Browse entries in the PDBbind-CN Database
HEADER HYDROLASE 22-AUG-16 5LRW TITLE STRUCTURE OF CEZANNE/OTUD7B OTU DOMAIN BOUND TO UBIQUITIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: OTU DOMAIN-CONTAINING PROTEIN 7B; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: CELLULAR ZINC FINGER ANTI-NF-KAPPA-B PROTEIN,ZINC FINGER A20 COMPND 5 DOMAIN-CONTAINING PROTEIN 1,ZINC FINGER PROTEIN CEZANNE; COMPND 6 EC: 3.4.19.12; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: POLYUBIQUITIN-B; COMPND 11 CHAIN: B, D; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES; COMPND 14 OTHER_DETAILS: GLY76 WAS REPLACED WITH 2-BROMOETHYLAMINE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: OTUD7B, ZA20D1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: UBB; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HYDROLASE, PROTEASE, DEUBIQUITINASE, OTU DOMAIN EXPDTA X-RAY DIFFRACTION AUTHOR T.E.T.MEVISSEN,Y.KULATHU,M.P.C.MULDER,P.P.GEURINK,S.L.MASLEN, AUTHOR 2 M.GERSCH,P.R.ELLIOTT,J.E.BURKE,B.D.M.VAN TOL,M.AKUTSU,F.EL OUALID, AUTHOR 3 M.KAWASAKI,S.M.V.FREUND,H.OVAA,D.KOMANDER REVDAT 3 13-SEP-17 5LRW 1 ATOM REVDAT 2 26-OCT-16 5LRW 1 JRNL REVDAT 1 19-OCT-16 5LRW 0 JRNL AUTH T.E.MEVISSEN,Y.KULATHU,M.P.MULDER,P.P.GEURINK,S.L.MASLEN, JRNL AUTH 2 M.GERSCH,P.R.ELLIOTT,J.E.BURKE,B.D.VAN TOL,M.AKUTSU, JRNL AUTH 3 F.EL OUALID,M.KAWASAKI,S.M.FREUND,H.OVAA,D.KOMANDER JRNL TITL MOLECULAR BASIS OF LYS11-POLYUBIQUITIN SPECIFICITY IN THE JRNL TITL 2 DEUBIQUITINASE CEZANNE. JRNL REF NATURE V. 538 402 2016 JRNL REFN ESSN 1476-4687 JRNL PMID 27732584 JRNL DOI 10.1038/NATURE19836 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.48 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 47215 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.178 REMARK 3 R VALUE (WORKING SET) : 0.176 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 2389 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 45.4954 - 5.1405 1.00 2623 144 0.1578 0.1779 REMARK 3 2 5.1405 - 4.0810 1.00 2650 133 0.1357 0.1708 REMARK 3 3 4.0810 - 3.5654 1.00 2652 126 0.1464 0.1983 REMARK 3 4 3.5654 - 3.2395 1.00 2631 148 0.1579 0.1874 REMARK 3 5 3.2395 - 3.0073 1.00 2655 141 0.1691 0.2036 REMARK 3 6 3.0073 - 2.8301 1.00 2621 144 0.1749 0.2196 REMARK 3 7 2.8301 - 2.6883 1.00 2645 142 0.1818 0.2538 REMARK 3 8 2.6883 - 2.5713 1.00 2640 139 0.1793 0.2298 REMARK 3 9 2.5713 - 2.4723 1.00 2629 157 0.1884 0.2581 REMARK 3 10 2.4723 - 2.3870 1.00 2621 162 0.2002 0.2414 REMARK 3 11 2.3870 - 2.3124 1.00 2628 141 0.2011 0.2646 REMARK 3 12 2.3124 - 2.2463 1.00 2645 138 0.2099 0.2426 REMARK 3 13 2.2463 - 2.1872 1.00 2623 140 0.2193 0.2382 REMARK 3 14 2.1872 - 2.1338 1.00 2642 148 0.2221 0.2366 REMARK 3 15 2.1338 - 2.0853 1.00 2639 121 0.2241 0.2881 REMARK 3 16 2.0853 - 2.0409 1.00 2669 126 0.2407 0.2929 REMARK 3 17 2.0409 - 2.0001 1.00 2613 139 0.2549 0.2815 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.580 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 5755 REMARK 3 ANGLE : 0.623 7837 REMARK 3 CHIRALITY : 0.025 886 REMARK 3 PLANARITY : 0.003 1002 REMARK 3 DIHEDRAL : 13.056 2099 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' REMARK 3 ORIGIN FOR THE GROUP (A): 65.6394 24.2626 -12.0961 REMARK 3 T TENSOR REMARK 3 T11: 0.1088 T22: 0.0683 REMARK 3 T33: 0.0910 T12: -0.0236 REMARK 3 T13: 0.0075 T23: 0.0021 REMARK 3 L TENSOR REMARK 3 L11: 1.0840 L22: 0.6466 REMARK 3 L33: 0.9860 L12: 0.0581 REMARK 3 L13: 0.3790 L23: 0.0795 REMARK 3 S TENSOR REMARK 3 S11: 0.0219 S12: 0.0123 S13: -0.0698 REMARK 3 S21: -0.0064 S22: -0.0018 S23: 0.0102 REMARK 3 S31: 0.0876 S32: -0.0452 S33: -0.0027 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' REMARK 3 ORIGIN FOR THE GROUP (A): 49.0641 0.0976 -15.5755 REMARK 3 T TENSOR REMARK 3 T11: 0.2340 T22: 0.1845 REMARK 3 T33: 0.4993 T12: -0.1711 REMARK 3 T13: 0.0000 T23: -0.0886 REMARK 3 L TENSOR REMARK 3 L11: 0.3841 L22: 0.9774 REMARK 3 L33: 0.7022 L12: -0.0438 REMARK 3 L13: 0.2623 L23: 0.1175 REMARK 3 S TENSOR REMARK 3 S11: -0.0595 S12: 0.1637 S13: -0.8193 REMARK 3 S21: 0.2104 S22: 0.1581 S23: -0.0349 REMARK 3 S31: 0.3104 S32: -0.3460 S33: -0.0236 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'C' REMARK 3 ORIGIN FOR THE GROUP (A): 12.8496 21.1079 0.7520 REMARK 3 T TENSOR REMARK 3 T11: 0.1153 T22: 0.1321 REMARK 3 T33: 0.1025 T12: -0.0079 REMARK 3 T13: -0.0023 T23: -0.0058 REMARK 3 L TENSOR REMARK 3 L11: 1.0720 L22: 0.7607 REMARK 3 L33: 1.8946 L12: 0.1091 REMARK 3 L13: -0.1479 L23: -0.1159 REMARK 3 S TENSOR REMARK 3 S11: 0.0442 S12: -0.0039 S13: 0.0706 REMARK 3 S21: 0.0027 S22: -0.0177 S23: -0.0392 REMARK 3 S31: -0.2225 S32: 0.2111 S33: -0.0091 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'D' REMARK 3 ORIGIN FOR THE GROUP (A): 29.2908 44.4789 -4.3121 REMARK 3 T TENSOR REMARK 3 T11: 0.8542 T22: 0.4945 REMARK 3 T33: 0.6130 T12: -0.3004 REMARK 3 T13: 0.0009 T23: 0.0954 REMARK 3 L TENSOR REMARK 3 L11: 1.5840 L22: 1.5350 REMARK 3 L33: 1.2550 L12: 0.4382 REMARK 3 L13: -0.9977 L23: -0.5260 REMARK 3 S TENSOR REMARK 3 S11: 0.1092 S12: 0.4354 S13: 0.7897 REMARK 3 S21: 0.2965 S22: -0.0955 S23: -0.4676 REMARK 3 S31: -1.4586 S32: 0.3026 S33: -0.0261 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5LRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-16. REMARK 100 THE DEPOSITION ID IS D_1200001257. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-JUL-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I02 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47250 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 66.130 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 4.200 REMARK 200 R MERGE (I) : 0.12500 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : 0.85400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE (PH 4.8), 6% REMARK 280 (W/V) PEG 6K, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 78.78000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.48365 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.20000 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 78.78000 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 45.48365 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 25.20000 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 78.78000 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 45.48365 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 25.20000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.96731 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 50.40000 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 90.96731 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 50.40000 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 90.96731 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 50.40000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 TRP A 401 REMARK 465 GLY A 402 REMARK 465 LYS A 403 REMARK 465 ASP A 404 REMARK 465 ASP A 405 REMARK 465 SER A 406 REMARK 465 ASP A 407 REMARK 465 ASN A 408 REMARK 465 VAL A 409 REMARK 465 ARG A 410 REMARK 465 SER A 438 REMARK 465 LYS A 439 REMARK 465 HIS A 440 REMARK 465 HIS A 441 REMARK 465 HIS A 442 REMARK 465 HIS A 443 REMARK 465 HIS A 444 REMARK 465 HIS A 445 REMARK 465 TRP C 401 REMARK 465 GLY C 402 REMARK 465 LYS C 403 REMARK 465 ASP C 404 REMARK 465 ASP C 405 REMARK 465 SER C 406 REMARK 465 ASP C 407 REMARK 465 ASN C 408 REMARK 465 VAL C 409 REMARK 465 ARG C 410 REMARK 465 LEU C 411 REMARK 465 LYS C 439 REMARK 465 HIS C 440 REMARK 465 HIS C 441 REMARK 465 HIS C 442 REMARK 465 HIS C 443 REMARK 465 HIS C 444 REMARK 465 HIS C 445 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 145 CG CD OE1 OE2 REMARK 470 ASP A 191 CG OD1 OD2 REMARK 470 GLN A 241 CG CD OE1 NE2 REMARK 470 GLN A 255 CG CD OE1 NE2 REMARK 470 SER A 321 OG REMARK 470 GLU A 324 CG CD OE1 OE2 REMARK 470 LEU A 411 CG CD1 CD2 REMARK 470 SER A 437 OG REMARK 470 GLN B 2 CG CD OE1 NE2 REMARK 470 LYS B 48 CG CD CE NZ REMARK 470 LYS B 63 CG CD CE NZ REMARK 470 GLU B 64 CG CD OE1 OE2 REMARK 470 GLU C 222 CG CD OE1 OE2 REMARK 470 LYS C 243 CG CD CE NZ REMARK 470 GLU C 244 CG CD OE1 OE2 REMARK 470 SER C 245 OG REMARK 470 GLU C 251 CG CD OE1 OE2 REMARK 470 LYS C 256 CG CD CE NZ REMARK 470 GLU C 260 CG CD OE1 OE2 REMARK 470 GLN C 289 CG CD OE1 NE2 REMARK 470 ASP C 320 CG OD1 OD2 REMARK 470 SER C 321 OG REMARK 470 GLU C 324 CG CD OE1 OE2 REMARK 470 GLU C 400 CG CD OE1 OE2 REMARK 470 SER C 413 OG REMARK 470 SER C 417 OG REMARK 470 LYS C 432 NZ REMARK 470 SER C 438 OG REMARK 470 MET D 1 CG SD CE REMARK 470 PHE D 4 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS D 6 CE NZ REMARK 470 LYS D 11 CG CD CE NZ REMARK 470 THR D 14 OG1 CG2 REMARK 470 GLU D 16 CG CD OE1 OE2 REMARK 470 VAL D 17 CG1 CG2 REMARK 470 GLU D 18 CG CD OE1 OE2 REMARK 470 SER D 20 OG REMARK 470 GLU D 24 CG CD OE1 OE2 REMARK 470 LYS D 29 CG CD CE NZ REMARK 470 ASP D 32 CG OD1 OD2 REMARK 470 LYS D 33 CG CD CE NZ REMARK 470 GLU D 34 CG CD OE1 OE2 REMARK 470 PHE D 45 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU D 51 CG CD OE1 OE2 REMARK 470 ARG D 54 CZ NH1 NH2 REMARK 470 GLN D 62 CG CD OE1 NE2 REMARK 470 LYS D 63 CG CD CE NZ REMARK 470 GLU D 64 CG CD OE1 OE2 REMARK 470 THR D 66 OG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE2 GLU C 257 O HOH C 601 2.08 REMARK 500 OE2 GLU A 373 O HOH A 601 2.12 REMARK 500 O HOH C 672 O HOH C 765 2.14 REMARK 500 OD1 ASP C 191 O HOH C 602 2.17 REMARK 500 O HOH C 776 O HOH C 845 2.17 REMARK 500 OH TYR A 218 OD2 ASP C 252 2.18 REMARK 500 O LEU A 137 O HOH A 601 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP C 208 42.01 -101.00 REMARK 500 GLU D 64 -1.86 69.96 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 910 DISTANCE = 6.00 ANGSTROMS REMARK 525 HOH A 911 DISTANCE = 6.42 ANGSTROMS REMARK 525 HOH A 912 DISTANCE = 6.44 ANGSTROMS REMARK 525 HOH A 913 DISTANCE = 7.87 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide CYS C 194 and NEH D REMARK 800 76 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY D 75 and NEH D REMARK 800 76 DBREF 5LRW A 128 438 UNP Q6GQQ9 OTU7B_HUMAN 128 438 DBREF 5LRW B 1 75 UNP P0CG47 UBB_HUMAN 1 75 DBREF 5LRW C 128 438 UNP Q6GQQ9 OTU7B_HUMAN 128 438 DBREF 5LRW D 1 75 UNP P0CG47 UBB_HUMAN 1 75 SEQADV 5LRW MET A 128 UNP Q6GQQ9 LEU 128 CLONING ARTIFACT SEQADV 5LRW A UNP Q6GQQ9 SER 267 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLU 268 DELETION SEQADV 5LRW A UNP Q6GQQ9 PRO 269 DELETION SEQADV 5LRW A UNP Q6GQQ9 ARG 270 DELETION SEQADV 5LRW A UNP Q6GQQ9 MET 271 DELETION SEQADV 5LRW A UNP Q6GQQ9 HIS 272 DELETION SEQADV 5LRW A UNP Q6GQQ9 LEU 273 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLY 274 DELETION SEQADV 5LRW A UNP Q6GQQ9 THR 275 DELETION SEQADV 5LRW A UNP Q6GQQ9 ASN 276 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLY 277 DELETION SEQADV 5LRW A UNP Q6GQQ9 ALA 278 DELETION SEQADV 5LRW A UNP Q6GQQ9 ASN 279 DELETION SEQADV 5LRW A UNP Q6GQQ9 CYS 280 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLY 281 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLY 282 DELETION SEQADV 5LRW A UNP Q6GQQ9 VAL 283 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLU 284 DELETION SEQADV 5LRW A UNP Q6GQQ9 SER 285 DELETION SEQADV 5LRW A UNP Q6GQQ9 SER 286 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLU 287 DELETION SEQADV 5LRW A UNP Q6GQQ9 GLU 288 DELETION SEQADV 5LRW GLN A 289 UNP Q6GQQ9 PRO 289 LINKER SEQADV 5LRW PRO A 290 UNP Q6GQQ9 VAL 290 LINKER SEQADV 5LRW GLY A 291 UNP Q6GQQ9 TYR 291 LINKER SEQADV 5LRW LYS A 439 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS A 440 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS A 441 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS A 442 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS A 443 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS A 444 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS A 445 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW NEH B 76 UNP P0CG47 LINKER SEQADV 5LRW MET C 128 UNP Q6GQQ9 LEU 128 CLONING ARTIFACT SEQADV 5LRW C UNP Q6GQQ9 SER 267 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLU 268 DELETION SEQADV 5LRW C UNP Q6GQQ9 PRO 269 DELETION SEQADV 5LRW C UNP Q6GQQ9 ARG 270 DELETION SEQADV 5LRW C UNP Q6GQQ9 MET 271 DELETION SEQADV 5LRW C UNP Q6GQQ9 HIS 272 DELETION SEQADV 5LRW C UNP Q6GQQ9 LEU 273 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLY 274 DELETION SEQADV 5LRW C UNP Q6GQQ9 THR 275 DELETION SEQADV 5LRW C UNP Q6GQQ9 ASN 276 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLY 277 DELETION SEQADV 5LRW C UNP Q6GQQ9 ALA 278 DELETION SEQADV 5LRW C UNP Q6GQQ9 ASN 279 DELETION SEQADV 5LRW C UNP Q6GQQ9 CYS 280 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLY 281 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLY 282 DELETION SEQADV 5LRW C UNP Q6GQQ9 VAL 283 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLU 284 DELETION SEQADV 5LRW C UNP Q6GQQ9 SER 285 DELETION SEQADV 5LRW C UNP Q6GQQ9 SER 286 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLU 287 DELETION SEQADV 5LRW C UNP Q6GQQ9 GLU 288 DELETION SEQADV 5LRW GLN C 289 UNP Q6GQQ9 PRO 289 LINKER SEQADV 5LRW PRO C 290 UNP Q6GQQ9 VAL 290 LINKER SEQADV 5LRW GLY C 291 UNP Q6GQQ9 TYR 291 LINKER SEQADV 5LRW LYS C 439 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS C 440 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS C 441 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS C 442 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS C 443 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS C 444 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW HIS C 445 UNP Q6GQQ9 EXPRESSION TAG SEQADV 5LRW NEH D 76 UNP P0CG47 LINKER SEQRES 1 A 296 MET GLU MET PRO ILE CYS ALA PHE GLN LEU PRO ASP LEU SEQRES 2 A 296 THR VAL TYR ASN GLU ASP PHE ARG SER PHE ILE GLU ARG SEQRES 3 A 296 ASP LEU ILE GLU GLN SER MET LEU VAL ALA LEU GLU GLN SEQRES 4 A 296 ALA GLY ARG LEU ASN TRP TRP VAL SER VAL ASP PRO THR SEQRES 5 A 296 SER GLN ARG LEU LEU PRO LEU ALA THR THR GLY ASP GLY SEQRES 6 A 296 ASN CYS LEU LEU HIS ALA ALA SER LEU GLY MET TRP GLY SEQRES 7 A 296 PHE HIS ASP ARG ASP LEU MET LEU ARG LYS ALA LEU TYR SEQRES 8 A 296 ALA LEU MET GLU LYS GLY VAL GLU LYS GLU ALA LEU LYS SEQRES 9 A 296 ARG ARG TRP ARG TRP GLN GLN THR GLN GLN ASN LYS GLU SEQRES 10 A 296 SER GLY LEU VAL TYR THR GLU ASP GLU TRP GLN LYS GLU SEQRES 11 A 296 TRP ASN GLU LEU ILE LYS LEU ALA SER GLN PRO GLY GLU SEQRES 12 A 296 SER LEU GLU GLU PHE HIS VAL PHE VAL LEU ALA HIS VAL SEQRES 13 A 296 LEU ARG ARG PRO ILE VAL VAL VAL ALA ASP THR MET LEU SEQRES 14 A 296 ARG ASP SER GLY GLY GLU ALA PHE ALA PRO ILE PRO PHE SEQRES 15 A 296 GLY GLY ILE TYR LEU PRO LEU GLU VAL PRO ALA SER GLN SEQRES 16 A 296 CYS HIS ARG SER PRO LEU VAL LEU ALA TYR ASP GLN ALA SEQRES 17 A 296 HIS PHE SER ALA LEU VAL SER MET GLU GLN LYS GLU ASN SEQRES 18 A 296 THR LYS GLU GLN ALA VAL ILE PRO LEU THR ASP SER GLU SEQRES 19 A 296 TYR LYS LEU LEU PRO LEU HIS PHE ALA VAL ASP PRO GLY SEQRES 20 A 296 LYS GLY TRP GLU TRP GLY LYS ASP ASP SER ASP ASN VAL SEQRES 21 A 296 ARG LEU ALA SER VAL ILE LEU SER LEU GLU VAL LYS LEU SEQRES 22 A 296 HIS LEU LEU HIS SER TYR MET ASN VAL LYS TRP ILE PRO SEQRES 23 A 296 LEU SER SER LYS HIS HIS HIS HIS HIS HIS SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 B 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 B 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 B 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY NEH SEQRES 1 C 296 MET GLU MET PRO ILE CYS ALA PHE GLN LEU PRO ASP LEU SEQRES 2 C 296 THR VAL TYR ASN GLU ASP PHE ARG SER PHE ILE GLU ARG SEQRES 3 C 296 ASP LEU ILE GLU GLN SER MET LEU VAL ALA LEU GLU GLN SEQRES 4 C 296 ALA GLY ARG LEU ASN TRP TRP VAL SER VAL ASP PRO THR SEQRES 5 C 296 SER GLN ARG LEU LEU PRO LEU ALA THR THR GLY ASP GLY SEQRES 6 C 296 ASN CYS LEU LEU HIS ALA ALA SER LEU GLY MET TRP GLY SEQRES 7 C 296 PHE HIS ASP ARG ASP LEU MET LEU ARG LYS ALA LEU TYR SEQRES 8 C 296 ALA LEU MET GLU LYS GLY VAL GLU LYS GLU ALA LEU LYS SEQRES 9 C 296 ARG ARG TRP ARG TRP GLN GLN THR GLN GLN ASN LYS GLU SEQRES 10 C 296 SER GLY LEU VAL TYR THR GLU ASP GLU TRP GLN LYS GLU SEQRES 11 C 296 TRP ASN GLU LEU ILE LYS LEU ALA SER GLN PRO GLY GLU SEQRES 12 C 296 SER LEU GLU GLU PHE HIS VAL PHE VAL LEU ALA HIS VAL SEQRES 13 C 296 LEU ARG ARG PRO ILE VAL VAL VAL ALA ASP THR MET LEU SEQRES 14 C 296 ARG ASP SER GLY GLY GLU ALA PHE ALA PRO ILE PRO PHE SEQRES 15 C 296 GLY GLY ILE TYR LEU PRO LEU GLU VAL PRO ALA SER GLN SEQRES 16 C 296 CYS HIS ARG SER PRO LEU VAL LEU ALA TYR ASP GLN ALA SEQRES 17 C 296 HIS PHE SER ALA LEU VAL SER MET GLU GLN LYS GLU ASN SEQRES 18 C 296 THR LYS GLU GLN ALA VAL ILE PRO LEU THR ASP SER GLU SEQRES 19 C 296 TYR LYS LEU LEU PRO LEU HIS PHE ALA VAL ASP PRO GLY SEQRES 20 C 296 LYS GLY TRP GLU TRP GLY LYS ASP ASP SER ASP ASN VAL SEQRES 21 C 296 ARG LEU ALA SER VAL ILE LEU SER LEU GLU VAL LYS LEU SEQRES 22 C 296 HIS LEU LEU HIS SER TYR MET ASN VAL LYS TRP ILE PRO SEQRES 23 C 296 LEU SER SER LYS HIS HIS HIS HIS HIS HIS SEQRES 1 D 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 D 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 D 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 D 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 D 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 D 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY NEH HET NEH B 76 3 HET NEH D 76 3 HET GOL A 501 6 HET GOL C 501 6 HETNAM NEH ETHANAMINE HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 NEH 2(C2 H7 N) FORMUL 5 GOL 2(C3 H8 O3) FORMUL 7 HOH *621(H2 O) HELIX 1 AA1 TYR A 143 ARG A 153 1 11 HELIX 2 AA2 GLU A 157 ALA A 167 1 11 HELIX 3 AA3 TRP A 172 ASP A 177 1 6 HELIX 4 AA4 ASN A 193 SER A 200 1 8 HELIX 5 AA5 LEU A 201 TRP A 204 5 4 HELIX 6 AA6 ASP A 208 LYS A 223 1 16 HELIX 7 AA7 GLU A 226 GLU A 244 1 19 HELIX 8 AA8 THR A 250 GLN A 289 1 18 HELIX 9 AA9 GLU A 295 ARG A 307 1 13 HELIX 10 AB1 PRO A 341 CYS A 345 5 5 HELIX 11 AB2 MET A 365 GLU A 369 1 5 HELIX 12 AB3 ASP A 394 GLY A 398 5 5 HELIX 13 AB4 ALA A 412 MET A 429 1 18 HELIX 14 AB5 THR B 22 GLY B 35 1 14 HELIX 15 AB6 PRO B 37 ASP B 39 5 3 HELIX 16 AB7 LEU B 56 ASN B 60 5 5 HELIX 17 AB8 TYR C 143 ARG C 153 1 11 HELIX 18 AB9 GLU C 157 ALA C 167 1 11 HELIX 19 AC1 TRP C 172 ASP C 177 1 6 HELIX 20 AC2 ASN C 193 SER C 200 1 8 HELIX 21 AC3 LEU C 201 TRP C 204 5 4 HELIX 22 AC4 ASP C 208 LYS C 223 1 16 HELIX 23 AC5 GLU C 226 SER C 245 1 20 HELIX 24 AC6 THR C 250 GLN C 289 1 18 HELIX 25 AC7 GLU C 295 ARG C 307 1 13 HELIX 26 AC8 PRO C 341 CYS C 345 5 5 HELIX 27 AC9 MET C 365 GLU C 369 1 5 HELIX 28 AD1 ASP C 394 GLY C 398 5 5 HELIX 29 AD2 SER C 413 MET C 429 1 17 HELIX 30 AD3 THR D 22 GLY D 35 1 14 HELIX 31 AD4 PRO D 37 ASP D 39 5 3 HELIX 32 AD5 LEU D 56 ASN D 60 5 5 SHEET 1 AA1 3 ALA A 375 PRO A 378 0 SHEET 2 AA1 3 GLU A 129 PHE A 135 -1 N PHE A 135 O ALA A 375 SHEET 3 AA1 3 LYS A 432 PRO A 435 -1 O LYS A 432 N ILE A 132 SHEET 1 AA2 5 LEU A 183 PRO A 185 0 SHEET 2 AA2 5 HIS A 358 SER A 364 -1 O VAL A 363 N LEU A 184 SHEET 3 AA2 5 LEU A 350 ASP A 355 -1 N ALA A 353 O SER A 360 SHEET 4 AA2 5 ILE A 310 VAL A 313 1 N VAL A 311 O LEU A 352 SHEET 5 AA2 5 GLY A 333 TYR A 335 -1 O TYR A 335 N ILE A 310 SHEET 1 AA3 2 MET A 317 ARG A 319 0 SHEET 2 AA3 2 ALA A 325 PRO A 328 -1 O ALA A 327 N LEU A 318 SHEET 1 AA4 5 THR B 12 GLU B 16 0 SHEET 2 AA4 5 GLN B 2 THR B 7 -1 N ILE B 3 O LEU B 15 SHEET 3 AA4 5 THR B 66 LEU B 71 1 O LEU B 67 N PHE B 4 SHEET 4 AA4 5 GLN B 41 PHE B 45 -1 N ILE B 44 O HIS B 68 SHEET 5 AA4 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45 SHEET 1 AA5 3 ALA C 375 PRO C 378 0 SHEET 2 AA5 3 GLU C 129 PHE C 135 -1 N PHE C 135 O ALA C 375 SHEET 3 AA5 3 LYS C 432 PRO C 435 -1 O LYS C 432 N ILE C 132 SHEET 1 AA6 5 LEU C 183 PRO C 185 0 SHEET 2 AA6 5 HIS C 358 SER C 364 -1 O VAL C 363 N LEU C 184 SHEET 3 AA6 5 LEU C 350 ASP C 355 -1 N ALA C 353 O SER C 360 SHEET 4 AA6 5 ILE C 310 VAL C 313 1 N VAL C 311 O LEU C 352 SHEET 5 AA6 5 GLY C 333 TYR C 335 -1 O TYR C 335 N ILE C 310 SHEET 1 AA7 2 MET C 317 ARG C 319 0 SHEET 2 AA7 2 ALA C 325 PRO C 328 -1 O ALA C 327 N LEU C 318 SHEET 1 AA8 5 THR D 12 GLU D 16 0 SHEET 2 AA8 5 GLN D 2 LYS D 6 -1 N VAL D 5 O ILE D 13 SHEET 3 AA8 5 THR D 66 LEU D 71 1 O LEU D 67 N PHE D 4 SHEET 4 AA8 5 GLN D 41 PHE D 45 -1 N ILE D 44 O HIS D 68 SHEET 5 AA8 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45 LINK SG CYS A 194 CB NEH B 76 1555 1555 1.80 LINK C GLY B 75 N NEH B 76 1555 1555 1.32 LINK SG CYS C 194 CB NEH D 76 1555 1555 1.78 LINK C GLY D 75 N NEH D 76 1555 1555 1.31 SITE 1 AC1 9 ALA A 342 SER A 343 HOH A 631 HOH A 690 SITE 2 AC1 9 HOH A 711 GLU C 145 ASP C 146 SER C 149 SITE 3 AC1 9 ARG C 153 SITE 1 AC2 7 GLN C 136 LEU C 137 PRO C 138 ARG C 308 SITE 2 AC2 7 HOH C 619 HOH C 624 HOH C 651 SITE 1 AC3 14 THR C 188 THR C 189 ASP C 191 GLY C 192 SITE 2 AC3 14 ASN C 193 LEU C 195 LEU C 196 HIS C 197 SITE 3 AC3 14 ALA C 198 SER C 293 ALA C 357 PHE C 359 SITE 4 AC3 14 HOH C 715 GLY D 75 SITE 1 AC4 9 ASP C 191 GLY C 192 CYS C 194 SER C 293 SITE 2 AC4 9 LEU C 294 ALA C 357 PHE C 359 HOH C 611 SITE 3 AC4 9 ARG D 74 CRYST1 157.560 157.560 75.600 90.00 90.00 120.00 H 3 18 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 0.006347 0.003664 0.000000 0.00000 SCALE2 0.000000 0.007329 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013227 0.00000 ATOM 1 N MET A 128 89.213 22.428 -26.111 1.00 35.74 N ANISOU 1 N MET A 128 3753 5644 4184 213 704 -557 N ATOM 2 CA MET A 128 87.782 22.602 -26.334 1.00 35.27 C ANISOU 2 CA MET A 128 3804 5501 4096 174 675 -522 C ATOM 3 C MET A 128 87.172 23.486 -25.252 1.00 31.50 C ANISOU 3 C MET A 128 3378 4917 3672 104 625 -425 C ATOM 4 O MET A 128 87.666 23.531 -24.124 1.00 31.05 O ANISOU 4 O MET A 128 3297 4811 3690 113 591 -409 O ATOM 5 CB MET A 128 87.074 21.246 -26.374 1.00 39.62 C ANISOU 5 CB MET A 128 4421 5966 4665 261 635 -610 C ATOM 6 CG MET A 128 87.538 20.330 -27.498 1.00 43.68 C ANISOU 6 CG MET A 128 4898 6576 5124 336 679 -720 C ATOM 7 SD MET A 128 87.218 20.999 -29.146 1.00 73.94 S ANISOU 7 SD MET A 128 8747 10516 8831 267 731 -686 S ATOM 8 CE MET A 128 85.428 21.083 -29.141 1.00 39.37 C ANISOU 8 CE MET A 128 4486 6044 4430 230 690 -663 C ATOM 9 N GLU A 129 86.094 24.182 -25.601 1.00 26.00 N ANISOU 9 N GLU A 129 2754 4189 2938 39 617 -365 N ATOM 10 CA GLU A 129 85.489 25.161 -24.705 1.00 27.20 C ANISOU 10 CA GLU A 129 2952 4252 3132 -29 575 -276 C ATOM 11 C GLU A 129 84.268 24.601 -23.980 1.00 25.07 C ANISOU 11 C GLU A 129 2773 3848 2906 -2 514 -285 C ATOM 12 O GLU A 129 83.631 23.664 -24.456 1.00 26.80 O ANISOU 12 O GLU A 129 3035 4044 3105 45 505 -343 O ATOM 13 CB GLU A 129 85.099 26.423 -25.484 1.00 27.24 C ANISOU 13 CB GLU A 129 2972 4303 3074 -121 601 -193 C ATOM 14 CG GLU A 129 83.842 26.285 -26.338 1.00 26.97 C ANISOU 14 CG GLU A 129 3016 4252 2981 -126 594 -195 C ATOM 15 CD GLU A 129 84.070 25.501 -27.620 1.00 29.95 C ANISOU 15 CD GLU A 129 3371 4732 3277 -83 641 -267 C ATOM 16 OE1 GLU A 129 85.218 25.080 -27.874 1.00 27.94 O ANISOU 16 OE1 GLU A 129 3037 4568 3012 -47 684 -318 O ATOM 17 OE2 GLU A 129 83.094 25.309 -28.378 1.00 30.47 O ANISOU 17 OE2 GLU A 129 3496 4793 3289 -84 633 -277 O ATOM 18 N MET A 130 83.950 25.178 -22.825 1.00 20.80 N ANISOU 18 N MET A 130 2260 3222 2422 -34 471 -230 N ATOM 19 CA MET A 130 82.739 24.809 -22.100 1.00 20.94 C ANISOU 19 CA MET A 130 2359 3124 2474 -23 418 -226 C ATOM 20 C MET A 130 82.160 26.010 -21.356 1.00 17.42 C ANISOU 20 C MET A 130 1945 2622 2050 -89 391 -147 C ATOM 21 O MET A 130 82.897 26.809 -20.777 1.00 16.75 O ANISOU 21 O MET A 130 1822 2551 1993 -123 391 -109 O ATOM 22 CB MET A 130 83.008 23.655 -21.126 1.00 24.47 C ANISOU 22 CB MET A 130 2807 3506 2983 48 380 -277 C ATOM 23 CG MET A 130 83.375 24.066 -19.714 1.00 26.98 C ANISOU 23 CG MET A 130 3115 3774 3363 34 345 -238 C ATOM 24 SD MET A 130 83.074 22.726 -18.542 1.00 46.90 S ANISOU 24 SD MET A 130 5680 6191 5948 102 285 -274 S ATOM 25 CE MET A 130 83.620 23.470 -17.009 1.00 39.04 C ANISOU 25 CE MET A 130 4664 5168 5002 74 251 -221 C ATOM 26 N PRO A 131 80.830 26.149 -21.395 1.00 12.80 N ANISOU 26 N PRO A 131 1431 1978 1456 -106 367 -127 N ATOM 27 CA PRO A 131 80.122 27.264 -20.764 1.00 14.18 C ANISOU 27 CA PRO A 131 1640 2096 1650 -160 340 -61 C ATOM 28 C PRO A 131 79.831 27.023 -19.285 1.00 12.04 C ANISOU 28 C PRO A 131 1393 1740 1440 -142 296 -62 C ATOM 29 O PRO A 131 79.396 25.938 -18.899 1.00 11.14 O ANISOU 29 O PRO A 131 1306 1581 1343 -98 275 -100 O ATOM 30 CB PRO A 131 78.823 27.340 -21.564 1.00 16.03 C ANISOU 30 CB PRO A 131 1930 2317 1843 -173 335 -51 C ATOM 31 CG PRO A 131 78.566 25.925 -21.959 1.00 13.63 C ANISOU 31 CG PRO A 131 1641 2012 1528 -116 334 -121 C ATOM 32 CD PRO A 131 79.924 25.306 -22.197 1.00 13.31 C ANISOU 32 CD PRO A 131 1538 2034 1484 -78 365 -168 C ATOM 33 N ILE A 132 80.077 28.041 -18.471 1.00 9.95 N ANISOU 33 N ILE A 132 1121 1455 1205 -180 281 -19 N ATOM 34 CA ILE A 132 79.770 27.989 -17.046 1.00 16.61 C ANISOU 34 CA ILE A 132 1989 2228 2094 -171 240 -15 C ATOM 35 C ILE A 132 79.136 29.302 -16.607 1.00 14.64 C ANISOU 35 C ILE A 132 1768 1940 1854 -220 222 32 C ATOM 36 O ILE A 132 79.164 30.288 -17.342 1.00 13.51 O ANISOU 36 O ILE A 132 1619 1821 1692 -264 236 68 O ATOM 37 CB ILE A 132 81.029 27.734 -16.193 1.00 17.47 C ANISOU 37 CB ILE A 132 2048 2350 2239 -152 231 -30 C ATOM 38 CG1 ILE A 132 82.014 28.896 -16.345 1.00 20.47 C ANISOU 38 CG1 ILE A 132 2377 2780 2622 -202 246 2 C ATOM 39 CG2 ILE A 132 81.689 26.422 -16.583 1.00 14.64 C ANISOU 39 CG2 ILE A 132 1660 2024 1880 -91 244 -83 C ATOM 40 CD1 ILE A 132 83.245 28.773 -15.472 1.00 23.28 C ANISOU 40 CD1 ILE A 132 2677 3153 3015 -190 231 -10 C ATOM 41 N ACYS A 133 78.568 29.321 -15.407 0.53 13.18 N ANISOU 41 N ACYS A 133 1614 1697 1698 -213 188 33 N ATOM 42 N BCYS A 133 78.563 29.297 -15.407 0.47 13.28 N ANISOU 42 N BCYS A 133 1627 1709 1711 -212 188 32 N ATOM 43 CA ACYS A 133 78.049 30.563 -14.850 0.53 13.43 C ANISOU 43 CA ACYS A 133 1669 1690 1744 -250 167 66 C ATOM 44 CA BCYS A 133 77.990 30.495 -14.809 0.47 13.78 C ANISOU 44 CA BCYS A 133 1716 1732 1789 -247 166 64 C ATOM 45 C ACYS A 133 78.194 30.584 -13.333 0.53 14.04 C ANISOU 45 C ACYS A 133 1751 1731 1852 -241 135 56 C ATOM 46 C BCYS A 133 78.326 30.560 -13.325 0.47 14.02 C ANISOU 46 C BCYS A 133 1743 1731 1850 -240 136 55 C ATOM 47 O ACYS A 133 78.093 29.552 -12.671 0.53 14.38 O ANISOU 47 O ACYS A 133 1802 1761 1900 -205 123 33 O ATOM 48 O BCYS A 133 78.488 29.530 -12.672 0.47 14.24 O ANISOU 48 O BCYS A 133 1771 1754 1886 -204 125 31 O ATOM 49 CB ACYS A 133 76.586 30.769 -15.244 0.53 14.77 C ANISOU 49 CB ACYS A 133 1886 1829 1896 -252 161 76 C ATOM 50 CB BCYS A 133 76.471 30.531 -15.003 0.47 15.09 C ANISOU 50 CB BCYS A 133 1931 1862 1940 -243 157 69 C ATOM 51 SG ACYS A 133 75.436 29.612 -14.486 0.53 17.21 S ANISOU 51 SG ACYS A 133 2232 2099 2209 -213 144 47 S ATOM 52 SG BCYS A 133 75.925 30.882 -16.688 0.47 29.91 S ANISOU 52 SG BCYS A 133 3818 3770 3775 -263 180 91 S ATOM 53 N ALA A 134 78.436 31.773 -12.795 1.00 12.66 N ANISOU 53 N ALA A 134 1573 1538 1697 -275 117 75 N ATOM 54 CA ALA A 134 78.617 31.953 -11.364 1.00 12.07 C ANISOU 54 CA ALA A 134 1504 1437 1644 -271 85 62 C ATOM 55 C ALA A 134 77.255 31.965 -10.676 1.00 14.02 C ANISOU 55 C ALA A 134 1801 1642 1886 -256 69 55 C ATOM 56 O ALA A 134 76.245 32.311 -11.290 1.00 12.86 O ANISOU 56 O ALA A 134 1679 1478 1728 -261 77 66 O ATOM 57 CB ALA A 134 79.378 33.240 -11.080 1.00 10.85 C ANISOU 57 CB ALA A 134 1329 1278 1515 -316 68 78 C ATOM 58 N PHE A 135 77.227 31.568 -9.408 1.00 7.81 N ANISOU 58 N PHE A 135 1024 844 1101 -238 47 38 N ATOM 59 CA PHE A 135 76.013 31.672 -8.612 1.00 10.50 C ANISOU 59 CA PHE A 135 1402 1156 1431 -228 35 30 C ATOM 60 C PHE A 135 76.371 31.922 -7.151 1.00 12.05 C ANISOU 60 C PHE A 135 1601 1348 1629 -227 6 15 C ATOM 61 O PHE A 135 77.500 31.678 -6.727 1.00 11.31 O ANISOU 61 O PHE A 135 1481 1272 1544 -226 -9 12 O ATOM 62 CB PHE A 135 75.151 30.412 -8.752 1.00 7.92 C ANISOU 62 CB PHE A 135 1095 830 1085 -202 48 28 C ATOM 63 CG PHE A 135 75.723 29.197 -8.078 1.00 9.62 C ANISOU 63 CG PHE A 135 1305 1053 1298 -179 37 23 C ATOM 64 CD1 PHE A 135 76.664 28.411 -8.719 1.00 11.66 C ANISOU 64 CD1 PHE A 135 1537 1327 1565 -163 44 19 C ATOM 65 CD2 PHE A 135 75.310 28.836 -6.804 1.00 11.63 C ANISOU 65 CD2 PHE A 135 1580 1300 1539 -172 18 22 C ATOM 66 CE1 PHE A 135 77.191 27.291 -8.100 1.00 12.82 C ANISOU 66 CE1 PHE A 135 1682 1472 1718 -135 26 16 C ATOM 67 CE2 PHE A 135 75.831 27.719 -6.181 1.00 13.19 C ANISOU 67 CE2 PHE A 135 1778 1499 1735 -151 1 27 C ATOM 68 CZ PHE A 135 76.772 26.944 -6.830 1.00 12.81 C ANISOU 68 CZ PHE A 135 1706 1455 1705 -131 2 23 C ATOM 69 N GLN A 136 75.407 32.417 -6.388 1.00 13.71 N ANISOU 69 N GLN A 136 1839 1542 1828 -224 -4 2 N ATOM 70 CA GLN A 136 75.650 32.737 -4.991 1.00 16.85 C ANISOU 70 CA GLN A 136 2243 1942 2216 -223 -31 -19 C ATOM 71 C GLN A 136 74.375 32.647 -4.168 1.00 15.93 C ANISOU 71 C GLN A 136 2156 1827 2070 -207 -28 -34 C ATOM 72 O GLN A 136 73.268 32.702 -4.706 1.00 12.84 O ANISOU 72 O GLN A 136 1776 1427 1675 -201 -9 -31 O ATOM 73 CB GLN A 136 76.250 34.136 -4.864 1.00 18.84 C ANISOU 73 CB GLN A 136 2489 2175 2496 -249 -54 -32 C ATOM 74 CG GLN A 136 75.295 35.247 -5.269 1.00 26.64 C ANISOU 74 CG GLN A 136 3499 3127 3496 -254 -52 -39 C ATOM 75 CD GLN A 136 75.927 36.620 -5.187 1.00 33.65 C ANISOU 75 CD GLN A 136 4385 3982 4419 -285 -82 -50 C ATOM 76 OE1 GLN A 136 76.955 36.882 -5.812 1.00 36.86 O ANISOU 76 OE1 GLN A 136 4766 4389 4850 -317 -85 -27 O ATOM 77 NE2 GLN A 136 75.318 37.506 -4.407 1.00 36.93 N ANISOU 77 NE2 GLN A 136 4826 4368 4838 -275 -104 -86 N ATOM 78 N LEU A 137 74.545 32.505 -2.858 1.00 15.48 N ANISOU 78 N LEU A 137 2106 1788 1988 -201 -48 -49 N ATOM 79 CA LEU A 137 73.428 32.566 -1.927 1.00 13.25 C ANISOU 79 CA LEU A 137 1845 1521 1668 -190 -43 -67 C ATOM 80 C LEU A 137 72.900 33.990 -1.849 1.00 12.75 C ANISOU 80 C LEU A 137 1789 1437 1617 -188 -49 -104 C ATOM 81 O LEU A 137 73.657 34.939 -2.033 1.00 11.03 O ANISOU 81 O LEU A 137 1566 1192 1431 -202 -71 -117 O ATOM 82 CB LEU A 137 73.860 32.090 -0.543 1.00 12.66 C ANISOU 82 CB LEU A 137 1778 1480 1554 -186 -65 -72 C ATOM 83 CG LEU A 137 74.243 30.618 -0.428 1.00 13.78 C ANISOU 83 CG LEU A 137 1919 1635 1682 -181 -66 -33 C ATOM 84 CD1 LEU A 137 75.036 30.387 0.845 1.00 16.30 C ANISOU 84 CD1 LEU A 137 2241 1982 1970 -179 -102 -33 C ATOM 85 CD2 LEU A 137 72.994 29.759 -0.445 1.00 12.68 C ANISOU 85 CD2 LEU A 137 1796 1504 1516 -179 -39 -12 C ATOM 86 N PRO A 138 71.599 34.145 -1.574 1.00 15.91 N ANISOU 86 N PRO A 138 2200 1848 1997 -172 -31 -122 N ATOM 87 CA PRO A 138 71.015 35.481 -1.404 1.00 18.87 C ANISOU 87 CA PRO A 138 2583 2201 2386 -159 -41 -165 C ATOM 88 C PRO A 138 71.700 36.268 -0.289 1.00 21.49 C ANISOU 88 C PRO A 138 2924 2533 2709 -160 -74 -209 C ATOM 89 O PRO A 138 72.253 35.674 0.638 1.00 20.07 O ANISOU 89 O PRO A 138 2744 2389 2491 -165 -84 -209 O ATOM 90 CB PRO A 138 69.552 35.186 -1.053 1.00 19.57 C ANISOU 90 CB PRO A 138 2671 2324 2440 -136 -13 -179 C ATOM 91 CG PRO A 138 69.548 33.777 -0.563 1.00 19.84 C ANISOU 91 CG PRO A 138 2704 2404 2432 -147 4 -146 C ATOM 92 CD PRO A 138 70.612 33.078 -1.350 1.00 16.16 C ANISOU 92 CD PRO A 138 2234 1915 1992 -165 -4 -104 C ATOM 93 N ASP A 139 71.672 37.592 -0.398 1.00 25.13 N ANISOU 93 N ASP A 139 3395 2948 3206 -156 -97 -246 N ATOM 94 CA ASP A 139 72.222 38.473 0.626 1.00 25.33 C ANISOU 94 CA ASP A 139 3432 2965 3229 -157 -135 -299 C ATOM 95 C ASP A 139 71.099 39.241 1.312 1.00 23.88 C ANISOU 95 C ASP A 139 3262 2784 3027 -118 -134 -364 C ATOM 96 O ASP A 139 70.479 40.115 0.707 1.00 23.48 O ANISOU 96 O ASP A 139 3218 2684 3020 -100 -139 -381 O ATOM 97 CB ASP A 139 73.231 39.451 0.021 1.00 33.84 C ANISOU 97 CB ASP A 139 4510 3978 4368 -188 -171 -296 C ATOM 98 CG ASP A 139 74.494 38.764 -0.463 1.00 43.61 C ANISOU 98 CG ASP A 139 5724 5227 5618 -224 -173 -244 C ATOM 99 OD1 ASP A 139 74.934 37.790 0.187 1.00 45.76 O ANISOU 99 OD1 ASP A 139 5987 5551 5851 -223 -170 -234 O ATOM 100 OD2 ASP A 139 75.051 39.201 -1.492 1.00 48.55 O ANISOU 100 OD2 ASP A 139 6340 5814 6292 -253 -179 -213 O ATOM 101 N LEU A 140 70.834 38.912 2.573 1.00 15.35 N ANISOU 101 N LEU A 140 2184 1766 1882 -102 -128 -400 N ATOM 102 CA LEU A 140 69.763 39.572 3.307 1.00 17.56 C ANISOU 102 CA LEU A 140 2470 2067 2135 -60 -120 -471 C ATOM 103 C LEU A 140 70.179 40.990 3.681 1.00 18.83 C ANISOU 103 C LEU A 140 2652 2170 2332 -50 -169 -542 C ATOM 104 O LEU A 140 71.332 41.234 4.030 1.00 19.00 O ANISOU 104 O LEU A 140 2684 2174 2363 -80 -208 -548 O ATOM 105 CB LEU A 140 69.390 38.779 4.564 1.00 18.59 C ANISOU 105 CB LEU A 140 2596 2293 2174 -52 -96 -485 C ATOM 106 CG LEU A 140 69.057 37.296 4.386 1.00 15.72 C ANISOU 106 CG LEU A 140 2217 1984 1772 -70 -55 -412 C ATOM 107 CD1 LEU A 140 68.430 36.726 5.654 1.00 11.47 C ANISOU 107 CD1 LEU A 140 1676 1541 1141 -61 -29 -429 C ATOM 108 CD2 LEU A 140 68.148 37.078 3.187 1.00 19.77 C ANISOU 108 CD2 LEU A 140 2713 2472 2325 -63 -24 -378 C ATOM 109 N THR A 141 69.237 41.922 3.602 1.00 21.69 N ANISOU 109 N THR A 141 3021 2501 2720 -8 -171 -597 N ATOM 110 CA THR A 141 69.507 43.307 3.971 1.00 22.07 C ANISOU 110 CA THR A 141 3094 2482 2808 8 -222 -673 C ATOM 111 C THR A 141 69.491 43.488 5.486 1.00 19.26 C ANISOU 111 C THR A 141 2748 2187 2383 31 -231 -758 C ATOM 112 O THR A 141 69.856 44.547 5.994 1.00 21.15 O ANISOU 112 O THR A 141 3012 2379 2646 41 -280 -833 O ATOM 113 CB THR A 141 68.492 44.270 3.332 1.00 22.63 C ANISOU 113 CB THR A 141 3171 2488 2938 55 -229 -705 C ATOM 114 OG1 THR A 141 67.162 43.869 3.686 1.00 20.90 O ANISOU 114 OG1 THR A 141 2928 2345 2670 106 -181 -733 O ATOM 115 CG2 THR A 141 68.632 44.253 1.818 1.00 27.04 C ANISOU 115 CG2 THR A 141 3728 2981 3564 27 -231 -621 C ATOM 116 N VAL A 142 69.066 42.451 6.202 1.00 17.56 N ANISOU 116 N VAL A 142 2514 2077 2079 37 -187 -747 N ATOM 117 CA VAL A 142 69.136 42.450 7.662 1.00 18.65 C ANISOU 117 CA VAL A 142 2661 2294 2133 50 -192 -815 C ATOM 118 C VAL A 142 69.213 41.016 8.190 1.00 15.51 C ANISOU 118 C VAL A 142 2248 1998 1649 24 -155 -751 C ATOM 119 O VAL A 142 68.552 40.119 7.670 1.00 16.09 O ANISOU 119 O VAL A 142 2300 2103 1712 20 -108 -687 O ATOM 120 CB VAL A 142 67.930 43.183 8.295 1.00 20.33 C ANISOU 120 CB VAL A 142 2869 2538 2316 117 -175 -915 C ATOM 121 CG1 VAL A 142 66.635 42.442 8.003 1.00 19.80 C ANISOU 121 CG1 VAL A 142 2766 2539 2218 140 -107 -881 C ATOM 122 CG2 VAL A 142 68.132 43.349 9.792 1.00 23.65 C ANISOU 122 CG2 VAL A 142 3302 3036 2646 130 -187 -996 C ATOM 123 N TYR A 143 70.041 40.812 9.211 1.00 15.20 N ANISOU 123 N TYR A 143 2222 2004 1549 4 -182 -767 N ATOM 124 CA TYR A 143 70.270 39.493 9.807 1.00 16.02 C ANISOU 124 CA TYR A 143 2319 2196 1572 -23 -161 -702 C ATOM 125 C TYR A 143 70.914 38.497 8.839 1.00 18.19 C ANISOU 125 C TYR A 143 2584 2436 1892 -62 -159 -595 C ATOM 126 O TYR A 143 70.688 37.293 8.942 1.00 13.90 O ANISOU 126 O TYR A 143 2032 1946 1303 -77 -128 -528 O ATOM 127 CB TYR A 143 68.958 38.911 10.349 1.00 14.16 C ANISOU 127 CB TYR A 143 2067 2059 1254 0 -99 -704 C ATOM 128 CG TYR A 143 68.345 39.739 11.457 1.00 15.15 C ANISOU 128 CG TYR A 143 2198 2246 1314 42 -95 -814 C ATOM 129 CD1 TYR A 143 69.038 39.975 12.636 1.00 15.87 C ANISOU 129 CD1 TYR A 143 2310 2384 1334 38 -131 -865 C ATOM 130 CD2 TYR A 143 67.075 40.284 11.321 1.00 15.46 C ANISOU 130 CD2 TYR A 143 2215 2299 1358 90 -55 -871 C ATOM 131 CE1 TYR A 143 68.488 40.738 13.651 1.00 16.87 C ANISOU 131 CE1 TYR A 143 2442 2572 1394 80 -127 -975 C ATOM 132 CE2 TYR A 143 66.513 41.046 12.332 1.00 16.46 C ANISOU 132 CE2 TYR A 143 2343 2488 1425 137 -49 -982 C ATOM 133 CZ TYR A 143 67.226 41.270 13.496 1.00 17.17 C ANISOU 133 CZ TYR A 143 2459 2625 1441 132 -84 -1036 C ATOM 134 OH TYR A 143 66.678 42.026 14.506 1.00 18.26 O ANISOU 134 OH TYR A 143 2597 2812 1529 175 -74 -1124 O ATOM 135 N ASN A 144 71.722 38.995 7.910 1.00 12.71 N ANISOU 135 N ASN A 144 1890 1653 1287 -80 -192 -581 N ATOM 136 CA ASN A 144 72.412 38.116 6.973 1.00 15.83 C ANISOU 136 CA ASN A 144 2271 2019 1724 -112 -189 -491 C ATOM 137 C ASN A 144 73.422 37.218 7.678 1.00 15.10 C ANISOU 137 C ASN A 144 2179 1974 1585 -136 -214 -452 C ATOM 138 O ASN A 144 73.609 36.062 7.299 1.00 11.65 O ANISOU 138 O ASN A 144 1732 1550 1146 -149 -197 -378 O ATOM 139 CB ASN A 144 73.107 38.929 5.880 1.00 18.78 C ANISOU 139 CB ASN A 144 2642 2300 2195 -130 -217 -487 C ATOM 140 CG ASN A 144 73.732 38.051 4.815 1.00 18.83 C ANISOU 140 CG ASN A 144 2628 2285 2240 -157 -206 -402 C ATOM 141 OD1 ASN A 144 73.030 37.437 4.012 1.00 15.57 O ANISOU 141 OD1 ASN A 144 2207 1871 1837 -150 -166 -359 O ATOM 142 ND2 ASN A 144 75.057 37.986 4.803 1.00 17.18 N ANISOU 142 ND2 ASN A 144 2408 2066 2055 -186 -243 -384 N ATOM 143 N GLU A 145 74.064 37.753 8.712 1.00 15.19 N ANISOU 143 N GLU A 145 2201 2008 1561 -139 -258 -506 N ATOM 144 CA GLU A 145 75.022 36.981 9.498 1.00 17.46 C ANISOU 144 CA GLU A 145 2489 2346 1799 -157 -292 -473 C ATOM 145 C GLU A 145 74.344 35.791 10.167 1.00 16.11 C ANISOU 145 C GLU A 145 2326 2256 1540 -150 -257 -427 C ATOM 146 O GLU A 145 74.883 34.685 10.181 1.00 14.18 O ANISOU 146 O GLU A 145 2078 2028 1283 -164 -266 -355 O ATOM 147 CB GLU A 145 75.692 37.860 10.555 1.00 22.39 C ANISOU 147 CB GLU A 145 3127 2988 2393 -160 -349 -550 C ATOM 148 N ASP A 146 73.157 36.022 10.717 1.00 17.23 N ANISOU 148 N ASP A 146 2477 2447 1622 -129 -219 -467 N ATOM 149 CA ASP A 146 72.400 34.958 11.365 1.00 18.64 C ANISOU 149 CA ASP A 146 2661 2710 1713 -132 -180 -420 C ATOM 150 C ASP A 146 72.010 33.892 10.346 1.00 16.25 C ANISOU 150 C ASP A 146 2345 2376 1452 -145 -143 -333 C ATOM 151 O ASP A 146 72.171 32.697 10.589 1.00 15.64 O ANISOU 151 O ASP A 146 2274 2327 1340 -163 -143 -258 O ATOM 152 CB ASP A 146 71.152 35.520 12.053 1.00 20.16 C ANISOU 152 CB ASP A 146 2853 2967 1838 -107 -139 -488 C ATOM 153 CG ASP A 146 71.481 36.310 13.306 1.00 27.10 C ANISOU 153 CG ASP A 146 3750 3901 2646 -93 -174 -574 C ATOM 154 OD1 ASP A 146 71.826 35.681 14.325 1.00 29.57 O ANISOU 154 OD1 ASP A 146 4076 4291 2867 -109 -190 -548 O ATOM 155 OD2 ASP A 146 71.388 37.555 13.275 1.00 29.19 O ANISOU 155 OD2 ASP A 146 4017 4129 2944 -67 -190 -668 O ATOM 156 N PHE A 147 71.505 34.344 9.203 1.00 15.52 N ANISOU 156 N PHE A 147 2237 2222 1436 -135 -118 -344 N ATOM 157 CA PHE A 147 71.140 33.456 8.105 1.00 14.09 C ANISOU 157 CA PHE A 147 2044 2006 1302 -146 -87 -273 C ATOM 158 C PHE A 147 72.318 32.589 7.676 1.00 15.26 C ANISOU 158 C PHE A 147 2193 2118 1486 -164 -119 -209 C ATOM 159 O PHE A 147 72.182 31.374 7.544 1.00 13.39 O ANISOU 159 O PHE A 147 1960 1890 1237 -177 -106 -141 O ATOM 160 CB PHE A 147 70.614 34.273 6.921 1.00 14.57 C ANISOU 160 CB PHE A 147 2091 2003 1440 -131 -69 -302 C ATOM 161 CG PHE A 147 70.645 33.545 5.606 1.00 13.50 C ANISOU 161 CG PHE A 147 1945 1818 1368 -144 -54 -239 C ATOM 162 CD1 PHE A 147 69.943 32.364 5.429 1.00 17.18 C ANISOU 162 CD1 PHE A 147 2408 2309 1812 -156 -21 -182 C ATOM 163 CD2 PHE A 147 71.358 34.061 4.535 1.00 12.51 C ANISOU 163 CD2 PHE A 147 1813 1621 1320 -146 -73 -238 C ATOM 164 CE1 PHE A 147 69.965 31.701 4.213 1.00 16.24 C ANISOU 164 CE1 PHE A 147 2281 2141 1747 -165 -11 -134 C ATOM 165 CE2 PHE A 147 71.380 33.406 3.318 1.00 15.68 C ANISOU 165 CE2 PHE A 147 2204 1985 1769 -156 -58 -187 C ATOM 166 CZ PHE A 147 70.684 32.223 3.159 1.00 14.04 C ANISOU 166 CZ PHE A 147 1996 1801 1539 -162 -28 -140 C ATOM 167 N ARG A 148 73.477 33.209 7.471 1.00 11.25 N ANISOU 167 N ARG A 148 1680 1570 1025 -166 -163 -232 N ATOM 168 CA ARG A 148 74.651 32.469 7.021 1.00 15.26 C ANISOU 168 CA ARG A 148 2178 2049 1572 -177 -193 -179 C ATOM 169 C ARG A 148 75.134 31.490 8.093 1.00 18.02 C ANISOU 169 C ARG A 148 2540 2450 1855 -181 -221 -139 C ATOM 170 O ARG A 148 75.739 30.463 7.781 1.00 11.32 O ANISOU 170 O ARG A 148 1688 1586 1029 -182 -236 -80 O ATOM 171 CB ARG A 148 75.772 33.429 6.621 1.00 16.16 C ANISOU 171 CB ARG A 148 2274 2119 1747 -183 -231 -214 C ATOM 172 CG ARG A 148 75.442 34.275 5.401 1.00 17.84 C ANISOU 172 CG ARG A 148 2477 2271 2031 -185 -209 -234 C ATOM 173 CD ARG A 148 75.032 33.420 4.205 1.00 19.26 C ANISOU 173 CD ARG A 148 2646 2425 2245 -184 -170 -179 C ATOM 174 NE ARG A 148 76.183 32.841 3.515 1.00 27.80 N ANISOU 174 NE ARG A 148 3705 3486 3371 -192 -187 -140 N ATOM 175 CZ ARG A 148 76.752 33.371 2.436 1.00 26.17 C ANISOU 175 CZ ARG A 148 3476 3238 3228 -204 -186 -140 C ATOM 176 NH1 ARG A 148 76.276 34.494 1.917 1.00 24.45 N ANISOU 176 NH1 ARG A 148 3263 2986 3040 -211 -176 -169 N ATOM 177 NH2 ARG A 148 77.797 32.778 1.873 1.00 28.98 N ANISOU 177 NH2 ARG A 148 3804 3591 3616 -208 -197 -108 N ATOM 178 N SER A 149 74.858 31.802 9.356 1.00 15.88 N ANISOU 178 N SER A 149 2288 2243 1503 -180 -231 -171 N ATOM 179 CA ASER A 149 75.196 30.879 10.446 0.58 15.86 C ANISOU 179 CA ASER A 149 2304 2298 1425 -187 -259 -124 C ATOM 180 CA BSER A 149 75.156 30.894 10.454 0.42 15.91 C ANISOU 180 CA BSER A 149 2309 2305 1429 -187 -258 -125 C ATOM 181 C SER A 149 74.347 29.604 10.376 1.00 15.23 C ANISOU 181 C SER A 149 2237 2233 1316 -197 -222 -48 C ATOM 182 O SER A 149 74.847 28.513 10.639 1.00 12.73 O ANISOU 182 O SER A 149 1933 1918 986 -203 -250 20 O ATOM 183 CB ASER A 149 75.013 31.541 11.808 0.58 16.66 C ANISOU 183 CB ASER A 149 2422 2476 1433 -185 -274 -180 C ATOM 184 CB BSER A 149 74.908 31.590 11.792 0.42 16.69 C ANISOU 184 CB BSER A 149 2426 2481 1436 -185 -269 -183 C ATOM 185 OG ASER A 149 73.639 31.628 12.143 0.58 17.99 O ANISOU 185 OG ASER A 149 2599 2694 1543 -184 -218 -196 O ATOM 186 OG BSER A 149 75.173 30.702 12.861 0.42 15.82 O ANISOU 186 OG BSER A 149 2336 2433 1241 -194 -296 -131 O ATOM 187 N PHE A 150 73.079 29.740 10.014 1.00 13.79 N ANISOU 187 N PHE A 150 2051 2057 1129 -200 -165 -59 N ATOM 188 CA PHE A 150 72.215 28.577 9.848 1.00 14.98 C ANISOU 188 CA PHE A 150 2211 2218 1264 -219 -129 12 C ATOM 189 C PHE A 150 72.657 27.744 8.644 1.00 14.90 C ANISOU 189 C PHE A 150 2195 2126 1339 -218 -137 62 C ATOM 190 O PHE A 150 72.581 26.518 8.667 1.00 16.13 O ANISOU 190 O PHE A 150 2367 2272 1489 -232 -142 134 O ATOM 191 CB PHE A 150 70.744 29.010 9.723 1.00 15.91 C ANISOU 191 CB PHE A 150 2316 2369 1360 -221 -67 -20 C ATOM 192 CG PHE A 150 70.084 29.273 11.048 1.00 19.53 C ANISOU 192 CG PHE A 150 2782 2929 1711 -227 -48 -45 C ATOM 193 CD1 PHE A 150 70.330 30.447 11.742 1.00 18.85 C ANISOU 193 CD1 PHE A 150 2695 2877 1588 -205 -64 -129 C ATOM 194 CD2 PHE A 150 69.224 28.341 11.602 1.00 21.51 C ANISOU 194 CD2 PHE A 150 3040 3242 1893 -258 -15 16 C ATOM 195 CE1 PHE A 150 69.723 30.689 12.967 1.00 18.96 C ANISOU 195 CE1 PHE A 150 2714 2994 1494 -206 -43 -161 C ATOM 196 CE2 PHE A 150 68.615 28.574 12.820 1.00 22.87 C ANISOU 196 CE2 PHE A 150 3214 3521 1955 -266 9 -5 C ATOM 197 CZ PHE A 150 68.865 29.751 13.505 1.00 21.13 C ANISOU 197 CZ PHE A 150 2992 3342 1694 -236 -4 -97 C ATOM 198 N ILE A 151 73.114 28.418 7.595 1.00 13.00 N ANISOU 198 N ILE A 151 1933 1829 1178 -202 -139 24 N ATOM 199 CA ILE A 151 73.680 27.733 6.442 1.00 14.05 C ANISOU 199 CA ILE A 151 2056 1895 1388 -197 -147 59 C ATOM 200 C ILE A 151 74.922 26.938 6.840 1.00 14.67 C ANISOU 200 C ILE A 151 2140 1965 1469 -188 -201 99 C ATOM 201 O ILE A 151 75.102 25.796 6.418 1.00 12.79 O ANISOU 201 O ILE A 151 1910 1692 1259 -185 -210 152 O ATOM 202 CB ILE A 151 74.059 28.722 5.315 1.00 15.50 C ANISOU 202 CB ILE A 151 2213 2032 1644 -186 -141 11 C ATOM 203 CG1 ILE A 151 72.807 29.381 4.739 1.00 13.21 C ANISOU 203 CG1 ILE A 151 1918 1738 1364 -188 -94 -19 C ATOM 204 CG2 ILE A 151 74.820 28.005 4.213 1.00 13.64 C ANISOU 204 CG2 ILE A 151 1963 1743 1475 -177 -151 42 C ATOM 205 CD1 ILE A 151 71.913 28.422 3.977 1.00 13.64 C ANISOU 205 CD1 ILE A 151 1974 1774 1432 -196 -60 23 C ATOM 206 N GLU A 152 75.764 27.540 7.675 1.00 17.43 N ANISOU 206 N GLU A 152 2486 2346 1791 -183 -242 71 N ATOM 207 CA GLU A 152 77.019 26.919 8.081 1.00 17.14 C ANISOU 207 CA GLU A 152 2447 2308 1760 -170 -301 103 C ATOM 208 C GLU A 152 76.787 25.658 8.916 1.00 19.84 C ANISOU 208 C GLU A 152 2823 2671 2045 -176 -320 177 C ATOM 209 O GLU A 152 77.543 24.690 8.814 1.00 19.99 O ANISOU 209 O GLU A 152 2844 2658 2093 -159 -359 225 O ATOM 210 CB GLU A 152 77.876 27.924 8.859 1.00 17.74 C ANISOU 210 CB GLU A 152 2510 2420 1813 -168 -344 52 C ATOM 211 CG GLU A 152 79.334 27.515 9.035 1.00 21.93 C ANISOU 211 CG GLU A 152 3018 2945 2369 -152 -408 72 C ATOM 212 CD GLU A 152 79.535 26.494 10.139 1.00 26.81 C ANISOU 212 CD GLU A 152 3665 3598 2922 -147 -452 132 C ATOM 213 OE1 GLU A 152 78.701 26.446 11.068 1.00 26.63 O ANISOU 213 OE1 GLU A 152 3678 3625 2814 -164 -439 144 O ATOM 214 OE2 GLU A 152 80.528 25.736 10.077 1.00 27.70 O ANISOU 214 OE2 GLU A 152 3765 3692 3069 -124 -500 169 O ATOM 215 N ARG A 153 75.741 25.668 9.735 1.00 12.55 N ANISOU 215 N ARG A 153 1926 1801 1042 -199 -293 187 N ATOM 216 CA ARG A 153 75.441 24.526 10.593 1.00 15.57 C ANISOU 216 CA ARG A 153 2345 2210 1362 -216 -308 266 C ATOM 217 C ARG A 153 74.520 23.519 9.905 1.00 14.69 C ANISOU 217 C ARG A 153 2248 2056 1279 -235 -272 321 C ATOM 218 O ARG A 153 74.156 22.501 10.492 1.00 15.40 O ANISOU 218 O ARG A 153 2370 2155 1326 -258 -282 396 O ATOM 219 CB ARG A 153 74.814 24.995 11.909 1.00 16.69 C ANISOU 219 CB ARG A 153 2505 2447 1389 -238 -297 254 C ATOM 220 CG ARG A 153 75.728 25.869 12.760 1.00 17.01 C ANISOU 220 CG ARG A 153 2540 2535 1389 -223 -344 201 C ATOM 221 CD ARG A 153 75.116 26.142 14.127 1.00 20.25 C ANISOU 221 CD ARG A 153 2974 3048 1673 -243 -335 194 C ATOM 222 NE ARG A 153 73.770 26.697 14.014 1.00 22.13 N ANISOU 222 NE ARG A 153 3204 3321 1884 -256 -261 153 N ATOM 223 CZ ARG A 153 73.497 27.997 13.981 1.00 24.38 C ANISOU 223 CZ ARG A 153 3469 3624 2168 -241 -238 55 C ATOM 224 NH1 ARG A 153 74.477 28.886 14.059 1.00 26.35 N ANISOU 224 NH1 ARG A 153 3710 3860 2444 -221 -284 -9 N ATOM 225 NH2 ARG A 153 72.241 28.409 13.873 1.00 26.27 N ANISOU 225 NH2 ARG A 153 3698 3896 2385 -246 -173 21 N ATOM 226 N ASP A 154 74.144 23.808 8.663 1.00 15.29 N ANISOU 226 N ASP A 154 2301 2084 1427 -228 -233 286 N ATOM 227 CA ASP A 154 73.269 22.921 7.899 1.00 17.69 C ANISOU 227 CA ASP A 154 2614 2343 1763 -247 -201 327 C ATOM 228 C ASP A 154 73.922 21.579 7.578 1.00 16.10 C ANISOU 228 C ASP A 154 2434 2074 1611 -235 -245 389 C ATOM 229 O ASP A 154 75.119 21.509 7.296 1.00 14.22 O ANISOU 229 O ASP A 154 2183 1802 1419 -198 -287 378 O ATOM 230 CB ASP A 154 72.834 23.593 6.594 1.00 21.45 C ANISOU 230 CB ASP A 154 3061 2786 2304 -238 -158 271 C ATOM 231 CG ASP A 154 71.524 24.340 6.728 1.00 32.70 C ANISOU 231 CG ASP A 154 4474 4261 3688 -259 -102 238 C ATOM 232 OD1 ASP A 154 70.704 23.961 7.591 1.00 38.74 O ANISOU 232 OD1 ASP A 154 5255 5080 4385 -289 -85 273 O ATOM 233 OD2 ASP A 154 71.310 25.303 5.962 1.00 36.97 O ANISOU 233 OD2 ASP A 154 4990 4791 4267 -245 -77 180 O ATOM 234 N LEU A 155 73.125 20.516 7.610 1.00 12.46 N ANISOU 234 N LEU A 155 2001 1590 1141 -267 -236 453 N ATOM 235 CA LEU A 155 73.597 19.204 7.188 1.00 13.57 C ANISOU 235 CA LEU A 155 2168 1650 1340 -255 -278 507 C ATOM 236 C LEU A 155 73.500 19.080 5.670 1.00 14.38 C ANISOU 236 C LEU A 155 2250 1684 1529 -236 -255 468 C ATOM 237 O LEU A 155 72.756 19.817 5.028 1.00 13.57 O ANISOU 237 O LEU A 155 2123 1599 1432 -248 -203 421 O ATOM 238 CB LEU A 155 72.795 18.092 7.864 1.00 18.33 C ANISOU 238 CB LEU A 155 2815 2248 1901 -303 -285 597 C ATOM 239 CG LEU A 155 73.009 17.928 9.370 1.00 20.83 C ANISOU 239 CG LEU A 155 3161 2627 2127 -322 -318 655 C ATOM 240 CD1 LEU A 155 72.065 16.881 9.930 1.00 23.15 C ANISOU 240 CD1 LEU A 155 3497 2920 2379 -384 -315 750 C ATOM 241 CD2 LEU A 155 74.455 17.569 9.676 1.00 22.93 C ANISOU 241 CD2 LEU A 155 3437 2859 2417 -273 -395 672 C ATOM 242 N ILE A 156 74.264 18.152 5.104 1.00 14.81 N ANISOU 242 N ILE A 156 2315 1664 1649 -203 -296 484 N ATOM 243 CA ILE A 156 74.210 17.880 3.672 1.00 18.55 C ANISOU 243 CA ILE A 156 2775 2075 2199 -184 -279 447 C ATOM 244 C ILE A 156 73.345 16.655 3.386 1.00 18.22 C ANISOU 244 C ILE A 156 2771 1971 2179 -216 -282 497 C ATOM 245 O ILE A 156 73.323 15.709 4.172 1.00 18.11 O ANISOU 245 O ILE A 156 2800 1932 2150 -233 -321 568 O ATOM 246 CB ILE A 156 75.623 17.662 3.089 1.00 22.38 C ANISOU 246 CB ILE A 156 3237 2518 2746 -120 -318 417 C ATOM 247 CG1 ILE A 156 76.454 18.942 3.212 1.00 21.82 C ANISOU 247 CG1 ILE A 156 3120 2507 2662 -99 -312 365 C ATOM 248 CG2 ILE A 156 75.544 17.222 1.636 1.00 27.53 C ANISOU 248 CG2 ILE A 156 3881 3112 3469 -100 -300 381 C ATOM 249 CD1 ILE A 156 75.828 20.146 2.547 1.00 21.38 C ANISOU 249 CD1 ILE A 156 3036 2486 2601 -119 -252 310 C ATOM 250 N GLU A 157 72.687 16.630 2.231 1.00 18.00 N ANISOU 250 N GLU A 157 2733 1920 2187 -228 -243 462 N ATOM 251 CA GLU A 157 71.846 15.496 1.873 1.00 20.64 C ANISOU 251 CA GLU A 157 3101 2188 2554 -259 -250 497 C ATOM 252 C GLU A 157 72.750 14.424 1.293 1.00 16.82 C ANISOU 252 C GLU A 157 2639 1611 2141 -210 -305 498 C ATOM 253 O GLU A 157 72.991 14.361 0.093 1.00 13.50 O ANISOU 253 O GLU A 157 2201 1155 1774 -175 -297 440 O ATOM 254 CB GLU A 157 70.791 15.889 0.838 1.00 24.50 C ANISOU 254 CB GLU A 157 3567 2685 3058 -283 -199 453 C ATOM 255 CG GLU A 157 69.568 16.585 1.405 1.00 32.79 C ANISOU 255 CG GLU A 157 4601 3811 4047 -338 -150 464 C ATOM 256 CD GLU A 157 68.545 15.629 1.988 1.00 39.89 C ANISOU 256 CD GLU A 157 5533 4702 4921 -404 -156 540 C ATOM 257 OE1 GLU A 157 67.605 16.112 2.645 1.00 40.93 O ANISOU 257 OE1 GLU A 157 5649 4910 4991 -449 -118 559 O ATOM 258 OE2 GLU A 157 68.673 14.403 1.788 1.00 45.11 O ANISOU 258 OE2 GLU A 157 6234 5280 5626 -412 -198 580 O ATOM 259 N GLN A 158 73.244 13.577 2.183 1.00 17.86 N ANISOU 259 N GLN A 158 2810 1706 2271 -205 -362 563 N ATOM 260 CA GLN A 158 74.259 12.586 1.832 1.00 20.30 C ANISOU 260 CA GLN A 158 3137 1926 2649 -145 -423 562 C ATOM 261 C GLN A 158 73.843 11.649 0.702 1.00 16.42 C ANISOU 261 C GLN A 158 2668 1343 2226 -142 -430 540 C ATOM 262 O GLN A 158 74.639 11.367 -0.193 1.00 19.06 O ANISOU 262 O GLN A 158 2988 1633 2621 -77 -447 482 O ATOM 263 CB GLN A 158 74.633 11.763 3.064 1.00 25.52 C ANISOU 263 CB GLN A 158 3846 2558 3293 -149 -489 651 C ATOM 264 CG GLN A 158 75.448 12.535 4.080 1.00 32.49 C ANISOU 264 CG GLN A 158 4705 3519 4119 -127 -504 660 C ATOM 265 CD GLN A 158 76.764 13.027 3.510 1.00 35.17 C ANISOU 265 CD GLN A 158 4993 3868 4501 -47 -516 587 C ATOM 266 OE1 GLN A 158 77.489 12.279 2.853 1.00 36.64 O ANISOU 266 OE1 GLN A 158 5180 3982 4761 12 -554 565 O ATOM 267 NE2 GLN A 158 77.075 14.294 3.753 1.00 35.50 N ANISOU 267 NE2 GLN A 158 4989 4000 4500 -46 -484 547 N ATOM 268 N SER A 159 72.605 11.166 0.749 1.00 14.48 N ANISOU 268 N SER A 159 2455 1075 1972 -214 -417 581 N ATOM 269 CA SER A 159 72.125 10.202 -0.238 1.00 15.91 C ANISOU 269 CA SER A 159 2659 1171 2216 -220 -427 559 C ATOM 270 C SER A 159 72.112 10.805 -1.639 1.00 13.88 C ANISOU 270 C SER A 159 2363 926 1985 -190 -386 465 C ATOM 271 O SER A 159 72.390 10.118 -2.622 1.00 13.63 O ANISOU 271 O SER A 159 2342 821 2015 -152 -408 417 O ATOM 272 CB SER A 159 70.725 9.701 0.130 1.00 17.81 C ANISOU 272 CB SER A 159 2909 1429 2431 -304 -401 603 C ATOM 273 OG SER A 159 69.766 10.740 0.036 1.00 21.23 O ANISOU 273 OG SER A 159 3310 1941 2813 -355 -340 593 O ATOM 274 N MET A 160 71.791 12.094 -1.719 1.00 14.25 N ANISOU 274 N MET A 160 2362 1070 1981 -206 -326 434 N ATOM 275 CA MET A 160 71.763 12.809 -2.992 1.00 15.52 C ANISOU 275 CA MET A 160 2481 1260 2154 -181 -283 352 C ATOM 276 C MET A 160 73.178 13.049 -3.519 1.00 16.48 C ANISOU 276 C MET A 160 2573 1383 2305 -99 -294 295 C ATOM 277 O MET A 160 73.457 12.828 -4.697 1.00 16.15 O ANISOU 277 O MET A 160 2520 1315 2301 -62 -289 233 O ATOM 278 CB MET A 160 71.020 14.140 -2.844 1.00 13.24 C ANISOU 278 CB MET A 160 2154 1068 1807 -220 -223 343 C ATOM 279 CG MET A 160 70.927 14.942 -4.135 1.00 13.59 C ANISOU 279 CG MET A 160 2160 1144 1860 -200 -182 270 C ATOM 280 SD MET A 160 70.014 16.491 -3.972 1.00 22.50 S ANISOU 280 SD MET A 160 3247 2370 2931 -238 -122 260 S ATOM 281 CE MET A 160 68.387 15.901 -3.513 1.00 17.41 C ANISOU 281 CE MET A 160 2625 1724 2268 -317 -114 312 C ATOM 282 N LEU A 161 74.064 13.503 -2.638 1.00 16.29 N ANISOU 282 N LEU A 161 2533 1398 2260 -73 -308 315 N ATOM 283 CA LEU A 161 75.468 13.704 -2.980 1.00 17.40 C ANISOU 283 CA LEU A 161 2637 1547 2428 1 -323 268 C ATOM 284 C LEU A 161 76.096 12.425 -3.528 1.00 18.73 C ANISOU 284 C LEU A 161 2827 1626 2664 58 -371 248 C ATOM 285 O LEU A 161 76.732 12.433 -4.583 1.00 12.52 O ANISOU 285 O LEU A 161 2008 839 1909 111 -359 179 O ATOM 286 CB LEU A 161 76.249 14.184 -1.756 1.00 13.97 C ANISOU 286 CB LEU A 161 2189 1158 1962 12 -346 304 C ATOM 287 CG LEU A 161 77.765 14.335 -1.902 1.00 19.20 C ANISOU 287 CG LEU A 161 2807 1835 2654 85 -370 267 C ATOM 288 CD1 LEU A 161 78.110 15.442 -2.886 1.00 17.63 C ANISOU 288 CD1 LEU A 161 2547 1698 2452 96 -316 198 C ATOM 289 CD2 LEU A 161 78.401 14.601 -0.548 1.00 20.00 C ANISOU 289 CD2 LEU A 161 2905 1971 2723 89 -409 313 C ATOM 290 N VAL A 162 75.909 11.328 -2.801 1.00 17.16 N ANISOU 290 N VAL A 162 2683 1351 2484 48 -426 309 N ATOM 291 CA VAL A 162 76.471 10.041 -3.187 1.00 19.75 C ANISOU 291 CA VAL A 162 3041 1578 2884 106 -485 294 C ATOM 292 C VAL A 162 75.918 9.539 -4.521 1.00 22.87 C ANISOU 292 C VAL A 162 3448 1923 3317 108 -468 231 C ATOM 293 O VAL A 162 76.666 9.048 -5.368 1.00 14.48 O ANISOU 293 O VAL A 162 2373 823 2305 180 -484 163 O ATOM 294 CB VAL A 162 76.206 8.976 -2.107 1.00 22.32 C ANISOU 294 CB VAL A 162 3435 1824 3223 80 -551 386 C ATOM 295 CG1 VAL A 162 76.514 7.582 -2.641 1.00 24.26 C ANISOU 295 CG1 VAL A 162 3708 1968 3540 128 -598 358 C ATOM 296 CG2 VAL A 162 77.019 9.279 -0.852 1.00 15.22 C ANISOU 296 CG2 VAL A 162 2526 966 2291 99 -584 440 C ATOM 297 N ALA A 163 74.609 9.666 -4.705 1.00 13.79 N ANISOU 297 N ALA A 163 2318 778 2142 30 -436 248 N ATOM 298 CA ALA A 163 73.953 9.141 -5.899 1.00 20.56 C ANISOU 298 CA ALA A 163 3192 1588 3032 21 -428 194 C ATOM 299 C ALA A 163 74.332 9.918 -7.159 1.00 19.84 C ANISOU 299 C ALA A 163 3046 1563 2931 62 -377 102 C ATOM 300 O ALA A 163 74.610 9.328 -8.202 1.00 13.64 O ANISOU 300 O ALA A 163 2264 736 2184 108 -387 32 O ATOM 301 CB ALA A 163 72.445 9.148 -5.715 1.00 13.70 C ANISOU 301 CB ALA A 163 2349 721 2136 -77 -408 241 C ATOM 302 N LEU A 164 74.337 11.242 -7.060 1.00 15.42 N ANISOU 302 N LEU A 164 2437 1105 2316 44 -323 102 N ATOM 303 CA LEU A 164 74.596 12.084 -8.220 1.00 14.00 C ANISOU 303 CA LEU A 164 2208 993 2119 68 -272 30 C ATOM 304 C LEU A 164 76.081 12.120 -8.591 1.00 14.92 C ANISOU 304 C LEU A 164 2282 1129 2258 152 -277 -21 C ATOM 305 O LEU A 164 76.428 12.235 -9.767 1.00 13.15 O ANISOU 305 O LEU A 164 2029 931 2037 187 -250 -92 O ATOM 306 CB LEU A 164 74.074 13.501 -7.973 1.00 13.14 C ANISOU 306 CB LEU A 164 2065 975 1951 18 -219 52 C ATOM 307 CG LEU A 164 72.551 13.637 -7.889 1.00 12.77 C ANISOU 307 CG LEU A 164 2041 932 1879 -59 -201 84 C ATOM 308 CD1 LEU A 164 72.140 15.085 -7.690 1.00 14.08 C ANISOU 308 CD1 LEU A 164 2170 1186 1993 -91 -153 94 C ATOM 309 CD2 LEU A 164 71.893 13.054 -9.134 1.00 12.55 C ANISOU 309 CD2 LEU A 164 2029 868 1871 -66 -199 36 C ATOM 310 N GLU A 165 76.958 12.015 -7.596 1.00 15.50 N ANISOU 310 N GLU A 165 2349 1198 2344 183 -311 13 N ATOM 311 CA GLU A 165 78.391 11.973 -7.872 1.00 16.78 C ANISOU 311 CA GLU A 165 2462 1380 2532 265 -321 -34 C ATOM 312 C GLU A 165 78.789 10.651 -8.518 1.00 19.89 C ANISOU 312 C GLU A 165 2880 1691 2988 333 -362 -86 C ATOM 313 O GLU A 165 79.606 10.622 -9.438 1.00 17.95 O ANISOU 313 O GLU A 165 2589 1474 2758 397 -345 -161 O ATOM 314 CB GLU A 165 79.201 12.199 -6.594 1.00 21.56 C ANISOU 314 CB GLU A 165 3053 2005 3136 281 -355 18 C ATOM 315 CG GLU A 165 79.329 13.660 -6.192 1.00 20.20 C ANISOU 315 CG GLU A 165 2835 1932 2910 242 -312 35 C ATOM 316 CD GLU A 165 80.387 13.882 -5.126 1.00 22.69 C ANISOU 316 CD GLU A 165 3122 2274 3226 271 -349 64 C ATOM 317 OE1 GLU A 165 80.722 12.916 -4.409 1.00 22.00 O ANISOU 317 OE1 GLU A 165 3065 2125 3168 304 -412 98 O ATOM 318 OE2 GLU A 165 80.887 15.022 -5.011 1.00 20.86 O ANISOU 318 OE2 GLU A 165 2838 2122 2966 260 -320 55 O ATOM 319 N GLN A 166 78.205 9.559 -8.037 1.00 20.09 N ANISOU 319 N GLN A 166 2973 1611 3047 319 -417 -47 N ATOM 320 CA GLN A 166 78.512 8.238 -8.570 1.00 22.49 C ANISOU 320 CA GLN A 166 3311 1816 3419 383 -468 -95 C ATOM 321 C GLN A 166 77.941 8.060 -9.973 1.00 21.95 C ANISOU 321 C GLN A 166 3247 1742 3350 380 -435 -176 C ATOM 322 O GLN A 166 78.540 7.394 -10.815 1.00 21.93 O ANISOU 322 O GLN A 166 3237 1708 3386 455 -450 -258 O ATOM 323 CB GLN A 166 77.981 7.145 -7.639 1.00 25.97 C ANISOU 323 CB GLN A 166 3830 2139 3897 355 -539 -20 C ATOM 324 CG GLN A 166 78.757 7.023 -6.335 1.00 31.98 C ANISOU 324 CG GLN A 166 4591 2897 4665 379 -586 51 C ATOM 325 CD GLN A 166 78.337 5.817 -5.515 1.00 33.99 C ANISOU 325 CD GLN A 166 4901 3080 4934 344 -634 122 C ATOM 326 OE1 GLN A 166 77.324 5.178 -5.801 1.00 35.57 O ANISOU 326 OE1 GLN A 166 5140 3237 5136 287 -629 130 O ATOM 327 NE2 GLN A 166 79.118 5.499 -4.490 1.00 33.29 N ANISOU 327 NE2 GLN A 166 4813 2980 4854 377 -683 174 N ATOM 328 N ALA A 167 76.783 8.662 -10.220 1.00 21.43 N ANISOU 328 N ALA A 167 3192 1714 3239 296 -393 -156 N ATOM 329 CA ALA A 167 76.153 8.587 -11.531 1.00 20.23 C ANISOU 329 CA ALA A 167 3043 1567 3075 285 -364 -226 C ATOM 330 C ALA A 167 76.861 9.500 -12.533 1.00 19.58 C ANISOU 330 C ALA A 167 2891 1596 2954 325 -302 -296 C ATOM 331 O ALA A 167 76.575 9.464 -13.729 1.00 20.36 O ANISOU 331 O ALA A 167 2985 1715 3036 330 -277 -364 O ATOM 332 CB ALA A 167 74.679 8.946 -11.431 1.00 18.97 C ANISOU 332 CB ALA A 167 2912 1416 2881 184 -344 -177 C ATOM 333 N GLY A 168 77.782 10.321 -12.036 1.00 16.99 N ANISOU 333 N GLY A 168 2508 1341 2608 347 -281 -275 N ATOM 334 CA GLY A 168 78.560 11.202 -12.891 1.00 17.48 C ANISOU 334 CA GLY A 168 2499 1510 2634 378 -224 -329 C ATOM 335 C GLY A 168 77.828 12.465 -13.306 1.00 18.76 C ANISOU 335 C GLY A 168 2641 1756 2732 307 -164 -310 C ATOM 336 O GLY A 168 78.168 13.082 -14.316 1.00 18.40 O ANISOU 336 O GLY A 168 2551 1789 2652 318 -116 -357 O ATOM 337 N AARG A 169 76.821 12.854 -12.530 0.61 17.17 N ANISOU 337 N AARG A 169 2471 1539 2513 234 -168 -239 N ATOM 338 N BARG A 169 76.827 12.851 -12.521 0.39 17.16 N ANISOU 338 N BARG A 169 2470 1538 2512 235 -168 -239 N ATOM 339 CA AARG A 169 76.041 14.046 -12.844 0.61 15.90 C ANISOU 339 CA AARG A 169 2295 1448 2299 171 -119 -219 C ATOM 340 CA BARG A 169 76.021 14.028 -12.822 0.39 15.65 C ANISOU 340 CA BARG A 169 2264 1414 2267 171 -120 -218 C ATOM 341 C AARG A 169 76.499 15.252 -12.024 0.61 15.66 C ANISOU 341 C AARG A 169 2226 1481 2244 152 -98 -171 C ATOM 342 C BARG A 169 76.473 15.245 -12.015 0.39 15.56 C ANISOU 342 C BARG A 169 2214 1467 2230 151 -98 -171 C ATOM 343 O AARG A 169 76.432 16.390 -12.489 0.61 15.77 O ANISOU 343 O AARG A 169 2207 1566 2219 126 -55 -172 O ATOM 344 O BARG A 169 76.374 16.380 -12.479 0.39 15.61 O ANISOU 344 O BARG A 169 2189 1544 2199 124 -55 -171 O ATOM 345 CB AARG A 169 74.549 13.789 -12.608 0.61 13.86 C ANISOU 345 CB AARG A 169 2087 1144 2035 105 -132 -182 C ATOM 346 CB BARG A 169 74.541 13.745 -12.548 0.39 13.87 C ANISOU 346 CB BARG A 169 2091 1142 2039 105 -135 -179 C ATOM 347 CG AARG A 169 74.011 12.538 -13.294 0.61 15.62 C ANISOU 347 CG AARG A 169 2355 1291 2289 113 -164 -224 C ATOM 348 CG BARG A 169 73.987 12.510 -13.250 0.39 15.48 C ANISOU 348 CG BARG A 169 2339 1270 2273 111 -166 -222 C ATOM 349 CD AARG A 169 74.255 12.559 -14.801 0.61 16.05 C ANISOU 349 CD AARG A 169 2389 1385 2324 147 -137 -308 C ATOM 350 CD BARG A 169 73.887 12.702 -14.758 0.39 15.87 C ANISOU 350 CD BARG A 169 2371 1365 2294 125 -134 -295 C ATOM 351 NE AARG A 169 73.525 13.629 -15.476 0.61 16.82 N ANISOU 351 NE AARG A 169 2465 1558 2366 99 -92 -303 N ATOM 352 NE BARG A 169 75.180 12.585 -15.426 0.39 17.07 N ANISOU 352 NE BARG A 169 2486 1550 2450 201 -121 -360 N ATOM 353 CZ AARG A 169 73.519 13.812 -16.795 0.61 16.83 C ANISOU 353 CZ AARG A 169 2451 1608 2334 112 -66 -363 C ATOM 354 CZ BARG A 169 75.709 11.435 -15.832 0.39 19.40 C ANISOU 354 CZ BARG A 169 2797 1787 2785 264 -153 -423 C ATOM 355 NH1AARG A 169 74.201 12.993 -17.581 0.61 16.20 N ANISOU 355 NH1AARG A 169 2372 1515 2268 173 -74 -439 N ATOM 356 NH1BARG A 169 76.890 11.419 -16.434 0.39 20.06 N ANISOU 356 NH1BARG A 169 2836 1918 2867 336 -134 -485 N ATOM 357 NH2AARG A 169 72.830 14.811 -17.328 0.61 10.91 N ANISOU 357 NH2AARG A 169 1687 924 1535 68 -32 -347 N ATOM 358 NH2BARG A 169 75.059 10.298 -15.630 0.39 22.68 N ANISOU 358 NH2BARG A 169 3274 2098 3246 254 -206 -424 N ATOM 359 N LEU A 170 76.966 14.999 -10.805 1.00 13.33 N ANISOU 359 N LEU A 170 1938 1158 1971 163 -133 -129 N ATOM 360 CA LEU A 170 77.388 16.075 -9.914 1.00 12.58 C ANISOU 360 CA LEU A 170 1811 1117 1853 144 -123 -88 C ATOM 361 C LEU A 170 78.898 16.078 -9.681 1.00 12.31 C ANISOU 361 C LEU A 170 1728 1109 1841 202 -136 -106 C ATOM 362 O LEU A 170 79.495 15.042 -9.393 1.00 15.20 O ANISOU 362 O LEU A 170 2104 1424 2247 255 -180 -115 O ATOM 363 CB LEU A 170 76.652 15.969 -8.576 1.00 14.81 C ANISOU 363 CB LEU A 170 2134 1365 2126 100 -150 -21 C ATOM 364 CG LEU A 170 76.953 16.997 -7.482 1.00 15.21 C ANISOU 364 CG LEU A 170 2163 1465 2149 77 -147 20 C ATOM 365 CD1 LEU A 170 76.558 18.402 -7.915 1.00 14.14 C ANISOU 365 CD1 LEU A 170 2001 1396 1978 39 -98 11 C ATOM 366 CD2 LEU A 170 76.243 16.614 -6.191 1.00 15.27 C ANISOU 366 CD2 LEU A 170 2217 1440 2144 42 -177 82 C ATOM 367 N ASN A 171 79.501 17.257 -9.821 1.00 11.76 N ANISOU 367 N ASN A 171 1603 1116 1747 191 -102 -111 N ATOM 368 CA ASN A 171 80.923 17.462 -9.547 1.00 14.66 C ANISOU 368 CA ASN A 171 1912 1525 2132 234 -112 -124 C ATOM 369 C ASN A 171 81.869 16.724 -10.493 1.00 21.56 C ANISOU 369 C ASN A 171 2746 2409 3035 305 -108 -188 C ATOM 370 O ASN A 171 83.031 16.488 -10.154 1.00 22.09 O ANISOU 370 O ASN A 171 2769 2494 3131 357 -131 -201 O ATOM 371 CB ASN A 171 81.235 17.067 -8.101 1.00 15.95 C ANISOU 371 CB ASN A 171 2094 1653 2313 245 -168 -78 C ATOM 372 CG ASN A 171 80.586 17.998 -7.097 1.00 13.42 C ANISOU 372 CG ASN A 171 1794 1349 1955 181 -166 -25 C ATOM 373 OD1 ASN A 171 80.468 19.201 -7.338 1.00 12.96 O ANISOU 373 OD1 ASN A 171 1710 1345 1869 142 -128 -27 O ATOM 374 ND2 ASN A 171 80.154 17.448 -5.968 1.00 11.80 N ANISOU 374 ND2 ASN A 171 1637 1100 1748 170 -208 23 N ATOM 375 N TRP A 172 81.381 16.373 -11.680 1.00 20.05 N ANISOU 375 N TRP A 172 2569 2214 2835 311 -80 -232 N ATOM 376 CA TRP A 172 82.245 15.781 -12.697 1.00 21.40 C ANISOU 376 CA TRP A 172 2698 2411 3023 380 -66 -305 C ATOM 377 C TRP A 172 83.267 16.811 -13.169 1.00 21.01 C ANISOU 377 C TRP A 172 2564 2470 2950 378 -19 -321 C ATOM 378 O TRP A 172 84.337 16.462 -13.668 1.00 20.22 O ANISOU 378 O TRP A 172 2404 2412 2866 439 -10 -373 O ATOM 379 CB TRP A 172 81.425 15.261 -13.884 1.00 20.00 C ANISOU 379 CB TRP A 172 2557 2213 2829 380 -46 -353 C ATOM 380 CG TRP A 172 80.568 16.304 -14.539 1.00 14.98 C ANISOU 380 CG TRP A 172 1927 1628 2138 309 2 -335 C ATOM 381 CD1 TRP A 172 79.243 16.532 -14.316 1.00 11.26 C ANISOU 381 CD1 TRP A 172 1510 1119 1649 248 -3 -294 C ATOM 382 CD2 TRP A 172 80.978 17.257 -15.530 1.00 15.65 C ANISOU 382 CD2 TRP A 172 1957 1810 2177 293 60 -355 C ATOM 383 NE1 TRP A 172 78.800 17.569 -15.103 1.00 13.84 N ANISOU 383 NE1 TRP A 172 1823 1510 1927 201 44 -289 N ATOM 384 CE2 TRP A 172 79.847 18.033 -15.858 1.00 15.12 C ANISOU 384 CE2 TRP A 172 1922 1753 2070 225 81 -321 C ATOM 385 CE3 TRP A 172 82.191 17.531 -16.171 1.00 17.68 C ANISOU 385 CE3 TRP A 172 2140 2153 2425 328 95 -393 C ATOM 386 CZ2 TRP A 172 79.892 19.062 -16.796 1.00 14.27 C ANISOU 386 CZ2 TRP A 172 1782 1727 1912 191 131 -320 C ATOM 387 CZ3 TRP A 172 82.234 18.556 -17.103 1.00 20.33 C ANISOU 387 CZ3 TRP A 172 2440 2577 2706 286 151 -390 C ATOM 388 CH2 TRP A 172 81.092 19.307 -17.407 1.00 16.19 C ANISOU 388 CH2 TRP A 172 1957 2050 2143 218 166 -351 C ATOM 389 N TRP A 173 82.925 18.082 -12.986 1.00 18.21 N ANISOU 389 N TRP A 173 2202 2158 2560 306 9 -275 N ATOM 390 CA TRP A 173 83.730 19.199 -13.472 1.00 19.82 C ANISOU 390 CA TRP A 173 2332 2459 2739 283 54 -277 C ATOM 391 C TRP A 173 84.975 19.467 -12.633 1.00 22.14 C ANISOU 391 C TRP A 173 2564 2787 3062 303 32 -265 C ATOM 392 O TRP A 173 85.914 20.115 -13.094 1.00 22.24 O ANISOU 392 O TRP A 173 2501 2884 3067 298 66 -279 O ATOM 393 CB TRP A 173 82.874 20.463 -13.520 1.00 18.61 C ANISOU 393 CB TRP A 173 2202 2322 2546 200 80 -229 C ATOM 394 CG TRP A 173 82.086 20.687 -12.263 1.00 20.13 C ANISOU 394 CG TRP A 173 2447 2454 2746 164 43 -177 C ATOM 395 CD1 TRP A 173 82.532 21.258 -11.106 1.00 24.43 C ANISOU 395 CD1 TRP A 173 2978 3003 3302 147 17 -142 C ATOM 396 CD2 TRP A 173 80.713 20.343 -12.036 1.00 19.39 C ANISOU 396 CD2 TRP A 173 2427 2297 2643 141 29 -157 C ATOM 397 NE1 TRP A 173 81.522 21.291 -10.173 1.00 23.59 N ANISOU 397 NE1 TRP A 173 2931 2843 3188 117 -9 -104 N ATOM 398 CE2 TRP A 173 80.394 20.734 -10.720 1.00 19.67 C ANISOU 398 CE2 TRP A 173 2486 2307 2681 111 0 -110 C ATOM 399 CE3 TRP A 173 79.722 19.739 -12.817 1.00 16.66 C ANISOU 399 CE3 TRP A 173 2124 1919 2286 139 38 -177 C ATOM 400 CZ2 TRP A 173 79.128 20.547 -10.168 1.00 19.87 C ANISOU 400 CZ2 TRP A 173 2571 2282 2695 81 -15 -80 C ATOM 401 CZ3 TRP A 173 78.464 19.554 -12.269 1.00 17.07 C ANISOU 401 CZ3 TRP A 173 2235 1917 2334 105 19 -145 C ATOM 402 CH2 TRP A 173 78.178 19.956 -10.956 1.00 18.04 C ANISOU 402 CH2 TRP A 173 2375 2021 2457 77 -4 -96 C ATOM 403 N VAL A 174 84.973 18.979 -11.398 1.00 24.77 N ANISOU 403 N VAL A 174 2927 3060 3426 321 -25 -237 N ATOM 404 CA VAL A 174 86.067 19.236 -10.469 1.00 29.45 C ANISOU 404 CA VAL A 174 3465 3680 4043 336 -57 -222 C ATOM 405 C VAL A 174 87.417 18.808 -11.042 1.00 35.32 C ANISOU 405 C VAL A 174 4121 4484 4814 405 -48 -276 C ATOM 406 O VAL A 174 88.434 19.462 -10.810 1.00 36.77 O ANISOU 406 O VAL A 174 4229 4737 5005 398 -45 -273 O ATOM 407 CB VAL A 174 85.833 18.519 -9.126 1.00 29.72 C ANISOU 407 CB VAL A 174 3553 3638 4102 357 -127 -185 C ATOM 408 CG1 VAL A 174 87.027 18.709 -8.205 1.00 31.55 C ANISOU 408 CG1 VAL A 174 3726 3904 4357 380 -167 -173 C ATOM 409 CG2 VAL A 174 84.561 19.038 -8.469 1.00 26.87 C ANISOU 409 CG2 VAL A 174 3265 3237 3708 286 -130 -132 C ATOM 410 N SER A 175 87.418 17.723 -11.809 1.00 39.44 N ANISOU 410 N SER A 175 4652 4983 5352 471 -45 -331 N ATOM 411 CA SER A 175 88.654 17.187 -12.372 1.00 45.49 C ANISOU 411 CA SER A 175 5334 5806 6146 551 -36 -395 C ATOM 412 C SER A 175 89.103 17.917 -13.642 1.00 47.17 C ANISOU 412 C SER A 175 5474 6131 6318 528 42 -430 C ATOM 413 O SER A 175 90.299 18.130 -13.848 1.00 53.30 O ANISOU 413 O SER A 175 6152 6995 7105 555 61 -457 O ATOM 414 CB SER A 175 88.495 15.691 -12.663 1.00 48.41 C ANISOU 414 CB SER A 175 5744 6098 6551 639 -69 -448 C ATOM 415 OG SER A 175 87.366 15.442 -13.482 1.00 49.38 O ANISOU 415 OG SER A 175 5935 6182 6644 614 -43 -465 O ATOM 416 N VAL A 176 88.152 18.302 -14.488 1.00 43.24 N ANISOU 416 N VAL A 176 5021 5637 5772 476 87 -427 N ATOM 417 CA VAL A 176 88.486 18.923 -15.768 1.00 41.83 C ANISOU 417 CA VAL A 176 4784 5565 5545 453 161 -455 C ATOM 418 C VAL A 176 88.617 20.442 -15.666 1.00 38.48 C ANISOU 418 C VAL A 176 4326 5204 5091 357 192 -393 C ATOM 419 O VAL A 176 89.122 21.090 -16.583 1.00 36.71 O ANISOU 419 O VAL A 176 4039 5078 4830 328 250 -400 O ATOM 420 CB VAL A 176 87.438 18.588 -16.848 1.00 40.83 C ANISOU 420 CB VAL A 176 4719 5419 5375 446 191 -484 C ATOM 421 CG1 VAL A 176 87.361 17.084 -17.063 1.00 40.64 C ANISOU 421 CG1 VAL A 176 4726 5330 5384 539 159 -555 C ATOM 422 CG2 VAL A 176 86.077 19.151 -16.466 1.00 39.57 C ANISOU 422 CG2 VAL A 176 4648 5192 5196 369 177 -420 C ATOM 423 N ASP A 177 88.155 21.005 -14.554 1.00 32.82 N ANISOU 423 N ASP A 177 3653 4428 4389 308 152 -331 N ATOM 424 CA ASP A 177 88.279 22.438 -14.311 1.00 30.78 C ANISOU 424 CA ASP A 177 3371 4211 4113 221 168 -276 C ATOM 425 C ASP A 177 88.768 22.692 -12.887 1.00 29.72 C ANISOU 425 C ASP A 177 3224 4050 4018 214 112 -244 C ATOM 426 O ASP A 177 87.974 22.717 -11.944 1.00 24.68 O ANISOU 426 O ASP A 177 2657 3334 3385 197 71 -211 O ATOM 427 CB ASP A 177 86.944 23.146 -14.556 1.00 30.23 C ANISOU 427 CB ASP A 177 3381 4100 4006 152 182 -235 C ATOM 428 CG ASP A 177 86.993 24.624 -14.211 1.00 33.61 C ANISOU 428 CG ASP A 177 3797 4549 4426 66 188 -179 C ATOM 429 OD1 ASP A 177 88.100 25.207 -14.207 1.00 33.83 O ANISOU 429 OD1 ASP A 177 3745 4645 4464 45 200 -174 O ATOM 430 OD2 ASP A 177 85.920 25.206 -13.946 1.00 34.78 O ANISOU 430 OD2 ASP A 177 4012 4642 4559 20 178 -143 O ATOM 431 N PRO A 178 90.087 22.882 -12.735 1.00 31.68 N ANISOU 431 N PRO A 178 3376 4370 4290 228 111 -257 N ATOM 432 CA PRO A 178 90.776 23.036 -11.447 1.00 31.97 C ANISOU 432 CA PRO A 178 3384 4399 4364 231 53 -237 C ATOM 433 C PRO A 178 90.239 24.177 -10.583 1.00 30.50 C ANISOU 433 C PRO A 178 3243 4178 4168 148 30 -181 C ATOM 434 O PRO A 178 90.380 24.124 -9.363 1.00 32.44 O ANISOU 434 O PRO A 178 3502 4389 4433 155 -28 -164 O ATOM 435 CB PRO A 178 92.226 23.318 -11.859 1.00 33.44 C ANISOU 435 CB PRO A 178 3444 4695 4566 239 78 -261 C ATOM 436 CG PRO A 178 92.357 22.713 -13.212 1.00 32.10 C ANISOU 436 CG PRO A 178 3243 4579 4377 284 137 -313 C ATOM 437 CD PRO A 178 91.027 22.925 -13.868 1.00 31.57 C ANISOU 437 CD PRO A 178 3267 4464 4263 242 169 -295 C ATOM 438 N THR A 179 89.637 25.188 -11.202 1.00 30.17 N ANISOU 438 N THR A 179 3224 4146 4094 74 72 -155 N ATOM 439 CA THR A 179 89.164 26.353 -10.460 1.00 30.40 C ANISOU 439 CA THR A 179 3291 4141 4116 -2 51 -111 C ATOM 440 C THR A 179 87.674 26.271 -10.152 1.00 29.96 C ANISOU 440 C THR A 179 3343 4002 4039 -10 40 -93 C ATOM 441 O THR A 179 87.075 27.239 -9.685 1.00 32.83 O ANISOU 441 O THR A 179 3746 4334 4393 -67 29 -64 O ATOM 442 CB THR A 179 89.448 27.665 -11.221 1.00 33.96 C ANISOU 442 CB THR A 179 3702 4646 4554 -84 93 -87 C ATOM 443 OG1 THR A 179 88.855 27.607 -12.524 1.00 36.94 O ANISOU 443 OG1 THR A 179 4100 5039 4896 -90 149 -89 O ATOM 444 CG2 THR A 179 90.946 27.883 -11.358 1.00 34.52 C ANISOU 444 CG2 THR A 179 3660 4808 4649 -91 101 -98 C ATOM 445 N SER A 180 87.077 25.115 -10.420 1.00 25.55 N ANISOU 445 N SER A 180 2827 3405 3475 46 41 -114 N ATOM 446 CA SER A 180 85.701 24.867 -10.013 1.00 23.09 C ANISOU 446 CA SER A 180 2607 3017 3147 41 26 -97 C ATOM 447 C SER A 180 85.689 24.275 -8.607 1.00 23.12 C ANISOU 447 C SER A 180 2641 2975 3167 70 -34 -85 C ATOM 448 O SER A 180 86.708 23.773 -8.129 1.00 23.31 O ANISOU 448 O SER A 180 2620 3019 3219 112 -66 -97 O ATOM 449 CB SER A 180 84.998 23.930 -10.996 1.00 23.55 C ANISOU 449 CB SER A 180 2701 3056 3192 77 52 -121 C ATOM 450 OG SER A 180 85.573 22.637 -10.965 1.00 27.16 O ANISOU 450 OG SER A 180 3141 3503 3675 152 31 -156 O ATOM 451 N GLN A 181 84.539 24.339 -7.946 1.00 21.52 N ANISOU 451 N GLN A 181 2513 2718 2947 48 -50 -61 N ATOM 452 CA GLN A 181 84.410 23.818 -6.590 1.00 20.48 C ANISOU 452 CA GLN A 181 2416 2548 2817 67 -104 -41 C ATOM 453 C GLN A 181 83.487 22.606 -6.549 1.00 17.34 C ANISOU 453 C GLN A 181 2082 2089 2416 97 -115 -35 C ATOM 454 O GLN A 181 82.551 22.501 -7.342 1.00 15.74 O ANISOU 454 O GLN A 181 1913 1867 2200 84 -81 -41 O ATOM 455 CB GLN A 181 83.877 24.895 -5.636 1.00 20.52 C ANISOU 455 CB GLN A 181 2451 2547 2797 12 -118 -17 C ATOM 456 CG GLN A 181 84.556 26.251 -5.748 1.00 27.53 C ANISOU 456 CG GLN A 181 3290 3480 3691 -34 -108 -21 C ATOM 457 CD GLN A 181 84.011 27.087 -6.894 1.00 32.74 C ANISOU 457 CD GLN A 181 3953 4146 4341 -75 -57 -22 C ATOM 458 OE1 GLN A 181 82.928 26.815 -7.417 1.00 31.26 O ANISOU 458 OE1 GLN A 181 3812 3928 4136 -74 -33 -18 O ATOM 459 NE2 GLN A 181 84.763 28.107 -7.293 1.00 35.17 N ANISOU 459 NE2 GLN A 181 4210 4492 4661 -115 -44 -22 N ATOM 460 N ARG A 182 83.754 21.688 -5.626 1.00 16.17 N ANISOU 460 N ARG A 182 1951 1911 2281 136 -165 -21 N ATOM 461 CA ARG A 182 82.799 20.629 -5.332 1.00 17.52 C ANISOU 461 CA ARG A 182 2192 2016 2449 149 -184 -1 C ATOM 462 C ARG A 182 81.518 21.269 -4.806 1.00 16.55 C ANISOU 462 C ARG A 182 2121 1882 2284 89 -170 29 C ATOM 463 O ARG A 182 81.565 22.112 -3.909 1.00 17.59 O ANISOU 463 O ARG A 182 2251 2039 2393 59 -182 46 O ATOM 464 CB ARG A 182 83.365 19.637 -4.310 1.00 15.21 C ANISOU 464 CB ARG A 182 1911 1693 2176 194 -248 22 C ATOM 465 CG ARG A 182 82.469 18.430 -4.053 1.00 18.35 C ANISOU 465 CG ARG A 182 2381 2015 2577 204 -273 50 C ATOM 466 CD ARG A 182 82.964 17.587 -2.877 1.00 22.24 C ANISOU 466 CD ARG A 182 2894 2475 3082 238 -343 89 C ATOM 467 NE ARG A 182 82.346 16.262 -2.858 1.00 25.18 N ANISOU 467 NE ARG A 182 3329 2764 3474 256 -372 113 N ATOM 468 CZ ARG A 182 82.366 15.436 -1.816 1.00 26.36 C ANISOU 468 CZ ARG A 182 3521 2867 3626 269 -433 166 C ATOM 469 NH1 ARG A 182 82.967 15.797 -0.690 1.00 27.27 N ANISOU 469 NH1 ARG A 182 3623 3019 3718 269 -472 198 N ATOM 470 NH2 ARG A 182 81.779 14.249 -1.897 1.00 24.82 N ANISOU 470 NH2 ARG A 182 3386 2589 3457 278 -459 189 N ATOM 471 N LEU A 183 80.381 20.886 -5.372 1.00 16.25 N ANISOU 471 N LEU A 183 2126 1810 2239 74 -146 31 N ATOM 472 CA LEU A 183 79.097 21.411 -4.922 1.00 9.73 C ANISOU 472 CA LEU A 183 1343 978 1376 23 -131 56 C ATOM 473 C LEU A 183 78.357 20.378 -4.078 1.00 14.62 C ANISOU 473 C LEU A 183 2017 1551 1986 20 -161 94 C ATOM 474 O LEU A 183 78.375 19.186 -4.387 1.00 14.60 O ANISOU 474 O LEU A 183 2035 1501 2011 49 -180 96 O ATOM 475 CB LEU A 183 78.238 21.835 -6.117 1.00 8.92 C ANISOU 475 CB LEU A 183 1244 879 1267 0 -83 36 C ATOM 476 CG LEU A 183 78.865 22.873 -7.049 1.00 13.25 C ANISOU 476 CG LEU A 183 1744 1473 1819 -7 -51 9 C ATOM 477 CD1 LEU A 183 77.875 23.304 -8.124 1.00 13.95 C ANISOU 477 CD1 LEU A 183 1844 1562 1892 -33 -12 0 C ATOM 478 CD2 LEU A 183 79.366 24.071 -6.253 1.00 15.27 C ANISOU 478 CD2 LEU A 183 1975 1761 2064 -32 -60 17 C ATOM 479 N LEU A 184 77.709 20.838 -3.013 1.00 16.98 N ANISOU 479 N LEU A 184 2340 1865 2246 -16 -166 125 N ATOM 480 CA LEU A 184 77.020 19.935 -2.096 1.00 14.80 C ANISOU 480 CA LEU A 184 2114 1558 1951 -30 -192 172 C ATOM 481 C LEU A 184 75.568 20.347 -1.858 1.00 10.84 C ANISOU 481 C LEU A 184 1638 1071 1410 -81 -159 187 C ATOM 482 O LEU A 184 75.263 21.533 -1.744 1.00 10.74 O ANISOU 482 O LEU A 184 1609 1102 1372 -102 -132 169 O ATOM 483 CB LEU A 184 77.767 19.866 -0.764 1.00 17.65 C ANISOU 483 CB LEU A 184 2478 1937 2292 -19 -238 203 C ATOM 484 CG LEU A 184 79.243 19.467 -0.840 1.00 22.30 C ANISOU 484 CG LEU A 184 3033 2519 2921 36 -279 190 C ATOM 485 CD1 LEU A 184 80.120 20.678 -1.124 1.00 20.94 C ANISOU 485 CD1 LEU A 184 2801 2401 2753 39 -263 148 C ATOM 486 CD2 LEU A 184 79.678 18.771 0.439 1.00 26.66 C ANISOU 486 CD2 LEU A 184 3611 3061 3458 50 -340 239 C ATOM 487 N PRO A 185 74.665 19.357 -1.781 1.00 11.25 N ANISOU 487 N PRO A 185 1730 1085 1461 -101 -164 220 N ATOM 488 CA PRO A 185 73.237 19.607 -1.562 1.00 12.36 C ANISOU 488 CA PRO A 185 1887 1245 1566 -151 -132 236 C ATOM 489 C PRO A 185 72.886 19.830 -0.091 1.00 13.25 C ANISOU 489 C PRO A 185 2015 1399 1621 -179 -139 276 C ATOM 490 O PRO A 185 73.178 18.981 0.752 1.00 11.63 O ANISOU 490 O PRO A 185 1838 1176 1405 -180 -177 324 O ATOM 491 CB PRO A 185 72.582 18.330 -2.088 1.00 10.62 C ANISOU 491 CB PRO A 185 1697 964 1374 -164 -141 257 C ATOM 492 CG PRO A 185 73.598 17.272 -1.830 1.00 12.90 C ANISOU 492 CG PRO A 185 2006 1201 1696 -127 -193 277 C ATOM 493 CD PRO A 185 74.947 17.930 -2.015 1.00 11.94 C ANISOU 493 CD PRO A 185 1844 1105 1588 -77 -200 239 C ATOM 494 N LEU A 186 72.265 20.968 0.203 1.00 11.57 N ANISOU 494 N LEU A 186 1784 1241 1369 -200 -106 255 N ATOM 495 CA LEU A 186 71.809 21.273 1.552 1.00 14.66 C ANISOU 495 CA LEU A 186 2187 1687 1697 -226 -104 280 C ATOM 496 C LEU A 186 70.583 20.443 1.913 1.00 19.68 C ANISOU 496 C LEU A 186 2848 2324 2306 -272 -90 329 C ATOM 497 O LEU A 186 69.688 20.256 1.090 1.00 17.89 O ANISOU 497 O LEU A 186 2616 2081 2102 -291 -64 321 O ATOM 498 CB LEU A 186 71.484 22.762 1.685 1.00 15.94 C ANISOU 498 CB LEU A 186 2322 1903 1831 -227 -72 231 C ATOM 499 CG LEU A 186 72.622 23.734 1.378 1.00 16.08 C ANISOU 499 CG LEU A 186 2314 1922 1874 -196 -85 186 C ATOM 500 CD1 LEU A 186 72.122 25.169 1.414 1.00 15.95 C ANISOU 500 CD1 LEU A 186 2278 1941 1840 -200 -57 138 C ATOM 501 CD2 LEU A 186 73.762 23.529 2.368 1.00 17.99 C ANISOU 501 CD2 LEU A 186 2562 2175 2097 -181 -131 203 C ATOM 502 N ALA A 187 70.549 19.947 3.144 1.00 22.39 N ANISOU 502 N ALA A 187 3217 2692 2600 -293 -110 382 N ATOM 503 CA ALA A 187 69.388 19.217 3.638 1.00 29.39 C ANISOU 503 CA ALA A 187 4123 3593 3451 -348 -94 437 C ATOM 504 C ALA A 187 68.216 20.176 3.834 1.00 36.46 C ANISOU 504 C ALA A 187 4988 4565 4301 -373 -38 406 C ATOM 505 O ALA A 187 68.411 21.325 4.230 1.00 36.12 O ANISOU 505 O ALA A 187 4923 4575 4226 -352 -24 360 O ATOM 506 CB ALA A 187 69.719 18.502 4.937 1.00 30.87 C ANISOU 506 CB ALA A 187 4346 3794 3588 -367 -131 508 C ATOM 507 N THR A 188 67.003 19.710 3.549 1.00 47.20 N ANISOU 507 N THR A 188 6342 5930 5661 -418 -9 429 N ATOM 508 CA THR A 188 65.813 20.540 3.726 1.00 59.73 C ANISOU 508 CA THR A 188 7892 7595 7208 -438 44 399 C ATOM 509 C THR A 188 65.405 20.628 5.197 1.00 75.02 C ANISOU 509 C THR A 188 9831 9620 9054 -469 60 432 C ATOM 510 O THR A 188 65.578 19.674 5.955 1.00 77.62 O ANISOU 510 O THR A 188 10194 9946 9352 -502 37 505 O ATOM 511 CB THR A 188 64.620 20.006 2.908 1.00 56.76 C ANISOU 511 CB THR A 188 7500 7202 6864 -478 68 411 C ATOM 512 OG1 THR A 188 63.508 20.902 3.039 1.00 54.54 O ANISOU 512 OG1 THR A 188 7172 7001 6549 -486 118 374 O ATOM 513 CG2 THR A 188 64.211 18.622 3.396 1.00 57.09 C ANISOU 513 CG2 THR A 188 7572 7224 6894 -540 53 495 C ATOM 514 N THR A 189 64.867 21.778 5.594 1.00 89.50 N ANISOU 514 N THR A 189 11629 11534 10842 -456 100 378 N ATOM 515 CA THR A 189 64.407 21.975 6.968 1.00 89.76 C ANISOU 515 CA THR A 189 11657 11668 10778 -481 124 395 C ATOM 516 C THR A 189 62.933 22.379 7.015 1.00 87.34 C ANISOU 516 C THR A 189 11302 11442 10441 -506 185 372 C ATOM 517 O THR A 189 62.439 23.076 6.126 1.00 89.18 O ANISOU 517 O THR A 189 11500 11664 10721 -479 205 313 O ATOM 518 CB THR A 189 65.244 23.050 7.705 1.00 92.41 C ANISOU 518 CB THR A 189 11996 12044 11072 -434 110 339 C ATOM 519 OG1 THR A 189 65.031 24.333 7.102 1.00 92.91 O ANISOU 519 OG1 THR A 189 12024 12111 11167 -391 132 250 O ATOM 520 CG2 THR A 189 66.728 22.706 7.658 1.00 93.91 C ANISOU 520 CG2 THR A 189 12222 12163 11295 -408 49 358 C ATOM 521 N GLY A 190 62.232 21.935 8.052 1.00 83.38 N ANISOU 521 N GLY A 190 10795 11026 9859 -556 212 421 N ATOM 522 CA GLY A 190 60.849 22.328 8.251 1.00 75.29 C ANISOU 522 CA GLY A 190 9714 10099 8795 -579 274 398 C ATOM 523 C GLY A 190 59.835 21.510 7.475 1.00 62.65 C ANISOU 523 C GLY A 190 8089 8476 7240 -633 292 440 C ATOM 524 O GLY A 190 60.163 20.483 6.877 1.00 57.34 O ANISOU 524 O GLY A 190 7451 7710 6624 -662 255 496 O ATOM 525 N ASP A 191 58.592 21.983 7.483 1.00 57.52 N ANISOU 525 N ASP A 191 7375 7912 6569 -644 347 406 N ATOM 526 CA ASP A 191 57.478 21.255 6.885 1.00 55.27 C ANISOU 526 CA ASP A 191 7054 7620 6327 -693 362 438 C ATOM 527 C ASP A 191 57.268 21.582 5.408 1.00 53.30 C ANISOU 527 C ASP A 191 6783 7305 6163 -669 354 393 C ATOM 528 O ASP A 191 56.579 20.853 4.699 1.00 53.64 O ANISOU 528 O ASP A 191 6810 7320 6252 -717 353 425 O ATOM 529 CB ASP A 191 56.191 21.545 7.658 1.00 55.02 C ANISOU 529 CB ASP A 191 6954 7709 6244 -704 416 418 C ATOM 530 N GLY A 192 57.853 22.682 4.950 1.00 51.96 N ANISOU 530 N GLY A 192 6615 7105 6024 -590 342 315 N ATOM 531 CA GLY A 192 57.658 23.135 3.585 1.00 52.05 C ANISOU 531 CA GLY A 192 6606 7055 6114 -553 330 266 C ATOM 532 C GLY A 192 58.150 22.145 2.547 1.00 53.32 C ANISOU 532 C GLY A 192 6809 7106 6346 -576 286 306 C ATOM 533 O GLY A 192 59.009 21.306 2.829 1.00 54.17 O ANISOU 533 O GLY A 192 6970 7158 6453 -596 254 358 O ATOM 534 N ASN A 193 57.592 