38.375 9.620 13.058 1.00 22.03 ? 82 ASP A C 1 ATOM 642 O O . ASP A 1 82 ? 37.273 9.077 13.162 1.00 28.02 ? 82 ASP A O 1 ATOM 643 C CB . ASP A 1 82 ? 40.592 8.991 12.014 1.00 24.51 ? 82 ASP A CB 1 ATOM 644 C CG . ASP A 1 82 ? 40.061 8.359 10.727 1.00 32.40 ? 82 ASP A CG 1 ATOM 645 O OD1 . ASP A 1 82 ? 38.830 8.305 10.521 1.00 34.79 ? 82 ASP A OD1 1 ATOM 646 O OD2 . ASP A 1 82 ? 40.893 7.928 9.899 1.00 39.16 ? 82 ASP A OD2 1 ATOM 647 N N . GLN A 1 83 ? 38.520 10.916 12.787 1.00 21.04 ? 83 GLN A N 1 ATOM 648 C CA . GLN A 1 83 ? 37.363 11.800 12.634 1.00 23.73 ? 83 GLN A CA 1 ATOM 649 C C . GLN A 1 83 ? 36.439 11.419 11.493 1.00 21.99 ? 83 GLN A C 1 ATOM 650 O O . GLN A 1 83 ? 35.218 11.519 11.621 1.00 21.68 ? 83 GLN A O 1 ATOM 651 C CB . GLN A 1 83 ? 37.800 13.254 12.480 1.00 27.64 ? 83 GLN A CB 1 ATOM 652 C CG . GLN A 1 83 ? 38.391 13.863 13.739 1.00 32.38 ? 83 GLN A CG 1 ATOM 653 C CD . GLN A 1 83 ? 38.797 15.314 13.549 1.00 39.94 ? 83 GLN A CD 1 ATOM 654 O OE1 . GLN A 1 83 ? 38.739 16.112 14.488 1.00 41.54 ? 83 GLN A OE1 1 ATOM 655 N NE2 . GLN A 1 83 ? 39.201 15.667 12.330 1.00 41.00 ? 83 GLN A NE2 1 ATOM 656 N N . GLN A 1 84 ? 37.017 10.983 10.379 1.00 23.16 ? 84 GLN A N 1 ATOM 657 C CA . GLN A 1 84 ? 36.213 10.583 9.231 1.00 27.70 ? 84 GLN A CA 1 ATOM 658 C C . GLN A 1 84 ? 35.293 9.425 9.614 1.00 24.54 ? 84 GLN A C 1 ATOM 659 O O . GLN A 1 84 ? 34.089 9.466 9.338 1.00 20.97 ? 84 GLN A O 1 ATOM 660 C CB . GLN A 1 84 ? 37.102 10.188 8.048 1.00 36.18 ? 84 GLN A CB 1 ATOM 661 C CG . GLN A 1 84 ? 36.307 9.704 6.836 1.00 50.12 ? 84 GLN A CG 1 ATOM 662 C CD . GLN A 1 84 ? 37.162 9.503 5.597 1.00 58.08 ? 84 GLN A CD 1 ATOM 663 O OE1 . GLN A 1 84 ? 37.992 10.348 5.256 1.00 57.17 ? 84 GLN A OE1 1 ATOM 664 N NE2 . GLN A 1 84 ? 36.938 8.392 4.895 1.00 62.96 ? 84 GLN A NE2 1 ATOM 665 N N . GLU A 1 85 ? 35.860 8.413 10.273 1.00 21.12 ? 85 GLU A N 1 ATOM 666 C CA . GLU A 1 85 ? 35.083 7.255 10.709 1.00 20.98 ? 85 GLU A CA 1 ATOM 667 C C . GLU A 1 85 ? 34.068 7.668 11.764 1.00 18.69 ? 85 GLU A C 1 ATOM 668 O O . GLU A 1 85 ? 32.944 7.169 11.765 1.00 23.76 ? 85 GLU A O 1 ATOM 669 C CB . GLU A 1 85 ? 35.984 6.148 11.258 1.00 19.30 ? 85 GLU A CB 1 ATOM 670 C CG . GLU A 1 85 ? 36.903 5.533 10.221 1.00 27.09 ? 85 GLU A CG 1 ATOM 671 C CD . GLU A 1 85 ? 37.334 4.115 10.564 1.00 31.89 ? 85 GLU A CD 1 ATOM 672 O OE1 . GLU A 1 85 ? 37.249 3.715 11.744 1.00 24.91 ? 85 GLU A OE1 1 ATOM 673 O OE2 . GLU A 1 85 ? 37.768 3.393 9.641 1.00 35.97 ? 85 GLU A OE2 1 ATOM 674 N N . ALA A 1 86 ? 34.461 8.591 12.644 1.00 15.73 ? 86 ALA A N 1 ATOM 675 C CA . ALA A 1 86 ? 33.578 9.090 13.699 1.00 12.91 ? 86 ALA A CA 1 ATOM 676 C C . ALA A 1 86 ? 32.331 9.705 13.078 1.00 13.59 ? 86 ALA A C 1 ATOM 677 O O . ALA A 1 86 ? 31.220 9.502 13.569 1.00 18.91 ? 86 ALA A O 1 ATOM 678 C CB . ALA A 1 86 ? 34.301 10.118 14.548 1.00 8.01 ? 86 ALA A CB 1 ATOM 679 N N . ALA A 1 87 ? 32.518 10.435 11.981 1.00 14.25 ? 87 ALA A N 1 ATOM 680 C CA . ALA A 1 87 ? 31.406 11.066 11.279 1.00 16.97 ? 87 ALA A CA 1 ATOM 681 C C . ALA A 1 87 ? 30.487 10.006 10.668 1.00 17.71 ? 87 ALA A C 1 ATOM 682 O O . ALA A 1 87 ? 29.262 10.136 10.708 1.00 19.60 ? 87 ALA A O 1 ATOM 683 C CB . ALA A 1 87 ? 31.933 12.003 10.194 1.00 19.44 ? 87 ALA A CB 1 ATOM 684 N N . LEU A 1 88 ? 31.083 8.946 10.124 1.00 19.06 ? 88 LEU A N 1 ATOM 685 C CA . LEU A 1 88 ? 30.315 7.861 9.512 1.00 18.23 ? 88 LEU A CA 1 ATOM 686 C C . LEU A 1 88 ? 29.525 7.075 10.557 1.00 15.42 ? 88 LEU A C 1 ATOM 687 O O . LEU A 1 88 ? 28.387 6.674 10.309 1.00 16.23 ? 88 LEU A O 1 ATOM 688 C CB . LEU A 1 88 ? 31.240 6.935 8.717 1.00 18.52 ? 88 LEU A CB 1 ATOM 689 C CG . LEU A 1 88 ? 32.029 7.627 7.600 1.00 22.88 ? 88 LEU A CG 1 ATOM 690 C CD1 . LEU A 1 88 ? 32.885 6.613 6.851 1.00 22.76 ? 88 LEU A CD1 1 ATOM 691 C CD2 . LEU A 1 88 ? 31.075 8.333 6.647 1.00 19.08 ? 88 LEU A CD2 1 ATOM 692 N N . VAL A 1 89 ? 30.125 6.884 11.732 1.00 14.71 ? 89 VAL A N 1 ATOM 693 C CA . VAL A 1 89 ? 29.477 6.172 12.837 1.00 14.76 ? 89 VAL A CA 1 ATOM 694 C C . VAL A 1 89 ? 28.221 6.938 13.260 1.00 12.99 ? 89 VAL A C 1 ATOM 695 O O . VAL A 1 89 ? 27.168 6.338 13.491 1.00 13.64 ? 89 VAL A O 1 ATOM 696 C CB . VAL A 1 89 ? 30.437 6.024 14.048 1.00 19.85 ? 89 VAL A CB 1 ATOM 697 C CG1 . VAL A 1 89 ? 29.708 5.422 15.235 1.00 18.51 ? 89 VAL A CG1 1 ATOM 698 C CG2 . VAL A 1 89 ? 31.630 5.154 13.674 1.00 14.51 ? 89 VAL A CG2 1 ATOM 699 N N . ASP A 1 90 ? 28.345 8.264 13.344 1.00 14.29 ? 90 ASP A N 1 ATOM 700 C CA . ASP A 1 90 ? 27.232 9.141 13.709 1.00 11.39 ? 90 ASP A CA 1 ATOM 701 C C . ASP A 1 90 ? 26.126 9.050 12.666 1.00 11.60 ? 90 ASP A C 1 ATOM 702 O O . ASP A 1 90 ? 24.947 8.987 13.006 1.00 11.04 ? 90 ASP A O 1 ATOM 703 C CB . ASP A 1 90 ? 27.698 10.603 13.812 1.00 11.00 ? 90 ASP A CB 1 ATOM 704 C CG . ASP A 1 90 ? 28.359 10.920 15.140 1.00 16.99 ? 90 ASP A CG 1 ATOM 705 O OD1 . ASP A 1 90 ? 28.036 10.253 16.145 1.00 21.77 ? 90 ASP A OD1 1 ATOM 706 O OD2 . ASP A 1 90 ? 29.183 11.856 15.204 1.00 16.30 ? 90 ASP A OD2 1 ATOM 707 N N . MET A 1 91 ? 26.515 9.064 11.393 1.00 12.69 ? 91 MET A N 1 ATOM 708 C CA . MET A 1 91 ? 25.559 8.986 10.294 1.00 11.58 ? 91 MET A CA 1 ATOM 709 C C . MET A 1 91 ? 24.767 7.687 10.358 1.00 11.44 ? 91 MET A C 1 ATOM 710 O O . MET A 1 91 ? 23.562 7.672 10.086 1.00 11.56 ? 91 MET A O 1 ATOM 711 C CB . MET A 1 91 ? 26.285 9.112 8.953 1.00 13.28 ? 91 MET A CB 1 ATOM 712 C CG . MET A 1 91 ? 25.365 9.077 7.742 1.00 19.12 ? 91 MET A CG 1 ATOM 713 S SD . MET A 1 91 ? 26.261 9.399 6.211 1.00 20.72 ? 91 MET A SD 1 ATOM 714 C CE . MET A 1 91 ? 27.389 7.993 6.160 1.00 19.81 ? 91 MET A CE 1 ATOM 715 N N . VAL A 1 92 ? 25.448 6.598 10.717 1.00 13.48 ? 92 VAL A N 1 ATOM 716 C CA . VAL A 1 92 ? 24.790 5.297 10.848 1.00 16.12 ? 92 VAL A CA 1 ATOM 717 C C . VAL A 1 92 ? 23.827 5.340 12.037 1.00 13.38 ? 92 VAL A C 1 ATOM 718 O O . VAL A 1 92 ? 22.655 4.994 11.902 1.00 15.39 ? 92 VAL A O 1 ATOM 719 C CB . VAL A 1 92 ? 25.821 4.145 11.051 1.00 16.05 ? 92 VAL A CB 1 ATOM 720 C CG1 . VAL A 1 92 ? 25.096 2.839 11.354 1.00 12.02 ? 92 VAL A CG1 1 ATOM 721 C CG2 . VAL A 1 92 ? 26.686 3.980 9.802 1.00 10.91 ? 92 VAL A CG2 1 ATOM 722 N N . ASN A 1 93 ? 24.307 5.821 13.183 1.00 12.98 ? 93 ASN A N 1 ATOM 723 C CA . ASN A 1 93 ? 23.479 5.900 14.382 1.00 9.74 ? 93 ASN A CA 1 ATOM 724 C C . ASN A 1 93 ? 22.250 6.778 14.203 1.00 8.46 ? 93 ASN A C 1 ATOM 725 O O . ASN A 1 93 ? 21.165 6.419 14.666 1.00 17.18 ? 93 ASN A O 1 ATOM 726 C CB . ASN A 1 93 ? 24.288 6.373 15.595 1.00 13.20 ? 93 ASN A CB 1 ATOM 727 C CG . ASN A 1 93 ? 23.665 5.908 16.906 1.00 19.58 ? 93 ASN A CG 1 ATOM 728 O OD1 . ASN A 1 93 ? 23.627 4.712 17.178 1.00 17.40 ? 93 ASN A OD1 1 ATOM 729 N ND2 . ASN A 1 93 ? 23.154 6.841 17.703 1.00 12.48 ? 93 ASN A ND2 1 ATOM 730 N N . ASP A 1 94 ? 22.415 7.919 13.535 1.00 9.64 ? 94 ASP A N 1 ATOM 731 C CA . ASP A 1 94 ? 21.289 8.824 13.290 1.00 12.35 ? 94 ASP A CA 1 ATOM 732 C C . ASP A 1 94 ? 20.267 8.122 12.411 1.00 11.61 ? 94 ASP A C 1 ATOM 733 O O . ASP A 1 94 ? 19.061 8.323 12.564 1.00 17.27 ? 94 ASP A O 1 ATOM 734 C CB . ASP A 1 94 ? 21.763 10.119 12.621 1.00 16.96 ? 94 ASP A CB 1 ATOM 735 C CG . ASP A 1 94 ? 22.494 11.048 13.581 1.00 23.49 ? 94 ASP A CG 1 ATOM 736 O OD1 . ASP A 1 94 ? 22.683 10.691 14.766 1.00 19.71 ? 94 ASP A OD1 1 ATOM 737 O OD2 . ASP A 1 94 ? 22.859 12.161 13.148 1.00 23.12 ? 94 ASP A OD2 1 ATOM 738 N N . GLY A 1 95 ? 20.761 7.293 11.493 1.00 13.22 ? 95 GLY A N 1 ATOM 739 C CA . GLY A 1 95 ? 19.880 6.538 10.619 1.00 10.03 ? 95 GLY A CA 1 ATOM 740 C C . GLY A 1 95 ? 19.112 5.525 11.445 1.00 11.14 ? 95 GLY A C 1 ATOM 741 O O . GLY A 1 95 ? 17.902 5.384 11.295 1.00 7.80 ? 95 GLY A O 1 ATOM 742 N N . VAL A 1 96 ? 19.814 4.835 12.341 1.00 12.14 ? 96 VAL A N 1 ATOM 743 C CA . VAL A 1 96 ? 19.182 3.849 13.216 1.00 15.54 ? 96 VAL A CA 1 ATOM 744 C C . VAL A 1 96 ? 18.107 4.531 14.072 1.00 16.58 ? 96 VAL A C 1 ATOM 745 O O . VAL A 1 96 ? 16.984 4.041 14.176 1.00 17.30 ? 96 VAL A O 1 ATOM 746 C CB . VAL A 1 96 ? 20.220 3.177 14.144 1.00 14.32 ? 96 VAL A CB 1 ATOM 747 C CG1 . VAL A 1 96 ? 19.522 2.296 15.178 1.00 16.11 ? 96 VAL A CG1 1 ATOM 748 C CG2 . VAL A 1 96 ? 21.207 2.364 13.320 1.00 11.14 ? 96 VAL A CG2 1 ATOM 749 N N . GLU A 1 97 ? 18.453 5.686 14.638 1.00 18.63 ? 97 GLU A N 1 ATOM 750 C CA . GLU A 1 97 ? 17.539 6.455 15.481 1.00 16.85 ? 97 GLU A CA 1 ATOM 751 C C . GLU A 1 97 ? 16.254 6.851 14.748 1.00 18.25 ? 97 GLU A C 1 ATOM 752 O O . GLU A 1 97 ? 15.164 6.790 15.326 1.00 18.70 ? 97 GLU A O 1 ATOM 753 C CB . GLU A 1 97 ? 18.257 7.692 16.042 1.00 17.30 ? 97 GLU A CB 1 ATOM 754 C CG . GLU A 1 97 ? 17.372 8.657 16.838 1.00 23.07 ? 97 GLU A CG 1 ATOM 755 C CD . GLU A 1 97 ? 16.645 8.001 18.012 1.00 25.82 ? 97 GLU A CD 1 ATOM 756 O OE1 . GLU A 1 97 ? 17.222 7.119 18.680 1.00 22.62 ? 97 GLU A OE1 1 ATOM 757 O OE2 . GLU A 1 97 ? 15.485 8.377 18.267 1.00 25.38 ? 97 GLU A OE2 1 ATOM 758 N N . ASP A 1 98 ? 16.381 7.249 13.481 1.00 20.78 ? 98 ASP A N 1 ATOM 759 C CA . ASP A 1 98 ? 15.216 7.630 12.677 1.00 17.53 ? 98 ASP A CA 1 ATOM 760 C C . ASP A 1 98 ? 14.257 6.455 12.514 1.00 17.65 ? 98 ASP A C 1 ATOM 761 O O . ASP A 1 98 ? 13.046 6.599 12.700 1.00 15.70 ? 98 ASP A O 1 ATOM 762 C CB . ASP A 1 98 ? 15.640 8.139 11.293 1.00 23.36 ? 98 ASP A CB 1 ATOM 763 C CG . ASP A 1 98 ? 16.111 9.590 11.309 1.00 26.68 ? 98 ASP A CG 1 ATOM 764 O OD1 . ASP A 1 98 ? 15.894 10.294 12.320 1.00 29.04 ? 98 ASP A OD1 1 ATOM 765 O OD2 . ASP A 1 98 ? 16.676 10.041 10.291 1.00 25.14 ? 98 ASP A OD2 1 ATOM 766 N N . LEU A 1 99 ? 14.799 5.290 12.166 1.00 16.91 ? 99 LEU A N 1 ATOM 767 C CA . LEU A 1 99 ? 13.960 4.108 12.000 1.00 19.92 ? 99 LEU A CA 1 ATOM 768 C C . LEU A 1 99 ? 13.397 3.643 13.346 1.00 13.19 ? 99 LEU A C 1 ATOM 769 O O . LEU A 1 99 ? 12.263 3.173 13.420 1.00 18.49 ? 99 LEU A O 1 ATOM 770 C CB . LEU A 1 99 ? 14.729 2.982 11.302 1.00 18.14 ? 99 LEU A CB 1 ATOM 771 C CG . LEU A 1 99 ? 13.939 1.700 11.014 1.00 17.66 ? 99 LEU A CG 1 ATOM 772 C CD1 . LEU A 1 99 ? 12.600 2.021 10.370 1.00 13.77 ? 99 LEU A CD1 1 ATOM 773 C CD2 . LEU A 1 99 ? 14.759 0.792 10.119 1.00 16.06 ? 99 LEU A CD2 1 ATOM 774 N N . ARG A 1 100 ? 14.170 3.824 14.415 1.00 14.47 ? 100 ARG A N 1 ATOM 775 C CA . ARG A 1 100 ? 13.717 3.435 15.748 1.00 15.31 ? 100 ARG A CA 1 ATOM 776 C C . ARG A 1 100 ? 12.487 4.256 16.153 1.00 17.03 ? 100 ARG A C 1 ATOM 777 O O . ARG A 1 100 ? 11.551 3.710 16.735 1.00 19.64 ? 100 ARG A O 1 ATOM 778 C CB . ARG A 1 100 ? 14.836 3.593 16.786 1.00 10.73 ? 100 ARG A CB 1 ATOM 779 C CG . ARG A 1 100 ? 14.465 3.035 18.156 1.00 10.42 ? 100 ARG A CG 1 ATOM 780 C CD . ARG A 1 100 ? 15.599 3.165 19.162 1.00 11.98 ? 100 ARG A CD 1 ATOM 781 N NE . ARG A 1 100 ? 16.748 2.327 18.828 1.00 11.76 ? 100 ARG A NE 1 ATOM 782 C CZ . ARG A 1 100 ? 16.822 1.019 19.057 1.00 15.85 ? 100 ARG A CZ 1 ATOM 783 N NH1 . ARG A 1 100 ? 15.807 0.373 19.621 1.00 11.89 ? 100 ARG A NH1 1 ATOM 784 N NH2 . ARG A 1 100 ? 17.923 0.354 18.732 1.00 15.06 ? 100 ARG A NH2 1 ATOM 785 N N . CYS A 1 101 ? 12.479 5.550 15.820 1.00 14.20 ? 101 CYS A N 1 ATOM 786 C CA . CYS A 1 101 ? 11.343 6.417 16.136 1.00 17.83 ? 101 CYS A CA 1 ATOM 787 C C . CYS A 1 101 ? 10.089 5.953 15.421 1.00 19.55 ? 101 CYS A C 1 ATOM 788 O O . CYS A 1 101 ? 8.996 5.993 15.985 1.00 22.33 ? 101 CYS A O 1 ATOM 789 C CB . CYS A 1 101 ? 11.628 7.871 15.765 1.00 19.32 ? 101 CYS A CB 1 ATOM 790 S SG . CYS A 1 101 ? 12.723 8.699 16.921 1.00 32.81 ? 101 CYS A SG 1 ATOM 791 N N . LYS A 1 102 ? 10.247 5.518 14.175 1.00 19.38 ? 102 LYS A N 1 ATOM 792 C CA . LYS A 1 102 ? 9.113 5.028 13.400 1.00 20.61 ? 102 LYS A CA 1 ATOM 793 C C . LYS A 1 102 ? 8.593 3.749 14.042 1.00 18.02 ? 102 LYS A C 1 ATOM 794 O O . LYS A 1 102 ? 7.386 3.549 14.152 1.00 19.13 ? 102 LYS A O 1 ATOM 795 C CB . LYS A 1 102 ? 9.528 4.764 11.956 1.00 22.86 ? 102 LYS A CB 1 ATOM 796 C CG . LYS A 1 102 ? 9.926 6.019 11.212 1.00 30.03 ? 102 LYS A CG 1 ATOM 797 C CD . LYS A 1 102 ? 10.355 5.710 9.800 1.00 32.90 ? 102 LYS A CD 1 ATOM 798 C CE . LYS A 1 102 ? 10.687 6.985 9.057 1.00 35.78 ? 102 LYS A CE 1 ATOM 799 N NZ . LYS A 1 102 ? 11.177 6.693 7.686 1.00 40.87 ? 102 LYS A NZ 1 ATOM 800 N N . TYR A 1 103 ? 9.520 2.900 14.485 1.00 20.01 ? 103 TYR A N 1 ATOM 801 C CA . TYR A 1 103 ? 9.180 1.640 15.140 1.00 21.91 ? 103 TYR A CA 1 ATOM 802 C C . TYR A 1 103 ? 8.402 1.933 16.422 1.00 22.68 ? 103 TYR A C 1 ATOM 803 O O . TYR A 1 103 ? 7.340 1.360 16.665 1.00 21.81 ? 103 TYR A O 1 ATOM 804 C CB . TYR A 1 103 ? 10.458 0.853 15.466 1.00 23.90 ? 103 TYR A CB 1 ATOM 805 C CG . TYR A 1 103 ? 10.249 -0.354 16.367 1.00 26.18 ? 103 TYR A CG 1 ATOM 806 C CD1 . TYR A 1 103 ? 9.838 -1.583 15.845 1.00 25.52 ? 103 TYR A CD1 1 ATOM 807 C CD2 . TYR A 1 103 ? 10.462 -0.265 17.745 1.00 25.90 ? 103 TYR A CD2 1 ATOM 808 C CE1 . TYR A 1 103 ? 9.645 -2.694 16.681 1.00 27.92 ? 103 TYR A CE1 1 ATOM 809 C CE2 . TYR A 1 103 ? 10.273 -1.363 18.585 1.00 25.72 ? 103 TYR A CE2 1 ATOM 810 C CZ . TYR A 1 103 ? 9.865 -2.573 18.050 1.00 31.25 ? 103 TYR A CZ 1 ATOM 811 O OH . TYR A 1 103 ? 9.681 -3.656 18.882 1.00 22.76 ? 103 TYR A OH 1 ATOM 812 N N . ILE A 1 104 ? 8.935 2.846 17.228 1.00 23.14 ? 104 ILE A N 1 ATOM 813 C CA . ILE A 1 104 ? 8.312 3.237 18.486 1.00 24.08 ? 104 ILE A CA 1 ATOM 814 C C . ILE A 1 104 ? 6.922 3.823 18.249 1.00 24.55 ? 104 ILE A C 1 ATOM 815 O O . ILE A 1 104 ? 5.977 3.516 18.973 1.00 23.23 ? 104 ILE A O 1 ATOM 816 C CB . ILE A 1 104 ? 9.210 4.239 19.250 1.00 22.12 ? 104 ILE A CB 1 ATOM 817 C CG1 . ILE A 1 104 ? 10.470 3.521 19.736 1.00 18.44 ? 104 ILE A CG1 1 ATOM 818 C CG2 . ILE A 1 104 ? 8.458 4.863 20.423 1.00 18.42 ? 104 ILE A CG2 1 ATOM 819 C CD1 . ILE A 1 104 ? 11.541 4.448 20.257 1.00 17.78 ? 104 ILE A CD1 1 ATOM 820 N N . SER A 1 105 ? 6.796 4.638 17.208 1.00 28.06 ? 105 SER A N 1 ATOM 821 C CA . SER A 1 105 ? 5.517 5.246 16.876 1.00 27.79 ? 105 SER A CA 1 ATOM 822 C C . SER A 1 105 ? 4.501 4.156 16.555 1.00 30.25 ? 105 SER A C 1 ATOM 823 O O . SER A 1 105 ? 3.354 4.239 16.973 1.00 30.82 ? 105 SER A O 1 ATOM 824 C CB . SER A 1 105 ? 5.665 6.190 15.684 1.00 28.66 ? 105 SER A CB 1 ATOM 825 O OG . SER A 1 105 ? 4.436 6.833 15.401 1.00 34.23 ? 105 SER A OG 1 ATOM 826 N N . LEU A 1 106 ? 4.929 3.128 15.827 1.00 27.81 ? 106 LEU A N 1 ATOM 827 C CA . LEU A 1 106 ? 4.042 2.021 15.472 1.00 25.38 ? 106 LEU A CA 1 ATOM 828 C C . LEU A 1 106 ? 3.581 1.263 16.716 1.00 26.48 ? 106 LEU A C 1 ATOM 829 O O . LEU A 1 106 ? 2.384 1.084 16.937 1.00 25.64 ? 106 LEU A O 1 ATOM 830 C CB . LEU A 1 106 ? 4.752 1.049 14.524 1.00 23.69 ? 106 LEU A CB 1 ATOM 831 C CG . LEU A 1 106 ? 4.014 -0.266 14.255 1.00 24.87 ? 106 LEU A CG 1 ATOM 832 C CD1 . LEU A 1 106 ? 2.744 -0.010 13.457 1.00 22.06 ? 106 LEU A CD1 1 ATOM 833 C CD2 . LEU A 1 106 ? 4.920 -1.225 13.515 1.00 21.05 ? 106 LEU A CD2 1 ATOM 834 N N . ILE A 1 107 ? 4.549 0.831 17.521 1.00 25.21 ? 107 ILE A N 1 ATOM 835 C CA . ILE A 1 107 ? 4.295 0.075 18.745 1.00 25.72 ? 107 ILE A CA 1 ATOM 836 C C . ILE A 1 107 ? 3.351 0.758 19.738 1.00 29.40 ? 107 ILE A C 1 ATOM 837 O O . ILE A 1 107 ? 2.390 0.149 20.212 1.00 30.38 ? 107 ILE A O 1 ATOM 838 C CB . ILE A 1 107 ? 5.625 -0.253 19.465 1.00 24.29 ? 107 ILE A CB 1 ATOM 839 C CG1 . ILE A 1 107 ? 6.497 -1.148 18.582 1.00 22.58 ? 107 ILE A CG1 1 ATOM 840 C CG2 . ILE A 1 107 ? 5.364 -0.923 20.802 1.00 23.25 ? 107 ILE A CG2 1 ATOM 841 C CD1 . ILE A 1 107 ? 5.864 -2.479 18.228 1.00 25.00 ? 107 ILE A CD1 1 ATOM 842 N N . TYR A 1 108 ? 3.608 2.031 20.018 1.00 30.44 ? 108 TYR A N 1 ATOM 843 C CA . TYR A 1 108 ? 2.807 2.785 20.975 1.00 30.83 ? 108 TYR A CA 1 ATOM 844 C C . TYR A 1 108 ? 1.609 3.571 20.439 1.00 30.90 ? 108 TYR A C 1 ATOM 845 O O . TYR A 1 108 ? 0.682 3.856 21.189 1.00 34.64 ? 108 TYR A O 1 ATOM 846 C CB . TYR A 1 108 ? 3.722 3.715 21.775 1.00 28.66 ? 108 TYR A CB 1 ATOM 847 C CG . TYR A 1 108 ? 4.720 2.979 22.647 1.00 25.90 ? 108 TYR A CG 1 ATOM 848 C CD1 . TYR A 1 108 ? 4.365 2.515 23.915 1.00 26.12 ? 108 TYR A CD1 1 ATOM 849 C CD2 . TYR A 1 108 ? 6.025 2.749 22.208 1.00 24.41 ? 108 TYR A CD2 1 ATOM 850 C CE1 . TYR A 1 108 ? 5.295 1.837 24.731 1.00 26.04 ? 108 TYR A CE1 1 ATOM 851 C CE2 . TYR A 1 108 ? 6.956 2.076 23.008 1.00 24.30 ? 108 TYR A CE2 1 ATOM 852 C CZ . TYR A 1 108 ? 6.587 1.623 24.267 1.00 26.98 ? 108 TYR A CZ 1 ATOM 853 O OH . TYR A 1 108 ? 7.520 0.967 25.041 1.00 21.61 ? 108 TYR A OH 1 ATOM 854 N N . THR A 1 109 ? 1.610 3.901 19.151 1.00 38.71 ? 109 THR A N 1 ATOM 855 C CA . THR A 1 109 ? 0.519 4.686 18.568 1.00 37.68 ? 109 THR A CA 1 ATOM 856 C C . THR A 1 109 ? -0.558 3.908 17.809 1.00 40.73 ? 109 THR A C 1 ATOM 857 O O . THR A 1 109 ? -1.747 4.110 18.057 1.00 45.84 ? 109 THR A O 1 ATOM 858 C CB . THR A 1 109 ? 1.076 5.835 17.695 1.00 38.41 ? 109 THR A CB 1 ATOM 859 O OG1 . THR A 1 109 ? 1.792 6.750 18.533 1.00 42.97 ? 109 THR A OG1 1 ATOM 860 C CG2 . THR A 1 109 ? -0.035 6.575 16.966 1.00 42.51 ? 109 THR A CG2 1 ATOM 861 N N . ASN A 1 110 ? -0.163 3.025 16.896 1.00 37.79 ? 110 ASN A N 1 ATOM 862 C CA . ASN A 1 110 ? -1.148 2.257 16.138 1.00 38.19 ? 110 ASN A CA 1 ATOM 863 C C . ASN A 1 110 ? -0.610 0.938 15.594 1.00 34.78 ? 110 ASN A C 1 ATOM 864 O O . ASN A 1 110 ? -0.471 0.748 14.385 1.00 33.68 ? 110 ASN A O 1 ATOM 865 C CB . ASN A 1 110 ? -1.760 3.113 15.016 1.00 40.98 ? 110 ASN A CB 1 ATOM 866 C CG . ASN A 1 110 ? -0.760 3.483 13.932 1.00 47.50 ? 110 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 110 ? -1.130 3.620 12.768 1.00 47.36 ? 110 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 110 ? 0.509 3.639 14.305 1.00 51.99 ? 110 ASN A ND2 1 ATOM 869 N N . TYR A 1 111 ? -0.326 0.020 16.510 1.00 34.51 ? 111 TYR A N 1 ATOM 870 C CA . TYR A 1 111 ? 0.192 -1.292 16.159 1.00 34.67 ? 111 TYR A CA 1 ATOM 871 C C . TYR A 1 111 ? -0.764 -2.088 15.271 1.00 35.97 ? 111 TYR A C 1 ATOM 872 O O . TYR A 1 111 ? -0.399 -2.504 14.174 1.00 36.36 ? 111 TYR A O 1 ATOM 873 C CB . TYR A 1 111 ? 0.503 -2.084 17.431 1.00 33.29 ? 111 TYR A CB 1 ATOM 874 C CG . TYR A 1 111 ? 1.084 -3.453 17.167 1.00 36.30 ? 111 TYR A CG 1 ATOM 875 C CD1 . TYR A 1 111 ? 2.460 -3.631 17.026 1.00 35.63 ? 111 TYR A CD1 1 ATOM 876 C CD2 . TYR A 1 111 ? 0.257 -4.569 17.042 1.00 35.82 ? 111 TYR A CD2 1 ATOM 877 C CE1 . TYR A 1 111 ? 2.999 -4.888 16.764 1.00 38.80 ? 111 TYR A CE1 1 ATOM 878 C CE2 . TYR A 1 111 ? 0.784 -5.827 16.779 1.00 42.59 ? 111 TYR A CE2 1 ATOM 879 C CZ . TYR A 1 111 ? 2.156 -5.980 16.640 1.00 41.19 ? 111 TYR A CZ 1 ATOM 880 O OH . TYR A 1 111 ? 2.677 -7.224 16.363 1.00 47.64 ? 111 TYR A OH 1 ATOM 881 N N . GLU A 1 112 ? -1.989 -2.281 15.752 1.00 39.49 ? 112 GLU A N 1 ATOM 882 C CA . GLU A 1 112 ? -3.007 -3.045 15.032 1.00 42.50 ? 112 GLU A CA 1 ATOM 883 C C . GLU A 1 112 ? -3.254 -2.534 13.627 1.00 41.35 ? 112 GLU A C 1 ATOM 884 O O . GLU A 1 112 ? -3.144 -3.283 12.656 1.00 40.61 ? 112 GLU A O 1 ATOM 885 C CB . GLU A 1 112 ? -4.331 -3.045 15.803 1.00 45.99 ? 112 GLU A CB 1 ATOM 886 C CG . GLU A 1 112 ? -4.324 -3.861 17.094 1.00 54.63 ? 112 GLU A CG 1 ATOM 887 C CD . GLU A 1 112 ? -3.417 -3.281 18.172 1.00 59.58 ? 112 GLU A CD 1 ATOM 888 O OE1 . GLU A 1 112 ? -3.449 -2.047 18.386 1.00 58.39 ? 112 GLU A OE1 1 ATOM 889 O OE2 . GLU A 1 112 ? -2.683 -4.065 18.813 1.00 60.37 ? 112 GLU A OE2 1 ATOM 890 N N . ALA A 1 113 ? -3.564 -1.247 13.528 1.00 41.54 ? 113 ALA A N 1 ATOM 891 C CA . ALA A 1 113 ? -3.849 -0.616 12.250 1.00 41.20 ? 113 ALA A CA 1 ATOM 892 C C . ALA A 1 113 ? -2.657 -0.486 11.305 1.00 42.16 ? 113 ALA A C 1 ATOM 893 O O . ALA A 1 113 ? -2.724 -0.928 10.161 1.00 48.91 ? 113 ALA A O 1 ATOM 894 C CB . ALA A 1 113 ? -4.485 0.746 12.478 1.00 37.49 ? 113 ALA A CB 1 ATOM 895 N N . GLY A 1 114 ? -1.558 0.080 11.794 1.00 41.37 ? 114 GLY A N 1 ATOM 896 C CA . GLY A 1 114 ? -0.394 0.294 10.949 1.00 37.31 ? 114 GLY A CA 1 ATOM 897 C C . GLY A 1 114 ? 0.639 -0.795 10.719 1.00 37.83 ? 114 GLY A C 1 ATOM 898 O O . GLY A 1 114 ? 1.560 -0.588 9.924 1.00 37.80 ? 114 GLY A O 1 ATOM 899 N N . LYS A 1 115 ? 0.492 -1.949 11.366 1.00 35.61 ? 115 LYS A N 1 ATOM 900 C CA . LYS A 1 115 ? 1.468 -3.033 11.221 1.00 36.68 ? 115 LYS A CA 1 ATOM 901 C C . LYS A 1 115 ? 1.736 -3.496 9.788 1.00 34.47 ? 115 LYS A C 1 ATOM 902 O O . LYS A 1 115 ? 2.882 -3.750 9.422 1.00 32.43 ? 115 LYS A O 1 ATOM 903 C CB . LYS A 1 115 ? 1.077 -4.233 12.091 1.00 36.74 ? 115 LYS A CB 1 ATOM 904 C CG . LYS A 1 115 ? 2.133 -5.332 12.151 1.00 35.81 ? 115 LYS A CG 1 ATOM 905 C CD . LYS A 1 115 ? 1.627 -6.547 12.921 1.00 43.03 ? 115 LYS A CD 1 ATOM 906 C CE . LYS A 1 115 ? 2.602 -7.713 12.839 1.00 41.39 ? 115 LYS A CE 1 ATOM 907 N NZ . LYS A 1 115 ? 3.915 -7.402 13.469 1.00 51.56 ? 115 LYS A NZ 1 ATOM 908 N N . ASP A 1 116 ? 0.689 -3.584 8.975 1.00 36.82 ? 116 ASP A N 1 ATOM 909 C CA . ASP A 1 116 ? 0.837 -4.035 7.594 1.00 40.04 ? 116 ASP A CA 1 ATOM 910 C C . ASP A 1 116 ? 1.599 -3.073 6.686 1.00 38.48 ? 116 ASP A C 1 ATOM 911 O O . ASP A 1 116 ? 2.517 -3.485 5.975 1.00 34.17 ? 116 ASP A O 1 ATOM 912 C CB . ASP A 1 116 ? -0.528 -4.380 6.997 1.00 46.19 ? 116 ASP A CB 1 ATOM 913 C CG . ASP A 1 116 ? -1.194 -5.549 7.707 1.00 52.56 ? 116 ASP A CG 1 ATOM 914 O OD1 . ASP A 1 116 ? -0.476 -6.491 8.114 1.00 49.30 ? 116 ASP A OD1 1 ATOM 915 O OD2 . ASP A 1 116 ? -2.436 -5.529 7.847 1.00 54.99 ? 116 ASP A OD2 1 ATOM 916 N N . ASP A 1 117 ? 1.230 -1.796 6.721 1.00 36.15 ? 117 ASP A N 1 ATOM 917 C CA . ASP A 1 117 ? 1.897 -0.788 5.903 1.00 35.75 ? 117 ASP A CA 1 ATOM 918 C C . ASP A 1 117 ? 3.364 -0.656 6.285 1.00 35.68 ? 117 ASP A C 1 ATOM 919 O O . ASP A 1 117 ? 4.231 -0.529 5.417 1.00 36.69 ? 117 ASP A O 1 ATOM 920 C CB . ASP A 1 117 ? 1.202 0.567 6.045 1.00 39.41 ? 117 ASP A CB 1 ATOM 921 C CG . ASP A 1 117 ? -0.170 0.596 5.394 1.00 46.88 ? 117 ASP A CG 1 ATOM 922 O OD1 . ASP A 1 117 ? -0.525 -0.364 4.671 1.00 47.91 ? 117 ASP A OD1 1 ATOM 923 O OD2 . ASP A 1 117 ? -0.900 1.586 5.612 1.00 46.96 ? 117 ASP A OD2 1 ATOM 924 N N . TYR A 1 118 ? 3.631 -0.700 7.589 1.00 31.28 ? 118 TYR A N 1 ATOM 925 C CA . TYR A 1 118 ? 4.987 -0.593 8.117 1.00 30.67 ? 118 TYR A CA 1 ATOM 926 C C . TYR A 1 118 ? 5.884 -1.718 7.598 1.00 29.93 ? 118 TYR A C 1 ATOM 927 O O . TYR A 1 118 ? 7.026 -1.475 7.198 1.00 28.34 ? 118 TYR A O 1 ATOM 928 C CB . TYR A 1 118 ? 4.959 -0.608 9.653 1.00 27.14 ? 118 TYR A CB 1 ATOM 929 C CG . TYR A 1 118 ? 6.302 -0.352 10.304 1.00 26.38 ? 118 TYR A CG 1 ATOM 930 C CD1 . TYR A 1 118 ? 7.217 -1.384 10.486 1.00 19.86 ? 118 TYR A CD1 1 ATOM 931 C CD2 . TYR A 1 118 ? 6.659 0.928 10.732 1.00 26.08 ? 118 TYR A CD2 1 ATOM 932 C CE1 . TYR A 1 118 ? 8.453 -1.151 11.075 1.00 29.45 ? 118 TYR A CE1 1 ATOM 933 C CE2 . TYR A 1 118 ? 7.891 1.172 11.324 1.00 24.22 ? 118 TYR A CE2 1 ATOM 934 C CZ . TYR A 1 118 ? 8.785 0.128 11.492 1.00 25.80 ? 118 TYR A CZ 1 ATOM 935 O OH . TYR A 1 118 ? 10.010 0.352 12.079 1.00 24.95 ? 118 TYR A OH 1 ATOM 936 N N . VAL A 1 119 ? 5.376 -2.948 7.625 1.00 29.06 ? 119 VAL A N 1 ATOM 937 C CA . VAL A 1 119 ? 6.144 -4.098 7.151 1.00 33.03 ? 119 VAL A CA 1 ATOM 938 C C . VAL A 1 119 ? 6.403 -4.022 5.637 1.00 34.40 ? 119 VAL A C 1 ATOM 939 O O . VAL A 1 119 ? 7.460 -4.445 5.164 1.00 34.05 ? 119 VAL A O 1 ATOM 940 C CB . VAL A 1 119 ? 5.451 -5.433 7.529 1.00 30.33 ? 119 VAL A CB 1 ATOM 941 C CG1 . VAL A 1 119 ? 6.251 -6.620 7.013 1.00 29.73 ? 119 VAL A CG1 1 ATOM 942 C CG2 . VAL A 1 119 ? 5.314 -5.532 9.037 1.00 31.80 ? 119 VAL A CG2 1 ATOM 943 N N . LYS A 1 120 ? 5.452 -3.460 4.890 1.00 35.61 ? 120 LYS A N 1 ATOM 944 C CA . LYS A 1 120 ? 5.590 -3.309 3.439 1.00 38.35 ? 120 LYS A CA 1 ATOM 945 C C . LYS A 1 120 ? 6.695 -2.307 3.108 1.00 35.33 ? 120 LYS A C 1 ATOM 946 O O . LYS A 1 120 ? 7.451 -2.494 2.155 1.00 32.78 ? 120 LYS A O 1 ATOM 947 C CB . LYS A 1 120 ? 4.279 -2.819 2.816 1.00 42.82 ? 120 LYS A CB 1 ATOM 948 C CG . LYS A 1 120 ? 3.118 -3.784 2.943 1.00 52.09 ? 120 LYS A CG 1 ATOM 949 C CD . LYS A 1 120 ? 1.806 -3.093 2.601 1.00 58.43 ? 120 LYS A CD 1 ATOM 950 C CE . LYS A 1 120 ? 0.608 -3.969 2.947 1.00 62.88 ? 120 LYS A CE 1 ATOM 951 N NZ . LYS A 1 120 ? -0.678 -3.221 2.833 1.00 66.35 ? 120 LYS A NZ 1 ATOM 952 N N . ALA A 1 121 ? 6.782 -1.247 3.910 1.00 33.79 ? 121 ALA A N 1 ATOM 953 C CA . ALA A 1 121 ? 7.782 -0.198 3.716 1.00 30.02 ? 121 ALA A CA 1 ATOM 954 C C . ALA A 1 121 ? 9.154 -0.551 4.280 1.00 25.90 ? 121 ALA A C 1 ATOM 955 O O . ALA A 1 121 ? 10.148 0.101 3.956 1.00 31.21 ? 121 ALA A O 1 ATOM 956 C CB . ALA A 1 121 ? 7.291 1.108 4.326 1.00 28.93 ? 121 ALA A CB 1 ATOM 957 N N . LEU A 1 122 ? 9.210 -1.591 5.107 1.00 23.28 ? 122 LEU A N 1 ATOM 958 C CA . LEU A 1 122 ? 10.460 -2.020 5.727 1.00 22.18 ? 122 LEU A CA 1 ATOM 959 C C . LEU A 1 122 ? 11.676 -2.186 4.810 1.00 22.91 ? 122 LEU A C 1 ATOM 960 O O . LEU A 1 122 ? 12.755 -1.693 5.130 1.00 25.90 ? 122 LEU A O 1 ATOM 961 C CB . LEU A 1 122 ? 10.252 -3.306 6.526 1.00 23.32 ? 122 LEU A CB 1 ATOM 962 C CG . LEU A 1 122 ? 10.454 -3.225 8.038 1.00 27.19 ? 122 LEU A CG 1 ATOM 963 C CD1 . LEU A 1 122 ? 10.569 -4.640 8.584 1.00 23.58 ? 122 LEU A CD1 1 ATOM 964 C CD2 . LEU A 1 122 ? 11.711 -2.429 8.373 1.00 16.96 ? 122 LEU A CD2 1 ATOM 965 N N . PRO A 1 123 ? 11.527 -2.896 3.672 1.00 22.26 ? 123 PRO A N 1 ATOM 966 C CA . PRO A 1 123 ? 12.660 -3.094 2.756 1.00 18.74 ? 123 PRO A CA 1 ATOM 967 C C . PRO A 1 123 ? 13.358 -1.797 2.365 1.00 16.63 ? 123 PRO A C 1 ATOM 968 O O . PRO A 1 123 ? 14.588 -1.730 2.334 1.00 17.65 ? 123 PRO A O 1 ATOM 969 C CB . PRO A 1 123 ? 12.003 -3.767 1.553 1.00 19.28 ? 123 PRO A CB 1 ATOM 970 C CG . PRO A 1 123 ? 10.920 -4.574 2.181 1.00 19.49 ? 123 PRO A CG 1 ATOM 971 C CD . PRO A 1 123 ? 10.332 -3.600 3.176 1.00 21.84 ? 123 PRO A CD 1 ATOM 972 N N . GLY A 1 124 ? 12.568 -0.762 2.095 1.00 22.67 ? 124 GLY A N 1 ATOM 973 C CA . GLY A 1 124 ? 13.130 0.523 1.720 1.00 19.75 ? 124 GLY A CA 1 ATOM 974 C C . GLY A 1 124 ? 13.902 1.143 2.865 1.00 20.52 ? 124 GLY A C 1 ATOM 975 O O . GLY A 1 124 ? 14.898 1.830 2.645 1.00 22.10 ? 124 GLY A O 1 ATOM 976 N N . GLN A 1 125 ? 13.438 0.890 4.087 1.00 20.90 ? 125 GLN A N 1 ATOM 977 C CA . GLN A 1 125 ? 14.077 1.403 5.297 1.00 22.94 ? 125 GLN A CA 1 ATOM 978 C C . GLN A 1 125 ? 15.373 0.672 5.632 1.00 20.70 ? 125 GLN A C 1 ATOM 979 O O . GLN A 1 125 ? 16.293 1.260 6.191 1.00 23.81 ? 125 GLN A O 1 ATOM 980 C CB . GLN A 1 125 ? 13.127 1.286 6.491 1.00 21.63 ? 125 GLN A CB 1 ATOM 981 C CG . GLN A 1 125 ? 11.857 2.102 6.356 1.00 30.39 ? 125 GLN A CG 1 ATOM 982 C CD . GLN A 1 125 ? 12.147 3.573 6.155 1.00 35.70 ? 125 GLN A CD 1 ATOM 983 O OE1 . GLN A 1 125 ? 12.847 4.187 6.960 1.00 40.10 ? 125 GLN A OE1 1 ATOM 984 N NE2 . GLN A 1 125 ? 11.607 4.148 5.093 1.00 41.34 ? 125 GLN A NE2 1 ATOM 985 N N . LEU A 1 126 ? 15.438 -0.613 5.295 1.00 22.14 ? 126 LEU A N 1 ATOM 986 C CA . LEU A 1 126 ? 16.622 -1.423 5.577 1.00 21.23 ? 126 LEU A CA 1 ATOM 987 C C . LEU A 1 126 ? 17.730 -1.341 4.530 1.00 21.20 ? 126 LEU A C 1 ATOM 988 O O . LEU A 1 126 ? 18.905 -1.537 4.860 1.00 21.15 ? 126 LEU A O 1 ATOM 989 C CB . LEU A 1 126 ? 16.220 -2.884 5.801 1.00 21.21 ? 126 LEU A CB 1 ATOM 990 C CG . LEU A 1 126 ? 15.309 -3.130 7.005 1.00 24.35 ? 126 LEU A CG 1 ATOM 991 C CD1 . LEU A 1 126 ? 14.871 -4.588 7.049 1.00 19.36 ? 126 LEU A CD1 1 ATOM 992 C CD2 . LEU A 1 126 ? 16.036 -2.735 8.285 1.00 18.94 ? 126 LEU A CD2 1 ATOM 993 N N . LYS A 1 127 ? 17.365 -1.054 3.278 1.00 22.93 ? 127 LYS A N 1 ATOM 994 C CA . LYS A 1 127 ? 18.350 -0.955 2.193 1.00 26.44 ? 127 LYS A CA 1 ATOM 995 C C . LYS A 1 127 ? 19.580 -0.097 2.486 1.00 20.06 ? 127 LYS A C 1 ATOM 996 O O . LYS A 1 127 ? 20.699 -0.511 2.187 1.00 22.94 ? 127 LYS A O 1 ATOM 997 C CB . LYS A 1 127 ? 17.693 -0.504 0.886 1.00 33.61 ? 127 LYS A CB 1 ATOM 998 C CG . LYS A 1 127 ? 17.200 -1.656 0.044 1.00 47.30 ? 127 LYS A CG 1 ATOM 999 C CD . LYS A 1 127 ? 16.323 -1.193 -1.104 1.00 56.32 ? 127 LYS A CD 1 ATOM 1000 C CE . LYS A 1 127 ? 15.743 -2.395 -1.838 1.00 58.09 ? 127 LYS A CE 1 ATOM 1001 N NZ . LYS A 1 127 ? 14.710 -2.002 -2.834 1.00 63.23 ? 127 LYS A NZ 1 ATOM 1002 N N . PRO A 1 128 ? 19.397 1.102 3.079 1.00 19.14 ? 128 PRO A N 1 ATOM 1003 C CA . PRO A 1 128 ? 20.549 1.958 3.381 1.00 15.28 ? 128 PRO A CA 1 ATOM 1004 C C . PRO A 1 128 ? 21.665 1.260 4.167 1.00 18.17 ? 128 PRO A C 1 ATOM 1005 O O . PRO A 1 128 ? 22.847 1.484 3.901 1.00 21.95 ? 128 PRO A O 1 ATOM 1006 C CB . PRO A 1 128 ? 19.920 3.089 4.189 1.00 12.31 ? 128 PRO A CB 1 ATOM 1007 C CG . PRO A 1 128 ? 18.589 3.241 3.542 1.00 14.29 ? 128 PRO A CG 1 ATOM 1008 C CD . PRO A 1 128 ? 18.137 1.804 3.401 1.00 15.76 ? 128 PRO A CD 1 ATOM 1009 N N . PHE A 1 129 ? 21.293 0.394 5.109 1.00 13.72 ? 129 PHE A N 1 ATOM 1010 C CA . PHE A 1 129 ? 22.279 -0.313 5.927 1.00 20.85 ? 129 PHE A CA 1 ATOM 1011 C C . PHE A 1 129 ? 22.978 -1.442 5.168 1.00 19.98 ? 129 PHE A C 1 ATOM 1012 O O . PHE A 1 129 ? 24.153 -1.729 5.413 1.00 18.84 ? 129 PHE A O 1 ATOM 1013 C CB . PHE A 1 129 ? 21.631 -0.804 7.226 1.00 20.05 ? 129 PHE A CB 1 ATOM 1014 C CG . PHE A 1 129 ? 20.973 0.300 8.017 1.00 20.02 ? 129 PHE A CG 1 ATOM 1015 C CD1 . PHE A 1 129 ? 21.740 1.275 8.652 1.00 22.94 ? 129 PHE A CD1 1 ATOM 1016 C CD2 . PHE A 1 129 ? 19.587 0.396 8.084 1.00 22.16 ? 129 PHE A CD2 1 ATOM 1017 C CE1 . PHE A 1 129 ? 21.133 2.330 9.337 1.00 19.18 ? 129 PHE A CE1 1 ATOM 1018 C CE2 . PHE A 1 129 ? 18.972 1.448 8.767 1.00 18.57 ? 129 PHE A CE2 1 ATOM 1019 C CZ . PHE A 1 129 ? 19.748 2.415 9.393 1.00 14.53 ? 129 PHE A CZ 1 ATOM 1020 N N . GLU A 1 130 ? 22.251 -2.068 4.243 1.00 19.42 ? 130 GLU A N 1 ATOM 1021 C CA . GLU A 1 130 ? 22.800 -3.126 3.398 1.00 18.85 ? 130 GLU A CA 1 ATOM 1022 C C . GLU A 1 130 ? 23.848 -2.466 2.493 1.00 21.85 ? 130 GLU A C 1 ATOM 1023 O O . GLU A 1 130 ? 24.926 -3.018 2.255 1.00 20.87 ? 130 GLU A O 1 ATOM 1024 C CB . GLU A 1 130 ? 21.680 -3.743 2.545 1.00 21.87 ? 130 GLU A CB 1 ATOM 1025 C CG . GLU A 1 130 ? 22.118 -4.851 1.575 1.00 27.47 ? 130 GLU A CG 1 ATOM 1026 C CD . GLU A 1 130 ? 22.396 -6.192 2.248 1.00 29.84 ? 130 GLU A CD 1 ATOM 1027 O OE1 . GLU A 1 130 ? 22.104 -6.336 3.453 1.00 29.88 ? 130 GLU A OE1 1 ATOM 1028 O OE2 . GLU A 1 130 ? 22.898 -7.111 1.564 1.00 32.39 ? 130 GLU A OE2 1 ATOM 1029 N N . THR A 1 131 ? 23.527 -1.256 2.031 1.00 22.30 ? 131 THR A N 1 ATOM 1030 C CA . THR A 1 131 ? 24.407 -0.468 1.167 1.00 21.34 ? 131 THR A CA 1 ATOM 1031 C C . THR A 1 131 ? 25.690 -0.079 1.897 1.00 20.14 ? 131 THR A C 1 ATOM 1032 O O . THR A 1 131 ? 26.787 -0.218 1.359 1.00 19.79 ? 131 THR A O 1 ATOM 1033 C CB . THR A 1 131 ? 23.704 0.819 0.699 1.00 26.14 ? 131 THR A CB 1 ATOM 1034 O OG1 . THR A 1 131 ? 22.470 0.483 0.053 1.00 25.68 ? 131 THR A OG1 1 ATOM 1035 C CG2 . THR A 1 131 ? 24.588 1.592 -0.269 1.00 23.33 ? 131 THR A CG2 1 ATOM 1036 N N . LEU A 1 132 ? 25.540 0.438 3.115 1.00 22.42 ? 132 LEU A N 1 ATOM 1037 C CA . LEU A 1 132 ? 26.688 0.833 3.930 1.00 24.35 ? 132 LEU A CA 1 ATOM 1038 C C . LEU A 1 132 ? 27.625 -0.360 4.110 1.00 24.17 ? 132 LEU A C 1 ATOM 1039 O O . LEU A 1 132 ? 28.840 -0.242 3.954 1.00 23.15 ? 132 LEU A O 1 ATOM 1040 C CB . LEU A 1 132 ? 26.218 1.335 5.299 1.00 25.57 ? 132 LEU A CB 1 ATOM 1041 C CG . LEU A 1 132 ? 25.560 2.719 5.320 1.00 29.69 ? 132 LEU A CG 1 ATOM 1042 C CD1 . LEU A 1 132 ? 24.784 2.930 6.608 1.00 24.66 ? 132 LEU A CD1 1 ATOM 1043 C CD2 . LEU A 1 132 ? 26.627 3.786 5.148 1.00 20.42 ? 132 LEU A CD2 1 ATOM 1044 N N . LEU A 1 133 ? 27.034 -1.515 4.398 1.00 25.87 ? 133 LEU A N 1 ATOM 1045 C CA . LEU A 1 133 ? 27.771 -2.755 4.595 1.00 23.23 ? 133 LEU A CA 1 ATOM 1046 C C . LEU A 1 133 ? 28.514 -3.154 3.316 1.00 25.78 ? 133 LEU A C 1 ATOM 1047 O O . LEU A 1 133 ? 29.706 -3.472 3.360 1.00 18.93 ? 133 LEU A O 1 ATOM 1048 C CB . LEU A 1 133 ? 26.793 -3.856 5.021 1.00 24.05 ? 133 LEU A CB 1 ATOM 1049 C CG . LEU A 1 133 ? 27.066 -4.681 6.283 1.00 26.72 ? 133 LEU A CG 1 ATOM 1050 C CD1 . LEU A 1 133 ? 27.859 -3.901 7.312 1.00 23.16 ? 133 LEU A CD1 1 ATOM 1051 C CD2 . LEU A 1 133 ? 25.739 -5.146 6.861 1.00 24.18 ? 133 LEU A CD2 1 ATOM 1052 N N . SER A 1 134 ? 27.832 -3.081 2.172 1.00 23.49 ? 134 SER A N 1 ATOM 1053 C CA . SER A 1 134 ? 28.447 -3.445 0.893 1.00 29.74 ? 134 SER A CA 1 ATOM 1054 C C . SER A 1 134 ? 29.633 -2.564 0.505 1.00 30.07 ? 134 SER A C 1 ATOM 1055 O O . SER A 1 134 ? 30.515 -3.003 -0.237 1.00 36.18 ? 134 SER A O 1 ATOM 1056 C CB . SER A 1 134 ? 27.407 -3.459 -0.236 1.00 27.59 ? 134 SER A CB 1 ATOM 1057 O OG . SER A 1 134 ? 26.940 -2.158 -0.544 1.00 32.05 ? 134 SER A OG 1 ATOM 1058 N N . GLN A 1 135 ? 29.666 -1.334 1.013 1.00 28.62 ? 135 GLN A N 1 ATOM 1059 C CA . GLN A 1 135 ? 30.760 -0.412 0.713 1.00 27.90 ? 135 GLN A CA 1 ATOM 1060 C C . GLN A 1 135 ? 31.928 -0.516 1.688 1.00 30.39 ? 135 GLN A C 1 ATOM 1061 O O . GLN A 1 135 ? 32.943 0.159 1.517 1.00 31.64 ? 135 GLN A O 1 ATOM 1062 C CB . GLN A 1 135 ? 30.241 1.019 0.685 1.00 32.68 ? 