HEADER METHYLTRANSFERASE 09-JUL-98 1BSP TITLE THERMOSTABLE THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE A; COMPND 3 CHAIN: A, B; COMPND 4 EC: 2.1.1.45; COMPND 5 ENGINEERED: YES; COMPND 6 BIOLOGICAL_UNIT: OBLIGATE DIMER SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_CELL_LINE: X2913; SOURCE 5 EXPRESSION_SYSTEM_VECTOR: PTRC 99A; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PTRC-THYA; SOURCE 7 EXPRESSION_SYSTEM_GENE: THYA KEYWDS METHYLTRANSFERASE, DTMP SYNTHASE EXPDTA X-RAY DIFFRACTION AUTHOR T.J.STOUT,U.SCHELLENBERGER,D.V.SANTI,R.M.STROUD REVDAT 1 16-FEB-99 1BSP 0 JRNL AUTH T.J.STOUT,U.SCHELLENBERGER,D.V.SANTI,R.M.STROUD JRNL TITL CRYSTAL STRUCTURES OF A UNIQUE THERMAL-STABLE JRNL TITL 2 THYMIDYLATE SYNTHASE FROM BACILLUS SUBTILIS JRNL REF BIOCHEMISTRY V. 37 14736 1998 JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.J.GREENE,P.L.YU,J.ZHAO,C.A.SCHIFFER,D.SANTI REMARK 1 TITL EXPRESSION, PURIFICATION, AND CHARACTERIZATION OF REMARK 1 TITL 2 THYMIDYLATE SYNTHASE FROM LACTOCOCCUS LACTIS REMARK 1 REF PROTEIN SCI. V. 3 1114 1994 REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368 0795 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.NEUHARD,A.R.PRICE,L.SCHACK,E.THOMASSEN REMARK 1 TITL TWO THYMIDYLATE SYNTHETASES IN BACILLUS SUBTILIS REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 75 1194 1978 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 0040 REMARK 2 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.00 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.4 REMARK 3 NUMBER OF REFLECTIONS : 20545 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : SHELLS REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.9 REMARK 3 FREE R VALUE TEST SET COUNT : 1819 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.5 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2887 REMARK 3 BIN R VALUE (WORKING SET) : 0.252 REMARK 3 BIN FREE R VALUE : 0.301 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.1 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 256 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4610 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 113 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.2 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.2 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00 REMARK 3 B22 (A**2) : 0.00 REMARK 3 B33 (A**2) : 0.00 REMARK 3 B12 (A**2) : 0.00 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27 REMARK 3 ESD FROM SIGMAA (A) : 0.29 REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.34 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.3 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.6 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.15 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) : 2.98 ; 1.50 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.59 ; 2.00 REMARK 3 SIDE-CHAIN BOND (A**2) : 4.56 ; 2.00 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.56 ; 2.50 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 : PARAM19.SOL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED REMARK 4 REMARK 4 1BSP COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : MAY-1996 REMARK 200 TEMPERATURE (KELVIN) : 287 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NONE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MOLECULAR STRUCTURE REMARK 200 CORPORATION REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31172 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.2 REMARK 200 RESOLUTION RANGE LOW (A) : 50. REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8 REMARK 200 DATA REDUNDANCY : 4.2 REMARK 200 R MERGE (I) : 0.095 REMARK 200 R SYM (I) : 0.095 REMARK 200 FOR THE DATA SET : 11.4 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) : 2.26 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.2 REMARK 200 R MERGE FOR SHELL (I) : 0.312 REMARK 200 R SYM FOR SHELL (I) : 0.312 REMARK 200 FOR SHELL : 3.1 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR/MR REMARK 200 SOFTWARE USED: MLPHARE, AMORE, DM, X-PLOR REMARK 200 STARTING MODEL: HOMOLOGY MODEL BASED ON 1TJS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.8 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20.4% PEG8000, 68 MM REMARK 280 NA CACODYLATE PH 6.5, 136 MM AMMONIUM SULFATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 28.61230 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.01098 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.71870 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.01098 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.61230 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.71870 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 295 REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY. REMARK 295 REMARK 295 APPLIED TO TRANSFORMED TO REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD REMARK 295 SSS REMARK 295 M 1 B 4 .. 279 A 4 .. 279 0.458 REMARK 295 REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS REMARK 295 REMARK 295 REMARK: NCS TWO-FOLD ROTATION REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 0 HOH 2 DISTANCE = 5.79 ANGSTROMS REMARK 550 REMARK 550 SEGID REMARK 550 AAAA: N-TERMINUS OF MONOMER A, AAAB: C-TERM OF MONOMER A, REMARK 550 AAAD: MONOMER B, AAAC: PHOSPHATE ION, AAAE: WATERS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CTA REMARK 800 SITE_DESCRIPTION: CATALYTIC CYSTEINE. REMARK 800 REMARK 800 SITE_IDENTIFIER: CTB REMARK 800 SITE_DESCRIPTION: CATALYTIC CYSTEINE. REMARK 999 REMARK 999 SEQUENCE REMARK 999 N-TERMINAL METHIONINE PROCESSED DURING EXPRESSION. REMARK 999 REMARK 999 SEQUENCE REMARK 999 1BSP A SWS P42326 1 - 1 NOT IN ATOMS LIST REMARK 999 1BSP B SWS P42326 1 - 1 NOT IN ATOMS LIST DBREF 1BSP A 2 22 SWS P42326 TYSA_BACSU 2 22 DBREF 1BSP A 24 279 SWS P42326 TYSA_BACSU 24 279 DBREF 1BSP B 2 279 SWS P42326 TYSA_BACSU 2 279 SEQADV 1BSP A SWS P42326 GLU 23 GAP IN PDB ENTRY SEQRES 1 A 278 THR GLN PHE ASP LYS GLN TYR ASN SER ILE ILE LYS ASP SEQRES 2 A 278 ILE ILE ASN ASN GLY ILE SER ASP GLU GLU PHE ASP VAL SEQRES 3 A 278 ARG THR LYS TRP ASP SER ASP GLY THR PRO ALA HIS THR SEQRES 4 A 278 LEU SER VAL ILE SER LYS GLN MET ARG PHE ASP ASN SER SEQRES 5 A 278 GLU VAL PRO ILE LEU THR THR LYS LYS VAL ALA TRP LYS SEQRES 6 A 278 THR ALA ILE LYS GLU LEU LEU TRP ILE TRP GLN LEU LYS SEQRES 7 A 278 SER ASN ASP VAL ASN ASP LEU ASN MET MET GLY VAL HIS SEQRES 8 A 278 ILE TRP ASP GLN TRP LYS GLN GLU ASP GLY THR ILE GLY SEQRES 9 A 278 HIS ALA TYR GLY PHE GLN LEU GLY LYS LYS ASN ARG SER SEQRES 10 A 278 LEU ASN GLY GLU LYS VAL ASP GLN VAL ASP TYR LEU LEU SEQRES 11 A 278 HIS GLN LEU LYS ASN ASN PRO SER SER ARG ARG HIS ILE SEQRES 12 A 278 THR MET LEU TRP ASN PRO ASP GLU LEU ASP ALA MET ALA SEQRES 13 A 278 LEU THR PRO CYS VAL TYR GLU THR GLN TRP TYR VAL LYS SEQRES 14 A 278 HIS GLY LYS LEU HIS LEU GLU VAL ARG ALA ARG SER ASN SEQRES 15 A 278 ASP MET ALA LEU GLY ASN PRO PHE ASN VAL PHE GLN TYR SEQRES 16 A 278 ASN VAL LEU GLN ARG MET ILE ALA GLN VAL THR GLY TYR SEQRES 17 A 278 GLU LEU GLY GLU TYR ILE PHE ASN ILE GLY ASP CYS HIS SEQRES 18 A 278 VAL TYR THR ARG HIS ILE ASP ASN LEU LYS ILE GLN MET SEQRES 19 A 278 GLU ARG GLU GLN PHE GLU ALA PRO GLU LEU TRP ILE ASN SEQRES 20 A 278 PRO GLU VAL LYS ASP PHE TYR ASP PHE THR ILE ASP ASP SEQRES 21 A 278 PHE LYS LEU ILE ASN TYR LYS HIS GLY ASP LYS LEU LEU SEQRES 22 A 278 PHE GLU VAL ALA VAL SEQRES 1 B 278 THR GLN PHE ASP LYS GLN TYR ASN SER ILE ILE LYS ASP SEQRES 2 B 278 ILE ILE ASN ASN GLY ILE SER ASP GLU GLU PHE ASP VAL SEQRES 3 B 278 ARG THR LYS TRP ASP SER ASP GLY THR PRO ALA HIS THR SEQRES 4 B 278 LEU SER VAL ILE SER LYS GLN MET ARG PHE ASP ASN SER SEQRES 5 B 278 GLU VAL PRO ILE LEU THR THR LYS LYS VAL ALA TRP LYS SEQRES 6 B 278 THR ALA ILE LYS GLU LEU LEU TRP ILE TRP GLN LEU LYS SEQRES 7 B 278 SER ASN ASP VAL ASN ASP LEU ASN MET MET GLY VAL HIS SEQRES 8 B 278 ILE TRP ASP GLN TRP LYS GLN GLU ASP GLY THR ILE GLY SEQRES 9 B 278 HIS ALA TYR GLY PHE GLN LEU GLY LYS LYS ASN ARG SER SEQRES 10 B 278 LEU ASN GLY GLU LYS VAL ASP GLN VAL ASP TYR LEU LEU SEQRES 11 B 278 HIS GLN LEU LYS ASN ASN PRO SER SER ARG ARG HIS ILE SEQRES 12 B 278 THR MET LEU TRP ASN PRO ASP GLU LEU ASP ALA MET ALA SEQRES 13 B 278 LEU THR PRO CYS VAL TYR GLU THR GLN TRP TYR VAL LYS SEQRES 14 B 278 HIS GLY LYS LEU HIS LEU GLU VAL ARG ALA ARG SER ASN SEQRES 15 B 278 ASP MET ALA LEU GLY ASN PRO PHE ASN VAL PHE GLN TYR SEQRES 16 B 278 ASN VAL LEU GLN ARG MET ILE ALA GLN VAL THR GLY TYR SEQRES 17 B 278 GLU LEU GLY GLU TYR ILE PHE ASN ILE GLY ASP CYS HIS SEQRES 18 B 278 VAL TYR THR ARG HIS ILE ASP ASN LEU LYS ILE GLN MET SEQRES 19 B 278 GLU ARG GLU GLN PHE GLU ALA PRO GLU LEU TRP ILE ASN SEQRES 20 B 278 PRO GLU VAL LYS ASP PHE TYR ASP PHE THR ILE ASP ASP SEQRES 21 B 278 PHE LYS LEU ILE ASN TYR LYS HIS GLY ASP LYS LEU LEU SEQRES 22 B 278 PHE GLU VAL ALA VAL HET PO4 300 10 HETNAM PO4 PHOSPHATE ION FORMUL 3 PO4 O4 P1 3- FORMUL 4 HOH *183(H2 O1) HELIX 1 1 PHE A 4 ASN A 18 1 15 HELIX 2 2 TRP A 65 TRP A 76 1 12 HELIX 3 3 VAL A 83 MET A 88 1 6 HELIX 4 4 ASP A 95 TRP A 97 5 3 HELIX 5 5 TYR A 108 GLY A 113 5 6 HELIX 6 6 GLN A 126 ASN A 136 1 11 HELIX 7 7 PRO A 150 ALA A 155 5 6 HELIX 8 8 GLY A 188 THR A 207 1 20 HELIX 9 9 THR A 225 GLU A 236 5 12 HELIX 10 10 PHE A 254 ASP A 256 5 3 HELIX 11 11 ILE A 259 ASP A 261 5 3 HELIX 12 12 PHE B 4 ASN B 18 1 15 HELIX 13 13 TRP B 65 ILE B 75 1 11 HELIX 14 14 VAL B 83 MET B 89 1 7 HELIX 15 15 ASP B 95 TRP B 97 5 3 HELIX 16 16 TYR B 108 LEU B 112 5 5 HELIX 17 17 GLN B 126 ASN B 136 1 11 HELIX 18 18 LEU B 153 ALA B 155 5 3 HELIX 19 19 ASN B 189 VAL B 206 1 18 HELIX 20 20 THR B 225 GLU B 236 5 12 HELIX 21 21 PHE B 254 ASP B 256 5 3 HELIX 22 22 ILE B 259 ASP B 261 5 3 SHEET 1 A 3 THR A 40 ILE A 44 0 SHEET 2 A 3 ASP A 220 TYR A 224 -1 N VAL A 223 O LEU A 41 SHEET 3 A 3 SER A 182 ASP A 184 1 N ASN A 183 O ASP A 220 SHEET 1 B 5 LYS A 46 PHE A 50 0 SHEET 2 B 5 TYR A 214 ILE A 218 -1 N ILE A 218 O LYS A 46 SHEET 3 B 5 LEU A 174 ALA A 180 1 N LEU A 176 O ILE A 215 SHEET 4 B 5 VAL A 162 VAL A 169 -1 N TYR A 168 O HIS A 175 SHEET 5 B 5 ILE A 144 MET A 146 -1 N THR A 145 O THR A 165 SHEET 1 C 2 GLU A 244 ILE A 247 0 SHEET 2 C 2 PHE A 262 ILE A 265 -1 N ILE A 265 O GLU A 244 SHEET 1 D 2 LYS A 115 LEU A 119 0 SHEET 2 D 2 GLU A 122 ASP A 125 -1 N VAL A 124 O ASN A 116 SHEET 1 E 3 THR B 40 ILE B 44 0 SHEET 2 E 3 ASP B 220 TYR B 224 -1 N VAL B 223 O LEU B 41 SHEET 3 E 3 SER B 182 ASP B 184 1 N ASN B 183 O ASP B 220 SHEET 1 F 5 LYS B 46 PHE B 50 0 SHEET 2 F 5 TYR B 214 ILE B 218 -1 N ILE B 218 O LYS B 46 SHEET 3 F 5 LYS B 173 ALA B 180 1 N LEU B 176 O ILE B 215 SHEET 4 F 5 VAL B 162 LYS B 170 -1 N LYS B 170 O LYS B 173 SHEET 5 F 5 ILE B 144 MET B 146 -1 N THR B 145 O THR B 165 SHEET 1 G 2 ARG B 117 LEU B 119 0 SHEET 2 G 2 GLU B 122 VAL B 124 -1 N VAL B 124 O ARG B 117 SHEET 1 H 2 GLU B 244 ILE B 247 0 SHEET 2 H 2 PHE B 262 ILE B 265 -1 N ILE B 265 O GLU B 244 SITE 1 CTA 1 CYS A 161 SITE 1 CTB 1 CYS B 161 CRYST1 57.223 97.438 118.019 90.00 90.00 90.00 P 21 21 21 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 0.017475 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010263 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008473 0.00000 MTRIX1 1 0.935180 0.085760 0.343630 -13.25410 1 MTRIX2 1 0.078770 -0.996300 0.034280 73.56630 1 MTRIX3 1 0.345300 -0.004990 -0.938480 57.56850 1 ATOM 1 N THR A 2 38.345 46.400 22.406 1.00 53.73 AAAA N ATOM 2 CA THR A 2 37.139 45.713 22.950 1.00 49.23 AAAA C ATOM 3 C THR A 2 36.754 44.520 22.072 1.00 47.56 AAAA C ATOM 4 O THR A 2 35.793 43.817 22.373 1.00 51.58 AAAA O ATOM 5 CB THR A 2 35.961 46.694 23.010 1.00 46.51 AAAA C ATOM 6 OG1 THR A 2 35.722 47.213 21.699 1.00 39.74 AAAA O ATOM 7 CG2 THR A 2 36.316 47.861 23.916 1.00 48.22 AAAA C ATOM 8 1H THR A 2 39.142 45.743 22.351 1.00 0.00 AAAA H ATOM 9 2H THR A 2 37.965 46.720 21.486 1.00 0.00 AAAA H ATOM 10 3H THR A 2 38.547 47.224 23.003 1.00 0.00 AAAA H ATOM 11 HG1 THR A 2 34.877 47.677 21.626 1.00 0.00 AAAA H ATOM 12 N GLN A 3 37.541 44.283 21.020 1.00 41.89 AAAA N ATOM 13 CA GLN A 3 37.315 43.196 20.072 1.00 36.55 AAAA C ATOM 14 C GLN A 3 36.503 42.000 20.531 1.00 35.30 AAAA C ATOM 15 O GLN A 3 36.764 41.392 21.578 1.00 35.15 AAAA O ATOM 16 CB GLN A 3 38.640 42.702 19.471 1.00 38.20 AAAA C ATOM 17 CG GLN A 3 38.940 43.199 18.048 1.00 37.74 AAAA C ATOM 18 CD GLN A 3 37.952 42.683 17.006 1.00 38.09 AAAA C ATOM 19 OE1 GLN A 3 36.968 42.020 17.337 1.00 42.53 AAAA O ATOM 20 NE2 GLN A 3 38.225 42.968 15.739 1.00 37.87 AAAA N ATOM 21 H GLN A 3 38.274 44.849 20.744 1.00 0.00 AAAA H ATOM 22 1HE2 GLN A 3 37.552 42.694 15.084 1.00 0.00 AAAA H ATOM 23 2HE2 GLN A 3 39.056 43.431 15.489 1.00 0.00 AAAA H ATOM 24 N PHE A 4 35.536 41.657 19.694 1.00 32.43 AAAA N ATOM 25 CA PHE A 4 34.658 40.527 19.914 1.00 27.62 AAAA C ATOM 26 C PHE A 4 35.515 39.264 19.769 1.00 28.15 AAAA C ATOM 27 O PHE A 4 35.350 38.308 20.525 1.00 28.23 AAAA O ATOM 28 CB PHE A 4 33.545 40.559 18.871 1.00 20.77 AAAA C ATOM 29 CG PHE A 4 32.461 39.572 19.107 1.00 21.03 AAAA C ATOM 30 CD1 PHE A 4 32.214 39.073 20.373 1.00 21.75 AAAA C ATOM 31 CD2 PHE A 4 31.677 39.134 18.051 1.00 24.16 AAAA C ATOM 32 CE1 PHE A 4 31.198 38.152 20.583 1.00 22.22 AAAA C ATOM 33 CE2 PHE A 4 30.660 38.216 18.252 1.00 22.96 AAAA C ATOM 34 CZ PHE A 4 30.422 37.724 19.517 1.00 22.55 AAAA C ATOM 35 H PHE A 4 35.453 42.223 18.903 1.00 0.00 AAAA H ATOM 36 N ASP A 5 36.470 39.289 18.838 1.00 27.40 AAAA N ATOM 37 CA ASP A 5 37.359 38.145 18.618 1.00 25.76 AAAA C ATOM 38 C ASP A 5 37.998 37.731 19.939 1.00 25.36 AAAA C ATOM 39 O ASP A 5 37.978 36.562 20.304 1.00 30.39 AAAA O ATOM 40 CB ASP A 5 38.494 38.485 17.639 1.00 22.96 AAAA C ATOM 41 CG ASP A 5 38.006 38.901 16.262 1.00 22.01 AAAA C ATOM 42 OD1 ASP A 5 36.995 38.364 15.767 1.00 23.29 AAAA O ATOM 43 OD2 ASP A 5 38.667 39.767 15.658 1.00 25.06 AAAA O ATOM 44 H ASP A 5 36.560 40.110 18.299 1.00 0.00 AAAA H ATOM 45 N LYS A 6 38.555 38.709 20.647 1.00 26.26 AAAA N ATOM 46 CA LYS A 6 39.220 38.493 21.929 1.00 26.09 AAAA C ATOM 47 C LYS A 6 38.370 37.761 22.963 1.00 26.58 AAAA C ATOM 48 O LYS A 6 38.806 36.763 23.542 1.00 26.04 AAAA O ATOM 49 CB LYS A 6 39.656 39.834 22.526 1.00 28.48 AAAA C ATOM 50 CG LYS A 6 41.160 40.101 22.503 1.00 36.36 AAAA C ATOM 51 CD LYS A 6 41.655 40.451 21.105 1.00 42.68 AAAA C ATOM 52 CE LYS A 6 43.160 40.704 21.094 1.00 48.09 AAAA C ATOM 53 NZ LYS A 6 43.664 41.109 19.744 1.00 52.28 AAAA N ATOM 54 H LYS A 6 38.513 39.620 20.303 1.00 0.00 AAAA H ATOM 55 1HZ LYS A 6 43.433 40.385 19.031 1.00 0.00 AAAA H ATOM 56 2HZ LYS A 6 43.224 42.010 19.469 1.00 0.00 AAAA H ATOM 57 3HZ LYS A 6 44.695 41.234 19.787 1.00 0.00 AAAA H ATOM 58 N GLN A 7 37.169 38.276 23.208 1.00 25.21 AAAA N ATOM 59 CA GLN A 7 36.260 37.699 24.191 1.00 24.29 AAAA C ATOM 60 C GLN A 7 35.604 36.397 23.734 1.00 23.25 AAAA C ATOM 61 O GLN A 7 35.311 35.514 24.549 1.00 21.73 AAAA O ATOM 62 CB GLN A 7 35.214 38.741 24.595 1.00 26.52 AAAA C ATOM 63 CG GLN A 7 35.826 39.946 25.307 1.00 26.07 AAAA C ATOM 64 CD GLN A 7 34.800 40.963 25.743 1.00 24.59 AAAA C ATOM 65 OE1 GLN A 7 34.018 40.718 26.655 1.00 23.29 AAAA O ATOM 66 NE2 GLN A 7 34.794 42.113 25.088 1.00 28.98 AAAA N ATOM 67 H GLN A 7 36.903 39.079 22.703 1.00 0.00 AAAA H ATOM 68 1HE2 GLN A 7 34.161 42.791 25.412 1.00 0.00 AAAA H ATOM 69 2HE2 GLN A 7 35.402 42.276 24.336 1.00 0.00 AAAA H ATOM 70 N TYR A 8 35.372 36.294 22.430 1.00 21.23 AAAA N ATOM 71 CA TYR A 8 34.784 35.110 21.814 1.00 19.60 AAAA C ATOM 72 C TYR A 8 35.749 33.963 22.070 1.00 21.02 AAAA C ATOM 73 O TYR A 8 35.381 32.949 22.672 1.00 22.77 AAAA O ATOM 74 CB TYR A 8 34.662 35.334 20.309 1.00 18.53 AAAA C ATOM 75 CG TYR A 8 33.971 34.236 19.551 1.00 15.01 AAAA C ATOM 76 CD1 TYR A 8 32.586 34.115 19.581 1.00 9.45 AAAA C ATOM 77 CD2 TYR A 8 34.699 33.350 18.756 1.00 11.50 AAAA C ATOM 78 CE1 TYR A 8 31.937 33.147 18.837 1.00 16.75 AAAA C ATOM 79 CE2 TYR A 8 34.057 32.374 18.001 1.00 14.44 AAAA C ATOM 80 CZ TYR A 8 32.671 32.279 18.045 1.00 17.81 AAAA C ATOM 81 OH TYR A 8 32.011 31.340 17.277 1.00 23.47 AAAA O ATOM 82 H TYR A 8 35.595 37.049 21.858 1.00 0.00 AAAA H ATOM 83 HH TYR A 8 31.052 31.392 17.404 1.00 0.00 AAAA H ATOM 84 N ASN A 9 37.000 34.165 21.656 1.00 19.20 AAAA N ATOM 85 CA ASN A 9 38.057 33.178 21.821 1.00 23.49 AAAA C ATOM 86 C ASN A 9 38.188 32.737 23.268 1.00 26.81 AAAA C ATOM 87 O ASN A 9 38.342 31.547 23.548 1.00 32.99 AAAA O ATOM 88 CB ASN A 9 39.395 33.733 21.335 1.00 22.28 AAAA C ATOM 89 CG ASN A 9 39.470 33.857 19.823 1.00 22.31 AAAA C ATOM 90 OD1 ASN A 9 40.514 34.211 19.276 1.00 27.14 AAAA O ATOM 91 ND2 ASN A 9 38.365 33.574 19.139 1.00 22.29 AAAA N ATOM 92 H ASN A 9 37.226 35.028 21.250 1.00 0.00 AAAA H ATOM 93 1HD2 ASN A 9 38.467 33.744 18.175 1.00 0.00 AAAA H ATOM 94 2HD2 ASN A 9 37.529 33.275 19.528 1.00 0.00 AAAA H ATOM 95 N SER A 10 38.117 33.694 24.184 1.00 27.42 AAAA N ATOM 96 CA SER A 10 38.219 33.401 25.604 1.00 25.53 AAAA C ATOM 97 C SER A 10 37.117 32.455 26.072 1.00 22.76 AAAA C ATOM 98 O SER A 10 37.393 31.479 26.764 1.00 23.08 AAAA O ATOM 99 CB SER A 10 38.189 34.705 26.398 1.00 27.17 AAAA C ATOM 100 OG SER A 10 39.283 35.521 26.018 1.00 32.90 AAAA O ATOM 101 H SER A 10 38.054 34.643 23.931 1.00 0.00 AAAA H ATOM 102 HG SER A 10 39.312 36.335 26.531 1.00 0.00 AAAA H ATOM 103 N ILE A 11 35.877 32.728 25.679 1.00 23.06 AAAA N ATOM 104 CA ILE A 11 34.768 31.875 26.078 1.00 24.10 AAAA C ATOM 105 C ILE A 11 34.890 30.505 25.419 1.00 25.28 AAAA C ATOM 106 O ILE A 11 34.815 29.485 26.099 1.00 29.37 AAAA O ATOM 107 CB ILE A 11 33.387 32.487 25.718 1.00 21.75 AAAA C ATOM 108 CG1 ILE A 11 33.133 33.759 26.528 1.00 20.32 AAAA C ATOM 109 CG2 ILE A 11 32.276 31.478 25.994 1.00 20.22 AAAA C ATOM 110 CD1 ILE A 11 31.736 34.346 26.323 1.00 19.31 AAAA C ATOM 111 H ILE A 11 35.706 33.503 25.099 1.00 0.00 AAAA H ATOM 112 N ILE A 12 35.089 30.486 24.102 1.00 22.73 AAAA N ATOM 113 CA ILE A 12 35.210 29.235 23.358 1.00 17.14 AAAA C ATOM 114 C ILE A 12 36.266 28.330 23.997 1.00 20.31 AAAA C ATOM 115 O ILE A 12 35.994 27.161 24.292 1.00 19.21 AAAA O ATOM 116 CB ILE A 12 35.585 29.488 21.888 1.00 15.44 AAAA C ATOM 117 CG1 ILE A 12 34.493 30.299 21.189 1.00 11.89 AAAA C ATOM 118 CG2 ILE A 12 35.779 28.171 21.163 1.00 18.00 AAAA C ATOM 119 CD1 ILE A 12 33.175 29.584 21.047 1.00 7.91 AAAA C ATOM 120 H ILE A 12 35.178 31.341 23.635 1.00 0.00 AAAA H ATOM 121 N LYS A 13 37.456 28.880 24.229 1.00 15.72 AAAA N ATOM 122 CA LYS A 13 38.540 28.129 24.841 1.00 15.35 AAAA C ATOM 123 C LYS A 13 38.088 27.586 26.193 1.00 17.83 AAAA C ATOM 124 O LYS A 13 38.343 26.436 26.526 1.00 21.69 AAAA O ATOM 125 CB LYS A 13 39.768 29.024 25.009 1.00 15.98 AAAA C ATOM 126 CG LYS A 13 41.030 28.296 25.447 0.00 17.53 AAAA C ATOM 127 CD LYS A 13 42.211 29.250 25.526 0.00 18.04 AAAA C ATOM 128 CE LYS A 13 43.486 28.522 25.921 0.00 19.07 AAAA C ATOM 129 NZ LYS A 13 44.657 29.442 25.993 0.00 19.31 AAAA N ATOM 130 H LYS A 13 37.611 29.816 23.981 1.00 0.00 AAAA H ATOM 131 1HZ LYS A 13 44.804 29.902 25.071 1.00 0.00 AAAA H ATOM 132 2HZ LYS A 13 44.491 30.169 26.718 1.00 0.00 AAAA H ATOM 133 3HZ LYS A 13 45.510 28.897 26.241 1.00 0.00 AAAA H ATOM 134 N ASP A 14 37.356 28.398 26.941 1.00 19.47 AAAA N ATOM 135 CA ASP A 14 36.863 27.991 28.245 1.00 20.64 AAAA C ATOM 136 C ASP A 14 35.940 26.790 28.111 1.00 21.85 AAAA C ATOM 137 O ASP A 14 36.133 25.773 28.773 1.00 22.67 AAAA O ATOM 138 CB ASP A 14 36.122 29.141 28.919 1.00 24.46 AAAA C ATOM 139 CG ASP A 14 35.548 28.751 30.260 1.00 30.53 AAAA C ATOM 140 OD1 ASP A 14 36.331 28.320 31.134 1.00 37.31 AAAA O ATOM 141 OD2 ASP A 14 34.317 28.856 30.439 1.00 31.55 AAAA O ATOM 142 H ASP A 14 37.140 29.288 26.607 1.00 0.00 AAAA H ATOM 143 N ILE A 15 34.937 26.909 27.250 1.00 22.80 AAAA N ATOM 144 CA ILE A 15 33.990 25.833 27.017 1.00 25.78 AAAA C ATOM 145 C ILE A 15 34.721 24.541 26.632 1.00 30.90 AAAA C ATOM 146 O ILE A 15 34.354 23.459 27.113 1.00 32.65 AAAA O ATOM 147 CB ILE A 15 32.989 26.172 25.897 1.00 23.90 AAAA C ATOM 148 CG1 ILE A 15 32.175 27.408 26.259 1.00 22.42 AAAA C ATOM 149 CG2 ILE A 15 32.050 24.998 25.652 1.00 27.31 AAAA C ATOM 150 CD1 ILE A 15 31.139 27.760 25.220 1.00 20.06 AAAA C ATOM 151 H ILE A 15 34.848 27.741 26.751 1.00 0.00 AAAA H ATOM 152 N ILE A 16 35.762 24.639 25.804 1.00 31.07 AAAA N ATOM 153 CA ILE A 16 36.470 23.428 25.398 1.00 33.17 AAAA C ATOM 154 C ILE A 16 37.241 22.761 26.530 1.00 33.05 AAAA C ATOM 155 O ILE A 16 37.085 21.564 26.752 1.00 31.40 AAAA O ATOM 156 CB ILE A 16 37.374 23.623 24.117 1.00 32.62 AAAA C ATOM 157 CG1 ILE A 16 38.678 24.343 24.438 1.00 32.34 AAAA C ATOM 158 CG2 ILE A 16 36.622 24.379 23.032 1.00 30.74 AAAA C ATOM 159 CD1 ILE A 16 39.842 23.413 24.708 1.00 38.89 AAAA C ATOM 160 H ILE A 16 36.035 25.527 25.487 1.00 0.00 AAAA H ATOM 161 N ASN A 17 38.010 23.533 27.292 1.00 32.31 AAAA N ATOM 162 CA ASN A 17 38.772 22.941 28.388 1.00 32.58 AAAA C ATOM 163 C ASN A 17 38.088 22.846 29.737 1.00 30.09 AAAA C ATOM 164 O ASN A 17 38.698 22.369 30.693 1.00 31.32 AAAA O ATOM 165 CB ASN A 17 40.156 23.572 28.529 1.00 37.66 AAAA C ATOM 166 CG ASN A 17 40.130 25.084 28.458 1.00 50.80 AAAA C ATOM 167 OD1 ASN A 17 40.795 25.671 27.604 1.00 57.26 AAAA O ATOM 168 ND2 ASN A 17 39.406 25.728 29.366 1.00 56.70 AAAA N ATOM 169 H ASN A 17 38.058 24.502 27.128 1.00 0.00 AAAA H ATOM 170 1HD2 ASN A 17 39.407 26.691 29.206 1.00 0.00 AAAA H ATOM 171 2HD2 ASN A 17 38.905 25.323 30.095 1.00 0.00 AAAA H ATOM 172 N ASN A 18 36.843 23.306 29.840 1.00 25.30 AAAA N ATOM 173 CA ASN A 18 36.117 23.224 31.114 1.00 22.31 AAAA C ATOM 174 C ASN A 18 34.625 22.997 30.918 1.00 20.68 AAAA C ATOM 175 O ASN A 18 33.846 23.109 31.863 1.00 23.54 AAAA O ATOM 176 CB ASN A 18 36.327 24.492 31.963 1.00 20.72 AAAA C ATOM 177 CG ASN A 18 37.791 24.773 32.249 1.00 28.13 AAAA C ATOM 178 OD1 ASN A 18 38.327 25.796 31.830 1.00 35.22 AAAA O ATOM 179 ND2 ASN A 18 38.458 23.846 32.927 1.00 28.08 AAAA N ATOM 180 H ASN A 18 36.425 23.773 29.093 1.00 0.00 AAAA H ATOM 181 1HD2 ASN A 18 39.397 24.037 33.125 1.00 0.00 AAAA H ATOM 182 2HD2 ASN A 18 38.011 23.015 33.197 1.00 0.00 AAAA H ATOM 183 N GLY A 19 34.216 22.693 29.695 1.00 18.80 AAAA N ATOM 184 CA GLY A 19 32.807 22.465 29.433 1.00 21.20 AAAA C ATOM 185 C GLY A 19 32.257 21.179 30.025 1.00 22.06 AAAA C ATOM 186 O GLY A 19 32.992 20.241 30.320 1.00 22.09 AAAA O ATOM 187 H GLY A 19 34.838 22.597 28.947 1.00 0.00 AAAA H ATOM 188 N ILE A 20 30.937 21.132 30.137 1.00 26.38 AAAA N ATOM 189 CA ILE A 20 30.217 19.992 30.677 1.00 26.26 AAAA C ATOM 190 C ILE A 20 29.485 19.322 29.527 1.00 29.16 AAAA C ATOM 191 O ILE A 20 28.669 19.954 28.852 1.00 29.21 AAAA O ATOM 192 CB ILE A 20 29.163 20.448 31.711 1.00 26.03 AAAA C ATOM 193 CG1 ILE A 20 29.831 21.187 32.869 1.00 26.83 AAAA C ATOM 194 CG2 ILE A 20 28.375 19.262 32.224 1.00 24.92 AAAA C ATOM 195 CD1 ILE A 20 28.849 21.739 33.893 1.00 35.11 AAAA C ATOM 196 H ILE A 20 30.412 21.906 29.869 1.00 0.00 AAAA H ATOM 197 N SER A 21 29.792 18.055 29.279 1.00 31.36 AAAA N ATOM 198 CA SER A 21 29.130 17.340 28.204 1.00 31.19 AAAA C ATOM 199 C SER A 21 27.767 16.869 28.654 1.00 32.00 AAAA C ATOM 200 O SER A 21 27.536 16.674 29.850 1.00 34.35 AAAA O ATOM 201 CB SER A 21 29.970 16.152 27.738 1.00 32.99 AAAA C ATOM 202 OG SER A 21 30.800 15.681 28.780 1.00 31.32 AAAA O ATOM 203 H SER A 21 30.468 17.562 29.777 1.00 0.00 AAAA H ATOM 204 HG SER A 21 31.240 14.873 28.516 1.00 0.00 AAAA H ATOM 205 N ASP A 22 26.858 16.772 27.690 1.00 34.71 AAAA N ATOM 206 CA ASP A 22 25.491 16.314 27.905 1.00 37.56 AAAA C ATOM 207 C ASP A 22 25.415 14.786 27.778 1.00 40.79 AAAA C ATOM 208 O ASP A 22 24.302 14.228 27.916 1.00 42.98 AAAA O ATOM 209 CB ASP A 22 24.573 16.938 26.854 1.00 40.94 AAAA C ATOM 210 CG ASP A 22 24.695 16.256 25.491 1.00 45.95 AAAA C ATOM 211 OD1 ASP A 22 25.820 16.181 24.955 1.00 47.34 AAAA O ATOM 212 OD2 ASP A 22 23.669 15.768 24.967 1.00 46.55 AAAA O ATOM 213 H ASP A 22 27.108 17.026 26.789 1.00 0.00 AAAA H ATOM 214 N GLU A 24 24.321 11.145 27.460 1.00 61.51 AAAB N ATOM 215 CA GLU A 24 23.755 11.577 26.142 1.00 61.52 AAAB C ATOM 216 C GLU A 24 22.239 11.453 26.033 1.00 61.03 AAAB C ATOM 217 O GLU A 24 21.650 11.892 25.051 1.00 61.33 AAAB O ATOM 218 CB GLU A 24 24.435 10.836 24.978 1.00 62.36 AAAB C ATOM 219 CG GLU A 24 24.142 11.458 23.616 1.00 64.36 AAAB C ATOM 220 CD GLU A 24 24.360 12.978 23.599 1.00 66.00 AAAB C ATOM 221 OE1 GLU A 24 25.254 13.465 24.324 1.00 66.24 AAAB O ATOM 222 OE2 GLU A 24 23.677 13.674 22.824 1.00 67.66 AAAB O ATOM 223 N PHE A 25 21.599 10.936 27.077 1.00 61.43 AAAB N ATOM 224 CA PHE A 25 20.138 10.798 27.081 1.00 57.99 AAAB C ATOM 225 C PHE A 25 19.543 12.206 27.239 1.00 59.35 AAAB C ATOM 226 O PHE A 25 18.330 12.372 27.384 1.00 59.00 AAAB O ATOM 227 CB PHE A 25 19.704 9.897 28.248 0.00 51.22 AAAB C ATOM 228 CG PHE A 25 18.248 9.528 28.237 0.00 44.72 AAAB C ATOM 229 CD1 PHE A 25 17.702 8.805 27.181 0.00 41.63 AAAB C ATOM 230 CD2 PHE A 25 17.422 9.904 29.289 0.00 41.38 AAAB C ATOM 231 CE1 PHE A 25 16.353 8.463 27.172 0.00 39.34 AAAB C ATOM 232 CE2 PHE A 25 16.072 9.567 29.292 0.00 39.39 AAAB C ATOM 233 CZ PHE A 25 15.535 8.846 28.231 0.00 38.65 AAAB C ATOM 234 N ASP A 26 20.417 13.189 27.184 1.00 60.31 AAAB N ATOM 235 CA ASP A 26 20.048 14.599 27.375 1.00 62.25 AAAB C ATOM 236 C ASP A 26 19.545 15.236 26.073 1.00 62.54 AAAB C ATOM 237 O ASP A 26 18.350 15.526 25.922 1.00 65.85 AAAB O ATOM 238 CB ASP A 26 21.249 15.392 27.887 1.00 64.18 AAAB C ATOM 239 CG ASP A 26 21.533 15.137 29.369 1.00 69.73 AAAB C ATOM 240 OD1 ASP A 26 20.621 14.624 30.122 1.00 68.81 AAAB O ATOM 241 OD2 ASP A 26 22.685 15.432 29.865 1.00 67.31 AAAB O ATOM 242 N VAL A 27 20.507 15.432 25.133 1.00 60.97 AAAB N ATOM 243 CA VAL A 27 20.149 16.085 23.880 1.00 62.38 AAAB C ATOM 244 C VAL A 27 20.098 15.203 22.645 1.00 59.16 AAAB C ATOM 245 O VAL A 27 21.041 14.481 22.322 1.00 57.98 AAAB O ATOM 246 CB VAL A 27 21.047 17.315 23.598 1.00 65.17 AAAB C ATOM 247 CG1 VAL A 27 20.667 17.972 22.273 1.00 65.83 AAAB C ATOM 248 CG2 VAL A 27 20.912 18.322 24.742 1.00 65.95 AAAB C ATOM 249 N ARG A 28 18.966 15.290 21.957 1.00 56.22 AAAB N ATOM 250 CA ARG A 28 18.718 14.549 20.735 1.00 52.21 AAAB C ATOM 251 C ARG A 28 18.861 15.579 19.625 1.00 53.79 AAAB C ATOM 252 O ARG A 28 18.023 16.476 19.492 1.00 53.95 AAAB O ATOM 253 CB ARG A 28 17.286 14.003 20.732 1.00 48.50 AAAB C ATOM 254 CG ARG A 28 16.921 13.208 19.489 0.00 41.12 AAAB C ATOM 255 CD ARG A 28 15.443 13.369 19.154 0.00 37.14 AAAB C ATOM 256 NE ARG A 28 14.572 13.094 20.295 0.00 33.41 AAAB N ATOM 257 CZ ARG A 28 13.245 13.023 20.224 0.00 32.12 AAAB C ATOM 258 NH1 ARG A 28 12.623 13.207 19.065 0.00 31.31 AAAB N ATOM 259 NH2 ARG A 28 12.535 12.778 21.316 0.00 31.36 AAAB N ATOM 260 N THR A 29 19.952 15.495 18.879 1.00 53.35 AAAB N ATOM 261 CA THR A 29 20.177 16.417 17.777 1.00 50.53 AAAB C ATOM 262 C THR A 29 20.930 15.685 16.678 1.00 47.19 AAAB C ATOM 263 O THR A 29 22.148 15.558 16.724 1.00 48.06 AAAB O ATOM 264 CB THR A 29 20.978 17.645 18.253 1.00 51.55 AAAB C ATOM 265 OG1 THR A 29 21.542 17.369 19.550 1.00 51.55 AAAB O ATOM 266 CG2 THR A 29 20.073 18.873 18.334 1.00 49.75 AAAB C ATOM 267 N LYS A 30 20.194 15.137 15.726 1.00 43.72 AAAB N ATOM 268 CA LYS A 30 20.820 14.415 14.639 1.00 42.02 AAAB C ATOM 269 C LYS A 30 21.442 15.396 13.644 1.00 41.31 AAAB C ATOM 270 O LYS A 30 20.783 16.322 13.170 1.00 41.26 AAAB O ATOM 271 CB LYS A 30 19.794 13.526 13.938 1.00 43.54 AAAB C ATOM 272 CG LYS A 30 19.041 12.572 14.864 1.00 51.21 AAAB C ATOM 273 CD LYS A 30 19.963 11.561 15.544 1.00 57.54 AAAB C ATOM 274 CE LYS A 30 19.163 10.573 16.395 1.00 63.03 AAAB C ATOM 275 NZ LYS A 30 19.981 9.429 16.907 1.00 64.07 AAAB N ATOM 276 N TRP A 31 22.735 15.238 13.386 1.00 40.98 AAAB N ATOM 277 CA TRP A 31 23.434 16.083 12.427 1.00 39.67 AAAB C ATOM 278 C TRP A 31 22.776 15.979 11.061 1.00 41.62 AAAB C ATOM 279 O TRP A 31 22.685 14.888 10.488 1.00 41.84 AAAB O ATOM 280 CB TRP A 31 24.897 15.653 12.279 1.00 36.75 AAAB C ATOM 281 CG TRP A 31 25.797 16.091 13.378 1.00 38.23 AAAB C ATOM 282 CD1 TRP A 31 26.564 15.293 14.171 1.00 38.69 AAAB C ATOM 283 CD2 TRP A 31 26.061 17.442 13.795 1.00 41.95 AAAB C ATOM 284 NE1 TRP A 31 27.289 16.054 15.054 1.00 42.84 AAAB N ATOM 285 CE2 TRP A 31 27.003 17.377 14.848 1.00 42.24 AAAB C ATOM 286 CE3 TRP A 31 25.594 18.699 13.380 1.00 37.97 AAAB C ATOM 287 CZ2 TRP A 31 27.487 18.519 15.488 1.00 41.78 AAAB C ATOM 288 CZ3 TRP A 31 26.080 19.837 14.021 1.00 37.10 AAAB C ATOM 289 CH2 TRP A 31 27.017 19.737 15.063 1.00 41.15 AAAB C ATOM 290 N ASP A 32 22.286 17.105 10.556 1.00 46.51 AAAB N ATOM 291 CA ASP A 32 21.684 17.143 9.232 1.00 50.58 AAAB C ATOM 292 C ASP A 32 22.867 17.072 8.269 1.00 51.00 AAAB C ATOM 293 O ASP A 32 23.420 18.098 7.866 1.00 56.38 AAAB O ATOM 294 CB ASP A 32 20.901 18.450 9.031 1.00 55.13 AAAB C ATOM 295 CG ASP A 32 20.663 18.776 7.558 1.00 60.46 AAAB C ATOM 296 OD1 ASP A 32 19.897 18.048 6.887 1.00 64.46 AAAB O ATOM 297 OD2 ASP A 32 21.267 19.759 7.072 1.00 59.42 AAAB O ATOM 298 N SER A 33 23.281 15.849 7.957 1.00 47.29 AAAB N ATOM 299 CA SER A 33 24.417 15.603 7.077 1.00 44.01 AAAB C ATOM 300 C SER A 33 24.610 14.092 6.958 1.00 42.69 AAAB C ATOM 301 O SER A 33 24.598 13.539 5.857 1.00 42.60 AAAB O ATOM 302 CB SER A 33 25.672 16.267 7.666 1.00 45.51 AAAB C ATOM 303 OG SER A 33 26.865 15.587 7.322 1.00 51.12 AAAB O ATOM 304 N ASP A 34 24.784 13.427 8.099 1.00 36.81 AAAB N ATOM 305 CA ASP A 34 24.966 11.984 8.122 1.00 31.64 AAAB C ATOM 306 C ASP A 34 24.031 11.274 9.098 1.00 27.66 AAAB C ATOM 307 O ASP A 34 24.120 10.062 9.288 1.00 33.29 AAAB O ATOM 308 CB ASP A 34 26.435 11.625 8.396 1.00 27.38 AAAB C ATOM 309 CG ASP A 34 27.036 12.403 9.551 1.00 26.26 AAAB C ATOM 310 OD1 ASP A 34 26.290 12.762 10.483 1.00 23.71 AAAB O ATOM 311 OD2 ASP A 34 28.263 12.648 9.530 1.00 29.94 AAAB O ATOM 312 N GLY A 35 23.119 12.038 9.691 1.00 25.62 AAAB N ATOM 313 CA GLY A 35 22.168 11.474 10.630 1.00 19.25 AAAB C ATOM 314 C GLY A 35 22.660 11.110 12.016 1.00 23.67 AAAB C ATOM 315 O GLY A 35 21.847 10.764 12.863 1.00 26.98 AAAB O ATOM 316 N THR A 36 23.963 11.203 12.267 1.00 25.76 AAAB N ATOM 317 CA THR A 36 24.520 10.859 13.575 1.00 27.43 AAAB C ATOM 318 C THR A 36 24.192 11.918 14.644 1.00 30.66 AAAB C ATOM 319 O THR A 36 23.971 13.070 14.318 1.00 33.92 AAAB O ATOM 320 CB THR A 36 26.067 10.646 13.496 1.00 26.47 AAAB C ATOM 321 OG1 THR A 36 26.718 11.889 13.225 1.00 26.35 AAAB O ATOM 322 CG2 THR A 36 26.418 9.687 12.379 1.00 23.78 AAAB C ATOM 323 N PRO A 37 24.138 11.529 15.934 1.00 33.87 AAAB N ATOM 324 CA PRO A 37 23.836 12.449 17.043 1.00 31.88 AAAB C ATOM 325 C PRO A 37 24.866 13.542 17.300 1.00 28.88 AAAB C ATOM 326 O PRO A 37 26.069 13.311 17.267 1.00 26.00 AAAB O ATOM 327 CB PRO A 37 23.731 11.506 18.244 1.00 34.09 AAAB C ATOM 328 CG PRO A 37 23.204 10.252 17.630 1.00 36.89 AAAB C ATOM 329 CD PRO A 37 24.086 10.136 16.409 1.00 38.65 AAAB C ATOM 330 N ALA A 38 24.361 14.726 17.619 1.00 30.25 AAAB N ATOM 331 CA ALA A 38 25.172 15.905 17.897 1.00 30.14 AAAB C ATOM 332 C ALA A 38 25.290 16.080 19.400 1.00 28.74 AAAB C ATOM 333 O ALA A 38 24.287 16.139 20.116 1.00 26.53 AAAB O ATOM 334 CB ALA A 38 24.530 17.144 17.272 1.00 27.45 AAAB C ATOM 335 N HIS A 39 26.527 16.194 19.864 1.00 30.71 AAAB N ATOM 336 CA HIS A 39 26.825 16.333 21.285 1.00 29.94 AAAB C ATOM 337 C HIS A 39 27.391 17.717 21.590 1.00 25.24 AAAB C ATOM 338 O HIS A 39 28.062 18.320 20.756 1.00 21.61 AAAB O ATOM 339 CB HIS A 39 27.844 15.263 21.694 1.00 38.92 AAAB C ATOM 340 CG HIS A 39 27.499 13.876 21.222 1.00 50.33 AAAB C ATOM 341 ND1 HIS A 39 26.619 13.070 21.901 1.00 48.51 AAAB N ATOM 342 CD2 HIS A 39 27.913 13.159 20.147 1.00 51.84 AAAB C ATOM 343 CE1 HIS A 39 26.498 11.912 21.276 1.00 51.41 AAAB C ATOM 344 NE2 HIS A 39 27.277 11.941 20.202 1.00 52.44 AAAB N ATOM 345 N THR A 40 27.143 18.211 22.791 1.00 24.47 AAAB N ATOM 346 CA THR A 40 27.642 19.520 23.155 1.00 21.82 AAAB C ATOM 347 C THR A 40 28.526 19.499 24.381 1.00 18.76 AAAB C ATOM 348 O THR A 40 28.711 18.470 25.035 1.00 15.43 AAAB O ATOM 349 CB THR A 40 26.487 20.500 23.477 1.00 20.85 AAAB C ATOM 350 OG1 THR A 40 25.652 19.942 24.500 1.00 23.44 AAAB O ATOM 351 CG2 THR A 40 25.651 20.788 22.247 1.00 20.28 AAAB C ATOM 352 N LEU A 41 29.134 20.650 24.619 1.00 19.42 AAAB N ATOM 353 CA LEU A 41 29.959 20.918 25.782 1.00 17.81 AAAB C ATOM 354 C LEU A 41 29.337 22.247 26.166 1.00 19.57 AAAB C ATOM 355 O LEU A 41 29.016 23.048 25.285 1.00 21.05 AAAB O ATOM 356 CB LEU A 41 31.422 21.111 25.390 1.00 11.76 AAAB C ATOM 357 CG LEU A 41 32.292 19.864 25.290 1.00 7.20 AAAB C ATOM 358 CD1 LEU A 41 33.662 20.256 24.823 1.00 3.71 AAAB C ATOM 359 CD2 LEU A 41 32.377 19.180 26.633 1.00 4.03 AAAB C ATOM 360 N SER A 42 29.074 22.461 27.445 1.00 18.45 AAAB N ATOM 361 CA SER A 42 28.458 23.707 27.844 1.00 19.86 AAAB C ATOM 362 C SER A 42 28.997 24.245 29.146 1.00 20.17 AAAB C ATOM 363 O SER A 42 29.487 23.501 29.992 1.00 23.69 AAAB O ATOM 364 CB SER A 42 26.946 23.527 27.948 1.00 17.27 AAAB C ATOM 365 OG SER A 42 26.656 22.630 28.995 1.00 30.09 AAAB O ATOM 366 N VAL A 43 28.895 25.558 29.279 1.00 19.74 AAAB N ATOM 367 CA VAL A 43 29.328 26.292 30.449 1.00 21.23 AAAB C ATOM 368 C VAL A 43 28.139 27.159 30.837 1.00 22.13 AAAB C ATOM 369 O VAL A 43 27.234 27.387 30.031 1.00 25.81 AAAB O ATOM 370 CB VAL A 43 30.561 27.148 30.127 1.00 23.31 AAAB C ATOM 371 CG1 VAL A 43 30.664 28.310 31.079 1.00 32.11 AAAB C ATOM 372 CG2 VAL A 43 31.813 26.301 30.233 1.00 21.93 AAAB C ATOM 373 N ILE A 44 28.118 27.610 32.080 1.00 23.42 AAAB N ATOM 374 CA ILE A 44 27.016 28.418 32.562 1.00 22.11 AAAB C ATOM 375 C ILE A 44 27.449 29.846 32.854 1.00 18.91 AAAB C ATOM 376 O ILE A 44 28.603 30.096 33.206 1.00 15.47 AAAB O ATOM 377 CB ILE A 44 26.409 27.796 33.849 1.00 22.64 AAAB C ATOM 378 CG1 ILE A 44 25.779 26.439 33.533 1.00 27.53 AAAB C ATOM 379 CG2 ILE A 44 25.356 28.707 34.444 1.00 30.11 AAAB C ATOM 380 CD1 ILE A 44 25.181 25.755 34.741 1.00 23.13 AAAB C ATOM 381 N SER A 45 26.520 30.765 32.618 1.00 18.97 AAAB N ATOM 382 CA SER A 45 26.671 32.188 32.892 1.00 18.82 AAAB C ATOM 383 C SER A 45 27.938 32.870 32.399 1.00 15.18 AAAB C ATOM 384 O SER A 45 28.896 33.068 33.156 1.00 10.71 AAAB O ATOM 385 CB SER A 45 26.503 32.422 34.397 1.00 22.83 AAAB C ATOM 386 OG SER A 45 26.199 33.768 34.690 1.00 26.65 AAAB O ATOM 387 N LYS A 46 27.924 33.264 31.135 1.00 11.79 AAAB N ATOM 388 CA LYS A 46 29.061 33.955 30.552 1.00 13.00 AAAB C ATOM 389 C LYS A 46 28.595 35.338 30.148 1.00 11.28 AAAB C ATOM 390 O LYS A 46 27.412 35.541 29.878 1.00 12.67 AAAB O ATOM 391 CB LYS A 46 29.613 33.192 29.350 1.00 10.68 AAAB C ATOM 392 CG LYS A 46 30.405 31.966 29.731 1.00 15.63 AAAB C ATOM 393 CD LYS A 46 31.621 32.360 30.530 1.00 17.68 AAAB C ATOM 394 CE LYS A 46 32.350 31.151 31.037 1.00 22.11 AAAB C ATOM 395 NZ LYS A 46 33.497 31.523 31.897 1.00 33.74 AAAB N ATOM 396 N GLN A 47 29.520 36.286 30.093 1.00 11.83 AAAB N ATOM 397 CA GLN A 47 29.171 37.650 29.740 1.00 11.20 AAAB C ATOM 398 C GLN A 47 30.282 38.321 28.956 1.00 10.60 AAAB C ATOM 399 O GLN A 47 31.458 38.116 29.235 1.00 10.20 AAAB O ATOM 400 CB GLN A 47 28.893 38.455 31.012 1.00 12.63 AAAB C ATOM 401 CG GLN A 47 28.690 39.941 30.772 1.00 15.87 AAAB C ATOM 402 CD GLN A 47 28.795 40.752 32.037 1.00 14.61 AAAB C ATOM 403 OE1 GLN A 47 29.893 41.085 32.489 1.00 15.38 AAAB O ATOM 404 NE2 GLN A 47 27.656 41.071 32.624 1.00 12.40 AAAB N ATOM 405 N MET A 48 29.900 39.082 27.938 1.00 14.18 AAAB N ATOM 406 CA MET A 48 30.851 39.839 27.123 1.00 14.91 AAAB C ATOM 407 C MET A 48 30.435 41.301 27.244 1.00 10.35 AAAB C ATOM 408 O MET A 48 29.244 41.610 27.173 1.00 11.58 AAAB O ATOM 409 CB MET A 48 30.803 39.389 25.667 1.00 17.64 AAAB C ATOM 410 CG MET A 48 31.363 38.005 25.437 1.00 25.04 AAAB C ATOM 411 SD MET A 48 31.099 37.473 23.748 1.00 23.06 AAAB S ATOM 412 CE MET A 48 29.337 37.249 23.768 1.00 25.25 AAAB C ATOM 413 N ARG A 49 31.396 42.180 27.506 1.00 9.16 AAAB N ATOM 414 CA ARG A 49 31.108 43.605 27.662 1.00 13.37 AAAB C ATOM 415 C ARG A 49 31.847 44.437 26.619 1.00 13.21 AAAB C ATOM 416 O ARG A 49 33.030 44.219 26.361 1.00 14.61 AAAB O ATOM 417 CB ARG A 49 31.500 44.077 29.065 1.00 13.42 AAAB C ATOM 418 CG ARG A 49 30.782 43.355 30.194 1.00 21.24 AAAB C ATOM 419 CD ARG A 49 31.182 43.889 31.571 1.00 26.49 AAAB C ATOM 420 NE ARG A 49 30.600 45.201 31.862 1.00 30.49 AAAB N ATOM 421 CZ ARG A 49 29.732 45.447 32.844 1.00 31.99 AAAB C ATOM 422 NH1 ARG A 49 29.331 44.478 33.659 1.00 31.24 AAAB N ATOM 423 NH2 ARG A 49 29.236 46.667 32.997 1.00 33.48 AAAB N ATOM 424 N PHE A 50 31.160 45.406 26.038 1.00 11.29 AAAB N ATOM 425 CA PHE A 50 31.771 46.258 25.028 1.00 16.15 AAAB C ATOM 426 C PHE A 50 31.463 47.726 25.328 1.00 17.14 AAAB C ATOM 427 O PHE A 50 30.327 48.069 25.659 1.00 14.61 AAAB O ATOM 428 CB PHE A 50 31.239 45.902 23.643 1.00 13.44 AAAB C ATOM 429 CG PHE A 50 31.379 44.453 23.288 1.00 14.52 AAAB C ATOM 430 CD1 PHE A 50 32.589 43.946 22.840 1.00 