22.239 1.344 1.00 42.68 N ANISOU 534 N ASN A 193 5434 5726 5057 -569 282 280 N ATOM 535 CA ASN A 193 58.028 21.402 0.236 1.00 32.29 C ANISOU 535 CA ASN A 193 4154 4308 3805 -582 242 300 C ATOM 536 C ASN A 193 59.489 21.687 -0.081 1.00 22.66 C ANISOU 536 C ASN A 193 2985 3014 2611 -527 207 279 C ATOM 537 O ASN A 193 59.903 22.846 -0.098 1.00 20.23 O ANISOU 537 O ASN A 193 2667 2720 2298 -471 211 228 O ATOM 538 CB ASN A 193 57.153 21.635 -0.996 1.00 32.79 C ANISOU 538 CB ASN A 193 4177 4365 3916 -578 244 265 C ATOM 539 CG ASN A 193 57.750 21.038 -2.253 1.00 29.89 C ANISOU 539 CG ASN A 193 3848 3897 3611 -572 201 264 C ATOM 540 OD1 ASN A 193 58.552 21.676 -2.935 1.00 28.06 O ANISOU 540 OD1 ASN A 193 3634 3623 3403 -516 185 225 O ATOM 541 ND2 ASN A 193 57.366 19.807 -2.564 1.00 28.69 N ANISOU 541 ND2 ASN A 193 3710 3707 3483 -632 184 306 N ATOM 542 N CYS A 194 60.261 20.632 -0.328 1.00 17.64 N ANISOU 542 N CYS A 194 2399 2301 2004 -544 170 319 N ATOM 543 CA CYS A 194 61.712 20.744 -0.478 1.00 16.51 C ANISOU 543 CA CYS A 194 2297 2096 1880 -496 137 306 C ATOM 544 C CYS A 194 62.138 21.709 -1.581 1.00 14.84 C ANISOU 544 C CYS A 194 2072 1859 1706 -440 133 244 C ATOM 545 O CYS A 194 63.153 22.390 -1.454 1.00 14.36 O ANISOU 545 O CYS A 194 2023 1788 1645 -396 123 219 O ATOM 546 CB CYS A 194 62.323 19.370 -0.747 1.00 17.92 C ANISOU 546 CB CYS A 194 2524 2191 2095 -517 96 352 C ATOM 547 SG CYS A 194 61.629 18.516 -2.181 1.00 18.88 S ANISOU 547 SG CYS A 194 2645 2251 2279 -546 82 346 S ATOM 548 N LEU A 195 61.374 21.761 -2.666 1.00 15.36 N ANISOU 548 N LEU A 195 2115 1917 1805 -445 139 223 N ATOM 549 CA LEU A 195 61.696 22.677 -3.753 1.00 15.92 C ANISOU 549 CA LEU A 195 2176 1968 1906 -398 135 173 C ATOM 550 C LEU A 195 61.518 24.126 -3.315 1.00 16.21 C ANISOU 550 C LEU A 195 2183 2057 1919 -362 156 135 C ATOM 551 O LEU A 195 62.400 24.958 -3.515 1.00 15.66 O ANISOU 551 O LEU A 195 2123 1968 1860 -322 146 107 O ATOM 552 CB LEU A 195 60.830 22.400 -4.981 1.00 16.40 C ANISOU 552 CB LEU A 195 2218 2016 1998 -413 132 161 C ATOM 553 CG LEU A 195 60.974 23.458 -6.079 1.00 14.26 C ANISOU 553 CG LEU A 195 1933 1738 1748 -369 129 117 C ATOM 554 CD1 LEU A 195 62.380 23.441 -6.674 1.00 13.87 C ANISOU 554 CD1 LEU A 195 1917 1634 1717 -338 109 108 C ATOM 555 CD2 LEU A 195 59.921 23.281 -7.164 1.00 11.50 C ANISOU 555 CD2 LEU A 195 1558 1393 1418 -385 125 107 C ATOM 556 N LEU A 196 60.368 24.418 -2.718 1.00 14.63 N ANISOU 556 N LEU A 196 1946 1924 1691 -378 184 131 N ATOM 557 CA LEU A 196 60.052 25.775 -2.293 1.00 15.12 C ANISOU 557 CA LEU A 196 1977 2035 1734 -338 203 85 C ATOM 558 C LEU A 196 60.989 26.243 -1.182 1.00 13.36 C ANISOU 558 C LEU A 196 1778 1824 1476 -318 200 77 C ATOM 559 O LEU A 196 61.388 27.406 -1.146 1.00 13.96 O ANISOU 559 O LEU A 196 1852 1896 1557 -274 196 33 O ATOM 560 CB LEU A 196 58.594 25.861 -1.838 1.00 13.74 C ANISOU 560 CB LEU A 196 1750 1940 1533 -357 236 80 C ATOM 561 CG LEU A 196 57.572 25.507 -2.924 1.00 14.82 C ANISOU 561 CG LEU A 196 1853 2074 1704 -377 235 83 C ATOM 562 CD1 LEU A 196 56.144 25.646 -2.409 1.00 14.92 C ANISOU 562 CD1 LEU A 196 1800 2176 1691 -395 270 74 C ATOM 563 CD2 LEU A 196 57.791 26.368 -4.162 1.00 17.98 C ANISOU 563 CD2 LEU A 196 2255 2429 2148 -330 212 47 C ATOM 564 N HIS A 197 61.344 25.329 -0.284 1.00 14.47 N ANISOU 564 N HIS A 197 1942 1973 1581 -351 198 120 N ATOM 565 CA HIS A 197 62.258 25.659 0.799 1.00 15.45 C ANISOU 565 CA HIS A 197 2090 2114 1668 -335 190 116 C ATOM 566 C HIS A 197 63.628 26.035 0.245 1.00 15.93 C ANISOU 566 C HIS A 197 2179 2107 1767 -301 156 100 C ATOM 567 O HIS A 197 64.251 26.993 0.703 1.00 17.33 O ANISOU 567 O HIS A 197 2359 2293 1933 -270 148 64 O ATOM 568 CB HIS A 197 62.388 24.495 1.781 1.00 19.08 C ANISOU 568 CB HIS A 197 2574 2592 2083 -381 187 179 C ATOM 569 CG HIS A 197 63.099 24.859 3.045 1.00 26.74 C ANISOU 569 CG HIS A 197 3563 3601 2997 -368 180 175 C ATOM 570 ND1 HIS A 197 62.550 25.701 3.987 1.00 29.32 N ANISOU 570 ND1 HIS A 197 3864 4012 3265 -356 209 137 N ATOM 571 CD2 HIS A 197 64.320 24.511 3.515 1.00 30.47 C ANISOU 571 CD2 HIS A 197 4073 4043 3461 -362 144 198 C ATOM 572 CE1 HIS A 197 63.399 25.849 4.988 1.00 32.73 C ANISOU 572 CE1 HIS A 197 4322 4463 3650 -348 191 138 C ATOM 573 NE2 HIS A 197 64.481 25.137 4.727 1.00 32.49 N ANISOU 573 NE2 HIS A 197 4328 4364 3650 -351 150 178 N ATOM 574 N ALA A 198 64.086 25.283 -0.750 1.00 13.96 N ANISOU 574 N ALA A 198 1947 1796 1563 -308 136 122 N ATOM 575 CA ALA A 198 65.364 25.567 -1.391 1.00 14.15 C ANISOU 575 CA ALA A 198 1987 1765 1623 -278 109 108 C ATOM 576 C ALA A 198 65.334 26.913 -2.109 1.00 17.24 C ANISOU 576 C ALA A 198 2360 2152 2040 -247 114 60 C ATOM 577 O ALA A 198 66.345 27.609 -2.183 1.00 21.33 O ANISOU 577 O ALA A 198 2884 2648 2572 -225 97 41 O ATOM 578 CB ALA A 198 65.729 24.456 -2.367 1.00 12.29 C ANISOU 578 CB ALA A 198 1769 1473 1428 -288 92 133 C ATOM 579 N ALA A 199 64.165 27.280 -2.627 1.00 13.30 N ANISOU 579 N ALA A 199 1835 1670 1548 -247 133 45 N ATOM 580 CA ALA A 199 64.038 28.478 -3.450 1.00 14.05 C ANISOU 580 CA ALA A 199 1915 1750 1672 -217 131 9 C ATOM 581 C ALA A 199 63.690 29.729 -2.646 1.00 13.79 C ANISOU 581 C ALA A 199 1869 1750 1622 -191 138 -33 C ATOM 582 O ALA A 199 63.698 30.836 -3.183 1.00 14.33 O ANISOU 582 O ALA A 199 1931 1795 1718 -163 128 -63 O ATOM 583 CB ALA A 199 62.990 28.253 -4.534 1.00 13.76 C ANISOU 583 CB ALA A 199 1859 1712 1656 -225 138 13 C ATOM 584 N SER A 200 63.383 29.559 -1.365 1.00 12.74 N ANISOU 584 N SER A 200 1730 1668 1441 -198 152 -37 N ATOM 585 CA SER A 200 62.917 30.684 -0.556 1.00 15.63 C ANISOU 585 CA SER A 200 2080 2074 1784 -168 162 -88 C ATOM 586 C SER A 200 63.928 31.149 0.495 1.00 16.16 C ANISOU 586 C SER A 200 2170 2146 1823 -158 146 -110 C ATOM 587 O SER A 200 63.555 31.806 1.467 1.00 17.33 O ANISOU 587 O SER A 200 2309 2341 1934 -139 156 -153 O ATOM 588 CB SER A 200 61.599 30.320 0.132 1.00 14.03 C ANISOU 588 CB SER A 200 1844 1950 1538 -180 198 -90 C ATOM 589 OG SER A 200 61.758 29.188 0.972 1.00 18.54 O ANISOU 589 OG SER A 200 2427 2555 2061 -222 208 -44 O ATOM 590 N LEU A 201 65.203 30.825 0.294 1.00 15.97 N ANISOU 590 N LEU A 201 2173 2077 1816 -168 119 -86 N ATOM 591 CA LEU A 201 66.246 31.217 1.244 1.00 20.00 C ANISOU 591 CA LEU A 201 2703 2592 2304 -162 96 -104 C ATOM 592 C LEU A 201 66.375 32.733 1.390 1.00 19.61 C ANISOU 592 C LEU A 201 2652 2527 2272 -131 81 -168 C ATOM 593 O LEU A 201 66.818 33.226 2.427 1.00 20.84 O ANISOU 593 O LEU A 201 2818 2706 2395 -122 67 -202 O ATOM 594 CB LEU A 201 67.596 30.626 0.833 1.00 18.85 C ANISOU 594 CB LEU A 201 2576 2402 2185 -175 67 -68 C ATOM 595 CG LEU A 201 67.737 29.109 0.973 1.00 21.63 C ANISOU 595 CG LEU A 201 2940 2760 2520 -201 68 -10 C ATOM 596 CD1 LEU A 201 69.138 28.668 0.579 1.00 22.77 C ANISOU 596 CD1 LEU A 201 3095 2860 2695 -200 37 12 C ATOM 597 CD2 LEU A 201 67.410 28.668 2.391 1.00 22.99 C ANISOU 597 CD2 LEU A 201 3120 2994 2622 -215 75 3 C ATOM 598 N GLY A 202 65.987 33.469 0.354 1.00 17.50 N ANISOU 598 N GLY A 202 2375 2218 2055 -113 79 -183 N ATOM 599 CA GLY A 202 66.048 34.918 0.391 1.00 19.20 C ANISOU 599 CA GLY A 202 2594 2402 2299 -83 59 -239 C ATOM 600 C GLY A 202 65.013 35.516 1.325 1.00 19.63 C ANISOU 600 C GLY A 202 2633 2508 2317 -51 76 -298 C ATOM 601 O GLY A 202 65.058 36.706 1.639 1.00 19.39 O ANISOU 601 O GLY A 202 2610 2454 2303 -20 55 -358 O ATOM 602 N MET A 203 64.075 34.688 1.770 1.00 17.05 N ANISOU 602 N MET A 203 2284 2251 1942 -59 113 -284 N ATOM 603 CA MET A 203 63.043 35.133 2.700 1.00 15.99 C ANISOU 603 CA MET A 203 2126 2187 1763 -29 139 -340 C ATOM 604 C MET A 203 63.267 34.567 4.096 1.00 17.14 C ANISOU 604 C MET A 203 2279 2409 1825 -48 153 -340 C ATOM 605 O MET A 203 62.334 34.497 4.899 1.00 14.76 O ANISOU 605 O MET A 203 1951 2193 1466 -39 188 -366 O ATOM 606 CB MET A 203 61.654 34.741 2.194 1.00 15.55 C ANISOU 606 CB MET A 203 2028 2170 1710 -25 174 -327 C ATOM 607 CG MET A 203 61.086 35.686 1.151 1.00 22.69 C ANISOU 607 CG MET A 203 2917 3022 2681 15 159 -354 C ATOM 608 SD MET A 203 59.509 35.116 0.493 1.00 57.66 S ANISOU 608 SD MET A 203 7289 7501 7116 14 194 -334 S ATOM 609 CE MET A 203 60.012 33.578 -0.272 1.00 16.17 C ANISOU 609 CE MET A 203 2053 2225 1864 -54 195 -241 C ATOM 610 N TRP A 204 64.503 34.159 4.374 1.00 15.92 N ANISOU 610 N TRP A 204 2156 2231 1661 -74 125 -309 N ATOM 611 CA TRP A 204 64.879 33.692 5.702 1.00 15.09 C ANISOU 611 CA TRP A 204 2065 2192 1475 -91 126 -305 C ATOM 612 C TRP A 204 64.497 34.739 6.743 1.00 17.21 C ANISOU 612 C TRP A 204 2327 2514 1697 -53 131 -393 C ATOM 613 O TRP A 204 64.697 35.934 6.530 1.00 20.99 O ANISOU 613 O TRP A 204 2813 2943 2220 -17 105 -458 O ATOM 614 CB TRP A 204 66.381 33.392 5.768 1.00 12.54 C ANISOU 614 CB TRP A 204 1774 1825 1164 -112 82 -273 C ATOM 615 CG TRP A 204 66.802 32.690 7.029 1.00 15.67 C ANISOU 615 CG TRP A 204 2188 2287 1478 -134 77 -249 C ATOM 616 CD1 TRP A 204 66.901 31.343 7.224 1.00 15.07 C ANISOU 616 CD1 TRP A 204 2121 2234 1372 -170 83 -170 C ATOM 617 CD2 TRP A 204 67.176 33.302 8.271 1.00 17.81 C ANISOU 617 CD2 TRP A 204 2472 2609 1687 -121 59 -304 C ATOM 618 NE1 TRP A 204 67.315 31.078 8.506 1.00 15.66 N ANISOU 618 NE1 TRP A 204 2213 2370 1365 -181 69 -164 N ATOM 619 CE2 TRP A 204 67.491 32.265 9.171 1.00 19.39 C ANISOU 619 CE2 TRP A 204 2688 2866 1812 -151 55 -248 C ATOM 620 CE3 TRP A 204 67.277 34.627 8.709 1.00 17.27 C ANISOU 620 CE3 TRP A 204 2406 2537 1617 -86 41 -396 C ATOM 621 CZ2 TRP A 204 67.902 32.508 10.481 1.00 22.05 C ANISOU 621 CZ2 TRP A 204 3042 3270 2068 -149 36 -279 C ATOM 622 CZ3 TRP A 204 67.683 34.868 10.012 1.00 21.45 C ANISOU 622 CZ3 TRP A 204 2953 3129 2068 -83 22 -436 C ATOM 623 CH2 TRP A 204 67.991 33.814 10.882 1.00 20.29 C ANISOU 623 CH2 TRP A 204 2820 3050 1841 -114 21 -377 C ATOM 624 N GLY A 205 63.938 34.288 7.861 1.00 14.66 N ANISOU 624 N GLY A 205 1994 2294 1283 -62 164 -396 N ATOM 625 CA GLY A 205 63.447 35.194 8.883 1.00 16.59 C ANISOU 625 CA GLY A 205 2227 2607 1470 -23 177 -488 C ATOM 626 C GLY A 205 61.931 35.219 8.929 1.00 14.30 C ANISOU 626 C GLY A 205 1886 2392 1154 -3 234 -513 C ATOM 627 O GLY A 205 61.338 35.648 9.912 1.00 15.47 O ANISOU 627 O GLY A 205 2015 2632 1232 24 262 -578 O ATOM 628 N PHE A 206 61.307 34.756 7.852 1.00 17.79 N ANISOU 628 N PHE A 206 2303 2803 1654 -15 251 -464 N ATOM 629 CA PHE A 206 59.856 34.637 7.782 1.00 18.90 C ANISOU 629 CA PHE A 206 2386 3018 1779 -5 304 -475 C ATOM 630 C PHE A 206 59.464 33.167 7.791 1.00 18.46 C ANISOU 630 C PHE A 206 2316 3013 1685 -73 337 -377 C ATOM 631 O PHE A 206 59.805 32.422 6.873 1.00 17.55 O ANISOU 631 O PHE A 206 2218 2827 1624 -108 319 -306 O ATOM 632 CB PHE A 206 59.321 35.329 6.526 1.00 23.70 C ANISOU 632 CB PHE A 206 2971 3552 2483 35 292 -500 C ATOM 633 CG PHE A 206 59.769 36.753 6.384 1.00 30.61 C ANISOU 633 CG PHE A 206 3869 4352 3410 96 249 -583 C ATOM 634 CD1 PHE A 206 59.834 37.586 7.489 1.00 36.49 C ANISOU 634 CD1 PHE A 206 4619 5140 4106 137 247 -673 C ATOM 635 CD2 PHE A 206 60.140 37.257 5.150 1.00 36.07 C ANISOU 635 CD2 PHE A 206 4579 4930 4198 109 209 -570 C ATOM 636 CE1 PHE A 206 60.250 38.898 7.364 1.00 38.46 C ANISOU 636 CE1 PHE A 206 4893 5309 4410 190 201 -751 C ATOM 637 CE2 PHE A 206 60.558 38.568 5.018 1.00 37.92 C ANISOU 637 CE2 PHE A 206 4838 5087 4484 156 165 -638 C ATOM 638 CZ PHE A 206 60.614 39.388 6.127 1.00 38.12 C ANISOU 638 CZ PHE A 206 4870 5145 4469 196 159 -729 C ATOM 639 N HIS A 207 58.751 32.749 8.831 1.00 17.42 N ANISOU 639 N HIS A 207 2155 3003 1460 -93 384 -375 N ATOM 640 CA HIS A 207 58.466 31.331 9.033 1.00 21.03 C ANISOU 640 CA HIS A 207 2607 3510 1873 -169 411 -275 C ATOM 641 C HIS A 207 57.668 30.713 7.887 1.00 20.30 C ANISOU 641 C HIS A 207 2481 3385 1847 -196 425 -225 C ATOM 642 O HIS A 207 57.924 29.580 7.484 1.00 21.74 O ANISOU 642 O HIS A 207 2685 3528 2047 -254 413 -137 O ATOM 643 CB HIS A 207 57.714 31.118 10.347 1.00 23.65 C ANISOU 643 CB HIS A 207 2906 3993 2088 -188 466 -283 C ATOM 644 CG HIS A 207 57.587 29.680 10.736 1.00 28.01 C ANISOU 644 CG HIS A 207 3465 4591 2585 -274 486 -171 C ATOM 645 ND1 HIS A 207 56.418 28.966 10.586 1.00 31.05 N ANISOU 645 ND1 HIS A 207 3796 5043 2959 -322 534 -124 N ATOM 646 CD2 HIS A 207 58.491 28.816 11.259 1.00 29.21 C ANISOU 646 CD2 HIS A 207 3674 4728 2698 -323 457 -93 C ATOM 647 CE1 HIS A 207 56.603 27.727 11.007 1.00 29.92 C ANISOU 647 CE1 HIS A 207 3682 4899 2786 -395 527 -19 C ATOM 648 NE2 HIS A 207 57.852 27.610 11.420 1.00 31.50 N ANISOU 648 NE2 HIS A 207 3949 5062 2956 -398 486 2 N ATOM 649 N ASP A 208 56.705 31.468 7.370 1.00 22.97 N ANISOU 649 N ASP A 208 2765 3739 2224 -150 444 -286 N ATOM 650 CA ASP A 208 55.796 30.975 6.339 1.00 25.73 C ANISOU 650 CA ASP A 208 3072 4076 2630 -173 457 -249 C ATOM 651 C ASP A 208 56.295 31.235 4.923 1.00 22.21 C ANISOU 651 C ASP A 208 2652 3500 2286 -152 408 -244 C ATOM 652 O ASP A 208 55.496 31.345 3.994 1.00 17.82 O ANISOU 652 O ASP A 208 2057 2930 1783 -140 410 -249 O ATOM 653 CB ASP A 208 54.417 31.615 6.507 1.00 33.80 C ANISOU 653 CB ASP A 208 4010 5194 3638 -133 502 -316 C ATOM 654 CG ASP A 208 53.575 30.917 7.549 1.00 43.92 C ANISOU 654 CG ASP A 208 5243 6620 4825 -183 564 -289 C ATOM 655 OD1 ASP A 208 54.119 30.062 8.279 1.00 46.37 O ANISOU 655 OD1 ASP A 208 5593 6954 5072 -244 569 -223 O ATOM 656 OD2 ASP A 208 52.369 31.226 7.638 1.00 50.87 O ANISOU 656 OD2 ASP A 208 6042 7592 5692 -162 608 -331 O ATOM 657 N ARG A 209 57.609 31.329 4.754 1.00 17.92 N ANISOU 657 N ARG A 209 2174 2868 1766 -148 364 -232 N ATOM 658 CA ARG A 209 58.164 31.692 3.455 1.00 18.65 C ANISOU 658 CA ARG A 209 2292 2848 1947 -127 321 -230 C ATOM 659 C ARG A 209 57.819 30.671 2.368 1.00 17.19 C ANISOU 659 C ARG A 209 2099 2628 1804 -172 318 -163 C ATOM 660 O ARG A 209 57.531 31.050 1.235 1.00 16.24 O ANISOU 660 O ARG A 209 1966 2458 1745 -150 301 -174 O ATOM 661 CB ARG A 209 59.684 31.882 3.550 1.00 19.68 C ANISOU 661 CB ARG A 209 2484 2904 2088 -124 278 -225 C ATOM 662 CG ARG A 209 60.466 30.736 4.174 1.00 18.90 C ANISOU 662 CG ARG A 209 2422 2815 1945 -177 273 -159 C ATOM 663 CD ARG A 209 61.948 31.103 4.252 1.00 16.45 C ANISOU 663 CD ARG A 209 2160 2439 1652 -163 228 -166 C ATOM 664 NE ARG A 209 62.725 30.185 5.083 1.00 16.72 N ANISOU 664 NE ARG A 209 2226 2491 1635 -200 217 -115 N ATOM 665 CZ ARG A 209 62.881 30.317 6.398 1.00 20.24 C ANISOU 665 CZ ARG A 209 2681 3007 2004 -201 223 -132 C ATOM 666 NH1 ARG A 209 62.308 31.325 7.043 1.00 19.52 N ANISOU 666 NH1 ARG A 209 2566 2974 1876 -164 243 -208 N ATOM 667 NH2 ARG A 209 63.610 29.438 7.073 1.00 22.02 N ANISOU 667 NH2 ARG A 209 2938 3243 2186 -234 205 -76 N ATOM 668 N ASP A 210 57.823 29.387 2.715 1.00 18.58 N ANISOU 668 N ASP A 210 2285 2830 1946 -236 331 -95 N ATOM 669 CA ASP A 210 57.509 28.332 1.751 1.00 22.87 C ANISOU 669 CA ASP A 210 2826 3336 2529 -283 325 -36 C ATOM 670 C ASP A 210 56.064 28.437 1.271 1.00 22.07 C ANISOU 670 C ASP A 210 2656 3286 2443 -283 351 -52 C ATOM 671 O ASP A 210 55.776 28.303 0.077 1.00 18.17 O ANISOU 671 O ASP A 210 2154 2744 2006 -284 332 -44 O ATOM 672 CB ASP A 210 57.758 26.951 2.362 1.00 25.52 C ANISOU 672 CB ASP A 210 3187 3684 2825 -351 329 40 C ATOM 673 CG ASP A 210 59.225 26.694 2.651 1.00 31.16 C ANISOU 673 CG ASP A 210 3966 4338 3536 -349 294 63 C ATOM 674 OD1 ASP A 210 60.073 27.436 2.117 1.00 34.19 O ANISOU 674 OD1 ASP A 210 4373 4659 3960 -305 265 28 O ATOM 675 OD2 ASP A 210 59.529 25.746 3.407 1.00 35.07 O ANISOU 675 OD2 ASP A 210 4487 4847 3990 -394 292 120 O ATOM 676 N LEU A 211 55.169 28.692 2.221 1.00 21.94 N ANISOU 676 N LEU A 211 2589 3375 2373 -281 394 -78 N ATOM 677 CA LEU A 211 53.743 28.845 1.949 1.00 20.84 C ANISOU 677 CA LEU A 211 2371 3306 2242 -277 423 -100 C ATOM 678 C LEU A 211 53.454 30.059 1.073 1.00 19.98 C ANISOU 678 C LEU A 211 2239 3160 2193 -201 401 -166 C ATOM 679 O LEU A 211 52.573 30.023 0.215 1.00 21.66 O ANISOU 679 O LEU A 211 2405 3378 2446 -199 397 -166 O ATOM 680 CB LEU A 211 52.963 28.958 3.260 1.00 29.73 C ANISOU 680 CB LEU A 211 3443 4565 3288 -283 479 -122 C ATOM 681 CG LEU A 211 51.433 28.877 3.155 1.00 37.66 C ANISOU 681 CG LEU A 211 4352 5667 4291 -296 518 -134 C ATOM 682 CD1 LEU A 211 50.919 27.688 2.331 1.00 40.21 C ANISOU 682 CD1 LEU A 211 4659 5968 4649 -374 510 -61 C ATOM 683 CD2 LEU A 211 50.805 28.864 4.539 1.00 41.59 C ANISOU 683 CD2 LEU A 211 4799 6307 4695 -311 580 -148 C ATOM 684 N MET A 212 54.201 31.134 1.301 1.00 14.43 N ANISOU 684 N MET A 212 1570 2416 1496 -139 381 -218 N ATOM 685 CA MET A 212 54.031 32.367 0.545 1.00 17.47 C ANISOU 685 CA MET A 212 1944 2753 1940 -65 352 -276 C ATOM 686 C MET A 212 54.534 32.197 -0.884 1.00 18.15 C ANISOU 686 C MET A 212 2067 2736 2092 -75 307 -238 C ATOM 687 O MET A 212 53.937 32.704 -1.832 1.00 18.20 O ANISOU 687 O MET A 212 2048 2721 2147 -42 287 -253 O ATOM 688 CB MET A 212 54.756 33.519 1.240 1.00 17.99 C ANISOU 688 CB MET A 212 2043 2796 1996 -6 338 -341 C ATOM 689 CG MET A 212 54.083 33.973 2.529 1.00 20.94 C ANISOU 689 CG MET A 212 2372 3278 2307 25 381 -404 C ATOM 690 SD MET A 212 54.941 35.358 3.297 1.00 62.70 S ANISOU 690 SD MET A 212 7705 8529 7589 96 355 -492 S ATOM 691 CE MET A 212 56.411 34.546 3.907 1.00 24.73 C ANISOU 691 CE MET A 212 2971 3693 2734 31 343 -433 C ATOM 692 N LEU A 213 55.634 31.469 -1.032 1.00 17.80 N ANISOU 692 N LEU A 213 2083 2635 2046 -118 291 -188 N ATOM 693 CA LEU A 213 56.187 31.197 -2.351 1.00 15.78 C ANISOU 693 CA LEU A 213 1862 2293 1842 -131 254 -152 C ATOM 694 C LEU A 213 55.234 30.320 -3.156 1.00 13.52 C ANISOU 694 C LEU A 213 1539 2027 1571 -169 258 -119 C ATOM 695 O LEU A 213 55.074 30.507 -4.364 1.00 13.45 O ANISOU 695 O LEU A 213 1530 1976 1606 -157 231 -115 O ATOM 696 CB LEU A 213 57.559 30.532 -2.235 1.00 15.81 C ANISOU 696 CB LEU A 213 1928 2243 1836 -164 239 -113 C ATOM 697 CG LEU A 213 58.354 30.408 -3.534 1.00 18.25 C ANISOU 697 CG LEU A 213 2275 2468 2193 -167 204 -88 C ATOM 698 CD1 LEU A 213 58.336 31.725 -4.299 1.00 17.37 C ANISOU 698 CD1 LEU A 213 2161 2316 2122 -115 180 -123 C ATOM 699 CD2 LEU A 213 59.783 29.981 -3.233 1.00 16.89 C ANISOU 699 CD2 LEU A 213 2154 2251 2011 -185 191 -64 C ATOM 700 N ARG A 214 54.595 29.371 -2.479 1.00 12.13 N ANISOU 700 N ARG A 214 1333 1918 1357 -221 291 -92 N ATOM 701 CA ARG A 214 53.626 28.493 -3.129 1.00 16.95 C ANISOU 701 CA ARG A 214 1904 2553 1982 -268 294 -61 C ATOM 702 C ARG A 214 52.419 29.274 -3.640 1.00 17.83 C ANISOU 702 C ARG A 214 1946 2709 2120 -226 294 -102 C ATOM 703 O ARG A 214 51.910 29.000 -4.727 1.00 18.58 O ANISOU 703 O ARG A 214 2023 2785 2251 -238 271 -90 O ATOM 704 CB ARG A 214 53.161 27.393 -2.175 1.00 17.09 C ANISOU 704 CB ARG A 214 1901 2638 1953 -338 330 -19 C ATOM 705 CG ARG A 214 52.062 26.516 -2.756 1.00 16.41 C ANISOU 705 CG ARG A 214 1767 2583 1886 -395 333 11 C ATOM 706 CD ARG A 214 51.615 25.440 -1.784 1.00 19.17 C ANISOU 706 CD ARG A 214 2098 2996 2190 -474 367 61 C ATOM 707 NE ARG A 214 52.649 24.434 -1.561 1.00 22.54 N ANISOU 707 NE ARG A 214 2600 3355 2608 -521 349 117 N ATOM 708 CZ ARG A 214 52.851 23.383 -2.350 1.00 19.93 C ANISOU 708 CZ ARG A 214 2304 2952 2315 -570 317 158 C ATOM 709 NH1 ARG A 214 52.094 23.201 -3.424 1.00 20.25 N ANISOU 709 NH1 ARG A 214 2311 2984 2398 -583 299 149 N ATOM 710 NH2 ARG A 214 53.816 22.517 -2.068 1.00 15.17 N ANISOU 710 NH2 ARG A 214 1769 2286 1707 -601 298 204 N ATOM 711 N LYS A 215 51.960 30.241 -2.851 1.00 19.14 N ANISOU 711 N LYS A 215 2073 2934 2268 -173 317 -155 N ATOM 712 CA LYS A 215 50.833 31.077 -3.250 1.00 20.98 C ANISOU 712 CA LYS A 215 2235 3208 2528 -119 314 -202 C ATOM 713 C LYS A 215 51.160 31.877 -4.506 1.00 15.60 C ANISOU 713 C LYS A 215 1584 2438 1906 -68 261 -213 C ATOM 714 O LYS A 215 50.304 32.063 -5.368 1.00 16.23 O ANISOU 714 O LYS A 215 1620 2528 2020 -50 240 -218 O ATOM 715 CB LYS A 215 50.429 32.021 -2.117 1.00 24.37 C ANISOU 715 CB LYS A 215 2623 3709 2927 -60 347 -267 C ATOM 716 CG LYS A 215 49.592 31.368 -1.027 1.00 31.03 C ANISOU 716 CG LYS A 215 3402 4678 3710 -103 406 -263 C ATOM 717 CD LYS A 215 49.329 32.336 0.119 1.00 36.36 C ANISOU 717 CD LYS A 215 4043 5427 4345 -38 440 -339 C ATOM 718 CE LYS A 215 48.548 31.673 1.245 1.00 40.49 C ANISOU 718 CE LYS A 215 4502 6089 4794 -87 506 -330 C ATOM 719 NZ LYS A 215 48.447 32.560 2.439 1.00 43.41 N ANISOU 719 NZ LYS A 215 4848 6535 5111 -24 542 -408 N ATOM 720 N ALA A 216 52.401 32.345 -4.609 1.00 17.93 N ANISOU 720 N ALA A 216 1953 2651 2210 -49 237 -212 N ATOM 721 CA ALA A 216 52.825 33.110 -5.778 1.00 18.40 C ANISOU 721 CA ALA A 216 2046 2625 2318 -10 188 -212 C ATOM 722 C ALA A 216 52.921 32.224 -7.019 1.00 15.70 C ANISOU 722 C ALA A 216 1723 2249 1993 -58 164 -161 C ATOM 723 O ALA A 216 52.601 32.658 -8.128 1.00 12.75 O ANISOU 723 O ALA A 216 1344 1848 1653 -34 128 -158 O ATOM 724 CB ALA A 216 54.156 33.792 -5.512 1.00 15.39 C ANISOU 724 CB ALA A 216 1733 2172 1940 11 172 -221 C ATOM 725 N LEU A 217 53.366 30.986 -6.828 1.00 17.40 N ANISOU 725 N LEU A 217 1962 2465 2183 -125 181 -122 N ATOM 726 CA LEU A 217 53.499 30.040 -7.931 1.00 17.31 C ANISOU 726 CA LEU A 217 1972 2420 2186 -171 159 -83 C ATOM 727 C LEU A 217 52.117 29.657 -8.444 1.00 15.74 C ANISOU 727 C LEU A 217 1708 2276 1997 -188 155 -82 C ATOM 728 O LEU A 217 51.883 29.592 -9.652 1.00 16.01 O ANISOU 728 O LEU A 217 1742 2286 2053 -189 121 -74 O ATOM 729 CB LEU A 217 54.279 28.799 -7.489 1.00 18.74 C ANISOU 729 CB LEU A 217 2195 2583 2343 -231 174 -46 C ATOM 730 CG LEU A 217 54.902 27.923 -8.580 1.00 22.26 C ANISOU 730 CG LEU A 217 2686 2970 2803 -265 147 -17 C ATOM 731 CD1 LEU A 217 55.931 26.978 -7.979 1.00 24.57 C ANISOU 731 CD1 LEU A 217 3027 3230 3079 -301 157 10 C ATOM 732 CD2 LEU A 217 53.839 27.143 -9.333 1.00 22.86 C ANISOU 732 CD2 LEU A 217 2725 3070 2890 -303 135 -7 C ATOM 733 N TYR A 218 51.203 29.415 -7.511 1.00 12.73 N ANISOU 733 N TYR A 218 1266 1975 1596 -204 190 -92 N ATOM 734 CA TYR A 218 49.817 29.134 -7.846 1.00 18.15 C ANISOU 734 CA TYR A 218 1874 2729 2294 -222 190 -97 C ATOM 735 C TYR A 218 49.147 30.337 -8.506 1.00 18.72 C ANISOU 735 C TYR A 218 1904 2808 2398 -146 161 -134 C ATOM 736 O TYR A 218 48.427 30.192 -9.492 1.00 17.31 O ANISOU 736 O TYR A 218 1694 2640 2244 -151 129 -128 O ATOM 737 CB TYR A 218 49.044 28.725 -6.593 1.00 25.46 C ANISOU 737 CB TYR A 218 2738 3750 3186 -254 242 -99 C ATOM 738 CG TYR A 218 47.544 28.826 -6.735 1.00 32.34 C ANISOU 738 CG TYR A 218 3507 4710 4069 -252 249 -119 C ATOM 739 CD1 TYR A 218 46.798 27.766 -7.230 1.00 35.57 C ANISOU 739 CD1 TYR A 218 3879 5149 4489 -325 241 -87 C ATOM 740 CD2 TYR A 218 46.872 29.985 -6.369 1.00 38.06 C ANISOU 740 CD2 TYR A 218 4170 5491 4800 -173 259 -174 C ATOM 741 CE1 TYR A 218 45.425 27.859 -7.358 1.00 38.27 C ANISOU 741 CE1 TYR A 218 4118 5579 4843 -326 246 -106 C ATOM 742 CE2 TYR A 218 45.506 30.087 -6.495 1.00 41.90 C ANISOU 742 CE2 TYR A 218 4554 6066 5301 -164 265 -196 C ATOM 743 CZ TYR A 218 44.788 29.024 -6.987 1.00 43.15 C ANISOU 743 CZ TYR A 218 4670 6259 5466 -243 259 -160 C ATOM 744 OH TYR A 218 43.425 29.138 -7.105 1.00 48.47 O ANISOU 744 OH TYR A 218 5233 7028 6155 -236 263 -182 O ATOM 745 N ALA A 219 49.384 31.521 -7.952 1.00 18.49 N ANISOU 745 N ALA A 219 1879 2772 2372 -75 166 -173 N ATOM 746 CA ALA A 219 48.779 32.743 -8.474 1.00 19.37 C ANISOU 746 CA ALA A 219 1958 2881 2522 6 132 -209 C ATOM 747 C ALA A 219 49.200 32.997 -9.918 1.00 19.51 C ANISOU 747 C ALA A 219 2024 2821 2570 16 75 -182 C ATOM 748 O ALA A 219 48.407 33.472 -10.733 1.00 22.18 O ANISOU 748 O ALA A 219 2324 3169 2936 52 37 -189 O ATOM 749 CB ALA A 219 49.144 33.932 -7.597 1.00 18.09 C ANISOU 749 CB ALA A 219 1807 2704 2360 77 142 -258 C ATOM 750 N LEU A 220 50.447 32.666 -10.232 1.00 17.84 N ANISOU 750 N LEU A 220 1893 2539 2347 -16 69 -150 N ATOM 751 CA LEU A 220 50.994 32.906 -11.564 1.00 20.04 C ANISOU 751 CA LEU A 220 2222 2751 2642 -11 22 -122 C ATOM 752 C LEU A 220 50.370 31.990 -12.613 1.00 18.80 C ANISOU 752 C LEU A 220 2044 2617 2483 -55 -1 -98 C ATOM 753 O LEU A 220 50.169 32.393 -13.760 1.00 19.25 O ANISOU 753 O LEU A 220 2106 2654 2554 -34 -46 -87 O ATOM 754 CB LEU A 220 52.513 32.727 -11.554 1.00 19.76 C ANISOU 754 CB LEU A 220 2268 2649 2592 -35 28 -99 C ATOM 755 CG LEU A 220 53.281 33.427 -12.675 1.00 25.68 C ANISOU 755 CG LEU A 220 3071 3330 3356 -15 -13 -76 C ATOM 756 CD1 LEU A 220 53.201 34.937 -12.508 1.00 25.80 C ANISOU 756 CD1 LEU A 220 3087 3314 3402 54 -37 -97 C ATOM 757 CD2 LEU A 220 54.728 32.964 -12.698 1.00 25.94 C ANISOU 757 CD2 LEU A 220 3169 3316 3370 -51 1 -53 C ATOM 758 N MET A 221 50.077 30.755 -12.220 1.00 18.12 N ANISOU 758 N MET A 221 1936 2571 2379 -120 27 -90 N ATOM 759 CA MET A 221 49.455 29.787 -13.120 1.00 16.90 C ANISOU 759 CA MET A 221 1760 2436 2224 -170 5 -73 C ATOM 760 C MET A 221 47.974 30.071 -13.306 1.00 16.96 C ANISOU 760 C MET A 221 1677 2515 2250 -151 -12 -92 C ATOM 761 O MET A 221 47.433 29.899 -14.395 1.00 21.09 O ANISOU 761 O MET A 221 2183 3046 2782 -158 -55 -86 O ATOM 762 CB MET A 221 49.635 28.365 -12.590 1.00 16.89 C ANISOU 762 CB MET A 221 1770 2443 2205 -250 35 -55 C ATOM 763 CG MET A 221 51.071 27.907 -12.490 1.00 17.34 C ANISOU 763 CG MET A 221 1911 2431 2246 -270 45 -37 C ATOM 764 SD MET A 221 51.172 26.306 -11.678 1.00 20.35 S ANISOU 764 SD MET A 221 2302 2817 2613 -355 74 -12 S ATOM 765 CE MET A 221 50.239 25.287 -12.816 1.00 25.74 C ANISOU 765 CE MET A 221 2958 3512 3311 -412 37 -8 C ATOM 766 N GLU A 222 47.328 30.503 -12.229 1.00 18.29 N ANISOU 766 N GLU A 222 1785 2743 2422 -124 22 -119 N ATOM 767 CA GLU A 222 45.884 30.711 -12.212 1.00 25.99 C ANISOU 767 CA GLU A 222 2658 3803 3416 -105 16 -143 C ATOM 768 C GLU A 222 45.493 32.096 -12.720 1.00 25.46 C ANISOU 768 C GLU A 222 2568 3725 3380 -9 -26 -168 C ATOM 769 O GLU A 222 44.445 32.268 -13.342 1.00 23.34 O ANISOU 769 O GLU A 222 2233 3502 3134 12 -62 -177 O ATOM 770 CB GLU A 222 45.344 30.505 -10.792 1.00 30.27 C ANISOU 770 CB GLU A 222 3136 4426 3940 -120 78 -163 C ATOM 771 CG GLU A 222 43.892 30.908 -10.607 1.00 37.37 C ANISOU 771 CG GLU A 222 3916 5424 4857 -85 81 -197 C ATOM 772 CD GLU A 222 42.945 30.117 -11.490 1.00 44.30 C ANISOU 772 CD GLU A 222 4737 6345 5751 -140 49 -179 C ATOM 773 OE1 GLU A 222 43.319 29.006 -11.924 1.00 45.23 O ANISOU 773 OE1 GLU A 222 4900 6429 5857 -223 41 -142 O ATOM 774 OE2 GLU A 222 41.828 30.610 -11.752 1.00 46.50 O ANISOU 774 OE2 GLU A 222 4924 6690 6055 -97 29 -206 O ATOM 775 N LYS A 223 46.343 33.077 -12.441 1.00 26.56 N ANISOU 775 N LYS A 223 2765 3802 3525 48 -28 -178 N ATOM 776 CA LYS A 223 46.090 34.461 -12.818 1.00 32.61 C ANISOU 776 CA LYS A 223 3524 4540 4328 142 -71 -200 C ATOM 777 C LYS A 223 47.361 35.087 -13.376 1.00 31.51 C ANISOU 777 C LYS A 223 3486 4295 4190 158 -101 -173 C ATOM 778 O LYS A 223 48.402 34.440 -13.443 1.00 31.75 O ANISOU 778 O LYS A 223 3583 4287 4195 102 -83 -144 O ATOM 779 CB LYS A 223 45.589 35.267 -11.616 1.00 39.26 C ANISOU 779 CB LYS A 223 4311 5426 5182 208 -40 -257 C ATOM 780 CG LYS A 223 44.213 34.861 -11.111 1.00 44.60 C ANISOU 780 CG LYS A 223 4869 6220 5857 204 -11 -288 C ATOM 781 CD LYS A 223 43.925 35.448 -9.735 1.00 50.02 C ANISOU 781 CD LYS A 223 5508 6961 6536 257 39 -348 C ATOM 782 CE LYS A 223 42.487 35.184 -9.300 1.00 53.56 C ANISOU 782 CE LYS A 223 5826 7540 6985 262 68 -382 C ATOM 783 NZ LYS A 223 42.286 35.502 -7.855 1.00 55.17 N ANISOU 783 NZ LYS A 223 5985 7817 7162 294 132 -439 N ATOM 784 N GLY A 224 47.277 36.347 -13.777 1.00 37.51 N ANISOU 784 N GLY A 224 4256 5010 4986 235 -147 -181 N ATOM 785 CA GLY A 224 48.441 37.041 -14.292 1.00 44.28 C ANISOU 785 CA GLY A 224 5206 5770 5850 246 -176 -150 C ATOM 786 C GLY A 224 48.532 37.019 -15.804 1.00 43.55 C ANISOU 786 C GLY A 224 5147 5648 5753 232 -232 -98 C ATOM 787 O GLY A 224 47.871 36.222 -16.472 1.00 44.27 O ANISOU 787 O GLY A 224 5201 5790 5828 198 -245 -86 O ATOM 788 N VAL A 225 49.374 37.897 -16.337 1.00 39.32 N ANISOU 788 N VAL A 225 4681 5031 5228 253 -266 -67 N ATOM 789 CA VAL A 225 49.474 38.122 -17.772 1.00 34.86 C ANISOU 789 CA VAL A 225 4152 4438 4655 248 -323 -13 C ATOM 790 C VAL A 225 50.036 36.938 -18.551 1.00 27.87 C ANISOU 790 C VAL A 225 3299 3573 3717 168 -308 20 C ATOM 791 O VAL A 225 49.621 36.685 -19.680 1.00 31.58 O ANISOU 791 O VAL A 225 3765 4065 4167 156 -348 47 O ATOM 792 CB VAL A 225 50.351 39.352 -18.065 1.00 36.00 C ANISOU 792 CB VAL A 225 4368 4489 4822 278 -357 20 C ATOM 793 CG1 VAL A 225 49.664 40.615 -17.586 1.00 38.01 C ANISOU 793 CG1 VAL A 225 4595 4711 5136 368 -394 -12 C ATOM 794 CG2 VAL A 225 51.711 39.198 -17.402 1.00 34.37 C ANISOU 794 CG2 VAL A 225 4219 4242 4600 237 -309 20 C ATOM 795 N GLU A 226 50.974 36.209 -17.957 1.00 21.97 N ANISOU 795 N GLU A 226 2584 2818 2947 118 -254 14 N ATOM 796 CA GLU A 226 51.700 35.195 -18.717 1.00 25.21 C ANISOU 796 CA GLU A 226 3035 3232 3311 53 -242 40 C ATOM 797 C GLU A 226 51.116 33.787 -18.615 1.00 17.82 C ANISOU 797 C GLU A 226 2059 2356 2355 3 -219 19 C ATOM 798 O GLU A 226 51.703 32.843 -19.137 1.00 17.44 O ANISOU 798 O GLU A 226 2044 2308 2273 -48 -209 30 O ATOM 799 CB GLU A 226 53.172 35.168 -18.288 1.00 32.69 C ANISOU 799 CB GLU A 226 4043 4130 4245 27 -205 50 C ATOM 800 CG GLU A 226 53.411 34.725 -16.857 1.00 37.55 C ANISOU 800 CG GLU A 226 4645 4754 4869 16 -152 15 C ATOM 801 CD GLU A 226 53.926 35.850 -15.982 1.00 41.39 C ANISOU 801 CD GLU A 226 5150 5193 5384 56 -146 2 C ATOM 802 OE1 GLU A 226 53.119 36.724 -15.603 1.00 45.25 O ANISOU 802 OE1 GLU A 226 5605 5683 5906 112 -166 -21 O ATOM 803 OE2 GLU A 226 55.138 35.860 -15.675 1.00 40.05 O ANISOU 803 OE2 GLU A 226 5027 4986 5206 34 -125 12 O ATOM 804 N LYS A 227 49.963 33.640 -17.970 1.00 15.83 N ANISOU 804 N LYS A 227 1734 2155 2125 16 -213 -12 N ATOM 805 CA LYS A 227 49.419 32.304 -17.731 1.00 19.05 C ANISOU 805 CA LYS A 227 2102 2615 2519 -42 -189 -27 C ATOM 806 C LYS A 227 49.046 31.574 -19.026 1.00 13.38 C ANISOU 806 C LYS A 227 1385 1920 1779 -79 -229 -14 C ATOM 807 O LYS A 227 49.193 30.357 -19.117 1.00 13.93 O ANISOU 807 O LYS A 227 1465 1998 1829 -140 -214 -19 O ATOM 808 CB LYS A 227 48.206 32.371 -16.797 1.00 23.26 C ANISOU 808 CB LYS A 227 2547 3212 3078 -23 -172 -60 C ATOM 809 CG LYS A 227 46.958 32.973 -17.408 1.00 30.48 C ANISOU 809 CG LYS A 227 3396 4169 4017 23 -223 -68 C ATOM 810 CD LYS A 227 45.754 32.742 -16.509 1.00 35.29 C ANISOU 810 CD LYS A 227 3906 4859 4645 26 -197 -103 C ATOM 811 CE LYS A 227 44.505 33.389 -17.077 1.00 38.37 C ANISOU 811 CE LYS A 227 4219 5295 5064 81 -249 -115 C ATOM 812 NZ LYS A 227 43.324 33.156 -16.200 1.00 39.92 N ANISOU 812 NZ LYS A 227 4305 5584 5277 83 -219 -152 N ATOM 813 N GLU A 228 48.577 32.308 -20.029 1.00 12.04 N ANISOU 813 N GLU A 228 1209 1755 1611 -41 -286 1 N ATOM 814 CA GLU A 228 48.194 31.679 -21.292 1.00 20.93 C ANISOU 814 CA GLU A 228 2336 2909 2708 -73 -330 11 C ATOM 815 C GLU A 228 49.415 31.177 -22.060 1.00 16.80 C ANISOU 815 C GLU A 228 1895 2350 2139 -110 -324 29 C ATOM 816 O GLU A 228 49.383 30.100 -22.653 1.00 11.91 O ANISOU 816 O GLU A 228 1285 1750 1492 -160 -331 17 O ATOM 817 CB GLU A 228 47.386 32.648 -22.158 1.00 25.27 C ANISOU 817 CB GLU A 228 2858 3477 3266 -19 -397 28 C ATOM 818 CG GLU A 228 46.006 32.960 -21.594 1.00 35.35 C ANISOU 818 CG GLU A 228 4037 4806 4586 18 -411 2 C ATOM 819 CD GLU A 228 45.176 31.708 -21.355 1.00 43.79 C ANISOU 819 CD GLU A 228 5043 5941 5656 -44 -397 -27 C ATOM 820 OE1 GLU A 228 45.204 30.797 -22.209 1.00 47.35 O ANISOU 820 OE1 GLU A 228 5513 6404 6075 -99 -419 -24 O ATOM 821 OE2 GLU A 228 44.498 31.633 -20.308 1.00 47.09 O ANISOU 821 OE2 GLU A 228 5390 6399 6104 -39 -363 -54 O ATOM 822 N ALA A 229 50.490 31.958 -22.033 1.00 16.17 N ANISOU 822 N ALA A 229 1871 2219 2052 -85 -310 53 N ATOM 823 CA ALA A 229 51.729 31.583 -22.704 1.00 15.37 C ANISOU 823 CA ALA A 229 1841 2092 1908 -116 -297 70 C ATOM 824 C ALA A 229 52.411 30.418 -21.986 1.00 13.60 C ANISOU 824 C ALA A 229 1633 1855 1681 -161 -245 43 C ATOM 825 O ALA A 229 52.945 29.507 -22.622 1.00 12.39 O ANISOU 825 O ALA A 229 1513 1703 1493 -197 -241 34 O ATOM 826 CB ALA A 229 52.661 32.778 -22.792 1.00 15.51 C ANISOU 826 CB ALA A 229 1905 2062 1925 -83 -297 107 C ATOM 827 N LEU A 230 52.391 30.453 -20.658 1.00 10.39 N ANISOU 827 N LEU A 230 1203 1435 1308 -155 -207 30 N ATOM 828 CA LEU A 230 52.915 29.355 -19.858 1.00 10.93 C ANISOU 828 CA LEU A 230 1284 1492 1377 -196 -163 12 C ATOM 829 C LEU A 230 52.193 28.056 -20.201 1.00 12.68 C ANISOU 829 C LEU A 230 1483 1743 1593 -246 -176 -9 C ATOM 830 O LEU A 230 52.822 27.015 -20.397 1.00 10.95 O ANISOU 830 O LEU A 230 1300 1503 1358 -283 -165 -20 O ATOM 831 CB LEU A 230 52.776 29.660 -18.364 1.00 9.85 C ANISOU 831 CB LEU A 230 1118 1353 1271 -183 -127 3 C ATOM 832 CG LEU A 230 53.667 30.779 -17.821 1.00 15.23 C ANISOU 832 CG LEU A 230 1829 1994 1962 -142 -111 14 C ATOM 833 CD1 LEU A 230 53.330 31.083 -16.367 1.00 15.93 C ANISOU 833 CD1 LEU A 230 1884 2094 2075 -125 -80 -6 C ATOM 834 CD2 LEU A 230 55.140 30.414 -17.968 1.00 13.88 C ANISOU 834 CD2 LEU A 230 1720 1783 1770 -163 -90 25 C ATOM 835 N LYS A 231 50.868 28.135 -20.286 1.00 13.39 N ANISOU 835 N LYS A 231 1510 1878 1698 -245 -203 -16 N ATOM 836 CA LYS A 231 50.041 26.973 -20.584 1.00 15.36 C ANISOU 836 CA LYS A 231 1730 2159 1949 -299 -222 -35 C ATOM 837 C LYS A 231 50.322 26.413 -21.982 1.00 13.90 C ANISOU 837 C LYS A 231 1586 1969 1726 -319 -260 -44 C ATOM 838 O LYS A 231 50.323 25.198 -22.181 1.00 11.45 O ANISOU 838 O LYS A 231 1290 1651 1412 -370 -264 -66 O ATOM 839 CB LYS A 231 48.561 27.337 -20.445 1.00 17.76 C ANISOU 839 CB LYS A 231 1948 2522 2278 -289 -246 -41 C ATOM 840 CG LYS A 231 47.608 26.159 -20.532 1.00 21.93 C ANISOU 840 CG LYS A 231 2430 3086 2815 -354 -262 -59 C ATOM 841 CD LYS A 231 46.178 26.602 -20.247 1.00 26.98 C ANISOU 841 CD LYS A 231 2971 3795 3483 -341 -278 -65 C ATOM 842 CE LYS A 231 45.203 25.441 -20.341 1.00 31.40 C ANISOU 842 CE LYS A 231 3480 4396 4056 -416 -295 -79 C ATOM 843 NZ LYS A 231 43.806 25.864 -20.043 1.00 32.56 N ANISOU 843 NZ LYS A 231 3518 4623 4232 -404 -308 -86 N ATOM 844 N ARG A 232 50.563 27.297 -22.946 1.00 13.92 N ANISOU 844 N ARG A 232 1611 1977 1701 -280 -289 -27 N ATOM 845 CA ARG A 232 50.882 26.857 -24.304 1.00 15.59 C ANISOU 845 CA ARG A 232 1864 2197 1863 -295 -322 -36 C ATOM 846 C ARG A 232 52.227 26.139 -24.342 1.00 14.14 C ANISOU 846 C ARG A 232 1745 1972 1657 -314 -286 -49 C ATOM 847 O ARG A 232 52.383 25.135 -25.036 1.00 13.35 O ANISOU 847 O ARG A 232 1670 1873 1530 -345 -300 -81 O ATOM 848 CB ARG A 232 50.893 28.037 -25.278 1.00 16.24 C ANISOU 848 CB ARG A 232 1960 2298 1914 -252 -359 -3 C ATOM 849 CG ARG A 232 49.516 28.542 -25.678 1.00 20.65 C ANISOU 849 CG ARG A 232 2459 2904 2485 -233 -416 4 C ATOM 850 CD ARG A 232 49.612 29.498 -26.861 1.00 17.86 C ANISOU 850 CD ARG A 232 2132 2565 2088 -198 -463 41 C ATOM 851 NE ARG A 232 50.511 30.613 -26.578 1.00 19.05 N ANISOU 851 NE ARG A 232 2322 2674 2244 -160 -439 82 N ATOM 852 CZ ARG A 232 50.113 31.792 -26.109 1.00 17.87 C ANISOU 852 CZ ARG A 232 2148 2508 2136 -109 -454 109 C ATOM 853 NH1 ARG A 232 48.827 32.013 -25.875 1.00 16.01 N ANISOU 853 NH1 ARG A 232 1842 2302 1937 -85 -488 98 N ATOM 854 NH2 ARG A 232 50.998 32.750 -25.874 1.00 17.58 N ANISOU 854 NH2 ARG A 232 2151 2422 2105 -83 -435 144 N ATOM 855 N ARG A 233 53.197 26.660 -23.596 1.00 13.41 N ANISOU 855 N ARG A 233 1676 1844 1575 -291 -243 -30 N ATOM 856 CA ARG A 233 54.517 26.047 -23.528 1.00 12.32 C ANISOU 856 CA ARG A 233 1590 1670 1421 -301 -208 -42 C ATOM 857 C ARG A 233 54.429 24.645 -22.932 1.00 14.49 C ANISOU 857 C ARG A 233 1865 1921 1721 -343 -196 -75 C ATOM 858 O ARG A 233 55.039 23.705 -23.443 1.00 12.40 O ANISOU 858 O ARG A 233 1637 1638 1436 -360 -196 -105 O ATOM 859 CB ARG A 233 55.476 26.915 -22.711 1.00 12.10 C ANISOU 859 CB ARG A 233 1578 1612 1408 -272 -168 -15 C ATOM 860 CG ARG A 233 55.876 28.216 -23.393 1.00 14.49 C ANISOU 860 CG ARG A 233 1897 1922 1686 -239 -180 22 C ATOM 861 CD ARG A 233 56.824 29.036 -22.516 1.00 14.77 C ANISOU 861 CD ARG A 233 1947 1921 1744 -218 -145 45 C ATOM 862 NE ARG A 233 57.225 30.284 -23.164 1.00 13.51 N ANISOU 862 NE ARG A 233 1806 1760 1566 -196 -160 87 N ATOM 863 CZ ARG A 233 58.296 30.412 -23.943 1.00 11.97 C ANISOU 863 CZ ARG A 233 1648 1570 1330 -203 -149 104 C ATOM 864 NH1 ARG A 233 59.082 29.369 -24.167 1.00 11.98 N ANISOU 864 NH1 ARG A 233 1668 1579 1306 -224 -122 74 N ATOM 865 NH2 ARG A 233 58.586 31.583 -24.494 1.00 11.15 N ANISOU 865 NH2 ARG A 233 1561 1463 1211 -191 -164 151 N ATOM 866 N TRP A 234 53.664 24.512 -21.852 1.00 13.39 N ANISOU 866 N TRP A 234 1684 1781 1623 -360 -186 -69 N ATOM 867 CA TRP A 234 53.440 23.212 -21.228 1.00 13.45 C ANISOU 867 CA TRP A 234 1688 1764 1656 -409 -179 -87 C ATOM 868 C TRP A 234 52.786 22.231 -22.193 1.00 13.50 C ANISOU 868 C TRP A 234 1695 1780 1654 -449 -223 -120 C ATOM 869 O TRP A 234 53.265 21.112 -22.381 1.00 11.83 O ANISOU 869 O TRP A 234 1523 1530 1444 -476 -228 -148 O ATOM 870 CB TRP A 234 52.571 23.355 -19.978 1.00 13.39 C ANISOU 870 CB TRP A 234 1627 1775 1686 -424 -160 -69 C ATOM 871 CG TRP A 234 51.943 22.057 -19.553 1.00 14.88 C ANISOU 871 CG TRP A 234 1801 1954 1900 -489 -167 -78 C ATOM 872 CD1 TRP A 234 52.566 21.008 -18.943 1.00 13.55 C ANISOU 872 CD1 TRP A 234 1670 1733 1746 -522 -150 -78 C ATOM 873 CD2 TRP A 234 50.570 21.675 -19.704 1.00 12.68 C ANISOU 873 CD2 TRP A 234 1464 1716 1637 -533 -195 -84 C ATOM 874 NE1 TRP A 234 51.669 19.995 -18.708 1.00 14.45 N ANISOU 874 NE1 TRP A 234 1758 1846 1885 -588 -167 -80 N ATOM 875 CE2 TRP A 234 50.435 20.380 -19.166 1.00 14.15 C ANISOU 875 CE2 TRP A 234 1659 1869 1849 -599 -193 -85 C ATOM 876 CE3 TRP A 234 49.443 22.300 -20.246 1.00 14.85 C ANISOU 876 CE3 TRP A 234 1678 2052 1911 -523 -226 -87 C ATOM 877 CZ2 TRP A 234 49.218 19.696 -19.153 1.00 16.36 C ANISOU 877 CZ2 TRP A 234 1888 2177 2152 -663 -218 -87 C ATOM 878 CZ3 TRP A 234 48.234 21.620 -20.232 1.00 19.30 C ANISOU 878 CZ3 TRP A 234 2185 2650 2497 -580 -251 -95 C ATOM 879 CH2 TRP A 234 48.132 20.333 -19.689 1.00 17.77 C ANISOU 879 CH2 TRP A 234 2000 2424 2328 -654 -245 -94 C ATOM 880 N ARG A 235 51.683 22.657 -22.799 1.00 11.41 N ANISOU 880 N ARG A 235 1386 1567 1383 -450 -260 -120 N ATOM 881 CA ARG A 235 50.925 21.789 -23.683 1.00 13.99 C ANISOU 881 CA ARG A 235 1704 1910 1702 -492 -310 -154 C ATOM 882 C ARG A 235 51.758 21.367 -24.887 1.00 14.78 C ANISOU 882 C ARG A 235 1866 1997 1754 -483 -328 -188 C ATOM 883 O ARG A 235 51.686 20.221 -25.330 1.00 12.58 O ANISOU 883 O ARG A 235 1609 1696 1476 -521 -354 -231 O ATOM 884 CB ARG A 235 49.640 22.481 -24.145 1.00 14.17 C ANISOU 884 CB ARG A 235 1663 1998 1724 -485 -350 -145 C ATOM 885 CG ARG A 235 48.881 21.714 -25.215 1.00 16.71 C ANISOU 885 CG ARG A 235 1976 2345 2029 -525 -410 -181 C ATOM 886 CD ARG A 235 47.453 22.223 -25.364 1.00 16.83 C ANISOU 886 CD ARG A 235 1910 2427 2060 -529 -451 -171 C ATOM 887 NE ARG A 235 46.737 21.515 -26.420 1.00 17.86 N ANISOU 887 NE ARG A 235 2029 2585 2172 -569 -515 -208 N ATOM 888 CZ ARG A 235 45.422 21.567 -26.601 1.00 16.27 C ANISOU 888 CZ ARG A 235 1753 2441 1990 -592 -559 -211 C ATOM 889 NH1 ARG A 235 44.662 22.289 -25.788 1.00 17.81 N ANISOU 889 NH1 ARG A 235 1871 2674 2222 -573 -543 -181 N ATOM 890 NH2 ARG A 235 44.865 20.887 -27.592 1.00 16.13 N ANISOU 890 NH2 ARG A 235 1731 2445 1952 -631 -622 -248 N ATOM 891 N ATRP A 236 52.553 22.297 -25.407 0.60 14.46 N ANISOU 891 N ATRP A 236 1853 1970 1672 -433 -315 -171 N ATOM 892 N BTRP A 236 52.553 22.296 -25.408 0.40 14.76 N ANISOU 892 N BTRP A 236 1890 2007 1710 -433 -315 -171 N ATOM 893 CA ATRP A 236 53.376 22.022 -26.579 0.60 16.62 C ANISOU 893 CA ATRP A 236 2178 2248 1887 -421 -324 -202 C ATOM 894 CA BTRP A 236 53.374 22.015 -26.578 0.40 16.47 C ANISOU 894 CA BTRP A 236 2159 2229 1869 -421 -325 -202 C ATOM 895 C ATRP A 236 54.425 20.956 -26.280 0.60 15.65 C ANISOU 895 C ATRP A 236 2101 2069 1775 -430 -296 -238 C ATOM 896 C BTRP A 236 54.412 20.942 -26.271 0.40 15.52 C ANISOU 896 C BTRP A 236 2085 2052 1759 -430 -296 -238 C ATOM 897 O ATRP A 236 54.642 20.054 -27.085 0.60 14.35 O ANISOU 897 O ATRP A 236 1970 1899 1586 -442 -318 -291 O ATOM 898 O BTRP A 236 54.611 20.022 -27.062 0.40 14.74 O ANISOU 898 O BTRP A 236 2018 1946 1637 -443 -319 -291 O ATOM 899 CB ATRP A 236 54.051 23.303 -27.076 0.60 17.29 C ANISOU 899 CB ATRP A 236 2279 2363 1929 -374 -310 -163 C ATOM 900 CB BTRP A 236 54.062 23.287 -27.077 0.40 17.58 C ANISOU 900 CB BTRP A 236 2316 2399 1965 -374 -310 -164 C ATOM 901 CG ATRP A 236 54.957 23.092 -28.254 0.60 20.53 C ANISOU 901 CG ATRP A 236 2737 2794 2269 -362 -310 -190 C ATOM 902 CG BTRP A 236 54.812 23.086 -28.359 0.40 20.68 C ANISOU 902 CG BTRP A 236 2754 2819 2286 -364 -317 -191 C ATOM 903 CD1ATRP A 236 56.302 22.863 -28.223 0.60 22.02 C ANISOU 903 CD1ATRP A 236 2965 2962 2441 -346 -266 -203 C ATOM 904 CD1BTRP A 236 54.353 23.323 -29.622 0.40 22.33 C ANISOU 904 CD1BTRP A 236 2965 3085 2433 -363 -361 -197 C ATOM 905 CD2ATRP A 236 54.583 23.092 -29.638 0.60 22.48 C ANISOU 905 CD2ATRP A 236 2994 3098 2449 -365 -354 -208 C ATOM 906 CD2BTRP A 236 56.150 22.597 -28.504 0.40 22.50 C ANISOU 906 CD2BTRP A 236 3028 3030 2493 -353 -279 -219 C ATOM 907 NE1ATRP A 236 56.789 22.722 -29.501 0.60 24.26 N ANISOU 907 NE1ATRP A 236 3278 3290 2650 -338 -276 -231 N ATOM 908 NE1BTRP A 236 55.324 23.017 -30.544 0.40 24.36 N ANISOU 908 NE1BTRP A 236 3268 3365 2624 -354 -348 -227 N ATOM 909 CE2ATRP A 236 55.753 22.858 -30.388 0.60 24.77 C ANISOU 909 CE2ATRP A 236 3330 3403 2679 -351 -330 -234 C ATOM 910 CE2BTRP A 236 56.438 22.569 -29.883 0.40 24.39 C ANISOU 910 CE2BTRP A 236 3294 3322 2652 -345 -296 -243 C ATOM 911 CE3ATRP A 236 53.372 23.268 -30.315 0.60 23.31 C ANISOU 911 CE3ATRP A 236 3070 3249 2536 -377 -414 -207 C ATOM 912 CE3BTRP A 236 57.135 22.181 -27.601 0.40 22.47 C ANISOU 912 CE3BTRP A 236 3040 2972 2524 -345 -232 -226 C ATOM 913 CZ2ATRP A 236 55.748 22.795 -31.780 0.60 25.87 C ANISOU 913 CZ2ATRP A 236 3491 3604 2733 -350 -360 -258 C ATOM 914 CZ2BTRP A 236 57.667 22.142 -30.381 0.40 24.29 C ANISOU 914 CZ2BTRP A 236 3318 3316 2595 -329 -264 -279 C ATOM 915 CZ3ATRP A 236 53.370 23.205 -31.699 0.60 26.16 C ANISOU 915 CZ3ATRP A 236 3456 3667 2817 -376 -450 -229 C ATOM 916 CZ3BTRP A 236 58.354 21.758 -28.097 0.40 22.80 C ANISOU 916 CZ3BTRP A 236 3119 3016 2530 -327 -206 -260 C ATOM 917 CH2ATRP A 236 54.550 22.971 -32.416 0.60 26.33 C ANISOU 917 CH2ATRP A 236 3526 3705 2771 -363 -421 -254 C ATOM 918 CH2BTRP A 236 58.610 21.742 -29.473 0.40 24.07 C ANISOU 918 CH2BTRP A 236 3300 3234 2612 -318 -219 -288 C ATOM 919 N GLN A 237 55.071 21.060 -25.121 1.00 14.13 N ANISOU 919 N GLN A 237 1913 1835 1620 -420 -251 -212 N ATOM 920 CA GLN A 237 56.088 20.087 -24.734 1.00 14.89 C ANISOU 920 CA GLN A 237 2051 1875 1734 -421 -228 -241 C ATOM 921 C GLN A 237 55.453 18.741 -24.400 1.00 15.97 C ANISOU 921 C GLN A 237 2189 1966 1914 -472 -255 -271 C ATOM 922 O GLN A 237 55.978 17.693 -24.773 1.00 16.70 O ANISOU 922 O GLN A 237 2322 2016 2007 -477 -268 -320 O ATOM 923 CB GLN A 237 56.915 20.584 -23.545 1.00 16.61 C ANISOU 923 CB GLN A 237 2269 2064 1978 -398 -180 -201 C ATOM 924 CG GLN A 237 58.058 19.640 -23.176 1.00 20.78 C ANISOU 924 CG GLN A 237 2838 2536 2523 -390 -160 -228 C ATOM 925 CD GLN A 237 59.005 20.217 -22.140 1.00 27.32 C ANISOU 925 CD GLN A 237 3667 3346 3368 -364 -117 -191 C ATOM 926 OE1 GLN A 237 59.795 21.117 -22.434 1.00 26.76 O ANISOU 926 OE1 GLN A 237 3599 3302 3268 -330 -94 -177 O ATOM 927 NE2 GLN A 237 58.936 19.696 -20.920 1.00 28.74 N ANISOU 927 NE2 GLN A 237 3845 3482 3593 -383 -108 -173 N ATOM 928 N GLN A 238 54.322 18.772 -23.703 1.00 15.06 N ANISOU 928 N GLN A 238 2028 1858 1835 -510 -266 -243 N ATOM 929 CA GLN A 238 53.622 17.545 -23.344 1.00 14.24 C ANISOU 929 CA GLN A 238 1921 1713 1775 -572 -293 -260 C ATOM 930 C GLN A 238 53.094 16.840 -24.587 1.00 13.75 C ANISOU 930 C GLN A 238 1871 1659 1694 -597 -349 -316 C ATOM 931 O GLN A 238 53.068 15.611 -24.650 1.00 14.44 O ANISOU 931 O GLN A 238 1988 1689 1810 -636 -377 -354 O ATOM 932 CB GLN A 238 52.471 17.832 -22.380 1.00 14.12 C ANISOU 932 CB GLN A 238 1842 1725 1796 -610 -288 -215 C ATOM 933 CG GLN A 238 51.740 16.579 -21.912 1.00 15.58 C ANISOU 933 CG GLN A 238 2020 1872 2029 -687 -312 -219 C ATOM 934 CD GLN A 238 52.633 15.650 -21.110 1.00 19.72 C ANISOU 934 CD GLN A 238 2597 2312 2585 -699 -295 -213 C ATOM 935 OE1 GLN A 238 53.219 16.052 -20.105 1.00 20.23 O ANISOU 935 OE1 GLN A 238 2664 2368 2654 -676 -251 -174 O ATOM 936 NE2 GLN A 238 52.745 14.404 -21.554 1.00 19.63 N ANISOU 936 NE2 GLN A 238 2629 2234 2594 -733 -334 -254 N ATOM 937 N THR A 239 52.673 17.630 -25.570 1.00 13.10 N ANISOU 937 N THR A 239 1768 1646 1564 -576 -371 -322 N ATOM 938 CA THR A 239 52.201 17.096 -26.841 1.00 18.00 C ANISOU 938 CA THR A 239 2399 2288 2151 -595 -427 -378 C ATOM 939 C THR A 239 53.300 16.306 -27.542 1.00 17.90 C ANISOU 939 C THR A 239 2454 2236 2109 -573 -428 -441 C ATOM 940 O THR A 239 53.058 15.214 -28.050 1.00 22.20 O ANISOU 940 O THR A 239 3024 2747 2663 -606 -471 -501 O ATOM 941 CB THR A 239 51.703 18.217 -27.774 1.00 18.23 C ANISOU 941 CB THR A 239 2399 2403 2124 -567 -448 -363 C ATOM 942 OG1 THR A 239 50.535 18.826 -27.211 1.00 16.54 O ANISOU 942 OG1 THR A 239 2115 2226 1942 -585 -458 -318 O ATOM 943 CG2 THR A 239 51.365 17.661 -29.149 1.00 18.42 C ANISOU 943 CG2 THR A 239 2443 2456 2099 -582 -507 -425 C ATOM 944 N GLN A 240 54.510 16.858 -27.562 1.00 17.08 N ANISOU 944 N GLN A 240 2378 2137 1974 -517 -382 -431 N ATOM 945 CA GLN A 240 55.645 16.167 -28.167 1.00 20.81 C ANISOU 945 CA GLN A 240 2906 2583 2419 -486 -374 -492 C ATOM 946 C GLN A 240 55.947 14.871 -27.417 1.00 20.58 C ANISOU 946 C GLN A 240 2907 2455 2457 -508 -379 -522 C ATOM 947 O GLN A 240 56.247 13.844 -28.025 1.00 19.66 O ANISOU 947 O GLN A 240 2832 2300 2339 -507 -407 -595 O ATOM 948 CB GLN A 240 56.883 17.066 -28.186 1.00 22.42 C ANISOU 948 CB GLN A 240 3121 2816 2583 -428 -318 -466 C ATOM 949 CG GLN A 240 56.625 18.476 -28.692 1.00 29.32 C ANISOU 949 CG GLN A 240 3966 3771 3402 -410 -311 -415 C ATOM 950 CD GLN A 240 55.777 18.509 -29.950 1.00 36.51 C ANISOU 950 CD GLN A 240 4872 4743 4257 -424 -363 -444 C ATOM 951 OE1 GLN A 240 56.029 17.774 -30.905 1.00 38.88 O ANISOU 951 OE1 GLN A 240 5204 5054 4512 -422 -385 -513 O ATOM 952 NE2 GLN A 240 54.758 19.360 -29.952 1.00 38.45 N ANISOU 952 NE2 GLN A 240 5076 5031 4502 -436 -387 -394 N ATOM 953 N GLN A 241 55.854 14.925 -26.092 1.00 17.30 N ANISOU 953 N GLN A 241 2474 1999 2101 -527 -355 -463 N ATOM 954 CA GLN A 241 56.066 13.745 -25.259 1.00 19.20 C ANISOU 954 CA GLN A 241 2744 2144 2408 -554 -363 -472 C ATOM 955 C GLN A 241 55.021 12.667 -25.542 1.00 23.26 C ANISOU 955 C GLN A 241 3263 2619 2958 -622 -425 -509 C ATOM 956 O GLN A 241 55.344 11.481 -25.617 1.00 29.54 O ANISOU 956 O GLN A 241 4104 3331 3787 -633 -455 -558 O ATOM 957 CB GLN A 241 56.041 14.124 -23.778 1.00 20.19 C ANISOU 957 CB GLN A 241 2844 2252 2577 -567 -326 -394 C ATOM 958 N ASN A 242 53.769 13.084 -25.706 1.00 18.95 N ANISOU 958 N ASN A 242 2665 2128 2406 -666 -448 -486 N ATOM 959 CA ASN A 242 52.674 12.154 -25.969 1.00 19.58 C ANISOU 959 CA ASN A 242 2738 2181 2521 -741 -509 -515 C ATOM 960 C ASN A 242 52.888 11.334 -27.237 1.00 20.73 C ANISOU 960 C ASN A 242 2932 2304 2640 -734 -560 -612 C ATOM 961 O ASN A 242 52.478 10.176 -27.314 1.00 19.44 O ANISOU 961 O ASN A 242 2785 2076 2525 -777 -602 -649 O ATOM 962 CB ASN A 242 51.345 12.910 -26.059 1.00 19.46 C ANISOU 962 CB ASN A 242 2647 2251 2494 -777 -524 -478 C ATOM 963 CG ASN A 242 50.793 13.288 -24.695 1.00 20.69 C ANISOU 963 CG ASN A 242 2750 2415 2695 -810 -488 -398 C ATOM 964 OD1 ASN A 242 51.368 12.941 -23.664 1.00 23.55 O ANISOU 964 OD1 ASN A 242 3135 2719 3094 -814 -456 -365 O ATOM 965 ND2 ASN A 242 49.677 14.008 -24.685 1.00 21.42 N ANISOU 965 ND2 ASN A 242 2770 2587 2782 -831 -495 -367 N ATOM 966 N LYS A 243 53.536 11.938 -28.228 1.00 23.12 N ANISOU 966 N LYS A 243 3250 2667 2867 -669 -546 -649 N ATOM 967 CA LYS A 243 53.761 11.279 -29.511 1.00 25.58 C ANISOU 967 CA LYS A 243 3606 2979 3136 -654 -589 -747 C ATOM 968 C LYS A 243 54.613 10.020 -29.366 1.00 25.38 C ANISOU 968 C LYS A 243 3643 2847 3155 -639 -598 -810 C ATOM 969 O LYS A 243 54.494 9.091 -30.163 1.00 24.38 O ANISOU 969 O LYS A 243 3532 2701 3029 -638 -627 -886 O ATOM 970 CB LYS A 243 54.416 12.245 -30.499 1.00 28.59 C ANISOU 970 CB LYS A 243 3989 3457 3419 -586 -560 -762 C ATOM 971 CG LYS A 243 53.519 13.403 -30.908 1.00 30.54 C ANISOU 971 CG LYS A 243 4182 3805 3617 -597 -569 -711 C ATOM 972 CD LYS A 243 54.185 14.290 -31.947 1.00 32.25 C ANISOU 972 CD LYS A 243 4409 4111 3732 -537 -546 -719 C ATOM 973 CE LYS A 243 53.308 15.485 -32.291 1.00 31.11 C ANISOU 973 CE LYS A 243 4216 4057 3548 -543 -561 -658 C ATOM 974 NZ LYS A 243 53.951 16.377 -33.290 1.00 31.17 N ANISOU 974 NZ LYS A 243 4238 4150 3456 -493 -542 -652 N ATOM 975 N GLU A 244 55.464 9.990 -28.345 1.00 24.61 N ANISOU 975 N GLU A 244 3560 2693 3098 -612 -555 -769 N ATOM 976 CA GLU A 244 56.315 8.831 -28.088 1.00 28.45 C ANISOU 976 CA GLU A 244 4091 3083 3637 -583 -551 -811 C ATOM 977 C GLU A 244 55.511 7.588 -27.721 1.00 29.51 C ANISOU 977 C GLU A 244 4222 3141 3851 -642 -581 -808 C ATOM 978 O GLU A 244 56.018 6.468 -27.802 1.00 32.40 O ANISOU 978 O GLU A 244 4627 3430 4252 -624 -588 -853 O ATOM 979 CB GLU A 244 57.312 9.133 -26.967 1.00 34.99 C ANISOU 979 CB GLU A 244 4932 3869 4493 -548 -507 -757 C ATOM 980 CG GLU A 244 58.513 9.957 -27.388 1.00 40.79 C ANISOU 980 CG GLU A 244 5667 4671 5161 -464 -453 -771 C ATOM 981 CD GLU A 244 59.598 9.972 -26.326 1.00 45.79 C ANISOU 981 CD GLU A 244 6308 5256 5833 -422 -410 -729 C ATOM 982 OE1 GLU A 244 59.566 10.863 -25.453 1.00 45.90 O ANISOU 982 OE1 GLU A 244 6287 5303 5850 -429 -370 -643 O ATOM 983 OE2 GLU A 244 60.480 9.088 -26.361 1.00 50.27 O ANISOU 983 OE2 GLU A 244 6919 5754 6430 -379 -421 -787 O ATOM 984 N SER A 245 54.264 7.785 -27.309 1.00 27.18 N ANISOU 984 N SER A 245 3878 2868 3581 -714 -599 -752 N ATOM 985 CA SER A 245 53.438 6.675 -26.849 1.00 29.83 C ANISOU 985 CA SER A 245 4205 3138 3992 -779 -623 -735 C ATOM 986 C SER A 245 52.186 6.497 -27.702 1.00 32.32 C ANISOU 986 C SER A 245 4485 3499 4295 -833 -669 -771 C ATOM 987 O SER A 245 51.301 5.711 -27.362 1.00 33.77 O ANISOU 987 O SER A 245 4650 3644 4536 -899 -692 -753 O ATOM 988 CB SER A 245 53.047 6.880 -25.383 1.00 29.53 C ANISOU 988 CB SER A 245 4135 3082 4005 -823 -596 -629 C ATOM 989 OG SER A 245 54.195 7.047 -24.567 1.00 26.44 O ANISOU 989 OG SER A 245 3773 2650 3622 -774 -557 -595 O ATOM 990 N GLY A 246 52.114 7.229 -28.810 1.00 32.51 N ANISOU 990 N GLY A 246 4500 3610 4242 -806 -684 -819 N ATOM 991 CA GLY A 246 50.964 7.159 -29.693 1.00 33.73 C ANISOU 991 CA GLY A 246 4619 3821 4377 -850 -732 -855 C ATOM 992 C GLY A 246 49.708 7.678 -29.023 1.00 33.31 C ANISOU 992 C GLY A 246 4491 3810 4356 -912 -740 -776 C ATOM 993 O GLY A 246 48.591 7.351 -29.426 1.00 34.45 O ANISOU 993 O GLY A 246 4595 3979 4515 -965 -780 -792 O ATOM 994 N LEU A 247 49.901 8.491 -27.990 1.00 31.32 N ANISOU 994 N LEU A 247 4218 3570 4111 -907 -698 -693 N ATOM 995 CA LEU A 247 48.799 9.055 -27.222 1.00 32.10 C ANISOU 995 CA LEU A 247 4241 3718 4236 -961 -690 -614 C ATOM 996 C LEU A 247 48.375 10.410 -27.775 1.00 30.88 C ANISOU 996 C LEU A 247 4042 3676 4014 -943 -698 -600 C ATOM 997 O LEU A 247 49.215 11.240 -28.120 1.00 29.56 O ANISOU 997 O LEU A 247 3905 3542 3783 -888 -680 -606 O ATOM 998 CB LEU A 247 49.195 9.191 -25.749 1.00 31.68 C ANISOU 998 CB LEU A 247 4187 3627 4224 -967 -636 -532 C ATOM 999 CG LEU A 247 48.242 9.978 -24.848 1.00 30.19 C ANISOU 999 CG LEU A 247 3919 3505 4047 -1009 -611 -450 C ATOM 1000 CD1 LEU A 247 46.904 9.264 -24.724 1.00 33.79 C ANISOU 1000 CD1 LEU A 247 4319 3966 4553 -1083 -638 -440 C ATOM 1001 CD2 LEU A 247 48.864 10.211 -23.481 1.00 25.78 C ANISOU 1001 CD2 LEU A 247 3370 2918 3509 -1001 -553 -379 C ATOM 1002 N VAL A 248 47.067 10.628 -27.861 1.00 31.54 N ANISOU 1002 N VAL A 248 4053 3822 4110 -989 -725 -580 N ATOM 1003 CA VAL A 248 46.534 11.902 -28.326 1.00 29.93 C ANISOU 1003 CA VAL A 248 3795 3726 3849 -972 -737 -559 C ATOM 1004 C VAL A 248 45.438 12.393 -27.388 1.00 29.06 C ANISOU 1004 C VAL A 248 3594 3668 3780 -1014 -720 -488 C ATOM 1005 O VAL A 248 44.366 11.796 -27.303 1.00 36.27 O ANISOU 1005 O VAL A 248 4456 4586 4741 -1068 -745 -487 O ATOM 1006 CB VAL A 248 45.973 11.799 -29.756 1.00 33.80 C ANISOU 1006 CB VAL A 248 4280 4268 4295 -966 -802 -625 C ATOM 1007 CG1 VAL A 248 45.355 13.124 -30.177 1.00 35.53 C ANISOU 1007 CG1 VAL A 248 4440 4601 4459 -946 -819 -592 C ATOM 1008 CG2 VAL A 248 47.068 11.384 -30.727 1.00 33.64 C ANISOU 1008 CG2 VAL A 248 4345 4216 4221 -917 -813 -702 C ATOM 1009 N TYR A 249 45.721 13.482 -26.681 1.00 22.83 N ANISOU 1009 N TYR A 249 2780 2920 2972 -990 -675 -431 N ATOM 1010 CA TYR A 249 44.770 14.066 -25.742 1.00 22.76 C ANISOU 1010 CA TYR A 249 2679 2971 2996 -1017 -650 -369 C ATOM 1011 C TYR A 249 43.615 14.781 -26.439 1.00 21.78 C ANISOU 1011 C TYR A 249 2474 2950 2852 -1013 -693 -373 C ATOM 1012 O TYR A 249 43.814 15.492 -27.423 1.00 20.44 O ANISOU 1012 O TYR A 249 2317 2824 2624 -956 -719 -394 O ATOM 1013 CB TYR A 249 45.476 15.062 -24.817 1.00 21.45 C ANISOU 1013 CB TYR A 249 2514 2817 2820 -953 -575 -315 C ATOM 1014 CG TYR A 249 46.149 14.468 -23.600 1.00 19.29 C ANISOU 1014 CG TYR A 249 2277 2469 2585 -977 -525 -282 C ATOM 1015 CD1 TYR A 249 45.874 13.174 -23.177 1.00 21.83 C ANISOU 1015 CD1 TYR A 249 2612 2723 2958 -1048 -539 -282 C ATOM 1016 CD2 TYR A 249 47.052 15.219 -22.862 1.00 15.48 C ANISOU 1016 CD2 TYR A 249 1816 1980 2088 -912 -462 -246 C ATOM 1017 CE1 TYR A 249 46.495 12.644 -22.049 1.00 21.59 C ANISOU 1017 CE1 TYR A 249 2618 2625 2961 -1058 -494 -243 C ATOM 1018 CE2 TYR A 249 47.672 14.704 -21.747 1.00 16.67 C ANISOU 1018 CE2 TYR A 249 1999 2068 2267 -930 -422 -214 C ATOM 1019 CZ TYR A 249 47.394 13.418 -21.343 1.00 17.63 C ANISOU 1019 CZ TYR A 249 2137 2125 2436 -1015 -444 -210 C ATOM 1020 OH TYR A 249 48.021 12.917 -20.226 1.00 17.48 O ANISOU 1020 OH TYR A 249 2154 2045 2444 -1023 -405 -170 O ATOM 1021 N THR A 250 42.411 14.594 -25.915 1.00 20.93 N ANISOU 1021 N THR A 250 2281 2878 2794 -1058 -694 -348 N ATOM 1022 CA THR A 250 41.279 15.432 -26.282 1.00 21.16 C ANISOU 1022 CA THR A 250 2214 3012 2815 -1045 -724 -339 C ATOM 1023 C THR A 250 41.413 16.773 -25.574 1.00 22.95 C ANISOU 1023 C THR A 250 2394 3300 3025 -992 -677 -290 C ATOM 1024 O THR A 250 42.261 16.931 -24.695 1.00 17.70 O ANISOU 1024 O THR A 250 1770 2591 2365 -965 -612 -261 O ATOM 1025 CB THR A 250 39.938 14.795 -25.891 1.00 22.96 C ANISOU 1025 CB THR A 250 2359 3262 3103 -1107 -733 -330 C ATOM 1026 OG1 THR A 250 39.903 14.606 -24.470 1.00 21.61 O ANISOU 1026 OG1 THR A 250 2162 3074 2973 -1138 -665 -278 O ATOM 1027 CG2 THR A 250 39.752 13.456 -26.585 1.00 21.07 C ANISOU 1027 CG2 THR A 250 2162 2956 2887 -1157 -782 -381 C ATOM 1028 N GLU A 251 40.571 17.735 -25.938 1.00 20.61 N ANISOU 1028 N GLU A 251 2019 3095 2718 -951 -703 -282 N ATOM 1029 CA GLU A 251 40.574 19.023 -25.252 1.00 18.18 C ANISOU 1029 CA GLU A 251 1668 2831 2409 -872 -652 -241 C ATOM 1030 C GLU A 251 40.195 18.860 -23.782 1.00 20.91 C ANISOU 1030 C GLU A 251 1953 3190 2802 -912 -589 -206 C ATOM 1031 O GLU A 251 40.715 19.563 -22.916 1.00 19.66 O ANISOU 1031 O GLU A 251 1802 3025 2642 -858 -526 -177 O ATOM 1032 CB GLU A 251 39.625 20.004 -25.940 1.00 22.41 C ANISOU 1032 CB GLU A 251 2124 3458 2932 -822 -703 -241 C ATOM 1033 CG GLU A 251 40.119 20.484 -27.292 1.00 23.58 C ANISOU 1033 CG GLU A 251 2338 3603 3019 -764 -755 -258 C ATOM 1034 CD GLU A 251 41.471 21.175 -27.211 1.00 27.16 C ANISOU 1034 CD GLU A 251 2881 4002 3436 -690 -706 -238 C ATOM 1035 OE1 GLU A 251 41.726 21.890 -26.217 1.00 25.90 O ANISOU 1035 OE1 GLU A 251 2706 3836 3298 -648 -647 -204 O ATOM 1036 OE2 GLU A 251 42.282 20.999 -28.144 1.00 29.82 O ANISOU 1036 OE2 GLU A 251 3302 4308 3720 -676 -727 -258 O ATOM 1037 N ASP A 252 39.293 17.925 -23.501 1.00 20.94 N ANISOU 1037 N ASP A 252 1901 3209 2847 -1003 -603 -208 N ATOM 1038 CA ASP A 252 38.875 17.676 -22.127 1.00 25.53 C ANISOU 1038 CA ASP A 252 2430 3802 3467 -1038 -536 -170 C ATOM 1039 C ASP A 252 40.021 17.088 -21.312 1.00 24.74 C ANISOU 1039 C ASP A 252 2419 3613 3366 -1061 -484 -148 C ATOM 1040 O ASP A 252 40.186 17.410 -20.137 1.00 24.87 O ANISOU 1040 O ASP A 252 2414 3646 3387 -1055 -419 -112 O ATOM 1041 CB ASP A 252 37.663 16.743 -22.087 1.00 29.83 C ANISOU 1041 CB ASP A 252 2917 4359 4057 -1107 -554 -172 C ATOM 1042 CG ASP A 252 37.163 16.503 -20.674 1.00 35.96 C ANISOU 1042 CG ASP A 252 3638 5162 4865 -1145 -483 -128 C ATOM 1043 OD1 ASP A 252 36.490 17.397 -20.119 1.00 34.57 O ANISOU 1043 OD1 ASP A 252 3367 5079 4690 -1108 -451 -114 O ATOM 1044 OD2 ASP A 252 37.442 15.419 -20.118 1.00 40.81 O ANISOU 1044 OD2 ASP A 252 4303 5703 5499 -1207 -460 -109 O ATOM 1045 N GLU A 253 40.812 16.225 -21.942 1.00 23.01 N ANISOU 1045 N GLU A 253 2300 3300 3141 -1081 -514 -174 N ATOM 1046 CA GLU A 253 41.963 15.632 -21.274 1.00 17.80 C ANISOU 1046 CA GLU A 253 1731 2547 2483 -1093 -474 -157 C ATOM 1047 C GLU A 253 43.033 16.683 -21.004 1.00 17.83 C ANISOU 1047 C GLU A 253 1776 2549 2451 -1007 -431 -145 C ATOM 1048 O GLU A 253 43.686 16.658 -19.958 1.00 17.71 O ANISOU 1048 O GLU A 253 1790 2501 2440 -1001 -375 -112 O ATOM 1049 CB GLU A 253 42.536 14.482 -22.104 1.00 22.97 C ANISOU 1049 CB GLU A 253 2480 3104 3144 -1115 -519 -199 C ATOM 1050 CG GLU A 253 41.597 13.290 -22.212 1.00 31.56 C ANISOU 1050 CG GLU A 253 3545 4166 4280 -1183 -548 -208 C ATOM 1051 CD GLU A 253 42.189 12.145 -23.007 1.00 37.61 C ANISOU 1051 CD GLU A 253 4402 4832 5056 -1198 -592 -259 C ATOM 1052 OE1 GLU A 253 42.415 12.317 -24.223 1.00 36.21 O ANISOU 1052 OE1 GLU A 253 4255 4660 4844 -1166 -641 -314 O ATOM 1053 OE2 GLU A 253 42.430 11.072 -22.413 1.00 41.40 O ANISOU 1053 OE2 GLU A 253 4924 5231 5575 -1237 -578 -245 O ATOM 1054 N TRP A 254 43.206 17.612 -21.941 1.00 17.48 N ANISOU 1054 N TRP A 254 1739 2533 2370 -927 -455 -169 N ATOM 1055 CA TRP A 254 44.139 18.715 -21.740 1.00 16.62 C ANISOU 1055 CA TRP A 254 1667 2418 2230 -832 -413 -154 C ATOM 1056 C TRP A 254 43.711 19.572 -20.555 1.00 17.61 C ANISOU 1056 C TRP A 254 1722 2601 2370 -805 -358 -118 C ATOM 1057 O TRP A 254 44.538 19.968 -19.736 1.00 17.59 O ANISOU 1057 O TRP A 254 1754 2569 2359 -767 -305 -97 O ATOM 1058 CB TRP A 254 44.253 19.580 -22.999 1.00 16.75 C ANISOU 1058 CB TRP A 254 1698 2461 2205 -762 -454 -176 C ATOM 1059 CG TRP A 254 45.156 18.997 -24.043 1.00 15.91 C ANISOU 1059 CG TRP A 254 1684 2297 2065 -759 -485 -212 C ATOM 1060 CD1 TRP A 254 44.809 18.607 -25.305 1.00 18.21 C ANISOU 1060 CD1 TRP A 254 1985 2602 2331 -777 -551 -253 C ATOM 1061 CD2 TRP A 254 46.555 18.724 -23.908 1.00 17.24 C ANISOU 1061 CD2 TRP A 254 1943 2392 2218 -735 -451 -216 C ATOM 1062 NE1 TRP A 254 45.908 18.115 -25.966 1.00 16.99 N ANISOU 1062 NE1 TRP A 254 1923 2390 2143 -763 -555 -286 N ATOM 1063 CE2 TRP A 254 46.992 18.173 -25.130 1.00 16.73 C ANISOU 1063 CE2 TRP A 254 1937 2302 2117 -736 -494 -264 C ATOM 1064 CE3 TRP A 254 47.480 18.892 -22.872 1.00 15.50 C ANISOU 1064 CE3 TRP A 254 1755 2128 2006 -711 -389 -188 C ATOM 1065 CZ2 TRP A 254 48.315 17.790 -25.344 1.00 15.00 C ANISOU 1065 CZ2 TRP A 254 1803 2020 1876 -711 -474 -285 C ATOM 1066 CZ3 TRP A 254 48.793 18.511 -23.087 1.00 15.95 C ANISOU 1066 CZ3 TRP A 254 1896 2119 2044 -689 -374 -205 C ATOM 1067 CH2 TRP A 254 49.198 17.967 -24.314 1.00 16.88 C ANISOU 1067 CH2 TRP A 254 2066 2217 2131 -687 -414 -254 C ATOM 1068 N GLN A 255 42.415 19.849 -20.459 1.00 17.14 N ANISOU 1068 N GLN A 255 1558 2625 2329 -822 -372 -116 N ATOM 1069 CA GLN A 255 41.901 20.653 -19.357 1.00 21.59 C ANISOU 1069 CA GLN A 255 2044 3256 2904 -793 -320 -93 C ATOM 1070 C GLN A 255 42.089 19.939 -18.019 1.00 20.36 C ANISOU 1070 C GLN A 255 1890 3083 2761 -855 -261 -62 C ATOM 1071 O GLN A 255 42.475 20.559 -17.028 1.00 18.95 O ANISOU 1071 O GLN A 255 1711 2915 2573 -813 -204 -44 O ATOM 1072 CB GLN A 255 40.425 20.991 -19.579 1.00 26.02 C ANISOU 1072 CB GLN A 255 2483 3918 3485 -801 -350 -103 C ATOM 1073 N LYS A 256 41.822 18.637 -18.001 1.00 16.86 N ANISOU 1073 N LYS A 256 1455 2611 2340 -957 -279 -55 N ATOM 1074 CA LYS A 256 41.963 17.842 -16.787 1.00 21.06 C ANISOU 1074 CA LYS A 256 1994 3122 2884 -1029 -231 -15 C ATOM 1075 C LYS A 256 43.412 17.751 -16.317 1.00 24.50 C ANISOU 1075 C LYS A 256 2538 3470 3302 -994 -199 0 C ATOM 1076 O LYS A 256 43.691 17.860 -15.121 1.00 21.09 O ANISOU 1076 O LYS A 256 2105 3048 2861 -995 -143 34 O ATOM 1077 CB LYS A 256 41.398 16.437 -17.004 1.00 25.59 C ANISOU 1077 CB LYS A 256 2581 3650 3491 -1111 -262 -10 C ATOM 1078 CG LYS A 256 39.884 16.361 -16.896 1.00 28.80 C ANISOU 1078 CG LYS A 256 2881 4141 3922 -1144 -265 -6 C ATOM 1079 CD LYS A 256 39.378 14.963 -17.193 1.00 30.54 C ANISOU 1079 CD LYS A 256 3122 4304 4179 -1223 -300 -5 C ATOM 1080 CE LYS A 256 37.923 14.808 -16.780 1.00 31.31 C ANISOU 1080 CE LYS A 256 3111 4485 4301 -1267 -287 11 C ATOM 1081 NZ LYS A 256 37.046 15.829 -17.415 1.00 31.02 N ANISOU 1081 NZ LYS A 256 2976 4549 4260 -1220 -312 -21 N ATOM 1082 N GLU A 257 44.331 17.547 -17.255 1.00 15.41 N ANISOU 1082 N GLU A 257 1476 2238 2142 -962 -235 -28 N ATOM 1083 CA GLU A 257 45.746 17.472 -16.910 1.00 21.30 C ANISOU 1083 CA GLU A 257 2318 2904 2873 -923 -209 -20 C ATOM 1084 C GLU A 257 46.242 18.815 -16.381 1.00 19.98 C ANISOU 1084 C GLU A 257 2143 2770 2678 -832 -163 -13 C ATOM 1085 O GLU A 257 47.058 18.866 -15.462 1.00 17.19 O ANISOU 1085 O GLU A 257 1829 2387 2315 -816 -121 11 O ATOM 1086 CB GLU A 257 46.578 17.029 -18.117 1.00 19.52 C ANISOU 1086 CB GLU A 257 2177 2601 2640 -902 -256 -60 C ATOM 1087 CG GLU A 257 46.372 15.572 -18.506 1.00 22.19 C ANISOU 1087 CG GLU A 257 2547 2877 3009 -989 -302 -73 C ATOM 1088 CD GLU A 257 46.812 14.609 -17.415 1.00 24.62 C ANISOU 1088 CD GLU A 257 2894 3117 3342 -1046 -278 -33 C ATOM 1089 OE1 GLU A 257 46.243 13.499 -17.332 1.00 28.00 O ANISOU 1089 OE1 GLU A 257 3323 3510 3805 -1098 -297 -25 O ATOM 1090 OE2 GLU A 257 47.730 14.958 -16.646 1.00 24.93 O ANISOU 1090 OE2 GLU A 257 2970 3135 3366 -1000 -234 -8 O ATOM 1091 N TRP A 258 45.736 19.901 -16.959 1.00 20.55 N ANISOU 1091 N TRP A 258 2166 2902 2740 -772 -176 -33 N ATOM 1092 CA TRP A 258 46.091 21.237 -16.500 1.00 18.51 C ANISOU 1092 CA TRP A 258 1898 2671 2464 -686 -141 -30 C ATOM 1093 C TRP A 258 45.533 21.499 -15.105 1.00 20.93 C ANISOU 1093 C TRP A 258 2139 3039 2773 -697 -86 -8 C ATOM 1094 O TRP A 258 46.210 22.084 -14.258 1.00 20.11 O ANISOU 1094 O TRP A 258 2059 2928 2655 -654 -44 1 O ATOM 1095 CB TRP A 258 45.585 22.297 -17.474 1.00 17.91 C ANISOU 1095 CB TRP A 258 1785 2638 2382 -622 -177 -53 C ATOM 1096 CG TRP A 258 45.870 23.693 -17.018 1.00 17.91 C ANISOU 1096 CG TRP A 258 1776 2656 2373 -534 -149 -51 C ATOM 1097 CD1 TRP A 258 44.972 24.597 -16.533 1.00 17.48 C ANISOU 1097 CD1 TRP A 258 1638 2674 2330 -494 -137 -57 C ATOM 1098 CD2 TRP A 258 47.147 24.344 -16.995 1.00 17.41 C ANISOU 1098 CD2 TRP A 258 1787 2535 2291 -477 -133 -47 C ATOM 1099 NE1 TRP A 258 45.609 25.773 -16.216 1.00 19.74 N ANISOU 1099 NE1 TRP A 258 1950 2942 2608 -413 -118 -59 N ATOM 1100 CE2 TRP A 258 46.945 25.642 -16.490 1.00 17.81 C ANISOU 1100 CE2 TRP A 258 1802 2619 2346 -406 -115 -50 C ATOM 1101 CE3 TRP A 258 48.441 23.953 -17.354 1.00 16.32 C ANISOU 1101 CE3 TRP A 258 1740 2324 2137 -477 -133 -44 C ATOM 1102 CZ2 TRP A 258 47.989 26.554 -16.335 1.00 19.37 C ANISOU 1102 CZ2 TRP A 258 2055 2773 2534 -346 -101 -47 C ATOM 1103 CZ3 TRP A 258 49.475 24.860 -17.199 1.00 17.85 C ANISOU 1103 CZ3 TRP A 258 1980 2484 2317 -417 -114 -38 C ATOM 1104 CH2 TRP A 258 49.243 26.145 -16.694 1.00 17.25 C ANISOU 1104 CH2 TRP A 258 1870 2437 2247 -356 -100 -38 C ATOM 1105 N ASN A 259 44.299 21.061 -14.874 1.00 17.83 N ANISOU 1105 N ASN A 259 1662 2715 2399 -758 -88 -2 N ATOM 1106 CA ASN A 259 43.669 21.200 -13.566 1.00 20.75 C ANISOU 1106 CA ASN A 259 1958 3161 2764 -780 -32 18 C ATOM 1107 C ASN A 259 44.468 20.522 -12.461 1.00 19.47 C ANISOU 1107 C ASN A 259 1855 2957 2588 -823 11 55 C ATOM 1108 O ASN A 259 44.562 21.042 -11.348 1.00 15.58 O ANISOU 1108 O ASN A 259 1342 2507 2072 -798 64 66 O ATOM 1109 CB ASN A 259 42.249 20.631 -13.587 1.00 25.60 C ANISOU 1109 CB ASN A 259 2471 3855 3400 -857 -43 23 C ATOM 1110 CG ASN A 259 41.288 21.489 -14.378 1.00 28.64 C ANISOU 1110 CG ASN A 259 2772 4310 3798 -804 -78 -12 C ATOM 1111 OD1 ASN A 259 41.569 22.651 -14.674 1.00 27.72 O ANISOU 1111 OD1 ASN A 259 2665 4194 3674 -704 -84 -36 O ATOM 1112 ND2 ASN A 259 40.136 20.922 -14.720 1.00 33.64 N ANISOU 1112 ND2 ASN A 259 3324 5003 4455 -873 -105 -13 N ATOM 1113 N GLU A 260 45.038 19.360 -12.763 1.00 18.20 N ANISOU 1113 N GLU A 260 1767 2710 2438 -884 -15 73 N ATOM 1114 CA GLU A 260 45.829 18.642 -11.772 1.00 19.45 C ANISOU 1114 CA GLU A 260 1986 2818 2586 -923 15 114 C ATOM 1115 C GLU A 260 47.099 19.413 -11.424 1.00 15.43 C ANISOU 1115 C GLU A 260 1542 2269 2051 -838 38 107 C ATOM 1116 O GLU A 260 47.527 19.410 -10.272 1.00 14.76 O ANISOU 1116 O GLU A 260 1473 2192 1944 -842 80 136 O ATOM 1117 CB GLU A 260 46.179 17.233 -12.259 1.00 23.81 C ANISOU 1117 CB GLU A 260 2606 3275 3166 -997 -29 129 C ATOM 1118 CG GLU A 260 47.088 16.447 -11.310 1.00 32.84 C ANISOU 1118 CG GLU A 260 3825 4348 4304 -1023 -9 173 C ATOM 1119 CD GLU A 260 46.469 16.186 -9.937 1.00 41.97 C ANISOU 1119 CD GLU A 260 4942 5562 5444 -1054 39 221 C ATOM 1120 OE1 GLU A 260 46.576 15.040 -9.447 1.00 45.23 O ANISOU 1120 OE1 GLU A 260 5400 5917 5869 -1097 31 260 O ATOM 1121 OE2 GLU A 260 45.895 17.119 -9.336 1.00 43.77 O ANISOU 1121 OE2 GLU A 260 5094 5893 5643 -1033 83 219 O ATOM 1122 N LEU A 261 47.694 20.074 -12.415 1.00 12.98 N ANISOU 1122 N LEU A 261 1269 1921 1742 -765 10 70 N ATOM 1123 CA LEU A 261 48.881 20.892 -12.174 1.00 14.37 C ANISOU 1123 CA LEU A 261 1500 2063 1898 -688 29 63 C ATOM 1124 C LEU A 261 48.551 22.074 -11.267 1.00 15.23 C ANISOU 1124 C LEU A 261 1555 2245 1987 -636 72 57 C ATOM 1125 O LEU A 261 49.340 22.435 -10.391 1.00 14.06 O ANISOU 1125 O LEU A 261 1439 2086 1818 -607 104 65 O ATOM 1126 CB LEU A 261 49.477 21.393 -13.490 1.00 17.85 C ANISOU 1126 CB LEU A 261 1983 2460 2340 -630 -9 30 C ATOM 1127 CG LEU A 261 50.273 20.383 -14.320 1.00 20.91 C ANISOU 1127 CG LEU A 261 2445 2764 2736 -654 -44 24 C ATOM 1128 CD1 LEU A 261 50.712 21.012 -15.637 1.00 17.53 C ANISOU 1128 CD1 LEU A 261 2044 2319 2296 -598 -75 -8 C ATOM 1129 CD2 LEU A 261 51.476 19.875 -13.536 1.00 19.20 C ANISOU 1129 CD2 LEU A 261 2296 2485 2515 -656 -22 45 C ATOM 1130 N ILE A 262 47.383 22.670 -11.482 1.00 13.18 N ANISOU 1130 N ILE A 262 1210 2062 1734 -622 70 37 N ATOM 1131 CA ILE A 262 46.910 23.761 -10.638 1.00 16.58 C ANISOU 1131 CA ILE A 262 1579 2569 2151 -569 108 21 C ATOM 1132 C ILE A 262 46.657 23.270 -9.214 1.00 16.04 C ANISOU 1132 C ILE A 262 1482 2554 2057 -621 162 48 C ATOM 1133 O ILE A 262 47.054 23.914 -8.241 1.00 16.58 O ANISOU 1133 O ILE A 262 1556 2646 2099 -580 201 42 O ATOM 1134 CB ILE A 262 45.616 24.391 -11.197 1.00 19.68 C ANISOU 1134 CB ILE A 262 1877 3036 2562 -542 90 -8 C ATOM 1135 CG1 ILE A 262 45.871 25.022 -12.569 1.00 17.78 C ANISOU 1135 CG1 ILE A 262 1668 2749 2339 -484 35 -30 C ATOM 1136 CG2 ILE A 262 45.061 25.424 -10.225 1.00 21.46 C ANISOU 1136 CG2 ILE A 262 2032 3345 2776 -485 132 -33 C ATOM 1137 CD1 ILE A 262 46.638 26.320 -12.515 1.00 19.60 C ANISOU 1137 CD1 ILE A 262 1936 2947 2563 -391 38 -48 C ATOM 1138 N LYS A 263 45.996 22.123 -9.100 1.00 16.65 N ANISOU 1138 N LYS A 263 1531 2653 2142 -715 162 81 N ATOM 1139 CA LYS A 263 45.685 21.547 -7.799 1.00 21.67 C ANISOU 1139 CA LYS A 263 2139 3346 2750 -781 212 120 C ATOM 1140 C LYS A 263 46.948 21.253 -6.994 1.00 20.41 C ANISOU 1140 C LYS A 263 2069 3125 2562 -781 229 150 C ATOM 1141 O LYS A 263 47.002 21.526 -5.797 1.00 20.03 O ANISOU 1141 O LYS A 263 2005 3133 2472 -778 277 162 O ATOM 1142 CB LYS A 263 44.861 20.268 -7.958 1.00 27.61 C ANISOU 1142 CB LYS A 263 2858 4111 3522 -895 198 159 C ATOM 1143 CG LYS A 263 44.659 19.519 -6.650 1.00 32.69 C ANISOU 1143 CG LYS A 263 3505 4781 4136 -951 239 211 C ATOM 1144 CD LYS A 263 43.488 18.556 -6.714 1.00 38.50 C ANISOU 1144 CD LYS A 263 4197 5536 4893 -1020 226 236 C ATOM 1145 CE LYS A 263 43.263 17.901 -5.359 1.00 43.54 C ANISOU 1145 CE LYS A 263 4842 6205 5497 -1065 267 288 C ATOM 1146 NZ LYS A 263 43.261 18.903 -4.252 1.00 45.74 N ANISOU 1146 NZ LYS A 263 5081 6580 5719 -1013 328 274 N ATOM 1147 N LEU A 264 47.961 20.701 -7.656 1.00 19.26 N ANISOU 1147 N LEU A 264 2013 2868 2436 -783 189 159 N ATOM 1148 CA LEU A 264 49.225 20.389 -6.995 1.00 20.86 C ANISOU 1148 CA LEU A 264 2300 3007 2620 -778 197 185 C ATOM 1149 C LEU A 264 49.882 21.649 -6.444 1.00 20.37 C ANISOU 1149 C LEU A 264 2247 2964 2528 -689 223 155 C ATOM 1150 O LEU A 264 50.454 21.639 -5.355 1.00 18.24 O ANISOU 1150 O LEU A 264 2004 2704 2222 -690 251 176 O ATOM 1151 CB LEU A 264 50.185 19.684 -7.958 1.00 16.21 C ANISOU 1151 CB LEU A 264 1795 2301 2062 -779 147 186 C ATOM 1152 CG LEU A 264 49.809 18.267 -8.392 1.00 18.19 C ANISOU 1152 CG LEU A 264 2062 2503 2344 -868 113 215 C ATOM 1153 CD1 LEU A 264 50.842 17.708 -9.365 1.00 13.97 C ANISOU 1153 CD1 LEU A 264 1612 1857 1838 -849 65 198 C ATOM 1154 CD2 LEU A 264 49.649 17.352 -7.184 1.00 20.17 C ANISOU 1154 CD2 LEU A 264 2319 2763 2580 -944 135 279 C ATOM 1155 N ALA A 265 49.797 22.734 -7.206 1.00 17.91 N ANISOU 1155 N ALA A 265 1917 2658 2232 -615 209 106 N ATOM 1156 CA ALA A 265 50.400 23.995 -6.795 1.00 15.89 C ANISOU 1156 CA ALA A 265 1671 2407 1957 -532 225 72 C ATOM 1157 C ALA A 265 49.610 24.643 -5.661 1.00 18.10 C ANISOU 1157 C ALA A 265 1881 2792 2205 -516 273 55 C ATOM 1158 O ALA A 265 50.173 25.344 -4.828 1.00 21.72 O ANISOU 1158 O ALA A 265 2357 3262 2634 -472 296 38 O ATOM 1159 CB ALA A 265 50.502 24.939 -7.978 1.00 17.61 C ANISOU 1159 CB ALA A 265 1892 2593 2205 -464 190 33 C ATOM 1160 N SER A 266 48.303 24.400 -5.633 1.00 20.52 N ANISOU 1160 N SER A 266 2104 3180 2514 -553 288 57 N ATOM 1161 CA SER A 266 47.429 25.025 -4.646 1.00 23.97 C ANISOU 1161 CA SER A 266 2458 3732 2918 -534 337 32 C ATOM 1162 C SER A 266 47.515 24.380 -3.259 1.00 26.60 C ANISOU 1162 C SER A 266 2792 4119 3194 -594 386 73 C ATOM 1163 O SER A 266 47.290 25.053 -2.253 1.00 30.33 O ANISOU 1163 O SER A 266 3228 4675 3623 -560 430 45 O ATOM 1164 CB SER A 266 45.976 24.996 -5.134 1.00 25.44 C ANISOU 1164 CB SER A 266 2541 3997 3127 -553 337 18 C ATOM 1165 OG SER A 266 45.461 23.678 -5.105 1.00 29.13 O ANISOU 1165 OG SER A 266 2991 4482 3596 -661 340 72 O ATOM 1166 N GLN A 289 47.828 23.088 -3.204 1.00 25.26 N ANISOU 1166 N GLN A 289 2668 3904 3023 -682 376 137 N ATOM 1167 CA GLN A 289 47.831 22.364 -1.933 1.00 27.87 C ANISOU 1167 CA GLN A 289 3003 4287 3300 -752 416 191 C ATOM 1168 C GLN A 289 49.184 22.397 -1.227 1.00 26.03 C ANISOU 1168 C GLN A 289 2859 3997 3033 -727 414 207 C ATOM 1169 O GLN A 289 50.183 21.925 -1.769 1.00 25.21 O ANISOU 1169 O GLN A 289 2836 3782 2959 -728 371 226 O ATOM 1170 CB GLN A 289 47.403 20.911 -2.144 1.00 32.46 C ANISOU 1170 CB GLN A 289 3600 4828 3907 -845 391 255 C ATOM 1171 CG GLN A 289 47.381 20.092 -0.857 1.00 38.24 C ANISOU 1171 CG GLN A 289 4359 5577 4593 -890 411 312 C ATOM 1172 CD GLN A 289 46.641 18.778 -1.000 1.00 42.54 C ANISOU 1172 CD GLN A 289 4902 6096 5168 -971 389 364 C ATOM 1173 OE1 GLN A 289 46.667 18.149 -2.057 1.00 42.23 O ANISOU 1173 OE1 GLN A 289 4887 5975 5184 -998 343 369 O ATOM 1174 NE2 GLN A 289 45.968 18.359 0.068 1.00 45.99 N ANISOU 1174 NE2 GLN A 289 5310 6603 5564 -1010 421 399 N ATOM 1175 N PRO A 290 49.215 22.947 0.002 1.00 27.41 N ANISOU 1175 N PRO A 290 3015 4255 3143 -705 460 195 N ATOM 1176 CA PRO A 290 50.472 23.009 0.755 1.00 24.46 C ANISOU 1176 CA PRO A 290 2722 3840 2733 -683 455 208 C ATOM 1177 C PRO A 290 51.013 21.621 1.079 1.00 19.84 C ANISOU 1177 C PRO A 290 2203 3194 2141 -763 434 294 C ATOM 1178 O PRO A 290 50.237 20.717 1.387 1.00 18.12 O ANISOU 1178 O PRO A 290 1967 2993 1925 -819 434 337 O ATOM 1179 CB PRO A 290 50.076 23.752 2.036 1.00 26.96 C ANISOU 1179 CB PRO A 290 2990 4282 2973 -658 512 177 C ATOM 1180 CG PRO A 290 48.621 23.467 2.183 1.00 28.85 C ANISOU 1180 CG PRO A 290 3145 4604 3211 -689 537 181 C ATOM 1181 CD PRO A 290 48.096 23.506 0.782 1.00 26.87 C ANISOU 1181 CD PRO A 290 2856 4322 3033 -691 512 163 C ATOM 1182 N GLY A 291 52.328 21.459 0.990 1.00 20.81 N ANISOU 1182 N GLY A 291 2410 3223 2274 -743 399 307 N ATOM 1183 CA GLY A 291 52.971 20.201 1.322 1.00 24.07 C ANISOU 1183 CA GLY A 291 2892 3563 2689 -795 368 380 C ATOM 1184 C GLY A 291 53.062 19.233 0.159 1.00 27.26 C ANISOU 1184 C GLY A 291 3331 3859 3168 -827 318 402 C ATOM 1185 O GLY A 291 53.805 18.254 0.210 1.00 29.47 O ANISOU 1185 O GLY A 291 3678 4050 3468 -844 279 446 O ATOM 1186 N GLU A 292 52.307 19.507 -0.897 1.00 23.24 N ANISOU 1186 N GLU A 292 2773 3358 2700 -828 317 367 N ATOM 1187 CA GLU A 292 52.299 18.634 -2.063 1.00 23.67 C ANISOU 1187 CA GLU A 292 2856 3317 2821 -856 269 375 C ATOM 1188 C GLU A 292 53.568 18.781 -2.898 1.00 19.61 C ANISOU 1188 C GLU A 292 2409 2699 2341 -801 229 347 C ATOM 1189 O GLU A 292 54.098 19.882 -3.058 1.00 17.03 O ANISOU 1189 O GLU A 292 2082 2379 2008 -722 234 297 O ATOM 1190 CB GLU A 292 51.071 18.913 -2.928 1.00 25.36 C ANISOU 1190 CB GLU A 292 2994 3579 3064 -870 274 342 C ATOM 1191 CG GLU A 292 50.908 17.939 -4.074 1.00 29.56 C ANISOU 1191 CG GLU A 292 3550 4023 3657 -905 222 347 C ATOM 1192 CD GLU A 292 50.815 16.497 -3.604 1.00 26.58 C ANISOU 1192 CD GLU A 292 3213 3593 3293 -959 200 403 C ATOM 1193 OE1 GLU A 292 51.858 15.808 -3.576 1.00 27.54 O ANISOU 1193 OE1 GLU A 292 3413 3621 3430 -952 167 425 O ATOM 1194 OE2 GLU A 292 49.698 16.052 -3.267 1.00 24.26 O ANISOU 1194 OE2 GLU A 292 2869 3352 2996 -1008 213 425 O ATOM 1195 N SER A 293 54.051 17.662 -3.428 1.00 20.18 N ANISOU 1195 N SER A 293 2539 2674 2455 -835 185 376 N ATOM 1196 CA SER A 293 55.241 17.663 -4.269 1.00 19.16 C ANISOU 1196 CA SER A 293 2470 2449 2361 -776 146 344 C ATOM 1197 C SER A 293 54.927 18.252 -5.647 1.00 15.90 C ANISOU 1197 C SER A 293 2031 2030 1981 -736 133 283 C ATOM 1198 O SER A 293 53.765 18.318 -6.051 1.00 14.37 O ANISOU 1198 O SER A 293 1781 1883 1796 -767 140 273 O ATOM 1199 CB SER A 293 55.804 16.247 -4.399 1.00 21.37 C ANISOU 1199 CB SER A 293 2815 2627 2677 -811 101 383 C ATOM 1200 OG SER A 293 54.830 15.354 -4.905 1.00 26.00 O ANISOU 1200 OG SER A 293 3384 3198 3298 -859 82 389 O ATOM 1201 N LEU A 294 55.965 18.673 -6.364 1.00 10.78 N ANISOU 1201 N LEU A 294 1420 1328 1349 -671 114 245 N ATOM 1202 CA LEU A 294 55.780 19.440 -7.592 1.00 10.37 C ANISOU 1202 CA LEU A 294 1346 1280 1314 -626 105 192 C ATOM 1203 C LEU A 294 56.491 18.830 -8.803 1.00 17.98 C ANISOU 1203 C LEU A 294 2357 2161 2311 -612 65 169 C ATOM 1204 O LEU A 294 57.471 18.097 -8.663 1.00 18.09 O ANISOU 1204 O LEU A 294 2426 2110 2338 -609 46 182 O ATOM 1205 CB LEU A 294 56.257 20.878 -7.377 1.00 9.85 C ANISOU 1205 CB LEU A 294 1267 1251 1226 -554 127 161 C ATOM 1206 CG LEU A 294 55.567 21.610 -6.223 1.00 13.92 C ANISOU 1206 CG LEU A 294 1733 1851 1704 -554 167 166 C ATOM 1207 CD1 LEU A 294 56.291 22.906 -5.885 1.00 16.70 C ANISOU 1207 CD1 LEU A 294 2090 2216 2039 -484 179 134 C ATOM 1208 CD2 LEU A 294 54.103 21.877 -6.556 1.00 13.81 C ANISOU 1208 CD2 LEU A 294 1648 1905 1696 -573 178 152 C ATOM 1209 N GLU A 295 55.988 19.155 -9.991 1.00 17.60 N ANISOU 1209 N GLU A 295 2287 2122 2276 -599 50 132 N ATOM 1210 CA GLU A 295 56.488 18.583 -11.238 1.00 17.07 C ANISOU 1210 CA GLU A 295 2259 1994 2233 -588 14 103 C ATOM 1211 C GLU A 295 57.487 19.482 -11.956 1.00 16.68 C ANISOU 1211 C GLU A 295 2227 1937 2172 -517 16 69 C ATOM 1212 O GLU A 295 57.781 20.592 -11.508 1.00 15.34 O ANISOU 1212 O GLU A 295 2042 1802 1984 -478 40 70 O ATOM 1213 CB GLU A 295 55.327 18.281 -12.188 1.00 17.49 C ANISOU 1213 CB GLU A 295 2281 2065 2300 -625 -9 84 C ATOM 1214 CG GLU A 295 54.351 17.234 -11.683 1.00 19.61 C ANISOU 1214 CG GLU A 295 2531 2332 2586 -709 -18 116 C ATOM 1215 CD GLU A 295 53.374 16.794 -12.756 1.00 23.96 C ANISOU 1215 CD GLU A 295 3058 2888 3158 -748 -52 90 C ATOM 1216 OE1 GLU A 295 52.291 16.280 -12.404 1.00 24.23 O ANISOU 1216 OE1 GLU A 295 3053 2950 3205 -818 -55 115 O ATOM 1217 OE2 GLU A 295 53.691 16.963 -13.953 1.00 25.56 O ANISOU 1217 OE2 GLU A 295 3280 3072 3360 -710 -77 46 O ATOM 1218 N GLU A 296 57.992 18.983 -13.082 1.00 15.62 N ANISOU 1218 N GLU A 296 2126 1760 2050 -504 -11 38 N ATOM 1219 CA GLU A 296 58.917 19.720 -13.936 1.00 11.69 C ANISOU 1219 CA GLU A 296 1642 1261 1538 -447 -9 9 C ATOM 1220 C GLU A 296 58.388 21.106 -14.298 1.00 12.39 C ANISOU 1220 C GLU A 296 1691 1409 1607 -421 3 4 C ATOM 1221 O GLU A 296 59.118 22.097 -14.215 1.00 9.47 O ANISOU 1221 O GLU A 296 1324 1050 1225 -379 19 4 O ATOM 1222 CB GLU A 296 59.201 18.928 -15.219 1.00 12.45 C ANISOU 1222 CB GLU A 296 1768 1321 1640 -445 -38 -30 C ATOM 1223 CG GLU A 296 60.140 19.636 -16.183 1.00 13.92 C ANISOU 1223 CG GLU A 296 1966 1520 1803 -392 -32 -58 C ATOM 1224 CD GLU A 296 60.067 19.085 -17.600 1.00 18.47 C ANISOU 1224 CD GLU A 296 2559 2090 2369 -391 -59 -102 C ATOM 1225 OE1 GLU A 296 60.675 19.695 -18.506 1.00 17.85 O ANISOU 1225 OE1 GLU A 296 2485 2038 2261 -356 -52 -122 O ATOM 1226 OE2 GLU A 296 59.405 18.046 -17.809 1.00 14.70 O ANISOU 1226 OE2 GLU A 296 2091 1584 1911 -430 -87 -118 O ATOM 1227 N PHE A 297 57.121 21.177 -14.700 1.00 12.76 N ANISOU 1227 N PHE A 297 1701 1492 1655 -446 -9 0 N ATOM 1228 CA PHE A 297 56.545 22.450 -15.124 1.00 12.35 C ANISOU 1228 CA PHE A 297 1612 1491 1591 -415 -7 -5 C ATOM 1229 C PHE A 297 56.467 23.454 -13.977 1.00 10.85 C ANISOU 1229 C PHE A 297 1396 1330 1398 -392 22 12 C ATOM 1230 O PHE A 297 56.611 24.660 -14.189 1.00 11.57 O ANISOU 1230 O PHE A 297 1478 1437 1482 -349 25 7 O ATOM 1231 CB PHE A 297 55.154 22.248 -15.727 1.00 9.37 C ANISOU 1231 CB PHE A 297 1192 1149 1219 -446 -32 -14 C ATOM 1232 CG PHE A 297 54.535 23.516 -16.245 1.00 13.18 C ANISOU 1232 CG PHE A 297 1637 1678 1692 -408 -39 -18 C ATOM 1233 CD1 PHE A 297 55.028 24.121 -17.388 1.00 9.23 C ANISOU 1233 CD1 PHE A 297 1159 1174 1173 -373 -58 -28 C ATOM 1234 CD2 PHE A 297 53.472 24.109 -15.584 1.00 13.52 C ANISOU 1234 CD2 PHE A 297 1620 1772 1744 -406 -29 -11 C ATOM 1235 CE1 PHE A 297 54.468 25.292 -17.869 1.00 17.24 C ANISOU 1235 CE1 PHE A 297 2145 2223 2182 -338 -73 -24 C ATOM 1236 CE2 PHE A 297 52.907 25.278 -16.060 1.00 15.87 C ANISOU 1236 CE2 PHE A 297 1884 2104 2040 -363 -44 -17 C ATOM 1237 CZ PHE A 297 53.405 25.871 -17.204 1.00 13.64 C ANISOU 1237 CZ PHE A 297 1633 1808 1744 -330 -69 -20 C ATOM 1238 N HIS A 298 56.229 22.959 -12.765 1.00 11.37 N ANISOU 1238 N HIS A 298 1451 1403 1467 -422 42 31 N ATOM 1239 CA HIS A 298 56.183 23.829 -11.597 1.00 12.57 C ANISOU 1239 CA HIS A 298 1580 1589 1609 -400 72 39 C ATOM 1240 C HIS A 298 57.528 24.521 -11.384 1.00 8.32 C ANISOU 1240 C HIS A 298 1080 1020 1063 -356 80 36 C ATOM 1241 O HIS A 298 57.576 25.683 -10.996 1.00 12.55 O ANISOU 1241 O HIS A 298 1601 1575 1594 -319 91 27 O ATOM 1242 CB HIS A 298 55.784 23.042 -10.347 1.00 9.92 C ANISOU 1242 CB HIS A 298 1233 1272 1266 -447 93 65 C ATOM 1243 CG HIS A 298 54.368 22.555 -10.369 1.00 9.70 C ANISOU 1243 CG HIS A 298 1153 1289 1245 -496 92 72 C ATOM 1244 ND1 HIS A 298 54.039 21.220 -10.310 1.00 10.45 N ANISOU 1244 ND1 HIS A 298 1256 1363 1351 -563 80 95 N ATOM 1245 CD2 HIS A 298 53.196 23.228 -10.451 1.00 13.19 C ANISOU 1245 CD2 HIS A 298 1529 1797 1687 -488 98 58 C ATOM 1246 CE1 HIS A 298 52.724 21.089 -10.349 1.00 11.12 C ANISOU 1246 CE1 HIS A 298 1281 1503 1442 -602 82 98 C ATOM 1247 NE2 HIS A 298 52.189 22.293 -10.436 1.00 14.89 N ANISOU 1247 NE2 HIS A 298 1709 2038 1912 -554 94 73 N ATOM 1248 N VAL A 299 58.615 23.805 -11.648 