135 GLN A CB 1 ATOM 1063 C CG . GLN A 1 135 ? 29.215 1.262 -0.393 1.00 39.38 ? 135 GLN A CG 1 ATOM 1064 C CD . GLN A 1 135 ? 28.499 2.581 -0.212 1.00 45.11 ? 135 GLN A CD 1 ATOM 1065 O OE1 . GLN A 1 135 ? 28.712 3.293 0.775 1.00 46.94 ? 135 GLN A OE1 1 ATOM 1066 N NE2 . GLN A 1 135 ? 27.625 2.907 -1.154 1.00 45.99 ? 135 GLN A NE2 1 ATOM 1067 N N . ASN A 1 136 ? 31.780 -1.335 2.724 1.00 27.75 ? 136 ASN A N 1 ATOM 1068 C CA . ASN A 1 136 ? 32.832 -1.515 3.709 1.00 28.91 ? 136 ASN A CA 1 ATOM 1069 C C . ASN A 1 136 ? 33.346 -2.952 3.680 1.00 29.42 ? 136 ASN A C 1 ATOM 1070 O O . ASN A 1 136 ? 32.749 -3.841 4.281 1.00 28.45 ? 136 ASN A O 1 ATOM 1071 C CB . ASN A 1 136 ? 32.329 -1.150 5.113 1.00 27.76 ? 136 ASN A CB 1 ATOM 1072 C CG . ASN A 1 136 ? 33.410 -1.294 6.176 1.00 28.46 ? 136 ASN A CG 1 ATOM 1073 O OD1 . ASN A 1 136 ? 34.596 -1.124 5.895 1.00 30.75 ? 136 ASN A OD1 1 ATOM 1074 N ND2 . ASN A 1 136 ? 33.001 -1.620 7.393 1.00 24.24 ? 136 ASN A ND2 1 ATOM 1075 N N . GLN A 1 137 ? 34.448 -3.170 2.956 1.00 36.91 ? 137 GLN A N 1 ATOM 1076 C CA . GLN A 1 137 ? 35.068 -4.498 2.828 1.00 38.50 ? 137 GLN A CA 1 ATOM 1077 C C . GLN A 1 137 ? 34.067 -5.603 2.494 1.00 37.08 ? 137 GLN A C 1 ATOM 1078 O O . GLN A 1 137 ? 34.145 -6.708 3.036 1.00 37.53 ? 137 GLN A O 1 ATOM 1079 C CB . GLN A 1 137 ? 35.820 -4.858 4.109 1.00 42.36 ? 137 GLN A CB 1 ATOM 1080 C CG . GLN A 1 137 ? 37.003 -3.968 4.421 1.00 49.91 ? 137 GLN A CG 1 ATOM 1081 C CD . GLN A 1 137 ? 37.478 -4.127 5.853 1.00 59.50 ? 137 GLN A CD 1 ATOM 1082 O OE1 . GLN A 1 137 ? 38.189 -5.084 6.172 1.00 59.71 ? 137 GLN A OE1 1 ATOM 1083 N NE2 . GLN A 1 137 ? 37.096 -3.193 6.717 1.00 62.55 ? 137 GLN A NE2 1 ATOM 1084 N N . GLY A 1 138 ? 33.109 -5.283 1.628 1.00 34.54 ? 138 GLY A N 1 ATOM 1085 C CA . GLY A 1 138 ? 32.106 -6.255 1.223 1.00 33.64 ? 138 GLY A CA 1 ATOM 1086 C C . GLY A 1 138 ? 31.214 -6.793 2.328 1.00 35.93 ? 138 GLY A C 1 ATOM 1087 O O . GLY A 1 138 ? 30.678 -7.895 2.206 1.00 40.71 ? 138 GLY A O 1 ATOM 1088 N N . GLY A 1 139 ? 31.047 -6.021 3.399 1.00 33.49 ? 139 GLY A N 1 ATOM 1089 C CA . GLY A 1 139 ? 30.209 -6.447 4.509 1.00 33.25 ? 139 GLY A CA 1 ATOM 1090 C C . GLY A 1 139 ? 30.785 -7.588 5.326 1.00 32.97 ? 139 GLY A C 1 ATOM 1091 O O . GLY A 1 139 ? 30.050 -8.282 6.024 1.00 35.18 ? 139 GLY A O 1 ATOM 1092 N N . LYS A 1 140 ? 32.102 -7.761 5.266 1.00 35.47 ? 140 LYS A N 1 ATOM 1093 C CA . LYS A 1 140 ? 32.778 -8.833 5.990 1.00 36.91 ? 140 LYS A CA 1 ATOM 1094 C C . LYS A 1 140 ? 33.083 -8.498 7.449 1.00 34.37 ? 140 LYS A C 1 ATOM 1095 O O . LYS A 1 140 ? 33.253 -9.404 8.263 1.00 35.42 ? 140 LYS A O 1 ATOM 1096 C CB . LYS A 1 140 ? 34.074 -9.228 5.266 1.00 39.70 ? 140 LYS A CB 1 ATOM 1097 C CG . LYS A 1 140 ? 33.871 -9.767 3.849 1.00 48.70 ? 140 LYS A CG 1 ATOM 1098 C CD . LYS A 1 140 ? 33.284 -11.175 3.843 1.00 55.06 ? 140 LYS A CD 1 ATOM 1099 C CE . LYS A 1 140 ? 34.358 -12.227 4.096 1.00 64.02 ? 140 LYS A CE 1 ATOM 1100 N NZ . LYS A 1 140 ? 33.805 -13.614 4.138 1.00 62.77 ? 140 LYS A NZ 1 ATOM 1101 N N . THR A 1 141 ? 33.139 -7.207 7.778 1.00 32.83 ? 141 THR A N 1 ATOM 1102 C CA . THR A 1 141 ? 33.442 -6.773 9.144 1.00 31.17 ? 141 THR A CA 1 ATOM 1103 C C . THR A 1 141 ? 32.293 -6.063 9.875 1.00 31.32 ? 141 THR A C 1 ATOM 1104 O O . THR A 1 141 ? 31.255 -6.671 10.135 1.00 32.43 ? 141 THR A O 1 ATOM 1105 C CB . THR A 1 141 ? 34.715 -5.896 9.192 1.00 28.55 ? 141 THR A CB 1 ATOM 1106 O OG1 . THR A 1 141 ? 34.603 -4.835 8.235 1.00 28.25 ? 141 THR A OG1 1 ATOM 1107 C CG2 . THR A 1 141 ? 35.956 -6.726 8.901 1.00 31.43 ? 141 THR A CG2 1 ATOM 1108 N N . PHE A 1 142 ? 32.481 -4.782 10.200 1.00 26.40 ? 142 PHE A N 1 ATOM 1109 C CA . PHE A 1 142 ? 31.481 -4.007 10.924 1.00 19.15 ? 142 PHE A CA 1 ATOM 1110 C C . PHE A 1 142 ? 30.814 -2.954 10.043 1.00 21.96 ? 142 PHE A C 1 ATOM 1111 O O . PHE A 1 142 ? 31.162 -2.817 8.872 1.00 24.65 ? 142 PHE A O 1 ATOM 1112 C CB . PHE A 1 142 ? 32.131 -3.388 12.158 1.00 19.57 ? 142 PHE A CB 1 ATOM 1113 C CG . PHE A 1 142 ? 32.807 -4.402 13.044 1.00 18.76 ? 142 PHE A CG 1 ATOM 1114 C CD1 . PHE A 1 142 ? 32.062 -5.181 13.928 1.00 20.46 ? 142 PHE A CD1 1 ATOM 1115 C CD2 . PHE A 1 142 ? 34.182 -4.604 12.971 1.00 19.75 ? 142 PHE A CD2 1 ATOM 1116 C CE1 . PHE A 1 142 ? 32.677 -6.150 14.720 1.00 18.82 ? 142 PHE A CE1 1 ATOM 1117 C CE2 . PHE A 1 142 ? 34.807 -5.570 13.757 1.00 18.62 ? 142 PHE A CE2 1 ATOM 1118 C CZ . PHE A 1 142 ? 34.053 -6.343 14.634 1.00 19.03 ? 142 PHE A CZ 1 ATOM 1119 N N . ILE A 1 143 ? 29.845 -2.224 10.590 1.00 18.32 ? 143 ILE A N 1 ATOM 1120 C CA . ILE A 1 143 ? 29.126 -1.227 9.802 1.00 19.44 ? 143 ILE A CA 1 ATOM 1121 C C . ILE A 1 143 ? 30.020 -0.086 9.302 1.00 21.45 ? 143 ILE A C 1 ATOM 1122 O O . ILE A 1 143 ? 29.805 0.444 8.211 1.00 21.50 ? 143 ILE A O 1 ATOM 1123 C CB . ILE A 1 143 ? 27.875 -0.687 10.560 1.00 20.67 ? 143 ILE A CB 1 ATOM 1124 C CG1 . ILE A 1 143 ? 26.946 0.047 9.593 1.00 19.72 ? 143 ILE A CG1 1 ATOM 1125 C CG2 . ILE A 1 143 ? 28.281 0.224 11.719 1.00 18.85 ? 143 ILE A CG2 1 ATOM 1126 C CD1 . ILE A 1 143 ? 26.301 -0.847 8.546 1.00 12.02 ? 143 ILE A CD1 1 ATOM 1127 N N . VAL A 1 144 ? 31.032 0.266 10.093 1.00 21.38 ? 144 VAL A N 1 ATOM 1128 C CA . VAL A 1 144 ? 31.981 1.325 9.743 1.00 20.03 ? 144 VAL A CA 1 ATOM 1129 C C . VAL A 1 144 ? 33.383 0.903 10.171 1.00 19.62 ? 144 VAL A C 1 ATOM 1130 O O . VAL A 1 144 ? 33.608 0.590 11.341 1.00 21.10 ? 144 VAL A O 1 ATOM 1131 C CB . VAL A 1 144 ? 31.644 2.669 10.449 1.00 16.54 ? 144 VAL A CB 1 ATOM 1132 C CG1 . VAL A 1 144 ? 32.764 3.681 10.217 1.00 16.44 ? 144 VAL A CG1 1 ATOM 1133 C CG2 . VAL A 1 144 ? 30.329 3.228 9.931 1.00 16.31 ? 144 VAL A CG2 1 ATOM 1134 N N . GLY A 1 145 ? 34.316 0.884 9.223 1.00 18.27 ? 145 GLY A N 1 ATOM 1135 C CA . GLY A 1 145 ? 35.686 0.504 9.534 1.00 19.01 ? 145 GLY A CA 1 ATOM 1136 C C . GLY A 1 145 ? 35.887 -0.978 9.801 1.00 25.00 ? 145 GLY A C 1 ATOM 1137 O O . GLY A 1 145 ? 35.046 -1.803 9.438 1.00 24.24 ? 145 GLY A O 1 ATOM 1138 N N . ASP A 1 146 ? 36.995 -1.316 10.456 1.00 27.91 ? 146 ASP A N 1 ATOM 1139 C CA . ASP A 1 146 ? 37.312 -2.709 10.761 1.00 34.30 ? 146 ASP A CA 1 ATOM 1140 C C . ASP A 1 146 ? 37.306 -3.027 12.257 1.00 35.84 ? 146 ASP A C 1 ATOM 1141 O O . ASP A 1 146 ? 37.840 -4.051 12.687 1.00 35.68 ? 146 ASP A O 1 ATOM 1142 C CB . ASP A 1 146 ? 38.657 -3.102 10.132 1.00 42.87 ? 146 ASP A CB 1 ATOM 1143 C CG . ASP A 1 146 ? 39.828 -2.277 10.659 1.00 52.43 ? 146 ASP A CG 1 ATOM 1144 O OD1 . ASP A 1 146 ? 39.608 -1.262 11.360 1.00 54.33 ? 146 ASP A OD1 1 ATOM 1145 O OD2 . ASP A 1 146 ? 40.984 -2.651 10.357 1.00 57.94 ? 146 ASP A OD2 1 ATOM 1146 N N . GLN A 1 147 ? 36.707 -2.136 13.042 1.00 34.42 ? 147 GLN A N 1 ATOM 1147 C CA . GLN A 1 147 ? 36.601 -2.303 14.488 1.00 30.30 ? 147 GLN A CA 1 ATOM 1148 C C . GLN A 1 147 ? 35.160 -1.956 14.863 1.00 30.17 ? 147 GLN A C 1 ATOM 1149 O O . GLN A 1 147 ? 34.537 -1.092 14.236 1.00 28.56 ? 147 GLN A O 1 ATOM 1150 C CB . GLN A 1 147 ? 37.592 -1.388 15.220 1.00 33.96 ? 147 GLN A CB 1 ATOM 1151 C CG . GLN A 1 147 ? 37.435 0.091 14.880 1.00 50.43 ? 147 GLN A CG 1 ATOM 1152 C CD . GLN A 1 147 ? 38.307 0.998 15.731 1.00 55.59 ? 147 GLN A CD 1 ATOM 1153 O OE1 . GLN A 1 147 ? 39.418 1.354 15.340 1.00 58.58 ? 147 GLN A OE1 1 ATOM 1154 N NE2 . GLN A 1 147 ? 37.796 1.390 16.897 1.00 54.63 ? 147 GLN A NE2 1 ATOM 1155 N N . ILE A 1 148 ? 34.617 -2.658 15.855 1.00 25.06 ? 148 ILE A N 1 ATOM 1156 C CA . ILE A 1 148 ? 33.241 -2.435 16.296 1.00 19.11 ? 148 ILE A CA 1 ATOM 1157 C C . ILE A 1 148 ? 33.045 -1.043 16.919 1.00 18.93 ? 148 ILE A C 1 ATOM 1158 O O . ILE A 1 148 ? 33.955 -0.495 17.541 1.00 17.85 ? 148 ILE A O 1 ATOM 1159 C CB . ILE A 1 148 ? 32.792 -3.554 17.276 1.00 15.67 ? 148 ILE A CB 1 ATOM 1160 C CG1 . ILE A 1 148 ? 31.267 -3.653 17.308 1.00 18.87 ? 148 ILE A CG1 1 ATOM 1161 C CG2 . ILE A 1 148 ? 33.347 -3.305 18.673 1.00 14.46 ? 148 ILE A CG2 1 ATOM 1162 C CD1 . ILE A 1 148 ? 30.755 -4.966 17.868 1.00 13.44 ? 148 ILE A CD1 1 ATOM 1163 N N . SER A 1 149 ? 31.867 -0.463 16.710 1.00 14.56 ? 149 SER A N 1 ATOM 1164 C CA . SER A 1 149 ? 31.556 0.859 17.245 1.00 15.61 ? 149 SER A CA 1 ATOM 1165 C C . SER A 1 149 ? 30.213 0.784 17.956 1.00 12.88 ? 149 SER A C 1 ATOM 1166 O O . SER A 1 149 ? 29.525 -0.232 17.867 1.00 12.22 ? 149 SER A O 1 ATOM 1167 C CB . SER A 1 149 ? 31.488 1.894 16.116 1.00 10.55 ? 149 SER A CB 1 ATOM 1168 O OG . SER A 1 149 ? 30.349 1.690 15.295 1.00 13.07 ? 149 SER A OG 1 ATOM 1169 N N . PHE A 1 150 ? 29.833 1.860 18.645 1.00 14.89 ? 150 PHE A N 1 ATOM 1170 C CA . PHE A 1 150 ? 28.557 1.881 19.357 1.00 15.23 ? 150 PHE A CA 1 ATOM 1171 C C . PHE A 1 150 ? 27.379 1.783 18.396 1.00 9.66 ? 150 PHE A C 1 ATOM 1172 O O . PHE A 1 150 ? 26.310 1.299 18.765 1.00 19.65 ? 150 PHE A O 1 ATOM 1173 C CB . PHE A 1 150 ? 28.435 3.119 20.270 1.00 14.25 ? 150 PHE A CB 1 ATOM 1174 C CG . PHE A 1 150 ? 28.325 4.432 19.531 1.00 8.22 ? 150 PHE A CG 1 ATOM 1175 C CD1 . PHE A 1 150 ? 27.084 4.915 19.129 1.00 2.64 ? 150 PHE A CD1 1 ATOM 1176 C CD2 . PHE A 1 150 ? 29.461 5.184 19.246 1.00 6.27 ? 150 PHE A CD2 1 ATOM 1177 C CE1 . PHE A 1 150 ? 26.974 6.130 18.449 1.00 11.07 ? 150 PHE A CE1 1 ATOM 1178 C CE2 . PHE A 1 150 ? 29.363 6.401 18.566 1.00 10.05 ? 150 PHE A CE2 1 ATOM 1179 C CZ . PHE A 1 150 ? 28.115 6.875 18.167 1.00 7.03 ? 150 PHE A CZ 1 ATOM 1180 N N . ALA A 1 151 ? 27.588 2.222 17.156 1.00 16.82 ? 151 ALA A N 1 ATOM 1181 C CA . ALA A 1 151 ? 26.545 2.170 16.130 1.00 17.83 ? 151 ALA A CA 1 ATOM 1182 C C . ALA A 1 151 ? 26.207 0.716 15.793 1.00 13.16 ? 151 ALA A C 1 ATOM 1183 O O . ALA A 1 151 ? 25.063 0.395 15.466 1.00 11.09 ? 151 ALA A O 1 ATOM 1184 C CB . ALA A 1 151 ? 26.991 2.923 14.873 1.00 17.78 ? 151 ALA A CB 1 ATOM 1185 N N . ASP A 1 152 ? 27.206 -0.157 15.888 1.00 8.88 ? 152 ASP A N 1 ATOM 1186 C CA . ASP A 1 152 ? 27.009 -1.575 15.618 1.00 15.04 ? 152 ASP A CA 1 ATOM 1187 C C . ASP A 1 152 ? 26.000 -2.181 16.578 1.00 17.03 ? 152 ASP A C 1 ATOM 1188 O O . ASP A 1 152 ? 25.059 -2.856 16.148 1.00 15.36 ? 152 ASP A O 1 ATOM 1189 C CB . ASP A 1 152 ? 28.335 -2.330 15.726 1.00 16.98 ? 152 ASP A CB 1 ATOM 1190 C CG . ASP A 1 152 ? 29.198 -2.166 14.497 1.00 16.02 ? 152 ASP A CG 1 ATOM 1191 O OD1 . ASP A 1 152 ? 28.763 -2.584 13.411 1.00 16.20 ? 152 ASP A OD1 1 ATOM 1192 O OD2 . ASP A 1 152 ? 30.310 -1.622 14.614 1.00 19.68 ? 152 ASP A OD2 1 ATOM 1193 N N . TYR A 1 153 ? 26.177 -1.910 17.873 1.00 16.69 ? 153 TYR A N 1 ATOM 1194 C CA . TYR A 1 153 ? 25.273 -2.436 18.901 1.00 14.36 ? 153 TYR A CA 1 ATOM 1195 C C . TYR A 1 153 ? 23.861 -1.912 18.711 1.00 13.55 ? 153 TYR A C 1 ATOM 1196 O O . TYR A 1 153 ? 22.898 -2.654 18.843 1.00 12.86 ? 153 TYR A O 1 ATOM 1197 C CB . TYR A 1 153 ? 25.778 -2.085 20.309 1.00 12.46 ? 153 TYR A CB 1 ATOM 1198 C CG . TYR A 1 153 ? 27.110 -2.701 20.625 1.00 8.60 ? 153 TYR A CG 1 ATOM 1199 C CD1 . TYR A 1 153 ? 27.225 -4.070 20.886 1.00 12.19 ? 153 TYR A CD1 1 ATOM 1200 C CD2 . TYR A 1 153 ? 28.269 -1.929 20.612 1.00 12.86 ? 153 TYR A CD2 1 ATOM 1201 C CE1 . TYR A 1 153 ? 28.472 -4.652 21.122 1.00 6.65 ? 153 TYR A CE1 1 ATOM 1202 C CE2 . TYR A 1 153 ? 29.514 -2.500 20.844 1.00 9.42 ? 153 TYR A CE2 1 ATOM 1203 C CZ . TYR A 1 153 ? 29.607 -3.859 21.097 1.00 9.97 ? 153 TYR A CZ 1 ATOM 1204 O OH . TYR A 1 153 ? 30.840 -4.419 21.320 1.00 15.89 ? 153 TYR A OH 1 ATOM 1205 N N . ASN A 1 154 ? 23.740 -0.634 18.361 1.00 14.34 ? 154 ASN A N 1 ATOM 1206 C CA . ASN A 1 154 ? 22.441 -0.022 18.163 1.00 10.38 ? 154 ASN A CA 1 ATOM 1207 C C . ASN A 1 154 ? 21.757 -0.575 16.909 1.00 11.97 ? 154 ASN A C 1 ATOM 1208 O O . ASN A 1 154 ? 20.550 -0.830 16.913 1.00 16.19 ? 154 ASN A O 1 ATOM 1209 C CB . ASN A 1 154 ? 22.570 1.500 18.093 1.00 9.39 ? 154 ASN A CB 1 ATOM 1210 C CG . ASN A 1 154 ? 21.255 2.204 18.378 1.00 14.97 ? 154 ASN A CG 1 ATOM 1211 O OD1 . ASN A 1 154 ? 20.266 1.567 18.750 1.00 13.26 ? 154 ASN A OD1 1 ATOM 1212 N ND2 . ASN A 1 154 ? 21.250 3.517 18.239 1.00 16.92 ? 154 ASN A ND2 1 ATOM 1213 N N . LEU A 1 155 ? 22.531 -0.765 15.844 1.00 19.22 ? 155 LEU A N 1 ATOM 1214 C CA . LEU A 1 155 ? 21.980 -1.296 14.597 1.00 14.98 ? 155 LEU A CA 1 ATOM 1215 C C . LEU A 1 155 ? 21.551 -2.744 14.831 1.00 15.25 ? 155 LEU A C 1 ATOM 1216 O O . LEU A 1 155 ? 20.461 -3.144 14.420 1.00 12.96 ? 155 LEU A O 1 ATOM 1217 C CB . LEU A 1 155 ? 23.015 -1.219 13.467 1.00 14.29 ? 155 LEU A CB 1 ATOM 1218 C CG . LEU A 1 155 ? 22.609 -1.888 12.144 1.00 11.29 ? 155 LEU A CG 1 ATOM 1219 C CD1 . LEU A 1 155 ? 21.292 -1.328 11.634 1.00 11.27 ? 155 LEU A CD1 1 ATOM 1220 C CD2 . LEU A 1 155 ? 23.708 -1.695 11.117 1.00 11.69 ? 155 LEU A CD2 1 ATOM 1221 N N . LEU A 1 156 ? 22.394 -3.507 15.529 1.00 11.39 ? 156 LEU A N 1 ATOM 1222 C CA . LEU A 1 156 ? 22.099 -4.907 15.840 1.00 15.34 ? 156 LEU A CA 1 ATOM 1223 C C . LEU A 1 156 ? 20.770 -5.011 16.575 1.00 16.71 ? 156 LEU A C 1 ATOM 1224 O O . LEU A 1 156 ? 19.918 -5.822 16.208 1.00 15.34 ? 156 LEU A O 1 ATOM 1225 C CB . LEU A 1 156 ? 23.206 -5.517 16.699 1.00 15.98 ? 156 LEU A CB 1 ATOM 1226 C CG . LEU A 1 156 ? 23.016 -6.998 17.041 1.00 20.69 ? 156 LEU A CG 1 ATOM 1227 C CD1 . LEU A 1 156 ? 22.962 -7.831 15.764 1.00 16.39 ? 156 LEU A CD1 1 ATOM 1228 C CD2 . LEU A 1 156 ? 24.150 -7.473 17.933 1.00 17.86 ? 156 LEU A CD2 1 ATOM 1229 N N . ASP A 1 157 ? 20.591 -4.182 17.605 1.00 14.16 ? 157 ASP A N 1 ATOM 1230 C CA . ASP A 1 157 ? 19.346 -4.187 18.362 1.00 12.86 ? 157 ASP A CA 1 ATOM 1231 C C . ASP A 1 157 ? 18.166 -3.885 17.443 1.00 15.32 ? 157 ASP A C 1 ATOM 1232 O O . ASP A 1 157 ? 17.145 -4.577 17.482 1.00 17.32 ? 157 ASP A O 1 ATOM 1233 C CB . ASP A 1 157 ? 19.381 -3.161 19.500 1.00 15.85 ? 157 ASP A CB 1 ATOM 1234 C CG . ASP A 1 157 ? 18.058 -3.075 20.232 1.00 17.29 ? 157 ASP A CG 1 ATOM 1235 O OD1 . ASP A 1 157 ? 17.627 -4.101 20.788 1.00 18.97 ? 157 ASP A OD1 1 ATOM 1236 O OD2 . ASP A 1 157 ? 17.401 -2.015 20.187 1.00 21.13 ? 157 ASP A OD2 1 ATOM 1237 N N . LEU A 1 158 ? 18.311 -2.853 16.615 1.00 17.19 ? 158 LEU A N 1 ATOM 1238 C CA . LEU A 1 158 ? 17.254 -2.470 15.687 1.00 16.57 ? 158 LEU A CA 1 ATOM 1239 C C . LEU A 1 158 ? 16.878 -3.653 14.781 1.00 16.21 ? 158 LEU A C 1 ATOM 1240 O O . LEU A 1 158 ? 15.698 -3.948 14.591 1.00 16.75 ? 158 LEU A O 1 ATOM 1241 C CB . LEU A 1 158 ? 17.690 -1.268 14.840 1.00 18.13 ? 158 LEU A CB 1 ATOM 1242 C CG . LEU A 1 158 ? 16.608 -0.654 13.942 1.00 17.58 ? 158 LEU A CG 1 ATOM 1243 C CD1 . LEU A 1 158 ? 15.533 0.000 14.795 1.00 16.39 ? 158 LEU A CD1 1 ATOM 1244 C CD2 . LEU A 1 158 ? 17.224 0.367 13.005 1.00 20.43 ? 158 LEU A CD2 1 ATOM 1245 N N . LEU A 1 159 ? 17.882 -4.359 14.271 1.00 15.78 ? 159 LEU A N 1 ATOM 1246 C CA . LEU A 1 159 ? 17.638 -5.507 13.394 1.00 16.75 ? 159 LEU A CA 1 ATOM 1247 C C . LEU A 1 159 ? 16.930 -6.650 14.124 1.00 17.74 ? 159 LEU A C 1 ATOM 1248 O O . LEU A 1 159 ? 15.953 -7.204 13.618 1.00 18.77 ? 159 LEU A O 1 ATOM 1249 C CB . LEU A 1 159 ? 18.955 -5.991 12.774 1.00 10.89 ? 159 LEU A CB 1 ATOM 1250 C CG . LEU A 1 159 ? 19.658 -4.948 11.901 1.00 13.04 ? 159 LEU A CG 1 ATOM 1251 C CD1 . LEU A 1 159 ? 21.008 -5.451 11.432 1.00 13.47 ? 159 LEU A CD1 1 ATOM 1252 C CD2 . LEU A 1 159 ? 18.776 -4.591 10.721 1.00 12.50 ? 159 LEU A CD2 1 ATOM 1253 N N . LEU A 1 160 ? 17.400 -6.968 15.330 1.00 21.94 ? 160 LEU A N 1 ATOM 1254 C CA . LEU A 1 160 ? 16.811 -8.035 16.136 1.00 18.20 ? 160 LEU A CA 1 ATOM 1255 C C . LEU A 1 160 ? 15.341 -7.806 16.466 1.00 15.43 ? 160 LEU A C 1 ATOM 1256 O O . LEU A 1 160 ? 14.534 -8.729 16.347 1.00 18.09 ? 160 LEU A O 1 ATOM 1257 C CB . LEU A 1 160 ? 17.607 -8.239 17.430 1.00 13.38 ? 160 LEU A CB 1 ATOM 1258 C CG . LEU A 1 160 ? 19.042 -8.755 17.277 1.00 12.46 ? 160 LEU A CG 1 ATOM 1259 C CD1 . LEU A 1 160 ? 19.712 -8.790 18.626 1.00 11.30 ? 160 LEU A CD1 1 ATOM 1260 C CD2 . LEU A 1 160 ? 19.050 -10.140 16.648 1.00 13.65 ? 160 LEU A CD2 1 ATOM 1261 N N . ILE A 1 161 ? 14.978 -6.586 16.863 1.00 16.94 ? 161 ILE A N 1 ATOM 1262 C CA . ILE A 1 161 ? 13.579 -6.313 17.201 1.00 16.79 ? 161 ILE A CA 1 ATOM 1263 C C . ILE A 1 161 ? 12.678 -6.332 15.971 1.00 20.31 ? 161 ILE A C 1 ATOM 1264 O O . ILE A 1 161 ? 11.464 -6.527 16.090 1.00 18.59 ? 161 ILE A O 1 ATOM 1265 C CB . ILE A 1 161 ? 13.388 -4.988 17.990 1.00 18.55 ? 161 ILE A CB 1 ATOM 1266 C CG1 . ILE A 1 161 ? 13.787 -3.775 17.144 1.00 17.34 ? 161 ILE A CG1 1 ATOM 1267 C CG2 . ILE A 1 161 ? 14.181 -5.037 19.285 1.00 17.38 ? 161 ILE A CG2 1 ATOM 1268 C CD1 . ILE A 1 161 ? 13.656 -2.450 17.877 1.00 17.09 ? 161 ILE A CD1 1 ATOM 1269 N N . HIS A 1 162 ? 13.264 -6.118 14.793 1.00 20.06 ? 162 HIS A N 1 ATOM 1270 C CA . HIS A 1 162 ? 12.488 -6.155 13.556 1.00 21.37 ? 162 HIS A CA 1 ATOM 1271 C C . HIS A 1 162 ? 12.280 -7.595 13.104 1.00 23.90 ? 162 HIS A C 1 ATOM 1272 O O . HIS A 1 162 ? 11.306 -7.896 12.420 1.00 25.36 ? 162 HIS A O 1 ATOM 1273 C CB . HIS A 1 162 ? 13.137 -5.315 12.459 1.00 21.13 ? 162 HIS A CB 1 ATOM 1274 C CG . HIS A 1 162 ? 12.784 -3.864 12.537 1.00 19.46 ? 162 HIS A CG 1 ATOM 1275 N ND1 . HIS A 1 162 ? 13.518 -2.955 13.265 1.00 17.03 ? 162 HIS A ND1 1 ATOM 1276 C CD2 . HIS A 1 162 ? 11.745 -3.170 12.012 1.00 17.18 ? 162 HIS A CD2 1 ATOM 1277 C CE1 . HIS A 1 162 ? 12.948 -1.765 13.191 1.00 19.49 ? 162 HIS A CE1 1 ATOM 1278 N NE2 . HIS A 1 162 ? 11.871 -1.872 12.435 1.00 16.66 ? 162 HIS A NE2 1 ATOM 1279 N N . GLU A 1 163 ? 13.209 -8.473 13.480 1.00 22.19 ? 163 GLU A N 1 ATOM 1280 C CA . GLU A 1 163 ? 13.102 -9.892 13.166 1.00 25.77 ? 163 GLU A CA 1 ATOM 1281 C C . GLU A 1 163 ? 11.895 -10.415 13.937 1.00 25.49 ? 163 GLU A C 1 ATOM 1282 O O . GLU A 1 163 ? 11.157 -11.269 13.452 1.00 29.64 ? 163 GLU A O 1 ATOM 1283 C CB . GLU A 1 163 ? 14.359 -10.638 13.620 1.00 31.23 ? 163 GLU A CB 1 ATOM 1284 C CG . GLU A 1 163 ? 15.385 -10.879 12.527 1.00 41.95 ? 163 GLU A CG 1 ATOM 1285 C CD . GLU A 1 163 ? 14.896 -11.866 11.476 1.00 54.94 ? 163 GLU A CD 1 ATOM 1286 O OE1 . GLU A 1 163 ? 14.238 -12.862 11.851 1.00 58.13 ? 163 GLU A OE1 1 ATOM 1287 O OE2 . GLU A 1 163 ? 15.162 -11.646 10.272 1.00 59.34 ? 163 GLU A OE2 1 ATOM 1288 N N . VAL A 1 164 ? 11.693 -9.871 15.134 1.00 22.87 ? 164 VAL A N 1 ATOM 1289 C CA . VAL A 1 164 ? 10.575 -10.255 15.984 1.00 20.92 ? 164 VAL A CA 1 ATOM 1290 C C . VAL A 1 164 ? 9.273 -9.677 15.424 1.00 28.41 ? 164 VAL A C 1 ATOM 1291 O O . VAL A 1 164 ? 8.242 -10.350 15.417 1.00 29.35 ? 164 VAL A O 1 ATOM 1292 C CB . VAL A 1 164 ? 10.775 -9.754 17.440 1.00 19.90 ? 164 VAL A CB 1 ATOM 1293 C CG1 . VAL A 1 164 ? 9.558 -10.094 18.297 1.00 16.40 ? 164 VAL A CG1 1 ATOM 1294 C CG2 . VAL A 1 164 ? 12.035 -10.365 18.041 1.00 14.12 ? 164 VAL A CG2 1 ATOM 1295 N N . LEU A 1 165 ? 9.330 -8.435 14.946 1.00 27.12 ? 165 LEU A N 1 ATOM 1296 C CA . LEU A 1 165 ? 8.154 -7.767 14.389 1.00 26.84 ? 165 LEU A CA 1 ATOM 1297 C C . LEU A 1 165 ? 7.706 -8.388 13.066 1.00 30.90 ? 165 LEU A C 1 ATOM 1298 O O . LEU A 1 165 ? 6.535 -8.718 12.887 1.00 30.74 ? 165 LEU A O 1 ATOM 1299 C CB . LEU A 1 165 ? 8.443 -6.278 14.180 1.00 26.41 ? 165 LEU A CB 1 ATOM 1300 C CG . LEU A 1 165 ? 7.319 -5.438 13.569 1.00 26.41 ? 165 LEU A CG 1 ATOM 1301 C CD1 . LEU A 1 165 ? 6.193 -5.259 14.570 1.00 25.87 ? 165 LEU A CD1 1 ATOM 1302 C CD2 . LEU A 1 165 ? 7.861 -4.090 13.140 1.00 27.12 ? 165 LEU A CD2 1 ATOM 1303 N N . ALA A 1 166 ? 8.649 -8.520 12.142 1.00 31.46 ? 166 ALA A N 1 ATOM 1304 C CA . ALA A 1 166 ? 8.392 -9.085 10.823 1.00 30.90 ? 166 ALA A CA 1 ATOM 1305 C C . ALA A 1 166 ? 9.403 -10.199 10.566 1.00 28.84 ? 166 ALA A C 1 ATOM 1306 O O . ALA A 1 166 ? 10.457 -9.967 9.973 1.00 26.85 ? 166 ALA A O 1 ATOM 1307 C CB . ALA A 1 166 ? 8.519 -7.999 9.758 1.00 24.89 ? 166 ALA A CB 1 ATOM 1308 N N . PRO A 1 167 ? 9.104 -11.420 11.045 1.00 28.75 ? 167 PRO A N 1 ATOM 1309 C CA . PRO A 1 167 ? 9.986 -12.581 10.873 1.00 28.20 ? 167 PRO A CA 1 ATOM 1310 C C . PRO A 1 167 ? 10.393 -12.789 9.417 1.00 27.27 ? 167 PRO A C 1 ATOM 1311 O O . PRO A 1 167 ? 9.550 -12.802 8.519 1.00 31.49 ? 167 PRO A O 1 ATOM 1312 C CB . PRO A 1 167 ? 9.124 -13.733 11.389 1.00 28.10 ? 167 PRO A CB 1 ATOM 1313 C CG . PRO A 1 167 ? 8.316 -13.082 12.462 1.00 26.81 ? 167 PRO A CG 1 ATOM 1314 C CD . PRO A 1 167 ? 7.894 -11.792 11.798 1.00 26.71 ? 167 PRO A CD 1 ATOM 1315 N N . GLY A 1 168 ? 11.696 -12.906 9.190 1.00 26.50 ? 168 GLY A N 1 ATOM 1316 C CA . GLY A 1 168 ? 12.200 -13.110 7.847 1.00 25.10 ? 168 GLY A CA 1 ATOM 1317 C C . GLY A 1 168 ? 12.401 -11.847 7.030 1.00 30.53 ? 168 GLY A C 1 ATOM 1318 O O . GLY A 1 168 ? 12.748 -11.929 5.855 1.00 29.45 ? 168 GLY A O 1 ATOM 1319 N N . CYS A 1 169 ? 12.193 -10.679 7.636 1.00 29.85 ? 169 CYS A N 1 ATOM 1320 C CA . CYS A 1 169 ? 12.371 -9.410 6.925 1.00 29.39 ? 169 CYS A CA 1 ATOM 1321 C C . CYS A 1 169 ? 13.805 -9.218 6.419 1.00 25.88 ? 169 CYS A C 1 ATOM 1322 O O . CYS A 1 169 ? 14.038 -8.450 5.489 1.00 33.52 ? 169 CYS A O 1 ATOM 1323 C CB . CYS A 1 169 ? 11.966 -8.223 7.813 1.00 30.10 ? 169 CYS A CB 1 ATOM 1324 S SG . CYS A 1 169 ? 12.993 -7.986 9.287 1.00 22.23 ? 169 CYS A SG 1 ATOM 1325 N N . LEU A 1 170 ? 14.758 -9.917 7.035 1.00 27.50 ? 170 LEU A N 1 ATOM 1326 C CA . LEU A 1 170 ? 16.168 -9.838 6.645 1.00 25.42 ? 170 LEU A CA 1 ATOM 1327 C C . LEU A 1 170 ? 16.587 -10.837 5.561 1.00 27.18 ? 170 LEU A C 1 ATOM 1328 O O . LEU A 1 170 ? 17.747 -10.845 5.142 1.00 24.27 ? 170 LEU A O 1 ATOM 1329 C CB . LEU A 1 170 ? 17.069 -10.023 7.868 1.00 24.92 ? 170 LEU A CB 1 ATOM 1330 C CG . LEU A 1 170 ? 17.552 -8.773 8.608 1.00 29.22 ? 170 LEU A CG 1 ATOM 1331 C CD1 . LEU A 1 170 ? 16.385 -7.864 8.965 1.00 26.39 ? 170 LEU A CD1 1 ATOM 1332 C CD2 . LEU A 1 170 ? 18.319 -9.194 9.853 1.00 25.70 ? 170 LEU A CD2 1 ATOM 1333 N N . ASP A 1 171 ? 15.654 -11.679 5.119 1.00 29.82 ? 171 ASP A N 1 ATOM 1334 C CA . ASP A 1 171 ? 15.938 -12.684 4.091 1.00 30.23 ? 171 ASP A CA 1 ATOM 1335 C C . ASP A 1 171 ? 16.437 -12.059 2.796 1.00 29.49 ? 171 ASP A C 1 ATOM 1336 O O . ASP A 1 171 ? 17.368 -12.568 2.170 1.00 30.95 ? 171 ASP A O 1 ATOM 1337 C CB . ASP A 1 171 ? 14.692 -13.525 3.797 1.00 31.47 ? 171 ASP A CB 1 ATOM 1338 C CG . ASP A 1 171 ? 14.366 -14.510 4.906 1.00 34.37 ? 171 ASP A CG 1 ATOM 1339 O OD1 . ASP A 1 171 ? 15.242 -14.771 5.762 1.00 36.67 ? 171 ASP A OD1 1 ATOM 1340 O OD2 . ASP A 1 171 ? 13.229 -15.034 4.910 1.00 30.92 ? 171 ASP A OD2 1 ATOM 1341 N N . ALA A 1 172 ? 15.827 -10.941 2.416 1.00 28.00 ? 172 ALA A N 1 ATOM 1342 C CA . ALA A 1 172 ? 16.192 -10.225 1.198 1.00 27.15 ? 172 ALA A CA 1 ATOM 1343 C C . ALA A 1 172 ? 17.515 -9.465 1.289 1.00 25.27 ? 172 ALA A C 1 ATOM 1344 O O . ALA A 1 172 ? 17.976 -8.899 0.298 1.00 29.11 ? 172 ALA A O 1 ATOM 1345 C CB . ALA A 1 172 ? 15.073 -9.267 0.816 1.00 30.36 ? 172 ALA A CB 1 ATOM 1346 N N . PHE A 1 173 ? 18.133 -9.461 2.469 1.00 25.07 ? 173 PHE A N 1 ATOM 1347 C CA . PHE A 1 173 ? 19.388 -8.742 2.672 1.00 20.75 ? 173 PHE A CA 1 ATOM 1348 C C . PHE A 1 173 ? 20.503 -9.646 3.186 1.00 25.58 ? 173 PHE A C 1 ATOM 1349 O O . PHE A 1 173 ? 20.754 -9.716 4.389 1.00 30.09 ? 173 PHE A O 1 ATOM 1350 C CB . PHE A 1 173 ? 19.161 -7.575 3.639 1.00 20.04 ? 173 PHE A CB 1 ATOM 1351 C CG . PHE A 1 173 ? 18.082 -6.626 3.198 1.00 21.17 ? 173 PHE A CG 1 ATOM 1352 C CD1 . PHE A 1 173 ? 18.353 -5.626 2.270 1.00 22.04 ? 173 PHE A CD1 1 ATOM 1353 C CD2 . PHE A 1 173 ? 16.783 -6.759 3.681 1.00 20.44 ? 173 PHE A CD2 1 ATOM 1354 C CE1 . PHE A 1 173 ? 17.346 -4.768 1.829 1.00 20.70 ? 173 PHE A CE1 1 ATOM 1355 C CE2 . PHE A 1 173 ? 15.767 -5.907 3.247 1.00 24.35 ? 173 PHE A CE2 1 ATOM 1356 C CZ . PHE A 1 173 ? 16.050 -4.911 2.317 1.00 22.90 ? 173 PHE A CZ 1 ATOM 1357 N N . PRO A 1 174 ? 21.226 -10.308 2.266 1.00 26.61 ? 174 PRO A N 1 ATOM 1358 C CA . PRO A 1 174 ? 22.326 -11.221 2.597 1.00 24.56 ? 174 PRO A CA 1 ATOM 1359 C C . PRO A 1 174 ? 23.421 -10.678 3.514 1.00 23.65 ? 174 PRO A C 1 ATOM 1360 O O . PRO A 1 174 ? 23.911 -11.401 4.380 1.00 27.88 ? 174 PRO A O 1 ATOM 1361 C CB . PRO A 1 174 ? 22.867 -11.624 1.221 1.00 23.89 ? 174 PRO A CB 1 ATOM 1362 C CG . PRO A 1 174 ? 22.428 -10.507 0.318 1.00 25.80 ? 174 PRO A CG 1 ATOM 1363 C CD . PRO A 1 174 ? 21.052 -10.214 0.808 1.00 25.20 ? 174 PRO A CD 1 ATOM 1364 N N . LEU A 1 175 ? 23.812 -9.421 3.320 1.00 24.36 ? 175 LEU A N 1 ATOM 1365 C CA . LEU A 1 175 ? 24.853 -8.810 4.147 1.00 21.66 ? 175 LEU A CA 1 ATOM 1366 C C . LEU A 1 175 ? 24.374 -8.521 5.573 1.00 22.29 ? 175 LEU A C 1 ATOM 1367 O O . LEU A 1 175 ? 25.099 -8.764 6.536 1.00 14.38 ? 175 LEU A O 1 ATOM 1368 C CB . LEU A 1 175 ? 25.387 -7.538 3.486 1.00 23.93 ? 175 LEU A CB 1 ATOM 1369 C CG . LEU A 1 175 ? 26.597 -7.654 2.549 1.00 25.32 ? 175 LEU A CG 1 ATOM 1370 C CD1 . LEU A 1 175 ? 26.691 -9.025 1.906 1.00 24.32 ? 175 LEU A CD1 1 ATOM 1371 C CD2 . LEU A 1 175 ? 26.524 -6.570 1.501 1.00 20.24 ? 175 LEU A CD2 1 ATOM 1372 N N . LEU A 1 176 ? 23.151 -8.015 5.706 1.00 19.43 ? 176 LEU A N 1 ATOM 1373 C CA . LEU A 1 176 ? 22.601 -7.726 7.025 1.00 20.80 ? 176 LEU A CA 1 ATOM 1374 C C . LEU A 1 176 ? 22.419 -9.024 7.810 1.00 26.52 ? 176 LEU A C 1 ATOM 1375 O O . LEU A 1 176 ? 22.737 -9.080 8.997 1.00 26.72 ? 176 LEU A O 1 ATOM 1376 C CB . LEU A 1 176 ? 21.270 -6.976 6.917 1.00 15.04 ? 176 LEU A CB 1 ATOM 1377 C CG . LEU A 1 176 ? 21.346 -5.504 6.497 1.00 15.49 ? 176 LEU A CG 1 ATOM 1378 C CD1 . LEU A 1 176 ? 19.948 -4.931 6.360 1.00 16.94 ? 176 LEU A CD1 1 ATOM 1379 C CD2 . LEU A 1 176 ? 22.152 -4.707 7.510 1.00 19.22 ? 176 LEU A CD2 1 ATOM 1380 N N . SER A 1 177 ? 21.942 -10.070 7.134 1.00 22.83 ? 177 SER A N 1 ATOM 1381 C CA . SER A 1 177 ? 21.735 -11.376 7.763 1.00 21.26 ? 177 SER A CA 1 ATOM 1382 C C . SER A 1 177 ? 23.046 -11.955 8.289 1.00 23.19 ? 177 SER A C 1 ATOM 1383 O O . SER A 1 177 ? 23.110 -12.438 9.423 1.00 21.54 ? 177 SER A O 1 ATOM 1384 C CB . SER A 1 177 ? 21.107 -12.356 6.773 1.00 23.24 ? 177 SER A CB 1 ATOM 1385 O OG . SER A 1 177 ? 19.812 -11.933 6.397 1.00 22.38 ? 177 SER A OG 1 ATOM 1386 N N . ALA A 1 178 ? 24.087 -11.909 7.462 1.00 10.68 ? 178 ALA A N 1 ATOM 1387 C CA . ALA A 1 178 ? 25.392 -12.423 7.865 1.00 15.92 ? 178 ALA A CA 1 ATOM 1388 C C . ALA A 1 178 ? 25.938 -11.572 9.010 1.00 22.27 ? 178 ALA A C 1 ATOM 1389 O O . ALA A 1 178 ? 26.549 -12.088 9.946 1.00 25.04 ? 178 ALA A O 1 ATOM 1390 C CB . ALA A 1 178 ? 26.355 -12.398 6.684 1.00 8.34 ? 178 ALA A CB 1 ATOM 1391 N N . TYR A 1 179 ? 25.713 -10.262 8.912 1.00 27.13 ? 179 TYR A N 1 ATOM 1392 C CA . TYR A 1 179 ? 26.153 -9.289 9.909 1.00 22.12 ? 179 TYR A CA 1 ATOM 1393 C C . TYR A 1 179 ? 25.547 -9.630 11.271 1.00 17.98 ? 179 TYR A C 1 ATOM 1394 O O . TYR A 1 179 ? 26.266 -9.713 12.269 1.00 21.41 ? 179 TYR A O 1 ATOM 1395 C CB . TYR A 1 179 ? 25.733 -7.889 9.447 1.00 21.29 ? 179 TYR A CB 1 ATOM 1396 C CG . TYR A 1 179 ? 25.950 -6.759 10.430 1.00 17.70 ? 179 TYR A CG 1 ATOM 1397 C CD1 . TYR A 1 179 ? 27.218 -6.215 10.639 1.00 16.63 ? 179 TYR A CD1 1 ATOM 1398 C CD2 . TYR A 1 179 ? 24.871 -6.191 11.106 1.00 19.36 ? 179 TYR A CD2 1 ATOM 1399 C CE1 . TYR A 1 179 ? 27.401 -5.124 11.495 1.00 18.66 ? 179 TYR A CE1 1 ATOM 1400 C CE2 . TYR A 1 179 ? 25.043 -5.108 11.961 1.00 17.79 ? 179 TYR A CE2 1 ATOM 1401 C CZ . TYR A 1 179 ? 26.306 -4.578 12.151 1.00 19.82 ? 179 TYR A CZ 1 ATOM 1402 O OH . TYR A 1 179 ? 26.461 -3.498 12.990 1.00 20.41 ? 179 TYR A OH 1 ATOM 1403 N N . VAL A 1 180 ? 24.236 -9.866 11.291 1.00 13.07 ? 180 VAL A N 1 ATOM 1404 C CA . VAL A 1 180 ? 23.515 -10.225 12.511 1.00 19.19 ? 180 VAL A CA 1 ATOM 1405 C C . VAL A 1 180 ? 24.049 -11.533 13.104 1.00 24.64 ? 180 VAL A C 1 ATOM 1406 O O . VAL A 1 180 ? 24.326 -11.605 14.299 1.00 27.93 ? 180 VAL A O 1 ATOM 1407 C CB . VAL A 1 180 ? 21.992 -10.363 12.249 1.00 18.03 ? 180 VAL A CB 1 ATOM 1408 C CG1 . VAL A 1 180 ? 21.289 -10.990 13.449 1.00 19.19 ? 180 VAL A CG1 1 ATOM 1409 C CG2 . VAL A 1 180 ? 21.395 -9.008 11.960 1.00 18.40 ? 180 VAL A CG2 1 ATOM 1410 N N . GLY A 1 181 ? 24.214 -12.554 12.263 1.00 26.02 ? 181 GLY A N 1 ATOM 1411 C CA . GLY A 1 181 ? 24.720 -13.831 12.737 1.00 17.35 ? 181 GLY A CA 1 ATOM 1412 C C . GLY A 1 181 ? 26.131 -13.720 13.288 1.00 22.26 ? 181 GLY A C 1 ATOM 1413 O O . GLY A 1 181 ? 26.453 -14.290 14.331 1.00 22.16 ? 181 GLY A O 1 ATOM 1414 N N . ARG A 1 182 ? 26.963 -12.951 12.596 1.00 17.36 ? 182 ARG A N 1 ATOM 1415 C CA . ARG A 1 182 ? 28.350 -12.743 12.981 1.00 19.45 ? 182 ARG A CA 1 ATOM 1416 C C . ARG A 1 182 ? 28.482 -12.033 14.334 1.00 24.92 ? 182 ARG A C 1 ATOM 1417 O O . ARG A 1 182 ? 29.239 -12.474 15.204 1.00 25.69 ? 182 ARG A O 1 ATOM 1418 C CB . ARG A 1 182 ? 29.061 -11.936 11.895 1.00 17.30 ? 182 ARG A CB 1 ATOM 1419 C CG . ARG A 1 182 ? 30.575 -11.862 12.029 1.00 20.82 ? 182 ARG A CG 1 ATOM 1420 C CD . ARG A 1 182 ? 31.154 -10.905 10.993 1.00 22.91 ? 182 ARG A CD 1 ATOM 1421 N NE . ARG A 1 182 ? 30.577 -11.137 9.675 1.00 30.38 ? 182 ARG A NE 1 ATOM 1422 C CZ . ARG A 1 182 ? 29.982 -10.204 8.938 1.00 32.33 ? 182 ARG A CZ 1 ATOM 1423 N NH1 . ARG A 1 182 ? 29.886 -8.954 9.369 1.00 29.87 ? 182 ARG A NH1 1 ATOM 1424 N NH2 . ARG A 1 182 ? 29.424 -10.540 7.786 1.00 33.52 ? 182 ARG A NH2 1 ATOM 1425 N N . LEU A 1 183 ? 27.754 -10.931 14.507 1.00 25.45 ? 183 LEU A N 1 ATOM 1426 C CA . LEU A 1 183 ? 27.813 -10.182 15.762 1.00 25.98 ? 183 LEU A CA 1 ATOM 1427 C C . LEU A 1 183 ? 27.200 -10.962 16.926 1.00 27.07 ? 183 LEU A C 1 ATOM 1428 O O . LEU A 1 183 ? 27.736 -10.949 18.032 1.00 26.87 ? 183 LEU A O 1 ATOM 1429 C CB . LEU A 1 183 ? 27.141 -8.813 15.621 1.00 22.10 ? 183 LEU A CB 1 ATOM 1430 C CG . LEU A 1 183 ? 27.844 -7.758 14.758 1.00 24.72 ? 183 LEU A CG 1 ATOM 1431 C CD1 . LEU A 1 183 ? 27.252 -6.391 15.057 1.00 24.76 ? 183 LEU A CD1 1 ATOM 1432 C CD2 . LEU A 1 183 ? 29.336 -7.732 15.045 1.00 25.15 ? 183 LEU A CD2 1 ATOM 1433 N N . SER A 1 184 ? 26.090 -11.650 16.661 1.00 26.24 ? 184 SER A N 1 ATOM 1434 C CA . SER A 1 184 ? 25.405 -12.458 17.666 1.00 24.33 ? 184 SER A CA 1 ATOM 1435 C C . SER A 1 184 ? 26.284 -13.607 18.155 1.00 29.02 ? 184 SER A C 1 ATOM 1436 O O . SER A 1 184 ? 25.998 -14.209 19.194 1.00 33.54 ? 184 SER A O 1 ATOM 1437 C CB . SER A 1 184 ? 24.118 -13.055 17.089 1.00 20.98 ? 184 SER A CB 1 ATOM 1438 O OG . SER A 1 184 ? 23.195 -12.052 16.720 1.00 28.40 ? 184 SER A OG 1 ATOM 1439 N N . ALA A 1 185 ? 27.334 -13.917 17.395 1.00 24.81 ? 185 ALA A N 1 ATOM 1440 C CA . ALA A 1 185 ? 28.244 -15.008 17.733 1.00 27.24 ? 185 ALA A CA 1 ATOM 1441 C C . ALA A 1 185 ? 29.406 -14.603 18.636 1.00 27.33 ? 185 ALA A C 1 ATOM 1442 O O . ALA A 1 185 ? 30.141 -15.462 19.126 1.00 31.32 ? 185 ALA A O 1 ATOM 1443 C CB . ALA A 1 185 ? 28.772 -15.663 16.461 1.00 26.67 ? 185 ALA A CB 1 ATOM 1444 N N . ARG A 1 186 ? 29.591 -13.302 18.841 1.00 26.43 ? 186 ARG A N 1 ATOM 1445 C CA . ARG A 1 186 ? 30.670 -12.824 19.702 1.00 21.21 ? 186 ARG A CA 1 ATOM 1446 C C . ARG A 1 186 ? 30.437 -13.421 21.092 1.00 24.23 ? 186 ARG A C 1 ATOM 1447 O O . ARG A 1 186 ? 29.338 -13.329 21.632 1.00 20.12 ? 186 ARG A O 1 ATOM 1448 C CB . ARG A 1 186 ? 30.678 -11.294 19.734 1.00 17.88 ? 186 ARG A CB 1 ATOM 1449 C CG . ARG A 1 186 ? 30.950 -10.678 18.362 1.00 22.26 ? 186 ARG A CG 1 ATOM 1450 C CD . ARG A 1 186 ? 30.751 -9.165 18.340 1.00 18.35 ? 186 ARG A CD 1 ATOM 1451 N NE . ARG A 1 186 ? 31.630 -8.475 19.278 1.00 13.60 ? 186 ARG A NE 1 ATOM 1452 C CZ . ARG A 1 186 ? 32.867 -8.070 19.000 1.00 16.80 ? 186 ARG A CZ 1 ATOM 1453 N NH1 . ARG A 1 186 ? 33.390 -8.268 17.797 1.00 14.21 ? 186 ARG A NH1 1 ATOM 1454 N NH2 . ARG A 1 186 ? 33.580 -7.452 19.929 1.00 12.32 ? 186 ARG A NH2 1 ATOM 1455 N N . PRO A 1 187 ? 31.467 -14.067 21.668 1.00 24.49 ? 187 PRO A N 1 ATOM 1456 C CA . PRO A 1 187 ? 31.462 -14.723 22.984 1.00 25.34 ? 187 PRO A CA 1 ATOM 1457 C C . PRO A 1 187 ? 30.621 -14.082 24.097 1.00 25.65 ? 187 PRO A C 1 ATOM 1458 O O . PRO A 1 187 ? 29.605 -14.650 24.519 1.00 21.08 ? 187 PRO A O 1 ATOM 1459 C CB . PRO A 1 187 ? 32.944 -14.761 23.339 1.00 26.35 ? 187 PRO A CB 1 ATOM 1460 C CG . PRO A 1 187 ? 33.573 -15.001 22.018 1.00 27.47 ? 187 PRO A CG 1 ATOM 1461 C CD . PRO A 1 187 ? 32.836 -14.028 21.121 1.00 23.82 ? 187 PRO A CD 1 ATOM 1462 N N . LYS A 1 188 ? 31.047 -12.910 24.567 1.00 24.65 ? 188 LYS A N 1 ATOM 1463 C CA . LYS A 1 188 ? 30.346 -12.198 25.636 1.00 23.53 ? 188 LYS A CA 1 ATOM 1464 C C . LYS A 1 188 ? 28.930 -11.764 25.267 1.00 22.47 ? 188 LYS A C 1 ATOM 1465 O O . LYS A 1 188 ? 28.028 -11.812 26.105 1.00 27.00 ? 188 LYS A O 1 ATOM 1466 C CB . LYS A 1 188 ? 31.165 -10.994 26.095 1.00 23.44 ? 188 LYS A CB 1 ATOM 1467 C CG . LYS A 1 188 ? 32.523 -11.372 26.653 1.00 25.87 ? 188 LYS A CG 1 ATOM 1468 C CD . LYS A 1 188 ? 33.392 -10.154 26.897 1.00 36.57 ? 188 LYS A CD 1 ATOM 1469 C CE . LYS A 1 188 ? 34.796 -10.565 27.302 1.00 42.81 ? 188 LYS A CE 1 ATOM 1470 N NZ . LYS A 1 188 ? 34.766 -11.441 28.509 1.00 55.19 ? 188 LYS A NZ 1 ATOM 1471 N N . LEU A 1 189 ? 28.733 -11.367 24.012 1.00 24.60 ? 