14.43 AAAB C ATOM 431 CD2 PHE A 50 30.286 43.598 23.370 1.00 15.48 AAAB C ATOM 432 CE1 PHE A 50 32.706 42.608 22.475 1.00 9.23 AAAB C ATOM 433 CE2 PHE A 50 30.396 42.262 23.007 1.00 9.30 AAAB C ATOM 434 CZ PHE A 50 31.608 41.770 22.559 1.00 7.84 AAAB C ATOM 435 N ASP A 51 32.468 48.592 25.202 1.00 16.07 AAAB N ATOM 436 CA ASP A 51 32.281 50.021 25.473 1.00 21.36 AAAB C ATOM 437 C ASP A 51 31.837 50.815 24.247 1.00 22.86 AAAB C ATOM 438 O ASP A 51 31.899 52.041 24.245 1.00 25.12 AAAB O ATOM 439 CB ASP A 51 33.566 50.642 26.040 1.00 18.11 AAAB C ATOM 440 CG ASP A 51 34.716 50.665 25.032 1.00 19.83 AAAB C ATOM 441 OD1 ASP A 51 34.506 50.288 23.862 1.00 24.06 AAAB O ATOM 442 OD2 ASP A 51 35.843 51.056 25.410 1.00 19.82 AAAB O ATOM 443 N ASN A 52 31.457 50.104 23.190 1.00 22.27 AAAB N ATOM 444 CA ASN A 52 31.019 50.724 21.944 1.00 19.99 AAAB C ATOM 445 C ASN A 52 32.053 51.626 21.253 1.00 20.87 AAAB C ATOM 446 O ASN A 52 31.688 52.496 20.468 1.00 19.95 AAAB O ATOM 447 CB ASN A 52 29.700 51.473 22.144 1.00 16.57 AAAB C ATOM 448 CG ASN A 52 28.498 50.579 21.982 1.00 17.67 AAAB C ATOM 449 OD1 ASN A 52 28.289 50.005 20.920 1.00 19.38 AAAB O ATOM 450 ND2 ASN A 52 27.708 50.444 23.030 1.00 17.22 AAAB N ATOM 451 N SER A 53 33.341 51.391 21.505 1.00 21.12 AAAB N ATOM 452 CA SER A 53 34.383 52.179 20.848 1.00 22.96 AAAB C ATOM 453 C SER A 53 34.618 51.582 19.456 1.00 27.54 AAAB C ATOM 454 O SER A 53 35.371 52.129 18.646 1.00 32.92 AAAB O ATOM 455 CB SER A 53 35.692 52.181 21.653 1.00 24.31 AAAB C ATOM 456 OG SER A 53 36.303 50.899 21.717 1.00 22.76 AAAB O ATOM 457 N GLU A 54 33.982 50.441 19.204 1.00 26.25 AAAB N ATOM 458 CA GLU A 54 34.067 49.740 17.932 1.00 25.06 AAAB C ATOM 459 C GLU A 54 32.886 48.788 17.874 1.00 23.00 AAAB C ATOM 460 O GLU A 54 32.309 48.444 18.911 1.00 24.47 AAAB O ATOM 461 CB GLU A 54 35.380 48.961 17.819 1.00 26.28 AAAB C ATOM 462 CG GLU A 54 35.555 47.865 18.840 1.00 24.82 AAAB C ATOM 463 CD GLU A 54 36.827 47.081 18.634 1.00 24.69 AAAB C ATOM 464 OE1 GLU A 54 37.917 47.684 18.589 1.00 24.34 AAAB O ATOM 465 OE2 GLU A 54 36.735 45.848 18.513 1.00 31.01 AAAB O ATOM 466 N VAL A 55 32.493 48.413 16.663 1.00 21.33 AAAB N ATOM 467 CA VAL A 55 31.373 47.508 16.459 1.00 18.83 AAAB C ATOM 468 C VAL A 55 31.809 46.127 16.916 1.00 21.77 AAAB C ATOM 469 O VAL A 55 32.901 45.661 16.552 1.00 25.77 AAAB O ATOM 470 CB VAL A 55 30.985 47.415 14.965 1.00 21.38 AAAB C ATOM 471 CG1 VAL A 55 29.622 46.720 14.809 1.00 21.22 AAAB C ATOM 472 CG2 VAL A 55 30.973 48.805 14.324 1.00 22.47 AAAB C ATOM 473 N PRO A 56 31.008 45.475 17.782 1.00 19.37 AAAB N ATOM 474 CA PRO A 56 31.374 44.137 18.255 1.00 17.18 AAAB C ATOM 475 C PRO A 56 31.039 43.099 17.171 1.00 16.79 AAAB C ATOM 476 O PRO A 56 29.889 42.668 17.042 1.00 16.41 AAAB O ATOM 477 CB PRO A 56 30.516 43.986 19.511 1.00 13.58 AAAB C ATOM 478 CG PRO A 56 29.278 44.735 19.157 1.00 12.07 AAAB C ATOM 479 CD PRO A 56 29.821 45.977 18.497 1.00 17.11 AAAB C ATOM 480 N ILE A 57 32.034 42.721 16.371 1.00 14.19 AAAB N ATOM 481 CA ILE A 57 31.807 41.761 15.296 1.00 18.28 AAAB C ATOM 482 C ILE A 57 33.054 40.911 15.036 1.00 20.27 AAAB C ATOM 483 O ILE A 57 34.181 41.350 15.296 1.00 24.32 AAAB O ATOM 484 CB ILE A 57 31.340 42.492 14.009 1.00 20.41 AAAB C ATOM 485 CG1 ILE A 57 30.898 41.490 12.943 1.00 20.71 AAAB C ATOM 486 CG2 ILE A 57 32.441 43.401 13.489 1.00 18.03 AAAB C ATOM 487 CD1 ILE A 57 30.142 42.112 11.787 1.00 14.30 AAAB C ATOM 488 N LEU A 58 32.839 39.679 14.580 1.00 19.73 AAAB N ATOM 489 CA LEU A 58 33.931 38.750 14.309 1.00 19.09 AAAB C ATOM 490 C LEU A 58 34.682 39.052 13.018 1.00 20.08 AAAB C ATOM 491 O LEU A 58 34.087 39.479 12.025 1.00 17.12 AAAB O ATOM 492 CB LEU A 58 33.406 37.311 14.231 1.00 21.09 AAAB C ATOM 493 CG LEU A 58 33.055 36.483 15.471 1.00 19.76 AAAB C ATOM 494 CD1 LEU A 58 32.788 35.061 15.004 1.00 17.57 AAAB C ATOM 495 CD2 LEU A 58 34.196 36.485 16.483 1.00 14.17 AAAB C ATOM 496 N THR A 59 35.992 38.817 13.041 1.00 20.40 AAAB N ATOM 497 CA THR A 59 36.822 39.019 11.864 1.00 21.05 AAAB C ATOM 498 C THR A 59 37.572 37.725 11.522 1.00 23.60 AAAB C ATOM 499 O THR A 59 38.182 37.621 10.459 1.00 26.40 AAAB O ATOM 500 CB THR A 59 37.828 40.165 12.060 1.00 21.98 AAAB C ATOM 501 OG1 THR A 59 38.745 39.831 13.109 1.00 27.81 AAAB O ATOM 502 CG2 THR A 59 37.101 41.458 12.419 1.00 28.98 AAAB C ATOM 503 N THR A 60 37.532 36.744 12.423 1.00 23.13 AAAB N ATOM 504 CA THR A 60 38.185 35.454 12.191 1.00 19.88 AAAB C ATOM 505 C THR A 60 37.257 34.567 11.355 1.00 21.36 AAAB C ATOM 506 O THR A 60 37.654 33.526 10.831 1.00 19.54 AAAB O ATOM 507 CB THR A 60 38.480 34.732 13.517 1.00 17.28 AAAB C ATOM 508 OG1 THR A 60 37.300 34.722 14.329 1.00 23.47 AAAB O ATOM 509 CG2 THR A 60 39.588 35.418 14.277 1.00 7.82 AAAB C ATOM 510 N LYS A 61 36.020 35.019 11.216 1.00 21.85 AAAB N ATOM 511 CA LYS A 61 34.996 34.311 10.470 1.00 22.52 AAAB C ATOM 512 C LYS A 61 34.025 35.406 10.046 1.00 21.39 AAAB C ATOM 513 O LYS A 61 33.871 36.396 10.751 1.00 20.67 AAAB O ATOM 514 CB LYS A 61 34.317 33.299 11.404 1.00 23.61 AAAB C ATOM 515 CG LYS A 61 33.023 32.672 10.899 1.00 30.00 AAAB C ATOM 516 CD LYS A 61 32.533 31.554 11.833 1.00 30.93 AAAB C ATOM 517 CE LYS A 61 32.091 32.073 13.209 1.00 35.02 AAAB C ATOM 518 NZ LYS A 61 31.894 31.001 14.259 1.00 25.53 AAAB N ATOM 519 N LYS A 62 33.450 35.282 8.861 1.00 21.22 AAAB N ATOM 520 CA LYS A 62 32.501 36.277 8.395 1.00 25.58 AAAB C ATOM 521 C LYS A 62 31.177 36.111 9.123 1.00 25.99 AAAB C ATOM 522 O LYS A 62 30.749 34.991 9.400 1.00 31.15 AAAB O ATOM 523 CB LYS A 62 32.280 36.152 6.887 1.00 32.09 AAAB C ATOM 524 CG LYS A 62 31.107 36.969 6.361 1.00 39.73 AAAB C ATOM 525 CD LYS A 62 30.893 36.739 4.883 1.00 47.52 AAAB C ATOM 526 CE LYS A 62 29.583 37.362 4.432 1.00 55.06 AAAB C ATOM 527 NZ LYS A 62 29.419 37.278 2.955 1.00 61.76 AAAB N ATOM 528 N VAL A 63 30.539 37.234 9.431 1.00 25.35 AAAB N ATOM 529 CA VAL A 63 29.248 37.233 10.110 1.00 25.30 AAAB C ATOM 530 C VAL A 63 28.233 37.813 9.130 1.00 25.08 AAAB C ATOM 531 O VAL A 63 28.533 38.773 8.419 1.00 27.15 AAAB O ATOM 532 CB VAL A 63 29.279 38.104 11.399 1.00 24.73 AAAB C ATOM 533 CG1 VAL A 63 27.894 38.164 12.040 1.00 17.82 AAAB C ATOM 534 CG2 VAL A 63 30.306 37.559 12.384 1.00 22.77 AAAB C ATOM 535 N ALA A 64 27.041 37.229 9.085 1.00 24.54 AAAB N ATOM 536 CA ALA A 64 25.997 37.694 8.180 1.00 22.21 AAAB C ATOM 537 C ALA A 64 25.314 38.932 8.737 1.00 23.16 AAAB C ATOM 538 O ALA A 64 24.131 38.896 9.097 1.00 22.87 AAAB O ATOM 539 CB ALA A 64 24.973 36.584 7.945 1.00 25.22 AAAB C ATOM 540 N TRP A 65 26.038 40.047 8.749 1.00 23.26 AAAB N ATOM 541 CA TRP A 65 25.496 41.293 9.284 1.00 24.48 AAAB C ATOM 542 C TRP A 65 24.147 41.741 8.707 1.00 23.12 AAAB C ATOM 543 O TRP A 65 23.234 42.081 9.460 1.00 24.69 AAAB O ATOM 544 CB TRP A 65 26.537 42.417 9.215 1.00 26.57 AAAB C ATOM 545 CG TRP A 65 26.932 42.851 7.839 1.00 29.38 AAAB C ATOM 546 CD1 TRP A 65 27.980 42.388 7.104 1.00 29.36 AAAB C ATOM 547 CD2 TRP A 65 26.325 43.893 7.061 1.00 30.34 AAAB C ATOM 548 NE1 TRP A 65 28.075 43.082 5.922 1.00 26.26 AAAB N ATOM 549 CE2 TRP A 65 27.070 44.011 5.869 1.00 29.86 AAAB C ATOM 550 CE3 TRP A 65 25.228 44.741 7.261 1.00 29.90 AAAB C ATOM 551 CZ2 TRP A 65 26.753 44.945 4.877 1.00 29.35 AAAB C ATOM 552 CZ3 TRP A 65 24.916 45.670 6.274 1.00 32.51 AAAB C ATOM 553 CH2 TRP A 65 25.678 45.762 5.097 1.00 27.39 AAAB C ATOM 554 N LYS A 66 24.007 41.706 7.385 1.00 22.66 AAAB N ATOM 555 CA LYS A 66 22.759 42.109 6.733 1.00 21.92 AAAB C ATOM 556 C LYS A 66 21.541 41.324 7.215 1.00 18.38 AAAB C ATOM 557 O LYS A 66 20.468 41.884 7.418 1.00 23.39 AAAB O ATOM 558 CB LYS A 66 22.869 41.943 5.214 1.00 28.65 AAAB C ATOM 559 CG LYS A 66 23.324 43.163 4.443 1.00 33.35 AAAB C ATOM 560 CD LYS A 66 23.024 42.962 2.963 1.00 35.57 AAAB C ATOM 561 CE LYS A 66 23.205 44.236 2.166 1.00 38.10 AAAB C ATOM 562 NZ LYS A 66 22.659 44.076 0.790 1.00 42.02 AAAB N ATOM 563 N THR A 67 21.706 40.020 7.371 1.00 18.33 AAAB N ATOM 564 CA THR A 67 20.616 39.164 7.810 1.00 18.80 AAAB C ATOM 565 C THR A 67 20.270 39.465 9.263 1.00 15.19 AAAB C ATOM 566 O THR A 67 19.094 39.477 9.639 1.00 16.33 AAAB O ATOM 567 CB THR A 67 20.988 37.678 7.636 1.00 20.11 AAAB C ATOM 568 OG1 THR A 67 21.539 37.484 6.327 1.00 19.64 AAAB O ATOM 569 CG2 THR A 67 19.762 36.788 7.801 1.00 25.09 AAAB C ATOM 570 N ALA A 68 21.298 39.719 10.068 1.00 10.66 AAAB N ATOM 571 CA ALA A 68 21.109 40.047 11.471 1.00 12.67 AAAB C ATOM 572 C ALA A 68 20.186 41.260 11.570 1.00 16.72 AAAB C ATOM 573 O ALA A 68 19.216 41.259 12.333 1.00 17.95 AAAB O ATOM 574 CB ALA A 68 22.451 40.342 12.124 1.00 11.54 AAAB C ATOM 575 N ILE A 69 20.448 42.263 10.734 1.00 18.74 AAAB N ATOM 576 CA ILE A 69 19.652 43.485 10.725 1.00 16.19 AAAB C ATOM 577 C ILE A 69 18.239 43.275 10.176 1.00 17.33 AAAB C ATOM 578 O ILE A 69 17.279 43.856 10.697 1.00 15.70 AAAB O ATOM 579 CB ILE A 69 20.376 44.634 9.971 1.00 17.27 AAAB C ATOM 580 CG1 ILE A 69 21.744 44.890 10.619 1.00 14.71 AAAB C ATOM 581 CG2 ILE A 69 19.535 45.913 10.004 1.00 17.48 AAAB C ATOM 582 CD1 ILE A 69 22.562 45.972 9.950 1.00 10.88 AAAB C ATOM 583 N LYS A 70 18.094 42.451 9.139 1.00 19.73 AAAB N ATOM 584 CA LYS A 70 16.764 42.190 8.567 1.00 19.85 AAAB C ATOM 585 C LYS A 70 15.848 41.509 9.579 1.00 18.10 AAAB C ATOM 586 O LYS A 70 14.672 41.858 9.702 1.00 19.10 AAAB O ATOM 587 CB LYS A 70 16.860 41.326 7.310 1.00 22.05 AAAB C ATOM 588 CG LYS A 70 17.589 41.970 6.160 1.00 26.75 AAAB C ATOM 589 CD LYS A 70 17.492 41.095 4.931 1.00 31.81 AAAB C ATOM 590 CE LYS A 70 18.200 41.719 3.753 1.00 31.26 AAAB C ATOM 591 NZ LYS A 70 18.187 40.797 2.595 1.00 32.59 AAAB N ATOM 592 N GLU A 71 16.388 40.536 10.306 1.00 17.23 AAAB N ATOM 593 CA GLU A 71 15.603 39.829 11.312 1.00 17.21 AAAB C ATOM 594 C GLU A 71 15.274 40.815 12.431 1.00 14.01 AAAB C ATOM 595 O GLU A 71 14.141 40.863 12.923 1.00 12.26 AAAB O ATOM 596 CB GLU A 71 16.382 38.647 11.879 1.00 14.68 AAAB C ATOM 597 CG GLU A 71 15.482 37.614 12.507 1.00 22.53 AAAB C ATOM 598 CD GLU A 71 16.139 36.881 13.648 1.00 28.79 AAAB C ATOM 599 OE1 GLU A 71 17.381 36.757 13.655 1.00 30.93 AAAB O ATOM 600 OE2 GLU A 71 15.406 36.440 14.555 1.00 36.73 AAAB O ATOM 601 N LEU A 72 16.273 41.606 12.817 1.00 12.48 AAAB N ATOM 602 CA LEU A 72 16.107 42.614 13.849 1.00 14.56 AAAB C ATOM 603 C LEU A 72 14.909 43.513 13.540 1.00 17.54 AAAB C ATOM 604 O LEU A 72 14.002 43.660 14.362 1.00 18.89 AAAB O ATOM 605 CB LEU A 72 17.366 43.463 13.953 1.00 15.86 AAAB C ATOM 606 CG LEU A 72 17.355 44.522 15.055 1.00 16.10 AAAB C ATOM 607 CD1 LEU A 72 17.291 43.835 16.412 1.00 20.59 AAAB C ATOM 608 CD2 LEU A 72 18.601 45.385 14.949 1.00 15.05 AAAB C ATOM 609 N LEU A 73 14.896 44.083 12.337 1.00 15.07 AAAB N ATOM 610 CA LEU A 73 13.821 44.975 11.908 1.00 16.16 AAAB C ATOM 611 C LEU A 73 12.458 44.284 11.928 1.00 15.59 AAAB C ATOM 612 O LEU A 73 11.453 44.876 12.331 1.00 15.73 AAAB O ATOM 613 CB LEU A 73 14.116 45.502 10.502 1.00 17.68 AAAB C ATOM 614 CG LEU A 73 15.339 46.408 10.370 1.00 19.89 AAAB C ATOM 615 CD1 LEU A 73 15.807 46.498 8.909 1.00 9.63 AAAB C ATOM 616 CD2 LEU A 73 14.995 47.772 10.941 1.00 14.81 AAAB C ATOM 617 N TRP A 74 12.434 43.043 11.461 1.00 13.37 AAAB N ATOM 618 CA TRP A 74 11.224 42.238 11.410 1.00 14.05 AAAB C ATOM 619 C TRP A 74 10.631 42.052 12.823 1.00 15.13 AAAB C ATOM 620 O TRP A 74 9.414 42.182 13.040 1.00 10.67 AAAB O ATOM 621 CB TRP A 74 11.576 40.895 10.755 1.00 13.54 AAAB C ATOM 622 CG TRP A 74 10.495 39.883 10.782 1.00 14.32 AAAB C ATOM 623 CD1 TRP A 74 9.241 40.006 10.260 1.00 12.67 AAAB C ATOM 624 CD2 TRP A 74 10.565 38.579 11.368 1.00 16.29 AAAB C ATOM 625 NE1 TRP A 74 8.522 38.857 10.484 1.00 16.93 AAAB N ATOM 626 CE2 TRP A 74 9.309 37.962 11.162 1.00 15.21 AAAB C ATOM 627 CE3 TRP A 74 11.567 37.871 12.053 1.00 13.64 AAAB C ATOM 628 CZ2 TRP A 74 9.023 36.666 11.615 1.00 15.78 AAAB C ATOM 629 CZ3 TRP A 74 11.281 36.582 12.507 1.00 16.82 AAAB C ATOM 630 CH2 TRP A 74 10.016 35.994 12.284 1.00 16.20 AAAB C ATOM 631 N ILE A 75 11.512 41.802 13.785 1.00 14.98 AAAB N ATOM 632 CA ILE A 75 11.112 41.612 15.175 1.00 18.25 AAAB C ATOM 633 C ILE A 75 10.770 42.934 15.886 1.00 18.84 AAAB C ATOM 634 O ILE A 75 9.631 43.143 16.323 1.00 20.30 AAAB O ATOM 635 CB ILE A 75 12.241 40.902 15.974 1.00 20.18 AAAB C ATOM 636 CG1 ILE A 75 12.464 39.490 15.430 1.00 18.45 AAAB C ATOM 637 CG2 ILE A 75 11.902 40.861 17.463 1.00 22.64 AAAB C ATOM 638 CD1 ILE A 75 13.793 38.897 15.822 1.00 10.91 AAAB C ATOM 639 N TRP A 76 11.748 43.833 15.960 1.00 14.32 AAAB N ATOM 640 CA TRP A 76 11.581 45.099 16.654 1.00 15.15 AAAB C ATOM 641 C TRP A 76 10.844 46.220 15.962 1.00 15.17 AAAB C ATOM 642 O TRP A 76 10.123 46.970 16.613 1.00 17.66 AAAB O ATOM 643 CB TRP A 76 12.926 45.614 17.143 1.00 17.31 AAAB C ATOM 644 CG TRP A 76 13.454 44.825 18.276 1.00 19.16 AAAB C ATOM 645 CD1 TRP A 76 14.107 43.638 18.210 1.00 15.62 AAAB C ATOM 646 CD2 TRP A 76 13.359 45.158 19.662 1.00 22.82 AAAB C ATOM 647 NE1 TRP A 76 14.425 43.204 19.468 1.00 20.55 AAAB N ATOM 648 CE2 TRP A 76 13.978 44.119 20.382 1.00 20.28 AAAB C ATOM 649 CE3 TRP A 76 12.811 46.240 20.367 1.00 26.97 AAAB C ATOM 650 CZ2 TRP A 76 14.067 44.125 21.769 1.00 20.09 AAAB C ATOM 651 CZ3 TRP A 76 12.899 46.246 21.747 1.00 21.29 AAAB C ATOM 652 CH2 TRP A 76 13.523 45.194 22.433 1.00 25.46 AAAB C ATOM 653 N GLN A 77 11.024 46.368 14.661 1.00 15.06 AAAB N ATOM 654 CA GLN A 77 10.346 47.458 13.991 1.00 17.36 AAAB C ATOM 655 C GLN A 77 8.968 47.092 13.472 1.00 16.55 AAAB C ATOM 656 O GLN A 77 7.981 47.735 13.835 1.00 15.73 AAAB O ATOM 657 CB GLN A 77 11.200 48.037 12.880 1.00 20.01 AAAB C ATOM 658 CG GLN A 77 10.690 49.372 12.416 1.00 24.79 AAAB C ATOM 659 CD GLN A 77 11.349 49.812 11.152 1.00 26.86 AAAB C ATOM 660 OE1 GLN A 77 10.903 49.458 10.064 1.00 31.13 AAAB O ATOM 661 NE2 GLN A 77 12.411 50.603 11.274 1.00 29.75 AAAB N ATOM 662 N LEU A 78 8.902 46.096 12.595 1.00 18.48 AAAB N ATOM 663 CA LEU A 78 7.617 45.668 12.051 1.00 24.35 AAAB C ATOM 664 C LEU A 78 6.800 45.003 13.158 1.00 26.42 AAAB C ATOM 665 O LEU A 78 5.565 45.070 13.151 1.00 24.52 AAAB O ATOM 666 CB LEU A 78 7.811 44.698 10.878 1.00 27.52 AAAB C ATOM 667 CG LEU A 78 8.644 45.174 9.685 1.00 26.21 AAAB C ATOM 668 CD1 LEU A 78 8.683 44.090 8.622 1.00 24.48 AAAB C ATOM 669 CD2 LEU A 78 8.053 46.444 9.120 1.00 27.98 AAAB C ATOM 670 N LYS A 79 7.508 44.369 14.100 1.00 26.35 AAAB N ATOM 671 CA LYS A 79 6.905 43.681 15.236 1.00 23.56 AAAB C ATOM 672 C LYS A 79 5.952 42.614 14.746 1.00 27.06 AAAB C ATOM 673 O LYS A 79 4.794 42.576 15.163 1.00 27.42 AAAB O ATOM 674 CB LYS A 79 6.146 44.663 16.122 1.00 24.21 AAAB C ATOM 675 CG LYS A 79 6.970 45.830 16.588 1.00 27.38 AAAB C ATOM 676 CD LYS A 79 6.074 46.903 17.149 1.00 30.80 AAAB C ATOM 677 CE LYS A 79 6.841 48.191 17.356 1.00 33.27 AAAB C ATOM 678 NZ LYS A 79 5.936 49.226 17.899 1.00 34.15 AAAB N ATOM 679 N SER A 80 6.431 41.753 13.854 1.00 31.40 AAAB N ATOM 680 CA SER A 80 5.579 40.701 13.322 1.00 32.82 AAAB C ATOM 681 C SER A 80 6.069 39.288 13.620 1.00 32.09 AAAB C ATOM 682 O SER A 80 7.249 39.054 13.903 1.00 27.45 AAAB O ATOM 683 CB SER A 80 5.341 40.896 11.813 1.00 37.57 AAAB C ATOM 684 OG SER A 80 6.527 40.741 11.052 1.00 36.88 AAAB O ATOM 685 N ASN A 81 5.117 38.365 13.642 1.00 34.84 AAAB N ATOM 686 CA ASN A 81 5.388 36.959 13.894 1.00 39.56 AAAB C ATOM 687 C ASN A 81 5.163 36.225 12.577 1.00 44.06 AAAB C ATOM 688 O ASN A 81 5.156 34.995 12.534 1.00 47.65 AAAB O ATOM 689 CB ASN A 81 4.412 36.427 14.947 1.00 37.42 AAAB C ATOM 690 CG ASN A 81 2.955 36.604 14.534 1.00 37.94 AAAB C ATOM 691 OD1 ASN A 81 2.659 37.200 13.499 1.00 38.99 AAAB O ATOM 692 ND2 ASN A 81 2.042 36.102 15.348 1.00 38.47 AAAB N ATOM 693 N ASP A 82 4.968 36.995 11.509 1.00 46.05 AAAB N ATOM 694 CA ASP A 82 4.711 36.450 10.181 1.00 45.78 AAAB C ATOM 695 C ASP A 82 6.005 36.229 9.404 1.00 45.25 AAAB C ATOM 696 O ASP A 82 6.716 37.186 9.083 1.00 47.09 AAAB O ATOM 697 CB ASP A 82 3.803 37.410 9.405 1.00 47.07 AAAB C ATOM 698 CG ASP A 82 3.118 36.751 8.221 1.00 50.07 AAAB C ATOM 699 OD1 ASP A 82 3.689 35.813 7.631 1.00 51.32 AAAB O ATOM 700 OD2 ASP A 82 1.994 37.174 7.879 1.00 51.06 AAAB O ATOM 701 N VAL A 83 6.268 34.975 9.044 1.00 42.86 AAAB N ATOM 702 CA VAL A 83 7.468 34.621 8.288 1.00 39.44 AAAB C ATOM 703 C VAL A 83 7.386 35.133 6.847 1.00 37.95 AAAB C ATOM 704 O VAL A 83 8.408 35.301 6.182 1.00 37.69 AAAB O ATOM 705 CB VAL A 83 7.722 33.098 8.292 1.00 37.34 AAAB C ATOM 706 CG1 VAL A 83 9.109 32.792 7.730 1.00 32.38 AAAB C ATOM 707 CG2 VAL A 83 7.583 32.553 9.700 1.00 37.15 AAAB C ATOM 708 N ASN A 84 6.171 35.379 6.365 1.00 35.36 AAAB N ATOM 709 CA ASN A 84 5.993 35.901 5.014 1.00 37.90 AAAB C ATOM 710 C ASN A 84 6.678 37.258 4.871 1.00 38.76 AAAB C ATOM 711 O ASN A 84 7.476 37.455 3.951 1.00 39.82 AAAB O ATOM 712 CB ASN A 84 4.513 36.021 4.661 1.00 41.68 AAAB C ATOM 713 CG ASN A 84 3.796 34.693 4.733 1.00 48.33 AAAB C ATOM 714 OD1 ASN A 84 4.344 33.662 4.340 1.00 52.43 AAAB O ATOM 715 ND2 ASN A 84 2.579 34.699 5.273 1.00 47.82 AAAB N ATOM 716 N ASP A 85 6.394 38.173 5.803 1.00 36.67 AAAB N ATOM 717 CA ASP A 85 6.991 39.509 5.792 1.00 32.80 AAAB C ATOM 718 C ASP A 85 8.495 39.351 5.707 1.00 32.99 AAAB C ATOM 719 O ASP A 85 9.150 39.958 4.865 1.00 37.95 AAAB O ATOM 720 CB ASP A 85 6.655 40.285 7.073 1.00 34.04 AAAB C ATOM 721 CG ASP A 85 5.173 40.620 7.201 1.00 39.08 AAAB C ATOM 722 OD1 ASP A 85 4.428 40.508 6.206 1.00 44.34 AAAB O ATOM 723 OD2 ASP A 85 4.749 41.005 8.313 1.00 45.50 AAAB O ATOM 724 N LEU A 86 9.036 38.496 6.563 1.00 32.18 AAAB N ATOM 725 CA LEU A 86 10.470 38.249 6.581 1.00 31.42 AAAB C ATOM 726 C LEU A 86 10.951 37.647 5.256 1.00 34.44 AAAB C ATOM 727 O LEU A 86 12.086 37.889 4.831 1.00 35.49 AAAB O ATOM 728 CB LEU A 86 10.820 37.340 7.753 1.00 24.93 AAAB C ATOM 729 CG LEU A 86 12.297 37.046 7.981 1.00 23.85 AAAB C ATOM 730 CD1 LEU A 86 13.081 38.312 8.273 1.00 14.55 AAAB C ATOM 731 CD2 LEU A 86 12.406 36.084 9.133 1.00 23.82 AAAB C ATOM 732 N ASN A 87 10.084 36.879 4.598 1.00 35.66 AAAB N ATOM 733 CA ASN A 87 10.426 36.267 3.314 1.00 35.81 AAAB C ATOM 734 C ASN A 87 10.543 37.339 2.244 1.00 33.95 AAAB C ATOM 735 O ASN A 87 11.431 37.281 1.384 1.00 31.84 AAAB O ATOM 736 CB ASN A 87 9.392 35.211 2.911 1.00 37.97 AAAB C ATOM 737 CG ASN A 87 9.761 33.802 3.389 1.00 41.29 AAAB C ATOM 738 OD1 ASN A 87 9.191 32.815 2.924 1.00 46.84 AAAB O ATOM 739 ND2 ASN A 87 10.729 33.700 4.290 1.00 40.45 AAAB N ATOM 740 N MET A 88 9.656 38.328 2.318 1.00 31.50 AAAB N ATOM 741 CA MET A 88 9.669 39.448 1.384 1.00 33.09 AAAB C ATOM 742 C MET A 88 10.921 40.300 1.600 1.00 34.48 AAAB C ATOM 743 O MET A 88 11.270 41.123 0.758 1.00 40.30 AAAB O ATOM 744 CB MET A 88 8.415 40.300 1.541 1.00 28.90 AAAB C ATOM 745 CG MET A 88 7.150 39.601 1.132 1.00 26.54 AAAB C ATOM 746 SD MET A 88 5.717 40.582 1.542 1.00 43.53 AAAB S ATOM 747 CE MET A 88 4.486 39.814 0.508 1.00 40.35 AAAB C ATOM 748 N MET A 89 11.571 40.124 2.747 1.00 33.77 AAAB N ATOM 749 CA MET A 89 12.806 40.838 3.049 1.00 31.78 AAAB C ATOM 750 C MET A 89 13.991 40.039 2.498 1.00 32.19 AAAB C ATOM 751 O MET A 89 15.149 40.405 2.714 1.00 32.99 AAAB O ATOM 752 CB MET A 89 12.987 41.000 4.555 1.00 36.41 AAAB C ATOM 753 CG MET A 89 11.885 41.760 5.259 1.00 41.06 AAAB C ATOM 754 SD MET A 89 12.367 42.132 6.960 1.00 43.19 AAAB S ATOM 755 CE MET A 89 12.016 43.879 7.031 1.00 44.90 AAAB C ATOM 756 N GLY A 90 13.700 38.926 1.829 1.00 29.73 AAAB N ATOM 757 CA GLY A 90 14.747 38.095 1.265 1.00 29.00 AAAB C ATOM 758 C GLY A 90 15.404 37.148 2.250 1.00 31.45 AAAB C ATOM 759 O GLY A 90 16.545 36.730 2.044 1.00 31.63 AAAB O ATOM 760 N VAL A 91 14.699 36.819 3.328 1.00 35.12 AAAB N ATOM 761 CA VAL A 91 15.222 35.911 4.348 1.00 37.07 AAAB C ATOM 762 C VAL A 91 14.357 34.656 4.438 1.00 39.63 AAAB C ATOM 763 O VAL A 91 13.126 34.739 4.455 1.00 38.94 AAAB O ATOM 764 CB VAL A 91 15.273 36.589 5.740 1.00 36.51 AAAB C ATOM 765 CG1 VAL A 91 15.772 35.607 6.799 1.00 30.24 AAAB C ATOM 766 CG2 VAL A 91 16.174 37.808 5.689 1.00 33.84 AAAB C ATOM 767 N HIS A 92 15.007 33.496 4.514 1.00 39.92 AAAB N ATOM 768 CA HIS A 92 14.297 32.219 4.590 1.00 39.77 AAAB C ATOM 769 C HIS A 92 14.717 31.316 5.750 1.00 38.51 AAAB C ATOM 770 O HIS A 92 14.258 30.175 5.843 1.00 39.87 AAAB O ATOM 771 CB HIS A 92 14.441 31.440 3.269 1.00 40.78 AAAB C ATOM 772 CG HIS A 92 13.500 31.887 2.190 1.00 39.09 AAAB C ATOM 773 ND1 HIS A 92 12.135 31.705 2.265 1.00 38.32 AAAB N ATOM 774 CD2 HIS A 92 13.730 32.507 1.008 1.00 39.88 AAAB C ATOM 775 CE1 HIS A 92 11.564 32.191 1.178 1.00 36.20 AAAB C ATOM 776 NE2 HIS A 92 12.511 32.685 0.399 1.00 40.24 AAAB N ATOM 777 N ILE A 93 15.505 31.847 6.677 1.00 35.45 AAAB N ATOM 778 CA ILE A 93 15.988 31.058 7.808 1.00 33.48 AAAB C ATOM 779 C ILE A 93 14.982 30.795 8.947 1.00 35.27 AAAB C ATOM 780 O ILE A 93 15.356 30.302 10.015 1.00 36.52 AAAB O ATOM 781 CB ILE A 93 17.299 31.660 8.366 1.00 32.60 AAAB C ATOM 782 CG1 ILE A 93 17.053 33.045 8.968 1.00 33.82 AAAB C ATOM 783 CG2 ILE A 93 18.321 31.789 7.243 1.00 34.52 AAAB C ATOM 784 CD1 ILE A 93 18.270 33.622 9.675 1.00 31.28 AAAB C ATOM 785 N TRP A 94 13.703 31.072 8.702 1.00 36.67 AAAB N ATOM 786 CA TRP A 94 12.665 30.864 9.715 1.00 38.91 AAAB C ATOM 787 C TRP A 94 11.486 30.022 9.227 1.00 39.48 AAAB C ATOM 788 O TRP A 94 10.572 29.713 9.995 1.00 34.31 AAAB O ATOM 789 CB TRP A 94 12.163 32.221 10.237 1.00 45.46 AAAB C ATOM 790 CG TRP A 94 13.183 32.928 11.079 1.00 51.93 AAAB C ATOM 791 CD1 TRP A 94 14.092 33.859 10.664 1.00 53.79 AAAB C ATOM 792 CD2 TRP A 94 13.470 32.677 12.455 1.00 55.96 AAAB C ATOM 793 NE1 TRP A 94 14.936 34.189 11.691 1.00 54.79 AAAB N ATOM 794 CE2 TRP A 94 14.576 33.477 12.803 1.00 56.75 AAAB C ATOM 795 CE3 TRP A 94 12.904 31.841 13.425 1.00 60.84 AAAB C ATOM 796 CZ2 TRP A 94 15.134 33.466 14.084 1.00 62.38 AAAB C ATOM 797 CZ3 TRP A 94 13.459 31.828 14.699 1.00 66.53 AAAB C ATOM 798 CH2 TRP A 94 14.565 32.637 15.017 1.00 65.32 AAAB C ATOM 799 N ASP A 95 11.535 29.616 7.961 1.00 43.80 AAAB N ATOM 800 CA ASP A 95 10.466 28.829 7.350 1.00 44.11 AAAB C ATOM 801 C ASP A 95 10.210 27.495 8.038 1.00 43.21 AAAB C ATOM 802 O ASP A 95 9.085 27.004 8.044 1.00 42.39 AAAB O ATOM 803 CB ASP A 95 10.741 28.620 5.853 1.00 43.33 AAAB C ATOM 804 CG ASP A 95 10.708 29.924 5.065 1.00 46.36 AAAB C ATOM 805 OD1 ASP A 95 11.635 30.738 5.240 1.00 43.27 AAAB O ATOM 806 OD2 ASP A 95 9.753 30.144 4.284 1.00 44.90 AAAB O ATOM 807 N GLN A 96 11.246 26.933 8.651 1.00 46.13 AAAB N ATOM 808 CA GLN A 96 11.132 25.652 9.349 1.00 49.64 AAAB C ATOM 809 C GLN A 96 10.241 25.719 10.595 1.00 48.04 AAAB C ATOM 810 O GLN A 96 9.965 24.692 11.215 1.00 47.01 AAAB O ATOM 811 CB GLN A 96 12.520 25.132 9.731 1.00 54.60 AAAB C ATOM 812 CG GLN A 96 13.202 25.940 10.818 1.00 66.30 AAAB C ATOM 813 CD GLN A 96 14.664 25.583 10.994 1.00 73.00 AAAB C ATOM 814 OE1 GLN A 96 15.542 26.261 10.460 1.00 78.97 AAAB O ATOM 815 NE2 GLN A 96 14.937 24.529 11.757 1.00 73.58 AAAB N ATOM 816 N TRP A 97 9.845 26.930 10.985 1.00 47.14 AAAB N ATOM 817 CA TRP A 97 8.979 27.133 12.145 1.00 44.24 AAAB C ATOM 818 C TRP A 97 7.681 27.809 11.732 1.00 42.98 AAAB C ATOM 819 O TRP A 97 6.888 28.221 12.577 1.00 43.69 AAAB O ATOM 820 CB TRP A 97 9.683 27.981 13.204 1.00 44.47 AAAB C ATOM 821 CG TRP A 97 10.742 27.246 13.943 1.00 44.61 AAAB C ATOM 822 CD1 TRP A 97 10.561 26.216 14.820 1.00 45.80 AAAB C ATOM 823 CD2 TRP A 97 12.154 27.458 13.860 1.00 45.43 AAAB C ATOM 824 NE1 TRP A 97 11.774 25.772 15.286 1.00 46.02 AAAB N ATOM 825 CE2 TRP A 97 12.770 26.517 14.712 1.00 45.73 AAAB C ATOM 826 CE3 TRP A 97 12.959 28.353 13.144 1.00 46.42 AAAB C ATOM 827 CZ2 TRP A 97 14.156 26.442 14.871 1.00 47.17 AAAB C ATOM 828 CZ3 TRP A 97 14.341 28.280 13.300 1.00 47.52 AAAB C ATOM 829 CH2 TRP A 97 14.924 27.330 14.159 1.00 50.20 AAAB C ATOM 830 N LYS A 98 7.471 27.920 10.428 1.00 42.74 AAAB N ATOM 831 CA LYS A 98 6.278 28.549 9.887 1.00 48.17 AAAB C ATOM 832 C LYS A 98 5.026 27.706 10.160 1.00 48.76 AAAB C ATOM 833 O LYS A 98 4.883 26.598 9.640 1.00 50.63 AAAB O ATOM 834 CB LYS A 98 6.460 28.763 8.382 1.00 53.11 AAAB C ATOM 835 CG LYS A 98 5.347 29.537 7.717 1.00 60.94 AAAB C ATOM 836 CD LYS A 98 5.644 29.762 6.247 1.00 68.91 AAAB C ATOM 837 CE LYS A 98 4.597 30.673 5.621 1.00 76.65 AAAB C ATOM 838 NZ LYS A 98 4.842 30.935 4.175 1.00 81.50 AAAB N ATOM 839 N GLN A 99 4.137 28.222 11.003 1.00 48.47 AAAB N ATOM 840 CA GLN A 99 2.897 27.523 11.327 1.00 49.36 AAAB C ATOM 841 C GLN A 99 1.927 27.548 10.144 1.00 50.55 AAAB C ATOM 842 O GLN A 99 2.231 28.111 9.094 1.00 50.08 AAAB O ATOM 843 CB GLN A 99 2.230 28.135 12.563 1.00 49.19 AAAB C ATOM 844 CG GLN A 99 2.860 27.729 13.893 1.00 50.59 AAAB C ATOM 845 CD GLN A 99 2.162 28.343 15.110 1.00 52.25 AAAB C ATOM 846 OE1 GLN A 99 2.573 28.120 16.250 1.00 50.60 AAAB O ATOM 847 NE2 GLN A 99 1.105 29.118 14.871 1.00 51.58 AAAB N ATOM 848 N GLU A 100 0.748 26.962 10.337 1.00 53.37 AAAB N ATOM 849 CA GLU A 100 -0.277 26.894 9.297 1.00 56.19 AAAB C ATOM 850 C GLU A 100 -0.603 28.247 8.684 1.00 55.23 AAAB C ATOM 851 O GLU A 100 -0.748 28.365 7.468 1.00 57.00 AAAB O ATOM 852 CB GLU A 100 -1.558 26.266 9.849 1.00 62.70 AAAB C ATOM 853 CG GLU A 100 -2.127 26.979 11.080 1.00 73.43 AAAB C ATOM 854 CD GLU A 100 -3.550 26.550 11.414 1.00 79.27 AAAB C ATOM 855 OE1 GLU A 100 -3.891 25.364 11.192 1.00 82.51 AAAB O ATOM 856 OE2 GLU A 100 -4.329 27.404 11.899 1.00 79.27 AAAB O ATOM 857 N ASP A 101 -0.720 29.262 9.534 1.00 53.23 AAAB N ATOM 858 CA ASP A 101 -1.036 30.614 9.078 1.00 49.55 AAAB C ATOM 859 C ASP A 101 0.189 31.431 8.659 1.00 44.45 AAAB C ATOM 860 O ASP A 101 0.077 32.617 8.370 1.00 46.72 AAAB O ATOM 861 CB ASP A 101 -1.859 31.368 10.140 1.00 49.89 AAAB C ATOM 862 CG ASP A 101 -1.250 31.290 11.545 1.00 51.79 AAAB C ATOM 863 OD1 ASP A 101 -0.080 30.869 11.694 1.00 52.82 AAAB O ATOM 864 OD2 ASP A 101 -1.955 31.656 12.509 1.00 52.45 AAAB O ATOM 865 N GLY A 102 1.353 30.795 8.623 1.00 41.49 AAAB N ATOM 866 CA GLY A 102 2.561 31.498 8.233 1.00 39.87 AAAB C ATOM 867 C GLY A 102 3.273 32.226 9.358 1.00 39.78 AAAB C ATOM 868 O GLY A 102 4.356 32.778 9.146 1.00 38.37 AAAB O ATOM 869 N THR A 103 2.678 32.231 10.549 1.00 38.69 AAAB N ATOM 870 CA THR A 103 3.267 32.905 11.704 1.00 36.78 AAAB C ATOM 871 C THR A 103 4.019 31.920 12.589 1.00 34.92 AAAB C ATOM 872 O THR A 103 3.970 30.713 12.355 1.00 39.89 AAAB O ATOM 873 CB THR A 103 2.183 33.562 12.569 1.00 37.76 AAAB C ATOM 874 OG1 THR A 103 1.372 32.544 13.171 1.00 41.01 AAAB O ATOM 875 CG2 THR A 103 1.301 34.476 11.728 1.00 38.16 AAAB C ATOM 876 N ILE A 104 4.716 32.435 13.600 1.00 28.21 AAAB N ATOM 877 CA ILE A 104 5.449 31.590 14.544 1.00 20.16 AAAB C ATOM 878 C ILE A 104 4.717 31.594 15.877 1.00 18.10 AAAB C ATOM 879 O ILE A 104 5.336 31.580 16.941 1.00 16.27 AAAB O ATOM 880 CB ILE A 104 6.890 32.084 14.787 1.00 17.65 AAAB C ATOM 881 CG1 ILE A 104 6.886 33.573 15.141 1.00 17.74 AAAB C ATOM 882 CG2 ILE A 104 7.771 31.777 13.583 1.00 18.55 AAAB C ATOM 883 CD1 ILE A 104 8.239 34.111 15.509 1.00 23.14 AAAB C ATOM 884 N GLY A 105 3.392 31.607 15.812 1.00 16.43 AAAB N ATOM 885 CA GLY A 105 2.593 31.627 17.018 1.00 18.26 AAAB C ATOM 886 C GLY A 105 2.591 33.015 17.621 1.00 20.06 AAAB C ATOM 887 O GLY A 105 2.582 34.009 16.904 1.00 27.17 AAAB O ATOM 888 N HIS A 106 2.609 33.088 18.943 1.00 18.35 AAAB N ATOM 889 CA HIS A 106 2.611 34.356 19.651 1.00 15.73 AAAB C ATOM 890 C HIS A 106 4.003 34.655 20.203 1.00 15.48 AAAB C ATOM 891 O HIS A 106 4.153 35.068 21.351 1.00 15.13 AAAB O ATOM 892 CB HIS A 106 1.582 34.307 20.776 1.00 17.56 AAAB C ATOM 893 CG HIS A 106 0.164 34.356 20.294 1.00 21.73 AAAB C ATOM 894 ND1 HIS A 106 -0.914 34.160 21.127 1.00 23.58 AAAB N ATOM 895 CD2 HIS A 106 -0.351 34.620 19.069 1.00 21.61 AAAB C ATOM 896 CE1 HIS A 106 -2.035 34.308 20.442 1.00 20.13 AAAB C ATOM 897 NE2 HIS A 106 -1.720 34.588 19.190 1.00 25.32 AAAB N ATOM 898 N ALA A 107 5.010 34.500 19.353 1.00 12.84 AAAB N ATOM 899 CA ALA A 107 6.395 34.713 19.750 1.00 11.49 AAAB C ATOM 900 C ALA A 107 7.019 35.963 19.141 1.00 14.87 AAAB C ATOM 901 O ALA A 107 6.441 36.605 18.259 1.00 17.98 AAAB O ATOM 902 CB ALA A 107 7.239 33.476 19.380 1.00 9.33 AAAB C ATOM 903 N TYR A 108 8.227 36.266 19.611 1.00 17.81 AAAB N ATOM 904 CA TYR A 108 9.023 37.402 19.161 1.00 19.14 AAAB C ATOM 905 C TYR A 108 8.230 38.678 18.855 1.00 19.91 AAAB C ATOM 906 O TYR A 108 7.575 39.223 19.745 1.00 24.07 AAAB O ATOM 907 CB TYR A 108 9.887 36.987 17.978 1.00 13.45 AAAB C ATOM 908 CG TYR A 108 11.060 36.127 18.365 1.00 14.94 AAAB C ATOM 909 CD1 TYR A 108 12.275 36.704 18.722 1.00 16.45 AAAB C ATOM 910 CD2 TYR A 108 10.970 34.732 18.348 1.00 22.70 AAAB C ATOM 911 CE1 TYR A 108 13.377 35.925 19.052 1.00 19.54 AAAB C ATOM 912 CE2 TYR A 108 12.075 33.932 18.681 1.00 21.64 AAAB C ATOM 913 CZ TYR A 108 13.274 34.540 19.031 1.00 24.10 AAAB C ATOM 914 OH TYR A 108 14.366 33.773 19.372 1.00 26.47 AAAB O ATOM 915 N GLY A 109 8.272 39.141 17.607 1.00 19.38 AAAB N ATOM 916 CA GLY A 109 7.565 40.353 17.230 1.00 17.34 AAAB C ATOM 917 C GLY A 109 6.152 40.470 17.765 1.00 18.65 AAAB C ATOM 918 O GLY A 109 5.715 41.557 18.134 1.00 20.19 AAAB O ATOM 919 N PHE A 110 5.443 39.352 17.865 1.00 18.95 AAAB N ATOM 920 CA PHE A 110 4.077 39.402 18.367 1.00 20.89 AAAB C ATOM 921 C PHE A 110 4.024 40.041 19.753 1.00 21.46 AAAB C ATOM 922 O PHE A 110 3.149 40.872 20.019 1.00 22.72 AAAB O ATOM 923 CB PHE A 110 3.447 38.007 18.399 1.00 18.14 AAAB C ATOM 924 CG PHE A 110 2.016 38.006 18.848 1.00 16.91 AAAB C ATOM 925 CD1 PHE A 110 0.993 38.184 17.934 1.00 14.70 AAAB C ATOM 926 CD2 PHE A 110 1.692 37.843 20.189 1.00 19.20 AAAB C ATOM 927 CE1 PHE A 110 -0.337 38.202 18.349 1.00 18.24 AAAB C ATOM 928 CE2 PHE A 110 0.366 37.859 20.611 1.00 21.17 AAAB C ATOM 929 CZ PHE A 110 -0.650 38.039 19.691 1.00 17.55 AAAB C ATOM 930 N GLN A 111 4.973 39.676 20.617 1.00 21.56 AAAB N ATOM 931 CA GLN A 111 5.047 40.208 21.983 1.00 20.84 AAAB C ATOM 932 C GLN A 111 5.319 41.705 22.015 1.00 17.65 AAAB C ATOM 933 O GLN A 111 4.684 42.442 22.767 1.00 18.98 AAAB O ATOM 934 CB GLN A 111 6.124 39.479 22.800 1.00 17.80 AAAB C ATOM 935 CG GLN A 111 5.737 38.079 23.212 1.00 16.81 AAAB C ATOM 936 CD GLN A 111 4.361 38.031 23.850 1.00 16.53 AAAB C ATOM 937 OE1 GLN A 111 4.032 38.838 24.724 1.00 14.33 AAAB O ATOM 938 NE2 GLN A 111 3.546 37.084 23.412 1.00 17.67 AAAB N ATOM 939 N LEU A 112 6.268 42.142 21.194 1.00 16.39 AAAB N ATOM 940 CA LEU A 112 6.641 43.549 21.115 1.00 11.89 AAAB C ATOM 941 C LEU A 112 5.502 44.417 20.597 1.00 10.63 AAAB C ATOM 942 O LEU A 112 5.425 45.597 20.918 1.00 18.83 AAAB O ATOM 943 CB LEU A 112 7.891 43.726 20.246 1.00 2.00 AAAB C ATOM 944 CG LEU A 112 9.151 43.108 20.854 1.00 2.00 AAAB C ATOM 945 CD1 LEU A 112 10.317 43.180 19.904 1.00 2.00 AAAB C ATOM 946 CD2 LEU A 112 9.481 43.815 22.145 1.00 6.06 AAAB C ATOM 947 N GLY A 113 4.603 43.831 19.824 1.00 11.27 AAAB N ATOM 948 CA GLY A 113 3.496 44.600 19.292 1.00 15.00 AAAB C ATOM 949 C GLY A 113 2.217 44.650 20.113 1.00 18.51 AAAB C ATOM 950 O GLY A 113 1.320 45.433 19.786 1.00 23.10 AAAB O ATOM 951 N LYS A 114 2.110 43.837 21.161 1.00 18.50 AAAB N ATOM 952 CA LYS A 114 0.900 43.823 21.988 1.00 20.19 AAAB C ATOM 953 C LYS A 114 0.714 45.165 22.693 1.00 20.94 AAAB C ATOM 954 O LYS A 114 1.621 45.646 23.368 1.00 15.67 AAAB O ATOM 955 CB LYS A 114 0.978 42.723 23.051 1.00 24.36 AAAB C ATOM 956 CG LYS A 114 1.194 41.317 22.536 1.00 24.36 AAAB C ATOM 957 CD LYS A 114 1.006 40.300 23.655 1.00 26.31 AAAB C ATOM 958 CE LYS A 114 -0.425 40.343 24.173 1.00 33.13 AAAB C ATOM 959 NZ LYS A 114 -0.729 39.248 25.129 1.00 33.51 AAAB N ATOM 960 N LYS A 115 -0.463 45.765 22.546 1.00 22.76 AAAB N ATOM 961 CA LYS A 115 -0.745 47.049 23.188 1.00 27.64 AAAB C ATOM 962 C LYS A 115 -1.177 46.782 24.620 1.00 26.51 AAAB C ATOM 963 O LYS A 115 -2.366 46.782 24.927 1.00 29.27 AAAB O ATOM 964 CB LYS A 115 -1.851 47.799 22.441 1.00 29.13 AAAB C ATOM 965 CG LYS A 115 -1.522 48.139 20.997 1.00 34.83 AAAB C ATOM 966 CD LYS A 115 -2.702 48.815 20.327 1.00 42.56 AAAB C ATOM 967 CE LYS A 115 -2.434 49.046 18.857 1.00 49.04 AAAB C ATOM 968 NZ LYS A 115 -3.600 49.689 18.177 1.00 54.43 AAAB N ATOM 969 N ASN A 116 -0.205 46.587 25.500 1.00 24.63 AAAB N ATOM 970 CA ASN A 116 -0.496 46.277 26.893 1.00 24.56 AAAB C ATOM 971 C ASN A 116 -0.066 47.313 27.942 1.00 24.08 AAAB C ATOM 972 O ASN A 116 -0.287 47.114 29.138 1.00 23.30 AAAB O ATOM 973 CB ASN A 116 0.083 44.902 27.229 1.00 26.65 AAAB C ATOM 974 CG ASN A 116 1.460 44.680 26.614 1.00 29.91 AAAB C ATOM 975 OD1 ASN A 116 2.238 45.620 26.447 1.00 29.82 AAAB O ATOM 976 ND2 ASN A 116 1.753 43.436 26.247 1.00 30.65 AAAB N ATOM 977 N ARG A 117 0.539 48.413 27.511 1.00 21.12 AAAB N ATOM 978 CA ARG A 117 0.967 49.440 28.451 1.00 24.22 AAAB C ATOM 979 C ARG A 117 0.132 50.718 28.367 1.00 24.80 AAAB C ATOM 980 O ARG A 117 -0.038 51.294 27.299 1.00 23.78 AAAB O ATOM 981 CB ARG A 117 2.455 49.740 28.277 1.00 22.53 AAAB C ATOM 982 CG ARG A 117 3.349 48.561 28.623 1.00 24.81 AAAB C ATOM 983 CD ARG A 117 2.979 47.947 29.985 1.00 27.62 AAAB C ATOM 984 NE ARG A 117 3.237 48.829 31.125 1.00 24.97 AAAB N ATOM 985 CZ ARG A 117 4.450 49.082 31.615 1.00 26.38 AAAB C ATOM 986 NH1 ARG A 117 5.526 48.525 31.068 1.00 20.89 AAAB N ATOM 987 NH2 ARG A 117 4.589 49.891 32.661 1.00 23.25 AAAB N ATOM 988 N SER A 118 -0.397 51.149 29.503 1.00 26.91 AAAB N ATOM 989 CA SER A 118 -1.225 52.338 29.560 1.00 30.80 AAAB C ATOM 990 C SER A 118 -0.358 53.584 29.568 1.00 32.16 AAAB C ATOM 991 O SER A 118 0.242 53.918 30.589 1.00 30.85 AAAB O ATOM 992 CB SER A 118 -2.088 52.320 30.826 1.00 35.69 AAAB C ATOM 993 OG SER A 118 -2.704 51.056 31.025 1.00 42.34 AAAB O ATOM 994 N LEU A 119 -0.278 54.260 28.426 1.00 35.55 AAAB N ATOM 995 CA LEU A 119 0.498 55.494 28.315 1.00 36.45 AAAB C ATOM 996 C LEU A 119 -0.395 56.625 27.816 1.00 37.73 AAAB C ATOM 997 O LEU A 119 -0.914 56.578 26.699 1.00 39.36 AAAB O ATOM 998 CB LEU A 119 1.686 55.317 27.371 1.00 34.11 AAAB C ATOM 999 CG LEU A 119 2.612 56.531 27.287 1.00 31.74 AAAB C ATOM 1000 CD1 LEU A 119 3.212 56.833 28.648 1.00 31.38 AAAB C ATOM 1001 CD2 LEU A 119 3.702 56.273 26.268 1.00 32.23 AAAB C ATOM 1002 N ASN A 120 -0.616 57.614 28.678 1.00 41.83 AAAB N ATOM 1003 CA ASN A 120 -1.438 58.779 28.358 1.00 43.97 AAAB C ATOM 1004 C ASN A 120 -2.845 58.439 27.891 1.00 47.17 AAAB C ATOM 1005 O ASN A 120 -3.304 58.922 26.855 1.00 46.38 AAAB O ATOM 1006 CB ASN A 120 -0.739 59.666 27.326 1.00 42.88 AAAB C ATOM 1007 CG ASN A 120 0.465 60.382 27.896 1.00 45.03 AAAB C ATOM 1008 OD1 ASN A 120 1.502 60.491 27.246 1.00 49.39 AAAB O ATOM 1009 ND2 ASN A 120 0.346 60.852 29.129 1.00 45.26 AAAB N ATOM 1010 N GLY A 121 -3.520 57.589 28.656 1.00 49.22 AAAB N ATOM 1011 CA GLY A 121 -4.878 57.214 28.318 1.00 49.74 AAAB C ATOM 1012 C GLY A 121 -5.034 56.232 27.177 1.00 50.10 AAAB C ATOM 1013 O GLY A 121 -6.162 55.917 26.801 1.00 53.80 AAAB O ATOM 1014 N GLU A 122 -3.933 55.746 26.615 1.00 50.11 AAAB N ATOM 1015 CA GLU A 122 -4.036 54.781 25.528 1.00 50.16 AAAB C ATOM 1016 C GLU A 122 -3.067 53.618 25.690 1.00 47.05 AAAB C ATOM 1017 O GLU A 122 -1.976 53.777 26.236 1.00 47.06 AAAB O ATOM 1018 CB GLU A 122 -3.841 55.455 24.166 1.00 52.90 AAAB C ATOM 1019 CG GLU A 122 -2.424 55.909 23.849 1.00 57.54 AAAB C ATOM 1020 CD GLU A 122 -2.277 56.387 22.410 1.00 62.54 AAAB C ATOM 1021 OE1 GLU A 122 -3.314 56.622 21.745 1.00 63.87 AAAB O ATOM 1022 OE2 GLU A 122 -1.123 56.526 21.940 1.00 63.14 AAAB O ATOM 1023 N LYS A 123 -3.493 52.445 25.231 1.00 46.48 AAAB N ATOM 1024 CA LYS A 123 -2.687 51.231 25.301 1.00 42.76 AAAB C ATOM 1025 C LYS A 123 -1.584 51.334 24.246 1.00 38.73 AAAB C ATOM 1026 O LYS A 123 -1.852 51.549 23.063 1.00 38.90 AAAB O ATOM 1027 CB LYS A 123 -3.562 50.004 25.027 1.00 49.22 AAAB C ATOM 1028 CG LYS A 123 -4.955 50.081 25.636 1.00 54.29 AAAB C ATOM 1029 CD LYS A 123 -5.825 48.897 25.217 1.00 63.89 AAAB C ATOM 1030 CE LYS A 123 -7.273 49.086 25.675 1.00 68.23 AAAB C ATOM 1031 NZ LYS A 123 -8.135 47.907 25.373 1.00 70.25 AAAB N ATOM 1032 N VAL A 124 -0.349 51.143 24.682 1.00 32.76 AAAB N ATOM 1033 CA VAL A 124 0.816 51.231 23.822 1.00 28.89 AAAB C ATOM 1034 C VAL A 124 1.621 49.927 23.961 1.00 26.98 AAAB C ATOM 1035 O VAL A 124 1.479 49.209 24.951 1.00 27.64 AAAB O ATOM 1036 CB VAL A 124 1.651 52.498 24.227 1.00 29.62 AAAB C ATOM 1037 CG1 VAL A 124 3.094 52.150 24.579 1.00 31.25 AAAB C ATOM 1038 CG2 VAL A 124 1.601 53.538 23.125 1.00 27.35 AAAB C ATOM 1039 N ASP A 125 2.420 49.588 22.956 1.00 25.57 AAAB N ATOM 1040 CA ASP A 125 3.210 48.368 23.048 1.00 23.21 AAAB C ATOM 1041 C ASP A 125 4.558 48.595 23.718 1.00 23.83 AAAB C ATOM 1042 O ASP A 125 4.969 49.739 23.930 1.00 31.02 AAAB O ATOM 1043 CB ASP A 125 3.360 47.664 21.687 1.00 21.19 AAAB C ATOM 1044 CG ASP A 125 4.173 48.459 20.665 1.00 17.80 AAAB C ATOM 1045 OD1 ASP A 125 5.233 49.013 21.004 1.00 12.95 AAAB O ATOM 1046 OD2 ASP A 125 3.770 48.463 19.484 1.00 17.51 AAAB O ATOM 1047 N GLN A 126 5.269 47.502 23.979 1.00 21.35 AAAB N ATOM 