1.00 8.45 N ANISOU 1248 N VAL A 299 1142 987 1082 -360 71 40 N ATOM 1249 CA VAL A 299 59.945 24.396 -11.577 1.00 9.84 C ANISOU 1249 CA VAL A 299 1346 1138 1254 -323 76 36 C ATOM 1250 C VAL A 299 60.075 25.534 -12.589 1.00 10.13 C ANISOU 1250 C VAL A 299 1378 1182 1290 -288 68 22 C ATOM 1251 O VAL A 299 60.685 26.565 -12.309 1.00 7.39 O ANISOU 1251 O VAL A 299 1034 833 941 -259 75 22 O ATOM 1252 CB VAL A 299 61.052 23.353 -11.838 1.00 13.10 C ANISOU 1252 CB VAL A 299 1801 1503 1674 -328 66 37 C ATOM 1253 CG1 VAL A 299 62.425 23.996 -11.705 1.00 13.53 C ANISOU 1253 CG1 VAL A 299 1872 1542 1724 -292 72 34 C ATOM 1254 CG2 VAL A 299 60.919 22.183 -10.881 1.00 14.59 C ANISOU 1254 CG2 VAL A 299 2002 1673 1868 -364 65 59 C ATOM 1255 N PHE A 300 59.494 25.337 -13.768 1.00 10.69 N ANISOU 1255 N PHE A 300 1442 1259 1360 -295 49 13 N ATOM 1256 CA PHE A 300 59.519 26.351 -14.816 1.00 10.38 C ANISOU 1256 CA PHE A 300 1401 1230 1314 -268 36 9 C ATOM 1257 C PHE A 300 58.770 27.603 -14.364 1.00 9.23 C ANISOU 1257 C PHE A 300 1223 1108 1176 -243 37 12 C ATOM 1258 O PHE A 300 59.257 28.724 -14.524 1.00 9.59 O ANISOU 1258 O PHE A 300 1277 1143 1223 -213 34 17 O ATOM 1259 CB PHE A 300 58.915 25.791 -16.107 1.00 9.46 C ANISOU 1259 CB PHE A 300 1282 1123 1188 -283 12 -1 C ATOM 1260 CG PHE A 300 58.988 26.732 -17.281 1.00 11.73 C ANISOU 1260 CG PHE A 300 1574 1424 1459 -259 -5 3 C ATOM 1261 CD1 PHE A 300 60.211 27.134 -17.791 1.00 13.17 C ANISOU 1261 CD1 PHE A 300 1785 1592 1626 -243 2 9 C ATOM 1262 CD2 PHE A 300 57.832 27.186 -17.893 1.00 9.54 C ANISOU 1262 CD2 PHE A 300 1268 1177 1180 -255 -31 4 C ATOM 1263 CE1 PHE A 300 60.280 27.991 -18.878 1.00 14.45 C ANISOU 1263 CE1 PHE A 300 1954 1770 1768 -229 -13 23 C ATOM 1264 CE2 PHE A 300 57.893 28.039 -18.982 1.00 13.82 C ANISOU 1264 CE2 PHE A 300 1819 1730 1703 -234 -52 17 C ATOM 1265 CZ PHE A 300 59.120 28.443 -19.474 1.00 15.09 C ANISOU 1265 CZ PHE A 300 2014 1876 1845 -224 -42 29 C ATOM 1266 N VAL A 301 57.589 27.406 -13.788 1.00 9.73 N ANISOU 1266 N VAL A 301 1248 1204 1246 -255 40 8 N ATOM 1267 CA VAL A 301 56.788 28.521 -13.297 1.00 9.42 C ANISOU 1267 CA VAL A 301 1170 1193 1215 -224 42 0 C ATOM 1268 C VAL A 301 57.506 29.233 -12.148 1.00 10.37 C ANISOU 1268 C VAL A 301 1303 1301 1336 -200 63 -5 C ATOM 1269 O VAL A 301 57.443 30.456 -12.026 1.00 11.77 O ANISOU 1269 O VAL A 301 1473 1474 1524 -160 56 -15 O ATOM 1270 CB VAL A 301 55.399 28.055 -12.827 1.00 8.65 C ANISOU 1270 CB VAL A 301 1019 1147 1122 -245 48 -7 C ATOM 1271 CG1 VAL A 301 54.608 29.226 -12.273 1.00 11.90 C ANISOU 1271 CG1 VAL A 301 1386 1593 1543 -201 53 -25 C ATOM 1272 CG2 VAL A 301 54.641 27.403 -13.975 1.00 11.62 C ANISOU 1272 CG2 VAL A 301 1380 1535 1500 -271 20 -6 C ATOM 1273 N LEU A 302 58.195 28.456 -11.316 1.00 10.79 N ANISOU 1273 N LEU A 302 1377 1345 1379 -224 83 2 N ATOM 1274 CA LEU A 302 58.957 29.005 -10.198 1.00 11.16 C ANISOU 1274 CA LEU A 302 1437 1383 1420 -207 98 -4 C ATOM 1275 C LEU A 302 60.042 29.972 -10.675 1.00 12.54 C ANISOU 1275 C LEU A 302 1642 1518 1605 -180 84 -5 C ATOM 1276 O LEU A 302 60.312 30.984 -10.025 1.00 12.67 O ANISOU 1276 O LEU A 302 1660 1528 1628 -153 85 -19 O ATOM 1277 CB LEU A 302 59.582 27.874 -9.377 1.00 10.92 C ANISOU 1277 CB LEU A 302 1429 1347 1375 -240 113 11 C ATOM 1278 CG LEU A 302 60.463 28.284 -8.192 1.00 13.19 C ANISOU 1278 CG LEU A 302 1733 1631 1650 -227 124 7 C ATOM 1279 CD1 LEU A 302 59.677 29.130 -7.197 1.00 12.06 C ANISOU 1279 CD1 LEU A 302 1558 1532 1494 -206 140 -16 C ATOM 1280 CD2 LEU A 302 61.056 27.058 -7.502 1.00 11.51 C ANISOU 1280 CD2 LEU A 302 1543 1408 1422 -259 130 31 C ATOM 1281 N ALA A 303 60.660 29.658 -11.809 1.00 11.39 N ANISOU 1281 N ALA A 303 1519 1347 1460 -189 72 9 N ATOM 1282 CA ALA A 303 61.664 30.539 -12.400 1.00 9.82 C ANISOU 1282 CA ALA A 303 1343 1119 1269 -173 61 17 C ATOM 1283 C ALA A 303 61.055 31.897 -12.743 1.00 10.05 C ANISOU 1283 C ALA A 303 1361 1142 1314 -143 42 15 C ATOM 1284 O ALA A 303 61.720 32.934 -12.653 1.00 11.46 O ANISOU 1284 O ALA A 303 1556 1292 1507 -129 32 18 O ATOM 1285 CB ALA A 303 62.267 29.900 -13.637 1.00 12.11 C ANISOU 1285 CB ALA A 303 1652 1401 1547 -189 56 30 C ATOM 1286 N HIS A 304 59.783 31.880 -13.127 1.00 9.50 N ANISOU 1286 N HIS A 304 1264 1098 1246 -135 31 10 N ATOM 1287 CA HIS A 304 59.068 33.102 -13.466 1.00 8.04 C ANISOU 1287 CA HIS A 304 1065 907 1082 -99 5 8 C ATOM 1288 C HIS A 304 58.682 33.887 -12.214 1.00 11.45 C ANISOU 1288 C HIS A 304 1478 1342 1531 -66 12 -23 C ATOM 1289 O HIS A 304 58.715 35.117 -12.212 1.00 12.02 O ANISOU 1289 O HIS A 304 1558 1381 1627 -32 -10 -29 O ATOM 1290 CB HIS A 304 57.825 32.779 -14.302 1.00 8.31 C ANISOU 1290 CB HIS A 304 1069 975 1114 -98 -13 10 C ATOM 1291 CG HIS A 304 58.139 32.359 -15.704 1.00 10.27 C ANISOU 1291 CG HIS A 304 1340 1220 1343 -119 -30 36 C ATOM 1292 ND1 HIS A 304 58.615 31.103 -16.015 1.00 11.09 N ANISOU 1292 ND1 HIS A 304 1458 1332 1424 -156 -15 36 N ATOM 1293 CD2 HIS A 304 58.066 33.034 -16.876 1.00 10.35 C ANISOU 1293 CD2 HIS A 304 1362 1222 1349 -107 -62 60 C ATOM 1294 CE1 HIS A 304 58.814 31.021 -17.319 1.00 14.78 C ANISOU 1294 CE1 HIS A 304 1943 1803 1871 -164 -33 52 C ATOM 1295 NE2 HIS A 304 58.489 32.179 -17.865 1.00 8.40 N ANISOU 1295 NE2 HIS A 304 1135 988 1070 -138 -61 71 N ATOM 1296 N VAL A 305 58.312 33.175 -11.154 1.00 12.88 N ANISOU 1296 N VAL A 305 1636 1561 1697 -78 41 -43 N ATOM 1297 CA VAL A 305 58.001 33.818 -9.881 1.00 14.62 C ANISOU 1297 CA VAL A 305 1837 1797 1920 -48 54 -79 C ATOM 1298 C VAL A 305 59.232 34.526 -9.321 1.00 16.10 C ANISOU 1298 C VAL A 305 2064 1940 2113 -40 50 -86 C ATOM 1299 O VAL A 305 59.150 35.661 -8.845 1.00 8.69 O ANISOU 1299 O VAL A 305 1125 981 1194 -1 37 -116 O ATOM 1300 CB VAL A 305 57.483 32.806 -8.842 1.00 14.57 C ANISOU 1300 CB VAL A 305 1803 1850 1884 -74 90 -88 C ATOM 1301 CG1 VAL A 305 57.395 33.452 -7.466 1.00 16.62 C ANISOU 1301 CG1 VAL A 305 2049 2133 2132 -45 108 -128 C ATOM 1302 CG2 VAL A 305 56.133 32.246 -9.270 1.00 13.17 C ANISOU 1302 CG2 VAL A 305 1576 1722 1707 -84 92 -86 C ATOM 1303 N LEU A 306 60.373 33.848 -9.386 1.00 12.14 N ANISOU 1303 N LEU A 306 1593 1421 1598 -76 58 -62 N ATOM 1304 CA LEU A 306 61.628 34.408 -8.898 1.00 12.84 C ANISOU 1304 CA LEU A 306 1714 1473 1693 -76 52 -66 C ATOM 1305 C LEU A 306 62.239 35.403 -9.882 1.00 14.83 C ANISOU 1305 C LEU A 306 1990 1672 1974 -70 23 -47 C ATOM 1306 O LEU A 306 63.123 36.183 -9.516 1.00 17.43 O ANISOU 1306 O LEU A 306 2339 1964 2318 -69 11 -53 O ATOM 1307 CB LEU A 306 62.633 33.291 -8.614 1.00 8.94 C ANISOU 1307 CB LEU A 306 1237 985 1176 -112 69 -47 C ATOM 1308 CG LEU A 306 62.241 32.210 -7.607 1.00 13.08 C ANISOU 1308 CG LEU A 306 1747 1554 1670 -129 94 -51 C ATOM 1309 CD1 LEU A 306 63.297 31.108 -7.580 1.00 12.79 C ANISOU 1309 CD1 LEU A 306 1733 1506 1621 -159 98 -26 C ATOM 1310 CD2 LEU A 306 62.050 32.813 -6.221 1.00 10.48 C ANISOU 1310 CD2 LEU A 306 1409 1248 1325 -109 102 -86 C ATOM 1311 N ARG A 307 61.763 35.367 -11.126 1.00 13.49 N ANISOU 1311 N ARG A 307 1816 1500 1809 -71 10 -21 N ATOM 1312 CA ARG A 307 62.361 36.127 -12.225 1.00 13.49 C ANISOU 1312 CA ARG A 307 1842 1459 1825 -77 -16 13 C ATOM 1313 C ARG A 307 63.860 35.868 -12.281 1.00 11.39 C ANISOU 1313 C ARG A 307 1598 1179 1550 -112 -4 32 C ATOM 1314 O ARG A 307 64.668 36.791 -12.382 1.00 12.11 O ANISOU 1314 O ARG A 307 1709 1231 1663 -119 -21 45 O ATOM 1315 CB ARG A 307 62.065 37.622 -12.081 1.00 13.14 C ANISOU 1315 CB ARG A 307 1805 1367 1819 -42 -49 2 C ATOM 1316 CG ARG A 307 60.585 37.931 -12.220 1.00 18.18 C ANISOU 1316 CG ARG A 307 2416 2022 2470 0 -65 -16 C ATOM 1317 CD ARG A 307 60.302 39.411 -12.376 1.00 23.26 C ANISOU 1317 CD ARG A 307 3073 2606 3159 41 -109 -19 C ATOM 1318 NE ARG A 307 58.907 39.634 -12.745 1.00 25.00 N ANISOU 1318 NE ARG A 307 3261 2845 3392 85 -130 -30 N ATOM 1319 CZ ARG A 307 58.420 40.794 -13.171 1.00 27.81 C ANISOU 1319 CZ ARG A 307 3625 3152 3789 128 -177 -24 C ATOM 1320 NH1 ARG A 307 59.215 41.848 -13.285 1.00 28.82 N ANISOU 1320 NH1 ARG A 307 3797 3202 3950 126 -209 -6 N ATOM 1321 NH2 ARG A 307 57.136 40.897 -13.487 1.00 29.50 N ANISOU 1321 NH2 ARG A 307 3801 3392 4014 171 -197 -36 N ATOM 1322 N ARG A 308 64.213 34.589 -12.211 1.00 9.64 N ANISOU 1322 N ARG A 308 1371 989 1303 -133 21 32 N ATOM 1323 CA ARG A 308 65.601 34.166 -12.128 1.00 10.29 C ANISOU 1323 CA ARG A 308 1465 1068 1378 -158 34 42 C ATOM 1324 C ARG A 308 65.756 32.798 -12.774 1.00 9.71 C ANISOU 1324 C ARG A 308 1388 1022 1279 -174 51 51 C ATOM 1325 O ARG A 308 64.885 31.944 -12.630 1.00 11.15 O ANISOU 1325 O ARG A 308 1561 1225 1451 -172 58 40 O ATOM 1326 CB ARG A 308 66.059 34.125 -10.667 1.00 14.12 C ANISOU 1326 CB ARG A 308 1948 1551 1864 -154 40 16 C ATOM 1327 CG ARG A 308 67.492 33.674 -10.464 1.00 14.99 C ANISOU 1327 CG ARG A 308 2063 1662 1970 -175 47 24 C ATOM 1328 CD ARG A 308 67.819 33.528 -8.982 1.00 18.15 C ANISOU 1328 CD ARG A 308 2464 2069 2365 -170 48 0 C ATOM 1329 NE ARG A 308 67.567 34.756 -8.232 1.00 19.59 N ANISOU 1329 NE ARG A 308 2651 2231 2563 -155 31 -26 N ATOM 1330 CZ ARG A 308 68.462 35.725 -8.059 1.00 18.00 C ANISOU 1330 CZ ARG A 308 2458 1998 2384 -163 11 -30 C ATOM 1331 NH1 ARG A 308 69.673 35.615 -8.588 1.00 14.21 N ANISOU 1331 NH1 ARG A 308 1976 1512 1912 -190 10 -5 N ATOM 1332 NH2 ARG A 308 68.144 36.806 -7.359 1.00 18.10 N ANISOU 1332 NH2 ARG A 308 2478 1985 2413 -145 -9 -62 N ATOM 1333 N PRO A 309 66.860 32.588 -13.499 1.00 9.58 N ANISOU 1333 N PRO A 309 1378 1008 1254 -191 58 67 N ATOM 1334 CA PRO A 309 67.127 31.273 -14.085 1.00 8.93 C ANISOU 1334 CA PRO A 309 1295 949 1151 -199 73 64 C ATOM 1335 C PRO A 309 67.313 30.213 -13.008 1.00 9.46 C ANISOU 1335 C PRO A 309 1360 1016 1219 -197 82 46 C ATOM 1336 O PRO A 309 67.886 30.503 -11.958 1.00 9.69 O ANISOU 1336 O PRO A 309 1388 1036 1258 -194 81 41 O ATOM 1337 CB PRO A 309 68.428 31.488 -14.865 1.00 12.50 C ANISOU 1337 CB PRO A 309 1746 1408 1596 -212 82 80 C ATOM 1338 CG PRO A 309 68.517 32.964 -15.073 1.00 12.45 C ANISOU 1338 CG PRO A 309 1744 1382 1603 -220 67 105 C ATOM 1339 CD PRO A 309 67.894 33.571 -13.858 1.00 9.94 C ANISOU 1339 CD PRO A 309 1429 1037 1311 -205 52 89 C ATOM 1340 N ILE A 310 66.821 29.007 -13.264 1.00 9.67 N ANISOU 1340 N ILE A 310 1388 1050 1235 -200 86 37 N ATOM 1341 CA ILE A 310 67.056 27.884 -12.370 1.00 9.42 C ANISOU 1341 CA ILE A 310 1362 1012 1206 -202 89 29 C ATOM 1342 C ILE A 310 67.838 26.796 -13.098 1.00 12.58 C ANISOU 1342 C ILE A 310 1769 1409 1603 -199 92 20 C ATOM 1343 O ILE A 310 67.516 26.436 -14.231 1.00 15.42 O ANISOU 1343 O ILE A 310 2131 1776 1951 -201 91 12 O ATOM 1344 CB ILE A 310 65.743 27.289 -11.823 1.00 10.72 C ANISOU 1344 CB ILE A 310 1523 1181 1367 -212 87 28 C ATOM 1345 CG1 ILE A 310 64.933 28.355 -11.079 1.00 10.64 C ANISOU 1345 CG1 ILE A 310 1499 1184 1358 -206 88 27 C ATOM 1346 CG2 ILE A 310 66.038 26.109 -10.907 1.00 8.98 C ANISOU 1346 CG2 ILE A 310 1315 949 1149 -220 86 32 C ATOM 1347 CD1 ILE A 310 63.623 27.836 -10.506 1.00 7.20 C ANISOU 1347 CD1 ILE A 310 1050 769 917 -219 92 26 C ATOM 1348 N VAL A 311 68.879 26.292 -12.446 1.00 10.22 N ANISOU 1348 N VAL A 311 1471 1099 1312 -190 91 18 N ATOM 1349 CA VAL A 311 69.676 25.205 -12.994 1.00 10.07 C ANISOU 1349 CA VAL A 311 1456 1073 1297 -177 91 2 C ATOM 1350 C VAL A 311 69.582 23.993 -12.079 1.00 10.16 C ANISOU 1350 C VAL A 311 1484 1054 1321 -175 77 3 C ATOM 1351 O VAL A 311 69.942 24.060 -10.904 1.00 12.83 O ANISOU 1351 O VAL A 311 1824 1387 1665 -174 70 17 O ATOM 1352 CB VAL A 311 71.153 25.609 -13.173 1.00 11.55 C ANISOU 1352 CB VAL A 311 1625 1276 1488 -162 100 -2 C ATOM 1353 CG1 VAL A 311 71.977 24.419 -13.647 1.00 12.45 C ANISOU 1353 CG1 VAL A 311 1737 1386 1608 -138 100 -27 C ATOM 1354 CG2 VAL A 311 71.270 26.773 -14.157 1.00 10.94 C ANISOU 1354 CG2 VAL A 311 1534 1226 1395 -174 114 7 C ATOM 1355 N VAL A 312 69.081 22.891 -12.623 1.00 9.40 N ANISOU 1355 N VAL A 312 1404 938 1229 -178 68 -11 N ATOM 1356 CA VAL A 312 68.909 21.672 -11.852 1.00 11.56 C ANISOU 1356 CA VAL A 312 1699 1172 1520 -183 48 -2 C ATOM 1357 C VAL A 312 69.899 20.603 -12.289 1.00 10.49 C ANISOU 1357 C VAL A 312 1575 1007 1404 -152 35 -28 C ATOM 1358 O VAL A 312 69.959 20.250 -13.466 1.00 13.31 O ANISOU 1358 O VAL A 312 1933 1365 1758 -140 38 -62 O ATOM 1359 CB VAL A 312 67.476 21.121 -11.991 1.00 12.52 C ANISOU 1359 CB VAL A 312 1834 1283 1641 -216 41 3 C ATOM 1360 CG1 VAL A 312 67.332 19.814 -11.235 1.00 7.98 C ANISOU 1360 CG1 VAL A 312 1285 660 1086 -231 17 20 C ATOM 1361 CG2 VAL A 312 66.465 22.147 -11.502 1.00 12.84 C ANISOU 1361 CG2 VAL A 312 1855 1358 1664 -239 54 23 C ATOM 1362 N VAL A 313 70.684 20.105 -11.339 1.00 11.61 N ANISOU 1362 N VAL A 313 1724 1125 1564 -135 18 -14 N ATOM 1363 CA VAL A 313 71.558 18.960 -11.577 1.00 10.45 C ANISOU 1363 CA VAL A 313 1588 939 1444 -98 -3 -38 C ATOM 1364 C VAL A 313 70.802 17.674 -11.261 1.00 13.80 C ANISOU 1364 C VAL A 313 2052 1300 1890 -116 -34 -26 C ATOM 1365 O VAL A 313 70.217 17.542 -10.183 1.00 13.42 O ANISOU 1365 O VAL A 313 2020 1239 1840 -148 -45 19 O ATOM 1366 CB VAL A 313 72.839 19.024 -10.718 1.00 10.05 C ANISOU 1366 CB VAL A 313 1523 890 1406 -66 -15 -27 C ATOM 1367 CG1 VAL A 313 73.715 17.804 -10.972 1.00 12.77 C ANISOU 1367 CG1 VAL A 313 1876 1191 1784 -18 -41 -55 C ATOM 1368 CG2 VAL A 313 73.604 20.310 -10.992 1.00 9.44 C ANISOU 1368 CG2 VAL A 313 1404 872 1311 -59 13 -35 C ATOM 1369 N ALA A 314 70.814 16.726 -12.193 1.00 12.66 N ANISOU 1369 N ALA A 314 1926 1120 1766 -98 -49 -67 N ATOM 1370 CA ALA A 314 70.070 15.485 -12.012 1.00 13.18 C ANISOU 1370 CA ALA A 314 2034 1116 1860 -122 -84 -58 C ATOM 1371 C ALA A 314 70.553 14.386 -12.950 1.00 16.80 C ANISOU 1371 C ALA A 314 2512 1523 2349 -81 -108 -117 C ATOM 1372 O ALA A 314 71.203 14.656 -13.958 1.00 17.87 O ANISOU 1372 O ALA A 314 2625 1694 2472 -41 -89 -170 O ATOM 1373 CB ALA A 314 68.583 15.729 -12.226 1.00 9.49 C ANISOU 1373 CB ALA A 314 1568 664 1374 -181 -74 -43 C ATOM 1374 N ASP A 315 70.228 13.145 -12.610 1.00 16.85 N ANISOU 1374 N ASP A 315 2561 1445 2395 -92 -152 -107 N ATOM 1375 CA ASP A 315 70.468 12.032 -13.516 1.00 17.41 C ANISOU 1375 CA ASP A 315 2660 1455 2501 -58 -182 -170 C ATOM 1376 C ASP A 315 69.405 12.063 -14.611 1.00 19.04 C ANISOU 1376 C ASP A 315 2870 1677 2687 -94 -174 -207 C ATOM 1377 O ASP A 315 68.401 12.768 -14.491 1.00 15.83 O ANISOU 1377 O ASP A 315 2449 1315 2252 -150 -153 -172 O ATOM 1378 CB ASP A 315 70.446 10.698 -12.768 1.00 19.68 C ANISOU 1378 CB ASP A 315 2999 1633 2845 -61 -241 -143 C ATOM 1379 CG ASP A 315 71.309 9.641 -13.437 1.00 22.74 C ANISOU 1379 CG ASP A 315 3409 1954 3279 10 -277 -214 C ATOM 1380 OD1 ASP A 315 71.730 9.857 -14.593 1.00 23.85 O ANISOU 1380 OD1 ASP A 315 3525 2137 3401 54 -253 -292 O ATOM 1381 OD2 ASP A 315 71.563 8.593 -12.808 1.00 24.65 O ANISOU 1381 OD2 ASP A 315 3692 2099 3573 24 -330 -193 O ATOM 1382 N THR A 316 69.625 11.301 -15.678 1.00 19.04 N ANISOU 1382 N THR A 316 2887 1645 2703 -60 -192 -282 N ATOM 1383 CA THR A 316 68.740 11.345 -16.836 1.00 20.33 C ANISOU 1383 CA THR A 316 3052 1833 2840 -88 -187 -328 C ATOM 1384 C THR A 316 67.743 10.188 -16.862 1.00 22.96 C ANISOU 1384 C THR A 316 3433 2078 3215 -135 -239 -333 C ATOM 1385 O THR A 316 66.725 10.254 -17.551 1.00 23.76 O ANISOU 1385 O THR A 316 3533 2198 3296 -180 -241 -350 O ATOM 1386 CB THR A 316 69.545 11.323 -18.149 1.00 22.21 C ANISOU 1386 CB THR A 316 3276 2109 3053 -24 -171 -418 C ATOM 1387 OG1 THR A 316 70.352 10.141 -18.191 1.00 24.74 O ANISOU 1387 OG1 THR A 316 3625 2351 3424 35 -209 -470 O ATOM 1388 CG2 THR A 316 70.446 12.545 -18.249 1.00 21.62 C ANISOU 1388 CG2 THR A 316 3148 2132 2933 9 -118 -408 C ATOM 1389 N MET A 317 68.034 9.131 -16.114 1.00 24.01 N ANISOU 1389 N MET A 317 3606 2110 3406 -128 -284 -314 N ATOM 1390 CA MET A 317 67.206 7.934 -16.164 1.00 28.68 C ANISOU 1390 CA MET A 317 4242 2613 4044 -174 -334 -317 C ATOM 1391 C MET A 317 66.981 7.316 -14.788 1.00 30.13 C ANISOU 1391 C MET A 317 4438 2749 4260 -212 -352 -224 C ATOM 1392 O MET A 317 67.914 7.166 -13.999 1.00 28.74 O ANISOU 1392 O MET A 317 4270 2549 4103 -170 -361 -194 O ATOM 1393 CB MET A 317 67.838 6.894 -17.094 1.00 30.06 C ANISOU 1393 CB MET A 317 4436 2741 4245 -110 -359 -406 C ATOM 1394 CG MET A 317 66.838 5.965 -17.766 1.00 34.07 C ANISOU 1394 CG MET A 317 4964 3213 4769 -155 -387 -436 C ATOM 1395 SD MET A 317 65.895 6.789 -19.065 1.00 40.87 S ANISOU 1395 SD MET A 317 5805 4154 5570 -192 -368 -493 S ATOM 1396 CE MET A 317 67.157 7.018 -20.316 1.00 50.33 C ANISOU 1396 CE MET A 317 6996 5396 6732 -88 -349 -609 C ATOM 1397 N LEU A 318 65.729 6.971 -14.511 1.00 28.84 N ANISOU 1397 N LEU A 318 4276 2581 4102 -293 -359 -178 N ATOM 1398 CA LEU A 318 65.392 6.129 -13.374 1.00 29.46 C ANISOU 1398 CA LEU A 318 4371 2612 4210 -335 -381 -100 C ATOM 1399 C LEU A 318 65.773 4.696 -13.731 1.00 29.31 C ANISOU 1399 C LEU A 318 4392 2501 4244 -302 -427 -139 C ATOM 1400 O LEU A 318 65.570 4.266 -14.865 1.00 29.37 O ANISOU 1400 O LEU A 318 4408 2489 4262 -291 -441 -215 O ATOM 1401 CB LEU A 318 63.900 6.235 -13.047 1.00 31.26 C ANISOU 1401 CB LEU A 318 4580 2875 4424 -430 -369 -46 C ATOM 1402 CG LEU A 318 63.450 6.228 -11.587 1.00 34.43 C ANISOU 1402 CG LEU A 318 4973 3293 4816 -484 -359 57 C ATOM 1403 CD1 LEU A 318 64.053 7.406 -10.836 1.00 32.48 C ANISOU 1403 CD1 LEU A 318 4705 3108 4527 -460 -324 93 C ATOM 1404 CD2 LEU A 318 61.929 6.254 -11.501 1.00 34.19 C ANISOU 1404 CD2 LEU A 318 4914 3302 4773 -573 -347 90 C ATOM 1405 N ARG A 319 66.339 3.959 -12.784 1.00 33.99 N ANISOU 1405 N ARG A 319 5009 3036 4868 -285 -455 -88 N ATOM 1406 CA ARG A 319 66.716 2.575 -13.057 1.00 39.68 C ANISOU 1406 CA ARG A 319 5770 3662 5643 -252 -504 -121 C ATOM 1407 C ARG A 319 66.198 1.618 -11.986 1.00 42.23 C ANISOU 1407 C ARG A 319 6123 3926 5997 -310 -537 -34 C ATOM 1408 O ARG A 319 66.019 1.993 -10.831 1.00 40.88 O ANISOU 1408 O ARG A 319 5942 3787 5803 -348 -524 54 O ATOM 1409 CB ARG A 319 68.235 2.451 -13.202 1.00 44.13 C ANISOU 1409 CB ARG A 319 6340 4201 6226 -146 -517 -170 C ATOM 1410 CG ARG A 319 69.035 3.138 -12.113 1.00 46.65 C ANISOU 1410 CG ARG A 319 6645 4554 6528 -119 -504 -108 C ATOM 1411 CD ARG A 319 70.510 3.196 -12.481 1.00 49.45 C ANISOU 1411 CD ARG A 319 6989 4904 6897 -10 -510 -172 C ATOM 1412 NE ARG A 319 70.763 4.097 -13.603 1.00 51.21 N ANISOU 1412 NE ARG A 319 7179 5193 7087 27 -470 -256 N ATOM 1413 CZ ARG A 319 70.878 3.707 -14.868 1.00 53.11 C ANISOU 1413 CZ ARG A 319 7421 5427 7332 66 -471 -354 C ATOM 1414 NH1 ARG A 319 70.764 2.424 -15.182 1.00 55.49 N ANISOU 1414 NH1 ARG A 319 7757 5651 7677 74 -513 -384 N ATOM 1415 NH2 ARG A 319 71.109 4.601 -15.821 1.00 52.09 N ANISOU 1415 NH2 ARG A 319 7260 5371 7161 95 -432 -423 N ATOM 1416 N ASP A 320 65.962 0.375 -12.391 1.00 47.86 N ANISOU 1416 N ASP A 320 6872 4554 6758 -317 -582 -61 N ATOM 1417 CA ASP A 320 65.282 -0.613 -11.556 1.00 53.25 C ANISOU 1417 CA ASP A 320 7585 5176 7472 -385 -616 17 C ATOM 1418 C ASP A 320 66.195 -1.295 -10.538 1.00 56.19 C ANISOU 1418 C ASP A 320 7990 5484 7873 -347 -655 73 C ATOM 1419 O ASP A 320 67.350 -0.909 -10.356 1.00 56.50 O ANISOU 1419 O ASP A 320 8024 5537 7908 -268 -652 58 O ATOM 1420 CB ASP A 320 64.626 -1.678 -12.444 1.00 55.62 C ANISOU 1420 CB ASP A 320 7914 5404 7816 -414 -653 -36 C ATOM 1421 CG ASP A 320 65.610 -2.335 -13.400 1.00 57.30 C ANISOU 1421 CG ASP A 320 8154 5552 8067 -320 -686 -137 C ATOM 1422 OD1 ASP A 320 66.830 -2.270 -13.147 1.00 56.55 O ANISOU 1422 OD1 ASP A 320 8062 5446 7978 -237 -692 -148 O ATOM 1423 OD2 ASP A 320 65.160 -2.922 -14.408 1.00 58.76 O ANISOU 1423 OD2 ASP A 320 8354 5700 8273 -330 -707 -208 O ATOM 1424 N SER A 321 65.655 -2.315 -9.877 1.00 58.70 N ANISOU 1424 N SER A 321 8344 5736 8224 -404 -694 138 N ATOM 1425 CA SER A 321 66.411 -3.100 -8.908 1.00 61.20 C ANISOU 1425 CA SER A 321 8699 5982 8572 -376 -741 198 C ATOM 1426 C SER A 321 67.543 -3.843 -9.608 1.00 62.61 C ANISOU 1426 C SER A 321 8906 6079 8805 -274 -786 115 C ATOM 1427 O SER A 321 68.612 -4.050 -9.039 1.00 63.34 O ANISOU 1427 O SER A 321 9011 6142 8913 -208 -813 133 O ATOM 1428 CB SER A 321 65.495 -4.085 -8.176 1.00 62.99 C ANISOU 1428 CB SER A 321 8960 6152 8823 -467 -775 282 C ATOM 1429 N GLY A 322 67.299 -4.236 -10.853 1.00 63.21 N ANISOU 1429 N GLY A 322 8988 6122 8906 -260 -794 21 N ATOM 1430 CA GLY A 322 68.308 -4.899 -11.658 1.00 62.75 C ANISOU 1430 CA GLY A 322 8951 5998 8893 -160 -830 -74 C ATOM 1431 C GLY A 322 69.410 -3.944 -12.075 1.00 60.23 C ANISOU 1431 C GLY A 322 8591 5752 8543 -66 -793 -137 C ATOM 1432 O GLY A 322 70.514 -4.365 -12.415 1.00 60.26 O ANISOU 1432 O GLY A 322 8600 5717 8577 31 -819 -199 O ATOM 1433 N GLY A 323 69.106 -2.650 -12.045 1.00 57.34 N ANISOU 1433 N GLY A 323 8179 5491 8115 -94 -733 -122 N ATOM 1434 CA GLY A 323 70.057 -1.626 -12.437 1.00 54.59 C ANISOU 1434 CA GLY A 323 7790 5218 7733 -17 -694 -176 C ATOM 1435 C GLY A 323 69.845 -1.162 -13.864 1.00 53.85 C ANISOU 1435 C GLY A 323 7673 5173 7614 0 -660 -281 C ATOM 1436 O GLY A 323 70.532 -0.260 -14.344 1.00 55.99 O ANISOU 1436 O GLY A 323 7907 5515 7851 57 -622 -332 O ATOM 1437 N GLU A 324 68.888 -1.785 -14.544 1.00 51.27 N ANISOU 1437 N GLU A 324 7369 4810 7302 -51 -676 -312 N ATOM 1438 CA GLU A 324 68.553 -1.418 -15.915 1.00 48.47 C ANISOU 1438 CA GLU A 324 6997 4503 6918 -45 -649 -410 C ATOM 1439 C GLU A 324 67.732 -0.130 -15.955 1.00 43.11 C ANISOU 1439 C GLU A 324 6279 3923 6178 -109 -596 -380 C ATOM 1440 O GLU A 324 67.020 0.191 -15.003 1.00 39.75 O ANISOU 1440 O GLU A 324 5846 3514 5742 -183 -587 -286 O ATOM 1441 CB GLU A 324 67.788 -2.555 -16.598 1.00 48.51 C ANISOU 1441 CB GLU A 324 7039 4432 6959 -80 -690 -453 C ATOM 1442 N ALA A 325 67.837 0.607 -17.057 1.00 41.06 N ANISOU 1442 N ALA A 325 5993 3733 5876 -79 -562 -462 N ATOM 1443 CA ALA A 325 67.087 1.847 -17.214 1.00 40.40 C ANISOU 1443 CA ALA A 325 5873 3741 5735 -134 -518 -442 C ATOM 1444 C ALA A 325 65.591 1.560 -17.198 1.00 39.29 C ANISOU 1444 C ALA A 325 5738 3590 5599 -237 -530 -406 C ATOM 1445 O ALA A 325 65.119 0.644 -17.869 1.00 38.81 O ANISOU 1445 O ALA A 325 5703 3479 5565 -253 -562 -453 O ATOM 1446 CB ALA A 325 67.480 2.553 -18.497 1.00 39.60 C ANISOU 1446 CB ALA A 325 5748 3711 5586 -82 -487 -541 C ATOM 1447 N PHE A 326 64.849 2.347 -16.429 1.00 35.50 N ANISOU 1447 N PHE A 326 5232 3162 5094 -304 -503 -324 N ATOM 1448 CA PHE A 326 63.419 2.118 -16.262 1.00 33.22 C ANISOU 1448 CA PHE A 326 4937 2876 4810 -403 -511 -279 C ATOM 1449 C PHE A 326 62.589 3.204 -16.938 1.00 29.04 C ANISOU 1449 C PHE A 326 4366 2439 4231 -441 -479 -301 C ATOM 1450 O PHE A 326 61.678 2.910 -17.712 1.00 30.32 O ANISOU 1450 O PHE A 326 4524 2602 4393 -486 -494 -339 O ATOM 1451 CB PHE A 326 63.071 2.035 -14.775 1.00 33.59 C ANISOU 1451 CB PHE A 326 4982 2915 4867 -457 -508 -164 C ATOM 1452 CG PHE A 326 61.613 1.808 -14.505 1.00 34.70 C ANISOU 1452 CG PHE A 326 5107 3067 5010 -559 -510 -113 C ATOM 1453 CD1 PHE A 326 61.058 0.549 -14.651 1.00 35.99 C ANISOU 1453 CD1 PHE A 326 5301 3152 5221 -601 -554 -116 C ATOM 1454 CD2 PHE A 326 60.800 2.852 -14.098 1.00 34.45 C ANISOU 1454 CD2 PHE A 326 5027 3127 4936 -613 -470 -64 C ATOM 1455 CE1 PHE A 326 59.715 0.336 -14.401 1.00 36.52 C ANISOU 1455 CE1 PHE A 326 5349 3234 5292 -697 -555 -70 C ATOM 1456 CE2 PHE A 326 59.458 2.645 -13.846 1.00 36.35 C ANISOU 1456 CE2 PHE A 326 5244 3387 5179 -703 -469 -20 C ATOM 1457 CZ PHE A 326 58.915 1.385 -13.998 1.00 35.82 C ANISOU 1457 CZ PHE A 326 5206 3244 5159 -747 -512 -22 C ATOM 1458 N ALA A 327 62.911 4.458 -16.640 1.00 21.92 N ANISOU 1458 N ALA A 327 3434 1610 3285 -424 -438 -278 N ATOM 1459 CA ALA A 327 62.205 5.595 -17.214 1.00 20.16 C ANISOU 1459 CA ALA A 327 3172 1475 3013 -455 -410 -292 C ATOM 1460 C ALA A 327 63.021 6.874 -17.041 1.00 19.29 C ANISOU 1460 C ALA A 327 3044 1426 2861 -408 -372 -287 C ATOM 1461 O ALA A 327 63.858 6.963 -16.143 1.00 22.58 O ANISOU 1461 O ALA A 327 3466 1826 3286 -375 -363 -245 O ATOM 1462 CB ALA A 327 60.834 5.747 -16.578 1.00 21.46 C ANISOU 1462 CB ALA A 327 3306 1672 3175 -548 -404 -219 C ATOM 1463 N PRO A 328 62.782 7.866 -17.908 1.00 18.88 N ANISOU 1463 N PRO A 328 2970 1444 2760 -406 -354 -328 N ATOM 1464 CA PRO A 328 63.533 9.128 -17.902 1.00 19.75 C ANISOU 1464 CA PRO A 328 3060 1621 2824 -361 -314 -328 C ATOM 1465 C PRO A 328 63.244 10.014 -16.689 1.00 19.92 C ANISOU 1465 C PRO A 328 3046 1694 2827 -394 -277 -234 C ATOM 1466 O PRO A 328 62.117 10.040 -16.195 1.00 19.69 O ANISOU 1466 O PRO A 328 3004 1675 2803 -468 -280 -183 O ATOM 1467 CB PRO A 328 63.063 9.826 -19.188 1.00 18.78 C ANISOU 1467 CB PRO A 328 2908 1584 2645 -358 -296 -382 C ATOM 1468 CG PRO A 328 62.439 8.751 -20.018 1.00 20.69 C ANISOU 1468 CG PRO A 328 3184 1763 2913 -387 -350 -445 C ATOM 1469 CD PRO A 328 61.849 7.789 -19.043 1.00 19.78 C ANISOU 1469 CD PRO A 328 3076 1584 2857 -440 -371 -383 C ATOM 1470 N ILE A 329 64.265 10.729 -16.224 1.00 18.50 N ANISOU 1470 N ILE A 329 2849 1552 2628 -340 -241 -216 N ATOM 1471 CA ILE A 329 64.093 11.781 -15.226 1.00 14.59 C ANISOU 1471 CA ILE A 329 2318 1122 2105 -359 -202 -146 C ATOM 1472 C ILE A 329 64.031 13.127 -15.936 1.00 17.46 C ANISOU 1472 C ILE A 329 2636 1585 2413 -338 -159 -165 C ATOM 1473 O ILE A 329 64.945 13.483 -16.677 1.00 19.50 O ANISOU 1473 O ILE A 329 2888 1870 2651 -281 -143 -210 O ATOM 1474 CB ILE A 329 65.233 11.782 -14.192 1.00 15.76 C ANISOU 1474 CB ILE A 329 2476 1248 2265 -318 -196 -111 C ATOM 1475 CG1 ILE A 329 65.197 10.493 -13.367 1.00 15.28 C ANISOU 1475 CG1 ILE A 329 2462 1085 2257 -345 -244 -73 C ATOM 1476 CG2 ILE A 329 65.143 13.013 -13.291 1.00 14.67 C ANISOU 1476 CG2 ILE A 329 2299 1187 2089 -329 -154 -54 C ATOM 1477 CD1 ILE A 329 66.399 10.305 -12.466 1.00 15.21 C ANISOU 1477 CD1 ILE A 329 2468 1045 2265 -295 -253 -45 C ATOM 1478 N PRO A 330 62.941 13.876 -15.722 1.00 17.81 N ANISOU 1478 N PRO A 330 2647 1684 2434 -385 -141 -129 N ATOM 1479 CA PRO A 330 62.678 15.098 -16.486 1.00 19.28 C ANISOU 1479 CA PRO A 330 2796 1955 2575 -371 -112 -144 C ATOM 1480 C PRO A 330 63.257 16.389 -15.899 1.00 17.48 C ANISOU 1480 C PRO A 330 2539 1781 2320 -341 -72 -112 C ATOM 1481 O PRO A 330 63.191 17.415 -16.569 1.00 20.80 O ANISOU 1481 O PRO A 330 2935 2261 2708 -325 -52 -122 O ATOM 1482 CB PRO A 330 61.151 15.166 -16.483 1.00 20.78 C ANISOU 1482 CB PRO A 330 2962 2169 2764 -434 -122 -124 C ATOM 1483 CG PRO A 330 60.781 14.591 -15.155 1.00 18.16 C ANISOU 1483 CG PRO A 330 2637 1801 2462 -479 -128 -68 C ATOM 1484 CD PRO A 330 61.791 13.495 -14.882 1.00 17.95 C ANISOU 1484 CD PRO A 330 2661 1689 2472 -457 -153 -77 C ATOM 1485 N PHE A 331 63.816 16.347 -14.694 1.00 14.62 N ANISOU 1485 N PHE A 331 2183 1399 1973 -336 -64 -73 N ATOM 1486 CA PHE A 331 64.127 17.583 -13.972 1.00 14.02 C ANISOU 1486 CA PHE A 331 2079 1374 1874 -320 -32 -41 C ATOM 1487 C PHE A 331 65.447 18.262 -14.353 1.00 12.17 C ANISOU 1487 C PHE A 331 1838 1161 1625 -266 -13 -62 C ATOM 1488 O PHE A 331 65.562 19.484 -14.263 1.00 12.88 O ANISOU 1488 O PHE A 331 1902 1298 1692 -256 11 -49 O ATOM 1489 CB PHE A 331 64.120 17.316 -12.464 1.00 11.51 C ANISOU 1489 CB PHE A 331 1769 1037 1568 -341 -32 10 C ATOM 1490 CG PHE A 331 62.771 16.950 -11.926 1.00 13.51 C ANISOU 1490 CG PHE A 331 2014 1294 1825 -403 -38 43 C ATOM 1491 CD1 PHE A 331 61.760 17.894 -11.866 1.00 14.76 C ANISOU 1491 CD1 PHE A 331 2131 1516 1960 -423 -15 52 C ATOM 1492 CD2 PHE A 331 62.511 15.665 -11.484 1.00 13.09 C ANISOU 1492 CD2 PHE A 331 1992 1181 1801 -442 -67 66 C ATOM 1493 CE1 PHE A 331 60.515 17.562 -11.378 1.00 16.52 C ANISOU 1493 CE1 PHE A 331 2336 1756 2186 -480 -16 80 C ATOM 1494 CE2 PHE A 331 61.268 15.327 -10.994 1.00 18.73 C ANISOU 1494 CE2 PHE A 331 2693 1906 2517 -508 -69 101 C ATOM 1495 CZ PHE A 331 60.268 16.277 -10.941 1.00 18.34 C ANISOU 1495 CZ PHE A 331 2594 1933 2441 -527 -40 107 C ATOM 1496 N GLY A 332 66.437 17.481 -14.770 1.00 13.11 N ANISOU 1496 N GLY A 332 1978 1245 1760 -231 -26 -95 N ATOM 1497 CA GLY A 332 67.755 18.021 -15.057 1.00 14.03 C ANISOU 1497 CA GLY A 332 2079 1386 1864 -183 -6 -114 C ATOM 1498 C GLY A 332 67.768 19.053 -16.169 1.00 12.78 C ANISOU 1498 C GLY A 332 1897 1291 1668 -175 19 -132 C ATOM 1499 O GLY A 332 67.179 18.841 -17.228 1.00 13.94 O ANISOU 1499 O GLY A 332 2050 1450 1799 -184 12 -162 O ATOM 1500 N GLY A 333 68.433 20.180 -15.930 1.00 8.21 N ANISOU 1500 N GLY A 333 1293 752 1074 -163 43 -112 N ATOM 1501 CA GLY A 333 68.598 21.177 -16.973 1.00 8.38 C ANISOU 1501 CA GLY A 333 1295 828 1060 -158 65 -119 C ATOM 1502 C GLY A 333 68.358 22.620 -16.570 1.00 10.23 C ANISOU 1502 C GLY A 333 1510 1093 1283 -174 79 -79 C ATOM 1503 O GLY A 333 68.382 22.972 -15.388 1.00 12.06 O ANISOU 1503 O GLY A 333 1738 1311 1532 -179 78 -52 O ATOM 1504 N ILE A 334 68.114 23.454 -17.577 1.00 11.17 N ANISOU 1504 N ILE A 334 1621 1252 1372 -180 88 -76 N ATOM 1505 CA ILE A 334 68.042 24.900 -17.407 1.00 10.73 C ANISOU 1505 CA ILE A 334 1550 1218 1309 -189 97 -41 C ATOM 1506 C ILE A 334 66.621 25.427 -17.565 1.00 12.74 C ANISOU 1506 C ILE A 334 1804 1478 1558 -207 83 -25 C ATOM 1507 O ILE A 334 65.963 25.170 -18.573 1.00 12.21 O ANISOU 1507 O ILE A 334 1743 1429 1469 -213 72 -38 O ATOM 1508 CB ILE A 334 68.952 25.618 -18.423 1.00 8.15 C ANISOU 1508 CB ILE A 334 1212 933 954 -184 116 -37 C ATOM 1509 CG1 ILE A 334 70.403 25.159 -18.257 1.00 12.77 C ANISOU 1509 CG1 ILE A 334 1783 1524 1546 -164 132 -55 C ATOM 1510 CG2 ILE A 334 68.836 27.128 -18.276 1.00 8.89 C ANISOU 1510 CG2 ILE A 334 1297 1035 1047 -199 117 5 C ATOM 1511 CD1 ILE A 334 71.324 25.625 -19.366 1.00 15.89 C ANISOU 1511 CD1 ILE A 334 2159 1973 1906 -163 157 -56 C ATOM 1512 N TYR A 335 66.160 26.167 -16.563 1.00 13.21 N ANISOU 1512 N TYR A 335 1857 1528 1636 -212 80 -2 N ATOM 1513 CA TYR A 335 64.832 26.768 -16.581 1.00 11.49 C ANISOU 1513 CA TYR A 335 1629 1318 1418 -220 67 9 C ATOM 1514 C TYR A 335 64.937 28.292 -16.623 1.00 13.28 C ANISOU 1514 C TYR A 335 1849 1551 1646 -212 66 34 C ATOM 1515 O TYR A 335 65.339 28.918 -15.642 1.00 10.36 O ANISOU 1515 O TYR A 335 1475 1166 1294 -206 72 42 O ATOM 1516 CB TYR A 335 64.026 26.344 -15.351 1.00 8.36 C ANISOU 1516 CB TYR A 335 1225 909 1042 -229 65 10 C ATOM 1517 CG TYR A 335 63.833 24.850 -15.178 1.00 10.54 C ANISOU 1517 CG TYR A 335 1513 1167 1325 -246 59 -5 C ATOM 1518 CD1 TYR A 335 64.875 24.034 -14.753 1.00 12.59 C ANISOU 1518 CD1 TYR A 335 1789 1400 1594 -239 63 -11 C ATOM 1519 CD2 TYR A 335 62.596 24.263 -15.407 1.00 10.28 C ANISOU 1519 CD2 TYR A 335 1472 1141 1294 -269 46 -10 C ATOM 1520 CE1 TYR A 335 64.692 22.672 -14.582 1.00 11.87 C ANISOU 1520 CE1 TYR A 335 1714 1280 1515 -254 51 -21 C ATOM 1521 CE2 TYR A 335 62.403 22.906 -15.238 1.00 9.90 C ANISOU 1521 CE2 TYR A 335 1437 1065 1258 -291 35 -20 C ATOM 1522 CZ TYR A 335 63.452 22.116 -14.825 1.00 12.65 C ANISOU 1522 CZ TYR A 335 1810 1379 1618 -283 37 -24 C ATOM 1523 OH TYR A 335 63.252 20.764 -14.657 1.00 13.34 O ANISOU 1523 OH TYR A 335 1918 1427 1724 -304 19 -31 O ATOM 1524 N LEU A 336 64.576 28.886 -17.755 1.00 12.65 N ANISOU 1524 N LEU A 336 1770 1490 1547 -212 55 47 N ATOM 1525 CA LEU A 336 64.618 30.338 -17.900 1.00 11.73 C ANISOU 1525 CA LEU A 336 1653 1368 1435 -207 46 76 C ATOM 1526 C LEU A 336 63.230 30.952 -17.760 1.00 10.55 C ANISOU 1526 C LEU A 336 1491 1216 1300 -195 22 81 C ATOM 1527 O LEU A 336 62.236 30.338 -18.144 1.00 12.43 O ANISOU 1527 O LEU A 336 1720 1474 1530 -197 10 69 O ATOM 1528 CB LEU A 336 65.222 30.721 -19.255 1.00 9.84 C ANISOU 1528 CB LEU A 336 1425 1152 1163 -216 46 99 C ATOM 1529 CG LEU A 336 66.620 30.167 -19.537 1.00 8.83 C ANISOU 1529 CG LEU A 336 1298 1040 1017 -224 73 90 C ATOM 1530 CD1 LEU A 336 67.075 30.512 -20.944 1.00 9.14 C ANISOU 1530 CD1 LEU A 336 1343 1120 1011 -236 78 112 C ATOM 1531 CD2 LEU A 336 67.614 30.682 -18.506 1.00 9.58 C ANISOU 1531 CD2 LEU A 336 1387 1112 1142 -225 86 97 C ATOM 1532 N PRO A 337 63.157 32.170 -17.201 1.00 11.97 N ANISOU 1532 N PRO A 337 1670 1372 1505 -180 12 95 N ATOM 1533 CA PRO A 337 61.896 32.917 -17.119 1.00 12.63 C ANISOU 1533 CA PRO A 337 1738 1453 1607 -157 -14 96 C ATOM 1534 C PRO A 337 61.550 33.545 -18.469 1.00 13.29 C ANISOU 1534 C PRO A 337 1831 1544 1675 -154 -44 128 C ATOM 1535 O PRO A 337 61.533 34.768 -18.608 1.00 13.17 O ANISOU 1535 O PRO A 337 1826 1500 1678 -140 -67 154 O ATOM 1536 CB PRO A 337 62.189 33.982 -16.063 1.00 14.17 C ANISOU 1536 CB PRO A 337 1935 1612 1835 -139 -16 92 C ATOM 1537 CG PRO A 337 63.660 34.215 -16.179 1.00 13.13 C ANISOU 1537 CG PRO A 337 1826 1462 1699 -160 -4 111 C ATOM 1538 CD PRO A 337 64.270 32.888 -16.553 1.00 11.49 C ANISOU 1538 CD PRO A 337 1620 1285 1463 -182 21 103 C ATOM 1539 N LEU A 338 61.269 32.693 -19.448 1.00 9.86 N ANISOU 1539 N LEU A 338 1396 1144 1205 -169 -47 126 N ATOM 1540 CA LEU A 338 61.140 33.100 -20.845 1.00 11.00 C ANISOU 1540 CA LEU A 338 1554 1308 1317 -173 -72 159 C ATOM 1541 C LEU A 338 59.972 34.041 -21.139 1.00 13.99 C ANISOU 1541 C LEU A 338 1922 1681 1713 -146 -117 179 C ATOM 1542 O LEU A 338 60.004 34.774 -22.127 1.00 14.50 O ANISOU 1542 O LEU A 338 2005 1746 1757 -146 -145 221 O ATOM 1543 CB LEU A 338 61.024 31.852 -21.725 1.00 11.40 C ANISOU 1543 CB LEU A 338 1607 1402 1324 -192 -68 138 C ATOM 1544 CG LEU A 338 62.262 30.955 -21.656 1.00 12.74 C ANISOU 1544 CG LEU A 338 1789 1577 1476 -210 -29 118 C ATOM 1545 CD1 LEU A 338 62.039 29.638 -22.384 1.00 12.61 C ANISOU 1545 CD1 LEU A 338 1774 1592 1425 -222 -29 82 C ATOM 1546 CD2 LEU A 338 63.465 31.695 -22.225 1.00 8.64 C ANISOU 1546 CD2 LEU A 338 1288 1062 934 -220 -16 153 C ATOM 1547 N GLU A 339 58.940 34.017 -20.302 1.00 12.15 N ANISOU 1547 N GLU A 339 1657 1445 1514 -123 -124 151 N ATOM 1548 CA GLU A 339 57.798 34.907 -20.496 1.00 15.43 C ANISOU 1548 CA GLU A 339 2053 1857 1953 -87 -168 162 C ATOM 1549 C GLU A 339 58.036 36.264 -19.845 1.00 16.71 C ANISOU 1549 C GLU A 339 2227 1964 2159 -56 -181 174 C ATOM 1550 O GLU A 339 57.267 37.203 -20.044 1.00 19.55 O ANISOU 1550 O GLU A 339 2578 2305 2545 -18 -223 188 O ATOM 1551 CB GLU A 339 56.516 34.273 -19.952 1.00 11.57 C ANISOU 1551 CB GLU A 339 1515 1403 1480 -75 -169 122 C ATOM 1552 CG GLU A 339 56.019 33.115 -20.796 1.00 13.92 C ANISOU 1552 CG GLU A 339 1800 1747 1741 -104 -176 113 C ATOM 1553 CD GLU A 339 55.841 33.506 -22.254 1.00 17.49 C ANISOU 1553 CD GLU A 339 2270 2216 2159 -102 -220 148 C ATOM 1554 OE1 GLU A 339 56.095 32.660 -23.140 1.00 18.34 O ANISOU 1554 OE1 GLU A 339 2394 2354 2221 -133 -219 145 O ATOM 1555 OE2 GLU A 339 55.448 34.665 -22.513 1.00 17.74 O ANISOU 1555 OE2 GLU A 339 2302 2230 2210 -67 -258 178 O ATOM 1556 N VAL A 340 59.111 36.359 -19.071 1.00 11.82 N ANISOU 1556 N VAL A 340 1626 1315 1550 -70 -149 168 N ATOM 1557 CA VAL A 340 59.495 37.612 -18.435 1.00 13.48 C ANISOU 1557 CA VAL A 340 1853 1466 1802 -48 -163 174 C ATOM 1558 C VAL A 340 60.604 38.276 -19.239 1.00 13.31 C ANISOU 1558 C VAL A 340 1873 1413 1769 -77 -174 229 C ATOM 1559 O VAL A 340 61.588 37.625 -19.583 1.00 15.17 O ANISOU 1559 O VAL A 340 2121 1673 1970 -117 -142 240 O ATOM 1560 CB VAL A 340 59.975 37.389 -16.984 1.00 12.96 C ANISOU 1560 CB VAL A 340 1779 1390 1755 -48 -127 131 C ATOM 1561 CG1 VAL A 340 60.351 38.715 -16.330 1.00 13.19 C ANISOU 1561 CG1 VAL A 340 1827 1355 1828 -25 -148 128 C ATOM 1562 CG2 VAL A 340 58.905 36.676 -16.178 1.00 18.11 C ANISOU 1562 CG2 VAL A 340 2388 2084 2410 -28 -111 84 C ATOM 1563 N PRO A 341 60.445 39.571 -19.554 1.00 17.64 N ANISOU 1563 N PRO A 341 2444 1910 2350 -58 -219 265 N ATOM 1564 CA PRO A 341 61.505 40.289 -20.269 1.00 18.93 C ANISOU 1564 CA PRO A 341 2647 2041 2504 -95 -230 327 C ATOM 1565 C PRO A 341 62.829 40.173 -19.524 1.00 16.48 C ANISOU 1565 C PRO A 341 2345 1717 2200 -130 -191 314 C ATOM 1566 O PRO A 341 62.852 40.317 -18.303 1.00 16.86 O ANISOU 1566 O PRO A 341 2383 1738 2285 -110 -182 267 O ATOM 1567 CB PRO A 341 61.001 41.736 -20.290 1.00 18.97 C ANISOU 1567 CB PRO A 341 2673 1971 2562 -60 -290 354 C ATOM 1568 CG PRO A 341 59.519 41.613 -20.174 1.00 17.20 C ANISOU 1568 CG PRO A 341 2415 1767 2354 -2 -315 319 C ATOM 1569 CD PRO A 341 59.291 40.439 -19.265 1.00 18.64 C ANISOU 1569 CD PRO A 341 2556 2003 2522 0 -264 251 C ATOM 1570 N ALA A 342 63.909 39.898 -20.247 1.00 14.50 N ANISOU 1570 N ALA A 342 2107 1493 1910 -180 -167 352 N ATOM 1571 CA ALA A 342 65.201 39.680 -19.613 1.00 15.69 C ANISOU 1571 CA ALA A 342 2256 1642 2065 -213 -130 339 C ATOM 1572 C ALA A 342 65.665 40.911 -18.840 1.00 16.07 C ANISOU 1572 C ALA A 342 2322 1613 2171 -216 -155 345 C ATOM 1573 O ALA A 342 66.424 40.793 -17.880 1.00 20.56 O ANISOU 1573 O ALA A 342 2883 2172 2758 -226 -134 313 O ATOM 1574 CB ALA A 342 66.237 39.282 -20.651 1.00 14.90 C ANISOU 1574 CB ALA A 342 2158 1591 1911 -263 -101 380 C ATOM 1575 N SER A 343 65.198 42.088 -19.250 1.00 14.30 N ANISOU 1575 N SER A 343 2124 1331 1978 -205 -206 386 N ATOM 1576 CA SER A 343 65.571 43.331 -18.577 1.00 16.06 C ANISOU 1576 CA SER A 343 2371 1466 2264 -206 -240 390 C ATOM 1577 C SER A 343 65.070 43.377 -17.136 1.00 19.05 C ANISOU 1577 C SER A 343 2736 1819 2685 -156 -242 308 C ATOM 1578 O SER A 343 65.594 44.126 -16.313 1.00 20.51 O ANISOU 1578 O SER A 343 2934 1944 2913 -160 -259 288 O ATOM 1579 CB SER A 343 65.035 44.545 -19.344 1.00 18.12 C ANISOU 1579 CB SER A 343 2668 1661 2555 -197 -303 450 C ATOM 1580 OG SER A 343 63.626 44.482 -19.498 1.00 20.07 O ANISOU 1580 OG SER A 343 2904 1914 2807 -134 -331 429 O ATOM 1581 N GLN A 344 64.056 42.572 -16.837 1.00 14.58 N ANISOU 1581 N GLN A 344 2140 1300 2100 -112 -226 261 N ATOM 1582 CA GLN A 344 63.432 42.586 -15.520 1.00 16.02 C ANISOU 1582 CA GLN A 344 2303 1474 2310 -63 -223 186 C ATOM 1583 C GLN A 344 63.809 41.359 -14.694 1.00 17.72 C ANISOU 1583 C GLN A 344 2491 1751 2490 -76 -169 142 C ATOM 1584 O GLN A 344 63.201 41.089 -13.658 1.00 20.74 O ANISOU 1584 O GLN A 344 2852 2152 2877 -41 -157 84 O ATOM 1585 CB GLN A 344 61.912 42.676 -15.663 1.00 10.80 C ANISOU 1585 CB GLN A 344 1621 823 1659 -2 -247 165 C ATOM 1586 CG GLN A 344 61.442 43.908 -16.420 1.00 17.26 C ANISOU 1586 CG GLN A 344 2467 1573 2518 23 -310 208 C ATOM 1587 CD GLN A 344 59.932 44.002 -16.495 1.00 23.19 C ANISOU 1587 CD GLN A 344 3188 2339 3284 91 -337 181 C ATOM 1588 OE1 GLN A 344 59.304 43.408 -17.373 1.00 23.42 O ANISOU 1588 OE1 GLN A 344 3199 2420 3278 90 -338 207 O ATOM 1589 NE2 GLN A 344 59.339 44.746 -15.569 1.00 23.20 N ANISOU 1589 NE2 GLN A 344 3181 2298 3336 152 -360 122 N ATOM 1590 N CYS A 345 64.818 40.624 -15.149 1.00 16.27 N ANISOU 1590 N CYS A 345 2308 1603 2272 -126 -138 171 N ATOM 1591 CA CYS A 345 65.202 39.376 -14.497 1.00 16.13 C ANISOU 1591 CA CYS A 345 2267 1638 2222 -137 -93 138 C ATOM 1592 C CYS A 345 66.573 39.440 -13.831 1.00 15.73 C ANISOU 1592 C CYS A 345 2223 1576 2179 -169 -80 132 C ATOM 1593 O CYS A 345 67.453 40.186 -14.259 1.00 18.95 O ANISOU 1593 O CYS A 345 2647 1952 2603 -202 -95 168 O ATOM 1594 CB CYS A 345 65.192 38.226 -15.511 1.00 13.97 C ANISOU 1594 CB CYS A 345 1983 1423 1901 -157 -68 161 C ATOM 1595 SG CYS A 345 63.555 37.726 -16.086 1.00 17.73 S ANISOU 1595 SG CYS A 345 2441 1933 2361 -124 -78 153 S ATOM 1596 N HIS A 346 66.742 38.646 -12.780 1.00 12.71 N ANISOU 1596 N HIS A 346 1823 1222 1782 -162 -55 90 N ATOM 1597 CA HIS A 346 68.055 38.410 -12.197 1.00 13.39 C ANISOU 1597 CA HIS A 346 1908 1313 1868 -192 -42 85 C ATOM 1598 C HIS A 346 68.799 37.432 -13.095 1.00 15.33 C ANISOU 1598 C HIS A 346 2141 1602 2080 -221 -14 115 C ATOM 1599 O HIS A 346 68.198 36.501 -13.627 1.00 13.05 O ANISOU 1599 O HIS A 346 1846 1350 1764 -211 3 116 O ATOM 1600 CB HIS A 346 67.936 37.858 -10.773 1.00 15.14 C ANISOU 1600 CB HIS A 346 2118 1554 2079 -172 -30 35 C ATOM 1601 CG HIS A 346 67.061 38.682 -9.880 1.00 19.92 C ANISOU 1601 CG HIS A 346 2729 2134 2706 -135 -50 -8 C ATOM 1602 ND1 HIS A 346 67.494 39.845 -9.281 1.00 21.09 N ANISOU 1602 ND1 HIS A 346 2894 2231 2887 -133 -80 -29 N ATOM 1603 CD2 HIS A 346 65.774 38.516 -9.493 1.00 20.86 C ANISOU 1603 CD2 HIS A 346 2835 2274 2816 -97 -45 -38 C ATOM 1604 CE1 HIS A 346 66.513 40.359 -8.562 1.00 24.12 C ANISOU 1604 CE1 HIS A 346 3278 2605 3282 -89 -92 -76 C ATOM 1605 NE2 HIS A 346 65.458 39.571 -8.673 1.00 24.92 N ANISOU 1605 NE2 HIS A 346 3357 2754 3356 -66 -68 -81 N ATOM 1606 N ARG A 347 70.099 37.638 -13.272 1.00 13.97 N ANISOU 1606 N ARG A 347 1965 1430 1913 -257 -9 136 N ATOM 1607 CA ARG A 347 70.858 36.817 -14.208 1.00 14.53 C ANISOU 1607 CA ARG A 347 2020 1548 1953 -280 19 160 C ATOM 1608 C ARG A 347 71.545 35.635 -13.526 1.00 15.49 C ANISOU 1608 C ARG A 347 2121 1704 2061 -273 43 130 C ATOM 1609 O ARG A 347 71.690 34.570 -14.125 1.00 17.29 O ANISOU 1609 O ARG A 347 2337 1971 2261 -269 66 129 O ATOM 1610 CB ARG A 347 71.882 37.680 -14.948 1.00 19.78 C ANISOU 1610 CB ARG A 347 2683 2205 2626 -325 15 205 C ATOM 1611 CG ARG A 347 71.249 38.862 -15.671 1.00 24.74 C ANISOU 1611 CG ARG A 347 3339 2791 3270 -334 -15 246 C ATOM 1612 CD ARG A 347 72.251 39.623 -16.517 1.00 26.42 C ANISOU 1612 CD ARG A 347 3551 3004 3485 -390 -16 305 C ATOM 1613 NE ARG A 347 72.636 38.882 -17.714 1.00 26.93 N ANISOU 1613 NE ARG A 347 3597 3138 3495 -408 20 332 N ATOM 1614 CZ ARG A 347 71.870 38.756 -18.793 1.00 25.03 C ANISOU 1614 CZ ARG A 347 3371 2919 3218 -400 20 358 C ATOM 1615 NH1 ARG A 347 70.667 39.313 -18.825 1.00 22.51 N ANISOU 1615 NH1 ARG A 347 3081 2555 2916 -373 -16 365 N ATOM 1616 NH2 ARG A 347 72.306 38.066 -19.839 1.00 25.49 N ANISOU 1616 NH2 ARG A 347 3413 3049 3222 -416 54 374 N ATOM 1617 N SER A 348 71.955 35.819 -12.275 1.00 13.07 N ANISOU 1617 N SER A 348 1812 1381 1774 -270 31 104 N ATOM 1618 CA SER A 348 72.590 34.744 -11.515 1.00 11.71 C ANISOU 1618 CA SER A 348 1623 1237 1591 -261 44 81 C ATOM 1619 C SER A 348 71.568 33.671 -11.138 1.00 10.33 C ANISOU 1619 C SER A 348 1456 1075 1396 -231 54 61 C ATOM 1620 O SER A 348 70.521 33.976 -10.571 1.00 12.13 O ANISOU 1620 O SER A 348 1696 1288 1625 -215 44 46 O ATOM 1621 CB SER A 348 73.268 35.304 -10.263 1.00 16.95 C ANISOU 1621 CB SER A 348 2283 1882 2275 -267 23 61 C ATOM 1622 OG SER A 348 74.065 34.319 -9.633 1.00 21.55 O ANISOU 1622 OG SER A 348 2847 2493 2847 -260 29 48 O ATOM 1623 N PRO A 349 71.868 32.403 -11.458 1.00 10.44 N ANISOU 1623 N PRO A 349 1460 1116 1392 -225 71 59 N ATOM 1624 CA PRO A 349 70.881 31.330 -11.297 1.00 8.91 C ANISOU 1624 CA PRO A 349 1276 929 1182 -208 78 47 C ATOM 1625 C PRO A 349 70.725 30.806 -9.870 1.00 11.11 C ANISOU 1625 C PRO A 349 1558 1205 1457 -197 71 32 C ATOM 1626 O PRO A 349 71.647 30.878 -9.058 1.00 9.50 O ANISOU 1626 O PRO A 349 1349 1001 1259 -198 62 27 O ATOM 1627 CB PRO A 349 71.428 30.223 -12.200 1.00 10.34 C ANISOU 1627 CB PRO A 349 1448 1129 1350 -205 93 48 C ATOM 1628 CG PRO A 349 72.906 30.424 -12.162 1.00 12.73 C ANISOU 1628 CG PRO A 349 1729 1443 1663 -211 96 50 C ATOM 1629 CD PRO A 349 73.113 31.920 -12.085 1.00 9.29 C ANISOU 1629 CD PRO A 349 1293 995 1243 -233 85 66 C ATOM 1630 N LEU A 350 69.537 30.291 -9.579 1.00 11.20 N ANISOU 1630 N LEU A 350 1578 1220 1457 -191 75 27 N ATOM 1631 CA LEU A 350 69.337 29.434 -8.423 1.00 10.07 C ANISOU 1631 CA LEU A 350 1441 1084 1300 -189 74 23 C ATOM 1632 C LEU A 350 69.752 28.024 -8.823 1.00 11.28 C ANISOU 1632 C LEU A 350 1598 1234 1453 -188 76 31 C ATOM 1633 O LEU A 350 69.208 27.462 -9.776 1.00 10.28 O ANISOU 1633 O LEU A 350 1475 1105 1326 -191 82 32 O ATOM 1634 CB LEU A 350 67.881 29.463 -7.961 1.00 9.22 C ANISOU 1634 CB LEU A 350 1334 990 1180 -189 80 18 C ATOM 1635 CG LEU A 350 67.462 28.380 -6.962 1.00 6.88 C ANISOU 1635 CG LEU A 350 1043 707 863 -198 84 26 C ATOM 1636 CD1 LEU A 350 68.111 28.609 -5.605 1.00 8.35 C ANISOU 1636 CD1 LEU A 350 1234 904 1033 -194 75 22 C ATOM 1637 CD2 LEU A 350 65.946 28.326 -6.836 1.00 7.01 C ANISOU 1637 CD2 LEU A 350 1049 747 868 -205 96 24 C ATOM 1638 N VAL A 351 70.718 27.458 -8.109 1.00 8.61 N ANISOU 1638 N VAL A 351 1261 893 1117 -182 65 34 N ATOM 1639 CA VAL A 351 71.281 26.168 -8.497 1.00 9.72 C ANISOU 1639 CA VAL A 351 1406 1021 1266 -172 61 36 C ATOM 1640 C VAL A 351 70.820 25.066 -7.554 1.00 13.24 C ANISOU 1640 C VAL A 351 1873 1455 1704 -176 49 52 C ATOM 1641 O VAL A 351 71.008 25.150 -6.338 1.00 13.17 O ANISOU 1641 O VAL A 351 1868 1453 1682 -178 38 63 O ATOM 1642 CB VAL A 351 72.821 26.219 -8.537 1.00 10.30 C ANISOU 1642 CB VAL A 351 1460 1099 1353 -156 53 31 C ATOM 1643 CG1 VAL A 351 73.393 24.875 -8.959 1.00 7.29 C ANISOU 1643 CG1 VAL A 351 1082 704 985 -134 47 25 C ATOM 1644 CG2 VAL A 351 73.283 27.317 -9.493 1.00 7.04 C ANISOU 1644 CG2 VAL A 351 1026 703 946 -163 67 25 C ATOM 1645 N LEU A 352 70.211 24.034 -8.132 1.00 12.01 N ANISOU 1645 N LEU A 352 1731 1279 1554 -181 49 54 N ATOM 1646 CA LEU A 352 69.606 22.954 -7.366 1.00 14.29 C ANISOU 1646 CA LEU A 352 2041 1549 1838 -196 37 77 C ATOM 1647 C LEU A 352 70.069 21.583 -7.846 1.00 14.83 C ANISOU 1647 C LEU A 352 2128 1575 1931 -183 17 75 C ATOM 1648 O LEU A 352 70.626 21.445 -8.936 1.00 11.62 O ANISOU 1648 O LEU A 352 1715 1161 1541 -161 20 47 O ATOM 1649 CB LEU A 352 68.078 23.022 -7.459 1.00 13.70 C ANISOU 1649 CB LEU A 352 1967 1489 1751 -227 51 83 C ATOM 1650 CG LEU A 352 67.379 24.367 -7.260 1.00 12.50 C ANISOU 1650 CG LEU A 352 1794 1375 1581 -231 70 74 C ATOM 1651 CD1 LEU A 352 65.903 24.240 -7.607 1.00 7.24 C ANISOU 1651 CD1 LEU A 352 1119 723 910 -254 80 75 C ATOM 1652 CD2 LEU A 352 67.558 24.864 -5.832 1.00 11.51 C ANISOU 1652 CD2 LEU A 352 1667 1274 1432 -231 69 82 C ATOM 1653 N ALA A 353 69.818 20.571 -7.025 1.00 11.76 N ANISOU 1653 N ALA A 353 1766 1159 1545 -197 -3 105 N ATOM 1654 CA ALA A 353 70.049 19.188 -7.413 1.00 13.25 C ANISOU 1654 CA ALA A 353 1980 1291 1764 -187 -29 105 C ATOM 1655 C ALA A 353 68.796 18.374 -7.127 1.00 14.53 C ANISOU 1655 C ALA A 353 2166 1429 1925 -233 -37 134 C ATOM 1656 O ALA A 353 68.065 18.662 -6.178 1.00 14.06 O ANISOU 1656 O ALA A 353 2105 1399 1837 -268 -27 168 O ATOM 1657 CB ALA A 353 71.246 18.612 -6.677 1.00 10.86 C ANISOU 1657 CB ALA A 353 1688 962 1476 -155 -61 119 C ATOM 1658 N TYR A 354 68.540 17.370 -7.957 1.00 12.44 N ANISOU 1658 N TYR A 354 1922 1115 1690 -236 -53 118 N ATOM 1659 CA TYR A 354 67.394 16.494 -7.755 1.00 12.49 C ANISOU 1659 CA TYR A 354 1951 1090 1703 -288 -66 148 C ATOM 1660 C TYR A 354 67.813 15.031 -7.709 1.00 15.75 C ANISOU 1660 C TYR A 354 2407 1418 2158 -282 -112 159 C ATOM 1661 O TYR A 354 68.607 14.568 -8.536 1.00 14.30 O ANISOU 1661 O TYR A 354 2232 1196 2005 -235 -129 114 O ATOM 1662 CB TYR A 354 66.340 16.689 -8.854 1.00 14.14 C ANISOU 1662 CB TYR A 354 2145 1316 1912 -312 -50 117 C ATOM 1663 CG TYR A 354 65.266 15.620 -8.827 1.00 15.15 C ANISOU 1663 CG TYR A 354 2295 1404 2059 -368 -71 140 C ATOM 1664 CD1 TYR A 354 64.132 15.763 -8.037 1.00 17.43 C ANISOU 1664 CD1 TYR A 354 2570 1729 2326 -426 -56 184 C ATOM 1665 CD2 TYR A 354 65.399 14.454 -9.575 1.00 15.49 C ANISOU 1665 CD2 TYR A 354 2371 1373 2141 -365 -106 116 C ATOM 1666 CE1 TYR A 354 63.155 14.780 -8.001 1.00 17.53 C ANISOU 1666 CE1 TYR A 354 2597 1707 2356 -487 -75 210 C ATOM 1667 CE2 TYR A 354 64.432 13.468 -9.543 1.00 18.17 C ANISOU 1667 CE2 TYR A 354 2732 1667 2504 -423 -131 138 C ATOM 1668 CZ TYR A 354 63.313 13.635 -8.756 1.00 20.13 C ANISOU 1668 CZ TYR A 354 2963 1955 2731 -489 -115 189 C ATOM 1669 OH TYR A 354 62.350 12.651 -8.726 1.00 21.91 O ANISOU 1669 OH TYR A 354 3205 2139 2981 -557 -139 216 O ATOM 1670 N ASP A 355 67.258 14.310 -6.740 1.00 14.06 N ANISOU 1670 N ASP A 355 2220 1176 1944 -328 -132 218 N ATOM 1671 CA ASP A 355 67.492 12.880 -6.594 1.00 17.46 C ANISOU 1671 CA ASP A 355 2700 1513 2419 -332 -183 241 C ATOM 1672 C ASP A 355 66.435 12.255 -5.684 1.00 18.87 C ANISOU 1672 C ASP A 355 2902 1678 2590 -411 -193 315 C ATOM 1673 O ASP A 355 66.142 12.781 -4.611 1.00 16.81 O ANISOU 1673 O ASP A 355 2628 1477 2283 -441 -172 364 O ATOM 1674 CB ASP A 355 68.893 12.615 -6.038 1.00 19.47 C ANISOU 1674 CB ASP A 355 2970 1738 2689 -273 -213 250 C ATOM 1675 CG ASP A 355 69.165 11.140 -5.816 1.00 23.37 C ANISOU 1675 CG ASP A 355 3520 2126 3236 -270 -274 278 C ATOM 1676 OD1 ASP A 355 69.249 10.396 -6.815 1.00 22.69 O ANISOU 1676 OD1 ASP A 355 3452 1974 3197 -247 -298 228 O ATOM 1677 OD2 ASP A 355 69.305 10.726 -4.643 1.00 26.32 O ANISOU 1677 OD2 ASP A 355 3920 2480 3602 -288 -302 348 O ATOM 1678 N GLN A 356 65.863 11.141 -6.134 1.00 21.64 N ANISOU 1678 N GLN A 356 3277 1966 2981 -441 -221 314 N ATOM 1679 CA GLN A 356 64.907 10.364 -5.349 1.00 23.09 C ANISOU 1679 CA GLN A 356 3463 2153 3159 -503 -225 374 C ATOM 1680 C GLN A 356 63.774 11.210 -4.774 1.00 20.30 C ANISOU 1680 C GLN A 356 3067 1896 2750 -562 -176 406 C ATOM 1681 O GLN A 356 63.539 11.207 -3.566 1.00 18.45 O ANISOU 1681 O GLN A 356 2829 1703 2478 -592 -166 467 O ATOM 1682 CB GLN A 356 65.634 9.629 -4.222 1.00 28.71 C ANISOU 1682 CB GLN A 356 4207 2828 3873 -489 -259 432 C ATOM 1683 CG GLN A 356 66.750 8.719 -4.715 1.00 37.10 C ANISOU 1683 CG GLN A 356 5306 3795 4994 -423 -310 400 C ATOM 1684 CD GLN A 356 67.395 7.924 -3.599 1.00 44.34 C ANISOU 1684 CD GLN A 356 6257 4674 5917 -411 -351 462 C ATOM 1685 OE1 GLN A 356 66.721 7.190 -2.875 1.00 48.33 O ANISOU 1685 OE1 GLN A 356 6776 5171 6415 -465 -361 522 O ATOM 1686 NE2 GLN A 356 68.708 8.065 -3.453 1.00 44.66 N ANISOU 1686 NE2 GLN A 356 6308 4692 5970 -340 -377 450 N ATOM 1687 N ALA A 357 63.085 11.936 -5.650 1.00 17.38 N ANISOU 1687 N ALA A 357 2665 1567 2374 -575 -148 362 N ATOM 1688 CA ALA A 357 61.920 12.734 -5.272 1.00 18.78 C ANISOU 1688 CA ALA A 357 2794 1836 2507 -625 -103 380 C ATOM 1689 C ALA A 357 62.268 13.851 -4.293 1.00 18.21 C ANISOU 1689 C ALA A 357 2705 1835 2377 -614 -70 403 C ATOM 1690 O ALA A 357 61.426 14.278 -3.508 1.00 17.42 O ANISOU 1690 O ALA A 357 2572 1813 2234 -653 -35 433 O ATOM 1691 CB ALA A 357 60.834 11.841 -4.681 1.00 20.53 C ANISOU 1691 CB ALA A 357 3005 2066 2729 -690 -105 429 C ATOM 1692 N AHIS A 358 63.524 14.287 -4.295 0.53 17.58 N ANISOU 1692 N AHIS A 358 2638 1744 2298 -546 -76 375 N ATOM 1693 N BHIS A 358 63.527 14.279 -4.285 0.47 17.57 N ANISOU 1693 N BHIS A 358 2636 1742 2296 -547 -77 376 N ATOM 1694 CA AHIS A 358 63.977 15.366 -3.419 0.53 16.85 C ANISOU 1694 CA AHIS A 358 2524 1724 2155 -518 -49 380 C ATOM 1695 CA BHIS A 358 63.963 15.379 -3.429 0.47 16.60 C ANISOU 1695 CA BHIS A 358 2491 1692 2123 -518 -48 379 C ATOM 1696 C AHIS A 358 64.694 16.477 -4.201 0.53 14.29 C ANISOU 1696 C AHIS A 358 2175 1421 1834 -450 -34 313 C ATOM 1697 C BHIS A 358 64.693 16.480 -4.205 0.47 14.30 C ANISOU 1697 C BHIS A 358 2175 1422 1835 -450 -33 312 C ATOM 1698 O AHIS A 358 65.443 16.193 -5.123 0.53 12.81 O ANISOU 1698 O AHIS A 358 2002 1182 1685 -408 -55 277 O ATOM 1699 O BHIS A 358 65.445 16.193 -5.124 0.47 12.93 O ANISOU 1699 O BHIS A 358 2015 1197 1699 -409 -54 275 O ATOM 1700 CB AHIS A 358 64.883 14.804 -2.321 0.53 19.23 C ANISOU 1700 CB AHIS A 358 2865 1996 2445 -512 -80 434 C ATOM 1701 CB BHIS A 358 64.834 14.856 -2.283 0.47 18.89 C ANISOU 1701 CB BHIS A 358 2820 1957 2401 -511 -78 433 C ATOM 1702 CG AHIS A 358 65.178 15.772 -1.219 0.53 19.82 C ANISOU 1702 CG AHIS A 358 2921 2153 2458 -500 -56 447 C ATOM 1703 CG BHIS A 358 64.052 14.209 -1.184 0.47 21.74 C ANISOU 1703 CG BHIS A 358 3197 2332 2731 -584 -80 512 C ATOM 1704 ND1AHIS A 358 64.227 16.183 -0.310 0.53 22.29 N ANISOU 1704 ND1AHIS A 358 3235 2469 2764 -441 -68 424 N ATOM 1705 ND1BHIS A 358 64.325 12.940 -0.721 0.47 25.42 N ANISOU 1705 ND1BHIS A 358 3623 2893 3143 -629 -34 528 N ATOM 1706 CD2AHIS A 358 66.322 16.412 -0.878 0.53 20.23 C ANISOU 1706 CD2AHIS A 358 2950 2288 2450 -541 -20 475 C ATOM 1707 CD2BHIS A 358 62.992 14.651 -0.467 0.47 24.91 C ANISOU 1707 CD2BHIS A 358 3631 2687 3148 -596 -117 562 C ATOM 1708 CE1AHIS A 358 64.773 17.032 0.542 0.53 18.87 C ANISOU 1708 CE1AHIS A 358 2786 2113 2271 -446 -45 436 C ATOM 1709 CE1BHIS A 358 63.474 12.632 0.240 0.47 25.93 C ANISOU 1709 CE1BHIS A 358 3693 2970 3188 -669 -39 585 C ATOM 1710 NE2AHIS A 358 66.044 17.184 0.222 0.53 19.96 N ANISOU 1710 NE2AHIS A 358 2909 2302 2372 -504 -15 465 N ATOM 1711 NE2BHIS A 358 62.654 13.653 0.414 0.47 27.23 N ANISOU 1711 NE2BHIS A 358 3904 3047 3395 -652 -91 609 N ATOM 1712 N PHE A 359 64.451 17.734 -3.830 1.00 13.98 N ANISOU 1712 N PHE A 359 2098 1459 1754 -440 3 296 N ATOM 1713 CA PHE A 359 65.201 18.870 -4.351 1.00 14.50 C ANISOU 1713 CA PHE A 359 2144 1545 1821 -384 15 245 C ATOM 1714 C PHE A 359 66.073 19.446 -3.241 1.00 14.75 C ANISOU 1714 C PHE A 359 2178 1606 1821 -360 13 256 C ATOM 1715 O PHE A 359 65.670 19.474 -2.079 1.00 14.43 O ANISOU 1715 O PHE A 359 2139 1606 1739 -388 22 291 O ATOM 1716 CB PHE A 359 64.271 19.959 -4.892 1.00 15.88 C ANISOU 1716 CB PHE A 359 2277 1774 1983 -386 48 211 C ATOM 1717 CG PHE A 359 63.652 19.635 -6.221 1.00 13.56 C ANISOU 1717 CG PHE A 359 1976 1456 1719 -395 45 186 C ATOM 1718 CD1 PHE A 359 64.371 19.796 -7.393 1.00 15.86 C ANISOU 1718 CD1 PHE A 359 2273 1719 2035 -357 35 147 C ATOM 1719 CD2 PHE A 359 62.342 19.193 -6.298 1.00 11.68 C ANISOU 1719 CD2 PHE A 359 1723 1233 1481 -445 51 201 C ATOM 1720 CE1 PHE A 359 63.799 19.509 -8.619 1.00 16.11 C ANISOU 1720 CE1 PHE A 359 2301 1737 2086 -365 30 122 C ATOM 1721 CE2 PHE A 359 61.763 18.904 -7.520 1.00 15.37 C ANISOU 1721 CE2 PHE A 359 2184 1683 1975 -455 42 176 C ATOM 1722 CZ PHE A 359 62.494 19.063 -8.684 1.00 14.95 C ANISOU 1722 CZ PHE A 359 2142 1600 1940 -414 30 134 C ATOM 1723 N SER A 360 67.263 19.911 -3.602 1.00 14.12 N ANISOU 1723 N SER A 360 2096 1512 1757 -312 3 225 N ATOM 1724 CA SER A 360 68.161 20.546 -2.643 1.00 14.25 C ANISOU 1724 CA SER A 360 2110 1556 1747 -288 -4 228 C ATOM 1725 C SER A 360 68.910 21.699 -3.290 1.00 14.94 C ANISOU 1725 C SER A 360 2172 1657 1848 -250 5 180 C ATOM 1726 O SER A 360 69.262 21.635 -4.468 1.00 12.89 O ANISOU 1726 O SER A 360 1905 1369 1622 -231 5 153 O ATOM 1727 CB SER A 360 69.163 19.537 -2.079 1.00 13.76 C ANISOU 1727 CB SER A 360 2079 1452 1697 -275 -46 262 C ATOM 1728 OG SER A 360 68.516 18.546 -1.303 1.00 19.83 O ANISOU 1728 OG SER A 360 2877 2209 2449 -317 -58 319 O ATOM 1729 N ALA A 361 69.152 22.751 -2.517 1.00 13.84 N ANISOU 1729 N ALA A 361 2019 1560 1679 -243 12 168 N ATOM 1730 CA ALA A 361 69.998 23.840 -2.978 1.00 15.14 C ANISOU 1730 CA ALA A 361 2163 1731 1860 -215 13 130 C ATOM 1731 C ALA A 361 71.453 23.391 -2.930 1.00 14.25 C ANISOU 1731 C ALA A 361 2052 1594 1768 -188 -17 134 C ATOM 1732 O ALA A 361 71.876 22.741 -1.977 1.00 12.65 O ANISOU 1732 O ALA A 361 1867 1389 1552 -187 -43 163 O ATOM 1733 CB ALA A 361 69.790 25.086 -2.133 1.00 14.08 C ANISOU 1733 CB ALA A 361 2017 1641 1693 -216 23 111 C ATOM 1734 N LEU A 362 72.213 23.728 -3.966 1.00 10.83 N ANISOU 1734 N LEU A 362 1600 1149 1367 -167 -15 107 N ATOM 1735 CA LEU A 362 73.623 23.368 -4.020 1.00 11.45 C ANISOU 1735 CA LEU A 362 1667 1215 1469 -137 -39 103 C ATOM 1736 C LEU A 362 74.501 24.533 -3.584 1.00 11.49 C ANISOU 1736 C LEU A 362 1646 1251 1469 -133 -46 86 C ATOM 1737 O LEU A 362 74.256 25.683 -3.953 1.00 14.43 O ANISOU 1737 O LEU A 362 2005 1639 1840 -145 -26 66 O ATOM 1738 CB LEU A 362 74.015 22.919 -5.430 1.00 11.33 C ANISOU 1738 CB LEU A 362 1639 1178 1488 -117 -30 82 C ATOM 1739 CG LEU A 362 73.461 21.582 -5.931 1.00 10.49 C ANISOU 1739 CG LEU A 362 1560 1030 1398 -114 -36 89 C ATOM 1740 CD1 LEU A 362 73.756 21.409 -7.414 1.00 9.54 C ANISOU 1740 CD1 LEU A 362 1423 901 1299 -95 -21 54 C ATOM 1741 CD2 LEU A 362 74.050 20.425 -5.132 1.00 8.61 C ANISOU 1741 CD2 LEU A 362 1343 758 1173 -95 -76 115 C ATOM 1742 N VAL A 363 75.522 24.228 -2.793 1.00 13.84 N ANISOU 1742 N VAL A 363 1938 1553 1767 -116 -79 96 N ATOM 1743 CA VAL A 363 76.511 25.223 -2.395 1.00 8.40 C ANISOU 1743 CA VAL A 363 1221 892 1080 -114 -93 78 C ATOM 1744 C VAL A 363 77.898 24.604 -2.388 1.00 8.76 C ANISOU 1744 C VAL A 363 1240 935 1153 -83 -125 79 C ATOM 1745 O VAL A 363 78.043 23.393 -2.199 1.00 10.24 O ANISOU 1745 O VAL A 363 1443 1098 1348 -59 -147 100 O ATOM 1746 CB VAL A 363 76.228 25.802 -0.993 1.00 12.10 C ANISOU 1746 CB VAL A 363 1704 1387 1504 -131 -110 82 C ATOM 1747 CG1 VAL A 363 74.890 26.529 -0.962 1.00 13.19 C ANISOU 1747 CG1 VAL A 363 1859 1536 1618 -154 -78 70 C ATOM 1748 CG2 VAL A 363 76.286 24.699 0.058 1.00 10.60 C ANISOU 1748 CG2 VAL A 363 1542 1197 1289 -123 -142 119 C ATOM 1749 N SER A 364 78.914 25.432 -2.601 1.00 12.87 N ANISOU 1749 N SER A 364 1719 1480 1692 -82 -129 58 N ATOM 1750 CA SER A 364 80.291 25.005 -2.393 1.00 9.28 C ANISOU 1750 CA SER A 364 1227 1037 1260 -53 -163 56 C ATOM 1751 C SER A 364 80.610 25.109 -0.907 1.00 9.78 C ANISOU 1751 C SER A 364 1302 1119 1296 -56 -208 70 C ATOM 1752 O SER A 364 79.855 25.721 -0.151 1.00 10.25 O ANISOU 1752 O SER A 364 1390 1187 1315 -83 -206 72 O ATOM 1753 CB SER A 364 81.264 25.853 -3.210 1.00 9.85 C ANISOU 1753 CB SER A 364 1243 1139 1363 -60 -148 30 C ATOM 1754 OG SER A 364 81.296 27.186 -2.729 1.00 12.09 O ANISOU 1754 OG SER A 364 1520 1440 1635 -98 -153 20 O ATOM 1755 N MET A 365 81.719 24.514 -0.484 1.00 11.72 N ANISOU 1755 N MET A 365 1523 1374 1558 -24 -251 77 N ATOM 1756 CA MET A 365 82.122 24.606 0.915 1.00 15.51 C ANISOU 1756 CA MET A 365 2011 1877 2007 -25 -302 92 C ATOM 1757 C MET A 365 82.550 26.027 1.256 1.00 13.96 C ANISOU 1757 C MET A 365 1786 1718 1802 -58 -307 61 C ATOM 1758 O MET A 365 82.436 26.462 2.405 1.00 16.68 O ANISOU 1758 O MET A 365 2150 2083 2103 -74 -335 61 O ATOM 1759 CB MET A 365 83.251 23.620 1.227 1.00 17.58 C ANISOU 1759 CB MET A 365 2247 2138 2293 22 -353 107 C ATOM 1760 CG MET A 365 82.799 22.169 1.290 1.00 23.80 C ANISOU 1760 CG MET A 365 3079 2878 3084 54 -369 145 C ATOM 1761 SD MET A 365 81.424 21.910 2.433 1.00 34.93 S ANISOU 1761 SD MET A 365 4568 4279 4424 17 -372 193 S ATOM 1762 CE MET A 365 82.090 22.621 3.941 1.00 11.79 C ANISOU 1762 CE MET A 365 1630 1407 1443 5 -424 197 C ATOM 1763 N GLU A 366 83.044 26.746 0.254 1.00 12.87 N ANISOU 1763 N GLU A 366 1602 1586 1702 -71 -280 35 N ATOM 1764 CA GLU A 366 83.429 28.139 0.435 1.00 17.05 C ANISOU 1764 CA GLU A 366 2106 2137 2234 -110 -286 7 C ATOM 1765 C GLU A 366 82.202 28.997 0.735 1.00 14.74 C ANISOU 1765 C GLU A 366 1862 1829 1908 -142 -264 -4 C ATOM 1766 O GLU A 366 82.237 29.856 1.615 1.00 10.82 O ANISOU 1766 O GLU A 366 1375 1347 1389 -163 -290 -25 O ATOM 1767 CB GLU A 366 84.159 28.670 -0.801 1.00 19.89 C ANISOU 1767 CB GLU A 366 2409 2506 2642 -125 -258 -7 C ATOM 1768 CG GLU A 366 85.549 28.083 -1.017 1.00 29.77 C ANISOU 1768 CG GLU A 366 3593 3789 3929 -95 -281 -8 C ATOM 1769 CD GLU A 366 85.519 26.691 -1.629 1.00 37.35 C ANISOU 1769 CD GLU A 366 4553 4734 4902 -41 -267 3 C ATOM 1770 OE1 GLU A 366 86.600 26.185 -2.002 1.00 42.17 O ANISOU 1770 OE1 GLU A 366 5105 5372 5547 -8 -278 -5 O ATOM 1771 OE2 GLU A 366 84.420 26.105 -1.741 1.00 36.67 O ANISOU 1771 OE2 GLU A 366 4525 4611 4796 -31 -248 17 O ATOM 1772 N GLN A 367 81.120 28.759 -0.001 1.00 10.59 N ANISOU 1772 N GLN A 367 1367 1278 1380 -141 -219 4 N ATOM 1773 CA GLN A 367 79.856 29.443 0.250 1.00 9.54 C ANISOU 1773 CA GLN A 367 1274 1133 1216 -161 -197 -7 C ATOM 1774 C GLN A 367 79.264 29.044 1.597 1.00 10.93 C ANISOU 1774 C GLN A 367 1490 1327 1335 -155 -217 2 C ATOM 1775 O GLN A 367 78.753 29.885 2.331 1.00 12.58 O ANISOU 1775 O GLN A 367 1719 1550 1512 -170 -221 -24 O ATOM 1776 CB GLN A 367 78.845 29.143 -0.857 1.00 11.70 C ANISOU 1776 CB GLN A 367 1564 1381 1499 -159 -149 3 C ATOM 1777 CG GLN A 367 79.209 29.707 -2.218 1.00 13.46 C ANISOU 1777 CG GLN A 367 1756 1594 1765 -171 -124 -4 C ATOM 1778 CD GLN A 367 78.308 29.180 -3.317 1.00 12.50 C ANISOU 1778 CD GLN A 367 1649 1453 1647 -164 -84 8 C ATOM 1779 OE1 GLN A 367 77.895 28.018 -3.295 1.00 14.10 O ANISOU 1779 OE1 GLN A 367 1871 1648 1840 -143 -80 24 O ATOM 1780 NE2 GLN A 367 77.989 30.035 -4.281 1.00 11.34 N ANISOU 1780 NE2 GLN A 367 1498 1297 1516 -184 -59 3 N ATOM 1781 N LYS A 368 79.327 27.755 1.912 1.00 9.72 N ANISOU 1781 N LYS A 368 1349 1175 1168 -133 -231 38 N ATOM 1782 CA LYS A 368 78.693 27.246 3.119 1.00 13.94 C ANISOU 1782 CA LYS A 368 1924 1730 1643 -133 -246 60 C ATOM 1783 C LYS A 368 79.366 27.794 4.379 1.00 12.01 C ANISOU 1783 C LYS A 368 1678 1526 1361 -138 -293 44 C ATOM 1784 O LYS A 368 78.703 28.026 5.393 1.00 12.33 O ANISOU 1784 O LYS A 368 1748 1598 1338 -150 -295 39 O ATOM 1785 CB LYS A 368 78.710 25.715 3.127 1.00 12.40 C ANISOU 1785 CB LYS A 368 1747 1515 1450 -112 -259 111 C ATOM 1786 CG LYS A 368 77.736 25.094 4.120 1.00 11.85 C ANISOU 1786 CG LYS A 368 1724 1461 1317 -125 -259 148 C ATOM 1787 CD LYS A 368 77.675 23.579 3.965 1.00 12.75 C ANISOU 1787 CD LYS A 368 1861 1538 1446 -111 -273 203 C ATOM 1788 CE LYS A 368 76.641 22.970 4.893 1.00 14.95 C ANISOU 1788 CE LYS A 368 2185 1832 1662 -137 -270 250 C ATOM 1789 NZ LYS A 368 76.911 23.306 6.320 1.00 13.25 N ANISOU 1789 NZ LYS A 368 1982 1675 1377 -145 -303 259 N ATOM 1790 N GLU A 369 80.677 28.004 4.304 1.00 10.76 N ANISOU 1790 N GLU A 369 1479 1373 1237 -131 -329 32 N ATOM 1791 CA GLU A 369 81.448 28.524 5.431 1.00 11.33 C ANISOU 1791 CA GLU A 369 1542 1484 1278 -137 -382 13 C ATOM 1792 C GLU A 369 81.594 30.040 5.352 1.00 16.43 C ANISOU 1792 C GLU A 369 2172 2132 1939 -166 -381 -44 C ATOM 1793 O GLU A 369 82.245 30.652 6.197 1.00 16.39 O ANISOU 1793 O GLU A 369 2157 2155 1916 -177 -427 -72 O ATOM 1794 CB GLU A 369 82.831 27.868 5.486 1.00 15.32 C ANISOU 1794 CB GLU A 369 2007 1998 1815 -112 -433 32 C ATOM 1795 CG GLU A 369 82.803 26.361 5.705 1.00 21.30 C ANISOU 1795 CG GLU A 369 2787 2745 2563 -78 -451 89 C ATOM 1796 CD GLU A 369 82.342 25.976 7.101 1.00 27.11 C ANISOU 1796 CD GLU A 369 3571 3511 3217 -82 -482 119 C ATOM 1797 OE1 GLU A 369 82.060 24.781 7.324 1.00 32.42 O ANISOU 1797 OE1 GLU A 369 4275 4167 3875 -65 -493 174 O ATOM 1798 OE2 GLU A 369 82.269 26.864 7.976 1.00 26.15 O ANISOU 1798 OE2 GLU A 369 3458 3431 3045 -104 -497 88 O ATOM 1799 N ASN A 370 80.996 30.635 4.324 1.00 15.77 N ANISOU 1799 N ASN A 370 2086 2014 1891 -179 -334 -59 N ATOM 1800 CA ASN A 370 80.946 32.087 4.187 1.00 16.34 C ANISOU 1800 CA ASN A 370 2153 2072 1982 -207 -332 -108 C ATOM 1801 C ASN A 370 82.319 32.703 3.903 1.00 17.58 C ANISOU 1801 C ASN A 370 2259 2228 2191 -228 -366 -123 C ATOM 1802 O ASN A 370 82.562 33.872 4.212 1.00 19.28 O ANISOU 1802 O ASN A 370 2473 2437 2416 -257 -390 -164 O ATOM 1803 CB ASN A 370 80.333 32.705 5.452 1.00 19.75 C ANISOU 1803 CB ASN A 370 2622 2529 2351 -211 -350 -147 C ATOM 1804 CG ASN A 370 79.758 34.087 5.211 1.00 23.52 C ANISOU 1804 CG ASN A 370 3113 2976 2849 -229 -336 -199 C ATOM 1805 OD1 ASN A 370 79.291 34.397 4.116 1.00 23.97 O ANISOU 1805 OD1 ASN A 370 3166 2992 2949 -233 -299 -192 O ATOM 1806 ND2 ASN A 370 79.788 34.926 6.240 1.00 26.60 N ANISOU 1806 ND2 ASN A 370 3520 3383 3206 -236 -370 -252 N ATOM 1807 N THR A 371 83.214 31.912 3.315 1.00 16.14 N ANISOU 1807 N THR A 371 2034 2054 2043 -215 -370 -92 N ATOM 1808 CA THR A 371 84.546 32.401 2.966 1.00 18.03 C ANISOU 1808 CA THR A 371 2212 2305 2333 -237 -396 -102 C ATOM 1809 C THR A 371 84.585 33.049 1.573 1.00 19.68 C ANISOU 1809 C THR A 371 2394 2486 2595 -265 -353 -100 C ATOM 1810 O THR A 371 85.394 33.939 1.323 1.00 21.47 O ANISOU 1810 O THR A 371 2582 2716 2861 -305 -370 -113 O ATOM 1811 CB THR A 371 85.598 31.266 3.035 1.00 19.63 C ANISOU 1811 CB THR A 371 2370 2541 2548 -203 -424 -75 C ATOM 1812 OG1 THR A 371 85.368 30.316 1.986 1.00 21.58 O ANISOU 1812 OG1 THR A 371 2611 2773 2817 -173 -379 -46 O ATOM 1813 CG2 THR A 371 85.535 30.565 4.382 1.00 18.63 C ANISOU 1813 CG2 THR A 371 2275 2439 2364 -176 -471 -64 C ATOM 1814 N LYS A 372 83.711 32.597 0.677 1.00 20.13 N ANISOU 1814 N LYS A 372 2474 2521 2653 -249 -301 -79 N ATOM 1815 CA LYS A 372 83.606 33.152 -0.675 1.00 23.31 C ANISOU 1815 CA LYS A 372 2861 2902 3095 -274 -259 -71 C ATOM 1816 C LYS A 372 82.149 33.134 -1.118 1.00 23.96 C ANISOU 1816 C LYS A 372 2996 2950 3157 -264 -218 -65 C ATOM 1817 O LYS A 372 81.413 32.198 -0.807 1.00 23.61 O ANISOU 1817 O LYS A 372 2982 2908 3079 -231 -207 -55 O ATOM 1818 CB LYS A 372 84.479 32.363 -1.659 1.00 28.18 C ANISOU 1818 CB LYS A 372 3421 3546 3741 -260 -238 -49 C ATOM 1819 CG LYS A 372 84.743 33.072 -2.986 1.00 34.28 C ANISOU 1819 CG LYS A 372 4161 4316 4548 -298 -201 -38 C ATOM 1820 CD LYS A 372 85.861 32.390 -3.767 1.00 38.01 C ANISOU 1820 CD LYS A 372 4563 4836 5045 -284 -185 -28 C ATOM 1821 CE LYS A 372 85.322 31.523 -4.900 1.00 39.39 C ANISOU 1821 CE LYS A 372 4746 5010 5211 -251 -133 -15 C ATOM 1822 NZ LYS A 372 84.731 32.331 -6.005 1.00 39.56 N ANISOU 1822 NZ LYS A 372 4783 5015 5234 -290 -92 -1 N ATOM 1823 N GLU A 373 81.731 34.172 -1.835 1.00 21.39 N ANISOU 1823 N GLU A 373 2680 2594 2854 -295 -199 -69 N ATOM 1824 CA GLU A 373 80.337 34.289 -2.243 1.00 22.17 C ANISOU 1824 CA GLU A 373 2824 2663 2938 -284 -166 -67 C ATOM 1825 C GLU A 373 80.004 33.490 -3.502 1.00 19.94 C ANISOU 1825 C GLU A 373 2535 2383 2660 -269 -122 -37 C ATOM 1826 O GLU A 373 78.975 32.819 -3.561 1.00 16.60 O ANISOU 1826 O GLU A 373 2141 1954 2211 -244 -101 -32 O ATOM 1827 CB GLU A 373 79.968 35.762 -2.442 1.00 27.93 C ANISOU 1827 CB GLU A 373 3571 3350 3691 -316 -174 -84 C ATOM 1828 CG GLU A 373 79.581 36.450 -1.138 1.00 37.33 C ANISOU 1828 CG GLU A 373 4793 4528 4861 -313 -209 -129 C ATOM 1829 CD GLU A 373 78.388 35.785 -0.466 1.00 44.37 C ANISOU 1829 CD GLU A 373 5721 5436 5702 -273 -192 -139 C ATOM 1830 OE1 GLU A 373 78.566 34.754 0.221 1.00 48.33 O ANISOU 1830 OE1 GLU A 373 6221 5976 6167 -253 -197 -130 O ATOM 1831 OE2 GLU A 373 77.261 36.292 -0.636 1.00 47.23 O ANISOU 1831 OE2 GLU A 373 6111 5773 6060 -263 -175 -154 O ATOM 1832 N GLN A 374 80.874 33.557 -4.501 1.00 20.39 N ANISOU 1832 N GLN A 374 2550 2454 2745 -287 -108 -21 N ATOM 1833 CA GLN A 374 80.562 32.977 -5.803 1.00 20.08 C ANISOU 1833 CA GLN A 374 2504 2420 2705 -277 -65 0 C ATOM 1834 C GLN A 374 81.085 31.555 -5.986 1.00 15.63 C ANISOU 1834 C GLN A 374 1916 1888 2136 -238 -56 4 C ATOM 1835 O GLN A 374 82.207 31.236 -5.605 1.00 14.06 O ANISOU 1835 O GLN A 374 1675 1717 1949 -231 -76 -1 O ATOM 1836 CB GLN A 374 81.111 33.867 -6.925 1.00 21.39 C ANISOU 1836 CB GLN A 374 2640 2591 2896 -320 -48 19 C ATOM 1837 CG GLN A 374 80.257 35.089 -7.230 1.00 27.23 C ANISOU 1837 CG GLN A 374 3417 3285 3644 -349 -49 26 C ATOM 1838 CD GLN A 374 80.573 35.695 -8.586 1.00 34.39 C ANISOU 1838 CD GLN A 374 4304 4197 4565 -388 -25 60 C ATOM 1839 OE1 GLN A 374 81.638 35.451 -9.155 1.00 35.68 O ANISOU 1839 OE1 GLN A 374 4417 4407 4735 -405 -8 74 O ATOM 1840 NE2 GLN A 374 79.642 36.480 -9.115 1.00 37.64 N ANISOU 1840 NE2 GLN A 374 4753 4568 4978 -401 -22 76 N ATOM 1841 N ALA A 375 80.253 30.706 -6.578 1.00 13.03 N ANISOU 1841 N ALA A 375 1611 1549 1790 -212 -30 9 N ATOM 1842 CA ALA A 375 80.672 29.382 -7.025 1.00 13.28 C ANISOU 1842 CA ALA A 375 1624 1598 1823 -174 -19 8 C ATOM 1843 C ALA A 375 80.320 29.260 -8.502 1.00 12.75 C ANISOU 1843 C ALA A 375 1554 1539 1752 -176 22 11 C ATOM 1844 O ALA A 375 79.684 30.155 -9.058 1.00 10.15 O ANISOU 1844 O ALA A 375 1241 1199 1417 -207 38 22 O ATOM 1845 CB ALA A 375 80.000 28.288 -6.210 1.00 8.49 C ANISOU 1845 CB ALA A 375 1057 970 1200 -141 -36 9 C ATOM 1846 N VAL A 376 80.725 28.169 -9.141 1.00 13.33 N ANISOU 1846 N VAL A 376 1608 1630 1827 -141 36 0 N ATOM 1847 CA VAL A 376 80.406 27.993 -10.554 1.00 16.50 C ANISOU 1847 CA VAL A 376 2007 2046 2215 -141 75 -4 C ATOM 1848 C VAL A 376 79.694 26.673 -10.846 1.00 15.81 C ANISOU 1848 C VAL A 376 1953 1936 2120 -102 78 -19 C ATOM 1849 O VAL A 376 79.885 25.668 -10.156 1.00 19.28 O ANISOU 1849 O VAL A 376 2400 2355 2571 -66 53 -28 O ATOM 1850 CB VAL A 376 81.669 28.088 -11.438 1.00 20.88 C ANISOU 1850 CB VAL A 376 2497 2660 2776 -142 99 -12 C ATOM 1851 CG1 VAL A 376 82.295 29.476 -11.318 1.00 19.05 C ANISOU 1851 CG1 VAL A 376 2234 2448 2556 -197 98 10 C ATOM 1852 CG2 VAL A 376 82.668 27.001 -11.073 1.00 23.56 C ANISOU 1852 CG2 VAL A 376 2799 3017 3135 -91 84 -38 C ATOM 1853 N ILE A 377 78.863 26.705 -11.880 1.00 11.89 N ANISOU 1853 N ILE A 377 1477 1438 1602 -111 103 -20 N ATOM 1854 CA ILE A 377 78.112 25.544 -12.329 1.00 14.78 C ANISOU 1854 CA ILE A 377 1875 1781 1961 -83 105 -38 C ATOM 1855 C ILE A 377 78.201 25.471 -13.853 1.00 15.44 C ANISOU 1855 C ILE A 377 1942 1902 2021 -81 139 -56 C ATOM 1856 O ILE A 377 77.997 26.474 -14.536 1.00 11.81 O ANISOU 1856 O ILE A 377 1477 1469 1542 -116 160 -36 O ATOM 1857 CB ILE A 377 76.632 25.613 -11.869 1.00 19.52 C ANISOU 1857 CB ILE A 377 2525 2339 2550 -102 94 -21 C ATOM 1858 CG1 ILE A 377 75.855 24.368 -12.307 1.00 17.87 C ANISOU 1858 CG1 ILE A 377 2348 2104 2339 -82 91 -38 C ATOM 1859 CG2 ILE A 377 75.960 26.884 -12.376 1.00 19.06 C ANISOU 1859 CG2 ILE A 377 2474 2292 2476 -139 109 -2 C ATOM 1860 CD1 ILE A 377 76.055 23.170 -11.400 1.00 13.84 C ANISOU 1860 CD1 ILE A 377 1853 1554 1849 -53 61 -42 C ATOM 1861 N PRO A 378 78.542 24.291 -14.389 1.00 18.36 N ANISOU 1861 N PRO A 378 2306 2277 2394 -38 144 -93 N ATOM 1862 CA PRO A 378 78.580 24.100 -15.843 1.00 17.46 C ANISOU 1862 CA PRO A 378 2180 2206 2249 -31 176 -120 C ATOM 1863 C PRO A 378 77.191 24.169 -16.470 1.00 15.86 C ANISOU 1863 C PRO A 378 2023 1985 2019 -54 178 -113 C ATOM 1864 O PRO A 378 76.199 23.849 -15.814 1.00 13.13 O ANISOU 1864 O PRO A 378 1718 1585 1686 -60 153 -103 O ATOM 1865 CB PRO A 378 79.178 22.697 -16.002 1.00 18.90 C ANISOU 1865 CB PRO A 378 2351 2380 2448 30 169 -172 C ATOM 1866 CG PRO A 378 79.883 22.428 -14.709 1.00 20.10 C ANISOU 1866 CG PRO A 378 2490 2506 2643 52 136 -162 C ATOM 1867 CD PRO A 378 79.077 23.128 -13.663 1.00 18.85 C ANISOU 1867 CD PRO A 378 2367 2309 2488 9 115 -114 C ATOM 1868 N LEU A 379 77.122 24.581 -17.730 1.00 15.12 N ANISOU 1868 N LEU A 379 1919 1941 1885 -69 208 -117 N ATOM 1869 CA LEU A 379 75.852 24.615 -18.441 1.00 14.81 C ANISOU 1869 CA LEU A 379 1920 1892 1817 -87 205 -113 C ATOM 1870 C LEU A 379 75.773 23.480 -19.459 1.00 14.44 C ANISOU 1870 C LEU A 379 1881 1860 1746 -54 212 -169 C ATOM 1871 O LEU A 379 74.947 23.506 -20.372 1.00 19.44 O ANISOU 1871 O LEU A 379 2536 2508 2342 -68 215 -175 O ATOM 1872 CB LEU A 379 75.656 25.969 -19.124 1.00 11.66 C ANISOU 1872 CB LEU A 379 1514 1532 1385 -132 223 -70 C ATOM 1873 CG LEU A 379 75.549 27.160 -18.169 1.00 14.88 C ANISOU 1873 CG LEU A 379 1923 1911 1818 -164 209 -22 C ATOM 1874 CD1 LEU A 379 75.379 28.464 -18.936 1.00 13.24 C ANISOU 1874 CD1 LEU A 379 1714 1732 1584 -206 220 23 C ATOM 1875 CD2 LEU A 379 74.408 26.963 -17.176 1.00 13.96 C ANISOU 1875 CD2 LEU A 379 1844 1733 1728 -162 178 -17 C ATOM 1876 N THR A 380 76.643 22.487 -19.293 1.00 13.91 N ANISOU 1876 N THR A 380 1796 1789 1702 -7 211 -214 N ATOM 1877 CA THR A 380 76.598 21.272 -20.098 1.00 16.25 C ANISOU 1877 CA THR A 380 2104 2083 1986 34 209 -279 C ATOM 1878 C THR A 380 76.530 20.048 -19.194 1.00 15.86 C ANISOU 1878 C THR A 380 2081 1952 1992 71 169 -303 C ATOM 1879 O THR A 380 76.721 20.153 -17.981 1.00 12.72 O ANISOU 1879 O THR A 380 1683 1516 1633 68 149 -269 O ATOM 1880 CB THR A 380 77.834 21.130 -21.017 1.00 17.05 C ANISOU 1880 CB THR A 380 2154 2266 2059 69 248 -325 C ATOM 1881 OG1 THR A 380 79.009 20.955 -20.215 1.00 18.72 O ANISOU 1881 OG1 THR A 380 2323 2477 2312 102 246 -330 O ATOM 1882 CG2 THR A 380 78.001 22.353 -21.911 1.00 15.04 C ANISOU 1882 CG2 THR A 380 1872 2098 1745 24 289 -290 C ATOM 1883 N ASP A 381 76.267 18.887 -19.785 1.00 16.17 N ANISOU 1883 N ASP A 381 2146 1964 2034 105 155 -362 N ATOM 1884 CA ASP A 381 76.409 17.631 -19.061 1.00 14.43 C ANISOU 1884 CA ASP A 381 1950 1663 1870 146 114 -389 C ATOM 1885 C ASP A 381 77.871 17.197 -19.085 1.00 15.72 C ANISOU 1885 C ASP A 381 2067 1852 2053 211 123 -433 C ATOM 1886 O ASP A 381 78.738 17.942 -19.551 1.00 13.72 O ANISOU 1886 O ASP A 381 1758 1686 1770 215 164 -435 O ATOM 1887 CB ASP A 381 75.497 16.541 -19.646 1.00 17.84 C ANISOU 1887 CB ASP A 381 2432 2039 2306 153 85 -436 C ATOM 1888 CG ASP A 381 75.740 16.282 -21.132 1.00 19.37 C ANISOU 1888 CG ASP A 381 2614 2293 2453 181 111 -510 C ATOM 1889 OD1 ASP A 381 76.890 16.402 -21.602 1.00 16.86 O ANISOU 1889 OD1 ASP A 381 2248 2042 2116 223 144 -546 O ATOM 1890 OD2 ASP A 381 74.763 15.941 -21.832 1.00 20.66 O ANISOU 1890 OD2 ASP A 381 2814 2443 2594 161 98 -536 O ATOM 1891 N SER A 382 78.142 15.993 -18.593 1.00 15.41 N ANISOU 1891 N SER A 382 2048 1739 2067 262 82 -465 N ATOM 1892 CA SER A 382 79.514 15.505 -18.494 1.00 18.15 C ANISOU 1892 CA SER A 382 2349 2104 2444 334 82 -508 C ATOM 1893 C SER A 382 80.113 15.199 -19.865 1.00 22.99 C ANISOU 1893 C SER A 382 2926 2787 3021 383 118 -594 C ATOM 1894 O SER A 382 81.325 15.027 -19.995 1.00 24.83 O ANISOU 1894 O SER A 382 3101 3069 3265 442 134 -635 O ATOM 1895 CB SER A 382 79.573 14.262 -17.602 1.00 21.91 C ANISOU 1895 CB SER A 382 2864 2471 2990 379 19 -515 C ATOM 1896 OG SER A 382 78.643 13.283 -18.029 1.00 27.68 O ANISOU 1896 OG SER A 382 3658 3126 3734 380 -12 -551 O ATOM 1897 N GLU A 383 79.264 15.131 -20.885 1.00 22.82 N ANISOU 1897 N GLU A 383 2936 2780 2954 360 131 -624 N ATOM 1898 CA GLU A 383 79.730 14.890 -22.247 1.00 26.46 C ANISOU 1898 CA GLU A 383 3368 3321 3366 401 169 -708 C ATOM 1899 C GLU A 383 79.838 16.201 -23.022 1.00 23.77 C ANISOU 1899 C GLU A 383 2985 3102 2946 349 231 -674 C ATOM 1900 O GLU A 383 80.016 16.204 -24.240 1.00 23.28 O ANISOU 1900 O GLU A 383 2903 3121 2820 363 268 -728 O ATOM 1901 CB GLU A 383 78.798 13.916 -22.970 1.00 32.30 C ANISOU 1901 CB GLU A 383 4170 4003 4099 412 140 -772 C ATOM 1902 CG GLU A 383 78.665 12.565 -22.284 1.00 41.02 C ANISOU 1902 CG GLU A 383 5323 4976 5285 458 73 -804 C ATOM 1903 CD GLU A 383 80.007 11.899 -22.032 1.00 48.61 C ANISOU 1903 CD GLU A 383 6242 5934 6294 550 66 -858 C ATOM 1904 OE1 GLU A 383 80.635 11.433 -23.007 1.00 50.82 O ANISOU 1904 OE1 GLU A 383 6493 6266 6551 616 89 -955 O ATOM 1905 OE2 GLU A 383 80.433 11.840 -20.858 1.00 52.03 O ANISOU 1905 OE2 GLU A 383 6669 6316 6785 561 37 -807 O ATOM 1906 N TYR A 384 79.715 17.310 -22.297 1.00 20.96 N ANISOU 1906 N TYR A 384 2618 2753 2592 289 237 -584 N ATOM 1907 CA TYR A 384 79.885 18.650 -22.852 1.00 20.29 C ANISOU 1907 CA TYR A 384 2496 2768 2447 234 287 -535 C ATOM 1908 C TYR A 384 78.780 19.014 -23.840 1.00 20.46 C ANISOU 1908 C TYR A 384 2557 2813 2404 188 296 -528 C ATOM 1909 O TYR A 384 78.939 19.910 -24.666 1.00 19.96 O ANISOU 1909 O TYR A 384 2467 2842 2276 153 338 -504 O ATOM 1910 CB TYR A 384 81.263 18.782 -23.508 1.00 21.73 C ANISOU 1910 CB TYR A 384 2598 3060 2599 270 339 -576 C ATOM 1911 CG TYR A 384 82.392 18.465 -22.555 1.00 25.30 C ANISOU 1911 CG TYR A 384 3002 3497 3115 317 326 -584 C ATOM 1912 CD1 TYR A 384 82.578 19.213 -21.399 1.00 28.64 C ANISOU 1912 CD1 TYR A 384 3412 3891 3577 279 309 -508 C ATOM 1913 CD2 TYR A 384 83.264 17.413 -22.802 1.00 27.00 C ANISOU 1913 CD2 TYR A 384 3181 3725 3351 405 326 -670 C ATOM 1914 CE1 TYR A 384 83.602 18.925 -20.518 1.00 31.00 C ANISOU 1914 CE1 TYR A 384 3666 4180 3932 322 291 -514 C ATOM 1915 CE2 TYR A 384 84.292 17.119 -21.927 1.00 30.08 C ANISOU 1915 CE2 TYR A 384 3523 4103 3803 453 308 -676 C ATOM 1916 CZ TYR A 384 84.456 17.879 -20.786 1.00 31.91 C ANISOU 1916 CZ TYR A 384 3744 4310 4070 409 289 -595 C ATOM 1917 OH TYR A 384 85.476 17.592 -19.909 1.00 34.31 O ANISOU 1917 OH TYR A 384 4000 4606 4432 456 265 -599 O ATOM 1918 N LYS A 385 77.656 18.317 -23.737 1.00 18.51 N ANISOU 1918 N LYS A 385 2373 2484 2175 185 254 -543 N ATOM 1919 CA LYS A 385 76.450 18.703 -24.452 1.00 17.01 C ANISOU 1919 CA LYS A 385 2222 2305 1937 137 249 -524 C ATOM 1920 C LYS A 385 75.693 19.743 -23.632 1.00 16.69 C ANISOU 1920 C LYS A 385 2197 2230 1913 75 235 -431 C ATOM 1921 O LYS A 385 75.534 19.585 -22.420 1.00 14.99 O ANISOU 1921 O LYS A 385 1996 1942 1759 72 206 -401 O ATOM 1922 CB LYS A 385 75.569 17.483 -24.720 1.00 23.05 C ANISOU 1922 CB LYS A 385 3041 2999 2717 157 206 -585 C ATOM 1923 CG LYS A 385 74.276 17.787 -25.451 1.00 26.03 C ANISOU 1923 CG LYS A 385 3456 3387 3047 108 194 -572 C ATOM 1924 CD LYS A 385 73.484 16.513 -25.704 1.00 29.80 C ANISOU 1924 CD LYS A 385 3983 3793 3545 125 147 -639 C ATOM 1925 CE LYS A 385 72.214 16.800 -26.488 1.00 34.58 C ANISOU 1925 CE LYS A 385 4618 4419 4101 77 131 -630 C ATOM 1926 NZ LYS A 385 71.415 15.570 -26.731 1.00 36.60 N ANISOU 1926 NZ LYS A 385 4921 4604 4381 83 81 -696 N ATOM 1927 N LEU A 386 75.246 20.811 -24.285 1.00 16.10 N ANISOU 1927 N LEU A 386 2121 2213 1784 27 255 -386 N ATOM 1928 CA LEU A 386 74.471 21.841 -23.601 1.00 17.92 C ANISOU 1928 CA LEU A 386 2367 2412 2032 -24 239 -306 C ATOM 1929 C LEU A 386 73.264 21.217 -22.917 1.00 16.13 C ANISOU 1929 C LEU A 386 2185 2097 1847 -32 194 -306 C ATOM 1930 O LEU A 386 72.564 20.399 -23.511 1.00 14.24 O ANISOU 1930 O LEU A 386 1974 1841 1594 -25 174 -351 O ATOM 1931 CB LEU A 386 74.024 22.931 -24.580 1.00 20.72 C ANISOU 1931 CB LEU A 386 2721 2831 2321 -67 256 -264 C ATOM 1932 CG LEU A 386 75.129 23.863 -25.085 1.00 22.76 C ANISOU 1932 CG LEU A 386 2934 3175 2539 -83 302 -234 C ATOM 1933 CD1 LEU A 386 74.627 24.741 -26.222 1.00 22.40 C ANISOU 1933 CD1 LEU A 386 2898 3192 2421 -123 313 -194 C ATOM 1934 CD2 LEU A 386 75.671 24.714 -23.947 1.00 21.21 C ANISOU 1934 CD2 LEU A 386 2714 2949 2394 -104 302 -177 C ATOM 1935 N LEU A 387 73.045 21.590 -21.659 1.00 13.98 N ANISOU 1935 N LEU A 387 1916 1772 1623 -49 177 -258 N ATOM 1936 CA LEU A 387 71.921 21.078 -20.887 1.00 13.29 C ANISOU 1936 CA LEU A 387 1865 1613 1574 -64 140 -248 C ATOM 1937 C LEU A 387 70.600 21.396 -21.574 1.00 14.63 C ANISOU 1937 C LEU A 387 2054 1793 1711 -97 127 -237 C ATOM 1938 O LEU A 387 70.492 22.395 -22.285 1.00 17.38 O ANISOU 1938 O LEU A 387 2392 2195 2017 -116 143 -210 O ATOM 1939 CB LEU A 387 71.928 21.663 -19.471 1.00 13.56 C ANISOU 1939 CB LEU A 387 1893 1611 1647 -80 133 -195 C ATOM 1940 CG LEU A 387 73.083 21.262 -18.552 1.00 14.76 C ANISOU 1940 CG LEU A 387 2028 1742 1838 -49 132 -200 C ATOM 1941 CD1 LEU A 387 73.141 22.181 -17.342 1.00 17.73 C ANISOU 1941 CD1 LEU A 387 2396 2108 2235 -71 129 -146 C ATOM 1942 CD2 LEU A 387 72.934 19.813 -18.116 1.00 13.64 C ANISOU 1942 CD2 LEU A 387 1915 1533 1733 -24 100 -232 C ATOM 1943 N PRO A 388 69.595 20.533 -21.373 1.00 12.95 N ANISOU 1943 N PRO A 388 1870 1529 1522 -107 94 -254 N ATOM 1944 CA PRO A 388 68.257 20.738 -21.935 1.00 14.61 C ANISOU 1944 CA PRO A 388 2094 1748 1709 -139 75 -246 C ATOM 1945 C PRO A 388 67.630 22.047 -21.464 1.00 15.02 C ANISOU 1945 C PRO A 388 2133 1814 1761 -167 78 -182 C ATOM 1946 O PRO A 388 67.788 22.435 -20.306 1.00 13.29 O ANISOU 1946 O PRO A 388 1905 1568 1575 -171 82 -148 O ATOM 1947 CB PRO A 388 67.469 19.536 -21.410 1.00 13.84 C ANISOU 1947 CB PRO A 388 2023 1582 1655 -150 39 -268 C ATOM 1948 CG PRO A 388 68.506 18.491 -21.158 1.00 15.19 C ANISOU 1948 CG PRO A 388 2204 1714 1855 -111 37 -309 C ATOM 1949 CD PRO A 388 69.708 19.243 -20.673 1.00 12.95 C ANISOU 1949 CD PRO A 388 1891 1459 1571 -89 70 -283 C ATOM 1950 N LEU A 389 66.933 22.720 -22.369 1.00 12.69 N ANISOU 1950 N LEU A 389 1836 1561 1426 -184 72 -169 N ATOM 1951 CA LEU A 389 66.217 23.941 -22.036 1.00 14.03 C ANISOU 1951 CA LEU A 389 1995 1738 1598 -204 67 -115 C ATOM 1952 C LEU A 389 64.724 23.631 -21.948 1.00 13.42 C ANISOU 1952 C LEU A 389 1921 1644 1534 -224 34 -116 C ATOM 1953 O LEU A 389 64.109 23.250 -22.941 1.00 14.37 O ANISOU 1953 O LEU A 389 2049 1787 1624 -232 15 -141 O ATOM 1954 CB LEU A 389 66.494 25.022 -23.081 1.00 16.31 C ANISOU 1954 CB LEU A 389 2277 2083 1836 -207 78 -88 C ATOM 1955 CG LEU A 389 66.001 26.441 -22.803 1.00 20.82 C ANISOU 1955 CG LEU A 389 2841 2655 2416 -220 70 -29 C ATOM 1956 CD1 LEU A 389 66.708 27.021 -21.589 1.00 23.53 C ANISOU 1956 CD1 LEU A 389 3173 2966 2800 -216 86 -5 C ATOM 1957 CD2 LEU A 389 66.212 27.320 -24.027 1.00 23.30 C ANISOU 1957 CD2 LEU A 389 3158 3022 2675 -228 73 1 C ATOM 1958 N HIS A 390 64.146 23.784 -20.760 1.00 8.34 N ANISOU 1958 N HIS A 390 1269 968 932 -235 29 -92 N ATOM 1959 CA HIS A 390 62.771 23.343 -20.522 1.00 11.97 C ANISOU 1959 CA HIS A 390 1722 1416 1409 -258 3 -95 C ATOM 1960 C HIS A 390 61.709 24.308 -21.044 1.00 9.31 C ANISOU 1960 C HIS