189 LEU A N 1 ATOM 1472 C CA . LEU A 1 189 ? 27.420 -10.930 23.537 1.00 21.70 ? 189 LEU A CA 1 ATOM 1473 C C . LEU A 1 189 ? 26.445 -12.096 23.449 1.00 20.13 ? 189 LEU A C 1 ATOM 1474 O O . LEU A 1 189 ? 25.268 -11.956 23.786 1.00 25.43 ? 189 LEU A O 1 ATOM 1475 C CB . LEU A 1 189 ? 27.535 -10.271 22.160 1.00 23.48 ? 189 LEU A CB 1 ATOM 1476 C CG . LEU A 1 189 ? 26.811 -8.942 21.938 1.00 24.03 ? 189 LEU A CG 1 ATOM 1477 C CD1 . LEU A 1 189 ? 26.780 -8.646 20.451 1.00 23.32 ? 189 LEU A CD1 1 ATOM 1478 C CD2 . LEU A 1 189 ? 25.402 -8.982 22.493 1.00 22.64 ? 189 LEU A CD2 1 ATOM 1479 N N . LYS A 1 190 ? 26.941 -13.238 22.976 1.00 19.82 ? 190 LYS A N 1 ATOM 1480 C CA . LYS A 1 190 ? 26.128 -14.445 22.838 1.00 23.37 ? 190 LYS A CA 1 ATOM 1481 C C . LYS A 1 190 ? 25.623 -14.899 24.203 1.00 19.46 ? 190 LYS A C 1 ATOM 1482 O O . LYS A 1 190 ? 24.449 -15.241 24.355 1.00 20.67 ? 190 LYS A O 1 ATOM 1483 C CB . LYS A 1 190 ? 26.936 -15.569 22.187 1.00 22.74 ? 190 LYS A CB 1 ATOM 1484 C CG . LYS A 1 190 ? 26.124 -16.825 21.959 1.00 27.44 ? 190 LYS A CG 1 ATOM 1485 C CD . LYS A 1 190 ? 26.974 -17.943 21.419 1.00 35.89 ? 190 LYS A CD 1 ATOM 1486 C CE . LYS A 1 190 ? 26.130 -19.186 21.199 1.00 44.62 ? 190 LYS A CE 1 ATOM 1487 N NZ . LYS A 1 190 ? 26.952 -20.310 20.677 1.00 50.83 ? 190 LYS A NZ 1 ATOM 1488 N N . ALA A 1 191 ? 26.522 -14.886 25.187 1.00 18.54 ? 191 ALA A N 1 ATOM 1489 C CA . ALA A 1 191 ? 26.197 -15.275 26.558 1.00 21.86 ? 191 ALA A CA 1 ATOM 1490 C C . ALA A 1 191 ? 25.126 -14.342 27.125 1.00 23.54 ? 191 ALA A C 1 ATOM 1491 O O . ALA A 1 191 ? 24.137 -14.797 27.704 1.00 28.98 ? 191 ALA A O 1 ATOM 1492 C CB . ALA A 1 191 ? 27.451 -15.229 27.418 1.00 14.77 ? 191 ALA A CB 1 ATOM 1493 N N . PHE A 1 192 ? 25.310 -13.040 26.913 1.00 25.87 ? 192 PHE A N 1 ATOM 1494 C CA . PHE A 1 192 ? 24.362 -12.033 27.392 1.00 23.23 ? 192 PHE A CA 1 ATOM 1495 C C . PHE A 1 192 ? 22.983 -12.159 26.746 1.00 18.39 ? 192 PHE A C 1 ATOM 1496 O O . PHE A 1 192 ? 21.969 -12.084 27.434 1.00 20.40 ? 192 PHE A O 1 ATOM 1497 C CB . PHE A 1 192 ? 24.919 -10.616 27.172 1.00 24.89 ? 192 PHE A CB 1 ATOM 1498 C CG . PHE A 1 192 ? 23.961 -9.517 27.558 1.00 22.37 ? 192 PHE A CG 1 ATOM 1499 C CD1 . PHE A 1 192 ? 23.748 -9.200 28.897 1.00 20.87 ? 192 PHE A CD1 1 ATOM 1500 C CD2 . PHE A 1 192 ? 23.250 -8.820 26.584 1.00 20.65 ? 192 PHE A CD2 1 ATOM 1501 C CE1 . PHE A 1 192 ? 22.840 -8.208 29.261 1.00 20.15 ? 192 PHE A CE1 1 ATOM 1502 C CE2 . PHE A 1 192 ? 22.339 -7.826 26.937 1.00 21.20 ? 192 PHE A CE2 1 ATOM 1503 C CZ . PHE A 1 192 ? 22.133 -7.520 28.280 1.00 20.41 ? 192 PHE A CZ 1 ATOM 1504 N N . LEU A 1 193 ? 22.946 -12.350 25.430 1.00 20.75 ? 193 LEU A N 1 ATOM 1505 C CA . LEU A 1 193 ? 21.676 -12.472 24.714 1.00 20.80 ? 193 LEU A CA 1 ATOM 1506 C C . LEU A 1 193 ? 20.875 -13.703 25.121 1.00 19.55 ? 193 LEU A C 1 ATOM 1507 O O . LEU A 1 193 ? 19.658 -13.741 24.947 1.00 18.50 ? 193 LEU A O 1 ATOM 1508 C CB . LEU A 1 193 ? 21.903 -12.477 23.198 1.00 21.35 ? 193 LEU A CB 1 ATOM 1509 C CG . LEU A 1 193 ? 22.401 -11.172 22.576 1.00 22.49 ? 193 LEU A CG 1 ATOM 1510 C CD1 . LEU A 1 193 ? 22.690 -11.381 21.100 1.00 24.89 ? 193 LEU A CD1 1 ATOM 1511 C CD2 . LEU A 1 193 ? 21.369 -10.074 22.768 1.00 20.59 ? 193 LEU A CD2 1 ATOM 1512 N N . ALA A 1 194 ? 21.557 -14.699 25.676 1.00 21.46 ? 194 ALA A N 1 ATOM 1513 C CA . ALA A 1 194 ? 20.897 -15.928 26.099 1.00 24.95 ? 194 ALA A CA 1 ATOM 1514 C C . ALA A 1 194 ? 20.485 -15.922 27.572 1.00 25.86 ? 194 ALA A C 1 ATOM 1515 O O . ALA A 1 194 ? 19.689 -16.761 27.993 1.00 26.94 ? 194 ALA A O 1 ATOM 1516 C CB . ALA A 1 194 ? 21.795 -17.124 25.811 1.00 19.38 ? 194 ALA A CB 1 ATOM 1517 N N . SER A 1 195 ? 21.010 -14.967 28.339 1.00 27.60 ? 195 SER A N 1 ATOM 1518 C CA . SER A 1 195 ? 20.725 -14.857 29.776 1.00 24.45 ? 195 SER A CA 1 ATOM 1519 C C . SER A 1 195 ? 19.299 -14.406 30.112 1.00 26.28 ? 195 SER A C 1 ATOM 1520 O O . SER A 1 195 ? 18.633 -13.767 29.298 1.00 30.32 ? 195 SER A O 1 ATOM 1521 C CB . SER A 1 195 ? 21.724 -13.899 30.429 1.00 26.01 ? 195 SER A CB 1 ATOM 1522 O OG . SER A 1 195 ? 21.421 -12.548 30.115 1.00 25.65 ? 195 SER A OG 1 ATOM 1523 N N . PRO A 1 196 ? 18.820 -14.733 31.332 1.00 24.59 ? 196 PRO A N 1 ATOM 1524 C CA . PRO A 1 196 ? 17.472 -14.362 31.795 1.00 24.19 ? 196 PRO A CA 1 ATOM 1525 C C . PRO A 1 196 ? 17.343 -12.843 31.883 1.00 24.62 ? 196 PRO A C 1 ATOM 1526 O O . PRO A 1 196 ? 16.266 -12.277 31.687 1.00 26.10 ? 196 PRO A O 1 ATOM 1527 C CB . PRO A 1 196 ? 17.414 -14.980 33.196 1.00 24.24 ? 196 PRO A CB 1 ATOM 1528 C CG . PRO A 1 196 ? 18.372 -16.125 33.115 1.00 27.98 ? 196 PRO A CG 1 ATOM 1529 C CD . PRO A 1 196 ? 19.517 -15.528 32.353 1.00 24.65 ? 196 PRO A CD 1 ATOM 1530 N N . GLU A 1 197 ? 18.467 -12.206 32.196 1.00 19.70 ? 197 GLU A N 1 ATOM 1531 C CA . GLU A 1 197 ? 18.591 -10.759 32.328 1.00 23.50 ? 197 GLU A CA 1 ATOM 1532 C C . GLU A 1 197 ? 18.065 -10.048 31.080 1.00 24.13 ? 197 GLU A C 1 ATOM 1533 O O . GLU A 1 197 ? 17.408 -9.007 31.169 1.00 26.91 ? 197 GLU A O 1 ATOM 1534 C CB . GLU A 1 197 ? 20.067 -10.439 32.517 1.00 22.94 ? 197 GLU A CB 1 ATOM 1535 C CG . GLU A 1 197 ? 20.387 -9.061 33.008 1.00 31.92 ? 197 GLU A CG 1 ATOM 1536 C CD . GLU A 1 197 ? 21.879 -8.869 33.215 1.00 31.00 ? 197 GLU A CD 1 ATOM 1537 O OE1 . GLU A 1 197 ? 22.582 -9.848 33.558 1.00 33.33 ? 197 GLU A OE1 1 ATOM 1538 O OE2 . GLU A 1 197 ? 22.359 -7.736 33.025 1.00 37.43 ? 197 GLU A OE2 1 ATOM 1539 N N . TYR A 1 198 ? 18.368 -10.627 29.921 1.00 25.29 ? 198 TYR A N 1 ATOM 1540 C CA . TYR A 1 198 ? 17.945 -10.092 28.634 1.00 18.96 ? 198 TYR A CA 1 ATOM 1541 C C . TYR A 1 198 ? 16.641 -10.738 28.163 1.00 20.57 ? 198 TYR A C 1 ATOM 1542 O O . TYR A 1 198 ? 15.644 -10.053 27.929 1.00 22.66 ? 198 TYR A O 1 ATOM 1543 C CB . TYR A 1 198 ? 19.059 -10.318 27.595 1.00 22.12 ? 198 TYR A CB 1 ATOM 1544 C CG . TYR A 1 198 ? 18.697 -9.913 26.178 1.00 26.53 ? 198 TYR A CG 1 ATOM 1545 C CD1 . TYR A 1 198 ? 18.924 -8.613 25.720 1.00 28.57 ? 198 TYR A CD1 1 ATOM 1546 C CD2 . TYR A 1 198 ? 18.109 -10.826 25.300 1.00 25.80 ? 198 TYR A CD2 1 ATOM 1547 C CE1 . TYR A 1 198 ? 18.567 -8.233 24.423 1.00 29.22 ? 198 TYR A CE1 1 ATOM 1548 C CE2 . TYR A 1 198 ? 17.752 -10.459 24.010 1.00 28.53 ? 198 TYR A CE2 1 ATOM 1549 C CZ . TYR A 1 198 ? 17.981 -9.163 23.577 1.00 29.40 ? 198 TYR A CZ 1 ATOM 1550 O OH . TYR A 1 198 ? 17.608 -8.801 22.305 1.00 31.79 ? 198 TYR A OH 1 ATOM 1551 N N . VAL A 1 199 ? 16.660 -12.063 28.048 1.00 24.03 ? 199 VAL A N 1 ATOM 1552 C CA . VAL A 1 199 ? 15.518 -12.845 27.577 1.00 17.51 ? 199 VAL A CA 1 ATOM 1553 C C . VAL A 1 199 ? 14.191 -12.642 28.301 1.00 16.40 ? 199 VAL A C 1 ATOM 1554 O O . VAL A 1 199 ? 13.144 -12.566 27.661 1.00 20.26 ? 199 VAL A O 1 ATOM 1555 C CB . VAL A 1 199 ? 15.863 -14.360 27.559 1.00 18.17 ? 199 VAL A CB 1 ATOM 1556 C CG1 . VAL A 1 199 ? 14.647 -15.186 27.192 1.00 13.57 ? 199 VAL A CG1 1 ATOM 1557 C CG2 . VAL A 1 199 ? 16.992 -14.625 26.577 1.00 13.24 ? 199 VAL A CG2 1 ATOM 1558 N N . ASN A 1 200 ? 14.224 -12.534 29.626 1.00 20.36 ? 200 ASN A N 1 ATOM 1559 C CA . ASN A 1 200 ? 12.987 -12.388 30.396 1.00 24.71 ? 200 ASN A CA 1 ATOM 1560 C C . ASN A 1 200 ? 12.413 -10.980 30.533 1.00 24.30 ? 200 ASN A C 1 ATOM 1561 O O . ASN A 1 200 ? 11.457 -10.756 31.277 1.00 26.01 ? 200 ASN A O 1 ATOM 1562 C CB . ASN A 1 200 ? 13.130 -13.064 31.760 1.00 23.91 ? 200 ASN A CB 1 ATOM 1563 C CG . ASN A 1 200 ? 13.303 -14.563 31.640 1.00 24.69 ? 200 ASN A CG 1 ATOM 1564 O OD1 . ASN A 1 200 ? 12.738 -15.191 30.744 1.00 27.46 ? 200 ASN A OD1 1 ATOM 1565 N ND2 . ASN A 1 200 ? 14.106 -15.140 32.523 1.00 19.32 ? 200 ASN A ND2 1 ATOM 1566 N N . LEU A 1 201 ? 12.986 -10.043 29.790 1.00 25.32 ? 201 LEU A N 1 ATOM 1567 C CA . LEU A 1 201 ? 12.527 -8.663 29.793 1.00 21.92 ? 201 LEU A CA 1 ATOM 1568 C C . LEU A 1 201 ? 11.732 -8.437 28.512 1.00 19.52 ? 201 LEU A C 1 ATOM 1569 O O . LEU A 1 201 ? 12.146 -8.880 27.439 1.00 19.36 ? 201 LEU A O 1 ATOM 1570 C CB . LEU A 1 201 ? 13.734 -7.730 29.805 1.00 19.53 ? 201 LEU A CB 1 ATOM 1571 C CG . LEU A 1 201 ? 13.899 -6.754 30.964 1.00 23.03 ? 201 LEU A CG 1 ATOM 1572 C CD1 . LEU A 1 201 ? 13.669 -7.450 32.294 1.00 12.43 ? 201 LEU A CD1 1 ATOM 1573 C CD2 . LEU A 1 201 ? 15.289 -6.146 30.895 1.00 20.31 ? 201 LEU A CD2 1 ATOM 1574 N N . PRO A 1 202 ? 10.548 -7.811 28.609 1.00 20.25 ? 202 PRO A N 1 ATOM 1575 C CA . PRO A 1 202 ? 9.763 -7.568 27.393 1.00 20.74 ? 202 PRO A CA 1 ATOM 1576 C C . PRO A 1 202 ? 10.473 -6.499 26.554 1.00 21.47 ? 202 PRO A C 1 ATOM 1577 O O . PRO A 1 202 ? 11.210 -5.676 27.097 1.00 19.63 ? 202 PRO A O 1 ATOM 1578 C CB . PRO A 1 202 ? 8.428 -7.063 27.944 1.00 19.86 ? 202 PRO A CB 1 ATOM 1579 C CG . PRO A 1 202 ? 8.824 -6.373 29.207 1.00 18.81 ? 202 PRO A CG 1 ATOM 1580 C CD . PRO A 1 202 ? 9.831 -7.328 29.804 1.00 16.60 ? 202 PRO A CD 1 ATOM 1581 N N . ILE A 1 203 ? 10.291 -6.535 25.238 1.00 22.14 ? 203 ILE A N 1 ATOM 1582 C CA . ILE A 1 203 ? 10.942 -5.559 24.363 1.00 21.07 ? 203 ILE A CA 1 ATOM 1583 C C . ILE A 1 203 ? 10.426 -4.145 24.631 1.00 20.67 ? 203 ILE A C 1 ATOM 1584 O O . ILE A 1 203 ? 11.210 -3.218 24.854 1.00 20.99 ? 203 ILE A O 1 ATOM 1585 C CB . ILE A 1 203 ? 10.748 -5.911 22.858 1.00 19.42 ? 203 ILE A CB 1 ATOM 1586 C CG1 . ILE A 1 203 ? 11.470 -7.222 22.533 1.00 21.91 ? 203 ILE A CG1 1 ATOM 1587 C CG2 . ILE A 1 203 ? 11.290 -4.792 21.975 1.00 16.48 ? 203 ILE A CG2 1 ATOM 1588 C CD1 . ILE A 1 203 ? 11.310 -7.677 21.095 1.00 23.11 ? 203 ILE A CD1 1 ATOM 1589 N N . ASN A 1 204 ? 9.104 -4.005 24.642 1.00 18.80 ? 204 ASN A N 1 ATOM 1590 C CA . ASN A 1 204 ? 8.464 -2.718 24.868 1.00 22.71 ? 204 ASN A CA 1 ATOM 1591 C C . ASN A 1 204 ? 7.588 -2.685 26.121 1.00 24.23 ? 204 ASN A C 1 ATOM 1592 O O . ASN A 1 204 ? 7.205 -3.725 26.660 1.00 21.79 ? 204 ASN A O 1 ATOM 1593 C CB . ASN A 1 204 ? 7.649 -2.329 23.628 1.00 24.47 ? 204 ASN A CB 1 ATOM 1594 C CG . ASN A 1 204 ? 8.483 -2.377 22.354 1.00 24.50 ? 204 ASN A CG 1 ATOM 1595 O OD1 . ASN A 1 204 ? 9.494 -1.685 22.239 1.00 18.23 ? 204 ASN A OD1 1 ATOM 1596 N ND2 . ASN A 1 204 ? 8.087 -3.225 21.414 1.00 21.47 ? 204 ASN A ND2 1 ATOM 1597 N N . GLY A 1 205 ? 7.276 -1.473 26.569 1.00 26.71 ? 205 GLY A N 1 ATOM 1598 C CA . GLY A 1 205 ? 6.467 -1.289 27.758 1.00 25.69 ? 205 GLY A CA 1 ATOM 1599 C C . GLY A 1 205 ? 4.988 -1.609 27.656 1.00 29.15 ? 205 GLY A C 1 ATOM 1600 O O . GLY A 1 205 ? 4.303 -1.633 28.676 1.00 34.75 ? 205 GLY A O 1 ATOM 1601 N N . ASN A 1 206 ? 4.477 -1.855 26.453 1.00 27.42 ? 206 ASN A N 1 ATOM 1602 C CA . ASN A 1 206 ? 3.057 -2.164 26.303 1.00 27.33 ? 206 ASN A CA 1 ATOM 1603 C C . ASN A 1 206 ? 2.778 -3.617 25.911 1.00 31.61 ? 206 ASN A C 1 ATOM 1604 O O . ASN A 1 206 ? 1.663 -3.958 25.508 1.00 32.48 ? 206 ASN A O 1 ATOM 1605 C CB . ASN A 1 206 ? 2.381 -1.197 25.319 1.00 27.41 ? 206 ASN A CB 1 ATOM 1606 C CG . ASN A 1 206 ? 2.868 -1.369 23.887 1.00 26.48 ? 206 ASN A CG 1 ATOM 1607 O OD1 . ASN A 1 206 ? 3.888 -2.011 23.635 1.00 25.11 ? 206 ASN A OD1 1 ATOM 1608 N ND2 . ASN A 1 206 ? 2.133 -0.798 22.943 1.00 22.41 ? 206 ASN A ND2 1 ATOM 1609 N N . GLY A 1 207 ? 3.797 -4.466 26.018 1.00 33.03 ? 207 GLY A N 1 ATOM 1610 C CA . GLY A 1 207 ? 3.631 -5.870 25.685 1.00 37.73 ? 207 GLY A CA 1 ATOM 1611 C C . GLY A 1 207 ? 3.508 -6.198 24.208 1.00 40.19 ? 207 GLY A C 1 ATOM 1612 O O . GLY A 1 207 ? 3.250 -7.348 23.847 1.00 44.39 ? 207 GLY A O 1 ATOM 1613 N N . LYS A 1 208 ? 3.653 -5.195 23.349 1.00 38.77 ? 208 LYS A N 1 ATOM 1614 C CA . LYS A 1 208 ? 3.575 -5.423 21.910 1.00 32.12 ? 208 LYS A CA 1 ATOM 1615 C C . LYS A 1 208 ? 4.988 -5.553 21.353 1.00 28.26 ? 208 LYS A C 1 ATOM 1616 O O . LYS A 1 208 ? 5.931 -5.001 21.911 1.00 30.78 ? 208 LYS A O 1 ATOM 1617 C CB . LYS A 1 208 ? 2.811 -4.289 21.225 1.00 31.16 ? 208 LYS A CB 1 ATOM 1618 C CG . LYS A 1 208 ? 1.361 -4.209 21.667 1.00 32.20 ? 208 LYS A CG 1 ATOM 1619 C CD . LYS A 1 208 ? 0.615 -3.101 20.964 1.00 32.83 ? 208 LYS A CD 1 ATOM 1620 C CE . LYS A 1 208 ? -0.821 -3.047 21.443 1.00 39.68 ? 208 LYS A CE 1 ATOM 1621 N NZ . LYS A 1 208 ? -1.594 -1.975 20.764 1.00 46.46 ? 208 LYS A NZ 1 ATOM 1622 N N . GLN A 1 209 ? 5.132 -6.327 20.283 1.00 28.94 ? 209 GLN A N 1 ATOM 1623 C CA . GLN A 1 209 ? 6.428 -6.558 19.650 1.00 28.11 ? 209 GLN A CA 1 ATOM 1624 C C . GLN A 1 209 ? 6.266 -7.178 18.260 1.00 30.09 ? 209 GLN A C 1 ATOM 1625 O O . GLN A 1 209 ? 7.299 -7.477 17.618 1.00 30.42 ? 209 GLN A O 1 ATOM 1626 C CB . GLN A 1 209 ? 7.263 -7.493 20.517 1.00 30.55 ? 209 GLN A CB 1 ATOM 1627 C CG . GLN A 1 209 ? 6.518 -8.755 20.919 1.00 32.09 ? 209 GLN A CG 1 ATOM 1628 C CD . GLN A 1 209 ? 7.415 -9.783 21.547 1.00 37.68 ? 209 GLN A CD 1 ATOM 1629 O OE1 . GLN A 1 209 ? 8.145 -9.501 22.493 1.00 40.65 ? 209 GLN A OE1 1 ATOM 1630 N NE2 . GLN A 1 209 ? 7.366 -11.004 21.011 1.00 36.70 ? 209 GLN A NE2 1 ATOM 1631 O OXT . GLN A 1 209 ? 5.111 -7.365 17.827 1.00 28.35 ? 209 GLN A OXT 1 ATOM 1632 N N . PRO B 1 2 ? 36.456 22.522 0.112 1.00 44.99 ? 2 PRO B N 1 ATOM 1633 C CA . PRO B 1 2 ? 35.928 23.163 1.346 1.00 38.33 ? 2 PRO B CA 1 ATOM 1634 C C . PRO B 1 2 ? 34.592 22.500 1.704 1.00 31.55 ? 2 PRO B C 1 ATOM 1635 O O . PRO B 1 2 ? 34.476 21.270 1.661 1.00 27.29 ? 2 PRO B O 1 ATOM 1636 C CB . PRO B 1 2 ? 35.742 24.637 1.013 1.00 39.93 ? 2 PRO B CB 1 ATOM 1637 C CG . PRO B 1 2 ? 35.408 24.539 -0.468 1.00 41.50 ? 2 PRO B CG 1 ATOM 1638 C CD . PRO B 1 2 ? 36.297 23.435 -1.037 1.00 46.22 ? 2 PRO B CD 1 ATOM 1639 N N . TYR B 1 3 ? 33.580 23.312 2.002 1.00 23.35 ? 3 TYR B N 1 ATOM 1640 C CA . TYR B 1 3 ? 32.265 22.800 2.366 1.00 21.38 ? 3 TYR B CA 1 ATOM 1641 C C . TYR B 1 3 ? 31.201 23.090 1.321 1.00 22.19 ? 3 TYR B C 1 ATOM 1642 O O . TYR B 1 3 ? 31.216 24.134 0.668 1.00 22.43 ? 3 TYR B O 1 ATOM 1643 C CB . TYR B 1 3 ? 31.815 23.414 3.689 1.00 21.29 ? 3 TYR B CB 1 ATOM 1644 C CG . TYR B 1 3 ? 32.793 23.230 4.822 1.00 20.74 ? 3 TYR B CG 1 ATOM 1645 C CD1 . TYR B 1 3 ? 33.159 21.957 5.265 1.00 21.60 ? 3 TYR B CD1 1 ATOM 1646 C CD2 . TYR B 1 3 ? 33.345 24.335 5.464 1.00 19.73 ? 3 TYR B CD2 1 ATOM 1647 C CE1 . TYR B 1 3 ? 34.056 21.799 6.325 1.00 20.76 ? 3 TYR B CE1 1 ATOM 1648 C CE2 . TYR B 1 3 ? 34.236 24.189 6.519 1.00 21.65 ? 3 TYR B CE2 1 ATOM 1649 C CZ . TYR B 1 3 ? 34.590 22.926 6.945 1.00 21.17 ? 3 TYR B CZ 1 ATOM 1650 O OH . TYR B 1 3 ? 35.492 22.800 7.974 1.00 24.95 ? 3 TYR B OH 1 ATOM 1651 N N . THR B 1 4 ? 30.243 22.177 1.221 1.00 19.47 ? 4 THR B N 1 ATOM 1652 C CA . THR B 1 4 ? 29.132 22.312 0.292 1.00 20.33 ? 4 THR B CA 1 ATOM 1653 C C . THR B 1 4 ? 27.886 21.755 0.964 1.00 21.18 ? 4 THR B C 1 ATOM 1654 O O . THR B 1 4 ? 27.889 20.616 1.428 1.00 27.50 ? 4 THR B O 1 ATOM 1655 C CB . THR B 1 4 ? 29.367 21.502 -1.009 1.00 17.61 ? 4 THR B CB 1 ATOM 1656 O OG1 . THR B 1 4 ? 30.582 21.927 -1.632 1.00 19.50 ? 4 THR B OG1 1 ATOM 1657 C CG2 . THR B 1 4 ? 28.206 21.693 -1.981 1.00 10.34 ? 4 THR B CG2 1 ATOM 1658 N N . VAL B 1 5 ? 26.843 22.569 1.075 1.00 16.83 ? 5 VAL B N 1 ATOM 1659 C CA . VAL B 1 5 ? 25.602 22.085 1.658 1.00 18.93 ? 5 VAL B CA 1 ATOM 1660 C C . VAL B 1 5 ? 24.546 22.032 0.554 1.00 22.66 ? 5 VAL B C 1 ATOM 1661 O O . VAL B 1 5 ? 24.322 23.009 -0.162 1.00 23.75 ? 5 VAL B O 1 ATOM 1662 C CB . VAL B 1 5 ? 25.117 22.916 2.909 1.00 19.36 ? 5 VAL B CB 1 ATOM 1663 C CG1 . VAL B 1 5 ? 26.209 23.841 3.418 1.00 16.06 ? 5 VAL B CG1 1 ATOM 1664 C CG2 . VAL B 1 5 ? 23.828 23.664 2.633 1.00 20.46 ? 5 VAL B CG2 1 ATOM 1665 N N . VAL B 1 6 ? 23.985 20.847 0.357 1.00 21.03 ? 6 VAL B N 1 ATOM 1666 C CA . VAL B 1 6 ? 22.953 20.631 -0.646 1.00 16.98 ? 6 VAL B CA 1 ATOM 1667 C C . VAL B 1 6 ? 21.639 20.575 0.123 1.00 20.71 ? 6 VAL B C 1 ATOM 1668 O O . VAL B 1 6 ? 21.448 19.706 0.982 1.00 20.99 ? 6 VAL B O 1 ATOM 1669 C CB . VAL B 1 6 ? 23.181 19.306 -1.404 1.00 19.05 ? 6 VAL B CB 1 ATOM 1670 C CG1 . VAL B 1 6 ? 22.174 19.168 -2.528 1.00 15.74 ? 6 VAL B CG1 1 ATOM 1671 C CG2 . VAL B 1 6 ? 24.608 19.241 -1.941 1.00 12.93 ? 6 VAL B CG2 1 ATOM 1672 N N . TYR B 1 7 ? 20.735 21.503 -0.175 1.00 18.95 ? 7 TYR B N 1 ATOM 1673 C CA . TYR B 1 7 ? 19.470 21.558 0.543 1.00 17.11 ? 7 TYR B CA 1 ATOM 1674 C C . TYR B 1 7 ? 18.410 22.353 -0.216 1.00 20.00 ? 7 TYR B C 1 ATOM 1675 O O . TYR B 1 7 ? 18.700 23.009 -1.215 1.00 28.30 ? 7 TYR B O 1 ATOM 1676 C CB . TYR B 1 7 ? 19.725 22.197 1.918 1.00 15.53 ? 7 TYR B CB 1 ATOM 1677 C CG . TYR B 1 7 ? 18.614 22.036 2.927 1.00 15.81 ? 7 TYR B CG 1 ATOM 1678 C CD1 . TYR B 1 7 ? 18.124 20.773 3.254 1.00 20.70 ? 7 TYR B CD1 1 ATOM 1679 C CD2 . TYR B 1 7 ? 18.064 23.143 3.573 1.00 17.41 ? 7 TYR B CD2 1 ATOM 1680 C CE1 . TYR B 1 7 ? 17.114 20.610 4.195 1.00 15.62 ? 7 TYR B CE1 1 ATOM 1681 C CE2 . TYR B 1 7 ? 17.053 22.993 4.520 1.00 13.96 ? 7 TYR B CE2 1 ATOM 1682 C CZ . TYR B 1 7 ? 16.583 21.719 4.826 1.00 19.69 ? 7 TYR B CZ 1 ATOM 1683 O OH . TYR B 1 7 ? 15.580 21.549 5.754 1.00 16.01 ? 7 TYR B OH 1 ATOM 1684 N N . PHE B 1 8 ? 17.173 22.278 0.265 1.00 21.14 ? 8 PHE B N 1 ATOM 1685 C CA . PHE B 1 8 ? 16.055 22.997 -0.330 1.00 23.27 ? 8 PHE B CA 1 ATOM 1686 C C . PHE B 1 8 ? 16.196 24.474 0.033 1.00 24.52 ? 8 PHE B C 1 ATOM 1687 O O . PHE B 1 8 ? 16.954 24.816 0.937 1.00 23.06 ? 8 PHE B O 1 ATOM 1688 C CB . PHE B 1 8 ? 14.742 22.431 0.206 1.00 20.81 ? 8 PHE B CB 1 ATOM 1689 C CG . PHE B 1 8 ? 14.568 20.966 -0.067 1.00 28.53 ? 8 PHE B CG 1 ATOM 1690 C CD1 . PHE B 1 8 ? 14.313 20.511 -1.363 1.00 27.87 ? 8 PHE B CD1 1 ATOM 1691 C CD2 . PHE B 1 8 ? 14.682 20.033 0.961 1.00 24.47 ? 8 PHE B CD2 1 ATOM 1692 C CE1 . PHE B 1 8 ? 14.175 19.149 -1.630 1.00 26.60 ? 8 PHE B CE1 1 ATOM 1693 C CE2 . PHE B 1 8 ? 14.546 18.664 0.705 1.00 28.36 ? 8 PHE B CE2 1 ATOM 1694 C CZ . PHE B 1 8 ? 14.293 18.222 -0.594 1.00 30.39 ? 8 PHE B CZ 1 ATOM 1695 N N . PRO B 1 9 ? 15.506 25.373 -0.688 1.00 26.31 ? 9 PRO B N 1 ATOM 1696 C CA . PRO B 1 9 ? 15.608 26.806 -0.384 1.00 25.99 ? 9 PRO B CA 1 ATOM 1697 C C . PRO B 1 9 ? 14.846 27.247 0.875 1.00 23.56 ? 9 PRO B C 1 ATOM 1698 O O . PRO B 1 9 ? 13.976 28.112 0.811 1.00 23.36 ? 9 PRO B O 1 ATOM 1699 C CB . PRO B 1 9 ? 15.055 27.456 -1.650 1.00 24.89 ? 9 PRO B CB 1 ATOM 1700 C CG . PRO B 1 9 ? 13.996 26.473 -2.082 1.00 23.72 ? 9 PRO B CG 1 ATOM 1701 C CD . PRO B 1 9 ? 14.698 25.148 -1.904 1.00 26.50 ? 9 PRO B CD 1 ATOM 1702 N N . VAL B 1 10 ? 15.171 26.631 2.009 1.00 25.41 ? 10 VAL B N 1 ATOM 1703 C CA . VAL B 1 10 ? 14.550 26.952 3.295 1.00 21.42 ? 10 VAL B CA 1 ATOM 1704 C C . VAL B 1 10 ? 15.627 26.876 4.372 1.00 21.85 ? 10 VAL B C 1 ATOM 1705 O O . VAL B 1 10 ? 16.718 26.351 4.129 1.00 24.62 ? 10 VAL B O 1 ATOM 1706 C CB . VAL B 1 10 ? 13.411 25.962 3.669 1.00 18.04 ? 10 VAL B CB 1 ATOM 1707 C CG1 . VAL B 1 10 ? 12.331 25.954 2.601 1.00 24.91 ? 10 VAL B CG1 1 ATOM 1708 C CG2 . VAL B 1 10 ? 13.962 24.564 3.887 1.00 22.55 ? 10 VAL B CG2 1 ATOM 1709 N N . ARG B 1 11 ? 15.338 27.424 5.548 1.00 19.09 ? 11 ARG B N 1 ATOM 1710 C CA . ARG B 1 11 ? 16.292 27.384 6.653 1.00 22.10 ? 11 ARG B CA 1 ATOM 1711 C C . ARG B 1 11 ? 16.294 25.967 7.214 1.00 20.11 ? 11 ARG B C 1 ATOM 1712 O O . ARG B 1 11 ? 17.339 25.313 7.264 1.00 17.99 ? 11 ARG B O 1 ATOM 1713 C CB . ARG B 1 11 ? 15.905 28.386 7.740 1.00 21.02 ? 11 ARG B CB 1 ATOM 1714 C CG . ARG B 1 11 ? 15.934 29.825 7.269 1.00 24.47 ? 11 ARG B CG 1 ATOM 1715 C CD . ARG B 1 11 ? 15.615 30.782 8.394 1.00 27.24 ? 11 ARG B CD 1 ATOM 1716 N NE . ARG B 1 11 ? 15.297 32.107 7.876 1.00 35.99 ? 11 ARG B NE 1 ATOM 1717 C CZ . ARG B 1 11 ? 14.600 33.022 8.539 1.00 35.08 ? 11 ARG B CZ 1 ATOM 1718 N NH1 . ARG B 1 11 ? 14.150 32.762 9.762 1.00 34.23 ? 11 ARG B NH1 1 ATOM 1719 N NH2 . ARG B 1 11 ? 14.322 34.185 7.961 1.00 33.00 ? 11 ARG B NH2 1 ATOM 1720 N N . GLY B 1 12 ? 15.107 25.510 7.614 1.00 17.29 ? 12 GLY B N 1 ATOM 1721 C CA . GLY B 1 12 ? 14.919 24.170 8.147 1.00 19.03 ? 12 GLY B CA 1 ATOM 1722 C C . GLY B 1 12 ? 16.043 23.580 8.979 1.00 21.68 ? 12 GLY B C 1 ATOM 1723 O O . GLY B 1 12 ? 16.525 24.201 9.930 1.00 19.53 ? 12 GLY B O 1 ATOM 1724 N N . ARG B 1 13 ? 16.494 22.393 8.587 1.00 18.60 ? 13 ARG B N 1 ATOM 1725 C CA . ARG B 1 13 ? 17.557 21.700 9.303 1.00 16.78 ? 13 ARG B CA 1 ATOM 1726 C C . ARG B 1 13 ? 18.984 22.143 8.997 1.00 17.85 ? 13 ARG B C 1 ATOM 1727 O O . ARG B 1 13 ? 19.941 21.511 9.453 1.00 14.77 ? 13 ARG B O 1 ATOM 1728 C CB . ARG B 1 13 ? 17.419 20.189 9.123 1.00 17.91 ? 13 ARG B CB 1 ATOM 1729 C CG . ARG B 1 13 ? 16.250 19.595 9.896 1.00 16.36 ? 13 ARG B CG 1 ATOM 1730 C CD . ARG B 1 13 ? 16.233 18.086 9.786 1.00 17.76 ? 13 ARG B CD 1 ATOM 1731 N NE . ARG B 1 13 ? 15.255 17.479 10.688 1.00 16.09 ? 13 ARG B NE 1 ATOM 1732 C CZ . ARG B 1 13 ? 15.511 17.133 11.947 1.00 14.76 ? 13 ARG B CZ 1 ATOM 1733 N NH1 . ARG B 1 13 ? 16.715 17.344 12.474 1.00 9.54 ? 13 ARG B NH1 1 ATOM 1734 N NH2 . ARG B 1 13 ? 14.558 16.583 12.686 1.00 12.19 ? 13 ARG B NH2 1 ATOM 1735 N N . CYS B 1 14 ? 19.137 23.223 8.234 1.00 13.59 ? 14 CYS B N 1 ATOM 1736 C CA . CYS B 1 14 ? 20.473 23.722 7.915 1.00 12.78 ? 14 CYS B CA 1 ATOM 1737 C C . CYS B 1 14 ? 20.777 25.056 8.583 1.00 14.39 ? 14 CYS B C 1 ATOM 1738 O O . CYS B 1 14 ? 21.923 25.518 8.566 1.00 17.05 ? 14 CYS B O 1 ATOM 1739 C CB . CYS B 1 14 ? 20.666 23.837 6.404 1.00 11.20 ? 14 CYS B CB 1 ATOM 1740 S SG . CYS B 1 14 ? 20.802 22.248 5.584 1.00 18.79 ? 14 CYS B SG 1 ATOM 1741 N N . ALA B 1 15 ? 19.754 25.658 9.187 1.00 12.33 ? 15 ALA B N 1 ATOM 1742 C CA . ALA B 1 15 ? 19.894 26.944 9.860 1.00 11.57 ? 15 ALA B CA 1 ATOM 1743 C C . ALA B 1 15 ? 21.024 26.948 10.892 1.00 15.07 ? 15 ALA B C 1 ATOM 1744 O O . ALA B 1 15 ? 21.909 27.802 10.851 1.00 19.37 ? 15 ALA B O 1 ATOM 1745 C CB . ALA B 1 15 ? 18.577 27.330 10.509 1.00 12.32 ? 15 ALA B CB 1 ATOM 1746 N N . ALA B 1 16 ? 21.022 25.956 11.777 1.00 18.57 ? 16 ALA B N 1 ATOM 1747 C CA . ALA B 1 16 ? 22.038 25.856 12.816 1.00 12.94 ? 16 ALA B CA 1 ATOM 1748 C C . ALA B 1 16 ? 23.447 25.658 12.272 1.00 14.92 ? 16 ALA B C 1 ATOM 1749 O O . ALA B 1 16 ? 24.385 26.332 12.714 1.00 20.76 ? 16 ALA B O 1 ATOM 1750 C CB . ALA B 1 16 ? 21.683 24.747 13.791 1.00 14.79 ? 16 ALA B CB 1 ATOM 1751 N N . LEU B 1 17 ? 23.600 24.755 11.305 1.00 14.18 ? 17 LEU B N 1 ATOM 1752 C CA . LEU B 1 17 ? 24.920 24.494 10.730 1.00 16.72 ? 17 LEU B CA 1 ATOM 1753 C C . LEU B 1 17 ? 25.433 25.696 9.934 1.00 12.67 ? 17 LEU B C 1 ATOM 1754 O O . LEU B 1 17 ? 26.639 25.927 9.860 1.00 16.54 ? 17 LEU B O 1 ATOM 1755 C CB . LEU B 1 17 ? 24.928 23.195 9.900 1.00 18.29 ? 17 LEU B CB 1 ATOM 1756 C CG . LEU B 1 17 ? 24.156 23.036 8.588 1.00 21.35 ? 17 LEU B CG 1 ATOM 1757 C CD1 . LEU B 1 17 ? 25.082 23.325 7.424 1.00 16.63 ? 17 LEU B CD1 1 ATOM 1758 C CD2 . LEU B 1 17 ? 23.615 21.612 8.473 1.00 20.25 ? 17 LEU B CD2 1 ATOM 1759 N N . ARG B 1 18 ? 24.515 26.476 9.367 1.00 12.74 ? 18 ARG B N 1 ATOM 1760 C CA . ARG B 1 18 ? 24.891 27.674 8.618 1.00 18.88 ? 18 ARG B CA 1 ATOM 1761 C C . ARG B 1 18 ? 25.375 28.751 9.588 1.00 16.51 ? 18 ARG B C 1 ATOM 1762 O O . ARG B 1 18 ? 26.380 29.416 9.331 1.00 13.17 ? 18 ARG B O 1 ATOM 1763 C CB . ARG B 1 18 ? 23.710 28.195 7.804 1.00 15.29 ? 18 ARG B CB 1 ATOM 1764 C CG . ARG B 1 18 ? 23.418 27.381 6.566 1.00 8.72 ? 18 ARG B CG 1 ATOM 1765 C CD . ARG B 1 18 ? 22.061 27.743 6.005 1.00 15.71 ? 18 ARG B CD 1 ATOM 1766 N NE . ARG B 1 18 ? 21.810 27.073 4.734 1.00 15.01 ? 18 ARG B NE 1 ATOM 1767 C CZ . ARG B 1 18 ? 20.604 26.797 4.254 1.00 12.98 ? 18 ARG B CZ 1 ATOM 1768 N NH1 . ARG B 1 18 ? 19.517 27.128 4.940 1.00 13.28 ? 18 ARG B NH1 1 ATOM 1769 N NH2 . ARG B 1 18 ? 20.486 26.195 3.078 1.00 20.09 ? 18 ARG B NH2 1 ATOM 1770 N N . MET B 1 19 ? 24.661 28.905 10.706 1.00 15.95 ? 19 MET B N 1 ATOM 1771 C CA . MET B 1 19 ? 25.034 29.882 11.728 1.00 15.28 ? 19 MET B CA 1 ATOM 1772 C C . MET B 1 19 ? 26.402 29.532 12.294 1.00 17.96 ? 19 MET B C 1 ATOM 1773 O O . MET B 1 19 ? 27.211 30.411 12.574 1.00 19.34 ? 19 MET B O 1 ATOM 1774 C CB . MET B 1 19 ? 24.021 29.901 12.870 1.00 18.95 ? 19 MET B CB 1 ATOM 1775 C CG . MET B 1 19 ? 22.626 30.337 12.477 1.00 24.87 ? 19 MET B CG 1 ATOM 1776 S SD . MET B 1 19 ? 21.554 30.545 13.921 1.00 34.59 ? 19 MET B SD 1 ATOM 1777 C CE . MET B 1 19 ? 21.340 28.900 14.412 1.00 33.63 ? 19 MET B CE 1 ATOM 1778 N N . LEU B 1 20 ? 26.648 28.236 12.459 1.00 18.78 ? 20 LEU B N 1 ATOM 1779 C CA . LEU B 1 20 ? 27.916 27.744 12.985 1.00 17.18 ? 20 LEU B CA 1 ATOM 1780 C C . LEU B 1 20 ? 29.064 28.113 12.046 1.00 20.02 ? 20 LEU B C 1 ATOM 1781 O O . LEU B 1 20 ? 30.083 28.655 12.485 1.00 16.87 ? 20 LEU B O 1 ATOM 1782 C CB . LEU B 1 20 ? 27.842 26.223 13.179 1.00 13.92 ? 20 LEU B CB 1 ATOM 1783 C CG . LEU B 1 20 ? 28.971 25.482 13.907 1.00 19.86 ? 20 LEU B CG 1 ATOM 1784 C CD1 . LEU B 1 20 ? 28.451 24.135 14.389 1.00 18.43 ? 20 LEU B CD1 1 ATOM 1785 C CD2 . LEU B 1 20 ? 30.198 25.303 13.017 1.00 13.99 ? 20 LEU B CD2 1 ATOM 1786 N N . LEU B 1 21 ? 28.897 27.801 10.760 1.00 19.50 ? 21 LEU B N 1 ATOM 1787 C CA . LEU B 1 21 ? 29.910 28.096 9.752 1.00 19.18 ? 21 LEU B CA 1 ATOM 1788 C C . LEU B 1 21 ? 30.167 29.596 9.656 1.00 17.53 ? 21 LEU B C 1 ATOM 1789 O O . LEU B 1 21 ? 31.316 30.031 9.662 1.00 15.83 ? 21 LEU B O 1 ATOM 1790 C CB . LEU B 1 21 ? 29.484 27.549 8.389 1.00 15.49 ? 21 LEU B CB 1 ATOM 1791 C CG . LEU B 1 21 ? 29.547 26.030 8.229 1.00 15.85 ? 21 LEU B CG 1 ATOM 1792 C CD1 . LEU B 1 21 ? 28.894 25.612 6.926 1.00 13.39 ? 21 LEU B CD1 1 ATOM 1793 C CD2 . LEU B 1 21 ? 30.993 25.564 8.281 1.00 12.67 ? 21 LEU B CD2 1 ATOM 1794 N N . ALA B 1 22 ? 29.092 30.378 9.604 1.00 15.69 ? 22 ALA B N 1 ATOM 1795 C CA . ALA B 1 22 ? 29.191 31.831 9.515 1.00 16.05 ? 22 ALA B CA 1 ATOM 1796 C C . ALA B 1 22 ? 29.941 32.414 10.711 1.00 19.44 ? 22 ALA B C 1 ATOM 1797 O O . ALA B 1 22 ? 30.927 33.135 10.548 1.00 23.53 ? 22 ALA B O 1 ATOM 1798 C CB . ALA B 1 22 ? 27.809 32.436 9.426 1.00 13.27 ? 22 ALA B CB 1 ATOM 1799 N N . ASP B 1 23 ? 29.500 32.051 11.912 1.00 19.70 ? 23 ASP B N 1 ATOM 1800 C CA . ASP B 1 23 ? 30.104 32.536 13.145 1.00 16.42 ? 23 ASP B CA 1 ATOM 1801 C C . ASP B 1 23 ? 31.563 32.119 13.318 1.00 20.57 ? 23 ASP B C 1 ATOM 1802 O O . ASP B 1 23 ? 32.342 32.832 13.950 1.00 27.27 ? 23 ASP B O 1 ATOM 1803 C CB . ASP B 1 23 ? 29.277 32.073 14.346 1.00 26.04 ? 23 ASP B CB 1 ATOM 1804 C CG . ASP B 1 23 ? 29.571 32.867 15.601 1.00 27.38 ? 23 ASP B CG 1 ATOM 1805 O OD1 . ASP B 1 23 ? 29.380 34.102 15.590 1.00 28.68 ? 23 ASP B OD1 1 ATOM 1806 O OD2 . ASP B 1 23 ? 29.966 32.245 16.603 1.00 29.14 ? 23 ASP B OD2 1 ATOM 1807 N N . GLN B 1 24 ? 31.932 30.967 12.767 1.00 22.55 ? 24 GLN B N 1 ATOM 1808 C CA . GLN B 1 24 ? 33.307 30.478 12.868 1.00 19.78 ? 24 GLN B CA 1 ATOM 1809 C C . GLN B 1 24 ? 34.195 31.012 11.754 1.00 23.29 ? 24 GLN B C 1 ATOM 1810 O O . GLN B 1 24 ? 35.357 30.622 11.644 1.00 26.51 ? 24 GLN B O 1 ATOM 1811 C CB . GLN B 1 24 ? 33.336 28.948 12.871 1.00 21.07 ? 24 GLN B CB 1 ATOM 1812 C CG . GLN B 1 24 ? 32.766 28.331 14.147 1.00 17.57 ? 24 GLN B CG 1 ATOM 1813 C CD . GLN B 1 24 ? 33.505 28.794 15.389 1.00 22.26 ? 24 GLN B CD 1 ATOM 1814 O OE1 . GLN B 1 24 ? 34.736 28.741 15.443 1.00 23.87 ? 24 GLN B OE1 1 ATOM 1815 N NE2 . GLN B 1 24 ? 32.764 29.221 16.399 1.00 22.26 ? 24 GLN B NE2 1 ATOM 1816 N N . GLY B 1 25 ? 33.635 31.896 10.930 1.00 23.55 ? 25 GLY B N 1 ATOM 1817 C CA . GLY B 1 25 ? 34.382 32.486 9.833 1.00 26.33 ? 25 GLY B CA 1 ATOM 1818 C C . GLY B 1 25 ? 34.715 31.517 8.716 1.00 25.96 ? 25 GLY B C 1 ATOM 1819 O O . GLY B 1 25 ? 35.752 31.648 8.071 1.00 32.53 ? 25 GLY B O 1 ATOM 1820 N N . GLN B 1 26 ? 33.841 30.542 8.488 1.00 27.12 ? 26 GLN B N 1 ATOM 1821 C CA . GLN B 1 26 ? 34.048 29.544 7.443 1.00 30.01 ? 26 GLN B CA 1 ATOM 1822 C C . GLN B 1 26 ? 33.286 29.887 6.169 1.00 29.99 ? 26 GLN B C 1 ATOM 1823 O O . GLN B 1 26 ? 32.208 30.479 6.217 1.00 31.54 ? 26 GLN B O 1 ATOM 1824 C CB . GLN B 1 26 ? 33.609 28.161 7.928 1.00 32.12 ? 26 GLN B CB 1 ATOM 1825 C CG . GLN B 1 26 ? 34.300 27.689 9.194 1.00 31.02 ? 26 GLN B CG 1 ATOM 1826 C CD . GLN B 1 26 ? 35.796 27.590 9.039 1.00 30.45 ? 26 GLN B CD 1 ATOM 1827 O OE1 . GLN B 1 26 ? 36.293 27.116 8.021 1.00 33.98 ? 26 GLN B OE1 1 ATOM 1828 N NE2 . GLN B 1 26 ? 36.525 28.013 10.064 1.00 34.96 ? 26 GLN B NE2 1 ATOM 1829 N N . SER B 1 27 ? 33.853 29.491 5.033 1.00 29.11 ? 27 SER B N 1 ATOM 1830 C CA . SER B 1 27 ? 33.250 29.730 3.726 1.00 28.11 ? 27 SER B CA 1 ATOM 1831 C C . SER B 1 27 ? 32.634 28.421 3.262 1.00 26.42 ? 27 SER B C 1 ATOM 1832 O O . SER B 1 27 ? 33.189 27.350 3.506 1.00 28.32 ? 27 SER B O 1 ATOM 1833 C CB . SER B 1 27 ? 34.319 30.144 2.709 1.00 29.93 ? 27 SER B CB 1 ATOM 1834 O OG . SER B 1 27 ? 35.229 31.082 3.255 1.00 40.28 ? 27 SER B OG 1 ATOM 1835 N N . TRP B 1 28 ? 31.494 28.501 2.591 1.00 22.19 ? 28 TRP B N 1 ATOM 1836 C CA . TRP B 1 28 ? 30.849 27.300 2.083 1.00 24.92 ? 28 TRP B CA 1 ATOM 1837 C C . TRP B 1 28 ? 30.034 27.599 0.834 1.00 25.73 ? 28 TRP B C 1 ATOM 1838 O O . TRP B 1 28 ? 29.657 28.740 0.582 1.00 25.19 ? 28 TRP B O 1 ATOM 1839 C CB . TRP B 1 28 ? 29.971 26.643 3.156 1.00 22.29 ? 28 TRP B CB 1 ATOM 1840 C CG . TRP B 1 28 ? 28.704 27.382 3.489 1.00 15.52 ? 28 TRP B CG 1 ATOM 1841 C CD1 . TRP B 1 28 ? 27.455 27.126 3.001 1.00 13.84 ? 28 TRP B CD1 1 ATOM 1842 C CD2 . TRP B 1 28 ? 28.560 28.458 4.431 1.00 10.54 ? 28 TRP B CD2 1 ATOM 1843 N NE1 . TRP B 1 28 ? 26.539 27.967 3.587 1.00 15.10 ? 28 TRP B NE1 1 ATOM 1844 C CE2 . TRP B 1 28 ? 27.186 28.790 4.467 1.00 12.21 ? 28 TRP B CE2 1 ATOM 1845 C CE3 . TRP B 1 28 ? 29.449 29.163 5.250 1.00 14.96 ? 28 TRP B CE3 1 ATOM 1846 C CZ2 . TRP B 1 28 ? 26.685 29.803 5.294 1.00 14.12 ? 28 TRP B CZ2 1 ATOM 1847 C CZ3 . TRP B 1 28 ? 28.949 30.168 6.071 1.00 12.06 ? 28 TRP B CZ3 1 ATOM 1848 C CH2 . TRP B 1 28 ? 27.577 30.476 6.086 1.00 11.62 ? 28 TRP B CH2 1 ATOM 1849 N N . LYS B 1 29 ? 29.774 26.556 0.057 1.00 29.57 ? 29 LYS B N 1 ATOM 1850 C CA . LYS B 1 29 ? 29.012 26.663 -1.175 1.00 25.01 ? 29 LYS B CA 1 ATOM 1851 C C . LYS B 1 29 ? 27.614 26.114 -0.941 1.00 26.43 ? 29 LYS B C 1 ATOM 1852 O O . LYS B 1 29 ? 27.443 25.087 -0.286 1.00 27.83 ? 29 LYS B O 1 ATOM 1853 C CB . LYS B 1 29 ? 29.717 25.869 -2.280 1.00 29.33 ? 29 LYS B CB 1 ATOM 1854 C CG . LYS B 1 29 ? 28.887 25.607 -3.523 1.00 38.61 ? 29 LYS B CG 1 ATOM 1855 C CD . LYS B 1 29 ? 28.694 26.854 -4.373 1.00 50.41 ? 29 LYS B CD 1 ATOM 1856 C CE . LYS B 1 29 ? 27.795 26.555 -5.569 1.00 57.90 ? 29 LYS B CE 1 ATOM 1857 N NZ . LYS B 1 29 ? 28.278 25.361 -6.331 1.00 62.68 ? 29 LYS B NZ 1 ATOM 1858 N N . GLU B 1 30 ? 26.614 26.825 -1.446 1.00 26.92 ? 30 GLU B N 1 ATOM 1859 C CA . GLU B 1 30 ? 25.232 26.397 -1.314 1.00 27.01 ? 30 GLU B CA 1 ATOM 1860 C C . GLU B 1 30 ? 24.750 25.834 -2.643 1.00 27.72 ? 30 GLU B C 1 ATOM 1861 O O . GLU B 1 30 ? 24.811 26.508 -3.671 1.00 34.02 ? 30 GLU B O 1 ATOM 1862 C CB . GLU B 1 30 ? 24.338 27.570 -0.905 1.00 25.94 ? 30 GLU B CB 1 ATOM 1863 C CG . GLU B 1 30 ? 24.514 28.050 0.532 1.00 29.24 ? 30 GLU B CG 1 ATOM 1864 C CD . GLU B 1 30 ? 23.715 27.251 1.555 1.00 30.58 ? 30 GLU B CD 1 ATOM 1865 O OE1 . GLU B 1 30 ? 22.968 26.320 1.174 1.00 25.23 ? 30 GLU B OE1 1 ATOM 1866 O OE2 . GLU B 1 30 ? 23.838 27.564 2.757 1.00 29.25 ? 30 GLU B OE2 1 ATOM 1867 N N . GLU B 1 31 ? 24.337 24.574 -2.623 1.00 28.52 ? 31 GLU B N 1 ATOM 1868 C CA . GLU B 1 31 ? 23.813 23.905 -3.803 1.00 25.72 ? 31 GLU B CA 1 ATOM 1869 C C . GLU B 1 31 ? 22.324 23.805 -3.558 1.00 25.94 ? 31 GLU B C 1 ATOM 1870 O O . GLU B 1 31 ? 21.868 22.946 -2.809 1.00 29.29 ? 31 GLU B O 1 ATOM 1871 C CB . GLU B 1 31 ? 24.419 22.511 -3.949 1.00 33.03 ? 31 GLU B CB 1 ATOM 1872 C CG . GLU B 1 31 ? 25.774 22.493 -4.623 1.00 50.55 ? 31 GLU B CG 1 ATOM 1873 C CD . GLU B 1 31 ? 25.678 22.761 -6.113 1.00 60.19 ? 31 GLU B CD 1 ATOM 1874 O OE1 . GLU B 1 31 ? 25.642 23.946 -6.515 1.00 63.47 ? 31 GLU B OE1 1 ATOM 1875 O OE2 . GLU B 1 31 ? 25.625 21.779 -6.883 1.00 67.54 ? 31 GLU B OE2 1 ATOM 1876 N N . VAL B 1 32 ? 21.572 24.725 -4.146 1.00 24.92 ? 32 VAL B N 1 ATOM 1877 C CA . VAL B 1 32 ? 20.132 24.751 -3.963 1.00 20.60 ? 32 VAL B CA 1 ATOM 1878 C C . VAL B 1 32 ? 19.401 23.743 -4.828 1.00 22.29 ? 32 VAL B C 1 ATOM 1879 O O . VAL B 1 32 ? 19.620 23.663 -6.033 1.00 29.25 ? 32 VAL B O 1 ATOM 1880 C CB . VAL B 1 32 ? 19.562 26.158 -4.219 1.00 19.92 ? 32 VAL B CB 1 ATOM 1881 C CG1 . VAL B 1 32 ? 18.067 26.176 -3.945 1.00 12.11 ? 32 VAL B CG1 1 ATOM 1882 C CG2 . VAL B 1 32 ? 20.279 27.174 -3.342 1.00 14.39 ? 32 VAL B CG2 1 ATOM 1883 N N . VAL B 1 33 ? 18.544 22.962 -4.185 1.00 24.44 ? 33 VAL B N 1 ATOM 1884 C CA . VAL B 1 33 ? 17.747 21.954 -4.859 1.00 21.44 ? 33 VAL B CA 1 ATOM 1885 C C . VAL B 1 33 ? 16.300 22.392 -4.727 1.00 28.87 ? 33 VAL B C 1 ATOM 1886 O O . VAL B 1 33 ? 15.805 22.594 -3.617 1.00 27.88 ? 33 VAL B O 1 ATOM 1887 C CB . VAL B 1 33 ? 17.915 20.563 -4.207 1.00 17.46 ? 33 VAL B CB 1 ATOM 1888 C CG1 . VAL B 1 33 ? 16.964 19.562 -4.845 1.00 16.26 ? 