1048 CA GLN A 126 6.571 47.529 24.643 1.00 17.78 AAAB C ATOM 1049 C GLN A 126 7.624 48.429 24.035 1.00 14.44 AAAB C ATOM 1050 O GLN A 126 8.408 49.027 24.758 1.00 17.00 AAAB O ATOM 1051 CB GLN A 126 7.153 46.117 24.751 1.00 18.58 AAAB C ATOM 1052 CG GLN A 126 6.504 45.235 25.800 1.00 15.43 AAAB C ATOM 1053 CD GLN A 126 7.242 43.926 25.961 1.00 16.46 AAAB C ATOM 1054 OE1 GLN A 126 8.436 43.920 26.235 1.00 17.22 AAAB O ATOM 1055 NE2 GLN A 126 6.547 42.813 25.763 1.00 14.71 AAAB N ATOM 1056 N VAL A 127 7.689 48.469 22.712 1.00 19.34 AAAB N ATOM 1057 CA VAL A 127 8.677 49.296 22.019 1.00 21.44 AAAB C ATOM 1058 C VAL A 127 8.335 50.779 22.170 1.00 22.83 AAAB C ATOM 1059 O VAL A 127 9.191 51.594 22.522 1.00 24.46 AAAB O ATOM 1060 CB VAL A 127 8.760 48.914 20.516 1.00 22.55 AAAB C ATOM 1061 CG1 VAL A 127 9.796 49.770 19.788 1.00 19.83 AAAB C ATOM 1062 CG2 VAL A 127 9.117 47.445 20.390 1.00 19.33 AAAB C ATOM 1063 N ASP A 128 7.067 51.112 21.952 1.00 21.81 AAAB N ATOM 1064 CA ASP A 128 6.618 52.489 22.067 1.00 21.93 AAAB C ATOM 1065 C ASP A 128 6.852 53.019 23.469 1.00 23.55 AAAB C ATOM 1066 O ASP A 128 7.532 54.032 23.653 1.00 24.87 AAAB O ATOM 1067 CB ASP A 128 5.142 52.605 21.692 1.00 20.24 AAAB C ATOM 1068 CG ASP A 128 4.903 52.452 20.197 1.00 20.79 AAAB C ATOM 1069 OD1 ASP A 128 5.817 52.733 19.391 1.00 18.13 AAAB O ATOM 1070 OD2 ASP A 128 3.785 52.060 19.824 1.00 25.37 AAAB O ATOM 1071 N TYR A 129 6.325 52.298 24.455 1.00 22.44 AAAB N ATOM 1072 CA TYR A 129 6.466 52.675 25.856 1.00 18.17 AAAB C ATOM 1073 C TYR A 129 7.927 52.944 26.200 1.00 17.76 AAAB C ATOM 1074 O TYR A 129 8.246 53.957 26.826 1.00 22.51 AAAB O ATOM 1075 CB TYR A 129 5.908 51.566 26.757 1.00 17.45 AAAB C ATOM 1076 CG TYR A 129 5.829 51.955 28.211 1.00 16.29 AAAB C ATOM 1077 CD1 TYR A 129 4.755 52.698 28.697 1.00 14.51 AAAB C ATOM 1078 CD2 TYR A 129 6.846 51.613 29.097 1.00 16.51 AAAB C ATOM 1079 CE1 TYR A 129 4.699 53.097 30.025 1.00 12.04 AAAB C ATOM 1080 CE2 TYR A 129 6.799 52.006 30.425 1.00 16.02 AAAB C ATOM 1081 CZ TYR A 129 5.723 52.750 30.882 1.00 11.77 AAAB C ATOM 1082 OH TYR A 129 5.680 53.143 32.194 1.00 15.65 AAAB O ATOM 1083 N LEU A 130 8.814 52.057 25.762 1.00 13.71 AAAB N ATOM 1084 CA LEU A 130 10.237 52.208 26.033 1.00 11.11 AAAB C ATOM 1085 C LEU A 130 10.794 53.502 25.461 1.00 10.90 AAAB C ATOM 1086 O LEU A 130 11.413 54.289 26.186 1.00 7.15 AAAB O ATOM 1087 CB LEU A 130 11.022 51.032 25.447 1.00 8.60 AAAB C ATOM 1088 CG LEU A 130 12.549 51.180 25.519 1.00 8.48 AAAB C ATOM 1089 CD1 LEU A 130 13.032 50.999 26.951 1.00 2.00 AAAB C ATOM 1090 CD2 LEU A 130 13.227 50.195 24.570 1.00 8.70 AAAB C ATOM 1091 N LEU A 131 10.605 53.694 24.154 1.00 14.57 AAAB N ATOM 1092 CA LEU A 131 11.104 54.883 23.459 1.00 13.44 AAAB C ATOM 1093 C LEU A 131 10.668 56.155 24.179 1.00 14.04 AAAB C ATOM 1094 O LEU A 131 11.487 57.026 24.470 1.00 16.50 AAAB O ATOM 1095 CB LEU A 131 10.630 54.901 22.001 1.00 14.04 AAAB C ATOM 1096 CG LEU A 131 11.287 53.935 21.002 1.00 10.43 AAAB C ATOM 1097 CD1 LEU A 131 10.575 54.003 19.658 1.00 6.31 AAAB C ATOM 1098 CD2 LEU A 131 12.762 54.263 20.832 1.00 3.00 AAAB C ATOM 1099 N HIS A 132 9.385 56.231 24.513 1.00 11.85 AAAB N ATOM 1100 CA HIS A 132 8.847 57.379 25.225 1.00 14.15 AAAB C ATOM 1101 C HIS A 132 9.505 57.561 26.592 1.00 19.47 AAAB C ATOM 1102 O HIS A 132 9.926 58.667 26.935 1.00 23.79 AAAB O ATOM 1103 CB HIS A 132 7.337 57.240 25.404 1.00 15.14 AAAB C ATOM 1104 CG HIS A 132 6.743 58.273 26.309 1.00 28.25 AAAB C ATOM 1105 ND1 HIS A 132 6.607 58.084 27.669 1.00 32.80 AAAB N ATOM 1106 CD2 HIS A 132 6.257 59.510 26.052 1.00 28.31 AAAB C ATOM 1107 CE1 HIS A 132 6.064 59.161 28.209 1.00 32.73 AAAB C ATOM 1108 NE2 HIS A 132 5.842 60.040 27.249 1.00 27.83 AAAB N ATOM 1109 N GLN A 133 9.568 56.485 27.377 1.00 18.93 AAAB N ATOM 1110 CA GLN A 133 10.164 56.524 28.713 1.00 17.45 AAAB C ATOM 1111 C GLN A 133 11.667 56.778 28.710 1.00 15.90 AAAB C ATOM 1112 O GLN A 133 12.224 57.173 29.730 1.00 19.81 AAAB O ATOM 1113 CB GLN A 133 9.877 55.229 29.478 1.00 24.49 AAAB C ATOM 1114 CG GLN A 133 8.419 55.007 29.811 1.00 25.69 AAAB C ATOM 1115 CD GLN A 133 7.924 55.940 30.885 1.00 27.03 AAAB C ATOM 1116 OE1 GLN A 133 7.043 56.767 30.645 1.00 31.13 AAAB O ATOM 1117 NE2 GLN A 133 8.488 55.821 32.078 1.00 26.90 AAAB N ATOM 1118 N LEU A 134 12.341 56.496 27.604 1.00 13.22 AAAB N ATOM 1119 CA LEU A 134 13.778 56.744 27.541 1.00 16.45 AAAB C ATOM 1120 C LEU A 134 14.069 58.244 27.439 1.00 21.89 AAAB C ATOM 1121 O LEU A 134 15.147 58.708 27.821 1.00 19.31 AAAB O ATOM 1122 CB LEU A 134 14.410 56.011 26.353 1.00 17.59 AAAB C ATOM 1123 CG LEU A 134 14.712 54.514 26.490 1.00 18.37 AAAB C ATOM 1124 CD1 LEU A 134 15.475 54.041 25.260 1.00 13.11 AAAB C ATOM 1125 CD2 LEU A 134 15.552 54.257 27.740 1.00 17.60 AAAB C ATOM 1126 N LYS A 135 13.121 58.998 26.885 1.00 20.73 AAAB N ATOM 1127 CA LYS A 135 13.293 60.436 26.746 1.00 18.01 AAAB C ATOM 1128 C LYS A 135 12.677 61.138 27.935 1.00 14.61 AAAB C ATOM 1129 O LYS A 135 13.348 61.877 28.647 1.00 14.41 AAAB O ATOM 1130 CB LYS A 135 12.630 60.948 25.462 1.00 20.62 AAAB C ATOM 1131 CG LYS A 135 13.151 60.315 24.185 0.00 21.46 AAAB C ATOM 1132 CD LYS A 135 12.446 60.885 22.964 0.00 22.58 AAAB C ATOM 1133 CE LYS A 135 13.005 60.295 21.683 0.00 23.54 AAAB C ATOM 1134 NZ LYS A 135 12.431 60.934 20.469 0.00 24.37 AAAB N ATOM 1135 N ASN A 136 11.418 60.817 28.198 1.00 16.08 AAAB N ATOM 1136 CA ASN A 136 10.652 61.432 29.272 1.00 15.82 AAAB C ATOM 1137 C ASN A 136 10.793 60.872 30.672 1.00 16.82 AAAB C ATOM 1138 O ASN A 136 10.070 61.295 31.571 1.00 19.30 AAAB O ATOM 1139 CB ASN A 136 9.177 61.420 28.901 1.00 19.14 AAAB C ATOM 1140 CG ASN A 136 8.917 62.082 27.565 1.00 29.84 AAAB C ATOM 1141 OD1 ASN A 136 8.369 61.456 26.654 1.00 33.87 AAAB O ATOM 1142 ND2 ASN A 136 9.326 63.345 27.430 1.00 25.84 AAAB N ATOM 1143 N ASN A 137 11.725 59.953 30.885 1.00 15.52 AAAB N ATOM 1144 CA ASN A 137 11.899 59.352 32.205 1.00 14.86 AAAB C ATOM 1145 C ASN A 137 13.161 58.513 32.178 1.00 16.95 AAAB C ATOM 1146 O ASN A 137 13.156 57.338 32.551 1.00 20.50 AAAB O ATOM 1147 CB ASN A 137 10.688 58.464 32.518 1.00 16.50 AAAB C ATOM 1148 CG ASN A 137 10.632 58.011 33.968 1.00 20.78 AAAB C ATOM 1149 OD1 ASN A 137 9.660 57.373 34.374 1.00 26.57 AAAB O ATOM 1150 ND2 ASN A 137 11.663 58.319 34.753 1.00 25.16 AAAB N ATOM 1151 N PRO A 138 14.278 59.124 31.783 1.00 15.50 AAAB N ATOM 1152 CA PRO A 138 15.563 58.434 31.701 1.00 18.33 AAAB C ATOM 1153 C PRO A 138 16.006 57.702 32.976 1.00 17.74 AAAB C ATOM 1154 O PRO A 138 16.379 56.530 32.921 1.00 21.44 AAAB O ATOM 1155 CB PRO A 138 16.519 59.566 31.314 1.00 15.97 AAAB C ATOM 1156 CG PRO A 138 15.910 60.741 31.974 1.00 14.57 AAAB C ATOM 1157 CD PRO A 138 14.461 60.572 31.623 1.00 12.43 AAAB C ATOM 1158 N SER A 139 15.879 58.364 34.120 1.00 21.42 AAAB N ATOM 1159 CA SER A 139 16.296 57.810 35.412 1.00 21.16 AAAB C ATOM 1160 C SER A 139 15.638 56.494 35.826 1.00 18.93 AAAB C ATOM 1161 O SER A 139 16.035 55.900 36.831 1.00 21.98 AAAB O ATOM 1162 CB SER A 139 16.053 58.843 36.511 1.00 10.88 AAAB C ATOM 1163 OG SER A 139 14.676 59.180 36.559 1.00 18.91 AAAB O ATOM 1164 N SER A 140 14.622 56.061 35.088 1.00 17.42 AAAB N ATOM 1165 CA SER A 140 13.918 54.832 35.430 1.00 15.46 AAAB C ATOM 1166 C SER A 140 14.794 53.590 35.466 1.00 15.27 AAAB C ATOM 1167 O SER A 140 15.667 53.399 34.612 1.00 14.70 AAAB O ATOM 1168 CB SER A 140 12.746 54.609 34.480 1.00 16.59 AAAB C ATOM 1169 OG SER A 140 12.026 53.444 34.839 1.00 13.68 AAAB O ATOM 1170 N ARG A 141 14.537 52.741 36.456 1.00 17.07 AAAB N ATOM 1171 CA ARG A 141 15.269 51.485 36.618 1.00 19.10 AAAB C ATOM 1172 C ARG A 141 14.461 50.329 36.027 1.00 17.02 AAAB C ATOM 1173 O ARG A 141 14.797 49.165 36.242 1.00 19.10 AAAB O ATOM 1174 CB ARG A 141 15.517 51.195 38.102 1.00 18.77 AAAB C ATOM 1175 CG ARG A 141 16.310 52.253 38.838 1.00 16.62 AAAB C ATOM 1176 CD ARG A 141 16.426 51.898 40.304 1.00 17.07 AAAB C ATOM 1177 NE ARG A 141 17.108 52.935 41.070 1.00 23.70 AAAB N ATOM 1178 CZ ARG A 141 16.503 53.772 41.909 1.00 24.64 AAAB C ATOM 1179 NH1 ARG A 141 15.195 53.698 42.098 1.00 24.18 AAAB N ATOM 1180 NH2 ARG A 141 17.210 54.685 42.561 1.00 26.87 AAAB N ATOM 1181 N ARG A 142 13.396 50.663 35.298 1.00 15.84 AAAB N ATOM 1182 CA ARG A 142 12.510 49.678 34.692 1.00 12.13 AAAB C ATOM 1183 C ARG A 142 12.445 49.683 33.155 1.00 12.67 AAAB C ATOM 1184 O ARG A 142 11.396 49.361 32.585 1.00 14.28 AAAB O ATOM 1185 CB ARG A 142 11.095 49.879 35.220 1.00 10.04 AAAB C ATOM 1186 CG ARG A 142 10.994 50.044 36.714 1.00 18.50 AAAB C ATOM 1187 CD ARG A 142 9.542 50.232 37.140 1.00 18.56 AAAB C ATOM 1188 NE ARG A 142 9.456 50.503 38.572 1.00 31.68 AAAB N ATOM 1189 CZ ARG A 142 8.359 50.910 39.201 1.00 30.27 AAAB C ATOM 1190 NH1 ARG A 142 7.232 51.093 38.530 1.00 30.72 AAAB N ATOM 1191 NH2 ARG A 142 8.394 51.137 40.505 1.00 30.35 AAAB N ATOM 1192 N HIS A 143 13.524 50.066 32.477 1.00 8.42 AAAB N ATOM 1193 CA HIS A 143 13.519 50.071 31.008 1.00 10.05 AAAB C ATOM 1194 C HIS A 143 13.761 48.631 30.551 1.00 9.66 AAAB C ATOM 1195 O HIS A 143 14.884 48.257 30.169 1.00 6.07 AAAB O ATOM 1196 CB HIS A 143 14.609 50.996 30.447 1.00 10.95 AAAB C ATOM 1197 CG HIS A 143 14.455 52.434 30.834 1.00 7.70 AAAB C ATOM 1198 ND1 HIS A 143 13.263 53.117 30.716 1.00 2.00 AAAB N ATOM 1199 CD2 HIS A 143 15.351 53.326 31.320 1.00 6.46 AAAB C ATOM 1200 CE1 HIS A 143 13.433 54.365 31.112 1.00 3.47 AAAB C ATOM 1201 NE2 HIS A 143 14.692 54.516 31.483 1.00 3.72 AAAB N ATOM 1202 N ILE A 144 12.693 47.840 30.551 1.00 12.18 AAAB N ATOM 1203 CA ILE A 144 12.780 46.421 30.216 1.00 11.94 AAAB C ATOM 1204 C ILE A 144 11.809 45.939 29.149 1.00 9.93 AAAB C ATOM 1205 O ILE A 144 10.608 46.233 29.227 1.00 11.35 AAAB O ATOM 1206 CB ILE A 144 12.487 45.567 31.491 1.00 8.50 AAAB C ATOM 1207 CG1 ILE A 144 13.508 45.864 32.588 1.00 2.00 AAAB C ATOM 1208 CG2 ILE A 144 12.438 44.078 31.154 1.00 11.83 AAAB C ATOM 1209 CD1 ILE A 144 13.122 45.323 33.928 1.00 2.15 AAAB C ATOM 1210 N THR A 145 12.321 45.177 28.180 1.00 8.70 AAAB N ATOM 1211 CA THR A 145 11.484 44.567 27.133 1.00 6.85 AAAB C ATOM 1212 C THR A 145 11.529 43.065 27.429 1.00 10.83 AAAB C ATOM 1213 O THR A 145 12.598 42.505 27.732 1.00 9.29 AAAB O ATOM 1214 CB THR A 145 11.967 44.877 25.687 1.00 7.43 AAAB C ATOM 1215 OG1 THR A 145 13.387 44.695 25.578 1.00 5.77 AAAB O ATOM 1216 CG2 THR A 145 11.609 46.302 25.306 1.00 11.16 AAAB C ATOM 1217 N MET A 146 10.367 42.425 27.393 1.00 9.27 AAAB N ATOM 1218 CA MET A 146 10.262 41.019 27.717 1.00 7.78 AAAB C ATOM 1219 C MET A 146 9.547 40.192 26.669 1.00 11.98 AAAB C ATOM 1220 O MET A 146 8.353 40.391 26.414 1.00 10.43 AAAB O ATOM 1221 CB MET A 146 9.523 40.890 29.054 1.00 11.68 AAAB C ATOM 1222 CG MET A 146 9.387 39.493 29.614 1.00 2.00 AAAB C ATOM 1223 SD MET A 146 10.973 38.729 29.772 1.00 11.54 AAAB S ATOM 1224 CE MET A 146 11.824 39.821 30.874 1.00 8.13 AAAB C ATOM 1225 N LEU A 147 10.279 39.258 26.071 1.00 9.41 AAAB N ATOM 1226 CA LEU A 147 9.695 38.355 25.087 1.00 11.78 AAAB C ATOM 1227 C LEU A 147 9.147 37.101 25.777 1.00 10.97 AAAB C ATOM 1228 O LEU A 147 8.155 36.529 25.330 1.00 12.58 AAAB O ATOM 1229 CB LEU A 147 10.715 37.977 24.011 1.00 12.58 AAAB C ATOM 1230 CG LEU A 147 11.060 39.070 22.990 1.00 15.22 AAAB C ATOM 1231 CD1 LEU A 147 12.136 38.572 22.053 1.00 10.55 AAAB C ATOM 1232 CD2 LEU A 147 9.817 39.476 22.202 1.00 13.25 AAAB C ATOM 1233 N TRP A 148 9.754 36.716 26.899 1.00 12.34 AAAB N ATOM 1234 CA TRP A 148 9.326 35.535 27.652 1.00 11.47 AAAB C ATOM 1235 C TRP A 148 8.014 35.757 28.410 1.00 11.90 AAAB C ATOM 1236 O TRP A 148 8.010 35.925 29.622 1.00 13.01 AAAB O ATOM 1237 CB TRP A 148 10.434 35.089 28.627 1.00 15.94 AAAB C ATOM 1238 CG TRP A 148 10.252 33.683 29.185 1.00 25.87 AAAB C ATOM 1239 CD1 TRP A 148 9.511 33.320 30.276 1.00 26.73 AAAB C ATOM 1240 CD2 TRP A 148 10.786 32.462 28.643 1.00 30.73 AAAB C ATOM 1241 NE1 TRP A 148 9.542 31.956 30.441 1.00 27.27 AAAB N ATOM 1242 CE2 TRP A 148 10.314 31.402 29.454 1.00 29.37 AAAB C ATOM 1243 CE3 TRP A 148 11.612 32.158 27.550 1.00 36.54 AAAB C ATOM 1244 CZ2 TRP A 148 10.640 30.063 29.203 1.00 29.43 AAAB C ATOM 1245 CZ3 TRP A 148 11.937 30.819 27.303 1.00 33.61 AAAB C ATOM 1246 CH2 TRP A 148 11.449 29.793 28.127 1.00 31.73 AAAB C ATOM 1247 N ASN A 149 6.898 35.777 27.693 1.00 16.84 AAAB N ATOM 1248 CA ASN A 149 5.593 35.965 28.320 1.00 18.39 AAAB C ATOM 1249 C ASN A 149 5.103 34.609 28.828 1.00 21.74 AAAB C ATOM 1250 O ASN A 149 4.675 33.756 28.047 1.00 23.16 AAAB O ATOM 1251 CB ASN A 149 4.598 36.546 27.320 1.00 19.29 AAAB C ATOM 1252 CG ASN A 149 3.313 37.004 27.979 1.00 22.60 AAAB C ATOM 1253 OD1 ASN A 149 2.691 36.264 28.748 1.00 25.01 AAAB O ATOM 1254 ND2 ASN A 149 2.908 38.229 27.684 1.00 19.59 AAAB N ATOM 1255 N PRO A 150 5.097 34.416 30.155 1.00 24.59 AAAB N ATOM 1256 CA PRO A 150 4.662 33.155 30.759 1.00 23.88 AAAB C ATOM 1257 C PRO A 150 3.237 32.709 30.432 1.00 24.18 AAAB C ATOM 1258 O PRO A 150 2.968 31.512 30.352 1.00 26.75 AAAB O ATOM 1259 CB PRO A 150 4.868 33.409 32.252 1.00 22.79 AAAB C ATOM 1260 CG PRO A 150 4.578 34.865 32.379 1.00 27.73 AAAB C ATOM 1261 CD PRO A 150 5.335 35.435 31.195 1.00 28.62 AAAB C ATOM 1262 N ASP A 151 2.336 33.660 30.219 1.00 24.38 AAAB N ATOM 1263 CA ASP A 151 0.946 33.338 29.903 1.00 23.12 AAAB C ATOM 1264 C ASP A 151 0.741 32.798 28.501 1.00 23.58 AAAB C ATOM 1265 O ASP A 151 -0.362 32.360 28.178 1.00 25.77 AAAB O ATOM 1266 CB ASP A 151 0.050 34.571 30.054 1.00 27.34 AAAB C ATOM 1267 CG ASP A 151 -0.264 34.899 31.490 1.00 31.38 AAAB C ATOM 1268 OD1 ASP A 151 -0.208 33.984 32.337 1.00 35.20 AAAB O ATOM 1269 OD2 ASP A 151 -0.582 36.073 31.773 1.00 30.58 AAAB O ATOM 1270 N GLU A 152 1.759 32.888 27.646 1.00 21.69 AAAB N ATOM 1271 CA GLU A 152 1.608 32.421 26.271 1.00 22.02 AAAB C ATOM 1272 C GLU A 152 2.733 31.551 25.731 1.00 20.65 AAAB C ATOM 1273 O GLU A 152 2.803 31.325 24.524 1.00 24.37 AAAB O ATOM 1274 CB GLU A 152 1.378 33.609 25.322 1.00 22.94 AAAB C ATOM 1275 CG GLU A 152 0.110 34.399 25.607 1.00 21.65 AAAB C ATOM 1276 CD GLU A 152 -0.166 35.484 24.582 1.00 29.60 AAAB C ATOM 1277 OE1 GLU A 152 0.674 36.397 24.412 1.00 24.44 AAAB O ATOM 1278 OE2 GLU A 152 -1.240 35.428 23.947 1.00 35.70 AAAB O ATOM 1279 N LEU A 153 3.580 31.022 26.609 1.00 20.74 AAAB N ATOM 1280 CA LEU A 153 4.695 30.177 26.175 1.00 21.91 AAAB C ATOM 1281 C LEU A 153 4.238 29.008 25.297 1.00 24.03 AAAB C ATOM 1282 O LEU A 153 4.952 28.585 24.392 1.00 23.58 AAAB O ATOM 1283 CB LEU A 153 5.476 29.640 27.376 1.00 17.10 AAAB C ATOM 1284 CG LEU A 153 6.337 30.623 28.166 1.00 17.57 AAAB C ATOM 1285 CD1 LEU A 153 6.819 29.966 29.444 1.00 15.40 AAAB C ATOM 1286 CD2 LEU A 153 7.509 31.102 27.329 1.00 16.57 AAAB C ATOM 1287 N ASP A 154 3.041 28.500 25.565 1.00 23.62 AAAB N ATOM 1288 CA ASP A 154 2.503 27.391 24.794 1.00 26.75 AAAB C ATOM 1289 C ASP A 154 2.091 27.802 23.400 1.00 28.05 AAAB C ATOM 1290 O ASP A 154 2.081 26.979 22.484 1.00 33.23 AAAB O ATOM 1291 CB ASP A 154 1.284 26.790 25.490 1.00 27.01 AAAB C ATOM 1292 CG ASP A 154 1.645 26.027 26.743 1.00 27.82 AAAB C ATOM 1293 OD1 ASP A 154 2.806 25.562 26.852 1.00 18.52 AAAB O ATOM 1294 OD2 ASP A 154 0.755 25.884 27.612 1.00 26.87 AAAB O ATOM 1295 N ALA A 155 1.709 29.064 23.246 1.00 23.19 AAAB N ATOM 1296 CA ALA A 155 1.261 29.561 21.954 1.00 17.79 AAAB C ATOM 1297 C ALA A 155 2.411 30.022 21.074 1.00 17.61 AAAB C ATOM 1298 O ALA A 155 2.185 30.658 20.052 1.00 19.01 AAAB O ATOM 1299 CB ALA A 155 0.253 30.687 22.147 1.00 14.91 AAAB C ATOM 1300 N MET A 156 3.636 29.673 21.441 1.00 17.88 AAAB N ATOM 1301 CA MET A 156 4.793 30.085 20.663 1.00 21.51 AAAB C ATOM 1302 C MET A 156 5.414 28.922 19.892 1.00 24.48 AAAB C ATOM 1303 O MET A 156 5.892 27.958 20.494 1.00 23.80 AAAB O ATOM 1304 CB MET A 156 5.848 30.705 21.585 1.00 22.81 AAAB C ATOM 1305 CG MET A 156 5.393 31.942 22.349 1.00 14.08 AAAB C ATOM 1306 SD MET A 156 6.700 32.597 23.407 1.00 18.52 AAAB S ATOM 1307 CE MET A 156 5.706 33.615 24.542 1.00 16.39 AAAB C ATOM 1308 N ALA A 157 5.471 29.050 18.566 1.00 24.85 AAAB N ATOM 1309 CA ALA A 157 6.049 28.021 17.704 1.00 24.82 AAAB C ATOM 1310 C ALA A 157 7.511 27.776 18.072 1.00 26.16 AAAB C ATOM 1311 O ALA A 157 8.127 26.810 17.617 1.00 26.88 AAAB O ATOM 1312 CB ALA A 157 5.932 28.426 16.249 1.00 23.59 AAAB C ATOM 1313 N LEU A 158 8.069 28.678 18.871 1.00 27.57 AAAB N ATOM 1314 CA LEU A 158 9.444 28.573 19.345 1.00 31.00 AAAB C ATOM 1315 C LEU A 158 9.687 29.666 20.382 1.00 26.65 AAAB C ATOM 1316 O LEU A 158 9.149 30.763 20.267 1.00 24.51 AAAB O ATOM 1317 CB LEU A 158 10.458 28.628 18.181 1.00 32.89 AAAB C ATOM 1318 CG LEU A 158 10.644 29.753 17.146 1.00 33.40 AAAB C ATOM 1319 CD1 LEU A 158 9.375 30.548 16.922 1.00 32.82 AAAB C ATOM 1320 CD2 LEU A 158 11.768 30.657 17.584 1.00 36.52 AAAB C ATOM 1321 N THR A 159 10.397 29.312 21.448 1.00 28.61 AAAB N ATOM 1322 CA THR A 159 10.719 30.241 22.523 1.00 29.27 AAAB C ATOM 1323 C THR A 159 12.020 30.949 22.162 1.00 29.18 AAAB C ATOM 1324 O THR A 159 12.903 30.360 21.537 1.00 30.57 AAAB O ATOM 1325 CB THR A 159 10.843 29.509 23.889 1.00 30.97 AAAB C ATOM 1326 OG1 THR A 159 11.730 28.388 23.775 1.00 33.11 AAAB O ATOM 1327 CG2 THR A 159 9.475 29.020 24.353 1.00 27.57 AAAB C ATOM 1328 N PRO A 160 12.146 32.230 22.534 1.00 28.42 AAAB N ATOM 1329 CA PRO A 160 13.341 33.022 22.236 1.00 25.96 AAAB C ATOM 1330 C PRO A 160 14.589 32.739 23.063 1.00 23.16 AAAB C ATOM 1331 O PRO A 160 14.507 32.458 24.258 1.00 21.79 AAAB O ATOM 1332 CB PRO A 160 12.865 34.459 22.476 1.00 29.30 AAAB C ATOM 1333 CG PRO A 160 11.365 34.370 22.483 1.00 30.35 AAAB C ATOM 1334 CD PRO A 160 11.121 33.071 23.165 1.00 28.61 AAAB C ATOM 1335 N CYS A 161 15.742 32.820 22.406 1.00 19.96 AAAB N ATOM 1336 CA CYS A 161 17.025 32.650 23.073 1.00 20.85 AAAB C ATOM 1337 C CYS A 161 17.282 33.998 23.753 1.00 21.41 AAAB C ATOM 1338 O CYS A 161 17.381 34.068 24.977 1.00 23.47 AAAB O ATOM 1339 CB CYS A 161 18.134 32.318 22.066 1.00 23.04 AAAB C ATOM 1340 SG CYS A 161 18.053 30.626 21.363 1.00 27.85 AAAB S ATOM 1341 N VAL A 162 17.369 35.066 22.956 1.00 21.58 AAAB N ATOM 1342 CA VAL A 162 17.552 36.422 23.487 1.00 18.93 AAAB C ATOM 1343 C VAL A 162 16.120 36.868 23.732 1.00 16.73 AAAB C ATOM 1344 O VAL A 162 15.404 37.206 22.797 1.00 19.15 AAAB O ATOM 1345 CB VAL A 162 18.208 37.389 22.476 1.00 17.98 AAAB C ATOM 1346 CG1 VAL A 162 18.425 38.745 23.131 1.00 18.15 AAAB C ATOM 1347 CG2 VAL A 162 19.545 36.833 21.993 1.00 17.95 AAAB C ATOM 1348 N TYR A 163 15.693 36.828 24.986 1.00 11.45 AAAB N ATOM 1349 CA TYR A 163 14.319 37.165 25.318 1.00 6.00 AAAB C ATOM 1350 C TYR A 163 14.124 38.469 26.090 1.00 8.22 AAAB C ATOM 1351 O TYR A 163 12.979 38.831 26.392 1.00 6.46 AAAB O ATOM 1352 CB TYR A 163 13.709 36.010 26.129 1.00 8.50 AAAB C ATOM 1353 CG TYR A 163 14.414 35.768 27.460 1.00 4.81 AAAB C ATOM 1354 CD1 TYR A 163 15.648 35.115 27.507 1.00 4.25 AAAB C ATOM 1355 CD2 TYR A 163 13.881 36.257 28.658 1.00 4.13 AAAB C ATOM 1356 CE1 TYR A 163 16.338 34.967 28.701 1.00 5.59 AAAB C ATOM 1357 CE2 TYR A 163 14.565 36.113 29.864 1.00 3.11 AAAB C ATOM 1358 CZ TYR A 163 15.793 35.470 29.873 1.00 8.32 AAAB C ATOM 1359 OH TYR A 163 16.494 35.348 31.051 1.00 18.26 AAAB O ATOM 1360 N GLU A 164 15.208 39.165 26.427 1.00 3.45 AAAB N ATOM 1361 CA GLU A 164 15.064 40.392 27.204 1.00 8.25 AAAB C ATOM 1362 C GLU A 164 16.212 41.383 27.077 1.00 10.39 AAAB C ATOM 1363 O GLU A 164 17.343 41.010 26.758 1.00 12.46 AAAB O ATOM 1364 CB GLU A 164 14.922 40.044 28.689 1.00 10.14 AAAB C ATOM 1365 CG GLU A 164 16.228 39.545 29.319 1.00 4.73 AAAB C ATOM 1366 CD GLU A 164 16.110 39.239 30.793 1.00 9.82 AAAB C ATOM 1367 OE1 GLU A 164 15.040 39.495 31.396 1.00 6.23 AAAB O ATOM 1368 OE2 GLU A 164 17.105 38.740 31.349 1.00 9.58 AAAB O ATOM 1369 N THR A 165 15.920 42.639 27.396 1.00 12.17 AAAB N ATOM 1370 CA THR A 165 16.916 43.703 27.369 1.00 11.67 AAAB C ATOM 1371 C THR A 165 16.564 44.698 28.472 1.00 10.90 AAAB C ATOM 1372 O THR A 165 15.399 44.787 28.895 1.00 6.41 AAAB O ATOM 1373 CB THR A 165 16.933 44.491 26.001 1.00 12.00 AAAB C ATOM 1374 OG1 THR A 165 15.745 45.276 25.867 1.00 7.81 AAAB O ATOM 1375 CG2 THR A 165 17.022 43.549 24.805 1.00 7.36 AAAB C ATOM 1376 N GLN A 166 17.586 45.365 29.001 1.00 9.69 AAAB N ATOM 1377 CA GLN A 166 17.388 46.410 29.993 1.00 7.54 AAAB C ATOM 1378 C GLN A 166 18.272 47.573 29.559 1.00 5.08 AAAB C ATOM 1379 O GLN A 166 19.454 47.389 29.241 1.00 2.00 AAAB O ATOM 1380 CB GLN A 166 17.731 45.971 31.417 1.00 9.47 AAAB C ATOM 1381 CG GLN A 166 17.421 47.075 32.440 1.00 16.71 AAAB C ATOM 1382 CD GLN A 166 17.385 46.591 33.873 1.00 23.98 AAAB C ATOM 1383 OE1 GLN A 166 18.179 45.739 34.284 1.00 25.39 AAAB O ATOM 1384 NE2 GLN A 166 16.457 47.135 34.647 1.00 22.64 AAAB N ATOM 1385 N TRP A 167 17.675 48.755 29.487 1.00 6.58 AAAB N ATOM 1386 CA TRP A 167 18.383 49.962 29.062 1.00 12.22 AAAB C ATOM 1387 C TRP A 167 18.592 50.878 30.248 1.00 11.34 AAAB C ATOM 1388 O TRP A 167 17.758 50.928 31.152 1.00 10.99 AAAB O ATOM 1389 CB TRP A 167 17.572 50.710 27.997 1.00 12.09 AAAB C ATOM 1390 CG TRP A 167 17.148 49.863 26.832 1.00 11.13 AAAB C ATOM 1391 CD1 TRP A 167 16.137 48.946 26.815 1.00 10.92 AAAB C ATOM 1392 CD2 TRP A 167 17.673 49.910 25.499 1.00 11.94 AAAB C ATOM 1393 NE1 TRP A 167 15.990 48.428 25.553 1.00 15.36 AAAB N ATOM 1394 CE2 TRP A 167 16.919 49.001 24.723 1.00 16.40 AAAB C ATOM 1395 CE3 TRP A 167 18.703 50.631 24.881 1.00 13.01 AAAB C ATOM 1396 CZ2 TRP A 167 17.163 48.797 23.359 1.00 11.71 AAAB C ATOM 1397 CZ3 TRP A 167 18.946 50.424 23.525 1.00 10.85 AAAB C ATOM 1398 CH2 TRP A 167 18.176 49.515 22.782 1.00 10.03 AAAB C ATOM 1399 N TYR A 168 19.692 51.621 30.236 1.00 12.33 AAAB N ATOM 1400 CA TYR A 168 19.991 52.544 31.323 1.00 13.47 AAAB C ATOM 1401 C TYR A 168 20.533 53.848 30.766 1.00 11.52 AAAB C ATOM 1402 O TYR A 168 21.421 53.833 29.912 1.00 10.81 AAAB O ATOM 1403 CB TYR A 168 21.084 51.992 32.251 1.00 18.44 AAAB C ATOM 1404 CG TYR A 168 20.982 50.531 32.636 1.00 20.33 AAAB C ATOM 1405 CD1 TYR A 168 21.457 49.528 31.778 1.00 20.84 AAAB C ATOM 1406 CD2 TYR A 168 20.465 50.153 33.879 1.00 16.56 AAAB C ATOM 1407 CE1 TYR A 168 21.423 48.196 32.148 1.00 21.48 AAAB C ATOM 1408 CE2 TYR A 168 20.428 48.833 34.261 1.00 18.97 AAAB C ATOM 1409 CZ TYR A 168 20.908 47.854 33.395 1.00 24.50 AAAB C ATOM 1410 OH TYR A 168 20.879 46.537 33.789 1.00 22.85 AAAB O ATOM 1411 N VAL A 169 20.010 54.970 31.248 1.00 9.71 AAAB N ATOM 1412 CA VAL A 169 20.529 56.273 30.842 1.00 6.16 AAAB C ATOM 1413 C VAL A 169 21.351 56.745 32.043 1.00 2.99 AAAB C ATOM 1414 O VAL A 169 20.796 56.995 33.106 1.00 2.89 AAAB O ATOM 1415 CB VAL A 169 19.413 57.289 30.541 1.00 2.90 AAAB C ATOM 1416 CG1 VAL A 169 20.021 58.575 30.099 1.00 2.00 AAAB C ATOM 1417 CG2 VAL A 169 18.487 56.761 29.449 1.00 2.64 AAAB C ATOM 1418 N LYS A 170 22.676 56.756 31.908 1.00 3.94 AAAB N ATOM 1419 CA LYS A 170 23.556 57.192 32.997 1.00 8.69 AAAB C ATOM 1420 C LYS A 170 24.523 58.231 32.458 1.00 14.07 AAAB C ATOM 1421 O LYS A 170 25.484 57.884 31.766 1.00 21.04 AAAB O ATOM 1422 CB LYS A 170 24.385 56.033 33.565 1.00 7.92 AAAB C ATOM 1423 CG LYS A 170 23.608 54.843 34.089 1.00 17.34 AAAB C ATOM 1424 CD LYS A 170 22.812 55.176 35.340 1.00 18.90 AAAB C ATOM 1425 CE LYS A 170 22.254 53.910 35.996 1.00 15.97 AAAB C ATOM 1426 NZ LYS A 170 21.561 54.190 37.287 1.00 19.93 AAAB N ATOM 1427 N HIS A 171 24.280 59.496 32.786 1.00 19.47 AAAB N ATOM 1428 CA HIS A 171 25.116 60.616 32.346 1.00 21.39 AAAB C ATOM 1429 C HIS A 171 25.029 60.909 30.845 1.00 19.21 AAAB C ATOM 1430 O HIS A 171 26.049 61.076 30.174 1.00 13.85 AAAB O ATOM 1431 CB HIS A 171 26.585 60.409 32.761 1.00 30.56 AAAB C ATOM 1432 CG HIS A 171 27.155 61.548 33.556 1.00 40.81 AAAB C ATOM 1433 ND1 HIS A 171 28.384 62.114 33.284 1.00 46.35 AAAB N ATOM 1434 CD2 HIS A 171 26.625 62.278 34.568 1.00 40.15 AAAB C ATOM 1435 CE1 HIS A 171 28.583 63.145 34.085 1.00 45.50 AAAB C ATOM 1436 NE2 HIS A 171 27.529 63.267 34.871 1.00 44.24 AAAB N ATOM 1437 N GLY A 172 23.807 60.999 30.330 1.00 17.10 AAAB N ATOM 1438 CA GLY A 172 23.615 61.283 28.918 1.00 15.47 AAAB C ATOM 1439 C GLY A 172 23.918 60.137 27.968 1.00 15.44 AAAB C ATOM 1440 O GLY A 172 23.680 60.251 26.759 1.00 12.14 AAAB O ATOM 1441 N LYS A 173 24.386 59.021 28.526 1.00 14.06 AAAB N ATOM 1442 CA LYS A 173 24.742 57.818 27.772 1.00 10.80 AAAB C ATOM 1443 C LYS A 173 23.692 56.731 27.859 1.00 2.00 AAAB C ATOM 1444 O LYS A 173 23.145 56.501 28.924 1.00 7.31 AAAB O ATOM 1445 CB LYS A 173 26.038 57.257 28.324 1.00 4.51 AAAB C ATOM 1446 CG LYS A 173 27.176 57.318 27.382 1.00 4.96 AAAB C ATOM 1447 CD LYS A 173 28.351 57.975 28.032 1.00 2.00 AAAB C ATOM 1448 CE LYS A 173 29.623 57.421 27.463 1.00 11.23 AAAB C ATOM 1449 NZ LYS A 173 30.716 58.426 27.473 1.00 23.94 AAAB N ATOM 1450 N LEU A 174 23.454 56.036 26.752 1.00 6.51 AAAB N ATOM 1451 CA LEU A 174 22.482 54.944 26.719 1.00 9.93 AAAB C ATOM 1452 C LEU A 174 23.216 53.600 26.729 1.00 13.71 AAAB C ATOM 1453 O LEU A 174 23.973 53.291 25.797 1.00 13.22 AAAB O ATOM 1454 CB LEU A 174 21.599 55.037 25.478 1.00 7.44 AAAB C ATOM 1455 CG LEU A 174 20.373 54.130 25.507 1.00 6.10 AAAB C ATOM 1456 CD1 LEU A 174 19.627 54.328 26.794 1.00 8.14 AAAB C ATOM 1457 CD2 LEU A 174 19.468 54.418 24.334 1.00 3.07 AAAB C ATOM 1458 N HIS A 175 23.021 52.836 27.807 1.00 16.13 AAAB N ATOM 1459 CA HIS A 175 23.638 51.517 28.006 1.00 11.97 AAAB C ATOM 1460 C HIS A 175 22.615 50.434 27.731 1.00 9.13 AAAB C ATOM 1461 O HIS A 175 21.419 50.615 28.015 1.00 6.35 AAAB O ATOM 1462 CB HIS A 175 24.121 51.362 29.447 1.00 15.66 AAAB C ATOM 1463 CG HIS A 175 24.871 52.549 29.959 1.00 11.83 AAAB C ATOM 1464 ND1 HIS A 175 26.245 52.574 30.057 1.00 8.11 AAAB N ATOM 1465 CD2 HIS A 175 24.439 53.767 30.362 1.00 6.40 AAAB C ATOM 1466 CE1 HIS A 175 26.630 53.761 30.492 1.00 2.00 AAAB C ATOM 1467 NE2 HIS A 175 25.553 54.503 30.686 1.00 9.63 AAAB N ATOM 1468 N LEU A 176 23.081 49.305 27.205 1.00 8.96 AAAB N ATOM 1469 CA LEU A 176 22.182 48.195 26.898 1.00 12.42 AAAB C ATOM 1470 C LEU A 176 22.708 46.870 27.421 1.00 14.21 AAAB C ATOM 1471 O LEU A 176 23.884 46.538 27.255 1.00 15.95 AAAB O ATOM 1472 CB LEU A 176 21.931 48.074 25.393 1.00 4.79 AAAB C ATOM 1473 CG LEU A 176 21.079 46.853 25.035 1.00 7.46 AAAB C ATOM 1474 CD1 LEU A 176 19.730 46.963 25.715 1.00 2.01 AAAB C ATOM 1475 CD2 LEU A 176 20.922 46.687 23.514 1.00 4.52 AAAB C ATOM 1476 N GLU A 177 21.815 46.123 28.054 1.00 19.57 AAAB N ATOM 1477 CA GLU A 177 22.133 44.810 28.592 1.00 16.97 AAAB C ATOM 1478 C GLU A 177 21.061 43.855 28.081 1.00 14.65 AAAB C ATOM 1479 O GLU A 177 19.855 44.111 28.235 1.00 6.61 AAAB O ATOM 1480 CB GLU A 177 22.130 44.833 30.115 1.00 13.39 AAAB C ATOM 1481 CG GLU A 177 22.606 43.536 30.726 1.00 17.44 AAAB C ATOM 1482 CD GLU A 177 22.816 43.636 32.219 1.00 20.64 AAAB C ATOM 1483 OE1 GLU A 177 21.989 44.280 32.885 1.00 14.88 AAAB O ATOM 1484 OE2 GLU A 177 23.814 43.080 32.724 1.00 17.04 AAAB O ATOM 1485 N VAL A 178 21.501 42.809 27.387 1.00 15.80 AAAB N ATOM 1486 CA VAL A 178 20.590 41.801 26.847 1.00 14.90 AAAB C ATOM 1487 C VAL A 178 20.990 40.438 27.403 1.00 12.86 AAAB C ATOM 1488 O VAL A 178 22.146 40.212 27.793 1.00 9.62 AAAB O ATOM 1489 CB VAL A 178 20.653 41.734 25.300 1.00 14.61 AAAB C ATOM 1490 CG1 VAL A 178 20.371 43.090 24.689 1.00 15.21 AAAB C ATOM 1491 CG2 VAL A 178 22.001 41.255 24.865 1.00 11.90 AAAB C ATOM 1492 N ARG A 179 20.034 39.528 27.450 1.00 12.26 AAAB N ATOM 1493 CA ARG A 179 20.329 38.207 27.942 1.00 11.22 AAAB C ATOM 1494 C ARG A 179 19.774 37.105 27.068 1.00 10.71 AAAB C ATOM 1495 O ARG A 179 18.624 37.173 26.610 1.00 9.54 AAAB O ATOM 1496 CB ARG A 179 19.822 38.023 29.368 1.00 15.57 AAAB C ATOM 1497 CG ARG A 179 20.276 36.694 29.945 1.00 18.32 AAAB C ATOM 1498 CD ARG A 179 19.893 36.469 31.382 1.00 16.92 AAAB C ATOM 1499 NE ARG A 179 20.623 35.306 31.876 1.00 15.33 AAAB N ATOM 1500 CZ ARG A 179 20.113 34.087 31.993 1.00 11.49 AAAB C ATOM 1501 NH1 ARG A 179 18.847 33.847 31.664 1.00 9.94 AAAB N ATOM 1502 NH2 ARG A 179 20.892 33.095 32.394 1.00 11.63 AAAB N ATOM 1503 N ALA A 180 20.621 36.109 26.828 1.00 8.66 AAAB N ATOM 1504 CA ALA A 180 20.274 34.926 26.053 1.00 10.44 AAAB C ATOM 1505 C ALA A 180 20.262 33.764 27.041 1.00 9.95 AAAB C ATOM 1506 O ALA A 180 21.250 33.531 27.741 1.00 6.85 AAAB O ATOM 1507 CB ALA A 180 21.316 34.677 24.976 1.00 12.83 AAAB C ATOM 1508 N ARG A 181 19.126 33.087 27.152 1.00 9.95 AAAB N ATOM 1509 CA ARG A 181 18.999 31.944 28.054 1.00 11.02 AAAB C ATOM 1510 C ARG A 181 19.892 30.792 27.580 1.00 11.03 AAAB C ATOM 1511 O ARG A 181 20.446 30.028 28.369 1.00 11.66 AAAB O ATOM 1512 CB ARG A 181 17.544 31.470 28.109 1.00 9.04 AAAB C ATOM 1513 CG ARG A 181 16.972 30.995 26.777 1.00 7.89 AAAB C ATOM 1514 CD ARG A 181 15.603 30.390 26.981 1.00 13.58 AAAB C ATOM 1515 NE ARG A 181 14.999 29.893 25.745 1.00 20.74 AAAB N ATOM 1516 CZ ARG A 181 15.467 28.878 25.015 1.00 23.02 AAAB C ATOM 1517 NH1 ARG A 181 16.573 28.232 25.365 1.00 16.98 AAAB N ATOM 1518 NH2 ARG A 181 14.774 28.455 23.967 1.00 20.85 AAAB N ATOM 1519 N SER A 182 20.050 30.709 26.271 1.00 14.09 AAAB N ATOM 1520 CA SER A 182 20.840 29.679 25.635 1.00 15.21 AAAB C ATOM 1521 C SER A 182 21.450 30.314 24.393 1.00 16.18 AAAB C ATOM 1522 O SER A 182 20.846 31.208 23.776 1.00 16.23 AAAB O ATOM 1523 CB SER A 182 19.907 28.540 25.216 1.00 10.47 AAAB C ATOM 1524 OG SER A 182 20.597 27.543 24.495 1.00 22.09 AAAB O ATOM 1525 N ASN A 183 22.637 29.867 24.017 1.00 15.58 AAAB N ATOM 1526 CA ASN A 183 23.271 30.408 22.826 1.00 15.97 AAAB C ATOM 1527 C ASN A 183 24.332 29.464 22.301 1.00 15.19 AAAB C ATOM 1528 O ASN A 183 25.124 28.911 23.064 1.00 12.14 AAAB O ATOM 1529 CB ASN A 183 23.881 31.789 23.106 1.00 17.66 AAAB C ATOM 1530 CG ASN A 183 23.612 32.790 21.990 1.00 16.64 AAAB C ATOM 1531 OD1 ASN A 183 24.494 33.557 21.608 1.00 18.73 AAAB O ATOM 1532 ND2 ASN A 183 22.385 32.802 21.479 1.00 9.55 AAAB N ATOM 1533 N ASP A 184 24.247 29.188 21.006 1.00 16.04 AAAB N ATOM 1534 CA ASP A 184 25.197 28.328 20.318 1.00 13.68 AAAB C ATOM 1535 C ASP A 184 26.345 29.273 19.981 1.00 12.44 AAAB C ATOM 1536 O ASP A 184 26.193 30.169 19.156 1.00 11.48 AAAB O ATOM 1537 CB ASP A 184 24.534 27.779 19.044 1.00 14.68 AAAB C ATOM 1538 CG ASP A 184 25.458 26.907 18.206 1.00 13.42 AAAB C ATOM 1539 OD1 ASP A 184 26.701 27.043 18.283 1.00 11.03 AAAB O ATOM 1540 OD2 ASP A 184 24.920 26.094 17.433 1.00 18.49 AAAB O ATOM 1541 N MET A 185 27.486 29.082 20.624 1.00 13.96 AAAB N ATOM 1542 CA MET A 185 28.635 29.947 20.394 1.00 16.81 AAAB C ATOM 1543 C MET A 185 29.145 29.998 18.961 1.00 19.91 AAAB C ATOM 1544 O MET A 185 29.584 31.048 18.494 1.00 22.52 AAAB O ATOM 1545 CB MET A 185 29.784 29.588 21.348 1.00 12.70 AAAB C ATOM 1546 CG MET A 185 29.478 29.825 22.823 1.00 20.33 AAAB C ATOM 1547 SD MET A 185 29.057 31.553 23.229 1.00 18.79 AAAB S ATOM 1548 CE MET A 185 27.282 31.441 23.207 1.00 12.21 AAAB C ATOM 1549 N ALA A 186 29.086 28.870 18.261 1.00 24.58 AAAB N ATOM 1550 CA ALA A 186 29.584 28.803 16.886 1.00 23.86 AAAB C ATOM 1551 C ALA A 186 28.727 29.501 15.839 1.00 21.92 AAAB C ATOM 1552 O ALA A 186 29.231 30.273 15.032 1.00 23.62 AAAB O ATOM 1553 CB ALA A 186 29.816 27.358 16.484 1.00 24.19 AAAB C ATOM 1554 N LEU A 187 27.432 29.222 15.853 1.00 22.41 AAAB N ATOM 1555 CA LEU A 187 26.531 29.799 14.870 1.00 23.40 AAAB C ATOM 1556 C LEU A 187 25.712 30.994 15.346 1.00 25.68 AAAB C ATOM 1557 O LEU A 187 25.813 32.091 14.788 1.00 31.23 AAAB O ATOM 1558 CB LEU A 187 25.597 28.707 14.341 1.00 27.65 AAAB C ATOM 1559 CG LEU A 187 26.285 27.488 13.709 1.00 30.10 AAAB C ATOM 1560 CD1 LEU A 187 25.294 26.349 13.539 1.00 30.22 AAAB C ATOM 1561 CD2 LEU A 187 26.937 27.861 12.385 1.00 24.53 AAAB C ATOM 1562 N GLY A 188 24.917 30.789 16.388 1.00 21.21 AAAB N ATOM 1563 CA GLY A 188 24.062 31.845 16.886 1.00 20.12 AAAB C ATOM 1564 C GLY A 188 24.659 33.055 17.584 1.00 22.86 AAAB C ATOM 1565 O GLY A 188 24.218 34.181 17.339 1.00 22.83 AAAB O ATOM 1566 N ASN A 189 25.666 32.855 18.425 1.00 20.56 AAAB N ATOM 1567 CA ASN A 189 26.239 33.969 19.176 1.00 18.99 AAAB C ATOM 1568 C ASN A 189 26.744 35.174 18.395 1.00 17.51 AAAB C ATOM 1569 O ASN A 189 26.272 36.287 18.618 1.00 19.13 AAAB O ATOM 1570 CB ASN A 189 27.315 33.499 20.150 1.00 16.81 AAAB C ATOM 1571 CG ASN A 189 27.787 34.609 21.054 1.00 12.14 AAAB C ATOM 1572 OD1 ASN A 189 28.910 35.097 20.933 1.00 13.57 AAAB O ATOM 1573 ND2 ASN A 189 26.914 35.039 21.949 1.00 11.57 AAAB N ATOM 1574 N PRO A 190 27.714 34.981 17.483 1.00 15.79 AAAB N ATOM 1575 CA PRO A 190 28.243 36.110 16.701 1.00 15.31 AAAB C ATOM 1576 C PRO A 190 27.136 36.915 16.019 1.00 12.38 AAAB C ATOM 1577 O PRO A 190 27.144 38.146 16.019 1.00 12.34 AAAB O ATOM 1578 CB PRO A 190 29.149 35.417 15.687 1.00 13.87 AAAB C ATOM 1579 CG PRO A 190 29.668 34.245 16.464 1.00 12.42 AAAB C ATOM 1580 CD PRO A 190 28.413 33.733 17.131 1.00 12.55 AAAB C ATOM 1581 N PHE A 191 26.151 36.200 15.501 1.00 11.81 AAAB N ATOM 1582 CA PHE A 191 25.016 36.798 14.825 1.00 12.21 AAAB C ATOM 1583 C PHE A 191 24.243 37.684 15.804 1.00 14.05 AAAB C ATOM 1584 O PHE A 191 23.982 38.850 15.514 1.00 17.83 AAAB O ATOM 1585 CB PHE A 191 24.140 35.661 14.280 1.00 5.25 AAAB C ATOM 1586 CG PHE A 191 22.888 36.105 13.564 1.00 2.00 AAAB C ATOM 1587 CD1 PHE A 191 21.689 36.265 14.260 1.00 4.11 AAAB C ATOM 1588 CD2 PHE A 191 22.884 36.264 12.179 1.00 2.00 AAAB C ATOM 1589 CE1 PHE A 191 20.490 36.571 13.580 1.00 2.00 AAAB C ATOM 1590 CE2 PHE A 191 21.706 36.568 11.495 1.00 3.17 AAAB C ATOM 1591 CZ PHE A 191 20.502 36.720 12.197 1.00 4.38 AAAB C ATOM 1592 N ASN A 192 23.949 37.159 16.991 1.00 17.54 AAAB N ATOM 1593 CA ASN A 192 23.180 37.905 17.991 1.00 14.50 AAAB C ATOM 1594 C ASN A 192 23.872 39.077 18.694 1.00 9.96 AAAB C ATOM 1595 O ASN A 192 23.220 40.058 19.023 1.00 12.61 AAAB O ATOM 1596 CB ASN A 192 22.573 36.955 19.017 1.00 13.45 AAAB C ATOM 1597 CG ASN A 192 21.469 36.107 18.433 1.00 15.31 AAAB C ATOM 1598 OD1 ASN A 192 20.375 36.594 18.137 1.00 23.54 AAAB O ATOM 1599 ND2 ASN A 192 21.751 34.833 18.241 1.00 20.86 AAAB N ATOM 1600 N VAL A 193 25.162 38.962 18.971 1.00 5.31 AAAB N ATOM 1601 CA VAL A 193 25.900 40.043 19.623 1.00 14.01 AAAB C ATOM 1602 C VAL A 193 25.881 41.304 18.753 1.00 17.70 AAAB C ATOM 1603 O VAL A 193 25.519 42.384 19.218 1.00 19.69 AAAB O ATOM 1604 CB VAL A 193 27.353 39.617 19.929 1.00 13.86 AAAB C ATOM 1605 CG1 VAL A 193 28.199 40.812 20.302 1.00 14.46 AAAB C ATOM 1606 CG2 VAL A 193 27.360 38.608 21.062 1.00 14.91 AAAB C ATOM 1607 N PHE A 194 26.257 41.155 17.487 1.00 18.96 AAAB N ATOM 1608 CA PHE A 194 26.247 42.266 16.545 1.00 16.96 AAAB C ATOM 1609 C PHE A 194 24.809 42.764 16.388 1.00 14.96 AAAB C ATOM 1610 O PHE A 194 24.541 43.965 16.430 1.00 19.29 AAAB O ATOM 1611 CB PHE A 194 26.789 41.798 15.185 1.00 18.52 AAAB C ATOM 1612 CG PHE A 194 26.487 42.739 14.042 1.00 18.49 AAAB C ATOM 1613 CD1 PHE A 194 27.317 43.826 13.774 1.00 23.28 AAAB C ATOM 1614 CD2 PHE A 194 25.374 42.539 13.233 1.00 18.51 AAAB C ATOM 1615 CE1 PHE A 194 27.040 44.697 12.716 1.00 22.51 AAAB C ATOM 1616 CE2 PHE A 194 25.089 43.405 12.174 1.00 17.69 AAAB C ATOM 1617 CZ PHE A 194 25.919 44.481 11.915 1.00 17.80 AAAB C ATOM 1618 N GLN A 195 23.884 41.830 16.233 1.00 10.86 AAAB N ATOM 1619 CA GLN A 195 22.481 42.170 16.043 1.00 11.48 AAAB C ATOM 1620 C GLN A 195 21.891 43.135 17.069 1.00 14.34 AAAB C ATOM 1621 O GLN A 195 21.129 44.031 16.705 1.00 17.40 AAAB O ATOM 1622 CB GLN A 195 21.637 40.903 15.982 1.00 2.57 AAAB C ATOM 1623 CG GLN A 195 20.169 41.168 15.808 1.00 12.10 AAAB C ATOM 1624 CD GLN A 195 19.356 39.899 15.746 1.00 14.67 AAAB C ATOM 1625 OE1 GLN A 195 18.751 39.590 14.718 1.00 15.07 AAAB O ATOM 1626 NE2 GLN A 195 19.319 39.161 16.852 1.00 10.43 AAAB N ATOM 1627 N TYR A 196 22.194 42.939 18.350 1.00 16.89 AAAB N ATOM 1628 CA TYR A 196 21.643 43.822 19.369 1.00 14.10 AAAB C ATOM 1629 C TYR A 196 22.406 45.120 19.560 1.00 15.61 AAAB C ATOM 1630 O TYR A 196 21.876 46.094 20.094 1.00 16.18 AAAB O ATOM 1631 CB TYR A 196 21.388 43.084 20.677 1.00 5.43 AAAB C ATOM 1632 CG TYR A 196 20.018 42.460 20.663 1.00 6.88 AAAB C ATOM 1633 CD1 TYR A 196 19.762 41.315 19.913 1.00 2.78 AAAB C ATOM 1634 CD2 TYR A 196 18.960 43.052 21.343 1.00 3.68 AAAB C ATOM 1635 CE1 TYR A 196 18.479 40.782 19.834 1.00 4.35 AAAB C ATOM 1636 CE2 TYR A 196 17.676 42.528 21.274 1.00 4.83 AAAB C ATOM 1637 CZ TYR A 196 17.442 41.393 20.516 1.00 7.73 AAAB C ATOM 1638 OH TYR A 196 16.164 40.886 20.420 1.00 10.51 AAAB O ATOM 1639 N ASN A 197 23.645 45.144 19.098 1.00 11.85 AAAB N ATOM 1640 CA ASN A 197 24.420 46.357 19.171 1.00 13.50 AAAB C ATOM 1641 C ASN A 197 23.761 47.329 18.190 1.00 13.98 AAAB C ATOM 1642 O ASN A 197 23.533 48.486 18.514 1.00 17.17 AAAB O ATOM 1643 CB ASN A 197 25.855 46.088 18.763 1.00 18.06 AAAB C ATOM 1644 CG ASN A 197 26.735 47.288 18.939 1.00 20.06 AAAB C ATOM 1645 OD1 ASN A 197 27.395 47.725 17.999 1.00 27.02 AAAB O ATOM 1646 ND2 ASN A 197 26.764 47.828 20.147 1.00 