A 390 1367 1114 1055 -265 -15 -72 C ATOM 1961 O HIS A 390 61.799 25.522 -20.846 1.00 11.95 O ANISOU 1961 O HIS A 390 1691 1461 1390 -253 -7 -38 O ATOM 1962 CB HIS A 390 62.556 23.101 -19.026 1.00 10.19 C ANISOU 1962 CB HIS A 390 1490 1154 1227 -269 9 -77 C ATOM 1963 CG HIS A 390 63.445 22.038 -18.462 1.00 14.23 C ANISOU 1963 CG HIS A 390 2022 1624 1760 -263 15 -94 C ATOM 1964 ND1 HIS A 390 63.017 20.746 -18.248 1.00 14.77 N ANISOU 1964 ND1 HIS A 390 2107 1655 1852 -284 -5 -113 N ATOM 1965 CD2 HIS A 390 64.747 22.070 -18.091 1.00 14.14 C ANISOU 1965 CD2 HIS A 390 2017 1601 1753 -238 34 -94 C ATOM 1966 CE1 HIS A 390 64.014 20.030 -17.761 1.00 16.98 C ANISOU 1966 CE1 HIS A 390 2406 1895 2151 -268 -1 -122 C ATOM 1967 NE2 HIS A 390 65.075 20.810 -17.656 1.00 17.74 N ANISOU 1967 NE2 HIS A 390 2493 2011 2235 -238 23 -113 N ATOM 1968 N PHE A 391 60.704 23.746 -21.711 1.00 10.53 N ANISOU 1968 N PHE A 391 1518 1282 1200 -283 -44 -93 N ATOM 1969 CA PHE A 391 59.551 24.498 -22.202 1.00 9.05 C ANISOU 1969 CA PHE A 391 1307 1129 1001 -287 -70 -74 C ATOM 1970 C PHE A 391 59.972 25.706 -23.036 1.00 12.99 C ANISOU 1970 C PHE A 391 1813 1662 1463 -266 -70 -45 C ATOM 1971 O PHE A 391 59.428 26.804 -22.891 1.00 12.33 O ANISOU 1971 O PHE A 391 1711 1586 1387 -255 -81 -11 O ATOM 1972 CB PHE A 391 58.676 24.934 -21.026 1.00 8.85 C ANISOU 1972 CB PHE A 391 1249 1096 1017 -293 -69 -51 C ATOM 1973 CG PHE A 391 58.245 23.794 -20.144 1.00 13.82 C ANISOU 1973 CG PHE A 391 1871 1699 1679 -323 -67 -66 C ATOM 1974 CD1 PHE A 391 57.255 22.913 -20.559 1.00 14.12 C ANISOU 1974 CD1 PHE A 391 1898 1744 1722 -356 -97 -88 C ATOM 1975 CD2 PHE A 391 58.831 23.599 -18.902 1.00 12.90 C ANISOU 1975 CD2 PHE A 391 1762 1552 1589 -323 -40 -55 C ATOM 1976 CE1 PHE A 391 56.859 21.859 -19.751 1.00 14.55 C ANISOU 1976 CE1 PHE A 391 1949 1770 1810 -394 -97 -93 C ATOM 1977 CE2 PHE A 391 58.437 22.549 -18.086 1.00 13.29 C ANISOU 1977 CE2 PHE A 391 1808 1576 1665 -356 -40 -57 C ATOM 1978 CZ PHE A 391 57.451 21.677 -18.510 1.00 14.09 C ANISOU 1978 CZ PHE A 391 1900 1680 1774 -394 -68 -74 C ATOM 1979 N ALA A 392 60.940 25.488 -23.918 1.00 14.26 N ANISOU 1979 N ALA A 392 1997 1840 1581 -260 -58 -60 N ATOM 1980 CA ALA A 392 61.599 26.583 -24.619 1.00 16.71 C ANISOU 1980 CA ALA A 392 2316 2182 1853 -249 -49 -24 C ATOM 1981 C ALA A 392 60.739 27.185 -25.723 1.00 16.25 C ANISOU 1981 C ALA A 392 2256 2165 1753 -252 -86 -2 C ATOM 1982 O ALA A 392 61.005 28.294 -26.181 1.00 14.77 O ANISOU 1982 O ALA A 392 2075 1996 1542 -246 -88 45 O ATOM 1983 CB ALA A 392 62.926 26.107 -25.193 1.00 14.86 C ANISOU 1983 CB ALA A 392 2100 1967 1581 -244 -18 -48 C ATOM 1984 N VAL A 393 59.708 26.462 -26.149 1.00 17.13 N ANISOU 1984 N VAL A 393 2360 2291 1857 -263 -119 -34 N ATOM 1985 CA VAL A 393 58.909 26.908 -27.286 1.00 17.65 C ANISOU 1985 CA VAL A 393 2425 2404 1877 -265 -161 -18 C ATOM 1986 C VAL A 393 57.465 27.254 -26.929 1.00 15.35 C ANISOU 1986 C VAL A 393 2100 2110 1624 -264 -202 -4 C ATOM 1987 O VAL A 393 56.708 26.402 -26.469 1.00 15.22 O ANISOU 1987 O VAL A 393 2062 2082 1640 -280 -214 -38 O ATOM 1988 CB VAL A 393 58.883 25.840 -28.397 1.00 21.94 C ANISOU 1988 CB VAL A 393 2987 2986 2365 -278 -177 -72 C ATOM 1989 CG1 VAL A 393 58.074 26.333 -29.589 1.00 22.64 C ANISOU 1989 CG1 VAL A 393 3075 3131 2397 -280 -226 -53 C ATOM 1990 CG2 VAL A 393 60.298 25.472 -28.817 1.00 23.69 C ANISOU 1990 CG2 VAL A 393 3235 3223 2545 -271 -135 -95 C ATOM 1991 N ASP A 394 57.096 28.515 -27.134 1.00 16.39 N ANISOU 1991 N ASP A 394 2222 2251 1753 -245 -225 48 N ATOM 1992 CA ASP A 394 55.691 28.904 -27.178 1.00 13.34 C ANISOU 1992 CA ASP A 394 1800 1879 1388 -236 -273 59 C ATOM 1993 C ASP A 394 55.270 28.949 -28.639 1.00 16.17 C ANISOU 1993 C ASP A 394 2170 2293 1680 -240 -321 67 C ATOM 1994 O ASP A 394 55.770 29.776 -29.405 1.00 16.48 O ANISOU 1994 O ASP A 394 2237 2351 1674 -231 -329 112 O ATOM 1995 CB ASP A 394 55.457 30.261 -26.503 1.00 12.33 C ANISOU 1995 CB ASP A 394 1656 1723 1305 -203 -279 106 C ATOM 1996 CG ASP A 394 53.995 30.707 -26.563 1.00 14.63 C ANISOU 1996 CG ASP A 394 1903 2035 1622 -182 -331 114 C ATOM 1997 OD1 ASP A 394 53.129 29.905 -26.974 1.00 14.99 O ANISOU 1997 OD1 ASP A 394 1922 2116 1657 -201 -360 82 O ATOM 1998 OD2 ASP A 394 53.706 31.863 -26.186 1.00 16.01 O ANISOU 1998 OD2 ASP A 394 2064 2187 1831 -146 -347 148 O ATOM 1999 N PRO A 395 54.351 28.055 -29.036 1.00 18.40 N ANISOU 1999 N PRO A 395 2433 2605 1954 -259 -355 24 N ATOM 2000 CA PRO A 395 53.900 28.018 -30.432 1.00 15.99 C ANISOU 2000 CA PRO A 395 2138 2359 1580 -265 -407 24 C ATOM 2001 C PRO A 395 53.143 29.280 -30.820 1.00 17.99 C ANISOU 2001 C PRO A 395 2374 2632 1831 -236 -458 85 C ATOM 2002 O PRO A 395 52.967 29.548 -32.003 1.00 17.63 O ANISOU 2002 O PRO A 395 2346 2636 1718 -236 -500 106 O ATOM 2003 CB PRO A 395 52.983 26.791 -30.475 1.00 17.94 C ANISOU 2003 CB PRO A 395 2357 2618 1840 -295 -435 -38 C ATOM 2004 CG PRO A 395 52.509 26.626 -29.073 1.00 18.03 C ANISOU 2004 CG PRO A 395 2326 2586 1937 -299 -413 -45 C ATOM 2005 CD PRO A 395 53.658 27.058 -28.202 1.00 17.71 C ANISOU 2005 CD PRO A 395 2311 2499 1921 -282 -352 -22 C ATOM 2006 N GLY A 396 52.712 30.041 -29.820 1.00 13.09 N ANISOU 2006 N GLY A 396 1720 1972 1281 -209 -455 110 N ATOM 2007 CA GLY A 396 52.041 31.309 -30.041 1.00 18.24 C ANISOU 2007 CA GLY A 396 2355 2627 1947 -171 -505 166 C ATOM 2008 C GLY A 396 53.010 32.379 -30.515 1.00 17.21 C ANISOU 2008 C GLY A 396 2276 2479 1782 -158 -499 232 C ATOM 2009 O GLY A 396 52.597 33.454 -30.959 1.00 18.65 O ANISOU 2009 O GLY A 396 2462 2661 1963 -129 -548 289 O ATOM 2010 N LYS A 397 54.303 32.080 -30.406 1.00 17.32 N ANISOU 2010 N LYS A 397 2329 2479 1772 -181 -440 227 N ATOM 2011 CA ALYS A 397 55.352 32.996 -30.862 0.59 18.10 C ANISOU 2011 CA ALYS A 397 2474 2569 1835 -182 -426 290 C ATOM 2012 CA BLYS A 397 55.351 32.975 -30.866 0.41 18.19 C ANISOU 2012 CA BLYS A 397 2485 2581 1845 -183 -425 289 C ATOM 2013 C LYS A 397 56.007 32.474 -32.145 1.00 18.32 C ANISOU 2013 C LYS A 397 2538 2663 1760 -213 -418 289 C ATOM 2014 O LYS A 397 57.006 33.024 -32.617 1.00 18.78 O ANISOU 2014 O LYS A 397 2632 2730 1773 -227 -395 337 O ATOM 2015 CB ALYS A 397 56.414 33.192 -29.784 0.59 18.74 C ANISOU 2015 CB ALYS A 397 2565 2594 1963 -185 -363 289 C ATOM 2016 CB BLYS A 397 56.397 33.164 -29.762 0.41 18.78 C ANISOU 2016 CB BLYS A 397 2568 2598 1969 -185 -363 287 C ATOM 2017 CG ALYS A 397 55.911 33.845 -28.497 0.59 20.34 C ANISOU 2017 CG ALYS A 397 2738 2734 2258 -152 -366 289 C ATOM 2018 CG BLYS A 397 55.853 33.826 -28.516 0.41 20.27 C ANISOU 2018 CG BLYS A 397 2727 2727 2248 -152 -368 288 C ATOM 2019 CD ALYS A 397 57.072 34.348 -27.663 0.59 19.81 C ANISOU 2019 CD ALYS A 397 2690 2613 2222 -156 -318 305 C ATOM 2020 CD BLYS A 397 56.931 34.095 -27.487 0.41 19.90 C ANISOU 2020 CD BLYS A 397 2693 2627 2241 -155 -314 288 C ATOM 2021 CE ALYS A 397 58.039 33.221 -27.378 0.59 20.40 C ANISOU 2021 CE ALYS A 397 2772 2701 2278 -186 -258 258 C ATOM 2022 CE BLYS A 397 56.427 34.990 -26.378 0.41 19.51 C ANISOU 2022 CE BLYS A 397 2621 2521 2271 -118 -326 294 C ATOM 2023 NZ ALYS A 397 59.410 33.727 -27.113 0.59 19.20 N ANISOU 2023 NZ ALYS A 397 2646 2522 2126 -199 -217 286 N ATOM 2024 NZ BLYS A 397 55.257 34.395 -25.678 0.41 19.59 N ANISOU 2024 NZ BLYS A 397 2578 2543 2320 -101 -333 242 N ATOM 2025 N GLY A 398 55.440 31.415 -32.705 1.00 16.65 N ANISOU 2025 N GLY A 398 2316 2500 1511 -226 -438 232 N ATOM 2026 CA GLY A 398 55.964 30.845 -33.930 1.00 22.20 C ANISOU 2026 CA GLY A 398 3052 3273 2111 -250 -434 216 C ATOM 2027 C GLY A 398 56.789 29.596 -33.675 1.00 26.62 C ANISOU 2027 C GLY A 398 3618 3833 2663 -268 -376 138 C ATOM 2028 O GLY A 398 57.275 29.380 -32.562 1.00 26.06 O ANISOU 2028 O GLY A 398 3537 3705 2660 -264 -330 119 O ATOM 2029 N TRP A 399 56.940 28.773 -34.710 1.00 28.35 N ANISOU 2029 N TRP A 399 3857 4117 2800 -283 -381 91 N ATOM 2030 CA TRP A 399 57.723 27.547 -34.627 1.00 31.41 C ANISOU 2030 CA TRP A 399 4255 4505 3175 -292 -334 9 C ATOM 2031 C TRP A 399 58.039 27.026 -36.023 1.00 33.27 C ANISOU 2031 C TRP A 399 4519 4828 3295 -303 -340 -28 C ATOM 2032 O TRP A 399 57.404 27.420 -37.001 1.00 30.68 O ANISOU 2032 O TRP A 399 4199 4559 2900 -307 -392 0 O ATOM 2033 CB TRP A 399 56.978 26.483 -33.820 1.00 32.42 C ANISOU 2033 CB TRP A 399 4358 4583 3379 -297 -347 -59 C ATOM 2034 CG TRP A 399 55.580 26.244 -34.295 1.00 34.07 C ANISOU 2034 CG TRP A 399 4546 4817 3582 -307 -419 -76 C ATOM 2035 CD1 TRP A 399 54.449 26.868 -33.854 1.00 35.77 C ANISOU 2035 CD1 TRP A 399 4723 5015 3852 -300 -462 -37 C ATOM 2036 CD2 TRP A 399 55.160 25.320 -35.306 1.00 37.70 C ANISOU 2036 CD2 TRP A 399 5017 5327 3979 -324 -458 -142 C ATOM 2037 NE1 TRP A 399 53.351 26.390 -34.526 1.00 37.90 N ANISOU 2037 NE1 TRP A 399 4976 5326 4099 -314 -526 -69 N ATOM 2038 CE2 TRP A 399 53.759 25.438 -35.422 1.00 40.06 C ANISOU 2038 CE2 TRP A 399 5282 5639 4300 -331 -527 -134 C ATOM 2039 CE3 TRP A 399 55.830 24.404 -36.123 1.00 39.35 C ANISOU 2039 CE3 TRP A 399 5260 5575 4115 -331 -443 -212 C ATOM 2040 CZ2 TRP A 399 53.018 24.675 -36.320 1.00 43.11 C ANISOU 2040 CZ2 TRP A 399 5669 6073 4639 -352 -585 -191 C ATOM 2041 CZ3 TRP A 399 55.092 23.649 -37.014 1.00 43.42 C ANISOU 2041 CZ3 TRP A 399 5782 6135 4583 -348 -500 -274 C ATOM 2042 CH2 TRP A 399 53.701 23.788 -37.106 1.00 44.91 C ANISOU 2042 CH2 TRP A 399 5936 6332 4794 -361 -572 -261 C ATOM 2043 N GLU A 400 59.021 26.135 -36.107 1.00 41.07 N ANISOU 2043 N GLU A 400 5521 5826 4259 -302 -290 -95 N ATOM 2044 CA GLU A 400 59.420 25.539 -37.378 1.00 50.10 C ANISOU 2044 CA GLU A 400 6689 7057 5290 -305 -287 -149 C ATOM 2045 C GLU A 400 58.785 24.165 -37.573 1.00 52.90 C ANISOU 2045 C GLU A 400 7047 7402 5651 -308 -323 -256 C ATOM 2046 O GLU A 400 58.611 23.706 -38.702 1.00 56.53 O ANISOU 2046 O GLU A 400 7526 7934 6019 -313 -350 -305 O ATOM 2047 CB GLU A 400 60.944 25.425 -37.459 1.00 56.15 C ANISOU 2047 CB GLU A 400 7465 7850 6018 -297 -210 -164 C ATOM 2048 CG GLU A 400 61.664 26.736 -37.734 1.00 60.08 C ANISOU 2048 CG GLU A 400 7966 8390 6471 -307 -179 -61 C ATOM 2049 CD GLU A 400 61.771 27.038 -39.214 1.00 64.24 C ANISOU 2049 CD GLU A 400 8515 9034 6858 -321 -189 -40 C ATOM 2050 OE1 GLU A 400 60.833 26.693 -39.964 1.00 66.40 O ANISOU 2050 OE1 GLU A 400 8800 9346 7081 -324 -248 -70 O ATOM 2051 OE2 GLU A 400 62.801 27.612 -39.630 1.00 64.67 O ANISOU 2051 OE2 GLU A 400 8574 9147 6850 -333 -139 7 O ATOM 2052 N LEU A 411 69.798 18.157 -40.315 1.00 71.43 N ANISOU 2052 N LEU A 411 9371 10032 7739 5 184 -899 N ATOM 2053 CA LEU A 411 70.620 18.823 -39.310 1.00 69.79 C ANISOU 2053 CA LEU A 411 9122 9816 7578 1 233 -838 C ATOM 2054 C LEU A 411 70.191 20.273 -39.110 1.00 67.29 C ANISOU 2054 C LEU A 411 8801 9533 7234 -61 233 -706 C ATOM 2055 O LEU A 411 70.455 20.867 -38.064 1.00 67.27 O ANISOU 2055 O LEU A 411 8778 9498 7285 -79 251 -649 O ATOM 2056 CB LEU A 411 72.098 18.765 -39.703 1.00 71.48 C ANISOU 2056 CB LEU A 411 9291 10103 7766 37 306 -858 C ATOM 2057 N ALA A 412 69.526 20.834 -40.117 1.00 63.97 N ANISOU 2057 N ALA A 412 8401 9174 6732 -93 208 -659 N ATOM 2058 CA ALA A 412 69.104 22.233 -40.084 1.00 58.73 C ANISOU 2058 CA ALA A 412 7736 8537 6040 -149 200 -527 C ATOM 2059 C ALA A 412 68.198 22.534 -38.891 1.00 52.86 C ANISOU 2059 C ALA A 412 7005 7708 5373 -177 156 -488 C ATOM 2060 O ALA A 412 68.339 23.571 -38.242 1.00 48.56 O ANISOU 2060 O ALA A 412 6446 7133 4873 -204 167 -384 O ATOM 2061 CB ALA A 412 68.402 22.600 -41.383 1.00 57.04 C ANISOU 2061 CB ALA A 412 7549 8390 5734 -169 166 -496 C ATOM 2062 N SER A 413 67.270 21.625 -38.610 1.00 50.35 N ANISOU 2062 N SER A 413 6711 7311 5110 -164 98 -557 N ATOM 2063 CA SER A 413 66.335 21.796 -37.503 1.00 46.62 C ANISOU 2063 CA SER A 413 6244 6718 4753 -181 51 -508 C ATOM 2064 C SER A 413 67.043 21.696 -36.154 1.00 44.30 C ANISOU 2064 C SER A 413 5927 6335 4571 -164 84 -497 C ATOM 2065 O SER A 413 66.798 22.497 -35.251 1.00 41.25 O ANISOU 2065 O SER A 413 5530 5890 4253 -185 78 -411 O ATOM 2066 CB SER A 413 65.215 20.758 -37.587 1.00 45.37 C ANISOU 2066 CB SER A 413 6112 6505 4623 -179 -16 -587 C ATOM 2067 OG SER A 413 64.297 20.906 -36.517 1.00 44.79 O ANISOU 2067 OG SER A 413 6034 6327 4656 -199 -57 -540 O ATOM 2068 N VAL A 414 67.922 20.707 -36.028 1.00 43.70 N ANISOU 2068 N VAL A 414 5843 6250 4511 -123 115 -587 N ATOM 2069 CA VAL A 414 68.657 20.487 -34.789 1.00 42.04 C ANISOU 2069 CA VAL A 414 5612 5960 4402 -101 141 -584 C ATOM 2070 C VAL A 414 69.623 21.633 -34.494 1.00 42.38 C ANISOU 2070 C VAL A 414 5619 6045 4437 -114 196 -497 C ATOM 2071 O VAL A 414 69.704 22.104 -33.360 1.00 40.36 O ANISOU 2071 O VAL A 414 5351 5718 4266 -125 196 -437 O ATOM 2072 CB VAL A 414 69.439 19.160 -34.829 1.00 40.68 C ANISOU 2072 CB VAL A 414 5439 5773 4246 -45 157 -703 C ATOM 2073 CG1 VAL A 414 70.424 19.087 -33.671 1.00 37.32 C ANISOU 2073 CG1 VAL A 414 4984 5289 3907 -19 190 -689 C ATOM 2074 CG2 VAL A 414 68.480 17.980 -34.793 1.00 41.01 C ANISOU 2074 CG2 VAL A 414 5520 5734 4330 -37 94 -783 C ATOM 2075 N ILE A 415 70.346 22.083 -35.516 1.00 42.97 N ANISOU 2075 N ILE A 415 5677 6241 4410 -119 240 -489 N ATOM 2076 CA ILE A 415 71.316 23.163 -35.342 1.00 43.09 C ANISOU 2076 CA ILE A 415 5656 6305 4413 -141 293 -405 C ATOM 2077 C ILE A 415 70.630 24.491 -35.020 1.00 42.41 C ANISOU 2077 C ILE A 415 5581 6187 4347 -194 266 -281 C ATOM 2078 O ILE A 415 71.174 25.316 -34.285 1.00 42.73 O ANISOU 2078 O ILE A 415 5599 6200 4435 -213 287 -210 O ATOM 2079 CB ILE A 415 72.203 23.342 -36.592 1.00 43.01 C ANISOU 2079 CB ILE A 415 5622 6443 4276 -143 350 -421 C ATOM 2080 CG1 ILE A 415 73.277 24.401 -36.333 1.00 42.03 C ANISOU 2080 CG1 ILE A 415 5454 6365 4151 -174 405 -333 C ATOM 2081 CG2 ILE A 415 71.362 23.715 -37.800 1.00 44.03 C ANISOU 2081 CG2 ILE A 415 5785 6643 4302 -173 321 -394 C ATOM 2082 CD1 ILE A 415 74.370 24.435 -37.378 1.00 43.26 C ANISOU 2082 CD1 ILE A 415 5572 6631 4233 -166 461 -344 C ATOM 2083 N LEU A 416 69.435 24.693 -35.570 1.00 39.28 N ANISOU 2083 N LEU A 416 5218 5792 3914 -214 214 -260 N ATOM 2084 CA LEU A 416 68.655 25.890 -35.273 1.00 37.69 C ANISOU 2084 CA LEU A 416 5029 5551 3739 -252 178 -152 C ATOM 2085 C LEU A 416 68.247 25.915 -33.803 1.00 35.01 C ANISOU 2085 C LEU A 416 4686 5088 3528 -245 154 -137 C ATOM 2086 O LEU A 416 68.280 26.958 -33.156 1.00 32.38 O ANISOU 2086 O LEU A 416 4346 4715 3240 -267 153 -54 O ATOM 2087 CB LEU A 416 67.418 25.965 -36.165 1.00 38.24 C ANISOU 2087 CB LEU A 416 5130 5650 3748 -266 121 -144 C ATOM 2088 CG LEU A 416 66.461 27.130 -35.907 1.00 36.65 C ANISOU 2088 CG LEU A 416 4942 5404 3578 -294 72 -41 C ATOM 2089 CD1 LEU A 416 67.228 28.435 -35.738 1.00 34.46 C ANISOU 2089 CD1 LEU A 416 4653 5138 3302 -323 103 63 C ATOM 2090 CD2 LEU A 416 65.455 27.243 -37.041 1.00 35.51 C ANISOU 2090 CD2 LEU A 416 4824 5319 3350 -306 19 -30 C ATOM 2091 N SER A 417 67.865 24.753 -33.282 1.00 35.51 N ANISOU 2091 N SER A 417 4756 5090 3646 -217 134 -217 N ATOM 2092 CA SER A 417 67.513 24.623 -31.873 1.00 35.02 C ANISOU 2092 CA SER A 417 4690 4920 3696 -212 116 -208 C ATOM 2093 C SER A 417 68.718 24.923 -30.998 1.00 30.56 C ANISOU 2093 C SER A 417 4099 4335 3180 -204 162 -187 C ATOM 2094 O SER A 417 68.582 25.455 -29.898 1.00 29.18 O ANISOU 2094 O SER A 417 3917 4093 3078 -212 154 -140 O ATOM 2095 CB SER A 417 66.980 23.221 -31.572 1.00 38.52 C ANISOU 2095 CB SER A 417 5148 5307 4182 -189 87 -297 C ATOM 2096 OG SER A 417 65.590 23.254 -31.300 1.00 39.88 O ANISOU 2096 OG SER A 417 5332 5431 4388 -209 33 -279 O ATOM 2097 N LEU A 418 69.900 24.578 -31.499 1.00 29.80 N ANISOU 2097 N LEU A 418 3982 4302 3038 -186 209 -226 N ATOM 2098 CA LEU A 418 71.143 24.818 -30.778 1.00 29.41 C ANISOU 2098 CA LEU A 418 3898 4249 3028 -178 253 -211 C ATOM 2099 C LEU A 418 71.493 26.304 -30.719 1.00 23.67 C ANISOU 2099 C LEU A 418 3157 3546 2292 -221 269 -109 C ATOM 2100 O LEU A 418 71.880 26.811 -29.669 1.00 18.66 O ANISOU 2100 O LEU A 418 2506 2857 1725 -229 273 -70 O ATOM 2101 CB LEU A 418 72.291 24.036 -31.420 1.00 35.54 C ANISOU 2101 CB LEU A 418 4648 5099 3756 -144 299 -286 C ATOM 2102 CG LEU A 418 72.187 22.514 -31.319 1.00 41.32 C ANISOU 2102 CG LEU A 418 5393 5789 4516 -93 282 -395 C ATOM 2103 CD1 LEU A 418 73.383 21.843 -31.980 1.00 43.09 C ANISOU 2103 CD1 LEU A 418 5586 6093 4692 -50 331 -473 C ATOM 2104 CD2 LEU A 418 72.064 22.087 -29.864 1.00 42.55 C ANISOU 2104 CD2 LEU A 418 5554 5830 4784 -79 257 -395 C ATOM 2105 N GLU A 419 71.359 27.000 -31.845 1.00 20.81 N ANISOU 2105 N GLU A 419 2803 3261 1844 -251 274 -63 N ATOM 2106 CA GLU A 419 71.665 28.429 -31.892 1.00 23.27 C ANISOU 2106 CA GLU A 419 3108 3590 2146 -298 283 41 C ATOM 2107 C GLU A 419 70.673 29.243 -31.064 1.00 16.03 C ANISOU 2107 C GLU A 419 2214 2576 1301 -313 232 102 C ATOM 2108 O GLU A 419 71.053 30.207 -30.401 1.00 18.33 O ANISOU 2108 O GLU A 419 2496 2829 1639 -337 234 165 O ATOM 2109 CB GLU A 419 71.681 28.932 -33.338 1.00 30.71 C ANISOU 2109 CB GLU A 419 4058 4637 2972 -329 295 81 C ATOM 2110 CG GLU A 419 73.069 28.966 -33.963 1.00 40.50 C ANISOU 2110 CG GLU A 419 5257 5985 4144 -343 363 79 C ATOM 2111 CD GLU A 419 73.992 29.963 -33.281 1.00 48.15 C ANISOU 2111 CD GLU A 419 6195 6935 5163 -381 389 154 C ATOM 2112 OE1 GLU A 419 74.998 29.533 -32.679 1.00 49.42 O ANISOU 2112 OE1 GLU A 419 6313 7100 5365 -362 427 112 O ATOM 2113 OE2 GLU A 419 73.714 31.179 -33.351 1.00 52.39 O ANISOU 2113 OE2 GLU A 419 6751 7452 5702 -429 367 255 O ATOM 2114 N VAL A 420 69.403 28.853 -31.108 1.00 17.04 N ANISOU 2114 N VAL A 420 2370 2668 1438 -298 184 79 N ATOM 2115 CA VAL A 420 68.374 29.514 -30.311 1.00 15.30 C ANISOU 2115 CA VAL A 420 2163 2363 1285 -302 136 123 C ATOM 2116 C VAL A 420 68.674 29.371 -28.825 1.00 16.30 C ANISOU 2116 C VAL A 420 2275 2410 1508 -288 144 107 C ATOM 2117 O VAL A 420 68.554 30.335 -28.064 1.00 13.61 O ANISOU 2117 O VAL A 420 1934 2016 1220 -299 130 160 O ATOM 2118 CB VAL A 420 66.971 28.949 -30.604 1.00 16.72 C ANISOU 2118 CB VAL A 420 2363 2529 1460 -288 87 90 C ATOM 2119 CG1 VAL A 420 65.945 29.560 -29.660 1.00 15.52 C ANISOU 2119 CG1 VAL A 420 2215 2297 1385 -285 44 125 C ATOM 2120 CG2 VAL A 420 66.588 29.205 -32.057 1.00 21.92 C ANISOU 2120 CG2 VAL A 420 3040 3268 2020 -303 69 113 C ATOM 2121 N LYS A 421 69.069 28.167 -28.416 1.00 15.29 N ANISOU 2121 N LYS A 421 2137 2273 1402 -260 163 33 N ATOM 2122 CA LYS A 421 69.432 27.922 -27.023 1.00 15.27 C ANISOU 2122 CA LYS A 421 2120 2201 1480 -246 169 18 C ATOM 2123 C LYS A 421 70.552 28.858 -26.586 1.00 17.37 C ANISOU 2123 C LYS A 421 2364 2472 1764 -264 197 66 C ATOM 2124 O LYS A 421 70.463 29.497 -25.541 1.00 17.42 O ANISOU 2124 O LYS A 421 2369 2419 1831 -270 184 97 O ATOM 2125 CB LYS A 421 69.862 26.469 -26.810 1.00 15.47 C ANISOU 2125 CB LYS A 421 2140 2220 1518 -212 183 -64 C ATOM 2126 CG LYS A 421 70.276 26.163 -25.370 1.00 18.89 C ANISOU 2126 CG LYS A 421 2561 2586 2030 -197 185 -74 C ATOM 2127 CD LYS A 421 70.726 24.716 -25.190 1.00 18.64 C ANISOU 2127 CD LYS A 421 2528 2540 2015 -161 191 -150 C ATOM 2128 CE LYS A 421 69.576 23.740 -25.397 1.00 19.41 C ANISOU 2128 CE LYS A 421 2655 2604 2116 -155 155 -193 C ATOM 2129 NZ LYS A 421 69.994 22.320 -25.215 1.00 18.92 N ANISOU 2129 NZ LYS A 421 2599 2511 2079 -120 153 -266 N ATOM 2130 N LEU A 422 71.598 28.945 -27.401 1.00 18.43 N ANISOU 2130 N LEU A 422 2477 2681 1844 -275 237 70 N ATOM 2131 CA LEU A 422 72.733 29.814 -27.104 1.00 16.18 C ANISOU 2131 CA LEU A 422 2164 2411 1572 -302 265 117 C ATOM 2132 C LEU A 422 72.318 31.275 -26.992 1.00 11.91 C ANISOU 2132 C LEU A 422 1641 1836 1047 -342 239 204 C ATOM 2133 O LEU A 422 72.798 31.992 -26.119 1.00 13.63 O ANISOU 2133 O LEU A 422 1848 2010 1320 -358 237 235 O ATOM 2134 CB LEU A 422 73.822 29.671 -28.171 1.00 23.92 C ANISOU 2134 CB LEU A 422 3114 3496 2478 -313 315 109 C ATOM 2135 CG LEU A 422 74.881 28.595 -27.923 1.00 27.66 C ANISOU 2135 CG LEU A 422 3548 4000 2961 -275 352 34 C ATOM 2136 CD1 LEU A 422 76.061 28.786 -28.863 1.00 28.01 C ANISOU 2136 CD1 LEU A 422 3548 4157 2936 -293 408 41 C ATOM 2137 CD2 LEU A 422 75.335 28.614 -26.473 1.00 26.68 C ANISOU 2137 CD2 LEU A 422 3407 3803 2928 -264 344 32 C ATOM 2138 N HIS A 423 71.435 31.715 -27.882 1.00 13.15 N ANISOU 2138 N HIS A 423 1827 2011 1159 -355 213 240 N ATOM 2139 CA HIS A 423 70.962 33.094 -27.849 1.00 14.52 C ANISOU 2139 CA HIS A 423 2022 2143 1351 -386 179 323 C ATOM 2140 C HIS A 423 70.079 33.364 -26.630 1.00 15.28 C ANISOU 2140 C HIS A 423 2133 2142 1532 -364 138 316 C ATOM 2141 O HIS A 423 70.106 34.462 -26.072 1.00 15.10 O ANISOU 2141 O HIS A 423 2117 2064 1556 -381 118 366 O ATOM 2142 CB HIS A 423 70.206 33.436 -29.135 1.00 12.58 C ANISOU 2142 CB HIS A 423 1804 1943 1033 -400 155 364 C ATOM 2143 CG HIS A 423 71.097 33.870 -30.257 1.00 12.97 C ANISOU 2143 CG HIS A 423 1846 2082 1001 -443 189 415 C ATOM 2144 ND1 HIS A 423 71.822 32.979 -31.021 1.00 18.00 N ANISOU 2144 ND1 HIS A 423 2459 2815 1565 -439 238 366 N ATOM 2145 CD2 HIS A 423 71.389 35.101 -30.737 1.00 13.57 C ANISOU 2145 CD2 HIS A 423 1933 2166 1056 -494 182 511 C ATOM 2146 CE1 HIS A 423 72.516 33.643 -31.928 1.00 16.65 C ANISOU 2146 CE1 HIS A 423 2281 2721 1325 -486 265 431 C ATOM 2147 NE2 HIS A 423 72.271 34.933 -31.777 1.00 18.19 N ANISOU 2147 NE2 HIS A 423 2499 2862 1551 -525 231 524 N ATOM 2148 N LEU A 424 69.300 32.367 -26.219 1.00 10.40 N ANISOU 2148 N LEU A 424 1517 1504 932 -327 126 254 N ATOM 2149 CA LEU A 424 68.439 32.518 -25.050 1.00 15.87 C ANISOU 2149 CA LEU A 424 2215 2119 1695 -306 94 243 C ATOM 2150 C LEU A 424 69.256 32.558 -23.764 1.00 14.16 C ANISOU 2150 C LEU A 424 1982 1862 1538 -304 112 229 C ATOM 2151 O LEU A 424 68.953 33.328 -22.852 1.00 9.41 O ANISOU 2151 O LEU A 424 1385 1202 988 -302 91 246 O ATOM 2152 CB LEU A 424 67.406 31.391 -24.984 1.00 15.28 C ANISOU 2152 CB LEU A 424 2144 2041 1620 -279 79 187 C ATOM 2153 CG LEU A 424 66.242 31.498 -25.972 1.00 18.13 C ANISOU 2153 CG LEU A 424 2520 2426 1941 -278 43 200 C ATOM 2154 CD1 LEU A 424 65.323 30.290 -25.857 1.00 18.23 C ANISOU 2154 CD1 LEU A 424 2531 2436 1959 -259 28 140 C ATOM 2155 CD2 LEU A 424 65.467 32.789 -25.746 1.00 17.77 C ANISOU 2155 CD2 LEU A 424 2485 2339 1929 -278 3 256 C ATOM 2156 N LEU A 425 70.288 31.721 -23.694 1.00 12.46 N ANISOU 2156 N LEU A 425 1745 1678 1311 -299 149 192 N ATOM 2157 CA LEU A 425 71.216 31.743 -22.569 1.00 14.49 C ANISOU 2157 CA LEU A 425 1982 1908 1617 -298 164 180 C ATOM 2158 C LEU A 425 71.905 33.101 -22.468 1.00 14.35 C ANISOU 2158 C LEU A 425 1959 1879 1616 -335 163 239 C ATOM 2159 O LEU A 425 72.080 33.641 -21.374 1.00 12.04 O ANISOU 2159 O LEU A 425 1665 1535 1377 -337 149 244 O ATOM 2160 CB LEU A 425 72.258 30.628 -22.705 1.00 14.10 C ANISOU 2160 CB LEU A 425 1906 1902 1550 -282 199 133 C ATOM 2161 CG LEU A 425 71.885 29.237 -22.181 1.00 21.36 C ANISOU 2161 CG LEU A 425 2830 2798 2487 -244 194 70 C ATOM 2162 CD1 LEU A 425 70.508 28.809 -22.664 1.00 27.11 C ANISOU 2162 CD1 LEU A 425 3586 3518 3197 -236 169 56 C ATOM 2163 CD2 LEU A 425 72.940 28.216 -22.590 1.00 18.70 C ANISOU 2163 CD2 LEU A 425 2469 2507 2128 -223 226 22 C ATOM 2164 N HIS A 426 72.289 33.650 -23.616 1.00 13.81 N ANISOU 2164 N HIS A 426 1889 1859 1498 -367 175 284 N ATOM 2165 CA HIS A 426 72.933 34.956 -23.663 1.00 13.05 C ANISOU 2165 CA HIS A 426 1791 1751 1416 -414 172 350 C ATOM 2166 C HIS A 426 71.990 36.061 -23.193 1.00 12.96 C ANISOU 2166 C HIS A 426 1815 1659 1451 -415 121 387 C ATOM 2167 O HIS A 426 72.413 37.019 -22.550 1.00 17.22 O ANISOU 2167 O HIS A 426 2355 2148 2038 -439 106 416 O ATOM 2168 CB HIS A 426 73.429 35.258 -25.079 1.00 13.04 C ANISOU 2168 CB HIS A 426 1785 1828 1343 -453 196 399 C ATOM 2169 CG HIS A 426 74.085 36.596 -25.216 1.00 14.80 C ANISOU 2169 CG HIS A 426 2007 2037 1578 -513 190 478 C ATOM 2170 ND1 HIS A 426 73.428 37.701 -25.714 1.00 18.77 N ANISOU 2170 ND1 HIS A 426 2550 2503 2080 -539 151 551 N ATOM 2171 CD2 HIS A 426 75.339 37.009 -24.916 1.00 18.15 C ANISOU 2171 CD2 HIS A 426 2397 2476 2022 -554 214 499 C ATOM 2172 CE1 HIS A 426 74.248 38.735 -25.716 1.00 19.87 C ANISOU 2172 CE1 HIS A 426 2684 2629 2238 -597 150 615 C ATOM 2173 NE2 HIS A 426 75.415 38.343 -25.236 1.00 19.93 N ANISOU 2173 NE2 HIS A 426 2644 2671 2259 -610 190 584 N ATOM 2174 N SER A 427 70.710 35.921 -23.520 1.00 13.52 N ANISOU 2174 N SER A 427 1910 1716 1510 -388 93 382 N ATOM 2175 CA SER A 427 69.712 36.919 -23.144 1.00 12.04 C ANISOU 2175 CA SER A 427 1750 1457 1366 -377 43 410 C ATOM 2176 C SER A 427 69.442 36.946 -21.642 1.00 11.09 C ANISOU 2176 C SER A 427 1626 1275 1314 -348 31 365 C ATOM 2177 O SER A 427 69.192 38.006 -21.069 1.00 13.34 O ANISOU 2177 O SER A 427 1927 1496 1647 -347 -2 384 O ATOM 2178 CB SER A 427 68.403 36.666 -23.892 1.00 13.96 C ANISOU 2178 CB SER A 427 2011 1716 1578 -352 16 410 C ATOM 2179 OG SER A 427 68.566 36.878 -25.282 1.00 21.95 O ANISOU 2179 OG SER A 427 3034 2783 2523 -381 18 461 O ATOM 2180 N TYR A 428 69.496 35.781 -21.007 1.00 9.14 N ANISOU 2180 N TYR A 428 1360 1046 1067 -324 54 305 N ATOM 2181 CA TYR A 428 69.068 35.656 -19.616 1.00 15.13 C ANISOU 2181 CA TYR A 428 2116 1759 1875 -295 44 263 C ATOM 2182 C TYR A 428 70.185 35.337 -18.625 1.00 16.89 C ANISOU 2182 C TYR A 428 2320 1978 2120 -302 65 237 C ATOM 2183 O TYR A 428 70.005 35.505 -17.418 1.00 17.72 O ANISOU 2183 O TYR A 428 2425 2045 2263 -286 53 212 O ATOM 2184 CB TYR A 428 67.984 34.580 -19.503 1.00 11.75 C ANISOU 2184 CB TYR A 428 1685 1346 1435 -263 43 221 C ATOM 2185 CG TYR A 428 66.632 35.016 -20.016 1.00 13.79 C ANISOU 2185 CG TYR A 428 1954 1594 1690 -247 10 236 C ATOM 2186 CD1 TYR A 428 66.283 34.842 -21.349 1.00 14.98 C ANISOU 2186 CD1 TYR A 428 2113 1785 1793 -255 3 259 C ATOM 2187 CD2 TYR A 428 65.702 35.600 -19.165 1.00 13.51 C ANISOU 2187 CD2 TYR A 428 1919 1517 1697 -220 -17 224 C ATOM 2188 CE1 TYR A 428 65.049 35.239 -21.819 1.00 16.30 C ANISOU 2188 CE1 TYR A 428 2287 1947 1959 -238 -34 274 C ATOM 2189 CE2 TYR A 428 64.466 35.999 -19.626 1.00 16.12 C ANISOU 2189 CE2 TYR A 428 2253 1843 2029 -199 -50 235 C ATOM 2190 CZ TYR A 428 64.145 35.817 -20.955 1.00 16.80 C ANISOU 2190 CZ TYR A 428 2346 1965 2071 -208 -61 262 C ATOM 2191 OH TYR A 428 62.913 36.214 -21.416 1.00 17.93 O ANISOU 2191 OH TYR A 428 2489 2107 2218 -185 -100 274 O ATOM 2192 N MET A 429 71.328 34.870 -19.116 1.00 9.42 N ANISOU 2192 N MET A 429 1354 1078 1148 -322 96 241 N ATOM 2193 CA MET A 429 72.395 34.454 -18.216 1.00 9.65 C ANISOU 2193 CA MET A 429 1358 1110 1198 -323 113 214 C ATOM 2194 C MET A 429 73.719 35.129 -18.537 1.00 13.40 C ANISOU 2194 C MET A 429 1811 1607 1675 -365 127 247 C ATOM 2195 O MET A 429 73.914 35.658 -19.633 1.00 13.25 O ANISOU 2195 O MET A 429 1793 1614 1626 -396 134 292 O ATOM 2196 CB MET A 429 72.567 32.933 -18.253 1.00 11.23 C ANISOU 2196 CB MET A 429 1544 1348 1376 -296 137 169 C ATOM 2197 CG MET A 429 71.296 32.157 -17.934 1.00 13.70 C ANISOU 2197 CG MET A 429 1874 1641 1688 -265 124 139 C ATOM 2198 SD MET A 429 71.587 30.397 -17.659 1.00 14.96 S ANISOU 2198 SD MET A 429 2025 1819 1842 -236 141 88 S ATOM 2199 CE MET A 429 72.429 30.433 -16.077 1.00 16.59 C ANISOU 2199 CE MET A 429 2217 1997 2089 -231 135 77 C ATOM 2200 N ASN A 430 74.620 35.118 -17.561 1.00 14.89 N ANISOU 2200 N ASN A 430 1977 1786 1894 -369 128 229 N ATOM 2201 CA ASN A 430 75.979 35.601 -17.763 1.00 16.35 C ANISOU 2201 CA ASN A 430 2128 2000 2084 -411 143 254 C ATOM 2202 C ASN A 430 76.921 34.427 -17.960 1.00 14.68 C ANISOU 2202 C ASN A 430 1874 1855 1850 -395 179 222 C ATOM 2203 O ASN A 430 77.593 33.993 -17.026 1.00 11.38 O ANISOU 2203 O ASN A 430 1431 1435 1457 -380 177 191 O ATOM 2204 CB ASN A 430 76.436 36.458 -16.583 1.00 15.93 C ANISOU 2204 CB ASN A 430 2073 1895 2084 -430 114 254 C ATOM 2205 CG ASN A 430 75.703 37.776 -16.508 1.00 17.23 C ANISOU 2205 CG ASN A 430 2278 1991 2277 -449 76 285 C ATOM 2206 OD1 ASN A 430 75.276 38.317 -17.526 1.00 16.47 O ANISOU 2206 OD1 ASN A 430 2201 1894 2163 -468 73 331 O ATOM 2207 ND2 ASN A 430 75.555 38.304 -15.299 1.00 17.82 N ANISOU 2207 ND2 ASN A 430 2367 2010 2395 -440 43 260 N ATOM 2208 N VAL A 431 76.954 33.915 -19.185 1.00 13.57 N ANISOU 2208 N VAL A 431 1724 1774 1659 -393 210 226 N ATOM 2209 CA VAL A 431 77.751 32.742 -19.508 1.00 9.75 C ANISOU 2209 CA VAL A 431 1200 1353 1150 -366 245 185 C ATOM 2210 C VAL A 431 79.217 33.098 -19.693 1.00 11.10 C ANISOU 2210 C VAL A 431 1314 1582 1323 -401 271 201 C ATOM 2211 O VAL A 431 79.552 34.099 -20.318 1.00 13.89 O ANISOU 2211 O VAL A 431 1658 1956 1662 -456 280 255 O ATOM 2212 CB VAL A 431 77.240 32.049 -20.793 1.00 13.23 C ANISOU 2212 CB VAL A 431 1652 1843 1531 -349 268 172 C ATOM 2213 CG1 VAL A 431 78.085 30.822 -21.108 1.00 14.37 C ANISOU 2213 CG1 VAL A 431 1756 2048 1655 -312 301 118 C ATOM 2214 CG2 VAL A 431 75.776 31.672 -20.642 1.00 13.19 C ANISOU 2214 CG2 VAL A 431 1697 1786 1527 -320 239 156 C ATOM 2215 N LYS A 432 80.092 32.267 -19.144 1.00 10.87 N ANISOU 2215 N LYS A 432 1242 1577 1311 -369 281 157 N ATOM 2216 CA LYS A 432 81.523 32.433 -19.348 1.00 17.02 C ANISOU 2216 CA LYS A 432 1952 2425 2090 -394 310 163 C ATOM 2217 C LYS A 432 82.113 31.160 -19.943 1.00 14.30 C ANISOU 2217 C LYS A 432 1566 2154 1715 -343 347 109 C ATOM 2218 O LYS A 432 81.745 30.054 -19.557 1.00 14.21 O ANISOU 2218 O LYS A 432 1572 2113 1713 -282 335 57 O ATOM 2219 CB LYS A 432 82.213 32.807 -18.034 1.00 20.28 C ANISOU 2219 CB LYS A 432 2341 2803 2562 -405 280 161 C ATOM 2220 CG LYS A 432 82.072 34.285 -17.696 1.00 25.65 C ANISOU 2220 CG LYS A 432 3043 3433 3271 -470 252 216 C ATOM 2221 CD LYS A 432 82.368 34.576 -16.237 1.00 33.39 C ANISOU 2221 CD LYS A 432 4022 4359 4306 -469 209 199 C ATOM 2222 CE LYS A 432 82.376 36.079 -15.983 1.00 37.87 C ANISOU 2222 CE LYS A 432 4607 4877 4906 -536 180 246 C ATOM 2223 NZ LYS A 432 81.247 36.772 -16.674 1.00 36.44 N ANISOU 2223 NZ LYS A 432 4486 4653 4708 -553 173 285 N ATOM 2224 N TRP A 433 83.017 31.325 -20.898 1.00 12.05 N ANISOU 2224 N TRP A 433 1224 1962 1392 -369 392 120 N ATOM 2225 CA TRP A 433 83.597 30.187 -21.597 1.00 14.78 C ANISOU 2225 CA TRP A 433 1526 2388 1703 -317 432 61 C ATOM 2226 C TRP A 433 85.038 29.944 -21.165 1.00 13.04 C ANISOU 2226 C TRP A 433 1218 2223 1511 -305 449 36 C ATOM 2227 O TRP A 433 85.877 30.839 -21.225 1.00 14.77 O ANISOU 2227 O TRP A 433 1386 2489 1735 -366 465 79 O ATOM 2228 CB TRP A 433 83.520 30.404 -23.113 1.00 16.39 C ANISOU 2228 CB TRP A 433 1724 2677 1826 -346 479 81 C ATOM 2229 CG TRP A 433 82.110 30.463 -23.622 1.00 17.02 C ANISOU 2229 CG TRP A 433 1883 2711 1873 -347 459 96 C ATOM 2230 CD1 TRP A 433 81.301 31.562 -23.675 1.00 15.81 C ANISOU 2230 CD1 TRP A 433 1781 2508 1720 -400 433 165 C ATOM 2231 CD2 TRP A 433 81.340 29.373 -24.145 1.00 16.78 C ANISOU 2231 CD2 TRP A 433 1888 2678 1808 -290 459 38 C ATOM 2232 NE1 TRP A 433 80.074 31.223 -24.197 1.00 16.63 N ANISOU 2232 NE1 TRP A 433 1944 2586 1790 -378 418 155 N ATOM 2233 CE2 TRP A 433 80.074 29.886 -24.495 1.00 15.94 C ANISOU 2233 CE2 TRP A 433 1848 2528 1681 -315 433 78 C ATOM 2234 CE3 TRP A 433 81.599 28.015 -24.351 1.00 14.55 C ANISOU 2234 CE3 TRP A 433 1588 2423 1516 -219 473 -46 C ATOM 2235 CZ2 TRP A 433 79.071 29.087 -25.041 1.00 16.08 C ANISOU 2235 CZ2 TRP A 433 1910 2533 1664 -278 422 37 C ATOM 2236 CZ3 TRP A 433 80.603 27.225 -24.892 1.00 15.74 C ANISOU 2236 CZ3 TRP A 433 1791 2554 1637 -183 461 -88 C ATOM 2237 CH2 TRP A 433 79.355 27.762 -25.231 1.00 16.67 C ANISOU 2237 CH2 TRP A 433 1969 2633 1730 -216 436 -46 C ATOM 2238 N ILE A 434 85.316 28.724 -20.725 1.00 17.80 N ANISOU 2238 N ILE A 434 1806 2820 2138 -227 440 -33 N ATOM 2239 CA ILE A 434 86.656 28.363 -20.286 1.00 22.29 C ANISOU 2239 CA ILE A 434 2289 3441 2740 -200 448 -64 C ATOM 2240 C ILE A 434 87.153 27.118 -21.012 1.00 23.41 C ANISOU 2240 C ILE A 434 2388 3651 2854 -122 482 -141 C ATOM 2241 O ILE A 434 86.360 26.262 -21.405 1.00 22.68 O ANISOU 2241 O ILE A 434 2349 3526 2741 -73 478 -183 O ATOM 2242 CB ILE A 434 86.708 28.121 -18.764 1.00 21.71 C ANISOU 2242 CB ILE A 434 2230 3283 2736 -172 389 -73 C ATOM 2243 CG1 ILE A 434 85.907 26.873 -18.387 1.00 20.76 C ANISOU 2243 CG1 ILE A 434 2170 3090 2628 -95 358 -121 C ATOM 2244 CG2 ILE A 434 86.191 29.341 -18.007 1.00 22.98 C ANISOU 2244 CG2 ILE A 434 2434 3376 2921 -241 354 -10 C ATOM 2245 CD1 ILE A 434 86.013 26.507 -16.922 1.00 23.83 C ANISOU 2245 CD1 ILE A 434 2572 3408 3076 -65 302 -127 C ATOM 2246 N PRO A 435 88.474 27.024 -21.203 1.00 26.04 N ANISOU 2246 N PRO A 435 2623 4082 3191 -111 516 -164 N ATOM 2247 CA PRO A 435 89.120 25.870 -21.836 1.00 29.43 C ANISOU 2247 CA PRO A 435 2996 4585 3602 -28 549 -248 C ATOM 2248 C PRO A 435 89.059 24.638 -20.943 1.00 33.25 C ANISOU 2248 C PRO A 435 3502 4985 4145 67 497 -309 C ATOM 2249 O PRO A 435 89.115 24.771 -19.721 1.00 34.31 O ANISOU 2249 O PRO A 435 3649 5048 4339 64 446 -284 O ATOM 2250 CB PRO A 435 90.573 26.329 -22.024 1.00 30.23 C ANISOU 2250 CB PRO A 435 2976 4808 3703 -53 591 -242 C ATOM 2251 CG PRO A 435 90.553 27.817 -21.828 1.00 31.05 C ANISOU 2251 CG PRO A 435 3082 4907 3807 -168 589 -146 C ATOM 2252 CD PRO A 435 89.442 28.080 -20.869 1.00 29.52 C ANISOU 2252 CD PRO A 435 2991 4572 3653 -182 524 -112 C ATOM 2253 N LEU A 436 88.936 23.459 -21.542 1.00 39.81 N ANISOU 2253 N LEU A 436 4343 5824 4960 149 507 -387 N ATOM 2254 CA LEU A 436 88.956 22.220 -20.775 1.00 47.07 C ANISOU 2254 CA LEU A 436 5284 6662 5939 241 456 -444 C ATOM 2255 C LEU A 436 90.389 21.830 -20.438 1.00 55.79 C ANISOU 2255 C LEU A 436 6282 7830 7084 300 459 -486 C ATOM 2256 O LEU A 436 91.241 21.742 -21.321 1.00 58.44 O ANISOU 2256 O LEU A 436 6533 8285 7387 322 515 -530 O ATOM 2257 CB LEU A 436 88.265 21.095 -21.546 1.00 46.95 C ANISOU 2257 CB LEU A 436 5322 6617 5898 306 457 -516 C ATOM 2258 CG LEU A 436 86.772 21.296 -21.815 1.00 45.20 C ANISOU 2258 CG LEU A 436 5205 6324 5644 259 444 -483 C ATOM 2259 CD1 LEU A 436 86.205 20.134 -22.620 1.00 45.11 C ANISOU 2259 CD1 LEU A 436 5238 6291 5609 322 442 -564 C ATOM 2260 CD2 LEU A 436 86.016 21.471 -20.509 1.00 44.49 C ANISOU 2260 CD2 LEU A 436 5183 6113 5608 232 381 -427 C ATOM 2261 N SER A 437 90.650 21.601 -19.155 1.00 65.07 N ANISOU 2261 N SER A 437 7460 8934 8329 325 397 -472 N ATOM 2262 CA SER A 437 91.988 21.249 -18.697 1.00 70.19 C ANISOU 2262 CA SER A 437 8008 9635 9025 382 387 -506 C ATOM 2263 C SER A 437 92.114 19.748 -18.456 1.00 74.47 C ANISOU 2263 C SER A 437 8564 10117 9613 504 344 -583 C ATOM 2264 O SER A 437 92.744 19.036 -19.237 1.00 80.02 O ANISOU 2264 O SER A 437 9208 10887 10308 579 376 -662 O ATOM 2265 CB SER A 437 92.336 22.018 -17.420 1.00 71.13 C ANISOU 2265 CB SER A 437 8112 9725 9189 331 340 -440 C TER 2266 SER A 437 ATOM 2267 N MET B 1 44.767 -13.559 -14.371 1.00 44.22 N ANISOU 2267 N MET B 1 5191 3740 7872 -2069 -104 -490 N ATOM 2268 CA MET B 1 45.557 -13.529 -15.594 1.00 43.52 C ANISOU 2268 CA MET B 1 5069 3685 7784 -1997 -135 -625 C ATOM 2269 C MET B 1 46.788 -12.644 -15.430 1.00 43.76 C ANISOU 2269 C MET B 1 5130 3731 7764 -1866 -141 -642 C ATOM 2270 O MET B 1 46.896 -11.880 -14.472 1.00 42.93 O ANISOU 2270 O MET B 1 5067 3637 7610 -1833 -124 -552 O ATOM 2271 CB MET B 1 44.710 -13.036 -16.769 1.00 43.79 C ANISOU 2271 CB MET B 1 5012 3874 7752 -2030 -130 -686 C ATOM 2272 CG MET B 1 44.363 -11.557 -16.699 1.00 42.55 C ANISOU 2272 CG MET B 1 4823 3872 7471 -1992 -105 -643 C ATOM 2273 SD MET B 1 43.220 -11.032 -17.990 1.00 50.24 S ANISOU 2273 SD MET B 1 5694 5022 8374 -2033 -103 -699 S ATOM 2274 CE MET B 1 43.254 -9.253 -17.781 1.00 43.46 C ANISOU 2274 CE MET B 1 4822 4315 7376 -1950 -79 -653 C ATOM 2275 N GLN B 2 47.713 -12.750 -16.376 1.00 42.76 N ANISOU 2275 N GLN B 2 4986 3608 7654 -1793 -164 -757 N ATOM 2276 CA GLN B 2 48.935 -11.957 -16.344 1.00 42.77 C ANISOU 2276 CA GLN B 2 5007 3629 7614 -1671 -171 -783 C ATOM 2277 C GLN B 2 48.973 -10.974 -17.505 1.00 41.20 C ANISOU 2277 C GLN B 2 4747 3586 7321 -1625 -159 -864 C ATOM 2278 O GLN B 2 48.711 -11.343 -18.645 1.00 44.67 O ANISOU 2278 O GLN B 2 5129 4062 7783 -1645 -158 -960 O ATOM 2279 CB GLN B 2 50.167 -12.864 -16.383 1.00 44.24 C ANISOU 2279 CB GLN B 2 5224 3684 7902 -1611 -202 -843 C ATOM 2280 N ILE B 3 49.292 -9.720 -17.208 1.00 40.40 N ANISOU 2280 N ILE B 3 4656 3569 7125 -1559 -147 -828 N ATOM 2281 CA ILE B 3 49.475 -8.712 -18.246 1.00 38.77 C ANISOU 2281 CA ILE B 3 4403 3502 6827 -1502 -134 -901 C ATOM 2282 C ILE B 3 50.864 -8.094 -18.140 1.00 38.67 C ANISOU 2282 C ILE B 3 4410 3480 6804 -1386 -138 -930 C ATOM 2283 O ILE B 3 51.539 -8.236 -17.122 1.00 40.18 O ANISOU 2283 O ILE B 3 4661 3579 7028 -1354 -156 -867 O ATOM 2284 CB ILE B 3 48.414 -7.595 -18.166 1.00 38.02 C ANISOU 2284 CB ILE B 3 4285 3546 6617 -1533 -113 -838 C ATOM 2285 CG1 ILE B 3 48.594 -6.767 -16.891 1.00 34.76 C ANISOU 2285 CG1 ILE B 3 3924 3126 6157 -1503 -107 -729 C ATOM 2286 CG2 ILE B 3 47.008 -8.177 -18.253 1.00 33.89 C ANISOU 2286 CG2 ILE B 3 3722 3038 6118 -1647 -107 -809 C ATOM 2287 CD1 ILE B 3 47.616 -5.617 -16.766 1.00 31.88 C ANISOU 2287 CD1 ILE B 3 3530 2897 5684 -1526 -85 -668 C ATOM 2288 N PHE B 4 51.290 -7.416 -19.200 1.00 36.02 N ANISOU 2288 N PHE B 4 4022 3240 6426 -1325 -119 -1024 N ATOM 2289 CA PHE B 4 52.609 -6.796 -19.226 1.00 36.73 C ANISOU 2289 CA PHE B 4 4116 3334 6507 -1220 -118 -1059 C ATOM 2290 C PHE B 4 52.523 -5.274 -19.255 1.00 33.66 C ANISOU 2290 C PHE B 4 3734 3079 5978 -1180 -101 -1026 C ATOM 2291 O PHE B 4 51.648 -4.702 -19.904 1.00 34.39 O ANISOU 2291 O PHE B 4 3794 3284 5987 -1210 -80 -1042 O ATOM 2292 CB PHE B 4 53.408 -7.291 -20.431 1.00 40.48 C ANISOU 2292 CB PHE B 4 4525 3800 7057 -1174 -102 -1203 C ATOM 2293 CG PHE B 4 53.517 -8.784 -20.510 1.00 45.21 C ANISOU 2293 CG PHE B 4 5114 4270 7796 -1210 -121 -1246 C ATOM 2294 CD1 PHE B 4 54.283 -9.486 -19.594 1.00 47.93 C ANISOU 2294 CD1 PHE B 4 5498 4478 8235 -1186 -155 -1206 C ATOM 2295 CD2 PHE B 4 52.857 -9.487 -21.503 1.00 46.60 C ANISOU 2295 CD2 PHE B 4 5242 4456 8007 -1267 -108 -1329 C ATOM 2296 CE1 PHE B 4 54.385 -10.861 -19.664 1.00 50.24 C ANISOU 2296 CE1 PHE B 4 5785 4648 8657 -1218 -176 -1246 C ATOM 2297 CE2 PHE B 4 52.955 -10.862 -21.580 1.00 50.49 C ANISOU 2297 CE2 PHE B 4 5729 4825 8628 -1302 -130 -1370 C ATOM 2298 CZ PHE B 4 53.721 -11.551 -20.659 1.00 51.50 C ANISOU 2298 CZ PHE B 4 5899 4818 8852 -1277 -163 -1328 C ATOM 2299 N VAL B 5 53.439 -4.627 -18.543 1.00 30.69 N ANISOU 2299 N VAL B 5 3399 2685 5576 -1111 -115 -981 N ATOM 2300 CA VAL B 5 53.523 -3.172 -18.531 1.00 29.19 C ANISOU 2300 CA VAL B 5 3222 2611 5258 -1066 -104 -952 C ATOM 2301 C VAL B 5 54.890 -2.729 -19.041 1.00 27.92 C ANISOU 2301 C VAL B 5 3035 2464 5110 -971 -96 -1029 C ATOM 2302 O VAL B 5 55.922 -3.160 -18.527 1.00 29.75 O ANISOU 2302 O VAL B 5 3280 2599 5424 -924 -119 -1026 O ATOM 2303 CB VAL B 5 53.290 -2.597 -17.123 1.00 29.91 C ANISOU 2303 CB VAL B 5 3396 2684 5286 -1076 -128 -813 C ATOM 2304 CG1 VAL B 5 53.337 -1.076 -17.161 1.00 28.86 C ANISOU 2304 CG1 VAL B 5 3277 2671 5020 -1032 -121 -787 C ATOM 2305 CG2 VAL B 5 51.960 -3.084 -16.565 1.00 30.94 C ANISOU 2305 CG2 VAL B 5 3529 2791 5434 -1172 -122 -743 C ATOM 2306 N LYS B 6 54.891 -1.863 -20.047 1.00 25.69 N ANISOU 2306 N LYS B 6 2712 2303 4745 -942 -61 -1095 N ATOM 2307 CA LYS B 6 56.121 -1.492 -20.736 1.00 30.16 C ANISOU 2307 CA LYS B 6 3238 2896 5326 -863 -40 -1180 C ATOM 2308 C LYS B 6 56.404 0.007 -20.657 1.00 30.03 C ANISOU 2308 C LYS B 6 3246 2981 5182 -814 -32 -1145 C ATOM 2309 O LYS B 6 55.512 0.829 -20.870 1.00 28.97 O ANISOU 2309 O LYS B 6 3125 2949 4934 -837 -17 -1119 O ATOM 2310 CB LYS B 6 56.039 -1.945 -22.195 1.00 32.52 C ANISOU 2310 CB LYS B 6 3461 3241 5655 -872 7 -1313 C ATOM 2311 CG LYS B 6 57.279 -1.705 -23.030 1.00 35.75 C ANISOU 2311 CG LYS B 6 3815 3680 6090 -802 40 -1412 C ATOM 2312 CD LYS B 6 57.132 -2.412 -24.374 1.00 39.13 C ANISOU 2312 CD LYS B 6 4173 4130 6564 -823 84 -1540 C ATOM 2313 CE LYS B 6 58.282 -2.100 -25.314 1.00 41.48 C ANISOU 2313 CE LYS B 6 4408 4477 6876 -764 130 -1642 C ATOM 2314 NZ LYS B 6 58.303 -0.664 -25.704 1.00 43.43 N ANISOU 2314 NZ LYS B 6 4663 4858 6982 -735 167 -1633 N ATOM 2315 N THR B 7 57.654 0.349 -20.350 1.00 27.26 N ANISOU 2315 N THR B 7 2899 2602 4857 -746 -44 -1146 N ATOM 2316 CA THR B 7 58.089 1.740 -20.250 1.00 25.31 C ANISOU 2316 CA THR B 7 2677 2439 4501 -697 -41 -1114 C ATOM 2317 C THR B 7 58.689 2.245 -21.560 1.00 25.27 C ANISOU 2317 C THR B 7 2605 2528 4469 -657 14 -1222 C ATOM 2318 O THR B 7 58.957 1.464 -22.471 1.00 24.23 O ANISOU 2318 O THR B 7 2406 2384 4416 -661 48 -1324 O ATOM 2319 CB THR B 7 59.136 1.924 -19.133 1.00 24.06 C ANISOU 2319 CB THR B 7 2561 2202 4380 -645 -89 -1047 C ATOM 2320 OG1 THR B 7 60.364 1.288 -19.514 1.00 24.38 O ANISOU 2320 OG1 THR B 7 2538 2185 4542 -597 -86 -1126 O ATOM 2321 CG2 THR B 7 58.640 1.316 -17.831 1.00 24.98 C ANISOU 2321 CG2 THR B 7 2746 2215 4531 -682 -135 -944 C ATOM 2322 N LEU B 8 58.908 3.555 -21.641 1.00 28.35 N ANISOU 2322 N LEU B 8 3015 3010 4745 -624 25 -1198 N ATOM 2323 CA LEU B 8 59.487 4.173 -22.833 1.00 31.97 C ANISOU 2323 CA LEU B 8 3418 3566 5164 -591 84 -1288 C ATOM 2324 C LEU B 8 60.880 3.637 -23.156 1.00 35.64 C ANISOU 2324 C LEU B 8 3818 3977 5748 -547 94 -1363 C ATOM 2325 O LEU B 8 61.314 3.680 -24.307 1.00 40.61 O ANISOU 2325 O LEU B 8 4379 4667 6383 -537 153 -1462 O ATOM 2326 CB LEU B 8 59.553 5.693 -22.670 1.00 31.13 C ANISOU 2326 CB LEU B 8 3355 3554 4919 -562 86 -1231 C ATOM 2327 CG LEU B 8 58.272 6.486 -22.923 1.00 33.65 C ANISOU 2327 CG LEU B 8 3707 3978 5099 -594 104 -1198 C ATOM 2328 CD1 LEU B 8 58.542 7.976 -22.786 1.00 33.63 C ANISOU 2328 CD1 LEU B 8 3744 4061 4973 -557 104 -1147 C ATOM 2329 CD2 LEU B 8 57.705 6.164 -24.297 1.00 33.36 C ANISOU 2329 CD2 LEU B 8 3609 4018 5050 -623 171 -1301 C ATOM 2330 N THR B 9 61.579 3.140 -22.140 1.00 34.35 N ANISOU 2330 N THR B 9 3672 3701 5679 -522 38 -1315 N ATOM 2331 CA THR B 9 62.920 2.594 -22.326 1.00 33.92 C ANISOU 2331 CA THR B 9 3550 3588 5751 -477 37 -1380 C ATOM 2332 C THR B 9 62.862 1.155 -22.814 1.00 36.49 C ANISOU 2332 C THR B 9 3818 3840 6206 -501 49 -1461 C ATOM 2333 O THR B 9 63.878 0.572 -23.185 1.00 37.56 O ANISOU 2333 O THR B 9 3882 3934 6455 -470 57 -1537 O ATOM 2334 CB THR B 9 63.740 2.635 -21.024 1.00 34.91 C ANISOU 2334 CB THR B 9 3714 3620 5930 -435 -34 -1296 C ATOM 2335 OG1 THR B 9 63.193 1.705 -20.081 1.00 35.37 O ANISOU 2335 OG1 THR B 9 3819 3570 6049 -464 -83 -1234 O ATOM 2336 CG2 THR B 9 63.731 4.032 -20.425 1.00 32.36 C ANISOU 2336 CG2 THR B 9 3461 3359 5477 -415 -55 -1207 C ATOM 2337 N GLY B 10 61.663 0.584 -22.801 1.00 35.54 N ANISOU 2337 N GLY B 10 3727 3704 6072 -559 47 -1446 N ATOM 2338 CA GLY B 10 61.469 -0.792 -23.212 1.00 36.65 C ANISOU 2338 CA GLY B 10 3825 3770 6329 -591 52 -1515 C ATOM 2339 C GLY B 10 61.442 -1.758 -22.043 1.00 37.39 C ANISOU 2339 C GLY B 10 3960 3724 6523 -603 -13 -1445 C ATOM 2340 O GLY B 10 61.263 -2.961 -22.229 1.00 38.31 O ANISOU 2340 O GLY B 10 4053 3762 6742 -632 -19 -1489 O ATOM 2341 N LYS B 11 61.627 -1.235 -20.835 1.00 35.17 N ANISOU 2341 N LYS B 11 3745 3409 6210 -581 -62 -1335 N ATOM 2342 CA LYS B 11 61.579 -2.063 -19.638 1.00 38.03 C ANISOU 2342 CA LYS B 11 4157 3640 6651 -593 -121 -1256 C ATOM 2343 C LYS B 11 60.191 -2.681 -19.509 1.00 35.85 C ANISOU 2343 C LYS B 11 3921 3343 6358 -675 -119 -1222 C ATOM 2344 O LYS B 11 59.183 -1.982 -19.591 1.00 31.09 O ANISOU 2344 O LYS B 11 3351 2824 5637 -715 -100 -1183 O ATOM 2345 CB LYS B 11 61.928 -1.241 -18.394 1.00 40.78 C ANISOU 2345 CB LYS B 11 4578 3972 6944 -558 -167 -1142 C ATOM 2346 CG LYS B 11 62.450 -2.062 -17.225 1.00 46.46 C ANISOU 2346 CG LYS B 11 5331 4551 7770 -538 -229 -1080 C ATOM 2347 CD LYS B 11 61.349 -2.878 -16.571 1.00 50.74 C ANISOU 2347 CD LYS B 11 5935 5018 8324 -607 -242 -1015 C ATOM 2348 CE LYS B 11 61.922 -3.823 -15.523 1.00 54.14 C ANISOU 2348 CE LYS B 11 6397 5304 8871 -585 -299 -965 C ATOM 2349 NZ LYS B 11 62.765 -3.108 -14.518 1.00 55.26 N ANISOU 2349 NZ LYS B 11 6581 5426 8990 -519 -345 -889 N ATOM 2350 N THR B 12 60.144 -3.995 -19.319 1.00 38.39 N ANISOU 2350 N THR B 12 4236 3552 6801 -701 -140 -1238 N ATOM 2351 CA THR B 12 58.873 -4.708 -19.263 1.00 40.46 C ANISOU 2351 CA THR B 12 4525 3785 7063 -786 -138 -1213 C ATOM 2352 C THR B 12 58.647 -5.379 -17.917 1.00 41.51 C ANISOU 2352 C THR B 12 4732 3794 7246 -813 -186 -1107 C ATOM 2353 O THR B 12 59.560 -5.964 -17.336 1.00 42.29 O ANISOU 2353 O THR B 12 4835 3788 7445 -770 -223 -1098 O ATOM 2354 CB THR B 12 58.777 -5.777 -20.366 1.00 44.45 C ANISOU 2354 CB THR B 12 4962 4267 7661 -814 -114 -1331 C ATOM 2355 OG1 THR B 12 58.912 -5.156 -21.651 1.00 45.35 O ANISOU 2355 OG1 THR B 12 5012 4500 7718 -793 -60 -1430 O ATOM 2356 CG2 THR B 12 57.437 -6.489 -20.292 1.00 45.13 C ANISOU 2356 CG2 THR B 12 5075 4325 7746 -907 -116 -1301 C ATOM 2357 N ILE B 13 57.414 -5.292 -17.432 1.00 42.02 N ANISOU 2357 N ILE B 13 4851 3874 7241 -886 -183 -1026 N ATOM 2358 CA ILE B 13 57.045 -5.871 -16.147 1.00 45.66 C ANISOU 2358 CA ILE B 13 5389 4225 7733 -923 -215 -918 C ATOM 2359 C ILE B 13 55.787 -6.721 -16.279 1.00 44.79 C ANISOU 2359 C ILE B 13 5284 4092 7643 -1025 -203 -907 C ATOM 2360 O ILE B 13 54.874 -6.375 -17.027 1.00 41.88 O ANISOU 2360 O ILE B 13 4882 3824 7206 -1075 -173 -935 O ATOM 2361 CB ILE B 13 56.808 -4.780 -15.090 1.00 47.98 C ANISOU 2361 CB ILE B 13 5761 4557 7911 -913 -222 -799 C ATOM 2362 CG1 ILE B 13 57.988 -3.809 -15.053 1.00 49.52 C ANISOU 2362 CG1 ILE B 13 5949 4793 8075 -816 -235 -812 C ATOM 2363 CG2 ILE B 13 56.572 -5.404 -13.724 1.00 49.87 C ANISOU 2363 CG2 ILE B 13 6085 4674 8187 -938 -247 -690 C ATOM 2364 CD1 ILE B 13 57.706 -2.537 -14.282 1.00 49.53 C ANISOU 2364 CD1 ILE B 13 6018 4858 7941 -805 -236 -715 C ATOM 2365 N THR B 14 55.743 -7.833 -15.553 1.00 46.53 N ANISOU 2365 N THR B 14 5544 4177 7958 -1057 -228 -866 N ATOM 2366 CA THR B 14 54.576 -8.705 -15.579 1.00 46.72 C ANISOU 2366 CA THR B 14 5575 4166 8009 -1161 -218 -847 C ATOM 2367 C THR B 14 53.739 -8.515 -14.321 1.00 45.26 C ANISOU 2367 C THR B 14 5468 3953 7775 -1215 -215 -710 C ATOM 2368 O THR B 14 54.272 -8.461 -13.213 1.00 44.72 O ANISOU 2368 O THR B 14 5463 3803 7724 -1171 -235 -632 O ATOM 2369 CB THR B 14 54.974 -10.186 -15.702 1.00 51.89 C ANISOU 2369 CB THR B 14 6219 4683 8816 -1172 -243 -900 C ATOM 2370 OG1 THR B 14 55.498 -10.650 -14.451 1.00 53.88 O ANISOU 2370 OG1 THR B 14 6545 4805 9123 -1147 -277 -816 O ATOM 2371 CG2 THR B 14 56.021 -10.367 -16.791 1.00 52.70 C ANISOU 2371 CG2 THR B 14 6240 4795 8988 -1101 -244 -1034 C ATOM 2372 N LEU B 15 52.426 -8.412 -14.500 1.00 45.32 N ANISOU 2372 N LEU B 15 5454 4025 7741 -1304 -188 -683 N ATOM 2373 CA LEU B 15 51.514 -8.231 -13.377 1.00 47.07 C ANISOU 2373 CA LEU B 15 5722 4224 7940 -1361 -171 -559 C ATOM 2374 C LEU B 15 50.399 -9.269 -13.379 1.00 47.86 C ANISOU 2374 C LEU B 15 5808 4277 8100 -1476 -159 -539 C ATOM 2375 O LEU B 15 49.815 -9.566 -14.422 1.00 48.73 O ANISOU 2375 O LEU B 15 5854 4450 8212 -1529 -152 -613 O ATOM 2376 CB LEU B 15 50.908 -6.827 -13.399 1.00 46.70 C ANISOU 2376 CB LEU B 15 5657 4322 7766 -1360 -144 -521 C ATOM 2377 CG LEU B 15 51.869 -5.655 -13.217 1.00 45.40 C ANISOU 2377 CG LEU B 15 5516 4205 7527 -1257 -155 -518 C ATOM 2378 CD1 LEU B 15 51.112 -4.340 -13.288 1.00 45.16 C ANISOU 2378 CD1 LEU B 15 5467 4318 7376 -1270 -129 -481 C ATOM 2379 CD2 LEU B 15 52.617 -5.777 -11.899 1.00 46.12 C ANISOU 2379 CD2 LEU B 15 5694 4172 7657 -1201 -177 -432 C ATOM 2380 N GLU B 16 50.112 -9.820 -12.204 1.00 49.12 N ANISOU 2380 N GLU B 16 6033 4323 8307 -1513 -155 -436 N ATOM 2381 CA GLU B 16 48.975 -10.715 -12.029 1.00 50.85 C ANISOU 2381 CA GLU B 16 6246 4499 8577 -1630 -136 -394 C ATOM 2382 C GLU B 16 47.720 -9.911 -11.719 1.00 48.62 C ANISOU 2382 C GLU B 16 5937 4326 8210 -1697 -90 -311 C ATOM 2383 O GLU B 16 47.641 -9.244 -10.688 1.00 48.49 O ANISOU 2383 O GLU B 16 5972 4305 8146 -1673 -69 -206 O ATOM 2384 CB GLU B 16 49.245 -11.728 -10.913 1.00 55.90 C ANISOU 2384 CB GLU B 16 6973 4962 9305 -1641 -149 -317 C ATOM 2385 CG GLU B 16 49.992 -12.967 -11.369 1.00 60.53 C ANISOU 2385 CG GLU B 16 7564 5434 10002 -1628 -190 -402 C ATOM 2386 CD GLU B 16 49.160 -13.839 -12.291 1.00 64.16 C ANISOU 2386 CD GLU B 16 7962 5903 10511 -1730 -185 -469 C ATOM 2387 OE1 GLU B 16 49.501 -13.936 -13.489 1.00 65.11 O ANISOU 2387 OE1 GLU B 16 8022 6076 10642 -1708 -201 -589 O ATOM 2388 OE2 GLU B 16 48.167 -14.432 -11.817 1.00 65.36 O ANISOU 2388 OE2 GLU B 16 8131 6011 10693 -1833 -164 -399 O ATOM 2389 N VAL B 17 46.745 -9.977 -12.619 1.00 47.33 N ANISOU 2389 N VAL B 17 5692 4263 8029 -1775 -76 -357 N ATOM 2390 CA VAL B 17 45.520 -9.200 -12.480 1.00 44.08 C ANISOU 2390 CA VAL B 17 5233 3977 7537 -1838 -35 -289 C ATOM 2391 C VAL B 17 44.279 -9.981 -12.889 1.00 45.44 C ANISOU 2391 C VAL B 17 5344 4173 7747 -1962 -20 -289 C ATOM 2392 O VAL B 17 44.365 -11.049 -13.490 1.00 46.77 O ANISOU 2392 O VAL B 17 5501 4273 7996 -1998 -47 -361 O ATOM 2393 CB VAL B 17 45.564 -7.913 -13.329 1.00 38.83 C ANISOU 2393 CB VAL B 17 4509 3479 6763 -1781 -36 -346 C ATOM 2394 CG1 VAL B 17 46.778 -7.073 -12.967 1.00 38.53 C ANISOU 2394 CG1 VAL B 17 4528 3428 6682 -1663 -51 -348 C ATOM 2395 CG2 VAL B 17 45.560 -8.253 -14.815 1.00 34.68 C ANISOU 2395 CG2 VAL B 17 3915 3013 6248 -1785 -61 -477 C ATOM 2396 N GLU B 18 43.120 -9.427 -12.554 1.00 46.40 N ANISOU 2396 N GLU B 18 5423 4395 7810 -2026 22 -207 N ATOM 2397 CA GLU B 18 41.839 -9.926 -13.037 1.00 50.08 C ANISOU 2397 CA GLU B 18 5810 4925 8295 -2141 35 -205 C ATOM 2398 C GLU B 18 41.195 -8.829 -13.874 1.00 48.66 C ANISOU 2398 C GLU B 18 5535 4937 8017 -2127 38 -235 C ATOM 2399 O GLU B 18 41.490 -7.651 -13.681 1.00 48.00 O ANISOU 2399 O GLU B 18 5458 4934 7847 -2052 49 -212 O ATOM 2400 CB GLU B 18 40.920 -10.321 -11.877 1.00 54.74 C ANISOU 2400 CB GLU B 18 6420 5470 8908 -2235 89 -71 C ATOM 2401 CG GLU B 18 41.610 -11.026 -10.716 1.00 59.80 C ANISOU 2401 CG GLU B 18 7178 5925 9617 -2219 96 -3 C ATOM 2402 CD GLU B 18 41.898 -12.488 -10.994 1.00 65.18 C ANISOU 2402 CD GLU B 18 7888 6462 10416 -2264 59 -60 C ATOM 2403 OE1 GLU B 18 42.130 -12.841 -12.168 1.00 67.05 O ANISOU 2403 OE1 GLU B 18 8074 6721 10679 -2259 15 -182 O ATOM 2404 OE2 GLU B 18 41.884 -13.287 -10.034 1.00 68.33 O ANISOU 2404 OE2 GLU B 18 8363 6723 10877 -2303 76 19 O ATOM 2405 N PRO B 19 40.309 -9.208 -14.809 1.00 50.66 N ANISOU 2405 N PRO B 19 5703 5260 8284 -2194 24 -283 N ATOM 2406 CA PRO B 19 39.640 -8.212 -15.653 1.00 51.00 C ANISOU 2406 CA PRO B 19 5655 5479 8242 -2172 22 -311 C ATOM 2407 C PRO B 19 38.815 -7.218 -14.843 1.00 52.38 C ANISOU 2407 C PRO B 19 5795 5765 8341 -2184 70 -189 C ATOM 2408 O PRO B 19 38.577 -6.100 -15.294 1.00 52.22 O ANISOU 2408 O PRO B 19 5723 5880 8238 -2125 70 -199 O ATOM 2409 CB PRO B 19 38.732 -9.065 -16.544 1.00 51.96 C ANISOU 2409 CB PRO B 19 5705 5619 8419 -2260 1 -361 C ATOM 2410 CG PRO B 19 38.521 -10.323 -15.770 1.00 52.91 C ANISOU 2410 CG PRO B 19 5865 5602 8637 -2360 13 -307 C ATOM 2411 CD PRO B 19 39.841 -10.571 -15.109 1.00 52.33 C ANISOU 2411 CD PRO B 19 5901 5388 8595 -2293 9 -311 C ATOM 2412 N SER B 20 38.388 -7.628 -13.654 1.00 52.36 N ANISOU 2412 N SER B 20 5826 5702 8367 -2255 116 -75 N ATOM 2413 CA SER B 20 37.561 -6.781 -12.805 1.00 51.56 C ANISOU 2413 CA SER B 20 5694 5704 8193 -2272 177 50 C ATOM 2414 C SER B 20 38.371 -5.674 -12.141 1.00 51.35 C ANISOU 2414 C SER B 20 5735 5688 8088 -2171 197 89 C ATOM 2415 O SER B 20 37.810 -4.679 -11.682 1.00 51.27 O ANISOU 2415 O SER B 20 5692 5793 7993 -2154 242 173 O ATOM 2416 CB SER B 20 36.859 -7.625 -11.737 1.00 52.10 C ANISOU 2416 CB SER B 20 5788 5697 8309 -2381 236 157 C ATOM 2417 OG SER B 20 37.792 -8.413 -11.019 1.00 51.39 O ANISOU 2417 OG SER B 20 5820 5417 8289 -2369 236 163 O ATOM 2418 N ASP B 21 39.688 -5.853 -12.090 1.00 49.71 N ANISOU 2418 N ASP B 21 5619 5360 7908 -2099 163 31 N ATOM 2419 CA ASP B 21 40.562 -4.909 -11.403 1.00 46.99 C ANISOU 2419 CA ASP B 21 5352 4998 7503 -2003 176 68 C ATOM 2420 C ASP B 21 40.517 -3.527 -12.042 1.00 42.41 C ANISOU 2420 C ASP B 21 4712 4583 6818 -1932 164 38 C ATOM 2421 O ASP B 21 40.516 -3.391 -13.265 1.00 38.77 O ANISOU 2421 O ASP B 21 4186 4194 6349 -1906 121 -65 O ATOM 2422 CB ASP B 21 42.003 -5.427 -11.382 1.00 48.80 C ANISOU 2422 CB ASP B 21 5675 5072 7795 -1933 129 1 C ATOM 2423 CG ASP B 21 42.133 -6.763 -10.673 1.00 53.39 C ANISOU 2423 CG ASP B 21 6325 5478 8485 -1984 134 40 C ATOM 2424 OD1 ASP B 21 41.210 -7.128 -9.913 1.00 56.80 O ANISOU 2424 OD1 ASP B 21 6757 5893 8930 -2065 187 141 O ATOM 2425 OD2 ASP B 21 43.159 -7.448 -10.870 1.00 54.04 O ANISOU 2425 OD2 ASP B 21 6458 5439 8636 -1941 88 -29 O ATOM 2426 N THR B 22 40.473 -2.503 -11.198 1.00 40.28 N ANISOU 2426 N THR B 22 4473 4364 6468 -1892 209 132 N ATOM 2427 CA THR B 22 40.480 -1.123 -11.660 1.00 35.44 C ANISOU 2427 CA THR B 22 3811 3896 5758 -1814 200 118 C ATOM 2428 C THR B 22 41.881 -0.708 -12.086 1.00 32.13 C ANISOU 2428 C THR B 22 3455 3428 5325 -1717 147 23 C ATOM 2429 O THR B 22 42.857 -1.405 -11.812 1.00 33.11 O ANISOU 2429 O THR B 22 3663 3406 5511 -1700 124 -9 O ATOM 2430 CB THR B 22 39.982 -0.159 -10.569 1.00 34.26 C ANISOU 2430 CB THR B 22 3681 3818 5519 -1801 273 259 C ATOM 2431 OG1 THR B 22 40.898 -0.168 -9.467 1.00 35.04 O ANISOU 2431 OG1 THR B 22 3925 3774 5617 -1761 305 305 O ATOM 2432 CG2 THR B 22 38.607 -0.572 -10.080 1.00 35.62 C ANISOU 2432 CG2 THR B 22 3799 4047 5688 -1880 342 351 C ATOM 2433 N ILE B 23 41.973 0.432 -12.759 1.00 29.64 N ANISOU 2433 N ILE B 23 3096 3234 4932 -1643 133 -25 N ATOM 2434 CA ILE B 23 43.262 0.970 -13.163 1.00 29.76 C ANISOU 2434 CA ILE B 23 3169 3225 4914 -1551 90 -111 C ATOM 2435 C ILE B 23 44.074 1.378 -11.936 1.00 29.37 C ANISOU 2435 C ILE B 23 3228 3085 4847 -1514 102 -27 C ATOM 2436 O ILE B 23 45.296 1.249 -11.924 1.00 27.64 O ANISOU 2436 O ILE B 23 3081 2769 4651 -1455 65 -80 O ATOM 2437 CB ILE B 23 43.098 2.172 -14.109 1.00 27.13 C ANISOU 2437 CB ILE B 23 2779 3047 4483 -1480 88 -183 C ATOM 2438 CG1 ILE B 23 42.325 1.754 -15.361 1.00 29.15 C ANISOU 2438 CG1 ILE B 23 2952 3376 4748 -1505 81 -275 C ATOM 2439 CG2 ILE B 23 44.453 2.743 -14.485 1.00 25.35 C ANISOU 2439 CG2 ILE B 23 2618 2800 4214 -1390 49 -263 C ATOM 2440 CD1 ILE B 23 42.996 0.654 -16.161 1.00 26.40 C ANISOU 2440 CD1 ILE B 23 2625 2934 4471 -1518 39 -375 C ATOM 2441 N GLU B 24 43.386 1.860 -10.903 1.00 32.38 N ANISOU 2441 N GLU B 24 3624 3494 5183 -1537 164 108 N ATOM 2442 CA GLU B 24 44.038 2.198 -9.639 1.00 35.47 C ANISOU 2442 CA GLU B 24 4141 3777 5559 -1486 197 203 C ATOM 2443 C GLU B 24 44.734 0.982 -9.041 1.00 30.87 C ANISOU 2443 C GLU B 24 3644 2994 5093 -1480 173 214 C ATOM 2444 O GLU B 24 45.877 1.069 -8.590 1.00 30.17 O ANISOU 2444 O GLU B 24 3645 2793 5025 -1394 132 220 O ATOM 2445 CB GLU B 24 43.031 2.757 -8.630 1.00 45.71 C ANISOU 2445 CB GLU B 24 5449 5129 6790 -1491 300 356 C ATOM 2446 CG GLU B 24 42.454 4.114 -8.995 1.00 54.68 C ANISOU 2446 CG GLU B 24 6505 6443 7828 -1442 349 361 C ATOM 2447 CD GLU B 24 41.908 4.858 -7.788 1.00 62.53 C ANISOU 2447 CD GLU B 24 7579 7507 8673 -1387 384 577 C ATOM 2448 OE1 GLU B 24 42.368 4.584 -6.659 1.00 65.47 O ANISOU 2448 OE1 GLU B 24 8077 7743 9057 -1339 374 703 O ATOM 2449 OE2 GLU B 24 41.018 5.716 -7.968 1.00 64.58 O ANISOU 2449 OE2 GLU B 24 7787 7965 8785 -1372 424 605 O ATOM 2450 N ASN B 25 44.035 -0.149 -9.038 1.00 33.00 N ANISOU 2450 N ASN B 25 3881 3225 5434 -1567 191 222 N ATOM 2451 CA ASN B 25 44.598 -1.398 -8.537 1.00 35.04 C ANISOU 2451 CA ASN B 25 4211 3301 5802 -1570 166 230 C ATOM 2452 C ASN B 25 45.864 -1.789 -9.291 1.00 31.71 C ANISOU 2452 C ASN B 25 3802 2814 5431 -1514 90 98 C ATOM 2453 O ASN B 25 46.834 -2.251 -8.693 1.00 29.84 O ANISOU 2453 O ASN B 25 3652 2436 5250 -1454 58 113 O ATOM 2454 CB ASN B 25 43.574 -2.532 -8.629 1.00 40.28 C ANISOU 2454 CB ASN B 25 4823 3951 6531 -1687 196 241 C ATOM 2455 CG ASN B 25 42.349 -2.284 -7.773 1.00 45.86 C ANISOU 2455 CG ASN B 25 5520 4713 7190 -1739 283 380 C ATOM 2456 OD1 ASN B 25 41.241 -2.695 -8.121 1.00 48.97 O ANISOU 2456 OD1 ASN B 25 5829 5187 7591 -1838 317 378 O ATOM 2457 ND2 ASN B 25 42.539 -1.603 -6.648 1.00 47.53 N ANISOU 2457 ND2 ASN B 25 5822 4890 7347 -1663 319 509 N ATOM 2458 N VAL B 26 45.848 -1.603 -10.607 1.00 27.57 N ANISOU 2458 N VAL B 26 3194 2401 4882 -1524 62 -26 N ATOM 2459 CA VAL B 26 47.006 -1.930 -11.430 1.00 27.36 C ANISOU 2459 CA VAL B 26 3173 2333 4889 -1464 6 -150 C ATOM 2460 C VAL B 26 48.186 -1.033 -11.080 1.00 26.04 C ANISOU 2460 C VAL B 26 3072 2145 4677 -1354 -19 -149 C ATOM 2461 O VAL B 26 49.307 -1.511 -10.909 1.00 26.22 O ANISOU 2461 O VAL B 26 3147 2060 4757 -1292 -55 -180 O ATOM 2462 CB VAL B 26 46.694 -1.797 -12.930 1.00 27.13 C ANISOU 2462 CB VAL B 26 3049 2435 4826 -1478 -10 -267 C ATOM 2463 CG1 VAL B 26 47.966 -1.943 -13.749 1.00 26.77 C ANISOU 2463 CG1 VAL B 26 3016 2359 4796 -1399 -50 -382 C ATOM 2464 CG2 VAL B 26 45.659 -2.830 -13.347 1.00 28.60 C ANISOU 2464 CG2 VAL B 26 3173 2621 5072 -1578 2 -278 C ATOM 2465 N LYS B 27 47.928 0.266 -10.969 1.00 24.77 N ANISOU 2465 N LYS B 27 2905 2092 4414 -1329 -3 -112 N ATOM 2466 CA LYS B 27 48.966 1.221 -10.595 1.00 24.74 C ANISOU 2466 CA LYS B 27 2966 2073 4359 -1229 -28 -101 C ATOM 2467 C LYS B 27 49.536 0.892 -9.219 1.00 25.35 C ANISOU 2467 C LYS B 27 3153 1991 4489 -1175 -36 8 C ATOM 2468 O LYS B 27 50.742 1.004 -8.991 1.00 23.84 O ANISOU 2468 O LYS B 27 3017 1732 4308 -1085 -80 -11 O ATOM 2469 CB LYS B 27 48.419 2.651 -10.609 1.00 24.99 C ANISOU 2469 CB LYS B 27 2977 2244 4275 -1223 -3 -62 C ATOM 2470 CG LYS B 27 48.082 3.176 -11.995 1.00 27.41 C ANISOU 2470 CG LYS B 27 3187 2715 4512 -1235 -15 -169 C ATOM 2471 CD LYS B 27 47.628 4.629 -11.940 1.00 26.73 C ANISOU 2471 CD LYS B 27 3081 2763 4313 -1214 3 -128 C ATOM 2472 CE LYS B 27 47.335 5.175 -13.330 1.00 27.24 C ANISOU 2472 CE LYS B 27 3059 2983 4309 -1189 -5 -241 C ATOM 2473 NZ LYS B 27 46.883 6.595 -13.293 1.00 26.61 N ANISOU 2473 NZ LYS B 27 2963 3047 4099 -1156 30 -225 N ATOM 2474 N ALA B 28 48.660 0.486 -8.307 1.00 25.75 N ANISOU 2474 N ALA B 28 3232 1992 4561 -1223 6 129 N ATOM 2475 CA ALA B 28 49.073 0.115 -6.963 1.00 26.79 C ANISOU 2475 CA ALA B 28 3477 1981 4721 -1165 -4 251 C ATOM 2476 C ALA B 28 49.974 -1.115 -7.007 1.00 29.71 C ANISOU 2476 C ALA B 28 3872 2222 5195 -1149 -50 186 C ATOM 2477 O ALA B 28 50.908 -1.243 -6.215 1.00 32.50 O ANISOU 2477 O ALA B 28 4313 2477 5560 -1062 -88 229 O ATOM 2478 CB ALA B 28 47.859 -0.142 -6.087 1.00 28.26 C ANISOU 2478 CB ALA B 28 3685 2157 4895 -1226 60 394 C ATOM 2479 N LYS B 29 49.688 -2.015 -7.942 1.00 27.64 N ANISOU 2479 N LYS B 29 3533 1970 5000 -1227 -48 85 N ATOM 2480 CA LYS B 29 50.509 -3.204 -8.132 1.00 30.35 C ANISOU 2480 CA LYS B 29 3888 2201 5443 -1214 -89 17 C ATOM 2481 C LYS B 29 51.851 -2.838 -8.753 1.00 30.02 C ANISOU 2481 C LYS B 29 3836 2176 5394 -1121 -137 -84 C ATOM 2482 O LYS B 29 52.859 -3.499 -8.506 1.00 29.49 O ANISOU 2482 O LYS B 29 3805 2009 5392 -1066 -176 -104 O ATOM 2483 CB LYS B 29 49.787 -4.231 -9.007 1.00 35.02 C ANISOU 2483 CB LYS B 29 4402 2805 6100 -1318 -74 -57 C ATOM 2484 CG LYS B 29 48.689 -5.002 -8.292 1.00 38.16 C ANISOU 2484 CG LYS B 29 4818 3142 6539 -1411 -34 42 C ATOM 2485 CD LYS B 29 48.252 -6.207 -9.111 1.00 42.02 C ANISOU 2485 CD LYS B 29 5245 3611 7111 -1500 -38 -39 C ATOM 2486 CE LYS B 29 47.318 -7.110 -8.320 1.00 45.21 C ANISOU 2486 CE LYS B 29 5679 3932 7568 -1593 -3 60 C ATOM 2487 NZ LYS B 29 46.030 -6.437 -7.998 1.00 47.32 N ANISOU 2487 NZ LYS B 29 5911 4304 7762 -1659 61 150 N ATOM 2488 N ILE B 30 51.858 -1.787 -9.565 1.00 29.61 N ANISOU 2488 N ILE B 30 3731 2258 5259 -1106 -131 -146 N ATOM 2489 CA ILE B 30 53.096 -1.304 -10.161 1.00 30.60 C ANISOU 2489 CA ILE B 30 3846 2416 5363 -1020 -167 -233 C ATOM 2490 C ILE B 30 53.997 -0.701 -9.087 1.00 32.05 C ANISOU 2490 C ILE B 30 4116 2541 5521 -920 -197 -155 C ATOM 2491 O ILE B 30 55.212 -0.898 -9.101 1.00 30.93 O ANISOU 2491 O ILE B 30 3985 2354 5413 -847 -236 -196 O ATOM 2492 CB ILE B 30 52.829 -0.262 -11.263 1.00 23.97 C ANISOU 2492 CB ILE B 30 2941 1740 4425 -1027 -152 -308 C ATOM 2493 CG1 ILE B 30 52.031 -0.893 -12.407 1.00 32.34 C ANISOU 2493 CG1 ILE B 30 3917 2866 5505 -1108 -132 -389 C ATOM 2494 CG2 ILE B 30 54.140 0.317 -11.776 1.00 23.06 C ANISOU 2494 CG2 ILE B 30 2824 1659 4280 -935 -181 -380 C ATOM 2495 CD1 ILE B 30 51.686 0.068 -13.531 1.00 23.64 C ANISOU 2495 CD1 ILE B 30 2753 1929 4300 -1108 -120 -455 C ATOM 2496 N GLN B 31 53.393 0.022 -8.150 1.00 35.80 N ANISOU 2496 N GLN B 31 4648 3022 5933 -914 -180 -36 N ATOM 2497 CA GLN B 31 54.138 0.600 -7.037 1.00 39.79 C ANISOU 2497 CA GLN B 31 5246 3475 6397 -812 -211 56 C ATOM 2498 C GLN B 31 54.754 -0.490 -6.163 1.00 42.05 C ANISOU 2498 C GLN B 31 5595 3622 6759 -778 -240 100 C ATOM 2499 O GLN B 31 55.845 -0.317 -5.624 1.00 43.09 O ANISOU 2499 O GLN B 31 5774 3717 6881 -685 -282 114 O ATOM 2500 CB GLN B 31 53.241 1.503 -6.190 1.00 42.22 C ANISOU 2500 CB GLN B 31 5609 3818 6613 -807 -181 191 C ATOM 2501 CG GLN B 31 53.980 2.192 -5.053 1.00 47.06 C ANISOU 2501 CG GLN B 31 6325 4403 7152 -687 -215 289 C ATOM 2502 CD GLN B 31 53.061 2.989 -4.148 1.00 51.77 C ANISOU 2502 CD GLN B 31 6989 5042 7639 -667 -181 439 C ATOM 2503 OE1 GLN B 31 51.858 2.734 -4.084 1.00 54.10 O ANISOU 2503 OE1 GLN B 31 7267 5353 7936 -749 -128 498 O ATOM 2504 NE2 GLN B 31 53.627 3.961 -3.441 1.00 52.08 N ANISOU 2504 NE2 GLN B 31 7101 5118 7572 -555 -208 501 N ATOM 2505 N ASP B 32 54.048 -1.608 -6.020 1.00 45.24 N ANISOU 2505 N ASP B 32 5998 3954 7236 -856 -216 121 N ATOM 2506 CA ASP B 32 54.569 -2.743 -5.265 1.00 50.30 C ANISOU 2506 CA ASP B 32 6699 4460 7954 -835 -243 155 C ATOM 2507 C ASP B 32 55.863 -3.244 -5.892 1.00 49.79 C ANISOU 2507 C ASP B 32 6591 4366 7960 -788 -292 42 C ATOM 2508 O ASP B 32 56.757 -3.731 -5.199 1.00 54.19 O ANISOU 2508 O ASP B 32 7201 4836 8553 -726 -332 67 O ATOM 2509 CB ASP B 32 53.544 -3.879 -5.203 1.00 57.29 C ANISOU 2509 CB ASP B 32 7578 5279 8910 -942 -208 181 C ATOM 2510 CG ASP B 32 52.319 -3.520 -4.385 1.00 62.26 C ANISOU 2510 CG ASP B 32 8255 5925 9475 -986 -153 314 C ATOM 2511 OD1 ASP B 32 52.396 -2.564 -3.585 1.00 63.08 O ANISOU 2511 OD1 ASP B 32 8426 6059 9481 -913 -149 406 O ATOM 2512 OD2 ASP B 32 51.283 -4.201 -4.535 1.00 64.19 O ANISOU 2512 OD2 ASP B 32 8469 6157 9762 -1090 -112 330 O ATOM 2513 N LYS B 33 55.952 -3.113 -7.211 1.00 45.33 N ANISOU 2513 N LYS B 33 5931 3884 7408 -815 -287 -79 N ATOM 2514 CA LYS B 33 57.105 -3.586 -7.964 1.00 44.06 C ANISOU 2514 CA LYS B 33 5717 3711 7314 -774 -322 -189 C ATOM 2515 C LYS B 33 58.201 -2.533 -8.110 1.00 40.90 C ANISOU 2515 C LYS B 33 5305 3379 6854 -681 -349 -218 C ATOM 2516 O LYS B 33 59.385 -2.853 -8.023 1.00 40.18 O ANISOU 2516 O LYS B 33 5209 3244 6814 -618 -390 -249 O ATOM 2517 CB LYS B 33 56.666 -4.053 -9.352 1.00 45.69 C ANISOU 2517 CB LYS B 33 5829 3975 7557 -844 -296 -305 C ATOM 2518 CG LYS B 33 56.386 -5.540 -9.469 1.00 49.12 C ANISOU 2518 CG LYS B 33 6253 4306 8103 -904 -298 -329 C ATOM 2519 CD LYS B 33 57.510 -6.232 -10.222 1.00 50.13 C ANISOU 2519 CD LYS B 33 6329 4403 8316 -860 -328 -437 C ATOM 2520 CE LYS B 33 57.069 -7.577 -10.771 1.00 52.77 C ANISOU 2520 CE LYS B 33 6630 4671 8748 -932 -323 -492 C ATOM 2521 NZ LYS B 33 58.062 -8.124 -11.739 1.00 53.93 N ANISOU 2521 NZ LYS B 33 6690 4801 8998 -886 -346 -615 N ATOM 2522 N GLU B 34 57.809 -1.283 -8.340 1.00 38.84 N ANISOU 2522 N GLU B 34 5039 3229 6489 -678 -327 -208 N ATOM 2523 CA GLU B 34 58.775 -0.244 -8.690 1.00 38.20 C ANISOU 2523 CA GLU B 34 4938 3228 6348 -604 -347 -249 C ATOM 2524 C GLU B 34 58.874 0.890 -7.673 1.00 36.43 C ANISOU 2524 C GLU B 34 4790 3025 6028 -542 -362 -147 C ATOM 2525 O GLU B 34 59.848 1.641 -7.675 1.00 37.20 O ANISOU 2525 O GLU B 34 4886 3165 6086 -472 -391 -161 O ATOM 2526 CB GLU B 34 58.438 0.338 -10.063 1.00 40.28 C ANISOU 2526 CB GLU B 34 5125 3620 6560 -642 -312 -347 C ATOM 2527 CG GLU B 34 58.540 -0.671 -11.191 1.00 46.60 C ANISOU 2527 CG GLU B 34 5847 4419 7441 -682 -300 -457 C ATOM 2528 CD GLU B 34 59.891 -1.362 -11.227 1.00 51.34 C ANISOU 2528 CD GLU B 34 6413 4940 8152 -617 -341 -505 C ATOM 2529 OE1 GLU B 34 60.916 -0.682 -11.006 1.00 52.86 O ANISOU 2529 OE1 GLU B 34 6601 5149 8336 -540 -373 -502 O ATOM 2530 OE2 GLU B 34 59.926 -2.587 -11.469 1.00 52.87 O ANISOU 2530 OE2 GLU B 34 6573 5055 8461 -642 -347 -548 O ATOM 2531 N GLY B 35 57.868 1.024 -6.817 1.00 35.36 N ANISOU 2531 N GLY B 35 4718 2864 5852 -567 -341 -40 N ATOM 2532 CA GLY B 35 57.893 2.045 -5.786 1.00 33.52 C ANISOU 2532 CA GLY B 35 4565 2652 5519 -499 -353 69 C ATOM 2533 C GLY B 35 57.412 3.417 -6.227 1.00 32.08 C ANISOU 2533 C GLY B 35 4370 2587 5234 -499 -335 69 C ATOM 2534 O GLY B 35 57.453 4.368 -5.450 1.00 34.40 O ANISOU 2534 O GLY B 35 4727 2913 5432 -434 -348 156 O ATOM 2535 N ILE B 36 56.955 3.533 -7.469 1.00 30.29 N ANISOU 2535 N ILE B 36 4062 2436 5013 -568 -306 -30 N ATOM 2536 CA ILE B 36 56.411 4.800 -7.945 1.00 29.94 C ANISOU 2536 CA ILE B 36 4002 2506 4868 -579 -289 -36 C ATOM 2537 C ILE B 36 54.946 4.927 -7.543 1.00 24.35 C ANISOU 2537 C ILE B 36 3311 1810 4130 -643 -249 57 C ATOM 2538 O ILE B 36 54.138 4.050 -7.846 1.00 27.70 O ANISOU 2538 O ILE B 36 3692 2218 4615 -733 -212 37 O ATOM 2539 CB ILE B 36 56.531 4.952 -9.477 1.00 31.65 C ANISOU 2539 CB ILE B 36 4127 2826 5073 -624 -268 -183 C ATOM 2540 CG1 ILE B 36 57.999 5.049 -9.898 1.00 33.29 C ANISOU 2540 CG1 ILE B 36 4315 3041 5291 -554 -299 -254 C ATOM 2541 CG2 ILE B 36 55.771 6.184 -9.951 1.00 27.32 C ANISOU 2541 CG2 ILE B 36 3564 2404 4414 -653 -247 -189 C ATOM 2542 CD1 ILE B 36 58.695 3.713 -10.002 1.00 38.73 C ANISOU 2542 CD1 ILE B 36 4975 3642 6099 -550 -314 -298 C ATOM 2543 N PRO B 37 54.603 6.019 -6.846 1.00 25.70 N ANISOU 2543 N PRO B 37 3546 2019 4199 -595 -259 169 N ATOM 2544 CA PRO B 37 53.218 6.262 -6.424 1.00 26.44 C ANISOU 2544 CA PRO B 37 3658 2146 4242 -647 -219 286 C ATOM 2545 C PRO B 37 52.270 6.368 -7.615 1.00 23.89 C ANISOU 2545 C PRO B 37 3223 1926 3927 -764 -174 198 C ATOM 2546 O PRO B 37 52.654 6.906 -8.654 1.00 23.73 O ANISOU 2546 O PRO B 37 3145 1992 3881 -772 -184 71 O ATOM 2547 CB PRO B 37 53.302 7.591 -5.661 1.00 27.74 C ANISOU 2547 CB PRO B 37 3916 2373 4250 -546 -251 406 C ATOM 2548 CG PRO B 37 54.609 8.201 -6.068 1.00 30.14 C ANISOU 2548 CG PRO B 37 4217 2696 4539 -473 -308 313 C ATOM 2549 CD PRO B 37 55.523 7.059 -6.359 1.00 27.28 C ANISOU 2549 CD PRO B 37 3809 2248 4310 -482 -310 207 C ATOM 2550 N PRO B 38 51.045 5.845 -7.464 1.00 23.86 N ANISOU 2550 N PRO B 38 3185 1935 3945 -853 -118 260 N ATOM 2551 CA PRO B 38 50.031 5.767 -8.522 1.00 22.49 C ANISOU 2551 CA PRO B 38 2887 1881 3776 -968 -64 173 C ATOM 2552 C PRO B 38 49.707 7.105 -9.186 1.00 21.91 C ANISOU 2552 C PRO B 38 2771 1971 3583 -977 -70 150 C ATOM 2553 O PRO B 38 49.512 7.141 -10.400 1.00 22.77 O ANISOU 2553 O PRO B 38 2779 2192 3682 -1029 -46 -7 O ATOM 2554 CB PRO B 38 48.806 5.225 -7.781 1.00 23.47 C ANISOU 2554 CB PRO B 38 3012 1994 3914 -1030 -4 308 C ATOM 2555 CG PRO B 38 49.382 4.414 -6.679 1.00 24.21 C ANISOU 2555 CG PRO B 38 3212 1924 4063 -971 -26 388 C ATOM 2556 CD PRO B 38 50.594 5.180 -6.230 1.00 24.33 C ANISOU 2556 CD PRO B 38 3321 1904 4020 -842 -94 407 C ATOM 2557 N ASP B 39 49.649 8.184 -8.411 1.00 23.23 N ANISOU 2557 N ASP B 39 3041 2219 3566 -875 -80 279 N ATOM 2558 CA ASP B 39 49.276 9.481 -8.968 1.00 24.16 C ANISOU 2558 CA ASP B 39 3145 2554 3479 -831 -66 247 C ATOM 2559 C ASP B 39 50.395 10.078 -9.824 1.00 21.86 C ANISOU 2559 C ASP B 39 2847 2283 3177 -793 -121 104 C ATOM 2560 O ASP B 39 50.190 11.078 -10.513 1.00 21.95 O ANISOU 2560 O ASP B 39 2837 2465 3036 -772 -113 45 O ATOM 2561 CB ASP B 39 48.883 10.454 -7.853 1.00 29.59 C ANISOU 2561 CB ASP B 39 3953 3316 3973 -727 -62 428 C ATOM 2562 CG ASP B 39 50.041 10.798 -6.941 1.00 35.22 C ANISOU 2562 CG ASP B 39 4806 3900 4675 -620 -140 510 C ATOM 2563 OD1 ASP B 39 50.025 11.904 -6.361 1.00 37.69 O ANISOU 2563 OD1 ASP B 39 5217 4297 4805 -519 -159 607 O ATOM 2564 OD2 ASP B 39 50.966 9.970 -6.802 1.00 38.24 O ANISOU 2564 OD2 ASP B 39 5200 4096 5233 -634 -188 476 O ATOM 2565 N GLN B 40 51.574 9.463 -9.783 1.00 19.29 N ANISOU 2565 N GLN B 40 2538 1780 3012 -787 -175 49 N ATOM 2566 CA GLN B 40 52.665 9.860 -10.670 1.00 18.14 C ANISOU 2566 CA GLN B 40 2365 1640 2886 -768 -218 -101 C ATOM 2567 C GLN B 40 52.803 8.880 -11.834 1.00 17.89 C ANISOU 2567 C GLN B 40 2242 1637 2919 -822 -176 -256 C ATOM 2568 O GLN B 40 53.790 8.909 -12.575 1.00 19.17 O ANISOU 2568 O GLN B 40 2401 1822 3060 -774 -198 -337 O ATOM 2569 CB GLN B 40 53.981 9.962 -9.899 1.00 16.79 C ANISOU 2569 CB GLN B 40 2289 1343 2747 -657 -278 -55 C ATOM 2570 CG GLN B 40 53.970 11.028 -8.813 1.00 17.68 C ANISOU 2570 CG GLN B 40 2543 1471 2705 -566 -331 117 C ATOM 2571 CD GLN B 40 55.283 11.112 -8.063 1.00 20.12 C ANISOU 2571 CD GLN B 40 2924 1677 3044 -451 -390 151 C ATOM 2572 OE1 GLN B 40 56.350 10.860 -8.625 1.00 17.86 O ANISOU 2572 OE1 GLN B 40 2575 1379 2831 -427 -389 29 O ATOM 2573 NE2 GLN B 40 55.213 11.461 -6.784 1.00 22.46 N ANISOU 2573 NE2 GLN B 40 3324 1964 3245 -360 -408 306 N ATOM 2574 N GLN B 41 51.806 8.015 -11.987 1.00 16.93 N ANISOU 2574 N GLN B 41 2060 1520 2853 -901 -142 -245 N ATOM 2575 CA GLN B 41 51.781 7.059 -13.088 1.00 21.21 C ANISOU 2575 CA GLN B 41 2532 2088 3440 -923 -139 -339 C ATOM 2576 C GLN B 41 50.696 7.406 -14.099 1.00 21.54 C ANISOU 2576 C GLN B 41 2482 2284 3420 -951 -111 -387 C ATOM 2577 O GLN B 41 49.624 7.887 -13.733 1.00 25.04 O ANISOU 2577 O GLN B 41 2894 2800 3818 -989 -74 -335 O ATOM 2578 CB GLN B 41 51.543 5.636 -12.577 1.00 18.22 C ANISOU 2578 CB GLN B 41 2155 1583 3186 -973 -122 -307 C ATOM 2579 CG GLN B 41 52.524 5.145 -11.538 1.00 21.63 C ANISOU 2579 CG GLN B 41 2670 1853 3696 -917 -142 -256 C ATOM 2580 CD GLN B 41 52.187 3.745 -11.062 1.00 22.61 C ANISOU 2580 CD GLN B 41 2796 1860 3936 -963 -129 -220 C ATOM 2581 OE1 GLN B 41 51.615 2.946 -11.806 1.00 20.89 O ANISOU 2581 OE1 GLN B 41 2512 1670 3755 -1029 -114 -277 O ATOM 2582 NE2 GLN B 41 52.530 3.443 -9.816 1.00 23.43 N ANISOU 2582 NE2 GLN B 41 2981 1832 4090 -920 -141 -118 N ATOM 2583 N ARG B 42 50.980 7.149 -15.370 1.00 17.61 N ANISOU 2583 N ARG B 42 1944 1835 2911 -924 -109 -487 N ATOM 2584 CA ARG B 42 49.961 7.197 -16.412 1.00 18.64 C ANISOU 2584 CA ARG B 42 2002 2084 2995 -945 -72 -543 C ATOM 2585 C ARG B 42 50.014 5.900 -17.209 1.00 18.15 C ANISOU 2585 C ARG B 42 1905 1968 3025 -976 -67 -608 C ATOM 2586 O ARG B 42 51.075 5.505 -17.692 1.00 20.79 O ANISOU 2586 O ARG B 42 2257 2250 3394 -937 -78 -664 O ATOM 2587 CB ARG B 42 50.164 8.397 -17.339 1.00 15.84 C ANISOU 2587 CB ARG B 42 1654 1860 2506 -875 -58 -602 C ATOM 2588 CG ARG B 42 50.059 9.752 -16.665 1.00 21.89 C ANISOU 2588 CG ARG B 42 2460 2705 3154 -843 -58 -552 C ATOM 2589 CD ARG B 42 48.670 9.991 -16.093 1.00 23.11 C ANISOU 2589 CD ARG B 42 2582 2946 3253 -904 -19 -499 C ATOM 2590 NE ARG B 42 48.512 11.364 -15.619 1.00 21.86 N ANISOU 2590 NE ARG B 42 2473 2912 2922 -879 -11 -457 N ATOM 2591 CZ ARG B 42 48.927 11.801 -14.435 1.00 23.23 C ANISOU 2591 CZ ARG B 42 2718 3048 3062 -890 -34 -371 C ATOM 2592 NH1 ARG B 42 49.533 10.974 -13.594 1.00 23.74 N ANISOU 2592 NH1 ARG B 42 2812 2929 3278 -915 -56 -321 N ATOM 2593 NH2 ARG B 42 48.738 13.068 -14.090 1.00 23.48 N ANISOU 2593 NH2 ARG B 42 2811 3219 2891 -865 -45 -314 N ATOM 2594 N LEU B 43 48.875 5.232 -17.337 1.00 20.90 N ANISOU 2594 N LEU B 43 2199 2329 3413 -1045 -46 -602 N ATOM 2595 CA LEU B 43 48.812 3.997 -18.107 1.00 20.29 C ANISOU 2595 CA LEU B 43 2088 2202 3419 -1081 -44 -667 C ATOM 2596 C LEU B 43 48.157 4.235 -19.463 1.00 26.19 C ANISOU 2596 C LEU B 43 2785 3063 4102 -1075 -17 -750 C ATOM 2597 O LEU B 43 47.123 4.897 -19.560 1.00 23.31 O ANISOU 2597 O LEU B 43 2391 2802 3662 -1087 5 -734 O ATOM 2598 CB LEU B 43 48.063 2.915 -17.331 1.00 21.56 C ANISOU 2598 CB LEU B 43 2230 2279 3682 -1170 -44 -604 C ATOM 2599 CG LEU B 43 48.863 2.283 -16.188 1.00 32.29 C ANISOU 2599 CG LEU B 43 3653 3489 5125 -1176 -64 -545 C ATOM 2600 CD1 LEU B 43 48.019 1.274 -15.420 1.00 23.27 C ANISOU 2600 CD1 LEU B 43 2501 2268 4071 -1267 -51 -473 C ATOM 2601 CD2 LEU B 43 50.133 1.631 -16.724 1.00 22.27 C ANISOU 2601 CD2 LEU B 43 2407 2142 3912 -1127 -82 -628 C ATOM 2602 N ILE B 44 48.774 3.695 -20.509 1.00 26.71 N ANISOU 2602 N ILE B 44 2843 3109 4195 -1054 -10 -843 N ATOM 2603 CA ILE B 44 48.294 3.887 -21.870 1.00 23.67 C ANISOU 2603 CA ILE B 44 2411 2824 3760 -1049 35 -952 C ATOM 2604 C ILE B 44 48.064 2.551 -22.567 1.00 24.42 C ANISOU 2604 C ILE B 44 2459 2861 3959 -1102 45 -1030 C ATOM 2605 O ILE B 44 48.907 1.654 -22.508 1.00 25.09 O ANISOU 2605 O ILE B 44 2548 2841 4146 -1102 36 -1062 O ATOM 2606 CB ILE B 44 49.286 4.725 -22.699 1.00 23.11 C ANISOU 2606 CB ILE B 44 2351 2815 3615 -971 72 -1035 C ATOM 2607 CG1 ILE B 44 49.606 6.037 -21.978 1.00 24.01 C ANISOU 2607 CG1 ILE B 44 2518 2977 3629 -918 57 -957 C ATOM 2608 CG2 ILE B 44 48.736 4.985 -24.095 1.00 25.11 C ANISOU 2608 CG2 ILE B 44 2562 3179 3799 -972 125 -1138 C ATOM 2609 CD1 ILE B 44 50.623 6.895 -22.695 1.00 26.39 C ANISOU 2609 CD1 ILE B 44 2830 3337 3859 -848 94 -1021 C ATOM 2610 N PHE B 45 46.919 2.426 -23.227 1.00 23.57 N ANISOU 2610 N PHE B 45 2307 2821 3828 -1147 60 -1062 N ATOM 2611 CA PHE B 45 46.597 1.221 -23.979 1.00 28.33 C ANISOU 2611 CA PHE B 45 2864 3378 4522 -1202 66 -1142 C ATOM 2612 C PHE B 45 45.770 1.565 -25.212 1.00 28.14 C ANISOU 2612 C PHE B 45 2799 3469 4424 -1210 100 -1228 C ATOM 2613 O PHE B 45 44.752 2.249 -25.114 1.00 26.08 O ANISOU 2613 O PHE B 45 2528 3299 4082 -1223 101 -1184 O ATOM 2614 CB PHE B 45 45.848 0.219 -23.097 1.00 30.39 C ANISOU 2614 CB PHE B 45 3114 3554 4881 -1286 29 -1054 C ATOM 2615 CG PHE B 45 45.506 -1.066 -23.795 1.00 33.25 C ANISOU 2615 CG PHE B 45 3433 3858 5341 -1348 28 -1129 C ATOM 2616 CD1 PHE B 45 46.440 -2.085 -23.897 1.00 34.95 C ANISOU 2616 CD1 PHE B 45 3657 3958 5663 -1346 23 -1184 C ATOM 2617 CD2 PHE B 45 44.248 -1.259 -24.339 1.00 35.11 C ANISOU 2617 CD2 PHE B 45 3619 4154 5567 -1408 31 -1146 C ATOM 2618 CE1 PHE B 45 46.126 -3.270 -24.535 1.00 36.20 C ANISOU 2618 CE1 PHE B 45 3780 4061 5914 -1402 20 -1254 C ATOM 2619 CE2 PHE B 45 43.927 -2.442 -24.979 1.00 37.16 C ANISOU 2619 CE2 PHE B 45 3843 4358 5920 -1469 25 -1214 C ATOM 2620 CZ PHE B 45 44.868 -3.449 -25.076 1.00 38.54 C ANISOU 2620 CZ PHE B 45 4031 4416 6197 -1467 19 -1269 C ATOM 2621 N ALA B 46 46.218 1.085 -26.368 1.00 30.72 N ANISOU 2621 N ALA B 46 3101 3793 4778 -1202 129 -1350 N ATOM 2622 CA ALA B 46 45.539 1.349 -27.634 1.00 32.76 C ANISOU 2622 CA ALA B 46 3325 4155 4967 -1211 162 -1441 C ATOM 2623 C ALA B 46 45.413 2.848 -27.895 1.00 32.28 C ANISOU 2623 C ALA B 46 3286 4231 4748 -1156 193 -1433 C ATOM 2624 O ALA B 46 44.383 3.320 -28.379 1.00 29.56 O ANISOU 2624 O ALA B 46 2923 3985 4324 -1174 203 -1444 O ATOM 2625 CB ALA B 46 44.168 0.688 -27.650 1.00 34.86 C ANISOU 2625 CB ALA B 46 3551 4421 5274 -1294 135 -1422 C ATOM 2626 N GLY B 47 46.465 3.589 -27.561 1.00 32.13 N ANISOU 2626 N GLY B 47 3305 4216 4687 -1089 208 -1411 N ATOM 2627 CA GLY B 47 46.526 5.013 -27.837 1.00 32.47 C ANISOU 2627 CA GLY B 47 3372 4382 4582 -1035 241 -1403 C ATOM 2628 C GLY B 47 45.704 5.884 -26.905 1.00 33.63 C ANISOU 2628 C GLY B 47 3548 4584 4645 -1033 217 -1297 C ATOM 2629 O GLY B 47 45.521 7.072 -27.167 1.00 35.21 O ANISOU 2629 O GLY B 47 3766 4897 4714 -994 244 -1288 O ATOM 2630 N LYS B 48 45.214 5.304 -25.814 1.00 31.46 N ANISOU 2630 N LYS B 48 3273 4232 4448 -1075 169 -1210 N ATOM 2631 CA LYS B 48 44.363 6.044 -24.886 1.00 27.65 C ANISOU 2631 CA LYS B 48 2804 3802 3900 -1079 147 -1104 C ATOM 2632 C LYS B 48 44.876 5.995 -23.446 1.00 24.02 C ANISOU 2632 C LYS B 48 2378 3250 3497 -1072 107 -990 C ATOM 2633 O LYS B 48 45.314 4.950 -22.966 1.00 24.11 O ANISOU 2633 O LYS B 48 2386 3139 3635 -1105 80 -968 O ATOM 2634 CB LYS B 48 42.931 5.507 -24.942 1.00 29.22 C ANISOU 2634 CB LYS B 48 2948 4024 4131 -1150 134 -1089 C ATOM 2635 N GLN B 49 44.816 7.132 -22.762 1.00 23.65 N ANISOU 2635 N GLN B 49 2368 3264 3354 -1029 102 -916 N ATOM 2636 CA GLN B 49 45.196 7.191 -21.355 1.00 21.53 C ANISOU 2636 CA GLN B 49 2124 2929 3128 -1033 78 -820 C ATOM 2637 C GLN B 49 44.073 6.631 -20.492 1.00 22.40 C ANISOU 2637 C GLN B 49 2183 3025 3304 -1111 79 -748 C ATOM 2638 O GLN B 49 42.953 7.135 -20.517 1.00 23.18 O ANISOU 2638 O GLN B 49 2248 3231 3327 -1128 102 -733 O ATOM 2639 CB GLN B 49 45.526 8.625 -20.936 1.00 18.94 C ANISOU 2639 CB GLN B 49 1847 2684 2664 -969 88 -787 C ATOM 2640 CG GLN B 49 46.024 8.747 -19.502 1.00 20.88 C ANISOU 2640 CG GLN B 49 2123 2862 2948 -973 65 -698 C ATOM 2641 CD GLN B 49 46.447 10.158 -19.141 1.00 24.64 C ANISOU 2641 CD GLN B 49 2658 3421 3282 -910 68 -671 C ATOM 2642 OE1 GLN B 49 47.528 10.613 -19.521 1.00 25.69 O ANISOU 2642 OE1 GLN B 49 2836 3536 3389 -846 57 -698 O ATOM 2643 NE2 GLN B 49 45.597 10.859 -18.400 1.00 23.84 N ANISOU 2643 NE2 GLN B 49 2556 3419 3082 -930 85 -608 N ATOM 2644 N LEU B 50 44.380 5.586 -19.732 1.00 20.31 N ANISOU 2644 N LEU B 50 1912 2629 3176 -1159 58 -698 N ATOM 2645 CA LEU B 50 43.375 4.898 -18.928 1.00 24.55 C ANISOU 2645 CA LEU B 50 2397 3135 3794 -1242 67 -617 C ATOM 2646 C LEU B 50 42.984 5.702 -17.690 1.00 20.75 C ANISOU 2646 C LEU B 50 1921 2701 3261 -1243 95 -510 C ATOM 2647 O LEU B 50 43.841 6.267 -17.013 1.00 22.31 O ANISOU 2647 O LEU B 50 2177 2869 3430 -1202 87 -475 O ATOM 2648 CB LEU B 50 43.888 3.518 -18.514 1.00 22.46 C ANISOU 2648 CB LEU B 50 2141 2713 3679 -1294 39 -594 C ATOM 2649 CG LEU B 50 44.494 2.686 -19.645 1.00 27.72 C ANISOU 2649 CG LEU B 50 2813 3327 4392 -1288 19 -701 C ATOM 2650 CD1 LEU B 50 44.913 1.314 -19.144 1.00 24.25 C ANISOU 2650 CD1 LEU B 50 2389 2739 4087 -1343 -3 -679 C ATOM 2651 CD2 LEU B 50 43.509 2.566 -20.796 1.00 30.01 C ANISOU 2651 CD2 LEU B 50 3047 3702 4653 -1312 32 -770 C ATOM 2652 N GLU B 51 41.687 5.746 -17.403 1.00 28.13 N ANISOU 2652 N GLU B 51 2796 3713 4181 -1290 131 -457 N ATOM 2653 CA GLU B 51 41.177 6.455 -16.232 1.00 32.86 C ANISOU 2653 CA GLU B 51 3397 4374 4715 -1295 178 -344 C ATOM 2654 C GLU B 51 41.175 5.553 -14.996 1.00 31.18 C ANISOU 2654 C GLU B 51 3182 4028 4637 -1358 196 -223 C ATOM 2655 O GLU B 51 40.813 4.380 -15.074 1.00 31.11 O ANISOU 2655 O GLU B 51 3131 3934 4755 -1424 184 -211 O ATOM 2656 CB GLU B 51 39.768 6.991 -16.504 1.00 39.31 C ANISOU 2656 CB GLU B 51 4153 5351 5433 -1305 216 -337 C ATOM 2657 CG GLU B 51 39.702 7.998 -17.648 1.00 45.11 C ANISOU 2657 CG GLU B 51 4908 6222 6011 -1242 199 -443 C ATOM 2658 CD GLU B 51 38.308 8.564 -17.856 1.00 51.99 C ANISOU 2658 CD GLU B 51 5727 7250 6777 -1247 226 -430 C ATOM 2659 OE1 GLU B 51 37.348 8.021 -17.269 1.00 54.49 O ANISOU 2659 OE1 GLU B 51 5977 7563 7164 -1303 260 -352 O ATOM 2660 OE2 GLU B 51 38.173 9.554 -18.607 1.00 52.78 O ANISOU 2660 OE2 GLU B 51 5856 7474 6724 -1194 215 -496 O ATOM 2661 N ASP B 52 41.569 6.118 -13.859 1.00 31.45 N ANISOU 2661 N ASP B 52 3277 4046 4627 -1342 225 -125 N ATOM 2662 CA ASP B 52 41.766 5.357 -12.624 1.00 37.06 C ANISOU 2662 CA ASP B 52 4024 4605 5452 -1389 245 2 C ATOM 2663 C ASP B 52 40.544 4.555 -12.175 1.00 37.65 C ANISOU 2663 C ASP B 52 4031 4670 5605 -1463 297 93 C ATOM 2664 O ASP B 52 40.684 3.480 -11.592 1.00 38.71 O ANISOU 2664 O ASP B 52 4183 4659 5867 -1521 282 164 O ATOM 2665 CB ASP B 52 42.191 6.297 -11.491 1.00 40.92 C ANISOU 2665 CB ASP B 52 4616 5110 5824 -1353 281 115 C ATOM 2666 CG ASP B 52 43.568 6.895 -11.712 1.00 42.40 C ANISOU 2666 CG ASP B 52 4880 5257 5971 -1293 219 47 C ATOM 2667 OD1 ASP B 52 44.293 6.412 -12.606 1.00 42.75 O ANISOU 2667 OD1 ASP B 52 4903 5234 6108 -1272 156 -79 O ATOM 2668 OD2 ASP B 52 43.929 7.843 -10.982 1.00 43.68 O ANISOU 2668 OD2 ASP B 52 5142 5461 5993 -1239 217 143 O ATOM 2669 N GLY B 53 39.353 5.077 -12.447 1.00 37.77 N ANISOU 2669 N GLY B 53 3979 4846 5528 -1462 347 94 N ATOM 2670 CA GLY B 53 38.118 4.458 -11.992 1.00 37.99 C ANISOU 2670 CA GLY B 53 3936 4881 5619 -1523 408 182 C ATOM 2671 C GLY B 53 37.676 3.223 -12.758 1.00 40.63 C