33 VAL B CG1 1 ATOM 1889 C CG2 . VAL B 1 33 ? 19.350 20.087 -4.348 1.00 17.19 ? 33 VAL B CG2 1 ATOM 1890 N N . THR B 1 34 ? 15.637 22.574 -5.864 1.00 32.86 ? 34 THR B N 1 ATOM 1891 C CA . THR B 1 34 ? 14.240 22.988 -5.875 1.00 37.55 ? 34 THR B CA 1 ATOM 1892 C C . THR B 1 34 ? 13.335 21.766 -5.754 1.00 40.42 ? 34 THR B C 1 ATOM 1893 O O . THR B 1 34 ? 13.777 20.635 -5.960 1.00 43.21 ? 34 THR B O 1 ATOM 1894 C CB . THR B 1 34 ? 13.892 23.739 -7.174 1.00 39.12 ? 34 THR B CB 1 ATOM 1895 O OG1 . THR B 1 34 ? 14.013 22.845 -8.287 1.00 42.63 ? 34 THR B OG1 1 ATOM 1896 C CG2 . THR B 1 34 ? 14.838 24.914 -7.378 1.00 36.51 ? 34 THR B CG2 1 ATOM 1897 N N . VAL B 1 35 ? 12.069 22.001 -5.418 1.00 47.06 ? 35 VAL B N 1 ATOM 1898 C CA . VAL B 1 35 ? 11.088 20.925 -5.277 1.00 51.36 ? 35 VAL B CA 1 ATOM 1899 C C . VAL B 1 35 ? 10.899 20.185 -6.607 1.00 52.28 ? 35 VAL B C 1 ATOM 1900 O O . VAL B 1 35 ? 10.598 18.991 -6.625 1.00 51.27 ? 35 VAL B O 1 ATOM 1901 C CB . VAL B 1 35 ? 9.719 21.477 -4.786 1.00 56.08 ? 35 VAL B CB 1 ATOM 1902 C CG1 . VAL B 1 35 ? 9.053 22.331 -5.876 1.00 61.15 ? 35 VAL B CG1 1 ATOM 1903 C CG2 . VAL B 1 35 ? 8.809 20.338 -4.349 1.00 56.80 ? 35 VAL B CG2 1 ATOM 1904 N N . GLU B 1 36 ? 11.097 20.901 -7.712 1.00 53.52 ? 36 GLU B N 1 ATOM 1905 C CA . GLU B 1 36 ? 10.962 20.330 -9.049 1.00 54.84 ? 36 GLU B CA 1 ATOM 1906 C C . GLU B 1 36 ? 12.079 19.323 -9.294 1.00 50.67 ? 36 GLU B C 1 ATOM 1907 O O . GLU B 1 36 ? 11.821 18.167 -9.636 1.00 53.55 ? 36 GLU B O 1 ATOM 1908 C CB . GLU B 1 36 ? 11.057 21.429 -10.105 1.00 63.16 ? 36 GLU B CB 1 ATOM 1909 C CG . GLU B 1 36 ? 10.280 22.693 -9.779 1.00 69.82 ? 36 GLU B CG 1 ATOM 1910 C CD . GLU B 1 36 ? 11.060 23.952 -10.125 1.00 76.70 ? 36 GLU B CD 1 ATOM 1911 O OE1 . GLU B 1 36 ? 11.947 23.895 -11.012 1.00 77.80 ? 36 GLU B OE1 1 ATOM 1912 O OE2 . GLU B 1 36 ? 10.796 24.996 -9.492 1.00 77.93 ? 36 GLU B OE2 1 ATOM 1913 N N . THR B 1 37 ? 13.319 19.778 -9.119 1.00 45.47 ? 37 THR B N 1 ATOM 1914 C CA . THR B 1 37 ? 14.498 18.940 -9.312 1.00 44.03 ? 37 THR B CA 1 ATOM 1915 C C . THR B 1 37 ? 14.421 17.681 -8.440 1.00 44.83 ? 37 THR B C 1 ATOM 1916 O O . THR B 1 37 ? 14.750 16.582 -8.892 1.00 45.66 ? 37 THR B O 1 ATOM 1917 C CB . THR B 1 37 ? 15.797 19.711 -8.961 1.00 45.59 ? 37 THR B CB 1 ATOM 1918 O OG1 . THR B 1 37 ? 15.770 21.007 -9.571 1.00 44.60 ? 37 THR B OG1 1 ATOM 1919 C CG2 . THR B 1 37 ? 17.022 18.958 -9.462 1.00 41.13 ? 37 THR B CG2 1 ATOM 1920 N N . TRP B 1 38 ? 13.957 17.852 -7.202 1.00 42.46 ? 38 TRP B N 1 ATOM 1921 C CA . TRP B 1 38 ? 13.827 16.750 -6.247 1.00 37.33 ? 38 TRP B CA 1 ATOM 1922 C C . TRP B 1 38 ? 12.808 15.704 -6.702 1.00 39.59 ? 38 TRP B C 1 ATOM 1923 O O . TRP B 1 38 ? 13.067 14.502 -6.616 1.00 39.62 ? 38 TRP B O 1 ATOM 1924 C CB . TRP B 1 38 ? 13.447 17.297 -4.864 1.00 33.40 ? 38 TRP B CB 1 ATOM 1925 C CG . TRP B 1 38 ? 13.438 16.274 -3.751 1.00 25.44 ? 38 TRP B CG 1 ATOM 1926 C CD1 . TRP B 1 38 ? 12.344 15.804 -3.081 1.00 26.44 ? 38 TRP B CD1 1 ATOM 1927 C CD2 . TRP B 1 38 ? 14.578 15.630 -3.163 1.00 19.69 ? 38 TRP B CD2 1 ATOM 1928 N NE1 . TRP B 1 38 ? 12.732 14.912 -2.109 1.00 26.62 ? 38 TRP B NE1 1 ATOM 1929 C CE2 . TRP B 1 38 ? 14.092 14.785 -2.135 1.00 23.60 ? 38 TRP B CE2 1 ATOM 1930 C CE3 . TRP B 1 38 ? 15.958 15.685 -3.397 1.00 22.42 ? 38 TRP B CE3 1 ATOM 1931 C CZ2 . TRP B 1 38 ? 14.945 14.002 -1.344 1.00 18.02 ? 38 TRP B CZ2 1 ATOM 1932 C CZ3 . TRP B 1 38 ? 16.804 14.907 -2.610 1.00 18.65 ? 38 TRP B CZ3 1 ATOM 1933 C CH2 . TRP B 1 38 ? 16.291 14.076 -1.595 1.00 16.32 ? 38 TRP B CH2 1 ATOM 1934 N N . GLN B 1 39 ? 11.661 16.164 -7.198 1.00 41.02 ? 39 GLN B N 1 ATOM 1935 C CA . GLN B 1 39 ? 10.611 15.261 -7.665 1.00 43.87 ? 39 GLN B CA 1 ATOM 1936 C C . GLN B 1 39 ? 10.977 14.507 -8.939 1.00 45.67 ? 39 GLN B C 1 ATOM 1937 O O . GLN B 1 39 ? 10.292 13.557 -9.322 1.00 46.37 ? 39 GLN B O 1 ATOM 1938 C CB . GLN B 1 39 ? 9.294 16.015 -7.833 1.00 43.05 ? 39 GLN B CB 1 ATOM 1939 C CG . GLN B 1 39 ? 8.703 16.459 -6.503 1.00 53.12 ? 39 GLN B CG 1 ATOM 1940 C CD . GLN B 1 39 ? 7.534 17.409 -6.652 1.00 59.71 ? 39 GLN B CD 1 ATOM 1941 O OE1 . GLN B 1 39 ? 7.303 17.975 -7.724 1.00 67.77 ? 39 GLN B OE1 1 ATOM 1942 N NE2 . GLN B 1 39 ? 6.802 17.611 -5.565 1.00 58.04 ? 39 GLN B NE2 1 ATOM 1943 N N . GLU B 1 40 ? 12.064 14.924 -9.586 1.00 49.44 ? 40 GLU B N 1 ATOM 1944 C CA . GLU B 1 40 ? 12.539 14.261 -10.795 1.00 52.01 ? 40 GLU B CA 1 ATOM 1945 C C . GLU B 1 40 ? 13.010 12.849 -10.408 1.00 53.92 ? 40 GLU B C 1 ATOM 1946 O O . GLU B 1 40 ? 12.970 11.927 -11.224 1.00 56.56 ? 40 GLU B O 1 ATOM 1947 C CB . GLU B 1 40 ? 13.664 15.079 -11.435 1.00 52.61 ? 40 GLU B CB 1 ATOM 1948 C CG . GLU B 1 40 ? 14.194 14.525 -12.744 1.00 60.77 ? 40 GLU B CG 1 ATOM 1949 C CD . GLU B 1 40 ? 15.502 13.778 -12.572 1.00 65.52 ? 40 GLU B CD 1 ATOM 1950 O OE1 . GLU B 1 40 ? 16.568 14.429 -12.577 1.00 70.14 ? 40 GLU B OE1 1 ATOM 1951 O OE2 . GLU B 1 40 ? 15.471 12.538 -12.443 1.00 68.28 ? 40 GLU B OE2 1 ATOM 1952 N N . GLY B 1 41 ? 13.457 12.695 -9.160 1.00 53.26 ? 41 GLY B N 1 ATOM 1953 C CA . GLY B 1 41 ? 13.873 11.392 -8.661 1.00 47.13 ? 41 GLY B CA 1 ATOM 1954 C C . GLY B 1 41 ? 15.333 10.985 -8.568 1.00 45.40 ? 41 GLY B C 1 ATOM 1955 O O . GLY B 1 41 ? 15.712 10.304 -7.613 1.00 45.80 ? 41 GLY B O 1 ATOM 1956 N N . SER B 1 42 ? 16.152 11.382 -9.537 1.00 43.84 ? 42 SER B N 1 ATOM 1957 C CA . SER B 1 42 ? 17.565 11.000 -9.556 1.00 45.07 ? 42 SER B CA 1 ATOM 1958 C C . SER B 1 42 ? 18.397 11.318 -8.310 1.00 42.77 ? 42 SER B C 1 ATOM 1959 O O . SER B 1 42 ? 19.101 10.443 -7.802 1.00 44.63 ? 42 SER B O 1 ATOM 1960 C CB . SER B 1 42 ? 18.254 11.561 -10.802 1.00 45.52 ? 42 SER B CB 1 ATOM 1961 O OG . SER B 1 42 ? 18.192 12.975 -10.822 1.00 56.12 ? 42 SER B OG 1 ATOM 1962 N N . LEU B 1 43 ? 18.326 12.559 -7.825 1.00 41.45 ? 43 LEU B N 1 ATOM 1963 C CA . LEU B 1 43 ? 19.088 12.968 -6.640 1.00 35.47 ? 43 LEU B CA 1 ATOM 1964 C C . LEU B 1 43 ? 18.646 12.201 -5.389 1.00 33.32 ? 43 LEU B C 1 ATOM 1965 O O . LEU B 1 43 ? 19.483 11.691 -4.642 1.00 28.91 ? 43 LEU B O 1 ATOM 1966 C CB . LEU B 1 43 ? 18.941 14.473 -6.389 1.00 34.88 ? 43 LEU B CB 1 ATOM 1967 C CG . LEU B 1 43 ? 20.116 15.266 -5.791 1.00 33.78 ? 43 LEU B CG 1 ATOM 1968 C CD1 . LEU B 1 43 ? 19.560 16.342 -4.879 1.00 30.86 ? 43 LEU B CD1 1 ATOM 1969 C CD2 . LEU B 1 43 ? 21.086 14.386 -5.015 1.00 31.60 ? 43 LEU B CD2 1 ATOM 1970 N N . LYS B 1 44 ? 17.333 12.136 -5.166 1.00 27.83 ? 44 LYS B N 1 ATOM 1971 C CA . LYS B 1 44 ? 16.767 11.434 -4.014 1.00 28.21 ? 44 LYS B CA 1 ATOM 1972 C C . LYS B 1 44 ? 17.281 10.002 -3.946 1.00 31.60 ? 44 LYS B C 1 ATOM 1973 O O . LYS B 1 44 ? 17.657 9.518 -2.880 1.00 32.06 ? 44 LYS B O 1 ATOM 1974 C CB . LYS B 1 44 ? 15.241 11.409 -4.106 1.00 26.24 ? 44 LYS B CB 1 ATOM 1975 C CG . LYS B 1 44 ? 14.554 10.883 -2.859 1.00 22.27 ? 44 LYS B CG 1 ATOM 1976 C CD . LYS B 1 44 ? 13.084 10.584 -3.116 1.00 23.13 ? 44 LYS B CD 1 ATOM 1977 C CE . LYS B 1 44 ? 12.238 10.808 -1.871 1.00 28.25 ? 44 LYS B CE 1 ATOM 1978 N NZ . LYS B 1 44 ? 12.829 10.214 -0.639 1.00 25.33 ? 44 LYS B NZ 1 ATOM 1979 N N . ALA B 1 45 ? 17.320 9.348 -5.105 1.00 35.21 ? 45 ALA B N 1 ATOM 1980 C CA . ALA B 1 45 ? 17.777 7.968 -5.217 1.00 32.44 ? 45 ALA B CA 1 ATOM 1981 C C . ALA B 1 45 ? 19.243 7.792 -4.834 1.00 29.63 ? 45 ALA B C 1 ATOM 1982 O O . ALA B 1 45 ? 19.628 6.735 -4.339 1.00 33.70 ? 45 ALA B O 1 ATOM 1983 C CB . ALA B 1 45 ? 17.535 7.454 -6.629 1.00 33.51 ? 45 ALA B CB 1 ATOM 1984 N N . SER B 1 46 ? 20.057 8.818 -5.064 1.00 25.77 ? 46 SER B N 1 ATOM 1985 C CA . SER B 1 46 ? 21.479 8.750 -4.731 1.00 27.32 ? 46 SER B CA 1 ATOM 1986 C C . SER B 1 46 ? 21.775 9.115 -3.277 1.00 28.24 ? 46 SER B C 1 ATOM 1987 O O . SER B 1 46 ? 22.907 8.956 -2.817 1.00 29.38 ? 46 SER B O 1 ATOM 1988 C CB . SER B 1 46 ? 22.293 9.644 -5.664 1.00 28.96 ? 46 SER B CB 1 ATOM 1989 O OG . SER B 1 46 ? 21.881 10.995 -5.558 1.00 42.89 ? 46 SER B OG 1 ATOM 1990 N N . CYS B 1 47 ? 20.774 9.645 -2.575 1.00 26.04 ? 47 CYS B N 1 ATOM 1991 C CA . CYS B 1 47 ? 20.923 10.015 -1.166 1.00 24.21 ? 47 CYS B CA 1 ATOM 1992 C C . CYS B 1 47 ? 20.761 8.769 -0.303 1.00 24.57 ? 47 CYS B C 1 ATOM 1993 O O . CYS B 1 47 ? 19.778 8.038 -0.453 1.00 25.43 ? 47 CYS B O 1 ATOM 1994 C CB . CYS B 1 47 ? 19.871 11.050 -0.761 1.00 23.70 ? 47 CYS B CB 1 ATOM 1995 S SG . CYS B 1 47 ? 20.106 12.681 -1.487 1.00 27.60 ? 47 CYS B SG 1 ATOM 1996 N N . LEU B 1 48 ? 21.702 8.558 0.619 1.00 21.07 ? 48 LEU B N 1 ATOM 1997 C CA . LEU B 1 48 ? 21.693 7.396 1.510 1.00 20.15 ? 48 LEU B CA 1 ATOM 1998 C C . LEU B 1 48 ? 20.336 7.054 2.132 1.00 22.33 ? 48 LEU B C 1 ATOM 1999 O O . LEU B 1 48 ? 19.904 5.906 2.072 1.00 28.05 ? 48 LEU B O 1 ATOM 2000 C CB . LEU B 1 48 ? 22.740 7.565 2.609 1.00 23.63 ? 48 LEU B CB 1 ATOM 2001 C CG . LEU B 1 48 ? 22.899 6.392 3.580 1.00 26.35 ? 48 LEU B CG 1 ATOM 2002 C CD1 . LEU B 1 48 ? 23.265 5.123 2.818 1.00 23.75 ? 48 LEU B CD1 1 ATOM 2003 C CD2 . LEU B 1 48 ? 23.967 6.724 4.606 1.00 23.99 ? 48 LEU B CD2 1 ATOM 2004 N N . TYR B 1 49 ? 19.674 8.041 2.730 1.00 20.96 ? 49 TYR B N 1 ATOM 2005 C CA . TYR B 1 49 ? 18.364 7.817 3.347 1.00 19.04 ? 49 TYR B CA 1 ATOM 2006 C C . TYR B 1 49 ? 17.243 8.473 2.536 1.00 23.06 ? 49 TYR B C 1 ATOM 2007 O O . TYR B 1 49 ? 16.103 8.592 3.013 1.00 14.83 ? 49 TYR B O 1 ATOM 2008 C CB . TYR B 1 49 ? 18.346 8.338 4.789 1.00 16.45 ? 49 TYR B CB 1 ATOM 2009 C CG . TYR B 1 49 ? 19.391 7.708 5.687 1.00 15.57 ? 49 TYR B CG 1 ATOM 2010 C CD1 . TYR B 1 49 ? 19.335 6.349 6.006 1.00 15.62 ? 49 TYR B CD1 1 ATOM 2011 C CD2 . TYR B 1 49 ? 20.433 8.468 6.223 1.00 12.65 ? 49 TYR B CD2 1 ATOM 2012 C CE1 . TYR B 1 49 ? 20.289 5.758 6.835 1.00 9.71 ? 49 TYR B CE1 1 ATOM 2013 C CE2 . TYR B 1 49 ? 21.394 7.887 7.058 1.00 12.31 ? 49 TYR B CE2 1 ATOM 2014 C CZ . TYR B 1 49 ? 21.314 6.531 7.360 1.00 17.11 ? 49 TYR B CZ 1 ATOM 2015 O OH . TYR B 1 49 ? 22.253 5.951 8.189 1.00 16.72 ? 49 TYR B OH 1 ATOM 2016 N N . GLY B 1 50 ? 17.576 8.877 1.306 1.00 20.59 ? 50 GLY B N 1 ATOM 2017 C CA . GLY B 1 50 ? 16.614 9.512 0.418 1.00 15.71 ? 50 GLY B CA 1 ATOM 2018 C C . GLY B 1 50 ? 16.169 10.891 0.867 1.00 18.57 ? 50 GLY B C 1 ATOM 2019 O O . GLY B 1 50 ? 15.067 11.329 0.532 1.00 21.67 ? 50 GLY B O 1 ATOM 2020 N N . GLN B 1 51 ? 17.017 11.577 1.633 1.00 20.16 ? 51 GLN B N 1 ATOM 2021 C CA . GLN B 1 51 ? 16.677 12.905 2.129 1.00 19.25 ? 51 GLN B CA 1 ATOM 2022 C C . GLN B 1 51 ? 17.852 13.870 2.166 1.00 20.17 ? 51 GLN B C 1 ATOM 2023 O O . GLN B 1 51 ? 19.008 13.467 2.050 1.00 18.88 ? 51 GLN B O 1 ATOM 2024 C CB . GLN B 1 51 ? 16.081 12.810 3.538 1.00 14.87 ? 51 GLN B CB 1 ATOM 2025 C CG . GLN B 1 51 ? 14.756 12.076 3.632 1.00 14.61 ? 51 GLN B CG 1 ATOM 2026 C CD . GLN B 1 51 ? 14.127 12.226 4.994 1.00 14.77 ? 51 GLN B CD 1 ATOM 2027 O OE1 . GLN B 1 51 ? 14.752 11.954 6.012 1.00 22.93 ? 51 GLN B OE1 1 ATOM 2028 N NE2 . GLN B 1 51 ? 12.881 12.684 5.021 1.00 16.66 ? 51 GLN B NE2 1 ATOM 2029 N N . LEU B 1 52 ? 17.528 15.153 2.307 1.00 22.03 ? 52 LEU B N 1 ATOM 2030 C CA . LEU B 1 52 ? 18.520 16.219 2.414 1.00 22.08 ? 52 LEU B CA 1 ATOM 2031 C C . LEU B 1 52 ? 18.382 16.774 3.844 1.00 21.71 ? 52 LEU B C 1 ATOM 2032 O O . LEU B 1 52 ? 17.341 16.601 4.477 1.00 20.23 ? 52 LEU B O 1 ATOM 2033 C CB . LEU B 1 52 ? 18.251 17.310 1.368 1.00 18.06 ? 52 LEU B CB 1 ATOM 2034 C CG . LEU B 1 52 ? 18.409 16.899 -0.100 1.00 16.20 ? 52 LEU B CG 1 ATOM 2035 C CD1 . LEU B 1 52 ? 18.006 18.047 -1.017 1.00 13.53 ? 52 LEU B CD1 1 ATOM 2036 C CD2 . LEU B 1 52 ? 19.846 16.468 -0.376 1.00 12.65 ? 52 LEU B CD2 1 ATOM 2037 N N . PRO B 1 53 ? 19.382 17.522 4.340 1.00 20.71 ? 53 PRO B N 1 ATOM 2038 C CA . PRO B 1 53 ? 20.643 17.930 3.718 1.00 18.98 ? 53 PRO B CA 1 ATOM 2039 C C . PRO B 1 53 ? 21.683 16.862 3.415 1.00 21.39 ? 53 PRO B C 1 ATOM 2040 O O . PRO B 1 53 ? 21.692 15.771 3.989 1.00 24.37 ? 53 PRO B O 1 ATOM 2041 C CB . PRO B 1 53 ? 21.200 18.936 4.724 1.00 17.12 ? 53 PRO B CB 1 ATOM 2042 C CG . PRO B 1 53 ? 20.752 18.362 6.035 1.00 14.53 ? 53 PRO B CG 1 ATOM 2043 C CD . PRO B 1 53 ? 19.311 18.013 5.731 1.00 17.11 ? 53 PRO B CD 1 ATOM 2044 N N . LYS B 1 54 ? 22.544 17.215 2.470 1.00 19.46 ? 54 LYS B N 1 ATOM 2045 C CA . LYS B 1 54 ? 23.671 16.408 2.048 1.00 18.15 ? 54 LYS B CA 1 ATOM 2046 C C . LYS B 1 54 ? 24.800 17.406 2.267 1.00 17.46 ? 54 LYS B C 1 ATOM 2047 O O . LYS B 1 54 ? 24.646 18.592 1.984 1.00 19.47 ? 54 LYS B O 1 ATOM 2048 C CB . LYS B 1 54 ? 23.562 16.044 0.568 1.00 25.72 ? 54 LYS B CB 1 ATOM 2049 C CG . LYS B 1 54 ? 24.774 15.291 0.037 1.00 25.89 ? 54 LYS B CG 1 ATOM 2050 C CD . LYS B 1 54 ? 24.657 15.058 -1.453 1.00 26.27 ? 54 LYS B CD 1 ATOM 2051 C CE . LYS B 1 54 ? 25.954 14.531 -2.029 1.00 28.22 ? 54 LYS B CE 1 ATOM 2052 N NZ . LYS B 1 54 ? 25.850 14.396 -3.504 1.00 30.93 ? 54 LYS B NZ 1 ATOM 2053 N N . PHE B 1 55 ? 25.926 16.941 2.780 1.00 17.93 ? 55 PHE B N 1 ATOM 2054 C CA . PHE B 1 55 ? 27.038 17.831 3.071 1.00 14.81 ? 55 PHE B CA 1 ATOM 2055 C C . PHE B 1 55 ? 28.334 17.255 2.542 1.00 16.42 ? 55 PHE B C 1 ATOM 2056 O O . PHE B 1 55 ? 28.500 16.045 2.471 1.00 23.75 ? 55 PHE B O 1 ATOM 2057 C CB . PHE B 1 55 ? 27.124 18.023 4.588 1.00 17.69 ? 55 PHE B CB 1 ATOM 2058 C CG . PHE B 1 55 ? 28.160 19.015 5.034 1.00 15.85 ? 55 PHE B CG 1 ATOM 2059 C CD1 . PHE B 1 55 ? 27.916 20.383 4.952 1.00 13.56 ? 55 PHE B CD1 1 ATOM 2060 C CD2 . PHE B 1 55 ? 29.357 18.578 5.599 1.00 16.92 ? 55 PHE B CD2 1 ATOM 2061 C CE1 . PHE B 1 55 ? 28.848 21.307 5.433 1.00 16.41 ? 55 PHE B CE1 1 ATOM 2062 C CE2 . PHE B 1 55 ? 30.297 19.495 6.085 1.00 23.68 ? 55 PHE B CE2 1 ATOM 2063 C CZ . PHE B 1 55 ? 30.039 20.863 6.001 1.00 18.10 ? 55 PHE B CZ 1 ATOM 2064 N N . GLN B 1 56 ? 29.243 18.132 2.140 1.00 20.41 ? 56 GLN B N 1 ATOM 2065 C CA . GLN B 1 56 ? 30.529 17.700 1.635 1.00 20.22 ? 56 GLN B CA 1 ATOM 2066 C C . GLN B 1 56 ? 31.664 18.498 2.251 1.00 21.92 ? 56 GLN B C 1 ATOM 2067 O O . GLN B 1 56 ? 31.611 19.723 2.347 1.00 26.13 ? 56 GLN B O 1 ATOM 2068 C CB . GLN B 1 56 ? 30.576 17.789 0.108 1.00 26.34 ? 56 GLN B CB 1 ATOM 2069 C CG . GLN B 1 56 ? 29.742 16.720 -0.584 1.00 35.71 ? 56 GLN B CG 1 ATOM 2070 C CD . GLN B 1 56 ? 29.643 16.915 -2.085 1.00 41.57 ? 56 GLN B CD 1 ATOM 2071 O OE1 . GLN B 1 56 ? 29.760 18.034 -2.593 1.00 41.39 ? 56 GLN B OE1 1 ATOM 2072 N NE2 . GLN B 1 56 ? 29.414 15.824 -2.807 1.00 46.42 ? 56 GLN B NE2 1 ATOM 2073 N N . ASP B 1 57 ? 32.649 17.764 2.746 1.00 19.80 ? 57 ASP B N 1 ATOM 2074 C CA . ASP B 1 57 ? 33.839 18.329 3.344 1.00 19.66 ? 57 ASP B CA 1 ATOM 2075 C C . ASP B 1 57 ? 34.932 17.612 2.565 1.00 24.38 ? 57 ASP B C 1 ATOM 2076 O O . ASP B 1 57 ? 35.308 16.486 2.898 1.00 23.76 ? 57 ASP B O 1 ATOM 2077 C CB . ASP B 1 57 ? 33.904 17.972 4.832 1.00 21.33 ? 57 ASP B CB 1 ATOM 2078 C CG . ASP B 1 57 ? 35.151 18.511 5.512 1.00 29.37 ? 57 ASP B CG 1 ATOM 2079 O OD1 . ASP B 1 57 ? 35.960 19.213 4.863 1.00 31.13 ? 57 ASP B OD1 1 ATOM 2080 O OD2 . ASP B 1 57 ? 35.323 18.240 6.716 1.00 31.27 ? 57 ASP B OD2 1 ATOM 2081 N N . GLY B 1 58 ? 35.412 18.252 1.502 1.00 23.00 ? 58 GLY B N 1 ATOM 2082 C CA . GLY B 1 58 ? 36.419 17.622 0.668 1.00 21.06 ? 58 GLY B CA 1 ATOM 2083 C C . GLY B 1 58 ? 35.688 16.504 -0.049 1.00 22.16 ? 58 GLY B C 1 ATOM 2084 O O . GLY B 1 58 ? 34.625 16.734 -0.627 1.00 27.12 ? 58 GLY B O 1 ATOM 2085 N N . ASP B 1 59 ? 36.210 15.285 0.025 1.00 28.11 ? 59 ASP B N 1 ATOM 2086 C CA . ASP B 1 59 ? 35.540 14.163 -0.624 1.00 35.77 ? 59 ASP B CA 1 ATOM 2087 C C . ASP B 1 59 ? 34.660 13.365 0.345 1.00 35.78 ? 59 ASP B C 1 ATOM 2088 O O . ASP B 1 59 ? 34.103 12.326 -0.021 1.00 37.51 ? 59 ASP B O 1 ATOM 2089 C CB . ASP B 1 59 ? 36.545 13.257 -1.356 1.00 42.69 ? 59 ASP B CB 1 ATOM 2090 C CG . ASP B 1 59 ? 37.405 12.430 -0.414 1.00 50.40 ? 59 ASP B CG 1 ATOM 2091 O OD1 . ASP B 1 59 ? 37.603 12.835 0.758 1.00 53.57 ? 59 ASP B OD1 1 ATOM 2092 O OD2 . ASP B 1 59 ? 37.898 11.372 -0.869 1.00 54.26 ? 59 ASP B OD2 1 ATOM 2093 N N . LEU B 1 60 ? 34.542 13.859 1.579 1.00 31.06 ? 60 LEU B N 1 ATOM 2094 C CA . LEU B 1 60 ? 33.711 13.213 2.591 1.00 25.13 ? 60 LEU B CA 1 ATOM 2095 C C . LEU B 1 60 ? 32.281 13.697 2.385 1.00 23.57 ? 60 LEU B C 1 ATOM 2096 O O . LEU B 1 60 ? 32.010 14.895 2.466 1.00 24.18 ? 60 LEU B O 1 ATOM 2097 C CB . LEU B 1 60 ? 34.175 13.600 3.999 1.00 23.83 ? 60 LEU B CB 1 ATOM 2098 C CG . LEU B 1 60 ? 33.950 12.636 5.174 1.00 23.92 ? 60 LEU B CG 1 ATOM 2099 C CD1 . LEU B 1 60 ? 33.643 13.432 6.425 1.00 18.58 ? 60 LEU B CD1 1 ATOM 2100 C CD2 . LEU B 1 60 ? 32.828 11.654 4.896 1.00 24.36 ? 60 LEU B CD2 1 ATOM 2101 N N . THR B 1 61 ? 31.378 12.767 2.094 1.00 22.69 ? 61 THR B N 1 ATOM 2102 C CA . THR B 1 61 ? 29.975 13.092 1.882 1.00 19.72 ? 61 THR B CA 1 ATOM 2103 C C . THR B 1 61 ? 29.190 12.613 3.100 1.00 25.74 ? 61 THR B C 1 ATOM 2104 O O . THR B 1 61 ? 29.277 11.445 3.483 1.00 28.39 ? 61 THR B O 1 ATOM 2105 C CB . THR B 1 61 ? 29.432 12.417 0.606 1.00 23.67 ? 61 THR B CB 1 ATOM 2106 O OG1 . THR B 1 61 ? 30.171 12.885 -0.530 1.00 26.64 ? 61 THR B OG1 1 ATOM 2107 C CG2 . THR B 1 61 ? 27.949 12.727 0.413 1.00 17.60 ? 61 THR B CG2 1 ATOM 2108 N N . LEU B 1 62 ? 28.434 13.525 3.704 1.00 22.33 ? 62 LEU B N 1 ATOM 2109 C CA . LEU B 1 62 ? 27.642 13.230 4.891 1.00 19.91 ? 62 LEU B CA 1 ATOM 2110 C C . LEU B 1 62 ? 26.154 13.511 4.715 1.00 18.73 ? 62 LEU B C 1 ATOM 2111 O O . LEU B 1 62 ? 25.751 14.300 3.862 1.00 20.87 ? 62 LEU B O 1 ATOM 2112 C CB . LEU B 1 62 ? 28.156 14.069 6.068 1.00 16.70 ? 62 LEU B CB 1 ATOM 2113 C CG . LEU B 1 62 ? 29.161 13.533 7.094 1.00 21.49 ? 62 LEU B CG 1 ATOM 2114 C CD1 . LEU B 1 62 ? 29.833 12.251 6.641 1.00 17.38 ? 62 LEU B CD1 1 ATOM 2115 C CD2 . LEU B 1 62 ? 30.181 14.617 7.399 1.00 15.96 ? 62 LEU B CD2 1 ATOM 2116 N N . TYR B 1 63 ? 25.348 12.821 5.513 1.00 16.77 ? 63 TYR B N 1 ATOM 2117 C CA . TYR B 1 63 ? 23.902 13.007 5.536 1.00 18.08 ? 63 TYR B CA 1 ATOM 2118 C C . TYR B 1 63 ? 23.547 13.126 7.016 1.00 14.44 ? 63 TYR B C 1 ATOM 2119 O O . TYR B 1 63 ? 24.398 12.882 7.872 1.00 19.30 ? 63 TYR B O 1 ATOM 2120 C CB . TYR B 1 63 ? 23.171 11.825 4.889 1.00 19.38 ? 63 TYR B CB 1 ATOM 2121 C CG . TYR B 1 63 ? 23.450 11.685 3.412 1.00 26.32 ? 63 TYR B CG 1 ATOM 2122 C CD1 . TYR B 1 63 ? 22.657 12.343 2.471 1.00 28.89 ? 63 TYR B CD1 1 ATOM 2123 C CD2 . TYR B 1 63 ? 24.521 10.918 2.952 1.00 23.96 ? 63 TYR B CD2 1 ATOM 2124 C CE1 . TYR B 1 63 ? 22.923 12.250 1.110 1.00 27.77 ? 63 TYR B CE1 1 ATOM 2125 C CE2 . TYR B 1 63 ? 24.797 10.818 1.590 1.00 27.29 ? 63 TYR B CE2 1 ATOM 2126 C CZ . TYR B 1 63 ? 23.994 11.488 0.674 1.00 30.44 ? 63 TYR B CZ 1 ATOM 2127 O OH . TYR B 1 63 ? 24.276 11.412 -0.670 1.00 28.82 ? 63 TYR B OH 1 ATOM 2128 N N . GLN B 1 64 ? 22.310 13.522 7.310 1.00 14.04 ? 64 GLN B N 1 ATOM 2129 C CA . GLN B 1 64 ? 21.836 13.696 8.685 1.00 15.23 ? 64 GLN B CA 1 ATOM 2130 C C . GLN B 1 64 ? 22.383 15.003 9.270 1.00 12.16 ? 64 GLN B C 1 ATOM 2131 O O . GLN B 1 64 ? 23.583 15.137 9.514 1.00 12.06 ? 64 GLN B O 1 ATOM 2132 C CB . GLN B 1 64 ? 22.230 12.490 9.551 1.00 16.44 ? 64 GLN B CB 1 ATOM 2133 C CG . GLN B 1 64 ? 21.594 11.170 9.112 1.00 16.05 ? 64 GLN B CG 1 ATOM 2134 C CD . GLN B 1 64 ? 20.127 11.068 9.493 1.00 17.17 ? 64 GLN B CD 1 ATOM 2135 O OE1 . GLN B 1 64 ? 19.565 11.983 10.087 1.00 17.01 ? 64 GLN B OE1 1 ATOM 2136 N NE2 . GLN B 1 64 ? 19.499 9.946 9.151 1.00 17.18 ? 64 GLN B NE2 1 ATOM 2137 N N . SER B 1 65 ? 21.486 15.962 9.485 1.00 11.92 ? 65 SER B N 1 ATOM 2138 C CA . SER B 1 65 ? 21.850 17.276 10.004 1.00 12.45 ? 65 SER B CA 1 ATOM 2139 C C . SER B 1 65 ? 22.703 17.242 11.274 1.00 14.60 ? 65 SER B C 1 ATOM 2140 O O . SER B 1 65 ? 23.700 17.964 11.365 1.00 16.80 ? 65 SER B O 1 ATOM 2141 C CB . SER B 1 65 ? 20.598 18.118 10.231 1.00 11.86 ? 65 SER B CB 1 ATOM 2142 O OG . SER B 1 65 ? 19.717 17.484 11.140 1.00 15.75 ? 65 SER B OG 1 ATOM 2143 N N . ASN B 1 66 ? 22.332 16.392 12.232 1.00 12.08 ? 66 ASN B N 1 ATOM 2144 C CA . ASN B 1 66 ? 23.085 16.286 13.484 1.00 12.31 ? 66 ASN B CA 1 ATOM 2145 C C . ASN B 1 66 ? 24.467 15.659 13.316 1.00 12.87 ? 66 ASN B C 1 ATOM 2146 O O . ASN B 1 66 ? 25.384 15.963 14.080 1.00 14.94 ? 66 ASN B O 1 ATOM 2147 C CB . ASN B 1 66 ? 22.277 15.536 14.550 1.00 14.74 ? 66 ASN B CB 1 ATOM 2148 C CG . ASN B 1 66 ? 21.072 16.325 15.011 1.00 15.06 ? 66 ASN B CG 1 ATOM 2149 O OD1 . ASN B 1 66 ? 21.211 17.435 15.525 1.00 15.55 ? 66 ASN B OD1 1 ATOM 2150 N ND2 . ASN B 1 66 ? 19.884 15.766 14.821 1.00 9.00 ? 66 ASN B ND2 1 ATOM 2151 N N . THR B 1 67 ? 24.619 14.775 12.331 1.00 14.29 ? 67 THR B N 1 ATOM 2152 C CA . THR B 1 67 ? 25.917 14.162 12.058 1.00 11.84 ? 67 THR B CA 1 ATOM 2153 C C . THR B 1 67 ? 26.813 15.281 11.531 1.00 13.44 ? 67 THR B C 1 ATOM 2154 O O . THR B 1 67 ? 27.978 15.382 11.898 1.00 13.87 ? 67 THR B O 1 ATOM 2155 C CB . THR B 1 67 ? 25.813 13.043 11.010 1.00 10.79 ? 67 THR B CB 1 ATOM 2156 O OG1 . THR B 1 67 ? 25.137 11.924 11.586 1.00 11.75 ? 67 THR B OG1 1 ATOM 2157 C CG2 . THR B 1 67 ? 27.182 12.605 10.546 1.00 8.81 ? 67 THR B CG2 1 ATOM 2158 N N . ILE B 1 68 ? 26.239 16.141 10.693 1.00 13.29 ? 68 ILE B N 1 ATOM 2159 C CA . ILE B 1 68 ? 26.965 17.275 10.130 1.00 15.73 ? 68 ILE B CA 1 ATOM 2160 C C . ILE B 1 68 ? 27.392 18.204 11.272 1.00 15.23 ? 68 ILE B C 1 ATOM 2161 O O . ILE B 1 68 ? 28.549 18.622 11.333 1.00 14.20 ? 68 ILE B O 1 ATOM 2162 C CB . ILE B 1 68 ? 26.089 18.036 9.109 1.00 18.12 ? 68 ILE B CB 1 ATOM 2163 C CG1 . ILE B 1 68 ? 25.690 17.090 7.972 1.00 12.03 ? 68 ILE B CG1 1 ATOM 2164 C CG2 . ILE B 1 68 ? 26.846 19.242 8.554 1.00 12.44 ? 68 ILE B CG2 1 ATOM 2165 C CD1 . ILE B 1 68 ? 24.511 17.563 7.158 1.00 10.03 ? 68 ILE B CD1 1 ATOM 2166 N N . LEU B 1 69 ? 26.470 18.492 12.192 1.00 10.94 ? 69 LEU B N 1 ATOM 2167 C CA . LEU B 1 69 ? 26.774 19.346 13.342 1.00 14.30 ? 69 LEU B CA 1 ATOM 2168 C C . LEU B 1 69 ? 27.904 18.758 14.187 1.00 16.71 ? 69 LEU B C 1 ATOM 2169 O O . LEU B 1 69 ? 28.863 19.456 14.527 1.00 18.11 ? 69 LEU B O 1 ATOM 2170 C CB . LEU B 1 69 ? 25.532 19.556 14.215 1.00 10.62 ? 69 LEU B CB 1 ATOM 2171 C CG . LEU B 1 69 ? 24.531 20.606 13.735 1.00 13.60 ? 69 LEU B CG 1 ATOM 2172 C CD1 . LEU B 1 69 ? 23.316 20.609 14.632 1.00 17.41 ? 69 LEU B CD1 1 ATOM 2173 C CD2 . LEU B 1 69 ? 25.189 21.984 13.736 1.00 14.10 ? 69 LEU B CD2 1 ATOM 2174 N N . ARG B 1 70 ? 27.813 17.462 14.483 1.00 17.46 ? 70 ARG B N 1 ATOM 2175 C CA . ARG B 1 70 ? 28.833 16.794 15.287 1.00 14.70 ? 70 ARG B CA 1 ATOM 2176 C C . ARG B 1 70 ? 30.183 16.747 14.589 1.00 16.69 ? 70 ARG B C 1 ATOM 2177 O O . ARG B 1 70 ? 31.228 16.885 15.230 1.00 15.84 ? 70 ARG B O 1 ATOM 2178 C CB . ARG B 1 70 ? 28.378 15.391 15.690 1.00 16.11 ? 70 ARG B CB 1 ATOM 2179 C CG . ARG B 1 70 ? 27.299 15.417 16.749 1.00 17.77 ? 70 ARG B CG 1 ATOM 2180 C CD . ARG B 1 70 ? 26.967 14.039 17.299 1.00 17.69 ? 70 ARG B CD 1 ATOM 2181 N NE . ARG B 1 70 ? 26.195 14.177 18.530 1.00 16.07 ? 70 ARG B NE 1 ATOM 2182 C CZ . ARG B 1 70 ? 24.867 14.161 18.600 1.00 18.45 ? 70 ARG B CZ 1 ATOM 2183 N NH1 . ARG B 1 70 ? 24.140 13.991 17.503 1.00 16.73 ? 70 ARG B NH1 1 ATOM 2184 N NH2 . ARG B 1 70 ? 24.264 14.389 19.760 1.00 13.69 ? 70 ARG B NH2 1 ATOM 2185 N N . HIS B 1 71 ? 30.154 16.584 13.270 1.00 16.68 ? 71 HIS B N 1 ATOM 2186 C CA . HIS B 1 71 ? 31.377 16.538 12.484 1.00 16.33 ? 71 HIS B CA 1 ATOM 2187 C C . HIS B 1 71 ? 32.098 17.883 12.556 1.00 16.31 ? 71 HIS B C 1 ATOM 2188 O O . HIS B 1 71 ? 33.309 17.940 12.777 1.00 23.11 ? 71 HIS B O 1 ATOM 2189 C CB . HIS B 1 71 ? 31.061 16.192 11.029 1.00 19.10 ? 71 HIS B CB 1 ATOM 2190 C CG . HIS B 1 71 ? 32.245 16.289 10.127 1.00 14.31 ? 71 HIS B CG 1 ATOM 2191 N ND1 . HIS B 1 71 ? 33.357 15.491 10.279 1.00 16.91 ? 71 HIS B ND1 1 ATOM 2192 C CD2 . HIS B 1 71 ? 32.519 17.127 9.101 1.00 19.97 ? 71 HIS B CD2 1 ATOM 2193 C CE1 . HIS B 1 71 ? 34.270 15.836 9.388 1.00 17.30 ? 71 HIS B CE1 1 ATOM 2194 N NE2 . HIS B 1 71 ? 33.786 16.828 8.662 1.00 21.25 ? 71 HIS B NE2 1 ATOM 2195 N N . LEU B 1 72 ? 31.345 18.959 12.349 1.00 19.96 ? 72 LEU B N 1 ATOM 2196 C CA . LEU B 1 72 ? 31.890 20.314 12.404 1.00 18.68 ? 72 LEU B CA 1 ATOM 2197 C C . LEU B 1 72 ? 32.360 20.642 13.825 1.00 20.71 ? 72 LEU B C 1 ATOM 2198 O O . LEU B 1 72 ? 33.411 21.261 14.010 1.00 19.88 ? 72 LEU B O 1 ATOM 2199 C CB . LEU B 1 72 ? 30.833 21.325 11.944 1.00 15.33 ? 72 LEU B CB 1 ATOM 2200 C CG . LEU B 1 72 ? 30.828 21.810 10.486 1.00 19.43 ? 72 LEU B CG 1 ATOM 2201 C CD1 . LEU B 1 72 ? 31.622 20.888 9.583 1.00 25.39 ? 72 LEU B CD1 1 ATOM 2202 C CD2 . LEU B 1 72 ? 29.393 21.953 9.991 1.00 11.24 ? 72 LEU B CD2 1 ATOM 2203 N N . GLY B 1 73 ? 31.594 20.197 14.821 1.00 14.96 ? 73 GLY B N 1 ATOM 2204 C CA . GLY B 1 73 ? 31.957 20.446 16.206 1.00 14.21 ? 73 GLY B CA 1 ATOM 2205 C C . GLY B 1 73 ? 33.255 19.749 16.563 1.00 19.62 ? 73 GLY B C 1 ATOM 2206 O O . GLY B 1 73 ? 34.080 20.275 17.301 1.00 25.40 ? 73 GLY B O 1 ATOM 2207 N N . ARG B 1 74 ? 33.459 18.575 15.984 1.00 20.36 ? 74 ARG B N 1 ATOM 2208 C CA . ARG B 1 74 ? 34.656 17.789 16.232 1.00 22.21 ? 74 ARG B CA 1 ATOM 2209 C C . ARG B 1 74 ? 35.887 18.368 15.528 1.00 24.14 ? 74 ARG B C 1 ATOM 2210 O O . ARG B 1 74 ? 36.944 18.524 16.140 1.00 23.68 ? 74 ARG B O 1 ATOM 2211 C CB . ARG B 1 74 ? 34.399 16.351 15.776 1.00 23.20 ? 74 ARG B CB 1 ATOM 2212 C CG . ARG B 1 74 ? 35.316 15.295 16.361 1.00 25.97 ? 74 ARG B CG 1 ATOM 2213 C CD . ARG B 1 74 ? 34.562 13.971 16.477 1.00 18.40 ? 74 ARG B CD 1 ATOM 2214 N NE . ARG B 1 74 ? 33.709 13.769 15.313 1.00 19.99 ? 74 ARG B NE 1 ATOM 2215 C CZ . ARG B 1 74 ? 32.470 13.288 15.352 1.00 19.18 ? 74 ARG B CZ 1 ATOM 2216 N NH1 . ARG B 1 74 ? 31.919 12.931 16.502 1.00 16.06 ? 74 ARG B NH1 1 ATOM 2217 N NH2 . ARG B 1 74 ? 31.748 13.248 14.242 1.00 14.93 ? 74 ARG B NH2 1 ATOM 2218 N N . THR B 1 75 ? 35.740 18.711 14.250 1.00 24.37 ? 75 THR B N 1 ATOM 2219 C CA . THR B 1 75 ? 36.852 19.252 13.466 1.00 22.93 ? 75 THR B CA 1 ATOM 2220 C C . THR B 1 75 ? 37.203 20.705 13.780 1.00 23.45 ? 75 THR B C 1 ATOM 2221 O O . THR B 1 75 ? 38.362 21.099 13.670 1.00 26.31 ? 75 THR B O 1 ATOM 2222 C CB . THR B 1 75 ? 36.596 19.118 11.949 1.00 22.94 ? 75 THR B CB 1 ATOM 2223 O OG1 . THR B 1 75 ? 35.351 19.744 11.617 1.00 24.40 ? 75 THR B OG1 1 ATOM 2224 C CG2 . THR B 1 75 ? 36.543 17.648 11.536 1.00 17.38 ? 75 THR B CG2 1 ATOM 2225 N N . LEU B 1 76 ? 36.206 21.494 14.171 1.00 21.16 ? 76 LEU B N 1 ATOM 2226 C CA . LEU B 1 76 ? 36.416 22.904 14.497 1.00 21.72 ? 76 LEU B CA 1 ATOM 2227 C C . LEU B 1 76 ? 36.640 23.192 15.986 1.00 22.20 ? 76 LEU B C 1 ATOM 2228 O O . LEU B 1 76 ? 36.898 24.333 16.366 1.00 19.86 ? 76 LEU B O 1 ATOM 2229 C CB . LEU B 1 76 ? 35.251 23.743 13.971 1.00 21.04 ? 76 LEU B CB 1 ATOM 2230 C CG . LEU B 1 76 ? 35.359 24.339 12.566 1.00 23.96 ? 76 LEU B CG 1 ATOM 2231 C CD1 . LEU B 1 76 ? 36.216 23.475 11.659 1.00 23.60 ? 76 LEU B CD1 1 ATOM 2232 C CD2 . LEU B 1 76 ? 33.962 24.527 11.995 1.00 18.34 ? 76 LEU B CD2 1 ATOM 2233 N N . GLY B 1 77 ? 36.537 22.160 16.822 1.00 25.08 ? 77 GLY B N 1 ATOM 2234 C CA . GLY B 1 77 ? 36.747 22.332 18.252 1.00 21.49 ? 77 GLY B CA 1 ATOM 2235 C C . GLY B 1 77 ? 35.595 22.964 19.020 1.00 22.81 ? 77 GLY B C 1 ATOM 2236 O O . GLY B 1 77 ? 35.814 23.785 19.912 1.00 26.73 ? 77 GLY B O 1 ATOM 2237 N N . LEU B 1 78 ? 34.369 22.585 18.670 1.00 19.13 ? 78 LEU B N 1 ATOM 2238 C CA . LEU B 1 78 ? 33.165 23.092 19.325 1.00 17.81 ? 78 LEU B CA 1 ATOM 2239 C C . LEU B 1 78 ? 32.432 21.911 19.972 1.00 19.78 ? 78 LEU B C 1 ATOM 2240 O O . LEU B 1 78 ? 31.208 21.791 19.861 1.00 17.32 ? 78 LEU B O 1 ATOM 2241 C CB . LEU B 1 78 ? 32.247 23.751 18.288 1.00 19.37 ? 78 LEU B CB 1 ATOM 2242 C CG . LEU B 1 78 ? 32.854 24.715 17.265 1.00 21.63 ? 78 LEU B CG 1 ATOM 2243 C CD1 . LEU B 1 78 ? 31.762 25.193 16.324 1.00 24.18 ? 78 LEU B CD1 1 ATOM 2244 C CD2 . LEU B 1 78 ? 33.512 25.889 17.962 1.00 15.44 ? 78 LEU B CD2 1 ATOM 2245 N N . TYR B 1 79 ? 33.180 21.071 20.686 1.00 19.64 ? 79 TYR B N 1 ATOM 2246 C CA . TYR B 1 79 ? 32.618 19.874 21.312 1.00 20.25 ? 79 TYR B CA 1 ATOM 2247 C C . TYR B 1 79 ? 33.033 19.698 22.782 1.00 21.38 ? 79 TYR B C 1 ATOM 2248 O O . TYR B 1 79 ? 33.209 18.571 23.251 1.00 26.49 ? 79 TYR B O 1 ATOM 2249 C CB . TYR B 1 79 ? 33.076 18.653 20.502 1.00 22.97 ? 79 TYR B CB 1 ATOM 2250 C CG . TYR B 1 79 ? 32.037 17.573 20.309 1.00 18.41 ? 79 TYR B CG 1 ATOM 2251 C CD1 . TYR B 1 79 ? 31.193 17.188 21.353 1.00 13.93 ? 79 TYR B CD1 1 ATOM 2252 C CD2 . TYR B 1 79 ? 31.906 16.929 19.079 1.00 15.23 ? 79 TYR B CD2 1 ATOM 2253 C CE1 . TYR B 1 79 ? 30.243 16.189 21.177 1.00 13.05 ? 79 TYR B CE1 1 ATOM 2254 C CE2 . TYR B 1 79 ? 30.960 15.927 18.891 1.00 17.16 ? 79 TYR B CE2 1 ATOM 2255 C CZ . TYR B 1 79 ? 30.129 15.563 19.946 1.00 19.13 ? 79 TYR B CZ 1 ATOM 2256 O OH . TYR B 1 79 ? 29.176 14.589 19.760 1.00 14.15 ? 79 TYR B OH 1 ATOM 2257 N N . GLY B 1 80 ? 33.160 20.807 23.508 1.00 19.91 ? 80 GLY B N 1 ATOM 2258 C CA . GLY B 1 80 ? 33.561 20.748 24.908 1.00 13.93 ? 80 GLY B CA 1 ATOM 2259 C C . GLY B 1 80 ? 35.066 20.664 25.082 1.00 18.01 ? 80 GLY B C 1 ATOM 2260 O O . GLY B 1 80 ? 35.788 20.366 24.130 1.00 18.02 ? 80 GLY B O 1 ATOM 2261 N N . LYS B 1 81 ? 35.547 20.902 26.299 1.00 20.25 ? 81 LYS B N 1 ATOM 2262 C CA . LYS B 1 81 ? 36.982 20.858 26.564 1.00 24.80 ? 81 LYS B CA 1 ATOM 2263 C C . LYS B 1 81 ? 37.467 19.447 26.886 1.00 22.49 ? 81 LYS B C 1 ATOM 2264 O O . LYS B 1 81 ? 38.660 19.159 26.798 1.00 26.88 ? 81 LYS B O 1 ATOM 2265 C CB . LYS B 1 81 ? 37.359 21.824 27.693 1.00 29.28 ? 81 LYS B CB 1 ATOM 2266 C CG . LYS B 1 81 ? 36.887 21.391 29.062 1.00 40.93 ? 81 LYS B CG 1 ATOM 2267 C CD . LYS B 1 81 ? 37.378 22.337 30.143 1.00 46.44 ? 81 LYS B CD 1 ATOM 2268 C CE . LYS B 1 81 ? 37.171 21.740 31.527 1.00 47.73 ? 81 LYS B CE 1 ATOM 2269 N NZ . LYS B 1 81 ? 35.744 21.403 31.797 1.00 53.48 ? 81 LYS B NZ 1 ATOM 2270 N N . ASP B 1 82 ? 36.541 18.570 27.260 1.00 19.00 ? 82 ASP B N 1 ATOM 2271 C CA . ASP B 1 82 ? 36.883 17.188 27.580 1.00 21.26 ? 82 ASP B CA 1 ATOM 2272 C C . ASP B 1 82 ? 35.704 16.241 27.343 1.00 16.97 ? 82 ASP B C 1 ATOM 2273 O O . ASP B 1 82 ? 34.642 16.671 26.892 1.00 18.12 ? 82 ASP B O 1 ATOM 2274 C CB . ASP B 1 82 ? 37.418 17.072 29.019 1.00 23.12 ? 82 ASP B CB 1 ATOM 2275 C CG . ASP B 1 82 ? 36.453 17.617 30.071 1.00 26.23 ? 82 ASP B CG 1 ATOM 2276 O OD1 . ASP B 1 82 ? 35.220 17.546 29.888 1.00 28.04 ? 82 ASP B OD1 1 ATOM 2277 O OD2 . ASP B 1 82 ? 36.942 18.108 31.108 1.00 32.29 ? 82 ASP B OD2 1 ATOM 2278 N N . GLN B 1 83 ? 35.884 14.960 27.665 1.00 17.70 ? 83 GLN B N 1 ATOM 2279 C CA . GLN B 1 83 ? 34.834 13.962 27.465 1.00 21.24 ? 83 GLN B CA 1 ATOM 2280 C C . GLN B 1 83 ? 33.572 14.230 28.261 1.00 18.81 ? 83 GLN B C 1 ATOM 2281 O O . GLN B 1 83 ? 32.466 14.012 27.765 1.00 21.48 ? 83 GLN B O 1 ATOM 2282 C CB . GLN B 1 83 ? 35.340 12.555 27.766 1.00 23.61 ? 83 GLN B CB 1 ATOM 2283 C CG . GLN B 1 83 ? 36.347 12.027 26.760 1.00 30.28 ? 83 GLN B CG 1 ATOM 2284 C CD . GLN B 1 83 ? 36.828 10.626 27.100 1.00 34.94 ? 83 GLN B CD 1 ATOM 2285 O OE1 . GLN B 1 83 ? 37.203 9.861 26.217 1.00 35.76 ? 83 GLN B OE1 1 ATOM 2286 N NE2 . GLN B 1 83 ? 36.837 10.292 28.390 1.00 32.08 ? 83 GLN B NE2 1 ATOM 2287 N N . GLN B 1 84 ? 33.729 14.703 29.492 1.00 20.99 ? 84 GLN B N 1 ATOM 2288 C CA . GLN B 1 84 ? 32.572 15.001 30.328 1.00 25.50 ? 84 GLN B CA 1 ATOM 2289 C C . GLN B 1 84 ? 31.706 16.068 29.664 1.00 21.51 ? 84 GLN B C 1 ATOM 2290 O O . GLN B 1 84 ? 30.487 15.904 29.555 1.00 19.93 ? 84 GLN B O 1 ATOM 2291 C CB . GLN B 1 84 ? 33.003 15.462 31.721 1.00 33.46 ? 84 GLN B CB 1 ATOM 2292 C CG . GLN B 1 84 ? 31.832 15.842 32.616 1.00 45.68 ? 84 GLN B CG 1 ATOM 2293 C CD . GLN B 1 84 ? 32.243 16.103 34.049 1.00 53.55 ? 84 GLN B CD 1 ATOM 2294 O OE1 . GLN B 1 84 ? 33.021 15.347 34.629 1.00 49.34 ? 84 GLN B OE1 1 ATOM 2295 N NE2 . GLN B 1 84 ? 31.713 17.174 34.631 1.00 62.37 ? 84 GLN B NE2 1 ATOM 2296 N N . GLU B 1 85 ? 32.346 17.141 29.197 1.00 17.09 ? 85 GLU B N 1 ATOM 2297 C CA . GLU B 1 85 ? 31.629 18.223 28.526 1.00 21.44 ? 85 GLU B CA 1 ATOM 2298 C C . GLU B 1 85 ? 31.038 17.732 27.213 1.00 19.55 ? 85 GLU B C 1 ATOM 2299 O O . GLU B 1 85 ? 29.926 18.118 26.856 1.00 15.23 ? 85 GLU B O 1 ATOM 2300 C CB . GLU B 1 85 ? 32.541 19.426 28.269 1.00 21.97 ? 85 GLU B CB 1 ATOM 2301 C CG . GLU B 1 85 ? 33.034 20.106 29.532 1.00 22.81 ? 85 GLU B CG 1 ATOM 2302 C CD . GLU B 1 85 ? 33.398 21.567 29.325 1.00 30.73 ? 85 GLU B CD 1 ATOM 2303 O OE1 . GLU B 1 85 ? 33.661 21.982 28.173 1.00 27.65 ? 85 GLU B OE1 1 ATOM 2304 O OE2 . GLU B 1 85 ? 33.404 22.308 30.332 1.00 32.23 ? 85 GLU B OE2 1 ATOM 2305 N N . ALA B 1 86 ? 31.776 16.866 26.514 1.00 16.11 ? 86 ALA B N 1 ATOM 2306 C CA . ALA B 1 86 ? 31.319 16.303 25.245 1.00 13.70 ? 86 ALA B CA 1 ATOM 2307 C C . ALA B 1 86 ? 30.008 15.557 25.452 1.00 16.13 ? 86 ALA B C 1 ATOM 2308 O O . ALA B 1 86 ? 29.086 15.662 24.636 1.00 18.51 ? 