21.14 AAAB N ATOM 1647 N VAL A 198 23.412 46.845 17.002 1.00 12.90 AAAB N ATOM 1648 CA VAL A 198 22.759 47.696 16.012 1.00 13.18 AAAB C ATOM 1649 C VAL A 198 21.497 48.321 16.612 1.00 13.82 AAAB C ATOM 1650 O VAL A 198 21.242 49.511 16.427 1.00 17.84 AAAB O ATOM 1651 CB VAL A 198 22.407 46.923 14.708 1.00 10.11 AAAB C ATOM 1652 CG1 VAL A 198 21.577 47.793 13.788 1.00 10.53 AAAB C ATOM 1653 CG2 VAL A 198 23.675 46.488 13.991 1.00 7.18 AAAB C ATOM 1654 N LEU A 199 20.719 47.532 17.345 1.00 11.53 AAAB N ATOM 1655 CA LEU A 199 19.498 48.050 17.970 1.00 10.00 AAAB C ATOM 1656 C LEU A 199 19.813 49.189 18.959 1.00 10.84 AAAB C ATOM 1657 O LEU A 199 19.066 50.161 19.059 1.00 11.45 AAAB O ATOM 1658 CB LEU A 199 18.765 46.934 18.700 1.00 2.00 AAAB C ATOM 1659 CG LEU A 199 17.450 47.313 19.371 1.00 4.19 AAAB C ATOM 1660 CD1 LEU A 199 16.415 47.649 18.330 1.00 2.00 AAAB C ATOM 1661 CD2 LEU A 199 16.969 46.162 20.244 1.00 6.10 AAAB C ATOM 1662 N GLN A 200 20.915 49.057 19.689 1.00 5.99 AAAB N ATOM 1663 CA GLN A 200 21.317 50.067 20.652 1.00 8.55 AAAB C ATOM 1664 C GLN A 200 21.609 51.349 19.900 1.00 11.38 AAAB C ATOM 1665 O GLN A 200 21.071 52.403 20.229 1.00 18.19 AAAB O ATOM 1666 CB GLN A 200 22.565 49.627 21.411 1.00 3.08 AAAB C ATOM 1667 CG GLN A 200 22.878 50.501 22.605 1.00 3.84 AAAB C ATOM 1668 CD GLN A 200 24.280 50.292 23.132 1.00 7.77 AAAB C ATOM 1669 OE1 GLN A 200 25.044 49.477 22.611 1.00 7.17 AAAB O ATOM 1670 NE2 GLN A 200 24.639 51.049 24.161 1.00 9.69 AAAB N ATOM 1671 N ARG A 201 22.451 51.240 18.877 1.00 11.88 AAAB N ATOM 1672 CA ARG A 201 22.831 52.364 18.027 1.00 8.97 AAAB C ATOM 1673 C ARG A 201 21.630 53.025 17.366 1.00 11.07 AAAB C ATOM 1674 O ARG A 201 21.597 54.239 17.198 1.00 17.96 AAAB O ATOM 1675 CB ARG A 201 23.836 51.902 16.975 1.00 2.00 AAAB C ATOM 1676 CG ARG A 201 25.166 51.593 17.597 1.00 2.37 AAAB C ATOM 1677 CD ARG A 201 26.186 51.047 16.631 1.00 3.27 AAAB C ATOM 1678 NE ARG A 201 27.407 50.715 17.358 1.00 3.50 AAAB N ATOM 1679 CZ ARG A 201 28.610 51.214 17.090 1.00 11.88 AAAB C ATOM 1680 NH1 ARG A 201 28.772 52.074 16.092 1.00 17.15 AAAB N ATOM 1681 NH2 ARG A 201 29.637 50.924 17.878 1.00 16.17 AAAB N ATOM 1682 N MET A 202 20.642 52.226 16.996 1.00 14.12 AAAB N ATOM 1683 CA MET A 202 19.433 52.747 16.379 1.00 14.59 AAAB C ATOM 1684 C MET A 202 18.656 53.553 17.399 1.00 18.04 AAAB C ATOM 1685 O MET A 202 18.331 54.714 17.162 1.00 25.05 AAAB O ATOM 1686 CB MET A 202 18.552 51.606 15.870 1.00 13.81 AAAB C ATOM 1687 CG MET A 202 19.012 50.999 14.570 1.00 15.86 AAAB C ATOM 1688 SD MET A 202 18.066 49.536 14.158 1.00 23.89 AAAB S ATOM 1689 CE MET A 202 16.413 50.144 14.248 1.00 8.30 AAAB C ATOM 1690 N ILE A 203 18.356 52.922 18.531 1.00 17.82 AAAB N ATOM 1691 CA ILE A 203 17.605 53.545 19.617 1.00 13.44 AAAB C ATOM 1692 C ILE A 203 18.289 54.803 20.142 1.00 10.71 AAAB C ATOM 1693 O ILE A 203 17.633 55.823 20.344 1.00 8.57 AAAB O ATOM 1694 CB ILE A 203 17.406 52.559 20.795 1.00 16.99 AAAB C ATOM 1695 CG1 ILE A 203 16.561 51.349 20.357 1.00 19.82 AAAB C ATOM 1696 CG2 ILE A 203 16.807 53.274 21.999 1.00 9.76 AAAB C ATOM 1697 CD1 ILE A 203 15.109 51.647 20.033 1.00 24.51 AAAB C ATOM 1698 N ALA A 204 19.605 54.738 20.332 1.00 4.96 AAAB N ATOM 1699 CA ALA A 204 20.362 55.875 20.848 1.00 6.72 AAAB C ATOM 1700 C ALA A 204 20.252 57.102 19.951 1.00 15.06 AAAB C ATOM 1701 O ALA A 204 20.197 58.237 20.437 1.00 19.69 AAAB O ATOM 1702 CB ALA A 204 21.820 55.494 21.048 1.00 2.00 AAAB C ATOM 1703 N GLN A 205 20.206 56.867 18.642 1.00 17.65 AAAB N ATOM 1704 CA GLN A 205 20.105 57.939 17.666 1.00 15.79 AAAB C ATOM 1705 C GLN A 205 18.741 58.609 17.726 1.00 18.23 AAAB C ATOM 1706 O GLN A 205 18.650 59.824 17.881 1.00 24.55 AAAB O ATOM 1707 CB GLN A 205 20.385 57.416 16.250 1.00 18.02 AAAB C ATOM 1708 CG GLN A 205 20.355 58.501 15.178 1.00 17.31 AAAB C ATOM 1709 CD GLN A 205 20.773 58.014 13.800 1.00 14.62 AAAB C ATOM 1710 OE1 GLN A 205 21.937 57.681 13.568 1.00 15.97 AAAB O ATOM 1711 NE2 GLN A 205 19.837 58.027 12.864 1.00 7.63 AAAB N ATOM 1712 N VAL A 206 17.678 57.824 17.647 1.00 20.01 AAAB N ATOM 1713 CA VAL A 206 16.337 58.394 17.689 1.00 21.58 AAAB C ATOM 1714 C VAL A 206 15.979 59.060 19.022 1.00 23.59 AAAB C ATOM 1715 O VAL A 206 15.046 59.858 19.067 1.00 27.98 AAAB O ATOM 1716 CB VAL A 206 15.242 57.354 17.321 1.00 21.40 AAAB C ATOM 1717 CG1 VAL A 206 15.530 56.746 15.970 1.00 22.98 AAAB C ATOM 1718 CG2 VAL A 206 15.125 56.282 18.386 1.00 23.17 AAAB C ATOM 1719 N THR A 207 16.682 58.711 20.102 1.00 25.05 AAAB N ATOM 1720 CA THR A 207 16.417 59.300 21.420 1.00 21.42 AAAB C ATOM 1721 C THR A 207 17.394 60.428 21.753 1.00 22.14 AAAB C ATOM 1722 O THR A 207 17.187 61.175 22.708 1.00 25.43 AAAB O ATOM 1723 CB THR A 207 16.467 58.239 22.553 1.00 18.13 AAAB C ATOM 1724 OG1 THR A 207 17.688 57.494 22.465 1.00 18.70 AAAB O ATOM 1725 CG2 THR A 207 15.290 57.291 22.462 1.00 10.14 AAAB C ATOM 1726 N GLY A 208 18.494 60.496 21.015 1.00 20.14 AAAB N ATOM 1727 CA GLY A 208 19.467 61.547 21.239 1.00 19.87 AAAB C ATOM 1728 C GLY A 208 20.391 61.344 22.420 1.00 20.62 AAAB C ATOM 1729 O GLY A 208 20.657 62.273 23.182 1.00 30.91 AAAB O ATOM 1730 N TYR A 209 20.899 60.135 22.576 1.00 19.09 AAAB N ATOM 1731 CA TYR A 209 21.812 59.845 23.662 1.00 14.46 AAAB C ATOM 1732 C TYR A 209 23.116 59.388 23.058 1.00 15.24 AAAB C ATOM 1733 O TYR A 209 23.144 58.894 21.934 1.00 19.44 AAAB O ATOM 1734 CB TYR A 209 21.265 58.731 24.546 1.00 12.88 AAAB C ATOM 1735 CG TYR A 209 20.143 59.180 25.423 1.00 8.46 AAAB C ATOM 1736 CD1 TYR A 209 20.364 60.106 26.439 1.00 10.23 AAAB C ATOM 1737 CD2 TYR A 209 18.847 58.703 25.229 1.00 8.45 AAAB C ATOM 1738 CE1 TYR A 209 19.319 60.549 27.242 1.00 8.96 AAAB C ATOM 1739 CE2 TYR A 209 17.791 59.142 26.031 1.00 6.90 AAAB C ATOM 1740 CZ TYR A 209 18.041 60.066 27.031 1.00 2.00 AAAB C ATOM 1741 OH TYR A 209 17.022 60.540 27.812 1.00 15.84 AAAB O ATOM 1742 N GLU A 210 24.202 59.582 23.786 1.00 9.36 AAAB N ATOM 1743 CA GLU A 210 25.489 59.134 23.310 1.00 12.45 AAAB C ATOM 1744 C GLU A 210 25.501 57.624 23.594 1.00 15.17 AAAB C ATOM 1745 O GLU A 210 24.631 57.122 24.318 1.00 15.27 AAAB O ATOM 1746 CB GLU A 210 26.605 59.870 24.056 1.00 17.68 AAAB C ATOM 1747 CG GLU A 210 27.983 59.640 23.493 1.00 35.23 AAAB C ATOM 1748 CD GLU A 210 29.030 60.522 24.135 1.00 45.95 AAAB C ATOM 1749 OE1 GLU A 210 29.313 60.353 25.342 1.00 54.20 AAAB O ATOM 1750 OE2 GLU A 210 29.585 61.383 23.425 1.00 52.92 AAAB O ATOM 1751 N LEU A 211 26.447 56.895 23.009 1.00 15.45 AAAB N ATOM 1752 CA LEU A 211 26.518 55.456 23.212 1.00 13.44 AAAB C ATOM 1753 C LEU A 211 27.176 55.051 24.519 1.00 15.72 AAAB C ATOM 1754 O LEU A 211 28.291 55.479 24.827 1.00 15.29 AAAB O ATOM 1755 CB LEU A 211 27.232 54.779 22.044 1.00 14.53 AAAB C ATOM 1756 CG LEU A 211 26.403 54.656 20.763 1.00 12.97 AAAB C ATOM 1757 CD1 LEU A 211 27.213 54.018 19.633 1.00 3.90 AAAB C ATOM 1758 CD2 LEU A 211 25.149 53.853 21.077 1.00 6.98 AAAB C ATOM 1759 N GLY A 212 26.455 54.239 25.287 1.00 13.31 AAAB N ATOM 1760 CA GLY A 212 26.960 53.744 26.545 1.00 12.71 AAAB C ATOM 1761 C GLY A 212 27.551 52.363 26.339 1.00 19.26 AAAB C ATOM 1762 O GLY A 212 27.910 51.989 25.221 1.00 17.56 AAAB O ATOM 1763 N GLU A 213 27.580 51.571 27.404 1.00 19.47 AAAB N ATOM 1764 CA GLU A 213 28.147 50.227 27.349 1.00 18.24 AAAB C ATOM 1765 C GLU A 213 27.162 49.177 26.805 1.00 13.74 AAAB C ATOM 1766 O GLU A 213 25.944 49.316 26.962 1.00 13.88 AAAB O ATOM 1767 CB GLU A 213 28.656 49.843 28.743 1.00 17.85 AAAB C ATOM 1768 CG GLU A 213 29.572 48.632 28.790 1.00 23.34 AAAB C ATOM 1769 CD GLU A 213 30.164 48.389 30.176 1.00 28.12 AAAB C ATOM 1770 OE1 GLU A 213 29.552 48.812 31.181 1.00 27.09 AAAB O ATOM 1771 OE2 GLU A 213 31.251 47.768 30.260 1.00 31.02 AAAB O ATOM 1772 N TYR A 214 27.700 48.163 26.128 1.00 8.97 AAAB N ATOM 1773 CA TYR A 214 26.915 47.066 25.562 1.00 8.11 AAAB C ATOM 1774 C TYR A 214 27.273 45.780 26.321 1.00 6.45 AAAB C ATOM 1775 O TYR A 214 28.437 45.361 26.349 1.00 2.04 AAAB O ATOM 1776 CB TYR A 214 27.230 46.898 24.068 1.00 8.12 AAAB C ATOM 1777 CG TYR A 214 26.456 45.781 23.386 1.00 6.17 AAAB C ATOM 1778 CD1 TYR A 214 25.072 45.699 23.511 1.00 7.08 AAAB C ATOM 1779 CD2 TYR A 214 27.105 44.812 22.617 1.00 7.79 AAAB C ATOM 1780 CE1 TYR A 214 24.352 44.695 22.901 1.00 7.42 AAAB C ATOM 1781 CE2 TYR A 214 26.379 43.790 21.988 1.00 7.47 AAAB C ATOM 1782 CZ TYR A 214 25.003 43.748 22.142 1.00 7.69 AAAB C ATOM 1783 OH TYR A 214 24.250 42.782 21.527 1.00 9.70 AAAB O ATOM 1784 N ILE A 215 26.281 45.145 26.925 1.00 3.58 AAAB N ATOM 1785 CA ILE A 215 26.543 43.934 27.688 1.00 9.63 AAAB C ATOM 1786 C ILE A 215 25.695 42.769 27.196 1.00 9.40 AAAB C ATOM 1787 O ILE A 215 24.471 42.884 27.102 1.00 6.63 AAAB O ATOM 1788 CB ILE A 215 26.306 44.199 29.191 1.00 14.67 AAAB C ATOM 1789 CG1 ILE A 215 27.184 45.380 29.645 1.00 15.88 AAAB C ATOM 1790 CG2 ILE A 215 26.641 42.965 30.012 1.00 14.69 AAAB C ATOM 1791 CD1 ILE A 215 26.583 46.228 30.750 1.00 11.35 AAAB C ATOM 1792 N PHE A 216 26.357 41.657 26.868 1.00 13.06 AAAB N ATOM 1793 CA PHE A 216 25.683 40.458 26.364 1.00 11.29 AAAB C ATOM 1794 C PHE A 216 25.860 39.305 27.360 1.00 10.77 AAAB C ATOM 1795 O PHE A 216 26.982 38.848 27.615 1.00 8.65 AAAB O ATOM 1796 CB PHE A 216 26.249 40.068 24.985 1.00 14.88 AAAB C ATOM 1797 CG PHE A 216 25.317 39.212 24.167 1.00 16.87 AAAB C ATOM 1798 CD1 PHE A 216 24.356 39.794 23.353 1.00 12.15 AAAB C ATOM 1799 CD2 PHE A 216 25.366 37.825 24.254 1.00 19.89 AAAB C ATOM 1800 CE1 PHE A 216 23.455 39.022 22.647 1.00 17.86 AAAB C ATOM 1801 CE2 PHE A 216 24.467 37.039 23.550 1.00 20.18 AAAB C ATOM 1802 CZ PHE A 216 23.508 37.638 22.747 1.00 24.67 AAAB C ATOM 1803 N ASN A 217 24.750 38.861 27.939 1.00 6.72 AAAB N ATOM 1804 CA ASN A 217 24.769 37.779 28.915 1.00 8.44 AAAB C ATOM 1805 C ASN A 217 24.223 36.498 28.344 1.00 7.38 AAAB C ATOM 1806 O ASN A 217 23.112 36.475 27.804 1.00 4.55 AAAB O ATOM 1807 CB ASN A 217 23.924 38.126 30.136 1.00 12.24 AAAB C ATOM 1808 CG ASN A 217 24.386 39.365 30.825 1.00 9.83 AAAB C ATOM 1809 OD1 ASN A 217 25.541 39.473 31.235 1.00 13.98 AAAB O ATOM 1810 ND2 ASN A 217 23.484 40.320 30.966 1.00 7.94 AAAB N ATOM 1811 N ILE A 218 24.968 35.420 28.544 1.00 7.67 AAAB N ATOM 1812 CA ILE A 218 24.567 34.112 28.054 1.00 12.07 AAAB C ATOM 1813 C ILE A 218 24.405 33.165 29.243 1.00 10.44 AAAB C ATOM 1814 O ILE A 218 25.283 33.084 30.108 1.00 13.49 AAAB O ATOM 1815 CB ILE A 218 25.617 33.545 27.071 1.00 10.54 AAAB C ATOM 1816 CG1 ILE A 218 26.054 34.626 26.072 1.00 8.89 AAAB C ATOM 1817 CG2 ILE A 218 25.017 32.374 26.317 1.00 8.39 AAAB C ATOM 1818 CD1 ILE A 218 27.464 34.435 25.523 1.00 6.87 AAAB C ATOM 1819 N GLY A 219 23.254 32.510 29.312 1.00 11.81 AAAB N ATOM 1820 CA GLY A 219 22.972 31.568 30.384 1.00 14.96 AAAB C ATOM 1821 C GLY A 219 23.638 30.233 30.106 1.00 15.86 AAAB C ATOM 1822 O GLY A 219 24.620 29.891 30.768 1.00 19.51 AAAB O ATOM 1823 N ASP A 220 23.116 29.484 29.135 1.00 13.83 AAAB N ATOM 1824 CA ASP A 220 23.702 28.200 28.755 1.00 14.03 AAAB C ATOM 1825 C ASP A 220 24.555 28.402 27.511 1.00 13.14 AAAB C ATOM 1826 O ASP A 220 24.042 28.484 26.390 1.00 12.09 AAAB O ATOM 1827 CB ASP A 220 22.621 27.152 28.485 1.00 24.26 AAAB C ATOM 1828 CG ASP A 220 23.197 25.747 28.323 1.00 25.65 AAAB C ATOM 1829 OD1 ASP A 220 24.122 25.377 29.079 1.00 27.61 AAAB O ATOM 1830 OD2 ASP A 220 22.723 25.014 27.435 1.00 34.11 AAAB O ATOM 1831 N CYS A 221 25.861 28.444 27.726 1.00 15.28 AAAB N ATOM 1832 CA CYS A 221 26.846 28.683 26.685 1.00 22.05 AAAB C ATOM 1833 C CYS A 221 27.402 27.357 26.179 1.00 24.54 AAAB C ATOM 1834 O CYS A 221 28.299 26.782 26.795 1.00 26.43 AAAB O ATOM 1835 CB CYS A 221 27.963 29.544 27.291 1.00 25.29 AAAB C ATOM 1836 SG CYS A 221 28.924 30.501 26.136 1.00 40.72 AAAB S ATOM 1837 N HIS A 222 26.928 26.909 25.019 1.00 27.25 AAAB N ATOM 1838 CA HIS A 222 27.363 25.623 24.477 1.00 25.08 AAAB C ATOM 1839 C HIS A 222 27.955 25.594 23.068 1.00 25.27 AAAB C ATOM 1840 O HIS A 222 27.721 26.484 22.248 1.00 28.50 AAAB O ATOM 1841 CB HIS A 222 26.209 24.638 24.539 1.00 19.38 AAAB C ATOM 1842 CG HIS A 222 24.986 25.105 23.813 1.00 18.23 AAAB C ATOM 1843 ND1 HIS A 222 23.948 25.747 24.450 1.00 11.87 AAAB N ATOM 1844 CD2 HIS A 222 24.622 24.990 22.515 1.00 12.15 AAAB C ATOM 1845 CE1 HIS A 222 22.991 26.003 23.577 1.00 13.71 AAAB C ATOM 1846 NE2 HIS A 222 23.375 25.551 22.394 1.00 12.33 AAAB N ATOM 1847 N VAL A 223 28.664 24.509 22.788 1.00 25.29 AAAB N ATOM 1848 CA VAL A 223 29.305 24.275 21.507 1.00 26.30 AAAB C ATOM 1849 C VAL A 223 29.062 22.817 21.151 1.00 28.18 AAAB C ATOM 1850 O VAL A 223 28.957 21.971 22.042 1.00 29.93 AAAB O ATOM 1851 CB VAL A 223 30.841 24.479 21.601 1.00 26.32 AAAB C ATOM 1852 CG1 VAL A 223 31.512 24.031 20.325 1.00 30.68 AAAB C ATOM 1853 CG2 VAL A 223 31.177 25.938 21.850 1.00 27.88 AAAB C ATOM 1854 N TYR A 224 28.922 22.539 19.856 1.00 27.71 AAAB N ATOM 1855 CA TYR A 224 28.746 21.174 19.354 1.00 23.59 AAAB C ATOM 1856 C TYR A 224 30.145 20.586 19.169 1.00 19.88 AAAB C ATOM 1857 O TYR A 224 31.009 21.217 18.558 1.00 23.44 AAAB O ATOM 1858 CB TYR A 224 27.999 21.179 18.021 1.00 22.85 AAAB C ATOM 1859 CG TYR A 224 26.503 21.260 18.174 1.00 29.27 AAAB C ATOM 1860 CD1 TYR A 224 25.798 20.257 18.843 1.00 31.18 AAAB C ATOM 1861 CD2 TYR A 224 25.789 22.342 17.671 1.00 33.33 AAAB C ATOM 1862 CE1 TYR A 224 24.417 20.334 19.009 1.00 32.83 AAAB C ATOM 1863 CE2 TYR A 224 24.405 22.429 17.831 1.00 35.21 AAAB C ATOM 1864 CZ TYR A 224 23.730 21.425 18.502 1.00 37.05 AAAB C ATOM 1865 OH TYR A 224 22.370 21.527 18.674 1.00 45.59 AAAB O ATOM 1866 N THR A 225 30.367 19.375 19.663 1.00 17.62 AAAB N ATOM 1867 CA THR A 225 31.685 18.747 19.572 1.00 17.85 AAAB C ATOM 1868 C THR A 225 32.260 18.687 18.156 1.00 14.05 AAAB C ATOM 1869 O THR A 225 33.467 18.862 17.951 1.00 11.59 AAAB O ATOM 1870 CB THR A 225 31.696 17.333 20.223 1.00 20.24 AAAB C ATOM 1871 OG1 THR A 225 30.803 16.456 19.524 1.00 22.91 AAAB O ATOM 1872 CG2 THR A 225 31.258 17.422 21.675 1.00 18.67 AAAB C ATOM 1873 N ARG A 226 31.391 18.484 17.175 1.00 12.26 AAAB N ATOM 1874 CA ARG A 226 31.817 18.410 15.786 1.00 15.78 AAAB C ATOM 1875 C ARG A 226 32.493 19.699 15.322 1.00 18.82 AAAB C ATOM 1876 O ARG A 226 33.387 19.667 14.471 1.00 22.05 AAAB O ATOM 1877 CB ARG A 226 30.621 18.082 14.887 1.00 14.72 AAAB C ATOM 1878 CG ARG A 226 30.915 18.117 13.394 1.00 19.61 AAAB C ATOM 1879 CD ARG A 226 29.807 17.441 12.597 1.00 22.66 AAAB C ATOM 1880 NE ARG A 226 29.941 15.981 12.587 1.00 29.92 AAAB N ATOM 1881 CZ ARG A 226 29.113 15.156 11.952 1.00 27.44 AAAB C ATOM 1882 NH1 ARG A 226 28.082 15.632 11.271 1.00 30.07 AAAB N ATOM 1883 NH2 ARG A 226 29.317 13.850 11.998 1.00 31.59 AAAB N ATOM 1884 N HIS A 227 32.100 20.822 15.922 1.00 15.85 AAAB N ATOM 1885 CA HIS A 227 32.639 22.133 15.559 1.00 11.66 AAAB C ATOM 1886 C HIS A 227 33.997 22.426 16.167 1.00 11.82 AAAB C ATOM 1887 O HIS A 227 34.781 23.168 15.591 1.00 14.72 AAAB O ATOM 1888 CB HIS A 227 31.669 23.237 15.967 1.00 4.83 AAAB C ATOM 1889 CG HIS A 227 30.341 23.171 15.274 1.00 4.30 AAAB C ATOM 1890 ND1 HIS A 227 29.215 23.785 15.770 1.00 3.05 AAAB N ATOM 1891 CD2 HIS A 227 29.971 22.593 14.109 1.00 2.60 AAAB C ATOM 1892 CE1 HIS A 227 28.206 23.594 14.943 1.00 3.28 AAAB C ATOM 1893 NE2 HIS A 227 28.638 22.873 13.924 1.00 4.06 AAAB N ATOM 1894 N ILE A 228 34.316 21.764 17.269 1.00 14.12 AAAB N ATOM 1895 CA ILE A 228 35.566 22.018 17.982 1.00 15.00 AAAB C ATOM 1896 C ILE A 228 36.837 22.119 17.155 1.00 15.71 AAAB C ATOM 1897 O ILE A 228 37.660 23.004 17.393 1.00 16.56 AAAB O ATOM 1898 CB ILE A 228 35.745 21.049 19.179 1.00 12.40 AAAB C ATOM 1899 CG1 ILE A 228 34.635 21.300 20.206 1.00 8.41 AAAB C ATOM 1900 CG2 ILE A 228 37.085 21.271 19.853 1.00 13.42 AAAB C ATOM 1901 CD1 ILE A 228 34.789 20.501 21.467 1.00 9.79 AAAB C ATOM 1902 N ASP A 229 36.988 21.253 16.161 1.00 22.39 AAAB N ATOM 1903 CA ASP A 229 38.185 21.278 15.324 1.00 22.17 AAAB C ATOM 1904 C ASP A 229 38.366 22.602 14.610 1.00 23.23 AAAB C ATOM 1905 O ASP A 229 39.438 23.200 14.679 1.00 24.02 AAAB O ATOM 1906 CB ASP A 229 38.156 20.147 14.299 1.00 24.46 AAAB C ATOM 1907 CG ASP A 229 38.401 18.798 14.923 1.00 22.17 AAAB C ATOM 1908 OD1 ASP A 229 39.219 18.723 15.862 1.00 23.21 AAAB O ATOM 1909 OD2 ASP A 229 37.777 17.817 14.467 1.00 21.75 AAAB O ATOM 1910 N ASN A 230 37.328 23.033 13.899 1.00 23.61 AAAB N ATOM 1911 CA ASN A 230 37.357 24.293 13.167 1.00 22.43 AAAB C ATOM 1912 C ASN A 230 37.431 25.469 14.121 1.00 24.40 AAAB C ATOM 1913 O ASN A 230 38.148 26.433 13.874 1.00 27.96 AAAB O ATOM 1914 CB ASN A 230 36.118 24.425 12.295 1.00 21.50 AAAB C ATOM 1915 CG ASN A 230 36.259 23.700 10.984 1.00 22.58 AAAB C ATOM 1916 OD1 ASN A 230 37.328 23.162 10.669 1.00 19.08 AAAB O ATOM 1917 ND2 ASN A 230 35.189 23.694 10.197 1.00 16.33 AAAB N ATOM 1918 N LEU A 231 36.672 25.383 15.206 1.00 23.03 AAAB N ATOM 1919 CA LEU A 231 36.641 26.418 16.229 1.00 23.76 AAAB C ATOM 1920 C LEU A 231 38.063 26.641 16.735 1.00 26.45 AAAB C ATOM 1921 O LEU A 231 38.454 27.771 17.028 1.00 30.50 AAAB O ATOM 1922 CB LEU A 231 35.737 25.966 17.368 1.00 18.53 AAAB C ATOM 1923 CG LEU A 231 34.722 26.934 17.955 1.00 16.81 AAAB C ATOM 1924 CD1 LEU A 231 34.022 27.733 16.877 1.00 18.96 AAAB C ATOM 1925 CD2 LEU A 231 33.726 26.117 18.735 1.00 16.03 AAAB C ATOM 1926 N LYS A 232 38.844 25.565 16.798 1.00 28.28 AAAB N ATOM 1927 CA LYS A 232 40.232 25.652 17.244 1.00 31.05 AAAB C ATOM 1928 C LYS A 232 41.111 26.269 16.156 1.00 29.71 AAAB C ATOM 1929 O LYS A 232 42.108 26.932 16.454 1.00 29.93 AAAB O ATOM 1930 CB LYS A 232 40.747 24.272 17.681 1.00 32.08 AAAB C ATOM 1931 CG LYS A 232 40.045 23.756 18.941 1.00 35.53 AAAB C ATOM 1932 CD LYS A 232 40.425 22.330 19.304 1.00 39.50 AAAB C ATOM 1933 CE LYS A 232 41.849 22.248 19.818 1.00 47.10 AAAB C ATOM 1934 NZ LYS A 232 42.247 20.850 20.156 1.00 49.09 AAAB N ATOM 1935 N ILE A 233 40.715 26.068 14.900 1.00 29.60 AAAB N ATOM 1936 CA ILE A 233 41.429 26.626 13.754 1.00 32.35 AAAB C ATOM 1937 C ILE A 233 41.128 28.125 13.713 1.00 33.94 AAAB C ATOM 1938 O ILE A 233 42.018 28.947 13.470 1.00 36.28 AAAB O ATOM 1939 CB ILE A 233 40.952 25.996 12.419 1.00 31.86 AAAB C ATOM 1940 CG1 ILE A 233 41.345 24.517 12.348 1.00 32.59 AAAB C ATOM 1941 CG2 ILE A 233 41.521 26.765 11.241 1.00 30.57 AAAB C ATOM 1942 CD1 ILE A 233 42.839 24.258 12.373 1.00 30.00 AAAB C ATOM 1943 N GLN A 234 39.875 28.465 14.000 1.00 31.71 AAAB N ATOM 1944 CA GLN A 234 39.412 29.844 14.012 1.00 29.50 AAAB C ATOM 1945 C GLN A 234 40.153 30.655 15.062 1.00 29.19 AAAB C ATOM 1946 O GLN A 234 40.482 31.811 14.827 1.00 32.66 AAAB O ATOM 1947 CB GLN A 234 37.903 29.899 14.277 1.00 30.20 AAAB C ATOM 1948 CG GLN A 234 37.282 31.260 14.011 1.00 31.34 AAAB C ATOM 1949 CD GLN A 234 35.794 31.312 14.304 1.00 29.56 AAAB C ATOM 1950 OE1 GLN A 234 35.115 30.290 14.358 1.00 28.29 AAAB O ATOM 1951 NE2 GLN A 234 35.277 32.521 14.478 1.00 34.56 AAAB N ATOM 1952 N MET A 235 40.452 30.039 16.203 1.00 28.64 AAAB N ATOM 1953 CA MET A 235 41.158 30.736 17.274 1.00 28.83 AAAB C ATOM 1954 C MET A 235 42.591 31.098 16.920 1.00 31.29 AAAB C ATOM 1955 O MET A 235 43.253 31.816 17.664 1.00 31.31 AAAB O ATOM 1956 CB MET A 235 41.129 29.920 18.569 1.00 30.85 AAAB C ATOM 1957 CG MET A 235 39.775 29.899 19.269 1.00 28.78 AAAB C ATOM 1958 SD MET A 235 39.796 28.893 20.760 1.00 38.26 AAAB S ATOM 1959 CE MET A 235 40.789 29.906 21.848 1.00 32.61 AAAB C ATOM 1960 N GLU A 236 43.085 30.576 15.803 1.00 35.29 AAAB N ATOM 1961 CA GLU A 236 44.445 30.877 15.368 1.00 38.26 AAAB C ATOM 1962 C GLU A 236 44.436 31.859 14.200 1.00 37.27 AAAB C ATOM 1963 O GLU A 236 45.477 32.417 13.841 1.00 35.79 AAAB O ATOM 1964 CB GLU A 236 45.182 29.594 14.975 1.00 44.61 AAAB C ATOM 1965 CG GLU A 236 45.492 28.662 16.143 1.00 54.57 AAAB C ATOM 1966 CD GLU A 236 46.432 29.283 17.169 1.00 59.68 AAAB C ATOM 1967 OE1 GLU A 236 47.662 29.257 16.944 1.00 62.29 AAAB O ATOM 1968 OE2 GLU A 236 45.940 29.789 18.204 1.00 64.14 AAAB O ATOM 1969 N ARG A 237 43.260 32.059 13.607 1.00 34.95 AAAB N ATOM 1970 CA ARG A 237 43.105 32.975 12.486 1.00 35.58 AAAB C ATOM 1971 C ARG A 237 43.321 34.433 12.898 1.00 37.58 AAAB C ATOM 1972 O ARG A 237 42.981 34.840 14.008 1.00 39.71 AAAB O ATOM 1973 CB ARG A 237 41.743 32.770 11.807 1.00 29.41 AAAB C ATOM 1974 CG ARG A 237 41.874 32.049 10.469 1.00 34.04 AAAB C ATOM 1975 CD ARG A 237 40.801 30.996 10.211 1.00 29.48 AAAB C ATOM 1976 NE ARG A 237 39.515 31.568 9.825 1.00 31.13 AAAB N ATOM 1977 CZ ARG A 237 38.795 31.177 8.775 1.00 27.20 AAAB C ATOM 1978 NH1 ARG A 237 39.231 30.212 7.979 1.00 26.65 AAAB N ATOM 1979 NH2 ARG A 237 37.605 31.714 8.555 1.00 24.29 AAAB N ATOM 1980 N GLU A 238 43.926 35.195 11.991 1.00 42.30 AAAB N ATOM 1981 CA GLU A 238 44.246 36.614 12.182 1.00 42.38 AAAB C ATOM 1982 C GLU A 238 43.016 37.453 12.502 1.00 41.77 AAAB C ATOM 1983 O GLU A 238 41.943 37.247 11.929 1.00 40.48 AAAB O ATOM 1984 CB GLU A 238 44.909 37.203 10.925 1.00 45.03 AAAB C ATOM 1985 CG GLU A 238 45.753 36.240 10.084 1.00 48.83 AAAB C ATOM 1986 CD GLU A 238 44.911 35.241 9.292 1.00 50.33 AAAB C ATOM 1987 OE1 GLU A 238 43.904 35.653 8.666 1.00 47.87 AAAB O ATOM 1988 OE2 GLU A 238 45.248 34.036 9.319 1.00 54.30 AAAB O ATOM 1989 N GLN A 239 43.195 38.430 13.385 1.00 43.12 AAAB N ATOM 1990 CA GLN A 239 42.116 39.328 13.786 1.00 46.09 AAAB C ATOM 1991 C GLN A 239 42.432 40.734 13.280 1.00 44.78 AAAB C ATOM 1992 O GLN A 239 43.521 41.256 13.523 1.00 43.60 AAAB O ATOM 1993 CB GLN A 239 41.979 39.346 15.310 1.00 49.09 AAAB C ATOM 1994 CG GLN A 239 41.753 37.977 15.942 1.00 53.16 AAAB C ATOM 1995 CD GLN A 239 41.700 38.028 17.459 1.00 55.70 AAAB C ATOM 1996 OE1 GLN A 239 41.682 39.104 18.055 1.00 56.35 AAAB O ATOM 1997 NE2 GLN A 239 41.654 36.862 18.090 1.00 60.40 AAAB N ATOM 1998 N PHE A 240 41.494 41.331 12.555 1.00 45.11 AAAB N ATOM 1999 CA PHE A 240 41.677 42.675 12.013 1.00 44.69 AAAB C ATOM 2000 C PHE A 240 40.971 43.711 12.870 1.00 44.59 AAAB C ATOM 2001 O PHE A 240 40.322 43.371 13.862 1.00 44.33 AAAB O ATOM 2002 CB PHE A 240 41.095 42.756 10.604 1.00 46.08 AAAB C ATOM 2003 CG PHE A 240 41.473 41.610 9.724 1.00 48.87 AAAB C ATOM 2004 CD1 PHE A 240 42.754 41.519 9.190 1.00 49.06 AAAB C ATOM 2005 CD2 PHE A 240 40.547 40.619 9.430 1.00 47.53 AAAB C ATOM 2006 CE1 PHE A 240 43.106 40.458 8.375 1.00 47.93 AAAB C ATOM 2007 CE2 PHE A 240 40.887 39.556 8.618 1.00 50.14 AAAB C ATOM 2008 CZ PHE A 240 42.171 39.473 8.088 1.00 51.02 AAAB C ATOM 2009 N GLU A 241 41.110 44.977 12.484 1.00 46.35 AAAB N ATOM 2010 CA GLU A 241 40.453 46.080 13.180 1.00 43.71 AAAB C ATOM 2011 C GLU A 241 38.980 46.013 12.809 1.00 38.63 AAAB C ATOM 2012 O GLU A 241 38.638 45.667 11.680 1.00 37.57 AAAB O ATOM 2013 CB GLU A 241 41.025 47.420 12.732 1.00 49.20 AAAB C ATOM 2014 CG GLU A 241 42.473 47.645 13.121 1.00 56.91 AAAB C ATOM 2015 CD GLU A 241 42.887 49.100 12.994 1.00 63.54 AAAB C ATOM 2016 OE1 GLU A 241 42.166 49.880 12.329 1.00 66.28 AAAB O ATOM 2017 OE2 GLU A 241 43.934 49.469 13.568 1.00 68.71 AAAB O ATOM 2018 N ALA A 242 38.110 46.353 13.749 1.00 32.92 AAAB N ATOM 2019 CA ALA A 242 36.680 46.296 13.494 1.00 31.76 AAAB C ATOM 2020 C ALA A 242 36.292 47.218 12.351 1.00 31.62 AAAB C ATOM 2021 O ALA A 242 36.950 48.231 12.125 1.00 35.87 AAAB O ATOM 2022 CB ALA A 242 35.922 46.677 14.750 1.00 34.44 AAAB C ATOM 2023 N PRO A 243 35.262 46.848 11.569 1.00 32.24 AAAB N ATOM 2024 CA PRO A 243 34.834 47.702 10.459 1.00 31.51 AAAB C ATOM 2025 C PRO A 243 33.974 48.846 11.005 1.00 35.86 AAAB C ATOM 2026 O PRO A 243 33.644 48.884 12.198 1.00 39.94 AAAB O ATOM 2027 CB PRO A 243 33.999 46.750 9.611 1.00 27.56 AAAB C ATOM 2028 CG PRO A 243 33.354 45.901 10.636 1.00 28.70 AAAB C ATOM 2029 CD PRO A 243 34.512 45.580 11.560 1.00 30.32 AAAB C ATOM 2030 N GLU A 244 33.600 49.775 10.140 1.00 35.02 AAAB N ATOM 2031 CA GLU A 244 32.777 50.888 10.569 1.00 34.76 AAAB C ATOM 2032 C GLU A 244 31.347 50.662 10.129 1.00 28.95 AAAB C ATOM 2033 O GLU A 244 31.099 50.264 9.002 1.00 28.21 AAAB O ATOM 2034 CB GLU A 244 33.305 52.205 10.001 1.00 41.58 AAAB C ATOM 2035 CG GLU A 244 34.717 52.531 10.473 1.00 54.01 AAAB C ATOM 2036 CD GLU A 244 35.176 53.919 10.074 1.00 61.69 AAAB C ATOM 2037 OE1 GLU A 244 34.667 54.458 9.064 1.00 63.31 AAAB O ATOM 2038 OE2 GLU A 244 36.052 54.470 10.776 1.00 66.09 AAAB O ATOM 2039 N LEU A 245 30.408 50.846 11.041 1.00 24.33 AAAB N ATOM 2040 CA LEU A 245 29.015 50.678 10.696 1.00 21.53 AAAB C ATOM 2041 C LEU A 245 28.436 52.063 10.403 1.00 23.82 AAAB C ATOM 2042 O LEU A 245 28.549 52.975 11.226 1.00 27.73 AAAB O ATOM 2043 CB LEU A 245 28.263 50.000 11.845 1.00 17.73 AAAB C ATOM 2044 CG LEU A 245 26.737 49.935 11.739 1.00 17.49 AAAB C ATOM 2045 CD1 LEU A 245 26.310 49.104 10.529 1.00 16.76 AAAB C ATOM 2046 CD2 LEU A 245 26.180 49.348 13.016 1.00 16.66 AAAB C ATOM 2047 N TRP A 246 27.893 52.235 9.203 1.00 21.03 AAAB N ATOM 2048 CA TRP A 246 27.279 53.491 8.805 1.00 16.39 AAAB C ATOM 2049 C TRP A 246 25.779 53.353 8.939 1.00 15.56 AAAB C ATOM 2050 O TRP A 246 25.197 52.375 8.476 1.00 20.35 AAAB O ATOM 2051 CB TRP A 246 27.613 53.833 7.344 1.00 19.53 AAAB C ATOM 2052 CG TRP A 246 26.870 55.055 6.807 1.00 17.71 AAAB C ATOM 2053 CD1 TRP A 246 27.231 56.361 6.963 1.00 16.83 AAAB C ATOM 2054 CD2 TRP A 246 25.632 55.068 6.073 1.00 12.71 AAAB C ATOM 2055 NE1 TRP A 246 26.294 57.183 6.385 1.00 14.36 AAAB N ATOM 2056 CE2 TRP A 246 25.305 56.418 5.830 1.00 10.18 AAAB C ATOM 2057 CE3 TRP A 246 24.765 54.073 5.604 1.00 16.58 AAAB C ATOM 2058 CZ2 TRP A 246 24.151 56.800 5.140 1.00 10.64 AAAB C ATOM 2059 CZ3 TRP A 246 23.608 54.457 4.915 1.00 14.49 AAAB C ATOM 2060 CH2 TRP A 246 23.318 55.809 4.693 1.00 8.64 AAAB C ATOM 2061 N ILE A 247 25.156 54.326 9.588 1.00 21.01 AAAB N ATOM 2062 CA ILE A 247 23.707 54.347 9.751 1.00 21.39 AAAB C ATOM 2063 C ILE A 247 23.276 55.740 9.273 1.00 22.10 AAAB C ATOM 2064 O ILE A 247 23.987 56.725 9.496 1.00 16.47 AAAB O ATOM 2065 CB ILE A 247 23.274 54.129 11.230 1.00 20.84 AAAB C ATOM 2066 CG1 ILE A 247 23.796 52.783 11.746 1.00 21.58 AAAB C ATOM 2067 CG2 ILE A 247 21.750 54.160 11.343 1.00 18.62 AAAB C ATOM 2068 CD1 ILE A 247 23.371 52.466 13.158 1.00 17.76 AAAB C ATOM 2069 N ASN A 248 22.162 55.797 8.547 1.00 22.22 AAAB N ATOM 2070 CA ASN A 248 21.634 57.051 8.023 1.00 24.16 AAAB C ATOM 2071 C ASN A 248 21.393 58.049 9.155 1.00 25.61 AAAB C ATOM 2072 O ASN A 248 20.379 57.971 9.855 1.00 24.33 AAAB O ATOM 2073 CB ASN A 248 20.333 56.797 7.253 1.00 23.44 AAAB C ATOM 2074 CG ASN A 248 19.866 58.012 6.462 1.00 26.43 AAAB C ATOM 2075 OD1 ASN A 248 20.573 59.019 6.352 1.00 26.75 AAAB O ATOM 2076 ND2 ASN A 248 18.665 57.922 5.906 1.00 30.30 AAAB N ATOM 2077 N PRO A 249 22.288 59.049 9.290 1.00 25.79 AAAB N ATOM 2078 CA PRO A 249 22.223 60.092 10.323 1.00 24.36 AAAB C ATOM 2079 C PRO A 249 20.945 60.918 10.254 1.00 26.79 AAAB C ATOM 2080 O PRO A 249 20.562 61.563 11.226 1.00 31.86 AAAB O ATOM 2081 CB PRO A 249 23.442 60.965 10.008 1.00 22.53 AAAB C ATOM 2082 CG PRO A 249 24.352 60.055 9.193 1.00 19.71 AAAB C ATOM 2083 CD PRO A 249 23.371 59.339 8.332 1.00 21.95 AAAB C ATOM 2084 N GLU A 250 20.295 60.902 9.096 1.00 26.71 AAAB N ATOM 2085 CA GLU A 250 19.074 61.665 8.892 1.00 25.69 AAAB C ATOM 2086 C GLU A 250 17.839 61.039 9.506 1.00 24.24 AAAB C ATOM 2087 O GLU A 250 16.812 61.698 9.627 1.00 26.47 AAAB O ATOM 2088 CB GLU A 250 18.832 61.881 7.397 1.00 31.38 AAAB C ATOM 2089 CG GLU A 250 19.956 62.619 6.678 1.00 35.67 AAAB C ATOM 2090 CD GLU A 250 19.612 62.974 5.243 1.00 36.49 AAAB C ATOM 2091 OE1 GLU A 250 18.467 62.726 4.807 1.00 38.17 AAAB O ATOM 2092 OE2 GLU A 250 20.493 63.517 4.550 1.00 43.52 AAAB O ATOM 2093 N VAL A 251 17.914 59.761 9.864 1.00 26.44 AAAB N ATOM 2094 CA VAL A 251 16.761 59.081 10.448 1.00 23.59 AAAB C ATOM 2095 C VAL A 251 16.542 59.505 11.901 1.00 22.17 AAAB C ATOM 2096 O VAL A 251 17.407 59.324 12.756 1.00 16.26 AAAB O ATOM 2097 CB VAL A 251 16.885 57.542 10.332 1.00 24.50 AAAB C ATOM 2098 CG1 VAL A 251 15.599 56.862 10.849 1.00 21.62 AAAB C ATOM 2099 CG2 VAL A 251 17.151 57.158 8.883 1.00 15.73 AAAB C ATOM 2100 N LYS A 252 15.364 60.063 12.155 1.00 24.68 AAAB N ATOM 2101 CA LYS A 252 14.990 60.559 13.472 1.00 30.84 AAAB C ATOM 2102 C LYS A 252 13.845 59.771 14.089 1.00 30.71 AAAB C ATOM 2103 O LYS A 252 13.552 59.924 15.274 1.00 31.06 AAAB O ATOM 2104 CB LYS A 252 14.574 62.031 13.371 1.00 37.12 AAAB C ATOM 2105 CG LYS A 252 15.652 62.969 12.842 1.00 47.18 AAAB C ATOM 2106 CD LYS A 252 16.842 63.021 13.785 1.00 55.20 AAAB C ATOM 2107 CE LYS A 252 17.862 64.047 13.325 1.00 62.79 AAAB C ATOM 2108 NZ LYS A 252 18.914 64.259 14.361 1.00 68.57 AAAB N ATOM 2109 N ASP A 253 13.134 59.010 13.265 1.00 28.24 AAAB N ATOM 2110 CA ASP A 253 12.031 58.199 13.755 1.00 25.51 AAAB C ATOM 2111 C ASP A 253 12.395 56.728 13.607 1.00 25.47 AAAB C ATOM 2112 O ASP A 253 12.743 56.274 12.516 1.00 24.85 AAAB O ATOM 2113 CB ASP A 253 10.746 58.514 12.990 1.00 28.96 AAAB C ATOM 2114 CG ASP A 253 9.598 57.586 13.357 1.00 31.79 AAAB C ATOM 2115 OD1 ASP A 253 9.427 57.278 14.553 1.00 37.95 AAAB O ATOM 2116 OD2 ASP A 253 8.861 57.164 12.443 1.00 39.32 AAAB O ATOM 2117 N PHE A 254 12.288 55.993 14.712 1.00 24.61 AAAB N ATOM 2118 CA PHE A 254 12.604 54.566 14.767 1.00 19.36 AAAB C ATOM 2119 C PHE A 254 11.972 53.768 13.639 1.00 20.30 AAAB C ATOM 2120 O PHE A 254 12.615 52.917 13.014 1.00 18.94 AAAB O ATOM 2121 CB PHE A 254 12.139 53.988 16.104 1.00 16.03 AAAB C ATOM 2122 CG PHE A 254 12.426 52.527 16.264 1.00 8.27 AAAB C ATOM 2123 CD1 PHE A 254 13.732 52.081 16.460 1.00 9.58 AAAB C ATOM 2124 CD2 PHE A 254 11.400 51.596 16.204 1.00 11.04 AAAB C ATOM 2125 CE1 PHE A 254 14.011 50.722 16.594 1.00 11.10 AAAB C ATOM 2126 CE2 PHE A 254 11.666 50.233 16.334 1.00 13.78 AAAB C ATOM 2127 CZ PHE A 254 12.976 49.796 16.529 1.00 10.65 AAAB C ATOM 2128 N TYR A 255 10.703 54.054 13.388 1.00 20.90 AAAB N ATOM 2129 CA TYR A 255 9.951 53.365 12.360 1.00 22.68 AAAB C ATOM 2130 C TYR A 255 10.266 53.826 10.947 1.00 24.07 AAAB C ATOM 2131 O TYR A 255 9.558 53.465 10.015 1.00 29.38 AAAB O ATOM 2132 CB TYR A 255 8.456 53.481 12.659 1.00 23.68 AAAB C ATOM 2133 CG TYR A 255 8.116 52.940 14.030 1.00 27.92 AAAB C ATOM 2134 CD1 TYR A 255 8.361 51.603 14.350 1.00 28.19 AAAB C ATOM 2135 CD2 TYR A 255 7.623 53.774 15.029 1.00 28.13 AAAB C ATOM 2136 CE1 TYR A 255 8.138 51.114 15.632 1.00 30.33 AAAB C ATOM 2137 CE2 TYR A 255 7.396 53.292 16.319 1.00 31.69 AAAB C ATOM 2138 CZ TYR A 255 7.661 51.961 16.612 1.00 30.09 AAAB C ATOM 2139 OH TYR A 255 7.498 51.484 17.889 1.00 27.70 AAAB O ATOM 2140 N ASP A 256 11.339 54.597 10.779 1.00 22.13 AAAB N ATOM 2141 CA ASP A 256 11.720 55.074 9.456 1.00 25.22 AAAB C ATOM 2142 C ASP A 256 13.016 54.460 8.934 1.00 26.55 AAAB C ATOM 2143 O ASP A 256 13.446 54.763 7.820 1.00 33.80 AAAB O ATOM 2144 CB ASP A 256 11.796 56.606 9.424 1.00 29.77 AAAB C ATOM 2145 CG ASP A 256 10.431 57.263 9.201 1.00 31.60 AAAB C ATOM 2146 OD1 ASP A 256 9.482 56.584 8.750 1.00 33.58 AAAB O ATOM 2147 OD2 ASP A 256 10.313 58.476 9.459 1.00 34.92 AAAB O ATOM 2148 N PHE A 257 13.657 53.623 9.747 1.00 25.56 AAAB N ATOM 2149 CA PHE A 257 14.889 52.943 9.339 1.00 19.85 AAAB C ATOM 2150 C PHE A 257 14.533 51.869 8.309 1.00 19.15 AAAB C ATOM 2151 O PHE A 257 13.492 51.217 8.420 1.00 18.03 AAAB O ATOM 2152 CB PHE A 257 15.553 52.252 10.532 1.00 13.11 AAAB C ATOM 2153 CG PHE A 257 16.318 53.172 11.429 1.00 9.06 AAAB C ATOM 2154 CD1 PHE A 257 17.529 53.716 11.020 1.00 11.79 AAAB C ATOM 2155 CD2 PHE A 257 15.861 53.448 12.712 1.00 10.27 AAAB C ATOM 2156 CE1 PHE A 257 18.279 54.524 11.888 1.00 14.66 AAAB C ATOM 2157 CE2 PHE A 257 16.605 54.255 13.587 1.00 9.24 AAAB C ATOM 2158 CZ PHE A 257 17.812 54.791 13.179 1.00 6.35 AAAB C ATOM 2159 N THR A 258 15.383 51.701 7.305 1.00 17.10 AAAB N ATOM 2160 CA THR A 258 15.174 50.684 6.283 1.00 18.51 AAAB C ATOM 2161 C THR A 258 16.500 49.951 6.180 1.00 19.41 AAAB C ATOM 2162 O THR A 258 17.515 50.396 6.732 1.00 18.11 AAAB O ATOM 2163 CB THR A 258 14.836 51.279 4.890 1.00 23.65 AAAB C ATOM 2164 OG1 THR A 258 16.027 51.792 4.273 1.00 28.65 AAAB O ATOM 2165 CG2 THR A 258 13.795 52.381 5.005 1.00 21.88 AAAB C ATOM 2166 N ILE A 259 16.511 48.851 5.445 1.00 19.00 AAAB N ATOM 2167 CA ILE A 259 17.729 48.066 5.293 1.00 21.54 AAAB C ATOM 2168 C ILE A 259 18.799 48.877 4.565 1.00 20.43 AAAB C ATOM 2169 O ILE A 259 19.998 48.665 4.761 1.00 20.25 AAAB O ATOM 2170 CB ILE A 259 17.447 46.712 4.561 1.00 23.01 AAAB C ATOM 2171 CG1 ILE A 259 18.739 45.913 4.372 1.00 23.99 AAAB C ATOM 2172 CG2 ILE A 259 16.773 46.958 3.222 1.00 26.45 AAAB C ATOM 2173 CD1 ILE A 259 19.366 45.450 5.666 1.00 26.23 AAAB C ATOM 2174 N ASP A 260 18.358 49.861 3.787 1.00 20.96 AAAB N ATOM 2175 CA ASP A 260 19.286 50.694 3.032 1.00 22.98 AAAB C ATOM 2176 C ASP A 260 20.091 51.649 3.906 1.00 23.96 AAAB C ATOM 2177 O ASP A 260 21.219 52.007 3.561 1.00 25.28 AAAB O ATOM 2178 CB ASP A 260 18.536 51.487 1.961 1.00 22.12 AAAB C ATOM 2179 CG ASP A 260 17.954 50.597 0.876 1.00 25.70 AAAB C ATOM 2180 OD1 ASP A 260 18.702 49.765 0.310 1.00 24.79 AAAB O ATOM 2181 OD2 ASP A 260 16.743 50.728 0.594 1.00 26.01 AAAB O ATOM 2182 N ASP A 261 19.530 52.008 5.060 1.00 26.36 AAAB N ATOM 2183 CA ASP A 261 20.165 52.947 5.993 1.00 25.12 AAAB C ATOM 2184 C ASP A 261 21.367 52.394 6.759 1.00 22.58 AAAB C ATOM 2185 O ASP A 261 21.977 53.106 7.556 1.00 23.57 AAAB O ATOM 2186 CB ASP A 261 19.124 53.502 6.983 1.00 24.62 AAAB C ATOM 2187 CG ASP A 261 17.958 54.214 6.287 1.00 24.21 AAAB C ATOM 2188 OD1 ASP A 261 18.163 54.850 5.231 1.00 28.51 AAAB O ATOM 2189 OD2 ASP A 261 16.827 54.143 6.804 1.00 27.86 AAAB O ATOM 2190 N PHE A 262 21.726 51.145 6.495 1.00 22.86 AAAB N ATOM 2191 CA PHE A 262 22.847 50.517 7.177 1.00 20.31 AAAB C ATOM 2192 C PHE A 262 23.869 50.030 6.167 1.00 22.26 AAAB C ATOM 2193 O PHE A 262 23.508 49.515 5.111 1.00 24.80 AAAB O ATOM 2194 CB PHE A 262 22.369 49.307 7.985 1.00 19.37 AAAB C ATOM 2195 CG PHE A 262 21.263 49.608 8.939 1.00 12.65 AAAB C ATOM 2196 CD1 PHE A 262 19.939 49.510 8.537 1.00 13.32 AAAB C ATOM 2197 CD2 PHE A 262 21.541 49.969 10.245 1.00 12.39 AAAB C ATOM 2198 CE1 PHE A 262 18.909 49.768 9.426 1.00 16.12 AAAB C ATOM 2199 CE2 PHE A 262 20.524 50.227 11.138 1.00 13.81 AAAB C ATOM 2200 CZ PHE A 262 19.203 50.126 10.731 1.00 13.30 AAAB C ATOM 2201 N LYS A 263 25.142 50.132 6.520 1.00 20.51 AAAB N ATOM 2202 CA LYS A 263 26.198 49.684 5.639 1.00 23.75 AAAB C ATOM 2203 C LYS A 263 27.460 49.475 6.445 1.00 25.11 AAAB C ATOM 2204 O LYS A 263 27.890 50.369 7.166 1.00 24.52 AAAB O ATOM 2205 CB LYS A 263 26.449 50.721 4.545 1.00 30.13 AAAB C ATOM 2206 CG LYS A 263 26.943 50.125 3.236 1.00 35.64 AAAB C ATOM 2207 CD LYS A 263 28.391 50.487 2.941 1.00 36.19 AAAB C ATOM 2208 CE LYS A 263 28.780 50.002 1.544 1.00 37.64 AAAB C ATOM 2209 NZ LYS A 263 30.108 50.513 1.094 1.00 37.08 AAAB N ATOM 2210 N LEU A 264 28.000 48.265 6.406 1.00 26.29 AAAB N ATOM 2211 CA LEU A 264 29.227 47.989 7.133 1.00 30.45 AAAB C ATOM 2212 C LEU A 264 30.333 48.415 6.177 1.00 29.64 AAAB C ATOM 2213 O LEU A 264 30.292 48.084 4.996 1.00 31.77 AAAB O ATOM 2214 CB LEU A 264 29.316 46.501 7.492 1.00 34.99 AAAB C ATOM 2215 CG LEU A 264 29.941 46.136 8.845 1.00 30.86 AAAB C ATOM 2216 CD1 LEU A 264 29.190 46.811 9.973 1.00 25.71 AAAB C ATOM 2217 CD2 LEU A 264 29.907 44.638 9.028 1.00 32.98 AAAB C ATOM 2218 N ILE A 265 31.315 49.142 6.693 1.00 30.65 AAAB N ATOM 2219 CA ILE A 265 32.410 49.678 5.893 1.00 30.60 AAAB C ATOM 2220 C ILE A 265 33.780 49.136 6.279 1.00 36.21 AAAB C ATOM 2221 O ILE A 265 34.268 49.384 7.385 1.00 35.08 AAAB O ATOM 2222 CB ILE A 265 32.409 51.212 5.987 1.00 28.45 AAAB C ATOM 2223 CG1 ILE A 265 31.127 51.750 5.348 1.00 28.31 AAAB C ATOM 2224 CG2 ILE A 265 33.661 51.798 5.358 1.00 26.62 AAAB C ATOM 2225 CD1 ILE A 265 30.947 53.225 5.481 1.00 35.07 AAAB C ATOM 2226 N ASN A 266 34.401 48.432 5.332 1.00 41.26 AAAB N ATOM 2227 CA ASN A 266 35.719 47.811 5.492 1.00 42.93 AAAB C ATOM 2228 C ASN A 266 35.720 46.549 6.348 1.00 41.54 AAAB C ATOM 2229 O ASN A 266 36.585 46.360 7.208 1.00 40.08 AAAB O ATOM 2230 CB ASN A 266 36.743 48.814 6.024 1.00 48.35 AAAB C ATOM 2231 CG ASN A 266 37.679 49.301 4.950 1.00 57.01 AAAB C ATOM 2232 OD1 ASN A 266 37.312 49.366 3.772 1.00 59.36 AAAB O ATOM 2233 ND2 ASN A 266 38.902 49.642 5.342 1.00 61.55 AAAB N ATOM 2234 N TYR A 267 34.768 45.664 6.080 1.00 40.36 AAAB N ATOM 2235 CA TYR A 267 34.657 44.420 6.825 1.00 43.00 AAAB C ATOM 2236 C TYR A 267 35.642 43.359 6.325 1.00 44.15 AAAB C ATOM 2237 O TYR A 267 35.306 42.547 5.464 1.00 42.46 AAAB O ATOM 2238 CB TYR A 267 33.218 43.889 6.752 1.00 43.71 AAAB C ATOM 2239 CG TYR A 267 32.932 42.684 7.632 1.00 39.83 AAAB C ATOM 2240 CD1 TYR A 267 33.828 42.285 8.629 1.00 36.62 AAAB C ATOM 2241 CD2 TYR A 267 31.751 41.960 7.481 1.00 37.75 AAAB C ATOM 2242 CE1 TYR A 267 33.555 41.203 9.448 1.00 38.19 AAAB C ATOM 2243 CE2 TYR A 267 31.465 40.879 8.294 1.00 38.81 AAAB C ATOM 2244 CZ TYR A 267 32.369 40.505 9.278 1.00 42.58 