ANISOU 2671 C GLY B 53 4187 5151 6099 -1597 360 127 C ATOM 2672 O GLY B 53 37.151 2.277 -12.170 1.00 44.57 O ANISOU 2672 O GLY B 53 4656 5571 6708 -1671 381 220 O ATOM 2673 N ARG B 54 37.879 3.230 -14.072 1.00 38.19 N ANISOU 2673 N ARG B 54 3856 4882 5771 -1580 295 -15 N ATOM 2674 CA ARG B 54 37.431 2.128 -14.919 1.00 39.61 C ANISOU 2674 CA ARG B 54 3978 5024 6048 -1649 251 -75 C ATOM 2675 C ARG B 54 38.233 0.850 -14.675 1.00 39.73 C ANISOU 2675 C ARG B 54 4048 4872 6176 -1712 200 -64 C ATOM 2676 O ARG B 54 39.286 0.875 -14.038 1.00 40.13 O ANISOU 2676 O ARG B 54 4187 4833 6228 -1689 185 -37 O ATOM 2677 CB ARG B 54 37.516 2.522 -16.398 1.00 43.03 C ANISOU 2677 CB ARG B 54 4402 5538 6411 -1602 209 -229 C ATOM 2678 CG ARG B 54 36.626 3.689 -16.791 1.00 47.42 C ANISOU 2678 CG ARG B 54 4920 6269 6829 -1554 245 -256 C ATOM 2679 CD ARG B 54 36.542 3.829 -18.305 1.00 53.02 C ANISOU 2679 CD ARG B 54 5622 7039 7485 -1530 203 -398 C ATOM 2680 NE ARG B 54 35.616 4.885 -18.702 1.00 57.03 N ANISOU 2680 NE ARG B 54 6101 7713 7855 -1493 227 -423 N ATOM 2681 CZ ARG B 54 35.975 6.004 -19.323 1.00 58.58 C ANISOU 2681 CZ ARG B 54 6352 8008 7897 -1417 216 -497 C ATOM 2682 NH1 ARG B 54 37.247 6.216 -19.637 1.00 58.03 N ANISOU 2682 NH1 ARG B 54 6360 7886 7801 -1366 189 -554 N ATOM 2683 NH2 ARG B 54 35.057 6.908 -19.640 1.00 58.88 N ANISOU 2683 NH2 ARG B 54 6367 8198 7805 -1390 231 -512 N ATOM 2684 N THR B 55 37.719 -0.263 -15.191 1.00 40.04 N ANISOU 2684 N THR B 55 4045 4873 6297 -1793 174 -95 N ATOM 2685 CA THR B 55 38.366 -1.564 -15.054 1.00 39.58 C ANISOU 2685 CA THR B 55 4047 4666 6326 -1859 136 -110 C ATOM 2686 C THR B 55 39.130 -1.952 -16.315 1.00 36.36 C ANISOU 2686 C THR B 55 3663 4224 5930 -1825 82 -264 C ATOM 2687 O THR B 55 39.031 -1.284 -17.341 1.00 29.72 O ANISOU 2687 O THR B 55 2789 3477 5025 -1766 73 -353 O ATOM 2688 CB THR B 55 37.343 -2.673 -14.745 1.00 41.29 C ANISOU 2688 CB THR B 55 4215 4850 6625 -1981 152 -46 C ATOM 2689 OG1 THR B 55 36.510 -2.886 -15.891 1.00 41.40 O ANISOU 2689 OG1 THR B 55 4138 4934 6656 -2003 132 -123 O ATOM 2690 CG2 THR B 55 36.480 -2.286 -13.559 1.00 42.37 C ANISOU 2690 CG2 THR B 55 4321 5037 6741 -2013 219 114 C ATOM 2691 N LEU B 56 39.883 -3.044 -16.232 1.00 34.49 N ANISOU 2691 N LEU B 56 3487 3848 5769 -1858 56 -297 N ATOM 2692 CA LEU B 56 40.646 -3.541 -17.372 1.00 35.48 C ANISOU 2692 CA LEU B 56 3633 3930 5918 -1824 16 -434 C ATOM 2693 C LEU B 56 39.728 -4.055 -18.481 1.00 39.49 C ANISOU 2693 C LEU B 56 4065 4489 6450 -1875 3 -502 C ATOM 2694 O LEU B 56 40.012 -3.867 -19.665 1.00 31.94 O ANISOU 2694 O LEU B 56 3102 3574 5460 -1825 -14 -614 O ATOM 2695 CB LEU B 56 41.609 -4.647 -16.930 1.00 34.75 C ANISOU 2695 CB LEU B 56 3618 3671 5915 -1842 -1 -447 C ATOM 2696 CG LEU B 56 42.775 -4.229 -16.031 1.00 34.17 C ANISOU 2696 CG LEU B 56 3634 3525 5825 -1773 1 -411 C ATOM 2697 CD1 LEU B 56 43.619 -5.435 -15.641 1.00 34.71 C ANISOU 2697 CD1 LEU B 56 3771 3421 5997 -1785 -16 -430 C ATOM 2698 CD2 LEU B 56 43.630 -3.170 -16.714 1.00 33.36 C ANISOU 2698 CD2 LEU B 56 3544 3494 5638 -1662 -14 -486 C ATOM 2699 N SER B 57 38.630 -4.699 -18.094 1.00 41.16 N ANISOU 2699 N SER B 57 4223 4696 6718 -1976 15 -431 N ATOM 2700 CA SER B 57 37.669 -5.227 -19.061 1.00 43.85 C ANISOU 2700 CA SER B 57 4489 5080 7091 -2034 -1 -486 C ATOM 2701 C SER B 57 37.013 -4.100 -19.851 1.00 44.75 C ANISOU 2701 C SER B 57 4541 5347 7114 -1977 8 -525 C ATOM 2702 O SER B 57 36.588 -4.291 -20.991 1.00 45.36 O ANISOU 2702 O SER B 57 4581 5465 7190 -1985 -12 -615 O ATOM 2703 CB SER B 57 36.600 -6.066 -18.356 1.00 44.85 C ANISOU 2703 CB SER B 57 4569 5179 7295 -2157 14 -387 C ATOM 2704 OG SER B 57 35.850 -5.277 -17.449 1.00 46.47 O ANISOU 2704 OG SER B 57 4730 5468 7458 -2162 60 -263 O ATOM 2705 N ASP B 58 36.935 -2.926 -19.234 1.00 45.73 N ANISOU 2705 N ASP B 58 4662 5552 7160 -1917 41 -460 N ATOM 2706 CA ASP B 58 36.364 -1.750 -19.879 1.00 47.05 C ANISOU 2706 CA ASP B 58 4786 5864 7226 -1852 58 -500 C ATOM 2707 C ASP B 58 37.210 -1.296 -21.063 1.00 44.78 C ANISOU 2707 C ASP B 58 4549 5601 6864 -1769 36 -636 C ATOM 2708 O ASP B 58 36.725 -0.590 -21.948 1.00 44.34 O ANISOU 2708 O ASP B 58 4469 5653 6726 -1731 41 -703 O ATOM 2709 CB ASP B 58 36.218 -0.607 -18.872 1.00 49.19 C ANISOU 2709 CB ASP B 58 5056 6207 7426 -1801 105 -404 C ATOM 2710 CG ASP B 58 35.170 -0.893 -17.814 1.00 53.37 C ANISOU 2710 CG ASP B 58 5520 6744 8015 -1874 147 -266 C ATOM 2711 OD1 ASP B 58 34.759 -2.065 -17.684 1.00 56.55 O ANISOU 2711 OD1 ASP B 58 5895 7074 8519 -1973 133 -232 O ATOM 2712 OD2 ASP B 58 34.759 0.053 -17.109 1.00 53.70 O ANISOU 2712 OD2 ASP B 58 5541 6868 7996 -1833 202 -191 O ATOM 2713 N TYR B 59 38.477 -1.703 -21.073 1.00 43.01 N ANISOU 2713 N TYR B 59 4398 5277 6665 -1740 16 -675 N ATOM 2714 CA TYR B 59 39.402 -1.320 -22.135 1.00 39.21 C ANISOU 2714 CA TYR B 59 3965 4812 6120 -1659 5 -794 C ATOM 2715 C TYR B 59 39.820 -2.513 -22.992 1.00 38.75 C ANISOU 2715 C TYR B 59 3917 4665 6140 -1692 -21 -885 C ATOM 2716 O TYR B 59 40.771 -2.424 -23.770 1.00 38.30 O ANISOU 2716 O TYR B 59 3894 4597 6061 -1633 -12 -994 O ATOM 2717 CB TYR B 59 40.642 -0.647 -21.544 1.00 36.82 C ANISOU 2717 CB TYR B 59 3736 4482 5772 -1580 11 -775 C ATOM 2718 CG TYR B 59 40.361 0.689 -20.897 1.00 33.50 C ANISOU 2718 CG TYR B 59 3315 4161 5253 -1531 39 -709 C ATOM 2719 CD1 TYR B 59 40.068 1.805 -21.669 1.00 27.96 C ANISOU 2719 CD1 TYR B 59 2610 3589 4426 -1470 55 -766 C ATOM 2720 CD2 TYR B 59 40.394 0.838 -19.516 1.00 33.02 C ANISOU 2720 CD2 TYR B 59 3265 4063 5216 -1547 52 -590 C ATOM 2721 CE1 TYR B 59 39.810 3.027 -21.088 1.00 29.64 C ANISOU 2721 CE1 TYR B 59 2828 3897 4535 -1425 82 -714 C ATOM 2722 CE2 TYR B 59 40.138 2.059 -18.924 1.00 31.45 C ANISOU 2722 CE2 TYR B 59 3067 3958 4923 -1501 84 -533 C ATOM 2723 CZ TYR B 59 39.847 3.151 -19.715 1.00 30.06 C ANISOU 2723 CZ TYR B 59 2887 3917 4619 -1439 98 -599 C ATOM 2724 OH TYR B 59 39.594 4.373 -19.138 1.00 25.90 O ANISOU 2724 OH TYR B 59 2370 3492 3980 -1394 130 -550 O ATOM 2725 N ASN B 60 39.105 -3.626 -22.842 1.00 39.39 N ANISOU 2725 N ASN B 60 3959 4688 6322 -1791 -36 -859 N ATOM 2726 CA ASN B 60 39.375 -4.833 -23.620 1.00 42.61 C ANISOU 2726 CA ASN B 60 4366 5008 6815 -1834 -54 -956 C ATOM 2727 C ASN B 60 40.780 -5.374 -23.366 1.00 40.81 C ANISOU 2727 C ASN B 60 4206 4660 6639 -1796 -57 -989 C ATOM 2728 O ASN B 60 41.371 -6.030 -24.225 1.00 40.69 O ANISOU 2728 O ASN B 60 4195 4591 6673 -1785 -57 -1106 O ATOM 2729 CB ASN B 60 39.178 -4.563 -25.116 1.00 46.15 C ANISOU 2729 CB ASN B 60 4783 5535 7216 -1805 -41 -1099 C ATOM 2730 CG ASN B 60 39.088 -5.840 -25.936 1.00 51.99 C ANISOU 2730 CG ASN B 60 5501 6199 8053 -1868 -58 -1194 C ATOM 2731 OD1 ASN B 60 38.753 -6.905 -25.416 1.00 54.03 O ANISOU 2731 OD1 ASN B 60 5750 6367 8412 -1953 -82 -1142 O ATOM 2732 ND2 ASN B 60 39.395 -5.737 -27.224 1.00 54.25 N ANISOU 2732 ND2 ASN B 60 5782 6523 8306 -1828 -43 -1333 N ATOM 2733 N ILE B 61 41.316 -5.091 -22.184 1.00 36.71 N ANISOU 2733 N ILE B 61 3737 4100 6111 -1774 -60 -887 N ATOM 2734 CA ILE B 61 42.624 -5.607 -21.806 1.00 36.49 C ANISOU 2734 CA ILE B 61 3775 3952 6136 -1738 -67 -907 C ATOM 2735 C ILE B 61 42.505 -7.081 -21.443 1.00 38.56 C ANISOU 2735 C ILE B 61 4046 4083 6523 -1826 -84 -893 C ATOM 2736 O ILE B 61 41.658 -7.465 -20.637 1.00 41.61 O ANISOU 2736 O ILE B 61 4414 4447 6951 -1911 -81 -802 O ATOM 2737 CB ILE B 61 43.224 -4.826 -20.628 1.00 36.54 C ANISOU 2737 CB ILE B 61 3831 3950 6104 -1689 -56 -817 C ATOM 2738 CG1 ILE B 61 43.497 -3.379 -21.042 1.00 36.24 C ANISOU 2738 CG1 ILE B 61 3795 4033 5941 -1596 -41 -840 C ATOM 2739 CG2 ILE B 61 44.497 -5.497 -20.135 1.00 36.72 C ANISOU 2739 CG2 ILE B 61 3920 3834 6197 -1659 -68 -830 C ATOM 2740 CD1 ILE B 61 44.111 -2.536 -19.948 1.00 36.08 C ANISOU 2740 CD1 ILE B 61 3824 4007 5878 -1545 -35 -760 C ATOM 2741 N GLN B 62 43.356 -7.906 -22.043 1.00 37.96 N ANISOU 2741 N GLN B 62 3985 3916 6522 -1805 -90 -998 N ATOM 2742 CA GLN B 62 43.256 -9.351 -21.876 1.00 41.12 C ANISOU 2742 CA GLN B 62 4394 4187 7044 -1884 -109 -1005 C ATOM 2743 C GLN B 62 44.570 -9.961 -21.418 1.00 41.31 C ANISOU 2743 C GLN B 62 4479 4076 7142 -1835 -117 -1026 C ATOM 2744 O GLN B 62 45.522 -9.248 -21.101 1.00 40.78 O ANISOU 2744 O GLN B 62 4448 4016 7032 -1746 -108 -1020 O ATOM 2745 CB GLN B 62 42.817 -10.006 -23.183 1.00 43.83 C ANISOU 2745 CB GLN B 62 4680 4539 7432 -1919 -114 -1126 C ATOM 2746 CG GLN B 62 41.521 -9.460 -23.748 1.00 47.41 C ANISOU 2746 CG GLN B 62 5069 5123 7822 -1962 -110 -1120 C ATOM 2747 CD GLN B 62 41.159 -10.102 -25.068 1.00 50.73 C ANISOU 2747 CD GLN B 62 5443 5548 8285 -1994 -117 -1248 C ATOM 2748 OE1 GLN B 62 41.971 -10.802 -25.672 1.00 53.57 O ANISOU 2748 OE1 GLN B 62 5816 5829 8708 -1968 -119 -1351 O ATOM 2749 NE2 GLN B 62 39.932 -9.873 -25.524 1.00 49.38 N ANISOU 2749 NE2 GLN B 62 5213 5468 8080 -2049 -123 -1241 N ATOM 2750 N LYS B 63 44.611 -11.289 -21.379 1.00 40.63 N ANISOU 2750 N LYS B 63 4404 3864 7170 -1893 -135 -1050 N ATOM 2751 CA LYS B 63 45.819 -12.002 -20.996 1.00 40.99 C ANISOU 2751 CA LYS B 63 4502 3771 7303 -1846 -146 -1077 C ATOM 2752 C LYS B 63 46.926 -11.708 -22.000 1.00 41.66 C ANISOU 2752 C LYS B 63 4562 3877 7389 -1741 -134 -1208 C ATOM 2753 O LYS B 63 46.679 -11.652 -23.206 1.00 41.38 O ANISOU 2753 O LYS B 63 4473 3910 7341 -1738 -122 -1310 O ATOM 2754 CB LYS B 63 45.559 -13.507 -20.905 1.00 43.37 C ANISOU 2754 CB LYS B 63 4814 3936 7727 -1931 -168 -1088 C ATOM 2755 N GLU B 64 48.136 -11.499 -21.490 1.00 38.01 N ANISOU 2755 N GLU B 64 4140 3361 6943 -1655 -135 -1202 N ATOM 2756 CA GLU B 64 49.303 -11.228 -22.323 1.00 42.58 C ANISOU 2756 CA GLU B 64 4692 3957 7531 -1554 -120 -1316 C ATOM 2757 C GLU B 64 49.206 -9.886 -23.050 1.00 41.64 C ANISOU 2757 C GLU B 64 4538 3997 7285 -1503 -87 -1352 C ATOM 2758 O GLU B 64 49.996 -9.607 -23.952 1.00 44.41 O ANISOU 2758 O GLU B 64 4857 4386 7630 -1432 -63 -1456 O ATOM 2759 CB GLU B 64 49.509 -12.358 -23.336 1.00 39.16 C ANISOU 2759 CB GLU B 64 4220 3458 7202 -1570 -124 -1442 C ATOM 2760 N SER B 65 48.244 -9.056 -22.658 1.00 39.40 N ANISOU 2760 N SER B 65 4261 3807 6901 -1538 -83 -1263 N ATOM 2761 CA SER B 65 48.145 -7.706 -23.205 1.00 38.61 C ANISOU 2761 CA SER B 65 4141 3855 6676 -1486 -55 -1283 C ATOM 2762 C SER B 65 49.252 -6.824 -22.640 1.00 38.34 C ANISOU 2762 C SER B 65 4144 3829 6596 -1393 -49 -1251 C ATOM 2763 O SER B 65 49.670 -6.995 -21.495 1.00 41.21 O ANISOU 2763 O SER B 65 4559 4108 6992 -1388 -72 -1165 O ATOM 2764 CB SER B 65 46.778 -7.089 -22.903 1.00 37.53 C ANISOU 2764 CB SER B 65 3993 3813 6453 -1548 -57 -1194 C ATOM 2765 OG SER B 65 45.752 -7.717 -23.651 1.00 39.55 O ANISOU 2765 OG SER B 65 4200 4089 6738 -1624 -60 -1240 O ATOM 2766 N THR B 66 49.721 -5.879 -23.447 1.00 36.59 N ANISOU 2766 N THR B 66 3899 3707 6296 -1322 -18 -1321 N ATOM 2767 CA THR B 66 50.796 -4.991 -23.026 1.00 37.15 C ANISOU 2767 CA THR B 66 4000 3794 6322 -1235 -12 -1298 C ATOM 2768 C THR B 66 50.314 -3.556 -22.846 1.00 36.12 C ANISOU 2768 C THR B 66 3886 3791 6048 -1215 -1 -1236 C ATOM 2769 O THR B 66 49.874 -2.912 -23.798 1.00 33.90 O ANISOU 2769 O THR B 66 3573 3623 5686 -1205 30 -1295 O ATOM 2770 CB THR B 66 51.960 -5.000 -24.035 1.00 37.77 C ANISOU 2770 CB THR B 66 4039 3881 6429 -1161 19 -1425 C ATOM 2771 OG1 THR B 66 52.574 -6.294 -24.043 1.00 41.78 O ANISOU 2771 OG1 THR B 66 4535 4261 7079 -1167 3 -1475 O ATOM 2772 CG2 THR B 66 52.999 -3.955 -23.659 1.00 36.20 C ANISOU 2772 CG2 THR B 66 3863 3716 6174 -1076 27 -1399 C ATOM 2773 N LEU B 67 50.396 -3.066 -21.613 1.00 33.29 N ANISOU 2773 N LEU B 67 3582 3410 5657 -1208 -27 -1118 N ATOM 2774 CA LEU B 67 50.096 -1.671 -21.319 1.00 32.47 C ANISOU 2774 CA LEU B 67 3501 3416 5422 -1180 -22 -1053 C ATOM 2775 C LEU B 67 51.378 -0.850 -21.330 1.00 28.45 C ANISOU 2775 C LEU B 67 3013 2922 4874 -1086 -14 -1077 C ATOM 2776 O LEU B 67 52.454 -1.366 -21.033 1.00 27.84 O ANISOU 2776 O LEU B 67 2948 2750 4879 -1050 -26 -1095 O ATOM 2777 CB LEU B 67 49.394 -1.536 -19.966 1.00 33.69 C ANISOU 2777 CB LEU B 67 3700 3547 5554 -1230 -54 -906 C ATOM 2778 CG LEU B 67 47.924 -1.948 -19.860 1.00 34.13 C ANISOU 2778 CG LEU B 67 3723 3629 5617 -1325 -55 -856 C ATOM 2779 CD1 LEU B 67 47.707 -3.392 -20.288 1.00 37.82 C ANISOU 2779 CD1 LEU B 67 4162 4009 6199 -1386 -59 -913 C ATOM 2780 CD2 LEU B 67 47.431 -1.728 -18.439 1.00 33.52 C ANISOU 2780 CD2 LEU B 67 3670 3521 5544 -1365 -57 -731 C ATOM 2781 N HIS B 68 51.262 0.427 -21.676 1.00 25.18 N ANISOU 2781 N HIS B 68 2602 2628 4339 -1047 6 -1078 N ATOM 2782 CA HIS B 68 52.417 1.314 -21.665 1.00 25.11 C ANISOU 2782 CA HIS B 68 2613 2643 4283 -965 13 -1090 C ATOM 2783 C HIS B 68 52.357 2.275 -20.481 1.00 23.94 C ANISOU 2783 C HIS B 68 2530 2508 4057 -950 -21 -966 C ATOM 2784 O HIS B 68 51.314 2.863 -20.192 1.00 24.25 O ANISOU 2784 O HIS B 68 2580 2617 4018 -982 -28 -900 O ATOM 2785 CB HIS B 68 52.515 2.083 -22.981 1.00 26.93 C ANISOU 2785 CB HIS B 68 2806 2996 4431 -926 67 -1189 C ATOM 2786 CG HIS B 68 52.830 1.214 -24.159 1.00 32.91 C ANISOU 2786 CG HIS B 68 3503 3739 5264 -930 104 -1317 C ATOM 2787 ND1 HIS B 68 51.871 0.469 -24.812 1.00 37.24 N ANISOU 2787 ND1 HIS B 68 4015 4295 5840 -991 114 -1366 N ATOM 2788 CD2 HIS B 68 53.999 0.962 -24.794 1.00 34.89 C ANISOU 2788 CD2 HIS B 68 3719 3967 5571 -883 131 -1405 C ATOM 2789 CE1 HIS B 68 52.434 -0.199 -25.803 1.00 39.76 C ANISOU 2789 CE1 HIS B 68 4287 4596 6226 -980 146 -1481 C ATOM 2790 NE2 HIS B 68 53.725 0.082 -25.814 1.00 37.35 N ANISOU 2790 NE2 HIS B 68 3977 4274 5940 -916 159 -1507 N ATOM 2791 N LEU B 69 53.486 2.416 -19.794 1.00 21.25 N ANISOU 2791 N LEU B 69 2230 2102 3744 -901 -44 -936 N ATOM 2792 CA LEU B 69 53.569 3.248 -18.600 1.00 20.15 C ANISOU 2792 CA LEU B 69 2162 1957 3538 -886 -81 -821 C ATOM 2793 C LEU B 69 54.486 4.449 -18.808 1.00 21.51 C ANISOU 2793 C LEU B 69 2350 2191 3631 -809 -77 -837 C ATOM 2794 O LEU B 69 55.647 4.296 -19.182 1.00 25.33 O ANISOU 2794 O LEU B 69 2813 2643 4169 -758 -66 -902 O ATOM 2795 CB LEU B 69 54.060 2.420 -17.411 1.00 20.72 C ANISOU 2795 CB LEU B 69 2285 1888 3701 -898 -116 -755 C ATOM 2796 CG LEU B 69 54.531 3.196 -16.177 1.00 19.87 C ANISOU 2796 CG LEU B 69 2246 1745 3559 -862 -142 -668 C ATOM 2797 CD1 LEU B 69 53.353 3.805 -15.426 1.00 19.46 C ANISOU 2797 CD1 LEU B 69 2212 1733 3450 -911 -138 -582 C ATOM 2798 CD2 LEU B 69 55.366 2.310 -15.260 1.00 21.35 C ANISOU 2798 CD2 LEU B 69 2471 1783 3858 -841 -165 -640 C ATOM 2799 N VAL B 70 53.951 5.643 -18.573 1.00 20.13 N ANISOU 2799 N VAL B 70 2208 2107 3335 -801 -85 -778 N ATOM 2800 CA VAL B 70 54.752 6.861 -18.571 1.00 18.25 C ANISOU 2800 CA VAL B 70 2000 1920 3012 -734 -89 -771 C ATOM 2801 C VAL B 70 54.591 7.545 -17.218 1.00 18.38 C ANISOU 2801 C VAL B 70 2093 1913 2976 -736 -138 -653 C ATOM 2802 O VAL B 70 53.557 7.404 -16.565 1.00 17.60 O ANISOU 2802 O VAL B 70 1992 1808 2889 -790 -139 -603 O ATOM 2803 CB VAL B 70 54.348 7.827 -19.703 1.00 20.57 C ANISOU 2803 CB VAL B 70 2260 2358 3199 -711 -40 -832 C ATOM 2804 CG1 VAL B 70 54.500 7.149 -21.057 1.00 18.31 C ANISOU 2804 CG1 VAL B 70 1898 2095 2963 -715 20 -958 C ATOM 2805 CG2 VAL B 70 52.924 8.315 -19.507 1.00 23.13 C ANISOU 2805 CG2 VAL B 70 2589 2759 3439 -746 -43 -777 C ATOM 2806 N LEU B 71 55.613 8.281 -16.795 1.00 19.36 N ANISOU 2806 N LEU B 71 2270 2023 3063 -681 -163 -627 N ATOM 2807 CA LEU B 71 55.619 8.866 -15.459 1.00 16.58 C ANISOU 2807 CA LEU B 71 1988 1628 2686 -678 -197 -542 C ATOM 2808 C LEU B 71 55.428 10.381 -15.456 1.00 18.08 C ANISOU 2808 C LEU B 71 2209 1920 2741 -643 -213 -513 C ATOM 2809 O LEU B 71 55.757 11.070 -16.423 1.00 18.98 O ANISOU 2809 O LEU B 71 2308 2121 2782 -596 -199 -552 O ATOM 2810 CB LEU B 71 56.928 8.521 -14.744 1.00 16.95 C ANISOU 2810 CB LEU B 71 2080 1563 2799 -633 -216 -528 C ATOM 2811 CG LEU B 71 57.333 7.046 -14.732 1.00 17.82 C ANISOU 2811 CG LEU B 71 2158 1564 3051 -643 -210 -560 C ATOM 2812 CD1 LEU B 71 58.577 6.849 -13.881 1.00 18.09 C ANISOU 2812 CD1 LEU B 71 2228 1493 3150 -579 -238 -533 C ATOM 2813 CD2 LEU B 71 56.188 6.171 -14.239 1.00 18.36 C ANISOU 2813 CD2 LEU B 71 2217 1576 3183 -714 -200 -525 C ATOM 2814 N ARG B 72 54.887 10.882 -14.351 1.00 18.52 N ANISOU 2814 N ARG B 72 2311 1958 2769 -661 -236 -443 N ATOM 2815 CA ARG B 72 54.831 12.311 -14.080 1.00 16.40 C ANISOU 2815 CA ARG B 72 2083 1765 2383 -611 -267 -416 C ATOM 2816 C ARG B 72 55.478 12.550 -12.720 1.00 15.88 C ANISOU 2816 C ARG B 72 2094 1606 2335 -594 -255 -376 C ATOM 2817 O ARG B 72 54.793 12.811 -11.730 1.00 14.19 O ANISOU 2817 O ARG B 72 1955 1347 2090 -591 -319 -243 O ATOM 2818 CB ARG B 72 53.391 12.824 -14.098 1.00 14.98 C ANISOU 2818 CB ARG B 72 1863 1721 2108 -646 -215 -416 C ATOM 2819 CG ARG B 72 52.644 12.556 -15.396 1.00 15.97 C ANISOU 2819 CG ARG B 72 1907 1951 2209 -661 -159 -480 C ATOM 2820 CD ARG B 72 53.158 13.421 -16.538 1.00 14.85 C ANISOU 2820 CD ARG B 72 1771 1899 1972 -583 -144 -520 C ATOM 2821 NE ARG B 72 52.602 12.995 -17.821 1.00 17.72 N ANISOU 2821 NE ARG B 72 2070 2324 2338 -602 -88 -583 N ATOM 2822 CZ ARG B 72 51.380 13.303 -18.244 1.00 19.45 C ANISOU 2822 CZ ARG B 72 2258 2661 2471 -625 -40 -594 C ATOM 2823 NH1 ARG B 72 50.582 14.046 -17.486 1.00 16.69 N ANISOU 2823 NH1 ARG B 72 1932 2399 2012 -636 -35 -538 N ATOM 2824 NH2 ARG B 72 50.956 12.869 -19.423 1.00 20.67 N ANISOU 2824 NH2 ARG B 72 2360 2854 2637 -640 3 -657 N ATOM 2825 N LEU B 73 56.803 12.444 -12.680 1.00 15.88 N ANISOU 2825 N LEU B 73 2122 1545 2368 -533 -266 -380 N ATOM 2826 CA LEU B 73 57.552 12.472 -11.427 1.00 15.73 C ANISOU 2826 CA LEU B 73 2167 1393 2418 -441 -333 -282 C ATOM 2827 C LEU B 73 57.439 13.802 -10.693 1.00 16.82 C ANISOU 2827 C LEU B 73 2415 1560 2416 -372 -420 -171 C ATOM 2828 O LEU B 73 57.344 14.860 -11.316 1.00 17.30 O ANISOU 2828 O LEU B 73 2477 1759 2336 -362 -414 -210 O ATOM 2829 CB LEU B 73 59.025 12.154 -11.688 1.00 16.39 C ANISOU 2829 CB LEU B 73 2230 1444 2552 -396 -324 -327 C ATOM 2830 CG LEU B 73 59.325 10.720 -12.122 1.00 22.00 C ANISOU 2830 CG LEU B 73 2892 2092 3376 -435 -298 -378 C ATOM 2831 CD1 LEU B 73 60.815 10.533 -12.357 1.00 22.13 C ANISOU 2831 CD1 LEU B 73 2886 2084 3439 -380 -311 -410 C ATOM 2832 CD2 LEU B 73 58.812 9.734 -11.081 1.00 22.24 C ANISOU 2832 CD2 LEU B 73 2945 1994 3511 -443 -315 -306 C ATOM 2833 N ARG B 74 57.464 13.741 -9.363 1.00 14.77 N ANISOU 2833 N ARG B 74 2265 1193 2155 -316 -483 -19 N ATOM 2834 CA ARG B 74 57.365 14.943 -8.541 1.00 14.50 C ANISOU 2834 CA ARG B 74 2372 1198 1939 -238 -547 112 C ATOM 2835 C ARG B 74 58.419 14.958 -7.438 1.00 15.33 C ANISOU 2835 C ARG B 74 2482 1287 2058 -137 -569 162 C ATOM 2836 O ARG B 74 58.834 13.910 -6.947 1.00 16.15 O ANISOU 2836 O ARG B 74 2543 1302 2292 -134 -550 167 O ATOM 2837 CB ARG B 74 55.966 15.062 -7.933 1.00 16.93 C ANISOU 2837 CB ARG B 74 2748 1558 2126 -246 -512 250 C ATOM 2838 CG ARG B 74 54.849 14.970 -8.963 1.00 20.93 C ANISOU 2838 CG ARG B 74 3141 2224 2586 -335 -424 162 C ATOM 2839 CD ARG B 74 53.622 15.747 -8.529 1.00 21.97 C ANISOU 2839 CD ARG B 74 3325 2514 2511 -298 -384 281 C ATOM 2840 NE ARG B 74 53.040 15.239 -7.290 1.00 23.56 N ANISOU 2840 NE ARG B 74 3593 2634 2724 -274 -369 445 N ATOM 2841 CZ ARG B 74 52.010 14.401 -7.241 1.00 23.74 C ANISOU 2841 CZ ARG B 74 3551 2664 2805 -348 -298 471 C ATOM 2842 NH1 ARG B 74 51.455 13.969 -8.364 1.00 24.54 N ANISOU 2842 NH1 ARG B 74 3517 2846 2962 -448 -243 340 N ATOM 2843 NH2 ARG B 74 51.537 13.994 -6.070 1.00 20.40 N ANISOU 2843 NH2 ARG B 74 3173 2185 2393 -309 -270 600 N ATOM 2844 N GLY B 75 58.850 16.155 -7.055 1.00 16.37 N ANISOU 2844 N GLY B 75 2645 1519 2056 -81 -579 162 N ATOM 2845 CA GLY B 75 59.869 16.299 -6.032 1.00 10.15 C ANISOU 2845 CA GLY B 75 1835 736 1287 -30 -567 166 C ATOM 2846 C GLY B 75 59.361 17.047 -4.818 1.00 10.88 C ANISOU 2846 C GLY B 75 1984 871 1279 0 -539 209 C ATOM 2847 O GLY B 75 58.671 18.057 -4.944 1.00 13.36 O ANISOU 2847 O GLY B 75 2314 1257 1503 7 -493 196 O HETATM 2848 N NEH B 76 59.705 16.549 -3.648 1.00 14.57 N ANISOU 2848 N NEH B 76 2479 1279 1779 21 -563 254 N HETATM 2849 CA NEH B 76 59.295 17.158 -2.427 1.00 16.90 C ANISOU 2849 CA NEH B 76 2831 1595 1997 53 -543 293 C HETATM 2850 CB NEH B 76 60.497 17.279 -1.519 1.00 17.90 C ANISOU 2850 CB NEH B 76 2999 1665 2136 69 -611 272 C TER 2851 NEH B 76 ATOM 2852 N MET C 128 -10.449 22.964 -13.735 1.00 34.96 N ANISOU 2852 N MET C 128 3774 5483 4025 872 -592 502 N ATOM 2853 CA MET C 128 -9.005 22.805 -13.861 1.00 34.18 C ANISOU 2853 CA MET C 128 3777 5299 3911 828 -576 483 C ATOM 2854 C MET C 128 -8.461 21.887 -12.773 1.00 29.88 C ANISOU 2854 C MET C 128 3221 4723 3409 760 -547 416 C ATOM 2855 O MET C 128 -9.073 21.726 -11.717 1.00 31.51 O ANISOU 2855 O MET C 128 3367 4939 3668 770 -520 397 O ATOM 2856 CB MET C 128 -8.308 24.166 -13.809 1.00 35.77 C ANISOU 2856 CB MET C 128 4091 5379 4122 919 -534 541 C ATOM 2857 CG MET C 128 -8.675 25.087 -14.965 1.00 39.00 C ANISOU 2857 CG MET C 128 4529 5804 4483 982 -564 614 C ATOM 2858 SD MET C 128 -8.262 24.385 -16.576 1.00 54.19 S ANISOU 2858 SD MET C 128 6466 7815 6309 896 -627 612 S ATOM 2859 CE MET C 128 -6.482 24.249 -16.432 1.00 39.45 C ANISOU 2859 CE MET C 128 4717 5844 4430 841 -585 589 C ATOM 2860 N GLU C 129 -7.305 21.289 -13.037 1.00 24.59 N ANISOU 2860 N GLU C 129 2609 4021 2712 693 -550 382 N ATOM 2861 CA GLU C 129 -6.735 20.300 -12.131 1.00 24.84 C ANISOU 2861 CA GLU C 129 2641 4011 2785 610 -522 310 C ATOM 2862 C GLU C 129 -5.586 20.875 -11.307 1.00 22.15 C ANISOU 2862 C GLU C 129 2403 3523 2492 623 -450 302 C ATOM 2863 O GLU C 129 -4.943 21.843 -11.707 1.00 23.44 O ANISOU 2863 O GLU C 129 2648 3620 2637 669 -432 344 O ATOM 2864 CB GLU C 129 -6.254 19.073 -12.917 1.00 24.92 C ANISOU 2864 CB GLU C 129 2664 4052 2752 494 -553 249 C ATOM 2865 CG GLU C 129 -4.970 19.286 -13.714 1.00 22.55 C ANISOU 2865 CG GLU C 129 2470 3686 2411 476 -536 246 C ATOM 2866 CD GLU C 129 -5.188 19.988 -15.045 1.00 21.14 C ANISOU 2866 CD GLU C 129 2306 3576 2151 525 -581 308 C ATOM 2867 OE1 GLU C 129 -6.345 20.333 -15.374 1.00 16.90 O ANISOU 2867 OE1 GLU C 129 1698 3128 1596 575 -624 353 O ATOM 2868 OE2 GLU C 129 -4.191 20.192 -15.768 1.00 20.63 O ANISOU 2868 OE2 GLU C 129 2323 3473 2043 508 -565 312 O ATOM 2869 N MET C 130 -5.339 20.274 -10.150 1.00 14.01 N ANISOU 2869 N MET C 130 1364 2443 1515 574 -411 251 N ATOM 2870 CA MET C 130 -4.219 20.670 -9.308 1.00 20.96 C ANISOU 2870 CA MET C 130 2331 3199 2434 569 -350 235 C ATOM 2871 C MET C 130 -3.573 19.445 -8.679 1.00 16.47 C ANISOU 2871 C MET C 130 1765 2602 1892 473 -333 168 C ATOM 2872 O MET C 130 -4.267 18.577 -8.151 1.00 15.93 O ANISOU 2872 O MET C 130 1629 2579 1844 434 -343 141 O ATOM 2873 CB MET C 130 -4.674 21.646 -8.218 1.00 22.54 C ANISOU 2873 CB MET C 130 2531 3354 2677 653 -309 260 C ATOM 2874 CG MET C 130 -3.619 21.913 -7.153 1.00 26.82 C ANISOU 2874 CG MET C 130 3151 3782 3257 629 -250 230 C ATOM 2875 SD MET C 130 -4.213 22.941 -5.793 1.00 46.16 S ANISOU 2875 SD MET C 130 5606 6182 5749 719 -197 241 S ATOM 2876 CE MET C 130 -5.677 22.041 -5.292 1.00 47.43 C ANISOU 2876 CE MET C 130 5627 6470 5925 722 -216 229 C ATOM 2877 N PRO C 131 -2.236 19.369 -8.745 1.00 13.63 N ANISOU 2877 N PRO C 131 1482 2168 1530 434 -306 146 N ATOM 2878 CA PRO C 131 -1.486 18.266 -8.140 1.00 14.32 C ANISOU 2878 CA PRO C 131 1579 2219 1642 360 -288 90 C ATOM 2879 C PRO C 131 -1.173 18.501 -6.666 1.00 11.45 C ANISOU 2879 C PRO C 131 1230 1792 1329 367 -242 82 C ATOM 2880 O PRO C 131 -0.733 19.587 -6.284 1.00 11.88 O ANISOU 2880 O PRO C 131 1332 1791 1391 406 -211 104 O ATOM 2881 CB PRO C 131 -0.202 18.230 -8.965 1.00 13.76 C ANISOU 2881 CB PRO C 131 1573 2118 1538 333 -280 78 C ATOM 2882 CG PRO C 131 0.008 19.658 -9.357 1.00 15.72 C ANISOU 2882 CG PRO C 131 1867 2340 1766 388 -267 133 C ATOM 2883 CD PRO C 131 -1.370 20.247 -9.553 1.00 11.87 C ANISOU 2883 CD PRO C 131 1334 1906 1272 454 -297 177 C ATOM 2884 N ILE C 132 -1.400 17.476 -5.854 1.00 15.47 N ANISOU 2884 N ILE C 132 1705 2307 1865 322 -238 49 N ATOM 2885 CA ILE C 132 -1.092 17.522 -4.430 1.00 16.00 C ANISOU 2885 CA ILE C 132 1783 2325 1969 319 -198 40 C ATOM 2886 C ILE C 132 -0.458 16.210 -3.977 1.00 14.28 C ANISOU 2886 C ILE C 132 1574 2085 1767 253 -195 3 C ATOM 2887 O ILE C 132 -0.513 15.207 -4.688 1.00 14.03 O ANISOU 2887 O ILE C 132 1533 2073 1723 211 -222 -19 O ATOM 2888 CB ILE C 132 -2.353 17.775 -3.580 1.00 17.15 C ANISOU 2888 CB ILE C 132 1869 2511 2134 352 -188 55 C ATOM 2889 CG1 ILE C 132 -3.335 16.612 -3.743 1.00 18.51 C ANISOU 2889 CG1 ILE C 132 1968 2757 2308 302 -218 44 C ATOM 2890 CG2 ILE C 132 -3.012 19.090 -3.965 1.00 15.42 C ANISOU 2890 CG2 ILE C 132 1645 2309 1904 439 -187 95 C ATOM 2891 CD1 ILE C 132 -4.589 16.747 -2.910 1.00 17.00 C ANISOU 2891 CD1 ILE C 132 1700 2625 2133 325 -204 60 C ATOM 2892 N ACYS C 133 0.143 16.216 -2.793 0.68 12.93 N ANISOU 2892 N ACYS C 133 1425 1870 1618 246 -163 -4 N ATOM 2893 N BCYS C 133 0.141 16.231 -2.791 0.32 12.82 N ANISOU 2893 N BCYS C 133 1412 1856 1604 247 -162 -3 N ATOM 2894 CA ACYS C 133 0.635 14.978 -2.205 0.68 11.93 C ANISOU 2894 CA ACYS C 133 1306 1721 1507 197 -159 -27 C ATOM 2895 CA BCYS C 133 0.699 15.030 -2.178 0.32 12.28 C ANISOU 2895 CA BCYS C 133 1352 1762 1551 198 -158 -26 C ATOM 2896 C ACYS C 133 0.460 14.989 -0.692 0.68 10.93 C ANISOU 2896 C ACYS C 133 1171 1582 1400 194 -131 -20 C ATOM 2897 C BCYS C 133 0.403 15.007 -0.682 0.32 11.08 C ANISOU 2897 C BCYS C 133 1188 1603 1419 195 -131 -19 C ATOM 2898 O ACYS C 133 0.530 16.039 -0.054 0.68 11.53 O ANISOU 2898 O ACYS C 133 1259 1647 1473 229 -106 -10 O ATOM 2899 O BCYS C 133 0.331 16.055 -0.042 0.32 11.00 O ANISOU 2899 O BCYS C 133 1186 1587 1408 231 -106 -8 O ATOM 2900 CB ACYS C 133 2.103 14.746 -2.566 0.68 12.01 C ANISOU 2900 CB ACYS C 133 1362 1692 1508 188 -155 -43 C ATOM 2901 CB BCYS C 133 2.210 14.950 -2.411 0.32 14.70 C ANISOU 2901 CB BCYS C 133 1707 2028 1849 193 -150 -40 C ATOM 2902 SG ACYS C 133 3.255 15.899 -1.809 0.68 22.15 S ANISOU 2902 SG ACYS C 133 2683 2942 2790 208 -123 -33 S ATOM 2903 SG BCYS C 133 2.702 14.714 -4.133 0.32 26.40 S ANISOU 2903 SG BCYS C 133 3207 3525 3299 189 -172 -56 S ATOM 2904 N ALA C 134 0.228 13.810 -0.129 1.00 10.63 N ANISOU 2904 N ALA C 134 1121 1543 1376 151 -133 -25 N ATOM 2905 CA ALA C 134 0.058 13.666 1.308 1.00 9.32 C ANISOU 2905 CA ALA C 134 948 1374 1219 140 -106 -14 C ATOM 2906 C ALA C 134 1.425 13.607 1.972 1.00 9.21 C ANISOU 2906 C ALA C 134 982 1315 1202 141 -94 -17 C ATOM 2907 O ALA C 134 2.412 13.195 1.356 1.00 11.15 O ANISOU 2907 O ALA C 134 1255 1534 1446 139 -107 -29 O ATOM 2908 CB ALA C 134 -0.755 12.422 1.637 1.00 10.86 C ANISOU 2908 CB ALA C 134 1116 1584 1426 85 -112 -9 C ATOM 2909 N PHE C 135 1.482 14.039 3.226 1.00 10.70 N ANISOU 2909 N PHE C 135 1176 1507 1384 148 -68 -9 N ATOM 2910 CA PHE C 135 2.699 13.916 4.014 1.00 9.14 C ANISOU 2910 CA PHE C 135 1012 1285 1176 142 -63 -8 C ATOM 2911 C PHE C 135 2.333 13.683 5.472 1.00 11.16 C ANISOU 2911 C PHE C 135 1263 1556 1420 127 -41 7 C ATOM 2912 O PHE C 135 1.193 13.912 5.876 1.00 10.49 O ANISOU 2912 O PHE C 135 1150 1503 1334 128 -21 13 O ATOM 2913 CB PHE C 135 3.587 15.156 3.863 1.00 8.11 C ANISOU 2913 CB PHE C 135 908 1144 1030 163 -56 -21 C ATOM 2914 CG PHE C 135 3.082 16.371 4.594 1.00 12.00 C ANISOU 2914 CG PHE C 135 1410 1642 1508 183 -28 -27 C ATOM 2915 CD1 PHE C 135 2.120 17.188 4.025 1.00 11.84 C ANISOU 2915 CD1 PHE C 135 1379 1626 1494 218 -19 -27 C ATOM 2916 CD2 PHE C 135 3.589 16.709 5.840 1.00 10.53 C ANISOU 2916 CD2 PHE C 135 1246 1456 1298 170 -11 -34 C ATOM 2917 CE1 PHE C 135 1.664 18.310 4.689 1.00 14.32 C ANISOU 2917 CE1 PHE C 135 1711 1934 1796 250 12 -36 C ATOM 2918 CE2 PHE C 135 3.134 17.831 6.511 1.00 11.75 C ANISOU 2918 CE2 PHE C 135 1421 1607 1436 190 19 -49 C ATOM 2919 CZ PHE C 135 2.175 18.633 5.935 1.00 10.90 C ANISOU 2919 CZ PHE C 135 1309 1492 1340 234 34 -52 C ATOM 2920 N GLN C 136 3.302 13.219 6.253 1.00 10.04 N ANISOU 2920 N GLN C 136 1145 1404 1265 116 -44 17 N ATOM 2921 CA GLN C 136 3.062 12.893 7.650 1.00 13.13 C ANISOU 2921 CA GLN C 136 1539 1814 1635 98 -27 38 C ATOM 2922 C GLN C 136 4.319 13.040 8.495 1.00 14.42 C ANISOU 2922 C GLN C 136 1727 1982 1768 100 -34 42 C ATOM 2923 O GLN C 136 5.430 13.086 7.972 1.00 19.98 O ANISOU 2923 O GLN C 136 2440 2676 2476 111 -55 34 O ATOM 2924 CB GLN C 136 2.540 11.466 7.775 1.00 16.13 C ANISOU 2924 CB GLN C 136 1916 2182 2032 66 -33 68 C ATOM 2925 CG GLN C 136 3.588 10.432 7.409 1.00 22.49 C ANISOU 2925 CG GLN C 136 2751 2943 2851 70 -60 79 C ATOM 2926 CD GLN C 136 3.062 9.015 7.424 1.00 28.36 C ANISOU 2926 CD GLN C 136 3511 3649 3615 36 -64 106 C ATOM 2927 OE1 GLN C 136 2.119 8.681 6.711 1.00 30.86 O ANISOU 2927 OE1 GLN C 136 3813 3959 3953 5 -66 95 O ATOM 2928 NE2 GLN C 136 3.678 8.168 8.240 1.00 32.61 N ANISOU 2928 NE2 GLN C 136 4083 4163 4144 37 -69 143 N ATOM 2929 N LEU C 137 4.130 13.109 9.807 1.00 11.13 N ANISOU 2929 N LEU C 137 1318 1595 1317 87 -16 55 N ATOM 2930 CA LEU C 137 5.253 13.079 10.732 1.00 11.65 C ANISOU 2930 CA LEU C 137 1401 1681 1343 81 -30 66 C ATOM 2931 C LEU C 137 5.823 11.668 10.794 1.00 12.14 C ANISOU 2931 C LEU C 137 1469 1726 1417 84 -56 109 C ATOM 2932 O LEU C 137 5.115 10.697 10.531 1.00 15.38 O ANISOU 2932 O LEU C 137 1881 2106 1854 75 -53 133 O ATOM 2933 CB LEU C 137 4.826 13.544 12.124 1.00 13.24 C ANISOU 2933 CB LEU C 137 1613 1925 1492 66 -3 66 C ATOM 2934 CG LEU C 137 4.508 15.033 12.245 1.00 15.52 C ANISOU 2934 CG LEU C 137 1914 2220 1761 73 25 16 C ATOM 2935 CD1 LEU C 137 3.706 15.309 13.508 1.00 17.19 C ANISOU 2935 CD1 LEU C 137 2134 2474 1926 66 65 12 C ATOM 2936 CD2 LEU C 137 5.799 15.836 12.241 1.00 13.89 C ANISOU 2936 CD2 LEU C 137 1730 2014 1532 62 4 -13 C ATOM 2937 N PRO C 138 7.114 11.553 11.134 1.00 20.01 N ANISOU 2937 N PRO C 138 2469 2742 2390 97 -82 121 N ATOM 2938 CA PRO C 138 7.764 10.254 11.334 1.00 21.53 C ANISOU 2938 CA PRO C 138 2671 2920 2589 119 -107 168 C ATOM 2939 C PRO C 138 7.054 9.416 12.393 1.00 20.12 C ANISOU 2939 C PRO C 138 2517 2739 2391 100 -95 219 C ATOM 2940 O PRO C 138 6.508 9.968 13.349 1.00 18.39 O ANISOU 2940 O PRO C 138 2298 2563 2129 72 -74 218 O ATOM 2941 CB PRO C 138 9.173 10.634 11.798 1.00 23.62 C ANISOU 2941 CB PRO C 138 2919 3240 2816 134 -134 171 C ATOM 2942 CG PRO C 138 9.383 12.022 11.285 1.00 21.97 C ANISOU 2942 CG PRO C 138 2695 3050 2602 114 -126 114 C ATOM 2943 CD PRO C 138 8.041 12.677 11.350 1.00 20.68 C ANISOU 2943 CD PRO C 138 2547 2867 2442 90 -91 90 C ATOM 2944 N ASP C 139 7.056 8.099 12.211 1.00 22.40 N ANISOU 2944 N ASP C 139 2830 2974 2707 113 -105 261 N ATOM 2945 CA ASP C 139 6.513 7.181 13.205 1.00 25.72 C ANISOU 2945 CA ASP C 139 3283 3382 3107 90 -95 323 C ATOM 2946 C ASP C 139 7.651 6.401 13.848 1.00 23.54 C ANISOU 2946 C ASP C 139 3029 3107 2806 135 -127 380 C ATOM 2947 O ASP C 139 8.276 5.564 13.198 1.00 25.08 O ANISOU 2947 O ASP C 139 3243 3245 3039 182 -146 395 O ATOM 2948 CB ASP C 139 5.510 6.213 12.574 1.00 35.46 C ANISOU 2948 CB ASP C 139 4543 4541 4390 59 -80 334 C ATOM 2949 CG ASP C 139 4.425 6.921 11.787 1.00 45.57 C ANISOU 2949 CG ASP C 139 5788 5832 5696 24 -58 280 C ATOM 2950 OD1 ASP C 139 3.918 7.958 12.265 1.00 49.65 O ANISOU 2950 OD1 ASP C 139 6273 6411 6182 10 -35 259 O ATOM 2951 OD2 ASP C 139 4.081 6.438 10.687 1.00 49.29 O ANISOU 2951 OD2 ASP C 139 6265 6250 6214 16 -63 259 O ATOM 2952 N LEU C 140 7.926 6.676 15.119 1.00 18.09 N ANISOU 2952 N LEU C 140 2338 2486 2049 128 -133 413 N ATOM 2953 CA LEU C 140 9.025 6.008 15.804 1.00 16.34 C ANISOU 2953 CA LEU C 140 2129 2286 1795 177 -170 475 C ATOM 2954 C LEU C 140 8.640 4.582 16.189 1.00 16.88 C ANISOU 2954 C LEU C 140 2260 2281 1875 183 -166 556 C ATOM 2955 O LEU C 140 7.492 4.314 16.534 1.00 15.34 O ANISOU 2955 O LEU C 140 2091 2061 1676 124 -132 574 O ATOM 2956 CB LEU C 140 9.444 6.792 17.049 1.00 13.91 C ANISOU 2956 CB LEU C 140 1800 2086 1399 159 -183 482 C ATOM 2957 CG LEU C 140 9.737 8.284 16.880 1.00 16.98 C ANISOU 2957 CG LEU C 140 2145 2541 1767 134 -182 401 C ATOM 2958 CD1 LEU C 140 10.374 8.840 18.147 1.00 18.25 C ANISOU 2958 CD1 LEU C 140 2294 2805 1833 116 -206 411 C ATOM 2959 CD2 LEU C 140 10.624 8.537 15.671 1.00 19.81 C ANISOU 2959 CD2 LEU C 140 2467 2884 2175 170 -203 361 C ATOM 2960 N THR C 141 9.606 3.672 16.129 1.00 17.82 N ANISOU 2960 N THR C 141 2400 2365 2005 256 -198 607 N ATOM 2961 CA THR C 141 9.361 2.284 16.502 1.00 19.01 C ANISOU 2961 CA THR C 141 2628 2428 2167 271 -196 691 C ATOM 2962 C THR C 141 9.394 2.113 18.017 1.00 18.45 C ANISOU 2962 C THR C 141 2576 2419 2013 259 -205 773 C ATOM 2963 O THR C 141 9.082 1.043 18.536 1.00 23.42 O ANISOU 2963 O THR C 141 3278 2984 2638 257 -199 856 O ATOM 2964 CB THR C 141 10.388 1.336 15.864 1.00 20.13 C ANISOU 2964 CB THR C 141 2797 2498 2353 372 -223 717 C ATOM 2965 OG1 THR C 141 11.712 1.774 16.191 1.00 22.46 O ANISOU 2965 OG1 THR C 141 3031 2895 2609 445 -264 726 O ATOM 2966 CG2 THR C 141 10.223 1.318 14.352 1.00 20.33 C ANISOU 2966 CG2 THR C 141 2820 2451 2455 377 -207 638 C ATOM 2967 N VAL C 142 9.781 3.173 18.719 1.00 15.55 N ANISOU 2967 N VAL C 142 2154 2178 1577 246 -219 750 N ATOM 2968 CA VAL C 142 9.714 3.186 20.177 1.00 17.53 C ANISOU 2968 CA VAL C 142 2420 2508 1733 221 -225 815 C ATOM 2969 C VAL C 142 9.604 4.618 20.699 1.00 17.02 C ANISOU 2969 C VAL C 142 2302 2563 1603 169 -217 745 C ATOM 2970 O VAL C 142 10.232 5.532 20.165 1.00 18.51 O ANISOU 2970 O VAL C 142 2437 2795 1802 180 -234 672 O ATOM 2971 CB VAL C 142 10.938 2.491 20.810 1.00 18.89 C ANISOU 2971 CB VAL C 142 2601 2714 1863 307 -281 903 C ATOM 2972 CG1 VAL C 142 12.219 3.253 20.492 1.00 20.76 C ANISOU 2972 CG1 VAL C 142 2756 3042 2088 358 -327 854 C ATOM 2973 CG2 VAL C 142 10.750 2.357 22.308 1.00 20.33 C ANISOU 2973 CG2 VAL C 142 2811 2971 1941 277 -286 981 C ATOM 2974 N TYR C 143 8.788 4.800 21.735 1.00 16.20 N ANISOU 2974 N TYR C 143 2220 2507 1431 108 -186 766 N ATOM 2975 CA TYR C 143 8.558 6.109 22.350 1.00 15.98 C ANISOU 2975 CA TYR C 143 2159 2580 1332 59 -168 697 C ATOM 2976 C TYR C 143 7.912 7.106 21.394 1.00 16.80 C ANISOU 2976 C TYR C 143 2232 2658 1495 31 -130 592 C ATOM 2977 O TYR C 143 8.111 8.315 21.515 1.00 14.67 O ANISOU 2977 O TYR C 143 1935 2449 1191 13 -128 518 O ATOM 2978 CB TYR C 143 9.867 6.687 22.895 1.00 16.29 C ANISOU 2978 CB TYR C 143 2165 2724 1300 85 -225 688 C ATOM 2979 CG TYR C 143 10.480 5.831 23.977 1.00 17.44 C ANISOU 2979 CG TYR C 143 2335 2922 1368 116 -267 796 C ATOM 2980 CD1 TYR C 143 9.777 5.544 25.138 1.00 18.19 C ANISOU 2980 CD1 TYR C 143 2475 3057 1381 74 -241 853 C ATOM 2981 CD2 TYR C 143 11.754 5.300 23.833 1.00 17.87 C ANISOU 2981 CD2 TYR C 143 2366 2996 1428 193 -331 846 C ATOM 2982 CE1 TYR C 143 10.325 4.755 26.129 1.00 22.70 C ANISOU 2982 CE1 TYR C 143 3075 3677 1874 104 -281 962 C ATOM 2983 CE2 TYR C 143 12.313 4.511 24.819 1.00 19.04 C ANISOU 2983 CE2 TYR C 143 2537 3196 1503 234 -374 954 C ATOM 2984 CZ TYR C 143 11.593 4.241 25.966 1.00 19.77 C ANISOU 2984 CZ TYR C 143 2682 3319 1511 188 -350 1014 C ATOM 2985 OH TYR C 143 12.138 3.454 26.953 1.00 21.04 O ANISOU 2985 OH TYR C 143 2872 3505 1616 225 -387 1101 O ATOM 2986 N ASN C 144 7.128 6.597 20.453 1.00 16.87 N ANISOU 2986 N ASN C 144 2248 2572 1589 25 -102 588 N ATOM 2987 CA ASN C 144 6.423 7.458 19.517 1.00 17.48 C ANISOU 2987 CA ASN C 144 2295 2627 1721 5 -69 502 C ATOM 2988 C ASN C 144 5.439 8.385 20.231 1.00 16.70 C ANISOU 2988 C ASN C 144 2186 2591 1568 -41 -18 461 C ATOM 2989 O ASN C 144 5.299 9.555 19.874 1.00 13.34 O ANISOU 2989 O ASN C 144 1736 2184 1147 -41 -2 380 O ATOM 2990 CB ASN C 144 5.690 6.621 18.471 1.00 19.15 C ANISOU 2990 CB ASN C 144 2517 2739 2020 -1 -53 512 C ATOM 2991 CG ASN C 144 5.018 7.473 17.420 1.00 17.67 C ANISOU 2991 CG ASN C 144 2291 2536 1886 -13 -28 430 C ATOM 2992 OD1 ASN C 144 5.686 8.128 16.619 1.00 19.64 O ANISOU 2992 OD1 ASN C 144 2519 2779 2163 18 -50 378 O ATOM 2993 ND2 ASN C 144 3.691 7.473 17.415 1.00 16.99 N ANISOU 2993 ND2 ASN C 144 2194 2450 1810 -58 17 425 N ATOM 2994 N GLU C 145 4.773 7.858 21.252 1.00 14.56 N ANISOU 2994 N GLU C 145 1939 2354 1242 -75 12 518 N ATOM 2995 CA GLU C 145 3.793 8.633 22.005 1.00 20.45 C ANISOU 2995 CA GLU C 145 2673 3169 1928 -112 70 483 C ATOM 2996 C GLU C 145 4.456 9.828 22.685 1.00 18.52 C ANISOU 2996 C GLU C 145 2430 3002 1606 -105 60 422 C ATOM 2997 O GLU C 145 3.918 10.934 22.688 1.00 14.74 O ANISOU 2997 O GLU C 145 1939 2548 1115 -109 100 344 O ATOM 2998 CB GLU C 145 3.097 7.753 23.041 1.00 30.05 C ANISOU 2998 CB GLU C 145 3915 4416 3087 -155 104 566 C ATOM 2999 CG GLU C 145 1.909 8.409 23.719 1.00 40.36 C ANISOU 2999 CG GLU C 145 5199 5796 4338 -192 177 533 C ATOM 3000 CD GLU C 145 0.772 8.692 22.756 1.00 48.75 C ANISOU 3000 CD GLU C 145 6213 6830 5481 -200 221 486 C ATOM 3001 OE1 GLU C 145 -0.141 7.844 22.648 1.00 52.19 O ANISOU 3001 OE1 GLU C 145 6637 7249 5944 -245 251 537 O ATOM 3002 OE2 GLU C 145 0.793 9.763 22.108 1.00 52.03 O ANISOU 3002 OE2 GLU C 145 6601 7239 5928 -165 223 401 O ATOM 3003 N ASP C 146 5.635 9.598 23.250 1.00 17.31 N ANISOU 3003 N ASP C 146 2294 2886 1399 -92 5 457 N ATOM 3004 CA ASP C 146 6.401 10.666 23.880 1.00 15.47 C ANISOU 3004 CA ASP C 146 2062 2730 1087 -99 -16 398 C ATOM 3005 C ASP C 146 6.803 11.712 22.848 1.00 14.67 C ANISOU 3005 C ASP C 146 1939 2591 1046 -86 -27 307 C ATOM 3006 O ASP C 146 6.675 12.912 23.083 1.00 17.31 O ANISOU 3006 O ASP C 146 2282 2951 1344 -105 -3 225 O ATOM 3007 CB ASP C 146 7.638 10.100 24.580 1.00 20.87 C ANISOU 3007 CB ASP C 146 2752 3470 1705 -87 -84 463 C ATOM 3008 CG ASP C 146 7.282 9.165 25.720 1.00 26.50 C ANISOU 3008 CG ASP C 146 3500 4228 2342 -100 -75 560 C ATOM 3009 OD1 ASP C 146 6.989 9.664 26.824 1.00 24.82 O ANISOU 3009 OD1 ASP C 146 3306 4101 2022 -136 -49 543 O ATOM 3010 OD2 ASP C 146 7.288 7.934 25.511 1.00 31.70 O ANISOU 3010 OD2 ASP C 146 4173 4829 3042 -76 -89 652 O ATOM 3011 N PHE C 147 7.282 11.247 21.699 1.00 14.07 N ANISOU 3011 N PHE C 147 1839 2446 1059 -55 -59 321 N ATOM 3012 CA PHE C 147 7.639 12.137 20.602 1.00 13.34 C ANISOU 3012 CA PHE C 147 1727 2314 1028 -45 -67 247 C ATOM 3013 C PHE C 147 6.456 13.017 20.201 1.00 12.99 C ANISOU 3013 C PHE C 147 1686 2236 1013 -52 -6 182 C ATOM 3014 O PHE C 147 6.599 14.230 20.047 1.00 13.53 O ANISOU 3014 O PHE C 147 1764 2304 1072 -61 5 107 O ATOM 3015 CB PHE C 147 8.141 11.320 19.406 1.00 12.84 C ANISOU 3015 CB PHE C 147 1641 2185 1053 -6 -99 280 C ATOM 3016 CG PHE C 147 8.097 12.056 18.098 1.00 12.17 C ANISOU 3016 CG PHE C 147 1537 2045 1040 3 -90 216 C ATOM 3017 CD1 PHE C 147 8.801 13.238 17.923 1.00 11.95 C ANISOU 3017 CD1 PHE C 147 1504 2041 995 -14 -103 152 C ATOM 3018 CD2 PHE C 147 7.368 11.553 17.035 1.00 11.59 C ANISOU 3018 CD2 PHE C 147 1458 1898 1048 21 -72 222 C ATOM 3019 CE1 PHE C 147 8.762 13.912 16.714 1.00 11.43 C ANISOU 3019 CE1 PHE C 147 1429 1923 992 -8 -93 103 C ATOM 3020 CE2 PHE C 147 7.327 12.222 15.822 1.00 16.91 C ANISOU 3020 CE2 PHE C 147 2116 2529 1778 31 -66 169 C ATOM 3021 CZ PHE C 147 8.027 13.403 15.662 1.00 12.20 C ANISOU 3021 CZ PHE C 147 1517 1953 1164 20 -75 114 C ATOM 3022 N ARG C 148 5.285 12.406 20.056 1.00 13.23 N ANISOU 3022 N ARG C 148 1711 2240 1078 -50 35 213 N ATOM 3023 CA ARG C 148 4.094 13.137 19.632 1.00 14.53 C ANISOU 3023 CA ARG C 148 1864 2385 1273 -45 91 161 C ATOM 3024 C ARG C 148 3.609 14.112 20.704 1.00 18.80 C ANISOU 3024 C ARG C 148 2426 2985 1732 -56 139 111 C ATOM 3025 O ARG C 148 2.965 15.114 20.394 1.00 13.26 O ANISOU 3025 O ARG C 148 1725 2268 1047 -35 180 47 O ATOM 3026 CB ARG C 148 2.971 12.165 19.261 1.00 17.97 C ANISOU 3026 CB ARG C 148 2275 2795 1758 -51 118 210 C ATOM 3027 CG ARG C 148 3.301 11.264 18.080 1.00 18.74 C ANISOU 3027 CG ARG C 148 2362 2821 1939 -40 79 242 C ATOM 3028 CD ARG C 148 3.869 12.065 16.922 1.00 22.97 C ANISOU 3028 CD ARG C 148 2887 3316 2526 -11 55 184 C ATOM 3029 NE ARG C 148 4.072 11.234 15.740 1.00 30.26 N ANISOU 3029 NE ARG C 148 3800 4175 3522 2 26 206 N ATOM 3030 CZ ARG C 148 3.195 11.122 14.748 1.00 30.14 C ANISOU 3030 CZ ARG C 148 3762 4125 3565 1 40 192 C ATOM 3031 NH1 ARG C 148 2.053 11.794 14.794 1.00 22.05 N ANISOU 3031 NH1 ARG C 148 2711 3128 2538 -2 83 165 N ATOM 3032 NH2 ARG C 148 3.462 10.343 13.710 1.00 36.52 N ANISOU 3032 NH2 ARG C 148 4571 4876 4429 9 12 205 N ATOM 3033 N ASER C 149 3.913 13.807 21.962 0.42 17.05 N ANISOU 3033 N ASER C 149 2228 2831 1420 -82 135 141 N ATOM 3034 N BSER C 149 3.912 13.822 21.965 0.58 17.04 N ANISOU 3034 N BSER C 149 2226 2830 1417 -82 135 140 N ATOM 3035 CA ASER C 149 3.567 14.699 23.062 0.42 17.44 C ANISOU 3035 CA ASER C 149 2307 2945 1376 -95 180 88 C ATOM 3036 CA BSER C 149 3.543 14.732 23.044 0.58 17.09 C ANISOU 3036 CA BSER C 149 2263 2899 1333 -94 181 85 C ATOM 3037 C ASER C 149 4.357 16.002 22.963 0.42 16.79 C ANISOU 3037 C ASER C 149 2257 2849 1273 -98 162 -1 C ATOM 3038 C BSER C 149 4.357 16.020 22.955 0.58 14.68 C ANISOU 3038 C BSER C 149 1991 2582 1007 -98 162 -3 C ATOM 3039 O ASER C 149 3.818 17.082 23.195 0.42 15.00 O ANISOU 3039 O ASER C 149 2059 2619 1020 -88 212 -77 O ATOM 3040 O BSER C 149 3.838 17.107 23.191 0.58 15.00 O ANISOU 3040 O BSER C 149 2059 2618 1020 -88 212 -79 O ATOM 3041 CB ASER C 149 3.822 14.021 24.410 0.42 19.45 C ANISOU 3041 CB ASER C 149 2582 3282 1526 -127 171 146 C ATOM 3042 CB BSER C 149 3.740 14.073 24.410 0.58 19.20 C ANISOU 3042 CB BSER C 149 2551 3251 1495 -127 177 142 C ATOM 3043 OG ASER C 149 3.435 14.857 25.486 0.42 19.87 O ANISOU 3043 OG ASER C 149 2668 3403 1479 -142 220 89 O ATOM 3044 OG BSER C 149 5.085 14.175 24.839 0.58 20.66 O ANISOU 3044 OG BSER C 149 2756 3471 1624 -145 111 142 O ATOM 3045 N PHE C 150 5.634 15.895 22.611 1.00 14.40 N ANISOU 3045 N PHE C 150 1953 2538 983 -112 93 9 N ATOM 3046 CA PHE C 150 6.489 17.070 22.456 1.00 18.28 C ANISOU 3046 CA PHE C 150 2472 3017 1456 -135 71 -70 C ATOM 3047 C PHE C 150 6.041 17.915 21.263 1.00 13.83 C ANISOU 3047 C PHE C 150 1912 2363 980 -105 100 -124 C ATOM 3048 O PHE C 150 6.121 19.143 21.295 1.00 14.09 O ANISOU 3048 O PHE C 150 1992 2368 994 -117 120 -203 O ATOM 3049 CB PHE C 150 7.956 16.656 22.304 1.00 17.81 C ANISOU 3049 CB PHE C 150 2388 2987 1391 -158 -9 -36 C ATOM 3050 CG PHE C 150 8.635 16.342 23.609 1.00 25.65 C ANISOU 3050 CG PHE C 150 3390 4084 2273 -193 -46 -9 C ATOM 3051 CD1 PHE C 150 8.372 15.157 24.275 1.00 28.32 C ANISOU 3051 CD1 PHE C 150 3717 4466 2577 -178 -51 81 C ATOM 3052 CD2 PHE C 150 9.535 17.234 24.171 1.00 26.84 C ANISOU 3052 CD2 PHE C 150 3564 4289 2346 -249 -77 -70 C ATOM 3053 CE1 PHE C 150 8.992 14.864 25.479 1.00 26.89 C ANISOU 3053 CE1 PHE C 150 3545 4387 2285 -206 -88 115 C ATOM 3054 CE2 PHE C 150 10.160 16.948 25.373 1.00 28.05 C ANISOU 3054 CE2 PHE C 150 3720 4553 2386 -284 -118 -44 C ATOM 3055 CZ PHE C 150 9.887 15.761 26.028 1.00 25.83 C ANISOU 3055 CZ PHE C 150 3425 4320 2069 -257 -124 51 C ATOM 3056 N ILE C 151 5.568 17.251 20.213 1.00 14.84 N ANISOU 3056 N ILE C 151 1998 2442 1199 -69 100 -80 N ATOM 3057 CA ILE C 151 5.009 17.946 19.060 1.00 14.73 C ANISOU 3057 CA ILE C 151 1982 2351 1262 -34 126 -117 C ATOM 3058 C ILE C 151 3.768 18.740 19.460 1.00 17.91 C ANISOU 3058 C ILE C 151 2408 2752 1646 -2 198 -165 C ATOM 3059 O ILE C 151 3.600 19.894 19.062 1.00 13.19 O ANISOU 3059 O ILE C 151 1846 2101 1065 20 223 -227 O ATOM 3060 CB ILE C 151 4.640 16.966 17.932 1.00 15.66 C ANISOU 3060 CB ILE C 151 2048 2433 1468 -6 111 -60 C ATOM 3061 CG1 ILE C 151 5.896 16.286 17.378 1.00 13.15 C ANISOU 3061 CG1 ILE C 151 1712 2108 1176 -20 47 -23 C ATOM 3062 CG2 ILE C 151 3.892 17.691 16.818 1.00 15.74 C ANISOU 3062 CG2 ILE C 151 2053 2383 1546 34 139 -94 C ATOM 3063 CD1 ILE C 151 6.782 17.210 16.572 1.00 14.37 C ANISOU 3063 CD1 ILE C 151 1879 2228 1354 -29 24 -69 C ATOM 3064 N GLU C 152 2.909 18.117 20.260 1.00 17.05 N ANISOU 3064 N GLU C 152 2278 2699 1500 3 235 -133 N ATOM 3065 CA GLU C 152 1.660 18.740 20.679 1.00 18.70 C ANISOU 3065 CA GLU C 152 2491 2926 1688 42 311 -172 C ATOM 3066 C GLU C 152 1.909 19.996 21.517 1.00 19.77 C ANISOU 3066 C GLU C 152 2702 3063 1747 39 342 -259 C ATOM 3067 O GLU C 152 1.149 20.961 21.436 1.00 17.57 O ANISOU 3067 O GLU C 152 2447 2753 1474 92 399 -317 O ATOM 3068 CB GLU C 152 0.806 17.736 21.459 1.00 17.95 C ANISOU 3068 CB GLU C 152 2355 2909 1558 32 345 -114 C ATOM 3069 CG GLU C 152 -0.654 18.140 21.634 1.00 21.62 C ANISOU 3069 CG GLU C 152 2788 3405 2020 80 427 -137 C ATOM 3070 CD GLU C 152 -0.865 19.145 22.749 1.00 25.43 C ANISOU 3070 CD GLU C 152 3326 3926 2412 98 486 -211 C ATOM 3071 OE1 GLU C 152 -0.024 19.203 23.672 1.00 28.21 O ANISOU 3071 OE1 GLU C 152 3732 4308 2680 51 465 -227 O ATOM 3072 OE2 GLU C 152 -1.875 19.880 22.703 1.00 27.07 O ANISOU 3072 OE2 GLU C 152 3522 4137 2626 163 553 -256 O ATOM 3073 N ARG C 153 2.974 19.980 22.313 1.00 15.13 N ANISOU 3073 N ARG C 153 2153 2512 1085 -20 303 -269 N ATOM 3074 CA ARG C 153 3.297 21.109 23.183 1.00 15.98 C ANISOU 3074 CA ARG C 153 2341 2624 1106 -42 325 -358 C ATOM 3075 C ARG C 153 4.220 22.117 22.501 1.00 19.45 C ANISOU 3075 C ARG C 153 2831 2982 1575 -67 291 -417 C ATOM 3076 O ARG C 153 4.565 23.148 23.078 1.00 16.55 O ANISOU 3076 O ARG C 153 2544 2598 1146 -97 305 -500 O ATOM 3077 CB ARG C 153 3.943 20.615 24.480 1.00 16.61 C ANISOU 3077 CB ARG C 153 2435 2803 1073 -104 298 -342 C ATOM 3078 CG ARG C 153 3.024 19.792 25.371 1.00 17.09 C ANISOU 3078 CG ARG C 153 2466 2949 1079 -91 343 -291 C ATOM 3079 CD ARG C 153 3.697 19.480 26.703 1.00 21.29 C ANISOU 3079 CD ARG C 153 3026 3580 1482 -151 316 -280 C ATOM 3080 NE ARG C 153 4.996 18.844 26.506 1.00 22.01 N ANISOU 3080 NE ARG C 153 3097 3687 1580 -194 222 -224 N ATOM 3081 CZ ARG C 153 5.187 17.530 26.480 1.00 23.87 C ANISOU 3081 CZ ARG C 153 3283 3955 1833 -195 183 -117 C ATOM 3082 NH1 ARG C 153 4.163 16.706 26.652 1.00 26.69 N ANISOU 3082 NH1 ARG C 153 3612 4330 2201 -172 229 -54 N ATOM 3083 NH2 ARG C 153 6.403 17.038 26.286 1.00 24.83 N ANISOU 3083 NH2 ARG C 153 3383 4090 1959 -218 101 -72 N ATOM 3084 N ASP C 154 4.614 21.819 21.269 1.00 19.02 N ANISOU 3084 N ASP C 154 2737 2877 1614 -60 248 -375 N ATOM 3085 CA ASP C 154 5.545 22.673 20.541 1.00 22.86 C ANISOU 3085 CA ASP C 154 3264 3293 2130 -94 215 -417 C ATOM 3086 C ASP C 154 4.923 24.024 20.176 1.00 20.99 C ANISOU 3086 C ASP C 154 3100 2958 1916 -52 272 -490 C ATOM 3087 O ASP C 154 3.735 24.109 19.864 1.00 15.13 O ANISOU 3087 O ASP C 154 2343 2191 1215 30 324 -485 O ATOM 3088 CB ASP C 154 6.033 21.959 19.281 1.00 24.39 C ANISOU 3088 CB ASP C 154 3392 3464 2411 -89 165 -351 C ATOM 3089 CG ASP C 154 7.473 22.284 18.950 1.00 34.39 C ANISOU 3089 CG ASP C 154 4669 4726 3673 -159 107 -364 C ATOM 3090 OD1 ASP C 154 8.364 21.872 19.724 1.00 37.62 O ANISOU 3090 OD1 ASP C 154 5062 5215 4017 -214 63 -352 O ATOM 3091 OD2 ASP C 154 7.714 22.941 17.916 1.00 38.52 O ANISOU 3091 OD2 ASP C 154 5209 5174 4252 -159 105 -381 O ATOM 3092 N LEU C 155 5.729 25.081 20.231 1.00 15.66 N ANISOU 3092 N LEU C 155 2505 2230 1214 -108 261 -558 N ATOM 3093 CA LEU C 155 5.289 26.404 19.800 1.00 18.70 C ANISOU 3093 CA LEU C 155 2980 2498 1626 -71 310 -623 C ATOM 3094 C LEU C 155 5.373 26.537 18.281 1.00 18.81 C ANISOU 3094 C LEU C 155 2972 2433 1741 -43 291 -582 C ATOM 3095 O LEU C 155 6.144 25.828 17.629 1.00 16.37 O ANISOU 3095 O LEU C 155 2598 2155 1465 -83 233 -526 O ATOM 3096 CB LEU C 155 6.127 27.499 20.460 1.00 17.14 C ANISOU 3096 CB LEU C 155 2893 2262 1358 -158 307 -715 C ATOM 3097 CG LEU C 155 5.967 27.704 21.968 1.00 18.18 C ANISOU 3097 CG LEU C 155 3079 2455 1376 -183 337 -781 C ATOM 3098 CD1 LEU C 155 6.947 28.753 22.467 1.00 23.55 C ANISOU 3098 CD1 LEU C 155 3867 3093 1987 -292 321 -873 C ATOM 3099 CD2 LEU C 155 4.539 28.099 22.304 1.00 18.73 C ANISOU 3099 CD2 LEU C 155 3181 2492 1442 -71 428 -816 C ATOM 3100 N ILE C 156 4.581 27.451 17.729 1.00 15.73 N ANISOU 3100 N ILE C 156 2638 1944 1393 33 341 -609 N ATOM 3101 CA ILE C 156 4.618 27.753 16.303 1.00 17.69 C ANISOU 3101 CA ILE C 156 2883 2112 1725 62 327 -573 C ATOM 3102 C ILE C 156 5.494 28.970 16.035 1.00 20.77 C ANISOU 3102 C ILE C 156 3385 2397 2108 -7 322 -625 C ATOM 3103 O ILE C 156 5.509 29.914 16.822 1.00 23.41 O ANISOU 3103 O ILE C 156 3826 2678 2390 -27 358 -703 O ATOM 3104 CB ILE C 156 3.203 28.009 15.742 1.00 18.89 C ANISOU 3104 CB ILE C 156 3023 2223 1930 193 379 -555 C ATOM 3105 CG1 ILE C 156 2.389 26.714 15.746 1.00 19.10 C ANISOU 3105 CG1 ILE C 156 2925 2356 1976 240 375 -492 C ATOM 3106 CG2 ILE C 156 3.275 28.579 14.333 1.00 22.66 C ANISOU 3106 CG2 ILE C 156 3525 2606 2478 222 367 -525 C ATOM 3107 CD1 ILE C 156 3.091 25.554 15.076 1.00 21.32 C ANISOU 3107 CD1 ILE C 156 3121 2689 2289 184 308 -423 C ATOM 3108 N GLU C 157 6.230 28.945 14.928 1.00 19.63 N ANISOU 3108 N GLU C 157 3221 2224 2012 -48 281 -583 N ATOM 3109 CA GLU C 157 7.033 30.095 14.533 1.00 21.42 C ANISOU 3109 CA GLU C 157 3552 2348 2238 -122 279 -620 C ATOM 3110 C GLU C 157 6.120 31.192 13.991 1.00 20.95 C ANISOU 3110 C GLU C 157 3591 2152 2219 -28 335 -636 C ATOM 3111 O GLU C 157 5.750 31.184 12.814 1.00 16.14 O ANISOU 3111 O GLU C 157 2956 1503 1672 35 333 -578 O ATOM 3112 CB GLU C 157 8.080 29.700 13.490 1.00 22.52 C ANISOU 3112 CB GLU C 157 3631 2512 2412 -193 224 -564 C ATOM 3113 CG GLU C 157 9.197 30.720 13.329 1.00 27.76 C ANISOU 3113 CG GLU C 157 4384 3109 3055 -316 213 -603 C ATOM 3114 CD GLU C 157 9.963 30.951 14.621 1.00 35.36 C ANISOU 3114 CD GLU C 157 5384 4119 3934 -427 197 -674 C ATOM 3115 OE1 GLU C 157 10.070 30.004 15.430 1.00 34.92 O ANISOU 3115 OE1 GLU C 157 5244 4186 3837 -431 171 -666 O ATOM 3116 OE2 GLU C 157 10.455 32.080 14.828 1.00 39.46 O ANISOU 3116 OE2 GLU C 157 6019 4550 4424 -514 211 -737 O ATOM 3117 N GLN C 158 5.765 32.132 14.860 1.00 18.96 N ANISOU 3117 N GLN C 158 3454 1827 1924 -13 386 -716 N ATOM 3118 CA GLN C 158 4.767 33.152 14.549 1.00 23.96 C ANISOU 3118 CA GLN C 158 4185 2330 2589 105 449 -736 C ATOM 3119 C GLN C 158 5.131 34.020 13.355 1.00 23.33 C ANISOU 3119 C GLN C 158 4187 2118 2560 92 444 -708 C ATOM 3120 O GLN C 158 4.303 34.239 12.473 1.00 20.89 O ANISOU 3120 O GLN C 158 3874 1755 2307 210 464 -657 O ATOM 3121 CB GLN C 158 4.533 34.049 15.767 1.00 28.25 C ANISOU 3121 CB GLN C 158 4845 2817 3072 107 501 -835 C ATOM 3122 CG GLN C 158 3.701 33.394 16.848 1.00 35.20 C ANISOU 3122 CG GLN C 158 5661 3807 3905 174 534 -860 C ATOM 3123 CD GLN C 158 2.370 32.904 16.320 1.00 37.72 C ANISOU 3123 CD GLN C 158 5892 4162 4277 333 567 -801 C ATOM 3124 OE1 GLN C 158 1.669 33.623 15.607 1.00 37.88 O ANISOU 3124 OE1 GLN C 158 5942 4095 4356 437 593 -778 O ATOM 3125 NE2 GLN C 158 2.019 31.668 16.656 1.00 37.65 N ANISOU 3125 NE2 GLN C 158 5745 4301 4258 342 550 -757 N ATOM 3126 N SER C 159 6.361 34.522 13.340 1.00 19.81 N ANISOU 3126 N SER C 159 3811 1626 2089 -55 417 -736 N ATOM 3127 CA SER C 159 6.800 35.450 12.304 1.00 24.43 C ANISOU 3127 CA SER C 159 4494 2077 2712 -91 419 -713 C ATOM 3128 C SER C 159 6.765 34.802 10.922 1.00 23.26 C ANISOU 3128 C SER C 159 4238 1974 2625 -52 383 -608 C ATOM 3129 O SER C 159 6.436 35.451 9.930 1.00 21.52 O ANISOU 3129 O SER C 159 4080 1649 2448 7 400 -564 O ATOM 3130 CB SER C 159 8.210 35.964 12.608 1.00 24.85 C ANISOU 3130 CB SER C 159 4594 2122 2726 -279 386 -748 C ATOM 3131 OG SER C 159 9.155 34.909 12.543 1.00 22.99 O ANISOU 3131 OG SER C 159 4240 2025 2469 -381 328 -725 O ATOM 3132 N MET C 160 7.104 33.518 10.865 1.00 22.32 N ANISOU 3132 N MET C 160 3967 2009 2505 -81 335 -567 N ATOM 3133 CA MET C 160 7.095 32.780 9.608 1.00 22.38 C ANISOU 3133 CA MET C 160 3870 2071 2561 -48 301 -478 C ATOM 3134 C MET C 160 5.669 32.548 9.125 1.00 20.56 C ANISOU 3134 C MET C 160 3598 1839 2374 117 324 -435 C ATOM 3135 O MET C 160 5.366 32.723 7.943 1.00 21.07 O ANISOU 3135 O MET C 160 3662 1865 2479 172 319 -374 O ATOM 3136 CB MET C 160 7.824 31.443 9.765 1.00 15.32 C ANISOU 3136 CB MET C 160 2835 1333 1653 -115 248 -455 C ATOM 3137 CG MET C 160 7.832 30.587 8.512 1.00 17.95 C ANISOU 3137 CG MET C 160 3063 1725 2030 -82 216 -375 C ATOM 3138 SD MET C 160 8.816 29.087 8.700 1.00 24.26 S ANISOU 3138 SD MET C 160 3719 2685 2813 -155 159 -352 S ATOM 3139 CE MET C 160 10.401 29.773 9.180 1.00 25.31 C ANISOU 3139 CE MET C 160 3902 2818 2896 -321 141 -397 C ATOM 3140 N LEU C 161 4.798 32.152 10.048 1.00 19.97 N ANISOU 3140 N LEU C 161 3485 1818 2283 191 348 -464 N ATOM 3141 CA LEU C 161 3.403 31.878 9.723 1.00 19.14 C ANISOU 3141 CA LEU C 161 3321 1737 2213 341 370 -427 C ATOM 3142 C LEU C 161 2.712 33.096 9.122 1.00 21.91 C ANISOU 3142 C LEU C 161 3778 1954 2593 445 411 -418 C ATOM 3143 O LEU C 161 2.053 32.998 8.088 1.00 20.48 O ANISOU 3143 O LEU C 161 3551 1778 2453 534 401 -352 O ATOM 3144 CB LEU C 161 2.644 31.418 10.967 1.00 18.21 C ANISOU 3144 CB LEU C 161 3158 1696 2063 389 401 -469 C ATOM 3145 CG LEU C 161 1.137 31.230 10.782 1.00 19.69 C ANISOU 3145 CG LEU C 161 3279 1921 2280 541 433 -439 C ATOM 3146 CD1 LEU C 161 0.853 30.104 9.795 1.00 17.07 C ANISOU 3146 CD1 LEU C 161 2811 1686 1989 555 385 -359 C ATOM 3147 CD2 LEU C 161 0.453 30.969 12.117 1.00 20.07 C ANISOU 3147 CD2 LEU C 161 3302 2037 2285 578 478 -489 C ATOM 3148 N VAL C 162 2.864 34.245 9.773 1.00 19.10 N ANISOU 3148 N VAL C 162 3568 1476 2212 436 455 -485 N ATOM 3149 CA VAL C 162 2.205 35.461 9.310 1.00 26.07 C ANISOU 3149 CA VAL C 162 4565 2217 3122 544 497 -476 C ATOM 3150 C VAL C 162 2.839 36.004 8.031 1.00 23.73 C ANISOU 3150 C VAL C 162 4333 1828 2855 499 471 -415 C ATOM 3151 O VAL C 162 2.136 36.478 7.141 1.00 21.44 O ANISOU 3151 O VAL C 162 4045 1500 2602 604 474 -350 O ATOM 3152 CB VAL C 162 2.222 36.557 10.390 1.00 33.25 C ANISOU 3152 CB VAL C 162 5578 3053 4004 521 534 -550 C ATOM 3153 CG1 VAL C 162 1.261 36.202 11.515 1.00 33.91 C ANISOU 3153 CG1 VAL C 162 5596 3223 4064 606 570 -596 C ATOM 3154 CG2 VAL C 162 3.628 36.760 10.923 1.00 37.58 C ANISOU 3154 CG2 VAL C 162 6199 3571 4507 337 514 -608 C ATOM 3155 N ALA C 163 4.163 35.926 7.936 1.00 23.39 N ANISOU 3155 N ALA C 163 4315 1781 2791 334 440 -427 N ATOM 3156 CA ALA C 163 4.865 36.428 6.758 1.00 24.50 C ANISOU 3156 CA ALA C 163 4513 1845 2950 271 420 -369 C ATOM 3157 C ALA C 163 4.484 35.652 5.495 1.00 22.21 C ANISOU 3157 C ALA C 163 4100 1644 2694 336 382 -272 C ATOM 3158 O ALA C 163 4.181 36.246 4.458 1.00 22.83 O ANISOU 3158 O ALA C 163 4233 1644 2796 398 386 -208 O ATOM 3159 CB ALA C 163 6.369 36.377 6.975 1.00 24.47 C ANISOU 3159 CB ALA C 163 4524 1861 2914 72 392 -399 C ATOM 3160 N LEU C 164 4.498 34.326 5.585 1.00 19.19 N ANISOU 3160 N LEU C 164 3559 1422 2309 321 344 -261 N ATOM 3161 CA LEU C 164 4.213 33.486 4.427 1.00 16.21 C ANISOU 3161 CA LEU C 164 3066 1136 1956 364 305 -183 C ATOM 3162 C LEU C 164 2.730 33.497 4.057 1.00 20.77 C ANISOU 3162 C LEU C 164 3606 1723 2561 535 317 -143 C ATOM 3163 O LEU C 164 2.379 33.375 2.883 1.00 21.95 O ANISOU 3163 O LEU C 164 3719 1893 2728 588 293 -72 O ATOM 3164 CB LEU C 164 4.676 32.048 4.676 1.00 15.25 C ANISOU 3164 CB LEU C 164 2801 1169 1826 296 264 -188 C ATOM 3165 CG LEU C 164 6.188 31.814 4.760 1.00 16.84 C ANISOU 3165 CG LEU C 164 2997 1399 2001 138 238 -205 C ATOM 3166 CD1 LEU C 164 6.492 30.334 4.922 1.00 16.03 C ANISOU 3166 CD1 LEU C 164 2752 1444 1896 107 199 -199 C ATOM 3167 CD2 LEU C 164 6.899 32.382 3.535 1.00 15.80 C ANISOU 3167 CD2 LEU C 164 2916 1212 1874 83 230 -156 C ATOM 3168 N GLU C 165 1.859 33.639 5.052 1.00 16.89 N ANISOU 3168 N GLU C 165 3118 1232 2068 621 355 -189 N ATOM 3169 CA GLU C 165 0.428 33.728 4.778 1.00 23.94 C ANISOU 3169 CA GLU C 165 3966 2146 2984 789 372 -154 C ATOM 3170 C GLU C 165 0.072 35.076 4.149 1.00 24.63 C ANISOU 3170 C GLU C 165 4185 2085 3087 885 400 -120 C ATOM 3171 O GLU C 165 -0.727 35.137 3.213 1.00 25.91 O ANISOU 3171 O GLU C 165 4292 2284 3269 981 379 -48 O ATOM 3172 CB GLU C 165 -0.390 33.500 6.054 1.00 21.55 C ANISOU 3172 CB GLU C 165 3622 1897 2670 854 412 -213 C ATOM 3173 CG GLU C 165 -0.509 32.032 6.448 1.00 21.77 C ANISOU 3173 CG GLU C 165 3492 2089 2689 806 382 -214 C ATOM 3174 CD GLU C 165 -1.532 31.798 7.550 1.00 26.35 C ANISOU 3174 CD GLU C 165 4017 2737 3256 886 426 -254 C ATOM 3175 OE1 GLU C 165 -1.805 32.740 8.327 1.00 25.45 O ANISOU 3175 OE1 GLU C 165 4002 2541 3126 944 484 -308 O ATOM 3176 OE2 GLU C 165 -2.065 30.671 7.636 1.00 25.25 O ANISOU 3176 OE2 GLU C 165 3741 2732 3120 887 407 -232 O ATOM 3177 N GLN C 166 0.674 36.149 4.654 1.00 23.68 N ANISOU 3177 N GLN C 166 4200 1842 2954 820 429 -165 N ATOM 3178 CA GLN C 166 0.443 37.478 4.096 1.00 29.49 C ANISOU 3178 CA GLN C 166 5038 2464 3704 865 442 -128 C ATOM 3179 C GLN C 166 0.935 37.558 2.653 1.00 27.86 C ANISOU 3179 C GLN C 166 4852 2227 3504 835 407 -42 C ATOM 3180 O GLN C 166 0.303 38.188 1.808 1.00 30.02 O ANISOU 3180 O GLN C 166 5140 2474 3793 926 401 25 O ATOM 3181 CB GLN C 166 1.130 38.554 4.942 1.00 35.56 C ANISOU 3181 CB GLN C 166 5951 3106 4453 778 477 -198 C ATOM 3182 CG GLN C 166 0.457 38.836 6.276 1.00 45.75 C ANISOU 3182 CG GLN C 166 7245 4405 5732 835 520 -275 C ATOM 3183 CD GLN C 166 1.080 40.016 7.001 1.00 53.64 C ANISOU 3183 CD GLN C 166 8396 5273 6712 755 551 -341 C ATOM 3184 OE1 GLN C 166 2.132 40.519 6.604 1.00 56.17 O ANISOU 3184 OE1 GLN C 166 8810 5509 7025 633 540 -334 O ATOM 3185 NE2 GLN C 166 0.429 40.466 8.067 1.00 54.90 N ANISOU 3185 NE2 GLN C 166 8578 5422 6861 820 592 -404 N ATOM 3186 N ALA C 167 2.060 36.906 2.378 1.00 25.76 N ANISOU 3186 N ALA C 167 4589 1975 3225 707 383 -43 N ATOM 3187 CA ALA C 167 2.650 36.918 1.043 1.00 25.83 C ANISOU 3187 CA ALA C 167 4619 1964 3233 660 353 37 C ATOM 3188 C ALA C 167 1.904 36.001 0.075 1.00 24.67 C ANISOU 3188 C ALA C 167 4324 1954 3094 747 308 109 C ATOM 3189 O ALA C 167 2.163 36.016 -1.127 1.00 24.94 O ANISOU 3189 O ALA C 167 4358 1998 3120 731 280 182 O ATOM 3190 CB ALA C 167 4.121 36.523 1.114 1.00 23.06 C ANISOU 3190 CB ALA C 167 4257 1646 2858 463 333 9 C ATOM 3191 N GLY C 168 0.982 35.202 0.602 1.00 23.10 N ANISOU 3191 N GLY C 168 4002 1871 2906 830 302 86 N ATOM 3192 CA GLY C 168 0.178 34.318 -0.224 1.00 21.50 C ANISOU 3192 CA GLY C 168 3656 1804 2708 904 258 143 C ATOM 3193 C GLY C 168 0.882 33.034 -0.625 1.00 21.08 C ANISOU 3193 C GLY C 168 3488 1881 2642 786 211 144 C ATOM 3194 O GLY C 168 0.467 32.360 -1.564 1.00 23.64 O ANISOU 3194 O GLY C 168 3718 2302 2962 816 169 194 O ATOM 3195 N AARG C 169 1.950 32.697 0.091 0.51 19.61 N ANISOU 3195 N AARG C 169 3309 1696 2445 654 216 86 N ATOM 3196 N BARG C 169 1.963 32.710 0.079 0.49 19.65 N ANISOU 3196 N BARG C 169 3317 1701 2451 653 216 86 N ATOM 3197 CA AARG C 169 2.724 31.496 -0.210 0.51 18.01 C ANISOU 3197 CA AARG C 169 3006 1606 2231 549 177 82 C ATOM 3198 CA BARG C 169 2.734 31.499 -0.191 0.49 18.04 C ANISOU 3198 CA BARG C 169 3011 1610 2236 548 177 81 C ATOM 3199 C AARG C 169 2.271 30.299 0.626 0.51 17.16 C ANISOU 3199 C AARG C 169 2778 1613 2131 556 166 41 C ATOM 3200 C BARG C 169 2.230 30.303 0.613 0.49 17.15 C ANISOU 3200 C BARG C 169 2775 1611 2129 559 166 43 C ATOM 3201 O AARG C 169 2.378 29.155 0.190 0.51 14.38 O ANISOU 3201 O AARG C 169 2324 1363 1777 523 129 53 O ATOM 3202 O BARG C 169 2.269 29.165 0.146 0.49 14.57 O ANISOU 3202 O BARG C 169 2345 1389 1802 533 129 57 O ATOM 3203 CB AARG C 169 4.219 31.750 0.015 0.51 17.69 C ANISOU 3203 CB AARG C 169 3028 1521 2172 403 184 53 C ATOM 3204 CB BARG C 169 4.216 31.734 0.115 0.49 17.54 C ANISOU 3204 CB BARG C 169 3009 1503 2154 402 185 48 C ATOM 3205 CG AARG C 169 4.760 32.975 -0.699 0.51 19.55 C ANISOU 3205 CG AARG C 169 3395 1634 2398 370 202 91 C ATOM 3206 CG BARG C 169 4.849 32.859 -0.681 0.49 19.21 C ANISOU 3206 CG BARG C 169 3342 1603 2354 359 199 88 C ATOM 3207 CD AARG C 169 4.535 32.888 -2.196 0.51 19.26 C ANISOU 3207 CD AARG C 169 3336 1628 2354 411 176 174 C ATOM 3208 CD BARG C 169 4.735 32.606 -2.175 0.49 19.10 C ANISOU 3208 CD BARG C 169 3290 1636 2331 386 170 166 C ATOM 3209 NE AARG C 169 5.281 31.789 -2.800 0.51 17.23 N ANISOU 3209 NE AARG C 169 2976 1490 2080 329 142 180 N ATOM 3210 NE BARG C 169 3.487 33.137 -2.710 0.49 21.15 N ANISOU 3210 NE BARG C 169 3575 1858 2601 532 170 220 N ATOM 3211 CZ AARG C 169 5.277 31.515 -4.101 0.51 17.13 C ANISOU 3211 CZ AARG C 169 2932 1529 2048 341 118 240 C ATOM 3212 CZ BARG C 169 3.398 34.234 -3.455 0.49 26.13 C ANISOU 3212 CZ BARG C 169 4320 2383 3226 571 184 281 C ATOM 3213 NH1AARG C 169 4.563 32.261 -4.931 0.51 18.37 N ANISOU 3213 NH1AARG C 169 3148 1632 2199 428 117 306 N ATOM 3214 NH1BARG C 169 2.214 34.643 -3.889 0.49 24.15 N ANISOU 3214 NH1BARG C 169 4078 2114 2984 720 180 333 N ATOM 3215 NH2AARG C 169 5.985 30.499 -4.572 0.51 15.24 N ANISOU 3215 NH2AARG C 169 2606 1395 1792 271 94 233 N ATOM 3216 NH2BARG C 169 4.488 34.920 -3.774 0.49 31.49 N ANISOU 3216 NH2BARG C 169 5101 2978 3888 460 201 295 N ATOM 3217 N LEU C 170 1.772 30.570 1.829 1.00 17.95 N ANISOU 3217 N LEU C 170 2897 1689 2234 595 201 -7 N ATOM 3218 CA LEU C 170 1.358 29.511 2.740 1.00 16.81 C ANISOU 3218 CA LEU C 170 2651 1646 2090 593 197 -42 C ATOM 3219 C LEU C 170 -0.149 29.510 2.963 1.00 17.67 C ANISOU 3219 C LEU C 170 2704 1796 2213 723 215 -32 C ATOM 3220 O LEU C 170 -0.738 30.539 3.286 1.00 21.35 O ANISOU 3220 O LEU C 170 3241 2187 2683 812 256 -41 O ATOM 3221 CB LEU C 170 2.088 29.652 4.080 1.00 15.68 C ANISOU 3221 CB LEU C 170 2557 1475 1927 515 223 -110 C ATOM 3222 CG LEU C 170 1.766 28.642 5.189 1.00 13.61 C ANISOU 3222 CG LEU C 170 2209 1309 1654 503 226 -145 C ATOM 3223 CD1 LEU C 170 2.158 27.236 4.770 1.00 12.75 C ANISOU 3223 CD1 LEU C 170 1994 1302 1550 444 178 -120 C ATOM 3224 CD2 LEU C 170 2.459 29.026 6.486 1.00 13.35 C ANISOU 3224 CD2 LEU C 170 2244 1240 1588 435 251 -211 C ATOM 3225 N ASN C 171 -0.761 28.343 2.782 1.00 16.77 N ANISOU 3225 N ASN C 171 2463 1802 2106 731 187 -14 N ATOM 3226 CA ASN C 171 -2.184 28.149 3.039 1.00 16.73 C ANISOU 3226 CA ASN C 171 2375 1870 2112 835 201 -4 C ATOM 3227 C ASN C 171 -3.108 28.920 2.096 1.00 17.12 C ANISOU 3227 C ASN C 171 2427 1905 2173 960 197 50 C ATOM 3228 O ASN C 171 -4.243 29.228 2.451 1.00 17.77 O ANISOU 3228 O ASN C 171 2469 2020 2262 1071 225 53 O ATOM 3229 CB ASN C 171 -2.503 28.518 4.491 1.00 16.85 C ANISOU 3229 CB ASN C 171 2419 1867 2116 863 258 -60 C ATOM 3230 CG ASN C 171 -1.840 27.579 5.481 1.00 15.15 C ANISOU 3230 CG ASN C 171 2174 1700 1882 754 256 -102 C ATOM 3231 OD1 ASN C 171 -1.704 26.385 5.216 1.00 12.91 O ANISOU 3231 OD1 ASN C 171 1804 1497 1602 692 217 -83 O ATOM 3232 ND2 ASN C 171 -1.416 28.114 6.620 1.00 13.91 N ANISOU 3232 ND2 ASN C 171 2095 1490 1701 730 296 -158 N ATOM 3233 N TRP C 172 -2.626 29.224 0.895 1.00 16.97 N ANISOU 3233 N TRP C 172 2450 1846 2152 946 164 96 N ATOM 3234 CA TRP C 172 -3.483 29.824 -0.122 1.00 19.68 C ANISOU 3234 CA TRP C 172 2786 2194 2499 1063 148 160 C ATOM 3235 C TRP C 172 -4.502 28.794 -0.597 1.00 18.40 C ANISOU 3235 C TRP C 172 2468 2187 2338 1091 106 189 C ATOM 3236 O TRP C 172 -5.580 29.138 -1.080 1.00 22.11 O ANISOU 3236 O TRP C 172 2887 2704 2809 1208 96 234 O ATOM 3237 CB TRP C 172 -2.657 30.341 -1.305 1.00 15.99 C ANISOU 3237 CB TRP C 172 2404 1653 2018 1027 122 207 C ATOM 3238 CG TRP C 172 -1.801 29.285 -1.942 1.00 14.56 C ANISOU 3238 CG TRP C 172 2173 1536 1822 903 77 207 C ATOM 3239 CD1 TRP C 172 -0.483 29.040 -1.692 1.00 13.86 C ANISOU 3239 CD1 TRP C 172 2131 1410 1726 778 82 172 C ATOM 3240 CD2 TRP C 172 -2.209 28.324 -2.925 1.00 15.51 C ANISOU 3240 CD2 TRP C 172 2189 1775 1930 894 24 240 C ATOM 3241 NE1 TRP C 172 -0.043 27.990 -2.459 1.00 15.53 N ANISOU 3241 NE1 TRP C 172 2273 1703 1923 707 40 182 N ATOM 3242 CE2 TRP C 172 -1.081 27.533 -3.225 1.00 16.14 C ANISOU 3242 CE2 TRP C 172 2265 1871 1996 771 4 219 C ATOM 3243 CE3 TRP C 172 -3.415 28.059 -3.582 1.00 18.27 C ANISOU 3243 CE3 TRP C 172 2445 2223 2274 978 -11 282 C ATOM 3244 CZ2 TRP C 172 -1.125 26.493 -4.155 1.00 18.37 C ANISOU 3244 CZ2 TRP C 172 2469 2250 2261 732 -44 233 C ATOM 3245 CZ3 TRP C 172 -3.457 27.026 -4.506 1.00 20.13 C ANISOU 3245 CZ3 TRP C 172 2599 2561 2489 924 -65 296 C ATOM 3246 CH2 TRP C 172 -2.317 26.256 -4.783 1.00 19.87 C ANISOU 3246 CH2 TRP C 172 2579 2527 2443 803 -78 268 C ATOM 3247 N TRP C 173 -4.144 27.524 -0.440 1.00 17.08 N ANISOU 3247 N TRP C 173 2226 2097 2167 982 80 162 N ATOM 3248 CA TRP C 173 -4.933 26.404 -0.944 1.00 19.42 C ANISOU 3248 CA TRP C 173 2386 2531 2460 971 36 181 C ATOM 3249 C TRP C 173 -6.212 26.138 -0.154 1.00 23.97 C ANISOU 3249 C TRP C 173 2858 3201 3047 1035 58 172 C ATOM 3250 O TRP C 173 -7.121 25.473 -0.650 1.00 22.45 O ANISOU 3250 O TRP C 173 2549 3129 2852 1046 23 197 O ATOM 3251 CB TRP C 173 -4.075 25.137 -0.953 1.00 18.51 C ANISOU 3251 CB TRP C 173 2246 2446 2340 833 9 151 C ATOM 3252 CG TRP C 173 -3.327 24.918 0.330 1.00 22.47 C ANISOU 3252 CG TRP C 173 2788 2902 2849 767 47 98 C ATOM 3253 CD1 TRP C 173 -3.817 24.378 1.483 1.00 25.34 C ANISOU 3253 CD1 TRP C 173 3098 3314 3218 757 74 68 C ATOM 3254 CD2 TRP C 173 -1.954 25.238 0.590 1.00 20.37 C ANISOU 3254 CD2 TRP C 173 2619 2545 2576 698 60 72 C ATOM 3255 NE1 TRP C 173 -2.836 24.342 2.445 1.00 24.64 N ANISOU 3255 NE1 TRP C 173 3071 3168 3123 691 99 27 N ATOM 3256 CE2 TRP C 173 -1.681 24.863 1.921 1.00 21.35 C ANISOU 3256 CE2 TRP C 173 2743 2669 2700 653 89 27 C ATOM 3257 CE3 TRP C 173 -0.929 25.806 -0.173 1.00 16.45 C ANISOU 3257 CE3 TRP C 173 2205 1976 2069 663 50 86 C ATOM 3258 CZ2 TRP C 173 -0.427 25.035 2.506 1.00 20.14 C ANISOU 3258 CZ2 TRP C 173 2663 2454 2536 578 102 -6 C ATOM 3259 CZ3 TRP C 173 0.317 25.975 0.408 1.00 18.62 C ANISOU 3259 CZ3 TRP C 173 2548 2190 2337 583 68 52 C ATOM 3260 CH2 TRP C 173 0.556 25.591 1.735 1.00 17.85 C ANISOU 3260 CH2 TRP C 173 2443 2100 2239 542 90 6 C ATOM 3261 N VAL C 174 -6.272 26.650 1.072 1.00 27.18 N ANISOU 3261 N VAL C 174 3306 3561 3461 1069 119 133 N ATOM 3262 CA VAL C 174 -7.368 26.346 1.987 1.00 33.49 C ANISOU 3262 CA VAL C 174 4007 4454 4264 1116 153 117 C ATOM 3263 C VAL C 174 -8.745 26.638 1.391 1.00 37.83 C ANISOU 3263 C VAL C 174 4465 5094 4816 1205 137 162 C ATOM 3264 O VAL C 174 -9.698 25.892 1.618 1.00 37.04 O ANISOU 3264 O VAL C 174 4240 5120 4715 1187 131 164 O ATOM 3265 CB VAL C 174 -7.221 27.132 3.306 1.00 37.82 C ANISOU 3265 CB VAL C 174 4637 4924 4809 1157 227 67 C ATOM 3266 CG1 VAL C 174 -8.448 26.937 4.184 1.00 38.85 C ANISOU 3266 CG1 VAL C 174 4666 5159 4937 1207 267 55 C ATOM 3267 CG2 VAL C 174 -5.961 26.702 4.040 1.00 38.96 C ANISOU 3267 CG2 VAL C 174 4855 5006 4943 1027 234 19 C ATOM 3268 N SER C 175 -8.842 27.716 0.619 1.00 43.82 N ANISOU 3268 N SER C 175 5290 5785 5574 1276 127 197 N ATOM 3269 CA SER C 175 -10.117 28.131 0.043 1.00 48.70 C ANISOU 3269 CA SER C 175 5834 6478 6190 1353 109 239 C ATOM 3270 C SER C 175 -10.472 27.362 -1.230 1.00 49.63 C ANISOU 3270 C SER C 175 5860 6704 6294 1312 34 283 C ATOM 3271 O SER C 175 -11.640 27.055 -1.470 1.00 54.11 O ANISOU 3271 O SER C 175 6311 7392 6855 1330 14 303 O ATOM 3272 CB SER C 175 -10.101 29.633 -0.248 1.00 52.29 C ANISOU 3272 CB SER C 175 6404 6815 6648 1451 131 262 C ATOM 3273 OG SER C 175 -9.022 29.973 -1.100 1.00 54.79 O ANISOU 3273 OG SER C 175 6828 7032 6958 1421 104 286 O ATOM 3274 N VAL C 176 -9.468 27.053 -2.043 1.00 46.89 N ANISOU 3274 N VAL C 176 5565 6315 5936 1253 -6 296 N ATOM 3275 CA VAL C 176 -9.712 26.378 -3.316 1.00 45.41 C ANISOU 3275 CA VAL C 176 5307 6221 5726 1210 -78 332 C ATOM 3276 C VAL C 176 -9.740 24.858 -3.158 1.00 42.71 C ANISOU 3276 C VAL C 176 4864 5982 5381 1101 -106 302 C ATOM 3277 O VAL C 176 -10.113 24.137 -4.084 1.00 40.93 O ANISOU 3277 O VAL C 176 4567 5851 5135 1051 -165 318 O ATOM 3278 CB VAL C 176 -8.652 26.761 -4.369 1.00 44.06 C ANISOU 3278 CB VAL C 176 5239 5966 5535 1197 -108 362 C ATOM 3279 CG1 VAL C 176 -8.662 28.266 -4.602 1.00 43.66 C ANISOU 3279 CG1 VAL C 176 5295 5809 5487 1294 -82 399 C ATOM 3280 CG2 VAL C 176 -7.274 26.293 -3.935 1.00 42.04 C ANISOU 3280 CG2 VAL C 176 5055 5635 5285 1125 -94 326 C ATOM 3281 N ASP C 177 -9.345 24.377 -1.983 1.00 39.73 N ANISOU 3281 N ASP C 177 4488 5585 5022 1062 -64 257 N ATOM 3282 CA ASP C 177 -9.414 22.953 -1.667 1.00 37.37 C ANISOU 3282 CA ASP C 177 4098 5375 4724 958 -83 231 C ATOM 3283 C ASP C 177 -9.976 22.765 -0.263 1.00 35.85 C ANISOU 3283 C ASP C 177 3856 5217 4548 960 -24 202 C ATOM 3284 O ASP C 177 -9.240 22.836 0.721 1.00 34.51 O ANISOU 3284 O ASP C 177 3759 4965 4386 935 23 166 O ATOM 3285 CB ASP C 177 -8.035 22.299 -1.791 1.00 36.16 C ANISOU 3285 CB ASP C 177 4034 5135 4570 839 -95 198 C ATOM 3286 CG ASP C 177 -8.049 20.820 -1.435 1.00 35.90 C ANISOU 3286 CG ASP C 177 3942 5157 4541 714 -109 166 C ATOM 3287 OD1 ASP C 177 -9.141 20.210 -1.418 1.00 32.84 O ANISOU 3287 OD1 ASP C 177 3438 4887 4152 698 -125 175 O ATOM 3288 OD2 ASP C 177 -6.961 20.265 -1.177 1.00 35.81 O ANISOU 3288 OD2 ASP C 177 4001 5072 4535 630 -104 136 O ATOM 3289 N PRO C 178 -11.292 22.520 -0.171 1.00 34.34 N ANISOU 3289 N PRO C 178 3554 5139 4354 964 -25 214 N ATOM 3290 CA PRO C 178 -12.025 22.450 1.099 1.00 34.40 C ANISOU 3290 CA PRO C 178 3506 5196 4368 975 34 194 C ATOM 3291 C PRO C 178 -11.562 21.329 2.033 1.00 34.07 C ANISOU 3291 C PRO C 178 3441 5175 4330 873 56 163 C ATOM 3292 O PRO C 178 -11.810 21.416 3.236 1.00 34.74 O ANISOU 3292 O PRO C 178 3516 5270 4414 886 118 142 O ATOM 3293 CB PRO C 178 -13.476 22.220 0.654 1.00 34.68 C ANISOU 3293 CB PRO C 178 3416 5366 4394 977 9 222 C ATOM 3294 CG PRO C 178 -13.373 21.644 -0.714 1.00 35.20 C ANISOU 3294 CG PRO C 178 3459 5469 4447 916 -71 243 C ATOM 3295 CD PRO C 178 -12.169 22.282 -1.330 1.00 34.43 C ANISOU 3295 CD PRO C 178 3487 5247 4349 953 -86 247 C ATOM 3296 N THR C 179 -10.900 20.305 1.502 1.00 30.75 N ANISOU 3296 N THR C 179 3028 4746 3909 761 8 157 N ATOM 3297 CA THR C 179 -10.432 19.204 2.343 1.00 30.83 C ANISOU 3297 CA THR C 179 3057 4736 3923 636 25 129 C ATOM 3298 C THR C 179 -8.946 19.315 2.665 1.00 29.87 C ANISOU 3298 C THR C 179 3076 4469 3803 602 36 101 C ATOM 3299 O THR C 179 -8.357 18.391 3.226 1.00 31.52 O ANISOU 3299 O THR C 179 3315 4649 4014 505 39 84 O ATOM 3300 CB THR C 179 -10.694 17.832 1.693 1.00 31.65 C ANISOU 3300 CB THR C 179 3097 4905 4026 509 -30 133 C ATOM 3301 OG1 THR C 179 -10.087 17.786 0.396 1.00 33.10 O ANISOU 3301 OG1 THR C 179 3329 5044 4203 494 -91 135 O ATOM 3302 CG2 THR C 179 -12.190 17.579 1.570 1.00 33.51 C ANISOU 3302 CG2 THR C 179 3175 5304 4254 513 -39 158 C ATOM 3303 N SER C 180 -8.340 20.441 2.306 1.00 27.15 N ANISOU 3303 N SER C 180 2818 4039 3459 681 40 101 N ATOM 3304 CA SER C 180 -6.964 20.708 2.700 1.00 25.74 C ANISOU 3304 CA SER C 180 2763 3737 3279 651 55 74 C ATOM 3305 C SER C 180 -6.955 21.335 4.090 1.00 24.42 C ANISOU 3305 C SER C 180 2633 3540 3105 691 122 48 C ATOM 3306 O SER C 180 -7.975 21.848 4.554 1.00 25.12 O ANISOU 3306 O SER C 180 2669 3686 3191 772 160 52 O ATOM 3307 CB SER C 180 -6.265 21.623 1.691 1.00 26.62 C ANISOU 3307 CB SER C 180 2957 3769 3390 697 32 86 C ATOM 3308 OG SER C 180 -6.845 22.915 1.685 1.00 29.31 O ANISOU 3308 OG SER C 180 3313 4093 3730 820 60 101 O ATOM 3309 N GLN C 181 -5.804 21.292 4.750 1.00 23.82 N ANISOU 3309 N GLN C 181 2646 3383 3020 636 135 19 N ATOM 3310 CA GLN C 181 -5.685 21.808 6.106 1.00 22.72 C ANISOU 3310 CA GLN C 181 2552 3218 2863 656 194 -14 C ATOM 3311 C GLN C 181 -4.729 22.994 6.161 1.00 22.97 C ANISOU 3311 C GLN C 181 2707 3133 2887 686 209 -39 C ATOM 3312 O GLN C 181 -3.795 23.088 5.362 1.00 20.05 O ANISOU 3312 O GLN C 181 2391 2702 2524 651 172 -33 O ATOM 3313 CB GLN C 181 -5.199 20.712 7.064 1.00 22.44 C ANISOU 3313 CB GLN C 181 2513 3201 2813 555 199 -25 C ATOM 3314 CG GLN C 181 -5.875 19.354 6.897 1.00 25.75 C ANISOU 3314 CG GLN C 181 2835 3707 3241 490 175 3 C ATOM 3315 CD GLN C 181 -5.278 18.532 5.764 1.00 30.40 C ANISOU 3315 CD GLN C 181 3429 4272 3849 426 113 17 C ATOM 3316 OE1 GLN C 181 -4.283 18.925 5.151 1.00 30.80 O ANISOU 3316 OE1 GLN C 181 3549 4250 3904 428 89 9 O ATOM 3317 NE2 GLN C 181 -5.885 17.384 5.481 1.00 29.60 N ANISOU 3317 NE2 GLN C 181 3256 4234 3757 364 89 36 N ATOM 3318 N ARG C 182 -4.963 23.897 7.109 1.00 18.36 N ANISOU 3318 N ARG C 182 2169 2521 2286 746 266 -71 N ATOM 3319 CA ARG C 182 -4.010 24.963 7.389 1.00 17.40 C ANISOU 3319 CA ARG C 182 2176 2283 2151 750 285 -107 C ATOM 3320 C ARG C 182 -2.707 24.362 7.908 1.00 17.10 C ANISOU 3320 C ARG C 182 2182 2222 2095 632 264 -129 C ATOM 3321 O ARG C 182 -2.714 23.579 8.856 1.00 17.39 O ANISOU 3321 O ARG C 182 2184 2314 2110 582 275 -140 O ATOM 3322 CB ARG C 182 -4.579 25.953 8.411 1.00 19.14 C ANISOU 3322 CB ARG C 182 2442 2479 2350 835 355 -149 C ATOM 3323 CG ARG C 182 -3.681 27.155 8.669 1.00 21.42 C ANISOU 3323 CG ARG C 182 2878 2635 2624 835 377 -192 C ATOM 3324 CD ARG C 182 -4.216 28.038 9.788 1.00 23.82 C ANISOU 3324 CD ARG C 182 3238 2912 2900 912 451 -247 C ATOM 3325 NE ARG C 182 -3.586 29.356 9.780 1.00 26.36 N ANISOU 3325 NE ARG C 182 3711 3088 3216 932 472 -285 N ATOM 3326 CZ ARG C 182 -3.647 30.225 10.783 1.00 29.48 C ANISOU 3326 CZ ARG C 182 4201 3422 3579 969 534 -352 C ATOM 3327 NH1 ARG C 182 -4.306 29.918 11.894 1.00 30.36 N ANISOU 3327 NH1 ARG C 182 4265 3616 3656 996 582 -386 N ATOM 3328 NH2 ARG C 182 -3.044 31.402 10.679 1.00 29.21 N ANISOU 3328 NH2 ARG C 182 4314 3241 3542 973 549 -386 N ATOM 3329 N LEU C 183 -1.591 24.720 7.283 1.00 15.50 N ANISOU 3329 N LEU C 183 2050 1943 1896 587 235 -130 N ATOM 3330 CA LEU C 183 -0.298 24.216 7.725 1.00 14.73 C ANISOU 3330 CA LEU C 183 1984 1835 1780 484 213 -147 C ATOM 3331 C LEU C 183 0.434 25.270 8.540 1.00 14.82 C ANISOU 3331 C LEU C 183 2100 1770 1759 463 242 -198 C ATOM 3332 O LEU C 183 0.422 26.450 8.195 1.00 17.04 O ANISOU 3332 O LEU C 183 2460 1969 2046 506 262 -210 O ATOM 3333 CB LEU C 183 0.552 23.780 6.531 1.00 14.31 C ANISOU 3333 CB LEU C 183 1924 1769 1746 434 161 -118 C ATOM 3334 CG LEU C 183 -0.071 22.712 5.631 1.00 14.47 C ANISOU 3334 CG LEU C 183 1852 1854 1791 441 127 -77 C ATOM 3335 CD1 LEU C 183 0.930 22.238 4.591 1.00 12.45 C ANISOU 3335 CD1 LEU C 183 1601 1586 1544 388 84 -60 C ATOM 3336 CD2 LEU C 183 -0.589 21.544 6.462 1.00 16.25 C ANISOU 3336 CD2 LEU C 183 2007 2155 2011 414 131 -75 C ATOM 3337 N LEU C 184 1.069 24.840 9.625 1.00 15.21 N ANISOU 3337 N LEU C 184 2158 1849 1772 394 243 -225 N ATOM 3338 CA LEU C 184 1.777 25.765 10.498 1.00 17.79 C ANISOU 3338 CA LEU C 184 2582 2119 2058 358 267 -281 C ATOM 3339 C LEU C 184 3.207 25.310 10.763 1.00 15.47 C ANISOU 3339 C LEU C 184 2296 1844 1740 248 225 -287 C ATOM 3340 O LEU C 184 3.469 24.117 10.907 1.00 15.16 O ANISOU 3340 O LEU C 184 2185 1878 1699 213 194 -258 O ATOM 3341 CB LEU C 184 1.023 25.936 11.819 1.00 20.65 C ANISOU 3341 CB LEU C 184 2954 2513 2380 394 319 -322 C ATOM 3342 CG LEU C 184 -0.417 26.447 11.709 1.00 22.62 C ANISOU 3342 CG LEU C 184 3186 2759 2647 515 369 -321 C ATOM 3343 CD1 LEU C 184 -1.393 25.306 11.454 1.00 22.10 C ANISOU 3343 CD1 LEU C 184 2993 2798 2606 544 360 -269 C ATOM 3344 CD2 LEU C 184 -0.809 27.234 12.948 1.00 23.94 C ANISOU 3344 CD2 LEU C 184 3420 2909 2766 552 433 -387 C ATOM 3345 N PRO C 185 4.139 26.273 10.829 1.00 12.37 N ANISOU 3345 N PRO C 185 1990 1384 1326 193 225 -324 N ATOM 3346 CA PRO C 185 5.561 26.006 11.061 1.00 12.16 C ANISOU 3346 CA PRO C 185 1964 1384 1272 86 185 -332 C ATOM 3347 C PRO C 185 5.893 25.805 12.539 1.00 13.24 C ANISOU 3347 C PRO C 185 2110 1576 1344 37 188 -372 C ATOM 3348 O PRO C 185 5.600 26.670 13.361 1.00 15.19 O ANISOU 3348 O PRO C 185 2434 1784 1553 42 227 -428 O ATOM 3349 CB PRO C 185 6.237 27.266 10.521 1.00 15.95 C ANISOU 3349 CB PRO C 185 2538 1768 1753 44 191 -356 C ATOM 3350 CG PRO C 185 5.237 28.345 10.780 1.00 18.36 C ANISOU 3350 CG PRO C 185 2929 1986 2059 120 246 -392 C ATOM 3351 CD PRO C 185 3.873 27.708 10.624 1.00 13.18 C ANISOU 3351 CD PRO C 185 2199 1377 1434 231 263 -357 C ATOM 3352 N LEU C 186 6.491 24.664 12.866 1.00 15.98 N ANISOU 3352 N LEU C 186 2383 2011 1675 -5 148 -341 N ATOM 3353 CA LEU C 186 6.982 24.416 14.215 1.00 15.03 C ANISOU 3353 CA LEU C 186 2269 1957 1486 -59 139 -368 C ATOM 3354 C LEU C 186 8.132 25.367 14.511 1.00 18.10 C ANISOU 3354 C LEU C 186 2724 2323 1832 -152 123 -419 C ATOM 3355 O LEU C 186 8.874 25.745 13.603 1.00 18.46 O ANISOU 3355 O LEU C 186 2776 2332 1906 -192 103 -411 O ATOM 3356 CB LEU C 186 7.429 22.962 14.373 1.00 15.83 C ANISOU 3356 CB LEU C 186 2279 2150 1584 -73 94 -311 C ATOM 3357 CG LEU C 186 6.353 21.901 14.117 1.00 14.65 C ANISOU 3357 CG LEU C 186 2068 2025 1475 -4 106 -259 C ATOM 3358 CD1 LEU C 186 6.934 20.501 14.243 1.00 14.34 C ANISOU 3358 CD1 LEU C 186 1962 2053 1435 -22 62 -204 C ATOM 3359 CD2 LEU C 186 5.180 22.082 15.067 1.00 15.23 C ANISOU 3359 CD2 LEU C 186 2160 2112 1516 36 157 -281 C ATOM 3360 N ALA C 187 8.269 25.756 15.777 1.00 17.51 N ANISOU 3360 N ALA C 187 2698 2273 1683 -194 134 -473 N ATOM 3361 CA ALA C 187 9.289 26.717 16.183 1.00 19.88 C ANISOU 3361 CA ALA C 187 3070 2553 1932 -298 120 -534 C ATOM 3362 C ALA C 187 10.673 26.336 15.674 1.00 24.76 C ANISOU 3362 C ALA C 187 3625 3228 2554 -381 58 -501 C ATOM 3363 O ALA C 187 11.120 25.202 15.836 1.00 24.05 O ANISOU 3363 O ALA C 187 3442 3240 2458 -379 17 -450 O ATOM 3364 CB ALA C 187 9.310 26.858 17.695 1.00 15.39 C ANISOU 3364 CB ALA C 187 2541 2039 1269 -337 128 -589 C ATOM 3365 N THR C 188 11.337 27.299 15.045 1.00 31.43 N ANISOU 3365 N THR C 188 4522 4007 3411 -449 57 -527 N ATOM 3366 CA THR C 188 12.691 27.109 14.545 1.00 37.98 C ANISOU 3366 CA THR C 188 5291 4899 4241 -537 6 -502 C ATOM 3367 C THR C 188 13.684 27.227 15.690 1.00 40.99 C ANISOU 3367 C THR C 188 5667 5373 4535 -648 -33 -544 C ATOM 3368 O THR C 188 13.354 27.745 16.754 1.00 42.07 O ANISOU 3368 O THR C 188 5878 5497 4610 -671 -15 -606 O ATOM 3369 CB THR C 188 13.042 28.139 13.455 1.00 39.66 C ANISOU 3369 CB THR C 188 5564 5012 4492 -586 23 -511 C ATOM 3370 OG1 THR C 188 14.332 27.840 12.908 1.00 39.95 O ANISOU 3370 OG1 THR C 188 5520 5129 4529 -666 -21 -479 O ATOM 3371 CG2 THR C 188 13.053 29.545 14.039 1.00 41.82 C ANISOU 3371 CG2 THR C 188 5976 5189 4723 -662 53 -593 C ATOM 3372 N THR C 189 14.903 26.748 15.474 1.00 47.12 N ANISOU 3372 N THR C 189 6351 6253 5299 -713 -87 -511 N ATOM 3373 CA THR C 189 15.926 26.811 16.510 1.00 52.76 C ANISOU 3373 CA THR C 189 7040 7080 5926 -820 -135 -543 C ATOM 3374 C THR C 189 16.849 28.012 16.302 1.00 55.99 C ANISOU 3374 C THR C 189 7502 7461 6311 -967 -142 -597 C ATOM 3375 O THR C 189 17.048 28.467 15.176 1.00 55.98 O ANISOU 3375 O THR C 189 7514 7391 6367 -986 -124 -581 O ATOM 3376 CB THR C 189 16.757 25.518 16.553 1.00 53.08 C ANISOU 3376 CB THR C 189 6935 7274 5959 -800 -195 -471 C ATOM 3377 OG1 THR C 189 17.314 25.264 15.259 1.00 52.54 O ANISOU 3377 OG1 THR C 189 6798 7209 5957 -790 -201 -423 O ATOM 3378 CG2 THR C 189 15.881 24.340 16.960 1.00 53.04 C ANISOU 3378 CG2 THR C 189 6896 7292 5966 -676 -190 -420 C ATOM 3379 N GLY C 190 17.406 28.516 17.398 1.00 61.70 N ANISOU 3379 N GLY C 190 8256 8238 6949 -1071 -167 -655 N ATOM 3380 CA GLY C 190 18.229 29.713 17.376 1.00 67.04 C ANISOU 3380 CA GLY C 190 8980 8871 7622 -1192 -162 -690 C ATOM 3381 C GLY C 190 19.512 29.629 16.568 1.00 70.11 C ANISOU 3381 C GLY C 190 9265 9343 8032 -1271 -196 -644 C ATOM 3382 O GLY C 190 19.879 30.580 15.878 1.00 74.92 O ANISOU 3382 O GLY C 190 9929 9872 8667 -1349 -171 -657 O ATOM 3383 N ASP C 191 20.202 28.496 16.655 1.00 62.54 N ANISOU 3383 N ASP C 191 8157 8544 7060 -1243 -248 -585 N ATOM 3384 CA ASP C 191 21.481 28.334 15.971 1.00 54.69 C ANISOU 3384 CA ASP C 191 7047 7653 6081 -1302 -276 -538 C ATOM 3385 C ASP C 191 21.300 28.083 14.474 1.00 46.38 C ANISOU 3385 C ASP C 191 5969 6556 5097 -1266 -256 -502 C ATOM 3386 O ASP C 191 20.177 28.002 13.977 1.00 41.98 O ANISOU 3386 O ASP C 191 5484 5886 4580 -1186 -222 -506 O ATOM 3387 CB ASP C 191 22.285 27.198 16.604 1.00 53.53 C ANISOU 3387 CB ASP C 191 6750 7688 5899 -1263 -334 -484 C ATOM 3388 CG ASP C 191 21.463 25.936 16.804 1.00 51.76 C ANISOU 3388 CG ASP C 191 6492 7492 5684 -1125 -349 -445 C ATOM 3389 OD1 ASP C 191 20.447 25.753 16.096 1.00 47.79 O ANISOU 3389 OD1 ASP C 191 6041 6895 5223 -1059 -319 -447 O ATOM 3390 OD2 ASP C 191 21.843 25.121 17.671 1.00 50.48 O ANISOU 