86 ALA B O 1 ATOM 2309 C CB . ALA B 1 86 ? 32.370 15.372 24.672 1.00 10.98 ? 86 ALA B CB 1 ATOM 2310 N N . ALA B 1 87 ? 29.919 14.829 26.565 1.00 16.89 ? 87 ALA B N 1 ATOM 2311 C CA . ALA B 1 87 ? 28.711 14.078 26.897 1.00 16.48 ? 87 ALA B CA 1 ATOM 2312 C C . ALA B 1 87 ? 27.547 15.033 27.175 1.00 16.98 ? 87 ALA B C 1 ATOM 2313 O O . ALA B 1 87 ? 26.414 14.784 26.757 1.00 15.22 ? 87 ALA B O 1 ATOM 2314 C CB . ALA B 1 87 ? 28.963 13.181 28.101 1.00 16.88 ? 87 ALA B CB 1 ATOM 2315 N N . LEU B 1 88 ? 27.836 16.138 27.862 1.00 19.94 ? 88 LEU B N 1 ATOM 2316 C CA . LEU B 1 88 ? 26.813 17.132 28.189 1.00 17.75 ? 88 LEU B CA 1 ATOM 2317 C C . LEU B 1 88 ? 26.309 17.856 26.939 1.00 15.35 ? 88 LEU B C 1 ATOM 2318 O O . LEU B 1 88 ? 25.115 18.135 26.813 1.00 14.44 ? 88 LEU B O 1 ATOM 2319 C CB . LEU B 1 88 ? 27.346 18.130 29.221 1.00 17.60 ? 88 LEU B CB 1 ATOM 2320 C CG . LEU B 1 88 ? 27.814 17.500 30.538 1.00 23.29 ? 88 LEU B CG 1 ATOM 2321 C CD1 . LEU B 1 88 ? 28.291 18.577 31.499 1.00 18.27 ? 88 LEU B CD1 1 ATOM 2322 C CD2 . LEU B 1 88 ? 26.685 16.686 31.159 1.00 17.93 ? 88 LEU B CD2 1 ATOM 2323 N N . VAL B 1 89 ? 27.222 18.129 26.006 1.00 15.34 ? 89 VAL B N 1 ATOM 2324 C CA . VAL B 1 89 ? 26.884 18.790 24.745 1.00 15.99 ? 89 VAL B CA 1 ATOM 2325 C C . VAL B 1 89 ? 25.902 17.905 23.963 1.00 18.47 ? 89 VAL B C 1 ATOM 2326 O O . VAL B 1 89 ? 24.910 18.398 23.412 1.00 14.65 ? 89 VAL B O 1 ATOM 2327 C CB . VAL B 1 89 ? 28.152 19.048 23.890 1.00 17.28 ? 89 VAL B CB 1 ATOM 2328 C CG1 . VAL B 1 89 ? 27.769 19.597 22.529 1.00 18.91 ? 89 VAL B CG1 1 ATOM 2329 C CG2 . VAL B 1 89 ? 29.079 20.024 24.603 1.00 14.77 ? 89 VAL B CG2 1 ATOM 2330 N N . ASP B 1 90 ? 26.182 16.598 23.937 1.00 15.26 ? 90 ASP B N 1 ATOM 2331 C CA . ASP B 1 90 ? 25.326 15.624 23.261 1.00 12.80 ? 90 ASP B CA 1 ATOM 2332 C C . ASP B 1 90 ? 23.949 15.585 23.907 1.00 13.24 ? 90 ASP B C 1 ATOM 2333 O O . ASP B 1 90 ? 22.933 15.535 23.218 1.00 13.97 ? 90 ASP B O 1 ATOM 2334 C CB . ASP B 1 90 ? 25.940 14.218 23.323 1.00 14.48 ? 90 ASP B CB 1 ATOM 2335 C CG . ASP B 1 90 ? 27.019 14.002 22.289 1.00 15.65 ? 90 ASP B CG 1 ATOM 2336 O OD1 . ASP B 1 90 ? 26.959 14.637 21.213 1.00 14.40 ? 90 ASP B OD1 1 ATOM 2337 O OD2 . ASP B 1 90 ? 27.936 13.204 22.566 1.00 17.26 ? 90 ASP B OD2 1 ATOM 2338 N N . MET B 1 91 ? 23.924 15.588 25.238 1.00 14.36 ? 91 MET B N 1 ATOM 2339 C CA . MET B 1 91 ? 22.672 15.555 25.986 1.00 12.69 ? 91 MET B CA 1 ATOM 2340 C C . MET B 1 91 ? 21.813 16.771 25.659 1.00 11.09 ? 91 MET B C 1 ATOM 2341 O O . MET B 1 91 ? 20.588 16.663 25.543 1.00 10.93 ? 91 MET B O 1 ATOM 2342 C CB . MET B 1 91 ? 22.956 15.477 27.488 1.00 14.64 ? 91 MET B CB 1 ATOM 2343 C CG . MET B 1 91 ? 21.707 15.396 28.351 1.00 19.85 ? 91 MET B CG 1 ATOM 2344 S SD . MET B 1 91 ? 22.102 15.155 30.091 1.00 18.21 ? 91 MET B SD 1 ATOM 2345 C CE . MET B 1 91 ? 23.017 16.647 30.464 1.00 23.76 ? 91 MET B CE 1 ATOM 2346 N N . VAL B 1 92 ? 22.458 17.927 25.515 1.00 10.63 ? 92 VAL B N 1 ATOM 2347 C CA . VAL B 1 92 ? 21.746 19.157 25.170 1.00 10.30 ? 92 VAL B CA 1 ATOM 2348 C C . VAL B 1 92 ? 21.214 19.040 23.741 1.00 11.62 ? 92 VAL B C 1 ATOM 2349 O O . VAL B 1 92 ? 20.031 19.262 23.500 1.00 10.63 ? 92 VAL B O 1 ATOM 2350 C CB . VAL B 1 92 ? 22.671 20.407 25.281 1.00 14.19 ? 92 VAL B CB 1 ATOM 2351 C CG1 . VAL B 1 92 ? 21.952 21.644 24.752 1.00 10.37 ? 92 VAL B CG1 1 ATOM 2352 C CG2 . VAL B 1 92 ? 23.086 20.631 26.732 1.00 7.97 ? 92 VAL B CG2 1 ATOM 2353 N N . ASN B 1 93 ? 22.072 18.629 22.808 1.00 14.15 ? 93 ASN B N 1 ATOM 2354 C CA . ASN B 1 93 ? 21.668 18.489 21.410 1.00 13.30 ? 93 ASN B CA 1 ATOM 2355 C C . ASN B 1 93 ? 20.535 17.488 21.208 1.00 13.41 ? 93 ASN B C 1 ATOM 2356 O O . ASN B 1 93 ? 19.615 17.745 20.426 1.00 12.03 ? 93 ASN B O 1 ATOM 2357 C CB . ASN B 1 93 ? 22.855 18.117 20.516 1.00 14.30 ? 93 ASN B CB 1 ATOM 2358 C CG . ASN B 1 93 ? 22.628 18.539 19.071 1.00 22.01 ? 93 ASN B CG 1 ATOM 2359 O OD1 . ASN B 1 93 ? 22.579 19.731 18.777 1.00 19.95 ? 93 ASN B OD1 1 ATOM 2360 N ND2 . ASN B 1 93 ? 22.480 17.570 18.173 1.00 15.93 ? 93 ASN B ND2 1 ATOM 2361 N N . ASP B 1 94 ? 20.599 16.355 21.910 1.00 11.97 ? 94 ASP B N 1 ATOM 2362 C CA . ASP B 1 94 ? 19.549 15.339 21.806 1.00 9.81 ? 94 ASP B CA 1 ATOM 2363 C C . ASP B 1 94 ? 18.238 15.923 22.316 1.00 12.96 ? 94 ASP B C 1 ATOM 2364 O O . ASP B 1 94 ? 17.166 15.611 21.793 1.00 17.36 ? 94 ASP B O 1 ATOM 2365 C CB . ASP B 1 94 ? 19.918 14.083 22.604 1.00 14.72 ? 94 ASP B CB 1 ATOM 2366 C CG . ASP B 1 94 ? 21.011 13.259 21.939 1.00 18.65 ? 94 ASP B CG 1 ATOM 2367 O OD1 . ASP B 1 94 ? 21.498 13.644 20.856 1.00 22.92 ? 94 ASP B OD1 1 ATOM 2368 O OD2 . ASP B 1 94 ? 21.404 12.224 22.509 1.00 24.15 ? 94 ASP B OD2 1 ATOM 2369 N N . GLY B 1 95 ? 18.336 16.778 23.333 1.00 12.02 ? 95 GLY B N 1 ATOM 2370 C CA . GLY B 1 95 ? 17.158 17.425 23.879 1.00 9.93 ? 95 GLY B CA 1 ATOM 2371 C C . GLY B 1 95 ? 16.588 18.374 22.842 1.00 14.76 ? 95 GLY B C 1 ATOM 2372 O O . GLY B 1 95 ? 15.378 18.397 22.616 1.00 14.61 ? 95 GLY B O 1 ATOM 2373 N N . VAL B 1 96 ? 17.463 19.141 22.190 1.00 14.66 ? 96 VAL B N 1 ATOM 2374 C CA . VAL B 1 96 ? 17.038 20.080 21.154 1.00 15.34 ? 96 VAL B CA 1 ATOM 2375 C C . VAL B 1 96 ? 16.352 19.311 20.018 1.00 20.89 ? 96 VAL B C 1 ATOM 2376 O O . VAL B 1 96 ? 15.270 19.694 19.564 1.00 15.99 ? 96 VAL B O 1 ATOM 2377 C CB . VAL B 1 96 ? 18.241 20.868 20.583 1.00 16.44 ? 96 VAL B CB 1 ATOM 2378 C CG1 . VAL B 1 96 ? 17.815 21.698 19.370 1.00 12.22 ? 96 VAL B CG1 1 ATOM 2379 C CG2 . VAL B 1 96 ? 18.839 21.762 21.660 1.00 14.38 ? 96 VAL B CG2 1 ATOM 2380 N N . GLU B 1 97 ? 16.970 18.204 19.602 1.00 22.54 ? 97 GLU B N 1 ATOM 2381 C CA . GLU B 1 97 ? 16.447 17.363 18.527 1.00 19.29 ? 97 GLU B CA 1 ATOM 2382 C C . GLU B 1 97 ? 15.045 16.827 18.829 1.00 17.91 ? 97 GLU B C 1 ATOM 2383 O O . GLU B 1 97 ? 14.189 16.795 17.943 1.00 17.10 ? 97 GLU B O 1 ATOM 2384 C CB . GLU B 1 97 ? 17.425 16.217 18.231 1.00 16.07 ? 97 GLU B CB 1 ATOM 2385 C CG . GLU B 1 97 ? 16.930 15.182 17.217 1.00 21.39 ? 97 GLU B CG 1 ATOM 2386 C CD . GLU B 1 97 ? 16.542 15.782 15.868 1.00 26.63 ? 97 GLU B CD 1 ATOM 2387 O OE1 . GLU B 1 97 ? 17.213 16.728 15.403 1.00 26.23 ? 97 GLU B OE1 1 ATOM 2388 O OE2 . GLU B 1 97 ? 15.558 15.300 15.270 1.00 26.95 ? 97 GLU B OE2 1 ATOM 2389 N N . ASP B 1 98 ? 14.811 16.422 20.078 1.00 17.96 ? 98 ASP B N 1 ATOM 2390 C CA . ASP B 1 98 ? 13.501 15.916 20.485 1.00 14.82 ? 98 ASP B CA 1 ATOM 2391 C C . ASP B 1 98 ? 12.428 16.985 20.324 1.00 14.91 ? 98 ASP B C 1 ATOM 2392 O O . ASP B 1 98 ? 11.354 16.722 19.773 1.00 16.61 ? 98 ASP B O 1 ATOM 2393 C CB . ASP B 1 98 ? 13.523 15.428 21.941 1.00 21.11 ? 98 ASP B CB 1 ATOM 2394 C CG . ASP B 1 98 ? 14.125 14.036 22.094 1.00 25.97 ? 98 ASP B CG 1 ATOM 2395 O OD1 . ASP B 1 98 ? 14.294 13.323 21.080 1.00 26.80 ? 98 ASP B OD1 1 ATOM 2396 O OD2 . ASP B 1 98 ? 14.436 13.658 23.242 1.00 26.63 ? 98 ASP B OD2 1 ATOM 2397 N N . LEU B 1 99 ? 12.712 18.192 20.808 1.00 16.65 ? 99 LEU B N 1 ATOM 2398 C CA . LEU B 1 99 ? 11.748 19.283 20.691 1.00 16.06 ? 99 LEU B CA 1 ATOM 2399 C C . LEU B 1 99 ? 11.590 19.711 19.229 1.00 12.76 ? 99 LEU B C 1 ATOM 2400 O O . LEU B 1 99 ? 10.497 20.071 18.801 1.00 21.60 ? 99 LEU B O 1 ATOM 2401 C CB . LEU B 1 99 ? 12.147 20.466 21.576 1.00 18.00 ? 99 LEU B CB 1 ATOM 2402 C CG . LEU B 1 99 ? 11.181 21.659 21.589 1.00 21.48 ? 99 LEU B CG 1 ATOM 2403 C CD1 . LEU B 1 99 ? 9.746 21.199 21.787 1.00 15.93 ? 99 LEU B CD1 1 ATOM 2404 C CD2 . LEU B 1 99 ? 11.587 22.628 22.685 1.00 17.55 ? 99 LEU B CD2 1 ATOM 2405 N N . ARG B 1 100 ? 12.669 19.625 18.457 1.00 13.56 ? 100 ARG B N 1 ATOM 2406 C CA . ARG B 1 100 ? 12.616 19.991 17.044 1.00 16.04 ? 100 ARG B CA 1 ATOM 2407 C C . ARG B 1 100 ? 11.662 19.064 16.289 1.00 16.92 ? 100 ARG B C 1 ATOM 2408 O O . ARG B 1 100 ? 10.905 19.522 15.438 1.00 19.33 ? 100 ARG B O 1 ATOM 2409 C CB . ARG B 1 100 ? 14.010 19.963 16.409 1.00 7.52 ? 100 ARG B CB 1 ATOM 2410 C CG . ARG B 1 100 ? 14.030 20.509 14.987 1.00 12.34 ? 100 ARG B CG 1 ATOM 2411 C CD . ARG B 1 100 ? 15.426 20.507 14.384 1.00 10.97 ? 100 ARG B CD 1 ATOM 2412 N NE . ARG B 1 100 ? 16.329 21.450 15.044 1.00 16.90 ? 100 ARG B NE 1 ATOM 2413 C CZ . ARG B 1 100 ? 16.341 22.765 14.831 1.00 19.86 ? 100 ARG B CZ 1 ATOM 2414 N NH1 . ARG B 1 100 ? 15.489 23.318 13.972 1.00 16.38 ? 100 ARG B NH1 1 ATOM 2415 N NH2 . ARG B 1 100 ? 17.218 23.530 15.469 1.00 13.57 ? 100 ARG B NH2 1 ATOM 2416 N N . CYS B 1 101 ? 11.678 17.770 16.622 1.00 16.14 ? 101 CYS B N 1 ATOM 2417 C CA . CYS B 1 101 ? 10.790 16.800 15.979 1.00 16.98 ? 101 CYS B CA 1 ATOM 2418 C C . CYS B 1 101 ? 9.335 17.124 16.262 1.00 20.79 ? 101 CYS B C 1 ATOM 2419 O O . CYS B 1 101 ? 8.483 16.982 15.386 1.00 25.84 ? 101 CYS B O 1 ATOM 2420 C CB . CYS B 1 101 ? 11.092 15.375 16.441 1.00 16.22 ? 101 CYS B CB 1 ATOM 2421 S SG . CYS B 1 101 ? 12.566 14.679 15.689 1.00 31.13 ? 101 CYS B SG 1 ATOM 2422 N N . LYS B 1 102 ? 9.052 17.550 17.489 1.00 16.81 ? 102 LYS B N 1 ATOM 2423 C CA . LYS B 1 102 ? 7.690 17.910 17.868 1.00 18.43 ? 102 LYS B CA 1 ATOM 2424 C C . LYS B 1 102 ? 7.270 19.145 17.081 1.00 19.03 ? 102 LYS B C 1 ATOM 2425 O O . LYS B 1 102 ? 6.141 19.227 16.605 1.00 20.26 ? 102 LYS B O 1 ATOM 2426 C CB . LYS B 1 102 ? 7.607 18.191 19.366 1.00 20.91 ? 102 LYS B CB 1 ATOM 2427 C CG . LYS B 1 102 ? 7.880 16.969 20.214 1.00 27.44 ? 102 LYS B CG 1 ATOM 2428 C CD . LYS B 1 102 ? 7.819 17.294 21.684 1.00 32.63 ? 102 LYS B CD 1 ATOM 2429 C CE . LYS B 1 102 ? 8.025 16.044 22.512 1.00 36.78 ? 102 LYS B CE 1 ATOM 2430 N NZ . LYS B 1 102 ? 8.034 16.358 23.964 1.00 42.67 ? 102 LYS B NZ 1 ATOM 2431 N N . TYR B 1 103 ? 8.198 20.090 16.935 1.00 19.86 ? 103 TYR B N 1 ATOM 2432 C CA . TYR B 1 103 ? 7.954 21.321 16.190 1.00 21.42 ? 103 TYR B CA 1 ATOM 2433 C C . TYR B 1 103 ? 7.651 20.977 14.733 1.00 22.22 ? 103 TYR B C 1 ATOM 2434 O O . TYR B 1 103 ? 6.667 21.450 14.167 1.00 19.68 ? 103 TYR B O 1 ATOM 2435 C CB . TYR B 1 103 ? 9.184 22.241 16.271 1.00 26.62 ? 103 TYR B CB 1 ATOM 2436 C CG . TYR B 1 103 ? 9.153 23.430 15.325 1.00 28.17 ? 103 TYR B CG 1 ATOM 2437 C CD1 . TYR B 1 103 ? 8.483 24.602 15.671 1.00 26.88 ? 103 TYR B CD1 1 ATOM 2438 C CD2 . TYR B 1 103 ? 9.793 23.384 14.084 1.00 29.97 ? 103 TYR B CD2 1 ATOM 2439 C CE1 . TYR B 1 103 ? 8.447 25.700 14.812 1.00 27.40 ? 103 TYR B CE1 1 ATOM 2440 C CE2 . TYR B 1 103 ? 9.761 24.482 13.213 1.00 27.93 ? 103 TYR B CE2 1 ATOM 2441 C CZ . TYR B 1 103 ? 9.086 25.636 13.587 1.00 29.94 ? 103 TYR B CZ 1 ATOM 2442 O OH . TYR B 1 103 ? 9.052 26.724 12.741 1.00 30.50 ? 103 TYR B OH 1 ATOM 2443 N N . ILE B 1 104 ? 8.495 20.132 14.145 1.00 24.07 ? 104 ILE B N 1 ATOM 2444 C CA . ILE B 1 104 ? 8.338 19.704 12.761 1.00 23.97 ? 104 ILE B CA 1 ATOM 2445 C C . ILE B 1 104 ? 7.009 18.978 12.564 1.00 26.57 ? 104 ILE B C 1 ATOM 2446 O O . ILE B 1 104 ? 6.310 19.200 11.577 1.00 28.55 ? 104 ILE B O 1 ATOM 2447 C CB . ILE B 1 104 ? 9.524 18.809 12.332 1.00 22.07 ? 104 ILE B CB 1 ATOM 2448 C CG1 . ILE B 1 104 ? 10.794 19.659 12.248 1.00 16.09 ? 104 ILE B CG1 1 ATOM 2449 C CG2 . ILE B 1 104 ? 9.239 18.129 10.989 1.00 21.11 ? 104 ILE B CG2 1 ATOM 2450 C CD1 . ILE B 1 104 ? 12.059 18.852 12.096 1.00 18.34 ? 104 ILE B CD1 1 ATOM 2451 N N . SER B 1 105 ? 6.647 18.138 13.528 1.00 27.61 ? 105 SER B N 1 ATOM 2452 C CA . SER B 1 105 ? 5.395 17.401 13.455 1.00 26.28 ? 105 SER B CA 1 ATOM 2453 C C . SER B 1 105 ? 4.225 18.376 13.427 1.00 28.13 ? 105 SER B C 1 ATOM 2454 O O . SER B 1 105 ? 3.277 18.187 12.676 1.00 26.69 ? 105 SER B O 1 ATOM 2455 C CB . SER B 1 105 ? 5.260 16.454 14.646 1.00 28.21 ? 105 SER B CB 1 ATOM 2456 O OG . SER B 1 105 ? 4.076 15.684 14.542 1.00 37.44 ? 105 SER B OG 1 ATOM 2457 N N . LEU B 1 106 ? 4.302 19.428 14.238 1.00 27.67 ? 106 LEU B N 1 ATOM 2458 C CA . LEU B 1 106 ? 3.243 20.435 14.283 1.00 27.62 ? 106 LEU B CA 1 ATOM 2459 C C . LEU B 1 106 ? 3.116 21.168 12.946 1.00 27.00 ? 106 LEU B C 1 ATOM 2460 O O . LEU B 1 106 ? 2.035 21.234 12.363 1.00 25.81 ? 106 LEU B O 1 ATOM 2461 C CB . LEU B 1 106 ? 3.521 21.456 15.390 1.00 25.45 ? 106 LEU B CB 1 ATOM 2462 C CG . LEU B 1 106 ? 2.609 22.690 15.396 1.00 24.87 ? 106 LEU B CG 1 ATOM 2463 C CD1 . LEU B 1 106 ? 1.190 22.296 15.764 1.00 27.15 ? 106 LEU B CD1 1 ATOM 2464 C CD2 . LEU B 1 106 ? 3.136 23.722 16.366 1.00 23.56 ? 106 LEU B CD2 1 ATOM 2465 N N . ILE B 1 107 ? 4.238 21.706 12.475 1.00 25.14 ? 107 ILE B N 1 ATOM 2466 C CA . ILE B 1 107 ? 4.301 22.455 11.222 1.00 27.04 ? 107 ILE B CA 1 ATOM 2467 C C . ILE B 1 107 ? 3.781 21.697 9.996 1.00 28.00 ? 107 ILE B C 1 ATOM 2468 O O . ILE B 1 107 ? 2.953 22.214 9.241 1.00 27.57 ? 107 ILE B O 1 ATOM 2469 C CB . ILE B 1 107 ? 5.750 22.927 10.947 1.00 23.95 ? 107 ILE B CB 1 ATOM 2470 C CG1 . ILE B 1 107 ? 6.208 23.887 12.046 1.00 23.85 ? 107 ILE B CG1 1 ATOM 2471 C CG2 . ILE B 1 107 ? 5.851 23.592 9.585 1.00 23.65 ? 107 ILE B CG2 1 ATOM 2472 C CD1 . ILE B 1 107 ? 5.366 25.145 12.168 1.00 24.91 ? 107 ILE B CD1 1 ATOM 2473 N N . TYR B 1 108 ? 4.242 20.464 9.824 1.00 27.63 ? 108 TYR B N 1 ATOM 2474 C CA . TYR B 1 108 ? 3.856 19.651 8.679 1.00 29.34 ? 108 TYR B CA 1 ATOM 2475 C C . TYR B 1 108 ? 2.638 18.741 8.828 1.00 30.46 ? 108 TYR B C 1 ATOM 2476 O O . TYR B 1 108 ? 2.021 18.380 7.832 1.00 34.36 ? 108 TYR B O 1 ATOM 2477 C CB . TYR B 1 108 ? 5.061 18.830 8.210 1.00 26.16 ? 108 TYR B CB 1 ATOM 2478 C CG . TYR B 1 108 ? 6.208 19.676 7.688 1.00 26.41 ? 108 TYR B CG 1 ATOM 2479 C CD1 . TYR B 1 108 ? 6.221 20.125 6.366 1.00 27.77 ? 108 TYR B CD1 1 ATOM 2480 C CD2 . TYR B 1 108 ? 7.282 20.026 8.508 1.00 23.76 ? 108 TYR B CD2 1 ATOM 2481 C CE1 . TYR B 1 108 ? 7.282 20.904 5.867 1.00 28.56 ? 108 TYR B CE1 1 ATOM 2482 C CE2 . TYR B 1 108 ? 8.347 20.806 8.020 1.00 26.85 ? 108 TYR B CE2 1 ATOM 2483 C CZ . TYR B 1 108 ? 8.341 21.240 6.698 1.00 29.26 ? 108 TYR B CZ 1 ATOM 2484 O OH . TYR B 1 108 ? 9.388 22.002 6.214 1.00 25.57 ? 108 TYR B OH 1 ATOM 2485 N N . THR B 1 109 ? 2.273 18.393 10.056 1.00 36.41 ? 109 THR B N 1 ATOM 2486 C CA . THR B 1 109 ? 1.141 17.493 10.283 1.00 36.88 ? 109 THR B CA 1 ATOM 2487 C C . THR B 1 109 ? -0.188 18.145 10.656 1.00 39.16 ? 109 THR B C 1 ATOM 2488 O O . THR B 1 109 ? -1.214 17.829 10.052 1.00 45.62 ? 109 THR B O 1 ATOM 2489 C CB . THR B 1 109 ? 1.513 16.391 11.303 1.00 38.45 ? 109 THR B CB 1 ATOM 2490 O OG1 . THR B 1 109 ? 2.545 15.570 10.741 1.00 39.55 ? 109 THR B OG1 1 ATOM 2491 C CG2 . THR B 1 109 ? 0.307 15.529 11.661 1.00 40.13 ? 109 THR B CG2 1 ATOM 2492 N N . ASN B 1 110 ? -0.187 19.046 11.634 1.00 37.69 ? 110 ASN B N 1 ATOM 2493 C CA . ASN B 1 110 ? -1.432 19.699 12.038 1.00 39.05 ? 110 ASN B CA 1 ATOM 2494 C C . ASN B 1 110 ? -1.225 21.057 12.703 1.00 38.04 ? 110 ASN B C 1 ATOM 2495 O O . ASN B 1 110 ? -1.492 21.239 13.894 1.00 33.79 ? 110 ASN B O 1 ATOM 2496 C CB . ASN B 1 110 ? -2.274 18.769 12.929 1.00 43.62 ? 110 ASN B CB 1 ATOM 2497 C CG . ASN B 1 110 ? -1.624 18.477 14.272 1.00 48.97 ? 110 ASN B CG 1 ATOM 2498 O OD1 . ASN B 1 110 ? -2.316 18.297 15.273 1.00 47.92 ? 110 ASN B OD1 1 ATOM 2499 N ND2 . ASN B 1 110 ? -0.291 18.437 14.304 1.00 51.09 ? 110 ASN B ND2 1 ATOM 2500 N N . TYR B 1 111 ? -0.765 22.016 11.905 1.00 34.78 ? 111 TYR B N 1 ATOM 2501 C CA . TYR B 1 111 ? -0.513 23.365 12.382 1.00 35.81 ? 111 TYR B CA 1 ATOM 2502 C C . TYR B 1 111 ? -1.771 24.047 12.921 1.00 38.74 ? 111 TYR B C 1 ATOM 2503 O O . TYR B 1 111 ? -1.804 24.479 14.073 1.00 38.42 ? 111 TYR B O 1 ATOM 2504 C CB . TYR B 1 111 ? 0.096 24.206 11.261 1.00 32.89 ? 111 TYR B CB 1 ATOM 2505 C CG . TYR B 1 111 ? 0.426 25.621 11.673 1.00 36.04 ? 111 TYR B CG 1 ATOM 2506 C CD1 . TYR B 1 111 ? 1.664 25.932 12.233 1.00 35.00 ? 111 TYR B CD1 1 ATOM 2507 C CD2 . TYR B 1 111 ? -0.505 26.647 11.520 1.00 35.41 ? 111 TYR B CD2 1 ATOM 2508 C CE1 . TYR B 1 111 ? 1.966 27.231 12.632 1.00 38.24 ? 111 TYR B CE1 1 ATOM 2509 C CE2 . TYR B 1 111 ? -0.215 27.947 11.918 1.00 37.46 ? 111 TYR B CE2 1 ATOM 2510 C CZ . TYR B 1 111 ? 1.021 28.232 12.473 1.00 40.15 ? 111 TYR B CZ 1 ATOM 2511 O OH . TYR B 1 111 ? 1.304 29.514 12.883 1.00 45.15 ? 111 TYR B OH 1 ATOM 2512 N N . GLU B 1 112 ? -2.799 24.128 12.081 1.00 42.24 ? 112 GLU B N 1 ATOM 2513 C CA . GLU B 1 112 ? -4.061 24.774 12.438 1.00 42.80 ? 112 GLU B CA 1 ATOM 2514 C C . GLU B 1 112 ? -4.682 24.216 13.704 1.00 39.71 ? 112 GLU B C 1 ATOM 2515 O O . GLU B 1 112 ? -4.957 24.955 14.646 1.00 39.18 ? 112 GLU B O 1 ATOM 2516 C CB . GLU B 1 112 ? -5.072 24.656 11.293 1.00 46.31 ? 112 GLU B CB 1 ATOM 2517 C CG . GLU B 1 112 ? -4.747 25.487 10.056 1.00 51.95 ? 112 GLU B CG 1 ATOM 2518 C CD . GLU B 1 112 ? -3.492 25.022 9.329 1.00 57.89 ? 112 GLU B CD 1 ATOM 2519 O OE1 . GLU B 1 112 ? -3.303 23.796 9.158 1.00 56.58 ? 112 GLU B OE1 1 ATOM 2520 O OE2 . GLU B 1 112 ? -2.683 25.888 8.932 1.00 59.52 ? 112 GLU B OE2 1 ATOM 2521 N N . ALA B 1 113 ? -4.875 22.902 13.721 1.00 39.33 ? 113 ALA B N 1 ATOM 2522 C CA . ALA B 1 113 ? -5.482 22.224 14.855 1.00 40.35 ? 113 ALA B CA 1 ATOM 2523 C C . ALA B 1 113 ? -4.635 22.194 16.128 1.00 43.21 ? 113 ALA B C 1 ATOM 2524 O O . ALA B 1 113 ? -5.099 22.605 17.190 1.00 49.97 ? 113 ALA B O 1 ATOM 2525 C CB . ALA B 1 113 ? -5.876 20.808 14.455 1.00 37.80 ? 113 ALA B CB 1 ATOM 2526 N N . GLY B 1 114 ? -3.386 21.751 16.011 1.00 45.06 ? 114 GLY B N 1 ATOM 2527 C CA . GLY B 1 114 ? -2.527 21.636 17.180 1.00 39.93 ? 114 GLY B CA 1 ATOM 2528 C C . GLY B 1 114 ? -1.730 22.819 17.700 1.00 37.84 ? 114 GLY B C 1 ATOM 2529 O O . GLY B 1 114 ? -1.086 22.692 18.743 1.00 38.69 ? 114 GLY B O 1 ATOM 2530 N N . LYS B 1 115 ? -1.782 23.963 17.023 1.00 34.92 ? 115 LYS B N 1 ATOM 2531 C CA . LYS B 1 115 ? -1.015 25.137 17.447 1.00 35.21 ? 115 LYS B CA 1 ATOM 2532 C C . LYS B 1 115 ? -1.252 25.599 18.888 1.00 37.65 ? 115 LYS B C 1 ATOM 2533 O O . LYS B 1 115 ? -0.306 25.962 19.589 1.00 33.26 ? 115 LYS B O 1 ATOM 2534 C CB . LYS B 1 115 ? -1.237 26.306 16.482 1.00 33.28 ? 115 LYS B CB 1 ATOM 2535 C CG . LYS B 1 115 ? -0.333 27.505 16.738 1.00 34.59 ? 115 LYS B CG 1 ATOM 2536 C CD . LYS B 1 115 ? -0.692 28.675 15.835 1.00 42.26 ? 115 LYS B CD 1 ATOM 2537 C CE . LYS B 1 115 ? 0.090 29.931 16.202 1.00 42.85 ? 115 LYS B CE 1 ATOM 2538 N NZ . LYS B 1 115 ? 1.560 29.765 16.014 1.00 50.95 ? 115 LYS B NZ 1 ATOM 2539 N N . ASP B 1 116 ? -2.505 25.568 19.335 1.00 40.00 ? 116 ASP B N 1 ATOM 2540 C CA . ASP B 1 116 ? -2.839 26.006 20.690 1.00 40.24 ? 116 ASP B CA 1 ATOM 2541 C C . ASP B 1 116 ? -2.306 25.108 21.802 1.00 39.40 ? 116 ASP B C 1 ATOM 2542 O O . ASP B 1 116 ? -1.699 25.596 22.757 1.00 39.07 ? 116 ASP B O 1 ATOM 2543 C CB . ASP B 1 116 ? -4.348 26.207 20.830 1.00 45.37 ? 116 ASP B CB 1 ATOM 2544 C CG . ASP B 1 116 ? -4.876 27.310 19.919 1.00 52.94 ? 116 ASP B CG 1 ATOM 2545 O OD1 . ASP B 1 116 ? -4.157 28.310 19.689 1.00 51.62 ? 116 ASP B OD1 1 ATOM 2546 O OD2 . ASP B 1 116 ? -6.009 27.171 19.413 1.00 57.21 ? 116 ASP B OD2 1 ATOM 2547 N N . ASP B 1 117 ? -2.517 23.801 21.672 1.00 39.40 ? 117 ASP B N 1 ATOM 2548 C CA . ASP B 1 117 ? -2.039 22.850 22.672 1.00 39.34 ? 117 ASP B CA 1 ATOM 2549 C C . ASP B 1 117 ? -0.516 22.871 22.767 1.00 39.16 ? 117 ASP B C 1 ATOM 2550 O O . ASP B 1 117 ? 0.047 22.817 23.864 1.00 37.90 ? 117 ASP B O 1 ATOM 2551 C CB . ASP B 1 117 ? -2.518 21.435 22.340 1.00 39.80 ? 117 ASP B CB 1 ATOM 2552 C CG . ASP B 1 117 ? -4.015 21.254 22.543 1.00 44.62 ? 117 ASP B CG 1 ATOM 2553 O OD1 . ASP B 1 117 ? -4.667 22.136 23.149 1.00 41.27 ? 117 ASP B OD1 1 ATOM 2554 O OD2 . ASP B 1 117 ? -4.538 20.205 22.115 1.00 46.63 ? 117 ASP B OD2 1 ATOM 2555 N N . TYR B 1 118 ? 0.137 22.965 21.609 1.00 36.72 ? 118 TYR B N 1 ATOM 2556 C CA . TYR B 1 118 ? 1.595 23.001 21.529 1.00 33.77 ? 118 TYR B CA 1 ATOM 2557 C C . TYR B 1 118 ? 2.170 24.200 22.286 1.00 31.74 ? 118 TYR B C 1 ATOM 2558 O O . TYR B 1 118 ? 3.147 24.064 23.025 1.00 29.32 ? 118 TYR B O 1 ATOM 2559 C CB . TYR B 1 118 ? 2.042 23.040 20.060 1.00 26.76 ? 118 TYR B CB 1 ATOM 2560 C CG . TYR B 1 118 ? 3.539 22.929 19.861 1.00 27.02 ? 118 TYR B CG 1 ATOM 2561 C CD1 . TYR B 1 118 ? 4.360 24.052 19.956 1.00 22.08 ? 118 TYR B CD1 1 ATOM 2562 C CD2 . TYR B 1 118 ? 4.137 21.701 19.584 1.00 25.26 ? 118 TYR B CD2 1 ATOM 2563 C CE1 . TYR B 1 118 ? 5.732 23.955 19.784 1.00 21.48 ? 118 TYR B CE1 1 ATOM 2564 C CE2 . TYR B 1 118 ? 5.512 21.594 19.408 1.00 23.74 ? 118 TYR B CE2 1 ATOM 2565 C CZ . TYR B 1 118 ? 6.301 22.725 19.511 1.00 22.53 ? 118 TYR B CZ 1 ATOM 2566 O OH . TYR B 1 118 ? 7.658 22.634 19.341 1.00 22.91 ? 118 TYR B OH 1 ATOM 2567 N N . VAL B 1 119 ? 1.577 25.374 22.085 1.00 33.54 ? 119 VAL B N 1 ATOM 2568 C CA . VAL B 1 119 ? 2.038 26.587 22.758 1.00 34.40 ? 119 VAL B CA 1 ATOM 2569 C C . VAL B 1 119 ? 1.817 26.511 24.277 1.00 34.73 ? 119 VAL B C 1 ATOM 2570 O O . VAL B 1 119 ? 2.627 27.029 25.046 1.00 36.01 ? 119 VAL B O 1 ATOM 2571 C CB . VAL B 1 119 ? 1.365 27.853 22.165 1.00 34.26 ? 119 VAL B CB 1 ATOM 2572 C CG1 . VAL B 1 119 ? 1.844 29.106 22.885 1.00 30.64 ? 119 VAL B CG1 1 ATOM 2573 C CG2 . VAL B 1 119 ? 1.691 27.963 20.684 1.00 32.59 ? 119 VAL B CG2 1 ATOM 2574 N N . LYS B 1 120 ? 0.740 25.844 24.700 1.00 35.93 ? 120 LYS B N 1 ATOM 2575 C CA . LYS B 1 120 ? 0.435 25.679 26.125 1.00 36.66 ? 120 LYS B CA 1 ATOM 2576 C C . LYS B 1 120 ? 1.476 24.785 26.796 1.00 34.60 ? 120 LYS B C 1 ATOM 2577 O O . LYS B 1 120 ? 1.872 25.029 27.934 1.00 33.78 ? 120 LYS B O 1 ATOM 2578 C CB . LYS B 1 120 ? -0.946 25.048 26.318 1.00 42.16 ? 120 LYS B CB 1 ATOM 2579 C CG . LYS B 1 120 ? -2.102 25.896 25.826 1.00 52.65 ? 120 LYS B CG 1 ATOM 2580 C CD . LYS B 1 120 ? -3.379 25.074 25.754 1.00 59.12 ? 120 LYS B CD 1 ATOM 2581 C CE . LYS B 1 120 ? -4.491 25.833 25.036 1.00 64.44 ? 120 LYS B CE 1 ATOM 2582 N NZ . LYS B 1 120 ? -5.667 24.959 24.755 1.00 66.81 ? 120 LYS B NZ 1 ATOM 2583 N N . ALA B 1 121 ? 1.914 23.754 26.077 1.00 32.64 ? 121 ALA B N 1 ATOM 2584 C CA . ALA B 1 121 ? 2.905 22.807 26.586 1.00 29.72 ? 121 ALA B CA 1 ATOM 2585 C C . ALA B 1 121 ? 4.346 23.304 26.472 1.00 24.52 ? 121 ALA B C 1 ATOM 2586 O O . ALA B 1 121 ? 5.249 22.747 27.094 1.00 26.35 ? 121 ALA B O 1 ATOM 2587 C CB . ALA B 1 121 ? 2.759 21.470 25.869 1.00 28.02 ? 121 ALA B CB 1 ATOM 2588 N N . LEU B 1 122 ? 4.552 24.358 25.687 1.00 22.27 ? 122 LEU B N 1 ATOM 2589 C CA . LEU B 1 122 ? 5.882 24.921 25.479 1.00 23.68 ? 122 LEU B CA 1 ATOM 2590 C C . LEU B 1 122 ? 6.729 25.192 26.726 1.00 23.00 ? 122 LEU B C 1 ATOM 2591 O O . LEU B 1 122 ? 7.901 24.812 26.762 1.00 27.31 ? 122 LEU B O 1 ATOM 2592 C CB . LEU B 1 122 ? 5.803 26.194 24.635 1.00 21.41 ? 122 LEU B CB 1 ATOM 2593 C CG . LEU B 1 122 ? 6.473 26.159 23.264 1.00 24.97 ? 122 LEU B CG 1 ATOM 2594 C CD1 . LEU B 1 122 ? 6.605 27.586 22.754 1.00 20.98 ? 122 LEU B CD1 1 ATOM 2595 C CD2 . LEU B 1 122 ? 7.844 25.500 23.355 1.00 12.67 ? 122 LEU B CD2 1 ATOM 2596 N N . PRO B 1 123 ? 6.167 25.863 27.752 1.00 22.31 ? 123 PRO B N 1 ATOM 2597 C CA . PRO B 1 123 ? 6.929 26.156 28.972 1.00 21.71 ? 123 PRO B CA 1 ATOM 2598 C C . PRO B 1 123 ? 7.599 24.929 29.583 1.00 17.26 ? 123 PRO B C 1 ATOM 2599 O O . PRO B 1 123 ? 8.756 24.985 29.994 1.00 19.83 ? 123 PRO B O 1 ATOM 2600 C CB . PRO B 1 123 ? 5.867 26.739 29.902 1.00 20.24 ? 123 PRO B CB 1 ATOM 2601 C CG . PRO B 1 123 ? 4.959 27.445 28.956 1.00 16.94 ? 123 PRO B CG 1 ATOM 2602 C CD . PRO B 1 123 ? 4.808 26.436 27.845 1.00 19.69 ? 123 PRO B CD 1 ATOM 2603 N N . GLY B 1 124 ? 6.875 23.815 29.603 1.00 22.52 ? 124 GLY B N 1 ATOM 2604 C CA . GLY B 1 124 ? 7.418 22.587 30.155 1.00 18.70 ? 124 GLY B CA 1 ATOM 2605 C C . GLY B 1 124 ? 8.564 22.068 29.314 1.00 19.03 ? 124 GLY B C 1 ATOM 2606 O O . GLY B 1 124 ? 9.505 21.477 29.841 1.00 21.95 ? 124 GLY B O 1 ATOM 2607 N N . GLN B 1 125 ? 8.479 22.294 28.004 1.00 20.58 ? 125 GLN B N 1 ATOM 2608 C CA . GLN B 1 125 ? 9.508 21.868 27.057 1.00 19.34 ? 125 GLN B CA 1 ATOM 2609 C C . GLN B 1 125 ? 10.764 22.730 27.133 1.00 20.61 ? 125 GLN B C 1 ATOM 2610 O O . GLN B 1 125 ? 11.866 22.246 26.898 1.00 22.56 ? 125 GLN B O 1 ATOM 2611 C CB . GLN B 1 125 ? 8.965 21.915 25.630 1.00 16.50 ? 125 GLN B CB 1 ATOM 2612 C CG . GLN B 1 125 ? 7.808 20.974 25.369 1.00 26.69 ? 125 GLN B CG 1 ATOM 2613 C CD . GLN B 1 125 ? 8.168 19.542 25.677 1.00 32.99 ? 125 GLN B CD 1 ATOM 2614 O OE1 . GLN B 1 125 ? 9.177 19.035 25.196 1.00 37.77 ? 125 GLN B OE1 1 ATOM 2615 N NE2 . GLN B 1 125 ? 7.359 18.890 26.494 1.00 40.20 ? 125 GLN B NE2 1 ATOM 2616 N N . LEU B 1 126 ? 10.593 24.010 27.454 1.00 20.58 ? 126 LEU B N 1 ATOM 2617 C CA . LEU B 1 126 ? 11.720 24.936 27.544 1.00 20.33 ? 126 LEU B CA 1 ATOM 2618 C C . LEU B 1 126 ? 12.449 24.947 28.888 1.00 22.06 ? 126 LEU B C 1 ATOM 2619 O O . LEU B 1 126 ? 13.640 25.263 28.939 1.00 21.85 ? 126 LEU B O 1 ATOM 2620 C CB . LEU B 1 126 ? 11.266 26.354 27.186 1.00 23.94 ? 126 LEU B CB 1 ATOM 2621 C CG . LEU B 1 126 ? 10.754 26.529 25.755 1.00 23.82 ? 126 LEU B CG 1 ATOM 2622 C CD1 . LEU B 1 126 ? 10.208 27.935 25.556 1.00 22.77 ? 126 LEU B CD1 1 ATOM 2623 C CD2 . LEU B 1 126 ? 11.876 26.229 24.770 1.00 18.90 ? 126 LEU B CD2 1 ATOM 2624 N N . LYS B 1 127 ? 11.745 24.601 29.968 1.00 22.88 ? 127 LYS B N 1 ATOM 2625 C CA . LYS B 1 127 ? 12.349 24.580 31.305 1.00 23.56 ? 127 LYS B CA 1 ATOM 2626 C C . LYS B 1 127 ? 13.688 23.855 31.419 1.00 19.01 ? 127 LYS B C 1 ATOM 2627 O O . LYS B 1 127 ? 14.613 24.371 32.047 1.00 18.84 ? 127 LYS B O 1 ATOM 2628 C CB . LYS B 1 127 ? 11.369 24.041 32.351 1.00 31.39 ? 127 LYS B CB 1 ATOM 2629 C CG . LYS B 1 127 ? 10.523 25.123 32.980 1.00 46.72 ? 127 LYS B CG 1 ATOM 2630 C CD . LYS B 1 127 ? 9.385 24.558 33.803 1.00 55.29 ? 127 LYS B CD 1 ATOM 2631 C CE . LYS B 1 127 ? 8.489 25.682 34.305 1.00 58.65 ? 127 LYS B CE 1 ATOM 2632 N NZ . LYS B 1 127 ? 7.241 25.172 34.936 1.00 64.54 ? 127 LYS B NZ 1 ATOM 2633 N N . PRO B 1 128 ? 13.818 22.654 30.814 1.00 18.13 ? 128 PRO B N 1 ATOM 2634 C CA . PRO B 1 128 ? 15.087 21.923 30.896 1.00 14.61 ? 128 PRO B CA 1 ATOM 2635 C C . PRO B 1 128 ? 16.317 22.741 30.488 1.00 18.54 ? 128 PRO B C 1 ATOM 2636 O O . PRO B 1 128 ? 17.377 22.628 31.112 1.00 17.61 ? 128 PRO B O 1 ATOM 2637 C CB . PRO B 1 128 ? 14.857 20.750 29.950 1.00 10.90 ? 128 PRO B CB 1 ATOM 2638 C CG . PRO B 1 128 ? 13.409 20.457 30.156 1.00 14.28 ? 128 PRO B CG 1 ATOM 2639 C CD . PRO B 1 128 ? 12.796 21.837 30.130 1.00 14.32 ? 128 PRO B CD 1 ATOM 2640 N N . PHE B 1 129 ? 16.171 23.580 29.462 1.00 17.24 ? 129 PHE B N 1 ATOM 2641 C CA . PHE B 1 129 ? 17.288 24.398 28.983 1.00 19.39 ? 129 PHE B CA 1 ATOM 2642 C C . PHE B 1 129 ? 17.600 25.577 29.910 1.00 19.51 ? 129 PHE B C 1 ATOM 2643 O O . PHE B 1 129 ? 18.758 25.980 30.047 1.00 17.23 ? 129 PHE B O 1 ATOM 2644 C CB . PHE B 1 129 ? 17.031 24.845 27.543 1.00 19.80 ? 129 PHE B CB 1 ATOM 2645 C CG . PHE B 1 129 ? 16.763 23.697 26.602 1.00 19.75 ? 129 PHE B CG 1 ATOM 2646 C CD1 . PHE B 1 129 ? 17.783 22.815 26.249 1.00 25.75 ? 129 PHE B CD1 1 ATOM 2647 C CD2 . PHE B 1 129 ? 15.482 23.466 26.109 1.00 21.30 ? 129 PHE B CD2 1 ATOM 2648 C CE1 . PHE B 1 129 ? 17.528 21.716 25.420 1.00 20.32 ? 129 PHE B CE1 1 ATOM 2649 C CE2 . PHE B 1 129 ? 15.218 22.371 25.280 1.00 18.54 ? 129 PHE B CE2 1 ATOM 2650 C CZ . PHE B 1 129 ? 16.242 21.497 24.938 1.00 17.85 ? 129 PHE B CZ 1 ATOM 2651 N N . GLU B 1 130 ? 16.561 26.112 30.552 1.00 19.92 ? 130 GLU B N 1 ATOM 2652 C CA . GLU B 1 130 ? 16.712 27.204 31.513 1.00 22.08 ? 130 GLU B CA 1 ATOM 2653 C C . GLU B 1 130 ? 17.490 26.636 32.711 1.00 25.40 ? 130 GLU B C 1 ATOM 2654 O O . GLU B 1 130 ? 18.383 27.287 33.260 1.00 24.97 ? 130 GLU B O 1 ATOM 2655 C CB . GLU B 1 130 ? 15.330 27.693 31.965 1.00 20.31 ? 130 GLU B CB 1 ATOM 2656 C CG . GLU B 1 130 ? 15.334 28.820 33.008 1.00 30.10 ? 130 GLU B CG 1 ATOM 2657 C CD . GLU B 1 130 ? 15.671 30.204 32.442 1.00 32.54 ? 130 GLU B CD 1 ATOM 2658 O OE1 . GLU B 1 130 ? 15.761 30.370 31.208 1.00 32.45 ? 130 GLU B OE1 1 ATOM 2659 O OE2 . GLU B 1 130 ? 15.837 31.147 33.245 1.00 31.25 ? 130 GLU B OE2 1 ATOM 2660 N N . THR B 1 131 ? 17.167 25.392 33.066 1.00 23.53 ? 131 THR B N 1 ATOM 2661 C CA . THR B 1 131 ? 17.807 24.682 34.169 1.00 19.38 ? 131 THR B CA 1 ATOM 2662 C C . THR B 1 131 ? 19.283 24.438 33.876 1.00 22.04 ? 131 THR B C 1 ATOM 2663 O O . THR B 1 131 ? 20.140 24.674 34.730 1.00 25.02 ? 131 THR B O 1 ATOM 2664 C CB . THR B 1 131 ? 17.126 23.323 34.411 1.00 24.86 ? 131 THR B CB 1 ATOM 2665 O OG1 . THR B 1 131 ? 15.725 23.525 34.636 1.00 21.83 ? 131 THR B OG1 1 ATOM 2666 C CG2 . THR B 1 131 ? 17.738 22.622 35.618 1.00 21.09 ? 131 THR B CG2 1 ATOM 2667 N N . LEU B 1 132 ? 19.571 23.933 32.679 1.00 22.06 ? 132 LEU B N 1 ATOM 2668 C CA . LEU B 1 132 ? 20.947 23.664 32.268 1.00 22.51 ? 132 LEU B CA 1 ATOM 2669 C C . LEU B 1 132 ? 21.768 24.944 32.373 1.00 21.76 ? 132 LEU B C 1 ATOM 2670 O O . LEU B 1 132 ? 22.879 24.943 32.904 1.00 26.98 ? 132 LEU B O 1 ATOM 2671 C CB . LEU B 1 132 ? 20.975 23.139 30.830 1.00 25.09 ? 132 LEU B CB 1 ATOM 2672 C CG . LEU B 1 132 ? 20.498 21.699 30.626 1.00 27.71 ? 132 LEU B CG 1 ATOM 2673 C CD1 . LEU B 1 132 ? 20.190 21.434 29.163 1.00 27.30 ? 132 LEU B CD1 1 ATOM 2674 C CD2 . LEU B 1 132 ? 21.558 20.739 31.138 1.00 20.21 ? 132 LEU B CD2 1 ATOM 2675 N N . LEU B 1 133 ? 21.183 26.040 31.902 1.00 22.36 ? 133 LEU B N 1 ATOM 2676 C CA . LEU B 1 133 ? 21.818 27.349 31.926 1.00 21.87 ? 133 LEU B CA 1 ATOM 2677 C C . LEU B 1 133 ? 22.087 27.796 33.364 1.00 23.92 ? 133 LEU B C 1 ATOM 2678 O O . LEU B 1 133 ? 23.195 28.224 33.686 1.00 22.09 ? 133 LEU B O 1 ATOM 2679 C CB . LEU B 1 133 ? 20.918 28.357 31.203 1.00 22.24 ? 133 LEU B CB 1 ATOM 2680 C CG . LEU B 1 133 ? 21.485 29.226 30.073 1.00 24.50 ? 133 LEU B CG 1 ATOM 2681 C CD1 . LEU B 1 133 ? 22.629 28.548 29.351 1.00 17.89 ? 133 LEU B CD1 1 ATOM 2682 C CD2 . LEU B 1 133 ? 20.365 29.566 29.107 1.00 20.75 ? 133 LEU B CD2 1 ATOM 2683 N N . SER B 1 134 ? 21.095 27.641 34.239 1.00 23.80 ? 134 SER B N 1 ATOM 2684 C CA . SER B 1 134 ? 21.242 28.038 35.640 1.00 29.27 ? 134 SER B CA 1 ATOM 2685 C C . SER B 1 134 ? 22.329 27.268 36.393 1.00 29.55 ? 134 SER B C 1 ATOM 2686 O O . SER B 1 134 ? 22.887 27.773 37.368 1.00 36.82 ? 134 SER B O 1 ATOM 2687 C CB . SER B 1 134 ? 19.904 27.928 36.387 1.00 27.85 ? 134 SER B CB 1 ATOM 2688 O OG . SER B 1 134 ? 19.504 26.580 36.554 1.00 36.33 ? 134 SER B OG 1 ATOM 2689 N N . GLN B 1 135 ? 22.641 26.059 35.935 1.00 28.71 ? 135 GLN B N 1 ATOM 2690 C CA . GLN B 1 135 ? 23.675 25.245 36.573 1.00 29.09 ? 135 GLN B CA 1 ATOM 2691 C C . GLN B 1 135 ? 25.072 25.482 36.007 1.00 31.52 ? 135 GLN B C 1 ATOM 2692 O O . GLN B 1 135 ? 26.046 24.908 36.492 1.00 32.56 ? 135 GLN B O 1 ATOM 2693 C CB . GLN B 1 135 ? 23.319 23.768 36.458 1.00 29.48 ? 135 GLN B CB 1 ATOM 2694 C CG . GLN B 1 135 ? 22.042 23.406 37.169 1.00 36.83 ? 135 GLN B CG 1 ATOM 2695 C CD . GLN B 1 135 ? 21.561 22.029 36.797 1.00 42.33 ? 135 GLN B CD 1 ATOM 2696 O OE1 . GLN B 1 135 ? 22.153 21.359 35.951 1.00 46.11 ? 135 GLN B OE1 1 ATOM 2697 N NE2 . GLN B 1 135 ? 20.480 21.596 37.421 1.00 46.26 ? 135 GLN B NE2 1 ATOM 2698 N N . ASN B 1 136 ? 25.172 26.301 34.967 1.00 30.31 ? 136 ASN B N 1 ATOM 2699 C CA . ASN B 1 136 ? 26.457 26.599 34.355 1.00 32.37 ? 136 ASN B CA 1 ATOM 2700 C C . ASN B 1 136 ? 26.792 28.081 34.523 1.00 34.88 ? 136 ASN B C 1 ATOM 2701 O O . ASN B 1 136 ? 26.325 28.919 33.754 1.00 39.57 ? 136 ASN B O 1 ATOM 2702 C CB . ASN B 1 136 ? 26.450 26.217 32.867 1.00 28.03 ? 136 ASN B CB 1 ATOM 2703 C CG . ASN B 1 136 ? 27.793 26.461 32.195 1.00 27.27 ? 136 ASN B CG 1 ATOM 2704 O OD1 . ASN B 1 136 ? 28.839 26.364 32.835 1.00 32.21 ? 136 ASN B OD1 1 ATOM 2705 N ND2 . ASN B 1 136 ? 27.767 26.728 30.901 1.00 24.89 ? 136 ASN B ND2 1 ATOM 2706 N N . GLN B 1 137 ? 27.587 28.395 35.550 1.00 38.39 ? 137 GLN B N 1 ATOM 2707 C CA . GLN B 1 137 ? 27.997 29.774 35.843 1.00 38.87 ? 137 GLN B CA 1 ATOM 2708 C C . GLN B 1 137 ? 26.836 30.769 35.834 1.00 37.46 ? 137 GLN B C 1 ATOM 2709 O O . GLN B 1 137 ? 26.969 31.886 35.325 1.00 38.66 ? 137 GLN B O 1 ATOM 2710 C CB . GLN B 1 137 ? 29.068 30.230 34.854 1.00 42.50 ? 137 GLN B CB 1 ATOM 2711 C CG . GLN B 1 137 ? 30.373 29.467 34.937 1.00 49.41 ? 137 GLN B CG 1 ATOM 2712 C CD . GLN B 1 137 ? 31.245 29.696 33.716 1.00 59.06 ? 137 GLN B CD 1 ATOM 2713 O OE1 . GLN B 1 137 ? 31.892 30.742 33.593 1.00 59.66 ? 137 GLN B OE1 1 ATOM 2714 N NE2 . GLN B 1 137 ? 31.247 28.736 32.796 1.00 60.93 ? 137 GLN B NE2 1 ATOM 2715 N N . GLY B 1 138 ? 25.692 30.340 36.365 1.00 33.21 ? 138 GLY B N 1 ATOM 2716 C CA . GLY B 1 138 ? 24.521 31.201 36.424 1.00 33.94 ? 138 GLY B CA 1 ATOM 2717 C C . GLY B 1 138 ? 23.967 31.671 35.089 1.00 33.48 ? 138 GLY B C 1 ATOM 2718 O O . GLY B 1 138 ? 23.312 32.710 35.024 1.00 33.52 ? 138 GLY B O 1 ATOM 2719 N N . GLY B 1 139 ? 24.219 30.904 34.031 1.00 33.09 ? 139 GLY B N 1 ATOM 2720 C CA . GLY B 1 139 ? 23.731 31.260 32.708 1.00 35.23 ? 