AAAB C ATOM 2245 OH TYR A 267 32.063 39.449 10.102 1.00 44.77 AAAB O ATOM 2246 N LYS A 268 36.858 43.382 6.866 1.00 47.17 AAAB N ATOM 2247 CA LYS A 268 37.896 42.416 6.513 1.00 48.29 AAAB C ATOM 2248 C LYS A 268 37.729 41.219 7.445 1.00 49.83 AAAB C ATOM 2249 O LYS A 268 37.588 41.392 8.655 1.00 50.27 AAAB O ATOM 2250 CB LYS A 268 39.285 43.024 6.726 1.00 48.90 AAAB C ATOM 2251 CG LYS A 268 39.560 44.282 5.925 1.00 53.29 AAAB C ATOM 2252 CD LYS A 268 39.836 43.968 4.470 1.00 60.17 AAAB C ATOM 2253 CE LYS A 268 40.238 45.223 3.707 1.00 63.86 AAAB C ATOM 2254 NZ LYS A 268 40.794 44.896 2.361 1.00 69.90 AAAB N ATOM 2255 N HIS A 269 37.724 40.010 6.895 1.00 50.31 AAAB N ATOM 2256 CA HIS A 269 37.573 38.819 7.722 1.00 49.30 AAAB C ATOM 2257 C HIS A 269 38.492 37.654 7.356 1.00 49.20 AAAB C ATOM 2258 O HIS A 269 39.233 37.728 6.379 1.00 49.41 AAAB O ATOM 2259 CB HIS A 269 36.105 38.380 7.829 1.00 48.79 AAAB C ATOM 2260 CG HIS A 269 35.354 38.395 6.533 1.00 50.02 AAAB C ATOM 2261 ND1 HIS A 269 35.552 37.459 5.543 1.00 51.55 AAAB N ATOM 2262 CD2 HIS A 269 34.358 39.202 6.094 1.00 49.81 AAAB C ATOM 2263 CE1 HIS A 269 34.709 37.684 4.550 1.00 51.56 AAAB C ATOM 2264 NE2 HIS A 269 33.973 38.736 4.862 1.00 50.67 AAAB N ATOM 2265 N GLY A 270 38.418 36.587 8.148 1.00 51.29 AAAB N ATOM 2266 CA GLY A 270 39.259 35.409 7.978 1.00 53.20 AAAB C ATOM 2267 C GLY A 270 39.225 34.535 6.737 1.00 54.15 AAAB C ATOM 2268 O GLY A 270 40.272 34.319 6.123 1.00 56.33 AAAB O ATOM 2269 N ASP A 271 38.062 33.969 6.423 1.00 52.88 AAAB N ATOM 2270 CA ASP A 271 37.877 33.089 5.261 1.00 54.12 AAAB C ATOM 2271 C ASP A 271 36.668 32.212 5.538 1.00 52.99 AAAB C ATOM 2272 O ASP A 271 35.963 32.413 6.528 1.00 54.44 AAAB O ATOM 2273 CB ASP A 271 39.092 32.179 5.028 1.00 55.83 AAAB C ATOM 2274 CG ASP A 271 39.792 32.466 3.712 1.00 60.96 AAAB C ATOM 2275 OD1 ASP A 271 39.157 32.279 2.651 1.00 64.95 AAAB O ATOM 2276 OD2 ASP A 271 40.975 32.878 3.738 1.00 62.86 AAAB O ATOM 2277 N LYS A 272 36.409 31.246 4.670 1.00 50.79 AAAB N ATOM 2278 CA LYS A 272 35.276 30.365 4.895 1.00 49.82 AAAB C ATOM 2279 C LYS A 272 35.634 29.287 5.915 1.00 46.07 AAAB C ATOM 2280 O LYS A 272 36.741 28.755 5.907 1.00 44.53 AAAB O ATOM 2281 CB LYS A 272 34.790 29.744 3.579 1.00 51.48 AAAB C ATOM 2282 CG LYS A 272 34.116 30.748 2.655 0.00 51.80 AAAB C ATOM 2283 CD LYS A 272 33.410 30.075 1.491 0.00 52.14 AAAB C ATOM 2284 CE LYS A 272 32.666 31.103 0.650 0.00 52.41 AAAB C ATOM 2285 NZ LYS A 272 31.885 30.486 -0.457 0.00 52.53 AAAB N ATOM 2286 N LEU A 273 34.707 29.031 6.829 1.00 46.58 AAAB N ATOM 2287 CA LEU A 273 34.856 28.019 7.875 1.00 46.69 AAAB C ATOM 2288 C LEU A 273 33.451 27.731 8.366 1.00 49.75 AAAB C ATOM 2289 O LEU A 273 33.116 28.037 9.508 1.00 54.13 AAAB O ATOM 2290 CB LEU A 273 35.674 28.543 9.057 1.00 41.36 AAAB C ATOM 2291 CG LEU A 273 37.137 28.156 9.252 1.00 41.35 AAAB C ATOM 2292 CD1 LEU A 273 37.534 28.516 10.678 1.00 39.33 AAAB C ATOM 2293 CD2 LEU A 273 37.356 26.676 9.009 1.00 37.22 AAAB C ATOM 2294 N LEU A 274 32.605 27.201 7.493 1.00 51.05 AAAB N ATOM 2295 CA LEU A 274 31.239 26.914 7.893 1.00 51.82 AAAB C ATOM 2296 C LEU A 274 31.167 25.706 8.826 1.00 50.72 AAAB C ATOM 2297 O LEU A 274 31.996 24.788 8.774 1.00 49.73 AAAB O ATOM 2298 CB LEU A 274 30.329 26.731 6.673 1.00 57.40 AAAB C ATOM 2299 CG LEU A 274 28.821 26.593 6.937 1.00 61.34 AAAB C ATOM 2300 CD1 LEU A 274 28.323 27.705 7.864 1.00 58.46 AAAB C ATOM 2301 CD2 LEU A 274 28.052 26.609 5.613 1.00 64.64 AAAB C ATOM 2302 N PHE A 275 30.189 25.756 9.718 1.00 46.17 AAAB N ATOM 2303 CA PHE A 275 29.954 24.711 10.689 1.00 38.24 AAAB C ATOM 2304 C PHE A 275 28.610 24.079 10.321 1.00 37.75 AAAB C ATOM 2305 O PHE A 275 27.689 24.787 9.910 1.00 37.88 AAAB O ATOM 2306 CB PHE A 275 29.893 25.336 12.090 1.00 35.27 AAAB C ATOM 2307 CG PHE A 275 31.147 26.085 12.486 1.00 30.13 AAAB C ATOM 2308 CD1 PHE A 275 31.338 27.407 12.107 1.00 30.40 AAAB C ATOM 2309 CD2 PHE A 275 32.139 25.460 13.230 1.00 31.00 AAAB C ATOM 2310 CE1 PHE A 275 32.499 28.089 12.465 1.00 32.21 AAAB C ATOM 2311 CE2 PHE A 275 33.299 26.132 13.590 1.00 28.95 AAAB C ATOM 2312 CZ PHE A 275 33.482 27.449 13.207 1.00 30.23 AAAB C ATOM 2313 N GLU A 276 28.514 22.755 10.432 1.00 35.07 AAAB N ATOM 2314 CA GLU A 276 27.277 22.042 10.114 1.00 33.47 AAAB C ATOM 2315 C GLU A 276 26.166 22.416 11.091 1.00 36.53 AAAB C ATOM 2316 O GLU A 276 26.436 22.742 12.254 1.00 38.42 AAAB O ATOM 2317 CB GLU A 276 27.495 20.527 10.177 1.00 32.53 AAAB C ATOM 2318 CG GLU A 276 28.664 20.018 9.345 1.00 33.85 AAAB C ATOM 2319 CD GLU A 276 28.723 18.502 9.240 1.00 28.70 AAAB C ATOM 2320 OE1 GLU A 276 27.685 17.833 9.426 1.00 23.09 AAAB O ATOM 2321 OE2 GLU A 276 29.820 17.982 8.953 1.00 33.65 AAAB O ATOM 2322 N VAL A 277 24.924 22.368 10.614 1.00 38.08 AAAB N ATOM 2323 CA VAL A 277 23.760 22.680 11.443 1.00 41.53 AAAB C ATOM 2324 C VAL A 277 23.104 21.382 11.911 1.00 45.36 AAAB C ATOM 2325 O VAL A 277 23.000 20.410 11.150 1.00 44.57 AAAB O ATOM 2326 CB VAL A 277 22.715 23.545 10.694 1.00 39.13 AAAB C ATOM 2327 CG1 VAL A 277 23.324 24.870 10.300 1.00 40.48 AAAB C ATOM 2328 CG2 VAL A 277 22.188 22.810 9.468 1.00 37.95 AAAB C ATOM 2329 N ALA A 278 22.702 21.355 13.177 1.00 48.66 AAAB N ATOM 2330 CA ALA A 278 22.063 20.175 13.748 1.00 49.62 AAAB C ATOM 2331 C ALA A 278 20.556 20.385 13.797 1.00 51.48 AAAB C ATOM 2332 O ALA A 278 20.085 21.435 14.253 1.00 51.19 AAAB O ATOM 2333 CB ALA A 278 22.603 19.897 15.139 1.00 47.37 AAAB C ATOM 2334 N VAL A 279 19.814 19.376 13.348 1.00 52.73 AAAB N ATOM 2335 CA VAL A 279 18.359 19.421 13.325 1.00 54.53 AAAB C ATOM 2336 C VAL A 279 17.847 18.283 14.219 1.00 56.12 AAAB C ATOM 2337 O VAL A 279 16.703 18.362 14.715 1.00 61.01 AAAB O ATOM 2338 CB VAL A 279 17.822 19.256 11.871 1.00 56.59 AAAB C ATOM 2339 CG1 VAL A 279 16.322 19.566 11.811 1.00 56.48 AAAB C ATOM 2340 CG2 VAL A 279 18.591 20.166 10.915 1.00 56.29 AAAB C ATOM 2341 OXT VAL A 279 18.617 17.329 14.458 1.00 57.14 AAAB O TER 2342 VAL A 279 ATOM 2343 N THR B 2 33.499 30.055 50.060 1.00 47.08 AAAD N ATOM 2344 CA THR B 2 33.002 31.298 49.406 1.00 46.36 AAAD C ATOM 2345 C THR B 2 32.934 32.326 50.527 1.00 47.57 AAAD C ATOM 2346 O THR B 2 33.628 32.156 51.537 1.00 52.96 AAAD O ATOM 2347 CB THR B 2 31.603 31.072 48.792 1.00 46.31 AAAD C ATOM 2348 OG1 THR B 2 30.863 30.144 49.601 1.00 47.07 AAAD O ATOM 2349 CG2 THR B 2 31.739 30.526 47.387 1.00 46.33 AAAD C ATOM 2350 N GLN B 3 32.186 33.409 50.324 1.00 41.30 AAAD N ATOM 2351 CA GLN B 3 32.003 34.439 51.340 1.00 35.19 AAAD C ATOM 2352 C GLN B 3 31.291 35.651 50.762 1.00 30.76 AAAD C ATOM 2353 O GLN B 3 31.841 36.393 49.952 1.00 27.69 AAAD O ATOM 2354 CB GLN B 3 33.324 34.842 52.019 1.00 34.35 AAAD C ATOM 2355 CG GLN B 3 33.175 35.865 53.160 1.00 39.47 AAAD C ATOM 2356 CD GLN B 3 32.013 35.561 54.099 1.00 42.30 AAAD C ATOM 2357 OE1 GLN B 3 30.927 36.111 53.938 1.00 46.25 AAAD O ATOM 2358 NE2 GLN B 3 32.238 34.707 55.086 1.00 46.19 AAAD N ATOM 2359 N PHE B 4 30.047 35.817 51.187 1.00 26.52 AAAD N ATOM 2360 CA PHE B 4 29.200 36.921 50.784 1.00 25.37 AAAD C ATOM 2361 C PHE B 4 29.888 38.244 51.139 1.00 26.15 AAAD C ATOM 2362 O PHE B 4 30.009 39.125 50.290 1.00 28.73 AAAD O ATOM 2363 CB PHE B 4 27.871 36.804 51.526 1.00 25.49 AAAD C ATOM 2364 CG PHE B 4 26.854 37.822 51.126 1.00 25.71 AAAD C ATOM 2365 CD1 PHE B 4 26.785 39.044 51.777 1.00 30.36 AAAD C ATOM 2366 CD2 PHE B 4 25.969 37.564 50.096 1.00 26.60 AAAD C ATOM 2367 CE1 PHE B 4 25.851 39.991 51.403 1.00 29.42 AAAD C ATOM 2368 CE2 PHE B 4 25.032 38.509 49.719 1.00 28.16 AAAD C ATOM 2369 CZ PHE B 4 24.973 39.723 50.370 1.00 27.09 AAAD C ATOM 2370 N ASP B 5 30.382 38.354 52.374 1.00 22.69 AAAD N ATOM 2371 CA ASP B 5 31.055 39.561 52.859 1.00 23.30 AAAD C ATOM 2372 C ASP B 5 32.136 40.118 51.943 1.00 23.26 AAAD C ATOM 2373 O ASP B 5 32.186 41.326 51.721 1.00 26.76 AAAD O ATOM 2374 CB ASP B 5 31.669 39.339 54.242 1.00 20.94 AAAD C ATOM 2375 CG ASP B 5 30.641 39.049 55.307 1.00 20.06 AAAD C ATOM 2376 OD1 ASP B 5 29.528 39.609 55.257 1.00 22.20 AAAD O ATOM 2377 OD2 ASP B 5 30.960 38.262 56.215 1.00 23.43 AAAD O ATOM 2378 N LYS B 6 33.004 39.250 51.433 1.00 23.43 AAAD N ATOM 2379 CA LYS B 6 34.087 39.671 50.546 1.00 26.22 AAAD C ATOM 2380 C LYS B 6 33.557 40.243 49.223 1.00 28.07 AAAD C ATOM 2381 O LYS B 6 33.965 41.329 48.798 1.00 26.76 AAAD O ATOM 2382 CB LYS B 6 35.019 38.494 50.234 1.00 29.87 AAAD C ATOM 2383 CG LYS B 6 35.512 37.695 51.437 1.00 33.68 AAAD C ATOM 2384 CD LYS B 6 36.545 38.434 52.268 1.00 40.10 AAAD C ATOM 2385 CE LYS B 6 37.113 37.530 53.360 1.00 41.70 AAAD C ATOM 2386 NZ LYS B 6 38.015 38.261 54.293 1.00 45.85 AAAD N ATOM 2387 N GLN B 7 32.656 39.503 48.578 1.00 24.27 AAAD N ATOM 2388 CA GLN B 7 32.079 39.920 47.303 1.00 24.85 AAAD C ATOM 2389 C GLN B 7 31.219 41.170 47.428 1.00 26.85 AAAD C ATOM 2390 O GLN B 7 31.229 42.032 46.549 1.00 29.87 AAAD O ATOM 2391 CB GLN B 7 31.260 38.786 46.699 1.00 23.03 AAAD C ATOM 2392 CG GLN B 7 32.105 37.665 46.160 1.00 20.10 AAAD C ATOM 2393 CD GLN B 7 31.268 36.602 45.517 1.00 19.73 AAAD C ATOM 2394 OE1 GLN B 7 30.501 36.880 44.609 1.00 20.68 AAAD O ATOM 2395 NE2 GLN B 7 31.380 35.377 46.010 1.00 29.94 AAAD N ATOM 2396 N TYR B 8 30.454 41.237 48.511 1.00 25.45 AAAD N ATOM 2397 CA TYR B 8 29.592 42.375 48.809 1.00 23.20 AAAD C ATOM 2398 C TYR B 8 30.460 43.636 48.935 1.00 22.76 AAAD C ATOM 2399 O TYR B 8 30.216 44.645 48.271 1.00 19.84 AAAD O ATOM 2400 CB TYR B 8 28.862 42.118 50.134 1.00 18.64 AAAD C ATOM 2401 CG TYR B 8 27.926 43.222 50.589 1.00 16.63 AAAD C ATOM 2402 CD1 TYR B 8 26.620 43.307 50.098 1.00 14.51 AAAD C ATOM 2403 CD2 TYR B 8 28.338 44.168 51.533 1.00 14.57 AAAD C ATOM 2404 CE1 TYR B 8 25.752 44.298 50.535 1.00 15.00 AAAD C ATOM 2405 CE2 TYR B 8 27.479 45.168 51.971 1.00 13.85 AAAD C ATOM 2406 CZ TYR B 8 26.190 45.225 51.472 1.00 15.14 AAAD C ATOM 2407 OH TYR B 8 25.336 46.202 51.922 1.00 22.24 AAAD O ATOM 2408 N ASN B 9 31.478 43.568 49.785 1.00 19.48 AAAD N ATOM 2409 CA ASN B 9 32.365 44.700 49.990 1.00 18.67 AAAD C ATOM 2410 C ASN B 9 32.981 45.142 48.689 1.00 21.29 AAAD C ATOM 2411 O ASN B 9 33.149 46.339 48.465 1.00 27.16 AAAD O ATOM 2412 CB ASN B 9 33.456 44.365 50.996 1.00 17.24 AAAD C ATOM 2413 CG ASN B 9 32.974 44.447 52.428 1.00 15.06 AAAD C ATOM 2414 OD1 ASN B 9 33.756 44.261 53.352 1.00 23.91 AAAD O ATOM 2415 ND2 ASN B 9 31.689 44.742 52.625 1.00 12.94 AAAD N ATOM 2416 N SER B 10 33.285 44.183 47.818 1.00 21.73 AAAD N ATOM 2417 CA SER B 10 33.874 44.499 46.522 1.00 20.03 AAAD C ATOM 2418 C SER B 10 32.940 45.332 45.667 1.00 18.08 AAAD C ATOM 2419 O SER B 10 33.373 46.276 45.014 1.00 18.42 AAAD O ATOM 2420 CB SER B 10 34.286 43.235 45.786 1.00 20.66 AAAD C ATOM 2421 OG SER B 10 35.438 42.685 46.402 1.00 33.48 AAAD O ATOM 2422 N ILE B 11 31.659 44.990 45.676 1.00 16.52 AAAD N ATOM 2423 CA ILE B 11 30.692 45.754 44.914 1.00 18.63 AAAD C ATOM 2424 C ILE B 11 30.521 47.139 45.551 1.00 21.98 AAAD C ATOM 2425 O ILE B 11 30.627 48.156 44.866 1.00 20.72 AAAD O ATOM 2426 CB ILE B 11 29.335 45.018 44.807 1.00 18.40 AAAD C ATOM 2427 CG1 ILE B 11 29.508 43.765 43.934 1.00 17.68 AAAD C ATOM 2428 CG2 ILE B 11 28.264 45.952 44.225 1.00 17.37 AAAD C ATOM 2429 CD1 ILE B 11 28.251 42.932 43.750 1.00 13.12 AAAD C ATOM 2430 N ILE B 12 30.320 47.179 46.865 1.00 19.81 AAAD N ATOM 2431 CA ILE B 12 30.146 48.442 47.569 1.00 18.25 AAAD C ATOM 2432 C ILE B 12 31.296 49.395 47.266 1.00 19.84 AAAD C ATOM 2433 O ILE B 12 31.070 50.565 46.947 1.00 22.33 AAAD O ATOM 2434 CB ILE B 12 30.049 48.250 49.101 1.00 17.13 AAAD C ATOM 2435 CG1 ILE B 12 28.817 47.415 49.463 1.00 17.65 AAAD C ATOM 2436 CG2 ILE B 12 29.994 49.598 49.796 1.00 17.43 AAAD C ATOM 2437 CD1 ILE B 12 27.528 47.962 48.933 1.00 12.05 AAAD C ATOM 2438 N LYS B 13 32.523 48.893 47.352 1.00 18.31 AAAD N ATOM 2439 CA LYS B 13 33.692 49.712 47.085 1.00 18.20 AAAD C ATOM 2440 C LYS B 13 33.694 50.141 45.619 1.00 22.07 AAAD C ATOM 2441 O LYS B 13 34.049 51.277 45.284 1.00 23.01 AAAD O ATOM 2442 CB LYS B 13 34.969 48.946 47.417 1.00 17.51 AAAD C ATOM 2443 CG LYS B 13 36.188 49.829 47.484 1.00 27.08 AAAD C ATOM 2444 CD LYS B 13 37.470 49.025 47.537 1.00 37.47 AAAD C ATOM 2445 CE LYS B 13 38.668 49.958 47.407 1.00 45.95 AAAD C ATOM 2446 NZ LYS B 13 39.961 49.239 47.199 1.00 53.67 AAAD N ATOM 2447 N ASP B 14 33.252 49.243 44.748 1.00 22.72 AAAD N ATOM 2448 CA ASP B 14 33.201 49.536 43.325 1.00 24.20 AAAD C ATOM 2449 C ASP B 14 32.303 50.743 43.099 1.00 24.53 AAAD C ATOM 2450 O ASP B 14 32.687 51.680 42.399 1.00 27.43 AAAD O ATOM 2451 CB ASP B 14 32.666 48.333 42.547 1.00 27.21 AAAD C ATOM 2452 CG ASP B 14 32.889 48.463 41.060 1.00 29.53 AAAD C ATOM 2453 OD1 ASP B 14 34.064 48.448 40.651 1.00 35.64 AAAD O ATOM 2454 OD2 ASP B 14 31.905 48.599 40.306 1.00 28.73 AAAD O ATOM 2455 N ILE B 15 31.126 50.722 43.724 1.00 20.70 AAAD N ATOM 2456 CA ILE B 15 30.153 51.801 43.619 1.00 18.36 AAAD C ATOM 2457 C ILE B 15 30.731 53.137 44.095 1.00 23.72 AAAD C ATOM 2458 O ILE B 15 30.683 54.144 43.377 1.00 20.76 AAAD O ATOM 2459 CB ILE B 15 28.882 51.495 44.450 1.00 16.88 AAAD C ATOM 2460 CG1 ILE B 15 28.210 50.224 43.937 1.00 14.86 AAAD C ATOM 2461 CG2 ILE B 15 27.902 52.668 44.378 1.00 17.15 AAAD C ATOM 2462 CD1 ILE B 15 26.857 49.948 44.570 1.00 16.22 AAAD C ATOM 2463 N ILE B 16 31.290 53.129 45.299 1.00 23.71 AAAD N ATOM 2464 CA ILE B 16 31.875 54.323 45.895 1.00 28.12 AAAD C ATOM 2465 C ILE B 16 32.915 54.997 44.988 1.00 31.53 AAAD C ATOM 2466 O ILE B 16 32.897 56.217 44.820 1.00 32.88 AAAD O ATOM 2467 CB ILE B 16 32.513 53.986 47.265 1.00 28.13 AAAD C ATOM 2468 CG1 ILE B 16 31.438 53.490 48.236 1.00 29.06 AAAD C ATOM 2469 CG2 ILE B 16 33.212 55.194 47.853 1.00 30.33 AAAD C ATOM 2470 CD1 ILE B 16 31.998 52.993 49.558 1.00 28.42 AAAD C ATOM 2471 N ASN B 17 33.777 54.196 44.369 1.00 30.53 AAAD N ATOM 2472 CA ASN B 17 34.838 54.710 43.506 1.00 32.35 AAAD C ATOM 2473 C ASN B 17 34.522 54.954 42.035 1.00 32.15 AAAD C ATOM 2474 O ASN B 17 35.100 55.850 41.425 1.00 34.01 AAAD O ATOM 2475 CB ASN B 17 36.060 53.787 43.568 1.00 36.56 AAAD C ATOM 2476 CG ASN B 17 36.855 53.946 44.845 1.00 41.61 AAAD C ATOM 2477 OD1 ASN B 17 36.470 53.442 45.900 1.00 46.11 AAAD O ATOM 2478 ND2 ASN B 17 37.988 54.628 44.752 1.00 45.26 AAAD N ATOM 2479 N ASN B 18 33.654 54.135 41.451 1.00 29.31 AAAD N ATOM 2480 CA ASN B 18 33.332 54.253 40.029 1.00 26.32 AAAD C ATOM 2481 C ASN B 18 31.866 54.497 39.733 1.00 25.17 AAAD C ATOM 2482 O ASN B 18 31.451 54.449 38.575 1.00 25.78 AAAD O ATOM 2483 CB ASN B 18 33.753 52.980 39.281 1.00 29.68 AAAD C ATOM 2484 CG ASN B 18 35.249 52.764 39.277 1.00 37.16 AAAD C ATOM 2485 OD1 ASN B 18 35.908 52.965 38.257 1.00 48.30 AAAD O ATOM 2486 ND2 ASN B 18 35.796 52.334 40.409 1.00 39.29 AAAD N ATOM 2487 N GLY B 19 31.074 54.751 40.762 1.00 26.24 AAAD N ATOM 2488 CA GLY B 19 29.657 54.961 40.541 1.00 23.88 AAAD C ATOM 2489 C GLY B 19 29.312 56.221 39.780 1.00 23.10 AAAD C ATOM 2490 O GLY B 19 30.102 57.164 39.700 1.00 26.71 AAAD O ATOM 2491 N ILE B 20 28.118 56.220 39.210 1.00 21.10 AAAD N ATOM 2492 CA ILE B 20 27.593 57.349 38.466 1.00 20.29 AAAD C ATOM 2493 C ILE B 20 26.295 57.726 39.168 1.00 18.35 AAAD C ATOM 2494 O ILE B 20 25.400 56.890 39.315 1.00 19.76 AAAD O ATOM 2495 CB ILE B 20 27.282 56.971 36.994 1.00 22.71 AAAD C ATOM 2496 CG1 ILE B 20 28.552 56.493 36.298 1.00 27.19 AAAD C ATOM 2497 CG2 ILE B 20 26.732 58.179 36.235 1.00 22.42 AAAD C ATOM 2498 CD1 ILE B 20 28.308 55.940 34.911 1.00 36.69 AAAD C ATOM 2499 N SER B 21 26.204 58.970 39.625 1.00 12.67 AAAD N ATOM 2500 CA SER B 21 25.016 59.421 40.320 1.00 7.34 AAAD C ATOM 2501 C SER B 21 23.926 59.791 39.345 1.00 4.71 AAAD C ATOM 2502 O SER B 21 24.161 59.871 38.141 1.00 8.35 AAAD O ATOM 2503 CB SER B 21 25.353 60.623 41.208 1.00 12.14 AAAD C ATOM 2504 OG SER B 21 26.020 61.653 40.492 1.00 14.92 AAAD O ATOM 2505 N ASP B 22 22.725 59.991 39.868 1.00 2.00 AAAD N ATOM 2506 CA ASP B 22 21.593 60.398 39.054 1.00 3.96 AAAD C ATOM 2507 C ASP B 22 21.136 61.730 39.647 1.00 9.08 AAAD C ATOM 2508 O ASP B 22 19.947 62.051 39.651 1.00 5.67 AAAD O ATOM 2509 CB ASP B 22 20.467 59.359 39.122 1.00 4.87 AAAD C ATOM 2510 CG ASP B 22 19.946 59.129 40.537 1.00 11.19 AAAD C ATOM 2511 OD1 ASP B 22 20.522 59.664 41.501 1.00 12.86 AAAD O ATOM 2512 OD2 ASP B 22 18.946 58.395 40.692 1.00 17.74 AAAD O ATOM 2513 N GLU B 23 22.100 62.480 40.181 1.00 15.30 AAAD N ATOM 2514 CA GLU B 23 21.842 63.767 40.827 1.00 17.78 AAAD C ATOM 2515 C GLU B 23 21.239 64.858 39.957 1.00 21.67 AAAD C ATOM 2516 O GLU B 23 20.531 65.731 40.473 1.00 23.84 AAAD O ATOM 2517 CB GLU B 23 23.099 64.272 41.544 1.00 11.93 AAAD C ATOM 2518 CG GLU B 23 23.251 63.680 42.959 1.00 11.40 AAAD C ATOM 2519 CD GLU B 23 24.686 63.637 43.466 1.00 9.09 AAAD C ATOM 2520 OE1 GLU B 23 25.615 63.468 42.646 1.00 14.67 AAAD O ATOM 2521 OE2 GLU B 23 24.882 63.720 44.699 1.00 10.25 AAAD O ATOM 2522 N GLU B 24 21.462 64.779 38.646 1.00 24.25 AAAD N ATOM 2523 CA GLU B 24 20.938 65.782 37.730 1.00 23.94 AAAD C ATOM 2524 C GLU B 24 19.517 65.487 37.258 1.00 25.88 AAAD C ATOM 2525 O GLU B 24 18.922 66.302 36.554 1.00 28.00 AAAD O ATOM 2526 CB GLU B 24 21.866 65.935 36.524 1.00 23.62 AAAD C ATOM 2527 CG GLU B 24 21.760 64.822 35.488 1.00 27.52 AAAD C ATOM 2528 CD GLU B 24 22.845 63.768 35.617 1.00 29.94 AAAD C ATOM 2529 OE1 GLU B 24 23.224 63.414 36.756 1.00 32.61 AAAD O ATOM 2530 OE2 GLU B 24 23.320 63.284 34.567 1.00 30.15 AAAD O ATOM 2531 N PHE B 25 18.975 64.334 37.651 1.00 26.84 AAAD N ATOM 2532 CA PHE B 25 17.631 63.934 37.243 1.00 26.72 AAAD C ATOM 2533 C PHE B 25 16.593 64.149 38.323 1.00 29.53 AAAD C ATOM 2534 O PHE B 25 16.915 64.165 39.512 1.00 32.11 AAAD O ATOM 2535 CB PHE B 25 17.591 62.447 36.888 1.00 24.72 AAAD C ATOM 2536 CG PHE B 25 18.405 62.074 35.689 1.00 27.61 AAAD C ATOM 2537 CD1 PHE B 25 18.063 62.548 34.429 1.00 26.61 AAAD C ATOM 2538 CD2 PHE B 25 19.499 61.223 35.814 1.00 27.15 AAAD C ATOM 2539 CE1 PHE B 25 18.801 62.181 33.312 1.00 28.63 AAAD C ATOM 2540 CE2 PHE B 25 20.245 60.849 34.699 1.00 31.04 AAAD C ATOM 2541 CZ PHE B 25 19.895 61.329 33.443 1.00 30.02 AAAD C ATOM 2542 N ASP B 26 15.335 64.250 37.899 1.00 33.20 AAAD N ATOM 2543 CA ASP B 26 14.210 64.391 38.819 1.00 38.74 AAAD C ATOM 2544 C ASP B 26 13.812 62.961 39.165 1.00 40.59 AAAD C ATOM 2545 O ASP B 26 13.107 62.306 38.396 1.00 42.45 AAAD O ATOM 2546 CB ASP B 26 13.031 65.094 38.144 1.00 42.90 AAAD C ATOM 2547 CG ASP B 26 13.227 66.586 38.036 1.00 50.81 AAAD C ATOM 2548 OD1 ASP B 26 13.206 67.257 39.090 1.00 52.33 AAAD O ATOM 2549 OD2 ASP B 26 13.400 67.086 36.901 1.00 54.57 AAAD O ATOM 2550 N VAL B 27 14.284 62.476 40.309 1.00 39.26 AAAD N ATOM 2551 CA VAL B 27 14.014 61.111 40.756 1.00 36.95 AAAD C ATOM 2552 C VAL B 27 12.696 60.920 41.505 1.00 38.33 AAAD C ATOM 2553 O VAL B 27 12.262 61.798 42.253 1.00 38.87 AAAD O ATOM 2554 CB VAL B 27 15.174 60.590 41.626 1.00 33.45 AAAD C ATOM 2555 CG1 VAL B 27 16.446 60.540 40.802 1.00 31.20 AAAD C ATOM 2556 CG2 VAL B 27 15.373 61.484 42.845 1.00 28.67 AAAD C ATOM 2557 N ARG B 28 12.071 59.760 41.305 1.00 38.94 AAAD N ATOM 2558 CA ARG B 28 10.806 59.444 41.966 1.00 43.94 AAAD C ATOM 2559 C ARG B 28 10.990 59.055 43.435 1.00 44.06 AAAD C ATOM 2560 O ARG B 28 10.029 59.020 44.204 1.00 43.85 AAAD O ATOM 2561 CB ARG B 28 10.086 58.304 41.244 1.00 49.30 AAAD C ATOM 2562 CG ARG B 28 10.739 56.929 41.407 1.00 56.67 AAAD C ATOM 2563 CD ARG B 28 9.689 55.825 41.535 1.00 63.50 AAAD C ATOM 2564 NE ARG B 28 8.722 55.833 40.436 1.00 71.86 AAAD N ATOM 2565 CZ ARG B 28 7.439 55.501 40.564 1.00 77.69 AAAD C ATOM 2566 NH1 ARG B 28 6.955 55.130 41.746 1.00 80.85 AAAD N ATOM 2567 NH2 ARG B 28 6.630 55.554 39.512 1.00 78.24 AAAD N ATOM 2568 N THR B 29 12.221 58.729 43.802 1.00 42.94 AAAD N ATOM 2569 CA THR B 29 12.532 58.326 45.159 1.00 43.40 AAAD C ATOM 2570 C THR B 29 12.811 59.551 46.026 1.00 44.44 AAAD C ATOM 2571 O THR B 29 13.520 60.464 45.611 1.00 43.96 AAAD O ATOM 2572 CB THR B 29 13.767 57.419 45.171 1.00 44.63 AAAD C ATOM 2573 OG1 THR B 29 13.737 56.554 44.027 1.00 50.25 AAAD O ATOM 2574 CG2 THR B 29 13.791 56.584 46.424 1.00 47.28 AAAD C ATOM 2575 N LYS B 30 12.297 59.535 47.249 1.00 46.83 AAAD N ATOM 2576 CA LYS B 30 12.486 60.627 48.194 1.00 48.65 AAAD C ATOM 2577 C LYS B 30 12.734 60.069 49.587 1.00 46.73 AAAD C ATOM 2578 O LYS B 30 12.390 58.923 49.878 1.00 48.33 AAAD O ATOM 2579 CB LYS B 30 11.264 61.542 48.208 1.00 53.79 AAAD C ATOM 2580 CG LYS B 30 9.963 60.839 48.543 1.00 62.37 AAAD C ATOM 2581 CD LYS B 30 8.802 61.804 48.423 1.00 70.61 AAAD C ATOM 2582 CE LYS B 30 7.499 61.141 48.819 1.00 75.73 AAAD C ATOM 2583 NZ LYS B 30 6.348 62.070 48.642 1.00 82.20 AAAD N ATOM 2584 N TRP B 31 13.387 60.859 50.430 1.00 42.88 AAAD N ATOM 2585 CA TRP B 31 13.681 60.438 51.793 1.00 38.45 AAAD C ATOM 2586 C TRP B 31 12.446 60.631 52.664 1.00 39.84 AAAD C ATOM 2587 O TRP B 31 11.885 61.726 52.711 1.00 38.57 AAAD O ATOM 2588 CB TRP B 31 14.844 61.250 52.350 1.00 32.24 AAAD C ATOM 2589 CG TRP B 31 16.152 60.972 51.676 1.00 28.53 AAAD C ATOM 2590 CD1 TRP B 31 16.867 61.827 50.890 1.00 30.67 AAAD C ATOM 2591 CD2 TRP B 31 16.924 59.765 51.757 1.00 30.88 AAAD C ATOM 2592 NE1 TRP B 31 18.040 61.234 50.481 1.00 28.71 AAAD N ATOM 2593 CE2 TRP B 31 18.098 59.965 50.994 1.00 29.56 AAAD C ATOM 2594 CE3 TRP B 31 16.738 58.533 52.403 1.00 24.09 AAAD C ATOM 2595 CZ2 TRP B 31 19.081 58.975 50.859 1.00 26.07 AAAD C ATOM 2596 CZ3 TRP B 31 17.717 57.556 52.269 1.00 18.26 AAAD C ATOM 2597 CH2 TRP B 31 18.871 57.783 51.503 1.00 17.90 AAAD C ATOM 2598 N ASP B 32 12.044 59.573 53.365 1.00 43.91 AAAD N ATOM 2599 CA ASP B 32 10.868 59.622 54.231 1.00 47.60 AAAD C ATOM 2600 C ASP B 32 11.002 60.654 55.352 1.00 46.90 AAAD C ATOM 2601 O ASP B 32 10.007 61.100 55.904 1.00 47.92 AAAD O ATOM 2602 CB ASP B 32 10.593 58.241 54.844 1.00 51.00 AAAD C ATOM 2603 CG ASP B 32 11.623 57.868 55.899 1.00 54.46 AAAD C ATOM 2604 OD1 ASP B 32 12.818 57.749 55.549 1.00 57.08 AAAD O ATOM 2605 OD2 ASP B 32 11.237 57.710 57.084 1.00 52.03 AAAD O ATOM 2606 N SER B 33 12.236 61.000 55.705 1.00 44.81 AAAD N ATOM 2607 CA SER B 33 12.469 61.971 56.768 1.00 44.63 AAAD C ATOM 2608 C SER B 33 12.143 63.408 56.366 1.00 45.58 AAAD C ATOM 2609 O SER B 33 11.253 64.029 56.943 1.00 48.62 AAAD O ATOM 2610 CB SER B 33 13.915 61.880 57.258 1.00 42.44 AAAD C ATOM 2611 OG SER B 33 14.834 62.187 56.223 1.00 46.01 AAAD O ATOM 2612 N ASP B 34 12.862 63.926 55.372 1.00 44.87 AAAD N ATOM 2613 CA ASP B 34 12.658 65.302 54.928 1.00 44.61 AAAD C ATOM 2614 C ASP B 34 12.053 65.494 53.542 1.00 43.95 AAAD C ATOM 2615 O ASP B 34 12.003 66.619 53.042 1.00 42.13 AAAD O ATOM 2616 CB ASP B 34 13.961 66.112 55.062 1.00 46.25 AAAD C ATOM 2617 CG ASP B 34 15.152 65.464 54.356 1.00 47.20 AAAD C ATOM 2618 OD1 ASP B 34 14.964 64.505 53.582 1.00 48.76 AAAD O ATOM 2619 OD2 ASP B 34 16.294 65.926 54.579 1.00 48.21 AAAD O ATOM 2620 N GLY B 35 11.627 64.403 52.915 1.00 42.30 AAAD N ATOM 2621 CA GLY B 35 11.025 64.488 51.593 1.00 42.37 AAAD C ATOM 2622 C GLY B 35 11.948 64.822 50.429 1.00 39.70 AAAD C ATOM 2623 O GLY B 35 11.538 64.712 49.271 1.00 38.69 AAAD O ATOM 2624 N THR B 36 13.182 65.226 50.718 1.00 36.47 AAAD N ATOM 2625 CA THR B 36 14.130 65.574 49.668 1.00 34.18 AAAD C ATOM 2626 C THR B 36 14.377 64.394 48.730 1.00 33.04 AAAD C ATOM 2627 O THR B 36 14.228 63.239 49.125 1.00 36.20 AAAD O ATOM 2628 CB THR B 36 15.457 66.074 50.264 1.00 35.31 AAAD C ATOM 2629 OG1 THR B 36 16.037 65.057 51.085 1.00 37.77 AAAD O ATOM 2630 CG2 THR B 36 15.212 67.307 51.111 1.00 38.18 AAAD C ATOM 2631 N PRO B 37 14.743 64.669 47.467 1.00 30.10 AAAD N ATOM 2632 CA PRO B 37 14.997 63.598 46.497 1.00 25.02 AAAD C ATOM 2633 C PRO B 37 16.101 62.652 46.936 1.00 20.89 AAAD C ATOM 2634 O PRO B 37 17.193 63.088 47.303 1.00 18.51 AAAD O ATOM 2635 CB PRO B 37 15.388 64.368 45.233 1.00 30.07 AAAD C ATOM 2636 CG PRO B 37 15.968 65.658 45.776 1.00 33.31 AAAD C ATOM 2637 CD PRO B 37 14.987 65.990 46.864 1.00 28.00 AAAD C ATOM 2638 N ALA B 38 15.796 61.356 46.899 1.00 19.50 AAAD N ATOM 2639 CA ALA B 38 16.736 60.306 47.280 1.00 16.34 AAAD C ATOM 2640 C ALA B 38 17.531 59.887 46.054 1.00 14.40 AAAD C ATOM 2641 O ALA B 38 17.007 59.237 45.139 1.00 9.45 AAAD O ATOM 2642 CB ALA B 38 15.986 59.105 47.866 1.00 14.31 AAAD C ATOM 2643 N HIS B 39 18.784 60.314 46.007 1.00 13.57 AAAD N ATOM 2644 CA HIS B 39 19.642 59.985 44.886 1.00 15.60 AAAD C ATOM 2645 C HIS B 39 20.491 58.747 45.110 1.00 14.79 AAAD C ATOM 2646 O HIS B 39 20.916 58.447 46.229 1.00 16.28 AAAD O ATOM 2647 CB HIS B 39 20.515 61.187 44.510 1.00 15.69 AAAD C ATOM 2648 CG HIS B 39 19.762 62.267 43.798 1.00 16.70 AAAD C ATOM 2649 ND1 HIS B 39 19.209 62.090 42.548 1.00 15.51 AAAD N ATOM 2650 CD2 HIS B 39 19.433 63.522 44.180 1.00 14.40 AAAD C ATOM 2651 CE1 HIS B 39 18.567 63.187 42.190 1.00 18.45 AAAD C ATOM 2652 NE2 HIS B 39 18.688 64.072 43.165 1.00 14.78 AAAD N ATOM 2653 N THR B 40 20.730 58.025 44.031 1.00 14.64 AAAD N ATOM 2654 CA THR B 40 21.530 56.824 44.094 1.00 14.33 AAAD C ATOM 2655 C THR B 40 22.848 57.046 43.373 1.00 13.91 AAAD C ATOM 2656 O THR B 40 23.034 58.051 42.688 1.00 14.78 AAAD O ATOM 2657 CB THR B 40 20.775 55.672 43.445 1.00 9.30 AAAD C ATOM 2658 OG1 THR B 40 20.277 56.096 42.168 1.00 10.60 AAAD O ATOM 2659 CG2 THR B 40 19.611 55.264 44.310 1.00 2.00 AAAD C ATOM 2660 N LEU B 41 23.771 56.124 43.586 1.00 13.76 AAAD N ATOM 2661 CA LEU B 41 25.093 56.144 42.978 1.00 13.69 AAAD C ATOM 2662 C LEU B 41 25.167 54.701 42.459 1.00 16.81 AAAD C ATOM 2663 O LEU B 41 24.945 53.757 43.229 1.00 17.11 AAAD O ATOM 2664 CB LEU B 41 26.112 56.383 44.079 1.00 12.68 AAAD C ATOM 2665 CG LEU B 41 27.540 56.756 43.724 1.00 15.97 AAAD C ATOM 2666 CD1 LEU B 41 27.558 58.042 42.952 1.00 18.03 AAAD C ATOM 2667 CD2 LEU B 41 28.317 56.901 45.004 1.00 21.38 AAAD C ATOM 2668 N SER B 42 25.407 54.499 41.168 1.00 16.00 AAAD N ATOM 2669 CA SER B 42 25.401 53.128 40.683 1.00 16.33 AAAD C ATOM 2670 C SER B 42 26.416 52.629 39.686 1.00 17.66 AAAD C ATOM 2671 O SER B 42 27.126 53.395 39.043 1.00 19.95 AAAD O ATOM 2672 CB SER B 42 24.010 52.784 40.158 1.00 18.01 AAAD C ATOM 2673 OG SER B 42 23.700 53.518 38.993 1.00 18.64 AAAD O ATOM 2674 N VAL B 43 26.465 51.303 39.602 1.00 18.07 AAAD N ATOM 2675 CA VAL B 43 27.320 50.549 38.699 1.00 16.85 AAAD C ATOM 2676 C VAL B 43 26.334 49.686 37.905 1.00 12.26 AAAD C ATOM 2677 O VAL B 43 25.247 49.375 38.393 1.00 13.67 AAAD O ATOM 2678 CB VAL B 43 28.291 49.646 39.481 1.00 21.69 AAAD C ATOM 2679 CG1 VAL B 43 29.074 48.775 38.524 1.00 30.30 AAAD C ATOM 2680 CG2 VAL B 43 29.243 50.489 40.300 1.00 20.25 AAAD C ATOM 2681 N ILE B 44 26.683 49.344 36.672 1.00 12.63 AAAD N ATOM 2682 CA ILE B 44 25.800 48.544 35.827 1.00 11.06 AAAD C ATOM 2683 C ILE B 44 26.306 47.130 35.616 1.00 9.04 AAAD C ATOM 2684 O ILE B 44 27.475 46.923 35.304 1.00 7.23 AAAD O ATOM 2685 CB ILE B 44 25.592 49.211 34.443 1.00 12.99 AAAD C ATOM 2686 CG1 ILE B 44 24.670 50.421 34.572 1.00 17.37 AAAD C ATOM 2687 CG2 ILE B 44 24.974 48.236 33.446 1.00 10.67 AAAD C ATOM 2688 CD1 ILE B 44 24.560 51.220 33.283 1.00 21.50 AAAD C ATOM 2689 N SER B 45 25.398 46.175 35.781 1.00 10.82 AAAD N ATOM 2690 CA SER B 45 25.672 44.758 35.586 1.00 15.26 AAAD C ATOM 2691 C SER B 45 26.674 44.159 36.563 1.00 14.95 AAAD C ATOM 2692 O SER B 45 27.865 44.087 36.269 1.00 16.31 AAAD O ATOM 2693 CB SER B 45 26.136 44.513 34.149 1.00 17.93 AAAD C ATOM 2694 OG SER B 45 26.153 43.129 33.843 1.00 18.57 AAAD O ATOM 2695 N LYS B 46 26.181 43.700 37.710 1.00 11.14 AAAD N ATOM 2696 CA LYS B 46 27.041 43.088 38.714 1.00 14.56 AAAD C ATOM 2697 C LYS B 46 26.582 41.674 39.017 1.00 13.92 AAAD C ATOM 2698 O LYS B 46 25.387 41.412 39.139 1.00 17.15 AAAD O ATOM 2699 CB LYS B 46 27.067 43.918 39.996 1.00 14.65 AAAD C ATOM 2700 CG LYS B 46 27.999 45.114 39.934 1.00 18.63 AAAD C ATOM 2701 CD LYS B 46 29.432 44.687 39.731 1.00 10.57 AAAD C ATOM 2702 CE LYS B 46 30.378 45.813 40.081 1.00 23.06 AAAD C ATOM 2703 NZ LYS B 46 31.819 45.405 40.111 1.00 30.14 AAAD N ATOM 2704 N GLN B 47 27.534 40.760 39.142 1.00 16.37 AAAD N ATOM 2705 CA GLN B 47 27.209 39.367 39.415 1.00 17.19 AAAD C ATOM 2706 C GLN B 47 28.023 38.841 40.581 1.00 16.49 AAAD C ATOM 2707 O GLN B 47 29.188 39.202 40.750 1.00 19.11 AAAD O ATOM 2708 CB GLN B 47 27.486 38.518 38.168 1.00 16.48 AAAD C ATOM 2709 CG GLN B 47 27.337 37.032 38.386 1.00 21.61 AAAD C ATOM 2710 CD GLN B 47 27.841 36.212 37.222 1.00 18.18 AAAD C ATOM 2711 OE1 GLN B 47 28.974 35.737 37.224 1.00 20.43 AAAD O ATOM 2712 NE2 GLN B 47 26.996 36.027 36.227 1.00 23.42 AAAD N ATOM 2713 N MET B 48 27.385 38.021 41.404 1.00 18.69 AAAD N ATOM 2714 CA MET B 48 28.044 37.400 42.546 1.00 18.10 AAAD C ATOM 2715 C MET B 48 27.830 35.898 42.375 1.00 16.43 AAAD C ATOM 2716 O MET B 48 26.693 35.462 42.167 1.00 16.01 AAAD O ATOM 2717 CB MET B 48 27.413 37.872 43.861 1.00 19.14 AAAD C ATOM 2718 CG MET B 48 27.398 39.388 44.049 1.00 22.34 AAAD C ATOM 2719 SD MET B 48 26.836 39.899 45.697 1.00 22.95 AAAD S ATOM 2720 CE MET B 48 25.085 39.926 45.472 1.00 20.30 AAAD C ATOM 2721 N ARG B 49 28.912 35.122 42.399 1.00 12.80 AAAD N ATOM 2722 CA ARG B 49 28.820 33.668 42.245 1.00 17.88 AAAD C ATOM 2723 C ARG B 49 29.231 32.948 43.519 1.00 18.15 AAAD C ATOM 2724 O ARG B 49 30.250 33.290 44.133 1.00 16.60 AAAD O ATOM 2725 CB ARG B 49 29.705 33.162 41.094 1.00 17.06 AAAD C ATOM 2726 CG ARG B 49 29.329 33.673 39.724 1.00 26.21 AAAD C ATOM 2727 CD ARG B 49 30.294 33.186 38.652 1.00 24.92 AAAD C ATOM 2728 NE ARG B 49 29.891 31.921 38.039 1.00 25.71 AAAD N ATOM 2729 CZ ARG B 49 29.319 31.817 36.843 1.00 22.95 AAAD C ATOM 2730 NH1 ARG B 49 29.067 32.901 36.117 1.00 21.71 AAAD N ATOM 2731 NH2 ARG B 49 29.022 30.619 36.361 1.00 21.18 AAAD N ATOM 2732 N PHE B 50 28.481 31.903 43.865 1.00 19.02 AAAD N ATOM 2733 CA PHE B 50 28.746 31.098 45.059 1.00 19.88 AAAD C ATOM 2734 C PHE B 50 28.654 29.599 44.741 1.00 20.15 AAAD C ATOM 2735 O PHE B 50 27.705 29.158 44.087 1.00 19.07 AAAD O ATOM 2736 CB PHE B 50 27.734 31.441 46.156 1.00 17.90 AAAD C ATOM 2737 CG PHE B 50 27.577 32.924 46.405 1.00 20.03 AAAD C ATOM 2738 CD1 PHE B 50 28.545 33.631 47.115 1.00 17.79 AAAD C ATOM 2739 CD2 PHE B 50 26.451 33.609 45.943 1.00 19.04 AAAD C ATOM 2740 CE1 PHE B 50 28.398 34.985 47.365 1.00 11.90 AAAD C ATOM 2741 CE2 PHE B 50 26.296 34.963 46.189 1.00 17.11 AAAD C ATOM 2742 CZ PHE B 50 27.273 35.653 46.904 1.00 20.37 AAAD C ATOM 2743 N ASP B 51 29.636 28.825 45.207 1.00 20.65 AAAD N ATOM 2744 CA ASP B 51 29.651 27.367 44.989 1.00 23.98 AAAD C ATOM 2745 C ASP B 51 28.869 26.571 46.049 1.00 24.64 AAAD C ATOM 2746 O ASP B 51 28.922 25.343 46.085 1.00 26.25 AAAD O ATOM 2747 CB ASP B 51 31.095 26.830 44.877 1.00 21.95 AAAD C ATOM 2748 CG ASP B 51 31.954 27.136 46.107 1.00 26.97 AAAD C ATOM 2749 OD1 ASP B 51 31.397 27.470 47.176 1.00 28.53 AAAD O ATOM 2750 OD2 ASP B 51 33.201 27.031 46.005 1.00 27.87 AAAD O ATOM 2751 N ASN B 52 28.177 27.288 46.927 1.00 22.47 AAAD N ATOM 2752 CA ASN B 52 27.385 26.673 47.984 1.00 20.55 AAAD C ATOM 2753 C ASN B 52 28.143 25.880 49.065 1.00 22.39 AAAD C ATOM 2754 O ASN B 52 27.560 25.063 49.789 1.00 17.62 AAAD O ATOM 2755 CB ASN B 52 26.234 25.874 47.383 1.00 19.55 AAAD C ATOM 2756 CG ASN B 52 25.006 26.724 47.167 1.00 16.60 AAAD C ATOM 2757 OD1 ASN B 52 24.585 27.443 48.067 1.00 12.02 AAAD O ATOM 2758 ND2 ASN B 52 24.441 26.674 45.970 1.00 10.34 AAAD N ATOM 2759 N SER B 53 29.441 26.150 49.195 1.00 19.56 AAAD N ATOM 2760 CA SER B 53 30.230 25.517 50.238 1.00 19.47 AAAD C ATOM 2761 C SER B 53 29.931 26.286 51.540 1.00 21.41 AAAD C ATOM 2762 O SER B 53 30.386 25.915 52.621 1.00 22.54 AAAD O ATOM 2763 CB SER B 53 31.722 25.580 49.901 1.00 20.99 AAAD C ATOM 2764 OG SER B 53 32.213 26.911 49.843 1.00 28.33 AAAD O ATOM 2765 N GLU B 54 29.152 27.361 51.413 1.00 20.78 AAAD N ATOM 2766 CA GLU B 54 28.762 28.222 52.526 1.00 22.11 AAAD C ATOM 2767 C GLU B 54 27.435 28.852 52.150 1.00 21.80 AAAD C ATOM 2768 O GLU B 54 27.173 29.070 50.968 1.00 26.60 AAAD O ATOM 2769 CB GLU B 54 29.744 29.393 52.689 1.00 18.30 AAAD C ATOM 2770 CG GLU B 54 31.189 29.053 52.999 1.00 27.78 AAAD C ATOM 2771 CD GLU B 54 32.046 30.298 53.199 1.00 26.10 AAAD C ATOM 2772 OE1 GLU B 54 31.491 31.416 53.208 1.00 26.73 AAAD O ATOM 2773 OE2 GLU B 54 33.280 30.165 53.345 1.00 33.81 AAAD O ATOM 2774 N VAL B 55 26.594 29.143 53.136 1.00 22.94 AAAD N ATOM 2775 CA VAL B 55 25.345 29.837 52.843 1.00 26.29 AAAD C ATOM 2776 C VAL B 55 25.761 31.306 52.715 1.00 25.35 AAAD C ATOM 2777 O VAL B 55 26.389 31.867 53.627 1.00 23.10 AAAD O ATOM 2778 CB VAL B 55 24.297 29.686 53.963 1.00 23.26 AAAD C ATOM 2779 CG1 VAL B 55 23.798 28.265 54.008 1.00 27.22 AAAD C ATOM 2780 CG2 VAL B 55 24.882 30.078 55.300 1.00 26.72 AAAD C ATOM 2781 N PRO B 56 25.493 31.926 51.555 1.00 24.59 AAAD N ATOM 2782 CA PRO B 56 25.865 33.330 51.354 1.00 22.51 AAAD C ATOM 2783 C PRO B 56 25.040 34.253 52.238 1.00 18.17 AAAD C ATOM 2784 O PRO B 56 23.866 34.493 51.970 1.00 20.77 AAAD O ATOM 2785 CB PRO B 56 25.571 33.547 49.866 1.00 20.65 AAAD C ATOM 2786 CG PRO B 56 24.383 32.664 49.631 1.00 19.85 AAAD C ATOM 2787 CD PRO B 56 24.776 31.398 50.379 1.00 25.96 AAAD C ATOM 2788 N ILE B 57 25.640 34.734 53.319 1.00 14.11 AAAD N ATOM 2789 CA ILE B 57 24.935 35.631 54.216 1.00 11.06 AAAD C ATOM 2790 C ILE B 57 25.930 36.637 54.758 1.00 12.93 AAAD C ATOM 2791 O ILE B 57 27.135 36.361 54.819 1.00 15.02 AAAD O ATOM 2792 CB ILE B 57 24.201 34.857 55.345 1.00 13.47 AAAD C ATOM 2793 CG1 ILE B 57 23.135 35.748 55.987 1.00 14.94 AAAD C ATOM 2794 CG2 ILE B 57 25.187 34.338 56.388 1.00 10.78 AAAD C ATOM 2795 CD1 ILE B 57 22.174 34.997 56.876 1.00 12.75 AAAD C ATOM 2796 N LEU B 58 25.433 37.836 55.041 1.00 16.33 AAAD N ATOM 2797 CA LEU B 58 26.253 38.928 55.548 1.00 15.37 AAAD C ATOM 2798 C LEU B 58 26.478 38.756 57.049 1.00 15.13 AAAD C ATOM 2799 O LEU B 58 25.564 38.376 57.785 1.00 10.34 AAAD O ATOM 2800 CB LEU B 58 25.549 40.264 55.255 1.00 15.06 AAAD C ATOM 2801 CG LEU B 58 26.322 41.590 55.181 1.00 16.85 AAAD C ATOM 2802 CD1 LEU B 58 27.341 41.558 54.052 1.00 18.24 AAAD C ATOM 2803 CD2 LEU B 58 25.346 42.722 54.950 1.00 12.15 AAAD C ATOM 2804 N THR B 59 27.706 38.996 57.492 1.00 16.83 AAAD N ATOM 2805 CA THR B 59 28.025 38.882 58.907 1.00 19.67 AAAD C ATOM 2806 C THR B 59 28.404 40.230 59.520 1.00 20.94 AAAD C ATOM 2807 O THR B 59 28.335 40.385 60.735 1.00 19.56 AAAD O ATOM 2808 CB THR B 59 29.161 37.871 59.164 1.00 20.67 AAAD C ATOM 2809 OG1 THR B 59 30.399 38.388 58.650 1.00 18.66 AAAD O ATOM 2810 CG2 THR B 59 28.841 36.515 58.501 1.00 21.21 AAAD C ATOM 2811 N THR B 60 28.768 41.206 58.683 1.00 21.15 AAAD N ATOM 2812 CA THR B 60 29.148 42.543 59.156 1.00 16.52 AAAD C ATOM 2813 C THR B 60 27.975 43.300 59.779 1.00 17.30 AAAD C ATOM 2814 O THR B 60 28.151 44.345 60.382 1.00 20.24 AAAD O ATOM 2815 CB THR B 60 29.748 43.380 58.032 1.00 14.89 AAAD C ATOM 2816 OG1 THR B 60 28.869 43.341 56.901 1.00 17.34 AAAD O ATOM 2817 CG2 THR B 60 31.144 42.859 57.645 1.00 2.00 AAAD C ATOM 2818 N LYS B 61 26.773 42.777 59.600 1.00 18.84 AAAD N ATOM 2819 CA LYS B 61 25.579 43.354 60.185 1.00 18.40 AAAD C ATOM 2820 C LYS B 61 24.606 42.190 60.151 1.00 21.69 AAAD C ATOM 2821 O LYS B 61 24.905 41.169 59.534 1.00 25.71 AAAD O ATOM 2822 CB LYS B 61 25.074 44.532 59.352 1.00 23.07 AAAD C ATOM 2823 CG LYS B 61 24.237 44.179 58.132 1.00 28.98 AAAD C ATOM 2824 CD LYS B 61 23.492 45.408 57.654 1.00 30.85 AAAD C ATOM 2825 CE LYS B 61 22.398 45.077 56.654 1.00 38.44 AAAD C ATOM 2826 NZ LYS B 61 21.817 46.332 56.083 1.00 39.08 AAAD N ATOM 2827 N LYS B 62 23.468 42.309 60.818 1.00 22.67 AAAD N ATOM 2828 CA LYS B 62 22.506 41.218 60.818 1.00 25.93 AAAD C ATOM 2829 C LYS B 62 21.574 41.257 59.612 1.00 28.84 AAAD C ATOM 2830 O LYS B 62 21.180 42.334 59.158 1.00 32.92 AAAD O ATOM 2831 CB LYS B 62 21.670 41.226 62.103 1.00 31.17 AAAD C ATOM 2832 CG LYS B 62 20.724 40.031 62.216 1.00 40.02 AAAD C ATOM 2833 CD LYS B 62 20.029 39.950 63.565 1.00 45.97 AAAD C ATOM 2834 CE LYS B 62 19.369 38.582 63.742 1.00 51.29 AAAD C ATOM 2835 NZ LYS B 62 18.778 38.377 65.102 1.00 54.89 AAAD N ATOM 2836 N VAL B 63 21.231 40.076 59.103 1.00 27.14 AAAD N ATOM 2837 CA VAL B 63 20.306 39.943 57.982 1.00 22.31 AAAD C ATOM 2838 C VAL B 63 19.036 39.332 58.571 1.00 24.37 AAAD C ATOM 2839 O VAL B 63 19.111 38.359 59.328 1.00 26.93 AAAD O ATOM 2840 CB VAL B 63 20.854 38.997 56.903 1.00 21.76 AAAD C ATOM 2841 CG1 VAL B 63 19.821 38.813 55.799 1.00 16.54 AAAD C ATOM 2842 CG2 VAL B 63 22.165 39.539 56.343 1.00 16.66 AAAD C ATOM 2843 N ALA B 64 17.880 39.895 58.234 1.00 18.92 AAAD N ATOM 2844 CA ALA B 64 16.604 39.404 58.754 1.00 18.72 AAAD C ATOM 2845 C ALA B 64 16.211 38.112 58.049 1.00 17.48 AAAD C ATOM 2846 O ALA B 64 15.207 38.063 57.325 1.00 17.44 AAAD O ATOM 2847 CB ALA B 64 15.508 40.475 58.576 1.00 15.14 AAAD C ATOM 2848 N TRP B 65 16.976 37.057 58.305 1.00 17.46 AAAD N ATOM 2849 CA TRP B 65 16.745 35.768 57.664 1.00 18.77 AAAD C ATOM 2850 C TRP B 65 15.367 35.132 57.835 1.00 16.63 AAAD C ATOM 2851 O