3390 OD2 ASP C 191 6253 7446 5482 -1083 -390 -409 O ATOM 3391 N GLY C 192 22.414 27.962 13.761 1.00 40.20 N ANISOU 3391 N GLY C 192 5081 5865 4328 -1312 -271 -460 N ATOM 3392 CA GLY C 192 22.380 27.807 12.319 1.00 37.40 C ANISOU 3392 CA GLY C 192 4698 5480 4032 -1292 -249 -425 C ATOM 3393 C GLY C 192 21.975 26.418 11.867 1.00 33.91 C ANISOU 3393 C GLY C 192 4166 5083 3634 -1133 -257 -364 C ATOM 3394 O GLY C 192 21.940 26.134 10.670 1.00 35.64 O ANISOU 3394 O GLY C 192 4355 5276 3910 -1075 -230 -322 O ATOM 3395 N ASN C 193 21.658 25.552 12.824 1.00 30.44 N ANISOU 3395 N ASN C 193 3695 4702 3169 -1052 -288 -353 N ATOM 3396 CA ASN C 193 21.306 24.173 12.513 1.00 28.46 C ANISOU 3396 CA ASN C 193 3369 4480 2962 -895 -293 -289 C ATOM 3397 C ASN C 193 19.804 23.950 12.322 1.00 23.44 C ANISOU 3397 C ASN C 193 2828 3700 2378 -781 -249 -286 C ATOM 3398 O ASN C 193 19.338 22.810 12.362 1.00 22.78 O ANISOU 3398 O ASN C 193 2704 3630 2320 -663 -255 -242 O ATOM 3399 CB ASN C 193 21.822 23.238 13.612 1.00 31.93 C ANISOU 3399 CB ASN C 193 3718 5067 3348 -863 -351 -263 C ATOM 3400 CG ASN C 193 23.299 23.438 13.907 1.00 36.45 C ANISOU 3400 CG ASN C 193 4190 5785 3875 -954 -389 -257 C ATOM 3401 OD1 ASN C 193 24.160 23.089 13.100 1.00 35.96 O ANISOU 3401 OD1 ASN C 193 4027 5797 3839 -938 -389 -217 O ATOM 3402 ND2 ASN C 193 23.598 23.989 15.080 1.00 39.05 N ANISOU 3402 ND2 ASN C 193 4552 6139 4144 -1026 -405 -288 N ATOM 3403 N CYS C 194 19.050 25.027 12.106 1.00 16.33 N ANISOU 3403 N CYS C 194 2049 2662 1492 -815 -205 -329 N ATOM 3404 CA CYS C 194 17.590 24.925 12.029 1.00 16.66 C ANISOU 3404 CA CYS C 194 2173 2582 1575 -711 -164 -330 C ATOM 3405 C CYS C 194 17.117 23.998 10.917 1.00 16.40 C ANISOU 3405 C CYS C 194 2092 2527 1613 -595 -150 -272 C ATOM 3406 O CYS C 194 16.072 23.358 11.042 1.00 17.01 O ANISOU 3406 O CYS C 194 2184 2563 1716 -498 -136 -255 O ATOM 3407 CB CYS C 194 16.952 26.301 11.839 1.00 16.60 C ANISOU 3407 CB CYS C 194 2302 2431 1576 -756 -118 -381 C ATOM 3408 SG CYS C 194 17.410 27.132 10.310 1.00 21.86 S ANISOU 3408 SG CYS C 194 2992 3028 2285 -812 -91 -365 S ATOM 3409 N LEU C 195 17.873 23.932 9.826 1.00 16.20 N ANISOU 3409 N LEU C 195 2009 2532 1612 -613 -151 -245 N ATOM 3410 CA LEU C 195 17.517 23.040 8.729 1.00 18.95 C ANISOU 3410 CA LEU C 195 2315 2868 2018 -511 -138 -199 C ATOM 3411 C LEU C 195 17.568 21.586 9.179 1.00 18.21 C ANISOU 3411 C LEU C 195 2141 2850 1926 -424 -168 -162 C ATOM 3412 O LEU C 195 16.641 20.815 8.935 1.00 16.86 O ANISOU 3412 O LEU C 195 1982 2631 1794 -330 -156 -141 O ATOM 3413 CB LEU C 195 18.446 23.248 7.531 1.00 17.34 C ANISOU 3413 CB LEU C 195 2061 2700 1826 -553 -130 -181 C ATOM 3414 CG LEU C 195 18.249 22.253 6.383 1.00 17.12 C ANISOU 3414 CG LEU C 195 1984 2676 1846 -452 -119 -140 C ATOM 3415 CD1 LEU C 195 16.831 22.325 5.833 1.00 17.18 C ANISOU 3415 CD1 LEU C 195 2072 2562 1895 -380 -90 -138 C ATOM 3416 CD2 LEU C 195 19.268 22.494 5.278 1.00 17.38 C ANISOU 3416 CD2 LEU C 195 1961 2764 1876 -500 -107 -125 C ATOM 3417 N LEU C 196 18.660 21.222 9.842 1.00 18.63 N ANISOU 3417 N LEU C 196 2115 3026 1938 -458 -208 -153 N ATOM 3418 CA LEU C 196 18.864 19.856 10.311 1.00 18.55 C ANISOU 3418 CA LEU C 196 2031 3090 1925 -372 -240 -110 C ATOM 3419 C LEU C 196 17.847 19.487 11.383 1.00 19.33 C ANISOU 3419 C LEU C 196 2187 3149 2010 -330 -242 -109 C ATOM 3420 O LEU C 196 17.358 18.355 11.431 1.00 18.59 O ANISOU 3420 O LEU C 196 2079 3043 1941 -238 -245 -70 O ATOM 3421 CB LEU C 196 20.287 19.682 10.852 1.00 21.18 C ANISOU 3421 CB LEU C 196 2263 3576 2207 -417 -287 -97 C ATOM 3422 CG LEU C 196 21.439 19.912 9.869 1.00 23.95 C ANISOU 3422 CG LEU C 196 2531 4003 2565 -458 -285 -90 C ATOM 3423 CD1 LEU C 196 21.188 19.172 8.564 1.00 22.80 C ANISOU 3423 CD1 LEU C 196 2369 3811 2482 -360 -252 -63 C ATOM 3424 CD2 LEU C 196 21.669 21.395 9.616 1.00 26.29 C ANISOU 3424 CD2 LEU C 196 2879 4269 2842 -598 -265 -137 C ATOM 3425 N HIS C 197 17.530 20.462 12.224 1.00 20.01 N ANISOU 3425 N HIS C 197 2340 3212 2051 -403 -237 -155 N ATOM 3426 CA HIS C 197 16.596 20.266 13.312 1.00 20.53 C ANISOU 3426 CA HIS C 197 2460 3251 2090 -375 -232 -161 C ATOM 3427 C HIS C 197 15.209 19.911 12.797 1.00 19.69 C ANISOU 3427 C HIS C 197 2402 3038 2043 -292 -190 -149 C ATOM 3428 O HIS C 197 14.553 19.035 13.329 1.00 17.87 O ANISOU 3428 O HIS C 197 2170 2806 1812 -233 -189 -120 O ATOM 3429 CB HIS C 197 16.518 21.529 14.160 1.00 25.41 C ANISOU 3429 CB HIS C 197 3152 3853 2647 -471 -224 -227 C ATOM 3430 CG HIS C 197 15.668 21.380 15.377 1.00 34.70 C ANISOU 3430 CG HIS C 197 4377 5031 3777 -450 -218 -238 C ATOM 3431 ND1 HIS C 197 16.051 20.621 16.460 1.00 38.18 N ANISOU 3431 ND1 HIS C 197 4903 5371 4232 -420 -167 -270 N ATOM 3432 CD2 HIS C 197 14.446 21.878 15.677 1.00 36.97 C ANISOU 3432 CD2 HIS C 197 4634 5415 3998 -452 -255 -218 C ATOM 3433 CE1 HIS C 197 15.104 20.664 17.378 1.00 39.41 C ANISOU 3433 CE1 HIS C 197 5078 5564 4331 -409 -167 -273 C ATOM 3434 NE2 HIS C 197 14.122 21.423 16.929 1.00 40.86 N ANISOU 3434 NE2 HIS C 197 5197 5864 4463 -430 -221 -240 N ATOM 3435 N ALA C 198 14.784 20.589 11.743 1.00 18.83 N ANISOU 3435 N ALA C 198 2331 2844 1980 -293 -156 -168 N ATOM 3436 CA ALA C 198 13.475 20.343 11.152 1.00 17.29 C ANISOU 3436 CA ALA C 198 2170 2561 1837 -220 -121 -158 C ATOM 3437 C ALA C 198 13.450 19.009 10.419 1.00 19.45 C ANISOU 3437 C ALA C 198 2385 2849 2156 -146 -133 -108 C ATOM 3438 O ALA C 198 12.388 18.429 10.206 1.00 25.01 O ANISOU 3438 O ALA C 198 3102 3507 2894 -89 -116 -91 O ATOM 3439 CB ALA C 198 13.098 21.472 10.208 1.00 20.13 C ANISOU 3439 CB ALA C 198 2588 2834 2225 -237 -87 -185 C ATOM 3440 N ALA C 199 14.629 18.523 10.047 1.00 17.33 N ANISOU 3440 N ALA C 199 2050 2647 1886 -151 -161 -86 N ATOM 3441 CA ALA C 199 14.745 17.323 9.226 1.00 16.64 C ANISOU 3441 CA ALA C 199 1917 2565 1841 -79 -167 -48 C ATOM 3442 C ALA C 199 15.069 16.063 10.027 1.00 18.15 C ANISOU 3442 C ALA C 199 2068 2810 2018 -30 -197 -6 C ATOM 3443 O ALA C 199 15.077 14.965 9.475 1.00 20.25 O ANISOU 3443 O ALA C 199 2312 3063 2319 37 -200 25 O ATOM 3444 CB ALA C 199 15.804 17.535 8.153 1.00 16.77 C ANISOU 3444 CB ALA C 199 1885 2618 1867 -95 -169 -50 C ATOM 3445 N SER C 200 15.338 16.218 11.320 1.00 18.32 N ANISOU 3445 N SER C 200 2089 2888 1984 -63 -219 -3 N ATOM 3446 CA SER C 200 15.816 15.099 12.132 1.00 19.47 C ANISOU 3446 CA SER C 200 2195 3097 2105 -17 -254 47 C ATOM 3447 C SER C 200 14.801 14.601 13.163 1.00 20.76 C ANISOU 3447 C SER C 200 2406 3231 2250 0 -248 69 C ATOM 3448 O SER C 200 15.165 13.888 14.101 1.00 20.02 O ANISOU 3448 O SER C 200 2295 3195 2118 22 -278 113 O ATOM 3449 CB SER C 200 17.111 15.488 12.847 1.00 19.28 C ANISOU 3449 CB SER C 200 2114 3193 2018 -66 -296 47 C ATOM 3450 OG SER C 200 16.890 16.566 13.739 1.00 22.01 O ANISOU 3450 OG SER C 200 2503 3550 2308 -151 -295 3 O ATOM 3451 N LEU C 201 13.535 14.967 12.985 1.00 20.15 N ANISOU 3451 N LEU C 201 2385 3073 2196 -6 -208 45 N ATOM 3452 CA LEU C 201 12.480 14.543 13.902 1.00 21.05 C ANISOU 3452 CA LEU C 201 2539 3168 2293 4 -192 64 C ATOM 3453 C LEU C 201 12.367 13.020 13.973 1.00 21.14 C ANISOU 3453 C LEU C 201 2541 3166 2327 64 -205 131 C ATOM 3454 O LEU C 201 11.937 12.466 14.986 1.00 23.18 O ANISOU 3454 O LEU C 201 2819 3438 2551 68 -206 168 O ATOM 3455 CB LEU C 201 11.137 15.150 13.492 1.00 18.40 C ANISOU 3455 CB LEU C 201 2247 2757 1988 -2 -145 29 C ATOM 3456 CG LEU C 201 11.016 16.669 13.622 1.00 20.01 C ANISOU 3456 CG LEU C 201 2486 2951 2166 -52 -123 -34 C ATOM 3457 CD1 LEU C 201 9.621 17.131 13.234 1.00 20.10 C ANISOU 3457 CD1 LEU C 201 2534 2893 2211 -32 -76 -57 C ATOM 3458 CD2 LEU C 201 11.355 17.112 15.038 1.00 22.25 C ANISOU 3458 CD2 LEU C 201 2789 3298 2368 -97 -133 -51 C ATOM 3459 N GLY C 202 12.758 12.349 12.896 1.00 18.32 N ANISOU 3459 N GLY C 202 2159 2777 2024 110 -212 145 N ATOM 3460 CA GLY C 202 12.750 10.899 12.860 1.00 19.10 C ANISOU 3460 CA GLY C 202 2263 2845 2149 171 -223 203 C ATOM 3461 C GLY C 202 13.785 10.294 13.789 1.00 19.09 C ANISOU 3461 C GLY C 202 2234 2918 2102 203 -265 257 C ATOM 3462 O GLY C 202 13.739 9.102 14.090 1.00 17.73 O ANISOU 3462 O GLY C 202 2081 2717 1938 255 -275 317 O ATOM 3463 N MET C 203 14.722 11.119 14.246 1.00 19.42 N ANISOU 3463 N MET C 203 2233 3055 2091 169 -291 238 N ATOM 3464 CA MET C 203 15.756 10.670 15.174 1.00 20.24 C ANISOU 3464 CA MET C 203 2296 3256 2139 195 -339 289 C ATOM 3465 C MET C 203 15.521 11.204 16.582 1.00 19.13 C ANISOU 3465 C MET C 203 2177 3179 1914 136 -351 290 C ATOM 3466 O MET C 203 16.450 11.282 17.388 1.00 21.26 O ANISOU 3466 O MET C 203 2405 3557 2117 128 -397 312 O ATOM 3467 CB MET C 203 17.139 11.094 14.679 1.00 22.57 C ANISOU 3467 CB MET C 203 2509 3640 2427 198 -368 272 C ATOM 3468 CG MET C 203 17.690 10.215 13.567 1.00 27.42 C ANISOU 3468 CG MET C 203 3089 4226 3103 286 -365 293 C ATOM 3469 SD MET C 203 19.234 10.846 12.880 1.00 67.05 S ANISOU 3469 SD MET C 203 7999 9364 8112 278 -386 266 S ATOM 3470 CE MET C 203 18.671 12.388 12.168 1.00 24.59 C ANISOU 3470 CE MET C 203 2653 3943 2747 164 -346 180 C ATOM 3471 N TRP C 204 14.277 11.577 16.867 1.00 18.64 N ANISOU 3471 N TRP C 204 2175 3058 1850 96 -310 264 N ATOM 3472 CA TRP C 204 13.898 12.042 18.198 1.00 19.68 C ANISOU 3472 CA TRP C 204 2337 3243 1897 44 -309 259 C ATOM 3473 C TRP C 204 14.270 10.997 19.243 1.00 20.42 C ANISOU 3473 C TRP C 204 2428 3395 1936 82 -347 345 C ATOM 3474 O TRP C 204 14.063 9.803 19.035 1.00 21.85 O ANISOU 3474 O TRP C 204 2624 3520 2158 146 -346 412 O ATOM 3475 CB TRP C 204 12.400 12.344 18.253 1.00 18.81 C ANISOU 3475 CB TRP C 204 2285 3057 1803 19 -250 230 C ATOM 3476 CG TRP C 204 11.960 13.043 19.505 1.00 19.02 C ANISOU 3476 CG TRP C 204 2346 3137 1742 -34 -235 203 C ATOM 3477 CD1 TRP C 204 11.798 14.387 19.677 1.00 18.87 C ANISOU 3477 CD1 TRP C 204 2351 3128 1691 -91 -213 121 C ATOM 3478 CD2 TRP C 204 11.619 12.434 20.757 1.00 17.16 C ANISOU 3478 CD2 TRP C 204 2135 2949 1435 -36 -237 258 C ATOM 3479 NE1 TRP C 204 11.379 14.653 20.958 1.00 22.02 N ANISOU 3479 NE1 TRP C 204 2786 3579 2001 -124 -199 112 N ATOM 3480 CE2 TRP C 204 11.261 13.471 21.642 1.00 18.53 C ANISOU 3480 CE2 TRP C 204 2342 3169 1531 -93 -213 198 C ATOM 3481 CE3 TRP C 204 11.583 11.113 21.217 1.00 14.45 C ANISOU 3481 CE3 TRP C 204 1799 2609 1083 6 -253 353 C ATOM 3482 CZ2 TRP C 204 10.872 13.230 22.958 1.00 19.82 C ANISOU 3482 CZ2 TRP C 204 2535 3394 1601 -112 -205 228 C ATOM 3483 CZ3 TRP C 204 11.197 10.875 22.526 1.00 18.33 C ANISOU 3483 CZ3 TRP C 204 2322 3158 1485 -15 -247 392 C ATOM 3484 CH2 TRP C 204 10.845 11.928 23.380 1.00 19.21 C ANISOU 3484 CH2 TRP C 204 2458 3329 1514 -74 -222 329 C ATOM 3485 N GLY C 205 14.828 11.447 20.361 1.00 21.04 N ANISOU 3485 N GLY C 205 2494 3584 1918 42 -381 346 N ATOM 3486 CA GLY C 205 15.281 10.541 21.402 1.00 20.82 C ANISOU 3486 CA GLY C 205 2459 3628 1822 80 -425 434 C ATOM 3487 C GLY C 205 16.796 10.480 21.469 1.00 21.56 C ANISOU 3487 C GLY C 205 2470 3837 1882 105 -494 458 C ATOM 3488 O GLY C 205 17.367 10.022 22.453 1.00 23.33 O ANISOU 3488 O GLY C 205 2678 4156 2033 125 -542 521 O ATOM 3489 N PHE C 206 17.445 10.941 20.404 1.00 20.46 N ANISOU 3489 N PHE C 206 2277 3696 1800 104 -497 411 N ATOM 3490 CA PHE C 206 18.899 11.035 20.366 1.00 22.89 C ANISOU 3490 CA PHE C 206 2489 4127 2080 116 -556 422 C ATOM 3491 C PHE C 206 19.305 12.502 20.341 1.00 23.15 C ANISOU 3491 C PHE C 206 2499 4218 2079 0 -558 327 C ATOM 3492 O PHE C 206 18.947 13.239 19.421 1.00 22.96 O ANISOU 3492 O PHE C 206 2494 4124 2108 -41 -518 260 O ATOM 3493 CB PHE C 206 19.462 10.290 19.156 1.00 28.60 C ANISOU 3493 CB PHE C 206 3163 4810 2894 210 -554 450 C ATOM 3494 CG PHE C 206 18.997 8.865 19.057 1.00 33.75 C ANISOU 3494 CG PHE C 206 3861 5371 3593 319 -543 532 C ATOM 3495 CD1 PHE C 206 19.391 7.927 19.996 1.00 38.00 C ANISOU 3495 CD1 PHE C 206 4408 5929 4102 377 -570 609 C ATOM 3496 CD2 PHE C 206 18.163 8.463 18.027 1.00 35.68 C ANISOU 3496 CD2 PHE C 206 4159 5468 3930 348 -489 514 C ATOM 3497 CE1 PHE C 206 18.962 6.616 19.912 1.00 40.06 C ANISOU 3497 CE1 PHE C 206 4726 6090 4406 470 -559 685 C ATOM 3498 CE2 PHE C 206 17.732 7.153 17.937 1.00 36.50 C ANISOU 3498 CE2 PHE C 206 4317 5474 4077 433 -477 582 C ATOM 3499 CZ PHE C 206 18.132 6.229 18.880 1.00 37.57 C ANISOU 3499 CZ PHE C 206 4458 5650 4165 500 -517 679 C ATOM 3500 N HIS C 207 20.056 12.915 21.358 1.00 27.90 N ANISOU 3500 N HIS C 207 3078 4911 2613 -55 -588 314 N ATOM 3501 CA HIS C 207 20.304 14.331 21.616 1.00 28.98 C ANISOU 3501 CA HIS C 207 3220 5087 2704 -181 -586 223 C ATOM 3502 C HIS C 207 21.061 15.050 20.503 1.00 28.75 C ANISOU 3502 C HIS C 207 3133 5067 2724 -224 -581 173 C ATOM 3503 O HIS C 207 20.729 16.183 20.166 1.00 30.42 O ANISOU 3503 O HIS C 207 3386 5241 2932 -315 -557 94 O ATOM 3504 CB HIS C 207 21.064 14.508 22.931 1.00 28.17 C ANISOU 3504 CB HIS C 207 3097 5087 2520 -225 -624 228 C ATOM 3505 CG HIS C 207 21.284 15.940 23.306 1.00 31.06 C ANISOU 3505 CG HIS C 207 3485 5481 2835 -359 -620 132 C ATOM 3506 ND1 HIS C 207 22.511 16.559 23.199 1.00 34.83 N ANISOU 3506 ND1 HIS C 207 3891 6036 3305 -424 -645 103 N ATOM 3507 CD2 HIS C 207 20.428 16.881 23.769 1.00 30.73 C ANISOU 3507 CD2 HIS C 207 3535 5392 2749 -438 -588 57 C ATOM 3508 CE1 HIS C 207 22.404 17.816 23.590 1.00 34.78 C ANISOU 3508 CE1 HIS C 207 3939 6022 3254 -544 -632 16 C ATOM 3509 NE2 HIS C 207 21.149 18.037 23.941 1.00 34.61 N ANISOU 3509 NE2 HIS C 207 4019 5919 3210 -549 -597 -16 N ATOM 3510 N ASP C 208 22.081 14.413 19.940 1.00 28.69 N ANISOU 3510 N ASP C 208 3037 5105 2761 -159 -600 218 N ATOM 3511 CA ASP C 208 22.854 15.061 18.885 1.00 29.51 C ANISOU 3511 CA ASP C 208 3080 5229 2905 -203 -589 177 C ATOM 3512 C ASP C 208 22.453 14.563 17.498 1.00 27.24 C ANISOU 3512 C ASP C 208 2786 4862 2701 -125 -559 190 C ATOM 3513 O ASP C 208 23.304 14.331 16.641 1.00 24.42 O ANISOU 3513 O ASP C 208 2355 4537 2388 -89 -554 202 O ATOM 3514 CB ASP C 208 24.360 14.867 19.112 1.00 40.88 C ANISOU 3514 CB ASP C 208 4415 6790 4328 -196 -621 205 C ATOM 3515 CG ASP C 208 24.763 13.409 19.218 1.00 48.93 C ANISOU 3515 CG ASP C 208 5390 7831 5372 -52 -640 294 C ATOM 3516 OD1 ASP C 208 23.925 12.530 18.936 1.00 50.46 O ANISOU 3516 OD1 ASP C 208 5634 7933 5607 41 -625 333 O ATOM 3517 OD2 ASP C 208 25.930 13.143 19.579 1.00 54.18 O ANISOU 3517 OD2 ASP C 208 5972 8601 6013 -33 -670 325 O ATOM 3518 N ARG C 209 21.150 14.408 17.282 1.00 21.60 N ANISOU 3518 N ARG C 209 2151 4052 2006 -102 -536 186 N ATOM 3519 CA ARG C 209 20.645 14.001 15.973 1.00 20.77 C ANISOU 3519 CA ARG C 209 2066 3828 1998 -35 -487 186 C ATOM 3520 C ARG C 209 20.993 15.032 14.897 1.00 20.45 C ANISOU 3520 C ARG C 209 2005 3775 1989 -107 -460 124 C ATOM 3521 O ARG C 209 21.262 14.674 13.753 1.00 20.53 O ANISOU 3521 O ARG C 209 1980 3760 2060 -54 -438 132 O ATOM 3522 CB ARG C 209 19.132 13.769 16.022 1.00 19.20 C ANISOU 3522 CB ARG C 209 1976 3486 1834 -13 -440 182 C ATOM 3523 CG ARG C 209 18.322 14.899 16.653 1.00 20.94 C ANISOU 3523 CG ARG C 209 2273 3671 2013 -109 -416 119 C ATOM 3524 CD ARG C 209 16.863 14.488 16.789 1.00 21.41 C ANISOU 3524 CD ARG C 209 2415 3617 2102 -72 -371 129 C ATOM 3525 NE ARG C 209 16.057 15.456 17.529 1.00 18.63 N ANISOU 3525 NE ARG C 209 2133 3241 1704 -142 -344 74 N ATOM 3526 CZ ARG C 209 15.895 15.443 18.849 1.00 22.84 C ANISOU 3526 CZ ARG C 209 2692 3832 2155 -167 -359 82 C ATOM 3527 NH1 ARG C 209 16.497 14.517 19.588 1.00 17.88 N ANISOU 3527 NH1 ARG C 209 2022 3291 1480 -129 -407 153 N ATOM 3528 NH2 ARG C 209 15.136 16.360 19.433 1.00 26.07 N ANISOU 3528 NH2 ARG C 209 3169 4214 2523 -223 -325 22 N ATOM 3529 N ASP C 210 20.988 16.305 15.269 1.00 21.99 N ANISOU 3529 N ASP C 210 2232 3985 2139 -231 -458 62 N ATOM 3530 CA ASP C 210 21.337 17.381 14.351 1.00 26.33 C ANISOU 3530 CA ASP C 210 2777 4516 2713 -314 -432 8 C ATOM 3531 C ASP C 210 22.786 17.278 13.881 1.00 25.74 C ANISOU 3531 C ASP C 210 2574 4579 2628 -325 -463 28 C ATOM 3532 O ASP C 210 23.090 17.492 12.714 1.00 24.46 O ANISOU 3532 O ASP C 210 2383 4400 2513 -327 -433 19 O ATOM 3533 CB ASP C 210 21.071 18.743 14.995 1.00 33.30 C ANISOU 3533 CB ASP C 210 3733 5375 3542 -446 -425 -63 C ATOM 3534 CG ASP C 210 19.591 19.059 15.095 1.00 38.39 C ANISOU 3534 CG ASP C 210 4501 5874 4209 -430 -377 -93 C ATOM 3535 OD1 ASP C 210 18.794 18.355 14.453 1.00 38.10 O ANISOU 3535 OD1 ASP C 210 4489 5747 4241 -339 -343 -66 O ATOM 3536 OD2 ASP C 210 19.224 20.008 15.814 1.00 40.72 O ANISOU 3536 OD2 ASP C 210 4868 6151 4453 -508 -371 -146 O ATOM 3537 N LEU C 211 23.672 16.936 14.805 1.00 27.15 N ANISOU 3537 N LEU C 211 2695 4861 2761 -320 -500 58 N ATOM 3538 CA LEU C 211 25.085 16.763 14.496 1.00 28.65 C ANISOU 3538 CA LEU C 211 2777 5155 2953 -311 -506 82 C ATOM 3539 C LEU C 211 25.307 15.536 13.616 1.00 24.93 C ANISOU 3539 C LEU C 211 2251 4678 2542 -166 -493 134 C ATOM 3540 O LEU C 211 26.172 15.540 12.740 1.00 24.80 O ANISOU 3540 O LEU C 211 2162 4712 2549 -156 -473 136 O ATOM 3541 CB LEU C 211 25.904 16.643 15.783 1.00 34.78 C ANISOU 3541 CB LEU C 211 3512 6037 3666 -330 -548 105 C ATOM 3542 CG LEU C 211 27.176 17.490 15.873 1.00 42.41 C ANISOU 3542 CG LEU C 211 4407 7112 4593 -438 -556 80 C ATOM 3543 CD1 LEU C 211 28.128 17.177 14.727 1.00 44.09 C ANISOU 3543 CD1 LEU C 211 4523 7383 4846 -394 -534 103 C ATOM 3544 CD2 LEU C 211 26.834 18.974 15.898 1.00 43.21 C ANISOU 3544 CD2 LEU C 211 4584 7164 4670 -599 -539 4 C ATOM 3545 N MET C 212 24.528 14.487 13.857 1.00 23.35 N ANISOU 3545 N MET C 212 2093 4413 2365 -54 -498 176 N ATOM 3546 CA MET C 212 24.653 13.256 13.087 1.00 25.05 C ANISOU 3546 CA MET C 212 2282 4597 2639 89 -482 221 C ATOM 3547 C MET C 212 24.165 13.472 11.664 1.00 24.16 C ANISOU 3547 C MET C 212 2183 4415 2583 95 -440 188 C ATOM 3548 O MET C 212 24.751 12.964 10.709 1.00 22.46 O ANISOU 3548 O MET C 212 1918 4211 2406 166 -414 198 O ATOM 3549 CB MET C 212 23.871 12.122 13.751 1.00 24.09 C ANISOU 3549 CB MET C 212 2221 4406 2526 191 -496 274 C ATOM 3550 CG MET C 212 24.255 11.878 15.204 1.00 27.65 C ANISOU 3550 CG MET C 212 2667 4924 2916 186 -538 312 C ATOM 3551 SD MET C 212 23.373 10.494 15.949 1.00 41.36 S ANISOU 3551 SD MET C 212 4481 6573 4659 300 -550 387 S ATOM 3552 CE MET C 212 24.085 9.113 15.058 1.00 44.67 C ANISOU 3552 CE MET C 212 4862 6960 5149 458 -533 435 C ATOM 3553 N LEU C 213 23.087 14.235 11.531 1.00 22.61 N ANISOU 3553 N LEU C 213 2071 4126 2392 22 -420 145 N ATOM 3554 CA LEU C 213 22.527 14.540 10.224 1.00 21.32 C ANISOU 3554 CA LEU C 213 1957 3855 2288 17 -364 110 C ATOM 3555 C LEU C 213 23.482 15.419 9.423 1.00 21.80 C ANISOU 3555 C LEU C 213 1947 3998 2339 -63 -351 82 C ATOM 3556 O LEU C 213 23.646 15.231 8.217 1.00 23.48 O ANISOU 3556 O LEU C 213 2139 4192 2591 -24 -315 77 O ATOM 3557 CB LEU C 213 21.169 15.222 10.374 1.00 21.32 C ANISOU 3557 CB LEU C 213 2080 3721 2301 -40 -336 73 C ATOM 3558 CG LEU C 213 20.304 15.278 9.117 1.00 19.61 C ANISOU 3558 CG LEU C 213 1925 3380 2145 -17 -285 51 C ATOM 3559 CD1 LEU C 213 20.253 13.916 8.448 1.00 17.74 C ANISOU 3559 CD1 LEU C 213 1673 3112 1955 107 -276 84 C ATOM 3560 CD2 LEU C 213 18.906 15.751 9.478 1.00 18.26 C ANISOU 3560 CD2 LEU C 213 1862 3094 1984 -47 -265 27 C ATOM 3561 N ARG C 214 24.115 16.372 10.101 1.00 20.30 N ANISOU 3561 N ARG C 214 1721 3902 2091 -182 -380 61 N ATOM 3562 CA ARG C 214 25.062 17.269 9.448 1.00 22.74 C ANISOU 3562 CA ARG C 214 1962 4294 2383 -283 -368 37 C ATOM 3563 C ARG C 214 26.277 16.509 8.922 1.00 24.63 C ANISOU 3563 C ARG C 214 2098 4627 2635 -200 -356 73 C ATOM 3564 O ARG C 214 26.745 16.765 7.813 1.00 23.29 O ANISOU 3564 O ARG C 214 1888 4482 2482 -216 -319 63 O ATOM 3565 CB ARG C 214 25.510 18.375 10.406 1.00 21.42 C ANISOU 3565 CB ARG C 214 1812 4171 2157 -427 -389 6 C ATOM 3566 CG ARG C 214 26.591 19.274 9.830 1.00 22.27 C ANISOU 3566 CG ARG C 214 1867 4347 2247 -537 -368 -12 C ATOM 3567 CD ARG C 214 27.004 20.370 10.798 1.00 26.70 C ANISOU 3567 CD ARG C 214 2459 4938 2749 -683 -387 -47 C ATOM 3568 NE ARG C 214 25.963 21.380 10.984 1.00 25.28 N ANISOU 3568 NE ARG C 214 2407 4636 2564 -779 -377 -101 N ATOM 3569 CZ ARG C 214 25.739 22.387 10.146 1.00 23.33 C ANISOU 3569 CZ ARG C 214 2217 4313 2332 -876 -341 -136 C ATOM 3570 NH1 ARG C 214 26.473 22.515 9.049 1.00 23.32 N ANISOU 3570 NH1 ARG C 214 2153 4358 2351 -897 -311 -118 N ATOM 3571 NH2 ARG C 214 24.777 23.262 10.399 1.00 20.40 N ANISOU 3571 NH2 ARG C 214 1977 3819 1957 -949 -330 -186 N ATOM 3572 N LYS C 215 26.782 15.575 9.723 1.00 24.47 N ANISOU 3572 N LYS C 215 2039 4658 2601 -111 -384 115 N ATOM 3573 CA LYS C 215 27.930 14.763 9.327 1.00 26.19 C ANISOU 3573 CA LYS C 215 2164 4961 2826 -17 -374 149 C ATOM 3574 C LYS C 215 27.614 13.888 8.119 1.00 25.10 C ANISOU 3574 C LYS C 215 2034 4758 2747 106 -333 156 C ATOM 3575 O LYS C 215 28.462 13.690 7.249 1.00 21.88 O ANISOU 3575 O LYS C 215 1559 4408 2345 141 -302 158 O ATOM 3576 CB LYS C 215 28.397 13.890 10.493 1.00 31.48 C ANISOU 3576 CB LYS C 215 2807 5684 3471 61 -415 197 C ATOM 3577 CG LYS C 215 29.197 14.637 11.546 1.00 35.49 C ANISOU 3577 CG LYS C 215 3270 6303 3911 -47 -452 193 C ATOM 3578 CD LYS C 215 29.551 13.732 12.715 1.00 39.56 C ANISOU 3578 CD LYS C 215 3763 6868 4399 36 -495 245 C ATOM 3579 CE LYS C 215 30.321 14.487 13.789 1.00 43.10 C ANISOU 3579 CE LYS C 215 4168 7435 4775 -76 -534 238 C ATOM 3580 NZ LYS C 215 30.521 13.670 15.021 1.00 44.04 N ANISOU 3580 NZ LYS C 215 4275 7598 4860 -3 -581 290 N ATOM 3581 N ALA C 216 26.392 13.363 8.071 1.00 23.20 N ANISOU 3581 N ALA C 216 1875 4397 2543 169 -332 158 N ATOM 3582 CA ALA C 216 25.957 12.548 6.943 1.00 23.61 C ANISOU 3582 CA ALA C 216 1951 4370 2649 279 -293 157 C ATOM 3583 C ALA C 216 25.837 13.392 5.679 1.00 24.29 C ANISOU 3583 C ALA C 216 2029 4454 2746 209 -251 115 C ATOM 3584 O ALA C 216 26.092 12.912 4.573 1.00 22.82 O ANISOU 3584 O ALA C 216 1823 4262 2584 279 -209 108 O ATOM 3585 CB ALA C 216 24.636 11.870 7.252 1.00 15.34 C ANISOU 3585 CB ALA C 216 998 3197 1633 344 -304 168 C ATOM 3586 N LEU C 217 25.447 14.651 5.851 1.00 22.36 N ANISOU 3586 N LEU C 217 1817 4198 2480 67 -255 86 N ATOM 3587 CA LEU C 217 25.310 15.574 4.732 1.00 22.84 C ANISOU 3587 CA LEU C 217 1908 4220 2548 -17 -208 52 C ATOM 3588 C LEU C 217 26.688 15.923 4.179 1.00 26.22 C ANISOU 3588 C LEU C 217 2211 4805 2948 -61 -193 55 C ATOM 3589 O LEU C 217 26.896 15.958 2.965 1.00 28.17 O ANISOU 3589 O LEU C 217 2435 5063 3205 -49 -146 46 O ATOM 3590 CB LEU C 217 24.558 16.837 5.165 1.00 21.97 C ANISOU 3590 CB LEU C 217 1897 4025 2425 -152 -211 22 C ATOM 3591 CG LEU C 217 23.887 17.676 4.073 1.00 23.45 C ANISOU 3591 CG LEU C 217 2171 4106 2633 -210 -163 -4 C ATOM 3592 CD1 LEU C 217 22.858 18.616 4.683 1.00 26.53 C ANISOU 3592 CD1 LEU C 217 2680 4380 3022 -289 -168 -28 C ATOM 3593 CD2 LEU C 217 24.913 18.460 3.273 1.00 21.78 C ANISOU 3593 CD2 LEU C 217 1890 3991 2396 -303 -136 -8 C ATOM 3594 N TYR C 218 27.629 16.172 5.084 1.00 24.20 N ANISOU 3594 N TYR C 218 1906 4640 2650 -112 -223 68 N ATOM 3595 CA TYR C 218 29.006 16.461 4.706 1.00 27.86 C ANISOU 3595 CA TYR C 218 2277 5227 3081 -153 -205 75 C ATOM 3596 C TYR C 218 29.671 15.262 4.035 1.00 29.11 C ANISOU 3596 C TYR C 218 2374 5429 3257 0 -179 97 C ATOM 3597 O TYR C 218 30.349 15.407 3.017 1.00 29.45 O ANISOU 3597 O TYR C 218 2365 5532 3292 -7 -137 92 O ATOM 3598 CB TYR C 218 29.812 16.891 5.933 1.00 30.09 C ANISOU 3598 CB TYR C 218 2521 5601 3313 -231 -249 84 C ATOM 3599 CG TYR C 218 31.312 16.846 5.745 1.00 31.50 C ANISOU 3599 CG TYR C 218 2587 5927 3456 -236 -241 102 C ATOM 3600 CD1 TYR C 218 31.997 17.927 5.204 1.00 31.94 C ANISOU 3600 CD1 TYR C 218 2609 6048 3479 -374 -217 85 C ATOM 3601 CD2 TYR C 218 32.045 15.727 6.121 1.00 34.79 C ANISOU 3601 CD2 TYR C 218 2932 6416 3869 -105 -257 138 C ATOM 3602 CE1 TYR C 218 33.370 17.891 5.037 1.00 33.89 C ANISOU 3602 CE1 TYR C 218 2746 6441 3689 -382 -210 103 C ATOM 3603 CE2 TYR C 218 33.417 15.681 5.955 1.00 38.14 C ANISOU 3603 CE2 TYR C 218 3247 6986 4259 -105 -251 155 C ATOM 3604 CZ TYR C 218 34.075 16.765 5.414 1.00 37.31 C ANISOU 3604 CZ TYR C 218 3101 6956 4120 -244 -228 136 C ATOM 3605 OH TYR C 218 35.441 16.721 5.252 1.00 38.98 O ANISOU 3605 OH TYR C 218 3195 7323 4293 -247 -222 154 O ATOM 3606 N ALA C 219 29.476 14.080 4.614 1.00 23.71 N ANISOU 3606 N ALA C 219 1703 4710 2595 135 -202 123 N ATOM 3607 CA ALA C 219 30.103 12.864 4.105 1.00 24.43 C ANISOU 3607 CA ALA C 219 1752 4825 2704 287 -180 142 C ATOM 3608 C ALA C 219 29.632 12.546 2.690 1.00 24.60 C ANISOU 3608 C ALA C 219 1809 4779 2761 346 -124 116 C ATOM 3609 O ALA C 219 30.384 11.997 1.884 1.00 25.88 O ANISOU 3609 O ALA C 219 1923 4989 2923 423 -87 115 O ATOM 3610 CB ALA C 219 29.818 11.691 5.035 1.00 21.69 C ANISOU 3610 CB ALA C 219 1440 4423 2377 411 -215 176 C ATOM 3611 N LEU C 220 28.384 12.895 2.394 1.00 23.06 N ANISOU 3611 N LEU C 220 1696 4475 2590 311 -117 92 N ATOM 3612 CA LEU C 220 27.808 12.640 1.082 1.00 26.01 C ANISOU 3612 CA LEU C 220 2110 4782 2991 360 -66 64 C ATOM 3613 C LEU C 220 28.448 13.528 0.018 1.00 28.22 C ANISOU 3613 C LEU C 220 2338 5144 3240 271 -21 47 C ATOM 3614 O LEU C 220 28.602 13.118 -1.131 1.00 29.54 O ANISOU 3614 O LEU C 220 2502 5311 3411 333 29 30 O ATOM 3615 CB LEU C 220 26.293 12.857 1.111 1.00 27.62 C ANISOU 3615 CB LEU C 220 2408 4863 3225 338 -76 47 C ATOM 3616 CG LEU C 220 25.485 12.100 0.057 1.00 25.81 C ANISOU 3616 CG LEU C 220 2269 4508 3029 426 -36 21 C ATOM 3617 CD1 LEU C 220 25.804 10.615 0.117 1.00 27.18 C ANISOU 3617 CD1 LEU C 220 2433 4668 3226 589 -35 33 C ATOM 3618 CD2 LEU C 220 24.000 12.332 0.263 1.00 22.41 C ANISOU 3618 CD2 LEU C 220 1977 3913 2624 381 -50 9 C ATOM 3619 N MET C 221 28.814 14.745 0.407 1.00 30.01 N ANISOU 3619 N MET C 221 2533 5435 3433 119 -35 50 N ATOM 3620 CA MET C 221 29.463 15.679 -0.505 1.00 30.58 C ANISOU 3620 CA MET C 221 2564 5583 3472 12 6 42 C ATOM 3621 C MET C 221 30.958 15.406 -0.612 1.00 32.87 C ANISOU 3621 C MET C 221 2751 6011 3730 38 16 59 C ATOM 3622 O MET C 221 31.549 15.537 -1.683 1.00 32.65 O ANISOU 3622 O MET C 221 2682 6041 3681 31 64 53 O ATOM 3623 CB MET C 221 29.242 17.124 -0.050 1.00 30.49 C ANISOU 3623 CB MET C 221 2580 5564 3438 -172 -11 38 C ATOM 3624 CG MET C 221 27.792 17.547 0.083 1.00 27.60 C ANISOU 3624 CG MET C 221 2318 5068 3102 -212 -21 21 C ATOM 3625 SD MET C 221 27.654 19.224 0.730 1.00 25.88 S ANISOU 3625 SD MET C 221 2164 4813 2856 -424 -40 10 S ATOM 3626 CE MET C 221 28.488 20.158 -0.548 1.00 41.94 C ANISOU 3626 CE MET C 221 4156 6924 4856 -543 20 17 C ATOM 3627 N GLU C 222 31.567 15.033 0.509 1.00 32.07 N ANISOU 3627 N GLU C 222 2602 5965 3617 68 -30 81 N ATOM 3628 CA GLU C 222 33.012 14.837 0.564 1.00 35.69 C ANISOU 3628 CA GLU C 222 2951 6570 4040 86 -28 100 C ATOM 3629 C GLU C 222 33.464 13.585 -0.187 1.00 36.53 C ANISOU 3629 C GLU C 222 3023 6693 4163 256 8 103 C ATOM 3630 O GLU C 222 34.467 13.609 -0.897 1.00 40.51 O ANISOU 3630 O GLU C 222 3447 7305 4639 262 42 104 O ATOM 3631 CB GLU C 222 33.482 14.770 2.019 1.00 33.64 C ANISOU 3631 CB GLU C 222 2654 6368 3759 73 -89 125 C ATOM 3632 N LYS C 223 32.723 12.495 -0.029 1.00 35.04 N ANISOU 3632 N LYS C 223 2900 6394 4018 393 1 102 N ATOM 3633 CA LYS C 223 33.090 11.229 -0.653 1.00 39.21 C ANISOU 3633 CA LYS C 223 3419 6913 4566 559 33 100 C ATOM 3634 C LYS C 223 31.868 10.366 -0.951 1.00 39.83 C ANISOU 3634 C LYS C 223 3613 6825 4695 660 44 80 C ATOM 3635 O LYS C 223 30.749 10.702 -0.577 1.00 38.45 O ANISOU 3635 O LYS C 223 3517 6553 4541 609 21 73 O ATOM 3636 CB LYS C 223 34.076 10.468 0.239 1.00 43.40 C ANISOU 3636 CB LYS C 223 3877 7526 5088 649 1 137 C ATOM 3637 CG LYS C 223 33.679 10.425 1.705 1.00 45.28 C ANISOU 3637 CG LYS C 223 4144 7729 5331 632 -64 167 C ATOM 3638 CD LYS C 223 34.817 9.941 2.590 1.00 47.93 C ANISOU 3638 CD LYS C 223 4387 8183 5640 690 -98 209 C ATOM 3639 CE LYS C 223 34.424 9.977 4.061 1.00 49.64 C ANISOU 3639 CE LYS C 223 4634 8374 5851 660 -163 239 C ATOM 3640 NZ LYS C 223 35.549 9.558 4.945 1.00 51.88 N ANISOU 3640 NZ LYS C 223 4824 8785 6103 711 -198 283 N ATOM 3641 N GLY C 224 32.091 9.254 -1.640 1.00 41.87 N ANISOU 3641 N GLY C 224 3886 7052 4973 800 79 67 N ATOM 3642 CA GLY C 224 31.013 8.355 -1.999 1.00 43.46 C ANISOU 3642 CA GLY C 224 4202 7093 5217 894 93 42 C ATOM 3643 C GLY C 224 30.683 8.378 -3.479 1.00 43.92 C ANISOU 3643 C GLY C 224 4298 7117 5271 902 154 -7 C ATOM 3644 O GLY C 224 31.271 9.136 -4.252 1.00 43.01 O ANISOU 3644 O GLY C 224 4121 7105 5118 832 189 -17 O ATOM 3645 N VAL C 225 29.727 7.544 -3.868 1.00 43.36 N ANISOU 3645 N VAL C 225 4336 6904 5235 982 167 -37 N ATOM 3646 CA VAL C 225 29.398 7.352 -5.275 1.00 39.77 C ANISOU 3646 CA VAL C 225 3931 6408 4771 1007 225 -89 C ATOM 3647 C VAL C 225 28.617 8.518 -5.878 1.00 36.43 C ANISOU 3647 C VAL C 225 3531 5985 4325 881 238 -109 C ATOM 3648 O VAL C 225 28.735 8.797 -7.070 1.00 41.90 O ANISOU 3648 O VAL C 225 4222 6714 4986 861 289 -140 O ATOM 3649 CB VAL C 225 28.584 6.057 -5.478 1.00 38.84 C ANISOU 3649 CB VAL C 225 3934 6128 4694 1122 232 -121 C ATOM 3650 CG1 VAL C 225 29.480 4.838 -5.322 1.00 41.44 C ANISOU 3650 CG1 VAL C 225 4248 6458 5040 1260 242 -112 C ATOM 3651 CG2 VAL C 225 27.423 6.003 -4.499 1.00 36.94 C ANISOU 3651 CG2 VAL C 225 3771 5771 4491 1098 180 -103 C ATOM 3652 N GLU C 226 27.832 9.204 -5.054 1.00 28.92 N ANISOU 3652 N GLU C 226 2603 4998 3389 797 195 -89 N ATOM 3653 CA GLU C 226 26.902 10.213 -5.551 1.00 29.24 C ANISOU 3653 CA GLU C 226 2680 5014 3415 692 206 -106 C ATOM 3654 C GLU C 226 27.522 11.602 -5.719 1.00 23.93 C ANISOU 3654 C GLU C 226 1929 4464 2700 550 218 -85 C ATOM 3655 O GLU C 226 26.953 12.458 -6.399 1.00 20.35 O ANISOU 3655 O GLU C 226 1505 4005 2225 462 243 -96 O ATOM 3656 CB GLU C 226 25.693 10.305 -4.616 1.00 35.27 C ANISOU 3656 CB GLU C 226 3516 5670 4216 667 155 -96 C ATOM 3657 CG GLU C 226 25.078 8.959 -4.263 1.00 40.15 C ANISOU 3657 CG GLU C 226 4215 6162 4878 791 137 -106 C ATOM 3658 CD GLU C 226 23.962 9.075 -3.242 1.00 42.04 C ANISOU 3658 CD GLU C 226 4543 6280 5150 736 82 -86 C ATOM 3659 OE1 GLU C 226 23.321 10.145 -3.178 1.00 41.79 O ANISOU 3659 OE1 GLU C 226 4546 6221 5109 613 68 -82 O ATOM 3660 OE2 GLU C 226 23.729 8.095 -2.500 1.00 43.69 O ANISOU 3660 OE2 GLU C 226 4788 6421 5392 820 56 -70 O ATOM 3661 N LYS C 227 28.684 11.820 -5.111 1.00 24.39 N ANISOU 3661 N LYS C 227 1895 4629 2743 523 200 -53 N ATOM 3662 CA LYS C 227 29.248 13.166 -4.988 1.00 25.98 C ANISOU 3662 CA LYS C 227 2032 4931 2908 367 198 -31 C ATOM 3663 C LYS C 227 29.555 13.842 -6.324 1.00 24.58 C ANISOU 3663 C LYS C 227 1841 4811 2687 298 259 -42 C ATOM 3664 O LYS C 227 29.316 15.039 -6.486 1.00 25.16 O ANISOU 3664 O LYS C 227 1926 4894 2739 157 266 -31 O ATOM 3665 CB LYS C 227 30.521 13.130 -4.137 1.00 32.52 C ANISOU 3665 CB LYS C 227 2763 5872 3721 361 168 0 C ATOM 3666 CG LYS C 227 31.702 12.445 -4.800 1.00 39.69 C ANISOU 3666 CG LYS C 227 3598 6875 4609 451 206 -2 C ATOM 3667 CD LYS C 227 32.938 12.498 -3.916 1.00 46.48 C ANISOU 3667 CD LYS C 227 4352 7860 5447 438 173 31 C ATOM 3668 CE LYS C 227 34.135 11.860 -4.605 1.00 51.83 C ANISOU 3668 CE LYS C 227 4946 8644 6103 528 214 30 C ATOM 3669 NZ LYS C 227 35.369 11.943 -3.775 1.00 54.94 N ANISOU 3669 NZ LYS C 227 5227 9178 6471 514 182 64 N ATOM 3670 N GLU C 228 30.086 13.086 -7.279 1.00 26.30 N ANISOU 3670 N GLU C 228 2042 5061 2890 394 304 -62 N ATOM 3671 CA GLU C 228 30.500 13.676 -8.547 1.00 27.76 C ANISOU 3671 CA GLU C 228 2208 5313 3026 332 362 -69 C ATOM 3672 C GLU C 228 29.299 14.173 -9.345 1.00 23.47 C ANISOU 3672 C GLU C 228 1763 4684 2470 281 388 -85 C ATOM 3673 O GLU C 228 29.337 15.257 -9.929 1.00 21.71 O ANISOU 3673 O GLU C 228 1545 4497 2209 156 415 -67 O ATOM 3674 CB GLU C 228 31.309 12.675 -9.370 1.00 32.64 C ANISOU 3674 CB GLU C 228 2790 5983 3629 457 406 -92 C ATOM 3675 CG GLU C 228 32.496 13.305 -10.079 1.00 42.00 C ANISOU 3675 CG GLU C 228 3885 7313 4762 385 448 -76 C ATOM 3676 CD GLU C 228 33.425 14.030 -9.120 1.00 46.11 C ANISOU 3676 CD GLU C 228 4309 7938 5274 288 411 -35 C ATOM 3677 OE1 GLU C 228 33.902 15.133 -9.465 1.00 47.50 O ANISOU 3677 OE1 GLU C 228 4447 8191 5411 148 428 -14 O ATOM 3678 OE2 GLU C 228 33.682 13.496 -8.021 1.00 47.82 O ANISOU 3678 OE2 GLU C 228 4492 8157 5519 348 363 -23 O ATOM 3679 N ALA C 229 28.232 13.382 -9.364 1.00 20.62 N ANISOU 3679 N ALA C 229 1487 4208 2139 375 379 -117 N ATOM 3680 CA ALA C 229 27.008 13.779 -10.046 1.00 21.38 C ANISOU 3680 CA ALA C 229 1682 4221 2219 336 396 -134 C ATOM 3681 C ALA C 229 26.359 14.971 -9.342 1.00 21.06 C ANISOU 3681 C ALA C 229 1702 4103 2198 196 347 -96 C ATOM 3682 O ALA C 229 25.893 15.911 -9.989 1.00 20.24 O ANISOU 3682 O ALA C 229 1664 3962 2065 99 360 -80 O ATOM 3683 CB ALA C 229 26.040 12.610 -10.121 1.00 21.72 C ANISOU 3683 CB ALA C 229 1828 4128 2299 456 376 -176 C ATOM 3684 N LEU C 230 26.330 14.922 -8.013 1.00 17.72 N ANISOU 3684 N LEU C 230 1260 3654 1817 193 293 -81 N ATOM 3685 CA LEU C 230 25.829 16.033 -7.212 1.00 19.15 C ANISOU 3685 CA LEU C 230 1493 3770 2013 67 251 -54 C ATOM 3686 C LEU C 230 26.580 17.321 -7.535 1.00 16.54 C ANISOU 3686 C LEU C 230 1116 3531 1638 -80 280 -25 C ATOM 3687 O LEU C 230 25.975 18.383 -7.692 1.00 19.50 O ANISOU 3687 O LEU C 230 1578 3824 2005 -186 276 -7 O ATOM 3688 CB LEU C 230 25.949 15.716 -5.719 1.00 18.79 C ANISOU 3688 CB LEU C 230 1412 3722 2005 88 195 -44 C ATOM 3689 CG LEU C 230 25.007 14.647 -5.162 1.00 21.01 C ANISOU 3689 CG LEU C 230 1766 3882 2335 200 158 -61 C ATOM 3690 CD1 LEU C 230 25.351 14.335 -3.716 1.00 21.44 C ANISOU 3690 CD1 LEU C 230 1769 3967 2411 221 109 -42 C ATOM 3691 CD2 LEU C 230 23.556 15.091 -5.287 1.00 23.96 C ANISOU 3691 CD2 LEU C 230 2276 4101 2727 158 140 -67 C ATOM 3692 N LYS C 231 27.900 17.215 -7.643 1.00 17.66 N ANISOU 3692 N LYS C 231 1117 3842 1749 -85 311 -17 N ATOM 3693 CA LYS C 231 28.736 18.366 -7.960 1.00 22.37 C ANISOU 3693 CA LYS C 231 1665 4533 2302 -235 339 11 C ATOM 3694 C LYS C 231 28.442 18.896 -9.363 1.00 18.66 C ANISOU 3694 C LYS C 231 1255 4049 1787 -283 399 20 C ATOM 3695 O LYS C 231 28.420 20.106 -9.582 1.00 20.96 O ANISOU 3695 O LYS C 231 1591 4321 2053 -429 411 51 O ATOM 3696 CB LYS C 231 30.218 18.003 -7.828 1.00 26.02 C ANISOU 3696 CB LYS C 231 2014 5124 2748 -208 336 15 C ATOM 3697 CG LYS C 231 31.162 19.189 -7.951 1.00 30.54 C ANISOU 3697 CG LYS C 231 2545 5778 3279 -370 346 43 C ATOM 3698 CD LYS C 231 32.596 18.789 -7.628 1.00 35.62 C ANISOU 3698 CD LYS C 231 3066 6562 3906 -338 336 48 C ATOM 3699 CE LYS C 231 33.527 19.990 -7.668 1.00 39.79 C ANISOU 3699 CE LYS C 231 3554 7174 4393 -510 342 73 C ATOM 3700 NZ LYS C 231 34.929 19.616 -7.325 1.00 43.03 N ANISOU 3700 NZ LYS C 231 3833 7735 4779 -482 330 79 N ATOM 3701 N ARG C 232 28.214 17.988 -10.308 1.00 18.64 N ANISOU 3701 N ARG C 232 1268 4043 1771 -161 432 -8 N ATOM 3702 CA ARG C 232 27.850 18.382 -11.667 1.00 22.35 C ANISOU 3702 CA ARG C 232 1806 4496 2188 -192 482 -1 C ATOM 3703 C ARG C 232 26.498 19.093 -11.697 1.00 21.23 C ANISOU 3703 C ARG C 232 1825 4177 2065 -245 445 16 C ATOM 3704 O ARG C 232 26.314 20.057 -12.439 1.00 18.02 O ANISOU 3704 O ARG C 232 1479 3750 1617 -341 470 51 O ATOM 3705 CB ARG C 232 27.811 17.169 -12.601 1.00 21.14 C ANISOU 3705 CB ARG C 232 1658 4356 2020 -43 514 -46 C ATOM 3706 CG ARG C 232 29.169 16.561 -12.915 1.00 24.69 C ANISOU 3706 CG ARG C 232 2006 4916 2457 18 537 -58 C ATOM 3707 CD ARG C 232 29.064 15.585 -14.078 1.00 23.94 C ANISOU 3707 CD ARG C 232 1944 4817 2333 137 580 -104 C ATOM 3708 NE ARG C 232 28.051 14.561 -13.837 1.00 20.43 N ANISOU 3708 NE ARG C 232 1573 4266 1925 256 555 -149 N ATOM 3709 CZ ARG C 232 28.317 13.332 -13.409 1.00 19.96 C ANISOU 3709 CZ ARG C 232 1492 4186 1907 391 541 -184 C ATOM 3710 NH1 ARG C 232 29.570 12.962 -13.181 1.00 21.06 N ANISOU 3710 NH1 ARG C 232 1533 4415 2053 433 549 -176 N ATOM 3711 NH2 ARG C 232 27.330 12.469 -13.213 1.00 19.20 N ANISOU 3711 NH2 ARG C 232 1477 3975 1843 482 518 -223 N ATOM 3712 N ARG C 233 25.554 18.608 -10.896 1.00 19.56 N ANISOU 3712 N ARG C 233 1678 3841 1912 -178 387 -5 N ATOM 3713 CA ARG C 233 24.228 19.213 -10.838 1.00 19.64 C ANISOU 3713 CA ARG C 233 1826 3694 1943 -210 350 8 C ATOM 3714 C ARG C 233 24.301 20.622 -10.259 1.00 19.67 C ANISOU 3714 C ARG C 233 1863 3660 1950 -353 338 50 C ATOM 3715 O ARG C 233 23.645 21.539 -10.754 1.00 15.86 O ANISOU 3715 O ARG C 233 1480 3094 1451 -415 341 81 O ATOM 3716 CB ARG C 233 23.270 18.351 -10.010 1.00 19.02 C ANISOU 3716 CB ARG C 233 1792 3508 1926 -113 295 -22 C ATOM 3717 CG ARG C 233 22.853 17.054 -10.685 1.00 19.54 C ANISOU 3717 CG ARG C 233 1874 3560 1991 15 303 -66 C ATOM 3718 CD ARG C 233 21.833 16.288 -9.846 1.00 19.67 C ANISOU 3718 CD ARG C 233 1946 3461 2067 87 250 -88 C ATOM 3719 NE ARG C 233 21.426 15.042 -10.494 1.00 20.79 N ANISOU 3719 NE ARG C 233 2114 3577 2207 194 257 -134 N ATOM 3720 CZ ARG C 233 20.378 14.925 -11.306 1.00 20.77 C ANISOU 3720 CZ ARG C 233 2198 3505 2189 205 249 -149 C ATOM 3721 NH1 ARG C 233 20.088 13.751 -11.853 1.00 13.61 N ANISOU 3721 NH1 ARG C 233 1316 2576 1277 292 255 -199 N ATOM 3722 NH2 ARG C 233 19.619 15.980 -11.571 1.00 16.82 N ANISOU 3722 NH2 ARG C 233 1759 2956 1674 131 234 -115 N ATOM 3723 N TRP C 234 25.100 20.786 -9.209 1.00 19.24 N ANISOU 3723 N TRP C 234 1729 3668 1913 -404 321 50 N ATOM 3724 CA TRP C 234 25.310 22.098 -8.602 1.00 20.29 C ANISOU 3724 CA TRP C 234 1892 3772 2044 -554 311 78 C ATOM 3725 C TRP C 234 25.926 23.075 -9.594 1.00 17.59 C ANISOU 3725 C TRP C 234 1553 3485 1645 -675 366 118 C ATOM 3726 O TRP C 234 25.415 24.176 -9.802 1.00 19.78 O ANISOU 3726 O TRP C 234 1942 3658 1914 -764 369 151 O ATOM 3727 CB TRP C 234 26.207 21.992 -7.367 1.00 19.73 C ANISOU 3727 CB TRP C 234 1716 3791 1988 -591 283 66 C ATOM 3728 CG TRP C 234 26.812 23.309 -6.981 1.00 17.77 C ANISOU 3728 CG TRP C 234 1472 3563 1718 -771 287 89 C ATOM 3729 CD1 TRP C 234 26.182 24.350 -6.364 1.00 23.47 C ANISOU 3729 CD1 TRP C 234 2311 4150 2456 -862 262 94 C ATOM 3730 CD2 TRP C 234 28.167 23.731 -7.198 1.00 19.08 C ANISOU 3730 CD2 TRP C 234 1521 3890 1839 -885 321 107 C ATOM 3731 NE1 TRP C 234 27.058 25.392 -6.183 1.00 25.01 N ANISOU 3731 NE1 TRP C 234 2483 4399 2620 -1033 276 111 N ATOM 3732 CE2 TRP C 234 28.282 25.038 -6.684 1.00 24.67 C ANISOU 3732 CE2 TRP C 234 2291 4543 2538 -1058 311 121 C ATOM 3733 CE3 TRP C 234 29.290 23.130 -7.773 1.00 19.98 C ANISOU 3733 CE3 TRP C 234 1508 4161 1924 -841 349 107 C ATOM 3734 CZ2 TRP C 234 29.477 25.754 -6.728 1.00 24.88 C ANISOU 3734 CZ2 TRP C 234 2273 4649 2532 -1176 316 132 C ATOM 3735 CZ3 TRP C 234 30.475 23.845 -7.818 1.00 25.23 C ANISOU 3735 CZ3 TRP C 234 2123 4907 2557 -954 353 121 C ATOM 3736 CH2 TRP C 234 30.558 25.142 -7.299 1.00 23.23 C ANISOU 3736 CH2 TRP C 234 1940 4591 2296 -1123 336 133 C ATOM 3737 N ARG C 235 27.032 22.665 -10.202 1.00 18.49 N ANISOU 3737 N ARG C 235 1544 3764 1717 -674 413 119 N ATOM 3738 CA ARG C 235 27.757 23.519 -11.133 1.00 19.63 C ANISOU 3738 CA ARG C 235 1670 3988 1799 -798 473 161 C ATOM 3739 C ARG C 235 26.908 23.909 -12.345 1.00 19.46 C ANISOU 3739 C ARG C 235 1776 3874 1744 -790 499 190 C ATOM 3740 O ARG C 235 26.994 25.036 -12.833 1.00 20.13 O ANISOU 3740 O ARG C 235 1925 3929 1793 -917 527 241 O ATOM 3741 CB ARG C 235 29.045 22.827 -11.585 1.00 22.29 C ANISOU 3741 CB ARG C 235 1868 4488 2112 -747 499 144 C ATOM 3742 CG ARG C 235 29.783 23.550 -12.692 1.00 27.24 C ANISOU 3742 CG ARG C 235 2497 5168 2685 -835 546 179 C ATOM 3743 CD ARG C 235 31.211 23.045 -12.812 1.00 31.10 C ANISOU 3743 CD ARG C 235 2844 5815 3159 -806 559 163 C ATOM 3744 NE ARG C 235 31.902 23.637 -13.952 1.00 35.44 N ANISOU 3744 NE ARG C 235 3386 6427 3654 -882 611 194 N ATOM 3745 CZ ARG C 235 33.205 23.511 -14.182 1.00 35.90 C ANISOU 3745 CZ ARG C 235 3327 6626 3686 -895 632 192 C ATOM 3746 NH1 ARG C 235 33.965 22.820 -13.343 1.00 34.64 N ANISOU 3746 NH1 ARG C 235 3052 6559 3549 -833 601 164 N ATOM 3747 NH2 ARG C 235 33.748 24.081 -15.247 1.00 35.88 N ANISOU 3747 NH2 ARG C 235 3325 6676 3632 -968 683 223 N ATOM 3748 N TRP C 236 26.084 22.982 -12.824 1.00 21.28 N ANISOU 3748 N TRP C 236 2045 4058 1983 -645 488 162 N ATOM 3749 CA TRP C 236 25.216 23.261 -13.966 1.00 27.93 C ANISOU 3749 CA TRP C 236 3000 4825 2786 -627 503 188 C ATOM 3750 C TRP C 236 24.210 24.371 -13.669 1.00 21.94 C ANISOU 3750 C TRP C 236 2386 3897 2053 -689 467 228 C ATOM 3751 O TRP C 236 24.077 25.320 -14.441 1.00 20.71 O ANISOU 3751 O TRP C 236 2309 3706 1853 -767 494 285 O ATOM 3752 CB TRP C 236 24.472 21.998 -14.399 1.00 32.08 C ANISOU 3752 CB TRP C 236 3539 5331 3319 -468 487 139 C ATOM 3753 CG TRP C 236 23.381 22.273 -15.390 1.00 40.86 C ANISOU 3753 CG TRP C 236 4771 6357 4396 -446 481 162 C ATOM 3754 CD1 TRP C 236 22.055 22.465 -15.120 1.00 43.99 C ANISOU 3754 CD1 TRP C 236 5274 6609 4830 -410 426 169 C ATOM 3755 CD2 TRP C 236 23.523 22.403 -16.810 1.00 45.99 C ANISOU 3755 CD2 TRP C 236 5440 7074 4958 -458 531 187 C ATOM 3756 NE1 TRP C 236 21.364 22.699 -16.283 1.00 47.12 N ANISOU 3756 NE1 TRP C 236 5750 6982 5170 -396 433 198 N ATOM 3757 CE2 TRP C 236 22.241 22.665 -17.335 1.00 47.36 C ANISOU 3757 CE2 TRP C 236 5735 7138 5120 -426 496 209 C ATOM 3758 CE3 TRP C 236 24.607 22.318 -17.687 1.00 48.25 C ANISOU 3758 CE3 TRP C 236 5648 7513 5170 -490 604 193 C ATOM 3759 CZ2 TRP C 236 22.016 22.844 -18.698 1.00 50.06 C ANISOU 3759 CZ2 TRP C 236 6128 7517 5375 -429 525 240 C ATOM 3760 CZ3 TRP C 236 24.381 22.495 -19.041 1.00 50.59 C ANISOU 3760 CZ3 TRP C 236 6000 7843 5379 -494 640 221 C ATOM 3761 CH2 TRP C 236 23.096 22.755 -19.533 1.00 50.36 C ANISOU 3761 CH2 TRP C 236 6098 7701 5337 -465 598 245 C ATOM 3762 N GLN C 237 23.496 24.241 -12.557 1.00 20.71 N ANISOU 3762 N GLN C 237 2267 3637 1966 -647 409 202 N ATOM 3763 CA GLN C 237 22.515 25.248 -12.166 1.00 23.81 C ANISOU 3763 CA GLN C 237 2792 3868 2387 -686 378 232 C ATOM 3764 C GLN C 237 23.185 26.590 -11.898 1.00 23.01 C ANISOU 3764 C GLN C 237 2724 3748 2272 -849 400 273 C ATOM 3765 O GLN C 237 22.683 27.638 -12.305 1.00 21.84 O ANISOU 3765 O GLN C 237 2697 3494 2109 -904 409 324 O ATOM 3766 CB GLN C 237 21.734 24.795 -10.930 1.00 24.09 C ANISOU 3766 CB GLN C 237 2842 3817 2493 -612 320 189 C ATOM 3767 CG GLN C 237 20.735 25.832 -10.422 1.00 27.33 C ANISOU 3767 CG GLN C 237 3383 4067 2935 -640 292 213 C ATOM 3768 CD GLN C 237 19.782 25.272 -9.381 1.00 28.18 C ANISOU 3768 CD GLN C 237 3506 4098 3102 -549 241 172 C ATOM 3769 OE1 GLN C 237 19.065 24.303 -9.636 1.00 27.95 O ANISOU 3769 OE1 GLN C 237 3465 4070 3087 -439 221 150 O ATOM 3770 NE2 GLN C 237 19.768 25.884 -8.199 1.00 25.08 N ANISOU 3770 NE2 GLN C 237 3145 3642 2743 -603 222 160 N ATOM 3771 N GLN C 238 24.323 26.552 -11.212 1.00 20.14 N ANISOU 3771 N GLN C 238 2255 3487 1910 -926 409 253 N ATOM 3772 CA GLN C 238 25.068 27.768 -10.920 1.00 21.62 C ANISOU 3772 CA GLN C 238 2464 3671 2081 -1103 430 285 C ATOM 3773 C GLN C 238 25.571 28.417 -12.203 1.00 22.45 C ANISOU 3773 C GLN C 238 2589 3824 2117 -1194 492 347 C ATOM 3774 O GLN C 238 25.639 29.641 -12.305 1.00 23.92 O ANISOU 3774 O GLN C 238 2872 3928 2287 -1327 510 394 O ATOM 3775 CB GLN C 238 26.242 27.475 -9.988 1.00 24.00 C ANISOU 3775 CB GLN C 238 2623 4108 2389 -1167 422 250 C ATOM 3776 CG GLN C 238 27.011 28.717 -9.582 1.00 28.51 C ANISOU 3776 CG GLN C 238 3215 4676 2943 -1366 435 272 C ATOM 3777 CD GLN C 238 26.136 29.721 -8.860 1.00 30.84 C ANISOU 3777 CD GLN C 238 3675 4770 3272 -1417 405 273 C ATOM 3778 OE1 GLN C 238 25.459 29.385 -7.888 1.00 32.78 O ANISOU 3778 OE1 GLN C 238 3947 4943 3566 -1337 356 230 O ATOM 3779 NE2 GLN C 238 26.137 30.959 -9.338 1.00 31.78 N ANISOU 3779 NE2 GLN C 238 3914 4789 3370 -1534 432 319 N ATOM 3780 N THR C 239 25.926 27.591 -13.181 1.00 22.37 N ANISOU 3780 N THR C 239 2494 3943 2063 -1124 528 346 N ATOM 3781 CA THR C 239 26.361 28.090 -14.476 1.00 27.22 C ANISOU 3781 CA THR C 239 3128 4603 2612 -1180 581 398 C ATOM 3782 C THR C 239 25.245 28.889 -15.143 1.00 27.11 C ANISOU 3782 C THR C 239 3286 4440 2574 -1188 583 461 C ATOM 3783 O THR C 239 25.469 29.994 -15.638 1.00 28.76 O ANISOU 3783 O THR C 239 3577 4585 2764 -1283 602 515 O ATOM 3784 CB THR C 239 26.797 26.943 -15.403 1.00 28.10 C ANISOU 3784 CB THR C 239 3131 4862 2684 -1070 612 370 C ATOM 3785 OG1 THR C 239 27.990 26.339 -14.888 1.00 26.14 O ANISOU 3785 OG1 THR C 239 2728 4750 2455 -1062 611 323 O ATOM 3786 CG2 THR C 239 27.063 27.460 -16.815 1.00 30.22 C ANISOU 3786 CG2 THR C 239 3443 5152 2888 -1106 657 420 C ATOM 3787 N GLN C 240 24.039 28.331 -15.135 1.00 27.37 N ANISOU 3787 N GLN C 240 3378 4384 2636 -1044 539 439 N ATOM 3788 CA GLN C 240 22.891 28.976 -15.761 1.00 31.02 C ANISOU 3788 CA GLN C 240 3993 4708 3086 -1010 524 494 C ATOM 3789 C GLN C 240 22.579 30.321 -15.111 1.00 35.67 C ANISOU 3789 C GLN C 240 4710 5132 3709 -1106 511 535 C ATOM 3790 O GLN C 240 22.220 31.276 -15.796 1.00 37.30 O ANISOU 3790 O GLN C 240 5040 5250 3882 -1149 528 611 O ATOM 3791 CB GLN C 240 21.667 28.062 -15.700 1.00 32.67 C ANISOU 3791 CB GLN C 240 4219 4865 3330 -841 470 452 C ATOM 3792 CG GLN C 240 21.912 26.687 -16.292 1.00 39.33 C ANISOU 3792 CG GLN C 240 4953 5846 4142 -744 481 400 C ATOM 3793 CD GLN C 240 22.670 26.747 -17.606 1.00 45.59 C ANISOU 3793 CD GLN C 240 5716 6765 4840 -791 546 437 C ATOM 3794 OE1 GLN C 240 22.356 27.552 -18.483 1.00 48.19 O ANISOU 3794 OE1 GLN C 240 6141 7056 5114 -834 564 508 O ATOM 3795 NE2 GLN C 240 23.685 25.902 -17.741 1.00 46.80 N ANISOU 3795 NE2 GLN C 240 5738 7075 4971 -780 585 391 N ATOM 3796 N GLN C 241 22.727 30.402 -13.793 1.00 36.76 N ANISOU 3796 N GLN C 241 4829 5228 3911 -1137 482 487 N ATOM 3797 CA GLN C 241 22.497 31.661 -13.095 1.00 41.90 C ANISOU 3797 CA GLN C 241 5608 5720 4593 -1231 473 510 C ATOM 3798 C GLN C 241 23.605 32.665 -13.402 1.00 43.25 C ANISOU 3798 C GLN C 241 5795 5916 4721 -1421 524 558 C ATOM 3799 O GLN C 241 23.338 33.851 -13.590 1.00 48.48 O ANISOU 3799 O GLN C 241 6599 6433 5389 -1473 529 605 O ATOM 3800 CB GLN C 241 22.395 31.443 -11.585 1.00 48.56 C ANISOU 3800 CB GLN C 241 6423 6524 5505 -1218 429 437 C ATOM 3801 CG GLN C 241 21.858 32.655 -10.837 1.00 56.11 C ANISOU 3801 CG GLN C 241 7534 7290 6496 -1277 416 447 C ATOM 3802 CD GLN C 241 21.998 32.525 -9.333 1.00 60.54 C ANISOU 3802 CD GLN C 241 8060 7836 7105 -1298 381 372 C ATOM 3803 OE1 GLN C 241 22.771 31.705 -8.839 1.00 62.01 O ANISOU 3803 OE1 GLN C 241 8102 8167 7292 -1309 370 325 O ATOM 3804 NE2 GLN C 241 21.249 33.338 -8.596 1.00 62.22 N ANISOU 3804 NE2 GLN C 241 8409 7878 7355 -1298 364 362 N ATOM 3805 N ASN C 242 24.845 32.184 -13.448 1.00 39.38 N ANISOU 3805 N ASN C 242 5151 5597 4215 -1468 541 524 N ATOM 3806 CA ASN C 242 25.990 33.034 -13.763 1.00 40.45 C ANISOU 3806 CA ASN C 242 5270 5768 4331 -1599 567 543 C ATOM 3807 C ASN C 242 25.848 33.721 -15.117 1.00 43.17 C ANISOU 3807 C ASN C 242 5706 6068 4628 -1612 604 622 C ATOM 3808 O ASN C 242 26.261 34.869 -15.288 1.00 43.18 O ANISOU 3808 O ASN C 242 5787 5996 4625 -1723 619 659 O ATOM 3809 CB ASN C 242 27.289 32.222 -13.738 1.00 38.36 C ANISOU 3809 CB ASN C 242 4811 5716 4049 -1614 578 499 C ATOM 3810 CG ASN C 242 27.783 31.949 -12.329 1.00 36.95 C ANISOU 3810 CG ASN C 242 4546 5582 3911 -1648 538 432 C ATOM 3811 OD1 ASN C 242 27.285 32.524 -11.360 1.00 37.59 O ANISOU 3811 OD1 ASN C 242 4720 5533 4030 -1689 506 415 O ATOM 3812 ND2 ASN C 242 28.779 31.078 -12.210 1.00 34.77 N ANISOU 3812 ND2 ASN C 242 4096 5491 3625 -1623 538 394 N ATOM 3813 N LYS C 243 25.269 33.008 -16.077 1.00 44.00 N ANISOU 3813 N LYS C 243 5803 6221 4694 -1499 617 647 N ATOM 3814 CA LYS C 243 25.078 33.544 -17.419 1.00 46.05 C ANISOU 3814 CA LYS C 243 6143 6454 4899 -1495 649 724 C ATOM 3815 C LYS C 243 24.139 34.744 -17.396 1.00 49.35 C ANISOU 3815 C LYS C 243 6754 6659 5337 -1506 633 787 C ATOM 3816 O LYS C 243 24.225 35.630 -18.247 1.00 52.17 O ANISOU 3816 O LYS C 243 7195 6963 5663 -1550 659 858 O ATOM 3817 CB LYS C 243 24.533 32.463 -18.356 1.00 42.81 C ANISOU 3817 CB LYS C 243 5689 6138 4437 -1359 655 725 C ATOM 3818 N GLU C 244 23.245 34.767 -16.413 1.00 51.47 N ANISOU 3818 N GLU C 244 7091 6806 5659 -1458 592 762 N ATOM 3819 CA GLU C 244 22.284 35.855 -16.272 1.00 55.31 C ANISOU 3819 CA GLU C 244 7760 7081 6175 -1440 574 812 C ATOM 3820 C GLU C 244 22.968 37.149 -15.845 1.00 59.78 C ANISOU 3820 C GLU C 244 8399 7546 6768 -1579 587 818 C ATOM 3821 O GLU C 244 22.426 38.238 -16.033 1.00 63.80 O ANISOU 3821 O GLU C 244 9061 7889 7290 -1579 588 872 O ATOM 3822 CB GLU C 244 21.197 35.479 -15.265 1.00 53.70 C ANISOU 3822 CB GLU C 244 7601 6782 6021 -1345 529 772 C ATOM 3823 N SER C 245 24.161 37.025 -15.273 1.00 59.94 N ANISOU 3823 N SER C 245 8309 7672 6794 -1694 596 761 N ATOM 3824 CA SER C 245 24.903 38.185 -14.793 1.00 60.73 C ANISOU 3824 CA SER C 245 8466 7696 6911 -1841 604 755 C ATOM 3825 C SER C 245 26.191 38.392 -15.583 1.00 59.50 C ANISOU 3825 C SER C 245 8226 7676 6706 -1956 645 781 C ATOM 3826 O SER C 245 26.916 39.361 -15.363 1.00 60.25 O ANISOU 3826 O SER C 245 8363 7729 6803 -2092 657 783 O ATOM 3827 CB SER C 245 25.219 38.038 -13.303 1.00 61.42 C ANISOU 3827 CB SER C 245 8507 7786 7044 -1892 570 663 C ATOM 3828 N GLY C 246 26.468 37.475 -16.504 1.00 57.85 N ANISOU 3828 N GLY C 246 7900 7631 6449 -1899 669 796 N ATOM 3829 CA GLY C 246 27.663 37.554 -17.324 1.00 58.39 C ANISOU 3829 CA GLY C 246 7877 7842 6466 -1990 713 820 C ATOM 3830 C GLY C 246 28.911 37.049 -16.624 1.00 56.95 C ANISOU 3830 C GLY C 246 7524 7827 6288 -2068 709 747 C ATOM 3831 O GLY C 246 30.026 37.277 -17.091 1.00 58.09 O ANISOU 3831 O GLY C 246 7592 8084 6394 -2167 742 760 O ATOM 3832 N LEU C 247 28.727 36.355 -15.505 1.00 54.11 N ANISOU 3832 N LEU C 247 7100 7488 5969 -2020 667 675 N ATOM 3833 CA LEU C 247 29.851 35.839 -14.727 1.00 53.49 C ANISOU 3833 CA LEU C 247 6859 7570 5896 -2075 652 608 C ATOM 3834 C LEU C 247 30.382 34.523 -15.286 1.00 52.76 C ANISOU 3834 C LEU C 247 6587 7686 5773 -1982 671 587 C ATOM 3835 O LEU C 247 29.612 33.630 -15.640 1.00 52.67 O ANISOU 3835 O LEU C 247 6565 7686 5760 -1843 670 584 O ATOM 3836 CB LEU C 247 29.448 35.648 -13.262 1.00 51.85 C ANISOU 3836 CB LEU C 247 6659 7301 5742 -2058 597 541 C ATOM 3837 CG LEU C 247 30.464 34.902 -12.390 1.00 51.93 C ANISOU 3837 CG LEU C 247 6489 7487 5755 -2078 571 473 C ATOM 3838 CD1 LEU C 247 31.767 35.685 -12.278 1.00 53.31 C ANISOU 3838 CD1 LEU C 247 6620 7736 5901 -2241 579 472 C ATOM 3839 CD2 LEU C 247 29.888 34.602 -11.013 1.00 50.32 C ANISOU 3839 CD2 LEU C 247 6300 7221 5599 -2038 518 413 C ATOM 3840 N VAL C 248 31.705 34.409 -15.352 1.00 51.57 N ANISOU 3840 N VAL C 248 6300 7700 5595 -2056 687 571 N ATOM 3841 CA VAL C 248 32.352 33.188 -15.817 1.00 47.60 C ANISOU 3841 CA VAL C 248 5623 7398 5065 -1963 707 544 C ATOM 3842 C VAL C 248 33.421 32.721 -14.833 1.00 45.75 C ANISOU 3842 C VAL C 248 5230 7311 4843 -1991 677 485 C ATOM 3843 O VAL C 248 34.385 33.437 -14.565 1.00 47.90 O ANISOU 3843 O VAL C 248 5471 7631 5099 -2129 677 488 O ATOM 3844 CB VAL C 248 32.994 33.381 -17.203 1.00 48.03 C ANISOU 3844 CB VAL C 248 5650 7544 5057 -1996 769 595 C ATOM 3845 CG1 VAL C 248 33.758 32.130 -17.611 1.00 46.69 C ANISOU 3845 CG1 VAL C 248 5298 7583 4860 -1897 792 558 C ATOM 3846 CG2 VAL C 248 31.931 33.727 -18.235 1.00 48.12 C ANISOU 3846 CG2 VAL C 248 5810 7429 5045 -1949 795 658 C ATOM 3847 N TYR C 249 33.238 31.519 -14.296 1.00 42.40 N ANISOU 3847 N TYR C 249 4709 6957 4444 -1857 649 435 N ATOM 3848 CA TYR C 249 34.202 30.931 -13.371 1.00 39.50 C ANISOU 3848 CA TYR C 249 4186 6735 4085 -1851 616 385 C ATOM 3849 C TYR C 249 35.299 30.173 -14.111 1.00 37.13 C ANISOU 3849 C TYR C 249 3724 6639 3745 -1799 654 381 C ATOM 3850 O TYR C 249 35.045 29.545 -15.138 1.00 38.14 O ANISOU 3850 O TYR C 249 3841 6799 3852 -1696 695 392 O ATOM 3851 CB TYR C 249 33.501 29.981 -12.397 1.00 34.46 C ANISOU 3851 CB TYR C 249 3525 6074 3496 -1724 568 336 C ATOM 3852 CG TYR C 249 32.778 30.654 -11.252 1.00 34.73 C ANISOU 3852 CG TYR C 249 3673 5952 3569 -1787 520 321 C ATOM 3853 CD1 TYR C 249 33.136 31.925 -10.822 1.00 36.14 C ANISOU 3853 CD1 TYR C 249 3929 6061 3741 -1954 509 330 C ATOM 3854 CD2 TYR C 249 31.741 30.007 -10.592 1.00 30.44 C ANISOU 3854 CD2 TYR C 249 3164 5333 3070 -1679 488 293 C ATOM 3855 CE1 TYR C 249 32.475 32.534 -9.768 1.00 34.04 C ANISOU 3855 CE1 TYR C 249 3778 5648 3509 -2004 469 308 C ATOM 3856 CE2 TYR C 249 31.074 30.607 -9.542 1.00 30.12 C ANISOU 3856 CE2 TYR C 249 3229 5152 3063 -1732 447 276 C ATOM 3857 CZ TYR C 249 31.444 31.869 -9.133 1.00 31.77 C ANISOU 3857 CZ TYR C 249 3519 5289 3263 -1891 438 280 C ATOM 3858 OH TYR C 249 30.776 32.461 -8.084 1.00 31.44 O ANISOU 3858 OH TYR C 249 3592 5102 3253 -1935 402 254 O ATOM 3859 N THR C 250 36.519 30.230 -13.587 1.00 36.13 N ANISOU 3859 N THR C 250 3475 6650 3602 -1868 639 365 N ATOM 3860 CA THR C 250 37.578 29.358 -14.074 1.00 33.44 C ANISOU 3860 CA THR C 250 2965 6512 3229 -1794 667 354 C ATOM 3861 C THR C 250 37.447 28.005 -13.386 1.00 35.26 C ANISOU 3861 C THR C 250 3103 6801 3494 -1618 632 305 C ATOM 3862 O THR C 250 36.702 27.869 -12.414 1.00 30.99 O ANISOU 3862 O THR C 250 2615 6163 2997 -1586 581 282 O ATOM 3863 CB THR C 250 38.981 29.938 -13.817 1.00 35.47 C ANISOU 3863 CB THR C 250 3119 6911 3450 -1934 667 361 C ATOM 3864 OG1 THR C 250 39.170 30.137 -12.410 1.00 40.44 O ANISOU 3864 OG1 THR C 250 3731 7534 4102 -1988 601 331 O ATOM 3865 CG2 THR C 250 39.155 31.261 -14.545 1.00 39.59 C ANISOU 3865 CG2 THR C 250 3734 7373 3936 -2110 707 412 C ATOM 3866 N GLU C 251 38.167 27.009 -13.892 1.00 35.31 N ANISOU 3866 N GLU C 251 2976 6961 3479 -1502 660 291 N ATOM 3867 CA GLU C 251 38.115 25.661 -13.334 1.00 36.26 C ANISOU 3867 CA GLU C 251 3013 7133 3631 -1320 632 249 C ATOM 3868 C GLU C 251 38.465 25.647 -11.849 1.00 37.43 C ANISOU 3868 C GLU C 251 3109 7309 3805 -1346 562 229 C ATOM 3869 O GLU C 251 37.942 24.834 -11.084 1.00 36.12 O ANISOU 3869 O GLU C 251 2940 7104 3679 -1226 522 201 O ATOM 3870 CB GLU C 251 39.061 24.731 -14.099 1.00 37.82 C ANISOU 3870 CB GLU C 251 3075 7499 3797 -1208 678 239 C ATOM 3871 N ASP C 252 39.345 26.557 -11.444 1.00 39.24 N ANISOU 3871 N ASP C 252 3299 7604 4004 -1507 549 244 N ATOM 3872 CA ASP C 252 39.781 26.625 -10.055 1.00 42.30 C ANISOU 3872 CA ASP C 252 3636 8034 4401 -1547 483 226 C ATOM 3873 C ASP C 252 38.805 27.413 -9.184 1.00 41.67 C ANISOU 3873 C ASP C 252 3702 7779 4354 -1637 439 217 C ATOM 3874 O ASP C 252 38.635 27.109 -8.002 1.00 39.87 O ANISOU 3874 O ASP C 252 3463 7537 4148 -1604 382 192 O ATOM 3875 CB ASP C 252 41.175 27.241 -9.962 1.00 47.71 C ANISOU 3875 CB ASP C 252 4215 8879 5034 -1684 486 240 C ATOM 3876 CG ASP C 252 41.657 27.363 -8.533 1.00 52.06 C ANISOU 3876 CG ASP C 252 4716 9483 5582 -1736 417 222 C ATOM 3877 OD1 ASP C 252 42.154 26.358 -7.981 1.00 52.62 O ANISOU 3877 OD1 ASP C 252 4668 9671 5656 -1608 391 209 O ATOM 3878 OD2 ASP C 252 41.538 28.467 -7.961 1.00 53.16 O ANISOU 3878 OD2 ASP C 252 4941 9543 5713 -1902 392 221 O ATOM 3879 N GLU C 253 38.169 28.426 -9.765 1.00 40.26 N ANISOU 3879 N GLU C 253 3661 7462 4173 -1748 466 239 N ATOM 3880 CA GLU C 253 37.156 29.191 -9.045 1.00 37.63 C ANISOU 3880 CA GLU C 253 3482 6943 3872 -1822 433 231 C ATOM 3881 C GLU C 253 35.957 28.303 -8.728 1.00 32.24 C ANISOU 3881 C GLU C 253 2846 6164 3240 -1665 412 210 C ATOM 3882 O GLU C 253 35.299 28.472 -7.700 1.00 29.31 O ANISOU 3882 O GLU C 253 2543 5693 2899 -1676 367 188 O ATOM 3883 CB GLU C 253 36.719 30.417 -9.849 1.00 39.49 C ANISOU 3883 CB GLU C 253 3865 7043 4096 -1954 472 268 C ATOM 3884 CG GLU C 253 37.777 31.504 -9.943 1.00 45.02 C ANISOU 3884 CG GLU C 253 4553 7802 4752 -2141 485 286 C ATOM 3885 CD GLU C 253 37.320 32.697 -10.761 1.00 48.11 C ANISOU 3885 CD GLU C 253 5102 8044 5134 -2260 526 329 C ATOM 3886 OE1 GLU C 253 37.038 32.522 -11.966 1.00 47.52 O ANISOU 3886 OE1 GLU C 253 5048 7960 5048 -2206 577 366 O ATOM 3887 OE2 GLU C 253 37.238 33.809 -10.198 1.00 48.96 O ANISOU 3887 OE2 GLU C 253 5321 8040 5243 -2403 507 327 O ATOM 3888 N TRP C 254 35.681 27.352 -9.616 1.00 30.37 N ANISOU 3888 N TRP C 254 2572 5960 3008 -1519 448 215 N ATOM 3889 CA TRP C 254 34.634 26.368 -9.377 1.00 28.22 C ANISOU 3889 CA TRP C 254 2327 5618 2779 -1361 432 193 C ATOM 3890 C TRP C 254 34.964 25.524 -8.148 1.00 32.17 C ANISOU 3890 C TRP C 254 2732 6190 3302 -1275 376 160 C ATOM 3891 O TRP C 254 34.088 25.225 -7.334 1.00 31.80 O ANISOU 3891 O TRP C 254 2737 6051 3294 -1222 338 141 O ATOM 3892 CB TRP C 254 34.443 25.473 -10.603 1.00 28.44 C ANISOU 3892 CB TRP C 254 2326 5682 2797 -1223 484 197 C ATOM 3893 CG TRP C 254 33.584 26.086 -11.670 1.00 28.71 C ANISOU 3893 CG TRP C 254 2491 5601 2818 -1263 529 228 C ATOM 3894 CD1 TRP C 254 33.965 26.437 -12.934 1.00 31.30 C ANISOU 3894 CD1 TRP C 254 2823 5969 3099 -1302 586 259 C ATOM 3895 CD2 TRP C 254 32.195 26.420 -11.562 1.00 28.62 C ANISOU 3895 CD2 TRP C 254 2623 5418 2833 -1263 519 236 C ATOM 3896 NE1 TRP C 254 32.897 26.967 -13.620 1.00 29.90 N ANISOU 3896 NE1 TRP C 254 2790 5654 2917 -1322 609 289 N ATOM 3897 CE2 TRP C 254 31.799 26.968 -12.799 1.00 29.33 C ANISOU 3897 CE2 TRP C 254 2805 5450 2889 -1297 568 276 C ATOM 3898 CE3 TRP C 254 31.248 26.311 -10.538 1.00 27.52 C ANISOU 3898 CE3 TRP C 254 2545 5171 2740 -1236 473 215 C ATOM 3899 CZ2 TRP C 254 30.497 27.403 -13.041 1.00 24.32 C ANISOU 3899 CZ2 TRP C 254 2321 4655 2263 -1298 570 301 C ATOM 3900 CZ3 TRP C 254 29.955 26.743 -10.779 1.00 26.93 C ANISOU 3900 CZ3 TRP C 254 2615 4939 2677 -1242 480 236 C ATOM 3901 CH2 TRP C 254 29.592 27.283 -12.022 1.00 25.61 C ANISOU 3901 CH2 TRP C 254 2539 4718 2473 -1269 527 280 C ATOM 3902 N GLN C 255 36.232 25.146 -8.019 1.00 35.03 N ANISOU 3902 N GLN C 255 2955 6719 3635 -1260 372 159 N ATOM 3903 CA GLN C 255 36.692 24.384 -6.863 1.00 38.68 C ANISOU 3903 CA GLN C 255 3325 7263 4109 -1181 319 139 C ATOM 3904 C GLN C 255 36.606 25.212 -5.586 1.00 36.83 C ANISOU 3904 C GLN C 255 3141 6978 3875 -1308 263 129 C ATOM 3905 O GLN C 255 36.299 24.687 -4.515 1.00 35.42 O ANISOU 3905 O GLN C 255 2957 6783 3720 -1241 213 111 O ATOM 3906 CB GLN C 255 38.128 23.896 -7.077 1.00 45.30 C ANISOU 3906 CB GLN C 255 4005 8298 4909 -1144 331 147 C ATOM 3907 CG GLN C 255 38.241 22.659 -7.949 1.00 49.44 C ANISOU 3907 CG GLN C 255 4465 8880 5440 -959 372 143 C ATOM 3908 CD GLN C 255 37.672 21.424 -7.275 1.00 53.35 C ANISOU 3908 CD GLN C 255 4958 9331 5981 -778 338 122 C ATOM 3909 OE1 GLN C 255 37.259 20.475 -7.940 1.00 55.64 O ANISOU 3909 OE1 GLN C 255 5258 9592 6291 -629 368 110 O ATOM 3910 NE2 GLN C 255 37.653 21.429 -5.945 1.00 54.51 N ANISOU 3910 NE2 GLN C 255 5099 9471 6141 -793 275 118 N ATOM 3911 N LYS C 256 36.878 26.507 -5.706 1.00 37.11 N ANISOU 3911 N LYS C 256 3234 6984 3881 -1493 272 139 N ATOM 3912 CA LYS C 256 36.823 27.404 -4.561 1.00 29.35 C ANISOU 3912 CA LYS C 256 2317 5943 2893 -1628 226 123 C ATOM 3913 C LYS C 256 35.394 27.538 -4.039 1.00 32.31 C ANISOU 3913 C LYS C 256 2833 6130 3314 -1605 205 104 C ATOM 3914 O LYS C 256 35.163 27.524 -2.829 1.00 32.20 O ANISOU 3914 O LYS C 256 2838 6087 3308 -1610 154 79 O ATOM 3915 CB LYS C 256 37.384 28.778 -4.929 1.00 32.70 C ANISOU 3915 CB LYS C 256 2790 6356 3277 -1829 248 137 C ATOM 3916 N GLU C 257 34.440 27.666 -4.957 1.00 28.18 N ANISOU 3916 N GLU C 257 2408 5485 2816 -1579 245 119 N ATOM 3917 CA GLU C 257 33.032 27.737 -4.590 1.00 27.87 C ANISOU 3917 CA GLU C 257 2496 5272 2820 -1547 232 106 C ATOM 3918 C GLU C 257 32.575 26.430 -3.957 1.00 26.91 C ANISOU 3918 C GLU C 257 2313 5179 2733 -1378 199 86 C ATOM 3919 O GLU C 257 31.836 26.428 -2.973 1.00 27.77 O ANISOU 3919 O GLU C 257 2481 5202 2868 -1370 159 64 O ATOM 3920 CB GLU C 257 32.170 28.059 -5.811 1.00 27.73 C ANISOU 3920 CB GLU C 257 2583 5139 2814 -1542 286 135 C ATOM 3921 CG GLU C 257 32.430 29.433 -6.391 1.00 29.43 C ANISOU 3921 CG GLU C 257 2894 5286 3001 -1705 317 162 C ATOM 3922 CD GLU C 257 32.233 30.534 -5.373 1.00 30.57 C ANISOU 3922 CD GLU C 257 3152 5314 3149 -1838 283 140 C ATOM 3923 OE1 GLU C 257 31.284 30.449 -4.566 1.00 29.33 O ANISOU 3923 OE1 GLU C 257 3071 5048 3027 -1799 253 115 O ATOM 3924 OE2 GLU C 257 33.037 31.488 -5.370 1.00 33.76 O ANISOU 3924 OE2 GLU C 257 3573 5737 3520 -1981 289 145 O ATOM 3925 N TRP C 258 33.025 25.318 -4.528 1.00 28.65 N ANISOU 3925 N TRP C 258 2420 5514 2952 -1242 217 94 N ATOM 3926 CA TRP C 258 32.655 24.004 -4.018 1.00 27.71 C ANISOU 3926 CA TRP C 258 2248 5415 2866 -1069 189 79 C ATOM 3927 C TRP C 258 33.198 23.805 -2.607 1.00 26.83 C ANISOU 3927 C TRP C 258 2079 5369 2748 -1072 127 65 C ATOM 3928 O TRP C 258 32.482 23.343 -1.719 1.00 23.85 O ANISOU 3928 O TRP C 258 1731 4930 2400 -1007 88 50 O ATOM 3929 CB TRP C 258 33.162 22.901 -4.950 1.00 27.49 C ANISOU 3929 CB TRP C 258 2122 5489 2833 -924 225 86 C ATOM 3930 CG TRP C 258 32.820 21.523 -4.481 1.00 29.24 C ANISOU 3930 CG TRP C 258 2305 5715 3091 -740 200 72 C ATOM 3931 CD1 TRP C 258 33.683 20.582 -4.000 1.00 30.34 C ANISOU 3931 CD1 TRP C 258 2338 5965 3226 -632 177 73 C ATOM 3932 CD2 TRP C 258 31.515 20.933 -4.433 1.00 30.13 C ANISOU 3932 CD2 TRP C 258 2491 5708 3248 -641 196 59 C ATOM 3933 NE1 TRP C 258 32.998 19.440 -3.664 1.00 32.15 N ANISOU 3933 NE1 TRP C 258 2582 6138 3496 -472 159 62 N ATOM 3934 CE2 TRP C 258 31.666 19.630 -3.919 1.00 31.97 C ANISOU 3934 CE2 TRP C 258 2666 5978 3504 -478 169 51 C ATOM 3935 CE3 TRP C 258 30.235 21.380 -4.777 1.00 29.49 C ANISOU 3935 CE3 TRP C 258 2523 5493 3187 -675 212 56 C ATOM 3936 CZ2 TRP C 258 30.584 18.770 -3.740 1.00 31.26 C ANISOU 3936 CZ2 TRP C 258 2628 5792 3458 -354 157 37 C ATOM 3937 CZ3 TRP C 258 29.164 20.524 -4.600 1.00 27.82 C ANISOU 3937 CZ3 TRP C 258 2349 5204 3017 -552 201 41 C ATOM 3938 CH2 TRP C 258 29.345 19.234 -4.087 1.00 29.28 C ANISOU 3938 CH2 TRP C 258 2475 5425 3225 -395 173 30 C ATOM 3939 N ASN C 259 34.459 24.171 -2.400 1.00 26.68 N ANISOU 3939 N ASN C 259 1977 5477 2685 -1151 119 72 N ATOM 3940 CA ASN C 259 35.084 24.018 -1.092 1.00 29.96 C ANISOU 3940 CA ASN C 259 2331 5972 3079 -1161 63 64 C ATOM 3941 C ASN C 259 34.338 24.792 -0.013 1.00 30.08 C ANISOU 3941 C ASN C 259 2458 5870 3101 -1260 23 39 C ATOM 3942 O ASN C 259 34.178 24.309 1.109 1.00 27.67 O ANISOU 3942 O ASN C 259 2141 5571 2800 -1205 -25 29 O ATOM 3943 CB ASN C 259 36.548 24.461 -1.139 1.00 34.71 C ANISOU 3943 CB ASN C 259 2830 6734 3625 -1257 65 76 C ATOM 3944 CG ASN C 259 37.411 23.527 -1.962 1.00 38.10 C ANISOU 3944 CG ASN C 259 3129 7303 4044 -1136 97 96 C ATOM 3945 OD1 ASN C 259 37.011 22.403 -2.268 1.00 37.85 O ANISOU 3945 OD1 ASN C 259 3078 7256 4046 -964 108 98 O ATOM 3946 ND2 ASN C 259 38.606 23.985 -2.319 1.00 39.27 N ANISOU 3946 ND2 ASN C 259 3189 7588 4143 -1225 114 110 N ATOM 3947 N GLU C 260 33.872 25.988 -0.362 1.00 29.01 N ANISOU 3947 N GLU C 260 2441 5620 2964 -1401 45 32 N ATOM 3948 CA GLU C 260 33.092 26.801 0.564 1.00 28.95 C ANISOU 3948 CA GLU C 260 2560 5476 2962 -1493 17 2 C ATOM 3949 C GLU C 260 31.799 26.094 0.965 1.00 27.16 C ANISOU 3949 C GLU C 260 2390 5144 2786 -1372 -1 -10 C ATOM 3950 O GLU C 260 31.380 26.161 2.121 1.00 29.02 O ANISOU 3950 O GLU C 260 2671 5334 3023 -1381 -44 -35 O ATOM 3951 CB GLU C 260 32.778 28.166 -0.052 1.00 30.13 C ANISOU 3951 CB GLU C 260 2843 5499 3107 -1645 54 2 C ATOM 3952 N LEU C 261 31.169 25.420 0.007 1.00 26.35 N ANISOU 3952 N LEU C 261 2285 5008 2720 -1262 32 7 N ATOM 3953 CA LEU C 261 29.953 24.659 0.283 1.00 24.26 C ANISOU 3953 CA LEU C 261 2061 4655 2502 -1143 17 -3 C ATOM 3954 C LEU C 261 30.252 23.485 1.204 1.00 25.31 C ANISOU 3954 C LEU C 261 2101 4878 2639 -1013 -30 -4 C ATOM 3955 O LEU C 261 29.459 23.158 2.087 1.00 27.03 O ANISOU 3955 O LEU C 261 2362 5032 2877 -966 -67 -19 O ATOM 3956 CB LEU C 261 29.317 24.160 -1.014 1.00 25.51 C ANISOU 3956 CB LEU C 261 2227 4774 2689 -1054 67 16 C ATOM 3957 CG LEU C 261 28.502 25.174 -1.819 1.00 25.60 C ANISOU 3957 CG LEU C 261 2368 4649 2708 -1150 111 25 C ATOM 3958 CD1 LEU C 261 28.042 24.565 -3.135 1.00 24.79 C ANISOU 3958 CD1 LEU C 261 2275 4525 2620 -1036 159 46 C ATOM 3959 CD2 LEU C 261 27.311 25.662 -1.007 1.00 22.93 C ANISOU 3959 CD2 LEU C 261 2181 4133 2399 -1158 81 0 C ATOM 3960 N ILE C 262 31.400 22.853 0.992 1.00 25.37 N ANISOU 3960 N ILE C 262 1986 5030 2624 -953 -27 16 N ATOM 3961 CA ILE C 262 31.830 21.748 1.837 1.00 27.87 C ANISOU 3961 CA ILE C 262 2219 5431 2939 -827 -68 25 C ATOM 3962 C ILE C 262 32.146 22.227 3.251 1.00 27.25 C ANISOU 3962 C ILE C 262 2148 5380 2827 -912 -121 13 C ATOM 3963 O ILE C 262 31.826 21.555 4.232 1.00 28.59 O ANISOU 3963 O ILE C 262 2317 5542 3004 -831 -163 15 O ATOM 3964 CB ILE C 262 33.063 21.040 1.250 1.00 32.93 C ANISOU 3964 CB ILE C 262 2732 6219 3560 -747 -47 49 C ATOM 3965 CG1 ILE C 262 32.678 20.285 -0.024 1.00 33.23 C ANISOU 3965 CG1 ILE C 262 2766 6227 3631 -624 3 55 C ATOM 3966 CG2 ILE C 262 33.674 20.095 2.276 1.00 34.24 C ANISOU 3966 CG2 ILE C 262 2818 6476 3716 -643 -93 65 C ATOM 3967 CD1 ILE C 262 33.847 19.625 -0.721 1.00 37.99 C ANISOU 3967 CD1 ILE C 262 3256 6964 4214 -543 32 72 C ATOM 3968 N LYS C 263 32.773 23.393 3.348 1.00 26.89 N ANISOU 3968 N LYS C 263 2116 5363 2739 -1078 -117 2 N ATOM 3969 CA LYS C 263 33.147 23.946 4.641 1.00 28.10 C ANISOU 3969 CA LYS C 263 2280 5548 2851 -1174 -163 -16 C ATOM 3970 C LYS C 263 31.913 24.243 5.493 1.00 26.87 C ANISOU 3970 C LYS C 263 2249 5247 2713 -1192 -188 -47 C ATOM 3971 O LYS C 263 31.885 23.945 6.685 1.00 25.95 O ANISOU 3971 O LYS C 263 2127 5154 2578 -1168 -233 -54 O ATOM 3972 CB LYS C 263 33.984 25.209 4.451 1.00 33.21 C ANISOU 3972 CB LYS C 263 2933 6234 3450 -1359 -148 -26 C ATOM 3973 CG LYS C 263 34.654 25.703 5.719 1.00 39.06 C ANISOU 3973 CG LYS C 263 3658 7047 4136 -1459 -193 -44 C ATOM 3974 CD LYS C 263 35.773 26.677 5.399 1.00 44.22 C ANISOU 3974 CD LYS C 263 4276 7787 4739 -1619 -177 -45 C ATOM 3975 CE LYS C 263 36.374 27.247 6.673 1.00 48.78 C ANISOU 3975 CE LYS C 263 4848 8430 5258 -1733 -221 -68 C ATOM 3976 NZ LYS C 263 36.869 26.178 7.586 1.00 50.50 N ANISOU 3976 NZ LYS C 263 4949 8783 5456 -1618 -268 -47 N ATOM 3977 N LEU C 264 30.890 24.820 4.870 1.00 26.86 N ANISOU 3977 N LEU C 264 2362 5099 2745 -1232 -157 -64 N ATOM 3978 CA LEU C 264 29.643 25.138 5.563 1.00 26.56 C ANISOU 3978 CA LEU C 264 2449 4915 2726 -1244 -175 -97 C ATOM 3979 C LEU C 264 28.977 23.886 6.120 1.00 26.36 C ANISOU 3979 C LEU C 264 2396 4890 2728 -1084 -207 -86 C ATOM 3980 O LEU C 264 28.455 23.892 7.234 1.00 28.95 O ANISOU 3980 O LEU C 264 2778 5177 3045 -1083 -243 -108 O ATOM 3981 CB LEU C 264 28.673 25.861 4.626 1.00 27.24 C ANISOU 3981 CB LEU C 264 2655 4848 2848 -1294 -131 -108 C ATOM 3982 CG LEU C 264 29.051 27.276 4.188 1.00 30.63 C ANISOU 3982 CG LEU C 264 3165 5220 3253 -1461 -98 -119 C ATOM 3983 CD1 LEU C 264 28.049 27.803 3.170 1.00 28.43 C ANISOU 3983 CD1 LEU C 264 3003 4785 3014 -1479 -52 -114 C ATOM 3984 CD2 LEU C 264 29.129 28.196 5.395 1.00 33.02 C ANISOU 3984 CD2 LEU C 264 3552 5477 3518 -1574 -125 -162 C ATOM 3985 N ALA C 265 28.992 22.816 5.333 1.00 24.97 N ANISOU 3985 N ALA C 265 2145 4756 2585 -948 -191 -54 N ATOM 3986 CA ALA C 265 28.384 21.557 5.743 1.00 26.57 C ANISOU 3986 CA ALA C 265 2329 4950 2818 -787 -218 -38 C ATOM 3987 C ALA C 265 29.176 20.895 6.870 1.00 29.61 C ANISOU 3987 C ALA C 265 2639 5441 3169 -733 -262 -18 C ATOM 3988 O ALA C 265 28.613 20.185 7.701 1.00 28.24 O ANISOU 3988 O ALA C 265 2486 5241 3003 -648 -296 -9 O ATOM 3989 CB ALA C 265 28.270 20.618 4.555 1.00 25.59 C ANISOU 3989 CB ALA C 265 2155 4833 2736 -657 -183 -13 C ATOM 3990 N SER C 266 30.484 21.138 6.892 1.00 31.15 N ANISOU 3990 N SER C 266 2748 5762 3325 -787 -262 -6 N ATOM 3991 CA SER C 266 31.370 20.517 7.873 1.00 33.48 C ANISOU 3991 CA SER C 266 2958 6178 3584 -737 -303 19 C ATOM 3992 C SER C 266 31.240 21.122 9.269 1.00 31.54 C ANISOU 3992 C SER C 266 2764 5927 3294 -831 -346 -4 C ATOM 3993 O SER C 266 31.400 20.426 10.269 1.00 35.19 O ANISOU 3993 O SER C 266 3194 6441 3738 -761 -386 17 O ATOM 3994 CB SER C 266 32.825 20.626 7.414 1.00 35.85 C ANISOU 3994 CB SER C 266 3143 6628 3850 -770 -289 37 C ATOM 3995 OG SER C 266 33.274 21.970 7.464 1.00 37.40 O ANISOU 3995 OG SER C 266 3363 6843 4005 -956 -282 9 O ATOM 3996 N GLN C 289 30.957 22.419 9.330 1.00 29.75 N ANISOU 3996 N GLN C 289 2624 5632 3049 -988 -335 -48 N ATOM 3997 CA GLN C 289 30.969 23.145 10.597 1.00 30.44 C ANISOU 3997 CA GLN C 289 2764 5716 3085 -1095 -369 -81 C ATOM 3998 C GLN C 289 29.595 23.213 11.262 1.00 32.35 C ANISOU 3998 C GLN C 289 3130 5821 3342 -1077 -381 -111 C ATOM 3999 O GLN C 289 28.656 23.778 10.703 1.00 31.52 O ANISOU 3999 O GLN C 289 3126 5582 3268 -1111 -351 -140 O ATOM 4000 CB GLN C 289 31.508 24.561 10.384 1.00 28.96 C ANISOU 4000 CB GLN C 289 2616 5523 2863 -1280 -349 -116 C ATOM 4001 N PRO C 290 29.478 22.635 12.468 1.00 34.75 N ANISOU 4001 N PRO C 290 3425 6160 3617 -1021 -423 -101 N ATOM 4002 CA PRO C 290 28.235 22.714 13.240 1.00 33.29 C ANISOU 4002 CA PRO C 290 3356 5863 3431 -1009 -435 -131 C ATOM 4003 C PRO C 290 27.861 24.162 13.543 1.00 32.07 C ANISOU 4003 C PRO C 290 3324 5612 3250 -1164 -418 -199 C ATOM 4004 O PRO C 290 28.735 24.963 13.875 1.00 32.26 O ANISOU 4004 O PRO C 290 3334 5694 3229 -1285 -423 -220 O ATOM 4005 CB PRO C 290 28.567 21.950 14.527 1.00 35.09 C ANISOU 4005 CB PRO C 290 3533 6185 3615 -948 -484 -102 C ATOM 4006 CG PRO C 290 29.691 21.044 14.149 1.00 35.58 C ANISOU 4006 CG PRO C 290 3455 6381 3684 -862 -494 -43 C ATOM 4007 CD PRO C 290 30.497 21.817 13.148 1.00 35.29 C ANISOU 4007 CD PRO C 290 3376 6380 3651 -958 -461 -57 C ATOM 4008 N GLY C 291 26.580 24.492 13.413 1.00 30.91 N ANISOU 4008 N GLY C 291 3299 5317 3130 -1158 -397 -234 N ATOM 4009 CA GLY C 291 26.107 25.832 13.707 1.00 32.46 C ANISOU 4009 CA GLY C 291 3633 5395 3306 -1282 -374 -301 C ATOM 4010 C GLY C 291 26.097 26.757 12.505 1.00 33.26 C ANISOU 4010 C GLY C 291 3791 5405 3442 -1363 -327 -317 C ATOM 4011 O GLY C 291 25.547 27.856 12.566 1.00 35.57 O ANISOU 4011 O GLY C 291 4220 5563 3732 -1446 -298 -369 O ATOM 4012 N GLU C 292 26.708 26.321 11.409 1.00 32.90 N ANISOU 4012 N GLU C 292 3647 5427 3428 -1334 -315 -272 N ATOM 4013 CA GLU C 292 26.720 27.118 10.187 1.00 32.53 C ANISOU 4013 CA GLU C 292 3647 5302 3411 -1406 -268 -275 C ATOM 4014 C GLU C 292 25.424 26.950 9.402 1.00 23.44 C ANISOU 4014 C GLU C 292 2575 4015 2316 -1336 -241 -278 C ATOM 4015 O GLU C 292 24.970 25.829 9.176 1.00 20.77 O ANISOU 4015 O GLU C 292 2177 3708 2008 -1209 -255 -249 O ATOM 4016 CB GLU C 292 27.917 26.741 9.307 1.00 38.38 C ANISOU 4016 CB GLU C 292 4250 6180 4154 -1404 -260 -227 C ATOM 4017 CG GLU C 292 29.253 27.222 9.842 1.00 45.24 C ANISOU 4017 CG GLU C 292 5053 7172 4964 -1510 -277 -228 C ATOM 4018 CD GLU C 292 29.325 28.734 9.935 1.00 50.74 C ANISOU 4018 CD GLU C 292 5872 7773 5634 -1677 -254 -274 C ATOM 4019 OE1 GLU C 292 28.935 29.411 8.960 1.00 50.68 O ANISOU 4019 OE1 GLU C 292 5949 7651 5658 -1723 -211 -277 O ATOM 4020 OE2 GLU C 292 29.766 29.245 10.986 1.00 54.59 O ANISOU 4020 OE2 GLU C 292 6378 8296 6069 -1762 -279 -305 O ATOM 4021 N ASER C 293 24.832 28.068 8.991 0.44 22.69 N ANISOU 4021 N ASER C 293 2621 3766 2236 -1415 -203 -311 N ATOM 4022 N BSER C 293 24.831 28.070 8.995 0.56 22.65 N ANISOU 4022 N BSER C 293 2616 3760 2230 -1415 -203 -311 N ATOM 4023 CA ASER C 293 23.615 28.033 8.188 0.44 21.51 C ANISOU 4023 CA ASER C 293 2562 3469 2142 -1333 -166 -305 C ATOM 4024 CA BSER C 293 23.619 28.042 8.181 0.56 21.53 C ANISOU 4024 CA BSER C 293 2565 3471 2144 -1334 -166 -305 C ATOM 4025 C ASER C 293 23.907 27.474 6.796 0.44 20.16 C ANISOU 4025 C ASER C 293 2309 3339 2013 -1268 -139 -246 C ATOM 4026 C BSER C 293 23.911 27.459 6.801 0.56 20.20 C ANISOU 4026 C BSER C 293 2312 3345 2017 -1267 -140 -246 C ATOM 4027 O ASER C 293 25.039 27.538 6.318 0.44 19.12 O ANISOU 4027 O ASER C 293 2076 3329 1860 -1352 -141 -227 O ATOM 4028 O BSER C 293 25.050 27.494 6.332 0.56 18.92 O ANISOU 4028 O BSER C 293 2046 3308 1835 -1349 -143 -226 O ATOM 4029 CB ASER C 293 22.997 29.428 8.088 0.44 22.69 C ANISOU 4029 CB ASER C 293 2892 3434 2296 -1418 -126 -346 C ATOM 4030 CB BSER C 293 23.024 29.445 8.052 0.56 22.77 C ANISOU 4030 CB BSER C 293 2900 3444 2306 -1421 -125 -345 C ATOM 4031 OG ASER C 293 23.938 30.371 7.609 0.44 23.76 O ANISOU 4031 OG ASER C 293 3037 3579 2412 -1563 -107 -343 O ATOM 4032 OG BSER C 293 22.591 29.932 9.309 0.56 23.62 O ANISOU 4032 OG BSER C 293 3102 3495 2376 -1458 -140 -408 O ATOM 4033 N LEU C 294 22.879 26.932 6.150 1.00 19.47 N ANISOU 4033 N LEU C 294 2262 3158 1977 -1122 -113 -219 N ATOM 4034 CA LEU C 294 23.066 26.193 4.906 1.00 20.13 C ANISOU 4034 CA LEU C 294 2268 3288 2094 -1038 -91 -170 C ATOM 4035 C LEU C 294 22.336 26.778 3.698 1.00 21.61 C ANISOU 4035 C LEU C 294 2556 3339 2315 -1019 -41 -150 C ATOM 4036 O LEU C 294 21.332 27.478 3.833 1.00 21.90 O ANISOU 4036 O LEU C 294 2727 3226 2367 -1010 -24 -168 O ATOM 4037 CB LEU C 294 22.631 24.741 5.115 1.00 17.16 C ANISOU 4037 CB LEU C 294 1824 2954 1743 -874 -112 -149 C ATOM 4038 CG LEU C 294 23.373 24.035 6.254 1.00 16.58 C ANISOU 4038 CG LEU C 294 1645 3022 1634 -871 -165 -152 C ATOM 4039 CD1 LEU C 294 22.793 22.655 6.513 1.00 19.22 C ANISOU 4039 CD1 LEU C 294 1945 3361 1995 -709 -182 -127 C ATOM 4040 CD2 LEU C 294 24.862 23.947 5.948 1.00 17.37 C ANISOU 4040 CD2 LEU C 294 1603 3295 1702 -941 -177 -134 C ATOM 4041 N GLU C 295 22.852 26.459 2.514 1.00 20.88 N ANISOU 4041 N GLU C 295 2395 3309 2229 -1004 -17 -112 N ATOM 4042 CA GLU C 295 22.346 27.003 1.259 1.00 21.10 C ANISOU 4042 CA GLU C 295 2505 3237 2275 -997 28 -84 C ATOM 4043 C GLU C 295 21.332 26.091 0.576 1.00 21.31 C ANISOU 4043 C GLU C 295 2540 3217 2341 -833 36 -63 C ATOM 4044 O GLU C 295 21.016 25.006 1.066 1.00 21.62 O ANISOU 4044 O GLU C 295 2526 3292 2397 -729 10 -71 O ATOM 4045 CB GLU C 295 23.503 27.269 0.293 1.00 22.31 C ANISOU 4045 CB GLU C 295 2583 3491 2401 -1091 56 -55 C ATOM 4046 CG GLU C 295 24.481 28.329 0.752 1.00 27.37 C ANISOU 4046 CG GLU C 295 3226 4170 3002 -1282 55 -71 C ATOM 4047 CD GLU C 295 25.467 28.714 -0.336 1.00 31.14 C ANISOU 4047 CD GLU C 295 3647 4733 3453 -1384 94 -34 C ATOM 4048 OE1 GLU C 295 25.199 28.409 -1.519 1.00 33.30 O ANISOU 4048 OE1 GLU C 295 3921 4994 3737 -1308 129 4 O ATOM 4049 OE2 GLU C 295 26.511 29.318 -0.008 1.00 29.46 O ANISOU 4049 OE2 GLU C 295 3386 4606 3202 -1545 90 -43 O ATOM 4050 N GLU C 296 20.843 26.549 -0.573 1.00 20.09 N ANISOU 4050 N GLU C 296 2455 2983 2195 -820 70 -35 N ATOM 4051 CA GLU C 296 19.893 25.800 -1.386 1.00 17.22 C ANISOU 4051 CA GLU C 296 2103 2581 1859 -685 77 -15 C ATOM 4052 C GLU C 296 20.399 24.405 -1.747 1.00 16.37 C ANISOU 4052 C GLU C 296 1871 2598 1753 -602 69 -11 C ATOM 4053 O GLU C 296 19.638 23.438 -1.720 1.00 13.34 O ANISOU 4053 O GLU C 296 1479 2194 1395 -487 54 -17 O ATOM 4054 CB GLU C 296 19.576 26.575 -2.669 1.00 17.96 C ANISOU 4054 CB GLU C 296 2275 2604 1944 -705 113 23 C ATOM 4055 CG GLU C 296 18.673 25.830 -3.637 1.00 16.92 C ANISOU 4055 CG GLU C 296 2148 2453 1828 -579 116 43 C ATOM 4056 CD GLU C 296 18.721 26.406 -5.044 1.00 21.69 C ANISOU 4056 CD GLU C 296 2795 3042 2405 -605 150 88 C ATOM 4057 OE1 GLU C 296 18.025 25.868 -5.932 1.00 20.51 O ANISOU 4057 OE1 GLU C 296 2651 2885 2256 -514 151 104 O ATOM 4058 OE2 GLU C 296 19.458 27.393 -5.264 1.00 22.59 O ANISOU 4058 OE2 GLU C 296 2939 3152 2491 -723 176 109 O ATOM 4059 N PHE C 297 21.678 24.300 -2.093 1.00 14.80 N ANISOU 4059 N PHE C 297 1573 2525 1524 -661 82 -3 N ATOM 4060 CA PHE C 297 22.223 23.022 -2.535 1.00 13.86 C ANISOU 4060 CA PHE C 297 1341 2522 1405 -572 84 0 C ATOM 4061 C PHE C 297 22.317 22.009 -1.396 1.00 13.55 C ANISOU 4061 C PHE C 297 1235 2530 1382 -500 43 -19 C ATOM 4062 O PHE C 297 22.207 20.806 -1.622 1.00 13.17 O ANISOU 4062 O PHE C 297 1142 2511 1351 -384 38 -20 O ATOM 4063 CB PHE C 297 23.600 23.205 -3.173 1.00 17.73 C ANISOU 4063 CB PHE C 297 1731 3150 1854 -648 114 16 C ATOM 4064 CG PHE C 297 24.203 21.923 -3.671 1.00 17.78 C ANISOU 4064 CG PHE C 297 1621 3276 1857 -543 125 15 C ATOM 4065 CD1 PHE C 297 23.658 21.269 -4.764 1.00 19.03 C ANISOU 4065 CD1 PHE C 297 1805 3404 2021 -444 149 17 C ATOM 4066 CD2 PHE C 297 25.303 21.366 -3.042 1.00 18.29 C ANISOU 4066 CD2 PHE C 297 1554 3484 1910 -538 109 10 C ATOM 4067 CE1 PHE C 297 24.203 20.083 -5.228 1.00 20.73 C ANISOU 4067 CE1 PHE C 297 1928 3716 2232 -341 164 7 C ATOM 4068 CE2 PHE C 297 25.854 20.181 -3.499 1.00 20.99 C ANISOU 4068 CE2 PHE C 297 1795 3927 2251 -423 123 9 C ATOM 4069 CZ PHE C 297 25.303 19.539 -4.594 1.00 20.60 C ANISOU 4069 CZ PHE C 297 1785 3832 2210 -324 154 4 C ATOM 4070 N HIS C 298 22.526 22.493 -0.175 1.00 16.23 N ANISOU 4070 N HIS C 298 1579 2875 1713 -570 13 -34 N ATOM 4071 CA HIS C 298 22.582 21.609 0.983 1.00 19.52 C ANISOU 4071 CA HIS C 298 1943 3336 2137 -507 -29 -45 C ATOM 4072 C HIS C 298 21.241 20.918 1.204 1.00 12.61 C ANISOU 4072 C HIS C 298 1140 2351 1300 -395 -40 -49 C ATOM 4073 O HIS C 298 21.195 19.757 1.607 1.00 17.32 O ANISOU 4073 O HIS C 298 1691 2978 1911 -300 -61 -45 O ATOM 4074 CB HIS C 298 22.993 22.382 2.235 1.00 14.17 C ANISOU 4074 CB HIS C 298 1270 2685 1431 -618 -60 -63 C ATOM 4075 CG HIS C 298 24.391 22.914 2.180 1.00 15.31 C ANISOU 4075 CG HIS C 298 1320 2964 1533 -737 -59 -60 C ATOM 4076 ND1 HIS C 298 24.674 24.262 2.181 1.00 16.01 N ANISOU 4076 ND1 HIS C 298 1465 3023 1597 -894 -45 -72 N ATOM 4077 CD2 HIS C 298 25.584 22.279 2.112 1.00 19.82 C ANISOU 4077 CD2 HIS C 298 1744 3704 2084 -725 -68 -44 C ATOM 4078 CE1 HIS C 298 25.983 24.435 2.123 1.00 18.03 C ANISOU 4078 CE1 HIS C 298 1606 3430 1816 -988 -48 -65 C ATOM 4079 NE2 HIS C 298 26.558 23.247 2.079 1.00 19.90 N ANISOU 4079 NE2 HIS C 298 1711 3797 2054 -882 -61 -47 N ATOM 4080 N VAL C 299 20.155 21.636 0.935 1.00 12.36 N ANISOU 4080 N VAL C 299 1220 2192 1284 -407 -25 -55 N ATOM 4081 CA VAL C 299 18.817 21.062 1.028 1.00 11.34 C ANISOU 4081 CA VAL C 299 1150 1968 1189 -311 -32 -57 C ATOM 4082 C VAL C 299 18.660 19.917 0.031 1.00 14.15 C ANISOU 4082 C VAL C 299 1471 2342 1564 -213 -22 -46 C ATOM 4083 O VAL C 299 18.057 18.889 0.340 1.00 10.78 O ANISOU 4083 O VAL C 299 1043 1892 1161 -128 -38 -48 O ATOM 4084 CB VAL C 299 17.720 22.116 0.767 1.00 14.14 C ANISOU 4084 CB VAL C 299 1620 2199 1554 -334 -14 -60 C ATOM 4085 CG1 VAL C 299 16.339 21.480 0.867 1.00 14.93 C ANISOU 4085 CG1 VAL C 299 1759 2225 1686 -237 -22 -61 C ATOM 4086 CG2 VAL C 299 17.847 23.273 1.743 1.00 13.69 C ANISOU 4086 CG2 VAL C 299 1618 2107 1478 -429 -17 -81 C ATOM 4087 N PHE C 300 19.207 20.112 -1.166 1.00 12.92 N ANISOU 4087 N PHE C 300 1293 2225 1392 -230 7 -37 N ATOM 4088 CA PHE C 300 19.198 19.089 -2.202 1.00 14.79 C ANISOU 4088 CA PHE C 300 1499 2486 1635 -145 22 -36 C ATOM 4089 C PHE C 300 19.967 17.862 -1.735 1.00 15.93 C ANISOU 4089 C PHE C 300 1554 2713 1784 -75 8 -40 C ATOM 4090 O PHE C 300 19.502 16.732 -1.882 1.00 15.08 O ANISOU 4090 O PHE C 300 1452 2576 1699 19 2 -47 O ATOM 4091 CB PHE C 300 19.799 19.639 -3.497 1.00 11.69 C ANISOU 4091 CB PHE C 300 1094 2139 1210 -189 60 -24 C ATOM 4092 CG PHE C 300 19.742 18.683 -4.654 1.00 11.66 C ANISOU 4092 CG PHE C 300 1071 2158 1200 -105 81 -31 C ATOM 4093 CD1 PHE C 300 18.525 18.301 -5.195 1.00 16.75 C ANISOU 4093 CD1 PHE C 300 1785 2719 1861 -48 74 -39 C ATOM 4094 CD2 PHE C 300 20.904 18.189 -5.217 1.00 12.31 C ANISOU 4094 CD2 PHE C 300 1065 2354 1258 -87 108 -34 C ATOM 4095 CE1 PHE C 300 18.469 17.431 -6.268 1.00 15.77 C ANISOU 4095 CE1 PHE C 300 1652 2614 1724 19 91 -55 C ATOM 4096 CE2 PHE C 300 20.856 17.320 -6.292 1.00 17.08 C ANISOU 4096 CE2 PHE C 300 1663 2976 1851 -8 132 -50 C ATOM 4097 CZ PHE C 300 19.638 16.939 -6.817 1.00 15.65 C ANISOU 4097 CZ PHE C 300 1563 2703 1683 41 122 -63 C ATOM 4098 N VAL C 301 21.146 18.098 -1.164 1.00 13.28 N ANISOU 4098 N VAL C 301 1139 2481 1427 -124 1 -34 N ATOM 4099 CA VAL C 301 21.956 17.026 -0.602 1.00 13.25 C ANISOU 4099 CA VAL C 301 1043 2568 1425 -52 -17 -29 C ATOM 4100 C VAL C 301 21.218 16.348 0.542 1.00 14.71 C ANISOU 4100 C VAL C 301 1264 2689 1634 3 -55 -26 C ATOM 