139 GLY B CA 1 ATOM 2721 C C . GLY B 1 139 ? 24.418 32.467 32.093 1.00 35.89 ? 139 GLY B C 1 ATOM 2722 O O . GLY B 1 139 ? 23.871 33.095 31.189 1.00 38.32 ? 139 GLY B O 1 ATOM 2723 N N . LYS B 1 140 ? 25.626 32.768 32.560 1.00 34.34 ? 140 LYS B N 1 ATOM 2724 C CA . LYS B 1 140 ? 26.386 33.916 32.068 1.00 38.71 ? 140 LYS B CA 1 ATOM 2725 C C . LYS B 1 140 ? 27.160 33.641 30.781 1.00 35.47 ? 140 LYS B C 1 ATOM 2726 O O . LYS B 1 140 ? 27.484 34.575 30.048 1.00 37.05 ? 140 LYS B O 1 ATOM 2727 C CB . LYS B 1 140 ? 27.346 34.427 33.154 1.00 38.79 ? 140 LYS B CB 1 ATOM 2728 C CG . LYS B 1 140 ? 26.660 34.918 34.427 1.00 48.49 ? 140 LYS B CG 1 ATOM 2729 C CD . LYS B 1 140 ? 25.961 36.260 34.233 1.00 56.54 ? 140 LYS B CD 1 ATOM 2730 C CE . LYS B 1 140 ? 26.952 37.417 34.311 1.00 64.72 ? 140 LYS B CE 1 ATOM 2731 N NZ . LYS B 1 140 ? 26.304 38.745 34.084 1.00 65.93 ? 140 LYS B NZ 1 ATOM 2732 N N . THR B 1 141 ? 27.446 32.369 30.503 1.00 34.07 ? 141 THR B N 1 ATOM 2733 C CA . THR B 1 141 ? 28.197 31.993 29.304 1.00 29.17 ? 141 THR B CA 1 ATOM 2734 C C . THR B 1 141 ? 27.407 31.185 28.262 1.00 29.06 ? 141 THR B C 1 ATOM 2735 O O . THR B 1 141 ? 26.446 31.689 27.684 1.00 28.74 ? 141 THR B O 1 ATOM 2736 C CB . THR B 1 141 ? 29.500 31.247 29.665 1.00 26.45 ? 141 THR B CB 1 ATOM 2737 O OG1 . THR B 1 141 ? 29.203 30.165 30.556 1.00 31.76 ? 141 THR B OG1 1 ATOM 2738 C CG2 . THR B 1 141 ? 30.499 32.190 30.318 1.00 31.11 ? 141 THR B CG2 1 ATOM 2739 N N . PHE B 1 142 ? 27.812 29.937 28.030 1.00 25.37 ? 142 PHE B N 1 ATOM 2740 C CA . PHE B 1 142 ? 27.169 29.076 27.046 1.00 21.42 ? 142 PHE B CA 1 ATOM 2741 C C . PHE B 1 142 ? 26.368 27.947 27.688 1.00 19.43 ? 142 PHE B C 1 ATOM 2742 O O . PHE B 1 142 ? 26.341 27.826 28.906 1.00 22.06 ? 142 PHE B O 1 ATOM 2743 C CB . PHE B 1 142 ? 28.228 28.548 26.083 1.00 20.30 ? 142 PHE B CB 1 ATOM 2744 C CG . PHE B 1 142 ? 29.040 29.643 25.436 1.00 17.19 ? 142 PHE B CG 1 ATOM 2745 C CD1 . PHE B 1 142 ? 28.533 30.359 24.353 1.00 16.59 ? 142 PHE B CD1 1 ATOM 2746 C CD2 . PHE B 1 142 ? 30.294 29.981 25.931 1.00 17.17 ? 142 PHE B CD2 1 ATOM 2747 C CE1 . PHE B 1 142 ? 29.261 31.395 23.778 1.00 16.36 ? 142 PHE B CE1 1 ATOM 2748 C CE2 . PHE B 1 142 ? 31.032 31.016 25.363 1.00 13.88 ? 142 PHE B CE2 1 ATOM 2749 C CZ . PHE B 1 142 ? 30.516 31.723 24.285 1.00 16.14 ? 142 PHE B CZ 1 ATOM 2750 N N . ILE B 1 143 ? 25.698 27.134 26.877 1.00 19.33 ? 143 ILE B N 1 ATOM 2751 C CA . ILE B 1 143 ? 24.872 26.056 27.414 1.00 23.03 ? 143 ILE B CA 1 ATOM 2752 C C . ILE B 1 143 ? 25.676 24.999 28.182 1.00 21.83 ? 143 ILE B C 1 ATOM 2753 O O . ILE B 1 143 ? 25.188 24.439 29.164 1.00 25.30 ? 143 ILE B O 1 ATOM 2754 C CB . ILE B 1 143 ? 23.978 25.410 26.314 1.00 20.01 ? 143 ILE B CB 1 ATOM 2755 C CG1 . ILE B 1 143 ? 22.872 24.569 26.957 1.00 19.19 ? 143 ILE B CG1 1 ATOM 2756 C CG2 . ILE B 1 143 ? 24.813 24.566 25.352 1.00 18.10 ? 143 ILE B CG2 1 ATOM 2757 C CD1 . ILE B 1 143 ? 21.853 25.373 27.737 1.00 13.87 ? 143 ILE B CD1 1 ATOM 2758 N N . VAL B 1 144 ? 26.912 24.763 27.751 1.00 17.84 ? 144 VAL B N 1 ATOM 2759 C CA . VAL B 1 144 ? 27.804 23.798 28.396 1.00 18.31 ? 144 VAL B CA 1 ATOM 2760 C C . VAL B 1 144 ? 29.220 24.366 28.418 1.00 21.53 ? 144 VAL B C 1 ATOM 2761 O O . VAL B 1 144 ? 29.767 24.714 27.373 1.00 23.94 ? 144 VAL B O 1 ATOM 2762 C CB . VAL B 1 144 ? 27.842 22.443 27.643 1.00 15.76 ? 144 VAL B CB 1 ATOM 2763 C CG1 . VAL B 1 144 ? 28.931 21.547 28.228 1.00 12.79 ? 144 VAL B CG1 1 ATOM 2764 C CG2 . VAL B 1 144 ? 26.496 21.745 27.729 1.00 11.21 ? 144 VAL B CG2 1 ATOM 2765 N N . GLY B 1 145 ? 29.805 24.463 29.609 1.00 21.97 ? 145 GLY B N 1 ATOM 2766 C CA . GLY B 1 145 ? 31.159 24.983 29.733 1.00 21.16 ? 145 GLY B CA 1 ATOM 2767 C C . GLY B 1 145 ? 31.284 26.482 29.523 1.00 25.36 ? 145 GLY B C 1 ATOM 2768 O O . GLY B 1 145 ? 30.295 27.212 29.599 1.00 24.11 ? 145 GLY B O 1 ATOM 2769 N N . ASP B 1 146 ? 32.502 26.938 29.240 1.00 28.44 ? 146 ASP B N 1 ATOM 2770 C CA . ASP B 1 146 ? 32.760 28.361 29.029 1.00 35.74 ? 146 ASP B CA 1 ATOM 2771 C C . ASP B 1 146 ? 33.186 28.702 27.600 1.00 32.93 ? 146 ASP B C 1 ATOM 2772 O O . ASP B 1 146 ? 33.714 29.780 27.342 1.00 34.73 ? 146 ASP B O 1 ATOM 2773 C CB . ASP B 1 146 ? 33.797 28.872 30.041 1.00 41.62 ? 146 ASP B CB 1 ATOM 2774 C CG . ASP B 1 146 ? 35.150 28.181 29.909 1.00 50.06 ? 146 ASP B CG 1 ATOM 2775 O OD1 . ASP B 1 146 ? 35.261 27.160 29.193 1.00 52.39 ? 146 ASP B OD1 1 ATOM 2776 O OD2 . ASP B 1 146 ? 36.118 28.670 30.528 1.00 58.74 ? 146 ASP B OD2 1 ATOM 2777 N N . GLN B 1 147 ? 32.957 27.769 26.682 1.00 34.08 ? 147 GLN B N 1 ATOM 2778 C CA . GLN B 1 147 ? 33.286 27.950 25.271 1.00 30.76 ? 147 GLN B CA 1 ATOM 2779 C C . GLN B 1 147 ? 32.075 27.471 24.470 1.00 27.26 ? 147 GLN B C 1 ATOM 2780 O O . GLN B 1 147 ? 31.377 26.544 24.886 1.00 27.27 ? 147 GLN B O 1 ATOM 2781 C CB . GLN B 1 147 ? 34.542 27.154 24.896 1.00 35.52 ? 147 GLN B CB 1 ATOM 2782 C CG . GLN B 1 147 ? 34.436 25.662 25.188 1.00 51.57 ? 147 GLN B CG 1 ATOM 2783 C CD . GLN B 1 147 ? 35.614 24.854 24.669 1.00 56.61 ? 147 GLN B CD 1 ATOM 2784 O OE1 . GLN B 1 147 ? 36.563 24.579 25.410 1.00 59.20 ? 147 GLN B OE1 1 ATOM 2785 N NE2 . GLN B 1 147 ? 35.543 24.436 23.402 1.00 54.77 ? 147 GLN B NE2 1 ATOM 2786 N N . ILE B 1 148 ? 31.802 28.130 23.346 1.00 22.04 ? 148 ILE B N 1 ATOM 2787 C CA . ILE B 1 148 ? 30.659 27.783 22.506 1.00 20.51 ? 148 ILE B CA 1 ATOM 2788 C C . ILE B 1 148 ? 30.803 26.389 21.873 1.00 19.28 ? 148 ILE B C 1 ATOM 2789 O O . ILE B 1 148 ? 31.912 25.944 21.571 1.00 12.08 ? 148 ILE B O 1 ATOM 2790 C CB . ILE B 1 148 ? 30.427 28.874 21.420 1.00 17.72 ? 148 ILE B CB 1 ATOM 2791 C CG1 . ILE B 1 148 ? 28.986 28.822 20.916 1.00 17.02 ? 148 ILE B CG1 1 ATOM 2792 C CG2 . ILE B 1 148 ? 31.411 28.706 20.270 1.00 16.29 ? 148 ILE B CG2 1 ATOM 2793 C CD1 . ILE B 1 148 ? 28.544 30.080 20.207 1.00 10.84 ? 148 ILE B CD1 1 ATOM 2794 N N . SER B 1 149 ? 29.682 25.690 21.717 1.00 10.71 ? 149 SER B N 1 ATOM 2795 C CA . SER B 1 149 ? 29.687 24.356 21.129 1.00 15.30 ? 149 SER B CA 1 ATOM 2796 C C . SER B 1 149 ? 28.632 24.307 20.034 1.00 15.09 ? 149 SER B C 1 ATOM 2797 O O . SER B 1 149 ? 27.846 25.246 19.893 1.00 16.35 ? 149 SER B O 1 ATOM 2798 C CB . SER B 1 149 ? 29.375 23.300 22.194 1.00 11.53 ? 149 SER B CB 1 ATOM 2799 O OG . SER B 1 149 ? 28.020 23.373 22.609 1.00 11.96 ? 149 SER B OG 1 ATOM 2800 N N . PHE B 1 150 ? 28.598 23.211 19.274 1.00 14.93 ? 150 PHE B N 1 ATOM 2801 C CA . PHE B 1 150 ? 27.614 23.076 18.201 1.00 15.07 ? 150 PHE B CA 1 ATOM 2802 C C . PHE B 1 150 ? 26.188 23.041 18.748 1.00 13.71 ? 150 PHE B C 1 ATOM 2803 O O . PHE B 1 150 ? 25.241 23.424 18.059 1.00 21.42 ? 150 PHE B O 1 ATOM 2804 C CB . PHE B 1 150 ? 27.908 21.848 17.315 1.00 13.85 ? 150 PHE B CB 1 ATOM 2805 C CG . PHE B 1 150 ? 27.701 20.518 18.001 1.00 10.83 ? 150 PHE B CG 1 ATOM 2806 C CD1 . PHE B 1 150 ? 26.448 19.907 18.007 1.00 9.79 ? 150 PHE B CD1 1 ATOM 2807 C CD2 . PHE B 1 150 ? 28.759 19.875 18.632 1.00 9.69 ? 150 PHE B CD2 1 ATOM 2808 C CE1 . PHE B 1 150 ? 26.254 18.678 18.633 1.00 13.21 ? 150 PHE B CE1 1 ATOM 2809 C CE2 . PHE B 1 150 ? 28.576 18.644 19.263 1.00 10.53 ? 150 PHE B CE2 1 ATOM 2810 C CZ . PHE B 1 150 ? 27.321 18.044 19.263 1.00 11.95 ? 150 PHE B CZ 1 ATOM 2811 N N . ALA B 1 151 ? 26.044 22.603 19.998 1.00 16.31 ? 151 ALA B N 1 ATOM 2812 C CA . ALA B 1 151 ? 24.736 22.533 20.646 1.00 14.50 ? 151 ALA B CA 1 ATOM 2813 C C . ALA B 1 151 ? 24.168 23.939 20.838 1.00 12.67 ? 151 ALA B C 1 ATOM 2814 O O . ALA B 1 151 ? 22.953 24.136 20.792 1.00 16.19 ? 151 ALA B O 1 ATOM 2815 C CB . ALA B 1 151 ? 24.845 21.807 21.992 1.00 16.55 ? 151 ALA B CB 1 ATOM 2816 N N . ASP B 1 152 ? 25.053 24.911 21.047 1.00 10.04 ? 152 ASP B N 1 ATOM 2817 C CA . ASP B 1 152 ? 24.640 26.297 21.227 1.00 13.99 ? 152 ASP B CA 1 ATOM 2818 C C . ASP B 1 152 ? 23.923 26.818 19.991 1.00 16.09 ? 152 ASP B C 1 ATOM 2819 O O . ASP B 1 152 ? 22.832 27.390 20.096 1.00 13.49 ? 152 ASP B O 1 ATOM 2820 C CB . ASP B 1 152 ? 25.851 27.184 21.527 1.00 14.41 ? 152 ASP B CB 1 ATOM 2821 C CG . ASP B 1 152 ? 26.304 27.086 22.967 1.00 14.53 ? 152 ASP B CG 1 ATOM 2822 O OD1 . ASP B 1 152 ? 25.525 27.460 23.862 1.00 12.69 ? 152 ASP B OD1 1 ATOM 2823 O OD2 . ASP B 1 152 ? 27.447 26.661 23.205 1.00 15.26 ? 152 ASP B OD2 1 ATOM 2824 N N . TYR B 1 153 ? 24.520 26.588 18.819 1.00 13.47 ? 153 TYR B N 1 ATOM 2825 C CA . TYR B 1 153 ? 23.932 27.041 17.555 1.00 17.07 ? 153 TYR B CA 1 ATOM 2826 C C . TYR B 1 153 ? 22.590 26.376 17.306 1.00 12.24 ? 153 TYR B C 1 ATOM 2827 O O . TYR B 1 153 ? 21.647 27.022 16.873 1.00 15.63 ? 153 TYR B O 1 ATOM 2828 C CB . TYR B 1 153 ? 24.880 26.766 16.377 1.00 11.50 ? 153 TYR B CB 1 ATOM 2829 C CG . TYR B 1 153 ? 26.180 27.517 16.484 1.00 9.35 ? 153 TYR B CG 1 ATOM 2830 C CD1 . TYR B 1 153 ? 26.234 28.896 16.252 1.00 10.53 ? 153 TYR B CD1 1 ATOM 2831 C CD2 . TYR B 1 153 ? 27.348 26.864 16.867 1.00 10.73 ? 153 TYR B CD2 1 ATOM 2832 C CE1 . TYR B 1 153 ? 27.424 29.603 16.405 1.00 9.45 ? 153 TYR B CE1 1 ATOM 2833 C CE2 . TYR B 1 153 ? 28.538 27.556 17.024 1.00 10.44 ? 153 TYR B CE2 1 ATOM 2834 C CZ . TYR B 1 153 ? 28.570 28.925 16.793 1.00 14.51 ? 153 TYR B CZ 1 ATOM 2835 O OH . TYR B 1 153 ? 29.750 29.609 16.961 1.00 18.39 ? 153 TYR B OH 1 ATOM 2836 N N . ASN B 1 154 ? 22.495 25.088 17.612 1.00 14.67 ? 154 ASN B N 1 ATOM 2837 C CA . ASN B 1 154 ? 21.266 24.342 17.407 1.00 13.67 ? 154 ASN B CA 1 ATOM 2838 C C . ASN B 1 154 ? 20.177 24.800 18.383 1.00 12.76 ? 154 ASN B C 1 ATOM 2839 O O . ASN B 1 154 ? 19.012 24.933 18.005 1.00 15.87 ? 154 ASN B O 1 ATOM 2840 C CB . ASN B 1 154 ? 21.522 22.838 17.535 1.00 9.31 ? 154 ASN B CB 1 ATOM 2841 C CG . ASN B 1 154 ? 20.439 22.013 16.872 1.00 16.45 ? 154 ASN B CG 1 ATOM 2842 O OD1 . ASN B 1 154 ? 19.547 22.556 16.218 1.00 18.35 ? 154 ASN B OD1 1 ATOM 2843 N ND2 . ASN B 1 154 ? 20.524 20.701 17.022 1.00 15.86 ? 154 ASN B ND2 1 ATOM 2844 N N . LEU B 1 155 ? 20.563 25.052 19.632 1.00 14.49 ? 155 LEU B N 1 ATOM 2845 C CA . LEU B 1 155 ? 19.601 25.502 20.636 1.00 12.89 ? 155 LEU B CA 1 ATOM 2846 C C . LEU B 1 155 ? 19.122 26.904 20.259 1.00 12.96 ? 155 LEU B C 1 ATOM 2847 O O . LEU B 1 155 ? 17.923 27.188 20.308 1.00 14.73 ? 155 LEU B O 1 ATOM 2848 C CB . LEU B 1 155 ? 20.234 25.507 22.034 1.00 12.24 ? 155 LEU B CB 1 ATOM 2849 C CG . LEU B 1 155 ? 19.373 26.105 23.158 1.00 15.93 ? 155 LEU B CG 1 ATOM 2850 C CD1 . LEU B 1 155 ? 18.026 25.406 23.245 1.00 9.78 ? 155 LEU B CD1 1 ATOM 2851 C CD2 . LEU B 1 155 ? 20.113 26.008 24.481 1.00 17.15 ? 155 LEU B CD2 1 ATOM 2852 N N . LEU B 1 156 ? 20.059 27.758 19.846 1.00 11.38 ? 156 LEU B N 1 ATOM 2853 C CA . LEU B 1 156 ? 19.735 29.127 19.442 1.00 14.38 ? 156 LEU B CA 1 ATOM 2854 C C . LEU B 1 156 ? 18.696 29.113 18.328 1.00 17.22 ? 156 LEU B C 1 ATOM 2855 O O . LEU B 1 156 ? 17.695 29.829 18.398 1.00 17.34 ? 156 LEU B O 1 ATOM 2856 C CB . LEU B 1 156 ? 20.990 29.861 18.962 1.00 17.64 ? 156 LEU B CB 1 ATOM 2857 C CG . LEU B 1 156 ? 20.768 31.321 18.555 1.00 19.65 ? 156 LEU B CG 1 ATOM 2858 C CD1 . LEU B 1 156 ? 20.232 32.127 19.737 1.00 20.09 ? 156 LEU B CD1 1 ATOM 2859 C CD2 . LEU B 1 156 ? 22.068 31.920 18.056 1.00 16.71 ? 156 LEU B CD2 1 ATOM 2860 N N . ASP B 1 157 ? 18.929 28.286 17.308 1.00 12.93 ? 157 ASP B N 1 ATOM 2861 C CA . ASP B 1 157 ? 17.987 28.182 16.200 1.00 12.10 ? 157 ASP B CA 1 ATOM 2862 C C . ASP B 1 157 ? 16.618 27.749 16.712 1.00 15.07 ? 157 ASP B C 1 ATOM 2863 O O . ASP B 1 157 ? 15.595 28.339 16.351 1.00 15.21 ? 157 ASP B O 1 ATOM 2864 C CB . ASP B 1 157 ? 18.482 27.186 15.150 1.00 13.31 ? 157 ASP B CB 1 ATOM 2865 C CG . ASP B 1 157 ? 17.480 26.978 14.029 1.00 18.22 ? 157 ASP B CG 1 ATOM 2866 O OD1 . ASP B 1 157 ? 17.115 27.969 13.360 1.00 16.95 ? 157 ASP B OD1 1 ATOM 2867 O OD2 . ASP B 1 157 ? 17.064 25.823 13.813 1.00 18.97 ? 157 ASP B OD2 1 ATOM 2868 N N . LEU B 1 158 ? 16.605 26.723 17.562 1.00 16.38 ? 158 LEU B N 1 ATOM 2869 C CA . LEU B 1 158 ? 15.353 26.222 18.124 1.00 18.41 ? 158 LEU B CA 1 ATOM 2870 C C . LEU B 1 158 ? 14.596 27.345 18.849 1.00 15.26 ? 158 LEU B C 1 ATOM 2871 O O . LEU B 1 158 ? 13.394 27.518 18.658 1.00 17.12 ? 158 LEU B O 1 ATOM 2872 C CB . LEU B 1 158 ? 15.622 25.057 19.084 1.00 15.64 ? 158 LEU B CB 1 ATOM 2873 C CG . LEU B 1 158 ? 14.379 24.318 19.605 1.00 19.50 ? 158 LEU B CG 1 ATOM 2874 C CD1 . LEU B 1 158 ? 13.689 23.577 18.466 1.00 17.37 ? 158 LEU B CD1 1 ATOM 2875 C CD2 . LEU B 1 158 ? 14.768 23.344 20.698 1.00 16.11 ? 158 LEU B CD2 1 ATOM 2876 N N . LEU B 1 159 ? 15.316 28.139 19.635 1.00 14.85 ? 159 LEU B N 1 ATOM 2877 C CA . LEU B 1 159 ? 14.698 29.241 20.375 1.00 15.96 ? 159 LEU B CA 1 ATOM 2878 C C . LEU B 1 159 ? 14.142 30.323 19.446 1.00 15.59 ? 159 LEU B C 1 ATOM 2879 O O . LEU B 1 159 ? 13.007 30.769 19.615 1.00 17.40 ? 159 LEU B O 1 ATOM 2880 C CB . LEU B 1 159 ? 15.702 29.839 21.364 1.00 16.12 ? 159 LEU B CB 1 ATOM 2881 C CG . LEU B 1 159 ? 16.201 28.856 22.431 1.00 16.52 ? 159 LEU B CG 1 ATOM 2882 C CD1 . LEU B 1 159 ? 17.284 29.483 23.291 1.00 13.09 ? 159 LEU B CD1 1 ATOM 2883 C CD2 . LEU B 1 159 ? 15.033 28.394 23.284 1.00 11.26 ? 159 LEU B CD2 1 ATOM 2884 N N . LEU B 1 160 ? 14.929 30.707 18.443 1.00 20.00 ? 160 LEU B N 1 ATOM 2885 C CA . LEU B 1 160 ? 14.516 31.723 17.477 1.00 16.53 ? 160 LEU B CA 1 ATOM 2886 C C . LEU B 1 160 ? 13.251 31.351 16.709 1.00 18.82 ? 160 LEU B C 1 ATOM 2887 O O . LEU B 1 160 ? 12.353 32.186 16.562 1.00 23.62 ? 160 LEU B O 1 ATOM 2888 C CB . LEU B 1 160 ? 15.648 32.025 16.493 1.00 10.59 ? 160 LEU B CB 1 ATOM 2889 C CG . LEU B 1 160 ? 16.904 32.675 17.080 1.00 9.52 ? 160 LEU B CG 1 ATOM 2890 C CD1 . LEU B 1 160 ? 17.960 32.798 16.002 1.00 11.92 ? 160 LEU B CD1 1 ATOM 2891 C CD2 . LEU B 1 160 ? 16.577 34.042 17.657 1.00 13.66 ? 160 LEU B CD2 1 ATOM 2892 N N . ILE B 1 161 ? 13.153 30.108 16.236 1.00 16.27 ? 161 ILE B N 1 ATOM 2893 C CA . ILE B 1 161 ? 11.962 29.704 15.484 1.00 16.31 ? 161 ILE B CA 1 ATOM 2894 C C . ILE B 1 161 ? 10.726 29.613 16.370 1.00 20.48 ? 161 ILE B C 1 ATOM 2895 O O . ILE B 1 161 ? 9.599 29.691 15.876 1.00 17.32 ? 161 ILE B O 1 ATOM 2896 C CB . ILE B 1 161 ? 12.159 28.382 14.692 1.00 20.84 ? 161 ILE B CB 1 ATOM 2897 C CG1 . ILE B 1 161 ? 12.388 27.200 15.636 1.00 20.14 ? 161 ILE B CG1 1 ATOM 2898 C CG2 . ILE B 1 161 ? 13.312 28.530 13.712 1.00 17.48 ? 161 ILE B CG2 1 ATOM 2899 C CD1 . ILE B 1 161 ? 12.634 25.887 14.913 1.00 22.07 ? 161 ILE B CD1 1 ATOM 2900 N N . HIS B 1 162 ? 10.935 29.438 17.676 1.00 20.52 ? 162 HIS B N 1 ATOM 2901 C CA . HIS B 1 162 ? 9.816 29.376 18.612 1.00 21.87 ? 162 HIS B CA 1 ATOM 2902 C C . HIS B 1 162 ? 9.335 30.778 18.957 1.00 21.47 ? 162 HIS B C 1 ATOM 2903 O O . HIS B 1 162 ? 8.171 30.970 19.300 1.00 19.89 ? 162 HIS B O 1 ATOM 2904 C CB . HIS B 1 162 ? 10.176 28.583 19.871 1.00 20.72 ? 162 HIS B CB 1 ATOM 2905 C CG . HIS B 1 162 ? 10.007 27.104 19.709 1.00 19.31 ? 162 HIS B CG 1 ATOM 2906 N ND1 . HIS B 1 162 ? 11.021 26.287 19.255 1.00 17.48 ? 162 HIS B ND1 1 ATOM 2907 C CD2 . HIS B 1 162 ? 8.932 26.305 19.886 1.00 18.21 ? 162 HIS B CD2 1 ATOM 2908 C CE1 . HIS B 1 162 ? 10.573 25.049 19.153 1.00 14.12 ? 162 HIS B CE1 1 ATOM 2909 N NE2 . HIS B 1 162 ? 9.309 25.031 19.529 1.00 15.10 ? 162 HIS B NE2 1 ATOM 2910 N N . GLU B 1 163 ? 10.245 31.749 18.880 1.00 22.78 ? 163 GLU B N 1 ATOM 2911 C CA . GLU B 1 163 ? 9.905 33.148 19.121 1.00 24.84 ? 163 GLU B CA 1 ATOM 2912 C C . GLU B 1 163 ? 8.949 33.560 18.006 1.00 23.79 ? 163 GLU B C 1 ATOM 2913 O O . GLU B 1 163 ? 8.013 34.322 18.223 1.00 30.64 ? 163 GLU B O 1 ATOM 2914 C CB . GLU B 1 163 ? 11.157 34.021 19.066 1.00 30.78 ? 163 GLU B CB 1 ATOM 2915 C CG . GLU B 1 163 ? 11.764 34.343 20.422 1.00 43.50 ? 163 GLU B CG 1 ATOM 2916 C CD . GLU B 1 163 ? 10.884 35.262 21.257 1.00 55.98 ? 163 GLU B CD 1 ATOM 2917 O OE1 . GLU B 1 163 ? 10.274 36.192 20.684 1.00 60.36 ? 163 GLU B OE1 1 ATOM 2918 O OE2 . GLU B 1 163 ? 10.814 35.064 22.491 1.00 61.63 ? 163 GLU B OE2 1 ATOM 2919 N N . VAL B 1 164 ? 9.188 33.024 16.812 1.00 25.34 ? 164 VAL B N 1 ATOM 2920 C CA . VAL B 1 164 ? 8.352 33.307 15.651 1.00 24.08 ? 164 VAL B CA 1 ATOM 2921 C C . VAL B 1 164 ? 7.006 32.593 15.788 1.00 29.96 ? 164 VAL B C 1 ATOM 2922 O O . VAL B 1 164 ? 5.963 33.160 15.465 1.00 34.15 ? 164 VAL B O 1 ATOM 2923 C CB . VAL B 1 164 ? 9.043 32.854 14.337 1.00 22.81 ? 164 VAL B CB 1 ATOM 2924 C CG1 . VAL B 1 164 ? 8.125 33.090 13.140 1.00 20.40 ? 164 VAL B CG1 1 ATOM 2925 C CG2 . VAL B 1 164 ? 10.359 33.598 14.150 1.00 17.22 ? 164 VAL B CG2 1 ATOM 2926 N N . LEU B 1 165 ? 7.035 31.355 16.276 1.00 29.54 ? 165 LEU B N 1 ATOM 2927 C CA . LEU B 1 165 ? 5.817 30.565 16.453 1.00 27.52 ? 165 LEU B CA 1 ATOM 2928 C C . LEU B 1 165 ? 4.922 31.116 17.560 1.00 31.18 ? 165 LEU B C 1 ATOM 2929 O O . LEU B 1 165 ? 3.726 31.327 17.360 1.00 30.02 ? 165 LEU B O 1 ATOM 2930 C CB . LEU B 1 165 ? 6.174 29.111 16.768 1.00 27.36 ? 165 LEU B CB 1 ATOM 2931 C CG . LEU B 1 165 ? 5.005 28.153 17.012 1.00 24.81 ? 165 LEU B CG 1 ATOM 2932 C CD1 . LEU B 1 165 ? 4.270 27.880 15.707 1.00 28.26 ? 165 LEU B CD1 1 ATOM 2933 C CD2 . LEU B 1 165 ? 5.521 26.859 17.605 1.00 25.85 ? 165 LEU B CD2 1 ATOM 2934 N N . ALA B 1 166 ? 5.516 31.325 18.731 1.00 32.61 ? 166 ALA B N 1 ATOM 2935 C CA . ALA B 1 166 ? 4.808 31.837 19.896 1.00 28.03 ? 166 ALA B CA 1 ATOM 2936 C C . ALA B 1 166 ? 5.573 33.037 20.436 1.00 29.47 ? 166 ALA B C 1 ATOM 2937 O O . ALA B 1 166 ? 6.410 32.898 21.328 1.00 27.43 ? 166 ALA B O 1 ATOM 2938 C CB . ALA B 1 166 ? 4.706 30.753 20.961 1.00 24.54 ? 166 ALA B CB 1 ATOM 2939 N N . PRO B 1 167 ? 5.316 34.232 19.875 1.00 29.66 ? 167 PRO B N 1 ATOM 2940 C CA . PRO B 1 167 ? 5.978 35.472 20.294 1.00 26.74 ? 167 PRO B CA 1 ATOM 2941 C C . PRO B 1 167 ? 5.890 35.695 21.801 1.00 26.93 ? 167 PRO B C 1 ATOM 2942 O O . PRO B 1 167 ? 4.812 35.612 22.392 1.00 28.15 ? 167 PRO B O 1 ATOM 2943 C CB . PRO B 1 167 ? 5.208 36.542 19.521 1.00 27.68 ? 167 PRO B CB 1 ATOM 2944 C CG . PRO B 1 167 ? 4.843 35.834 18.259 1.00 27.80 ? 167 PRO B CG 1 ATOM 2945 C CD . PRO B 1 167 ? 4.365 34.497 18.778 1.00 27.30 ? 167 PRO B CD 1 ATOM 2946 N N . GLY B 1 168 ? 7.040 35.938 22.419 1.00 28.32 ? 168 GLY B N 1 ATOM 2947 C CA . GLY B 1 168 ? 7.082 36.167 23.850 1.00 28.39 ? 168 GLY B CA 1 ATOM 2948 C C . GLY B 1 168 ? 7.144 34.914 24.707 1.00 31.42 ? 168 GLY B C 1 ATOM 2949 O O . GLY B 1 168 ? 7.100 35.012 25.931 1.00 32.53 ? 168 GLY B O 1 ATOM 2950 N N . CYS B 1 169 ? 7.250 33.741 24.083 1.00 27.03 ? 169 CYS B N 1 ATOM 2951 C CA . CYS B 1 169 ? 7.323 32.484 24.830 1.00 26.35 ? 169 CYS B CA 1 ATOM 2952 C C . CYS B 1 169 ? 8.541 32.426 25.758 1.00 26.61 ? 169 CYS B C 1 ATOM 2953 O O . CYS B 1 169 ? 8.551 31.667 26.724 1.00 34.29 ? 169 CYS B O 1 ATOM 2954 C CB . CYS B 1 169 ? 7.335 31.282 23.877 1.00 25.43 ? 169 CYS B CB 1 ATOM 2955 S SG . CYS B 1 169 ? 8.792 31.171 22.808 1.00 25.37 ? 169 CYS B SG 1 ATOM 2956 N N . LEU B 1 170 ? 9.561 33.229 25.461 1.00 28.46 ? 170 LEU B N 1 ATOM 2957 C CA . LEU B 1 170 ? 10.781 33.282 26.271 1.00 26.87 ? 170 LEU B CA 1 ATOM 2958 C C . LEU B 1 170 ? 10.742 34.301 27.416 1.00 29.62 ? 170 LEU B C 1 ATOM 2959 O O . LEU B 1 170 ? 11.709 34.420 28.173 1.00 25.36 ? 170 LEU B O 1 ATOM 2960 C CB . LEU B 1 170 ? 11.992 33.575 25.384 1.00 25.97 ? 170 LEU B CB 1 ATOM 2961 C CG . LEU B 1 170 ? 12.803 32.394 24.848 1.00 28.21 ? 170 LEU B CG 1 ATOM 2962 C CD1 . LEU B 1 170 ? 11.902 31.383 24.160 1.00 26.98 ? 170 LEU B CD1 1 ATOM 2963 C CD2 . LEU B 1 170 ? 13.872 32.913 23.900 1.00 22.98 ? 170 LEU B CD2 1 ATOM 2964 N N . ASP B 1 171 ? 9.640 35.040 27.532 1.00 30.40 ? 171 ASP B N 1 ATOM 2965 C CA . ASP B 1 171 ? 9.488 36.048 28.585 1.00 32.42 ? 171 ASP B CA 1 ATOM 2966 C C . ASP B 1 171 ? 9.623 35.456 29.982 1.00 31.61 ? 171 ASP B C 1 ATOM 2967 O O . ASP B 1 171 ? 10.257 36.049 30.855 1.00 29.65 ? 171 ASP B O 1 ATOM 2968 C CB . ASP B 1 171 ? 8.133 36.755 28.467 1.00 33.03 ? 171 ASP B CB 1 ATOM 2969 C CG . ASP B 1 171 ? 8.071 37.724 27.298 1.00 37.32 ? 171 ASP B CG 1 ATOM 2970 O OD1 . ASP B 1 171 ? 9.138 38.086 26.753 1.00 34.25 ? 171 ASP B OD1 1 ATOM 2971 O OD2 . ASP B 1 171 ? 6.946 38.132 26.930 1.00 34.04 ? 171 ASP B OD2 1 ATOM 2972 N N . ALA B 1 172 ? 9.037 34.277 30.175 1.00 29.44 ? 172 ALA B N 1 ATOM 2973 C CA . ALA B 1 172 ? 9.076 33.582 31.458 1.00 26.95 ? 172 ALA B CA 1 ATOM 2974 C C . ALA B 1 172 ? 10.435 32.960 31.791 1.00 25.40 ? 172 ALA B C 1 ATOM 2975 O O . ALA B 1 172 ? 10.623 32.432 32.886 1.00 28.29 ? 172 ALA B O 1 ATOM 2976 C CB . ALA B 1 172 ? 7.992 32.508 31.491 1.00 29.79 ? 172 ALA B CB 1 ATOM 2977 N N . PHE B 1 173 ? 11.381 33.032 30.859 1.00 24.25 ? 173 PHE B N 1 ATOM 2978 C CA . PHE B 1 173 ? 12.701 32.443 31.066 1.00 21.71 ? 173 PHE B CA 1 ATOM 2979 C C . PHE B 1 173 ? 13.825 33.463 30.910 1.00 23.67 ? 173 PHE B C 1 ATOM 2980 O O . PHE B 1 173 ? 14.427 33.581 29.844 1.00 30.17 ? 173 PHE B O 1 ATOM 2981 C CB . PHE B 1 173 ? 12.902 31.277 30.094 1.00 24.75 ? 173 PHE B CB 1 ATOM 2982 C CG . PHE B 1 173 ? 11.837 30.219 30.191 1.00 22.15 ? 173 PHE B CG 1 ATOM 2983 C CD1 . PHE B 1 173 ? 11.906 29.234 31.171 1.00 20.75 ? 173 PHE B CD1 1 ATOM 2984 C CD2 . PHE B 1 173 ? 10.749 30.229 29.323 1.00 18.88 ? 173 PHE B CD2 1 ATOM 2985 C CE1 . PHE B 1 173 ? 10.904 28.276 31.290 1.00 21.32 ? 173 PHE B CE1 1 ATOM 2986 C CE2 . PHE B 1 173 ? 9.740 29.275 29.432 1.00 22.97 ? 173 PHE B CE2 1 ATOM 2987 C CZ . PHE B 1 173 ? 9.818 28.296 30.419 1.00 22.28 ? 173 PHE B CZ 1 ATOM 2988 N N . PRO B 1 174 ? 14.159 34.175 31.998 1.00 26.80 ? 174 PRO B N 1 ATOM 2989 C CA . PRO B 1 174 ? 15.211 35.196 32.015 1.00 25.62 ? 174 PRO B CA 1 ATOM 2990 C C . PRO B 1 174 ? 16.584 34.781 31.492 1.00 25.00 ? 174 PRO B C 1 ATOM 2991 O O . PRO B 1 174 ? 17.246 35.562 30.809 1.00 31.27 ? 174 PRO B O 1 ATOM 2992 C CB . PRO B 1 174 ? 15.255 35.625 33.487 1.00 22.08 ? 174 PRO B CB 1 ATOM 2993 C CG . PRO B 1 174 ? 14.677 34.453 34.223 1.00 22.18 ? 174 PRO B CG 1 ATOM 2994 C CD . PRO B 1 174 ? 13.551 34.038 33.333 1.00 24.14 ? 174 PRO B CD 1 ATOM 2995 N N . LEU B 1 175 ? 17.018 33.566 31.814 1.00 24.34 ? 175 LEU B N 1 ATOM 2996 C CA . LEU B 1 175 ? 18.320 33.078 31.359 1.00 20.62 ? 175 LEU B CA 1 ATOM 2997 C C . LEU B 1 175 ? 18.340 32.767 29.861 1.00 22.51 ? 175 LEU B C 1 ATOM 2998 O O . LEU B 1 175 ? 19.303 33.096 29.170 1.00 17.17 ? 175 LEU B O 1 ATOM 2999 C CB . LEU B 1 175 ? 18.747 31.853 32.170 1.00 23.80 ? 175 LEU B CB 1 ATOM 3000 C CG . LEU B 1 175 ? 19.588 32.073 33.435 1.00 23.93 ? 175 LEU B CG 1 ATOM 3001 C CD1 . LEU B 1 175 ? 19.345 33.431 34.057 1.00 21.68 ? 175 LEU B CD1 1 ATOM 3002 C CD2 . LEU B 1 175 ? 19.298 30.969 34.420 1.00 20.50 ? 175 LEU B CD2 1 ATOM 3003 N N . LEU B 1 176 ? 17.277 32.143 29.359 1.00 20.38 ? 176 LEU B N 1 ATOM 3004 C CA . LEU B 1 176 ? 17.193 31.824 27.939 1.00 22.75 ? 176 LEU B CA 1 ATOM 3005 C C . LEU B 1 176 ? 17.136 33.113 27.117 1.00 27.36 ? 176 LEU B C 1 ATOM 3006 O O . LEU B 1 176 ? 17.803 33.221 26.087 1.00 26.22 ? 176 LEU B O 1 ATOM 3007 C CB . LEU B 1 176 ? 15.972 30.946 27.643 1.00 17.98 ? 176 LEU B CB 1 ATOM 3008 C CG . LEU B 1 176 ? 16.059 29.481 28.085 1.00 19.14 ? 176 LEU B CG 1 ATOM 3009 C CD1 . LEU B 1 176 ? 14.751 28.769 27.786 1.00 13.79 ? 176 LEU B CD1 1 ATOM 3010 C CD2 . LEU B 1 176 ? 17.216 28.783 27.379 1.00 20.71 ? 176 LEU B CD2 1 ATOM 3011 N N . SER B 1 177 ? 16.373 34.095 27.598 1.00 22.20 ? 177 SER B N 1 ATOM 3012 C CA . SER B 1 177 ? 16.242 35.385 26.919 1.00 22.70 ? 177 SER B CA 1 ATOM 3013 C C . SER B 1 177 ? 17.585 36.099 26.816 1.00 20.12 ? 177 SER B C 1 ATOM 3014 O O . SER B 1 177 ? 17.950 36.600 25.751 1.00 16.16 ? 177 SER B O 1 ATOM 3015 C CB . SER B 1 177 ? 15.242 36.279 27.653 1.00 25.67 ? 177 SER B CB 1 ATOM 3016 O OG . SER B 1 177 ? 13.941 35.722 27.614 1.00 27.61 ? 177 SER B OG 1 ATOM 3017 N N . ALA B 1 178 ? 18.318 36.141 27.924 1.00 12.08 ? 178 ALA B N 1 ATOM 3018 C CA . ALA B 1 178 ? 19.623 36.786 27.942 1.00 12.63 ? 178 ALA B CA 1 ATOM 3019 C C . ALA B 1 178 ? 20.579 36.019 27.036 1.00 20.42 ? 178 ALA B C 1 ATOM 3020 O O . ALA B 1 178 ? 21.392 36.614 26.325 1.00 24.13 ? 178 ALA B O 1 ATOM 3021 C CB . ALA B 1 178 ? 20.168 36.831 29.363 1.00 10.47 ? 178 ALA B CB 1 ATOM 3022 N N . TYR B 1 179 ? 20.468 34.693 27.079 1.00 26.21 ? 179 TYR B N 1 ATOM 3023 C CA . TYR B 1 179 ? 21.291 33.784 26.279 1.00 21.36 ? 179 TYR B CA 1 ATOM 3024 C C . TYR B 1 179 ? 21.106 34.087 24.790 1.00 16.25 ? 179 TYR B C 1 ATOM 3025 O O . TYR B 1 179 ? 22.082 34.258 24.061 1.00 17.66 ? 179 TYR B O 1 ATOM 3026 C CB . TYR B 1 179 ? 20.892 32.339 26.609 1.00 22.39 ? 179 TYR B CB 1 ATOM 3027 C CG . TYR B 1 179 ? 21.514 31.257 25.759 1.00 17.96 ? 179 TYR B CG 1 ATOM 3028 C CD1 . TYR B 1 179 ? 22.831 30.842 25.963 1.00 16.55 ? 179 TYR B CD1 1 ATOM 3029 C CD2 . TYR B 1 179 ? 20.759 30.598 24.786 1.00 22.96 ? 179 TYR B CD2 1 ATOM 3030 C CE1 . TYR B 1 179 ? 23.378 29.792 25.222 1.00 13.49 ? 179 TYR B CE1 1 ATOM 3031 C CE2 . TYR B 1 179 ? 21.295 29.549 24.041 1.00 16.87 ? 179 TYR B CE2 1 ATOM 3032 C CZ . TYR B 1 179 ? 22.598 29.151 24.264 1.00 19.04 ? 179 TYR B CZ 1 ATOM 3033 O OH . TYR B 1 179 ? 23.110 28.108 23.527 1.00 22.39 ? 179 TYR B OH 1 ATOM 3034 N N . VAL B 1 180 ? 19.850 34.194 24.362 1.00 14.69 ? 180 VAL B N 1 ATOM 3035 C CA . VAL B 1 180 ? 19.513 34.500 22.973 1.00 19.93 ? 180 VAL B CA 1 ATOM 3036 C C . VAL B 1 180 ? 20.072 35.863 22.559 1.00 23.03 ? 180 VAL B C 1 ATOM 3037 O O . VAL B 1 180 ? 20.697 35.980 21.510 1.00 27.98 ? 180 VAL B O 1 ATOM 3038 C CB . VAL B 1 180 ? 17.978 34.484 22.745 1.00 20.59 ? 180 VAL B CB 1 ATOM 3039 C CG1 . VAL B 1 180 ? 17.625 35.055 21.374 1.00 17.36 ? 180 VAL B CG1 1 ATOM 3040 C CG2 . VAL B 1 180 ? 17.452 33.068 22.856 1.00 24.86 ? 180 VAL B CG2 1 ATOM 3041 N N . GLY B 1 181 ? 19.865 36.879 23.395 1.00 25.76 ? 181 GLY B N 1 ATOM 3042 C CA . GLY B 1 181 ? 20.361 38.210 23.083 1.00 19.47 ? 181 GLY B CA 1 ATOM 3043 C C . GLY B 1 181 ? 21.875 38.254 22.999 1.00 23.23 ? 181 GLY B C 1 ATOM 3044 O O . GLY B 1 181 ? 22.445 38.877 22.102 1.00 25.56 ? 181 GLY B O 1 ATOM 3045 N N . ARG B 1 182 ? 22.522 37.554 23.923 1.00 20.89 ? 182 ARG B N 1 ATOM 3046 C CA . ARG B 1 182 ? 23.978 37.496 23.994 1.00 21.36 ? 182 ARG B CA 1 ATOM 3047 C C . ARG B 1 182 ? 24.591 36.826 22.759 1.00 25.10 ? 182 ARG B C 1 ATOM 3048 O O . ARG B 1 182 ? 25.530 37.356 22.162 1.00 25.87 ? 182 ARG B O 1 ATOM 3049 C CB . ARG B 1 182 ? 24.393 36.743 25.260 1.00 16.90 ? 182 ARG B CB 1 ATOM 3050 C CG . ARG B 1 182 ? 25.872 36.818 25.602 1.00 24.25 ? 182 ARG B CG 1 ATOM 3051 C CD . ARG B 1 182 ? 26.198 35.901 26.779 1.00 25.43 ? 182 ARG B CD 1 ATOM 3052 N NE . ARG B 1 182 ? 25.217 36.053 27.848 1.00 33.34 ? 182 ARG B NE 1 ATOM 3053 C CZ . ARG B 1 182 ? 24.516 35.055 28.377 1.00 33.74 ? 182 ARG B CZ 1 ATOM 3054 N NH1 . ARG B 1 182 ? 24.685 33.808 27.956 1.00 30.68 ? 182 ARG B NH1 1 ATOM 3055 N NH2 . ARG B 1 182 ? 23.594 35.315 29.291 1.00 33.52 ? 182 ARG B NH2 1 ATOM 3056 N N . LEU B 1 183 ? 24.069 35.659 22.384 1.00 24.67 ? 183 LEU B N 1 ATOM 3057 C CA . LEU B 1 183 ? 24.586 34.942 21.220 1.00 25.51 ? 183 LEU B CA 1 ATOM 3058 C C . LEU B 1 183 ? 24.290 35.679 19.910 1.00 25.86 ? 183 LEU B C 1 ATOM 3059 O O . LEU B 1 183 ? 25.139 35.736 19.024 1.00 21.11 ? 183 LEU B O 1 ATOM 3060 C CB . LEU B 1 183 ? 24.045 33.510 21.165 1.00 19.82 ? 183 LEU B CB 1 ATOM 3061 C CG . LEU B 1 183 ? 24.545 32.516 22.220 1.00 22.88 ? 183 LEU B CG 1 ATOM 3062 C CD1 . LEU B 1 183 ? 24.214 31.104 21.769 1.00 23.82 ? 183 LEU B CD1 1 ATOM 3063 C CD2 . LEU B 1 183 ? 26.046 32.644 22.408 1.00 23.87 ? 183 LEU B CD2 1 ATOM 3064 N N . SER B 1 184 ? 23.088 36.246 19.806 1.00 25.81 ? 184 SER B N 1 ATOM 3065 C CA . SER B 1 184 ? 22.673 37.002 18.627 1.00 23.93 ? 184 SER B CA 1 ATOM 3066 C C . SER B 1 184 ? 23.539 38.243 18.419 1.00 28.11 ? 184 SER B C 1 ATOM 3067 O O . SER B 1 184 ? 23.526 38.835 17.337 1.00 31.16 ? 184 SER B O 1 ATOM 3068 C CB . SER B 1 184 ? 21.222 37.457 18.768 1.00 14.90 ? 184 SER B CB 1 ATOM 3069 O OG . SER B 1 184 ? 20.335 36.362 18.844 1.00 30.76 ? 184 SER B OG 1 ATOM 3070 N N . ALA B 1 185 ? 24.266 38.642 19.462 1.00 26.80 ? 185 ALA B N 1 ATOM 3071 C CA . ALA B 1 185 ? 25.122 39.823 19.411 1.00 27.09 ? 185 ALA B CA 1 ATOM 3072 C C . ALA B 1 185 ? 26.542 39.550 18.918 1.00 28.52 ? 185 ALA B C 1 ATOM 3073 O O . ALA B 1 185 ? 27.303 40.486 18.666 1.00 30.61 ? 185 ALA B O 1 ATOM 3074 C CB . ALA B 1 185 ? 25.160 40.503 20.777 1.00 21.64 ? 185 ALA B CB 1 ATOM 3075 N N . ARG B 1 186 ? 26.911 38.278 18.801 1.00 25.71 ? 186 ARG B N 1 ATOM 3076 C CA . ARG B 1 186 ? 28.247 37.925 18.324 1.00 23.55 ? 186 ARG B CA 1 ATOM 3077 C C . ARG B 1 186 ? 28.400 38.520 16.923 1.00 22.21 ? 186 ARG B C 1 ATOM 3078 O O . ARG B 1 186 ? 27.537 38.330 16.069 1.00 23.51 ? 186 ARG B O 1 ATOM 3079 C CB . ARG B 1 186 ? 28.419 36.402 18.319 1.00 19.99 ? 186 ARG B CB 1 ATOM 3080 C CG . ARG B 1 186 ? 28.309 35.792 19.719 1.00 21.64 ? 186 ARG B CG 1 ATOM 3081 C CD . ARG B 1 186 ? 28.265 34.267 19.701 1.00 16.75 ? 186 ARG B CD 1 ATOM 3082 N NE . ARG B 1 186 ? 29.456 33.685 19.091 1.00 11.01 ? 186 ARG B NE 1 ATOM 3083 C CZ . ARG B 1 186 ? 30.578 33.396 19.744 1.00 17.73 ? 186 ARG B CZ 1 ATOM 3084 N NH1 . ARG B 1 186 ? 30.676 33.621 21.050 1.00 17.95 ? 186 ARG B NH1 1 ATOM 3085 N NH2 . ARG B 1 186 ? 31.604 32.869 19.090 1.00 10.28 ? 186 ARG B NH2 1 ATOM 3086 N N . PRO B 1 187 ? 29.488 39.274 16.686 1.00 22.42 ? 187 PRO B N 1 ATOM 3087 C CA . PRO B 1 187 ? 29.827 39.950 15.425 1.00 24.57 ? 187 PRO B CA 1 ATOM 3088 C C . PRO B 1 187 ? 29.441 39.247 14.115 1.00 26.00 ? 187 PRO B C 1 ATOM 3089 O O . PRO B 1 187 ? 28.553 39.717 13.390 1.00 25.25 ? 187 PRO B O 1 ATOM 3090 C CB . PRO B 1 187 ? 31.335 40.139 15.548 1.00 24.22 ? 187 PRO B CB 1 ATOM 3091 C CG . PRO B 1 187 ? 31.496 40.416 16.994 1.00 27.95 ? 187 PRO B CG 1 ATOM 3092 C CD . PRO B 1 187 ? 30.617 39.361 17.630 1.00 23.17 ? 187 PRO B CD 1 ATOM 3093 N N . LYS B 1 188 ? 30.106 38.132 13.817 1.00 23.67 ? 188 LYS B N 1 ATOM 3094 C CA . LYS B 1 188 ? 29.845 37.374 12.593 1.00 23.78 ? 188 LYS B CA 1 ATOM 3095 C C . LYS B 1 188 ? 28.436 36.797 12.510 1.00 20.64 ? 188 LYS B C 1 ATOM 3096 O O . LYS B 1 188 ? 27.838 36.774 11.434 1.00 25.30 ? 188 LYS B O 1 ATOM 3097 C CB . LYS B 1 188 ? 30.881 36.265 12.427 1.00 20.40 ? 188 LYS B CB 1 ATOM 3098 C CG . LYS B 1 188 ? 32.297 36.785 12.316 1.00 24.48 ? 188 LYS B CG 1 ATOM 3099 C CD . LYS B 1 188 ? 33.317 35.663 12.365 1.00 36.35 ? 188 LYS B CD 1 ATOM 3100 C CE . LYS B 1 188 ? 34.731 36.219 12.413 1.00 43.75 ? 188 LYS B CE 1 ATOM 3101 N NZ . LYS B 1 188 ? 34.991 37.115 11.248 1.00 55.43 ? 188 LYS B NZ 1 ATOM 3102 N N . LEU B 1 189 ? 27.900 36.357 13.647 1.00 23.46 ? 189 LEU B N 1 ATOM 3103 C CA . LEU B 1 189 ? 26.554 35.785 13.697 1.00 21.09 ? 189 LEU B CA 1 ATOM 3104 C C . LEU B 1 189 ? 25.487 36.847 13.462 1.00 21.58 ? 189 LEU B C 1 ATOM 3105 O O . LEU B 1 189 ? 24.491 36.594 12.780 1.00 23.91 ? 189 LEU B O 1 ATOM 3106 C CB . LEU B 1 189 ? 26.301 35.116 15.050 1.00 22.39 ? 189 LEU B CB 1 ATOM 3107 C CG . LEU B 1 189 ? 25.680 33.717 15.053 1.00 21.83 ? 189 LEU B CG 1 ATOM 3108 C CD1 . LEU B 1 189 ? 25.217 33.395 16.463 1.00 25.64 ? 189 LEU B CD1 1 ATOM 3109 C CD2 . LEU B 1 189 ? 24.513 33.625 14.092 1.00 18.77 ? 189 LEU B CD2 1 ATOM 3110 N N . LYS B 1 190 ? 25.695 38.025 14.049 1.00 21.42 ? 190 LYS B N 1 ATOM 3111 C CA . LYS B 1 190 ? 24.762 39.142 13.912 1.00 24.54 ? 190 LYS B CA 1 ATOM 3112 C C . LYS B 1 190 ? 24.663 39.571 12.448 1.00 22.51 ? 190 LYS B C 1 ATOM 3113 O O . LYS B 1 190 ? 23.568 39.802 11.932 1.00 18.33 ? 190 LYS B O 1 ATOM 3114 C CB . LYS B 1 190 ? 25.213 40.329 14.764 1.00 23.82 ? 190 LYS B CB 1 ATOM 3115 C CG . LYS B 1 190 ? 24.250 41.493 14.713 1.00 30.28 ? 190 LYS B CG 1 ATOM 3116 C CD . LYS B 1 190 ? 24.779 42.685 15.469 1.00 34.82 ? 190 LYS B CD 1 ATOM 3117 C CE . LYS B 1 190 ? 23.784 43.830 15.405 1.00 40.28 ? 190 LYS B CE 1 ATOM 3118 N NZ . LYS B 1 190 ? 24.286 45.018 16.141 1.00 49.70 ? 190 LYS B NZ 1 ATOM 3119 N N . ALA B 1 191 ? 25.819 39.665 11.794 1.00 19.36 ? 191 ALA B N 1 ATOM 3120 C CA . ALA B 1 191 ? 25.898 40.042 10.385 1.00 23.33 ? 191 ALA B CA 1 ATOM 3121 C C . ALA B 1 191 ? 25.154 39.015 9.527 1.00 24.35 ? 191 ALA B C 1 ATOM 3122 O O . ALA B 1 191 ? 24.355 39.377 8.661 1.00 27.15 ? 191 ALA B O 1 ATOM 3123 C CB . ALA B 1 191 ? 27.357 40.133 9.957 1.00 16.25 ? 191 ALA B CB 1 ATOM 3124 N N . PHE B 1 192 ? 25.393 37.733 9.803 1.00 26.56 ? 192 PHE B N 1 ATOM 3125 C CA . PHE B 1 192 ? 24.747 36.647 9.071 1.00 23.56 ? 192 PHE B CA 1 ATOM 3126 C C . PHE B 1 192 ? 23.232 36.623 9.256 1.00 20.20 ? 192 PHE B C 1 ATOM 3127 O O . PHE B 1 192 ? 22.489 36.459 8.290 1.00 22.15 ? 192 PHE B O 1 ATOM 3128 C CB . PHE B 1 192 ? 25.346 35.292 9.473 1.00 24.14 ? 192 PHE B CB 1 ATOM 3129 C CG . PHE B 1 192 ? 