TRP B 65 14.826 34.589 56.875 1.00 21.81 AAAD O ATOM 2852 CB TRP B 65 17.855 34.768 58.002 1.00 22.44 AAAD C ATOM 2853 CG TRP B 65 17.854 34.255 59.408 1.00 32.07 AAAD C ATOM 2854 CD1 TRP B 65 18.509 34.791 60.474 1.00 31.25 AAAD C ATOM 2855 CD2 TRP B 65 17.209 33.066 59.886 1.00 35.26 AAAD C ATOM 2856 NE1 TRP B 65 18.318 34.009 61.586 1.00 34.44 AAAD N ATOM 2857 CE2 TRP B 65 17.524 32.944 61.256 1.00 34.90 AAAD C ATOM 2858 CE3 TRP B 65 16.400 32.090 59.288 1.00 35.87 AAAD C ATOM 2859 CZ2 TRP B 65 17.058 31.886 62.042 1.00 34.02 AAAD C ATOM 2860 CZ3 TRP B 65 15.936 31.037 60.067 1.00 34.65 AAAD C ATOM 2861 CH2 TRP B 65 16.268 30.945 61.433 1.00 35.97 AAAD C ATOM 2862 N LYS B 66 14.765 35.225 59.016 1.00 13.95 AAAD N ATOM 2863 CA LYS B 66 13.447 34.615 59.201 1.00 17.10 AAAD C ATOM 2864 C LYS B 66 12.363 35.275 58.361 1.00 16.68 AAAD C ATOM 2865 O LYS B 66 11.371 34.641 58.004 1.00 16.45 AAAD O ATOM 2866 CB LYS B 66 13.022 34.606 60.667 1.00 22.94 AAAD C ATOM 2867 CG LYS B 66 13.508 33.409 61.451 1.00 28.47 AAAD C ATOM 2868 CD LYS B 66 12.814 33.336 62.795 1.00 38.53 AAAD C ATOM 2869 CE LYS B 66 13.191 32.074 63.543 1.00 46.90 AAAD C ATOM 2870 NZ LYS B 66 12.546 32.028 64.885 1.00 53.97 AAAD N ATOM 2871 N THR B 67 12.548 36.550 58.050 1.00 17.83 AAAD N ATOM 2872 CA THR B 67 11.584 37.275 57.240 1.00 18.14 AAAD C ATOM 2873 C THR B 67 11.830 36.960 55.759 1.00 15.90 AAAD C ATOM 2874 O THR B 67 10.895 36.879 54.960 1.00 16.17 AAAD O ATOM 2875 CB THR B 67 11.687 38.778 57.497 1.00 18.86 AAAD C ATOM 2876 OG1 THR B 67 11.803 39.006 58.910 1.00 21.81 AAAD O ATOM 2877 CG2 THR B 67 10.440 39.480 56.980 1.00 18.47 AAAD C ATOM 2878 N ALA B 68 13.098 36.752 55.416 1.00 11.81 AAAD N ATOM 2879 CA ALA B 68 13.493 36.416 54.058 1.00 11.07 AAAD C ATOM 2880 C ALA B 68 12.800 35.124 53.658 1.00 14.34 AAAD C ATOM 2881 O ALA B 68 12.139 35.053 52.617 1.00 19.19 AAAD O ATOM 2882 CB ALA B 68 14.998 36.249 53.980 1.00 11.75 AAAD C ATOM 2883 N ILE B 69 12.912 34.114 54.513 1.00 14.58 AAAD N ATOM 2884 CA ILE B 69 12.287 32.827 54.249 1.00 13.77 AAAD C ATOM 2885 C ILE B 69 10.754 32.924 54.272 1.00 14.02 AAAD C ATOM 2886 O ILE B 69 10.095 32.357 53.402 1.00 11.66 AAAD O ATOM 2887 CB ILE B 69 12.790 31.739 55.223 1.00 10.42 AAAD C ATOM 2888 CG1 ILE B 69 14.319 31.707 55.226 1.00 11.81 AAAD C ATOM 2889 CG2 ILE B 69 12.307 30.379 54.770 1.00 17.56 AAAD C ATOM 2890 CD1 ILE B 69 14.916 30.740 56.214 1.00 2.96 AAAD C ATOM 2891 N LYS B 70 10.188 33.637 55.250 1.00 15.54 AAAD N ATOM 2892 CA LYS B 70 8.727 33.808 55.337 1.00 17.94 AAAD C ATOM 2893 C LYS B 70 8.193 34.441 54.057 1.00 19.98 AAAD C ATOM 2894 O LYS B 70 7.151 34.032 53.525 1.00 20.22 AAAD O ATOM 2895 CB LYS B 70 8.343 34.709 56.514 1.00 19.84 AAAD C ATOM 2896 CG LYS B 70 8.400 34.051 57.882 1.00 29.24 AAAD C ATOM 2897 CD LYS B 70 8.422 35.109 58.976 1.00 30.65 AAAD C ATOM 2898 CE LYS B 70 8.557 34.497 60.351 1.00 29.64 AAAD C ATOM 2899 NZ LYS B 70 7.259 33.989 60.862 1.00 31.27 AAAD N ATOM 2900 N GLU B 71 8.911 35.452 53.579 1.00 17.75 AAAD N ATOM 2901 CA GLU B 71 8.538 36.158 52.360 1.00 17.88 AAAD C ATOM 2902 C GLU B 71 8.631 35.186 51.191 1.00 13.64 AAAD C ATOM 2903 O GLU B 71 7.737 35.137 50.346 1.00 16.28 AAAD O ATOM 2904 CB GLU B 71 9.477 37.346 52.134 1.00 19.32 AAAD C ATOM 2905 CG GLU B 71 9.173 38.178 50.900 1.00 20.96 AAAD C ATOM 2906 CD GLU B 71 10.120 39.356 50.759 1.00 26.55 AAAD C ATOM 2907 OE1 GLU B 71 10.039 40.286 51.597 1.00 28.07 AAAD O ATOM 2908 OE2 GLU B 71 10.956 39.346 49.827 1.00 24.52 AAAD O ATOM 2909 N LEU B 72 9.701 34.392 51.169 1.00 12.52 AAAD N ATOM 2910 CA LEU B 72 9.919 33.401 50.115 1.00 11.64 AAAD C ATOM 2911 C LEU B 72 8.753 32.420 50.020 1.00 13.01 AAAD C ATOM 2912 O LEU B 72 8.209 32.196 48.935 1.00 16.53 AAAD O ATOM 2913 CB LEU B 72 11.213 32.635 50.367 1.00 11.44 AAAD C ATOM 2914 CG LEU B 72 11.631 31.670 49.262 1.00 18.98 AAAD C ATOM 2915 CD1 LEU B 72 11.860 32.452 47.963 1.00 21.08 AAAD C ATOM 2916 CD2 LEU B 72 12.899 30.927 49.680 1.00 16.38 AAAD C ATOM 2917 N LEU B 73 8.342 31.875 51.161 1.00 12.27 AAAD N ATOM 2918 CA LEU B 73 7.240 30.922 51.202 1.00 17.20 AAAD C ATOM 2919 C LEU B 73 5.962 31.528 50.658 1.00 16.94 AAAD C ATOM 2920 O LEU B 73 5.235 30.879 49.913 1.00 21.37 AAAD O ATOM 2921 CB LEU B 73 6.987 30.429 52.629 1.00 15.98 AAAD C ATOM 2922 CG LEU B 73 8.133 29.729 53.348 1.00 18.69 AAAD C ATOM 2923 CD1 LEU B 73 7.588 29.179 54.637 1.00 22.73 AAAD C ATOM 2924 CD2 LEU B 73 8.719 28.618 52.501 1.00 15.78 AAAD C ATOM 2925 N TRP B 74 5.689 32.768 51.047 1.00 19.67 AAAD N ATOM 2926 CA TRP B 74 4.493 33.494 50.617 1.00 17.10 AAAD C ATOM 2927 C TRP B 74 4.443 33.663 49.096 1.00 13.96 AAAD C ATOM 2928 O TRP B 74 3.424 33.383 48.461 1.00 14.79 AAAD O ATOM 2929 CB TRP B 74 4.470 34.854 51.325 1.00 18.33 AAAD C ATOM 2930 CG TRP B 74 3.354 35.781 50.950 1.00 14.21 AAAD C ATOM 2931 CD1 TRP B 74 2.014 35.572 51.116 1.00 10.24 AAAD C ATOM 2932 CD2 TRP B 74 3.491 37.088 50.377 1.00 14.74 AAAD C ATOM 2933 NE1 TRP B 74 1.310 36.667 50.680 1.00 9.76 AAAD N ATOM 2934 CE2 TRP B 74 2.188 37.613 50.223 1.00 14.15 AAAD C ATOM 2935 CE3 TRP B 74 4.590 37.865 49.979 1.00 11.97 AAAD C ATOM 2936 CZ2 TRP B 74 1.949 38.885 49.687 1.00 13.29 AAAD C ATOM 2937 CZ3 TRP B 74 4.353 39.129 49.448 1.00 14.38 AAAD C ATOM 2938 CH2 TRP B 74 3.039 39.626 49.307 1.00 16.03 AAAD C ATOM 2939 N ILE B 75 5.564 34.084 48.523 1.00 14.45 AAAD N ATOM 2940 CA ILE B 75 5.689 34.302 47.078 1.00 16.63 AAAD C ATOM 2941 C ILE B 75 5.676 32.983 46.287 1.00 19.20 AAAD C ATOM 2942 O ILE B 75 4.829 32.774 45.408 1.00 15.03 AAAD O ATOM 2943 CB ILE B 75 7.028 35.039 46.746 1.00 17.14 AAAD C ATOM 2944 CG1 ILE B 75 7.086 36.402 47.440 1.00 14.01 AAAD C ATOM 2945 CG2 ILE B 75 7.196 35.210 45.241 1.00 12.05 AAAD C ATOM 2946 CD1 ILE B 75 8.428 37.081 47.304 1.00 12.25 AAAD C ATOM 2947 N TRP B 76 6.632 32.109 46.601 1.00 17.44 AAAD N ATOM 2948 CA TRP B 76 6.784 30.828 45.919 1.00 16.17 AAAD C ATOM 2949 C TRP B 76 5.864 29.676 46.307 1.00 17.64 AAAD C ATOM 2950 O TRP B 76 5.154 29.146 45.454 1.00 23.47 AAAD O ATOM 2951 CB TRP B 76 8.228 30.363 46.010 1.00 15.74 AAAD C ATOM 2952 CG TRP B 76 9.135 31.115 45.117 1.00 19.72 AAAD C ATOM 2953 CD1 TRP B 76 9.633 32.366 45.319 1.00 19.64 AAAD C ATOM 2954 CD2 TRP B 76 9.667 30.664 43.870 1.00 23.55 AAAD C ATOM 2955 NE1 TRP B 76 10.448 32.726 44.276 1.00 21.13 AAAD N ATOM 2956 CE2 TRP B 76 10.487 31.700 43.369 1.00 26.29 AAAD C ATOM 2957 CE3 TRP B 76 9.536 29.482 43.126 1.00 20.63 AAAD C ATOM 2958 CZ2 TRP B 76 11.175 31.589 42.153 1.00 29.03 AAAD C ATOM 2959 CZ3 TRP B 76 10.216 29.370 41.924 1.00 20.89 AAAD C ATOM 2960 CH2 TRP B 76 11.026 30.418 41.448 1.00 27.48 AAAD C ATOM 2961 N GLN B 77 5.877 29.269 47.574 1.00 15.35 AAAD N ATOM 2962 CA GLN B 77 5.055 28.138 48.008 1.00 14.02 AAAD C ATOM 2963 C GLN B 77 3.559 28.397 48.045 1.00 12.65 AAAD C ATOM 2964 O GLN B 77 2.782 27.666 47.435 1.00 14.13 AAAD O ATOM 2965 CB GLN B 77 5.513 27.636 49.366 1.00 17.24 AAAD C ATOM 2966 CG GLN B 77 4.864 26.334 49.776 1.00 21.46 AAAD C ATOM 2967 CD GLN B 77 5.082 26.042 51.235 1.00 20.83 AAAD C ATOM 2968 OE1 GLN B 77 4.267 26.413 52.073 1.00 29.08 AAAD O ATOM 2969 NE2 GLN B 77 6.196 25.411 51.556 1.00 19.06 AAAD N ATOM 2970 N LEU B 78 3.148 29.393 48.816 1.00 15.66 AAAD N ATOM 2971 CA LEU B 78 1.734 29.726 48.914 1.00 18.64 AAAD C ATOM 2972 C LEU B 78 1.256 30.401 47.634 1.00 16.96 AAAD C ATOM 2973 O LEU B 78 0.057 30.416 47.364 1.00 14.61 AAAD O ATOM 2974 CB LEU B 78 1.475 30.659 50.100 1.00 21.23 AAAD C ATOM 2975 CG LEU B 78 1.989 30.238 51.476 1.00 28.81 AAAD C ATOM 2976 CD1 LEU B 78 1.640 31.325 52.493 1.00 30.06 AAAD C ATOM 2977 CD2 LEU B 78 1.390 28.894 51.888 1.00 29.26 AAAD C ATOM 2978 N LYS B 79 2.194 30.984 46.879 1.00 19.30 AAAD N ATOM 2979 CA LYS B 79 1.894 31.697 45.632 1.00 22.23 AAAD C ATOM 2980 C LYS B 79 0.785 32.707 45.892 1.00 23.09 AAAD C ATOM 2981 O LYS B 79 -0.172 32.815 45.108 1.00 24.07 AAAD O ATOM 2982 CB LYS B 79 1.453 30.729 44.529 1.00 21.56 AAAD C ATOM 2983 CG LYS B 79 2.476 29.682 44.160 1.00 24.48 AAAD C ATOM 2984 CD LYS B 79 1.801 28.542 43.431 1.00 27.20 AAAD C ATOM 2985 CE LYS B 79 2.545 27.238 43.636 1.00 29.68 AAAD C ATOM 2986 NZ LYS B 79 1.748 26.083 43.135 1.00 25.97 AAAD N ATOM 2987 N SER B 80 0.915 33.430 47.002 1.00 20.34 AAAD N ATOM 2988 CA SER B 80 -0.081 34.414 47.392 1.00 19.49 AAAD C ATOM 2989 C SER B 80 0.320 35.868 47.122 1.00 17.88 AAAD C ATOM 2990 O SER B 80 1.499 36.230 47.149 1.00 15.97 AAAD O ATOM 2991 CB SER B 80 -0.437 34.234 48.870 1.00 16.45 AAAD C ATOM 2992 OG SER B 80 -1.379 35.207 49.304 1.00 15.76 AAAD O ATOM 2993 N ASN B 81 -0.674 36.682 46.800 1.00 16.56 AAAD N ATOM 2994 CA ASN B 81 -0.446 38.099 46.564 1.00 21.95 AAAD C ATOM 2995 C ASN B 81 -1.209 38.838 47.666 1.00 25.47 AAAD C ATOM 2996 O ASN B 81 -1.199 40.070 47.748 1.00 26.28 AAAD O ATOM 2997 CB ASN B 81 -0.934 38.513 45.170 1.00 19.07 AAAD C ATOM 2998 CG ASN B 81 -2.440 38.410 45.014 1.00 19.76 AAAD C ATOM 2999 OD1 ASN B 81 -3.128 37.836 45.850 1.00 21.67 AAAD O ATOM 3000 ND2 ASN B 81 -2.959 38.973 43.934 1.00 20.02 AAAD N ATOM 3001 N ASP B 82 -1.851 38.049 48.526 1.00 30.03 AAAD N ATOM 3002 CA ASP B 82 -2.640 38.544 49.646 1.00 27.76 AAAD C ATOM 3003 C ASP B 82 -1.690 38.859 50.792 1.00 27.11 AAAD C ATOM 3004 O ASP B 82 -0.958 37.989 51.262 1.00 28.59 AAAD O ATOM 3005 CB ASP B 82 -3.637 37.467 50.080 1.00 26.03 AAAD C ATOM 3006 CG ASP B 82 -4.817 38.028 50.837 1.00 25.68 AAAD C ATOM 3007 OD1 ASP B 82 -4.603 38.698 51.862 1.00 27.25 AAAD O ATOM 3008 OD2 ASP B 82 -5.966 37.787 50.405 1.00 25.77 AAAD O ATOM 3009 N VAL B 83 -1.718 40.101 51.251 1.00 27.66 AAAD N ATOM 3010 CA VAL B 83 -0.856 40.534 52.338 1.00 24.33 AAAD C ATOM 3011 C VAL B 83 -1.308 39.967 53.678 1.00 23.28 AAAD C ATOM 3012 O VAL B 83 -0.487 39.755 54.569 1.00 20.64 AAAD O ATOM 3013 CB VAL B 83 -0.772 42.072 52.397 1.00 25.04 AAAD C ATOM 3014 CG1 VAL B 83 0.205 42.511 53.479 1.00 23.47 AAAD C ATOM 3015 CG2 VAL B 83 -0.335 42.612 51.042 1.00 24.13 AAAD C ATOM 3016 N ASN B 84 -2.599 39.680 53.811 1.00 21.26 AAAD N ATOM 3017 CA ASN B 84 -3.116 39.121 55.059 1.00 25.35 AAAD C ATOM 3018 C ASN B 84 -2.433 37.788 55.370 1.00 27.33 AAAD C ATOM 3019 O ASN B 84 -2.086 37.515 56.524 1.00 28.08 AAAD O ATOM 3020 CB ASN B 84 -4.635 38.939 55.001 1.00 33.60 AAAD C ATOM 3021 CG ASN B 84 -5.374 40.248 54.730 1.00 42.26 AAAD C ATOM 3022 OD1 ASN B 84 -5.043 41.286 55.298 1.00 46.47 AAAD O ATOM 3023 ND2 ASN B 84 -6.372 40.203 53.844 1.00 43.62 AAAD N ATOM 3024 N ASP B 85 -2.186 36.987 54.334 1.00 24.76 AAAD N ATOM 3025 CA ASP B 85 -1.524 35.692 54.506 1.00 23.10 AAAD C ATOM 3026 C ASP B 85 -0.112 35.898 55.024 1.00 21.95 AAAD C ATOM 3027 O ASP B 85 0.404 35.083 55.783 1.00 28.40 AAAD O ATOM 3028 CB ASP B 85 -1.469 34.906 53.189 1.00 20.12 AAAD C ATOM 3029 CG ASP B 85 -2.840 34.547 52.659 1.00 20.11 AAAD C ATOM 3030 OD1 ASP B 85 -3.825 34.608 53.426 1.00 25.03 AAAD O ATOM 3031 OD2 ASP B 85 -2.932 34.209 51.464 1.00 20.01 AAAD O ATOM 3032 N LEU B 86 0.523 36.977 54.593 1.00 19.37 AAAD N ATOM 3033 CA LEU B 86 1.871 37.279 55.040 1.00 18.11 AAAD C ATOM 3034 C LEU B 86 1.799 37.777 56.488 1.00 19.34 AAAD C ATOM 3035 O LEU B 86 2.697 37.513 57.292 1.00 19.25 AAAD O ATOM 3036 CB LEU B 86 2.481 38.336 54.133 1.00 14.93 AAAD C ATOM 3037 CG LEU B 86 3.966 38.649 54.287 1.00 23.60 AAAD C ATOM 3038 CD1 LEU B 86 4.827 37.393 54.112 1.00 12.76 AAAD C ATOM 3039 CD2 LEU B 86 4.326 39.712 53.262 1.00 20.34 AAAD C ATOM 3040 N ASN B 87 0.710 38.464 56.825 1.00 17.48 AAAD N ATOM 3041 CA ASN B 87 0.525 38.981 58.177 1.00 20.15 AAAD C ATOM 3042 C ASN B 87 0.407 37.844 59.177 1.00 22.93 AAAD C ATOM 3043 O ASN B 87 1.028 37.883 60.238 1.00 23.36 AAAD O ATOM 3044 CB ASN B 87 -0.702 39.893 58.265 1.00 18.44 AAAD C ATOM 3045 CG ASN B 87 -0.450 41.283 57.692 1.00 19.35 AAAD C ATOM 3046 OD1 ASN B 87 -1.384 42.062 57.530 1.00 22.86 AAAD O ATOM 3047 ND2 ASN B 87 0.810 41.608 57.405 1.00 9.19 AAAD N ATOM 3048 N MET B 88 -0.376 36.828 58.825 1.00 25.91 AAAD N ATOM 3049 CA MET B 88 -0.559 35.649 59.667 1.00 25.72 AAAD C ATOM 3050 C MET B 88 0.783 34.956 59.940 1.00 24.31 AAAD C ATOM 3051 O MET B 88 0.892 34.142 60.853 1.00 27.37 AAAD O ATOM 3052 CB MET B 88 -1.521 34.668 58.999 1.00 33.34 AAAD C ATOM 3053 CG MET B 88 -2.883 35.250 58.688 1.00 44.22 AAAD C ATOM 3054 SD MET B 88 -3.947 34.062 57.836 1.00 61.60 AAAD S ATOM 3055 CE MET B 88 -5.553 34.501 58.509 1.00 58.18 AAAD C ATOM 3056 N MET B 89 1.787 35.242 59.118 1.00 23.18 AAAD N ATOM 3057 CA MET B 89 3.124 34.675 59.303 1.00 23.09 AAAD C ATOM 3058 C MET B 89 3.941 35.635 60.178 1.00 24.00 AAAD C ATOM 3059 O MET B 89 5.149 35.467 60.348 1.00 21.01 AAAD O ATOM 3060 CB MET B 89 3.829 34.481 57.951 1.00 25.49 AAAD C ATOM 3061 CG MET B 89 3.170 33.452 57.022 1.00 31.76 AAAD C ATOM 3062 SD MET B 89 4.039 33.208 55.447 1.00 27.71 AAAD S ATOM 3063 CE MET B 89 5.478 32.353 56.016 1.00 29.06 AAAD C ATOM 3064 N GLY B 90 3.271 36.644 60.725 1.00 22.83 AAAD N ATOM 3065 CA GLY B 90 3.928 37.624 61.562 1.00 20.97 AAAD C ATOM 3066 C GLY B 90 4.777 38.645 60.832 1.00 23.16 AAAD C ATOM 3067 O GLY B 90 5.757 39.131 61.396 1.00 29.02 AAAD O ATOM 3068 N VAL B 91 4.430 38.980 59.594 1.00 22.40 AAAD N ATOM 3069 CA VAL B 91 5.203 39.969 58.838 1.00 19.50 AAAD C ATOM 3070 C VAL B 91 4.296 41.121 58.453 1.00 18.13 AAAD C ATOM 3071 O VAL B 91 3.211 40.914 57.927 1.00 18.26 AAAD O ATOM 3072 CB VAL B 91 5.812 39.386 57.536 1.00 19.78 AAAD C ATOM 3073 CG1 VAL B 91 6.567 40.469 56.790 1.00 19.16 AAAD C ATOM 3074 CG2 VAL B 91 6.740 38.206 57.839 1.00 17.69 AAAD C ATOM 3075 N HIS B 92 4.739 42.339 58.728 1.00 20.76 AAAD N ATOM 3076 CA HIS B 92 3.954 43.525 58.406 1.00 19.93 AAAD C ATOM 3077 C HIS B 92 4.669 44.500 57.473 1.00 19.98 AAAD C ATOM 3078 O HIS B 92 4.098 45.532 57.113 1.00 19.55 AAAD O ATOM 3079 CB HIS B 92 3.496 44.238 59.688 1.00 19.89 AAAD C ATOM 3080 CG HIS B 92 2.402 43.519 60.421 1.00 21.34 AAAD C ATOM 3081 ND1 HIS B 92 1.068 43.687 60.119 1.00 18.19 AAAD N ATOM 3082 CD2 HIS B 92 2.449 42.601 61.417 1.00 20.13 AAAD C ATOM 3083 CE1 HIS B 92 0.338 42.901 60.892 1.00 21.61 AAAD C ATOM 3084 NE2 HIS B 92 1.154 42.232 61.688 1.00 19.68 AAAD N ATOM 3085 N ILE B 93 5.868 44.135 57.010 1.00 19.17 AAAD N ATOM 3086 CA ILE B 93 6.645 45.005 56.122 1.00 22.52 AAAD C ATOM 3087 C ILE B 93 6.031 45.307 54.755 1.00 21.32 AAAD C ATOM 3088 O ILE B 93 6.376 46.313 54.140 1.00 25.74 AAAD O ATOM 3089 CB ILE B 93 8.116 44.520 55.928 1.00 22.05 AAAD C ATOM 3090 CG1 ILE B 93 8.162 43.219 55.127 1.00 26.10 AAAD C ATOM 3091 CG2 ILE B 93 8.808 44.349 57.281 1.00 22.60 AAAD C ATOM 3092 CD1 ILE B 93 9.575 42.781 54.748 1.00 21.08 AAAD C ATOM 3093 N TRP B 94 5.121 44.463 54.277 1.00 23.84 AAAD N ATOM 3094 CA TRP B 94 4.482 44.698 52.975 1.00 24.00 AAAD C ATOM 3095 C TRP B 94 3.158 45.462 53.085 1.00 25.50 AAAD C ATOM 3096 O TRP B 94 2.577 45.850 52.071 1.00 25.15 AAAD O ATOM 3097 CB TRP B 94 4.233 43.376 52.236 1.00 24.25 AAAD C ATOM 3098 CG TRP B 94 5.467 42.735 51.679 1.00 21.50 AAAD C ATOM 3099 CD1 TRP B 94 6.524 42.234 52.386 1.00 23.34 AAAD C ATOM 3100 CD2 TRP B 94 5.772 42.521 50.297 1.00 21.85 AAAD C ATOM 3101 NE1 TRP B 94 7.468 41.721 51.529 1.00 21.91 AAAD N ATOM 3102 CE2 TRP B 94 7.034 41.885 50.240 1.00 19.61 AAAD C ATOM 3103 CE3 TRP B 94 5.104 42.805 49.100 1.00 19.11 AAAD C ATOM 3104 CZ2 TRP B 94 7.640 41.526 49.031 1.00 20.06 AAAD C ATOM 3105 CZ3 TRP B 94 5.710 42.448 47.896 1.00 23.86 AAAD C ATOM 3106 CH2 TRP B 94 6.965 41.815 47.873 1.00 18.62 AAAD C ATOM 3107 N ASP B 95 2.698 45.698 54.313 1.00 28.95 AAAD N ATOM 3108 CA ASP B 95 1.425 46.392 54.567 1.00 28.66 AAAD C ATOM 3109 C ASP B 95 1.266 47.710 53.816 1.00 28.51 AAAD C ATOM 3110 O ASP B 95 0.166 48.089 53.425 1.00 29.83 AAAD O ATOM 3111 CB ASP B 95 1.245 46.636 56.071 1.00 28.68 AAAD C ATOM 3112 CG ASP B 95 0.926 45.370 56.842 1.00 26.94 AAAD C ATOM 3113 OD1 ASP B 95 1.324 44.272 56.411 1.00 27.83 AAAD O ATOM 3114 OD2 ASP B 95 0.265 45.476 57.890 1.00 31.96 AAAD O ATOM 3115 N GLN B 96 2.372 48.412 53.635 1.00 29.30 AAAD N ATOM 3116 CA GLN B 96 2.375 49.683 52.934 1.00 31.41 AAAD C ATOM 3117 C GLN B 96 1.926 49.548 51.483 1.00 33.60 AAAD C ATOM 3118 O GLN B 96 1.406 50.498 50.911 1.00 36.42 AAAD O ATOM 3119 CB GLN B 96 3.781 50.266 52.964 1.00 33.77 AAAD C ATOM 3120 CG GLN B 96 4.831 49.238 52.596 1.00 39.14 AAAD C ATOM 3121 CD GLN B 96 6.212 49.819 52.446 1.00 40.62 AAAD C ATOM 3122 OE1 GLN B 96 6.435 50.723 51.642 1.00 43.21 AAAD O ATOM 3123 NE2 GLN B 96 7.161 49.274 53.192 1.00 41.31 AAAD N ATOM 3124 N TRP B 97 2.102 48.359 50.908 1.00 34.98 AAAD N ATOM 3125 CA TRP B 97 1.763 48.106 49.512 1.00 33.31 AAAD C ATOM 3126 C TRP B 97 0.394 47.506 49.232 1.00 34.00 AAAD C ATOM 3127 O TRP B 97 0.044 47.315 48.065 1.00 34.34 AAAD O ATOM 3128 CB TRP B 97 2.811 47.189 48.884 1.00 35.85 AAAD C ATOM 3129 CG TRP B 97 4.207 47.659 49.059 1.00 41.73 AAAD C ATOM 3130 CD1 TRP B 97 5.125 47.200 49.965 1.00 41.84 AAAD C ATOM 3131 CD2 TRP B 97 4.855 48.694 48.320 1.00 42.21 AAAD C ATOM 3132 NE1 TRP B 97 6.304 47.895 49.837 1.00 43.61 AAAD N ATOM 3133 CE2 TRP B 97 6.165 48.820 48.835 1.00 42.72 AAAD C ATOM 3134 CE3 TRP B 97 4.456 49.530 47.271 1.00 44.96 AAAD C ATOM 3135 CZ2 TRP B 97 7.078 49.750 48.338 1.00 45.53 AAAD C ATOM 3136 CZ3 TRP B 97 5.370 50.457 46.772 1.00 49.13 AAAD C ATOM 3137 CH2 TRP B 97 6.665 50.558 47.309 1.00 47.25 AAAD C ATOM 3138 N LYS B 98 -0.392 47.201 50.258 1.00 33.62 AAAD N ATOM 3139 CA LYS B 98 -1.683 46.591 49.971 1.00 37.20 AAAD C ATOM 3140 C LYS B 98 -2.778 47.545 49.511 1.00 36.61 AAAD C ATOM 3141 O LYS B 98 -2.966 48.630 50.066 1.00 36.83 AAAD O ATOM 3142 CB LYS B 98 -2.171 45.691 51.112 1.00 36.36 AAAD C ATOM 3143 CG LYS B 98 -2.413 46.373 52.430 1.00 40.77 AAAD C ATOM 3144 CD LYS B 98 -3.255 45.488 53.318 1.00 45.39 AAAD C ATOM 3145 CE LYS B 98 -3.551 46.142 54.656 1.00 50.98 AAAD C ATOM 3146 NZ LYS B 98 -4.714 45.482 55.324 1.00 57.79 AAAD N ATOM 3147 N GLN B 99 -3.449 47.138 48.438 1.00 36.45 AAAD N ATOM 3148 CA GLN B 99 -4.547 47.888 47.847 1.00 34.20 AAAD C ATOM 3149 C GLN B 99 -5.772 47.660 48.722 1.00 35.28 AAAD C ATOM 3150 O GLN B 99 -5.683 46.977 49.744 1.00 37.02 AAAD O ATOM 3151 CB GLN B 99 -4.810 47.385 46.431 1.00 31.57 AAAD C ATOM 3152 CG GLN B 99 -3.557 47.321 45.576 1.00 34.84 AAAD C ATOM 3153 CD GLN B 99 -3.784 46.604 44.263 1.00 38.92 AAAD C ATOM 3154 OE1 GLN B 99 -3.223 46.979 43.234 1.00 41.22 AAAD O ATOM 3155 NE2 GLN B 99 -4.607 45.562 44.290 1.00 42.84 AAAD N ATOM 3156 N GLU B 100 -6.927 48.160 48.299 1.00 36.24 AAAD N ATOM 3157 CA GLU B 100 -8.132 48.009 49.107 1.00 39.41 AAAD C ATOM 3158 C GLU B 100 -8.473 46.557 49.381 1.00 37.54 AAAD C ATOM 3159 O GLU B 100 -8.821 46.200 50.508 1.00 34.40 AAAD O ATOM 3160 CB GLU B 100 -9.324 48.727 48.473 1.00 47.26 AAAD C ATOM 3161 CG GLU B 100 -10.474 48.946 49.457 1.00 56.84 AAAD C ATOM 3162 CD GLU B 100 -11.586 49.822 48.908 1.00 58.77 AAAD C ATOM 3163 OE1 GLU B 100 -11.320 50.649 48.006 1.00 60.93 AAAD O ATOM 3164 OE2 GLU B 100 -12.729 49.685 49.397 1.00 58.70 AAAD O ATOM 3165 N ASP B 101 -8.318 45.721 48.358 1.00 35.28 AAAD N ATOM 3166 CA ASP B 101 -8.603 44.291 48.477 1.00 34.02 AAAD C ATOM 3167 C ASP B 101 -7.590 43.532 49.335 1.00 30.78 AAAD C ATOM 3168 O ASP B 101 -7.712 42.328 49.519 1.00 33.30 AAAD O ATOM 3169 CB ASP B 101 -8.717 43.639 47.091 1.00 34.57 AAAD C ATOM 3170 CG ASP B 101 -7.449 43.782 46.255 1.00 37.02 AAAD C ATOM 3171 OD1 ASP B 101 -6.460 44.389 46.723 1.00 38.97 AAAD O ATOM 3172 OD2 ASP B 101 -7.441 43.276 45.112 1.00 41.35 AAAD O ATOM 3173 N GLY B 102 -6.579 44.229 49.836 1.00 28.56 AAAD N ATOM 3174 CA GLY B 102 -5.587 43.581 50.672 1.00 27.25 AAAD C ATOM 3175 C GLY B 102 -4.559 42.778 49.910 1.00 26.48 AAAD C ATOM 3176 O GLY B 102 -3.802 42.018 50.512 1.00 27.42 AAAD O ATOM 3177 N THR B 103 -4.533 42.927 48.591 1.00 28.14 AAAD N ATOM 3178 CA THR B 103 -3.563 42.213 47.763 1.00 24.99 AAAD C ATOM 3179 C THR B 103 -2.625 43.253 47.173 1.00 23.09 AAAD C ATOM 3180 O THR B 103 -2.942 44.445 47.166 1.00 21.34 AAAD O ATOM 3181 CB THR B 103 -4.235 41.476 46.589 1.00 21.70 AAAD C ATOM 3182 OG1 THR B 103 -4.725 42.433 45.641 1.00 20.68 AAAD O ATOM 3183 CG2 THR B 103 -5.397 40.619 47.077 1.00 21.77 AAAD C ATOM 3184 N ILE B 104 -1.473 42.806 46.687 1.00 18.81 AAAD N ATOM 3185 CA ILE B 104 -0.511 43.703 46.067 1.00 14.29 AAAD C ATOM 3186 C ILE B 104 -0.697 43.693 44.551 1.00 14.43 AAAD C ATOM 3187 O ILE B 104 0.242 43.926 43.789 1.00 20.35 AAAD O ATOM 3188 CB ILE B 104 0.934 43.307 46.413 1.00 14.85 AAAD C ATOM 3189 CG1 ILE B 104 1.189 41.837 46.056 1.00 11.87 AAAD C ATOM 3190 CG2 ILE B 104 1.216 43.600 47.892 1.00 14.46 AAAD C ATOM 3191 CD1 ILE B 104 2.663 41.456 46.049 1.00 10.33 AAAD C ATOM 3192 N GLY B 105 -1.920 43.433 44.114 1.00 15.05 AAAD N ATOM 3193 CA GLY B 105 -2.198 43.389 42.693 1.00 18.01 AAAD C ATOM 3194 C GLY B 105 -1.793 42.068 42.065 1.00 18.77 AAAD C ATOM 3195 O GLY B 105 -1.691 41.049 42.747 1.00 20.02 AAAD O ATOM 3196 N HIS B 106 -1.581 42.084 40.754 1.00 18.73 AAAD N ATOM 3197 CA HIS B 106 -1.193 40.896 40.006 1.00 17.56 AAAD C ATOM 3198 C HIS B 106 0.321 40.707 39.963 1.00 18.14 AAAD C ATOM 3199 O HIS B 106 0.877 40.293 38.943 1.00 19.97 AAAD O ATOM 3200 CB HIS B 106 -1.749 40.975 38.588 1.00 16.90 AAAD C ATOM 3201 CG HIS B 106 -3.233 40.824 38.515 1.00 18.69 AAAD C ATOM 3202 ND1 HIS B 106 -3.911 40.714 37.322 1.00 22.78 AAAD N ATOM 3203 CD2 HIS B 106 -4.170 40.733 39.489 1.00 23.90 AAAD C ATOM 3204 CE1 HIS B 106 -5.200 40.559 37.560 1.00 26.91 AAAD C ATOM 3205 NE2 HIS B 106 -5.384 40.566 38.868 1.00 25.60 AAAD N ATOM 3206 N ALA B 107 0.981 40.961 41.086 1.00 15.82 AAAD N ATOM 3207 CA ALA B 107 2.431 40.832 41.158 1.00 14.09 AAAD C ATOM 3208 C ALA B 107 2.894 39.626 41.981 1.00 14.80 AAAD C ATOM 3209 O ALA B 107 2.096 38.965 42.660 1.00 8.16 AAAD O ATOM 3210 CB ALA B 107 3.035 42.116 41.727 1.00 11.66 AAAD C ATOM 3211 N TYR B 108 4.188 39.336 41.876 1.00 16.11 AAAD N ATOM 3212 CA TYR B 108 4.840 38.248 42.604 1.00 19.46 AAAD C ATOM 3213 C TYR B 108 4.094 36.909 42.636 1.00 19.43 AAAD C ATOM 3214 O TYR B 108 3.921 36.261 41.594 1.00 19.37 AAAD O ATOM 3215 CB TYR B 108 5.174 38.706 44.024 1.00 17.99 AAAD C ATOM 3216 CG TYR B 108 6.246 39.764 44.094 1.00 16.59 AAAD C ATOM 3217 CD1 TYR B 108 7.591 39.405 44.147 1.00 19.01 AAAD C ATOM 3218 CD2 TYR B 108 5.922 41.115 44.152 1.00 12.23 AAAD C ATOM 3219 CE1 TYR B 108 8.593 40.359 44.263 1.00 14.56 AAAD C ATOM 3220 CE2 TYR B 108 6.919 42.082 44.264 1.00 16.66 AAAD C ATOM 3221 CZ TYR B 108 8.252 41.693 44.327 1.00 15.91 AAAD C ATOM 3222 OH TYR B 108 9.247 42.629 44.494 1.00 13.35 AAAD O ATOM 3223 N GLY B 109 3.648 36.515 43.827 1.00 17.64 AAAD N ATOM 3224 CA GLY B 109 2.943 35.262 44.008 1.00 18.84 AAAD C ATOM 3225 C GLY B 109 1.827 35.006 43.026 1.00 17.33 AAAD C ATOM 3226 O GLY B 109 1.585 33.855 42.662 1.00 16.61 AAAD O ATOM 3227 N PHE B 110 1.151 36.066 42.588 1.00 18.51 AAAD N ATOM 3228 CA PHE B 110 0.057 35.916 41.633 1.00 18.49 AAAD C ATOM 3229 C PHE B 110 0.559 35.347 40.309 1.00 17.72 AAAD C ATOM 3230 O PHE B 110 -0.103 34.510 39.693 1.00 21.21 AAAD O ATOM 3231 CB PHE B 110 -0.634 37.247 41.380 1.00 15.64 AAAD C ATOM 3232 CG PHE B 110 -1.779 37.155 40.411 1.00 12.05 AAAD C ATOM 3233 CD1 PHE B 110 -3.056 36.837 40.853 1.00 10.78 AAAD C ATOM 3234 CD2 PHE B 110 -1.578 37.411 39.059 1.00 8.17 AAAD C ATOM 3235 CE1 PHE B 110 -4.117 36.780 39.959 1.00 15.91 AAAD C ATOM 3236 CE2 PHE B 110 -2.627 37.357 38.161 1.00 7.23 AAAD C ATOM 3237 CZ PHE B 110 -3.901 37.043 38.608 1.00 11.95 AAAD C ATOM 3238 N GLN B 111 1.727 35.800 39.875 1.00 10.58 AAAD N ATOM 3239 CA GLN B 111 2.297 35.310 38.632 1.00 14.83 AAAD C ATOM 3240 C GLN B 111 2.695 33.836 38.785 1.00 17.12 AAAD C ATOM 3241 O GLN B 111 2.367 33.002 37.934 1.00 17.54 AAAD O ATOM 3242 CB GLN B 111 3.506 36.159 38.223 1.00 11.45 AAAD C ATOM 3243 CG GLN B 111 3.150 37.562 37.754 1.00 10.03 AAAD C ATOM 3244 CD GLN B 111 2.129 37.553 36.633 1.00 14.19 AAAD C ATOM 3245 OE1 GLN B 111 2.245 36.786 35.684 1.00 19.16 AAAD O ATOM 3246 NE2 GLN B 111 1.123 38.406 36.737 1.00 17.51 AAAD N ATOM 3247 N LEU B 112 3.353 33.516 39.895 1.00 16.95 AAAD N ATOM 3248 CA LEU B 112 3.789 32.150 40.152 1.00 17.05 AAAD C ATOM 3249 C LEU B 112 2.634 31.165 40.326 1.00 19.50 AAAD C ATOM 3250 O LEU B 112 2.803 29.960 40.118 1.00 25.08 AAAD O ATOM 3251 CB LEU B 112 4.709 32.098 41.373 1.00 11.30 AAAD C ATOM 3252 CG LEU B 112 6.066 32.785 41.218 1.00 9.36 AAAD C ATOM 3253 CD1 LEU B 112 6.867 32.648 42.503 1.00 2.98 AAAD C ATOM 3254 CD2 LEU B 112 6.831 32.198 40.029 1.00 5.10 AAAD C ATOM 3255 N GLY B 113 1.465 31.674 40.691 1.00 17.23 AAAD N ATOM 3256 CA GLY B 113 0.325 30.802 40.882 1.00 16.54 AAAD C ATOM 3257 C GLY B 113 -0.644 30.801 39.721 1.00 19.18 AAAD C ATOM 3258 O GLY B 113 -1.708 30.190 39.803 1.00 21.55 AAAD O ATOM 3259 N LYS B 114 -0.305 31.495 38.641 1.00 21.66 AAAD N ATOM 3260 CA LYS B 114 -1.183 31.538 37.479 1.00 20.56 AAAD C ATOM 3261 C LYS B 114 -1.039 30.229 36.694 1.00 20.79 AAAD C ATOM 3262 O LYS B 114 0.060 29.884 36.239 1.00 16.46 AAAD O ATOM 3263 CB LYS B 114 -0.834 32.744 36.606 1.00 16.18 AAAD C ATOM 3264 CG LYS B 114 -2.029 33.596 36.251 1.00 13.23 AAAD C ATOM 3265 CD LYS B 114 -1.656 34.734 35.311 1.00 13.68 AAAD C ATOM 3266 CE LYS B 114 -2.896 35.490 34.879 1.00 15.66 AAAD C ATOM 3267 NZ LYS B 114 -2.643 36.326 33.669 1.00 20.01 AAAD N ATOM 3268 N LYS B 115 -2.136 29.485 36.574 1.00 24.06 AAAD N ATOM 3269 CA LYS B 115 -2.135 28.207 35.852 1.00 28.97 AAAD C ATOM 3270 C LYS B 115 -2.164 28.463 34.343 1.00 25.24 AAAD C ATOM 3271 O LYS B 115 -3.221 28.526 33.714 1.00 20.33 AAAD O ATOM 3272 CB LYS B 115 -3.305 27.324 36.314 1.00 36.76 AAAD C ATOM 3273 CG LYS B 115 -4.673 27.991 36.279 1.00 49.63 AAAD C ATOM 3274 CD LYS B 115 -5.750 27.133 36.946 1.00 59.58 AAAD C ATOM 3275 CE LYS B 115 -7.122 27.798 36.813 1.00 64.89 AAAD C ATOM 3276 NZ LYS B 115 -8.210 27.175 37.625 1.00 68.04 AAAD N ATOM 3277 N ASN B 116 -0.975 28.610 33.773 1.00 26.08 AAAD N ATOM 3278 CA ASN B 116 -0.838 28.918 32.360 1.00 27.24 AAAD C ATOM 3279 C ASN B 116 -0.040 27.943 31.489 1.00 29.19 AAAD C ATOM 3280 O ASN B 116 0.122 28.180 30.294 1.00 28.39 AAAD O ATOM 3281 CB ASN B 116 -0.266 30.331 32.205 1.00 24.75 AAAD C ATOM 3282 CG ASN B 116 0.879 30.614 33.169 1.00 25.23 AAAD C ATOM 3283 OD1 ASN B 116 0.900 31.647 33.836 1.00 29.35 AAAD O ATOM 3284 ND2 ASN B 116 1.832 29.694 33.254 1.00 27.46 AAAD N ATOM 3285 N ARG B 117 0.493 26.874 32.071 1.00 29.29 AAAD N ATOM 3286 CA ARG B 117 1.251 25.921 31.268 1.00 30.31 AAAD C ATOM 3287 C ARG B 117 0.524 24.602 31.125 1.00 30.21 AAAD C ATOM 3288 O ARG B 117 -0.012 24.064 32.089 1.00 31.47 AAAD O ATOM 3289 CB ARG B 117 2.657 25.705 31.823 1.00 26.07 AAAD C ATOM 3290 CG ARG B 117 3.534 26.932 31.714 1.00 27.68 AAAD C ATOM 3291 CD ARG B 117 3.668 27.399 30.268 1.00 27.30 AAAD C ATOM 3292 NE ARG B 117 4.542 26.544 29.466 1.00 25.33 AAAD N ATOM 3293 CZ ARG B 117 5.845 26.394 29.678 1.00 28.06 AAAD C ATOM 3294 NH1 ARG B 117 6.435 27.032 30.678 1.00 31.75 AAAD N ATOM 3295 NH2 ARG B 117 6.573 25.652 28.854 1.00 25.78 AAAD N ATOM 3296 N SER B 118 0.480 24.095 29.903 1.00 33.29 AAAD N ATOM 3297 CA SER B 118 -0.192 22.838 29.648 1.00 34.49 AAAD C ATOM 3298 C SER B 118 0.775 21.724 30.009 1.00 34.30 AAAD C ATOM 3299 O SER B 118 1.943 21.756 29.623 1.00 38.33 AAAD O ATOM 3300 CB SER B 118 -0.597 22.742 28.180 1.00 34.42 AAAD C ATOM 3301 OG SER B 118 -1.674 21.838 28.007 1.00 41.99 AAAD O ATOM 3302 N LEU B 119 0.296 20.761 30.783 1.00 33.60 AAAD N ATOM 3303 CA LEU B 119 1.108 19.636 31.205 1.00 34.53 AAAD C ATOM 3304 C LEU B 119 0.171 18.455 31.399 1.00 36.18 AAAD C ATOM 3305 O LEU B 119 -0.733 18.504 32.234 1.00 34.64 AAAD O ATOM 3306 CB LEU B 119 1.811 19.958 32.518 1.00 30.94 AAAD C ATOM 3307 CG LEU B 119 2.894 18.982 32.970 1.00 29.78 AAAD C ATOM 3308 CD1 LEU B 119 4.136 19.135 32.109 1.00 31.36 AAAD C ATOM 3309 CD2 LEU B 119 3.232 19.256 34.420 1.00 30.87 AAAD C ATOM 3310 N ASN B 120 0.359 17.426 30.573 1.00 39.19 AAAD N ATOM 3311 CA ASN B 120 -0.443 16.202 30.611 1.00 37.15 AAAD C ATOM 3312 C ASN B 120 -1.935 16.506 30.648 1.00 40.38 AAAD C ATOM 3313 O ASN B 120 -2.657 15.999 31.504 1.00 39.63 AAAD O ATOM 3314 CB ASN B 120 -0.048 15.328 31.807 1.00 35.89 AAAD C ATOM 3315 CG ASN B 120 1.420 14.948 31.795 1.00 39.67 AAAD C ATOM 3316 OD1 ASN B 120 2.108 15.041 32.815 1.00 44.22 AAAD O ATOM 3317 ND2 ASN B 120 1.918 14.537 30.634 1.00 38.18 AAAD N ATOM 3318 N GLY B 121 -2.381 17.347 29.714 1.00 43.66 AAAD N ATOM 3319 CA GLY B 121 -3.786 17.716 29.636 1.00 43.95 AAAD C ATOM 3320 C GLY B 121 -4.308 18.407 30.881 1.00 44.80 AAAD C ATOM 3321 O GLY B 121 -5.506 18.363 31.168 1.00 46.02 AAAD O ATOM 3322 N GLU B 122 -3.421 19.100 31.585 1.00 45.64 AAAD N ATOM 3323 CA GLU B 122 -3.775 19.801 32.812 1.00 43.56 AAAD C ATOM 3324 C GLU B 122 -2.994 21.118 32.798 1.00 40.38 AAAD C ATOM 3325 O GLU B 122 -1.862 21.160 32.322 1.00 41.56 AAAD O ATOM 3326 CB GLU B 122 -3.333 18.945 34.005 1.00 45.53 AAAD C ATOM 3327 CG GLU B 122 -4.025 19.250 35.321 1.00 55.18 AAAD C ATOM 3328 CD GLU B 122 -5.121 18.251 35.649 1.00 59.75 AAAD C ATOM 3329 OE1 GLU B 122 -4.821 17.039 35.723 1.00 63.98 AAAD O ATOM 3330 OE2 GLU B 122 -6.282 18.675 35.843 1.00 63.03 AAAD O ATOM 3331 N LYS B 123 -3.602 22.199 33.269 1.00 36.55 AAAD N ATOM 3332 CA LYS B 123 -2.911 23.488 33.311 1.00 33.15 AAAD C ATOM 3333 C LYS B 123 -2.210 23.648 34.663 1.00 29.16 AAAD C ATOM 3334 O LYS B 123 -2.856 23.581 35.708 1.00 30.84 AAAD O ATOM 3335 CB LYS B 123 -3.902 24.642 33.130 1.00 37.82 AAAD C ATOM 3336 CG LYS B 123 -4.637 24.668 31.806 1.00 42.51 AAAD C ATOM 3337 CD LYS B 123 -3.703 24.985 30.655 1.00 47.11 AAAD C ATOM 3338 CE LYS B 123 -4.503 25.162 29.378 1.00 52.65 AAAD C ATOM 3339 NZ LYS B 123 -3.659 25.382 28.174 1.00 59.50 AAAD N ATOM 3340 N VAL B 124 -0.893 23.810 34.649 1.00 23.58 AAAD N ATOM 3341 CA VAL B 124 -0.135 24.005 35.882 1.00 22.83 AAAD C ATOM 3342 C VAL B 124 0.473 25.404 35.928 1.00 24.69 AAAD C ATOM 3343 O VAL B 124 0.375 26.165 34.956 1.00 26.06 AAAD O ATOM 3344 CB VAL B 124 1.003 22.959 36.044 1.00 22.42 AAAD C ATOM 3345 CG1 VAL B 124 0.423 21.578 36.280 1.00 22.32 AAAD C ATOM 3346 CG2 VAL B 124 1.915 22.959 34.828 1.00 21.12 AAAD C ATOM 3347 N ASP B 125 1.040 25.769 37.075 1.00 24.13 AAAD N ATOM 3348 CA ASP B 125 1.679 27.075 37.211 1.00 22.53 AAAD C ATOM 3349 C ASP B 125 3.193 26.942 37.070 1.00 21.27 AAAD C ATOM 3350 O ASP B 125 3.726 25.832 37.050 1.00 26.16 AAAD O ATOM 3351 CB ASP B 125 1.283 27.769 38.525 1.00 20.79 AAAD C ATOM 3352 CG ASP B 125 1.607 26.945 39.762 1.00 21.85 AAAD C ATOM 3353 OD1 ASP B 125 2.784 26.553 39.949 1.00 16.38 AAAD O ATOM 3354 OD2 ASP B 125 0.680 26.718 40.567 1.00 11.37 AAAD O ATOM 3355 N GLN B 126 3.884 28.071 36.998 1.00 21.54 AAAD N ATOM 3356 CA GLN B 126 5.336 28.082 36.835 1.00 21.97 AAAD C ATOM 3357 C GLN B 126 6.106 27.226 37.824 1.00 17.22 AAAD C ATOM 3358 O GLN B 126 7.161 26.689 37.487 1.00 14.93 AAAD O ATOM 3359 CB GLN B 126 5.879 29.510 36.896 1.00 22.11 AAAD C ATOM 3360 CG GLN B 126 5.544 30.356 35.692 1.00 23.67 AAAD C ATOM 3361 CD GLN B 126 6.169 31.727 35.781 1.00 27.32 AAAD C ATOM 3362 OE1 GLN B 126 7.389 31.854 35.826 1.00 24.20 AAAD O ATOM 3363 NE2 GLN B 126 5.339 32.758 35.845 1.00 23.05 AAAD N ATOM 3364 N VAL B 127 5.610 27.129 39.051 1.00 20.64 AAAD N ATOM 3365 CA VAL B 127 6.296 26.338 40.068 1.00 23.85 AAAD C ATOM 3366 C VAL B 127 6.123 24.843 39.815 1.00 22.51 AAAD C ATOM 3367 O VAL B 127 7.107 24.107 39.749 1.00 25.88 AAAD O ATOM 3368 CB VAL B 127 5.841 26.718 41.495 1.00 22.39 AAAD C ATOM 3369 CG1 VAL B 127 6.715 26.021 42.528 1.00 23.30 AAAD C ATOM 3370 CG2 VAL B 127 5.919 28.220 41.678 1.00 23.73 AAAD C ATOM 3371 N ASP B 128 4.883 24.402 39.628 1.00 21.79 AAAD N ATOM 3372 CA ASP B 128 4.618 22.992 39.360 1.00 23.88 AAAD C ATOM 3373 C ASP B 128 5.366 22.538 38.108 1.00 25.56 AAAD C ATOM 3374 O ASP B 128 6.062 21.515 38.117 1.00 28.12 AAAD O ATOM 3375 CB ASP B 128 3.113 22.741 39.187 1.00 22.01 AAAD C ATOM 3376 CG ASP B 128 2.342 22.842 40.496 1.00 19.38 AAAD C ATOM 3377 OD1 ASP B 128 2.927 22.544 41.563 1.00 16.08 AAAD O ATOM 3378 OD2 ASP B 128 1.143 23.203 40.449 1.00 16.61 AAAD O ATOM 3379 N TYR B 129 5.247 23.328 37.045 1.00 25.17 AAAD N ATOM 3380 CA TYR B 129 5.901 23.030 35.778 1.00 23.16 AAAD C ATOM 3381 C TYR B 129 7.412 22.889 35.960 1.00 22.27 AAAD C ATOM 3382 O TYR B 129 8.017 21.949 35.454 1.00 23.53 AAAD O ATOM 3383 CB TYR B 129 5.590 24.124 34.754 1.00 19.21 AAAD C ATOM 3384 CG TYR B 129 5.927 23.735 33.338 1.00 21.72 AAAD C ATOM 3385 CD1 TYR B 129 4.998 23.072 32.542 1.00 23.96 AAAD C ATOM 3386 CD2 TYR B 129 7.182 24.013 32.793 1.00 21.72 AAAD C ATOM 3387 CE1 TYR B 129 5.307 22.691 31.232 1.00 24.68 AAAD C ATOM 3388 CE2 TYR B 129 7.500 23.640 31.490 1.00 21.30 AAAD C ATOM 3389 CZ TYR B 129 6.559 22.978 30.715 1.00 24.30 AAAD C ATOM 3390 OH TYR B 129 6.881 22.608 29.429 1.00 26.54 AAAD O ATOM 3391 N LEU B 130 8.011 23.810 36.705 1.00 21.32 AAAD N ATOM 3392 CA LEU B 130 9.446 23.787 36.955 1.00 20.11 AAAD C ATOM 3393 C LEU B 130 9.854 22.499 37.659 1.00 23.07 AAAD C ATOM 3394 O LEU B 130 10.774 21.805 37.212 1.00 23.60 AAAD O ATOM 3395 CB LEU B 130 9.850 24.987 37.820 1.00 19.61 AAAD C ATOM 3396 CG LEU B 130 11.280 24.992 38.370 1.00 18.01 AAAD C ATOM 3397 CD1 LEU B 130 12.273 25.288 37.254 1.00 20.75 AAAD C ATOM 3398 CD2 LEU B 130 11.403 26.005 39.491 1.00 13.71 AAAD C ATOM 3399 N LEU B 131 9.166 22.192 38.760 1.00 24.45 AAAD N ATOM 3400 CA LEU B 131 9.437 20.997 39.569 1.00 22.36 AAAD C ATOM 3401 C LEU B 131 9.388 19.718 38.737 1.00 19.99 AAAD C ATOM 3402 O LEU B 131 10.327 18.927 38.757 1.00 18.04 AAAD O ATOM 3403 CB LEU B 131 8.459 20.926 40.742 1.00 19.00 AAAD C ATOM 3404 CG LEU B 131 8.659 22.055 41.762 1.00 22.05 AAAD C ATOM 3405 CD1 LEU B 131 7.495 22.100 42.742 1.00 19.34 AAAD C ATOM 3406 CD2 LEU B 131 9.986 21.872 42.485 1.00 17.46 AAAD C ATOM 3407 N HIS B 132 8.306 19.544 37.980 1.00 20.77 AAAD N ATOM 3408 CA HIS B 132 8.149 18.383 37.105 1.00 18.69 AAAD C ATOM 3409 C HIS B 132 9.316 18.314 36.125 1.00 18.87 AAAD C ATOM 3410 O HIS B 132 10.028 17.318 36.069 1.00 20.53 AAAD O ATOM 3411 CB HIS B 132 6.835 18.488 36.320 1.00 20.74 AAAD C ATOM 3412 CG HIS B 132 6.656 17.422 35.284 1.00 28.94 AAAD C ATOM 3413 ND1 HIS B 132 5.731 16.407 35.410 1.00 29.46 AAAD N ATOM 3414 CD2 HIS B 132 7.267 17.225 34.091 1.00 28.92 AAAD C ATOM 3415 CE1 HIS B 132 5.780 15.632 34.342 1.00 26.66 AAAD C ATOM 3416 NE2 HIS B 132 6.704 16.106 33.528 1.00 26.63 AAAD N ATOM 3417 N GLN B 133 9.515 19.386 35.364 1.00 20.24 AAAD N ATOM 3418 CA GLN B 133 10.583 19.457 34.370 1.00 18.61 AAAD C ATOM 3419 C GLN B 133 11.986 19.249 34.918 1.00 19.14 AAAD C ATOM 3420 O GLN B 133 12.861 18.781 34.194 1.00 17.38 AAAD O ATOM 3421 CB GLN B 133 10.543 20.790 33.623 1.00 19.78 AAAD C ATOM 3422 CG GLN B 133 9.225 21.106 32.933 1.00 20.42 AAAD C ATOM 3423 CD GLN B 133 8.863 20.118 31.850 1.00 27.52 AAAD C ATOM 3424 OE1 GLN B 133 7.781 19.522 31.882 1.00 32.84 AAAD O ATOM 3425 NE2 GLN B 133 9.760 19.932 30.884 1.00 24.20 AAAD N ATOM 3426 N LEU B 134 12.241 19.642 36.159 1.00 22.64 AAAD N ATOM 3427 CA LEU B 134 13.584 19.456 36.704 1.00 25.02 AAAD C ATOM 3428 C LEU B 134 13.900 17.972 36.841 1.00 26.52 AAAD C ATOM 3429 O LEU B 134 15.016 17.538 36.565 1.00 25.19 AAAD O ATOM 3430 CB LEU B 134 13.750 20.172 38.048 1.00 23.87 AAAD C ATOM 3431 CG LEU B 134 13.974 21.688 38.006 1.00 24.31 AAAD C ATOM 3432 CD1 LEU B 134 13.903 22.256 39.417 1.00 22.74 AAAD C ATOM 3433 CD2 LEU B 134 15.319 22.002 37.375 1.00 20.29 AAAD C ATOM 3434 N LYS B 135 12.892 17.194 37.216 1.00 28.79 AAAD N ATOM 3435 CA LYS B 135 13.058 15.758 37.387 1.00 32.31 AAAD C ATOM 3436 C LYS B 135 12.833 15.037 36.066 1.00 29.12 AAAD C ATOM 3437 O LYS B 135 13.704 14.316 35.583 1.00 32.22 AAAD O ATOM 3438 CB LYS B 135 12.073 15.240 38.443 1.00 38.09 AAAD C ATOM 3439 CG LYS B 135 12.264 13.776 38.869 1.00 46.26 AAAD C ATOM 3440 CD LYS B 135 13.357 13.586 39.932 1.00 52.59 AAAD C ATOM 3441 CE LYS B 135 14.765 13.597 39.339 1.00 56.44 AAAD C ATOM 3442 NZ LYS B 135 15.814 13.273 40.351 1.00 58.30 AAAD N ATOM 3443 N ASN B 136 11.672 15.266 35.468 1.00 27.10 AAAD N ATOM 3444 CA ASN B 136 11.302 14.628 34.210 1.00 31.72 AAAD C ATOM 3445 C ASN B 136 12.034 15.084 32.952 1.00 33.31 AAAD C ATOM 3446 O ASN B 136 12.348 14.269 32.087 1.00 38.67 AAAD O ATOM 3447 CB ASN B 136 9.794 14.728 33.988 1.00 31.72 AAAD C ATOM 3448 CG ASN B 136 8.998 14.012 35.060 1.00 34.44 AAAD C ATOM 3449 OD1 ASN B 136 8.141 14.615 35.705 1.00 35.56 AAAD O ATOM 3450 ND2 ASN B 136 9.262 12.720 35.243 1.00 30.40 AAAD N ATOM 3451 N ASN B 137 12.292 16.375 32.827 1.00 32.25 AAAD N ATOM 3452 CA ASN B 137 12.986 16.869 31.649 1.00 29.75 AAAD C ATOM 3453 C ASN B 137 14.212 17.675 32.009 1.00 29.60 AAAD C ATOM 3454 O ASN B 137 14.330 18.856 31.650 1.00 26.11 AAAD O ATOM 3455 CB ASN B 137 12.058 17.703 30.769 1.00 30.82 AAAD C ATOM 3456 CG ASN B 137 12.772 18.287 29.556 1.00 33.23 AAAD C ATOM 3457 OD1 ASN B 137 12.362 19.319 29.029 1.00 37.83 AAAD O ATOM 3458 ND2 ASN B 137 13.852 17.643 29.121 1.00 34.19 AAAD N ATOM 3459 N PRO B 138 15.138 17.065 32.758 1.00 30.47 AAAD N ATOM 3460 CA PRO B 138 16.337 17.821 33.112 1.00 33.98 AAAD C ATOM 3461 C PRO B 138 17.065 18.159 31.814 1.00 36.13 AAAD C ATOM 3462 O PRO B 138 16.708 17.654 30.738 1.00 43.13 AAAD O ATOM 3463 CB PRO B 138 17.127 16.821 33.960 1.00 30.57 AAAD C ATOM 3464 CG PRO B 138 16.751 15.512 33.360 1.00 28.43 AAAD C ATOM 3465 CD PRO B 138 15.259 15.663 33.183 1.00 27.42 AAAD C ATOM 3466 N SER B 139 18.044 19.044 31.901 1.00 34.45 AAAD N ATOM 3467 CA SER B 139 18.818 19.430 30.731 1.00 31.35 AAAD C ATOM 3468 C SER B 139 18.100 20.373 29.764 1.00 26.58 AAAD C ATOM 3469 O SER B 139 18.685 20.767 28.755 1.00 28.79 AAAD O ATOM 3470 CB SER B 139 19.350 18.183 30.001 1.00 32.46 AAAD C ATOM 3471 OG SER B 139 19.994 17.293 30.911 1.00 36.99 AAAD O ATOM 3472 N SER B 140 16.848 20.731 30.047 1.00 20.49 AAAD N ATOM 3473 CA SER B 140 16.155 21.672 29.174 1.00 19.25 AAAD C ATOM 3474 C SER B 140 16.814 23.024 29.411 1.00 19.27 AAAD C ATOM 3475 O SER B 140 17.304 23.300 30.509 1.00 22.95 AAAD O ATOM 3476 CB SER B 140 14.668 21.759 29.495 1.00 14.45 AAAD C ATOM 3477 OG SER B 140 14.422 22.597 30.605 1.00 21.21 AAAD O ATOM 3478 N ARG B 141 16.861 23.852 28.379 1.00 21.75 AAAD N ATOM 3479 CA ARG B 141 17.473 25.169 28.503 1.00 20.51 AAAD C ATOM 3480 C ARG B 141 16.388 26.205 28.720 1.00 17.79 AAAD C ATOM 3481 O ARG B 141 16.594 27.394 28.496 1.00 22.44 AAAD O ATOM 3482 CB ARG B 141 18.276 25.480 27.241 1.00 18.15 AAAD C ATOM 3483 CG ARG B 141 19.434 24.526 27.025 1.00 20.49 AAAD C ATOM 3484 CD ARG B 141 19.880 24.508 25.592 1.00 18.45 AAAD C ATOM 3485 NE ARG B 141 21.072 23.688 25.438 1.00 25.24 AAAD N ATOM 3486 CZ ARG B 141 21.368 23.006 24.341 1.00 24.85 AAAD C ATOM 3487 NH1 ARG B 141 20.550 23.042 23.301 1.00 22.10 AAAD N ATOM 3488 NH2 ARG B 141 22.527 22.366 24.253 1.00 20.23 AAAD N ATOM 3489 N ARG B 142 15.246 25.741 29.208 1.00 14.69 AAAD N ATOM 3490 CA ARG B 142 14.109 26.605 29.439 1.00 12.35 AAAD C ATOM 3491 C ARG B 142 13.578 26.544 30.864 1.00 7.64 AAAD C ATOM 3492 O ARG B 142 12.393 26.765 31.092 1.00 8.39 AAAD O ATOM 3493 CB ARG B 142 12.995 26.256 28.451 1.00 19.38 AAAD C ATOM 3494 CG ARG B 142 13.473 26.142 27.015 1.00 27.23 AAAD C ATOM 3495 CD ARG B 142 12.374 25.677 26.074 1.00 31.22 AAAD C ATOM 3496 NE ARG B 142 12.934 25.275 24.784 1.00 39.91 AAAD N ATOM 3497 CZ ARG B 142 12.219 24.851 23.746 1.00 41.02 AAAD C ATOM 3498 NH1 ARG B 142 10.899 24.763 23.831 1.00 44.05 AAAD N ATOM 3499 NH2 ARG B 142 12.832 24.469 22.635 1.00 38.80 AAAD N ATOM 3500 N HIS B 143 14.442 26.221 31.817 1.00 7.43 AAAD N ATOM 3501 CA HIS B 143 14.044 26.178 33.227 1.00 12.11 AAAD C ATOM 3502 C HIS B 143 14.077 27.620 33.730 1.00 9.65 AAAD C ATOM 3503 O HIS B 143 15.016 28.039 34.413 1.00 7.38 AAAD O ATOM 3504 CB HIS B 143 15.005 25.295 34.031 1.00 10.89 AAAD C ATOM 3505 CG HIS B 143 14.831 23.832 33.772 1.00 10.49 AAAD C ATOM 3506 ND1 HIS B 143 15.890 22.958 33.680 1.00 7.35 AAAD N ATOM 3507 CD2 HIS B 143 13.713 23.091 33.577 1.00 9.31 AAAD C ATOM 3508 CE1 HIS B 143 15.437 21.743 33.441 1.00 12.53 AAAD C ATOM 3509 NE2 HIS B 143 14.119 21.795 33.373 1.00 8.63 AAAD N ATOM 3510 N ILE B 144 13.035 28.361 33.376 1.00 8.66 AAAD N ATOM 3511 CA ILE B 144 12.921 29.773 33.697 1.00 7.30 AAAD C ATOM 3512 C ILE B 144 11.576 30.183 34.290 1.00 6.32 AAAD C ATOM 3513 O ILE B 144 10.519 29.750 33.819 1.00 3.36 AAAD O ATOM 3514 CB ILE B 144 13.160 30.606 32.393 1.00 8.21 AAAD C ATOM 3515 CG1 ILE B 144 14.619 30.493 31.963 1.00 10.54 AAAD C ATOM 3516 CG2 ILE B 144 12.777 32.074 32.577 1.00 14.40 AAAD C ATOM 3517 CD1 ILE B 144 14.916 31.151 30.648 1.00 14.21 AAAD C ATOM 3518 N THR B 145 11.631 30.980 35.356 1.00 5.34 AAAD N ATOM 3519 CA THR B 145 10.423 31.527 35.966 1.00 7.03 AAAD C ATOM 3520 C THR B 145 10.474 33.028 35.651 1.00 6.37 AAAD C ATOM 3521 O THR B 145 11.557 33.620 35.525 1.00 2.00 AAAD O ATOM 3522 CB THR B 145 10.351 31.290 37.495 1.00 12.45 AAAD C ATOM 3523 OG1 THR B 145 11.644 31.492 38.079 1.00 16.07 AAAD O ATOM 3524 CG2 THR B 145 9.885 29.872 37.805 1.00 13.11 AAAD C ATOM 3525 N MET B 146 9.310 33.634 35.479 1.00 7.54 AAAD N ATOM 3526 CA MET B 146 9.234 35.040 35.149 1.00 6.71 AAAD C ATOM 3527 C MET B 146 8.145 35.759 35.924 1.00 6.99 AAAD C ATOM 3528 O MET B 146 6.970 35.392 35.862 1.00 7.93 AAAD O ATOM 3529 CB MET B 146 8.989 35.192 33.639 1.00 10.58 AAAD C ATOM 3530 CG MET B 146 9.024 36.624 33.093 1.00 9.54 AAAD C ATOM 3531 SD MET B 146 10.605 37.412 33.362 1.00 7.23 AAAD S ATOM 3532 CE MET B 146 11.708 36.134 32.836 1.00 10.67 AAAD C ATOM 3533 N LEU B 147 8.543 36.768 36.684 1.00 8.22 AAAD N ATOM 3534 CA LEU B 147 7.576 37.568 37.429 1.00 14.46 AAAD C ATOM 3535 C LEU B 147 7.195 38.775 36.572 1.00 13.59 AAAD C ATOM 3536 O LEU B 147 6.094 39.312 36.678 1.00 16.01 AAAD O ATOM 3537 CB LEU B 147 8.168 38.025 38.765 1.00 14.86 AAAD C ATOM 3538 CG LEU B 147 8.466 36.903 39.773 1.00 16.74 AAAD C ATOM 3539 CD1 LEU B 147 9.053 37.490 41.054 1.00 14.11 AAAD C ATOM 3540 CD2 LEU B 147 7.196 36.107 40.078 1.00 12.30 AAAD C ATOM 3541 N TRP B 148 8.115 39.170 35.699 1.00 12.19 AAAD N ATOM 3542 CA TRP B 148 7.916 40.300 34.809 1.00 14.07 AAAD C ATOM 3543 C TRP B 148 6.958 39.961 33.675 1.00 11.97 AAAD C ATOM 3544 O TRP B 148 7.379 39.778 32.543 1.00 17.56 AAAD O ATOM 3545 CB TRP B 148 9.260 40.760 34.227 1.00 15.40 AAAD C ATOM 3546 CG TRP B 148 9.204 42.142 33.620 1.00 25.72 AAAD C ATOM 3547 CD1 TRP B 148 8.980 42.462 32.309 1.00 22.96 AAAD C ATOM 3548 CD2 TRP B 148 9.380 43.388 34.314 1.00 29.93 AAAD C ATOM 3549 NE1 TRP B 148 9.011 43.826 32.144 1.00 24.71 AAAD N ATOM 3550 CE2 TRP B 148 9.254 44.420 33.355 1.00 27.52 AAAD C ATOM 3551 CE3 TRP B 148 9.637 43.733 35.651 1.00 30.35 AAAD C ATOM 3552 CZ2 TRP B 148 9.377 45.777 33.693 1.00 31.24 AAAD C ATOM 3553 CZ3 TRP B 148 9.760 45.086 35.984 1.00 31.47 AAAD C ATOM 3554 CH2 TRP B 148 9.628 46.089 35.005 1.00 27.66 AAAD C ATOM 3555 N ASN B 149 5.674 39.843 33.978 1.00 12.72 AAAD N ATOM 3556 CA ASN B 149 4.684 39.544 32.943 1.00 18.46 AAAD C ATOM 3557 C ASN B 149 4.328 40.856 32.239 1.00 21.94 AAAD C ATOM 3558 O ASN B 149 3.689 41.730 32.826 1.00 22.31 AAAD O ATOM 3559 CB ASN B 149 3.436 38.911 33.557 1.00 15.58 AAAD C ATOM 3560 CG ASN B 149 2.430 38.478 32.514 1.00 18.29 AAAD C ATOM 3561 OD1 ASN B 149 2.359 39.048 31.426 1.00 28.66 AAAD O ATOM 3562 ND2 ASN B 149 1.647 37.461 32.835 1.00 17.71 AAAD N ATOM 3563 N PRO B 150 4.695 40.985 30.952 1.00 25.50 AAAD N ATOM 3564 CA PRO B 150 4.432 42.187 30.154 1.00 25.02 AAAD C ATOM 3565 C PRO B 150 2.979 42.644 30.141 1.00 25.75 AAAD C ATOM 3566 O PRO B 150 2.706 43.843 30.187 1.00 22.96 AAAD O ATOM 3567 CB PRO B 150 4.887 41.773 28.753 1.00 26.30 AAAD C ATOM 3568 CG PRO B 150 5.960 40.772 29.020 1.00 27.49 AAAD C ATOM 3569 CD PRO B 150 5.342 39.951 30.124 1.00 26.74 AAAD C ATOM 3570 N ASP B 151 2.055 41.689 30.079 1.00 25.20 AAAD N ATOM 3571 CA ASP B 151 0.623 41.992 30.038 1.00 24.79 AAAD C ATOM 3572 C ASP B 151 0.060 42.493 31.363 1.00 24.17 AAAD C ATOM 3573 O ASP B 151 -0.921 43.243 31.392 1.00 22.16 AAAD O ATOM 3574 CB ASP B 151 -0.173 40.743 29.634 1.00 22.72 AAAD C ATOM 3575 CG ASP B 151 0.044 40.340 28.192 1.00 26.33 AAAD C ATOM 3576 OD1 ASP B 151 0.073 41.233 27.318 1.00 28.92 AAAD O ATOM 3577 OD2 ASP B 151 0.158 39.123 27.930 1.00 20.62 AAAD O ATOM 3578 N GLU B 152 0.679 42.052 32.454 1.00 23.67 AAAD N ATOM 3579 CA GLU B 152 0.228 42.380 33.801 1.00 22.35 AAAD C ATOM 3580 C GLU B 152 0.888 43.587 34.470 1.00 18.49 AAAD C ATOM 3581 O GLU B 152 0.426 44.055 35.505 1.00 22.30 AAAD O ATOM 3582 CB GLU B 152 0.399 41.142 34.684 1.00 22.92 AAAD C ATOM 3583 CG GLU B 152 -0.402 39.937 34.216 1.00 20.79 AAAD C ATOM 3584 CD GLU B 152 -1.860 39.999 34.649 1.00 25.16 AAAD C ATOM 3585 OE1 GLU B 152 -2.449 41.101 34.684 1.00 26.27 AAAD O ATOM 3586 OE2 GLU B 152 -2.421 38.938 34.974 1.00 24.93 AAAD O ATOM 3587 N LEU B 153 1.946 44.100 33.861 1.00 15.95 AAAD N ATOM 3588 CA LEU B 153 2.697 45.224 34.396 1.00 13.52 AAAD C ATOM 3589 C LEU B 153 1.917 46.378 35.024 1.00 18.13 AAAD C ATOM 3590 O LEU B 153 2.304 46.876 36.078 1.00 22.65 AAAD O ATOM 3591 CB LEU B 153 3.660 45.736 33.338 1.00 4.94 AAAD C ATOM 3592 CG LEU B 153 5.144 45.525 33.634 1.00 7.09 AAAD C ATOM 3593 CD1 LEU B 153 5.407 44.355 34.562 1.00 6.27 AAAD C ATOM 3594 CD2 LEU B 153 5.856 45.327 32.326 1.00 6.65 AAAD C ATOM 3595 N ASP B 154 0.815 46.797 34.415 1.00 20.22 AAAD N ATOM 3596 CA ASP B 154 0.040 47.905 34.977 1.00 23.69 AAAD C ATOM 3597 C ASP B 154 -0.878 47.508 36.129 1.00 25.76 AAAD C ATOM 3598 O ASP B 154 -1.371 48.380 36.855 1.00 28.55 AAAD O ATOM 3599 CB ASP B 154 -0.812 48.600 33.909 1.00 20.43 AAAD C ATOM 3600 CG ASP B 154 0.008 49.326 32.875 1.00 16.89 AAAD C ATOM 3601 OD1 ASP B 154 1.115 49.815 33.185 1.00 23.78 AAAD O ATOM 3602 OD2 ASP B 154 -0.473 49.409 31.733 1.00 19.15 AAAD O ATOM 3603 N ALA B 155 -1.152 46.213 36.266 1.00 24.07 AAAD N ATOM 3604 CA ALA B 155 -2.037 45.730 37.323 1.00 21.07 AAAD C ATOM 3605 C ALA B 155 -1.261 45.259 38.542 1.00 19.68 AAAD C ATOM 3606 O ALA B 155 -1.770 44.482 39.346 1.00 21.10 AAAD O ATOM 3607 CB ALA B 155 -2.920 44.614 36.800 1.00 20.11 AAAD C ATOM 3608 N MET B 156 -0.031 45.736 38.681 1.00 16.58 AAAD N ATOM 3609 CA MET B 156 0.816 45.358 39.796 1.00 16.83 AAAD C ATOM 3610 C MET B 156 1.030 46.534 40.748 1.00 20.39 AAAD C ATOM 3611 O MET B 156 1.535 47.584 40.341 1.00 17.30 AAAD O ATOM 3612 CB MET B 156 2.170 44.875 39.275 1.00 16.93 AAAD C ATOM 3613 CG MET B 156 2.112 43.644 38.401 1.00 9.03 AAAD C ATOM 3614 SD MET B 156 3.775 43.092 37.946 1.00 22.25 AAAD S ATOM 3615 CE MET B 156 3.360 41.772 36.784 1.00 22.21 AAAD C ATOM 3616 N ALA B 157 0.687 46.344 42.020 1.00 21.06 AAAD N ATOM 3617 CA ALA B 157 0.851 47.396 43.015 1.00 24.08 AAAD C ATOM 3618 C ALA B 157 2.316 47.800 43.103 1.00 26.93 AAAD C ATOM 3619 O ALA B 157 2.637 48.921 43.498 1.00 30.47 AAAD O ATOM 3620 CB ALA B 157 0.340 46.935 44.383 1.00 21.05 AAAD C ATOM 3621 N LEU B 158 3.200 46.880 42.727 1.00 27.88 AAAD N ATOM 3622 CA LEU B 158 4.635 47.132 42.748 1.00 27.93 AAAD C ATOM 3623 C LEU B 158 5.370 46.146 41.840 1.00 27.43 AAAD C ATOM 3624 O LEU B 158 4.994 44.981 41.747 1.00 28.33 AAAD O ATOM 3625 CB LEU B 158 5.181 47.124 44.189 1.00 24.52 AAAD C ATOM 3626 CG LEU B 158 5.053 45.980 45.200 1.00 24.40 AAAD C ATOM 3627 CD1 LEU B 158 3.851 45.097 44.918 1.00 25.44 AAAD C ATOM 3628 CD2 LEU B 158 6.325 45.169 45.205 1.00 27.92 AAAD C ATOM 3629 N THR B 159 6.359 46.648 41.108 1.00 26.98 AAAD N ATOM 3630 CA THR B 159 7.140 45.837 40.182 1.00 28.53 AAAD C ATOM 3631 C THR B 159 8.342 45.208 40.889 1.00 27.13 AAAD C ATOM 3632 O THR B 159 9.063 45.881 41.631 1.00 30.55 AAAD O ATOM 3633 CB THR B 159 7.582 46.671 38.958 1.00 27.30 AAAD C ATOM 3634 OG1 THR B 159 8.196 47.887 39.395 1.00 27.71 AAAD O ATOM 3635 CG2 THR B 159 6.381 47.026 38.103 1.00 26.18 AAAD C ATOM 3636 N PRO B 160 8.551 43.896 40.690 1.00 22.41 AAAD N ATOM 3637 CA PRO B 160 9.642 43.122 41.293 1.00 17.52 AAAD C ATOM 3638 C PRO B 160 11.070 43.464 40.890 1.00 16.32 AAAD C ATOM 3639 O PRO B 160 11.342 43.835 39.753 1.00 18.10 AAAD O ATOM 3640 CB PRO B 160 9.269 41.682 40.936 1.00 15.21 AAAD C ATOM 3641 CG PRO B 160 8.555 41.831 39.640 1.00 20.07 AAAD C ATOM 3642 CD PRO B 160 7.674 43.026 39.886 1.00 20.76 AAAD C ATOM 3643 N CYS B 161 11.977 43.355 41.852 1.00 12.90 AAAD N ATOM 3644 CA CYS B 161 13.380 43.626 41.599 1.00 18.56 AAAD C ATOM 3645 C CYS B 161 13.992 42.311 41.129 1.00 18.86 AAAD C ATOM 3646 O CYS B 161 14.558 42.250 40.037 1.00 20.09 AAAD O ATOM 3647 CB CYS B 161 14.067 44.180 42.857 1.00 22.58 AAAD C ATOM 3648 SG CYS B 161 13.447 45.833 43.365 1.00 28.24 AAAD S ATOM 3649 N VAL B 162 13.881 41.265 41.952 1.00 16.70 AAAD N ATOM 3650 CA VAL B 162 14.365 39.937 41.572 1.00 12.22 AAAD C ATOM 3651 C VAL B 162 13.150 39.406 40.847 1.00 10.89 AAAD C ATOM 3652 O VAL B 162 12.152 39.052 41.478 1.00 12.04 AAAD O ATOM 3653 CB VAL B 162 14.663 39.039 42.786 1.00 9.31 AAAD C ATOM 3654 CG1 VAL B 162 15.013 37.655 42.314 1.00 9.62 AAAD C ATOM 3655 CG2 VAL B 162 15.840 39.590 43.570 1.00 16.04 AAAD C ATOM 3656 N TYR B 163 13.203 39.405 39.522 1.00 9.33 AAAD N ATOM 3657 CA TYR B 163 12.046 38.983 38.742 1.00 7.97 AAAD C ATOM 3658 C TYR B 163 12.161 37.675 37.964 1.00 7.04 AAAD C ATOM 3659 O TYR B 163 11.159 37.210 37.417 1.00 4.50 AAAD O ATOM 3660 CB TYR B 163 11.622 40.115 37.796 1.00 11.89 AAAD C ATOM 3661 CG TYR B 163 12.658 40.414 36.729 1.00 12.22 AAAD C ATOM 3662 CD1 TYR B 163 13.819 41.119 37.037 1.00 3.79 AAAD C ATOM 3663 CD2 TYR B 163 12.517 39.911 35.438 1.00 8.85 AAAD C ATOM 3664 CE1 TYR B 163 14.813 41.303 36.100 1.00 5.12 AAAD C ATOM 3665 CE2 TYR B 163 13.508 40.087 34.496 1.00 8.80 AAAD C ATOM 3666 CZ TYR B 163 14.652 40.780 34.832 1.00 9.38 AAAD C ATOM 3667 OH TYR B 163 15.649 40.924 33.899 1.00 13.82 AAAD O ATOM 3668 N GLU B 164 13.355 37.085 37.914 1.00 7.63 AAAD N ATOM 3669 CA GLU B 164 13.553 35.826 37.185 1.00 10.48 AAAD C ATOM 3670 C GLU B 164 14.613 34.884 37.778 1.00 9.72 AAAD C ATOM 3671 O GLU B 164 15.425 35.292 38.619 1.00 9.08 AAAD O ATOM 3672 CB GLU B 164 13.937 36.123 35.733 1.00 13.43 AAAD C ATOM 3673 CG GLU B 164 15.267 36.857 35.581 1.00 11.63 AAAD C ATOM 3674 CD GLU B 164 15.647 37.085 34.131 1.00 15.21 AAAD C ATOM 3675 OE1 GLU B 164 14.838 36.750 33.238 1.00 16.04 AAAD O ATOM 3676 OE2 GLU B 164 16.763 37.588 33.879 1.00 12.31 AAAD O ATOM 3677 N THR B 165 14.586 33.624 37.338 1.00 8.16 AAAD N ATOM 3678 CA THR B 165 15.560 32.607 37.757 1.00 8.92 AAAD C ATOM 3679 C THR B 165 15.750 31.640 36.598 1.00 6.31 AAAD C ATOM 3680 O THR B 165 14.859 31.472 35.772 1.00 5.17 AAAD O ATOM 3681 CB THR B 165 15.075 31.722 38.942 1.00 4.42 AAAD C ATOM 3682 OG1 THR B 165 13.907 31.006 38.542 1.00 5.79 AAAD O ATOM 3683 CG2 THR B 165 14.770 32.536 40.188 1.00 2.00 AAAD C ATOM 3684 N GLN B 166 16.931 31.045 36.519 1.00 10.39 AAAD N ATOM 3685 CA GLN B 166 17.226 30.043 35.508 1.00 14.81 AAAD C ATOM 3686 C GLN B 166 17.955 28.923 36.243 1.00 17.74 AAAD C ATOM 3687 O GLN B 166 18.895 29.179 37.007 1.00 16.07 AAAD O ATOM 3688 CB GLN B 166 18.083 30.597 34.370 1.00 14.41 AAAD C ATOM 3689 CG GLN B 166 18.436 29.526 33.354 1.00 18.58 AAAD C ATOM 3690 CD GLN B 166 18.434 30.018 31.921 1.00 22.96 AAAD C ATOM 3691 OE1 GLN B 166 19.277 30.819 31.518 1.00 26.81 AAAD O ATOM 3692 NE2 GLN B 166 17.491 29.527 31.139 1.00 25.30 AAAD N ATOM 3693 N TRP B 167 17.462 27.699 36.076 1.00 18.02 AAAD N ATOM 3694 CA TRP B 167 18.043 26.529 36.730 1.00 19.97 AAAD C ATOM 3695 C TRP B 167 18.760 25.660 35.712 1.00 20.87 AAAD C ATOM 3696 O TRP B 167 18.302 25.512 34.572 1.00 20.54 AAAD O ATOM 3697 CB TRP B 167 16.949 25.705 37.414 1.00 16.21 AAAD C ATOM 3698 CG TRP B 167 15.999 26.509 38.241 1.00 8.57 AAAD C ATOM 3699 CD1 TRP B 167 14.927 27.224 37.791 1.00 10.40 AAAD C ATOM 3700 CD2 TRP B 167 16.001 26.637 39.668 1.00 11.23 AAAD C ATOM 3701 NE1 TRP B 167 14.255 27.787 38.851 1.00 8.04 AAAD N ATOM 3702 CE2 TRP B 167 14.893 27.445 40.016 1.00 8.49 AAAD C ATOM 3703 CE3 TRP B 167 16.826 26.145 40.688 1.00 8.42 AAAD C ATOM 3704 CZ2 TRP B 167 14.591 27.771 41.344 1.00 8.58 AAAD C ATOM 3705 CZ3 TRP B 167 16.524 26.470 42.009 1.00 4.85 AAAD C ATOM 3706 CH2 TRP B 167 15.416 27.276 42.323 1.00 4.69 AAAD C ATOM 3707 N TYR B 168 19.864 25.056 36.136 1.00 22.32 AAAD N ATOM 3708 CA TYR B 168 20.656 24.208 35.260 1.00 23.12 AAAD C ATOM 3709 C TYR B 168 21.035 22.896 35.944 1.00 24.01 AAAD C ATOM 3710 O TYR B 168 21.758 22.898 36.940 1.00 23.47 AAAD O ATOM 3711 CB TYR B 168 21.957 24.913 34.858 1.00 25.40 AAAD C ATOM 3712 CG TYR B 168 21.824 26.333 34.338 1.00 28.99 AAAD C ATOM 3713 CD1 TYR B 168 21.528 26.584 32.997 1.00 28.73 AAAD C ATOM 3714 CD2 TYR B 168 22.032 27.428 35.183 1.00 27.58 AAAD C ATOM 3715 CE1 TYR B 168 21.439 27.890 32.512 1.00 25.93 AAAD C ATOM 3716 CE2 TYR B 168 21.946 28.732 34.708 1.00 21.76 AAAD C ATOM 3717 CZ TYR B 168 21.649 28.951 33.379 1.00 23.68 AAAD C ATOM 3718 OH TYR B 168 21.526 30.233 32.924 1.00 25.20 AAAD O ATOM 3719 N VAL B 169 20.562 21.778 35.404 1.00 25.39 AAAD N ATOM 3720 CA VAL B 169 20.915 20.467 35.952 1.00 23.67 AAAD C ATOM 3721 C VAL B 169 22.045 19.887 35.093 1.00 21.41 AAAD C ATOM 3722 O VAL B 169 21.865 19.617 33.911 1.00 20.32 AAAD O ATOM 3723 CB VAL B 169 19.718 19.478 35.961 1.00 21.37 AAAD C ATOM 3724 CG1 VAL B 169 20.161 18.145 36.536 1.00 17.55 AAAD C ATOM 3725 CG2 VAL B 169 18.541 20.049 36.771 1.00 15.98 AAAD C ATOM 3726 N LYS B 170 23.226 19.766 35.681 1.00 23.51 AAAD N ATOM 3727 CA LYS B 170 24.378 19.228 34.982 1.00 26.25 AAAD C ATOM 3728 C LYS B 170 25.098 18.248 35.881 1.00 30.71 AAAD C ATOM 3729 O LYS B 170 25.664 18.633 36.909 1.00 33.93 AAAD O ATOM 3730 CB LYS B 170 25.353 20.334 34.560 1.00 27.58 AAAD C ATOM 3731 CG LYS B 170 25.038 20.982 33.216 1.00 32.09 AAAD C ATOM 3732 CD LYS B 170 24.151 22.210 33.369 1.00 30.28 AAAD C ATOM 3733 CE LYS B 170 23.665 22.731 32.024 1.00 25.78 AAAD C ATOM 3734 NZ LYS B 170 24.778 22.904 31.068 1.00 10.61 AAAD N ATOM 3735 N HIS B 171 25.067 16.977 35.483 1.00 30.74 AAAD N ATOM 3736 CA HIS B 171 25.716 15.900 36.224 1.00 27.33 AAAD C ATOM 3737 C HIS B 171 25.218 15.834 37.665 1.00 27.26 AAAD C ATOM 3738 O HIS B 171 26.003 15.889 38.618 1.00 23.37 AAAD O ATOM 3739 CB HIS B 171 27.243 16.060 36.176 1.00 25.61 AAAD C ATOM 3740 CG HIS B 171 27.825 15.860 34.810 1.00 28.90 AAAD C ATOM 3741 ND1 HIS B 171 29.148 16.120 34.514 1.00 27.71 AAAD N ATOM 3742 CD2 HIS B 171 27.261 15.427 33.656 1.00 26.03 AAAD C ATOM 3743 CE1 HIS B 171 29.372 15.856 33.239 1.00 30.27 AAAD C ATOM 3744 NE2 HIS B 171 28.243 15.435 32.696 1.00 28.25 AAAD N ATOM 3745 N GLY B 172 23.897 15.770 37.808 1.00 24.85 AAAD N ATOM 3746 CA GLY B 172 23.289 15.683 39.125 1.00 25.68 AAAD C ATOM 3747 C GLY B 172 23.125 16.994 39.864 1.00 27.93 AAAD C ATOM 3748 O GLY B 172 22.135 17.178 40.577 1.00 28.22 AAAD O ATOM 3749 N LYS B 173 24.096 17.894 39.711 1.00 25.60 AAAD N ATOM 3750 CA LYS B 173 24.075 19.197 40.366 1.00 16.87 AAAD C ATOM 3751 C LYS B 173 23.052 20.143 39.757 1.00 16.29 AAAD C ATOM 3752 O LYS B 173 22.960 20.259 38.533 1.00 21.16 AAAD O ATOM 3753 CB LYS B 173 25.458 19.832 40.288 1.00 19.29 AAAD C ATOM 3754 CG LYS B 173 26.563 19.004 40.923 1.00 22.14 AAAD C ATOM 3755 CD LYS B 173 27.917 19.663 40.735 1.00 23.94 AAAD C ATOM 3756 CE LYS B 173 29.029 18.851 41.377 1.00 34.08 AAAD C ATOM 3757 NZ LYS B 173 30.364 19.511 41.168 1.00 44.36 AAAD N ATOM 3758 N LEU B 174 22.271 20.790 40.620 1.00 14.75 AAAD N ATOM 3759 CA LEU B 174 21.251 21.768 40.222 1.00 11.55 AAAD C ATOM 3760 C LEU B 174 21.868 23.157 40.440 1.00 18.28 AAAD C ATOM 3761 O LEU B 174 22.276 23.492 41.560 1.00 18.71 AAAD O ATOM 3762 CB LEU B 174 20.011 21.637 41.104 1.00 3.93 AAAD C ATOM 3763 CG LEU B 174 18.880 22.640 40.879 1.00 6.67 AAAD C ATOM 3764 CD1 LEU B 174 18.218 22.394 39.535 1.00 10.45 AAAD C ATOM 3765 CD2 LEU B 174 17.852 22.519 41.978 1.00 7.95 AAAD C ATOM 3766 N HIS B 175 21.960 23.953 39.378 1.00 16.87 AAAD N ATOM 3767 CA HIS B 175 22.538 25.293 39.463 1.00 11.01 AAAD C ATOM 3768 C HIS B 175 21.431 26.313 39.378 1.00 8.80 AAAD C ATOM 3769 O HIS B 175 20.422 26.089 38.700 1.00 9.71 AAAD O ATOM 3770 CB HIS B 175 23.512 25.541 38.323 1.00 10.87 AAAD C ATOM 3771 CG HIS B 175 24.625 24.547 38.253 1.00 12.11 AAAD C ATOM 3772 ND1 HIS B 175 25.903 24.836 38.674 1.00 7.44 AAAD N ATOM 3773 CD2 HIS B 175 24.655 23.271 37.797 1.00 9.73 AAAD C ATOM 3774 CE1 HIS B 175 26.675 23.780 38.484 1.00 14.63 AAAD C ATOM 3775 NE2 HIS B 175 25.941 22.817 37.951 1.00 13.42 AAAD N ATOM 3776 N LEU B 176 21.603 27.421 40.086 1.00 9.64 AAAD N ATOM 3777 CA LEU B 176 20.596 28.471 40.078 1.00 15.33 AAAD C ATOM 3778 C LEU B 176 21.214 29.820 39.766 1.00 16.05 AAAD C ATOM 3779 O LEU B 176 22.263 30.183 40.310 1.00 16.39 AAAD O ATOM 3780 CB LEU B 176 19.873 28.539 41.422 1.00 14.43 AAAD C ATOM 3781 CG LEU B 176 18.916 29.716 41.614 1.00 13.40 AAAD C ATOM 3782 CD1 LEU B 176 17.792 29.657 40.589 1.00 6.83 AAAD C ATOM 3783 CD2 LEU B 176 18.364 29.704 43.028 1.00 11.14 AAAD C ATOM 3784 N GLU B 177 20.556 30.543 38.870 1.00 15.47 AAAD N ATOM 3785 CA GLU B 177 20.980 31.874 38.469 1.00 19.40 AAAD C ATOM 3786 C GLU B 177 19.752 32.784 38.481 1.00 16.74 AAAD C ATOM 3787 O GLU B 177 18.779 32.527 37.762 1.00 14.36 AAAD O ATOM 3788 CB GLU B 177 21.600 31.840 37.070 1.00 17.08 AAAD C ATOM 3789 CG GLU B 177 21.911 33.212 36.517 1.00 15.70 AAAD C ATOM 3790 CD GLU B 177 22.788 33.170 35.295 1.00 18.10 AAAD C ATOM 3791 OE1 GLU B 177 22.512 32.370 34.384 1.00 14.02 AAAD O ATOM 3792 OE2 GLU B 177 23.767 33.939 35.246 1.00 20.07 AAAD O ATOM 3793 N VAL B 178 19.757 33.792 39.348 1.00 15.58 AAAD N ATOM 3794 CA VAL B 178 18.626 34.716 39.413 1.00 15.74 AAAD C ATOM 3795 C VAL B 178 19.093 36.103 38.997 1.00 14.60 AAAD C ATOM 3796 O VAL B 178 20.297 36.401 39.005 1.00 14.99 AAAD O ATOM 3797 CB VAL B 178 17.977 34.774 40.830 1.00 14.81 AAAD C ATOM 3798 CG1 VAL B 178 17.853 33.377 41.406 1.00 20.12 AAAD C ATOM 3799 CG2 VAL B 178 18.759 35.668 41.766 1.00 12.11 AAAD C ATOM 3800 N ARG B 179 18.146 36.949 38.618 1.00 14.16 AAAD N ATOM 3801 CA ARG B 179 18.487 38.300 38.212 1.00 11.76 AAAD C ATOM 3802 C ARG B 179 17.603 39.361 38.836 1.00 6.08 AAAD C ATOM 3803 O ARG B 179 16.382 39.198 38.899 1.00 4.18 AAAD O ATOM 3804 CB ARG B 179 18.437 38.451 36.688 1.00 11.82 AAAD C ATOM 3805 CG ARG B 179 18.950 39.818 36.247 1.00 20.75 AAAD C ATOM 3806 CD ARG B 179 18.922 40.066 34.745 1.00 19.97 AAAD C ATOM 3807 NE ARG B 179 19.634 41.307 34.428 1.00 16.48 AAAD N ATOM 3808 CZ ARG B 179 19.053 42.480 34.178 1.00 13.08 AAAD C ATOM 3809 NH1 ARG B 179 17.736 42.603 34.180 1.00 13.21 AAAD N ATOM 3810 NH2 ARG B 179 19.793 43.564 34.044 1.00 11.57 AAAD N ATOM 3811 N ALA B 180 18.236 40.423 39.328 1.00 4.58 AAAD N ATOM 3812 CA ALA B 180 17.531 41.574 39.901 1.00 9.30 AAAD C ATOM 3813 C ALA B 180 17.726 42.747 38.921 1.00 8.46 AAAD C ATOM 3814 O ALA B 180 18.851 43.013 38.482 1.00 2.00 AAAD O ATOM 3815 CB ALA B 180 18.100 41.927 41.277 1.00 4.68 AAAD C ATOM 3816 N ARG B 181 16.637 43.395 38.518 1.00 8.72 AAAD N ATOM 3817 CA ARG B 181 16.743 44.522 37.588 1.00 10.57 AAAD C ATOM 3818 C ARG B 181 17.502 45.668 38.246 1.00 10.54 AAAD C ATOM 3819 O ARG B 181 18.321 46.336 37.618 1.00 10.42 AAAD O ATOM 3820 CB ARG B 181 15.368 44.984 37.119 1.00 6.24 AAAD C ATOM 3821 CG ARG B 181 14.448 45.465 38.213 1.00 6.36 AAAD C ATOM 3822 CD ARG B 181 13.145 45.924 37.584 1.00 7.57 AAAD C ATOM 3823 NE ARG B 181 12.151 46.348 38.560 1.00 11.29 AAAD N ATOM 3824 CZ ARG B 181 12.167 47.515 39.187 1.00 11.46 AAAD C ATOM 3825 NH1 ARG B 181 13.135 48.383 38.940 1.00 12.95 AAAD N ATOM 3826 NH2 ARG B 181 11.194 47.822 40.033 1.00 17.29 AAAD N ATOM 3827 N SER B 182 17.237 45.871 39.525 1.00 12.26 AAAD N ATOM 3828 CA SER B 182 17.920 46.894 40.292 1.00 14.33 AAAD C ATOM 3829 C SER B 182 17.939 46.371 41.712 1.00 11.38 AAAD C ATOM 3830 O SER B 182 17.031 45.649 42.120 1.00 12.15 AAAD O ATOM 3831 CB SER B 182 17.188 48.242 40.206 1.00 16.26 AAAD C ATOM 3832 OG SER B 182 15.829 48.132 40.585 1.00 16.79 AAAD O ATOM 3833 N ASN B 183 19.007 46.662 42.437 1.00 9.76 AAAD N ATOM 3834 CA ASN B 183 19.097 46.201 43.798 1.00 10.84 AAAD C ATOM 3835 C ASN B 183 19.844 47.189 44.689 1.00 11.00 AAAD C ATOM 3836 O ASN B 183 20.942 47.631 44.365 1.00 12.58 AAAD O ATOM 3837 CB ASN B 183 19.774 44.830 43.824 1.00 13.07 AAAD C ATOM 3838 CG ASN B 183 19.185 43.902 44.867 1.00 16.20 AAAD C ATOM 3839 OD1 ASN B 183 19.919 43.264 45.619 1.00 18.38 AAAD O ATOM 3840 ND2 ASN B 183 17.856 43.811 44.912 1.00 13.05 AAAD N ATOM 3841 N ASP B 184 19.174 47.621 45.750 1.00 12.76 AAAD N ATOM 3842 CA ASP B 184 19.732 48.527 46.750 1.00 11.50 AAAD C ATOM 3843 C ASP B 184 20.707 47.643 47.521 1.00 9.86 AAAD C ATOM 3844 O ASP B 184 20.289 46.743 48.248 1.00 14.17 AAAD O ATOM 3845 CB ASP B 184 18.591 49.012 47.669 1.00 14.10 AAAD C ATOM 3846 CG ASP B 184 19.070 49.840 48.858 1.00 15.67 AAAD C ATOM 3847 OD1 ASP B 184 20.286 49.975 49.089 1.00 16.94 AAAD O ATOM 3848 OD2 ASP B 184 18.195 50.357 49.590 1.00 26.22 AAAD O ATOM 3849 N MET B 185 21.997 47.892 47.359 1.00 3.00 AAAD N ATOM 3850 CA MET B 185 23.020 47.104 48.026 1.00 8.86 AAAD C ATOM 3851 C MET B 185 23.029 47.125 49.557 1.00 16.49 AAAD C ATOM 3852 O MET B 185 23.431 46.148 50.189 1.00 18.52 AAAD O ATOM 3853 CB MET B 185 24.396 47.487 47.501 1.00 6.11 AAAD C ATOM 3854 CG MET B 185 24.571 47.178 46.046 1.00 15.70 AAAD C ATOM 3855 SD MET B 185 24.389 45.424 45.749 1.00 17.16 AAAD S ATOM 3856 CE MET B 185 25.903 44.858 46.433 1.00 15.17 AAAD C ATOM 3857 N ALA B 186 22.570 48.211 50.163 1.00 17.97 AAAD N ATOM 3858 CA ALA B 186 22.580 48.297 51.619 1.00 19.29 AAAD C ATOM 3859 C ALA B 186 21.427 47.607 52.337 1.00 19.15 AAAD C ATOM 3860 O ALA B 186 21.636 46.957 53.358 1.00 20.14 AAAD O ATOM 3861 CB ALA B 186 22.669 49.757 52.064 1.00 20.33 AAAD C ATOM 3862 N LEU B 187 20.221 47.745 51.802 1.00 15.71 AAAD N ATOM 3863 CA LEU B 187 19.050 47.179 52.442 1.00 15.09 AAAD C ATOM 3864 C LEU B 187 18.407 45.978 51.790 1.00 16.10 AAAD C ATOM 3865 O LEU B 187 17.966 45.064 52.475 1.00 23.93 AAAD O ATOM 3866 CB LEU B 187 17.990 48.268 52.633 1.00 20.56 AAAD C ATOM 3867 CG LEU B 187 18.294 49.363 53.666 1.00 22.30 AAAD C ATOM 3868 CD1 LEU B 187 17.154 50.375 53.729 1.00 20.97 AAAD C ATOM 3869 CD2 LEU B 187 18.524 48.729 55.034 1.00 22.00 AAAD C ATOM 3870 N GLY B 188 18.312 45.979 50.470 1.00 18.94 AAAD N ATOM 3871 CA GLY B 188 17.672 44.862 49.802 1.00 16.42 AAAD C ATOM 3872 C GLY B 188 18.566 43.700 49.407 1.00 17.32 AAAD C ATOM 3873 O GLY B 188 18.152 42.551 49.518 1.00 19.15 AAAD O ATOM 3874 N ASN B 189 19.797 43.984 48.990 1.00 12.84 AAAD N ATOM 3875 CA ASN B 189 20.702 42.938 48.535 1.00 12.94 AAAD C ATOM 3876 C ASN B 189 20.975 41.777 49.487 1.00 15.46 AAAD C ATOM 3877 O ASN B 189 20.685 40.621 49.150 1.00 12.34 AAAD O ATOM 3878 CB ASN B 189 22.011 43.533 48.028 1.00 11.82 AAAD C ATOM 3879 CG ASN B 189 22.897 42.503 47.359 1.00 16.31 AAAD C ATOM 3880 OD1 ASN B 189 23.877 42.033 47.940 1.00 20.95 AAAD O ATOM 3881 ND2 ASN B 189 22.558 42.148 46.127 1.00 16.23 AAAD N ATOM 3882 N PRO B 190 21.498 42.058 50.698 1.00 17.86 AAAD N ATOM 3883 CA PRO B 190 21.777 40.959 51.634 1.00 16.32 AAAD C ATOM 3884 C PRO B 190 20.557 40.062 51.825 1.00 14.41 AAAD C ATOM 3885 O PRO B 190 20.660 38.832 51.796 1.00 16.75 AAAD O ATOM 3886 CB PRO B 190 22.136 41.696 52.915 1.00 16.77 AAAD C ATOM 3887 CG PRO B 190 22.787 42.952 52.400 1.00 15.85 AAAD C ATOM 3888 CD PRO B 190 21.829 43.357 51.312 1.00 14.98 AAAD C ATOM 3889 N PHE B 191 19.397 40.694 51.950 1.00 9.13 AAAD N ATOM 3890 CA PHE B 191 18.129 40.001 52.132 1.00 6.48 AAAD C ATOM 3891 C PHE B 191 17.803 39.090 50.931 1.00 10.34 AAAD C ATOM 3892 O PHE B 191 17.560 37.891 51.093 1.00 9.33 AAAD O ATOM 3893 CB PHE B 191 17.048 41.061 52.302 1.00 2.00 AAAD C ATOM 3894 CG PHE B 191 15.713 40.530 52.721 1.00 2.00 AAAD C ATOM 3895 CD1 PHE B 191 15.408 40.378 54.070 1.00 2.00 AAAD C ATOM 3896 CD2 PHE B 191 14.712 40.298 51.779 1.00 3.42 AAAD C ATOM 3897 CE1 PHE B 191 14.129 40.019 54.471 1.00 5.00 AAAD C ATOM 3898 CE2 PHE B 191 13.417 39.936 52.171 1.00 2.91 AAAD C ATOM 3899 CZ PHE B 191 13.125 39.800 53.516 1.00 7.47 AAAD C ATOM 3900 N ASN B 192 17.832 39.672 49.730 1.00 11.33 AAAD N ATOM 3901 CA ASN B 192 17.524 38.972 48.484 1.00 9.91 AAAD C ATOM 3902 C ASN B 192 18.458 37.822 48.118 1.00 13.06 AAAD C ATOM 3903 O ASN B 192 17.997 36.766 47.684 1.00 14.90 AAAD O ATOM 3904 CB ASN B 192 17.499 39.956 47.315 1.00 10.94 AAAD C ATOM 3905 CG ASN B 192 16.271 40.824 47.301 1.00 7.66 AAAD C ATOM 3906 OD1 ASN B 192 16.340 41.996 46.932 1.00 15.19 AAAD O ATOM 3907 ND2 ASN B 192 15.135 40.256 47.657 1.00 9.51 AAAD N ATOM 3908 N VAL B 193 19.766 38.043 48.221 1.00 12.52 AAAD N ATOM 3909 CA VAL B 193 20.733 37.008 47.886 1.00 14.92 AAAD C ATOM 3910 C VAL B 193 20.516 35.753 48.728 1.00 21.56 AAAD C ATOM 3911 O VAL B 193 20.320 34.662 48.184 1.00 26.97 AAAD O ATOM 3912 CB VAL B 193 22.175 37.492 48.065 1.00 10.87 AAAD C ATOM 3913 CG1 VAL B 193 23.144 36.335 47.822 1.00 6.57 AAAD C ATOM 3914 CG2 VAL B 193 22.459 38.628 47.098 1.00 8.59 AAAD C ATOM 3915 N PHE B 194 20.546 35.912 50.049 1.00 20.41 AAAD N ATOM 3916 CA PHE B 194 20.334 34.800 50.965 1.00 15.49 AAAD C ATOM 3917 C PHE B 194 19.001 34.130 50.633 1.00 12.14 AAAD C ATOM 3918 O PHE B 194 18.935 32.919 50.422 1.00 13.25 AAAD O ATOM 3919 CB PHE B 194 20.335 35.309 52.413 1.00 17.33 AAAD C ATOM 3920 CG PHE B 194 19.814 34.316 53.407 1.00 17.97 AAAD C ATOM 3921 CD1 PHE B 194 20.619 33.269 53.857 1.00 15.87 AAAD C ATOM 3922 CD2 PHE B 194 18.508 34.408 53.876 1.00 16.05 AAAD C ATOM 3923 CE1 PHE B 194 20.130 32.333 54.752 1.00 17.25 AAAD C ATOM 3924 CE2 PHE B 194 18.006 33.471 54.775 1.00 16.25 AAAD C ATOM 3925 CZ PHE B 194 18.819 32.432 55.213 1.00 16.99 AAAD C ATOM 3926 N GLN B 195 17.957 34.934 50.516 1.00 6.65 AAAD N ATOM 3927 CA GLN B 195 16.622 34.435 50.207 1.00 11.45 AAAD C ATOM 3928 C GLN B 195 16.583 33.449 49.042 1.00 15.13 AAAD C ATOM 3929 O GLN B 195 15.989 32.371 49.151 1.00 17.77 AAAD O ATOM 3930 CB GLN B 195 15.705 35.607 49.896 1.00 13.21 AAAD C ATOM 3931 CG GLN B 195 14.256 35.270 49.765 1.00 13.34 AAAD C ATOM 3932 CD GLN B 195 13.437 36.491 49.422 1.00 23.97 AAAD C ATOM 3933 OE1 GLN B 195 13.885 37.372 48.677 1.00 26.69 AAAD O ATOM 3934 NE2 GLN B 195 12.248 36.577 49.994 1.00 26.39 AAAD N ATOM 3935 N TYR B 196 17.208 33.800 47.924 1.00 18.34 AAAD N ATOM 3936 CA TYR B 196 17.174 32.893 46.794 1.00 15.60 AAAD C ATOM 3937 C TYR B 196 18.041 31.659 46.913 1.00 13.26 AAAD C ATOM 3938 O TYR B 196 17.717 30.615 46.341 1.00 11.04 AAAD O ATOM 3939 CB TYR B 196 17.331 33.623 45.462 1.00 13.89 AAAD C ATOM 3940 CG TYR B 196 15.976 34.057 44.956 1.00 9.25 AAAD C ATOM 3941 CD1 TYR B 196 15.324 35.132 45.543 1.00 2.84 AAAD C ATOM 3942 CD2 TYR B 196 15.298 33.322 43.980 1.00 2.00 AAAD C ATOM 3943 CE1 TYR B 196 14.030 35.471 45.188 1.00 8.44 AAAD C ATOM 3944 CE2 TYR B 196 13.991 33.656 43.612 1.00 9.21 AAAD C ATOM 3945 CZ TYR B 196 13.364 34.735 44.229 1.00 9.59 AAAD C ATOM 3946 OH TYR B 196 12.076 35.093 43.900 1.00 10.29 AAAD O ATOM 3947 N ASN B 197 19.098 31.741 47.709 1.00 11.17 AAAD N ATOM 3948 CA ASN B 197 19.941 30.574 47.915 1.00 15.69 AAAD C ATOM 3949 C ASN B 197 19.104 29.505 48.617 1.00 16.39 AAAD C ATOM 3950 O ASN B 197 19.138 28.329 48.261 1.00 21.44 AAAD O ATOM 3951 CB ASN B 197 21.133 30.905 48.789 1.00 16.68 AAAD C ATOM 3952 CG ASN B 197 21.980 29.697 49.062 1.00 21.51 AAAD C ATOM 3953 OD1 ASN B 197 22.150 29.291 50.214 1.00 26.95 AAAD O ATOM 3954 ND2 ASN B 197 22.484 29.084 48.004 1.00 19.10 AAAD N ATOM 3955 N VAL B 198 18.325 29.939 49.598 1.00 16.10 AAAD N ATOM 3956 CA VAL B 198 17.456 29.058 50.365 1.00 14.75 AAAD C ATOM 3957 C VAL B 198 16.463 28.342 49.438 1.00 16.72 AAAD C ATOM 3958 O VAL B 198 16.159 27.157 49.626 1.00 17.25 AAAD O ATOM 3959 CB VAL B 198 16.744 29.868 51.491 1.00 14.25 AAAD C ATOM 3960 CG1 VAL B 198 15.567 29.106 52.085 1.00 5.30 AAAD C ATOM 3961 CG2 VAL B 198 17.765 30.215 52.579 1.00 10.07 AAAD C ATOM 3962 N LEU B 199 15.972 29.052 48.430 1.00 12.79 AAAD N ATOM 3963 CA LEU B 199 15.039 28.464 47.475 1.00 10.85 AAAD C ATOM 3964 C LEU B 199 15.760 27.389 46.661 1.00 11.93 AAAD C ATOM 3965 O LEU B 199 15.156 26.395 46.254 1.00 7.82 AAAD O ATOM 3966 CB LEU B 199 14.493 29.537 46.525 1.00 7.64 AAAD C ATOM 3967 CG LEU B 199 13.609 29.030 45.379 1.00 8.90 AAAD C ATOM 3968 CD1 LEU B 199 12.250 28.577 45.897 1.00 5.65 AAAD C ATOM 3969 CD2 LEU B 199 13.443 30.103 44.335 1.00 9.00 AAAD C ATOM 3970 N GLN B 200 17.048 27.611 46.405 1.00 9.55 AAAD N ATOM 3971 CA GLN B 200 17.846 26.671 45.635 1.00 11.58 AAAD C ATOM 3972 C GLN B 200 17.931 25.364 46.415 1.00 18.22 AAAD C ATOM 3973 O GLN B 200 17.722 24.274 45.867 1.00 21.94 AAAD O ATOM 3974 CB GLN B 200 19.258 27.224 45.395 1.00 3.49 AAAD C ATOM 3975 CG GLN B 200 20.044 26.447 44.362 1.00 2.00 AAAD C ATOM 3976 CD GLN B 200 21.521 26.740 44.407 1.00 2.00 AAAD C ATOM 3977 OE1 GLN B 200 21.975 27.541 45.212 1.00 8.37 AAAD O ATOM 3978 NE2 GLN B 200 22.288 26.072 43.561 1.00 3.80 AAAD N ATOM 3979 N ARG B 201 18.221 25.495 47.704 1.00 17.50 AAAD N ATOM 3980 CA ARG B 201 18.349 24.362 48.608 1.00 15.95 AAAD C ATOM 3981 C ARG B 201 17.046 23.598 48.810 1.00 15.28 AAAD C ATOM 3982 O ARG B 201 17.046 22.365 48.809 1.00 17.42 AAAD O ATOM 3983 CB ARG B 201 18.919 24.845 49.932 1.00 10.52 AAAD C ATOM 3984 CG ARG B 201 20.286 25.432 49.734 1.00 5.65 AAAD C ATOM 3985 CD ARG B 201 20.856 26.056 50.976 1.00 6.15 AAAD C ATOM 3986 NE ARG B 201 22.223 26.476 50.715 1.00 5.86 AAAD N ATOM 3987 CZ ARG B 201 23.286 25.998 51.349 1.00 13.11 AAAD C ATOM 3988 NH1 ARG B 201 23.136 25.084 52.298 1.00 15.69 AAAD N ATOM 3989 NH2 ARG B 201 24.503 26.365 50.970 1.00 15.07 AAAD N ATOM 3990 N MET B 202 15.941 24.322 48.963 1.00 12.23 AAAD N ATOM 3991 CA MET B 202 14.631 23.693 49.124 1.00 16.20 AAAD C ATOM 3992 C MET B 202 14.308 22.816 47.921 1.00 20.36 AAAD C ATOM 3993 O MET B 202 13.892 21.668 48.081 1.00 28.60 AAAD O ATOM 3994 CB MET B 202 13.529 24.743 49.242 1.00 14.74 AAAD C ATOM 3995 CG MET B 202 13.586 25.585 50.482 1.00 19.26 AAAD C ATOM 3996 SD MET B 202 12.322 26.846 50.411 1.00 25.66 AAAD S ATOM 3997 CE MET B 202 10.843 25.888 50.183 1.00 22.68 AAAD C ATOM 3998 N ILE B 203 14.497 23.367 46.724 1.00 19.47 AAAD N ATOM 3999 CA ILE B 203 14.218 22.666 45.477 1.00 19.03 AAAD C ATOM 4000 C ILE B 203 15.193 21.520 45.186 1.00 20.99 AAAD C ATOM 4001 O ILE B 203 14.783 20.454 44.709 1.00 14.73 AAAD O ATOM 4002 CB ILE B 203 14.128 23.668 44.304 1.00 23.48 AAAD C ATOM 4003 CG1 ILE B 203 12.866 24.522 44.486 1.00 23.85 AAAD C ATOM 4004 CG2 ILE B 203 14.118 22.945 42.952 1.00 22.92 AAAD C ATOM 4005 CD1 ILE B 203 12.557 25.441 43.343 1.00 29.07 AAAD C ATOM 4006 N ALA B 204 16.470 21.730 45.494 1.00 20.83 AAAD N ATOM 4007 CA ALA B 204 17.487 20.702 45.298 1.00 18.44 AAAD C ATOM 4008 C ALA B 204 17.254 19.520 46.250 1.00 20.61 AAAD C ATOM 4009 O ALA B 204 17.688 18.403 45.984 1.00 23.93 AAAD O ATOM 4010 CB ALA B 204 18.861 21.285 45.515 1.00 21.32 AAAD C ATOM 4011 N GLN B 205 16.596 19.777 47.374 1.00 19.90 AAAD N ATOM 4012 CA GLN B 205 16.300 18.728 48.335 1.00 20.48 AAAD C ATOM 4013 C GLN B 205 15.095 17.927 47.889 1.00 19.68 AAAD C ATOM 4014 O GLN B 205 15.099 16.712 47.991 1.00 24.56 AAAD O ATOM 4015 CB GLN B 205 16.055 19.303 49.738 1.00 27.38 AAAD C ATOM 4016 CG GLN B 205 15.490 18.289 50.733 1.00 27.50 AAAD C ATOM 4017 CD GLN B 205 15.529 18.772 52.171 1.00 29.50 AAAD C ATOM 4018 OE1 GLN B 205 16.580 19.161 52.680 1.00 29.17 AAAD O ATOM 4019 NE2 GLN B 205 14.391 18.712 52.845 1.00 26.73 AAAD N ATOM 4020 N VAL B 206 14.067 18.597 47.385 1.00 17.98 AAAD N ATOM 4021 CA VAL B 206 12.878 17.885 46.948 1.00 18.66 AAAD C ATOM 4022 C VAL B 206 12.953 17.259 45.552 1.00 21.56 AAAD C ATOM 4023 O VAL B 206 12.007 16.592 45.130 1.00 26.06 AAAD O ATOM 4024 CB VAL B 206 11.601 18.741 47.084 1.00 19.52 AAAD C ATOM 4025 CG1 VAL B 206 11.455 19.234 48.522 1.00 20.29 AAAD C ATOM 4026 CG2 VAL B 206 11.617 19.886 46.102 1.00 19.85 AAAD C ATOM 4027 N THR B 207 14.040 17.510 44.823 1.00 18.26 AAAD N ATOM 4028 CA THR B 207 14.222 16.930 43.490 1.00 16.03 AAAD C ATOM 4029 C THR B 207 15.411 15.965 43.518 1.00 17.91 AAAD C ATOM 4030 O THR B 207 15.720 15.297 42.532 1.00 16.34 AAAD O ATOM 4031 CB THR B 207 14.430 18.014 42.393 1.00 15.29 AAAD C ATOM 4032 OG1 THR B 207 15.563 18.826 42.714 1.00 19.15 AAAD O ATOM 4033 CG2 THR B 207 13.214 18.905 42.274 1.00 8.41 AAAD C ATOM 4034 N GLY B 208 16.080 15.910 44.665 1.00 18.70 AAAD N ATOM 4035 CA GLY B 208 17.201 15.011 44.837 1.00 13.49 AAAD C ATOM 4036 C GLY B 208 18.402 15.302 43.979 1.00 17.23 AAAD C ATOM 4037 O GLY B 208 18.958 14.395 43.362 1.00 22.45 AAAD O ATOM 4038 N TYR B 209 18.837 16.555 43.982 1.00 16.84 AAAD N ATOM 4039 CA TYR B 209 19.999 16.962 43.218 1.00 13.31 AAAD C ATOM 4040 C TYR B 209 21.002 17.545 44.188 1.00 16.13 AAAD C ATOM 4041 O TYR B 209 20.645 17.999 45.280 1.00 19.67 AAAD O ATOM 4042 CB TYR B 209 19.621 18.024 42.184 1.00 13.22 AAAD C ATOM 4043 CG TYR B 209 18.872 17.485 40.994 1.00 10.92 AAAD C ATOM 4044 CD1 TYR B 209 19.466 16.573 40.125 1.00 14.47 AAAD C ATOM 4045 CD2 TYR B 209 17.558 17.861 40.752 1.00 12.69 AAAD C ATOM 4046 CE1 TYR B 209 18.761 16.045 39.046 1.00 16.95 AAAD C ATOM 4047 CE2 TYR B 209 16.846 17.343 39.680 1.00 15.03 AAAD C ATOM 4048 CZ TYR B 209 17.453 16.435 38.839 1.00 14.80 AAAD C ATOM 4049 OH TYR B 209 16.738 15.897 37.809 1.00 20.37 AAAD O ATOM 4050 N GLU B 210 22.270 17.500 43.816 1.00 19.84 AAAD N ATOM 4051 CA GLU B 210 23.299 18.082 44.665 1.00 23.81 AAAD C ATOM 4052 C GLU B 210 23.290 19.566 44.358 1.00 20.18 AAAD C ATOM 4053 O GLU B 210 22.805 19.977 43.302 1.00 18.87 AAAD O ATOM 4054 CB GLU B 210 