24.670 34.111 8.822 1.00 24.70 ? 192 PHE B CG 1 ATOM 3130 C CD1 . PHE B 1 192 ? 24.921 33.794 7.488 1.00 25.11 ? 192 PHE B CD1 1 ATOM 3131 C CD2 . PHE B 1 192 ? 23.762 33.329 9.536 1.00 20.51 ? 192 PHE B CD2 1 ATOM 3132 C CE1 . PHE B 1 192 ? 24.274 32.721 6.871 1.00 22.20 ? 192 PHE B CE1 1 ATOM 3133 C CE2 . PHE B 1 192 ? 23.110 32.256 8.930 1.00 22.34 ? 192 PHE B CE2 1 ATOM 3134 C CZ . PHE B 1 192 ? 23.367 31.951 7.593 1.00 19.70 ? 192 PHE B CZ 1 ATOM 3135 N N . LEU B 1 193 ? 22.773 36.789 10.492 1.00 19.04 ? 193 LEU B N 1 ATOM 3136 C CA . LEU B 1 193 ? 21.336 36.771 10.775 1.00 21.91 ? 193 LEU B CA 1 ATOM 3137 C C . LEU B 1 193 ? 20.581 37.923 10.123 1.00 23.67 ? 193 LEU B C 1 ATOM 3138 O O . LEU B 1 193 ? 19.370 37.834 9.914 1.00 24.03 ? 193 LEU B O 1 ATOM 3139 C CB . LEU B 1 193 ? 21.076 36.772 12.286 1.00 17.76 ? 193 LEU B CB 1 ATOM 3140 C CG . LEU B 1 193 ? 21.483 35.511 13.052 1.00 24.07 ? 193 LEU B CG 1 ATOM 3141 C CD1 . LEU B 1 193 ? 21.284 35.724 14.541 1.00 23.33 ? 193 LEU B CD1 1 ATOM 3142 C CD2 . LEU B 1 193 ? 20.676 34.320 12.567 1.00 19.04 ? 193 LEU B CD2 1 ATOM 3143 N N . ALA B 1 194 ? 21.300 38.993 9.790 1.00 22.81 ? 194 ALA B N 1 ATOM 3144 C CA . ALA B 1 194 ? 20.686 40.157 9.166 1.00 22.80 ? 194 ALA B CA 1 ATOM 3145 C C . ALA B 1 194 ? 20.754 40.134 7.639 1.00 25.52 ? 194 ALA B C 1 ATOM 3146 O O . ALA B 1 194 ? 20.049 40.896 6.977 1.00 29.76 ? 194 ALA B O 1 ATOM 3147 C CB . ALA B 1 194 ? 21.328 41.430 9.699 1.00 19.44 ? 194 ALA B CB 1 ATOM 3148 N N . SER B 1 195 ? 21.581 39.247 7.087 1.00 26.56 ? 195 SER B N 1 ATOM 3149 C CA . SER B 1 195 ? 21.767 39.134 5.634 1.00 25.66 ? 195 SER B CA 1 ATOM 3150 C C . SER B 1 195 ? 20.570 38.551 4.875 1.00 26.69 ? 195 SER B C 1 ATOM 3151 O O . SER B 1 195 ? 19.751 37.834 5.450 1.00 28.26 ? 195 SER B O 1 ATOM 3152 C CB . SER B 1 195 ? 23.009 38.296 5.336 1.00 23.10 ? 195 SER B CB 1 ATOM 3153 O OG . SER B 1 195 ? 22.754 36.920 5.553 1.00 29.46 ? 195 SER B OG 1 ATOM 3154 N N . PRO B 1 196 ? 20.459 38.850 3.566 1.00 26.01 ? 196 PRO B N 1 ATOM 3155 C CA . PRO B 1 196 ? 19.368 38.363 2.712 1.00 24.55 ? 196 PRO B CA 1 ATOM 3156 C C . PRO B 1 196 ? 19.424 36.837 2.613 1.00 24.15 ? 196 PRO B C 1 ATOM 3157 O O . PRO B 1 196 ? 18.404 36.167 2.472 1.00 22.73 ? 196 PRO B O 1 ATOM 3158 C CB . PRO B 1 196 ? 19.684 38.997 1.354 1.00 23.65 ? 196 PRO B CB 1 ATOM 3159 C CG . PRO B 1 196 ? 20.451 40.225 1.711 1.00 26.05 ? 196 PRO B CG 1 ATOM 3160 C CD . PRO B 1 196 ? 21.359 39.731 2.794 1.00 24.65 ? 196 PRO B CD 1 ATOM 3161 N N . GLU B 1 197 ? 20.648 36.319 2.669 1.00 20.70 ? 197 GLU B N 1 ATOM 3162 C CA . GLU B 1 197 ? 20.949 34.893 2.601 1.00 22.38 ? 197 GLU B CA 1 ATOM 3163 C C . GLU B 1 197 ? 20.135 34.114 3.635 1.00 26.67 ? 197 GLU B C 1 ATOM 3164 O O . GLU B 1 197 ? 19.642 33.013 3.363 1.00 25.57 ? 197 GLU B O 1 ATOM 3165 C CB . GLU B 1 197 ? 22.436 34.720 2.888 1.00 26.03 ? 197 GLU B CB 1 ATOM 3166 C CG . GLU B 1 197 ? 23.027 33.392 2.540 1.00 28.07 ? 197 GLU B CG 1 ATOM 3167 C CD . GLU B 1 197 ? 24.517 33.359 2.798 1.00 31.05 ? 197 GLU B CD 1 ATOM 3168 O OE1 . GLU B 1 197 ? 25.173 34.412 2.628 1.00 34.49 ? 197 GLU B OE1 1 ATOM 3169 O OE2 . GLU B 1 197 ? 25.031 32.280 3.159 1.00 38.12 ? 197 GLU B OE2 1 ATOM 3170 N N . TYR B 1 198 ? 20.005 34.702 4.823 1.00 25.70 ? 198 TYR B N 1 ATOM 3171 C CA . TYR B 1 198 ? 19.261 34.105 5.923 1.00 19.98 ? 198 TYR B CA 1 ATOM 3172 C C . TYR B 1 198 ? 17.818 34.610 5.957 1.00 21.34 ? 198 TYR B C 1 ATOM 3173 O O . TYR B 1 198 ? 16.867 33.826 5.883 1.00 24.11 ? 198 TYR B O 1 ATOM 3174 C CB . TYR B 1 198 ? 19.967 34.420 7.254 1.00 19.33 ? 198 TYR B CB 1 ATOM 3175 C CG . TYR B 1 198 ? 19.226 33.955 8.490 1.00 24.19 ? 198 TYR B CG 1 ATOM 3176 C CD1 . TYR B 1 198 ? 19.427 32.677 9.012 1.00 28.61 ? 198 TYR B CD1 1 ATOM 3177 C CD2 . TYR B 1 198 ? 18.309 34.789 9.127 1.00 22.65 ? 198 TYR B CD2 1 ATOM 3178 C CE1 . TYR B 1 198 ? 18.727 32.239 10.140 1.00 29.02 ? 198 TYR B CE1 1 ATOM 3179 C CE2 . TYR B 1 198 ? 17.608 34.367 10.249 1.00 28.33 ? 198 TYR B CE2 1 ATOM 3180 C CZ . TYR B 1 198 ? 17.817 33.092 10.750 1.00 30.29 ? 198 TYR B CZ 1 ATOM 3181 O OH . TYR B 1 198 ? 17.103 32.675 11.849 1.00 29.25 ? 198 TYR B OH 1 ATOM 3182 N N . VAL B 1 199 ? 17.670 35.927 6.049 1.00 20.52 ? 199 VAL B N 1 ATOM 3183 C CA . VAL B 1 199 ? 16.366 36.582 6.134 1.00 18.57 ? 199 VAL B CA 1 ATOM 3184 C C . VAL B 1 199 ? 15.352 36.264 5.038 1.00 19.49 ? 199 VAL B C 1 ATOM 3185 O O . VAL B 1 199 ? 14.171 36.078 5.326 1.00 20.62 ? 199 VAL B O 1 ATOM 3186 C CB . VAL B 1 199 ? 16.534 38.123 6.238 1.00 20.57 ? 199 VAL B CB 1 ATOM 3187 C CG1 . VAL B 1 199 ? 15.184 38.817 6.206 1.00 16.74 ? 199 VAL B CG1 1 ATOM 3188 C CG2 . VAL B 1 199 ? 17.271 38.484 7.512 1.00 15.97 ? 199 VAL B CG2 1 ATOM 3189 N N . ASN B 1 200 ? 15.803 36.184 3.790 1.00 22.85 ? 200 ASN B N 1 ATOM 3190 C CA . ASN B 1 200 ? 14.886 35.928 2.675 1.00 24.75 ? 200 ASN B CA 1 ATOM 3191 C C . ASN B 1 200 ? 14.529 34.473 2.387 1.00 24.89 ? 200 ASN B C 1 ATOM 3192 O O . ASN B 1 200 ? 13.881 34.168 1.385 1.00 27.66 ? 200 ASN B O 1 ATOM 3193 C CB . ASN B 1 200 ? 15.377 36.642 1.412 1.00 25.85 ? 200 ASN B CB 1 ATOM 3194 C CG . ASN B 1 200 ? 15.353 38.154 1.561 1.00 27.06 ? 200 ASN B CG 1 ATOM 3195 O OD1 . ASN B 1 200 ? 14.457 38.706 2.201 1.00 25.98 ? 200 ASN B OD1 1 ATOM 3196 N ND2 . ASN B 1 200 ? 16.351 38.828 1.000 1.00 24.47 ? 200 ASN B ND2 1 ATOM 3197 N N . LEU B 1 201 ? 14.936 33.584 3.283 1.00 24.34 ? 201 LEU B N 1 ATOM 3198 C CA . LEU B 1 201 ? 14.641 32.164 3.155 1.00 25.53 ? 201 LEU B CA 1 ATOM 3199 C C . LEU B 1 201 ? 13.515 31.839 4.129 1.00 23.67 ? 201 LEU B C 1 ATOM 3200 O O . LEU B 1 201 ? 13.528 32.304 5.271 1.00 24.51 ? 201 LEU B O 1 ATOM 3201 C CB . LEU B 1 201 ? 15.881 31.355 3.532 1.00 23.76 ? 201 LEU B CB 1 ATOM 3202 C CG . LEU B 1 201 ? 16.493 30.419 2.496 1.00 25.37 ? 201 LEU B CG 1 ATOM 3203 C CD1 . LEU B 1 201 ? 16.619 31.110 1.151 1.00 14.82 ? 201 LEU B CD1 1 ATOM 3204 C CD2 . LEU B 1 201 ? 17.848 29.953 3.002 1.00 24.74 ? 201 LEU B CD2 1 ATOM 3205 N N . PRO B 1 202 ? 12.488 31.097 3.676 1.00 24.64 ? 202 PRO B N 1 ATOM 3206 C CA . PRO B 1 202 ? 11.390 30.756 4.594 1.00 24.48 ? 202 PRO B CA 1 ATOM 3207 C C . PRO B 1 202 ? 11.907 29.747 5.625 1.00 25.08 ? 202 PRO B C 1 ATOM 3208 O O . PRO B 1 202 ? 12.851 29.003 5.345 1.00 24.30 ? 202 PRO B O 1 ATOM 3209 C CB . PRO B 1 202 ? 10.350 30.134 3.662 1.00 19.43 ? 202 PRO B CB 1 ATOM 3210 C CG . PRO B 1 202 ? 11.187 29.505 2.596 1.00 18.26 ? 202 PRO B CG 1 ATOM 3211 C CD . PRO B 1 202 ? 12.232 30.566 2.328 1.00 19.55 ? 202 PRO B CD 1 ATOM 3212 N N . ILE B 1 203 ? 11.325 29.746 6.822 1.00 21.21 ? 203 ILE B N 1 ATOM 3213 C CA . ILE B 1 203 ? 11.769 28.824 7.865 1.00 25.05 ? 203 ILE B CA 1 ATOM 3214 C C . ILE B 1 203 ? 11.506 27.368 7.468 1.00 23.81 ? 203 ILE B C 1 ATOM 3215 O O . ILE B 1 203 ? 12.410 26.528 7.505 1.00 19.68 ? 203 ILE B O 1 ATOM 3216 C CB . ILE B 1 203 ? 11.087 29.126 9.234 1.00 24.97 ? 203 ILE B CB 1 ATOM 3217 C CG1 . ILE B 1 203 ? 11.539 30.496 9.751 1.00 21.90 ? 203 ILE B CG1 1 ATOM 3218 C CG2 . ILE B 1 203 ? 11.443 28.047 10.257 1.00 17.71 ? 203 ILE B CG2 1 ATOM 3219 C CD1 . ILE B 1 203 ? 10.893 30.904 11.060 1.00 28.08 ? 203 ILE B CD1 1 ATOM 3220 N N . ASN B 1 204 ? 10.273 27.098 7.053 1.00 21.16 ? 204 ASN B N 1 ATOM 3221 C CA . ASN B 1 204 ? 9.868 25.757 6.658 1.00 25.06 ? 204 ASN B CA 1 ATOM 3222 C C . ASN B 1 204 ? 9.429 25.659 5.195 1.00 27.97 ? 204 ASN B C 1 ATOM 3223 O O . ASN B 1 204 ? 9.132 26.666 4.548 1.00 23.05 ? 204 ASN B O 1 ATOM 3224 C CB . ASN B 1 204 ? 8.749 25.268 7.586 1.00 23.58 ? 204 ASN B CB 1 ATOM 3225 C CG . ASN B 1 204 ? 9.135 25.365 9.053 1.00 25.14 ? 204 ASN B CG 1 ATOM 3226 O OD1 . ASN B 1 204 ? 10.094 24.730 9.492 1.00 17.03 ? 204 ASN B OD1 1 ATOM 3227 N ND2 . ASN B 1 204 ? 8.392 26.159 9.813 1.00 23.78 ? 204 ASN B ND2 1 ATOM 3228 N N . GLY B 1 205 ? 9.396 24.430 4.688 1.00 30.19 ? 205 GLY B N 1 ATOM 3229 C CA . GLY B 1 205 ? 9.018 24.184 3.311 1.00 26.72 ? 205 GLY B CA 1 ATOM 3230 C C . GLY B 1 205 ? 7.556 24.355 2.944 1.00 30.67 ? 205 GLY B C 1 ATOM 3231 O O . GLY B 1 205 ? 7.223 24.334 1.761 1.00 36.72 ? 205 GLY B O 1 ATOM 3232 N N . ASN B 1 206 ? 6.676 24.527 3.925 1.00 28.40 ? 206 ASN B N 1 ATOM 3233 C CA . ASN B 1 206 ? 5.256 24.695 3.624 1.00 26.69 ? 206 ASN B CA 1 ATOM 3234 C C . ASN B 1 206 ? 4.724 26.105 3.889 1.00 31.27 ? 206 ASN B C 1 ATOM 3235 O O . ASN B 1 206 ? 3.511 26.327 3.918 1.00 30.68 ? 206 ASN B O 1 ATOM 3236 C CB . ASN B 1 206 ? 4.406 23.646 4.359 1.00 27.24 ? 206 ASN B CB 1 ATOM 3237 C CG . ASN B 1 206 ? 4.395 23.837 5.869 1.00 30.67 ? 206 ASN B CG 1 ATOM 3238 O OD1 . ASN B 1 206 ? 5.209 24.572 6.426 1.00 30.77 ? 206 ASN B OD1 1 ATOM 3239 N ND2 . ASN B 1 206 ? 3.457 23.173 6.537 1.00 27.18 ? 206 ASN B ND2 1 ATOM 3240 N N . GLY B 1 207 ? 5.634 27.054 4.089 1.00 33.79 ? 207 GLY B N 1 ATOM 3241 C CA . GLY B 1 207 ? 5.230 28.428 4.331 1.00 39.51 ? 207 GLY B CA 1 ATOM 3242 C C . GLY B 1 207 ? 4.623 28.715 5.693 1.00 42.29 ? 207 GLY B C 1 ATOM 3243 O O . GLY B 1 207 ? 4.155 29.828 5.936 1.00 45.87 ? 207 GLY B O 1 ATOM 3244 N N . LYS B 1 208 ? 4.597 27.717 6.571 1.00 38.26 ? 208 LYS B N 1 ATOM 3245 C CA . LYS B 1 208 ? 4.056 27.909 7.911 1.00 33.75 ? 208 LYS B CA 1 ATOM 3246 C C . LYS B 1 208 ? 5.206 28.170 8.878 1.00 32.71 ? 208 LYS B C 1 ATOM 3247 O O . LYS B 1 208 ? 6.328 27.720 8.647 1.00 30.30 ? 208 LYS B O 1 ATOM 3248 C CB . LYS B 1 208 ? 3.233 26.695 8.341 1.00 34.70 ? 208 LYS B CB 1 ATOM 3249 C CG . LYS B 1 208 ? 2.007 26.480 7.474 1.00 34.73 ? 208 LYS B CG 1 ATOM 3250 C CD . LYS B 1 208 ? 1.195 25.291 7.926 1.00 36.87 ? 208 LYS B CD 1 ATOM 3251 C CE . LYS B 1 208 ? -0.012 25.107 7.027 1.00 37.22 ? 208 LYS B CE 1 ATOM 3252 N NZ . LYS B 1 208 ? -0.843 23.951 7.447 1.00 41.92 ? 208 LYS B NZ 1 ATOM 3253 N N . GLN B 1 209 ? 4.930 28.935 9.932 1.00 31.28 ? 209 GLN B N 1 ATOM 3254 C CA . GLN B 1 209 ? 5.937 29.288 10.932 1.00 30.34 ? 209 GLN B CA 1 ATOM 3255 C C . GLN B 1 209 ? 5.293 29.857 12.198 1.00 32.42 ? 209 GLN B C 1 ATOM 3256 O O . GLN B 1 209 ? 6.039 30.248 13.126 1.00 30.09 ? 209 GLN B O 1 ATOM 3257 C CB . GLN B 1 209 ? 6.903 30.317 10.352 1.00 29.10 ? 209 GLN B CB 1 ATOM 3258 C CG . GLN B 1 209 ? 6.206 31.505 9.726 1.00 31.66 ? 209 GLN B CG 1 ATOM 3259 C CD . GLN B 1 209 ? 7.146 32.636 9.396 1.00 37.34 ? 209 GLN B CD 1 ATOM 3260 O OE1 . GLN B 1 209 ? 6.914 33.780 9.783 1.00 42.45 ? 209 GLN B OE1 1 ATOM 3261 N NE2 . GLN B 1 209 ? 8.237 32.319 8.697 1.00 35.16 ? 209 GLN B NE2 1 ATOM 3262 O OXT . GLN B 1 209 ? 4.045 29.916 12.245 1.00 32.94 ? 209 GLN B OXT 1 HETATM 3263 N N . VWW C 2 . ? 15.088 10.798 23.547 1.00 14.90 ? 210 VWW A N 1 HETATM 3264 C CA . VWW C 2 . ? 15.010 9.987 24.792 1.00 20.92 ? 210 VWW A CA 1 HETATM 3265 C C . VWW C 2 . ? 16.115 8.924 24.830 1.00 21.55 ? 210 VWW A C 1 HETATM 3266 O O . VWW C 2 . ? 16.520 8.515 25.940 1.00 17.16 ? 210 VWW A O 1 HETATM 3267 C CB . VWW C 2 . ? 13.635 9.327 24.908 1.00 14.23 ? 210 VWW A CB 1 HETATM 3268 C CG . VWW C 2 . ? 13.394 8.708 26.271 1.00 18.34 ? 210 VWW A CG 1 HETATM 3269 C CD . VWW C 2 . ? 12.045 8.046 26.402 1.00 18.27 ? 210 VWW A CD 1 HETATM 3270 O OE1 . VWW C 2 . ? 11.293 7.936 25.435 1.00 19.98 ? 210 VWW A OE1 1 HETATM 3271 O OXT . VWW C 2 . ? 16.578 8.524 23.744 1.00 21.48 ? 210 VWW A OXT 1 HETATM 3272 N N1 . VWW C 2 . ? 11.726 7.642 27.628 1.00 23.67 ? 210 VWW A N1 1 HETATM 3273 C CA1 . VWW C 2 . ? 10.472 6.967 27.934 1.00 24.20 ? 210 VWW A CA1 1 HETATM 3274 C CB1 . VWW C 2 . ? 10.726 5.484 28.206 1.00 26.79 ? 210 VWW A CB1 1 HETATM 3275 S SG . VWW C 2 . ? 11.291 4.524 26.810 1.00 31.02 ? 210 VWW A SG 1 HETATM 3276 C CD1 . VWW C 2 . ? 9.729 3.804 26.262 1.00 32.02 ? 210 VWW A CD1 1 HETATM 3277 C CE . VWW C 2 . ? 8.930 3.171 27.370 1.00 33.22 ? 210 VWW A CE 1 HETATM 3278 C CZ1 . VWW C 2 . ? 7.640 3.614 27.650 1.00 35.26 ? 210 VWW A CZ1 1 HETATM 3279 C CZ2 . VWW C 2 . ? 9.464 2.135 28.133 1.00 31.51 ? 210 VWW A CZ2 1 HETATM 3280 C CT1 . VWW C 2 . ? 6.893 3.037 28.673 1.00 35.56 ? 210 VWW A CT1 1 HETATM 3281 C CT2 . VWW C 2 . ? 8.723 1.550 29.161 1.00 27.28 ? 210 VWW A CT2 1 HETATM 3282 C CH . VWW C 2 . ? 7.437 2.001 29.430 1.00 30.54 ? 210 VWW A CH 1 HETATM 3283 C C1 . VWW C 2 . ? 9.834 7.550 29.180 1.00 22.41 ? 210 VWW A C1 1 HETATM 3284 O O1 . VWW C 2 . ? 10.522 8.023 30.084 1.00 21.77 ? 210 VWW A O1 1 HETATM 3285 N N2 . VWW C 2 . ? 8.512 7.468 29.229 1.00 21.35 ? 210 VWW A N2 1 HETATM 3286 C CA2 . VWW C 2 . ? 7.740 7.933 30.366 1.00 24.25 ? 210 VWW A CA2 1 HETATM 3287 C CB2 . VWW C 2 . ? 6.555 7.062 30.633 1.00 24.94 ? 210 VWW A CB2 1 HETATM 3288 C CG1 . VWW C 2 . ? 5.330 7.315 30.027 1.00 25.47 ? 210 VWW A CG1 1 HETATM 3289 C CD11 . VWW C 2 . ? 4.250 6.459 30.220 1.00 26.21 ? 210 VWW A CD11 1 HETATM 3290 C CE1 . VWW C 2 . ? 4.392 5.339 31.027 1.00 24.08 ? 210 VWW A CE1 1 HETATM 3291 C CD2 . VWW C 2 . ? 5.611 5.081 31.640 1.00 25.33 ? 210 VWW A CD2 1 HETATM 3292 C CG2 . VWW C 2 . ? 6.683 5.941 31.441 1.00 26.11 ? 210 VWW A CG2 1 HETATM 3293 C C2 . VWW C 2 . ? 7.452 9.433 30.354 1.00 29.42 ? 210 VWW A C2 1 HETATM 3294 O O2 . VWW C 2 . ? 7.116 9.957 31.433 1.00 30.71 ? 210 VWW A O2 1 HETATM 3295 O OXT1 . VWW C 2 . ? 7.569 10.068 29.284 1.00 29.96 ? 210 VWW A OXT1 1 HETATM 3296 O O1 . MES D 3 . ? 22.426 -6.667 36.176 1.00 47.79 ? 211 MES A O1 1 HETATM 3297 C C2 . MES D 3 . ? 22.801 -7.743 37.079 1.00 46.49 ? 211 MES A C2 1 HETATM 3298 C C3 . MES D 3 . ? 23.908 -8.618 36.449 1.00 45.47 ? 211 MES A C3 1 HETATM 3299 N N4 . MES D 3 . ? 24.406 -8.004 35.114 1.00 49.73 ? 211 MES A N4 1 HETATM 3300 C C5 . MES D 3 . ? 24.696 -6.484 35.214 1.00 41.90 ? 211 MES A C5 1 HETATM 3301 C C6 . MES D 3 . ? 23.492 -5.734 35.827 1.00 45.08 ? 211 MES A C6 1 HETATM 3302 C C7 . MES D 3 . ? 25.584 -8.790 34.500 1.00 49.89 ? 211 MES A C7 1 HETATM 3303 C C8 . MES D 3 . ? 25.740 -8.580 32.981 1.00 55.35 ? 211 MES A C8 1 HETATM 3304 S S . MES D 3 . ? 26.952 -9.695 32.274 1.00 57.16 ? 211 MES A S 1 HETATM 3305 O O1S . MES D 3 . ? 27.719 -9.006 31.068 1.00 60.43 ? 211 MES A O1S 1 HETATM 3306 O O2S . MES D 3 . ? 26.255 -11.032 31.776 1.00 58.34 ? 211 MES A O2S 1 HETATM 3307 O O3S . MES D 3 . ? 28.102 -10.124 33.414 1.00 56.85 ? 211 MES A O3S 1 HETATM 3308 N N . VWW E 2 . ? 17.077 12.945 10.162 1.00 16.89 ? 210 VWW B N 1 HETATM 3309 C CA . VWW E 2 . ? 17.306 13.763 8.940 1.00 21.84 ? 210 VWW B CA 1 HETATM 3310 C C . VWW E 2 . ? 18.253 14.931 9.229 1.00 24.69 ? 210 VWW B C 1 HETATM 3311 O O . VWW E 2 . ? 18.940 15.391 8.288 1.00 19.58 ? 210 VWW B O 1 HETATM 3312 C CB . VWW E 2 . ? 15.973 14.285 8.391 1.00 21.52 ? 210 VWW B CB 1 HETATM 3313 C CG . VWW E 2 . ? 16.106 14.903 7.011 1.00 21.74 ? 210 VWW B CG 1 HETATM 3314 C CD . VWW E 2 . ? 14.805 15.431 6.460 1.00 19.99 ? 210 VWW B CD 1 HETATM 3315 O OE1 . VWW E 2 . ? 13.783 15.449 7.146 1.00 22.91 ? 210 VWW B OE1 1 HETATM 3316 O OXT . VWW E 2 . ? 18.308 15.365 10.399 1.00 24.44 ? 210 VWW B OXT 1 HETATM 3317 N N1 . VWW E 2 . ? 14.842 15.822 5.191 1.00 19.67 ? 210 VWW B N1 1 HETATM 3318 C CA1 . VWW E 2 . ? 13.684 16.374 4.504 1.00 22.40 ? 210 VWW B CA1 1 HETATM 3319 C CB1 . VWW E 2 . ? 13.860 17.880 4.304 1.00 25.98 ? 210 VWW B CB1 1 HETATM 3320 S SG . VWW E 2 . ? 13.864 18.870 5.795 1.00 35.19 ? 210 VWW B SG 1 HETATM 3321 C CD1 . VWW E 2 . ? 12.146 19.418 5.816 1.00 31.95 ? 210 VWW B CD1 1 HETATM 3322 C CE . VWW E 2 . ? 11.671 19.986 4.505 1.00 31.48 ? 210 VWW B CE 1 HETATM 3323 C CZ1 . VWW E 2 . ? 10.584 19.426 3.847 1.00 31.71 ? 210 VWW B CZ1 1 HETATM 3324 C CZ2 . VWW E 2 . ? 12.309 21.081 3.929 1.00 30.47 ? 210 VWW B CZ2 1 HETATM 3325 C CT1 . VWW E 2 . ? 10.137 19.946 2.637 1.00 34.94 ? 210 VWW B CT1 1 HETATM 3326 C CT2 . VWW E 2 . ? 11.868 21.609 2.717 1.00 29.43 ? 210 VWW B CT2 1 HETATM 3327 C CH . VWW E 2 . ? 10.781 21.040 2.071 1.00 29.23 ? 210 VWW B CH 1 HETATM 3328 C C1 . VWW E 2 . ? 13.527 15.754 3.130 1.00 22.49 ? 210 VWW B C1 1 HETATM 3329 O O1 . VWW E 2 . ? 14.506 15.367 2.491 1.00 21.23 ? 210 VWW B O1 1 HETATM 3330 N N2 . VWW E 2 . ? 12.284 15.705 2.672 1.00 24.26 ? 210 VWW B N2 1 HETATM 3331 C CA2 . VWW E 2 . ? 11.953 15.187 1.357 1.00 26.47 ? 210 VWW B CA2 1 HETATM 3332 C CB2 . VWW E 2 . ? 10.828 15.943 0.724 1.00 27.64 ? 210 VWW B CB2 1 HETATM 3333 C CG1 . VWW E 2 . ? 9.506 15.556 0.922 1.00 28.67 ? 210 VWW B CG1 1 HETATM 3334 C CD11 . VWW E 2 . ? 8.460 16.304 0.392 1.00 26.56 ? 210 VWW B CD11 1 HETATM 3335 C CE1 . VWW E 2 . ? 8.734 17.449 -0.345 1.00 24.74 ? 210 VWW B CE1 1 HETATM 3336 C CD2 . VWW E 2 . ? 10.051 17.840 -0.551 1.00 27.11 ? 210 VWW B CD2 1 HETATM 3337 C CG2 . VWW E 2 . ? 11.088 17.086 -0.019 1.00 27.10 ? 210 VWW B CG2 1 HETATM 3338 C C2 . VWW E 2 . ? 11.827 13.665 1.299 1.00 32.59 ? 210 VWW B C2 1 HETATM 3339 O O2 . VWW E 2 . ? 11.904 13.131 0.176 1.00 37.14 ? 210 VWW B O2 1 HETATM 3340 O OXT1 . VWW E 2 . ? 11.666 13.022 2.358 1.00 31.09 ? 210 VWW B OXT1 1 HETATM 3341 O O1 . MES F 3 . ? 26.183 31.272 0.193 1.00 47.12 ? 211 MES B O1 1 HETATM 3342 C C2 . MES F 3 . ? 26.710 32.396 -0.566 1.00 47.61 ? 211 MES B C2 1 HETATM 3343 C C3 . MES F 3 . ? 27.473 33.366 0.366 1.00 47.56 ? 211 MES B C3 1 HETATM 3344 N N4 . MES F 3 . ? 27.589 32.781 1.797 1.00 49.71 ? 211 MES B N4 1 HETATM 3345 C C5 . MES F 3 . ? 28.048 31.299 1.811 1.00 44.05 ? 211 MES B C5 1 HETATM 3346 C C6 . MES F 3 . ? 27.174 30.444 0.869 1.00 43.80 ? 211 MES B C6 1 HETATM 3347 C C7 . MES F 3 . ? 28.433 33.671 2.737 1.00 50.84 ? 211 MES B C7 1 HETATM 3348 C C8 . MES F 3 . ? 28.128 33.451 4.233 1.00 55.09 ? 211 MES B C8 1 HETATM 3349 S S . MES F 3 . ? 28.942 34.670 5.266 1.00 57.55 ? 211 MES B S 1 HETATM 3350 O O1S . MES F 3 . ? 29.363 34.038 6.659 1.00 62.19 ? 211 MES B O1S 1 HETATM 3351 O O2S . MES F 3 . ? 28.000 35.922 5.502 1.00 57.67 ? 211 MES B O2S 1 HETATM 3352 O O3S . MES F 3 . ? 30.342 35.231 4.534 1.00 60.73 ? 211 MES B O3S 1 HETATM 3353 O O . HOH G 4 . ? 16.856 5.713 8.800 1.00 16.93 ? 212 HOH A O 1 HETATM 3354 O O . HOH G 4 . ? 24.864 12.790 14.954 1.00 15.27 ? 213 HOH A O 1 HETATM 3355 O O . HOH G 4 . ? 19.222 10.125 22.641 1.00 14.60 ? 214 HOH A O 1 HETATM 3356 O O . HOH G 4 . ? 17.994 -5.269 27.742 1.00 26.25 ? 215 HOH A O 1 HETATM 3357 O O . HOH G 4 . ? 14.836 11.499 17.763 1.00 45.60 ? 216 HOH A O 1 HETATM 3358 O O . HOH G 4 . ? 12.296 -1.485 21.696 1.00 22.48 ? 217 HOH A O 1 HETATM 3359 O O . HOH G 4 . ? 18.264 -0.347 22.604 1.00 24.01 ? 218 HOH A O 1 HETATM 3360 O O . HOH G 4 . ? 18.984 -6.819 30.132 1.00 24.49 ? 219 HOH A O 1 HETATM 3361 O O . HOH G 4 . ? 8.846 0.722 7.703 1.00 38.31 ? 220 HOH A O 1 HETATM 3362 O O . HOH G 4 . ? 15.392 13.020 31.056 1.00 15.92 ? 221 HOH A O 1 HETATM 3363 O O . HOH G 4 . ? 32.502 -9.851 15.386 1.00 39.94 ? 222 HOH A O 1 HETATM 3364 O O . HOH G 4 . ? 15.654 -5.183 22.314 1.00 19.30 ? 223 HOH A O 1 HETATM 3365 O O . HOH G 4 . ? 20.867 1.758 24.123 1.00 14.59 ? 224 HOH A O 1 HETATM 3366 O O . HOH G 4 . ? 15.898 12.316 28.420 1.00 22.41 ? 225 HOH A O 1 HETATM 3367 O O . HOH G 4 . ? 20.408 -5.887 32.343 1.00 22.92 ? 226 HOH A O 1 HETATM 3368 O O . HOH G 4 . ? 27.482 -9.504 6.105 1.00 28.92 ? 227 HOH A O 1 HETATM 3369 O O . HOH G 4 . ? 20.742 13.852 12.295 1.00 9.82 ? 228 HOH A O 1 HETATM 3370 O O . HOH G 4 . ? 11.227 5.784 23.411 1.00 34.16 ? 229 HOH A O 1 HETATM 3371 O O . HOH G 4 . ? 32.290 -8.743 12.401 1.00 27.08 ? 230 HOH A O 1 HETATM 3372 O O . HOH G 4 . ? 31.990 11.506 26.647 1.00 12.76 ? 231 HOH A O 1 HETATM 3373 O O . HOH G 4 . ? 14.962 -2.529 21.860 1.00 18.34 ? 232 HOH A O 1 HETATM 3374 O O . HOH G 4 . ? 16.967 8.325 7.992 1.00 24.06 ? 233 HOH A O 1 HETATM 3375 O O . HOH G 4 . ? 15.543 -2.258 33.685 1.00 25.16 ? 234 HOH A O 1 HETATM 3376 O O . HOH G 4 . ? 17.114 -0.678 35.263 1.00 19.58 ? 235 HOH A O 1 HETATM 3377 O O . HOH G 4 . ? 8.791 9.465 39.334 1.00 37.60 ? 236 HOH A O 1 HETATM 3378 O O . HOH G 4 . ? 34.310 14.016 12.452 1.00 12.67 ? 237 HOH A O 1 HETATM 3379 O O . HOH G 4 . ? 13.969 12.616 26.601 1.00 21.95 ? 238 HOH A O 1 HETATM 3380 O O . HOH G 4 . ? 10.160 0.310 24.282 1.00 20.56 ? 239 HOH A O 1 HETATM 3381 O O . HOH G 4 . ? 19.312 2.039 21.582 1.00 18.05 ? 240 HOH A O 1 HETATM 3382 O O . HOH G 4 . ? 10.029 -8.816 33.060 1.00 39.55 ? 241 HOH A O 1 HETATM 3383 O O . HOH G 4 . ? 35.056 1.807 16.312 1.00 32.72 ? 242 HOH A O 1 HETATM 3384 O O . HOH G 4 . ? 13.779 5.993 9.092 1.00 28.71 ? 243 HOH A O 1 HETATM 3385 O O . HOH G 4 . ? 18.411 4.734 18.522 1.00 18.23 ? 244 HOH A O 1 HETATM 3386 O O . HOH G 4 . ? 18.955 4.897 21.430 1.00 34.55 ? 245 HOH A O 1 HETATM 3387 O O . HOH G 4 . ? 12.692 -15.663 2.165 1.00 27.14 ? 246 HOH A O 1 HETATM 3388 O O . HOH G 4 . ? 9.528 -6.057 17.702 1.00 30.61 ? 247 HOH A O 1 HETATM 3389 O O . HOH G 4 . ? 27.848 11.658 24.970 1.00 22.35 ? 248 HOH A O 1 HETATM 3390 O O . HOH G 4 . ? 7.063 -5.964 24.445 1.00 25.56 ? 249 HOH A O 1 HETATM 3391 O O . HOH G 4 . ? 31.718 -4.759 6.672 1.00 25.20 ? 250 HOH A O 1 HETATM 3392 O O . HOH G 4 . ? 37.235 5.300 19.246 1.00 28.68 ? 251 HOH A O 1 HETATM 3393 O O . HOH G 4 . ? 22.335 -4.853 39.078 1.00 31.25 ? 252 HOH A O 1 HETATM 3394 O O . HOH G 4 . ? 11.924 9.200 12.190 1.00 27.02 ? 253 HOH A O 1 HETATM 3395 O O . HOH G 4 . ? 22.634 -16.179 22.533 1.00 23.30 ? 254 HOH A O 1 HETATM 3396 O O . HOH G 4 . ? 23.228 -14.875 19.924 1.00 29.84 ? 255 HOH A O 1 HETATM 3397 O O . HOH G 4 . ? 16.518 4.011 6.773 1.00 26.05 ? 256 HOH A O 1 HETATM 3398 O O . HOH G 4 . ? 17.155 11.725 38.434 1.00 29.61 ? 257 HOH A O 1 HETATM 3399 O O . HOH G 4 . ? 19.367 -6.248 21.908 1.00 41.40 ? 258 HOH A O 1 HETATM 3400 O O . HOH G 4 . ? 13.105 11.178 13.974 1.00 35.34 ? 259 HOH A O 1 HETATM 3401 O O . HOH G 4 . ? 23.943 -14.188 3.426 1.00 35.78 ? 260 HOH A O 1 HETATM 3402 O O . HOH G 4 . ? 18.267 11.003 14.044 1.00 24.26 ? 261 HOH A O 1 HETATM 3403 O O . HOH G 4 . ? 32.513 -10.999 23.068 1.00 30.58 ? 262 HOH A O 1 HETATM 3404 O O . HOH G 4 . ? 16.471 -1.866 41.441 1.00 32.83 ? 263 HOH A O 1 HETATM 3405 O O . HOH G 4 . ? 10.393 2.476 2.672 1.00 43.77 ? 264 HOH A O 1 HETATM 3406 O O . HOH G 4 . ? 26.084 15.089 36.221 1.00 33.85 ? 265 HOH A O 1 HETATM 3407 O O . HOH G 4 . ? 11.074 16.591 34.671 1.00 26.74 ? 266 HOH A O 1 HETATM 3408 O O . HOH G 4 . ? 16.029 -5.074 34.430 1.00 29.28 ? 267 HOH A O 1 HETATM 3409 O O . HOH G 4 . ? 33.504 14.579 37.879 1.00 37.22 ? 268 HOH A O 1 HETATM 3410 O O . HOH G 4 . ? 20.015 14.786 37.509 1.00 31.57 ? 269 HOH A O 1 HETATM 3411 O O . HOH G 4 . ? 9.850 -0.734 0.799 1.00 44.55 ? 270 HOH A O 1 HETATM 3412 O O . HOH G 4 . ? 18.006 7.436 40.198 1.00 40.60 ? 271 HOH A O 1 HETATM 3413 O O . HOH G 4 . ? 5.802 14.337 37.928 1.00 47.63 ? 272 HOH A O 1 HETATM 3414 O O . HOH G 4 . ? 17.859 -6.963 33.405 1.00 37.00 ? 273 HOH A O 1 HETATM 3415 O O . HOH G 4 . ? 6.322 16.122 35.511 1.00 28.36 ? 274 HOH A O 1 HETATM 3416 O O . HOH G 4 . ? 11.584 2.588 23.272 1.00 23.29 ? 275 HOH A O 1 HETATM 3417 O O . HOH G 4 . ? 9.668 -6.831 4.979 1.00 37.46 ? 276 HOH A O 1 HETATM 3418 O O . HOH G 4 . ? 15.345 -11.632 16.617 1.00 35.47 ? 277 HOH A O 1 HETATM 3419 O O . HOH G 4 . ? 21.967 9.383 17.161 1.00 11.59 ? 278 HOH A O 1 HETATM 3420 O O . HOH G 4 . ? 33.769 2.278 6.604 1.00 31.81 ? 279 HOH A O 1 HETATM 3421 O O . HOH G 4 . ? 12.853 1.052 20.658 1.00 33.35 ? 280 HOH A O 1 HETATM 3422 O O . HOH G 4 . ? 27.322 -14.924 9.874 1.00 39.84 ? 281 HOH A O 1 HETATM 3423 O O . HOH G 4 . ? 5.859 4.345 12.095 1.00 46.01 ? 282 HOH A O 1 HETATM 3424 O O . HOH G 4 . ? 36.569 -0.737 18.630 1.00 34.35 ? 283 HOH A O 1 HETATM 3425 O O . HOH G 4 . ? 10.770 15.081 27.119 1.00 36.53 ? 284 HOH A O 1 HETATM 3426 O O . HOH G 4 . ? -1.304 -1.156 7.791 1.00 42.24 ? 285 HOH A O 1 HETATM 3427 O O . HOH G 4 . ? 12.014 18.258 32.649 1.00 30.71 ? 286 HOH A O 1 HETATM 3428 O O . HOH G 4 . ? 35.197 -9.125 12.192 1.00 44.56 ? 287 HOH A O 1 HETATM 3429 O O . HOH G 4 . ? 5.317 -9.782 15.687 1.00 42.83 ? 288 HOH A O 1 HETATM 3430 O O . HOH G 4 . ? 17.900 -13.931 22.827 1.00 31.70 ? 289 HOH A O 1 HETATM 3431 O O . HOH G 4 . ? 30.457 1.930 5.937 1.00 34.51 ? 290 HOH A O 1 HETATM 3432 O O . HOH G 4 . ? 0.159 1.325 24.052 1.00 33.35 ? 291 HOH A O 1 HETATM 3433 O O . HOH G 4 . ? 27.422 4.747 39.020 1.00 28.33 ? 292 HOH A O 1 HETATM 3434 O O . HOH G 4 . ? 8.527 -6.033 32.765 1.00 28.41 ? 293 HOH A O 1 HETATM 3435 O O . HOH G 4 . ? 12.675 -10.466 3.337 1.00 33.14 ? 294 HOH A O 1 HETATM 3436 O O . HOH G 4 . ? 33.330 5.562 30.933 1.00 28.38 ? 295 HOH A O 1 HETATM 3437 O O . HOH G 4 . ? 11.028 12.083 23.872 1.00 38.22 ? 296 HOH A O 1 HETATM 3438 O O . HOH G 4 . ? 37.257 -1.627 32.977 1.00 49.09 ? 297 HOH A O 1 HETATM 3439 O O . HOH G 4 . ? 36.471 -4.552 17.071 1.00 24.34 ? 298 HOH A O 1 HETATM 3440 O O . HOH G 4 . ? 3.874 1.565 28.811 1.00 42.87 ? 299 HOH A O 1 HETATM 3441 O O . HOH G 4 . ? 8.600 7.749 17.971 1.00 29.12 ? 300 HOH A O 1 HETATM 3442 O O . HOH G 4 . ? 41.584 12.051 12.322 1.00 33.56 ? 301 HOH A O 1 HETATM 3443 O O . HOH G 4 . ? 31.419 0.293 13.055 1.00 23.07 ? 302 HOH A O 1 HETATM 3444 O O . HOH G 4 . ? 16.415 9.458 28.524 1.00 17.32 ? 303 HOH A O 1 HETATM 3445 O O . HOH G 4 . ? 7.037 7.219 26.157 1.00 22.76 ? 304 HOH A O 1 HETATM 3446 O O . HOH H 4 . ? 13.454 17.756 24.597 1.00 11.01 ? 212 HOH B O 1 HETATM 3447 O O . HOH H 4 . ? 18.085 19.167 15.835 1.00 20.98 ? 213 HOH B O 1 HETATM 3448 O O . HOH H 4 . ? 28.073 24.985 25.071 1.00 20.71 ? 214 HOH B O 1 HETATM 3449 O O . HOH H 4 . ? 8.484 29.206 13.621 1.00 22.56 ? 215 HOH B O 1 HETATM 3450 O O . HOH H 4 . ? 21.680 22.641 11.177 1.00 20.63 ? 216 HOH B O 1 HETATM 3451 O O . HOH H 4 . ? 12.796 19.616 26.586 1.00 22.96 ? 217 HOH B O 1 HETATM 3452 O O . HOH H 4 . ? 23.867 11.810 21.308 1.00 14.20 ? 218 HOH B O 1 HETATM 3453 O O . HOH H 4 . ? 28.411 23.073 31.892 1.00 38.20 ? 219 HOH B O 1 HETATM 3454 O O . HOH H 4 . ? 13.508 15.158 25.523 1.00 21.69 ? 220 HOH B O 1 HETATM 3455 O O . HOH H 4 . ? 32.876 23.696 23.150 1.00 31.35 ? 221 HOH B O 1 HETATM 3456 O O . HOH H 4 . ? 19.426 29.201 7.021 1.00 29.18 ? 222 HOH B O 1 HETATM 3457 O O . HOH H 4 . ? 21.360 24.690 -0.419 1.00 18.00 ? 223 HOH B O 1 HETATM 3458 O O . HOH H 4 . ? 20.012 14.460 5.832 1.00 16.04 ? 224 HOH B O 1 HETATM 3459 O O . HOH H 4 . ? 36.423 28.055 4.818 1.00 43.31 ? 225 HOH B O 1 HETATM 3460 O O . HOH H 4 . ? 19.814 10.908 2.980 1.00 28.43 ? 226 HOH B O 1 HETATM 3461 O O . HOH H 4 . ? 12.712 24.833 10.939 1.00 23.65 ? 227 HOH B O 1 HETATM 3462 O O . HOH H 4 . ? 19.813 21.921 13.343 1.00 14.31 ? 228 HOH B O 1 HETATM 3463 O O . HOH H 4 . ? 17.244 11.061 6.881 1.00 12.39 ? 229 HOH B O 1 HETATM 3464 O O . HOH H 4 . ? 15.170 26.190 11.302 1.00 13.73 ? 230 HOH B O 1 HETATM 3465 O O . HOH H 4 . ? 11.046 18.004 27.978 1.00 30.85 ? 231 HOH B O 1 HETATM 3466 O O . HOH H 4 . ? 20.516 31.037 5.021 1.00 25.86 ? 232 HOH B O 1 HETATM 3467 O O . HOH H 4 . ? 5.351 22.274 23.007 1.00 30.70 ? 233 HOH B O 1 HETATM 3468 O O . HOH H 4 . ? 21.403 33.860 30.311 1.00 25.27 ? 234 HOH B O 1 HETATM 3469 O O . HOH H 4 . ? 18.828 24.080 11.817 1.00 23.57 ? 235 HOH B O 1 HETATM 3470 O O . HOH H 4 . ? 15.756 29.068 11.383 1.00 32.38 ? 236 HOH B O 1 HETATM 3471 O O . HOH H 4 . ? 4.305 23.672 30.142 1.00 33.02 ? 237 HOH B O 1 HETATM 3472 O O . HOH H 4 . ? 35.926 20.607 21.381 1.00 34.53 ? 238 HOH B O 1 HETATM 3473 O O . HOH H 4 . ? 13.712 22.115 11.957 1.00 32.52 ? 239 HOH B O 1 HETATM 3474 O O . HOH H 4 . ? 35.901 20.117 8.789 1.00 28.22 ? 240 HOH B O 1 HETATM 3475 O O . HOH H 4 . ? 21.023 40.639 20.260 1.00 39.76 ? 241 HOH B O 1 HETATM 3476 O O . HOH H 4 . ? 26.051 29.906 31.091 1.00 19.51 ? 242 HOH B O 1 HETATM 3477 O O . HOH H 4 . ? 5.040 20.399 28.595 1.00 30.69 ? 243 HOH B O 1 HETATM 3478 O O . HOH H 4 . ? 12.948 20.736 9.025 1.00 32.24 ? 244 HOH B O 1 HETATM 3479 O O . HOH H 4 . ? 19.519 11.655 5.700 1.00 13.35 ? 245 HOH B O 1 HETATM 3480 O O . HOH H 4 . ? 21.185 40.432 13.086 1.00 24.15 ? 246 HOH B O 1 HETATM 3481 O O . HOH H 4 . ? 15.496 27.009 36.045 1.00 38.12 ? 247 HOH B O 1 HETATM 3482 O O . HOH H 4 . ? 8.232 29.139 7.075 1.00 37.92 ? 248 HOH B O 1 HETATM 3483 O O . HOH H 4 . ? 23.635 37.390 2.269 1.00 27.76 ? 249 HOH B O 1 HETATM 3484 O O . HOH H 4 . ? 28.841 37.090 8.825 1.00 33.25 ? 250 HOH B O 1 HETATM 3485 O O . HOH H 4 . ? 17.405 12.665 20.396 1.00 36.33 ? 251 HOH B O 1 HETATM 3486 O O . HOH H 4 . ? 21.360 39.448 26.486 1.00 35.67 ? 252 HOH B O 1 HETATM 3487 O O . HOH H 4 . ? 15.307 5.358 4.523 1.00 41.74 ? 253 HOH B O 1 HETATM 3488 O O . HOH H 4 . ? 19.157 26.110 0.532 1.00 20.88 ? 254 HOH B O 1 HETATM 3489 O O . HOH H 4 . ? 29.444 13.529 12.853 1.00 27.96 ? 255 HOH B O 1 HETATM 3490 O O . HOH H 4 . ? 33.907 30.157 22.715 1.00 35.59 ? 256 HOH B O 1 HETATM 3491 O O . HOH H 4 . ? 18.367 30.578 13.288 1.00 40.73 ? 257 HOH B O 1 HETATM 3492 O O . HOH H 4 . ? 10.744 17.520 23.522 1.00 30.43 ? 258 HOH B O 1 HETATM 3493 O O . HOH H 4 . ? 23.552 12.315 -3.486 1.00 32.43 ? 259 HOH B O 1 HETATM 3494 O O . HOH H 4 . ? 7.831 27.765 2.466 1.00 57.19 ? 260 HOH B O 1 HETATM 3495 O O . HOH H 4 . ? -0.154 21.656 8.944 1.00 29.55 ? 261 HOH B O 1 HETATM 3496 O O . HOH H 4 . ? 32.082 14.883 -1.225 1.00 39.42 ? 262 HOH B O 1 HETATM 3497 O O . HOH H 4 . ? 15.054 7.963 5.666 1.00 37.56 ? 263 HOH B O 1 HETATM 3498 O O . HOH H 4 . ? 20.953 39.600 15.834 1.00 42.54 ? 264 HOH B O 1 HETATM 3499 O O . HOH H 4 . ? 12.952 32.530 -0.873 1.00 26.67 ? 265 HOH B O 1 HETATM 3500 O O . HOH H 4 . ? 12.340 15.041 11.905 1.00 41.80 ? 266 HOH B O 1 HETATM 3501 O O . HOH H 4 . ? 19.239 28.961 -0.427 1.00 38.64 ? 267 HOH B O 1 HETATM 3502 O O . HOH H 4 . ? 32.271 23.932 26.288 1.00 32.90 ? 268 HOH B O 1 HETATM 3503 O O . HOH H 4 . ? 31.221 36.442 15.893 1.00 36.29 ? 269 HOH B O 1 HETATM 3504 O O . HOH H 4 . ? 8.747 32.091 35.052 1.00 28.20 ? 270 HOH B O 1 HETATM 3505 O O . HOH H 4 . ? 17.008 6.889 -1.756 1.00 30.88 ? 271 HOH B O 1 HETATM 3506 O O . HOH H 4 . ? 22.759 30.393 3.495 1.00 20.28 ? 272 HOH B O 1 HETATM 3507 O O . HOH H 4 . ? 34.578 26.557 21.290 1.00 34.08 ? 273 HOH B O 1 HETATM 3508 O O . HOH H 4 . ? 3.412 32.437 13.821 1.00 51.39 ? 274 HOH B O 1 HETATM 3509 O O . HOH H 4 . ? 11.493 22.916 7.603 1.00 35.42 ? 275 HOH B O 1 HETATM 3510 O O . HOH H 4 . ? 27.933 38.505 22.492 1.00 34.14 ? 276 HOH B O 1 HETATM 3511 O O . HOH H 4 . ? 16.161 35.587 13.217 1.00 45.32 ? 277 HOH B O 1 HETATM 3512 O O . HOH H 4 . ? 38.124 18.161 7.834 1.00 37.78 ? 278 HOH B O 1 HETATM 3513 O O . HOH H 4 . ? 34.808 11.002 19.084 1.00 46.41 ? 279 HOH B O 1 HETATM 3514 O O . HOH H 4 . ? 12.943 34.982 16.348 1.00 31.71 ? 280 HOH B O 1 HETATM 3515 O O . HOH H 4 . ? 33.453 33.293 22.322 1.00 38.86 ? 281 HOH B O 1 HETATM 3516 O O . HOH H 4 . ? 11.583 34.856 4.214 1.00 45.28 ? 282 HOH B O 1 HETATM 3517 O O . HOH H 4 . ? 37.564 10.772 22.960 1.00 45.16 ? 283 HOH B O 1 HETATM 3518 O O . HOH H 4 . ? 26.947 9.801 -1.180 1.00 33.54 ? 284 HOH B O 1 HETATM 3519 O O . HOH H 4 . ? 28.871 12.308 -3.005 1.00 33.00 ? 285 HOH B O 1 HETATM 3520 O O . HOH H 4 . ? 21.585 14.640 18.240 1.00 14.49 ? 286 HOH B O 1 HETATM 3521 O O . HOH H 4 . ? 12.893 16.815 9.297 1.00 40.60 ? 