24.675 17.487 44.369 1.00 29.05 AAAD C ATOM 4055 CG GLU B 210 24.920 16.171 45.076 1.00 42.34 AAAD C ATOM 4056 CD GLU B 210 24.686 16.275 46.575 1.00 51.30 AAAD C ATOM 4057 OE1 GLU B 210 25.571 16.807 47.284 1.00 58.68 AAAD O ATOM 4058 OE2 GLU B 210 23.614 15.826 47.043 1.00 53.98 AAAD O ATOM 4059 N LEU B 211 23.798 20.376 45.276 1.00 21.47 AAAD N ATOM 4060 CA LEU B 211 23.813 21.814 45.049 1.00 19.16 AAAD C ATOM 4061 C LEU B 211 24.876 22.245 44.066 1.00 19.36 AAAD C ATOM 4062 O LEU B 211 26.050 21.900 44.201 1.00 18.93 AAAD O ATOM 4063 CB LEU B 211 24.010 22.584 46.353 1.00 17.58 AAAD C ATOM 4064 CG LEU B 211 22.817 22.639 47.301 1.00 16.39 AAAD C ATOM 4065 CD1 LEU B 211 23.211 23.422 48.531 1.00 17.55 AAAD C ATOM 4066 CD2 LEU B 211 21.629 23.274 46.612 1.00 13.23 AAAD C ATOM 4067 N GLY B 212 24.438 22.949 43.038 1.00 20.58 AAAD N ATOM 4068 CA GLY B 212 25.368 23.468 42.065 1.00 22.25 AAAD C ATOM 4069 C GLY B 212 25.620 24.915 42.450 1.00 22.61 AAAD C ATOM 4070 O GLY B 212 25.279 25.361 43.555 1.00 14.97 AAAD O ATOM 4071 N GLU B 213 26.137 25.673 41.492 1.00 24.63 AAAD N ATOM 4072 CA GLU B 213 26.451 27.080 41.693 1.00 22.61 AAAD C ATOM 4073 C GLU B 213 25.209 27.934 41.872 1.00 20.28 AAAD C ATOM 4074 O GLU B 213 24.117 27.562 41.420 1.00 17.61 AAAD O ATOM 4075 CB GLU B 213 27.264 27.603 40.511 1.00 23.01 AAAD C ATOM 4076 CG GLU B 213 28.476 28.407 40.932 1.00 33.39 AAAD C ATOM 4077 CD GLU B 213 29.370 28.807 39.774 1.00 38.17 AAAD C ATOM 4078 OE1 GLU B 213 29.118 28.376 38.622 1.00 41.01 AAAD O ATOM 4079 OE2 GLU B 213 30.341 29.555 40.027 1.00 45.13 AAAD O ATOM 4080 N TYR B 214 25.396 29.059 42.558 1.00 17.12 AAAD N ATOM 4081 CA TYR B 214 24.349 30.036 42.816 1.00 12.70 AAAD C ATOM 4082 C TYR B 214 24.915 31.335 42.272 1.00 15.28 AAAD C ATOM 4083 O TYR B 214 25.968 31.795 42.720 1.00 15.64 AAAD O ATOM 4084 CB TYR B 214 24.108 30.183 44.312 1.00 10.17 AAAD C ATOM 4085 CG TYR B 214 23.091 31.244 44.659 1.00 9.34 AAAD C ATOM 4086 CD1 TYR B 214 21.850 31.271 44.027 1.00 8.43 AAAD C ATOM 4087 CD2 TYR B 214 23.358 32.208 45.631 1.00 3.53 AAAD C ATOM 4088 CE1 TYR B 214 20.898 32.228 44.352 1.00 10.67 AAAD C ATOM 4089 CE2 TYR B 214 22.406 33.172 45.965 1.00 2.00 AAAD C ATOM 4090 CZ TYR B 214 21.180 33.172 45.323 1.00 4.17 AAAD C ATOM 4091 OH TYR B 214 20.211 34.086 45.655 1.00 2.94 AAAD O ATOM 4092 N ILE B 215 24.227 31.912 41.296 1.00 17.42 AAAD N ATOM 4093 CA ILE B 215 24.670 33.144 40.656 1.00 12.30 AAAD C ATOM 4094 C ILE B 215 23.591 34.221 40.810 1.00 10.30 AAAD C ATOM 4095 O ILE B 215 22.418 33.985 40.488 1.00 9.52 AAAD O ATOM 4096 CB ILE B 215 24.961 32.874 39.146 1.00 15.37 AAAD C ATOM 4097 CG1 ILE B 215 26.014 31.761 38.997 1.00 12.33 AAAD C ATOM 4098 CG2 ILE B 215 25.464 34.133 38.473 1.00 14.27 AAAD C ATOM 4099 CD1 ILE B 215 25.849 30.919 37.758 1.00 9.35 AAAD C ATOM 4100 N PHE B 216 23.987 35.387 41.321 1.00 7.27 AAAD N ATOM 4101 CA PHE B 216 23.063 36.505 41.525 1.00 11.98 AAAD C ATOM 4102 C PHE B 216 23.487 37.701 40.673 1.00 14.70 AAAD C ATOM 4103 O PHE B 216 24.505 38.345 40.954 1.00 14.81 AAAD O ATOM 4104 CB PHE B 216 23.052 36.926 42.994 1.00 13.61 AAAD C ATOM 4105 CG PHE B 216 21.846 37.731 43.391 1.00 17.56 AAAD C ATOM 4106 CD1 PHE B 216 21.823 39.111 43.226 1.00 16.82 AAAD C ATOM 4107 CD2 PHE B 216 20.730 37.104 43.934 1.00 11.50 AAAD C ATOM 4108 CE1 PHE B 216 20.706 39.854 43.594 1.00 16.34 AAAD C ATOM 4109 CE2 PHE B 216 19.609 37.842 44.303 1.00 16.32 AAAD C ATOM 4110 CZ PHE B 216 19.596 39.219 44.134 1.00 12.91 AAAD C ATOM 4111 N ASN B 217 22.712 37.994 39.632 1.00 12.18 AAAD N ATOM 4112 CA ASN B 217 23.022 39.111 38.746 1.00 13.54 AAAD C ATOM 4113 C ASN B 217 22.182 40.308 39.125 1.00 12.72 AAAD C ATOM 4114 O ASN B 217 21.016 40.155 39.506 1.00 10.36 AAAD O ATOM 4115 CB ASN B 217 22.731 38.754 37.286 1.00 11.10 AAAD C ATOM 4116 CG ASN B 217 23.453 37.513 36.835 1.00 10.83 AAAD C ATOM 4117 OD1 ASN B 217 24.693 37.458 36.840 1.00 6.63 AAAD O ATOM 4118 ND2 ASN B 217 22.686 36.489 36.464 1.00 4.18 AAAD N ATOM 4119 N ILE B 218 22.764 41.495 38.972 1.00 11.05 AAAD N ATOM 4120 CA ILE B 218 22.091 42.754 39.287 1.00 9.84 AAAD C ATOM 4121 C ILE B 218 22.231 43.728 38.115 1.00 8.15 AAAD C ATOM 4122 O ILE B 218 23.340 43.967 37.631 1.00 8.48 AAAD O ATOM 4123 CB ILE B 218 22.713 43.415 40.544 1.00 12.09 AAAD C ATOM 4124 CG1 ILE B 218 22.787 42.411 41.701 1.00 12.18 AAAD C ATOM 4125 CG2 ILE B 218 21.868 44.608 40.976 1.00 11.07 AAAD C ATOM 4126 CD1 ILE B 218 23.672 42.855 42.831 1.00 12.69 AAAD C ATOM 4127 N GLY B 219 21.106 44.272 37.656 1.00 9.16 AAAD N ATOM 4128 CA GLY B 219 21.127 45.233 36.564 1.00 10.44 AAAD C ATOM 4129 C GLY B 219 21.683 46.555 37.072 1.00 10.82 AAAD C ATOM 4130 O GLY B 219 22.886 46.834 36.959 1.00 6.58 AAAD O ATOM 4131 N ASP B 220 20.809 47.343 37.686 1.00 8.14 AAAD N ATOM 4132 CA ASP B 220 21.183 48.622 38.258 1.00 6.02 AAAD C ATOM 4133 C ASP B 220 21.602 48.387 39.702 1.00 7.17 AAAD C ATOM 4134 O ASP B 220 20.764 48.359 40.613 1.00 2.00 AAAD O ATOM 4135 CB ASP B 220 20.001 49.589 38.212 1.00 12.34 AAAD C ATOM 4136 CG ASP B 220 20.396 51.020 38.547 1.00 11.91 AAAD C ATOM 4137 OD1 ASP B 220 21.412 51.237 39.236 1.00 10.61 AAAD O ATOM 4138 OD2 ASP B 220 19.671 51.935 38.112 1.00 18.76 AAAD O ATOM 4139 N CYS B 221 22.902 48.210 39.891 1.00 9.62 AAAD N ATOM 4140 CA CYS B 221 23.500 47.969 41.199 1.00 12.24 AAAD C ATOM 4141 C CYS B 221 23.801 49.334 41.833 1.00 15.09 AAAD C ATOM 4142 O CYS B 221 24.686 50.049 41.366 1.00 16.65 AAAD O ATOM 4143 CB CYS B 221 24.797 47.183 40.990 1.00 8.47 AAAD C ATOM 4144 SG CYS B 221 25.579 46.595 42.471 1.00 17.83 AAAD S ATOM 4145 N HIS B 222 23.138 49.679 42.932 1.00 15.74 AAAD N ATOM 4146 CA HIS B 222 23.365 51.000 43.519 1.00 16.61 AAAD C ATOM 4147 C HIS B 222 23.267 51.128 45.035 1.00 19.96 AAAD C ATOM 4148 O HIS B 222 22.791 50.228 45.726 1.00 22.01 AAAD O ATOM 4149 CB HIS B 222 22.342 51.953 42.944 1.00 10.93 AAAD C ATOM 4150 CG HIS B 222 20.932 51.590 43.293 1.00 6.02 AAAD C ATOM 4151 ND1 HIS B 222 20.172 50.747 42.516 1.00 11.35 AAAD N ATOM 4152 CD2 HIS B 222 20.144 51.969 44.324 1.00 9.43 AAAD C ATOM 4153 CE1 HIS B 222 18.969 50.628 43.049 1.00 10.22 AAAD C ATOM 4154 NE2 HIS B 222 18.929 51.360 44.148 1.00 11.02 AAAD N ATOM 4155 N VAL B 223 23.654 52.299 45.529 1.00 17.40 AAAD N ATOM 4156 CA VAL B 223 23.563 52.621 46.945 1.00 16.46 AAAD C ATOM 4157 C VAL B 223 23.069 54.058 47.008 1.00 15.94 AAAD C ATOM 4158 O VAL B 223 23.363 54.851 46.117 1.00 22.49 AAAD O ATOM 4159 CB VAL B 223 24.929 52.489 47.674 1.00 16.44 AAAD C ATOM 4160 CG1 VAL B 223 25.474 51.070 47.536 1.00 20.40 AAAD C ATOM 4161 CG2 VAL B 223 25.931 53.476 47.140 1.00 15.88 AAAD C ATOM 4162 N TYR B 224 22.225 54.367 47.982 1.00 15.59 AAAD N ATOM 4163 CA TYR B 224 21.731 55.731 48.122 1.00 12.89 AAAD C ATOM 4164 C TYR B 224 22.831 56.551 48.777 1.00 11.99 AAAD C ATOM 4165 O TYR B 224 23.503 56.064 49.685 1.00 13.84 AAAD O ATOM 4166 CB TYR B 224 20.456 55.774 48.956 1.00 12.73 AAAD C ATOM 4167 CG TYR B 224 19.271 55.212 48.227 1.00 9.46 AAAD C ATOM 4168 CD1 TYR B 224 19.074 53.834 48.139 1.00 15.09 AAAD C ATOM 4169 CD2 TYR B 224 18.368 56.051 47.584 1.00 10.59 AAAD C ATOM 4170 CE1 TYR B 224 18.008 53.307 47.421 1.00 16.35 AAAD C ATOM 4171 CE2 TYR B 224 17.297 55.538 46.865 1.00 16.34 AAAD C ATOM 4172 CZ TYR B 224 17.120 54.168 46.784 1.00 21.15 AAAD C ATOM 4173 OH TYR B 224 16.056 53.662 46.066 1.00 24.56 AAAD O ATOM 4174 N THR B 225 23.011 57.784 48.312 1.00 12.05 AAAD N ATOM 4175 CA THR B 225 24.057 58.677 48.815 1.00 13.81 AAAD C ATOM 4176 C THR B 225 24.159 58.782 50.342 1.00 15.63 AAAD C ATOM 4177 O THR B 225 25.261 58.805 50.896 1.00 18.32 AAAD O ATOM 4178 CB THR B 225 23.915 60.087 48.209 1.00 14.56 AAAD C ATOM 4179 OG1 THR B 225 22.640 60.642 48.573 1.00 10.83 AAAD O ATOM 4180 CG2 THR B 225 24.045 60.016 46.694 1.00 12.25 AAAD C ATOM 4181 N ARG B 226 23.022 58.844 51.025 1.00 16.69 AAAD N ATOM 4182 CA ARG B 226 23.039 58.928 52.485 1.00 19.50 AAAD C ATOM 4183 C ARG B 226 23.513 57.645 53.188 1.00 18.86 AAAD C ATOM 4184 O ARG B 226 23.777 57.660 54.388 1.00 24.31 AAAD O ATOM 4185 CB ARG B 226 21.663 59.338 53.036 1.00 15.88 AAAD C ATOM 4186 CG ARG B 226 21.292 60.806 52.787 1.00 16.96 AAAD C ATOM 4187 CD ARG B 226 20.043 61.205 53.574 1.00 18.11 AAAD C ATOM 4188 NE ARG B 226 19.558 62.537 53.223 1.00 18.11 AAAD N ATOM 4189 CZ ARG B 226 18.372 63.033 53.579 1.00 17.42 AAAD C ATOM 4190 NH1 ARG B 226 17.525 62.321 54.306 1.00 7.33 AAAD N ATOM 4191 NH2 ARG B 226 18.016 64.242 53.176 1.00 24.22 AAAD N ATOM 4192 N HIS B 227 23.647 56.546 52.455 1.00 12.21 AAAD N ATOM 4193 CA HIS B 227 24.074 55.293 53.076 1.00 14.04 AAAD C ATOM 4194 C HIS B 227 25.582 55.048 53.039 1.00 18.07 AAAD C ATOM 4195 O HIS B 227 26.087 54.157 53.735 1.00 18.69 AAAD O ATOM 4196 CB HIS B 227 23.359 54.101 52.435 1.00 6.53 AAAD C ATOM 4197 CG HIS B 227 21.876 54.117 52.609 1.00 4.61 AAAD C ATOM 4198 ND1 HIS B 227 21.029 53.329 51.858 1.00 7.31 AAAD N ATOM 4199 CD2 HIS B 227 21.081 54.813 53.459 1.00 5.11 AAAD C ATOM 4200 CE1 HIS B 227 19.780 53.536 52.239 1.00 8.73 AAAD C ATOM 4201 NE2 HIS B 227 19.784 54.430 53.208 1.00 4.46 AAAD N ATOM 4202 N ILE B 228 26.305 55.899 52.317 1.00 17.47 AAAD N ATOM 4203 CA ILE B 228 27.746 55.739 52.147 1.00 15.48 AAAD C ATOM 4204 C ILE B 228 28.644 55.737 53.385 1.00 19.24 AAAD C ATOM 4205 O ILE B 228 29.573 54.933 53.476 1.00 17.86 AAAD O ATOM 4206 CB ILE B 228 28.265 56.711 51.066 1.00 15.13 AAAD C ATOM 4207 CG1 ILE B 228 27.529 56.428 49.747 1.00 16.03 AAAD C ATOM 4208 CG2 ILE B 228 29.758 56.538 50.862 1.00 11.31 AAAD C ATOM 4209 CD1 ILE B 228 27.884 57.352 48.618 1.00 19.49 AAAD C ATOM 4210 N ASP B 229 28.369 56.603 54.353 1.00 25.29 AAAD N ATOM 4211 CA ASP B 229 29.198 56.648 55.554 1.00 25.54 AAAD C ATOM 4212 C ASP B 229 29.139 55.380 56.400 1.00 24.83 AAAD C ATOM 4213 O ASP B 229 30.163 54.907 56.889 1.00 20.30 AAAD O ATOM 4214 CB ASP B 229 28.885 57.894 56.378 1.00 33.25 AAAD C ATOM 4215 CG ASP B 229 29.487 59.157 55.775 1.00 36.43 AAAD C ATOM 4216 OD1 ASP B 229 30.634 59.103 55.267 1.00 35.89 AAAD O ATOM 4217 OD2 ASP B 229 28.810 60.204 55.820 1.00 42.61 AAAD O ATOM 4218 N ASN B 230 27.949 54.803 56.532 1.00 25.91 AAAD N ATOM 4219 CA ASN B 230 27.781 53.573 57.297 1.00 27.60 AAAD C ATOM 4220 C ASN B 230 28.341 52.394 56.509 1.00 28.75 AAAD C ATOM 4221 O ASN B 230 28.919 51.479 57.089 1.00 27.29 AAAD O ATOM 4222 CB ASN B 230 26.313 53.335 57.652 1.00 30.23 AAAD C ATOM 4223 CG ASN B 230 25.890 54.071 58.913 1.00 33.35 AAAD C ATOM 4224 OD1 ASN B 230 26.717 54.656 59.612 1.00 33.85 AAAD O ATOM 4225 ND2 ASN B 230 24.600 54.029 59.218 1.00 30.74 AAAD N ATOM 4226 N LEU B 231 28.175 52.423 55.187 1.00 25.56 AAAD N ATOM 4227 CA LEU B 231 28.701 51.369 54.325 1.00 26.32 AAAD C ATOM 4228 C LEU B 231 30.213 51.374 54.492 1.00 25.01 AAAD C ATOM 4229 O LEU B 231 30.856 50.330 54.489 1.00 27.12 AAAD O ATOM 4230 CB LEU B 231 28.324 51.629 52.860 1.00 24.23 AAAD C ATOM 4231 CG LEU B 231 27.332 50.699 52.149 1.00 22.44 AAAD C ATOM 4232 CD1 LEU B 231 26.211 50.263 53.070 1.00 18.28 AAAD C ATOM 4233 CD2 LEU B 231 26.779 51.395 50.916 1.00 18.59 AAAD C ATOM 4234 N LYS B 232 30.767 52.569 54.649 1.00 29.05 AAAD N ATOM 4235 CA LYS B 232 32.197 52.745 54.850 1.00 31.01 AAAD C ATOM 4236 C LYS B 232 32.591 52.055 56.152 1.00 30.23 AAAD C ATOM 4237 O LYS B 232 33.590 51.330 56.207 1.00 31.68 AAAD O ATOM 4238 CB LYS B 232 32.529 54.240 54.924 1.00 36.26 AAAD C ATOM 4239 CG LYS B 232 32.871 54.884 53.593 1.00 41.01 AAAD C ATOM 4240 CD LYS B 232 34.249 54.431 53.160 1.00 51.42 AAAD C ATOM 4241 CE LYS B 232 34.731 55.116 51.895 1.00 55.73 AAAD C ATOM 4242 NZ LYS B 232 36.161 54.745 51.647 1.00 62.88 AAAD N ATOM 4243 N ILE B 233 31.785 52.277 57.188 1.00 28.53 AAAD N ATOM 4244 CA ILE B 233 31.996 51.698 58.513 1.00 27.31 AAAD C ATOM 4245 C ILE B 233 31.961 50.170 58.427 1.00 29.23 AAAD C ATOM 4246 O ILE B 233 32.919 49.485 58.795 1.00 31.32 AAAD O ATOM 4247 CB ILE B 233 30.889 52.175 59.492 1.00 25.43 AAAD C ATOM 4248 CG1 ILE B 233 31.044 53.665 59.781 1.00 30.15 AAAD C ATOM 4249 CG2 ILE B 233 30.919 51.371 60.784 1.00 30.84 AAAD C ATOM 4250 CD1 ILE B 233 29.933 54.226 60.653 1.00 33.92 AAAD C ATOM 4251 N GLN B 234 30.845 49.662 57.919 1.00 26.95 AAAD N ATOM 4252 CA GLN B 234 30.599 48.240 57.743 1.00 26.84 AAAD C ATOM 4253 C GLN B 234 31.738 47.527 57.014 1.00 26.81 AAAD C ATOM 4254 O GLN B 234 32.093 46.407 57.360 1.00 30.15 AAAD O ATOM 4255 CB GLN B 234 29.277 48.067 56.992 1.00 23.49 AAAD C ATOM 4256 CG GLN B 234 28.871 46.657 56.672 1.00 26.07 AAAD C ATOM 4257 CD GLN B 234 27.498 46.596 56.033 1.00 27.86 AAAD C ATOM 4258 OE1 GLN B 234 27.003 47.588 55.501 1.00 31.16 AAAD O ATOM 4259 NE2 GLN B 234 26.877 45.429 56.078 1.00 29.12 AAAD N ATOM 4260 N MET B 235 32.336 48.180 56.028 1.00 28.66 AAAD N ATOM 4261 CA MET B 235 33.425 47.554 55.299 1.00 31.93 AAAD C ATOM 4262 C MET B 235 34.627 47.292 56.200 1.00 34.14 AAAD C ATOM 4263 O MET B 235 35.285 46.264 56.073 1.00 35.97 AAAD O ATOM 4264 CB MET B 235 33.837 48.407 54.102 1.00 34.13 AAAD C ATOM 4265 CG MET B 235 32.891 48.323 52.919 1.00 37.12 AAAD C ATOM 4266 SD MET B 235 33.573 49.100 51.441 1.00 41.57 AAAD S ATOM 4267 CE MET B 235 34.913 47.956 51.063 1.00 39.78 AAAD C ATOM 4268 N GLU B 236 34.886 48.207 57.128 1.00 37.68 AAAD N ATOM 4269 CA GLU B 236 36.011 48.083 58.052 1.00 42.16 AAAD C ATOM 4270 C GLU B 236 35.745 47.107 59.205 1.00 42.56 AAAD C ATOM 4271 O GLU B 236 36.629 46.865 60.034 1.00 44.42 AAAD O ATOM 4272 CB GLU B 236 36.381 49.462 58.614 1.00 50.92 AAAD C ATOM 4273 CG GLU B 236 37.525 50.167 57.878 1.00 61.70 AAAD C ATOM 4274 CD GLU B 236 38.830 50.190 58.677 1.00 68.78 AAAD C ATOM 4275 OE1 GLU B 236 38.969 49.407 59.645 1.00 72.12 AAAD O ATOM 4276 OE2 GLU B 236 39.723 50.999 58.338 1.00 72.83 AAAD O ATOM 4277 N ARG B 237 34.537 46.551 59.257 1.00 37.72 AAAD N ATOM 4278 CA ARG B 237 34.168 45.618 60.319 1.00 32.75 AAAD C ATOM 4279 C ARG B 237 34.789 44.231 60.228 1.00 33.04 AAAD C ATOM 4280 O ARG B 237 35.273 43.813 59.180 1.00 31.89 AAAD O ATOM 4281 CB ARG B 237 32.650 45.483 60.425 1.00 25.45 AAAD C ATOM 4282 CG ARG B 237 32.001 46.596 61.199 1.00 14.64 AAAD C ATOM 4283 CD ARG B 237 30.543 46.291 61.406 1.00 11.72 AAAD C ATOM 4284 NE ARG B 237 29.879 47.292 62.234 1.00 11.29 AAAD N ATOM 4285 CZ ARG B 237 28.590 47.249 62.553 1.00 15.07 AAAD C ATOM 4286 NH1 ARG B 237 27.837 46.254 62.115 1.00 15.65 AAAD N ATOM 4287 NH2 ARG B 237 28.053 48.194 63.309 1.00 16.93 AAAD N ATOM 4288 N GLU B 238 34.751 43.527 61.355 1.00 37.75 AAAD N ATOM 4289 CA GLU B 238 35.282 42.178 61.472 1.00 40.39 AAAD C ATOM 4290 C GLU B 238 34.240 41.222 60.916 1.00 38.65 AAAD C ATOM 4291 O GLU B 238 33.065 41.282 61.291 1.00 36.25 AAAD O ATOM 4292 CB GLU B 238 35.557 41.839 62.943 1.00 44.76 AAAD C ATOM 4293 CG GLU B 238 36.111 40.430 63.181 1.00 52.20 AAAD C ATOM 4294 CD GLU B 238 36.132 40.031 64.656 1.00 53.68 AAAD C ATOM 4295 OE1 GLU B 238 36.174 40.924 65.528 1.00 53.49 AAAD O ATOM 4296 OE2 GLU B 238 36.104 38.816 64.946 1.00 55.48 AAAD O ATOM 4297 N GLN B 239 34.671 40.362 60.002 1.00 38.90 AAAD N ATOM 4298 CA GLN B 239 33.777 39.393 59.391 1.00 36.86 AAAD C ATOM 4299 C GLN B 239 33.848 38.115 60.211 1.00 37.98 AAAD C ATOM 4300 O GLN B 239 34.827 37.874 60.925 1.00 37.83 AAAD O ATOM 4301 CB GLN B 239 34.191 39.128 57.939 1.00 34.26 AAAD C ATOM 4302 CG GLN B 239 34.226 40.371 57.062 1.00 28.99 AAAD C ATOM 4303 CD GLN B 239 34.908 40.138 55.725 1.00 33.36 AAAD C ATOM 4304 OE1 GLN B 239 35.166 39.001 55.328 1.00 32.27 AAAD O ATOM 4305 NE2 GLN B 239 35.201 41.218 55.022 1.00 35.70 AAAD N ATOM 4306 N PHE B 240 32.777 37.334 60.165 1.00 39.12 AAAD N ATOM 4307 CA PHE B 240 32.714 36.078 60.896 1.00 35.86 AAAD C ATOM 4308 C PHE B 240 32.557 34.905 59.949 1.00 35.84 AAAD C ATOM 4309 O PHE B 240 32.119 35.069 58.812 1.00 39.93 AAAD O ATOM 4310 CB PHE B 240 31.546 36.099 61.872 1.00 30.80 AAAD C ATOM 4311 CG PHE B 240 31.700 37.101 62.956 1.00 31.86 AAAD C ATOM 4312 CD1 PHE B 240 32.711 36.973 63.899 1.00 34.43 AAAD C ATOM 4313 CD2 PHE B 240 30.844 38.183 63.037 1.00 32.82 AAAD C ATOM 4314 CE1 PHE B 240 32.865 37.913 64.906 1.00 33.98 AAAD C ATOM 4315 CE2 PHE B 240 30.989 39.127 64.039 1.00 36.46 AAAD C ATOM 4316 CZ PHE B 240 32.000 38.993 64.975 1.00 35.21 AAAD C ATOM 4317 N GLU B 241 32.905 33.718 60.433 1.00 34.03 AAAD N ATOM 4318 CA GLU B 241 32.798 32.503 59.643 1.00 31.12 AAAD C ATOM 4319 C GLU B 241 31.340 32.329 59.243 1.00 29.36 AAAD C ATOM 4320 O GLU B 241 30.442 32.716 59.988 1.00 25.08 AAAD O ATOM 4321 CB GLU B 241 33.263 31.301 60.469 1.00 32.78 AAAD C ATOM 4322 CG GLU B 241 34.671 31.446 61.067 1.00 34.35 AAAD C ATOM 4323 CD GLU B 241 35.775 31.562 60.012 1.00 39.86 AAAD C ATOM 4324 OE1 GLU B 241 35.567 31.129 58.858 1.00 45.48 AAAD O ATOM 4325 OE2 GLU B 241 36.864 32.082 60.341 1.00 43.02 AAAD O ATOM 4326 N ALA B 242 31.105 31.776 58.061 1.00 29.73 AAAD N ATOM 4327 CA ALA B 242 29.739 31.570 57.593 1.00 31.58 AAAD C ATOM 4328 C ALA B 242 29.033 30.557 58.465 1.00 32.09 AAAD C ATOM 4329 O ALA B 242 29.582 29.495 58.751 1.00 35.77 AAAD O ATOM 4330 CB ALA B 242 29.746 31.079 56.175 1.00 37.94 AAAD C ATOM 4331 N PRO B 243 27.783 30.845 58.850 1.00 29.38 AAAD N ATOM 4332 CA PRO B 243 26.994 29.948 59.694 1.00 28.90 AAAD C ATOM 4333 C PRO B 243 26.530 28.717 58.917 1.00 28.89 AAAD C ATOM 4334 O PRO B 243 26.804 28.572 57.722 1.00 29.75 AAAD O ATOM 4335 CB PRO B 243 25.812 30.826 60.094 1.00 26.15 AAAD C ATOM 4336 CG PRO B 243 25.591 31.631 58.848 1.00 23.04 AAAD C ATOM 4337 CD PRO B 243 27.000 32.040 58.487 1.00 27.59 AAAD C ATOM 4338 N GLU B 244 25.803 27.844 59.596 1.00 29.47 AAAD N ATOM 4339 CA GLU B 244 25.303 26.639 58.971 1.00 31.22 AAAD C ATOM 4340 C GLU B 244 23.789 26.735 58.913 1.00 29.59 AAAD C ATOM 4341 O GLU B 244 23.155 27.188 59.865 1.00 29.72 AAAD O ATOM 4342 CB GLU B 244 25.737 25.411 59.773 1.00 38.98 AAAD C ATOM 4343 CG GLU B 244 25.605 24.103 59.008 1.00 57.79 AAAD C ATOM 4344 CD GLU B 244 26.195 22.911 59.748 1.00 64.95 AAAD C ATOM 4345 OE1 GLU B 244 27.308 23.038 60.313 1.00 67.09 AAAD O ATOM 4346 OE2 GLU B 244 25.545 21.840 59.749 1.00 70.02 AAAD O ATOM 4347 N LEU B 245 23.216 26.382 57.771 1.00 28.23 AAAD N ATOM 4348 CA LEU B 245 21.774 26.422 57.613 1.00 25.12 AAAD C ATOM 4349 C LEU B 245 21.280 24.992 57.690 1.00 28.78 AAAD C ATOM 4350 O LEU B 245 21.793 24.120 56.990 1.00 33.68 AAAD O ATOM 4351 CB LEU B 245 21.395 27.022 56.259 1.00 18.85 AAAD C ATOM 4352 CG LEU B 245 19.910 26.986 55.891 1.00 15.55 AAAD C ATOM 4353 CD1 LEU B 245 19.113 27.837 56.850 1.00 13.90 AAAD C ATOM 4354 CD2 LEU B 245 19.715 27.472 54.478 1.00 13.08 AAAD C ATOM 4355 N TRP B 246 20.315 24.747 58.567 1.00 26.14 AAAD N ATOM 4356 CA TRP B 246 19.750 23.419 58.721 1.00 20.35 AAAD C ATOM 4357 C TRP B 246 18.347 23.402 58.146 1.00 19.38 AAAD C ATOM 4358 O TRP B 246 17.527 24.263 58.470 1.00 20.78 AAAD O ATOM 4359 CB TRP B 246 19.696 23.038 60.206 1.00 23.02 AAAD C ATOM 4360 CG TRP B 246 18.884 21.800 60.491 1.00 20.72 AAAD C ATOM 4361 CD1 TRP B 246 19.334 20.513 60.502 1.00 18.58 AAAD C ATOM 4362 CD2 TRP B 246 17.480 21.735 60.789 1.00 13.70 AAAD C ATOM 4363 NE1 TRP B 246 18.301 19.654 60.784 1.00 23.36 AAAD N ATOM 4364 CE2 TRP B 246 17.154 20.378 60.966 1.00 15.84 AAAD C ATOM 4365 CE3 TRP B 246 16.470 22.698 60.921 1.00 14.22 AAAD C ATOM 4366 CZ2 TRP B 246 15.860 19.951 61.270 1.00 19.83 AAAD C ATOM 4367 CZ3 TRP B 246 15.175 22.273 61.224 1.00 12.91 AAAD C ATOM 4368 CH2 TRP B 246 14.886 20.913 61.394 1.00 20.56 AAAD C ATOM 4369 N ILE B 247 18.079 22.459 57.255 1.00 18.90 AAAD N ATOM 4370 CA ILE B 247 16.741 22.339 56.697 1.00 21.41 AAAD C ATOM 4371 C ILE B 247 16.311 20.922 57.042 1.00 21.75 AAAD C ATOM 4372 O ILE B 247 17.112 19.996 56.939 1.00 24.05 AAAD O ATOM 4373 CB ILE B 247 16.678 22.547 55.143 1.00 20.62 AAAD C ATOM 4374 CG1 ILE B 247 17.160 23.951 54.744 1.00 19.36 AAAD C ATOM 4375 CG2 ILE B 247 15.231 22.391 54.650 1.00 17.50 AAAD C ATOM 4376 CD1 ILE B 247 18.660 24.091 54.586 1.00 24.57 AAAD C ATOM 4377 N ASN B 248 15.080 20.778 57.528 1.00 22.67 AAAD N ATOM 4378 CA ASN B 248 14.518 19.482 57.897 1.00 25.21 AAAD C ATOM 4379 C ASN B 248 14.787 18.478 56.774 1.00 27.60 AAAD C ATOM 4380 O ASN B 248 14.206 18.579 55.686 1.00 25.53 AAAD O ATOM 4381 CB ASN B 248 13.010 19.612 58.151 1.00 25.68 AAAD C ATOM 4382 CG ASN B 248 12.374 18.310 58.623 1.00 29.69 AAAD C ATOM 4383 OD1 ASN B 248 13.040 17.275 58.725 1.00 29.81 AAAD O ATOM 4384 ND2 ASN B 248 11.073 18.353 58.896 1.00 25.98 AAAD N ATOM 4385 N PRO B 249 15.664 17.487 57.036 1.00 30.10 AAAD N ATOM 4386 CA PRO B 249 16.055 16.437 56.087 1.00 29.54 AAAD C ATOM 4387 C PRO B 249 14.924 15.479 55.743 1.00 27.82 AAAD C ATOM 4388 O PRO B 249 15.068 14.641 54.862 1.00 31.93 AAAD O ATOM 4389 CB PRO B 249 17.175 15.696 56.829 1.00 26.56 AAAD C ATOM 4390 CG PRO B 249 17.629 16.663 57.902 1.00 30.52 AAAD C ATOM 4391 CD PRO B 249 16.338 17.284 58.330 1.00 31.26 AAAD C ATOM 4392 N GLU B 250 13.808 15.594 56.451 1.00 26.97 AAAD N ATOM 4393 CA GLU B 250 12.678 14.720 56.218 1.00 28.27 AAAD C ATOM 4394 C GLU B 250 11.666 15.249 55.232 1.00 26.80 AAAD C ATOM 4395 O GLU B 250 10.794 14.507 54.785 1.00 28.21 AAAD O ATOM 4396 CB GLU B 250 12.002 14.379 57.543 1.00 35.68 AAAD C ATOM 4397 CG GLU B 250 12.879 13.502 58.437 1.00 42.93 AAAD C ATOM 4398 CD GLU B 250 12.483 13.537 59.902 1.00 48.78 AAAD C ATOM 4399 OE1 GLU B 250 11.693 14.421 60.303 1.00 52.81 AAAD O ATOM 4400 OE2 GLU B 250 12.984 12.677 60.659 1.00 52.97 AAAD O ATOM 4401 N VAL B 251 11.751 16.529 54.896 1.00 28.43 AAAD N ATOM 4402 CA VAL B 251 10.800 17.080 53.939 1.00 28.08 AAAD C ATOM 4403 C VAL B 251 11.165 16.610 52.537 1.00 26.49 AAAD C ATOM 4404 O VAL B 251 12.281 16.829 52.063 1.00 24.01 AAAD O ATOM 4405 CB VAL B 251 10.743 18.611 53.982 1.00 28.89 AAAD C ATOM 4406 CG1 VAL B 251 9.628 19.111 53.070 1.00 29.36 AAAD C ATOM 4407 CG2 VAL B 251 10.501 19.078 55.403 1.00 33.73 AAAD C ATOM 4408 N LYS B 252 10.226 15.922 51.904 1.00 24.74 AAAD N ATOM 4409 CA LYS B 252 10.425 15.406 50.565 1.00 30.62 AAAD C ATOM 4410 C LYS B 252 9.590 16.174 49.547 1.00 31.00 AAAD C ATOM 4411 O LYS B 252 9.740 15.967 48.341 1.00 32.34 AAAD O ATOM 4412 CB LYS B 252 10.027 13.928 50.503 1.00 37.82 AAAD C ATOM 4413 CG LYS B 252 10.808 12.984 51.408 1.00 42.47 AAAD C ATOM 4414 CD LYS B 252 10.320 11.553 51.202 1.00 45.79 AAAD C ATOM 4415 CE LYS B 252 11.036 10.555 52.100 1.00 49.00 AAAD C ATOM 4416 NZ LYS B 252 10.529 9.168 51.837 1.00 53.22 AAAD N ATOM 4417 N ASP B 253 8.689 17.029 50.027 1.00 28.16 AAAD N ATOM 4418 CA ASP B 253 7.824 17.802 49.132 1.00 24.74 AAAD C ATOM 4419 C ASP B 253 7.914 19.306 49.360 1.00 24.87 AAAD C ATOM 4420 O ASP B 253 7.756 19.773 50.490 1.00 24.41 AAAD O ATOM 4421 CB ASP B 253 6.371 17.344 49.275 1.00 19.23 AAAD C ATOM 4422 CG ASP B 253 5.441 18.036 48.307 1.00 17.88 AAAD C ATOM 4423 OD1 ASP B 253 5.881 18.384 47.194 1.00 24.73 AAAD O ATOM 4424 OD2 ASP B 253 4.259 18.224 48.657 1.00 23.46 AAAD O ATOM 4425 N PHE B 254 8.099 20.044 48.262 1.00 25.44 AAAD N ATOM 4426 CA PHE B 254 8.222 21.507 48.258 1.00 19.35 AAAD C ATOM 4427 C PHE B 254 7.165 22.199 49.120 1.00 17.18 AAAD C ATOM 4428 O PHE B 254 7.489 23.073 49.927 1.00 19.20 AAAD O ATOM 4429 CB PHE B 254 8.139 22.025 46.811 1.00 20.03 AAAD C ATOM 4430 CG PHE B 254 8.348 23.512 46.673 1.00 14.80 AAAD C ATOM 4431 CD1 PHE B 254 9.624 24.062 46.778 1.00 15.11 AAAD C ATOM 4432 CD2 PHE B 254 7.265 24.368 46.456 1.00 14.39 AAAD C ATOM 4433 CE1 PHE B 254 9.822 25.443 46.678 1.00 12.04 AAAD C ATOM 4434 CE2 PHE B 254 7.452 25.747 46.354 1.00 9.66 AAAD C ATOM 4435 CZ PHE B 254 8.736 26.285 46.466 1.00 9.73 AAAD C ATOM 4436 N TYR B 255 5.913 21.782 48.959 1.00 9.16 AAAD N ATOM 4437 CA TYR B 255 4.783 22.342 49.690 1.00 10.83 AAAD C ATOM 4438 C TYR B 255 4.620 21.874 51.138 1.00 13.49 AAAD C ATOM 4439 O TYR B 255 3.658 22.245 51.804 1.00 16.50 AAAD O ATOM 4440 CB TYR B 255 3.492 22.075 48.917 1.00 8.85 AAAD C ATOM 4441 CG TYR B 255 3.533 22.638 47.518 1.00 19.53 AAAD C ATOM 4442 CD1 TYR B 255 3.199 23.965 47.272 1.00 22.85 AAAD C ATOM 4443 CD2 TYR B 255 3.958 21.860 46.445 1.00 23.42 AAAD C ATOM 4444 CE1 TYR B 255 3.291 24.505 45.990 1.00 27.46 AAAD C ATOM 4445 CE2 TYR B 255 4.054 22.387 45.163 1.00 24.44 AAAD C ATOM 4446 CZ TYR B 255 3.721 23.711 44.942 1.00 28.28 AAAD C ATOM 4447 OH TYR B 255 3.818 24.237 43.676 1.00 27.12 AAAD O ATOM 4448 N ASP B 256 5.531 21.041 51.622 1.00 17.96 AAAD N ATOM 4449 CA ASP B 256 5.446 20.557 53.001 1.00 23.16 AAAD C ATOM 4450 C ASP B 256 6.261 21.417 53.951 1.00 22.84 AAAD C ATOM 4451 O ASP B 256 6.137 21.302 55.171 1.00 27.91 AAAD O ATOM 4452 CB ASP B 256 5.907 19.094 53.110 1.00 22.53 AAAD C ATOM 4453 CG ASP B 256 4.851 18.111 52.652 1.00 19.69 AAAD C ATOM 4454 OD1 ASP B 256 3.641 18.432 52.716 1.00 17.48 AAAD O ATOM 4455 OD2 ASP B 256 5.237 17.004 52.240 1.00 19.27 AAAD O ATOM 4456 N PHE B 257 7.118 22.256 53.383 1.00 20.74 AAAD N ATOM 4457 CA PHE B 257 7.957 23.136 54.175 1.00 18.62 AAAD C ATOM 4458 C PHE B 257 7.142 24.153 54.979 1.00 19.98 AAAD C ATOM 4459 O PHE B 257 6.064 24.587 54.561 1.00 17.33 AAAD O ATOM 4460 CB PHE B 257 8.927 23.882 53.268 1.00 13.71 AAAD C ATOM 4461 CG PHE B 257 10.068 23.053 52.783 1.00 10.12 AAAD C ATOM 4462 CD1 PHE B 257 11.105 22.715 53.642 1.00 11.43 AAAD C ATOM 4463 CD2 PHE B 257 10.150 22.668 51.448 1.00 15.41 AAAD C ATOM 4464 CE1 PHE B 257 12.217 22.012 53.186 1.00 9.10 AAAD C ATOM 4465 CE2 PHE B 257 11.260 21.962 50.972 1.00 12.39 AAAD C ATOM 4466 CZ PHE B 257 12.298 21.634 51.847 1.00 14.73 AAAD C ATOM 4467 N THR B 258 7.652 24.478 56.162 1.00 23.09 AAAD N ATOM 4468 CA THR B 258 7.067 25.463 57.060 1.00 21.29 AAAD C ATOM 4469 C THR B 258 8.304 26.197 57.558 1.00 21.73 AAAD C ATOM 4470 O THR B 258 9.412 25.659 57.486 1.00 20.63 AAAD O ATOM 4471 CB THR B 258 6.346 24.824 58.276 1.00 24.33 AAAD C ATOM 4472 OG1 THR B 258 7.295 24.144 59.110 1.00 28.68 AAAD O ATOM 4473 CG2 THR B 258 5.263 23.862 57.826 1.00 22.91 AAAD C ATOM 4474 N ILE B 259 8.135 27.405 58.079 1.00 22.42 AAAD N ATOM 4475 CA ILE B 259 9.287 28.171 58.553 1.00 18.66 AAAD C ATOM 4476 C ILE B 259 10.105 27.416 59.616 1.00 18.25 AAAD C ATOM 4477 O ILE B 259 11.326 27.542 59.664 1.00 15.97 AAAD O ATOM 4478 CB ILE B 259 8.842 29.564 59.067 1.00 15.22 AAAD C ATOM 4479 CG1 ILE B 259 10.042 30.403 59.513 1.00 16.47 AAAD C ATOM 4480 CG2 ILE B 259 7.821 29.411 60.178 1.00 17.76 AAAD C ATOM 4481 CD1 ILE B 259 10.945 30.858 58.399 1.00 12.39 AAAD C ATOM 4482 N ASP B 260 9.439 26.571 60.403 1.00 21.67 AAAD N ATOM 4483 CA ASP B 260 10.100 25.797 61.465 1.00 22.93 AAAD C ATOM 4484 C ASP B 260 11.157 24.813 60.973 1.00 19.96 AAAD C ATOM 4485 O ASP B 260 12.001 24.357 61.748 1.00 18.42 AAAD O ATOM 4486 CB ASP B 260 9.066 25.036 62.295 1.00 28.50 AAAD C ATOM 4487 CG ASP B 260 8.092 25.960 63.008 1.00 34.61 AAAD C ATOM 4488 OD1 ASP B 260 8.458 26.495 64.075 1.00 39.47 AAAD O ATOM 4489 OD2 ASP B 260 6.964 26.150 62.500 1.00 38.53 AAAD O ATOM 4490 N ASP B 261 11.098 24.481 59.687 1.00 17.58 AAAD N ATOM 4491 CA ASP B 261 12.038 23.547 59.086 1.00 13.17 AAAD C ATOM 4492 C ASP B 261 13.365 24.209 58.798 1.00 15.29 AAAD C ATOM 4493 O ASP B 261 14.310 23.555 58.348 1.00 13.71 AAAD O ATOM 4494 CB ASP B 261 11.451 22.976 57.796 1.00 11.03 AAAD C ATOM 4495 CG ASP B 261 10.205 22.131 58.048 1.00 15.28 AAAD C ATOM 4496 OD1 ASP B 261 10.240 21.281 58.958 1.00 21.88 AAAD O ATOM 4497 OD2 ASP B 261 9.187 22.305 57.346 1.00 11.94 AAAD O ATOM 4498 N PHE B 262 13.444 25.502 59.084 1.00 17.52 AAAD N ATOM 4499 CA PHE B 262 14.645 26.281 58.821 1.00 19.70 AAAD C ATOM 4500 C PHE B 262 15.258 26.799 60.107 1.00 21.75 AAAD C ATOM 4501 O PHE B 262 14.566 27.357 60.966 1.00 21.94 AAAD O ATOM 4502 CB PHE B 262 14.306 27.451 57.889 1.00 15.26 AAAD C ATOM 4503 CG PHE B 262 13.748 27.021 56.568 1.00 9.45 AAAD C ATOM 4504 CD1 PHE B 262 14.588 26.560 55.564 1.00 2.00 AAAD C ATOM 4505 CD2 PHE B 262 12.371 27.056 56.332 1.00 10.31 AAAD C ATOM 4506 CE1 PHE B 262 14.072 26.139 54.341 1.00 7.62 AAAD C ATOM 4507 CE2 PHE B 262 11.842 26.639 55.112 1.00 6.11 AAAD C ATOM 4508 CZ PHE B 262 12.689 26.180 54.116 1.00 7.75 AAAD C ATOM 4509 N LYS B 263 16.569 26.646 60.228 1.00 22.09 AAAD N ATOM 4510 CA LYS B 263 17.243 27.089 61.429 1.00 24.51 AAAD C ATOM 4511 C LYS B 263 18.702 27.388 61.155 1.00 22.37 AAAD C ATOM 4512 O LYS B 263 19.435 26.543 60.646 1.00 25.46 AAAD O ATOM 4513 CB LYS B 263 17.114 26.012 62.510 1.00 32.01 AAAD C ATOM 4514 CG LYS B 263 17.601 26.427 63.878 1.00 47.02 AAAD C ATOM 4515 CD LYS B 263 17.339 25.331 64.894 1.00 55.17 AAAD C ATOM 4516 CE LYS B 263 17.750 25.768 66.295 1.00 60.43 AAAD C ATOM 4517 NZ LYS B 263 17.467 24.695 67.296 1.00 66.32 AAAD N ATOM 4518 N LEU B 264 19.100 28.628 61.400 1.00 23.55 AAAD N ATOM 4519 CA LEU B 264 20.486 29.012 61.207 1.00 25.10 AAAD C ATOM 4520 C LEU B 264 21.214 28.719 62.510 1.00 24.11 AAAD C ATOM 4521 O LEU B 264 20.743 29.073 63.591 1.00 23.36 AAAD O ATOM 4522 CB LEU B 264 20.611 30.495 60.841 1.00 26.53 AAAD C ATOM 4523 CG LEU B 264 20.423 30.872 59.373 1.00 26.63 AAAD C ATOM 4524 CD1 LEU B 264 20.603 32.365 59.220 1.00 32.03 AAAD C ATOM 4525 CD2 LEU B 264 21.435 30.145 58.514 1.00 27.94 AAAD C ATOM 4526 N ILE B 265 22.346 28.041 62.397 1.00 27.10 AAAD N ATOM 4527 CA ILE B 265 23.155 27.671 63.546 1.00 32.49 AAAD C ATOM 4528 C ILE B 265 24.471 28.439 63.554 1.00 34.14 AAAD C ATOM 4529 O ILE B 265 25.165 28.504 62.537 1.00 33.43 AAAD O ATOM 4530 CB ILE B 265 23.451 26.133 63.552 1.00 33.00 AAAD C ATOM 4531 CG1 ILE B 265 22.225 25.349 64.028 1.00 26.91 AAAD C ATOM 4532 CG2 ILE B 265 24.668 25.809 64.422 1.00 34.10 AAAD C ATOM 4533 CD1 ILE B 265 21.162 25.157 62.984 1.00 22.96 AAAD C ATOM 4534 N ASN B 266 24.795 29.022 64.708 1.00 37.53 AAAD N ATOM 4535 CA ASN B 266 26.030 29.782 64.905 1.00 39.47 AAAD C ATOM 4536 C ASN B 266 26.118 31.012 64.009 1.00 38.80 AAAD C ATOM 4537 O ASN B 266 27.135 31.244 63.343 1.00 41.93 AAAD O ATOM 4538 CB ASN B 266 27.254 28.875 64.692 1.00 44.15 AAAD C ATOM 4539 CG ASN B 266 28.477 29.335 65.482 1.00 51.10 AAAD C ATOM 4540 OD1 ASN B 266 28.496 30.429 66.048 1.00 53.17 AAAD O ATOM 4541 ND2 ASN B 266 29.488 28.475 65.554 1.00 53.32 AAAD N ATOM 4542 N TYR B 267 25.038 31.786 63.971 1.00 34.46 AAAD N ATOM 4543 CA TYR B 267 25.016 32.998 63.167 1.00 29.01 AAAD C ATOM 4544 C TYR B 267 25.535 34.183 63.992 1.00 29.25 AAAD C ATOM 4545 O TYR B 267 24.790 34.784 64.772 1.00 30.68 AAAD O ATOM 4546 CB TYR B 267 23.605 33.271 62.636 1.00 22.88 AAAD C ATOM 4547 CG TYR B 267 23.499 34.516 61.775 1.00 23.55 AAAD C ATOM 4548 CD1 TYR B 267 24.613 35.030 61.097 1.00 20.50 AAAD C ATOM 4549 CD2 TYR B 267 22.292 35.201 61.667 1.00 22.54 AAAD C ATOM 4550 CE1 TYR B 267 24.520 36.192 60.348 1.00 16.01 AAAD C ATOM 4551 CE2 TYR B 267 22.189 36.360 60.925 1.00 18.42 AAAD C ATOM 4552 CZ TYR B 267 23.302 36.850 60.268 1.00 16.23 AAAD C ATOM 4553 OH TYR B 267 23.183 37.996 59.526 1.00 20.38 AAAD O ATOM 4554 N LYS B 268 26.829 34.473 63.843 1.00 29.27 AAAD N ATOM 4555 CA LYS B 268 27.494 35.579 64.528 1.00 28.64 AAAD C ATOM 4556 C LYS B 268 27.632 36.761 63.575 1.00 29.99 AAAD C ATOM 4557 O LYS B 268 28.084 36.605 62.443 1.00 29.89 AAAD O ATOM 4558 CB LYS B 268 28.871 35.157 65.021 1.00 32.53 AAAD C ATOM 4559 CG LYS B 268 28.829 34.151 66.139 1.00 37.33 AAAD C ATOM 4560 CD LYS B 268 30.221 33.804 66.596 1.00 39.83 AAAD C ATOM 4561 CE LYS B 268 30.157 32.805 67.724 1.00 48.95 AAAD C ATOM 4562 NZ LYS B 268 31.491 32.538 68.307 1.00 53.39 AAAD N ATOM 4563 N HIS B 269 27.315 37.956 64.062 1.00 30.37 AAAD N ATOM 4564 CA HIS B 269 27.357 39.149 63.225 1.00 29.38 AAAD C ATOM 4565 C HIS B 269 27.669 40.440 63.981 1.00 28.21 AAAD C ATOM 4566 O HIS B 269 27.535 40.502 65.207 1.00 26.94 AAAD O ATOM 4567 CB HIS B 269 26.018 39.291 62.497 1.00 29.02 AAAD C ATOM 4568 CG HIS B 269 24.832 39.282 63.410 1.00 25.90 AAAD C ATOM 4569 ND1 HIS B 269 24.642 40.225 64.398 1.00 30.08 AAAD N ATOM 4570 CD2 HIS B 269 23.771 38.445 63.484 1.00 26.65 AAAD C ATOM 4571 CE1 HIS B 269 23.517 39.971 65.040 1.00 26.41 AAAD C ATOM 4572 NE2 HIS B 269 22.969 38.896 64.504 1.00 28.17 AAAD N ATOM 4573 N GLY B 270 28.017 41.478 63.222 1.00 27.91 AAAD N ATOM 4574 CA GLY B 270 28.346 42.777 63.782 1.00 27.41 AAAD C ATOM 4575 C GLY B 270 27.166 43.502 64.395 1.00 28.45 AAAD C ATOM 4576 O GLY B 270 26.025 43.031 64.317 1.00 26.28 AAAD O ATOM 4577 N ASP B 271 27.447 44.657 64.995 1.00 34.80 AAAD N ATOM 4578 CA ASP B 271 26.434 45.480 65.659 1.00 42.69 AAAD C ATOM 4579 C ASP B 271 25.463 46.181 64.707 1.00 42.14 AAAD C ATOM 4580 O ASP B 271 25.684 46.240 63.501 1.00 42.90 AAAD O ATOM 4581 CB ASP B 271 27.105 46.514 66.570 1.00 50.81 AAAD C ATOM 4582 CG ASP B 271 27.855 45.879 67.731 1.00 58.69 AAAD C ATOM 4583 OD1 ASP B 271 27.287 44.989 68.403 1.00 63.95 AAAD O ATOM 4584 OD2 ASP B 271 29.012 46.286 67.979 1.00 64.67 AAAD O ATOM 4585 N LYS B 272 24.407 46.757 65.265 1.00 38.01 AAAD N ATOM 4586 CA LYS B 272 23.398 47.431 64.459 1.00 38.31 AAAD C ATOM 4587 C LYS B 272 23.893 48.694 63.748 1.00 37.40 AAAD C ATOM 4588 O LYS B 272 24.498 49.572 64.370 1.00 37.26 AAAD O ATOM 4589 CB LYS B 272 22.186 47.767 65.330 1.00 39.01 AAAD C ATOM 4590 CG LYS B 272 20.929 48.118 64.555 1.00 41.71 AAAD C ATOM 4591 CD LYS B 272 19.748 48.286 65.493 1.00 43.83 AAAD C ATOM 4592 CE LYS B 272 18.468 48.577 64.718 1.00 54.34 AAAD C ATOM 4593 NZ LYS B 272 17.325 48.984 65.600 1.00 57.15 AAAD N ATOM 4594 N LEU B 273 23.646 48.753 62.439 1.00 34.90 AAAD N ATOM 4595 CA LEU B 273 23.996 49.898 61.594 1.00 29.23 AAAD C ATOM 4596 C LEU B 273 22.657 50.416 61.083 1.00 30.44 AAAD C ATOM 4597 O LEU B 273 21.861 49.631 60.569 1.00 35.29 AAAD O ATOM 4598 CB LEU B 273 24.829 49.456 60.393 1.00 27.06 AAAD C ATOM 4599 CG LEU B 273 26.321 49.165 60.524 1.00 26.71 AAAD C ATOM 4600 CD1 LEU B 273 26.848 48.696 59.188 1.00 28.85 AAAD C ATOM 4601 CD2 LEU B 273 27.060 50.412 60.961 1.00 29.96 AAAD C ATOM 4602 N LEU B 274 22.387 51.711 61.229 1.00 28.90 AAAD N ATOM 4603 CA LEU B 274 21.109 52.266 60.770 1.00 28.40 AAAD C ATOM 4604 C LEU B 274 21.183 52.804 59.340 1.00 25.43 AAAD C ATOM 4605 O LEU B 274 22.219 53.312 58.915 1.00 24.74 AAAD O ATOM 4606 CB LEU B 274 20.625 53.360 61.726 1.00 27.85 AAAD C ATOM 4607 CG LEU B 274 20.447 52.942 63.190 1.00 29.12 AAAD C ATOM 4608 CD1 LEU B 274 20.211 54.166 64.044 1.00 30.44 AAAD C ATOM 4609 CD2 LEU B 274 19.294 51.964 63.340 1.00 28.08 AAAD C ATOM 4610 N PHE B 275 20.093 52.653 58.591 1.00 24.81 AAAD N ATOM 4611 CA PHE B 275 20.024 53.123 57.205 1.00 23.20 AAAD C ATOM 4612 C PHE B 275 18.668 53.737 56.931 1.00 22.86 AAAD C ATOM 4613 O PHE B 275 17.652 53.055 57.020 1.00 26.43 AAAD O ATOM 4614 CB PHE B 275 20.237 51.970 56.215 1.00 16.63 AAAD C ATOM 4615 CG PHE B 275 21.616 51.411 56.229 1.00 12.58 AAAD C ATOM 4616 CD1 PHE B 275 22.638 52.044 55.537 1.00 11.93 AAAD C ATOM 4617 CD2 PHE B 275 21.900 50.251 56.932 1.00 10.96 AAAD C ATOM 4618 CE1 PHE B 275 23.928 51.532 55.540 1.00 10.60 AAAD C ATOM 4619 CE2 PHE B 275 23.193 49.725 56.945 1.00 15.96 AAAD C ATOM 4620 CZ PHE B 275 24.208 50.370 56.244 1.00 10.62 AAAD C ATOM 4621 N GLU B 276 18.666 55.013 56.563 1.00 22.88 AAAD N ATOM 4622 CA GLU B 276 17.434 55.728 56.257 1.00 24.32 AAAD C ATOM 4623 C GLU B 276 16.670 55.065 55.125 1.00 25.92 AAAD C ATOM 4624 O GLU B 276 17.258 54.656 54.112 1.00 20.07 AAAD O ATOM 4625 CB GLU B 276 17.731 57.172 55.857 1.00 29.08 AAAD C ATOM 4626 CG GLU B 276 17.396 58.201 56.910 1.00 32.42 AAAD C ATOM 4627 CD GLU B 276 17.459 59.608 56.361 1.00 34.69 AAAD C ATOM 4628 OE1 GLU B 276 16.467 60.030 55.730 1.00 32.11 AAAD O ATOM 4629 OE2 GLU B 276 18.497 60.282 56.548 1.00 37.19 AAAD O ATOM 4630 N VAL B 277 15.353 55.019 55.278 1.00 29.80 AAAD N ATOM 4631 CA VAL B 277 14.490 54.411 54.279 1.00 36.42 AAAD C ATOM 4632 C VAL B 277 14.092 55.379 53.174 1.00 38.55 AAAD C ATOM 4633 O VAL B 277 13.690 56.510 53.445 1.00 37.46 AAAD O ATOM 4634 CB VAL B 277 13.216 53.828 54.924 1.00 36.20 AAAD C ATOM 4635 CG1 VAL B 277 12.349 53.146 53.873 1.00 34.59 AAAD C ATOM 4636 CG2 VAL B 277 13.595 52.837 56.001 1.00 40.10 AAAD C ATOM 4637 N ALA B 278 14.245 54.927 51.929 1.00 43.41 AAAD N ATOM 4638 CA ALA B 278 13.881 55.706 50.747 1.00 45.70 AAAD C ATOM 4639 C ALA B 278 12.470 55.267 50.362 1.00 47.70 AAAD C ATOM 4640 O ALA B 278 12.121 54.094 50.520 1.00 48.32 AAAD O ATOM 4641 CB ALA B 278 14.853 55.430 49.612 1.00 46.99 AAAD C ATOM 4642 N VAL B 279 11.671 56.190 49.844 1.00 50.89 AAAD N ATOM 4643 CA VAL B 279 10.292 55.881 49.475 1.00 54.65 AAAD C ATOM 4644 C VAL B 279 10.024 56.304 48.040 1.00 56.31 AAAD C ATOM 4645 O VAL B 279 10.566 57.350 47.633 1.00 59.57 AAAD O ATOM 4646 CB VAL B 279 9.281 56.557 50.463 1.00 54.91 AAAD C ATOM 4647 CG1 VAL B 279 9.955 57.677 51.227 1.00 55.76 AAAD C ATOM 4648 CG2 VAL B 279 8.051 57.095 49.729 1.00 56.10 AAAD C ATOM 4649 OXT VAL B 279 9.300 55.574 47.333 1.00 58.97 AAAD O TER 4650 VAL B 279 END