287 HOH B 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 PRO 1 1 ? ? ? A . n A 1 2 PRO 2 2 2 PRO PRO A . n A 1 3 TYR 3 3 3 TYR TYR A . n A 1 4 THR 4 4 4 THR THR A . n A 1 5 VAL 5 5 5 VAL VAL A . n A 1 6 VAL 6 6 6 VAL VAL A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 PHE 8 8 8 PHE PHE A . n A 1 9 PRO 9 9 9 PRO PRO A . n A 1 10 VAL 10 10 10 VAL VAL A . n A 1 11 ARG 11 11 11 ARG ARG A . n A 1 12 GLY 12 12 12 GLY GLY A . n A 1 13 ARG 13 13 13 ARG ARG A . n A 1 14 CYS 14 14 14 CYS CYS A . n A 1 15 ALA 15 15 15 ALA ALA A . n A 1 16 ALA 16 16 16 ALA ALA A . n A 1 17 LEU 17 17 17 LEU LEU A . n A 1 18 ARG 18 18 18 ARG ARG A . n A 1 19 MET 19 19 19 MET MET A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 ASP 23 23 23 ASP ASP A . n A 1 24 GLN 24 24 24 GLN GLN A . n A 1 25 GLY 25 25 25 GLY GLY A . n A 1 26 GLN 26 26 26 GLN GLN A . n A 1 27 SER 27 27 27 SER SER A . n A 1 28 TRP 28 28 28 TRP TRP A . n A 1 29 LYS 29 29 29 LYS LYS A . n A 1 30 GLU 30 30 30 GLU GLU A . n A 1 31 GLU 31 31 31 GLU GLU A . n A 1 32 VAL 32 32 32 VAL VAL A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 THR 34 34 34 THR THR A . n A 1 35 VAL 35 35 35 VAL VAL A . n A 1 36 GLU 36 36 36 GLU GLU A . n A 1 37 THR 37 37 37 THR THR A . n A 1 38 TRP 38 38 38 TRP TRP A . n A 1 39 GLN 39 39 39 GLN GLN A . n A 1 40 GLU 40 40 40 GLU GLU A . n A 1 41 GLY 41 41 41 GLY GLY A . n A 1 42 SER 42 42 42 SER SER A . n A 1 43 LEU 43 43 43 LEU LEU A . n A 1 44 LYS 44 44 44 LYS LYS A . n A 1 45 ALA 45 45 45 ALA ALA A . n A 1 46 SER 46 46 46 SER SER A . n A 1 47 CYS 47 47 47 CYS CYS A . n A 1 48 LEU 48 48 48 LEU LEU A . n A 1 49 TYR 49 49 49 TYR TYR A . n A 1 50 GLY 50 50 50 GLY GLY A . n A 1 51 GLN 51 51 51 GLN GLN A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 PRO 53 53 53 PRO PRO A . n A 1 54 LYS 54 54 54 LYS LYS A . n A 1 55 PHE 55 55 55 PHE PHE A . n A 1 56 GLN 56 56 56 GLN GLN A . n A 1 57 ASP 57 57 57 ASP ASP A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 ASP 59 59 59 ASP ASP A . n A 1 60 LEU 60 60 60 LEU LEU A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 TYR 63 63 63 TYR TYR A . n A 1 64 GLN 64 64 64 GLN GLN A . n A 1 65 SER 65 65 65 SER SER A . n A 1 66 ASN 66 66 66 ASN ASN A . n A 1 67 THR 67 67 67 THR THR A . n A 1 68 ILE 68 68 68 ILE ILE A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 ARG 70 70 70 ARG ARG A . n A 1 71 HIS 71 71 71 HIS HIS A . n A 1 72 LEU 72 72 72 LEU LEU A . n A 1 73 GLY 73 73 73 GLY GLY A . n A 1 74 ARG 74 74 74 ARG ARG A . n A 1 75 THR 75 75 75 THR THR A . n A 1 76 LEU 76 76 76 LEU LEU A . n A 1 77 GLY 77 77 77 GLY GLY A . n A 1 78 LEU 78 78 78 LEU LEU A . n A 1 79 TYR 79 79 79 TYR TYR A . n A 1 80 GLY 80 80 80 GLY GLY A . n A 1 81 LYS 81 81 81 LYS LYS A . n A 1 82 ASP 82 82 82 ASP ASP A . n A 1 83 GLN 83 83 83 GLN GLN A . n A 1 84 GLN 84 84 84 GLN GLN A . n A 1 85 GLU 85 85 85 GLU GLU A . n A 1 86 ALA 86 86 86 ALA ALA A . n A 1 87 ALA 87 87 87 ALA ALA A . n A 1 88 LEU 88 88 88 LEU LEU A . n A 1 89 VAL 89 89 89 VAL VAL A . n A 1 90 ASP 90 90 90 ASP ASP A . n A 1 91 MET 91 91 91 MET MET A . n A 1 92 VAL 92 92 92 VAL VAL A . n A 1 93 ASN 93 93 93 ASN ASN A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 GLY 95 95 95 GLY GLY A . n A 1 96 VAL 96 96 96 VAL VAL A . n A 1 97 GLU 97 97 97 GLU GLU A . n A 1 98 ASP 98 98 98 ASP ASP A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 CYS 101 101 101 CYS CYS A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 TYR 103 103 103 TYR TYR A . n A 1 104 ILE 104 104 104 ILE ILE A . n A 1 105 SER 105 105 105 SER SER A . n A 1 106 LEU 106 106 106 LEU LEU A . n A 1 107 ILE 107 107 107 ILE ILE A . n A 1 108 TYR 108 108 108 TYR TYR A . n A 1 109 THR 109 109 109 THR THR A . n A 1 110 ASN 110 110 110 ASN ASN A . n A 1 111 TYR 111 111 111 TYR TYR A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 GLY 114 114 114 GLY GLY A . n A 1 115 LYS 115 115 115 LYS LYS A . n A 1 116 ASP 116 116 116 ASP ASP A . n A 1 117 ASP 117 117 117 ASP ASP A . n A 1 118 TYR 118 118 118 TYR TYR A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 LYS 120 120 120 LYS LYS A . n A 1 121 ALA 121 121 121 ALA ALA A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 PRO 123 123 123 PRO PRO A . n A 1 124 GLY 124 124 124 GLY GLY A . n A 1 125 GLN 125 125 125 GLN GLN A . n A 1 126 LEU 126 126 126 LEU LEU A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 PRO 128 128 128 PRO PRO A . n A 1 129 PHE 129 129 129 PHE PHE A . n A 1 130 GLU 130 130 130 GLU GLU A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 LEU 132 132 132 LEU LEU A . n A 1 133 LEU 133 133 133 LEU LEU A . n A 1 134 SER 134 134 134 SER SER A . n A 1 135 GLN 135 135 135 GLN GLN A . n A 1 136 ASN 136 136 136 ASN ASN A . n A 1 137 GLN 137 137 137 GLN GLN A . n A 1 138 GLY 138 138 138 GLY GLY A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 THR 141 141 141 THR THR A . n A 1 142 PHE 142 142 142 PHE PHE A . n A 1 143 ILE 143 143 143 ILE ILE A . n A 1 144 VAL 144 144 144 VAL VAL A . n A 1 145 GLY 145 145 145 GLY GLY A . n A 1 146 ASP 146 146 146 ASP ASP A . n A 1 147 GLN 147 147 147 GLN GLN A . n A 1 148 ILE 148 148 148 ILE ILE A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 PHE 150 150 150 PHE PHE A . n A 1 151 ALA 151 151 151 ALA ALA A . n A 1 152 ASP 152 152 152 ASP ASP A . n A 1 153 TYR 153 153 153 TYR TYR A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 LEU 155 155 155 LEU LEU A . n A 1 156 LEU 156 156 156 LEU LEU A . n A 1 157 ASP 157 157 157 ASP ASP A . n A 1 158 LEU 158 158 158 LEU LEU A . n A 1 159 LEU 159 159 159 LEU LEU A . n A 1 160 LEU 160 160 160 LEU LEU A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 HIS 162 162 162 HIS HIS A . n A 1 163 GLU 163 163 163 GLU GLU A . n A 1 164 VAL 164 164 164 VAL VAL A . n A 1 165 LEU 165 165 165 LEU LEU A . n A 1 166 ALA 166 166 166 ALA ALA A . n A 1 167 PRO 167 167 167 PRO PRO A . n A 1 168 GLY 168 168 168 GLY GLY A . n A 1 169 CYS 169 169 169 CYS CYS A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 ALA 172 172 172 ALA ALA A . n A 1 173 PHE 173 173 173 PHE PHE A . n A 1 174 PRO 174 174 174 PRO PRO A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 SER 177 177 177 SER SER A . n A 1 178 ALA 178 178 178 ALA ALA A . n A 1 179 TYR 179 179 179 TYR TYR A . n A 1 180 VAL 180 180 180 VAL VAL A . n A 1 181 GLY 181 181 181 GLY GLY A . n A 1 182 ARG 182 182 182 ARG ARG A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 SER 184 184 184 SER SER A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 ARG 186 186 186 ARG ARG A . n A 1 187 PRO 187 187 187 PRO PRO A . n A 1 188 LYS 188 188 188 LYS LYS A . n A 1 189 LEU 189 189 189 LEU LEU A . n A 1 190 LYS 190 190 190 LYS LYS A . n A 1 191 ALA 191 191 191 ALA ALA A . n A 1 192 PHE 192 192 192 PHE PHE A . n A 1 193 LEU 193 193 193 LEU LEU A . n A 1 194 ALA 194 194 194 ALA ALA A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 PRO 196 196 196 PRO PRO A . n A 1 197 GLU 197 197 197 GLU GLU A . n A 1 198 TYR 198 198 198 TYR TYR A . n A 1 199 VAL 199 199 199 VAL VAL A . n A 1 200 ASN 200 200 200 ASN ASN A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 PRO 202 202 202 PRO PRO A . n A 1 203 ILE 203 203 203 ILE ILE A . n A 1 204 ASN 204 204 204 ASN ASN A . n A 1 205 GLY 205 205 205 GLY GLY A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLY 207 207 207 GLY GLY A . n A 1 208 LYS 208 208 208 LYS LYS A . n A 1 209 GLN 209 209 209 GLN GLN A . n B 1 1 PRO 1 1 ? ? ? B . n B 1 2 PRO 2 2 2 PRO PRO B . n B 1 3 TYR 3 3 3 TYR TYR B . n B 1 4 THR 4 4 4 THR THR B . n B 1 5 VAL 5 5 5 VAL VAL B . n B 1 6 VAL 6 6 6 VAL VAL B . n B 1 7 TYR 7 7 7 TYR TYR B . n B 1 8 PHE 8 8 8 PHE PHE B . n B 1 9 PRO 9 9 9 PRO PRO B . n B 1 10 VAL 10 10 10 VAL VAL B . n B 1 11 ARG 11 11 11 ARG ARG B . n B 1 12 GLY 12 12 12 GLY GLY B . n B 1 13 ARG 13 13 13 ARG ARG B . n B 1 14 CYS 14 14 14 CYS CYS B . n B 1 15 ALA 15 15 15 ALA ALA B . n B 1 16 ALA 16 16 16 ALA ALA B . n B 1 17 LEU 17 17 17 LEU LEU B . n B 1 18 ARG 18 18 18 ARG ARG B . n B 1 19 MET 19 19 19 MET MET B . n B 1 20 LEU 20 20 20 LEU LEU B . n B 1 21 LEU 21 21 21 LEU LEU B . n B 1 22 ALA 22 22 22 ALA ALA B . n B 1 23 ASP 23 23 23 ASP ASP B . n B 1 24 GLN 24 24 24 GLN GLN B . n B 1 25 GLY 25 25 25 GLY GLY B . n B 1 26 GLN 26 26 26 GLN GLN B . n B 1 27 SER 27 27 27 SER SER B . n B 1 28 TRP 28 28 28 TRP TRP B . n B 1 29 LYS 29 29 29 LYS LYS B . n B 1 30 GLU 30 30 30 GLU GLU B . n B 1 31 GLU 31 31 31 GLU GLU B . n B 1 32 VAL 32 32 32 VAL VAL B . n B 1 33 VAL 33 33 33 VAL VAL B . n B 1 34 THR 34 34 34 THR THR B . n B 1 35 VAL 35 35 35 VAL VAL B . n B 1 36 GLU 36 36 36 GLU GLU B . n B 1 37 THR 37 37 37 THR THR B . n B 1 38 TRP 38 38 38 TRP TRP B . n B 1 39 GLN 39 39 39 GLN GLN B . n B 1 40 GLU 40 40 40 GLU GLU B . n B 1 41 GLY 41 41 41 GLY GLY B . n B 1 42 SER 42 42 42 SER SER B . n B 1 43 LEU 43 43 43 LEU LEU B . n B 1 44 LYS 44 44 44 LYS LYS B . n B 1 45 ALA 45 45 45 ALA ALA B . n B 1 46 SER 46 46 46 SER SER B . n B 1 47 CYS 47 47 47 CYS CYS B . n B 1 48 LEU 48 48 48 LEU LEU B . n B 1 49 TYR 49 49 49 TYR TYR B . n B 1 50 GLY 50 50 50 GLY GLY B . n B 1 51 GLN 51 51 51 GLN GLN B . n B 1 52 LEU 52 52 52 LEU LEU B . n B 1 53 PRO 53 53 53 PRO PRO B . n B 1 54 LYS 54 54 54 LYS LYS B . n B 1 55 PHE 55 55 55 PHE PHE B . n B 1 56 GLN 56 56 56 GLN GLN B . n B 1 57 ASP 57 57 57 ASP ASP B . n B 1 58 GLY 58 58 58 GLY GLY B . n B 1 59 ASP 59 59 59 ASP ASP B . n B 1 60 LEU 60 60 60 LEU LEU B . n B 1 61 THR 61 61 61 THR THR B . n B 1 62 LEU 62 62 62 LEU LEU B . n B 1 63 TYR 63 63 63 TYR TYR B . n B 1 64 GLN 64 64 64 GLN GLN B . n B 1 65 SER 65 65 65 SER SER B . n B 1 66 ASN 66 66 66 ASN ASN B . n B 1 67 THR 67 67 67 THR THR B . n B 1 68 ILE 68 68 68 ILE ILE B . n B 1 69 LEU 69 69 69 LEU LEU B . n B 1 70 ARG 70 70 70 ARG ARG B . n B 1 71 HIS 71 71 71 HIS HIS B . n B 1 72 LEU 72 72 72 LEU LEU B . n B 1 73 GLY 73 73 73 GLY GLY B . n B 1 74 ARG 74 74 74 ARG ARG B . n B 1 75 THR 75 75 75 THR THR B . n B 1 76 LEU 76 76 76 LEU LEU B . n B 1 77 GLY 77 77 77 GLY GLY B . n B 1 78 LEU 78 78 78 LEU LEU B . n B 1 79 TYR 79 79 79 TYR TYR B . n B 1 80 GLY 80 80 80 GLY GLY B . n B 1 81 LYS 81 81 81 LYS LYS B . n B 1 82 ASP 82 82 82 ASP ASP B . n B 1 83 GLN 83 83 83 GLN GLN B . n B 1 84 GLN 84 84 84 GLN GLN B . n B 1 85 GLU 85 85 85 GLU GLU B . n B 1 86 ALA 86 86 86 ALA ALA B . n B 1 87 ALA 87 87 87 ALA ALA B . n B 1 88 LEU 88 88 88 LEU LEU B . n B 1 89 VAL 89 89 89 VAL VAL B . n B 1 90 ASP 90 90 90 ASP ASP B . n B 1 91 MET 91 91 91 MET MET B . n B 1 92 VAL 92 92 92 VAL VAL B . n B 1 93 ASN 93 93 93 ASN ASN B . n B 1 94 ASP 94 94 94 ASP ASP B . n B 1 95 GLY 95 95 95 GLY GLY B . n B 1 96 VAL 96 96 96 VAL VAL B . n B 1 97 GLU 97 97 97 GLU GLU B . n B 1 98 ASP 98 98 98 ASP ASP B . n B 1 99 LEU 99 99 99 LEU LEU B . n B 1 100 ARG 100 100 100 ARG ARG B . n B 1 101 CYS 101 101 101 CYS CYS B . n B 1 102 LYS 102 102 102 LYS LYS B . n B 1 103 TYR 103 103 103 TYR TYR B . n B 1 104 ILE 104 104 104 ILE ILE B . n B 1 105 SER 105 105 105 SER SER B . n B 1 106 LEU 106 106 106 LEU LEU B . n B 1 107 ILE 107 107 107 ILE ILE B . n B 1 108 TYR 108 108 108 TYR TYR B . n B 1 109 THR 109 109 109 THR THR B . n B 1 110 ASN 110 110 110 ASN ASN B . n B 1 111 TYR 111 111 111 TYR TYR B . n B 1 112 GLU 112 112 112 GLU GLU B . n B 1 113 ALA 113 113 113 ALA ALA B . n B 1 114 GLY 114 114 114 GLY GLY B . n B 1 115 LYS 115 115 115 LYS LYS B . n B 1 116 ASP 116 116 116 ASP ASP B . n B 1 117 ASP 117 117 117 ASP ASP B . n B 1 118 TYR 118 118 118 TYR TYR B . n B 1 119 VAL 119 119 119 VAL VAL B . n B 1 120 LYS 120 120 120 LYS LYS B . n B 1 121 ALA 121 121 121 ALA ALA B . n B 1 122 LEU 122 122 122 LEU LEU B . n B 1 123 PRO 123 123 123 PRO PRO B . n B 1 124 GLY 124 124 124 GLY GLY B . n B 1 125 GLN 125 125 125 GLN GLN B . n B 1 126 LEU 126 126 126 LEU LEU B . n B 1 127 LYS 127 127 127 LYS LYS B . n B 1 128 PRO 128 128 128 PRO PRO B . n B 1 129 PHE 129 129 129 PHE PHE B . n B 1 130 GLU 130 130 130 GLU GLU B . n B 1 131 THR 131 131 131 THR THR B . n B 1 132 LEU 132 132 132 LEU LEU B . n B 1 133 LEU 133 133 133 LEU LEU B . n B 1 134 SER 134 134 134 SER SER B . n B 1 135 GLN 135 135 135 GLN GLN B . n B 1 136 ASN 136 136 136 ASN ASN B . n B 1 137 GLN 137 137 137 GLN GLN B . n B 1 138 GLY 138 138 138 GLY GLY B . n B 1 139 GLY 139 139 139 GLY GLY B . n B 1 140 LYS 140 140 140 LYS LYS B . n B 1 141 THR 141 141 141 THR THR B . n B 1 142 PHE 142 142 142 PHE PHE B . n B 1 143 ILE 143 143 143 ILE ILE B . n B 1 144 VAL 144 144 144 VAL VAL B . n B 1 145 GLY 145 145 145 GLY GLY B . n B 1 146 ASP 146 146 146 ASP ASP B . n B 1 147 GLN 147 147 147 GLN GLN B . n B 1 148 ILE 148 148 148 ILE ILE B . n B 1 149 SER 149 149 149 SER SER B . n B 1 150 PHE 150 150 150 PHE PHE B . n B 1 151 ALA 151 151 151 ALA ALA B . n B 1 152 ASP 152 152 152 ASP ASP B . n B 1 153 TYR 153 153 153 TYR TYR B . n B 1 154 ASN 154 154 154 ASN ASN B . n B 1 155 LEU 155 155 155 LEU LEU B . n B 1 156 LEU 156 156 156 LEU LEU B . n B 1 157 ASP 157 157 157 ASP ASP B . n B 1 158 LEU 158 158 158 LEU LEU B . n B 1 159 LEU 159 159 159 LEU LEU B . n B 1 160 LEU 160 160 160 LEU LEU B . n B 1 161 ILE 161 161 161 ILE ILE B . n B 1 162 HIS 162 162 162 HIS HIS B . n B 1 163 GLU 163 163 163 GLU GLU B . n B 1 164 VAL 164 164 164 VAL VAL B . n B 1 165 LEU 165 165 165 LEU LEU B . n B 1 166 ALA 166 166 166 ALA ALA B . n B 1 167 PRO 167 167 167 PRO PRO B . n B 1 168 GLY 168 168 168 GLY GLY B . n B 1 169 CYS 169 169 169 CYS CYS B . n B 1 170 LEU 170 170 170 LEU LEU B . n B 1 171 ASP 171 171 171 ASP ASP B . n B 1 172 ALA 172 172 172 ALA ALA B . n B 1 173 PHE 173 173 173 PHE PHE B . n B 1 174 PRO 174 174 174 PRO PRO B . n B 1 175 LEU 175 175 175 LEU LEU B . n B 1 176 LEU 176 176 176 LEU LEU B . n B 1 177 SER 177 177 177 SER SER B . n B 1 178 ALA 178 178 178 ALA ALA B . n B 1 179 TYR 179 179 179 TYR TYR B . n B 1 180 VAL 180 180 180 VAL VAL B . n B 1 181 GLY 181 181 181 GLY GLY B . n B 1 182 ARG 182 182 182 ARG ARG B . n B 1 183 LEU 183 183 183 LEU LEU B . n B 1 184 SER 184 184 184 SER SER B . n B 1 185 ALA 185 185 185 ALA ALA B . n B 1 186 ARG 186 186 186 ARG ARG B . n B 1 187 PRO 187 187 187 PRO PRO B . n B 1 188 LYS 188 188 188 LYS LYS B . n B 1 189 LEU 189 189 189 LEU LEU B . n B 1 190 LYS 190 190 190 LYS LYS B . n B 1 191 ALA 191 191 191 ALA ALA B . n B 1 192 PHE 192 192 192 PHE PHE B . n B 1 193 LEU 193 193 193 LEU LEU B . n B 1 194 ALA 194 194 194 ALA ALA B . n B 1 195 SER 195 195 195 SER SER B . n B 1 196 PRO 196 196 196 PRO PRO B . n B 1 197 GLU 197 197 197 GLU GLU B . n B 1 198 TYR 198 198 198 TYR TYR B . n B 1 199 VAL 199 199 199 VAL VAL B . n B 1 200 ASN 200 200 200 ASN ASN B . n B 1 201 LEU 201 201 201 LEU LEU B . n B 1 202 PRO 202 202 202 PRO PRO B . n B 1 203 ILE 203 203 203 ILE ILE B . n B 1 204 ASN 204 204 204 ASN ASN B . n B 1 205 GLY 205 205 205 GLY GLY B . n B 1 206 ASN 206 206 206 ASN ASN B . n B 1 207 GLY 207 207 207 GLY GLY B . n B 1 208 LYS 208 208 208 LYS LYS B . n B 1 209 GLN 209 209 209 GLN GLN B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 VWW 1 210 1 VWW GLU A . D 3 MES 1 211 1 MES MES A . E 2 VWW 1 210 1 VWW GLU B . F 3 MES 1 211 1 MES MES B . G 4 HOH 1 212 3 HOH HOH A . G 4 HOH 2 213 6 HOH HOH A . G 4 HOH 3 214 7 HOH HOH A . G 4 HOH 4 215 8 HOH HOH A . G 4 HOH 5 216 9 HOH HOH A . G 4 HOH 6 217 11 HOH HOH A . G 4 HOH 7 218 12 HOH HOH A . G 4 HOH 8 219 14 HOH HOH A . G 4 HOH 9 220 18 HOH HOH A . G 4 HOH 10 221 20 HOH HOH A . G 4 HOH 11 222 21 HOH HOH A . G 4 HOH 12 223 23 HOH HOH A . G 4 HOH 13 224 25 HOH HOH A . G 4 HOH 14 225 26 HOH HOH A . G 4 HOH 15 226 27 HOH HOH A . G 4 HOH 16 227 28 HOH HOH A . G 4 HOH 17 228 29 HOH HOH A . G 4 HOH 18 229 31 HOH HOH A . G 4 HOH 19 230 32 HOH HOH A . G 4 HOH 20 231 35 HOH HOH A . G 4 HOH 21 232 37 HOH HOH A . G 4 HOH 22 233 39 HOH HOH A . G 4 HOH 23 234 40 HOH HOH A . G 4 HOH 24 235 43 HOH HOH A . G 4 HOH 25 236 44 HOH HOH A . G 4 HOH 26 237 45 HOH HOH A . G 4 HOH 27 238 46 HOH HOH A . G 4 HOH 28 239 47 HOH HOH A . G 4 HOH 29 240 48 HOH HOH A . G 4 HOH 30 241 49 HOH HOH A . G 4 HOH 31 242 50 HOH HOH A . G 4 HOH 32 243 51 HOH HOH A . G 4 HOH 33 244 52 HOH HOH A . G 4 HOH 34 245 53 HOH HOH A . G 4 HOH 35 246 59 HOH HOH A . G 4 HOH 36 247 62 HOH HOH A . G 4 HOH 37 248 63 HOH HOH A . G 4 HOH 38 249 65 HOH HOH A . G 4 HOH 39 250 66 HOH HOH A . G 4 HOH 40 251 68 HOH HOH A . G 4 HOH 41 252 74 HOH HOH A . G 4 HOH 42 253 76 HOH HOH A . G 4 HOH 43 254 81 HOH HOH A . G 4 HOH 44 255 82 HOH HOH A . G 4 HOH 45 256 83 HOH HOH A . G 4 HOH 46 257 85 HOH HOH A . G 4 HOH 47 258 86 HOH HOH A . G 4 HOH 48 259 89 HOH HOH A . G 4 HOH 49 260 91 HOH HOH A . G 4 HOH 50 261 92 HOH HOH A . G 4 HOH 51 262 94 HOH HOH A . G 4 HOH 52 263 96 HOH HOH A . G 4 HOH 53 264 98 HOH HOH A . G 4 HOH 54 265 100 HOH HOH A . G 4 HOH 55 266 104 HOH HOH A . G 4 HOH 56 267 105 HOH HOH A . G 4 HOH 57 268 106 HOH HOH A . G 4 HOH 58 269 108 HOH HOH A . G 4 HOH 59 270 109 HOH HOH A . G 4 HOH 60 271 110 HOH HOH A . G 4 HOH 61 272 112 HOH HOH A . G 4 HOH 62 273 117 HOH HOH A . G 4 HOH 63 274 119 HOH HOH A . G 4 HOH 64 275 120 HOH HOH A . G 4 HOH 65 276 123 HOH HOH A . G 4 HOH 66 277 125 HOH HOH A . G 4 HOH 67 278 126 HOH HOH A . G 4 HOH 68 279 130 HOH HOH A . G 4 HOH 69 280 131 HOH HOH A . G 4 HOH 70 281 133 HOH HOH A . G 4 HOH 71 282 134 HOH HOH A . G 4 HOH 72 283 138 HOH HOH A . G 4 HOH 73 284 139 HOH HOH A . G 4 HOH 74 285 140 HOH HOH A . G 4 HOH 75 286 142 HOH HOH A . G 4 HOH 76 287 144 HOH HOH A . G 4 HOH 77 288 145 HOH HOH A . G 4 HOH 78 289 146 HOH HOH A . G 4 HOH 79 290 148 HOH HOH A . G 4 HOH 80 291 149 HOH HOH A . G 4 HOH 81 292 150 HOH HOH A . G 4 HOH 82 293 151 HOH HOH A . G 4 HOH 83 294 152 HOH HOH A . G 4 HOH 84 295 153 HOH HOH A . G 4 HOH 85 296 155 HOH HOH A . G 4 HOH 86 297 158 HOH HOH A . G 4 HOH 87 298 160 HOH HOH A . G 4 HOH 88 299 162 HOH HOH A . G 4 HOH 89 300 163 HOH HOH A . G 4 HOH 90 301 164 HOH HOH A . G 4 HOH 91 302 1 HOH HOH A . G 4 HOH 92 303 19 HOH HOH A . G 4 HOH 93 304 156 HOH HOH A . H 4 HOH 1 212 4 HOH HOH B . H 4 HOH 2 213 5 HOH HOH B . H 4 HOH 3 214 10 HOH HOH B . H 4 HOH 4 215 13 HOH HOH B . H 4 HOH 5 216 15 HOH HOH B . H 4 HOH 6 217 16 HOH HOH B . H 4 HOH 7 218 17 HOH HOH B . H 4 HOH 8 219 22 HOH HOH B . H 4 HOH 9 220 24 HOH HOH B . H 4 HOH 10 221 30 HOH HOH B . H 4 HOH 11 222 33 HOH HOH B . H 4 HOH 12 223 34 HOH HOH B . H 4 HOH 13 224 36 HOH HOH B . H 4 HOH 14 225 38 HOH HOH B . H 4 HOH 15 226 41 HOH HOH B . H 4 HOH 16 227 42 HOH HOH B . H 4 HOH 17 228 54 HOH HOH B . H 4 HOH 18 229 55 HOH HOH B . H 4 HOH 19 230 56 HOH HOH B . H 4 HOH 20 231 57 HOH HOH B . H 4 HOH 21 232 58 HOH HOH B . H 4 HOH 22 233 60 HOH HOH B . H 4 HOH 23 234 64 HOH HOH B . H 4 HOH 24 235 67 HOH HOH B . H 4 HOH 25 236 69 HOH HOH B . H 4 HOH 26 237 70 HOH HOH B . H 4 HOH 27 238 71 HOH HOH B . H 4 HOH 28 239 72 HOH HOH B . H 4 HOH 29 240 73 HOH HOH B . H 4 HOH 30 241 75 HOH HOH B . H 4 HOH 31 242 77 HOH HOH B . H 4 HOH 32 243 78 HOH HOH B . H 4 HOH 33 244 79 HOH HOH B . H 4 HOH 34 245 80 HOH HOH B . H 4 HOH 35 246 84 HOH HOH B . H 4 HOH 36 247 87 HOH HOH B . H 4 HOH 37 248 88 HOH HOH B . H 4 HOH 38 249 90 HOH HOH B . H 4 HOH 39 250 93 HOH HOH B . H 4 HOH 40 251 95 HOH HOH B . H 4 HOH 41 252 97 HOH HOH B . H 4 HOH 42 253 99 HOH HOH B . H 4 HOH 43 254 101 HOH HOH B . H 4 HOH 44 255 102 HOH HOH B . H 4 HOH 45 256 103 HOH HOH B . H 4 HOH 46 257 107 HOH HOH B . H 4 HOH 47 258 111 HOH HOH B . H 4 HOH 48 259 113 HOH HOH B . H 4 HOH 49 260 114 HOH HOH B . H 4 HOH 50 261 115 HOH HOH B . H 4 HOH 51 262 116 HOH HOH B . H 4 HOH 52 263 118 HOH HOH B . H 4 HOH 53 264 121 HOH HOH B . H 4 HOH 54 265 122 HOH HOH B . H 4 HOH 55 266 124 HOH HOH B . H 4 HOH 56 267 127 HOH HOH B . H 4 HOH 57 268 128 HOH HOH B . H 4 HOH 58 269 129 HOH HOH B . H 4 HOH 59 270 132 HOH HOH B . H 4 HOH 60 271 135 HOH HOH B . H 4 HOH 61 272 136 HOH HOH B . H 4 HOH 62 273 137 HOH HOH B . H 4 HOH 63 274 141 HOH HOH B . H 4 HOH 64 275 143 HOH HOH B . H 4 HOH 65 276 147 HOH HOH B . H 4 HOH 66 277 154 HOH HOH B . H 4 HOH 67 278 157 HOH HOH B . H 4 HOH 68 279 159 HOH HOH B . H 4 HOH 69 280 161 HOH HOH B . H 4 HOH 70 281 165 HOH HOH B . H 4 HOH 71 282 166 HOH HOH B . H 4 HOH 72 283 167 HOH HOH B . H 4 HOH 73 284 168 HOH HOH B . H 4 HOH 74 285 169 HOH HOH B . H 4 HOH 75 286 2 HOH HOH B . H 4 HOH 76 287 61 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H # 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)' 4410 ? 1 MORE -19 ? 1 'SSA (A^2)' 17730 ? # _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_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 1998-09-16 2 'Structure model' 1 1 2008-03-03 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2013-02-13 5 'Structure model' 1 4 2023-08-02 # _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' 'Atomic model' 3 3 'Structure model' 'Database references' 4 3 'Structure model' 'Derived calculations' 5 3 'Structure model' 'Non-polymer description' 6 3 'Structure model' 'Structure summary' 7 3 'Structure model' 'Version format compliance' 8 4 'Structure model' 'Structure summary' 9 5 'Structure model' 'Database references' 10 5 'Structure model' 'Derived calculations' 11 5 'Structure model' Other 12 5 'Structure model' 'Refinement description' # 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 5 'Structure model' database_2 2 5 'Structure model' pdbx_database_status 3 5 'Structure model' pdbx_initial_refinement_model 4 5 '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 5 'Structure model' '_database_2.pdbx_DOI' 2 5 'Structure model' '_database_2.pdbx_database_accession' 3 5 'Structure model' '_pdbx_database_status.process_site' 4 5 'Structure model' '_struct_site.pdbx_auth_asym_id' 5 5 'Structure model' '_struct_site.pdbx_auth_comp_id' 6 5 'Structure model' '_struct_site.pdbx_auth_seq_id' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal X-PLOR 'model building' 3.1 ? 1 X-PLOR refinement 3.1 ? 2 DENZO 'data reduction' . ? 3 SCALEPACK 'data scaling' . ? 4 X-PLOR phasing 3.1 ? 5 # 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 GLN A 64 ? ? 76.75 111.49 2 1 ASN A 110 ? ? -155.80 67.97 3 1 THR A 141 ? ? -113.73 -115.50 4 1 GLN B 64 ? ? 76.76 111.19 5 1 ASN B 110 ? ? -155.72 68.01 6 1 THR B 141 ? ? -113.63 -115.38 # 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 PRO 1 ? A PRO 1 2 1 Y 1 B PRO 1 ? B PRO 1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'L-gamma-glutamyl-S-benzyl-N-[(S)-carboxy(phenyl)methyl]-L-cysteinamide' VWW 3 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 4 water HOH # _pdbx_initial_refinement_model.id 1 _pdbx_initial_refinement_model.entity_id_list ? _pdbx_initial_refinement_model.type 'experimental model' _pdbx_initial_refinement_model.source_name PDB _pdbx_initial_refinement_model.accession_code 1GSS _pdbx_initial_refinement_model.details 'PDB ENTRY 1GSS' #
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通过调用函数，我们成功下载了10gs的mmcif格式结构文件。
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附：如何获取结构对应的fasta序列文件
在进行蛋白质结构处理时，可能存在缺失结构需要对其进行修复。传统的软件修复缺失的gap时一般需要提供参考序列，如果PDB文件中没有存储序列信息，则需要提供结构对应的fasta文件。
因此，我们定义一个函数get_fasta来完成这项工作。这个函数的输入很简单，只需要输入需要下载的PDB ID即可完成工作。
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[38]
import os
import requests
import urllib.request
def get_fasta(ID):
work_path = ID
pdb_id = ID
print(f'>>> Download {pdb_id} fasta file from RCSB')
if not os.path.exists(work_path):
os.makedirs(work_path)
url = f"https://www.rcsb.org/fasta/entry/{pdb_id}"
fasta_file = os.path.join(work_path, pdb_id + '.fasta')
urllib.request.urlretrieve(url, fasta_file)
print('Done')
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假如我们需要下载10gs的fasta序列文件，我们只需要运行：
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[39]
get_fasta('10gs')
>>> Download 10gs fasta file from RCSB Done
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[40]
cat 10gs/10gs.fasta
>10GS_1|Chains A, B|GLUTATHIONE S-TRANSFERASE P1-1|Homo sapiens (9606) PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ
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可以看到，已成功下载到10gs的fasta序列文件
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**总结：**根据给出的两个函数，只需要指定PDB ID即可完成下载PDB/mmcif或者fasta文件的任务，如果你存在一系列的ID需要下载。将PDB ID逐行写入一个文件，读取该文件并依次调用目标函数并将你的ID做为函数的输入参数，即可帮你完成整个任务。
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PubChem数据库相关连接
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PubChem的链接比RCSB数据库的稍复杂一些。其可以分为三个部分：
https://pubchem.ncbi.nlm.nih.gov/rest/pug/ 输入参数的类型(如ID，smiles等)/输入参数/需要进行的操作
输入参数的类型又可以分为三个部分： domain/namespace/indetifiers
domain: 可以指定为 substance或 compound 或assay
substance的namespace包含：sid, sourceid, name等等
compound的namespace包含：cid, name, smiles, inchi, sdf, inchikey, formula 等等
assay的namespace包含：aid, listkey, type, sourceall, target, activity等等
例如：需要对cid为 23676814 的分子进行操作，输入参数部分为：
https://pubchem.ncbi.nlm.nih.gov/rest/pug/compound/cid/2367814/
如果想获取该分子的分子量，则操作部分为：
property/MolecularWeight/CSV
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[4]
# 现在，我们尝试使用一下该链接：
import requests
import urllib.request
url = "https://pubchem.ncbi.nlm.nih.gov/rest/pug/compound/cid/2367814/property/MolecularWeight/CSV"
urllib.request.urlretrieve(url, "mol.csv")
('mol.csv', <http.client.HTTPMessage at 0x7fde6e763df0>)代码
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[5]
!cat mol.csv
"CID","MolecularWeight" 2367814,365.3
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可以看到，我们已经成功获取了CID为2367814分子的分子量，为365.3
注意，如果需要一次查询多个数据，是可以使用 ',' 来分割多个关键词
例如，现在我们需要查询 2367814 分子的分子量，分子式，氢键供体数量，氢键受体数量，inchi等属性。则定义的操作部分为：
property/MolecularWeight,MolecularFormula,HBondDonorCount,HBondAcceptorCount,InChI/csv
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[10]
#现在，我们尝试一下该链接：
import requests
import urllib.request
url = "https://pubchem.ncbi.nlm.nih.gov/rest/pug/compound/cid/2367814/property/MolecularWeight,MolecularFormula,HBondDonorCount,HBondAcceptorCount,InChI/csv"
urllib.request.urlretrieve(url, "mol-1.csv")
('mol-1.csv', <http.client.HTTPMessage at 0x7fde840b7e50>)代码
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[11]
!cat mol-1.csv
"CID","MolecularWeight","MolecularFormula","HBondDonorCount","HBondAcceptorCount","InChI" 2367814,365.3,"C19H18F3NO3",1,6,"InChI=1S/C19H18F3NO3/c1-3-13-4-10-16(11-5-13)23-17(24)12(2)26-18(25)14-6-8-15(9-7-14)19(20,21)22/h4-12H,3H2,1-2H3,(H,23,24)/t12-/m0/s1"
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可以看到，已经成功获取了3467814 分子的分子量，分子式，氢键供体数量，氢键受体数量，InChI等参数
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分子3D结构的获取(sdf格式)
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获取3D格式，则操作部分的定义为：
record/SDF?record_type=3d&response_type=save&response_basename=<output filename>
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[14]
#现在，我们尝试一下下载2367814分子的3D sdf文件
import requests
import urllib.request
url = "https://pubchem.ncbi.nlm.nih.gov/rest/pug/compound/cid/2367814/record/SDF?record_type=3d&response_type=save&response_basename=2367814"
#注意： filename部分可以自行定义，该参数决定下载文件的文件名称
urllib.request.urlretrieve(url, "str.sdf")
('str.sdf', <http.client.HTTPMessage at 0x7fde6e718910>)代码
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[15]
!cat str.sdf
2367814
-OEChem-09172323283D
44 45 0 1 0 0 0 0 0999 V2000
6.6083 1.7521 1.3773 F 0 0 0 0 0 0 0 0 0 0 0 0
6.9665 1.7594 -0.7618 F 0 0 0 0 0 0 0 0 0 0 0 0
7.2947 -0.0578 0.3865 F 0 0 0 0 0 0 0 0 0 0 0 0
0.7665 -1.8237 -0.0681 O 0 0 0 0 0 0 0 0 0 0 0 0
-1.2671 -0.6024 1.2823 O 0 0 0 0 0 0 0 0 0 0 0 0
0.2245 0.0348 -1.3137 O 0 0 0 0 0 0 0 0 0 0 0 0
-2.7484 -1.3552 -0.3765 N 0 0 0 0 0 0 0 0 0 0 0 0
-0.5484 -2.3333 -0.2242 C 0 0 2 0 0 0 0 0 0 0 0 0
-6.1592 0.9800 0.2768 C 0 0 0 0 0 0 0 0 0 0 0 0
-3.9018 -0.5653 -0.1554 C 0 0 0 0 0 0 0 0 0 0 0 0
-7.3748 1.8123 0.5098 C 0 0 0 0 0 0 0 0 0 0 0 0
-1.5481 -1.3190 0.3258 C 0 0 0 0 0 0 0 0 0 0 0 0
-5.0305 1.1548 1.0775 C 0 0 0 0 0 0 0 0 0 0 0 0
-6.1512 0.0269 -0.7415 C 0 0 0 0 0 0 0 0 0 0 0 0
-3.8936 0.3765 0.8597 C 0 0 0 0 0 0 0 0 0 0 0 0
-5.0142 -0.7514 -0.9591 C 0 0 0 0 0 0 0 0 0 0 0 0
-0.6560 -3.6721 0.4906 C 0 0 0 0 0 0 0 0 0 0 0 0
2.4258 -0.2052 -0.4298 C 0 0 0 0 0 0 0 0 0 0 0 0
-7.3577 3.1048 -0.3021 C 0 0 0 0 0 0 0 0 0 0 0 0
1.0215 -0.6255 -0.6655 C 0 0 0 0 0 0 0 0 0 0 0 0
5.0346 0.5785 0.0109 C 0 0 0 0 0 0 0 0 0 0 0 0
3.0602 0.5667 -1.3815 C 0 0 0 0 0 0 0 0 0 0 0 0
3.0527 -0.5982 0.7351 C 0 0 0 0 0 0 0 0 0 0 0 0
4.3790 0.9628 -1.1588 C 0 0 0 0 0 0 0 0 0 0 0 0
4.3715 -0.2019 0.9578 C 0 0 0 0 0 0 0 0 0 0 0 0
6.4452 1.0015 0.2479 C 0 0 0 0 0 0 0 0 0 0 0 0
-0.7248 -2.4975 -1.2949 H 0 0 0 0 0 0 0 0 0 0 0 0
-8.2755 1.2376 0.2600 H 0 0 0 0 0 0 0 0 0 0 0 0
-7.4645 2.0537 1.5764 H 0 0 0 0 0 0 0 0 0 0 0 0
-2.8272 -2.0254 -1.1383 H 0 0 0 0 0 0 0 0 0 0 0 0
-5.0248 1.8962 1.8724 H 0 0 0 0 0 0 0 0 0 0 0 0
-7.0236 -0.1177 -1.3733 H 0 0 0 0 0 0 0 0 0 0 0 0
-3.0608 0.5737 1.5182 H 0 0 0 0 0 0 0 0 0 0 0 0
-5.0180 -1.4906 -1.7552 H 0 0 0 0 0 0 0 0 0 0 0 0
-1.6548 -4.1048 0.3785 H 0 0 0 0 0 0 0 0 0 0 0 0
0.0834 -4.3782 0.0985 H 0 0 0 0 0 0 0 0 0 0 0 0
-0.4518 -3.5583 1.5612 H 0 0 0 0 0 0 0 0 0 0 0 0
-7.3138 2.8971 -1.3766 H 0 0 0 0 0 0 0 0 0 0 0 0
-8.2636 3.6868 -0.1047 H 0 0 0 0 0 0 0 0 0 0 0 0
-6.4922 3.7238 -0.0429 H 0 0 0 0 0 0 0 0 0 0 0 0
2.5612 0.8694 -2.2973 H 0 0 0 0 0 0 0 0 0 0 0 0
2.5541 -1.1938 1.4938 H 0 0 0 0 0 0 0 0 0 0 0 0
4.8790 1.5697 -1.9085 H 0 0 0 0 0 0 0 0 0 0 0 0
4.8733 -0.5037 1.8734 H 0 0 0 0 0 0 0 0 0 0 0 0
1 26 1 0 0 0 0
2 26 1 0 0 0 0
3 26 1 0 0 0 0
4 8 1 0 0 0 0
4 20 1 0 0 0 0
5 12 2 0 0 0 0
6 20 2 0 0 0 0
7 10 1 0 0 0 0
7 12 1 0 0 0 0
7 30 1 0 0 0 0
8 12 1 0 0 0 0
8 17 1 0 0 0 0
8 27 1 0 0 0 0
9 11 1 0 0 0 0
9 13 2 0 0 0 0
9 14 1 0 0 0 0
10 15 2 0 0 0 0
10 16 1 0 0 0 0
11 19 1 0 0 0 0
11 28 1 0 0 0 0
11 29 1 0 0 0 0
13 15 1 0 0 0 0
13 31 1 0 0 0 0
14 16 2 0 0 0 0
14 32 1 0 0 0 0
15 33 1 0 0 0 0
16 34 1 0 0 0 0
17 35 1 0 0 0 0
17 36 1 0 0 0 0
17 37 1 0 0 0 0
18 20 1 0 0 0 0
18 22 2 0 0 0 0
18 23 1 0 0 0 0
19 38 1 0 0 0 0
19 39 1 0 0 0 0
19 40 1 0 0 0 0
21 24 2 0 0 0 0
21 25 1 0 0 0 0
21 26 1 0 0 0 0
22 24 1 0 0 0 0
22 41 1 0 0 0 0
23 25 2 0 0 0 0
23 42 1 0 0 0 0
24 43 1 0 0 0 0
25 44 1 0 0 0 0
M END
> <PUBCHEM_COMPOUND_CID>
2367814
> <PUBCHEM_CONFORMER_RMSD>
0.8
> <PUBCHEM_CONFORMER_DIVERSEORDER>
1
41
13
5
75
64
21
38
40
61
27
54
65
44
77
67
79
52
70
24
30
35
49
73
15
48
4
46
37
43
55
26
22
66
56
8
25
58
71
60
32
23
76
9
78
29
72
10
14
74
33
69
42
63
39
47
16
11
20
50
34
28
17
36
59
62
51
31
12
2
19
7
68
6
57
80
45
53
18
3
> <PUBCHEM_MMFF94_PARTIAL_CHARGES>
33
1 -0.34
10 0.12
11 0.14
12 0.57
13 -0.15
14 -0.15
15 -0.15
16 -0.15
18 0.09
2 -0.34
20 0.63
21 -0.14
22 -0.15
23 -0.15
24 -0.15
25 -0.15
26 1.16
3 -0.34
30 0.37
31 0.15
32 0.15
33 0.15
34 0.15
4 -0.43
41 0.15
42 0.15
43 0.15
44 0.15
5 -0.57
6 -0.57
7 -0.55
8 0.34
9 -0.14
> <PUBCHEM_EFFECTIVE_ROTOR_COUNT>
8
> <PUBCHEM_PHARMACOPHORE_FEATURES>
6
1 19 hydrophobe
1 5 acceptor
1 6 acceptor
1 7 donor
6 18 21 22 23 24 25 rings
6 9 10 13 14 15 16 rings
> <PUBCHEM_HEAVY_ATOM_COUNT>
26
> <PUBCHEM_ATOM_DEF_STEREO_COUNT>
1
> <PUBCHEM_ATOM_UDEF_STEREO_COUNT>
0
> <PUBCHEM_BOND_DEF_STEREO_COUNT>
0
> <PUBCHEM_BOND_UDEF_STEREO_COUNT>
0
> <PUBCHEM_ISOTOPIC_ATOM_COUNT>
0
> <PUBCHEM_COMPONENT_COUNT>
1
> <PUBCHEM_CACTVS_TAUTO_COUNT>
2
> <PUBCHEM_CONFORMER_ID>
0024214600000001
> <PUBCHEM_MMFF94_ENERGY>
64.6094
> <PUBCHEM_FEATURE_SELFOVERLAP>
30.447
> <PUBCHEM_SHAPE_FINGERPRINT>
10 15 16443346494186761172
11089746 13 18340484573257676428
11475781 23 18059863856788814868
11524674 6 15140961777099634953
11823591 26 18409163303697338247
11991303 11 15410606051413537932
12166972 35 12823299018061805274
12236239 1 18187080711203894706
12293681 160 17846782888588078083
12516196 113 9727629497324841799
12760667 363 10447932780358494719
12838862 33 18338504271523656605
13533116 47 18272650104878038642
13540713 4 18266482982406990419
13631057 29 18340482392174828895
13668630 136 9799692601531549417
13673619 4 11746935408168498774
13685833 64 10665233652701477341
13690498 29 17059760240097343591
13862211 1 9583518720079808215
14123256 34 8790881882943747409
14178184 131 11314614016634935273
14251764 18 17822292430646011639
14251764 30 9007059063014202859
14347332 77 10375330902389718980
14556957 393 13901640687146958842
14931854 50 17561085761446363257
15183329 4 15769781230073216611
15188451 53 13262691374218635449
15238133 3 18335989756949488628
15348495 7 15575006116656640845
15352257 5 12035721012128421848
15439362 3 18340489941809541519
1577012 14 18411696574087187291
17134984 74 13758065281833759596
17492 89 9870657264380328900
17780758 139 12757143581135532783
1813 80 9223229667775363779
18222031 100 10087634876009908175
19427546 20 18201432606912414911
200 152 12247691473601214854
20105231 36 16008750183087976570
20554085 129 18060126635841997050
21150785 3 14692568814752667825
21298829 104 18410013213195374621
21304304 249 10809636917710063873
21424621 283 18412544306041774179
21521239 73 12679189306317028532
21774942 28 17774728541128810928
22950370 63 9583520914982540023
23522609 53 17241624981994944374
270888 7 18411138005200562635
2767999 5 18410292519086545517
2838139 119 18412261766018799077
312425 54 16153432731684598417
3411729 13 18262236616775769779
351380 3 9295288331175069829
3633792 109 18200599094877152506
397830 11 13479423828223695095
406291 66 7997384115978210705
465052 167 8214131972024954987
474113 269 11675460586592790961
5104073 3 17242168179367546320
5385378 56 18187928326640963827
54039377 194 9583519828218748920
543368 44 18273216362330369577
5937810 71 17203616948230261345
59755656 520 18340761615417421918
6058803 2 17317897098502201822
6328613 192 18337113492266952676
636775 8 8502378862663984912
7970288 3 9511457806438966069
999808 66 12035446138220805609
> <PUBCHEM_SHAPE_MULTIPOLES>
490.66
21.51
2.61
1.17
0.61
1.14
0.03
-19.77
-1.78
-2.36
-0.2
0.43
-0.19
-0.54
> <PUBCHEM_SHAPE_SELFOVERLAP>
1045.545
> <PUBCHEM_SHAPE_VOLUME>
273.2
> <PUBCHEM_COORDINATE_TYPE>
2
5
10
$$$$
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可以看到，我们已经成功获取了2367814分子的3D结构的SDF文件
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注意：
不是所有的检索关键词都会有搜索结果。同时，由于pubchem的限制，一次搜索的最长时间是30s。如果你一次提交大量的ID和搜索的参数，超过了30s的响应时间则会失败。
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写在最后：RCSB与pubchem均为公开数据库，如果你是使用爬虫或者多线程来操作，建议控制速度。每秒访问次数>10次。
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更新于 2024-04-03
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