4101 O VAL C 301 21.286 15.127 0.699 1.00 14.38 O ANISOU 4101 O VAL C 301 1197 2655 1611 105 -65 -20 O ATOM 4102 CB VAL C 301 23.314 17.544 -0.092 1.00 15.24 C ANISOU 4102 CB VAL C 301 1193 2957 1641 -129 -25 -19 C ATOM 4103 CG1 VAL C 301 24.075 16.430 0.606 1.00 16.76 C ANISOU 4103 CG1 VAL C 301 1288 3245 1834 -38 -52 -5 C ATOM 4104 CG2 VAL C 301 24.133 18.112 -1.242 1.00 16.80 C ANISOU 4104 CG2 VAL C 301 1341 3234 1810 -187 19 -16 C ATOM 4105 N LEU C 302 20.510 17.148 1.336 1.00 12.52 N ANISOU 4105 N LEU C 302 1053 2348 1357 -63 -72 -31 N ATOM 4106 CA LEU C 302 19.746 16.630 2.466 1.00 14.44 C ANISOU 4106 CA LEU C 302 1334 2536 1616 -24 -103 -27 C ATOM 4107 C LEU C 302 18.688 15.630 2.011 1.00 12.77 C ANISOU 4107 C LEU C 302 1175 2235 1442 67 -96 -27 C ATOM 4108 O LEU C 302 18.450 14.625 2.677 1.00 12.81 O ANISOU 4108 O LEU C 302 1180 2225 1462 131 -116 -14 O ATOM 4109 CB LEU C 302 19.084 17.771 3.244 1.00 15.77 C ANISOU 4109 CB LEU C 302 1573 2647 1773 -109 -110 -41 C ATOM 4110 CG LEU C 302 18.257 17.347 4.462 1.00 18.93 C ANISOU 4110 CG LEU C 302 2013 3001 2179 -79 -135 -38 C ATOM 4111 CD1 LEU C 302 19.124 16.613 5.474 1.00 17.42 C ANISOU 4111 CD1 LEU C 302 1750 2905 1965 -54 -170 -17 C ATOM 4112 CD2 LEU C 302 17.571 18.547 5.109 1.00 19.79 C ANISOU 4112 CD2 LEU C 302 2197 3049 2272 -154 -130 -61 C ATOM 4113 N ALA C 303 18.055 15.909 0.875 1.00 12.75 N ANISOU 4113 N ALA C 303 1219 2175 1451 65 -70 -40 N ATOM 4114 CA ALA C 303 17.073 14.986 0.316 1.00 11.81 C ANISOU 4114 CA ALA C 303 1145 1982 1362 135 -66 -46 C ATOM 4115 C ALA C 303 17.719 13.634 0.012 1.00 13.99 C ANISOU 4115 C ALA C 303 1377 2291 1646 224 -64 -46 C ATOM 4116 O ALA C 303 17.111 12.579 0.213 1.00 15.70 O ANISOU 4116 O ALA C 303 1626 2450 1889 284 -74 -45 O ATOM 4117 CB ALA C 303 16.446 15.571 -0.933 1.00 11.29 C ANISOU 4117 CB ALA C 303 1123 1873 1292 115 -43 -58 C ATOM 4118 N HIS C 304 18.958 13.667 -0.466 1.00 10.82 N ANISOU 4118 N HIS C 304 904 1983 1223 231 -48 -46 N ATOM 4119 CA HIS C 304 19.673 12.438 -0.777 1.00 11.35 C ANISOU 4119 CA HIS C 304 927 2089 1298 330 -39 -47 C ATOM 4120 C HIS C 304 20.044 11.682 0.494 1.00 11.66 C ANISOU 4120 C HIS C 304 936 2148 1347 382 -72 -19 C ATOM 4121 O HIS C 304 19.948 10.457 0.538 1.00 13.17 O ANISOU 4121 O HIS C 304 1146 2297 1561 475 -74 -15 O ATOM 4122 CB HIS C 304 20.919 12.735 -1.611 1.00 12.04 C ANISOU 4122 CB HIS C 304 932 2289 1354 327 -7 -53 C ATOM 4123 CG HIS C 304 20.616 13.087 -3.034 1.00 14.84 C ANISOU 4123 CG HIS C 304 1320 2624 1693 307 30 -77 C ATOM 4124 ND1 HIS C 304 20.177 14.337 -3.414 1.00 11.60 N ANISOU 4124 ND1 HIS C 304 948 2195 1266 209 37 -74 N ATOM 4125 CD2 HIS C 304 20.674 12.348 -4.167 1.00 14.50 C ANISOU 4125 CD2 HIS C 304 1287 2578 1644 374 62 -104 C ATOM 4126 CE1 HIS C 304 19.983 14.355 -4.720 1.00 12.34 C ANISOU 4126 CE1 HIS C 304 1067 2281 1340 217 68 -91 C ATOM 4127 NE2 HIS C 304 20.277 13.160 -5.202 1.00 14.41 N ANISOU 4127 NE2 HIS C 304 1312 2557 1606 312 84 -114 N ATOM 4128 N VAL C 305 20.463 12.410 1.525 1.00 16.00 N ANISOU 4128 N VAL C 305 1446 2759 1875 320 -97 1 N ATOM 4129 CA VAL C 305 20.761 11.793 2.816 1.00 16.98 C ANISOU 4129 CA VAL C 305 1544 2912 1996 361 -135 34 C ATOM 4130 C VAL C 305 19.532 11.072 3.357 1.00 19.41 C ANISOU 4130 C VAL C 305 1942 3100 2334 393 -147 44 C ATOM 4131 O VAL C 305 19.622 9.938 3.828 1.00 19.49 O ANISOU 4131 O VAL C 305 1958 3090 2358 477 -162 71 O ATOM 4132 CB VAL C 305 21.234 12.827 3.858 1.00 16.68 C ANISOU 4132 CB VAL C 305 1463 2954 1919 266 -164 45 C ATOM 4133 CG1 VAL C 305 21.303 12.194 5.244 1.00 18.83 C ANISOU 4133 CG1 VAL C 305 1727 3247 2181 305 -206 82 C ATOM 4134 CG2 VAL C 305 22.579 13.410 3.463 1.00 19.89 C ANISOU 4134 CG2 VAL C 305 1765 3498 2294 227 -156 43 C ATOM 4135 N LEU C 306 18.382 11.738 3.276 1.00 16.02 N ANISOU 4135 N LEU C 306 1583 2593 1913 326 -141 25 N ATOM 4136 CA LEU C 306 17.126 11.177 3.762 1.00 17.85 C ANISOU 4136 CA LEU C 306 1890 2724 2168 339 -148 33 C ATOM 4137 C LEU C 306 16.534 10.156 2.792 1.00 15.48 C ANISOU 4137 C LEU C 306 1637 2341 1903 398 -130 17 C ATOM 4138 O LEU C 306 15.689 9.346 3.179 1.00 13.81 O ANISOU 4138 O LEU C 306 1481 2053 1714 419 -137 29 O ATOM 4139 CB LEU C 306 16.108 12.294 4.011 1.00 18.41 C ANISOU 4139 CB LEU C 306 2008 2754 2233 255 -144 17 C ATOM 4140 CG LEU C 306 16.500 13.393 5.001 1.00 19.86 C ANISOU 4140 CG LEU C 306 2170 2996 2379 183 -159 19 C ATOM 4141 CD1 LEU C 306 15.485 14.527 4.964 1.00 17.27 C ANISOU 4141 CD1 LEU C 306 1900 2612 2051 118 -143 -5 C ATOM 4142 CD2 LEU C 306 16.625 12.828 6.410 1.00 19.84 C ANISOU 4142 CD2 LEU C 306 2160 3021 2358 201 -188 51 C ATOM 4143 N ARG C 307 16.985 10.200 1.539 1.00 14.66 N ANISOU 4143 N ARG C 307 1515 2256 1797 416 -105 -11 N ATOM 4144 CA ARG C 307 16.394 9.403 0.461 1.00 14.31 C ANISOU 4144 CA ARG C 307 1523 2140 1775 456 -87 -40 C ATOM 4145 C ARG C 307 14.889 9.642 0.413 1.00 13.16 C ANISOU 4145 C ARG C 307 1442 1913 1643 401 -92 -50 C ATOM 4146 O ARG C 307 14.089 8.708 0.367 1.00 12.91 O ANISOU 4146 O ARG C 307 1464 1804 1636 420 -96 -55 O ATOM 4147 CB ARG C 307 16.715 7.917 0.641 1.00 16.31 C ANISOU 4147 CB ARG C 307 1794 2352 2050 551 -89 -30 C ATOM 4148 CG ARG C 307 18.207 7.626 0.555 1.00 19.71 C ANISOU 4148 CG ARG C 307 2149 2872 2466 627 -80 -21 C ATOM 4149 CD ARG C 307 18.516 6.149 0.382 1.00 23.17 C ANISOU 4149 CD ARG C 307 2620 3255 2929 743 -70 -21 C ATOM 4150 NE ARG C 307 19.916 5.953 0.010 1.00 26.95 N ANISOU 4150 NE ARG C 307 3016 3832 3391 827 -51 -22 N ATOM 4151 CZ ARG C 307 20.435 4.797 -0.390 1.00 30.74 C ANISOU 4151 CZ ARG C 307 3511 4281 3886 948 -30 -32 C ATOM 4152 NH1 ARG C 307 19.673 3.714 -0.474 1.00 33.20 N ANISOU 4152 NH1 ARG C 307 3931 4453 4230 987 -28 -44 N ATOM 4153 NH2 ARG C 307 21.720 4.723 -0.709 1.00 33.63 N ANISOU 4153 NH2 ARG C 307 3786 4758 4235 1027 -9 -32 N ATOM 4154 N ARG C 308 14.524 10.919 0.425 1.00 9.42 N ANISOU 4154 N ARG C 308 963 1460 1154 332 -92 -52 N ATOM 4155 CA ARG C 308 13.137 11.341 0.533 1.00 12.57 C ANISOU 4155 CA ARG C 308 1409 1805 1564 287 -97 -55 C ATOM 4156 C ARG C 308 12.975 12.720 -0.096 1.00 11.05 C ANISOU 4156 C ARG C 308 1215 1633 1352 237 -86 -65 C ATOM 4157 O ARG C 308 13.832 13.585 0.074 1.00 14.46 O ANISOU 4157 O ARG C 308 1617 2116 1762 207 -80 -59 O ATOM 4158 CB ARG C 308 12.700 11.363 2.004 1.00 15.45 C ANISOU 4158 CB ARG C 308 1781 2158 1933 269 -113 -27 C ATOM 4159 CG ARG C 308 11.277 11.837 2.239 1.00 15.49 C ANISOU 4159 CG ARG C 308 1820 2120 1946 229 -112 -29 C ATOM 4160 CD ARG C 308 10.984 11.985 3.728 1.00 16.65 C ANISOU 4160 CD ARG C 308 1970 2273 2085 210 -119 -5 C ATOM 4161 NE ARG C 308 11.212 10.750 4.475 1.00 17.11 N ANISOU 4161 NE ARG C 308 2034 2318 2150 243 -132 23 N ATOM 4162 CZ ARG C 308 10.297 9.803 4.656 1.00 16.05 C ANISOU 4162 CZ ARG C 308 1932 2128 2037 246 -132 36 C ATOM 4163 NH1 ARG C 308 9.084 9.943 4.139 1.00 16.06 N ANISOU 4163 NH1 ARG C 308 1951 2098 2053 217 -124 19 N ATOM 4164 NH2 ARG C 308 10.593 8.713 5.354 1.00 16.28 N ANISOU 4164 NH2 ARG C 308 1978 2138 2071 276 -142 69 N ATOM 4165 N PRO C 309 11.881 12.930 -0.837 1.00 11.36 N ANISOU 4165 N PRO C 309 1288 1633 1396 224 -84 -76 N ATOM 4166 CA PRO C 309 11.634 14.251 -1.423 1.00 8.31 C ANISOU 4166 CA PRO C 309 912 1255 991 187 -75 -76 C ATOM 4167 C PRO C 309 11.482 15.327 -0.349 1.00 10.27 C ANISOU 4167 C PRO C 309 1168 1499 1237 149 -75 -61 C ATOM 4168 O PRO C 309 10.980 15.047 0.740 1.00 10.31 O ANISOU 4168 O PRO C 309 1178 1487 1254 151 -84 -55 O ATOM 4169 CB PRO C 309 10.321 14.059 -2.188 1.00 16.67 C ANISOU 4169 CB PRO C 309 2000 2278 2057 193 -83 -84 C ATOM 4170 CG PRO C 309 10.222 12.582 -2.419 1.00 14.30 C ANISOU 4170 CG PRO C 309 1704 1957 1771 223 -90 -102 C ATOM 4171 CD PRO C 309 10.847 11.952 -1.214 1.00 11.46 C ANISOU 4171 CD PRO C 309 1330 1595 1428 240 -93 -89 C ATOM 4172 N ILE C 310 11.925 16.541 -0.654 1.00 9.88 N ANISOU 4172 N ILE C 310 1126 1463 1167 112 -62 -58 N ATOM 4173 CA ILE C 310 11.713 17.671 0.238 1.00 12.38 C ANISOU 4173 CA ILE C 310 1468 1758 1476 73 -58 -54 C ATOM 4174 C ILE C 310 10.929 18.760 -0.482 1.00 15.12 C ANISOU 4174 C ILE C 310 1863 2062 1821 66 -46 -47 C ATOM 4175 O ILE C 310 11.292 19.176 -1.585 1.00 14.83 O ANISOU 4175 O ILE C 310 1834 2034 1768 55 -36 -39 O ATOM 4176 CB ILE C 310 13.044 18.257 0.760 1.00 12.36 C ANISOU 4176 CB ILE C 310 1444 1801 1450 21 -54 -56 C ATOM 4177 CG1 ILE C 310 13.838 17.192 1.518 1.00 11.63 C ANISOU 4177 CG1 ILE C 310 1297 1763 1357 41 -71 -54 C ATOM 4178 CG2 ILE C 310 12.785 19.457 1.662 1.00 15.18 C ANISOU 4178 CG2 ILE C 310 1846 2124 1796 -26 -48 -63 C ATOM 4179 CD1 ILE C 310 15.178 17.686 2.043 1.00 13.61 C ANISOU 4179 CD1 ILE C 310 1507 2084 1579 -11 -75 -54 C ATOM 4180 N VAL C 311 9.845 19.206 0.143 1.00 11.04 N ANISOU 4180 N VAL C 311 1377 1503 1316 80 -45 -47 N ATOM 4181 CA VAL C 311 9.034 20.289 -0.394 1.00 13.34 C ANISOU 4181 CA VAL C 311 1715 1749 1605 91 -34 -35 C ATOM 4182 C VAL C 311 9.139 21.504 0.516 1.00 15.15 C ANISOU 4182 C VAL C 311 1994 1937 1827 61 -16 -43 C ATOM 4183 O VAL C 311 8.825 21.429 1.705 1.00 15.09 O ANISOU 4183 O VAL C 311 1987 1924 1821 63 -14 -59 O ATOM 4184 CB VAL C 311 7.555 19.880 -0.545 1.00 13.38 C ANISOU 4184 CB VAL C 311 1712 1744 1629 144 -43 -29 C ATOM 4185 CG1 VAL C 311 6.723 21.057 -1.040 1.00 12.65 C ANISOU 4185 CG1 VAL C 311 1662 1611 1533 173 -34 -10 C ATOM 4186 CG2 VAL C 311 7.426 18.692 -1.490 1.00 14.77 C ANISOU 4186 CG2 VAL C 311 1850 1953 1807 160 -63 -29 C ATOM 4187 N VAL C 312 9.590 22.621 -0.043 1.00 9.17 N ANISOU 4187 N VAL C 312 1284 1146 1053 28 0 -33 N ATOM 4188 CA VAL C 312 9.788 23.832 0.740 1.00 10.45 C ANISOU 4188 CA VAL C 312 1512 1254 1206 -12 19 -48 C ATOM 4189 C VAL C 312 8.824 24.931 0.312 1.00 11.81 C ANISOU 4189 C VAL C 312 1758 1344 1384 30 37 -30 C ATOM 4190 O VAL C 312 8.763 25.294 -0.864 1.00 13.39 O ANISOU 4190 O VAL C 312 1980 1529 1580 41 39 4 O ATOM 4191 CB VAL C 312 11.235 24.354 0.619 1.00 13.05 C ANISOU 4191 CB VAL C 312 1849 1600 1510 -104 25 -51 C ATOM 4192 CG1 VAL C 312 11.425 25.596 1.475 1.00 12.82 C ANISOU 4192 CG1 VAL C 312 1898 1505 1467 -162 43 -75 C ATOM 4193 CG2 VAL C 312 12.229 23.267 1.018 1.00 9.78 C ANISOU 4193 CG2 VAL C 312 1349 1278 1087 -130 6 -63 C ATOM 4194 N VAL C 313 8.068 25.450 1.275 1.00 10.26 N ANISOU 4194 N VAL C 313 1602 1100 1195 60 52 -51 N ATOM 4195 CA VAL C 313 7.195 26.596 1.044 1.00 10.84 C ANISOU 4195 CA VAL C 313 1755 1088 1276 114 75 -37 C ATOM 4196 C VAL C 313 7.938 27.883 1.379 1.00 17.46 C ANISOU 4196 C VAL C 313 2693 1842 2097 46 100 -54 C ATOM 4197 O VAL C 313 8.462 28.036 2.484 1.00 16.99 O ANISOU 4197 O VAL C 313 2651 1780 2023 -11 107 -98 O ATOM 4198 CB VAL C 313 5.912 26.517 1.892 1.00 17.78 C ANISOU 4198 CB VAL C 313 2626 1961 2170 195 87 -54 C ATOM 4199 CG1 VAL C 313 5.012 27.716 1.608 1.00 18.02 C ANISOU 4199 CG1 VAL C 313 2734 1904 2209 271 112 -36 C ATOM 4200 CG2 VAL C 313 5.180 25.209 1.631 1.00 10.27 C ANISOU 4200 CG2 VAL C 313 1574 1093 1234 240 61 -39 C ATOM 4201 N ALA C 314 7.992 28.808 0.428 1.00 12.15 N ANISOU 4201 N ALA C 314 2092 1101 1422 46 113 -18 N ATOM 4202 CA ALA C 314 8.707 30.057 0.646 1.00 14.99 C ANISOU 4202 CA ALA C 314 2561 1367 1767 -33 139 -30 C ATOM 4203 C ALA C 314 8.239 31.139 -0.316 1.00 16.10 C ANISOU 4203 C ALA C 314 2801 1404 1911 11 158 21 C ATOM 4204 O ALA C 314 7.581 30.855 -1.315 1.00 17.60 O ANISOU 4204 O ALA C 314 2958 1620 2108 89 144 72 O ATOM 4205 CB ALA C 314 10.205 29.838 0.503 1.00 13.90 C ANISOU 4205 CB ALA C 314 2390 1287 1605 -162 129 -36 C ATOM 4206 N ASP C 315 8.579 32.383 -0.004 1.00 17.35 N ANISOU 4206 N ASP C 315 3086 1444 2063 -40 188 8 N ATOM 4207 CA ASP C 315 8.321 33.484 -0.917 1.00 19.83 C ANISOU 4207 CA ASP C 315 3514 1644 2378 -12 208 64 C ATOM 4208 C ASP C 315 9.348 33.429 -2.040 1.00 20.74 C ANISOU 4208 C ASP C 315 3613 1799 2469 -109 200 113 C ATOM 4209 O ASP C 315 10.353 32.727 -1.927 1.00 17.80 O ANISOU 4209 O ASP C 315 3155 1527 2080 -205 186 90 O ATOM 4210 CB ASP C 315 8.383 34.827 -0.190 1.00 22.46 C ANISOU 4210 CB ASP C 315 4003 1819 2710 -43 248 30 C ATOM 4211 CG ASP C 315 7.581 35.905 -0.890 1.00 24.32 C ANISOU 4211 CG ASP C 315 4365 1918 2960 55 272 88 C ATOM 4212 OD1 ASP C 315 7.249 35.725 -2.082 1.00 26.04 O ANISOU 4212 OD1 ASP C 315 4550 2168 3176 113 255 164 O ATOM 4213 OD2 ASP C 315 7.285 36.934 -0.248 1.00 25.41 O ANISOU 4213 OD2 ASP C 315 4636 1915 3105 78 308 57 O ATOM 4214 N THR C 316 9.100 34.166 -3.118 1.00 22.70 N ANISOU 4214 N THR C 316 3940 1975 2710 -78 211 184 N ATOM 4215 CA THR C 316 9.986 34.133 -4.275 1.00 23.74 C ANISOU 4215 CA THR C 316 4057 2152 2810 -162 209 238 C ATOM 4216 C THR C 316 10.989 35.285 -4.279 1.00 25.86 C ANISOU 4216 C THR C 316 4448 2318 3061 -302 242 247 C ATOM 4217 O THR C 316 12.039 35.197 -4.914 1.00 26.48 O ANISOU 4217 O THR C 316 4495 2456 3108 -416 247 271 O ATOM 4218 CB THR C 316 9.189 34.176 -5.594 1.00 25.15 C ANISOU 4218 CB THR C 316 4244 2334 2979 -58 197 322 C ATOM 4219 OG1 THR C 316 8.392 35.365 -5.632 1.00 29.36 O ANISOU 4219 OG1 THR C 316 4916 2715 3525 22 217 360 O ATOM 4220 CG2 THR C 316 8.284 32.960 -5.714 1.00 23.54 C ANISOU 4220 CG2 THR C 316 3910 2248 2787 54 159 313 C ATOM 4221 N MET C 317 10.666 36.363 -3.573 1.00 25.49 N ANISOU 4221 N MET C 317 4540 2117 3030 -297 269 224 N ATOM 4222 CA MET C 317 11.504 37.558 -3.603 1.00 28.80 C ANISOU 4222 CA MET C 317 5099 2411 3432 -434 304 233 C ATOM 4223 C MET C 317 11.693 38.202 -2.233 1.00 32.86 C ANISOU 4223 C MET C 317 5703 2826 3955 -499 323 146 C ATOM 4224 O MET C 317 10.740 38.357 -1.469 1.00 33.96 O ANISOU 4224 O MET C 317 5885 2901 4120 -385 330 106 O ATOM 4225 CB MET C 317 10.908 38.592 -4.567 1.00 29.03 C ANISOU 4225 CB MET C 317 5273 2297 3461 -366 326 323 C ATOM 4226 CG MET C 317 10.796 38.112 -6.007 1.00 29.69 C ANISOU 4226 CG MET C 317 5287 2473 3520 -320 307 414 C ATOM 4227 SD MET C 317 12.400 37.946 -6.812 1.00 61.18 S ANISOU 4227 SD MET C 317 9225 6561 7458 -520 318 445 S ATOM 4228 CE MET C 317 12.040 36.686 -8.034 1.00 40.05 C ANISOU 4228 CE MET C 317 6394 4068 4757 -420 282 496 C ATOM 4229 N LEU C 318 12.934 38.573 -1.930 1.00 35.19 N ANISOU 4229 N LEU C 318 6025 3121 4226 -687 333 116 N ATOM 4230 CA LEU C 318 13.206 39.475 -0.820 1.00 38.12 C ANISOU 4230 CA LEU C 318 6507 3384 4593 -770 353 39 C ATOM 4231 C LEU C 318 12.772 40.870 -1.238 1.00 42.51 C ANISOU 4231 C LEU C 318 7203 3791 5158 -719 381 76 C ATOM 4232 O LEU C 318 13.055 41.301 -2.356 1.00 41.21 O ANISOU 4232 O LEU C 318 7068 3605 4984 -747 389 155 O ATOM 4233 CB LEU C 318 14.688 39.475 -0.440 1.00 40.55 C ANISOU 4233 CB LEU C 318 6760 3782 4865 -980 344 -3 C ATOM 4234 CG LEU C 318 15.305 38.227 0.189 1.00 43.36 C ANISOU 4234 CG LEU C 318 6950 4318 5206 -1037 309 -52 C ATOM 4235 CD1 LEU C 318 16.758 38.499 0.552 1.00 45.59 C ANISOU 4235 CD1 LEU C 318 7198 4674 5449 -1247 302 -87 C ATOM 4236 CD2 LEU C 318 14.515 37.790 1.414 1.00 42.52 C ANISOU 4236 CD2 LEU C 318 6822 4220 5113 -931 295 -127 C ATOM 4237 N ARG C 319 12.085 41.578 -0.351 1.00 46.87 N ANISOU 4237 N ARG C 319 7840 4243 5726 -642 397 20 N ATOM 4238 CA ARG C 319 11.596 42.906 -0.690 1.00 55.39 C ANISOU 4238 CA ARG C 319 9055 5173 6817 -580 425 53 C ATOM 4239 C ARG C 319 12.246 43.979 0.168 1.00 60.78 C ANISOU 4239 C ARG C 319 9839 5772 7482 -704 445 -16 C ATOM 4240 O ARG C 319 12.524 43.766 1.347 1.00 62.41 O ANISOU 4240 O ARG C 319 10023 6017 7673 -761 440 -106 O ATOM 4241 CB ARG C 319 10.074 42.956 -0.564 1.00 56.14 C ANISOU 4241 CB ARG C 319 9168 5215 6946 -358 432 63 C ATOM 4242 CG ARG C 319 9.384 42.163 -1.658 1.00 54.09 C ANISOU 4242 CG ARG C 319 8828 5024 6700 -233 411 151 C ATOM 4243 CD ARG C 319 7.893 42.023 -1.433 1.00 54.25 C ANISOU 4243 CD ARG C 319 8825 5037 6751 -18 411 153 C ATOM 4244 NE ARG C 319 7.353 40.943 -2.253 1.00 54.60 N ANISOU 4244 NE ARG C 319 8756 5188 6799 78 381 218 N ATOM 4245 CZ ARG C 319 7.258 40.989 -3.578 1.00 56.30 C ANISOU 4245 CZ ARG C 319 8966 5419 7006 111 365 317 C ATOM 4246 NH1 ARG C 319 7.664 42.065 -4.239 1.00 58.07 N ANISOU 4246 NH1 ARG C 319 9291 5552 7220 56 381 367 N ATOM 4247 NH2 ARG C 319 6.757 39.957 -4.244 1.00 54.90 N ANISOU 4247 NH2 ARG C 319 8682 5352 6826 195 334 367 N ATOM 4248 N ASP C 320 12.495 45.131 -0.446 1.00 67.16 N ANISOU 4248 N ASP C 320 10761 6469 8288 -746 466 28 N ATOM 4249 CA ASP C 320 13.189 46.227 0.215 1.00 71.91 C ANISOU 4249 CA ASP C 320 11472 6981 8869 -879 486 -29 C ATOM 4250 C ASP C 320 12.350 46.826 1.334 1.00 76.06 C ANISOU 4250 C ASP C 320 12087 7405 9408 -778 508 -104 C ATOM 4251 O ASP C 320 11.194 46.449 1.530 1.00 77.26 O ANISOU 4251 O ASP C 320 12212 7557 9587 -599 510 -105 O ATOM 4252 CB ASP C 320 13.559 47.313 -0.799 1.00 74.02 C ANISOU 4252 CB ASP C 320 11848 7141 9134 -937 507 47 C ATOM 4253 N SER C 321 12.945 47.759 2.070 1.00 77.02 N ANISOU 4253 N SER C 321 12309 7448 9507 -897 525 -168 N ATOM 4254 CA SER C 321 12.230 48.474 3.118 1.00 75.61 C ANISOU 4254 CA SER C 321 12232 7160 9335 -815 552 -242 C ATOM 4255 C SER C 321 11.060 49.240 2.511 1.00 74.40 C ANISOU 4255 C SER C 321 12180 6866 9223 -630 581 -183 C ATOM 4256 O SER C 321 10.013 49.398 3.139 1.00 72.94 O ANISOU 4256 O SER C 321 12023 6634 9057 -476 599 -220 O ATOM 4257 CB SER C 321 13.169 49.424 3.862 1.00 76.84 C ANISOU 4257 CB SER C 321 12492 7248 9455 -993 565 -313 C ATOM 4258 N GLY C 322 11.248 49.705 1.279 1.00 74.52 N ANISOU 4258 N GLY C 322 12241 6826 9248 -644 583 -87 N ATOM 4259 CA GLY C 322 10.198 50.383 0.541 1.00 74.71 C ANISOU 4259 CA GLY C 322 12346 6732 9307 -469 602 -13 C ATOM 4260 C GLY C 322 9.152 49.415 0.017 1.00 73.03 C ANISOU 4260 C GLY C 322 12011 6617 9119 -282 582 43 C ATOM 4261 O GLY C 322 8.058 49.821 -0.376 1.00 70.80 O ANISOU 4261 O GLY C 322 11766 6269 8866 -103 592 93 O ATOM 4262 N GLY C 323 9.494 48.130 0.009 1.00 73.86 N ANISOU 4262 N GLY C 323 11967 6884 9212 -326 550 37 N ATOM 4263 CA GLY C 323 8.570 47.097 -0.422 1.00 75.92 C ANISOU 4263 CA GLY C 323 12103 7249 9492 -167 527 82 C ATOM 4264 C GLY C 323 8.828 46.575 -1.824 1.00 77.17 C ANISOU 4264 C GLY C 323 12195 7478 9646 -180 501 187 C ATOM 4265 O GLY C 323 8.190 45.617 -2.260 1.00 76.38 O ANISOU 4265 O GLY C 323 11984 7480 9556 -70 477 227 O ATOM 4266 N GLU C 324 9.762 47.201 -2.533 1.00 80.90 N ANISOU 4266 N GLU C 324 12735 7902 10100 -318 508 234 N ATOM 4267 CA GLU C 324 10.096 46.781 -3.891 1.00 78.86 C ANISOU 4267 CA GLU C 324 12421 7714 9829 -345 488 336 C ATOM 4268 C GLU C 324 10.912 45.490 -3.885 1.00 77.12 C ANISOU 4268 C GLU C 324 12059 7658 9585 -457 463 316 C ATOM 4269 O GLU C 324 11.651 45.217 -2.939 1.00 78.39 O ANISOU 4269 O GLU C 324 12192 7862 9732 -581 463 231 O ATOM 4270 CB GLU C 324 10.864 47.886 -4.622 1.00 80.72 C ANISOU 4270 CB GLU C 324 12771 7851 10049 -465 508 392 C ATOM 4271 N ALA C 325 10.769 44.698 -4.944 1.00 70.78 N ANISOU 4271 N ALA C 325 11167 6952 8773 -412 441 396 N ATOM 4272 CA ALA C 325 11.509 43.447 -5.067 1.00 63.06 C ANISOU 4272 CA ALA C 325 10058 6131 7772 -507 420 387 C ATOM 4273 C ALA C 325 13.010 43.715 -5.135 1.00 57.85 C ANISOU 4273 C ALA C 325 9400 5503 7080 -731 431 374 C ATOM 4274 O ALA C 325 13.475 44.480 -5.979 1.00 57.41 O ANISOU 4274 O ALA C 325 9406 5400 7007 -798 447 438 O ATOM 4275 CB ALA C 325 11.047 42.674 -6.291 1.00 61.48 C ANISOU 4275 CB ALA C 325 9778 6020 7560 -413 398 481 C ATOM 4276 N PHE C 326 13.764 43.080 -4.243 1.00 51.41 N ANISOU 4276 N PHE C 326 8506 4775 6251 -845 422 293 N ATOM 4277 CA PHE C 326 15.202 43.311 -4.144 1.00 48.53 C ANISOU 4277 CA PHE C 326 8119 4467 5854 -1058 428 268 C ATOM 4278 C PHE C 326 16.030 42.171 -4.734 1.00 43.94 C ANISOU 4278 C PHE C 326 7384 4067 5244 -1144 413 296 C ATOM 4279 O PHE C 326 16.959 42.408 -5.505 1.00 43.40 O ANISOU 4279 O PHE C 326 7293 4051 5145 -1264 424 342 O ATOM 4280 CB PHE C 326 15.597 43.537 -2.684 1.00 51.02 C ANISOU 4280 CB PHE C 326 8449 4769 6165 -1141 426 156 C ATOM 4281 CG PHE C 326 17.064 43.372 -2.422 1.00 52.60 C ANISOU 4281 CG PHE C 326 8569 5090 6328 -1348 417 121 C ATOM 4282 CD1 PHE C 326 17.531 42.287 -1.702 1.00 53.23 C ANISOU 4282 CD1 PHE C 326 8510 5319 6395 -1397 389 62 C ATOM 4283 CD2 PHE C 326 17.975 44.296 -2.900 1.00 56.16 C ANISOU 4283 CD2 PHE C 326 9074 5510 6754 -1490 435 148 C ATOM 4284 CE1 PHE C 326 18.881 42.129 -1.457 1.00 54.69 C ANISOU 4284 CE1 PHE C 326 8602 5635 6542 -1574 377 33 C ATOM 4285 CE2 PHE C 326 19.325 44.144 -2.660 1.00 57.64 C ANISOU 4285 CE2 PHE C 326 9171 5826 6903 -1674 425 117 C ATOM 4286 CZ PHE C 326 19.779 43.059 -1.938 1.00 56.63 C ANISOU 4286 CZ PHE C 326 8895 5861 6763 -1711 395 60 C ATOM 4287 N ALA C 327 15.693 40.939 -4.365 1.00 37.62 N ANISOU 4287 N ALA C 327 6477 3365 4452 -1080 390 268 N ATOM 4288 CA ALA C 327 16.419 39.768 -4.849 1.00 33.23 C ANISOU 4288 CA ALA C 327 5769 2988 3870 -1148 377 289 C ATOM 4289 C ALA C 327 15.624 38.489 -4.613 1.00 30.63 C ANISOU 4289 C ALA C 327 5339 2739 3560 -1010 350 273 C ATOM 4290 O ALA C 327 14.817 38.413 -3.685 1.00 27.66 O ANISOU 4290 O ALA C 327 4985 2311 3215 -911 338 216 O ATOM 4291 CB ALA C 327 17.782 39.674 -4.181 1.00 33.34 C ANISOU 4291 CB ALA C 327 5697 3111 3858 -1331 371 226 C ATOM 4292 N PRO C 328 15.860 37.472 -5.453 1.00 29.46 N ANISOU 4292 N PRO C 328 5043 2757 3394 -977 334 309 N ATOM 4293 CA PRO C 328 15.098 36.220 -5.401 1.00 30.05 C ANISOU 4293 CA PRO C 328 4985 2943 3487 -819 297 290 C ATOM 4294 C PRO C 328 15.456 35.335 -4.210 1.00 27.52 C ANISOU 4294 C PRO C 328 4545 2731 3180 -837 271 202 C ATOM 4295 O PRO C 328 16.610 35.302 -3.781 1.00 26.90 O ANISOU 4295 O PRO C 328 4415 2724 3080 -979 272 168 O ATOM 4296 CB PRO C 328 15.477 35.530 -6.715 1.00 29.99 C ANISOU 4296 CB PRO C 328 4880 3069 3447 -814 296 351 C ATOM 4297 CG PRO C 328 16.839 36.054 -7.027 1.00 30.78 C ANISOU 4297 CG PRO C 328 4987 3199 3508 -1002 326 370 C ATOM 4298 CD PRO C 328 16.850 37.477 -6.545 1.00 31.90 C ANISOU 4298 CD PRO C 328 5309 3152 3658 -1090 353 371 C ATOM 4299 N ILE C 329 14.458 34.637 -3.680 1.00 22.77 N ANISOU 4299 N ILE C 329 3898 2145 2609 -695 246 170 N ATOM 4300 CA ILE C 329 14.683 33.607 -2.676 1.00 21.84 C ANISOU 4300 CA ILE C 329 3658 2142 2499 -689 217 102 C ATOM 4301 C ILE C 329 14.742 32.258 -3.383 1.00 21.09 C ANISOU 4301 C ILE C 329 3414 2199 2401 -623 194 122 C ATOM 4302 O ILE C 329 13.813 31.893 -4.102 1.00 20.87 O ANISOU 4302 O ILE C 329 3379 2167 2383 -504 186 158 O ATOM 4303 CB ILE C 329 13.580 33.602 -1.603 1.00 21.45 C ANISOU 4303 CB ILE C 329 3647 2024 2480 -583 209 53 C ATOM 4304 CG1 ILE C 329 13.574 34.933 -0.846 1.00 21.98 C ANISOU 4304 CG1 ILE C 329 3870 1934 2546 -648 237 19 C ATOM 4305 CG2 ILE C 329 13.774 32.433 -0.643 1.00 22.48 C ANISOU 4305 CG2 ILE C 329 3648 2280 2613 -571 178 -3 C ATOM 4306 CD1 ILE C 329 12.377 35.118 0.062 1.00 19.97 C ANISOU 4306 CD1 ILE C 329 3675 1595 2316 -527 242 -23 C ATOM 4307 N PRO C 330 15.842 31.519 -3.190 1.00 21.97 N ANISOU 4307 N PRO C 330 3407 2445 2493 -699 183 98 N ATOM 4308 CA PRO C 330 16.104 30.286 -3.943 1.00 23.23 C ANISOU 4308 CA PRO C 330 3438 2743 2645 -648 170 115 C ATOM 4309 C PRO C 330 15.491 29.012 -3.352 1.00 20.01 C ANISOU 4309 C PRO C 330 2942 2397 2264 -536 137 79 C ATOM 4310 O PRO C 330 15.461 27.993 -4.041 1.00 18.05 O ANISOU 4310 O PRO C 330 2611 2234 2013 -475 127 90 O ATOM 4311 CB PRO C 330 17.629 30.196 -3.909 1.00 22.88 C ANISOU 4311 CB PRO C 330 3312 2810 2569 -780 179 105 C ATOM 4312 CG PRO C 330 17.982 30.779 -2.577 1.00 22.65 C ANISOU 4312 CG PRO C 330 3320 2743 2543 -869 171 55 C ATOM 4313 CD PRO C 330 16.986 31.896 -2.340 1.00 21.88 C ANISOU 4313 CD PRO C 330 3384 2466 2463 -845 185 57 C ATOM 4314 N PHE C 331 15.007 29.067 -2.115 1.00 21.18 N ANISOU 4314 N PHE C 331 3114 2501 2434 -515 124 35 N ATOM 4315 CA PHE C 331 14.661 27.849 -1.381 1.00 18.70 C ANISOU 4315 CA PHE C 331 2712 2256 2139 -439 95 2 C ATOM 4316 C PHE C 331 13.311 27.216 -1.735 1.00 17.87 C ANISOU 4316 C PHE C 331 2602 2129 2060 -306 83 16 C ATOM 4317 O PHE C 331 13.139 26.005 -1.587 1.00 13.66 O ANISOU 4317 O PHE C 331 1985 1667 1538 -250 62 4 O ATOM 4318 CB PHE C 331 14.699 28.128 0.121 1.00 16.43 C ANISOU 4318 CB PHE C 331 2447 1943 1851 -476 87 -48 C ATOM 4319 CG PHE C 331 16.068 28.455 0.637 1.00 16.55 C ANISOU 4319 CG PHE C 331 2435 2018 1835 -610 84 -71 C ATOM 4320 CD1 PHE C 331 17.031 27.465 0.759 1.00 15.80 C ANISOU 4320 CD1 PHE C 331 2213 2063 1727 -629 63 -75 C ATOM 4321 CD2 PHE C 331 16.394 29.749 1.005 1.00 20.17 C ANISOU 4321 CD2 PHE C 331 2994 2393 2276 -716 102 -88 C ATOM 4322 CE1 PHE C 331 18.293 27.760 1.238 1.00 13.89 C ANISOU 4322 CE1 PHE C 331 1929 1897 1453 -752 56 -92 C ATOM 4323 CE2 PHE C 331 17.655 30.051 1.482 1.00 21.12 C ANISOU 4323 CE2 PHE C 331 3082 2580 2363 -856 96 -112 C ATOM 4324 CZ PHE C 331 18.605 29.054 1.599 1.00 18.05 C ANISOU 4324 CZ PHE C 331 2549 2351 1959 -874 70 -112 C ATOM 4325 N GLY C 332 12.358 28.021 -2.188 1.00 15.94 N ANISOU 4325 N GLY C 332 2445 1788 1824 -258 96 43 N ATOM 4326 CA GLY C 332 11.025 27.517 -2.476 1.00 16.03 C ANISOU 4326 CA GLY C 332 2444 1790 1857 -138 82 56 C ATOM 4327 C GLY C 332 10.986 26.461 -3.569 1.00 17.60 C ANISOU 4327 C GLY C 332 2566 2075 2048 -99 64 79 C ATOM 4328 O GLY C 332 11.563 26.646 -4.641 1.00 20.83 O ANISOU 4328 O GLY C 332 2978 2506 2429 -133 74 111 O ATOM 4329 N GLY C 333 10.313 25.345 -3.300 1.00 12.40 N ANISOU 4329 N GLY C 333 1841 1461 1408 -32 41 60 N ATOM 4330 CA GLY C 333 10.131 24.323 -4.316 1.00 15.28 C ANISOU 4330 CA GLY C 333 2147 1894 1765 7 24 71 C ATOM 4331 C GLY C 333 10.363 22.882 -3.893 1.00 14.05 C ANISOU 4331 C GLY C 333 1908 1807 1622 20 6 37 C ATOM 4332 O GLY C 333 10.290 22.540 -2.710 1.00 12.14 O ANISOU 4332 O GLY C 333 1648 1563 1400 21 0 11 O ATOM 4333 N ILE C 334 10.655 22.040 -4.882 1.00 11.80 N ANISOU 4333 N ILE C 334 1583 1582 1321 32 -1 38 N ATOM 4334 CA ILE C 334 10.729 20.595 -4.697 1.00 9.12 C ANISOU 4334 CA ILE C 334 1181 1291 994 59 -17 9 C ATOM 4335 C ILE C 334 12.144 20.055 -4.869 1.00 17.25 C ANISOU 4335 C ILE C 334 2162 2384 2006 29 -4 -5 C ATOM 4336 O ILE C 334 12.780 20.267 -5.903 1.00 14.27 O ANISOU 4336 O ILE C 334 1783 2043 1597 8 14 7 O ATOM 4337 CB ILE C 334 9.806 19.864 -5.693 1.00 10.40 C ANISOU 4337 CB ILE C 334 1335 1468 1150 108 -36 9 C ATOM 4338 CG1 ILE C 334 8.381 20.412 -5.601 1.00 10.48 C ANISOU 4338 CG1 ILE C 334 1373 1436 1173 145 -51 29 C ATOM 4339 CG2 ILE C 334 9.841 18.361 -5.456 1.00 12.42 C ANISOU 4339 CG2 ILE C 334 1545 1752 1423 131 -50 -25 C ATOM 4340 CD1 ILE C 334 7.440 19.837 -6.636 1.00 17.51 C ANISOU 4340 CD1 ILE C 334 2250 2356 2049 181 -76 32 C ATOM 4341 N TYR C 335 12.624 19.344 -3.853 1.00 9.06 N ANISOU 4341 N TYR C 335 1085 1369 989 31 -11 -26 N ATOM 4342 CA TYR C 335 13.947 18.734 -3.887 1.00 9.71 C ANISOU 4342 CA TYR C 335 1109 1523 1059 20 -2 -37 C ATOM 4343 C TYR C 335 13.832 17.214 -3.926 1.00 13.35 C ANISOU 4343 C TYR C 335 1537 1999 1536 85 -14 -58 C ATOM 4344 O TYR C 335 13.450 16.591 -2.935 1.00 13.40 O ANISOU 4344 O TYR C 335 1538 1983 1570 108 -33 -64 O ATOM 4345 CB TYR C 335 14.774 19.159 -2.670 1.00 11.96 C ANISOU 4345 CB TYR C 335 1370 1829 1345 -28 -4 -38 C ATOM 4346 CG TYR C 335 14.964 20.652 -2.515 1.00 12.39 C ANISOU 4346 CG TYR C 335 1470 1855 1382 -106 10 -26 C ATOM 4347 CD1 TYR C 335 13.920 21.468 -2.091 1.00 11.86 C ANISOU 4347 CD1 TYR C 335 1474 1703 1328 -107 8 -22 C ATOM 4348 CD2 TYR C 335 16.194 21.243 -2.769 1.00 10.39 C ANISOU 4348 CD2 TYR C 335 1189 1657 1100 -179 29 -18 C ATOM 4349 CE1 TYR C 335 14.095 22.834 -1.939 1.00 10.14 C ANISOU 4349 CE1 TYR C 335 1316 1439 1097 -174 23 -14 C ATOM 4350 CE2 TYR C 335 16.380 22.607 -2.618 1.00 14.21 C ANISOU 4350 CE2 TYR C 335 1728 2101 1569 -263 42 -8 C ATOM 4351 CZ TYR C 335 15.328 23.397 -2.203 1.00 15.67 C ANISOU 4351 CZ TYR C 335 2001 2184 1770 -258 40 -8 C ATOM 4352 OH TYR C 335 15.509 24.753 -2.050 1.00 12.60 O ANISOU 4352 OH TYR C 335 1684 1736 1368 -338 57 -1 O ATOM 4353 N LEU C 336 14.155 16.621 -5.071 1.00 11.92 N ANISOU 4353 N LEU C 336 1342 1853 1336 112 -1 -70 N ATOM 4354 CA LEU C 336 14.096 15.171 -5.223 1.00 12.16 C ANISOU 4354 CA LEU C 336 1357 1883 1379 173 -8 -97 C ATOM 4355 C LEU C 336 15.493 14.566 -5.114 1.00 14.06 C ANISOU 4355 C LEU C 336 1539 2192 1613 199 10 -105 C ATOM 4356 O LEU C 336 16.464 15.165 -5.569 1.00 14.90 O ANISOU 4356 O LEU C 336 1609 2365 1689 169 35 -98 O ATOM 4357 CB LEU C 336 13.457 14.791 -6.566 1.00 13.34 C ANISOU 4357 CB LEU C 336 1537 2024 1506 194 -6 -115 C ATOM 4358 CG LEU C 336 12.016 15.255 -6.818 1.00 12.19 C ANISOU 4358 CG LEU C 336 1437 1830 1364 181 -29 -104 C ATOM 4359 CD1 LEU C 336 11.522 14.810 -8.190 1.00 11.36 C ANISOU 4359 CD1 LEU C 336 1354 1738 1224 196 -32 -124 C ATOM 4360 CD2 LEU C 336 11.079 14.756 -5.721 1.00 10.66 C ANISOU 4360 CD2 LEU C 336 1251 1586 1214 192 -55 -105 C ATOM 4361 N PRO C 337 15.598 13.376 -4.501 1.00 14.09 N ANISOU 4361 N PRO C 337 1529 2181 1643 256 -2 -117 N ATOM 4362 CA PRO C 337 16.878 12.662 -4.434 1.00 15.00 C ANISOU 4362 CA PRO C 337 1586 2362 1754 306 14 -123 C ATOM 4363 C PRO C 337 17.209 12.005 -5.775 1.00 13.60 C ANISOU 4363 C PRO C 337 1409 2207 1552 355 45 -157 C ATOM 4364 O PRO C 337 17.262 10.778 -5.883 1.00 12.75 O ANISOU 4364 O PRO C 337 1314 2071 1459 429 48 -182 O ATOM 4365 CB PRO C 337 16.639 11.618 -3.341 1.00 18.14 C ANISOU 4365 CB PRO C 337 1992 2712 2188 357 -11 -118 C ATOM 4366 CG PRO C 337 15.172 11.350 -3.407 1.00 9.82 C ANISOU 4366 CG PRO C 337 1010 1566 1155 345 -29 -127 C ATOM 4367 CD PRO C 337 14.516 12.643 -3.821 1.00 11.82 C ANISOU 4367 CD PRO C 337 1283 1817 1391 277 -29 -120 C ATOM 4368 N LEU C 338 17.443 12.841 -6.781 1.00 14.02 N ANISOU 4368 N LEU C 338 1456 2308 1564 313 70 -157 N ATOM 4369 CA LEU C 338 17.569 12.406 -8.170 1.00 13.01 C ANISOU 4369 CA LEU C 338 1342 2204 1398 345 101 -191 C ATOM 4370 C LEU C 338 18.749 11.475 -8.449 1.00 13.18 C ANISOU 4370 C LEU C 338 1309 2290 1409 425 136 -217 C ATOM 4371 O LEU C 338 18.733 10.732 -9.430 1.00 12.69 O ANISOU 4371 O LEU C 338 1274 2225 1323 476 160 -260 O ATOM 4372 CB LEU C 338 17.663 13.637 -9.076 1.00 12.78 C ANISOU 4372 CB LEU C 338 1315 2222 1320 274 122 -170 C ATOM 4373 CG LEU C 338 16.447 14.561 -8.963 1.00 15.38 C ANISOU 4373 CG LEU C 338 1704 2482 1656 215 91 -143 C ATOM 4374 CD1 LEU C 338 16.694 15.891 -9.650 1.00 13.04 C ANISOU 4374 CD1 LEU C 338 1415 2224 1316 145 112 -108 C ATOM 4375 CD2 LEU C 338 15.216 13.872 -9.536 1.00 15.14 C ANISOU 4375 CD2 LEU C 338 1735 2391 1628 245 68 -171 C ATOM 4376 N GLU C 339 19.770 11.516 -7.600 1.00 12.53 N ANISOU 4376 N GLU C 339 1150 2272 1339 440 138 -193 N ATOM 4377 CA GLU C 339 20.930 10.649 -7.783 1.00 19.60 C ANISOU 4377 CA GLU C 339 1980 3241 2226 532 171 -211 C ATOM 4378 C GLU C 339 20.738 9.287 -7.124 1.00 22.72 C ANISOU 4378 C GLU C 339 2406 3560 2667 632 152 -226 C ATOM 4379 O GLU C 339 21.594 8.409 -7.230 1.00 25.14 O ANISOU 4379 O GLU C 339 2674 3906 2974 734 178 -242 O ATOM 4380 CB GLU C 339 22.192 11.323 -7.243 1.00 17.37 C ANISOU 4380 CB GLU C 339 1584 3086 1930 502 181 -175 C ATOM 4381 CG GLU C 339 22.726 12.399 -8.163 1.00 21.12 C ANISOU 4381 CG GLU C 339 2019 3654 2351 420 221 -167 C ATOM 4382 CD GLU C 339 22.945 11.882 -9.577 1.00 24.07 C ANISOU 4382 CD GLU C 339 2402 4063 2681 476 274 -208 C ATOM 4383 OE1 GLU C 339 22.687 12.636 -10.540 1.00 22.54 O ANISOU 4383 OE1 GLU C 339 2239 3882 2442 407 296 -206 O ATOM 4384 OE2 GLU C 339 23.378 10.718 -9.725 1.00 23.66 O ANISOU 4384 OE2 GLU C 339 2331 4022 2636 592 295 -242 O ATOM 4385 N VAL C 340 19.608 9.113 -6.449 1.00 17.71 N ANISOU 4385 N VAL C 340 1844 2816 2069 607 110 -217 N ATOM 4386 CA VAL C 340 19.286 7.838 -5.826 1.00 18.03 C ANISOU 4386 CA VAL C 340 1932 2767 2152 685 92 -224 C ATOM 4387 C VAL C 340 18.127 7.179 -6.557 1.00 16.20 C ANISOU 4387 C VAL C 340 1805 2425 1926 682 89 -269 C ATOM 4388 O VAL C 340 17.106 7.819 -6.796 1.00 18.35 O ANISOU 4388 O VAL C 340 2115 2665 2192 600 70 -269 O ATOM 4389 CB VAL C 340 18.917 8.005 -4.338 1.00 20.46 C ANISOU 4389 CB VAL C 340 2239 3041 2494 654 47 -175 C ATOM 4390 CG1 VAL C 340 18.691 6.643 -3.691 1.00 18.92 C ANISOU 4390 CG1 VAL C 340 2096 2755 2339 736 32 -171 C ATOM 4391 CG2 VAL C 340 20.004 8.772 -3.604 1.00 27.95 C ANISOU 4391 CG2 VAL C 340 3085 4106 3428 634 41 -135 C ATOM 4392 N PRO C 341 18.283 5.897 -6.918 1.00 15.40 N ANISOU 4392 N PRO C 341 1749 2267 1835 772 108 -309 N ATOM 4393 CA PRO C 341 17.205 5.151 -7.573 1.00 16.34 C ANISOU 4393 CA PRO C 341 1974 2278 1957 760 103 -359 C ATOM 4394 C PRO C 341 15.897 5.249 -6.789 1.00 15.95 C ANISOU 4394 C PRO C 341 1973 2145 1942 682 55 -332 C ATOM 4395 O PRO C 341 15.884 5.013 -5.578 1.00 13.34 O ANISOU 4395 O PRO C 341 1637 1782 1650 693 33 -288 O ATOM 4396 CB PRO C 341 17.735 3.714 -7.593 1.00 18.20 C ANISOU 4396 CB PRO C 341 2255 2448 2214 878 126 -392 C ATOM 4397 CG PRO C 341 19.220 3.870 -7.579 1.00 20.01 C ANISOU 4397 CG PRO C 341 2385 2794 2426 963 162 -376 C ATOM 4398 CD PRO C 341 19.487 5.071 -6.717 1.00 15.68 C ANISOU 4398 CD PRO C 341 1744 2337 1879 894 135 -309 C ATOM 4399 N ALA C 342 14.818 5.611 -7.478 1.00 15.25 N ANISOU 4399 N ALA C 342 1925 2034 1834 606 40 -356 N ATOM 4400 CA ALA C 342 13.520 5.811 -6.840 1.00 17.46 C ANISOU 4400 CA ALA C 342 2235 2258 2141 530 0 -331 C ATOM 4401 C ALA C 342 13.078 4.578 -6.057 1.00 20.77 C ANISOU 4401 C ALA C 342 2716 2569 2606 550 -15 -329 C ATOM 4402 O ALA C 342 12.377 4.687 -5.051 1.00 22.60 O ANISOU 4402 O ALA C 342 2951 2769 2867 507 -41 -288 O ATOM 4403 CB ALA C 342 12.473 6.176 -7.881 1.00 13.36 C ANISOU 4403 CB ALA C 342 1748 1740 1589 462 -14 -363 C ATOM 4404 N SER C 343 13.500 3.408 -6.521 1.00 19.63 N ANISOU 4404 N SER C 343 2628 2365 2465 619 7 -374 N ATOM 4405 CA SER C 343 13.157 2.147 -5.871 1.00 22.42 C ANISOU 4405 CA SER C 343 3060 2598 2861 642 -1 -372 C ATOM 4406 C SER C 343 13.754 2.020 -4.468 1.00 21.99 C ANISOU 4406 C SER C 343 2973 2541 2841 692 -9 -301 C ATOM 4407 O SER C 343 13.372 1.135 -3.703 1.00 23.19 O ANISOU 4407 O SER C 343 3186 2596 3028 699 -21 -277 O ATOM 4408 CB SER C 343 13.623 0.973 -6.732 1.00 23.63 C ANISOU 4408 CB SER C 343 3290 2681 3007 719 31 -440 C ATOM 4409 OG SER C 343 15.032 0.994 -6.889 1.00 27.53 O ANISOU 4409 OG SER C 343 3730 3243 3489 830 68 -439 O ATOM 4410 N GLN C 344 14.696 2.896 -4.137 1.00 17.98 N ANISOU 4410 N GLN C 344 2370 2144 2319 722 -3 -266 N ATOM 4411 CA GLN C 344 15.352 2.852 -2.834 1.00 15.68 C ANISOU 4411 CA GLN C 344 2035 1875 2047 768 -16 -199 C ATOM 4412 C GLN C 344 14.955 4.039 -1.961 1.00 16.94 C ANISOU 4412 C GLN C 344 2137 2098 2200 683 -43 -152 C ATOM 4413 O GLN C 344 15.499 4.231 -0.872 1.00 18.95 O ANISOU 4413 O GLN C 344 2346 2395 2458 703 -58 -99 O ATOM 4414 CB GLN C 344 16.872 2.811 -3.006 1.00 14.57 C ANISOU 4414 CB GLN C 344 1824 1820 1891 873 10 -196 C ATOM 4415 CG GLN C 344 17.384 1.521 -3.629 1.00 16.88 C ANISOU 4415 CG GLN C 344 2177 2043 2194 988 42 -237 C ATOM 4416 CD GLN C 344 18.885 1.528 -3.846 1.00 21.78 C ANISOU 4416 CD GLN C 344 2710 2770 2797 1101 73 -234 C ATOM 4417 OE1 GLN C 344 19.403 2.289 -4.663 1.00 27.53 O ANISOU 4417 OE1 GLN C 344 3368 3606 3487 1086 98 -262 O ATOM 4418 NE2 GLN C 344 19.592 0.678 -3.112 1.00 17.98 N ANISOU 4418 NE2 GLN C 344 2227 2265 2339 1217 72 -195 N ATOM 4419 N CYS C 345 13.994 4.824 -2.438 1.00 15.01 N ANISOU 4419 N CYS C 345 1899 1861 1944 593 -51 -171 N ATOM 4420 CA CYS C 345 13.606 6.060 -1.765 1.00 12.76 C ANISOU 4420 CA CYS C 345 1567 1633 1650 520 -69 -137 C ATOM 4421 C CYS C 345 12.224 6.006 -1.119 1.00 15.52 C ANISOU 4421 C CYS C 345 1957 1921 2018 453 -90 -120 C ATOM 4422 O CYS C 345 11.332 5.292 -1.581 1.00 19.17 O ANISOU 4422 O CYS C 345 2478 2313 2494 429 -93 -145 O ATOM 4423 CB CYS C 345 13.650 7.227 -2.756 1.00 11.99 C ANISOU 4423 CB CYS C 345 1433 1603 1518 478 -57 -161 C ATOM 4424 SG CYS C 345 15.310 7.743 -3.253 1.00 20.03 S ANISOU 4424 SG CYS C 345 2373 2731 2505 524 -29 -164 S ATOM 4425 N HIS C 346 12.059 6.770 -0.043 1.00 12.85 N ANISOU 4425 N HIS C 346 1585 1619 1677 417 -103 -79 N ATOM 4426 CA HIS C 346 10.741 7.027 0.525 1.00 15.51 C ANISOU 4426 CA HIS C 346 1942 1928 2024 351 -115 -64 C ATOM 4427 C HIS C 346 10.002 7.999 -0.386 1.00 15.18 C ANISOU 4427 C HIS C 346 1888 1912 1967 303 -114 -92 C ATOM 4428 O HIS C 346 10.617 8.890 -0.963 1.00 15.97 O ANISOU 4428 O HIS C 346 1956 2066 2045 307 -105 -103 O ATOM 4429 CB HIS C 346 10.851 7.607 1.938 1.00 14.56 C ANISOU 4429 CB HIS C 346 1793 1845 1896 335 -124 -19 C ATOM 4430 CG HIS C 346 11.763 6.836 2.840 1.00 20.68 C ANISOU 4430 CG HIS C 346 2568 2619 2673 389 -131 18 C ATOM 4431 ND1 HIS C 346 11.383 5.666 3.459 1.00 25.56 N ANISOU 4431 ND1 HIS C 346 3237 3166 3310 404 -136 47 N ATOM 4432 CD2 HIS C 346 13.039 7.070 3.229 1.00 23.43 C ANISOU 4432 CD2 HIS C 346 2867 3033 3002 432 -136 36 C ATOM 4433 CE1 HIS C 346 12.385 5.210 4.189 1.00 25.47 C ANISOU 4433 CE1 HIS C 346 3213 3173 3292 466 -145 86 C ATOM 4434 NE2 HIS C 346 13.402 6.045 4.067 1.00 26.56 N ANISOU 4434 NE2 HIS C 346 3283 3403 3406 484 -147 78 N ATOM 4435 N ARG C 347 8.691 7.836 -0.514 1.00 11.21 N ANISOU 4435 N ARG C 347 1407 1377 1474 256 -123 -99 N ATOM 4436 CA ARG C 347 7.925 8.658 -1.448 1.00 13.08 C ANISOU 4436 CA ARG C 347 1631 1643 1694 223 -127 -120 C ATOM 4437 C ARG C 347 7.247 9.854 -0.782 1.00 14.33 C ANISOU 4437 C ARG C 347 1759 1836 1849 194 -128 -93 C ATOM 4438 O ARG C 347 7.131 10.921 -1.386 1.00 17.21 O ANISOU 4438 O ARG C 347 2109 2236 2196 189 -126 -97 O ATOM 4439 CB ARG C 347 6.888 7.793 -2.169 1.00 18.91 C ANISOU 4439 CB ARG C 347 2403 2343 2440 190 -140 -148 C ATOM 4440 CG ARG C 347 7.510 6.610 -2.901 1.00 22.90 C ANISOU 4440 CG ARG C 347 2956 2799 2946 220 -134 -186 C ATOM 4441 CD ARG C 347 6.493 5.825 -3.707 1.00 27.72 C ANISOU 4441 CD ARG C 347 3606 3372 3555 171 -150 -225 C ATOM 4442 NE ARG C 347 6.089 6.530 -4.921 1.00 32.01 N ANISOU 4442 NE ARG C 347 4129 3973 4062 151 -161 -253 N ATOM 4443 CZ ARG C 347 6.864 6.678 -5.991 1.00 30.93 C ANISOU 4443 CZ ARG C 347 4000 3861 3891 186 -150 -286 C ATOM 4444 NH1 ARG C 347 8.093 6.178 -5.994 1.00 29.45 N ANISOU 4444 NH1 ARG C 347 3832 3651 3707 247 -124 -299 N ATOM 4445 NH2 ARG C 347 6.412 7.332 -7.055 1.00 28.78 N ANISOU 4445 NH2 ARG C 347 3713 3644 3579 164 -163 -302 N ATOM 4446 N SER C 348 6.802 9.678 0.458 1.00 13.01 N ANISOU 4446 N SER C 348 1590 1657 1695 179 -127 -66 N ATOM 4447 CA SER C 348 6.155 10.756 1.199 1.00 13.06 C ANISOU 4447 CA SER C 348 1574 1694 1695 160 -121 -47 C ATOM 4448 C SER C 348 7.184 11.826 1.560 1.00 12.25 C ANISOU 4448 C SER C 348 1459 1621 1573 175 -112 -42 C ATOM 4449 O SER C 348 8.241 11.511 2.102 1.00 15.67 O ANISOU 4449 O SER C 348 1890 2061 2001 191 -112 -33 O ATOM 4450 CB SER C 348 5.477 10.209 2.459 1.00 15.24 C ANISOU 4450 CB SER C 348 1852 1957 1981 138 -117 -20 C ATOM 4451 OG SER C 348 4.732 11.216 3.119 1.00 24.57 O ANISOU 4451 OG SER C 348 3011 3170 3152 127 -105 -11 O ATOM 4452 N PRO C 349 6.877 13.097 1.257 1.00 9.59 N ANISOU 4452 N PRO C 349 1116 1302 1223 169 -105 -46 N ATOM 4453 CA PRO C 349 7.866 14.170 1.393 1.00 11.07 C ANISOU 4453 CA PRO C 349 1304 1510 1391 166 -95 -47 C ATOM 4454 C PRO C 349 8.029 14.704 2.811 1.00 11.76 C ANISOU 4454 C PRO C 349 1394 1607 1468 151 -87 -37 C ATOM 4455 O PRO C 349 7.111 14.631 3.627 1.00 13.11 O ANISOU 4455 O PRO C 349 1567 1771 1642 148 -82 -30 O ATOM 4456 CB PRO C 349 7.307 15.266 0.484 1.00 11.38 C ANISOU 4456 CB PRO C 349 1354 1547 1423 166 -89 -50 C ATOM 4457 CG PRO C 349 5.832 15.080 0.568 1.00 14.09 C ANISOU 4457 CG PRO C 349 1690 1884 1780 172 -94 -45 C ATOM 4458 CD PRO C 349 5.606 13.588 0.697 1.00 12.89 C ANISOU 4458 CD PRO C 349 1529 1724 1644 165 -106 -48 C ATOM 4459 N LEU C 350 9.218 15.223 3.091 1.00 10.57 N ANISOU 4459 N LEU C 350 1238 1480 1297 137 -86 -40 N ATOM 4460 CA LEU C 350 9.422 16.107 4.227 1.00 11.54 C ANISOU 4460 CA LEU C 350 1373 1614 1397 110 -79 -43 C ATOM 4461 C LEU C 350 9.006 17.506 3.792 1.00 13.53 C ANISOU 4461 C LEU C 350 1658 1840 1644 96 -62 -56 C ATOM 4462 O LEU C 350 9.493 18.016 2.781 1.00 11.86 O ANISOU 4462 O LEU C 350 1452 1625 1430 87 -59 -58 O ATOM 4463 CB LEU C 350 10.882 16.089 4.687 1.00 10.37 C ANISOU 4463 CB LEU C 350 1200 1513 1225 89 -91 -41 C ATOM 4464 CG LEU C 350 11.286 17.148 5.715 1.00 13.13 C ANISOU 4464 CG LEU C 350 1566 1882 1541 41 -88 -54 C ATOM 4465 CD1 LEU C 350 10.585 16.898 7.042 1.00 10.14 C ANISOU 4465 CD1 LEU C 350 1202 1503 1148 45 -88 -50 C ATOM 4466 CD2 LEU C 350 12.798 17.167 5.898 1.00 8.89 C ANISOU 4466 CD2 LEU C 350 989 1411 978 12 -106 -52 C ATOM 4467 N VAL C 351 8.095 18.120 4.539 1.00 12.80 N ANISOU 4467 N VAL C 351 1590 1725 1547 99 -46 -63 N ATOM 4468 CA VAL C 351 7.561 19.415 4.145 1.00 8.32 C ANISOU 4468 CA VAL C 351 1064 1119 980 105 -26 -72 C ATOM 4469 C VAL C 351 8.053 20.512 5.081 1.00 13.72 C ANISOU 4469 C VAL C 351 1793 1787 1635 68 -11 -95 C ATOM 4470 O VAL C 351 7.870 20.440 6.298 1.00 13.82 O ANISOU 4470 O VAL C 351 1810 1813 1630 61 -5 -108 O ATOM 4471 CB VAL C 351 6.024 19.395 4.113 1.00 11.82 C ANISOU 4471 CB VAL C 351 1503 1548 1440 152 -15 -65 C ATOM 4472 CG1 VAL C 351 5.479 20.750 3.692 1.00 8.67 C ANISOU 4472 CG1 VAL C 351 1148 1104 1040 178 5 -68 C ATOM 4473 CG2 VAL C 351 5.540 18.309 3.164 1.00 9.87 C ANISOU 4473 CG2 VAL C 351 1214 1320 1214 171 -35 -48 C ATOM 4474 N LEU C 352 8.692 21.523 4.500 1.00 9.51 N ANISOU 4474 N LEU C 352 1296 1224 1092 36 -4 -101 N ATOM 4475 CA LEU C 352 9.299 22.595 5.273 1.00 12.12 C ANISOU 4475 CA LEU C 352 1680 1532 1395 -19 9 -129 C ATOM 4476 C LEU C 352 8.804 23.958 4.818 1.00 15.67 C ANISOU 4476 C LEU C 352 2207 1898 1848 -9 36 -136 C ATOM 4477 O LEU C 352 8.225 24.097 3.739 1.00 16.92 O ANISOU 4477 O LEU C 352 2371 2029 2028 36 40 -109 O ATOM 4478 CB LEU C 352 10.824 22.546 5.155 1.00 12.08 C ANISOU 4478 CB LEU C 352 1648 1574 1369 -91 -9 -131 C ATOM 4479 CG LEU C 352 11.537 21.237 5.497 1.00 10.91 C ANISOU 4479 CG LEU C 352 1420 1509 1215 -89 -38 -118 C ATOM 4480 CD1 LEU C 352 13.035 21.382 5.266 1.00 13.02 C ANISOU 4480 CD1 LEU C 352 1653 1834 1460 -153 -52 -118 C ATOM 4481 CD2 LEU C 352 11.243 20.823 6.932 1.00 9.94 C ANISOU 4481 CD2 LEU C 352 1294 1411 1072 -84 -45 -128 C ATOM 4482 N ALA C 353 9.037 24.962 5.654 1.00 12.34 N ANISOU 4482 N ALA C 353 1853 1434 1401 -51 55 -171 N ATOM 4483 CA ALA C 353 8.802 26.345 5.277 1.00 13.37 C ANISOU 4483 CA ALA C 353 2080 1467 1533 -53 83 -179 C ATOM 4484 C ALA C 353 10.082 27.140 5.507 1.00 14.85 C ANISOU 4484 C ALA C 353 2315 1636 1690 -165 83 -204 C ATOM 4485 O ALA C 353 10.861 26.823 6.407 1.00 13.51 O ANISOU 4485 O ALA C 353 2116 1528 1491 -229 66 -231 O ATOM 4486 CB ALA C 353 7.646 26.935 6.068 1.00 11.60 C ANISOU 4486 CB ALA C 353 1912 1186 1309 12 116 -206 C ATOM 4487 N TYR C 354 10.305 28.156 4.682 1.00 13.34 N ANISOU 4487 N TYR C 354 2197 1368 1504 -193 100 -190 N ATOM 4488 CA TYR C 354 11.463 29.024 4.844 1.00 15.51 C ANISOU 4488 CA TYR C 354 2527 1617 1749 -316 104 -213 C ATOM 4489 C TYR C 354 11.032 30.483 4.915 1.00 18.21 C ANISOU 4489 C TYR C 354 3014 1815 2091 -321 142 -234 C ATOM 4490 O TYR C 354 10.204 30.933 4.122 1.00 16.03 O ANISOU 4490 O TYR C 354 2788 1462 1842 -240 161 -199 O ATOM 4491 CB TYR C 354 12.467 28.833 3.698 1.00 13.62 C ANISOU 4491 CB TYR C 354 2239 1427 1510 -376 91 -172 C ATOM 4492 CG TYR C 354 13.566 29.877 3.698 1.00 16.69 C ANISOU 4492 CG TYR C 354 2689 1781 1869 -513 101 -187 C ATOM 4493 CD1 TYR C 354 13.404 31.085 3.028 1.00 18.82 C ANISOU 4493 CD1 TYR C 354 3076 1928 2144 -537 132 -170 C ATOM 4494 CD2 TYR C 354 14.757 29.663 4.382 1.00 16.16 C ANISOU 4494 CD2 TYR C 354 2565 1806 1768 -623 79 -216 C ATOM 4495 CE1 TYR C 354 14.397 32.048 3.036 1.00 23.84 C ANISOU 4495 CE1 TYR C 354 3779 2526 2755 -679 144 -183 C ATOM 4496 CE2 TYR C 354 15.759 30.624 4.394 1.00 18.26 C ANISOU 4496 CE2 TYR C 354 2883 2051 2005 -766 87 -233 C ATOM 4497 CZ TYR C 354 15.572 31.813 3.719 1.00 25.29 C ANISOU 4497 CZ TYR C 354 3896 2809 2903 -800 121 -217 C ATOM 4498 OH TYR C 354 16.561 32.771 3.724 1.00 32.43 O ANISOU 4498 OH TYR C 354 4860 3685 3779 -957 131 -232 O ATOM 4499 N ASP C 355 11.605 31.215 5.866 1.00 19.13 N ANISOU 4499 N ASP C 355 3200 1895 2173 -416 150 -290 N ATOM 4500 CA ASP C 355 11.363 32.648 5.991 1.00 21.33 C ANISOU 4500 CA ASP C 355 3636 2021 2448 -438 189 -319 C ATOM 4501 C ASP C 355 12.408 33.308 6.885 1.00 20.50 C ANISOU 4501 C ASP C 355 3591 1903 2295 -592 187 -384 C ATOM 4502 O ASP C 355 12.704 32.821 7.977 1.00 17.59 O ANISOU 4502 O ASP C 355 3172 1619 1891 -628 166 -430 O ATOM 4503 CB ASP C 355 9.958 32.913 6.539 1.00 20.06 C ANISOU 4503 CB ASP C 355 3534 1786 2301 -303 221 -343 C ATOM 4504 CG ASP C 355 9.671 34.395 6.716 1.00 25.73 C ANISOU 4504 CG ASP C 355 4428 2332 3017 -307 267 -378 C ATOM 4505 OD1 ASP C 355 9.535 35.103 5.695 1.00 26.36 O ANISOU 4505 OD1 ASP C 355 4582 2313 3122 -285 284 -330 O ATOM 4506 OD2 ASP C 355 9.575 34.852 7.876 1.00 26.82 O ANISOU 4506 OD2 ASP C 355 4637 2429 3123 -328 288 -453 O ATOM 4507 N GLN C 356 12.966 34.414 6.401 1.00 20.98 N ANISOU 4507 N GLN C 356 3759 1860 2350 -689 206 -383 N ATOM 4508 CA GLN C 356 13.922 35.219 7.156 1.00 25.52 C ANISOU 4508 CA GLN C 356 4413 2405 2880 -854 206 -447 C ATOM 4509 C GLN C 356 15.068 34.394 7.742 1.00 24.86 C ANISOU 4509 C GLN C 356 4193 2499 2754 -964 157 -466 C ATOM 4510 O GLN C 356 15.350 34.467 8.936 1.00 22.55 O ANISOU 4510 O GLN C 356 3912 2241 2415 -1028 143 -535 O ATOM 4511 CB GLN C 356 13.197 35.983 8.267 1.00 27.21 C ANISOU 4511 CB GLN C 356 4761 2503 3074 -822 239 -527 C ATOM 4512 CG GLN C 356 12.063 36.859 7.754 1.00 28.84 C ANISOU 4512 CG GLN C 356 5105 2530 3321 -697 290 -510 C ATOM 4513 CD GLN C 356 11.355 37.617 8.859 1.00 33.00 C ANISOU 4513 CD GLN C 356 5732 2974 3832 -638 325 -579 C ATOM 4514 OE1 GLN C 356 11.970 38.404 9.580 1.00 34.66 O ANISOU 4514 OE1 GLN C 356 5999 3163 4008 -741 327 -628 O ATOM 4515 NE2 GLN C 356 10.054 37.382 9.001 1.00 30.23 N ANISOU 4515 NE2 GLN C 356 5384 2595 3506 -465 352 -578 N ATOM 4516 N ALA C 357 15.715 33.606 6.890 1.00 23.15 N ANISOU 4516 N ALA C 357 3845 2400 2551 -977 131 -404 N ATOM 4517 CA ALA C 357 16.882 32.825 7.285 1.00 23.44 C ANISOU 4517 CA ALA C 357 3743 2612 2552 -1069 85 -409 C ATOM 4518 C ALA C 357 16.526 31.730 8.284 1.00 23.27 C ANISOU 4518 C ALA C 357 3629 2695 2516 -985 55 -428 C ATOM 4519 O ALA C 357 17.378 31.279 9.047 1.00 24.13 O ANISOU 4519 O ALA C 357 3656 2932 2582 -1059 16 -450 O ATOM 4520 CB ALA C 357 17.957 33.735 7.862 1.00 27.83 C ANISOU 4520 CB ALA C 357 4353 3166 3056 -1262 77 -463 C ATOM 4521 N HIS C 358 15.270 31.307 8.266 1.00 19.00 N ANISOU 4521 N HIS C 358 3101 2107 2010 -832 72 -415 N ATOM 4522 CA HIS C 358 14.805 30.250 9.149 1.00 21.14 C ANISOU 4522 CA HIS C 358 3295 2466 2271 -749 51 -423 C ATOM 4523 C HIS C 358 14.121 29.114 8.393 1.00 16.99 C ANISOU 4523 C HIS C 358 2679 1983 1795 -616 46 -360 C ATOM 4524 O HIS C 358 13.361 29.354 7.468 1.00 17.36 O ANISOU 4524 O HIS C 358 2762 1949 1883 -543 72 -327 O ATOM 4525 CB HIS C 358 13.836 30.804 10.190 1.00 24.84 C ANISOU 4525 CB HIS C 358 3869 2848 2721 -702 81 -481 C ATOM 4526 CG HIS C 358 14.426 31.858 11.068 1.00 31.43 C ANISOU 4526 CG HIS C 358 4806 3638 3498 -831 86 -558 C ATOM 4527 ND1 HIS C 358 13.694 32.922 11.545 1.00 35.74 N ANISOU 4527 ND1 HIS C 358 5304 4280 3994 -979 45 -579 N ATOM 4528 CD2 HIS C 358 15.678 32.013 11.557 1.00 34.33 C ANISOU 4528 CD2 HIS C 358 5323 3875 3848 -834 127 -624 C ATOM 4529 CE1 HIS C 358 14.468 33.685 12.293 1.00 36.61 C ANISOU 4529 CE1 HIS C 358 5533 4322 4055 -1083 57 -657 C ATOM 4530 NE2 HIS C 358 15.677 33.158 12.314 1.00 35.90 N ANISOU 4530 NE2 HIS C 358 5571 4086 3984 -995 109 -688 N ATOM 4531 N PHE C 359 14.398 27.886 8.814 1.00 13.65 N ANISOU 4531 N PHE C 359 2142 1684 1362 -587 12 -342 N ATOM 4532 CA PHE C 359 13.685 26.708 8.332 1.00 18.32 C ANISOU 4532 CA PHE C 359 2658 2309 1994 -467 6 -295 C ATOM 4533 C PHE C 359 12.795 26.140 9.435 1.00 17.29 C ANISOU 4533 C PHE C 359 2524 2194 1851 -399 7 -311 C ATOM 4534 O PHE C 359 13.197 26.075 10.592 1.00 19.97 O ANISOU 4534 O PHE C 359 2858 2588 2140 -447 -10 -342 O ATOM 4535 CB PHE C 359 14.662 25.631 7.856 1.00 18.46 C ANISOU 4535 CB PHE C 359 2553 2444 2015 -476 -29 -254 C ATOM 4536 CG PHE C 359 15.261 25.902 6.507 1.00 15.31 C ANISOU 4536 CG PHE C 359 2140 2041 1637 -507 -21 -224 C ATOM 4537 CD1 PHE C 359 14.536 25.661 5.352 1.00 18.16 C ANISOU 4537 CD1 PHE C 359 2505 2354 2040 -426 -3 -188 C ATOM 4538 CD2 PHE C 359 16.555 26.381 6.393 1.00 15.87 C ANISOU 4538 CD2 PHE C 359 2186 2166 1678 -623 -31 -231 C ATOM 4539 CE1 PHE C 359 15.086 25.902 4.107 1.00 18.59 C ANISOU 4539 CE1 PHE C 359 2548 2412 2102 -455 7 -159 C ATOM 4540 CE2 PHE C 359 17.112 26.623 5.150 1.00 19.27 C ANISOU 4540 CE2 PHE C 359 2599 2602 2121 -655 -16 -200 C ATOM 4541 CZ PHE C 359 16.375 26.383 4.005 1.00 17.38 C ANISOU 4541 CZ PHE C 359 2373 2311 1920 -568 4 -163 C ATOM 4542 N SER C 360 11.587 25.728 9.073 1.00 15.21 N ANISOU 4542 N SER C 360 2258 1893 1627 -293 27 -287 N ATOM 4543 CA SER C 360 10.673 25.111 10.029 1.00 16.83 C ANISOU 4543 CA SER C 360 2450 2123 1822 -230 34 -294 C ATOM 4544 C SER C 360 9.899 23.975 9.377 1.00 14.16 C ANISOU 4544 C SER C 360 2043 1808 1530 -142 29 -244 C ATOM 4545 O SER C 360 9.558 24.047 8.199 1.00 12.63 O ANISOU 4545 O SER C 360 1847 1575 1377 -104 36 -218 O ATOM 4546 CB SER C 360 9.695 26.143 10.598 1.00 17.25 C ANISOU 4546 CB SER C 360 2601 2090 1864 -201 79 -339 C ATOM 4547 OG SER C 360 10.344 27.050 11.471 1.00 20.92 O ANISOU 4547 OG SER C 360 3138 2536 2275 -288 83 -398 O ATOM 4548 N ALA C 361 9.624 22.929 10.148 1.00 12.57 N ANISOU 4548 N ALA C 361 1792 1669 1317 -115 17 -229 N ATOM 4549 CA ALA C 361 8.771 21.846 9.681 1.00 14.98 C ANISOU 4549 CA ALA C 361 2043 1987 1661 -44 15 -188 C ATOM 4550 C ALA C 361 7.311 22.279 9.727 1.00 15.07 C ANISOU 4550 C ALA C 361 2086 1952 1690 19 55 -198 C ATOM 4551 O ALA C 361 6.873 22.907 10.691 1.00 15.37 O ANISOU 4551 O ALA C 361 2169 1976 1695 21 83 -233 O ATOM 4552 CB ALA C 361 8.982 20.594 10.518 1.00 12.05 C ANISOU 4552 CB ALA C 361 1618 1690 1271 -43 -9 -164 C ATOM 4553 N LEU C 362 6.565 21.949 8.677 1.00 12.18 N ANISOU 4553 N LEU C 362 1691 1567 1368 72 56 -168 N ATOM 4554 CA LEU C 362 5.146 22.276 8.617 1.00 13.86 C ANISOU 4554 CA LEU C 362 1911 1756 1598 141 89 -169 C ATOM 4555 C LEU C 362 4.291 21.107 9.093 1.00 13.91 C ANISOU 4555 C LEU C 362 1855 1821 1611 165 90 -145 C ATOM 4556 O LEU C 362 4.581 19.948 8.793 1.00 12.25 O ANISOU 4556 O LEU C 362 1597 1644 1415 149 60 -115 O ATOM 4557 CB LEU C 362 4.737 22.672 7.193 1.00 11.76 C ANISOU 4557 CB LEU C 362 1648 1450 1372 182 87 -147 C ATOM 4558 CG LEU C 362 5.208 24.030 6.670 1.00 10.20 C ANISOU 4558 CG LEU C 362 1529 1177 1171 171 99 -162 C ATOM 4559 CD1 LEU C 362 4.848 24.187 5.197 1.00 11.53 C ANISOU 4559 CD1 LEU C 362 1689 1322 1369 212 89 -125 C ATOM 4560 CD2 LEU C 362 4.608 25.157 7.494 1.00 10.93 C ANISOU 4560 CD2 LEU C 362 1694 1214 1246 204 142 -199 C ATOM 4561 N VAL C 363 3.246 21.424 9.848 1.00 13.13 N ANISOU 4561 N VAL C 363 1761 1730 1498 203 128 -160 N ATOM 4562 CA VAL C 363 2.270 20.432 10.277 1.00 12.26 C ANISOU 4562 CA VAL C 363 1590 1678 1391 221 138 -134 C ATOM 4563 C VAL C 363 0.870 21.030 10.259 1.00 12.54 C ANISOU 4563 C VAL C 363 1611 1718 1437 291 180 -141 C ATOM 4564 O VAL C 363 0.703 22.243 10.380 1.00 12.42 O ANISOU 4564 O VAL C 363 1650 1657 1411 332 211 -175 O ATOM 4565 CB VAL C 363 2.565 19.901 11.698 1.00 13.93 C ANISOU 4565 CB VAL C 363 1804 1936 1553 181 145 -138 C ATOM 4566 CG1 VAL C 363 3.913 19.195 11.744 1.00 14.62 C ANISOU 4566 CG1 VAL C 363 1891 2034 1631 125 99 -122 C ATOM 4567 CG2 VAL C 363 2.510 21.033 12.711 1.00 13.39 C ANISOU 4567 CG2 VAL C 363 1796 1855 1436 188 186 -190 C ATOM 4568 N SER C 364 -0.134 20.176 10.092 1.00 14.92 N ANISOU 4568 N SER C 364 1838 2073 1758 306 182 -110 N ATOM 4569 CA SER C 364 -1.514 20.595 10.276 1.00 11.21 C ANISOU 4569 CA SER C 364 1331 1640 1290 372 226 -112 C ATOM 4570 C SER C 364 -1.838 20.498 11.759 1.00 11.71 C ANISOU 4570 C SER C 364 1395 1749 1305 363 271 -130 C ATOM 4571 O SER C 364 -1.105 19.862 12.514 1.00 11.51 O ANISOU 4571 O SER C 364 1387 1737 1248 300 258 -126 O ATOM 4572 CB SER C 364 -2.472 19.734 9.453 1.00 14.34 C ANISOU 4572 CB SER C 364 1637 2090 1722 378 206 -72 C ATOM 4573 OG SER C 364 -2.444 18.381 9.880 1.00 14.71 O ANISOU 4573 OG SER C 364 1645 2179 1764 309 192 -46 O ATOM 4574 N MET C 365 -2.931 21.123 12.179 1.00 12.45 N ANISOU 4574 N MET C 365 1468 1875 1387 431 325 -147 N ATOM 4575 CA MET C 365 -3.333 21.040 13.575 1.00 18.65 C ANISOU 4575 CA MET C 365 2250 2717 2118 426 377 -165 C ATOM 4576 C MET C 365 -3.809 19.628 13.914 1.00 17.16 C ANISOU 4576 C MET C 365 1982 2612 1926 366 371 -115 C ATOM 4577 O MET C 365 -3.695 19.188 15.056 1.00 13.23 O ANISOU 4577 O MET C 365 1494 2156 1377 324 393 -114 O ATOM 4578 CB MET C 365 -4.414 22.074 13.886 1.00 22.29 C ANISOU 4578 CB MET C 365 2705 3196 2568 527 444 -198 C ATOM 4579 CG MET C 365 -3.885 23.501 13.928 1.00 23.38 C ANISOU 4579 CG MET C 365 2954 3235 2694 577 463 -255 C ATOM 4580 SD MET C 365 -2.422 23.665 14.977 1.00 30.31 S ANISOU 4580 SD MET C 365 3940 4069 3509 484 451 -302 S ATOM 4581 CE MET C 365 -3.046 23.038 16.538 1.00 14.82 C ANISOU 4581 CE MET C 365 1939 2217 1473 466 505 -309 C ATOM 4582 N GLU C 366 -4.326 18.917 12.915 1.00 15.83 N ANISOU 4582 N GLU C 366 1742 2466 1807 356 339 -75 N ATOM 4583 CA GLU C 366 -4.718 17.524 13.103 1.00 18.40 C ANISOU 4583 CA GLU C 366 2005 2850 2134 284 329 -27 C ATOM 4584 C GLU C 366 -3.497 16.651 13.383 1.00 18.24 C ANISOU 4584 C GLU C 366 2040 2787 2103 208 287 -8 C ATOM 4585 O GLU C 366 -3.520 15.812 14.284 1.00 16.41 O ANISOU 4585 O GLU C 366 1803 2592 1839 155 299 20 O ATOM 4586 CB GLU C 366 -5.476 17.001 11.881 1.00 22.91 C ANISOU 4586 CB GLU C 366 2498 3447 2758 281 298 2 C ATOM 4587 CG GLU C 366 -6.898 17.527 11.757 1.00 28.15 C ANISOU 4587 CG GLU C 366 3075 4194 3428 347 338 2 C ATOM 4588 CD GLU C 366 -7.631 16.956 10.555 1.00 35.87 C ANISOU 4588 CD GLU C 366 3967 5213 4448 330 298 32 C ATOM 4589 OE1 GLU C 366 -7.030 16.892 9.460 1.00 38.55 O ANISOU 4589 OE1 GLU C 366 4337 5492 4818 323 242 33 O ATOM 4590 OE2 GLU C 366 -8.809 16.567 10.706 1.00 39.23 O ANISOU 4590 OE2 GLU C 366 4293 5742 4872 318 323 54 O ATOM 4591 N GLN C 367 -2.434 16.853 12.608 1.00 13.61 N ANISOU 4591 N GLN C 367 1501 2128 1541 208 239 -20 N ATOM 4592 CA GLN C 367 -1.170 16.162 12.851 1.00 11.01 C ANISOU 4592 CA GLN C 367 1219 1764 1201 155 200 -5 C ATOM 4593 C GLN C 367 -0.579 16.546 14.202 1.00 12.69 C ANISOU 4593 C GLN C 367 1481 1992 1348 143 221 -23 C ATOM 4594 O GLN C 367 -0.108 15.691 14.951 1.00 14.01 O ANISOU 4594 O GLN C 367 1660 2179 1484 98 209 9 O ATOM 4595 CB GLN C 367 -0.157 16.479 11.751 1.00 12.07 C ANISOU 4595 CB GLN C 367 1384 1832 1367 163 154 -19 C ATOM 4596 CG GLN C 367 -0.521 15.950 10.373 1.00 10.09 C ANISOU 4596 CG GLN C 367 1095 1567 1171 165 123 -1 C ATOM 4597 CD GLN C 367 0.458 16.407 9.310 1.00 17.03 C ANISOU 4597 CD GLN C 367 2007 2392 2071 178 88 -17 C ATOM 4598 OE1 GLN C 367 0.885 17.564 9.301 1.00 14.35 O ANISOU 4598 OE1 GLN C 367 1708 2025 1720 204 98 -46 O ATOM 4599 NE2 GLN C 367 0.825 15.499 8.407 1.00 9.25 N ANISOU 4599 NE2 GLN C 367 1012 1389 1116 155 51 1 N ATOM 4600 N LYS C 368 -0.592 17.841 14.498 1.00 13.85 N ANISOU 4600 N LYS C 368 1665 2128 1470 184 252 -75 N ATOM 4601 CA LYS C 368 0.055 18.363 15.694 1.00 16.82 C ANISOU 4601 CA LYS C 368 2100 2514 1777 166 268 -108 C ATOM 4602 C LYS C 368 -0.606 17.848 16.968 1.00 12.62 C ANISOU 4602 C LYS C 368 1549 2059 1186 149 310 -90 C ATOM 4603 O LYS C 368 0.066 17.630 17.975 1.00 12.85 O ANISOU 4603 O LYS C 368 1614 2116 1153 109 303 -88 O ATOM 4604 CB LYS C 368 0.049 19.894 15.679 1.00 12.31 C ANISOU 4604 CB LYS C 368 1585 1899 1194 213 298 -174 C ATOM 4605 CG LYS C 368 0.995 20.527 16.692 1.00 14.59 C ANISOU 4605 CG LYS C 368 1949 2181 1412 177 299 -221 C ATOM 4606 CD LYS C 368 1.069 22.037 16.516 1.00 17.41 C ANISOU 4606 CD LYS C 368 2380 2468 1767 213 326 -290 C ATOM 4607 CE LYS C 368 2.086 22.659 17.466 1.00 19.39 C ANISOU 4607 CE LYS C 368 2711 2711 1945 156 320 -344 C ATOM 4608 NZ LYS C 368 1.786 22.354 18.897 1.00 14.18 N ANISOU 4608 NZ LYS C 368 2055 2131 1203 139 352 -356 N ATOM 4609 N GLU C 369 -1.922 17.659 16.917 1.00 12.99 N ANISOU 4609 N GLU C 369 1535 2152 1249 175 353 -75 N ATOM 4610 CA GLU C 369 -2.677 17.168 18.067 1.00 13.72 C ANISOU 4610 CA GLU C 369 1600 2329 1284 155 403 -53 C ATOM 4611 C GLU C 369 -2.865 15.656 17.985 1.00 16.59 C ANISOU 4611 C GLU C 369 1919 2718 1668 91 379 23 C ATOM 4612 O GLU C 369 -3.542 15.058 18.822 1.00 17.48 O ANISOU 4612 O GLU C 369 2003 2899 1740 58 418 58 O ATOM 4613 CB GLU C 369 -4.034 17.871 18.158 1.00 15.31 C ANISOU 4613 CB GLU C 369 1752 2581 1484 221 474 -81 C ATOM 4614 CG GLU C 369 -3.939 19.367 18.430 1.00 17.59 C ANISOU 4614 CG GLU C 369 2103 2836 1745 292 511 -160 C ATOM 4615 CD GLU C 369 -3.474 19.676 19.840 1.00 24.29 C ANISOU 4615 CD GLU C 369 3018 3713 2497 268 542 -197 C ATOM 4616 OE1 GLU C 369 -3.029 20.818 20.085 1.00 27.58 O ANISOU 4616 OE1 GLU C 369 3515 4080 2886 299 557 -268 O ATOM 4617 OE2 GLU C 369 -3.557 18.778 20.707 1.00 22.84 O ANISOU 4617 OE2 GLU C 369 2815 3601 2263 212 552 -156 O ATOM 4618 N ASN C 370 -2.266 15.053 16.961 1.00 14.93 N ANISOU 4618 N ASN C 370 1710 2446 1518 71 318 49 N ATOM 4619 CA ASN C 370 -2.246 13.602 16.799 1.00 17.19 C ANISOU 4619 CA ASN C 370 1978 2725 1827 10 289 115 C ATOM 4620 C ASN C 370 -3.626 13.001 16.528 1.00 18.11 C ANISOU 4620 C ASN C 370 2020 2890 1971 -15 319 146 C ATOM 4621 O ASN C 370 -3.877 11.842 16.855 1.00 22.81 O ANISOU 4621 O ASN C 370 2608 3498 2562 -81 319 203 O ATOM 4622 CB ASN C 370 -1.631 12.947 18.040 1.00 20.40 C ANISOU 4622 CB ASN C 370 2429 3154 2167 -32 287 156 C ATOM 4623 CG ASN C 370 -1.076 11.564 17.757 1.00 25.14 C ANISOU 4623 CG ASN C 370 3047 3707 2796 -77 239 221 C ATOM 4624 OD1 ASN C 370 -0.663 11.265 16.638 1.00 25.44 O ANISOU 4624 OD1 ASN C 370 3087 3681 2899 -69 196 218 O ATOM 4625 ND2 ASN C 370 -1.064 10.713 18.774 1.00 29.11 N ANISOU 4625 ND2 ASN C 370 3573 4239 3250 -120 249 280 N ATOM 4626 N THR C 371 -4.517 13.785 15.928 1.00 16.09 N ANISOU 4626 N THR C 371 1709 2663 1742 34 344 112 N ATOM 4627 CA THR C 371 -5.844 13.286 15.569 1.00 18.81 C ANISOU 4627 CA THR C 371 1963 3072 2113 8 367 138 C ATOM 4628 C THR C 371 -5.824 12.655 14.181 1.00 22.09 C ANISOU 4628 C THR C 371 2359 3438 2597 -19 310 151 C ATOM 4629 O THR C 371 -6.648 11.800 13.863 1.00 22.71 O ANISOU 4629 O THR C 371 2380 3553 2698 -80 309 183 O ATOM 4630 CB THR C 371 -6.907 14.402 15.593 1.00 18.41 C ANISOU 4630 CB THR C 371 1847 3094 2053 85 422 100 C ATOM 4631 OG1 THR C 371 -6.681 15.309 14.508 1.00 17.73 O ANISOU 4631 OG1 THR C 371 1769 2955 2011 159 392 62 O ATOM 4632 CG2 THR C 371 -6.858 15.162 16.913 1.00 19.95 C ANISOU 4632 CG2 THR C 371 2077 3328 2176 123 483 70 C ATOM 4633 N LYS C 372 -4.876 13.094 13.361 1.00 20.23 N ANISOU 4633 N LYS C 372 2172 3125 2391 20 264 122 N ATOM 4634 CA LYS C 372 -4.713 12.584 12.005 1.00 23.40 C ANISOU 4634 CA LYS C 372 2567 3478 2847 2 209 126 C ATOM 4635 C LYS C 372 -3.237 12.524 11.638 1.00 21.65 C ANISOU 4635 C LYS C 372 2423 3166 2635 12 164 115 C ATOM 4636 O LYS C 372 -2.453 13.372 12.058 1.00 22.15 O ANISOU 4636 O LYS C 372 2532 3211 2674 53 169 89 O ATOM 4637 CB LYS C 372 -5.468 13.460 11.004 1.00 29.00 C ANISOU 4637 CB LYS C 372 3217 4218 3584 61 207 98 C ATOM 4638 CG LYS C 372 -6.872 12.984 10.682 1.00 33.31 C ANISOU 4638 CG LYS C 372 3662 4850 4144 27 219 119 C ATOM 4639 CD LYS C 372 -6.980 12.627 9.210 1.00 36.58 C ANISOU 4639 CD LYS C 372 4054 5245 4601 9 162 116 C ATOM 4640 CE LYS C 372 -6.490 13.775 8.338 1.00 37.14 C ANISOU 4640 CE LYS C 372 4151 5277 4684 99 140 85 C ATOM 4641 NZ LYS C 372 -6.400 13.400 6.901 1.00 34.21 N ANISOU 4641 NZ LYS C 372 3774 4883 4343 80 82 81 N ATOM 4642 N GLU C 373 -2.858 11.519 10.855 1.00 16.82 N ANISOU 4642 N GLU C 373 1829 2504 2058 -29 121 131 N ATOM 4643 CA GLU C 373 -1.472 11.378 10.428 1.00 16.80 C ANISOU 4643 CA GLU C 373 1889 2429 2067 -13 81 123 C ATOM 4644 C GLU C 373 -1.190 12.179 9.161 1.00 12.77 C ANISOU 4644 C GLU C 373 1374 1896 1582 33 56 86 C ATOM 4645 O GLU C 373 -0.146 12.819 9.034 1.00 14.70 O ANISOU 4645 O GLU C 373 1656 2109 1819 66 44 65 O ATOM 4646 CB GLU C 373 -1.129 9.904 10.198 1.00 22.17 C ANISOU 4646 CB GLU C 373 2600 3056 2768 -65 53 155 C ATOM 4647 CG GLU C 373 -0.972 9.110 11.481 1.00 29.04 C ANISOU 4647 CG GLU C 373 3501 3925 3606 -101 69 203 C ATOM 4648 CD GLU C 373 -0.007 9.771 12.447 1.00 34.38 C ANISOU 4648 CD GLU C 373 4210 4617 4238 -63 74 201 C ATOM 4649 OE1 GLU C 373 1.181 9.932 12.091 1.00 31.83 O ANISOU 4649 OE1 GLU C 373 3917 4256 3919 -28 42 187 O ATOM 4650 OE2 GLU C 373 -0.440 10.139 13.559 1.00 41.16 O ANISOU 4650 OE2 GLU C 373 5059 5531 5048 -70 111 211 O ATOM 4651 N GLN C 374 -2.132 12.139 8.229 1.00 16.28 N ANISOU 4651 N GLN C 374 1769 2364 2052 28 49 80 N ATOM 4652 CA GLN C 374 -1.910 12.695 6.904 1.00 19.20 C ANISOU 4652 CA GLN C 374 2138 2714 2443 64 20 55 C ATOM 4653 C GLN C 374 -2.434 14.117 6.757 1.00 16.54 C ANISOU 4653 C GLN C 374 1776 2410 2098 130 40 38 C ATOM 4654 O GLN C 374 -3.547 14.434 7.177 1.00 17.56 O ANISOU 4654 O GLN C 374 1851 2600 2219 145 70 44 O ATOM 4655 CB GLN C 374 -2.557 11.796 5.852 1.00 27.09 C ANISOU 4655 CB GLN C 374 3106 3721 3467 20 -11 58 C ATOM 4656 CG GLN C 374 -2.074 10.361 5.902 1.00 39.52 C ANISOU 4656 CG GLN C 374 4722 5241 5052 -42 -28 71 C ATOM 4657 CD GLN C 374 -0.631 10.218 5.467 1.00 49.11 C ANISOU 4657 CD GLN C 374 6000 6387 6272 -15 -51 57 C ATOM 4658 OE1 GLN C 374 -0.139 10.994 4.648 1.00 51.69 O ANISOU 4658 OE1 GLN C 374 6331 6709 6598 28 -64 33 O ATOM 4659 NE2 GLN C 374 0.059 9.226 6.019 1.00 53.10 N ANISOU 4659 NE2 GLN C 374 6553 6842 6779 -36 -54 76 N ATOM 4660 N ALA C 375 -1.607 14.969 6.163 1.00 14.15 N ANISOU 4660 N ALA C 375 1515 2066 1796 170 27 18 N ATOM 4661 CA ALA C 375 -2.040 16.274 5.689 1.00 15.56 C ANISOU 4661 CA ALA C 375 1686 2253 1974 237 38 7 C ATOM 4662 C ALA C 375 -1.629 16.377 4.224 1.00 18.46 C ANISOU 4662 C ALA C 375 2066 2594 2355 246 -1 5 C ATOM 4663 O ALA C 375 -0.948 15.490 3.709 1.00 19.37 O ANISOU 4663 O ALA C 375 2197 2686 2477 203 -30 4 O ATOM 4664 CB ALA C 375 -1.428 17.389 6.514 1.00 9.79 C ANISOU 4664 CB ALA C 375 1012 1488 1221 271 70 -13 C ATOM 4665 N VAL C 376 -2.035 17.443 3.546 1.00 18.07 N ANISOU 4665 N VAL C 376 2013 2549 2306 305 0 7 N ATOM 4666 CA VAL C 376 -1.696 17.574 2.134 1.00 17.41 C ANISOU 4666 CA VAL C 376 1942 2449 2225 313 -36 11 C ATOM 4667 C VAL C 376 -0.970 18.878 1.817 1.00 17.17 C ANISOU 4667 C VAL C 376 1976 2362 2185 356 -26 8 C ATOM 4668 O VAL C 376 -1.152 19.894 2.489 1.00 18.48 O ANISOU 4668 O VAL C 376 2169 2506 2346 401 7 4 O ATOM 4669 CB VAL C 376 -2.950 17.464 1.242 1.00 21.74 C ANISOU 4669 CB VAL C 376 2419 3065 2776 334 -60 29 C ATOM 4670 CG1 VAL C 376 -3.562 16.073 1.360 1.00 23.75 C ANISOU 4670 CG1 VAL C 376 2618 3369 3039 265 -77 28 C ATOM 4671 CG2 VAL C 376 -3.965 18.534 1.605 1.00 23.74 C ANISOU 4671 CG2 VAL C 376 2640 3352 3027 415 -32 42 C ATOM 4672 N ILE C 377 -0.136 18.825 0.785 1.00 18.25 N ANISOU 4672 N ILE C 377 2143 2474 2316 338 -52 10 N ATOM 4673 CA ILE C 377 0.607 19.983 0.316 1.00 16.40 C ANISOU 4673 CA ILE C 377 1972 2188 2071 361 -44 14 C ATOM 4674 C ILE C 377 0.527 20.029 -1.210 1.00 12.67 C ANISOU 4674 C ILE C 377 1496 1732 1588 373 -76 35 C ATOM 4675 O ILE C 377 0.720 19.010 -1.871 1.00 11.65 O ANISOU 4675 O ILE C 377 1340 1631 1453 335 -104 28 O ATOM 4676 CB ILE C 377 2.084 19.936 0.783 1.00 17.40 C ANISOU 4676 CB ILE C 377 2147 2273 2190 309 -35 -5 C ATOM 4677 CG1 ILE C 377 2.825 21.218 0.395 1.00 17.08 C ANISOU 4677 CG1 ILE C 377 2175 2178 2137 315 -22 -1 C ATOM 4678 CG2 ILE C 377 2.791 18.702 0.238 1.00 19.77 C ANISOU 4678 CG2 ILE C 377 2427 2595 2491 263 -62 -12 C ATOM 4679 CD1 ILE C 377 2.450 22.414 1.240 1.00 16.36 C ANISOU 4679 CD1 ILE C 377 2130 2040 2044 351 13 -8 C ATOM 4680 N PRO C 378 0.202 21.202 -1.772 1.00 9.89 N ANISOU 4680 N PRO C 378 1173 1359 1226 429 -72 61 N ATOM 4681 CA PRO C 378 0.146 21.352 -3.230 1.00 13.84 C ANISOU 4681 CA PRO C 378 1675 1879 1704 443 -103 89 C ATOM 4682 C PRO C 378 1.534 21.305 -3.858 1.00 14.05 C ANISOU 4682 C PRO C 378 1752 1875 1712 390 -104 83 C ATOM 4683 O PRO C 378 2.510 21.654 -3.198 1.00 11.00 O ANISOU 4683 O PRO C 378 1409 1439 1330 359 -77 67 O ATOM 4684 CB PRO C 378 -0.492 22.734 -3.421 1.00 17.13 C ANISOU 4684 CB PRO C 378 2126 2266 2118 527 -90 127 C ATOM 4685 CG PRO C 378 -1.183 23.025 -2.130 1.00 16.32 C ANISOU 4685 CG PRO C 378 2008 2155 2039 567 -57 111 C ATOM 4686 CD PRO C 378 -0.330 22.385 -1.078 1.00 15.08 C ANISOU 4686 CD PRO C 378 1861 1978 1890 494 -38 69 C ATOM 4687 N LEU C 379 1.619 20.879 -5.115 1.00 17.43 N ANISOU 4687 N LEU C 379 2167 2342 2113 379 -133 93 N ATOM 4688 CA LEU C 379 2.897 20.839 -5.816 1.00 15.12 C ANISOU 4688 CA LEU C 379 1914 2036 1796 334 -128 88 C ATOM 4689 C LEU C 379 3.010 21.974 -6.832 1.00 15.66 C ANISOU 4689 C LEU C 379 2033 2086 1831 360 -127 135 C ATOM 4690 O LEU C 379 3.893 21.968 -7.689 1.00 17.05 O ANISOU 4690 O LEU C 379 2234 2271 1974 325 -124 140 O ATOM 4691 CB LEU C 379 3.089 19.487 -6.506 1.00 14.20 C ANISOU 4691 CB LEU C 379 1759 1971 1664 299 -153 59 C ATOM 4692 CG LEU C 379 3.171 18.285 -5.564 1.00 16.59 C ANISOU 4692 CG LEU C 379 2030 2276 1999 268 -151 20 C ATOM 4693 CD1 LEU C 379 3.375 16.998 -6.348 1.00 17.64 C ANISOU 4693 CD1 LEU C 379 2146 2441 2115 238 -173 -12 C ATOM 4694 CD2 LEU C 379 4.278 18.475 -4.538 1.00 14.65 C ANISOU 4694 CD2 LEU C 379 1808 1988 1770 246 -120 8 C ATOM 4695 N THR C 380 2.104 22.943 -6.731 1.00 13.77 N ANISOU 4695 N THR C 380 1811 1823 1597 424 -126 171 N ATOM 4696 CA THR C 380 2.172 24.157 -7.539 1.00 15.14 C ANISOU 4696 CA THR C 380 2051 1959 1744 458 -121 226 C ATOM 4697 C THR C 380 2.246 25.380 -6.637 1.00 14.32 C ANISOU 4697 C THR C 380 2018 1758 1666 485 -82 236 C ATOM 4698 O THR C 380 2.095 25.272 -5.420 1.00 13.37 O ANISOU 4698 O THR C 380 1885 1616 1579 486 -63 199 O ATOM 4699 CB THR C 380 0.946 24.316 -8.465 1.00 16.13 C ANISOU 4699 CB THR C 380 2144 2140 1843 531 -160 272 C ATOM 4700 OG1 THR C 380 -0.226 24.541 -7.670 1.00 18.36 O ANISOU 4700 OG1 THR C 380 2388 2428 2159 603 -160 276 O ATOM 4701 CG2 THR C 380 0.746 23.080 -9.331 1.00 14.95 C ANISOU 4701 CG2 THR C 380 1928 2090 1663 497 -203 252 C ATOM 4702 N ASP C 381 2.469 26.545 -7.234 1.00 16.00 N ANISOU 4702 N ASP C 381 2313 1908 1858 505 -69 286 N ATOM 4703 CA ASP C 381 2.324 27.796 -6.503 1.00 18.27 C ANISOU 4703 CA ASP C 381 2684 2088 2168 545 -33 298 C ATOM 4704 C ASP C 381 0.861 28.229 -6.537 1.00 17.04 C ANISOU 4704 C ASP C 381 2510 1941 2024 670 -46 334 C ATOM 4705 O ASP C 381 0.008 27.506 -7.055 1.00 15.36 O ANISOU 4705 O ASP C 381 2208 1828 1800 709 -85 346 O ATOM 4706 CB ASP C 381 3.237 28.886 -7.077 1.00 21.77 C ANISOU 4706 CB ASP C 381 3239 2445 2588 504 -9 338 C ATOM 4707 CG ASP C 381 3.019 29.127 -8.564 1.00 23.78 C ANISOU 4707 CG ASP C 381 3509 2730 2797 535 -35 411 C ATOM 4708 OD1 ASP C 381 1.935 28.792 -9.087 1.00 22.40 O ANISOU 4708 OD1 ASP C 381 3274 2625 2611 616 -73 438 O ATOM 4709 OD2 ASP C 381 3.941 29.665 -9.210 1.00 23.57 O ANISOU 4709 OD2 ASP C 381 3552 2664 2739 473 -19 443 O ATOM 4710 N SER C 382 0.573 29.410 -6.000 1.00 18.12 N ANISOU 4710 N SER C 382 2731 1976 2179 734 -12 349 N ATOM 4711 CA SER C 382 -0.804 29.887 -5.921 1.00 17.95 C ANISOU 4711 CA SER C 382 2687 1962 2170 871 -16 381 C ATOM 4712 C SER C 382 -1.394 30.165 -7.303 1.00 21.57 C ANISOU 4712 C SER C 382 3138 2464 2594 943 -56 464 C ATOM 4713 O SER C 382 -2.612 30.243 -7.459 1.00 22.90 O ANISOU 4713 O SER C 382 3246 2691 2765 1055 -78 496 O ATOM 4714 CB SER C 382 -0.886 31.144 -5.049 1.00 22.62 C ANISOU 4714 CB SER C 382 3390 2417 2787 930 38 374 C ATOM 4715 OG SER C 382 -0.073 32.185 -5.562 1.00 23.61 O ANISOU 4715 OG SER C 382 3652 2421 2897 898 57 412 O ATOM 4716 N GLU C 383 -0.528 30.315 -8.300 1.00 18.04 N ANISOU 4716 N GLU C 383 2746 1999 2108 877 -67 499 N ATOM 4717 CA GLU C 383 -0.971 30.544 -9.672 1.00 21.82 C ANISOU 4717 CA GLU C 383 3224 2527 2540 932 -108 581 C ATOM 4718 C GLU C 383 -1.097 29.230 -10.442 1.00 21.30 C ANISOU 4718 C GLU C 383 3042 2613 2438 882 -161 565 C ATOM 4719 O GLU C 383 -1.323 29.227 -11.652 1.00 21.20 O ANISOU 4719 O GLU C 383 3021 2663 2372 902 -201 622 O ATOM 4720 CB GLU C 383 -0.008 31.490 -10.392 1.00 28.95 C ANISOU 4720 CB GLU C 383 4259 3330 3411 889 -87 636 C ATOM 4721 CG GLU C 383 0.024 32.893 -9.805 1.00 40.15 C ANISOU 4721 CG GLU C 383 5814 4581 4859 942 -38 662 C ATOM 4722 CD GLU C 383 1.199 33.713 -10.306 1.00 49.45 C ANISOU 4722 CD GLU C 383 7128 5651 6011 853 -7 700 C ATOM 4723 OE1 GLU C 383 2.263 33.692 -9.651 1.00 50.15 O ANISOU 4723 OE1 GLU C 383 7253 5687 6116 734 29 642 O ATOM 4724 OE2 GLU C 383 1.057 34.382 -11.352 1.00 55.54 O ANISOU 4724 OE2 GLU C 383 7965 6395 6742 897 -20 792 O ATOM 4725 N TYR C 384 -0.939 28.120 -9.728 1.00 17.83 N ANISOU 4725 N TYR C 384 2524 2227 2024 815 -161 487 N ATOM 4726 CA TYR C 384 -1.106 26.782 -10.294 1.00 16.77 C ANISOU 4726 CA TYR C 384 2288 2220 1864 763 -206 456 C ATOM 4727 C TYR C 384 -0.012 26.440 -11.301 1.00 19.31 C ANISOU 4727 C TYR C 384 2644 2558 2135 676 -212 458 C ATOM 4728 O TYR C 384 -0.191 25.578 -12.163 1.00 22.09 O ANISOU 4728 O TYR C 384 2939 3010 2444 650 -253 449 O ATOM 4729 CB TYR C 384 -2.491 26.644 -10.933 1.00 21.61 C ANISOU 4729 CB TYR C 384 2818 2939 2452 849 -260 498 C ATOM 4730 CG TYR C 384 -3.604 26.998 -9.978 1.00 22.54 C ANISOU 4730 CG TYR C 384 2889 3058 2617 946 -249 500 C ATOM 4731 CD1 TYR C 384 -3.797 26.271 -8.811 1.00 23.75 C ANISOU 4731 CD1 TYR C 384 2981 3228 2816 912 -228 433 C ATOM 4732 CD2 TYR C 384 -4.452 28.067 -10.232 1.00 22.12 C ANISOU 4732 CD2 TYR C 384 2855 2991 2558 1077 -255 572 C ATOM 4733 CE1 TYR C 384 -4.805 26.595 -7.925 1.00 24.22 C ANISOU 4733 CE1 TYR C 384 2993 3298 2910 999 -210 433 C ATOM 4734 CE2 TYR C 384 -5.467 28.397 -9.353 1.00 22.53 C ANISOU 4734 CE2 TYR C 384 2858 3046 2657 1147 -231 556 C ATOM 4735 CZ TYR C 384 -5.637 27.658 -8.200 1.00 26.05 C ANISOU 4735 CZ TYR C 384 3238 3520 3140 1123 -210 493 C ATOM 4736 OH TYR C 384 -6.643 27.978 -7.318 1.00 29.75 O ANISOU 4736 OH TYR C 384 3657 4001 3645 1185 -181 476 O ATOM 4737 N LYS C 385 1.123 27.119 -11.184 1.00 16.19 N ANISOU 4737 N LYS C 385 2341 2070 1740 626 -168 465 N ATOM 4738 CA LYS C 385 2.313 26.734 -11.926 1.00 19.70 C ANISOU 4738 CA LYS C 385 2806 2537 2143 533 -159 454 C ATOM 4739 C LYS C 385 3.104 25.738 -11.089 1.00 18.99 C ANISOU 4739 C LYS C 385 2671 2457 2086 454 -140 371 C ATOM 4740 O LYS C 385 3.311 25.956 -9.894 1.00 16.98 O ANISOU 4740 O LYS C 385 2431 2140 1881 444 -111 340 O ATOM 4741 CB LYS C 385 3.169 27.953 -12.267 1.00 26.10 C ANISOU 4741 CB LYS C 385 3729 3255 2932 507 -121 509 C ATOM 4742 CG LYS C 385 4.409 27.636 -13.092 1.00 28.69 C ANISOU 4742 CG LYS C 385 4071 3620 3209 411 -105 505 C ATOM 4743 CD LYS C 385 5.223 28.893 -13.364 1.00 35.01 C ANISOU 4743 CD LYS C 385 4984 4328 3990 371 -64 565 C ATOM 4744 CE LYS C 385 6.329 28.637 -14.379 1.00 40.19 C ANISOU 4744 CE LYS C 385 5645 5046 4581 284 -46 576 C ATOM 4745 NZ LYS C 385 7.315 27.628 -13.902 1.00 42.13 N ANISOU 4745 NZ LYS C 385 5821 5344 4844 205 -27 493 N ATOM 4746 N LEU C 386 3.527 24.639 -11.708 1.00 18.29 N ANISOU 4746 N LEU C 386 2535 2449 1967 404 -156 336 N ATOM 4747 CA LEU C 386 4.303 23.621 -11.004 1.00 18.28 C ANISOU 4747 CA LEU C 386 2492 2458 1994 343 -139 264 C ATOM 4748 C LEU C 386 5.495 24.245 -10.288 1.00 17.64 C ANISOU 4748 C LEU C 386 2461 2308 1935 290 -92 257 C ATOM 4749 O LEU C 386 6.186 25.096 -10.848 1.00 18.03 O ANISOU 4749 O LEU C 386 2571 2327 1952 260 -69 297 O ATOM 4750 CB LEU C 386 4.779 22.538 -11.974 1.00 18.09 C ANISOU 4750 CB LEU C 386 2435 2515 1923 304 -153 232 C ATOM 4751 CG LEU C 386 3.726 21.518 -12.411 1.00 24.54 C ANISOU 4751 CG LEU C 386 3192 3406 2727 326 -202 207 C ATOM 4752 CD1 LEU C 386 4.222 20.707 -13.597 1.00 25.97 C ANISOU 4752 CD1 LEU C 386 3368 3656 2845 291 -211 180 C ATOM 4753 CD2 LEU C 386 3.365 20.604 -11.248 1.00 25.27 C ANISOU 4753 CD2 LEU C 386 3233 3489 2880 319 -206 153 C ATOM 4754 N LEU C 387 5.716 23.831 -9.042 1.00 15.96 N ANISOU 4754 N LEU C 387 2222 2073 1770 271 -79 209 N ATOM 4755 CA LEU C 387 6.837 24.331 -8.257 1.00 17.59 C ANISOU 4755 CA LEU C 387 2463 2228 1993 212 -42 195 C ATOM 4756 C LEU C 387 8.155 24.018 -8.955 1.00 16.79 C ANISOU 4756 C LEU C 387 2352 2173 1855 145 -24 188 C ATOM 4757 O LEU C 387 8.250 23.040 -9.695 1.00 18.55 O ANISOU 4757 O LEU C 387 2529 2465 2053 148 -38 170 O ATOM 4758 CB LEU C 387 6.826 23.725 -6.850 1.00 15.63 C ANISOU 4758 CB LEU C 387 2175 1972 1790 205 -39 144 C ATOM 4759 CG LEU C 387 5.714 24.185 -5.901 1.00 17.35 C ANISOU 4759 CG LEU C 387 2405 2144 2043 261 -40 144 C ATOM 4760 CD1 LEU C 387 5.714 23.363 -4.617 1.00 16.36 C ANISOU 4760 CD1 LEU C 387 2233 2033 1951 248 -39 95 C ATOM 4761 CD2 LEU C 387 5.861 25.667 -5.587 1.00 16.58 C ANISOU 4761 CD2 LEU C 387 2397 1954 1947 261 -11 169 C ATOM 4762 N PRO C 388 9.171 24.862 -8.734 1.00 18.42 N ANISOU 4762 N PRO C 388 2602 2342 2055 81 9 201 N ATOM 4763 CA PRO C 388 10.502 24.625 -9.300 1.00 19.74 C ANISOU 4763 CA PRO C 388 2746 2566 2187 13 33 196 C ATOM 4764 C PRO C 388 11.103 23.310 -8.820 1.00 16.06 C ANISOU 4764 C PRO C 388 2197 2167 1737 6 29 139 C ATOM 4765 O PRO C 388 10.965 22.958 -7.649 1.00 14.42 O ANISOU 4765 O PRO C 388 1966 1941 1572 15 20 106 O ATOM 4766 CB PRO C 388 11.317 25.817 -8.788 1.00 20.57 C ANISOU 4766 CB PRO C 388 2909 2611 2295 -64 65 215 C ATOM 4767 CG PRO C 388 10.301 26.881 -8.527 1.00 22.84 C ANISOU 4767 CG PRO C 388 3281 2795 2601 -21 61 248 C ATOM 4768 CD PRO C 388 9.095 26.149 -8.022 1.00 19.51 C ANISOU 4768 CD PRO C 388 2818 2382 2214 68 29 222 C ATOM 4769 N LEU C 389 11.752 22.592 -9.729 1.00 13.08 N ANISOU 4769 N LEU C 389 1780 1867 1323 -2 38 128 N ATOM 4770 CA LEU C 389 12.481 21.380 -9.380 1.00 17.05 C ANISOU 4770 CA LEU C 389 2211 2429 1837 1 41 78 C ATOM 4771 C LEU C 389 13.971 21.706 -9.329 1.00 16.28 C ANISOU 4771 C LEU C 389 2085 2380 1720 -67 77 80 C ATOM 4772 O LEU C 389 14.565 22.077 -10.341 1.00 17.96 O ANISOU 4772 O LEU C 389 2304 2637 1884 -101 105 105 O ATOM 4773 CB LEU C 389 12.195 20.269 -10.392 1.00 17.52 C ANISOU 4773 CB LEU C 389 2245 2542 1868 46 30 53 C ATOM 4774 CG LEU C 389 12.641 18.845 -10.060 1.00 21.79 C ANISOU 4774 CG LEU C 389 2730 3120 2428 76 29 -2 C ATOM 4775 CD1 LEU C 389 11.931 18.335 -8.816 1.00 22.30 C ANISOU 4775 CD1 LEU C 389 2787 3135 2552 102 0 -21 C ATOM 4776 CD2 LEU C 389 12.376 17.926 -11.243 1.00 22.99 C ANISOU 4776 CD2 LEU C 389 2881 3314 2541 110 24 -31 C ATOM 4777 N HIS C 390 14.571 21.571 -8.152 1.00 11.89 N ANISOU 4777 N HIS C 390 1493 1828 1197 -91 77 58 N ATOM 4778 CA HIS C 390 15.948 22.019 -7.942 1.00 14.66 C ANISOU 4778 CA HIS C 390 1807 2232 1530 -168 106 63 C ATOM 4779 C HIS C 390 16.999 21.052 -8.484 1.00 15.82 C ANISOU 4779 C HIS C 390 1870 2489 1652 -152 127 41 C ATOM 4780 O HIS C 390 16.877 19.837 -8.326 1.00 14.42 O ANISOU 4780 O HIS C 390 1653 2333 1493 -81 113 7 O ATOM 4781 CB HIS C 390 16.190 22.261 -6.451 1.00 12.10 C ANISOU 4781 CB HIS C 390 1472 1884 1241 -201 92 46 C ATOM 4782 CG HIS C 390 15.293 23.305 -5.866 1.00 13.31 C ANISOU 4782 CG HIS C 390 1712 1930 1414 -217 82 60 C ATOM 4783 ND1 HIS C 390 15.691 24.612 -5.686 1.00 12.32 N ANISOU 4783 ND1 HIS C 390 1644 1760 1276 -304 100 81 N ATOM 4784 CD2 HIS C 390 14.008 23.241 -5.445 1.00 13.70 C ANISOU 4784 CD2 HIS C 390 1803 1908 1494 -154 59 55 C ATOM 4785 CE1 HIS C 390 14.693 25.306 -5.170 1.00 13.39 C ANISOU 4785 CE1 HIS C 390 1860 1794 1435 -283 91 85 C ATOM 4786 NE2 HIS C 390 13.661 24.498 -5.013 1.00 14.74 N ANISOU 4786 NE2 HIS C 390 2015 1955 1631 -190 67 71 N ATOM 4787 N PHE C 391 18.023 21.615 -9.125 1.00 17.85 N ANISOU 4787 N PHE C 391 2104 2812 1866 -219 165 63 N ATOM 4788 CA PHE C 391 19.173 20.863 -9.625 1.00 18.75 C ANISOU 4788 CA PHE C 391 2126 3047 1950 -209 196 45 C ATOM 4789 C PHE C 391 18.761 19.637 -10.437 1.00 18.02 C ANISOU 4789 C PHE C 391 2025 2975 1846 -109 196 12 C ATOM 4790 O PHE C 391 19.339 18.557 -10.295 1.00 17.38 O ANISOU 4790 O PHE C 391 1877 2953 1773 -50 203 -24 O ATOM 4791 CB PHE C 391 20.070 20.447 -8.457 1.00 13.68 C ANISOU 4791 CB PHE C 391 1400 2462 1337 -216 187 23 C ATOM 4792 CG PHE C 391 20.497 21.596 -7.589 1.00 14.96 C ANISOU 4792 CG PHE C 391 1571 2608 1504 -325 182 44 C ATOM 4793 CD1 PHE C 391 21.491 22.466 -8.008 1.00 16.17 C ANISOU 4793 CD1 PHE C 391 1699 2828 1617 -432 218 71 C ATOM 4794 CD2 PHE C 391 19.902 21.809 -6.356 1.00 15.18 C ANISOU 4794 CD2 PHE C 391 1637 2557 1572 -328 144 33 C ATOM 4795 CE1 PHE C 391 21.885 23.530 -7.214 1.00 17.80 C ANISOU 4795 CE1 PHE C 391 1925 3013 1826 -547 213 83 C ATOM 4796 CE2 PHE C 391 20.289 22.870 -5.556 1.00 15.15 C ANISOU 4796 CE2 PHE C 391 1653 2535 1567 -432 141 41 C ATOM 4797 CZ PHE C 391 21.284 23.733 -5.987 1.00 19.17 C ANISOU 4797 CZ PHE C 391 2144 3101 2039 -546 173 64 C ATOM 4798 N ALA C 392 17.767 19.823 -11.298 1.00 16.15 N ANISOU 4798 N ALA C 392 1861 2689 1588 -91 187 25 N ATOM 4799 CA ALA C 392 17.119 18.714 -11.984 1.00 20.29 C ANISOU 4799 CA ALA C 392 2395 3214 2102 -9 175 -13 C ATOM 4800 C ALA C 392 17.954 18.154 -13.128 1.00 20.98 C ANISOU 4800 C ALA C 392 2443 3400 2127 11 221 -34 C ATOM 4801 O ALA C 392 17.683 17.058 -13.614 1.00 23.79 O ANISOU 4801 O ALA C 392 2800 3765 2474 80 218 -82 O ATOM 4802 CB ALA C 392 15.753 19.150 -12.500 1.00 20.26 C ANISOU 4802 CB ALA C 392 2470 3139 2087 0 144 10 C ATOM 4803 N VAL C 393 18.966 18.899 -13.557 1.00 20.95 N ANISOU 4803 N VAL C 393 2408 3473 2081 -54 266 -3 N ATOM 4804 CA VAL C 393 19.757 18.484 -14.710 1.00 24.60 C ANISOU 4804 CA VAL C 393 2831 4042 2473 -39 318 -19 C ATOM 4805 C VAL C 393 21.207 18.164 -14.362 1.00 22.22 C ANISOU 4805 C VAL C 393 2420 3851 2173 -42 361 -34 C ATOM 4806 O VAL C 393 21.965 19.035 -13.932 1.00 22.14 O ANISOU 4806 O VAL C 393 2369 3880 2163 -127 377 4 O ATOM 4807 CB VAL C 393 19.748 19.562 -15.812 1.00 28.13 C ANISOU 4807 CB VAL C 393 3326 4516 2848 -112 347 37 C ATOM 4808 CG1 VAL C 393 20.594 19.115 -16.996 1.00 27.97 C ANISOU 4808 CG1 VAL C 393 3261 4620 2746 -98 408 17 C ATOM 4809 CG2 VAL C 393 18.323 19.855 -16.254 1.00 29.99 C ANISOU 4809 CG2 VAL C 393 3660 4661 3074 -95 302 57 C ATOM 4810 N ASP C 394 21.578 16.901 -14.546 1.00 20.39 N ANISOU 4810 N ASP C 394 2141 3666 1939 54 378 -91 N ATOM 4811 CA ASP C 394 22.977 16.492 -14.535 1.00 21.40 C ANISOU 4811 CA ASP C 394 2157 3924 2051 78 429 -107 C ATOM 4812 C ASP C 394 23.451 16.394 -15.981 1.00 22.22 C ANISOU 4812 C ASP C 394 2249 4128 2066 86 494 -119 C ATOM 4813 O ASP C 394 23.039 15.491 -16.709 1.00 22.18 O ANISOU 4813 O ASP C 394 2285 4109 2034 168 502 -172 O ATOM 4814 CB ASP C 394 23.154 15.154 -13.805 1.00 21.59 C ANISOU 4814 CB ASP C 394 2139 3936 2128 195 413 -158 C ATOM 4815 CG ASP C 394 24.576 14.613 -13.893 1.00 23.85 C ANISOU 4815 CG ASP C 394 2303 4365 2393 249 467 -176 C ATOM 4816 OD1 ASP C 394 25.500 15.374 -14.248 1.00 23.01 O ANISOU 4816 OD1 ASP C 394 2123 4378 2241 175 512 -144 O ATOM 4817 OD2 ASP C 394 24.771 13.416 -13.595 1.00 26.23 O ANISOU 4817 OD2 ASP C 394 2581 4660 2724 368 467 -220 O ATOM 4818 N PRO C 395 24.316 17.332 -16.402 1.00 20.06 N ANISOU 4818 N PRO C 395 1925 3957 1741 -8 542 -73 N ATOM 4819 CA PRO C 395 24.819 17.361 -17.781 1.00 20.26 C ANISOU 4819 CA PRO C 395 1936 4092 1670 -14 612 -75 C ATOM 4820 C PRO C 395 25.538 16.069 -18.152 1.00 22.76 C ANISOU 4820 C PRO C 395 2188 4479 1979 108 648 -144 C ATOM 4821 O PRO C 395 25.632 15.730 -19.330 1.00 20.39 O ANISOU 4821 O PRO C 395 1917 4207 1621 139 683 -170 O ATOM 4822 CB PRO C 395 25.786 18.550 -17.778 1.00 23.96 C ANISOU 4822 CB PRO C 395 2344 4648 2112 -146 648 -8 C ATOM 4823 CG PRO C 395 26.180 18.716 -16.346 1.00 23.19 C ANISOU 4823 CG PRO C 395 2179 4543 2088 -175 614 2 C ATOM 4824 CD PRO C 395 24.951 18.363 -15.564 1.00 21.87 C ANISOU 4824 CD PRO C 395 2102 4212 1994 -119 537 -19 C ATOM 4825 N GLY C 396 26.034 15.356 -17.146 1.00 21.62 N ANISOU 4825 N GLY C 396 1973 4339 1904 178 631 -170 N ATOM 4826 CA GLY C 396 26.658 14.064 -17.360 1.00 25.20 C ANISOU 4826 CA GLY C 396 2388 4813 2372 308 650 -229 C ATOM 4827 C GLY C 396 25.677 13.033 -17.885 1.00 24.49 C ANISOU 4827 C GLY C 396 2401 4632 2275 405 641 -297 C ATOM 4828 O GLY C 396 26.078 12.025 -18.469 1.00 24.11 O ANISOU 4828 O GLY C 396 2355 4588 2216 499 669 -351 O ATOM 4829 N ALYS C 397 24.388 13.282 -17.674 0.40 24.82 N ANISOU 4829 N ALYS C 397 2527 4586 2317 378 601 -297 N ATOM 4830 N BLYS C 397 24.387 13.283 -17.668 0.60 24.68 N ANISOU 4830 N BLYS C 397 2509 4568 2299 378 600 -297 N ATOM 4831 CA ALYS C 397 23.346 12.387 -18.160 0.40 25.82 C ANISOU 4831 CA ALYS C 397 2761 4612 2437 444 576 -360 C ATOM 4832 CA BLYS C 397 23.336 12.395 -18.156 0.60 25.83 C ANISOU 4832 CA BLYS C 397 2763 4613 2439 443 575 -359 C ATOM 4833 C ALYS C 397 22.691 12.942 -19.424 0.40 26.20 C ANISOU 4833 C ALYS C 397 2887 4671 2397 382 583 -353 C ATOM 4834 C BLYS C 397 22.722 12.907 -19.454 0.60 26.25 C ANISOU 4834 C BLYS C 397 2892 4680 2401 385 586 -355 C ATOM 4835 O ALYS C 397 21.624 12.486 -19.838 0.40 25.21 O ANISOU 4835 O ALYS C 397 2857 4461 2260 399 546 -390 O ATOM 4836 O BLYS C 397 21.698 12.397 -19.909 0.60 25.17 O ANISOU 4836 O BLYS C 397 2849 4464 2250 408 552 -397 O ATOM 4837 CB ALYS C 397 22.299 12.143 -17.069 0.40 25.07 C ANISOU 4837 CB ALYS C 397 2726 4368 2433 447 494 -355 C ATOM 4838 CB BLYS C 397 22.239 12.221 -17.103 0.60 24.75 C ANISOU 4838 CB BLYS C 397 2690 4324 2389 440 492 -352 C ATOM 4839 CG ALYS C 397 22.858 11.450 -15.832 0.40 25.89 C ANISOU 4839 CG ALYS C 397 2767 4454 2616 520 481 -362 C ATOM 4840 CG BLYS C 397 22.706 11.594 -15.802 0.60 25.88 C ANISOU 4840 CG BLYS C 397 2775 4441 2616 504 473 -355 C ATOM 4841 CD ALYS C 397 21.761 11.114 -14.835 0.40 25.91 C ANISOU 4841 CD ALYS C 397 2839 4310 2697 523 407 -360 C ATOM 4842 CD BLYS C 397 21.516 11.092 -14.995 0.60 25.50 C ANISOU 4842 CD BLYS C 397 2808 4241 2639 519 402 -365 C ATOM 4843 CE ALYS C 397 22.301 10.304 -13.665 0.40 26.55 C ANISOU 4843 CE ALYS C 397 2868 4372 2847 606 394 -364 C ATOM 4844 CE BLYS C 397 20.399 12.121 -14.956 0.60 22.19 C ANISOU 4844 CE BLYS C 397 2452 3757 2222 416 352 -320 C ATOM 4845 NZ ALYS C 397 23.261 11.079 -12.832 0.40 26.72 N ANISOU 4845 NZ ALYS C 397 2781 4486 2885 562 397 -306 N ATOM 4846 NZ BLYS C 397 19.137 11.558 -14.394 0.60 20.34 N ANISOU 4846 NZ BLYS C 397 2294 3392 2042 431 291 -337 N ATOM 4847 N GLY C 398 23.342 13.928 -20.035 1.00 29.04 N ANISOU 4847 N GLY C 398 3208 5130 2697 301 626 -298 N ATOM 4848 CA GLY C 398 22.843 14.522 -21.260 1.00 31.80 C ANISOU 4848 CA GLY C 398 3629 5497 2957 241 635 -276 C ATOM 4849 C GLY C 398 22.020 15.769 -21.002 1.00 35.63 C ANISOU 4849 C GLY C 398 4168 5925 3446 140 587 -194 C ATOM 4850 O GLY C 398 21.550 15.996 -19.888 1.00 32.50 O ANISOU 4850 O GLY C 398 3779 5430 3138 125 530 -171 O ATOM 4851 N TRP C 399 21.848 16.579 -22.040 1.00 39.26 N ANISOU 4851 N TRP C 399 4673 6430 3816 73 606 -146 N ATOM 4852 CA TRP C 399 21.064 17.804 -21.942 1.00 46.15 C ANISOU 4852 CA TRP C 399 5613 7227 4695 -14 559 -60 C ATOM 4853 C TRP C 399 20.732 18.337 -23.332 1.00 54.73 C ANISOU 4853 C TRP C 399 6765 8365 5663 -53 578 -21 C ATOM 4854 O TRP C 399 21.358 17.948 -24.318 1.00 54.61 O ANISOU 4854 O TRP C 399 6734 8426 5588 -36 626 -51 O ATOM 4855 CB TRP C 399 21.816 18.860 -21.131 1.00 45.05 C ANISOU 4855 CB TRP C 399 5423 7095 4600 -104 576 11 C ATOM 4856 CG TRP C 399 23.217 19.081 -21.605 1.00 45.02 C ANISOU 4856 CG TRP C 399 5333 7231 4542 -148 658 25 C ATOM 4857 CD1 TRP C 399 24.331 18.400 -21.210 1.00 45.90 C ANISOU 4857 CD1 TRP C 399 5336 7408 4694 -104 690 -20 C ATOM 4858 CD2 TRP C 399 23.658 20.044 -22.571 1.00 47.35 C ANISOU 4858 CD2 TRP C 399 5651 7567 4774 -237 695 92 C ATOM 4859 NE1 TRP C 399 25.438 18.879 -21.867 1.00 47.51 N ANISOU 4859 NE1 TRP C 399 5488 7701 4862 -163 743 11 N ATOM 4860 CE2 TRP C 399 25.052 19.889 -22.707 1.00 48.74 C ANISOU 4860 CE2 TRP C 399 5725 7841 4954 -249 750 79 C ATOM 4861 CE3 TRP C 399 23.009 21.022 -23.332 1.00 48.66 C ANISOU 4861 CE3 TRP C 399 5916 7694 4879 -303 684 167 C ATOM 4862 CZ2 TRP C 399 25.810 20.676 -23.574 1.00 51.25 C ANISOU 4862 CZ2 TRP C 399 6035 8223 5216 -332 798 133 C ATOM 4863 CZ3 TRP C 399 23.764 21.802 -24.193 1.00 51.15 C ANISOU 4863 CZ3 TRP C 399 6230 8061 5141 -381 732 224 C ATOM 4864 CH2 TRP C 399 25.149 21.624 -24.306 1.00 52.28 C ANISOU 4864 CH2 TRP C 399 6269 8305 5288 -400 790 204 C ATOM 4865 N GLU C 400 19.745 19.224 -23.407 1.00 64.77 N ANISOU 4865 N GLU C 400 8119 9556 6933 -97 524 49 N ATOM 4866 CA GLU C 400 19.336 19.802 -24.684 1.00 68.40 C ANISOU 4866 CA GLU C 400 8649 10060 7279 -131 530 102 C ATOM 4867 C GLU C 400 19.594 21.306 -24.726 1.00 71.44 C ANISOU 4867 C GLU C 400 9066 10431 7648 -234 547 220 C ATOM 4868 O GLU C 400 20.130 21.827 -25.706 1.00 75.62 O ANISOU 4868 O GLU C 400 9611 11006 8116 -280 588 264 O ATOM 4869 CB GLU C 400 17.857 19.513 -24.952 1.00 68.98 C ANISOU 4869 CB GLU C 400 8800 10062 7347 -84 447 88 C ATOM 4870 N ALA C 412 10.462 24.075 -28.731 1.00 68.24 N ANISOU 4870 N ALA C 412 9165 9805 6959 -10 31 604 N ATOM 4871 CA ALA C 412 9.587 23.587 -27.671 1.00 67.03 C ANISOU 4871 CA ALA C 412 8968 9613 6887 40 -28 563 C ATOM 4872 C ALA C 412 10.380 23.252 -26.411 1.00 65.56 C ANISOU 4872 C ALA C 412 8734 9352 6822 19 20 496 C ATOM 4873 O ALA C 412 10.164 22.212 -25.787 1.00 64.24 O ANISOU 4873 O ALA C 412 8514 9175 6720 42 1 396 O ATOM 4874 CB ALA C 412 8.810 22.371 -28.145 1.00 66.87 C ANISOU 4874 CB ALA C 412 8911 9657 6838 69 -87 462 C ATOM 4875 N SER C 413 11.294 24.144 -26.045 1.00 66.05 N ANISOU 4875 N SER C 413 8820 9363 6914 -31 81 555 N ATOM 4876 CA SER C 413 12.154 23.939 -24.886 1.00 65.43 C ANISOU 4876 CA SER C 413 8694 9227 6941 -60 127 501 C ATOM 4877 C SER C 413 11.367 23.914 -23.576 1.00 65.16 C ANISOU 4877 C SER C 413 8642 9082 7033 -17 78 480 C ATOM 4878 O SER C 413 11.678 23.135 -22.672 1.00 66.10 O ANISOU 4878 O SER C 413 8704 9181 7230 -12 87 397 O ATOM 4879 CB SER C 413 13.227 25.029 -24.828 1.00 66.55 C ANISOU 4879 CB SER C 413 8868 9343 7076 -139 196 578 C ATOM 4880 N VAL C 414 10.351 24.766 -23.478 1.00 62.90 N ANISOU 4880 N VAL C 414 8408 8730 6763 21 29 558 N ATOM 4881 CA VAL C 414 9.567 24.891 -22.252 1.00 58.81 C ANISOU 4881 CA VAL C 414 7877 8110 6357 66 -10 547 C ATOM 4882 C VAL C 414 8.754 23.633 -21.948 1.00 55.01 C ANISOU 4882 C VAL C 414 7330 7663 5909 113 -62 455 C ATOM 4883 O VAL C 414 8.729 23.167 -20.807 1.00 52.02 O ANISOU 4883 O VAL C 414 6910 7231 5625 121 -63 397 O ATOM 4884 CB VAL C 414 8.610 26.101 -22.316 1.00 59.82 C ANISOU 4884 CB VAL C 414 8075 8168 6488 113 -47 654 C ATOM 4885 CG1 VAL C 414 7.617 26.060 -21.162 1.00 58.60 C ANISOU 4885 CG1 VAL C 414 7895 7936 6436 177 -91 631 C ATOM 4886 CG2 VAL C 414 9.396 27.405 -22.298 1.00 60.23 C ANISOU 4886 CG2 VAL C 414 8208 8141 6534 58 7 742 C ATOM 4887 N ILE C 415 8.098 23.083 -22.968 1.00 51.92 N ANISOU 4887 N ILE C 415 6932 7362 5434 137 -105 443 N ATOM 4888 CA ILE C 415 7.217 21.933 -22.776 1.00 47.43 C ANISOU 4888 CA ILE C 415 6308 6825 4887 168 -160 361 C ATOM 4889 C ILE C 415 7.977 20.651 -22.434 1.00 44.90 C ANISOU 4889 C ILE C 415 5945 6520 4596 141 -126 246 C ATOM 4890 O ILE C 415 7.498 19.838 -21.641 1.00 41.91 O ANISOU 4890 O ILE C 415 5526 6109 4289 156 -152 181 O ATOM 4891 CB ILE C 415 6.344 21.676 -24.021 1.00 46.62 C ANISOU 4891 CB ILE C 415 6212 6826 4676 187 -220 373 C ATOM 4892 CG1 ILE C 415 5.377 20.517 -23.762 1.00 44.82 C ANISOU 4892 CG1 ILE C 415 5928 6626 4475 201 -280 287 C ATOM 4893 CG2 ILE C 415 7.211 21.397 -25.238 1.00 48.56 C ANISOU 4893 CG2 ILE C 415 6484 7164 4802 146 -180 356 C ATOM 4894 CD1 ILE C 415 4.250 20.421 -24.767 1.00 45.25 C ANISOU 4894 CD1 ILE C 415 5976 6780 4436 220 -357 310 C ATOM 4895 N LEU C 416 9.151 20.464 -23.030 1.00 43.00 N ANISOU 4895 N LEU C 416 5712 6329 4298 105 -65 224 N ATOM 4896 CA LEU C 416 9.969 19.297 -22.714 1.00 38.81 C ANISOU 4896 CA LEU C 416 5142 5810 3794 97 -26 121 C ATOM 4897 C LEU C 416 10.410 19.348 -21.259 1.00 34.26 C ANISOU 4897 C LEU C 416 4533 5146 3339 96 -4 110 C ATOM 4898 O LEU C 416 10.373 18.341 -20.554 1.00 34.62 O ANISOU 4898 O LEU C 416 4544 5163 3446 113 -11 35 O ATOM 4899 CB LEU C 416 11.190 19.208 -23.631 1.00 40.83 C ANISOU 4899 CB LEU C 416 5404 6149 3961 68 44 108 C ATOM 4900 CG LEU C 416 12.147 18.049 -23.327 1.00 42.24 C ANISOU 4900 CG LEU C 416 5538 6344 4166 77 94 6 C ATOM 4901 CD1 LEU C 416 11.382 16.745 -23.133 1.00 41.27 C ANISOU 4901 CD1 LEU C 416 5409 6199 4072 111 47 -89 C ATOM 4902 CD2 LEU C 416 13.189 17.899 -24.428 1.00 45.24 C ANISOU 4902 CD2 LEU C 416 5920 6829 4439 60 162 -12 C ATOM 4903 N SER C 417 10.823 20.531 -20.815 1.00 33.54 N ANISOU 4903 N SER C 417 4460 5008 3276 71 21 186 N ATOM 4904 CA SER C 417 11.218 20.734 -19.428 1.00 30.92 C ANISOU 4904 CA SER C 417 4103 4596 3048 62 38 181 C ATOM 4905 C SER C 417 10.044 20.438 -18.506 1.00 25.68 C ANISOU 4905 C SER C 417 3428 3867 2462 103 -19 162 C ATOM 4906 O SER C 417 10.224 19.943 -17.394 1.00 25.29 O ANISOU 4906 O SER C 417 3345 3774 2492 108 -15 118 O ATOM 4907 CB SER C 417 11.721 22.163 -19.207 1.00 30.04 C ANISOU 4907 CB SER C 417 4031 4439 2943 17 69 266 C ATOM 4908 N LEU C 418 8.841 20.742 -18.984 1.00 26.45 N ANISOU 4908 N LEU C 418 3549 3970 2533 134 -71 200 N ATOM 4909 CA LEU C 418 7.620 20.498 -18.227 1.00 27.48 C ANISOU 4909 CA LEU C 418 3658 4059 2726 173 -125 188 C ATOM 4910 C LEU C 418 7.285 19.013 -18.144 1.00 23.20 C ANISOU 4910 C LEU C 418 3073 3545 2196 177 -149 96 C ATOM 4911 O LEU C 418 6.968 18.505 -17.072 1.00 20.54 O ANISOU 4911 O LEU C 418 2707 3160 1938 186 -160 61 O ATOM 4912 CB LEU C 418 6.444 21.257 -18.846 1.00 30.58 C ANISOU 4912 CB LEU C 418 4075 4467 3078 211 -175 260 C ATOM 4913 CG LEU C 418 6.461 22.780 -18.699 1.00 36.06 C ANISOU 4913 CG LEU C 418 4824 5096 3779 224 -159 357 C ATOM 4914 CD1 LEU C 418 5.237 23.398 -19.361 1.00 38.46 C ANISOU 4914 CD1 LEU C 418 5147 5426 4040 282 -215 430 C ATOM 4915 CD2 LEU C 418 6.541 23.176 -17.233 1.00 36.60 C ANISOU 4915 CD2 LEU C 418 4891 5066 3951 228 -140 351 C ATOM 4916 N GLU C 419 7.339 18.323 -19.278 1.00 20.07 N ANISOU 4916 N GLU C 419 2683 3224 1718 168 -156 58 N ATOM 4917 CA GLU C 419 7.002 16.905 -19.303 1.00 19.97 C ANISOU 4917 CA GLU C 419 2650 3228 1711 164 -179 -34 C ATOM 4918 C GLU C 419 8.006 16.107 -18.476 1.00 16.94 C ANISOU 4918 C GLU C 419 2249 2798 1389 162 -132 -96 C ATOM 4919 O GLU C 419 7.640 15.154 -17.791 1.00 17.27 O ANISOU 4919 O GLU C 419 2275 2801 1487 166 -149 -150 O ATOM 4920 CB GLU C 419 6.951 16.383 -20.741 1.00 27.60 C ANISOU 4920 CB GLU C 419 3639 4283 2565 151 -191 -70 C ATOM 4921 CG GLU C 419 6.308 15.009 -20.880 1.00 35.82 C ANISOU 4921 CG GLU C 419 4674 5335 3602 138 -228 -164 C ATOM 4922 CD GLU C 419 4.834 15.012 -20.514 1.00 41.19 C ANISOU 4922 CD GLU C 419 5323 6013 4313 135 -301 -145 C ATOM 4923 OE1 GLU C 419 4.197 16.083 -20.611 1.00 43.11 O ANISOU 4923 OE1 GLU C 419 5557 6279 4545 156 -331 -60 O ATOM 4924 OE2 GLU C 419 4.312 13.945 -20.127 1.00 41.38 O ANISOU 4924 OE2 GLU C 419 5335 6014 4373 114 -326 -213 O ATOM 4925 N VAL C 420 9.271 16.510 -18.537 1.00 13.58 N ANISOU 4925 N VAL C 420 1825 2383 951 154 -72 -81 N ATOM 4926 CA VAL C 420 10.312 15.872 -17.742 1.00 13.93 C ANISOU 4926 CA VAL C 420 1842 2400 1051 161 -28 -127 C ATOM 4927 C VAL C 420 10.038 16.042 -16.248 1.00 16.27 C ANISOU 4927 C VAL C 420 2116 2617 1448 166 -43 -110 C ATOM 4928 O VAL C 420 10.228 15.112 -15.466 1.00 13.29 O ANISOU 4928 O VAL C 420 1719 2204 1126 182 -40 -158 O ATOM 4929 CB VAL C 420 11.707 16.437 -18.072 1.00 13.54 C ANISOU 4929 CB VAL C 420 1782 2396 965 145 36 -103 C ATOM 4930 CG1 VAL C 420 12.733 15.954 -17.052 1.00 13.15 C ANISOU 4930 CG1 VAL C 420 1689 2326 983 157 73 -134 C ATOM 4931 CG2 VAL C 420 12.116 16.055 -19.492 1.00 18.50 C ANISOU 4931 CG2 VAL C 420 2428 3112 1490 145 64 -134 C ATOM 4932 N LYS C 421 9.590 17.230 -15.854 1.00 19.21 N ANISOU 4932 N LYS C 421 2499 2960 1841 157 -57 -40 N ATOM 4933 CA LYS C 421 9.281 17.475 -14.452 1.00 21.27 C ANISOU 4933 CA LYS C 421 2744 3151 2187 162 -68 -26 C ATOM 4934 C LYS C 421 8.142 16.569 -13.984 1.00 15.96 C ANISOU 4934 C LYS C 421 2057 2455 1554 180 -112 -63 C ATOM 4935 O LYS C 421 8.184 16.040 -12.874 1.00 14.09 O ANISOU 4935 O LYS C 421 1800 2174 1381 184 -111 -87 O ATOM 4936 CB LYS C 421 8.936 18.950 -14.216 1.00 23.11 C ANISOU 4936 CB LYS C 421 3004 3349 2427 155 -71 50 C ATOM 4937 CG LYS C 421 8.659 19.276 -12.751 1.00 23.29 C ANISOU 4937 CG LYS C 421 3018 3302 2530 161 -75 57 C ATOM 4938 CD LYS C 421 9.127 20.678 -12.360 1.00 24.86 C ANISOU 4938 CD LYS C 421 3253 3457 2738 137 -48 112 C ATOM 4939 CE LYS C 421 8.242 21.766 -12.942 1.00 21.33 C ANISOU 4939 CE LYS C 421 2854 2987 2263 160 -66 177 C ATOM 4940 NZ LYS C 421 8.612 23.122 -12.438 1.00 17.95 N ANISOU 4940 NZ LYS C 421 2480 2488 1853 137 -39 225 N ATOM 4941 N LEU C 422 7.137 16.374 -14.834 1.00 16.08 N ANISOU 4941 N LEU C 422 2080 2505 1526 184 -153 -66 N ATOM 4942 CA LEU C 422 6.025 15.494 -14.488 1.00 14.88 C ANISOU 4942 CA LEU C 422 1907 2343 1403 184 -196 -101 C ATOM 4943 C LEU C 422 6.467 14.039 -14.339 1.00 13.72 C ANISOU 4943 C LEU C 422 1763 2178 1273 174 -185 -180 C ATOM 4944 O LEU C 422 5.983 13.327 -13.458 1.00 13.60 O ANISOU 4944 O LEU C 422 1734 2118 1314 168 -199 -203 O ATOM 4945 CB LEU C 422 4.909 15.592 -15.530 1.00 17.53 C ANISOU 4945 CB LEU C 422 2243 2741 1678 181 -247 -89 C ATOM 4946 CG LEU C 422 3.883 16.698 -15.281 1.00 19.69 C ANISOU 4946 CG LEU C 422 2499 3018 1963 208 -278 -16 C ATOM 4947 CD1 LEU C 422 2.649 16.506 -16.147 1.00 23.53 C ANISOU 4947 CD1 LEU C 422 2963 3580 2396 207 -340 -12 C ATOM 4948 CD2 LEU C 422 3.507 16.754 -13.807 1.00 17.96 C ANISOU 4948 CD2 LEU C 422 2253 2738 1834 219 -272 -10 C ATOM 4949 N HIS C 423 7.378 13.594 -15.199 1.00 13.71 N ANISOU 4949 N HIS C 423 1783 2207 1220 176 -155 -218 N ATOM 4950 CA HIS C 423 7.858 12.217 -15.131 1.00 12.06 C ANISOU 4950 CA HIS C 423 1588 1971 1024 182 -138 -294 C ATOM 4951 C HIS C 423 8.728 11.988 -13.895 1.00 15.44 C ANISOU 4951 C HIS C 423 1997 2345 1525 205 -104 -292 C ATOM 4952 O HIS C 423 8.675 10.921 -13.284 1.00 15.03 O ANISOU 4952 O HIS C 423 1954 2240 1517 214 -107 -332 O ATOM 4953 CB HIS C 423 8.632 11.848 -16.399 1.00 13.77 C ANISOU 4953 CB HIS C 423 1831 2241 1160 191 -108 -340 C ATOM 4954 CG HIS C 423 7.763 11.346 -17.510 1.00 14.43 C ANISOU 4954 CG HIS C 423 1947 2364 1174 165 -146 -383 C ATOM 4955 ND1 HIS C 423 6.951 12.175 -18.254 1.00 18.18 N ANISOU 4955 ND1 HIS C 423 2417 2901 1589 144 -186 -337 N ATOM 4956 CD2 HIS C 423 7.575 10.097 -18.000 1.00 14.94 C ANISOU 4956 CD2 HIS C 423 2050 2414 1213 154 -154 -469 C ATOM 4957 CE1 HIS C 423 6.306 11.460 -19.158 1.00 17.98 C ANISOU 4957 CE1 HIS C 423 2418 2913 1501 117 -221 -393 C ATOM 4958 NE2 HIS C 423 6.666 10.196 -19.025 1.00 18.66 N ANISOU 4958 NE2 HIS C 423 2535 2949 1606 117 -201 -478 N ATOM 4959 N LEU C 424 9.521 12.991 -13.527 1.00 12.95 N ANISOU 4959 N LEU C 424 1658 2044 1217 211 -75 -242 N ATOM 4960 CA LEU C 424 10.368 12.887 -12.341 1.00 13.63 C ANISOU 4960 CA LEU C 424 1718 2098 1363 227 -50 -235 C ATOM 4961 C LEU C 424 9.534 12.860 -11.065 1.00 12.03 C ANISOU 4961 C LEU C 424 1507 1836 1226 219 -79 -215 C ATOM 4962 O LEU C 424 9.836 12.112 -10.135 1.00 12.48 O ANISOU 4962 O LEU C 424 1556 1854 1331 235 -74 -231 O ATOM 4963 CB LEU C 424 11.373 14.038 -12.290 1.00 15.98 C ANISOU 4963 CB LEU C 424 1993 2434 1646 214 -15 -189 C ATOM 4964 CG LEU C 424 12.453 14.008 -13.373 1.00 16.05 C ANISOU 4964 CG LEU C 424 1995 2513 1591 220 29 -205 C ATOM 4965 CD1 LEU C 424 13.393 15.193 -13.230 1.00 15.39 C ANISOU 4965 CD1 LEU C 424 1885 2466 1495 187 62 -153 C ATOM 4966 CD2 LEU C 424 13.220 12.694 -13.320 1.00 18.64 C ANISOU 4966 CD2 LEU C 424 2310 2844 1929 269 54 -266 C ATOM 4967 N LEU C 425 8.489 13.681 -11.019 1.00 11.60 N ANISOU 4967 N LEU C 425 1454 1780 1172 200 -108 -177 N ATOM 4968 CA LEU C 425 7.570 13.668 -9.886 1.00 13.59 C ANISOU 4968 CA LEU C 425 1693 1989 1479 195 -132 -161 C ATOM 4969 C LEU C 425 6.877 12.312 -9.785 1.00 13.14 C ANISOU 4969 C LEU C 425 1645 1907 1442 186 -155 -206 C ATOM 4970 O LEU C 425 6.700 11.770 -8.695 1.00 11.20 O ANISOU 4970 O LEU C 425 1391 1617 1245 184 -157 -207 O ATOM 4971 CB LEU C 425 6.534 14.786 -10.012 1.00 14.17 C ANISOU 4971 CB LEU C 425 1764 2076 1544 192 -155 -115 C ATOM 4972 CG LEU C 425 7.034 16.221 -9.816 1.00 17.48 C ANISOU 4972 CG LEU C 425 2193 2490 1959 195 -132 -64 C ATOM 4973 CD1 LEU C 425 5.899 17.216 -10.011 1.00 15.82 C ANISOU 4973 CD1 LEU C 425 1989 2282 1741 210 -156 -19 C ATOM 4974 CD2 LEU C 425 7.667 16.393 -8.443 1.00 17.96 C ANISOU 4974 CD2 LEU C 425 2244 2512 2068 189 -110 -61 C ATOM 4975 N HIS C 426 6.494 11.764 -10.934 1.00 12.56 N ANISOU 4975 N HIS C 426 1590 1859 1323 174 -172 -242 N ATOM 4976 CA HIS C 426 5.863 10.450 -10.980 1.00 13.73 C ANISOU 4976 CA HIS C 426 1758 1976 1482 151 -194 -293 C ATOM 4977 C HIS C 426 6.804 9.363 -10.470 1.00 15.36 C ANISOU 4977 C HIS C 426 1991 2123 1721 174 -164 -329 C ATOM 4978 O HIS C 426 6.381 8.436 -9.778 1.00 16.40 O ANISOU 4978 O HIS C 426 2140 2198 1894 158 -174 -345 O ATOM 4979 CB HIS C 426 5.410 10.120 -12.403 1.00 18.00 C ANISOU 4979 CB HIS C 426 2322 2562 1955 127 -218 -334 C ATOM 4980 CG HIS C 426 4.733 8.791 -12.527 1.00 18.41 C ANISOU 4980 CG HIS C 426 2403 2578 2012 86 -242 -393 C ATOM 4981 ND1 HIS C 426 5.396 7.651 -12.926 1.00 20.06 N ANISOU 4981 ND1 HIS C 426 2669 2743 2211 94 -221 -461 N ATOM 4982 CD2 HIS C 426 3.451 8.420 -12.299 1.00 19.51 C ANISOU 4982 CD2 HIS C 426 2528 2719 2167 31 -284 -396 C ATOM 4983 CE1 HIS C 426 4.552 6.635 -12.943 1.00 19.68 C ANISOU 4983 CE1 HIS C 426 2652 2656 2171 39 -249 -506 C ATOM 4984 NE2 HIS C 426 3.365 7.075 -12.566 1.00 22.00 N ANISOU 4984 NE2 HIS C 426 2897 2984 2480 -6 -289 -466 N ATOM 4985 N SER C 427 8.081 9.482 -10.817 1.00 14.69 N ANISOU 4985 N SER C 427 1909 2056 1615 215 -127 -338 N ATOM 4986 CA SER C 427 9.081 8.505 -10.404 1.00 13.60 C ANISOU 4986 CA SER C 427 1789 1876 1504 258 -96 -368 C ATOM 4987 C SER C 427 9.345 8.523 -8.897 1.00 13.54 C ANISOU 4987 C SER C 427 1757 1830 1558 272 -93 -326 C ATOM 4988 O SER C 427 9.596 7.479 -8.299 1.00 16.68 O ANISOU 4988 O SER C 427 2179 2169 1991 298 -87 -341 O ATOM 4989 CB SER C 427 10.394 8.744 -11.155 1.00 15.76 C ANISOU 4989 CB SER C 427 2051 2203 1734 301 -53 -382 C ATOM 4990 OG SER C 427 10.240 8.518 -12.545 1.00 22.29 O ANISOU 4990 OG SER C 427 2910 3063 2495 293 -51 -429 O ATOM 4991 N TYR C 428 9.286 9.703 -8.284 1.00 13.13 N ANISOU 4991 N TYR C 428 1665 1808 1516 257 -96 -273 N ATOM 4992 CA TYR C 428 9.711 9.848 -6.892 1.00 14.20 C ANISOU 4992 CA TYR C 428 1776 1925 1695 269 -90 -237 C ATOM 4993 C TYR C 428 8.597 10.177 -5.900 1.00 17.28 C ANISOU 4993 C TYR C 428 2158 2290 2116 235 -114 -204 C ATOM 4994 O TYR C 428 8.794 10.051 -4.689 1.00 16.09 O ANISOU 4994 O TYR C 428 1998 2119 1997 241 -112 -181 O ATOM 4995 CB TYR C 428 10.790 10.929 -6.783 1.00 12.53 C ANISOU 4995 CB TYR C 428 1525 1769 1466 277 -67 -208 C ATOM 4996 CG TYR C 428 12.145 10.499 -7.292 1.00 12.09 C ANISOU 4996 CG TYR C 428 1453 1750 1390 321 -35 -230 C ATOM 4997 CD1 TYR C 428 12.520 10.732 -8.607 1.00 10.32 C ANISOU 4997 CD1 TYR C 428 1232 1574 1115 323 -14 -253 C ATOM 4998 CD2 TYR C 428 13.050 9.857 -6.454 1.00 12.17 C ANISOU 4998 CD2 TYR C 428 1442 1756 1427 365 -24 -226 C ATOM 4999 CE1 TYR C 428 13.760 10.337 -9.076 1.00 16.44 C ANISOU 4999 CE1 TYR C 428 1984 2396 1868 368 23 -275 C ATOM 5000 CE2 TYR C 428 14.288 9.458 -6.912 1.00 12.46 C ANISOU 5000 CE2 TYR C 428 1451 1838 1444 418 8 -245 C ATOM 5001 CZ TYR C 428 14.639 9.702 -8.223 1.00 15.78 C ANISOU 5001 CZ TYR C 428 1871 2310 1817 419 34 -272 C ATOM 5002 OH TYR C 428 15.871 9.310 -8.682 1.00 16.50 O ANISOU 5002 OH TYR C 428 1926 2458 1885 476 73 -292 O ATOM 5003 N MET C 429 7.441 10.608 -6.396 1.00 13.91 N ANISOU 5003 N MET C 429 1732 1877 1676 203 -136 -202 N ATOM 5004 CA MET C 429 6.363 11.032 -5.503 1.00 12.28 C ANISOU 5004 CA MET C 429 1508 1664 1496 178 -152 -171 C ATOM 5005 C MET C 429 5.038 10.357 -5.831 1.00 13.98 C ANISOU 5005 C MET C 429 1726 1873 1713 142 -180 -188 C ATOM 5006 O MET C 429 4.856 9.814 -6.920 1.00 15.66 O ANISOU 5006 O MET C 429 1959 2094 1898 129 -194 -224 O ATOM 5007 CB MET C 429 6.187 12.555 -5.554 1.00 14.50 C ANISOU 5007 CB MET C 429 1769 1979 1761 181 -149 -136 C ATOM 5008 CG MET C 429 7.457 13.351 -5.270 1.00 15.98 C ANISOU 5008 CG MET C 429 1955 2176 1942 195 -122 -120 C ATOM 5009 SD MET C 429 7.164 15.122 -5.075 1.00 20.15 S ANISOU 5009 SD MET C 429 2484 2713 2460 190 -115 -80 S ATOM 5010 CE MET C 429 6.401 15.169 -3.453 1.00 21.19 C ANISOU 5010 CE MET C 429 2604 2816 2630 188 -116 -67 C ATOM 5011 N ASN C 430 4.114 10.397 -4.876 1.00 13.75 N ANISOU 5011 N ASN C 430 1675 1839 1712 120 -188 -163 N ATOM 5012 CA ASN C 430 2.757 9.914 -5.100 1.00 14.03 C ANISOU 5012 CA ASN C 430 1694 1890 1748 74 -215 -172 C ATOM 5013 C ASN C 430 1.804 11.086 -5.276 1.00 13.50 C ANISOU 5013 C ASN C 430 1578 1884 1666 82 -228 -142 C ATOM 5014 O ASN C 430 1.169 11.534 -4.321 1.00 11.85 O ANISOU 5014 O ASN C 430 1336 1687 1479 85 -220 -112 O ATOM 5015 CB ASN C 430 2.294 9.024 -3.945 1.00 16.68 C ANISOU 5015 CB ASN C 430 2032 2184 2121 40 -210 -162 C ATOM 5016 CG ASN C 430 3.092 7.743 -3.842 1.00 19.81 C ANISOU 5016 CG ASN C 430 2486 2507 2532 38 -201 -188 C ATOM 5017 OD1 ASN C 430 3.629 7.252 -4.836 1.00 21.43 O ANISOU 5017 OD1 ASN C 430 2728 2695 2718 49 -203 -229 O ATOM 5018 ND2 ASN C 430 3.174 7.192 -2.635 1.00 19.37 N ANISOU 5018 ND2 ASN C 430 2444 2409 2508 32 -187 -162 N ATOM 5019 N VAL C 431 1.712 11.585 -6.502 1.00 13.81 N ANISOU 5019 N VAL C 431 1615 1966 1666 93 -246 -147 N ATOM 5020 CA VAL C 431 0.902 12.763 -6.778 1.00 12.98 C ANISOU 5020 CA VAL C 431 1472 1917 1544 119 -260 -111 C ATOM 5021 C VAL C 431 -0.572 12.404 -6.914 1.00 15.12 C ANISOU 5021 C VAL C 431 1688 2244 1812 85 -295 -109 C ATOM 5022 O VAL C 431 -0.923 11.406 -7.544 1.00 17.60 O ANISOU 5022 O VAL C 431 2006 2572 2110 32 -322 -146 O ATOM 5023 CB VAL C 431 1.368 13.480 -8.061 1.00 13.53 C ANISOU 5023 CB VAL C 431 1562 2015 1564 146 -268 -105 C ATOM 5024 CG1 VAL C 431 0.475 14.681 -8.353 1.00 14.13 C ANISOU 5024 CG1 VAL C 431 1606 2142 1623 184 -285 -57 C ATOM 5025 CG2 VAL C 431 2.824 13.908 -7.931 1.00 16.32 C ANISOU 5025 CG2 VAL C 431 1956 2327 1917 169 -230 -103 C ATOM 5026 N LYS C 432 -1.427 13.220 -6.307 1.00 14.46 N ANISOU 5026 N LYS C 432 1555 2197 1743 115 -292 -70 N ATOM 5027 CA LYS C 432 -2.869 13.091 -6.473 1.00 15.69 C ANISOU 5027 CA LYS C 432 1637 2433 1892 94 -324 -60 C ATOM 5028 C LYS C 432 -3.394 14.313 -7.215 1.00 16.57 C ANISOU 5028 C LYS C 432 1718 2608 1972 160 -344 -20 C ATOM 5029 O LYS C 432 -3.020 15.441 -6.899 1.00 16.02 O ANISOU 5029 O LYS C 432 1670 2508 1909 227 -317 12 O ATOM 5030 CB LYS C 432 -3.573 12.954 -5.119 1.00 18.81 C ANISOU 5030 CB LYS C 432 1987 2834 2327 82 -300 -44 C ATOM 5031 CG LYS C 432 -3.043 11.842 -4.222 1.00 25.78 C ANISOU 5031 CG LYS C 432 2908 3647 3241 26 -277 -67 C ATOM 5032 CD LYS C 432 -3.687 10.497 -4.534 1.00 31.73 C ANISOU 5032 CD LYS C 432 3648 4414 3992 -67 -305 -96 C ATOM 5033 CE LYS C 432 -3.290 9.989 -5.910 1.00 34.04 C ANISOU 5033 CE LYS C 432 3983 4700 4250 -93 -339 -138 C ATOM 5034 N TRP C 433 -4.259 14.095 -8.198 1.00 12.18 N ANISOU 5034 N TRP C 433 1114 2138 1378 139 -394 -21 N ATOM 5035 CA TRP C 433 -4.835 15.205 -8.943 1.00 12.70 C ANISOU 5035 CA TRP C 433 1145 2272 1407 210 -420 27 C ATOM 5036 C TRP C 433 -6.272 15.450 -8.509 1.00 13.37 C ANISOU 5036 C TRP C 433 1126 2450 1504 233 -437 58 C ATOM 5037 O TRP C 433 -7.101 14.542 -8.534 1.00 17.91 O ANISOU 5037 O TRP C 433 1635 3093 2075 160 -467 36 O ATOM 5038 CB TRP C 433 -4.760 14.938 -10.450 1.00 14.93 C ANISOU 5038 CB TRP C 433 1444 2607 1624 183 -469 12 C ATOM 5039 CG TRP C 433 -3.350 14.807 -10.945 1.00 13.73 C ANISOU 5039 CG TRP C 433 1386 2379 1453 174 -445 -15 C ATOM 5040 CD1 TRP C 433 -2.579 13.679 -10.935 1.00 14.90 C ANISOU 5040 CD1 TRP C 433 1583 2472 1608 110 -432 -76 C ATOM 5041 CD2 TRP C 433 -2.536 15.844 -11.511 1.00 12.52 C ANISOU 5041 CD2 TRP C 433 1287 2199 1270 231 -428 20 C ATOM 5042 NE1 TRP C 433 -1.339 13.949 -11.461 1.00 12.04 N ANISOU 5042 NE1 TRP C 433 1289 2065 1221 131 -406 -83 N ATOM 5043 CE2 TRP C 433 -1.287 15.269 -11.824 1.00 16.85 C ANISOU 5043 CE2 TRP C 433 1902 2692 1807 196 -403 -24 C ATOM 5044 CE3 TRP C 433 -2.744 17.200 -11.787 1.00 14.57 C ANISOU 5044 CE3 TRP C 433 1550 2474 1514 311 -429 87 C ATOM 5045 CZ2 TRP C 433 -0.250 16.004 -12.398 1.00 14.56 C ANISOU 5045 CZ2 TRP C 433 1670 2376 1486 225 -378 -3 C ATOM 5046 CZ3 TRP C 433 -1.713 17.928 -12.356 1.00 15.72 C ANISOU 5046 CZ3 TRP C 433 1768 2576 1629 334 -406 110 C ATOM 5047 CH2 TRP C 433 -0.481 17.328 -12.655 1.00 16.17 C ANISOU 5047 CH2 TRP C 433 1879 2592 1672 286 -380 65 C ATOM 5048 N ILE C 434 -6.555 16.682 -8.100 1.00 13.47 N ANISOU 5048 N ILE C 434 1124 2464 1530 333 -414 108 N ATOM 5049 CA ILE C 434 -7.898 17.057 -7.675 1.00 18.49 C ANISOU 5049 CA ILE C 434 1654 3195 2177 381 -421 142 C ATOM 5050 C ILE C 434 -8.378 18.303 -8.405 1.00 18.90 C ANISOU 5050 C ILE C 434 1687 3297 2198 496 -444 203 C ATOM 5051 O ILE C 434 -7.571 19.110 -8.868 1.00 21.89 O ANISOU 5051 O ILE C 434 2153 3602 2561 547 -433 225 O ATOM 5052 CB ILE C 434 -7.965 17.314 -6.154 1.00 13.88 C ANISOU 5052 CB ILE C 434 1064 2564 1645 409 -358 142 C ATOM 5053 CG1 ILE C 434 -7.175 18.573 -5.788 1.00 13.46 C ANISOU 5053 CG1 ILE C 434 1098 2409 1605 502 -313 164 C ATOM 5054 CG2 ILE C 434 -7.456 16.105 -5.383 1.00 17.82 C ANISOU 5054 CG2 ILE C 434 1590 3009 2171 303 -336 94 C ATOM 5055 CD1 ILE C 434 -7.313 18.984 -4.327 1.00 17.63 C ANISOU 5055 CD1 ILE C 434 1625 2899 2173 540 -251 161 C ATOM 5056 N PRO C 435 -9.703 18.455 -8.517 1.00 20.59 N ANISOU 5056 N PRO C 435 1790 3629 2402 531 -471 233 N ATOM 5057 CA PRO C 435 -10.321 19.638 -9.124 1.00 24.26 C ANISOU 5057 CA PRO C 435 2257 4111 2851 634 -477 290 C ATOM 5058 C PRO C 435 -10.136 20.874 -8.255 1.00 27.29 C ANISOU 5058 C PRO C 435 2691 4406 3273 750 -414 319 C ATOM 5059 O PRO C 435 -10.049 20.757 -7.033 1.00 25.72 O ANISOU 5059 O PRO C 435 2484 4172 3115 751 -366 296 O ATOM 5060 CB PRO C 435 -11.806 19.260 -9.215 1.00 24.08 C ANISOU 5060 CB PRO C 435 2115 4211 2824 609 -501 294 C ATOM 5061 CG PRO C 435 -11.857 17.777 -9.017 1.00 24.05 C ANISOU 5061 CG PRO C 435 2065 4252 2820 468 -522 238 C ATOM 5062 CD PRO C 435 -10.705 17.451 -8.127 1.00 21.76 C ANISOU 5062 CD PRO C 435 1838 3866 2562 443 -483 206 C ATOM 5063 N LEU C 436 -10.070 22.041 -8.883 1.00 33.33 N ANISOU 5063 N LEU C 436 3515 5128 4021 842 -414 369 N ATOM 5064 CA LEU C 436 -10.041 23.302 -8.152 1.00 37.93 C ANISOU 5064 CA LEU C 436 4155 5619 4636 952 -356 395 C ATOM 5065 C LEU C 436 -11.453 23.750 -7.801 1.00 41.08 C ANISOU 5065 C LEU C 436 4471 6089 5050 1022 -343 415 C ATOM 5066 O LEU C 436 -12.361 23.660 -8.625 1.00 41.50 O ANISOU 5066 O LEU C 436 4451 6242 5074 1027 -389 441 O ATOM 5067 CB LEU C 436 -9.342 24.387 -8.972 1.00 42.18 C ANISOU 5067 CB LEU C 436 4807 6070 5151 1015 -358 443 C ATOM 5068 CG LEU C 436 -7.856 24.189 -9.260 1.00 43.14 C ANISOU 5068 CG LEU C 436 5026 6111 5255 963 -359 431 C ATOM 5069 CD1 LEU C 436 -7.337 25.326 -10.124 1.00 43.26 C ANISOU 5069 CD1 LEU C 436 5147 6049 5241 1020 -359 490 C ATOM 5070 CD2 LEU C 436 -7.082 24.098 -7.960 1.00 42.27 C ANISOU 5070 CD2 LEU C 436 4960 5911 5189 948 -303 388 C ATOM 5071 N SER C 437 -11.634 24.233 -6.577 1.00 46.11 N ANISOU 5071 N SER C 437 5116 6678 5727 1077 -280 401 N ATOM 5072 CA SER C 437 -12.917 24.792 -6.165 1.00 53.57 C ANISOU 5072 CA SER C 437 5989 7683 6683 1160 -258 419 C ATOM 5073 C SER C 437 -12.875 26.314 -6.254 1.00 58.62 C ANISOU 5073 C SER C 437 6721 8223 7328 1289 -227 458 C ATOM 5074 O SER C 437 -11.799 26.910 -6.293 1.00 60.13 O ANISOU 5074 O SER C 437 7037 8286 7525 1303 -208 461 O ATOM 5075 CB SER C 437 -13.276 24.348 -4.744 1.00 54.02 C ANISOU 5075 CB SER C 437 5991 7762 6771 1139 -204 377 C ATOM 5076 OG SER C 437 -13.486 22.948 -4.680 1.00 52.18 O ANISOU 5076 OG SER C 437 5668 7625 6533 1017 -233 347 O ATOM 5077 N SER C 438 -14.048 26.939 -6.291 1.00 63.41 N ANISOU 5077 N SER C 438 7268 8891 7934 1382 -223 489 N ATOM 5078 CA SER C 438 -14.134 28.394 -6.363 1.00 66.11 C ANISOU 5078 CA SER C 438 7696 9139 8283 1512 -193 527 C ATOM 5079 C SER C 438 -13.800 29.031 -5.017 1.00 65.55 C ANISOU 5079 C SER C 438 7702 8954 8249 1559 -113 489 C ATOM 5080 O SER C 438 -12.720 29.596 -4.836 1.00 64.16 O ANISOU 5080 O SER C 438 7660 8635 8083 1559 -85 479 O ATOM 5081 CB SER C 438 -15.528 28.829 -6.820 1.00 69.44 C ANISOU 5081 CB SER C 438 8023 9670 8691 1604 -215 573 C TER 5082 SER C 438 ATOM 5083 N MET D 1 34.611 58.192 -6.182 1.00103.88 N ANISOU 5083 N MET D 1 17126 8636 13707 -4359 580 1956 N ATOM 5084 CA MET D 1 33.535 57.941 -7.132 1.00102.22 C ANISOU 5084 CA MET D 1 16934 8499 13407 -4095 696 2160 C ATOM 5085 C MET D 1 32.299 57.392 -6.426 1.00100.55 C ANISOU 5085 C MET D 1 16854 8277 13073 -3855 668 2042 C ATOM 5086 O MET D 1 32.334 57.101 -5.231 1.00101.02 O ANISOU 5086 O MET D 1 16965 8306 13112 -3905 553 1797 O ATOM 5087 CB MET D 1 33.997 56.969 -8.220 1.00 99.41 C ANISOU 5087 CB MET D 1 16240 8519 13012 -4135 694 2292 C ATOM 5088 N GLN D 2 31.206 57.261 -7.170 1.00 99.87 N ANISOU 5088 N GLN D 2 16816 8229 12901 -3584 775 2222 N ATOM 5089 CA GLN D 2 29.973 56.688 -6.641 1.00 97.60 C ANISOU 5089 CA GLN D 2 16631 7954 12498 -3324 765 2136 C ATOM 5090 C GLN D 2 29.494 55.567 -7.555 1.00 94.71 C ANISOU 5090 C GLN D 2 16046 7936 12005 -3186 778 2271 C ATOM 5091 O GLN D 2 29.351 55.762 -8.762 1.00 95.82 O ANISOU 5091 O GLN D 2 16117 8172 12118 -3106 882 2528 O ATOM 5092 CB GLN D 2 28.896 57.765 -6.495 1.00101.31 C ANISOU 5092 CB GLN D 2 17413 8092 12988 -3068 899 2214 C ATOM 5093 CG GLN D 2 29.280 58.896 -5.555 1.00106.91 C ANISOU 5093 CG GLN D 2 18352 8455 13812 -3197 903 2068 C ATOM 5094 CD GLN D 2 28.499 58.867 -4.256 1.00107.34 C ANISOU 5094 CD GLN D 2 18604 8357 13823 -3059 872 1831 C ATOM 5095 OE1 GLN D 2 27.286 58.655 -4.253 1.00106.53 O ANISOU 5095 OE1 GLN D 2 18584 8243 13650 -2754 937 1867 O ATOM 5096 NE2 GLN D 2 29.191 59.080 -3.143 1.00108.22 N ANISOU 5096 NE2 GLN D 2 18779 8369 13969 -3276 775 1591 N ATOM 5097 N ILE D 3 29.247 54.395 -6.980 1.00 89.75 N ANISOU 5097 N ILE D 3 15302 7509 11289 -3159 674 2101 N ATOM 5098 CA ILE D 3 28.903 53.220 -7.773 1.00 84.44 C ANISOU 5098 CA ILE D 3 14389 7201 10492 -3070 676 2197 C ATOM 5099 C ILE D 3 27.453 52.781 -7.583 1.00 80.72 C ANISOU 5099 C ILE D 3 14040 6736 9893 -2739 718 2199 C ATOM 5100 O ILE D 3 26.773 53.223 -6.657 1.00 80.76 O ANISOU 5100 O ILE D 3 14291 6476 9917 -2589 725 2074 O ATOM 5101 CB ILE D 3 29.827 52.037 -7.434 1.00 79.05 C ANISOU 5101 CB ILE D 3 13399 6819 9816 -3300 532 2023 C ATOM 5102 CG1 ILE D 3 29.565 51.549 -6.007 1.00 75.08 C ANISOU 5102 CG1 ILE D 3 12981 6244 9303 -3285 412 1744 C ATOM 5103 CG2 ILE D 3 31.285 52.436 -7.605 1.00 79.60 C ANISOU 5103 CG2 ILE D 3 13320 6904 10020 -3594 492 2018 C ATOM 5104 CD1 ILE D 3 30.461 50.411 -5.576 1.00 72.09 C ANISOU 5104 CD1 ILE D 3 12288 6158 8946 -3484 267 1573 C ATOM 5105 N PHE D 4 26.992 51.907 -8.473 1.00 77.71 N ANISOU 5105 N PHE D 4 13355 6765 9407 -2541 736 2281 N ATOM 5106 CA PHE D 4 25.632 51.385 -8.418 1.00 76.56 C ANISOU 5106 CA PHE D 4 13165 6767 9158 -2154 759 2247 C ATOM 5107 C PHE D 4 25.634 49.857 -8.444 1.00 73.65 C ANISOU 5107 C PHE D 4 12416 6855 8714 -2113 670 2088 C ATOM 5108 O PHE D 4 26.453 49.241 -9.126 1.00 73.32 O ANISOU 5108 O PHE D 4 12091 7103 8663 -2292 647 2121 O ATOM 5109 CB PHE D 4 24.800 51.935 -9.579 1.00 78.50 C ANISOU 5109 CB PHE D 4 13439 7055 9334 -1894 890 2537 C ATOM 5110 N VAL D 5 24.716 49.254 -7.695 1.00 70.68 N ANISOU 5110 N VAL D 5 12036 6529 8290 -1878 634 1916 N ATOM 5111 CA VAL D 5 24.615 47.799 -7.619 1.00 64.83 C ANISOU 5111 CA VAL D 5 10956 6191 7486 -1817 563 1751 C ATOM 5112 C VAL D 5 23.184 47.330 -7.882 1.00 60.83 C ANISOU 5112 C VAL D 5 10373 5869 6870 -1427 614 1766 C ATOM 5113 O VAL D 5 22.231 47.859 -7.306 1.00 60.24 O ANISOU 5113 O VAL D 5 10541 5552 6796 -1202 651 1752 O ATOM 5114 CB VAL D 5 25.077 47.274 -6.245 1.00 64.08 C ANISOU 5114 CB VAL D 5 10882 6015 7451 -1966 442 1474 C ATOM 5115 CG1 VAL D 5 25.125 45.757 -6.247 1.00 60.99 C ANISOU 5115 CG1 VAL D 5 10117 6041 7014 -1932 382 1325 C ATOM 5116 CG2 VAL D 5 26.441 47.840 -5.894 1.00 66.45 C ANISOU 5116 CG2 VAL D 5 11280 6107 7861 -2357 379 1460 C ATOM 5117 N LYS D 6 23.038 46.339 -8.757 1.00 57.95 N ANISOU 5117 N LYS D 6 9669 5934 6413 -1353 623 1793 N ATOM 5118 CA LYS D 6 21.719 45.826 -9.110 1.00 57.13 C ANISOU 5118 CA LYS D 6 9454 6054 6198 -1006 664 1812 C ATOM 5119 C LYS D 6 21.693 44.304 -9.144 1.00 56.47 C ANISOU 5119 C LYS D 6 9015 6383 6058 -985 620 1631 C ATOM 5120 O LYS D 6 22.687 43.666 -9.493 1.00 53.66 O ANISOU 5120 O LYS D 6 8432 6238 5720 -1218 595 1591 O ATOM 5121 CB LYS D 6 21.274 46.373 -10.470 1.00 56.25 C ANISOU 5121 CB LYS D 6 9318 6058 5997 -879 756 2103 C ATOM 5122 CG LYS D 6 22.074 45.832 -11.649 1.00 53.93 C ANISOU 5122 CG LYS D 6 8735 6115 5640 -1065 770 2196 C ATOM 5123 CD LYS D 6 21.472 46.263 -12.978 1.00 55.26 C ANISOU 5123 CD LYS D 6 8867 6444 5684 -906 853 2477 C ATOM 5124 N THR D 7 20.520 43.750 -8.858 1.00 61.21 N ANISOU 5124 N THR D 7 9567 7088 6601 -703 623 1527 N ATOM 5125 CA THR D 7 20.270 42.317 -8.946 1.00 66.10 C ANISOU 5125 CA THR D 7 9848 8111 7157 -641 607 1376 C ATOM 5126 C THR D 7 19.516 42.022 -10.243 1.00 73.96 C ANISOU 5126 C THR D 7 10658 9430 8013 -478 675 1547 C ATOM 5127 O THR D 7 18.617 42.764 -10.618 1.00 76.39 O ANISOU 5127 O THR D 7 11120 9631 8273 -296 721 1743 O ATOM 5128 CB THR D 7 19.499 41.809 -7.712 1.00 64.94 C ANISOU 5128 CB THR D 7 9730 7921 7023 -439 575 1155 C ATOM 5129 OG1 THR D 7 19.717 40.405 -7.551 1.00 62.84 O ANISOU 5129 OG1 THR D 7 9173 7939 6762 -526 538 955 O ATOM 5130 CG2 THR D 7 18.001 42.094 -7.828 1.00 64.29 C ANISOU 5130 CG2 THR D 7 9653 7924 6851 -84 632 1231 C ATOM 5131 N LEU D 8 19.903 40.959 -10.939 1.00 83.11 N ANISOU 5131 N LEU D 8 11488 10984 9107 -547 685 1477 N ATOM 5132 CA LEU D 8 19.466 40.750 -12.318 1.00 87.35 C ANISOU 5132 CA LEU D 8 11839 11855 9494 -462 746 1638 C ATOM 5133 C LEU D 8 17.969 40.998 -12.504 1.00 88.98 C ANISOU 5133 C LEU D 8 12103 12101 9605 -121 767 1728 C ATOM 5134 O LEU D 8 17.533 41.405 -13.581 1.00 91.14 O ANISOU 5134 O LEU D 8 12349 12519 9761 -31 807 1949 O ATOM 5135 CB LEU D 8 19.829 39.336 -12.787 1.00 85.29 C ANISOU 5135 CB LEU D 8 11219 12006 9180 -563 765 1488 C ATOM 5136 CG LEU D 8 19.493 38.956 -14.237 1.00 87.29 C ANISOU 5136 CG LEU D 8 11255 12650 9259 -524 832 1617 C ATOM 5137 CD1 LEU D 8 18.047 38.491 -14.368 1.00 86.64 C ANISOU 5137 CD1 LEU D 8 11086 12774 9059 -222 836 1582 C ATOM 5138 CD2 LEU D 8 19.783 40.107 -15.199 1.00 91.05 C ANISOU 5138 CD2 LEU D 8 11872 13044 9679 -591 866 1913 C ATOM 5139 N THR D 9 17.191 40.771 -11.451 1.00 84.60 N ANISOU 5139 N THR D 9 11627 11418 9100 69 739 1569 N ATOM 5140 CA THR D 9 15.751 40.980 -11.521 1.00 80.82 C ANISOU 5140 CA THR D 9 11193 10962 8552 402 761 1646 C ATOM 5141 C THR D 9 15.318 42.212 -10.729 1.00 77.69 C ANISOU 5141 C THR D 9 11157 10109 8252 538 772 1732 C ATOM 5142 O THR D 9 15.106 42.141 -9.521 1.00 74.35 O ANISOU 5142 O THR D 9 10871 9458 7920 598 752 1553 O ATOM 5143 CB THR D 9 14.974 39.747 -11.007 1.00 76.76 C ANISOU 5143 CB THR D 9 10478 10673 8015 561 748 1410 C ATOM 5144 OG1 THR D 9 15.272 39.527 -9.623 1.00 75.17 O ANISOU 5144 OG1 THR D 9 10395 10224 7942 514 712 1186 O ATOM 5145 CG2 THR D 9 15.352 38.507 -11.804 1.00 74.31 C ANISOU 5145 CG2 THR D 9 9815 10806 7613 431 760 1315 C ATOM 5146 N GLY D 10 15.213 43.345 -11.417 1.00 79.01 N ANISOU 5146 N GLY D 10 11486 10136 8399 581 814 2009 N ATOM 5147 CA GLY D 10 14.587 44.529 -10.855 1.00 80.43 C ANISOU 5147 CA GLY D 10 11993 9906 8659 763 856 2128 C ATOM 5148 C GLY D 10 15.451 45.610 -10.227 1.00 81.96 C ANISOU 5148 C GLY D 10 12513 9640 8987 573 869 2153 C ATOM 5149 O GLY D 10 16.435 46.064 -10.811 1.00 83.09 O ANISOU 5149 O GLY D 10 12682 9750 9139 336 874 2274 O ATOM 5150 N LYS D 11 15.061 46.013 -9.019 1.00 81.87 N ANISOU 5150 N LYS D 11 12756 9275 9077 674 881 2031 N ATOM 5151 CA LYS D 11 15.581 47.210 -8.352 1.00 83.65 C ANISOU 5151 CA LYS D 11 13348 9009 9424 553 915 2064 C ATOM 5152 C LYS D 11 17.103 47.337 -8.291 1.00 83.15 C ANISOU 5152 C LYS D 11 13315 8862 9416 159 864 2009 C ATOM 5153 O LYS D 11 17.818 46.365 -8.052 1.00 80.98 O ANISOU 5153 O LYS D 11 12837 8798 9133 -32 784 1817 O ATOM 5154 CB LYS D 11 15.028 47.281 -6.927 1.00 82.46 C ANISOU 5154 CB LYS D 11 13420 8556 9354 679 924 1856 C ATOM 5155 N THR D 12 17.578 48.561 -8.499 1.00 84.40 N ANISOU 5155 N THR D 12 13727 8700 9642 45 919 2187 N ATOM 5156 CA THR D 12 18.995 48.880 -8.400 1.00 82.86 C ANISOU 5156 CA THR D 12 13599 8365 9517 -331 880 2155 C ATOM 5157 C THR D 12 19.210 49.914 -7.299 1.00 81.00 C ANISOU 5157 C THR D 12 13762 7608 9406 -419 906 2082 C ATOM 5158 O THR D 12 18.335 50.735 -7.030 1.00 80.46 O ANISOU 5158 O THR D 12 13950 7250 9373 -192 999 2170 O ATOM 5159 CB THR D 12 19.552 49.416 -9.735 1.00 85.85 C ANISOU 5159 CB THR D 12 13914 8840 9865 -450 930 2435 C ATOM 5160 OG1 THR D 12 20.946 49.716 -9.592 1.00 87.39 O ANISOU 5160 OG1 THR D 12 14167 8893 10145 -824 894 2397 O ATOM 5161 CG2 THR D 12 18.806 50.670 -10.161 1.00 88.89 C ANISOU 5161 CG2 THR D 12 14550 8955 10268 -238 1047 2711 C ATOM 5162 N ILE D 13 20.373 49.869 -6.660 1.00 78.64 N ANISOU 5162 N ILE D 13 13514 7192 9175 -753 828 1922 N ATOM 5163 CA ILE D 13 20.673 50.790 -5.571 1.00 78.86 C ANISOU 5163 CA ILE D 13 13917 6741 9306 -886 840 1821 C ATOM 5164 C ILE D 13 21.883 51.659 -5.879 1.00 79.51 C ANISOU 5164 C ILE D 13 14128 6613 9468 -1225 847 1929 C ATOM 5165 O ILE D 13 22.790 51.246 -6.602 1.00 78.36 O ANISOU 5165 O ILE D 13 13740 6723 9310 -1440 797 1987 O ATOM 5166 CB ILE D 13 20.939 50.043 -4.254 1.00 77.55 C ANISOU 5166 CB ILE D 13 13750 6567 9150 -996 727 1500 C ATOM 5167 CG1 ILE D 13 22.141 49.110 -4.414 1.00 75.87 C ANISOU 5167 CG1 ILE D 13 13231 6666 8932 -1298 601 1403 C ATOM 5168 CG2 ILE D 13 19.701 49.276 -3.814 1.00 74.83 C ANISOU 5168 CG2 ILE D 13 13322 6369 8740 -658 736 1382 C ATOM 5169 CD1 ILE D 13 22.684 48.583 -3.107 1.00 75.13 C ANISOU 5169 CD1 ILE D 13 13168 6514 8865 -1482 479 1123 C ATOM 5170 N THR D 14 21.887 52.866 -5.325 1.00 81.53 N ANISOU 5170 N THR D 14 14772 6395 9813 -1276 921 1952 N ATOM 5171 CA THR D 14 23.029 53.759 -5.446 1.00 84.08 C ANISOU 5171 CA THR D 14 15241 6475 10229 -1613 929 2019 C ATOM 5172 C THR D 14 23.810 53.764 -4.139 1.00 85.58 C ANISOU 5172 C THR D 14 15506 6526 10486 -1874 810 1717 C ATOM 5173 O THR D 14 23.234 53.935 -3.065 1.00 86.56 O ANISOU 5173 O THR D 14 15793 6477 10619 -1749 808 1527 O ATOM 5174 CB THR D 14 22.598 55.194 -5.798 1.00 85.33 C ANISOU 5174 CB THR D 14 15583 6359 10481 -1462 1065 2195 C ATOM 5175 N LEU D 15 25.121 53.571 -4.230 1.00 87.20 N ANISOU 5175 N LEU D 15 15564 6837 10731 -2227 710 1675 N ATOM 5176 CA LEU D 15 25.958 53.504 -3.040 1.00 89.68 C ANISOU 5176 CA LEU D 15 15891 7089 11093 -2480 576 1404 C ATOM 5177 C LEU D 15 26.982 54.631 -2.991 1.00 95.53 C ANISOU 5177 C LEU D 15 16706 7638 11952 -2733 577 1418 C ATOM 5178 O LEU D 15 27.658 54.916 -3.980 1.00 98.66 O ANISOU 5178 O LEU D 15 16987 8100 12398 -2869 610 1604 O ATOM 5179 CB LEU D 15 26.674 52.155 -2.967 1.00 87.88 C ANISOU 5179 CB LEU D 15 15373 7197 10821 -2676 430 1300 C ATOM 5180 CG LEU D 15 25.799 50.917 -2.766 1.00 85.09 C ANISOU 5180 CG LEU D 15 14892 7076 10362 -2449 402 1213 C ATOM 5181 CD1 LEU D 15 26.650 49.659 -2.794 1.00 83.00 C ANISOU 5181 CD1 LEU D 15 14237 7210 10087 -2627 265 1110 C ATOM 5182 CD2 LEU D 15 25.031 51.018 -1.460 1.00 85.07 C ANISOU 5182 CD2 LEU D 15 15146 6841 10336 -2300 392 1001 C ATOM 5183 N GLU D 16 27.088 55.267 -1.829 1.00 97.51 N ANISOU 5183 N GLU D 16 17145 7662 12241 -2792 547 1219 N ATOM 5184 CA GLU D 16 28.096 56.292 -1.603 1.00 99.93 C ANISOU 5184 CA GLU D 16 17528 7789 12652 -3049 535 1195 C ATOM 5185 C GLU D 16 29.373 55.642 -1.090 1.00 98.44 C ANISOU 5185 C GLU D 16 17124 7809 12470 -3362 355 1038 C ATOM 5186 O GLU D 16 29.392 55.055 -0.009 1.00 98.24 O ANISOU 5186 O GLU D 16 17081 7861 12385 -3388 240 820 O ATOM 5187 CB GLU D 16 27.595 57.342 -0.611 1.00103.04 C ANISOU 5187 CB GLU D 16 18227 7850 13073 -2966 602 1066 C ATOM 5188 N VAL D 17 30.439 55.742 -1.875 1.00 97.37 N ANISOU 5188 N VAL D 17 16805 7780 12410 -3583 335 1162 N ATOM 5189 CA VAL D 17 31.699 55.109 -1.517 1.00 94.59 C ANISOU 5189 CA VAL D 17 16198 7660 12083 -3857 173 1046 C ATOM 5190 C VAL D 17 32.890 55.928 -1.994 1.00 97.76 C ANISOU 5190 C VAL D 17 16542 7994 12609 -4108 185 1140 C ATOM 5191 O VAL D 17 32.732 57.046 -2.490 1.00100.52 O ANISOU 5191 O VAL D 17 17076 8089 13026 -4083 318 1276 O ATOM 5192 CB VAL D 17 31.800 53.688 -2.104 1.00 88.58 C ANISOU 5192 CB VAL D 17 15109 7279 11269 -3840 109 1090 C ATOM 5193 N GLU D 18 34.080 55.363 -1.821 1.00 98.80 N ANISOU 5193 N GLU D 18 16406 8355 12779 -4334 52 1070 N ATOM 5194 CA GLU D 18 35.307 55.948 -2.336 1.00104.50 C ANISOU 5194 CA GLU D 18 17012 9069 13626 -4571 57 1160 C ATOM 5195 C GLU D 18 36.087 54.860 -3.057 1.00108.00 C ANISOU 5195 C GLU D 18 17061 9886 14089 -4652 -2 1228 C ATOM 5196 O GLU D 18 36.009 53.691 -2.682 1.00106.27 O ANISOU 5196 O GLU D 18 16651 9923 13802 -4601 -103 1127 O ATOM 5197 CB GLU D 18 36.142 56.561 -1.211 1.00105.19 C ANISOU 5197 CB GLU D 18 17184 9022 13761 -4784 -44 984 C ATOM 5198 N PRO D 19 36.843 55.239 -4.097 1.00115.72 N ANISOU 5198 N PRO D 19 17908 10895 15165 -4766 72 1401 N ATOM 5199 CA PRO D 19 37.612 54.284 -4.903 1.00114.28 C ANISOU 5199 CA PRO D 19 17345 11061 15014 -4828 50 1479 C ATOM 5200 C PRO D 19 38.565 53.432 -4.072 1.00113.59 C ANISOU 5200 C PRO D 19 17002 11206 14952 -4955 -120 1305 C ATOM 5201 O PRO D 19 39.002 52.377 -4.528 1.00112.64 O ANISOU 5201 O PRO D 19 16557 11402 14840 -4942 -147 1327 O ATOM 5202 CB PRO D 19 38.394 55.187 -5.859 1.00116.74 C ANISOU 5202 CB PRO D 19 17636 11271 15448 -4962 159 1656 C ATOM 5203 CG PRO D 19 37.553 56.402 -5.987 1.00119.09 C ANISOU 5203 CG PRO D 19 18294 11212 15742 -4869 286 1750 C ATOM 5204 CD PRO D 19 36.934 56.608 -4.632 1.00118.74 C ANISOU 5204 CD PRO D 19 18500 10979 15638 -4817 206 1544 C ATOM 5205 N SER D 20 38.869 53.888 -2.862 1.00112.31 N ANISOU 5205 N SER D 20 16982 10892 14799 -5061 -224 1139 N ATOM 5206 CA SER D 20 39.812 53.202 -1.987 1.00107.29 C ANISOU 5206 CA SER D 20 16123 10457 14184 -5179 -387 991 C ATOM 5207 C SER D 20 39.246 51.931 -1.353 1.00 99.77 C ANISOU 5207 C SER D 20 15051 9732 13123 -5024 -481 871 C ATOM 5208 O SER D 20 39.984 50.971 -1.128 1.00 97.60 O ANISOU 5208 O SER D 20 14474 9732 12876 -5054 -576 823 O ATOM 5209 CB SER D 20 40.285 54.152 -0.885 1.00108.28 C ANISOU 5209 CB SER D 20 16456 10350 14335 -5347 -464 861 C ATOM 5210 N ASP D 21 37.948 51.930 -1.059 1.00 95.60 N ANISOU 5210 N ASP D 21 14760 9082 12484 -4847 -445 826 N ATOM 5211 CA ASP D 21 37.319 50.830 -0.327 1.00 92.36 C ANISOU 5211 CA ASP D 21 14281 8842 11969 -4698 -529 695 C ATOM 5212 C ASP D 21 37.522 49.475 -0.996 1.00 87.72 C ANISOU 5212 C ASP D 21 13320 8620 11391 -4624 -536 750 C ATOM 5213 O ASP D 21 37.532 49.368 -2.220 1.00 86.21 O ANISOU 5213 O ASP D 21 13004 8518 11233 -4601 -430 906 O ATOM 5214 CB ASP D 21 35.818 51.083 -0.160 1.00 92.69 C ANISOU 5214 CB ASP D 21 14635 8682 11902 -4494 -450 671 C ATOM 5215 CG ASP D 21 35.518 52.397 0.528 1.00 97.22 C ANISOU 5215 CG ASP D 21 15584 8887 12467 -4525 -417 606 C ATOM 5216 OD1 ASP D 21 36.431 52.958 1.168 1.00100.17 O ANISOU 5216 OD1 ASP D 21 15977 9189 12893 -4717 -492 532 O ATOM 5217 OD2 ASP D 21 34.365 52.867 0.429 1.00 97.71 O ANISOU 5217 OD2 ASP D 21 15917 8732 12475 -4347 -307 630 O ATOM 5218 N THR D 22 37.686 48.442 -0.174 1.00 84.10 N ANISOU 5218 N THR D 22 12681 8372 10901 -4578 -651 621 N ATOM 5219 CA THR D 22 37.806 47.075 -0.664 1.00 78.20 C ANISOU 5219 CA THR D 22 11582 7965 10164 -4476 -649 647 C ATOM 5220 C THR D 22 36.429 46.498 -0.957 1.00 73.73 C ANISOU 5220 C THR D 22 11087 7435 9491 -4274 -582 647 C ATOM 5221 O THR D 22 35.415 47.021 -0.492 1.00 73.88 O ANISOU 5221 O THR D 22 11423 7223 9423 -4193 -564 594 O ATOM 5222 CB THR D 22 38.529 46.168 0.347 1.00 75.72 C ANISOU 5222 CB THR D 22 11043 7857 9872 -4482 -785 523 C ATOM 5223 OG1 THR D 22 37.747 46.068 1.544 1.00 74.46 O ANISOU 5223 OG1 THR D 22 11082 7606 9604 -4396 -860 376 O ATOM 5224 CG2 THR D 22 39.896 46.736 0.686 1.00 78.25 C ANISOU 5224 CG2 THR D 22 11296 8142 10294 -4688 -857 526 C ATOM 5225 N ILE D 23 36.396 45.416 -1.727 1.00 69.43 N ANISOU 5225 N ILE D 23 10247 7177 8954 -4182 -532 702 N ATOM 5226 CA ILE D 23 35.138 44.775 -2.089 1.00 65.89 C ANISOU 5226 CA ILE D 23 9827 6803 8406 -4004 -462 708 C ATOM 5227 C ILE D 23 34.398 44.290 -0.843 1.00 64.22 C ANISOU 5227 C ILE D 23 9730 6556 8112 -3889 -550 530 C ATOM 5228 O ILE D 23 33.168 44.271 -0.811 1.00 63.16 O ANISOU 5228 O ILE D 23 9796 6318 7883 -3755 -499 509 O ATOM 5229 CB ILE D 23 35.364 43.593 -3.053 1.00 63.09 C ANISOU 5229 CB ILE D 23 9088 6803 8078 -3931 -394 772 C ATOM 5230 CG1 ILE D 23 36.194 44.044 -4.258 1.00 61.62 C ANISOU 5230 CG1 ILE D 23 8776 6663 7974 -4034 -302 936 C ATOM 5231 CG2 ILE D 23 34.035 43.010 -3.508 1.00 62.40 C ANISOU 5231 CG2 ILE D 23 9030 6800 7878 -3770 -308 790 C ATOM 5232 CD1 ILE D 23 35.535 45.125 -5.085 1.00 61.93 C ANISOU 5232 CD1 ILE D 23 9083 6487 7960 -4053 -190 1095 C ATOM 5233 N GLU D 24 35.154 43.912 0.184 1.00 64.40 N ANISOU 5233 N GLU D 24 9634 6662 8173 -3930 -672 413 N ATOM 5234 CA GLU D 24 34.568 43.486 1.452 1.00 63.03 C ANISOU 5234 CA GLU D 24 9564 6462 7921 -3823 -756 248 C ATOM 5235 C GLU D 24 33.840 44.641 2.137 1.00 63.55 C ANISOU 5235 C GLU D 24 10063 6174 7909 -3822 -757 183 C ATOM 5236 O GLU D 24 32.795 44.448 2.759 1.00 61.77 O ANISOU 5236 O GLU D 24 10016 5864 7590 -3667 -753 79 O ATOM 5237 CB GLU D 24 35.645 42.921 2.380 1.00 62.85 C ANISOU 5237 CB GLU D 24 9324 6599 7956 -3875 -877 171 C ATOM 5238 N ASN D 25 34.401 45.840 2.018 1.00 67.04 N ANISOU 5238 N ASN D 25 10670 6407 8396 -3978 -748 240 N ATOM 5239 CA ASN D 25 33.782 47.032 2.584 1.00 69.87 C ANISOU 5239 CA ASN D 25 11436 6415 8699 -3969 -720 187 C ATOM 5240 C ASN D 25 32.484 47.387 1.867 1.00 68.60 C ANISOU 5240 C ASN D 25 11510 6072 8483 -3800 -577 262 C ATOM 5241 O ASN D 25 31.517 47.820 2.495 1.00 67.09 O ANISOU 5241 O ASN D 25 11616 5657 8217 -3657 -539 176 O ATOM 5242 CB ASN D 25 34.749 48.217 2.530 1.00 75.82 C ANISOU 5242 CB ASN D 25 12282 6996 9531 -4183 -728 238 C ATOM 5243 CG ASN D 25 36.017 47.970 3.323 1.00 79.46 C ANISOU 5243 CG ASN D 25 12546 7605 10041 -4348 -868 167 C ATOM 5244 OD1 ASN D 25 37.105 48.383 2.920 1.00 81.90 O ANISOU 5244 OD1 ASN D 25 12734 7934 10449 -4527 -882 243 O ATOM 5245 ND2 ASN D 25 35.884 47.288 4.455 1.00 78.85 N ANISOU 5245 ND2 ASN D 25 12433 7632 9896 -4279 -966 29 N ATOM 5246 N VAL D 26 32.473 47.206 0.550 1.00 67.70 N ANISOU 5246 N VAL D 26 11256 6061 8405 -3800 -487 432 N ATOM 5247 CA VAL D 26 31.285 47.474 -0.252 1.00 64.98 C ANISOU 5247 CA VAL D 26 11107 5578 8006 -3630 -343 548 C ATOM 5248 C VAL D 26 30.131 46.576 0.184 1.00 61.14 C ANISOU 5248 C VAL D 26 10657 5150 7422 -3412 -339 441 C ATOM 5249 O VAL D 26 28.999 47.035 0.333 1.00 56.88 O ANISOU 5249 O VAL D 26 10418 4374 6821 -3215 -253 436 O ATOM 5250 CB VAL D 26 31.553 47.267 -1.753 1.00 63.38 C ANISOU 5250 CB VAL D 26 10690 5552 7839 -3675 -250 763 C ATOM 5251 CG1 VAL D 26 30.281 47.497 -2.554 1.00 58.70 C ANISOU 5251 CG1 VAL D 26 10295 4843 7165 -3472 -99 913 C ATOM 5252 CG2 VAL D 26 32.660 48.196 -2.227 1.00 62.19 C ANISOU 5252 CG2 VAL D 26 10513 5324 7792 -3871 -237 870 C ATOM 5253 N LYS D 27 30.429 45.295 0.389 1.00 57.50 N ANISOU 5253 N LYS D 27 9881 5006 6959 -3423 -422 358 N ATOM 5254 CA LYS D 27 29.442 44.350 0.900 1.00 55.03 C ANISOU 5254 CA LYS D 27 9570 4773 6568 -3230 -429 230 C ATOM 5255 C LYS D 27 28.977 44.767 2.290 1.00 58.35 C ANISOU 5255 C LYS D 27 10263 4975 6933 -3124 -480 50 C ATOM 5256 O LYS D 27 27.805 44.611 2.635 1.00 57.56 O ANISOU 5256 O LYS D 27 10350 4764 6758 -2899 -424 -28 O ATOM 5257 CB LYS D 27 30.015 42.932 0.946 1.00 51.45 C ANISOU 5257 CB LYS D 27 8691 4713 6143 -3265 -505 169 C ATOM 5258 CG LYS D 27 30.278 42.309 -0.413 1.00 50.73 C ANISOU 5258 CG LYS D 27 8266 4920 6089 -3272 -419 320 C ATOM 5259 CD LYS D 27 30.781 40.882 -0.262 1.00 48.50 C ANISOU 5259 CD LYS D 27 7582 4998 5848 -3286 -474 241 C ATOM 5260 CE LYS D 27 31.092 40.253 -1.608 1.00 48.63 C ANISOU 5260 CE LYS D 27 7256 5321 5901 -3289 -367 376 C ATOM 5261 NZ LYS D 27 31.553 38.845 -1.460 1.00 47.72 N ANISOU 5261 NZ LYS D 27 6743 5550 5839 -3210 -386 290 N ATOM 5262 N ALA D 28 29.906 45.295 3.082 1.00 60.49 N ANISOU 5262 N ALA D 28 10546 5199 7239 -3277 -574 -11 N ATOM 5263 CA ALA D 28 29.597 45.771 4.426 1.00 62.69 C ANISOU 5263 CA ALA D 28 11064 5298 7457 -3211 -614 -167 C ATOM 5264 C ALA D 28 28.606 46.928 4.371 1.00 65.12 C ANISOU 5264 C ALA D 28 11764 5250 7730 -3071 -484 -146 C ATOM 5265 O ALA D 28 27.675 47.001 5.175 1.00 64.05 O ANISOU 5265 O ALA D 28 11823 4992 7522 -2873 -447 -261 O ATOM 5266 CB ALA D 28 30.869 46.191 5.148 1.00 63.36 C ANISOU 5266 CB ALA D 28 11084 5403 7586 -3437 -730 -206 C ATOM 5267 N LYS D 29 28.814 47.831 3.419 1.00 67.10 N ANISOU 5267 N LYS D 29 12110 5346 8040 -3153 -399 14 N ATOM 5268 CA LYS D 29 27.893 48.938 3.200 1.00 68.94 C ANISOU 5268 CA LYS D 29 12681 5250 8262 -2992 -251 77 C ATOM 5269 C LYS D 29 26.546 48.412 2.716 1.00 68.20 C ANISOU 5269 C LYS D 29 12648 5152 8111 -2691 -141 123 C ATOM 5270 O LYS D 29 25.494 48.935 3.084 1.00 68.75 O ANISOU 5270 O LYS D 29 12968 5010 8145 -2450 -39 90 O ATOM 5271 CB LYS D 29 28.471 49.933 2.192 1.00 72.61 C ANISOU 5271 CB LYS D 29 13190 5585 8815 -3137 -178 268 C ATOM 5272 N ILE D 30 26.589 47.373 1.888 1.00 66.14 N ANISOU 5272 N ILE D 30 12141 5143 7847 -2701 -154 204 N ATOM 5273 CA ILE D 30 25.375 46.734 1.392 1.00 64.30 C ANISOU 5273 CA ILE D 30 11814 5064 7553 -2343 -55 242 C ATOM 5274 C ILE D 30 24.616 46.057 2.530 1.00 63.84 C ANISOU 5274 C ILE D 30 11809 5019 7428 -2157 -91 26 C ATOM 5275 O ILE D 30 23.385 46.064 2.556 1.00 63.47 O ANISOU 5275 O ILE D 30 11858 4924 7336 -1824 15 21 O ATOM 5276 CB ILE D 30 25.688 45.695 0.296 1.00 59.63 C ANISOU 5276 CB ILE D 30 10769 4923 6964 -2317 -58 344 C ATOM 5277 CG1 ILE D 30 26.293 46.382 -0.931 1.00 59.40 C ANISOU 5277 CG1 ILE D 30 10695 4888 6986 -2459 5 577 C ATOM 5278 CG2 ILE D 30 24.431 44.933 -0.090 1.00 49.27 C ANISOU 5278 CG2 ILE D 30 9301 3841 5579 -1930 28 345 C ATOM 5279 CD1 ILE D 30 26.699 45.427 -2.036 1.00 55.64 C ANISOU 5279 CD1 ILE D 30 9793 4838 6509 -2470 15 675 C ATOM 5280 N GLN D 31 25.359 45.476 3.468 1.00 64.76 N ANISOU 5280 N GLN D 31 11858 5204 7542 -2374 -239 -141 N ATOM 5281 CA GLN D 31 24.760 44.821 4.626 1.00 65.62 C ANISOU 5281 CA GLN D 31 11968 5380 7586 -2196 -278 -340 C ATOM 5282 C GLN D 31 23.933 45.809 5.439 1.00 69.55 C ANISOU 5282 C GLN D 31 12778 5602 8046 -2002 -191 -400 C ATOM 5283 O GLN D 31 22.850 45.480 5.922 1.00 70.87 O ANISOU 5283 O GLN D 31 13005 5761 8159 -1723 -127 -485 O ATOM 5284 CB GLN D 31 25.840 44.194 5.511 1.00 66.71 C ANISOU 5284 CB GLN D 31 11862 5751 7735 -2392 -441 -450 C ATOM 5285 CG GLN D 31 25.297 43.483 6.744 1.00 66.66 C ANISOU 5285 CG GLN D 31 11818 5845 7664 -2209 -476 -620 C ATOM 5286 CD GLN D 31 26.392 43.035 7.692 1.00 67.14 C ANISOU 5286 CD GLN D 31 11672 6094 7743 -2387 -622 -687 C ATOM 5287 OE1 GLN D 31 27.510 43.551 7.657 1.00 68.16 O ANISOU 5287 OE1 GLN D 31 11762 6213 7922 -2634 -696 -631 O ATOM 5288 NE2 GLN D 31 26.075 42.069 8.548 1.00 65.88 N ANISOU 5288 NE2 GLN D 31 11372 6108 7550 -2244 -657 -794 N ATOM 5289 N ASP D 32 24.451 47.024 5.579 1.00 73.21 N ANISOU 5289 N ASP D 32 13414 5856 8545 -2153 -179 -354 N ATOM 5290 CA ASP D 32 23.780 48.065 6.349 1.00 74.92 C ANISOU 5290 CA ASP D 32 13914 5812 8739 -2015 -88 -409 C ATOM 5291 C ASP D 32 22.473 48.500 5.692 1.00 72.95 C ANISOU 5291 C ASP D 32 13832 5391 8493 -1700 92 -304 C ATOM 5292 O ASP D 32 21.521 48.878 6.376 1.00 71.66 O ANISOU 5292 O ASP D 32 13818 5109 8300 -1476 182 -371 O ATOM 5293 CB ASP D 32 24.704 49.272 6.526 1.00 77.99 C ANISOU 5293 CB ASP D 32 14440 6017 9178 -2270 -108 -382 C ATOM 5294 N LYS D 33 22.430 48.437 4.365 1.00 71.59 N ANISOU 5294 N LYS D 33 13612 5230 8360 -1679 149 -118 N ATOM 5295 CA LYS D 33 21.274 48.910 3.610 1.00 70.88 C ANISOU 5295 CA LYS D 33 13656 4997 8281 -1372 321 38 C ATOM 5296 C LYS D 33 20.207 47.834 3.401 1.00 68.36 C ANISOU 5296 C LYS D 33 13228 4839 7906 -1064 364 22 C ATOM 5297 O LYS D 33 19.011 48.121 3.451 1.00 68.28 O ANISOU 5297 O LYS D 33 13308 4748 7886 -737 489 52 O ATOM 5298 CB LYS D 33 21.721 49.455 2.251 1.00 70.57 C ANISOU 5298 CB LYS D 33 13611 4903 8298 -1477 376 294 C ATOM 5299 N GLU D 34 20.639 46.600 3.165 1.00 65.81 N ANISOU 5299 N GLU D 34 12558 4890 7556 -1129 258 -26 N ATOM 5300 CA GLU D 34 19.709 45.530 2.818 1.00 63.96 C ANISOU 5300 CA GLU D 34 12040 4988 7275 -817 294 -36 C ATOM 5301 C GLU D 34 19.540 44.515 3.944 1.00 61.77 C ANISOU 5301 C GLU D 34 11694 4822 6953 -780 218 -276 C ATOM 5302 O GLU D 34 18.512 43.845 4.035 1.00 61.02 O ANISOU 5302 O GLU D 34 11492 4870 6821 -483 276 -328 O ATOM 5303 CB GLU D 34 20.172 44.821 1.544 1.00 63.15 C ANISOU 5303 CB GLU D 34 11529 5290 7173 -864 268 104 C ATOM 5304 N GLY D 35 20.553 44.403 4.796 1.00 61.48 N ANISOU 5304 N GLY D 35 11713 4727 6920 -1084 86 -415 N ATOM 5305 CA GLY D 35 20.505 43.475 5.910 1.00 58.32 C ANISOU 5305 CA GLY D 35 11228 4458 6475 -1068 3 -622 C ATOM 5306 C GLY D 35 21.049 42.104 5.558 1.00 55.46 C ANISOU 5306 C GLY D 35 10451 4504 6117 -1136 -86 -651 C ATOM 5307 O GLY D 35 20.940 41.164 6.345 1.00 54.42 O ANISOU 5307 O GLY D 35 10212 4511 5953 -1091 -142 -807 O ATOM 5308 N ILE D 36 21.634 41.986 4.371 1.00 53.90 N ANISOU 5308 N ILE D 36 9997 4519 5965 -1234 -87 -490 N ATOM 5309 CA ILE D 36 22.240 40.731 3.945 1.00 49.89 C ANISOU 5309 CA ILE D 36 9065 4413 5478 -1310 -149 -499 C ATOM 5310 C ILE D 36 23.719 40.693 4.309 1.00 47.51 C ANISOU 5310 C ILE D 36 8698 4125 5228 -1697 -297 -523 C ATOM 5311 O ILE D 36 24.480 41.577 3.919 1.00 45.63 O ANISOU 5311 O ILE D 36 8566 3737 5033 -1928 -320 -413 O ATOM 5312 CB ILE D 36 22.092 40.511 2.427 1.00 50.28 C ANISOU 5312 CB ILE D 36 8843 4719 5540 -1213 -61 -319 C ATOM 5313 CG1 ILE D 36 20.616 40.519 2.026 1.00 50.37 C ANISOU 5313 CG1 ILE D 36 8889 4752 5498 -833 72 -281 C ATOM 5314 CG2 ILE D 36 22.763 39.208 2.012 1.00 45.93 C ANISOU 5314 CG2 ILE D 36 7867 4566 5020 -1307 -105 -342 C ATOM 5315 CD1 ILE D 36 19.784 39.470 2.733 1.00 49.15 C ANISOU 5315 CD1 ILE D 36 8628 4740 5306 -604 84 -453 C ATOM 5316 N PRO D 37 24.129 39.665 5.065 1.00 46.57 N ANISOU 5316 N PRO D 37 8397 4186 5111 -1768 -396 -658 N ATOM 5317 CA PRO D 37 25.532 39.501 5.465 1.00 46.97 C ANISOU 5317 CA PRO D 37 8341 4289 5216 -2125 -549 -674 C ATOM 5318 C PRO D 37 26.450 39.327 4.257 1.00 46.76 C ANISOU 5318 C PRO D 37 8011 4481 5274 -2295 -542 -510 C ATOM 5319 O PRO D 37 26.041 38.734 3.259 1.00 46.14 O ANISOU 5319 O PRO D 37 7683 4646 5202 -2120 -437 -436 O ATOM 5320 CB PRO D 37 25.510 38.240 6.338 1.00 43.73 C ANISOU 5320 CB PRO D 37 7684 4128 4804 -2013 -601 -798 C ATOM 5321 CG PRO D 37 24.243 37.537 5.978 1.00 41.28 C ANISOU 5321 CG PRO D 37 7314 3931 4441 -1695 -481 -854 C ATOM 5322 CD PRO D 37 23.267 38.606 5.614 1.00 42.38 C ANISOU 5322 CD PRO D 37 7752 3817 4536 -1508 -366 -795 C ATOM 5323 N PRO D 38 27.680 39.851 4.349 1.00 48.58 N ANISOU 5323 N PRO D 38 8246 4644 5569 -2615 -642 -452 N ATOM 5324 CA PRO D 38 28.655 39.902 3.252 1.00 49.19 C ANISOU 5324 CA PRO D 38 8094 4861 5734 -2825 -634 -290 C ATOM 5325 C PRO D 38 28.998 38.538 2.658 1.00 48.10 C ANISOU 5325 C PRO D 38 7509 5117 5651 -2807 -614 -271 C ATOM 5326 O PRO D 38 29.139 38.424 1.440 1.00 47.54 O ANISOU 5326 O PRO D 38 7240 5211 5612 -2791 -515 -137 O ATOM 5327 CB PRO D 38 29.888 40.521 3.916 1.00 49.93 C ANISOU 5327 CB PRO D 38 8180 4902 5890 -2993 -735 -270 C ATOM 5328 CG PRO D 38 29.340 41.320 5.044 1.00 51.05 C ANISOU 5328 CG PRO D 38 8678 4764 5955 -2918 -760 -378 C ATOM 5329 CD PRO D 38 28.187 40.517 5.561 1.00 49.31 C ANISOU 5329 CD PRO D 38 8486 4590 5658 -2666 -726 -507 C ATOM 5330 N ASP D 39 29.134 37.524 3.506 1.00 47.21 N ANISOU 5330 N ASP D 39 7194 5189 5553 -2693 -666 -379 N ATOM 5331 CA ASP D 39 29.501 36.187 3.046 1.00 47.31 C ANISOU 5331 CA ASP D 39 6778 5559 5638 -2626 -623 -363 C ATOM 5332 C ASP D 39 28.388 35.544 2.222 1.00 42.57 C ANISOU 5332 C ASP D 39 6077 5120 4977 -2436 -490 -388 C ATOM 5333 O ASP D 39 28.606 34.540 1.543 1.00 42.48 O ANISOU 5333 O ASP D 39 5718 5404 5018 -2402 -416 -363 O ATOM 5334 CB ASP D 39 29.857 35.296 4.235 1.00 51.65 C ANISOU 5334 CB ASP D 39 7174 6218 6231 -2504 -690 -453 C ATOM 5335 CG ASP D 39 28.740 35.214 5.253 1.00 56.27 C ANISOU 5335 CG ASP D 39 7985 6680 6715 -2332 -707 -604 C ATOM 5336 OD1 ASP D 39 27.925 36.159 5.316 1.00 60.77 O ANISOU 5336 OD1 ASP D 39 8908 6995 7188 -2319 -693 -643 O ATOM 5337 OD2 ASP D 39 28.677 34.208 5.990 1.00 55.86 O ANISOU 5337 OD2 ASP D 39 7767 6767 6690 -2181 -717 -675 O ATOM 5338 N GLN D 40 27.193 36.123 2.291 1.00 37.81 N ANISOU 5338 N GLN D 40 5746 4344 4276 -2199 -426 -420 N ATOM 5339 CA GLN D 40 26.080 35.666 1.467 1.00 32.33 C ANISOU 5339 CA GLN D 40 4943 3815 3524 -1895 -276 -407 C ATOM 5340 C GLN D 40 25.905 36.591 0.269 1.00 35.49 C ANISOU 5340 C GLN D 40 5432 4154 3897 -1884 -188 -235 C ATOM 5341 O GLN D 40 24.880 36.561 -0.411 1.00 36.60 O ANISOU 5341 O GLN D 40 5567 4370 3968 -1634 -77 -198 O ATOM 5342 CB GLN D 40 24.789 35.595 2.286 1.00 31.69 C ANISOU 5342 CB GLN D 40 5064 3618 3359 -1609 -251 -541 C ATOM 5343 CG GLN D 40 24.880 34.676 3.493 1.00 29.91 C ANISOU 5343 CG GLN D 40 4766 3452 3147 -1601 -329 -707 C ATOM 5344 CD GLN D 40 23.565 34.553 4.236 1.00 34.75 C ANISOU 5344 CD GLN D 40 5561 3963 3678 -1306 -282 -837 C ATOM 5345 OE1 GLN D 40 22.491 34.651 3.644 1.00 28.32 O ANISOU 5345 OE1 GLN D 40 4776 3171 2815 -1053 -164 -811 O ATOM 5346 NE2 GLN D 40 23.645 34.339 5.544 1.00 30.48 N ANISOU 5346 NE2 GLN D 40 5141 3318 3120 -1339 -373 -971 N ATOM 5347 N GLN D 41 26.917 37.415 0.020 1.00 36.00 N ANISOU 5347 N GLN D 41 5574 4085 4018 -2161 -241 -122 N ATOM 5348 CA GLN D 41 26.901 38.331 -1.112 1.00 38.95 C ANISOU 5348 CA GLN D 41 6033 4391 4375 -2183 -160 61 C ATOM 5349 C GLN D 41 27.988 37.989 -2.122 1.00 41.14 C ANISOU 5349 C GLN D 41 6010 4894 4725 -2398 -133 182 C ATOM 5350 O GLN D 41 29.034 37.443 -1.769 1.00 40.98 O ANISOU 5350 O GLN D 41 5799 4973 4797 -2618 -210 145 O ATOM 5351 CB GLN D 41 27.083 39.776 -0.647 1.00 41.25 C ANISOU 5351 CB GLN D 41 6716 4285 4672 -2316 -212 108 C ATOM 5352 CG GLN D 41 26.035 40.274 0.327 1.00 42.67 C ANISOU 5352 CG GLN D 41 7234 4195 4785 -2116 -215 -2 C ATOM 5353 CD GLN D 41 26.289 41.707 0.753 1.00 45.80 C ANISOU 5353 CD GLN D 41 8022 4186 5195 -2273 -246 39 C ATOM 5354 OE1 GLN D 41 26.826 42.507 -0.015 1.00 45.68 O ANISOU 5354 OE1 GLN D 41 8057 4079 5218 -2426 -214 198 O ATOM 5355 NE2 GLN D 41 25.915 42.037 1.984 1.00 45.46 N ANISOU 5355 NE2 GLN D 41 8263 3891 5120 -2244 -299 -109 N ATOM 5356 N ARG D 42 27.727 38.318 -3.381 1.00 38.48 N ANISOU 5356 N ARG D 42 5632 4643 4345 -2332 -19 335 N ATOM 5357 CA ARG D 42 28.726 38.218 -4.435 1.00 39.20 C ANISOU 5357 CA ARG D 42 5494 4905 4493 -2541 28 473 C ATOM 5358 C ARG D 42 28.655 39.461 -5.311 1.00 41.58 C ANISOU 5358 C ARG D 42 6001 5040 4758 -2571 91 669 C ATOM 5359 O ARG D 42 27.578 39.842 -5.767 1.00 41.68 O ANISOU 5359 O ARG D 42 6145 5022 4669 -2328 167 729 O ATOM 5360 CB ARG D 42 28.516 36.960 -5.279 1.00 37.03 C ANISOU 5360 CB ARG D 42 4858 5021 4191 -2421 135 454 C ATOM 5361 CG ARG D 42 28.666 35.654 -4.516 1.00 41.45 C ANISOU 5361 CG ARG D 42 5181 5762 4808 -2398 98 278 C ATOM 5362 CD ARG D 42 30.054 35.516 -3.913 1.00 43.92 C ANISOU 5362 CD ARG D 42 5387 6039 5262 -2703 -7 268 C ATOM 5363 NE ARG D 42 30.307 34.158 -3.439 1.00 43.16 N ANISOU 5363 NE ARG D 42 5026 6138 5233 -2545 -12 135 N ATOM 5364 CZ ARG D 42 29.980 33.714 -2.229 1.00 42.00 C ANISOU 5364 CZ ARG D 42 4928 5939 5090 -2467 -95 -7 C ATOM 5365 NH1 ARG D 42 30.249 32.461 -1.887 1.00 39.48 N ANISOU 5365 NH1 ARG D 42 4394 5763 4843 -2259 -77 -87 N ATOM 5366 NH2 ARG D 42 29.383 34.521 -1.362 1.00 40.80 N ANISOU 5366 NH2 ARG D 42 5092 5539 4870 -2526 -188 -63 N ATOM 5367 N LEU D 43 29.799 40.098 -5.536 1.00 43.63 N ANISOU 5367 N LEU D 43 6283 5189 5105 -2867 60 777 N ATOM 5368 CA LEU D 43 29.851 41.265 -6.408 1.00 48.80 C ANISOU 5368 CA LEU D 43 7118 5685 5739 -2919 131 978 C ATOM 5369 C LEU D 43 30.553 40.930 -7.718 1.00 48.78 C ANISOU 5369 C LEU D 43 6838 5946 5752 -3044 227 1123 C ATOM 5370 O LEU D 43 31.658 40.387 -7.722 1.00 48.69 O ANISOU 5370 O LEU D 43 6591 6064 5843 -3276 199 1107 O ATOM 5371 CB LEU D 43 30.547 42.430 -5.707 1.00 52.44 C ANISOU 5371 CB LEU D 43 7868 5773 6283 -3164 42 1002 C ATOM 5372 CG LEU D 43 29.720 43.076 -4.594 1.00 53.11 C ANISOU 5372 CG LEU D 43 8313 5538 6330 -3027 -13 892 C ATOM 5373 CD1 LEU D 43 30.498 44.191 -3.918 1.00 51.89 C ANISOU 5373 CD1 LEU D 43 8437 5022 6256 -3309 -94 899 C ATOM 5374 CD2 LEU D 43 28.399 43.596 -5.149 1.00 49.35 C ANISOU 5374 CD2 LEU D 43 8015 4989 5746 -2707 103 985 C ATOM 5375 N ILE D 44 29.901 41.253 -8.828 1.00 48.67 N ANISOU 5375 N ILE D 44 6848 6012 5631 -2887 344 1272 N ATOM 5376 CA ILE D 44 30.420 40.913 -10.146 1.00 48.77 C ANISOU 5376 CA ILE D 44 6611 6294 5624 -2977 454 1408 C ATOM 5377 C ILE D 44 30.577 42.152 -11.020 1.00 51.61 C ANISOU 5377 C ILE D 44 7162 6488 5958 -3051 522 1645 C ATOM 5378 O ILE D 44 29.718 43.034 -11.023 1.00 51.02 O ANISOU 5378 O ILE D 44 7361 6210 5814 -2879 537 1726 O ATOM 5379 CB ILE D 44 29.503 39.902 -10.861 1.00 46.28 C ANISOU 5379 CB ILE D 44 6080 6330 5176 -2724 546 1368 C ATOM 5380 CG1 ILE D 44 29.172 38.733 -9.930 1.00 43.46 C ANISOU 5380 CG1 ILE D 44 5570 6100 4841 -2613 489 1133 C ATOM 5381 CG2 ILE D 44 30.148 39.410 -12.147 1.00 45.16 C ANISOU 5381 CG2 ILE D 44 5663 6484 5011 -2849 664 1474 C ATOM 5382 CD1 ILE D 44 28.255 37.702 -10.548 1.00 41.09 C ANISOU 5382 CD1 ILE D 44 5058 6133 4420 -2377 580 1068 C ATOM 5383 N PHE D 45 31.681 42.212 -11.759 1.00 52.10 N ANISOU 5383 N PHE D 45 7075 6635 6086 -3302 574 1762 N ATOM 5384 CA PHE D 45 31.949 43.331 -12.656 1.00 55.61 C ANISOU 5384 CA PHE D 45 7669 6940 6519 -3371 649 1985 C ATOM 5385 C PHE D 45 32.795 42.888 -13.844 1.00 56.07 C ANISOU 5385 C PHE D 45 7435 7256 6612 -3381 737 2013 C ATOM 5386 O PHE D 45 33.832 42.247 -13.673 1.00 53.76 O ANISOU 5386 O PHE D 45 6917 7052 6458 -3445 700 1871 O ATOM 5387 CB PHE D 45 32.649 44.468 -11.907 1.00 58.33 C ANISOU 5387 CB PHE D 45 8264 6892 7005 -3546 566 1991 C ATOM 5388 N ALA D 46 32.342 43.234 -15.045 1.00 57.39 N ANISOU 5388 N ALA D 46 7628 7530 6650 -3292 855 2197 N ATOM 5389 CA ALA D 46 33.049 42.882 -16.272 1.00 58.27 C ANISOU 5389 CA ALA D 46 7511 7858 6771 -3291 952 2227 C ATOM 5390 C ALA D 46 33.212 41.372 -16.412 1.00 56.80 C ANISOU 5390 C ALA D 46 7001 7982 6596 -3186 960 2014 C ATOM 5391 O ALA D 46 34.254 40.889 -16.856 1.00 56.50 O ANISOU 5391 O ALA D 46 6772 8024 6670 -3225 991 1940 O ATOM 5392 CB ALA D 46 34.408 43.568 -16.317 1.00 58.25 C ANISOU 5392 CB ALA D 46 7523 7661 6949 -3487 946 2262 C ATOM 5393 N GLY D 47 32.176 40.633 -16.025 1.00 55.15 N ANISOU 5393 N GLY D 47 6750 7924 6281 -3032 939 1915 N ATOM 5394 CA GLY D 47 32.174 39.188 -16.163 1.00 53.65 C ANISOU 5394 CA GLY D 47 6286 7999 6100 -2890 952 1703 C ATOM 5395 C GLY D 47 33.063 38.477 -15.163 1.00 54.61 C ANISOU 5395 C GLY D 47 6280 8058 6413 -2937 862 1507 C ATOM 5396 O GLY D 47 33.318 37.281 -15.294 1.00 54.22 O ANISOU 5396 O GLY D 47 6024 8163 6415 -2808 876 1340 O ATOM 5397 N LYS D 48 33.536 39.212 -14.161 1.00 56.00 N ANISOU 5397 N LYS D 48 6602 7982 6695 -3100 764 1527 N ATOM 5398 CA LYS D 48 34.405 38.643 -13.136 1.00 54.39 C ANISOU 5398 CA LYS D 48 6291 7711 6663 -3134 662 1359 C ATOM 5399 C LYS D 48 33.843 38.867 -11.739 1.00 50.68 C ANISOU 5399 C LYS D 48 5984 7083 6187 -3175 539 1290 C ATOM 5400 O LYS D 48 33.302 39.931 -11.439 1.00 50.71 O ANISOU 5400 O LYS D 48 6261 6876 6128 -3273 512 1404 O ATOM 5401 CB LYS D 48 35.812 39.238 -13.227 1.00 57.98 C ANISOU 5401 CB LYS D 48 6736 8014 7279 -3297 646 1413 C ATOM 5402 CG LYS D 48 36.703 38.614 -14.294 1.00 61.01 C ANISOU 5402 CG LYS D 48 6904 8542 7734 -3240 752 1403 C ATOM 5403 CD LYS D 48 37.011 37.150 -13.993 1.00 60.79 C ANISOU 5403 CD LYS D 48 6661 8646 7793 -3067 745 1214 C ATOM 5404 CE LYS D 48 35.976 36.217 -14.608 1.00 59.86 C ANISOU 5404 CE LYS D 48 6469 8736 7537 -2862 817 1145 C ATOM 5405 NZ LYS D 48 36.216 34.793 -14.237 1.00 58.32 N ANISOU 5405 NZ LYS D 48 6114 8605 7441 -2677 809 966 N ATOM 5406 N GLN D 49 33.975 37.856 -10.887 1.00 47.54 N ANISOU 5406 N GLN D 49 5448 6756 5860 -3082 470 1106 N ATOM 5407 CA GLN D 49 33.549 37.972 -9.500 1.00 44.03 C ANISOU 5407 CA GLN D 49 5147 6164 5419 -3119 346 1014 C ATOM 5408 C GLN D 49 34.618 38.694 -8.688 1.00 51.30 C ANISOU 5408 C GLN D 49 6171 6845 6475 -3292 227 1010 C ATOM 5409 O GLN D 49 35.760 38.242 -8.609 1.00 46.22 O ANISOU 5409 O GLN D 49 5348 6246 5968 -3289 207 959 O ATOM 5410 CB GLN D 49 33.262 36.594 -8.906 1.00 41.27 C ANISOU 5410 CB GLN D 49 4610 5985 5085 -2927 326 826 C ATOM 5411 CG GLN D 49 32.610 36.635 -7.536 1.00 42.19 C ANISOU 5411 CG GLN D 49 4876 5978 5175 -2942 215 723 C ATOM 5412 CD GLN D 49 32.281 35.252 -7.012 1.00 39.54 C ANISOU 5412 CD GLN D 49 4353 5815 4853 -2727 213 549 C ATOM 5413 OE1 GLN D 49 31.272 34.656 -7.389 1.00 37.76 O ANISOU 5413 OE1 GLN D 49 4062 5761 4525 -2575 296 505 O ATOM 5414 NE2 GLN D 49 33.135 34.731 -6.139 1.00 37.33 N ANISOU 5414 NE2 GLN D 49 3993 5487 4703 -2696 126 458 N ATOM 5415 N LEU D 50 34.243 39.818 -8.089 1.00 51.66 N ANISOU 5415 N LEU D 50 6525 6619 6484 -3426 158 1063 N ATOM 5416 CA LEU D 50 35.189 40.649 -7.355 1.00 53.32 C ANISOU 5416 CA LEU D 50 6865 6590 6806 -3590 48 1053 C ATOM 5417 C LEU D 50 35.623 39.995 -6.046 1.00 55.01 C ANISOU 5417 C LEU D 50 6998 6813 7092 -3559 -85 878 C ATOM 5418 O LEU D 50 34.790 39.615 -5.222 1.00 52.91 O ANISOU 5418 O LEU D 50 6814 6531 6756 -3479 -140 770 O ATOM 5419 CB LEU D 50 34.579 42.023 -7.078 1.00 53.08 C ANISOU 5419 CB LEU D 50 7229 6225 6713 -3697 24 1138 C ATOM 5420 CG LEU D 50 33.973 42.732 -8.291 1.00 54.15 C ANISOU 5420 CG LEU D 50 7497 6319 6758 -3687 164 1345 C ATOM 5421 CD1 LEU D 50 33.430 44.095 -7.897 1.00 56.41 C ANISOU 5421 CD1 LEU D 50 8209 6217 7009 -3741 149 1424 C ATOM 5422 CD2 LEU D 50 34.995 42.858 -9.412 1.00 54.08 C ANISOU 5422 CD2 LEU D 50 7291 6431 6824 -3749 248 1457 C ATOM 5423 N GLU D 51 36.933 39.869 -5.862 1.00 57.56 N ANISOU 5423 N GLU D 51 7161 7158 7550 -3615 -126 858 N ATOM 5424 CA GLU D 51 37.482 39.273 -4.650 1.00 58.24 C ANISOU 5424 CA GLU D 51 7160 7262 7707 -3581 -242 724 C ATOM 5425 C GLU D 51 37.373 40.241 -3.477 1.00 62.75 C ANISOU 5425 C GLU D 51 8020 7575 8248 -3713 -379 674 C ATOM 5426 O GLU D 51 37.567 41.446 -3.636 1.00 66.03 O ANISOU 5426 O GLU D 51 8642 7780 8667 -3871 -387 750 O ATOM 5427 CB GLU D 51 38.939 38.860 -4.864 1.00 58.06 C ANISOU 5427 CB GLU D 51 6887 7331 7841 -3597 -228 736 C ATOM 5428 N ASP D 52 37.064 39.702 -2.301 1.00 64.37 N ANISOU 5428 N ASP D 52 8246 7788 8424 -3635 -475 542 N ATOM 5429 CA ASP D 52 36.852 40.510 -1.104 1.00 69.36 C ANISOU 5429 CA ASP D 52 9166 8182 9005 -3726 -599 465 C ATOM 5430 C ASP D 52 38.078 41.340 -0.728 1.00 72.85 C ANISOU 5430 C ASP D 52 9644 8500 9535 -3914 -675 490 C ATOM 5431 O ASP D 52 37.950 42.453 -0.214 1.00 74.02 O ANISOU 5431 O ASP D 52 10081 8398 9644 -4037 -731 474 O ATOM 5432 CB ASP D 52 36.455 39.617 0.074 1.00 70.11 C ANISOU 5432 CB ASP D 52 9224 8353 9061 -3591 -678 321 C ATOM 5433 CG ASP D 52 35.115 38.936 -0.135 1.00 69.56 C ANISOU 5433 CG ASP D 52 9170 8365 8894 -3420 -611 274 C ATOM 5434 OD1 ASP D 52 34.384 39.337 -1.065 1.00 69.92 O ANISOU 5434 OD1 ASP D 52 9318 8369 8880 -3429 -518 353 O ATOM 5435 OD2 ASP D 52 34.789 38.007 0.635 1.00 68.12 O ANISOU 5435 OD2 ASP D 52 8898 8289 8696 -3278 -646 166 O ATOM 5436 N GLY D 53 39.262 40.797 -0.990 1.00 74.92 N ANISOU 5436 N GLY D 53 9620 8925 9921 -3928 -666 522 N ATOM 5437 CA GLY D 53 40.502 41.459 -0.629 1.00 79.82 C ANISOU 5437 CA GLY D 53 10233 9461 10634 -4109 -738 542 C ATOM 5438 C GLY D 53 40.860 42.644 -1.507 1.00 84.56 C ANISOU 5438 C GLY D 53 10949 9905 11273 -4277 -677 658 C ATOM 5439 O GLY D 53 41.432 43.625 -1.031 1.00 88.86 O ANISOU 5439 O GLY D 53 11642 10273 11847 -4454 -747 656 O ATOM 5440 N ARG D 54 40.524 42.558 -2.790 1.00 83.81 N ANISOU 5440 N ARG D 54 10789 9877 11177 -4221 -541 761 N ATOM 5441 CA ARG D 54 40.890 43.598 -3.747 1.00 84.90 C ANISOU 5441 CA ARG D 54 11012 9887 11360 -4361 -459 893 C ATOM 5442 C ARG D 54 40.056 44.865 -3.549 1.00 83.62 C ANISOU 5442 C ARG D 54 11233 9427 11110 -4444 -467 916 C ATOM 5443 O ARG D 54 39.110 44.879 -2.762 1.00 80.47 O ANISOU 5443 O ARG D 54 11035 8931 10609 -4376 -524 826 O ATOM 5444 CB ARG D 54 40.733 43.082 -5.181 1.00 85.31 C ANISOU 5444 CB ARG D 54 10884 10113 11418 -4261 -302 1001 C ATOM 5445 CG ARG D 54 41.348 41.708 -5.436 1.00 85.06 C ANISOU 5445 CG ARG D 54 10501 10353 11464 -4122 -261 959 C ATOM 5446 CD ARG D 54 42.827 41.659 -5.073 1.00 87.68 C ANISOU 5446 CD ARG D 54 10668 10698 11948 -4220 -311 941 C ATOM 5447 NE ARG D 54 43.043 41.548 -3.633 1.00 88.67 N ANISOU 5447 NE ARG D 54 10836 10779 12074 -4250 -466 829 N ATOM 5448 N THR D 55 40.417 45.925 -4.268 1.00 83.91 N ANISOU 5448 N THR D 55 11380 9305 11197 -4576 -396 1037 N ATOM 5449 CA THR D 55 39.726 47.209 -4.165 1.00 82.85 C ANISOU 5449 CA THR D 55 11621 8851 11006 -4640 -374 1075 C ATOM 5450 C THR D 55 39.023 47.574 -5.469 1.00 81.57 C ANISOU 5450 C THR D 55 11541 8652 10801 -4578 -215 1247 C ATOM 5451 O THR D 55 39.131 46.853 -6.461 1.00 78.67 O ANISOU 5451 O THR D 55 10930 8522 10439 -4507 -128 1329 O ATOM 5452 CB THR D 55 40.701 48.344 -3.798 1.00 84.40 C ANISOU 5452 CB THR D 55 11932 8835 11300 -4851 -417 1077 C ATOM 5453 OG1 THR D 55 41.547 48.632 -4.918 1.00 84.99 O ANISOU 5453 OG1 THR D 55 11852 8957 11482 -4940 -316 1221 O ATOM 5454 CG2 THR D 55 41.557 47.951 -2.605 1.00 83.86 C ANISOU 5454 CG2 THR D 55 11743 8845 11274 -4926 -571 934 C ATOM 5455 N LEU D 56 38.300 48.692 -5.464 1.00 83.09 N ANISOU 5455 N LEU D 56 12081 8544 10946 -4588 -167 1304 N ATOM 5456 CA LEU D 56 37.685 49.201 -6.687 1.00 84.25 C ANISOU 5456 CA LEU D 56 12331 8625 11053 -4525 -9 1501 C ATOM 5457 C LEU D 56 38.767 49.531 -7.707 1.00 90.05 C ANISOU 5457 C LEU D 56 12889 9427 11898 -4647 74 1638 C ATOM 5458 O LEU D 56 38.617 49.262 -8.899 1.00 89.84 O ANISOU 5458 O LEU D 56 12738 9557 11842 -4579 196 1784 O ATOM 5459 CB LEU D 56 36.830 50.441 -6.405 1.00 82.37 C ANISOU 5459 CB LEU D 56 12513 8012 10773 -4494 37 1541 C ATOM 5460 CG LEU D 56 35.444 50.263 -5.777 1.00 77.49 C ANISOU 5460 CG LEU D 56 12131 7285 10028 -4309 26 1466 C ATOM 5461 CD1 LEU D 56 35.534 49.597 -4.414 1.00 75.22 C ANISOU 5461 CD1 LEU D 56 11803 7055 9721 -4318 -132 1229 C ATOM 5462 CD2 LEU D 56 34.733 51.607 -5.675 1.00 78.95 C ANISOU 5462 CD2 LEU D 56 12719 7078 10201 -4250 111 1534 C ATOM 5463 N SER D 57 39.861 50.113 -7.225 1.00 97.93 N ANISOU 5463 N SER D 57 13879 10312 13017 -4825 12 1588 N ATOM 5464 CA SER D 57 40.997 50.440 -8.077 1.00101.80 C ANISOU 5464 CA SER D 57 14202 10848 13632 -4953 86 1700 C ATOM 5465 C SER D 57 41.666 49.179 -8.617 1.00100.18 C ANISOU 5465 C SER D 57 13604 10997 13464 -4902 99 1687 C ATOM 5466 O SER D 57 42.181 49.175 -9.734 1.00102.04 O ANISOU 5466 O SER D 57 13689 11330 13750 -4919 219 1813 O ATOM 5467 CB SER D 57 42.013 51.291 -7.313 1.00107.89 C ANISOU 5467 CB SER D 57 15045 11423 14524 -5159 5 1630 C ATOM 5468 OG SER D 57 42.421 50.650 -6.117 1.00109.74 O ANISOU 5468 OG SER D 57 15175 11757 14766 -5187 -157 1445 O ATOM 5469 N ASP D 58 41.657 48.112 -7.823 1.00 97.02 N ANISOU 5469 N ASP D 58 13047 10777 13040 -4826 -11 1534 N ATOM 5470 CA ASP D 58 42.235 46.838 -8.246 1.00 93.13 C ANISOU 5470 CA ASP D 58 12193 10601 12590 -4738 13 1504 C ATOM 5471 C ASP D 58 41.527 46.299 -9.485 1.00 87.46 C ANISOU 5471 C ASP D 58 11386 10060 11785 -4589 157 1610 C ATOM 5472 O ASP D 58 42.131 45.612 -10.309 1.00 85.01 O ANISOU 5472 O ASP D 58 10817 9957 11527 -4541 243 1641 O ATOM 5473 CB ASP D 58 42.168 45.810 -7.114 1.00 91.72 C ANISOU 5473 CB ASP D 58 11899 10558 12392 -4649 -120 1330 C ATOM 5474 CG ASP D 58 43.120 46.128 -5.978 1.00 93.71 C ANISOU 5474 CG ASP D 58 12157 10714 12735 -4792 -258 1231 C ATOM 5475 OD1 ASP D 58 43.633 47.266 -5.931 1.00 97.00 O ANISOU 5475 OD1 ASP D 58 12722 10920 13212 -4968 -264 1278 O ATOM 5476 OD2 ASP D 58 43.352 45.242 -5.128 1.00 92.03 O ANISOU 5476 OD2 ASP D 58 11800 10638 12530 -4726 -356 1111 O ATOM 5477 N TYR D 59 40.242 46.618 -9.608 1.00 84.39 N ANISOU 5477 N TYR D 59 11223 9582 11258 -4509 189 1664 N ATOM 5478 CA TYR D 59 39.458 46.200 -10.762 1.00 80.53 C ANISOU 5478 CA TYR D 59 10676 9263 10658 -4370 323 1778 C ATOM 5479 C TYR D 59 39.151 47.390 -11.664 1.00 82.93 C ANISOU 5479 C TYR D 59 11200 9383 10927 -4415 444 1983 C ATOM 5480 O TYR D 59 38.390 47.274 -12.625 1.00 83.26 O ANISOU 5480 O TYR D 59 11251 9533 10850 -4300 558 2111 O ATOM 5481 CB TYR D 59 38.163 45.520 -10.317 1.00 74.71 C ANISOU 5481 CB TYR D 59 10000 8608 9780 -4212 288 1704 C ATOM 5482 CG TYR D 59 38.384 44.248 -9.531 1.00 69.37 C ANISOU 5482 CG TYR D 59 9091 8134 9132 -4133 193 1515 C ATOM 5483 CD1 TYR D 59 38.847 43.097 -10.155 1.00 66.96 C ANISOU 5483 CD1 TYR D 59 8461 8118 8860 -4030 256 1480 C ATOM 5484 CD2 TYR D 59 38.123 44.194 -8.169 1.00 68.82 C ANISOU 5484 CD2 TYR D 59 9143 7950 9057 -4140 51 1370 C ATOM 5485 CE1 TYR D 59 39.049 41.930 -9.443 1.00 65.30 C ANISOU 5485 CE1 TYR D 59 8053 8067 8690 -3926 187 1318 C ATOM 5486 CE2 TYR D 59 38.320 43.031 -7.448 1.00 66.74 C ANISOU 5486 CE2 TYR D 59 8670 7870 8819 -4048 -27 1214 C ATOM 5487 CZ TYR D 59 38.783 41.902 -8.091 1.00 64.88 C ANISOU 5487 CZ TYR D 59 8112 7909 8628 -3935 45 1196 C ATOM 5488 OH TYR D 59 38.982 40.742 -7.378 1.00 62.39 O ANISOU 5488 OH TYR D 59 7604 7747 8352 -3815 -15 1052 O ATOM 5489 N ASN D 60 39.748 48.533 -11.337 1.00 84.12 N ANISOU 5489 N ASN D 60 11524 9260 11177 -4572 421 2017 N ATOM 5490 CA ASN D 60 39.627 49.740 -12.148 1.00 84.57 C ANISOU 5490 CA ASN D 60 11786 9110 11235 -4617 544 2216 C ATOM 5491 C ASN D 60 38.176 50.191 -12.306 1.00 81.72 C ANISOU 5491 C ASN D 60 11708 8618 10726 -4470 600 2325 C ATOM 5492 O ASN D 60 37.776 50.671 -13.367 1.00 79.45 O ANISOU 5492 O ASN D 60 11494 8318 10374 -4402 737 2527 O ATOM 5493 CB ASN D 60 40.262 49.515 -13.522 1.00 86.21 C ANISOU 5493 CB ASN D 60 11772 9516 11468 -4621 685 2350 C ATOM 5494 CG ASN D 60 40.937 50.760 -14.065 1.00 91.75 C ANISOU 5494 CG ASN D 60 12595 9994 12271 -4760 776 2501 C ATOM 5495 OD1 ASN D 60 40.481 51.880 -13.834 1.00 94.02 O ANISOU 5495 OD1 ASN D 60 13181 9987 12557 -4786 792 2582 O ATOM 5496 ND2 ASN D 60 42.036 50.570 -14.786 1.00 93.42 N ANISOU 5496 ND2 ASN D 60 12581 10332 12582 -4839 847 2535 N ATOM 5497 N ILE D 61 37.395 50.030 -11.242 1.00 80.53 N ANISOU 5497 N ILE D 61 11714 8367 10516 -4404 497 2195 N ATOM 5498 CA ILE D 61 35.986 50.408 -11.251 1.00 79.38 C ANISOU 5498 CA ILE D 61 11849 8076 10237 -4233 547 2281 C ATOM 5499 C ILE D 61 35.804 51.903 -10.996 1.00 83.67 C ANISOU 5499 C ILE D 61 12752 8208 10833 -4263 588 2363 C ATOM 5500 O ILE D 61 36.492 52.488 -10.158 1.00 85.21 O ANISOU 5500 O ILE D 61 13036 8197 11144 -4416 510 2245 O ATOM 5501 CB ILE D 61 35.188 49.613 -10.199 1.00 73.10 C ANISOU 5501 CB ILE D 61 11091 7323 9361 -4132 437 2098 C ATOM 5502 CG1 ILE D 61 35.190 48.122 -10.546 1.00 67.78 C ANISOU 5502 CG1 ILE D 61 10065 7060 8629 -4064 425 2034 C ATOM 5503 CG2 ILE D 61 33.765 50.138 -10.097 1.00 71.46 C ANISOU 5503 CG2 ILE D 61 11214 6904 9034 -3940 493 2181 C ATOM 5504 CD1 ILE D 61 34.401 47.270 -9.578 1.00 62.48 C ANISOU 5504 CD1 ILE D 61 9405 6452 7883 -3961 332 1863 C ATOM 5505 N GLN D 62 34.870 52.513 -11.721 1.00 87.32 N ANISOU 5505 N GLN D 62 13410 8561 11208 -4102 714 2566 N ATOM 5506 CA GLN D 62 34.659 53.957 -11.654 1.00 92.68 C ANISOU 5506 CA GLN D 62 14412 8852 11949 -4090 788 2676 C ATOM 5507 C GLN D 62 33.213 54.328 -11.323 1.00 94.57 C ANISOU 5507 C GLN D 62 14954 8891 12087 -3840 827 2718 C ATOM 5508 O GLN D 62 32.361 53.458 -11.137 1.00 91.66 O ANISOU 5508 O GLN D 62 14551 8685 11591 -3683 792 2664 O ATOM 5509 CB GLN D 62 35.070 54.611 -12.976 1.00 95.02 C ANISOU 5509 CB GLN D 62 14663 9163 12278 -4114 936 2930 C ATOM 5510 N LYS D 63 32.948 55.631 -11.265 1.00 98.64 N ANISOU 5510 N LYS D 63 15756 9054 12670 -3792 909 2818 N ATOM 5511 CA LYS D 63 31.648 56.156 -10.850 1.00 99.79 C ANISOU 5511 CA LYS D 63 16203 8954 12758 -3537 958 2846 C ATOM 5512 C LYS D 63 30.514 55.866 -11.834 1.00 99.83 C ANISOU 5512 C LYS D 63 16195 9128 12608 -3249 1058 3073 C ATOM 5513 O LYS D 63 30.724 55.802 -13.047 1.00101.12 O ANISOU 5513 O LYS D 63 16199 9498 12726 -3245 1137 3287 O ATOM 5514 CB LYS D 63 31.746 57.667 -10.626 1.00103.45 C ANISOU 5514 CB LYS D 63 16940 9008 13356 -3560 1037 2905 C ATOM 5515 N GLU D 64 29.314 55.691 -11.283 1.00 98.88 N ANISOU 5515 N GLU D 64 16237 8931 12401 -3000 1053 3020 N ATOM 5516 CA GLU D 64 28.082 55.515 -12.055 1.00 99.12 C ANISOU 5516 CA GLU D 64 16285 9095 12283 -2677 1141 3226 C ATOM 5517 C GLU D 64 28.010 54.176 -12.787 1.00 96.88 C ANISOU 5517 C GLU D 64 15700 9279 11832 -2663 1110 3261 C ATOM 5518 O GLU D 64 27.015 53.878 -13.447 1.00 96.73 O ANISOU 5518 O GLU D 64 15641 9448 11663 -2396 1164 3410 O ATOM 5519 CB GLU D 64 27.913 56.662 -13.056 1.00103.14 C ANISOU 5519 CB GLU D 64 16885 9476 12829 -2571 1279 3527 C ATOM 5520 N SER D 65 29.061 53.372 -12.670 1.00 95.08 N ANISOU 5520 N SER D 65 15225 9262 11637 -2931 1021 3112 N ATOM 5521 CA SER D 65 29.062 52.040 -13.262 1.00 91.55 C ANISOU 5521 CA SER D 65 14444 9283 11060 -2923 990 3093 C ATOM 5522 C SER D 65 28.203 51.100 -12.426 1.00 84.20 C ANISOU 5522 C SER D 65 13431 8493 10068 -2698 901 2854 C ATOM 5523 O SER D 65 28.083 51.273 -11.214 1.00 81.82 O ANISOU 5523 O SER D 65 13316 7933 9838 -2712 832 2669 O ATOM 5524 CB SER D 65 30.487 51.500 -13.386 1.00 93.24 C ANISOU 5524 CB SER D 65 14377 9681 11370 -3238 936 2992 C ATOM 5525 OG SER D 65 31.236 52.260 -14.319 1.00 97.31 O ANISOU 5525 OG SER D 65 14855 10163 11956 -3338 1028 3169 O ATOM 5526 N THR D 66 27.601 50.109 -13.074 1.00 80.06 N ANISOU 5526 N THR D 66 12633 8379 9407 -2498 908 2856 N ATOM 5527 CA THR D 66 26.692 49.200 -12.387 1.00 75.71 C ANISOU 5527 CA THR D 66 11993 7981 8794 -2261 842 2648 C ATOM 5528 C THR D 66 27.362 47.874 -12.043 1.00 71.37 C ANISOU 5528 C THR D 66 11130 7728 8261 -2415 753 2422 C ATOM 5529 O THR D 66 27.829 47.153 -12.925 1.00 69.36 O ANISOU 5529 O THR D 66 10585 7814 7955 -2499 783 2466 O ATOM 5530 CB THR D 66 25.434 48.919 -13.231 1.00 75.17 C ANISOU 5530 CB THR D 66 11828 8171 8563 -1913 905 2778 C ATOM 5531 N LEU D 67 27.408 47.564 -10.751 1.00 68.50 N ANISOU 5531 N LEU D 67 10830 7228 7968 -2449 653 2184 N ATOM 5532 CA LEU D 67 27.941 46.290 -10.282 1.00 62.97 C ANISOU 5532 CA LEU D 67 9844 6790 7292 -2561 566 1968 C ATOM 5533 C LEU D 67 26.814 45.279 -10.123 1.00 59.44 C ANISOU 5533 C LEU D 67 9249 6596 6739 -2254 560 1838 C ATOM 5534 O LEU D 67 25.690 45.640 -9.774 1.00 60.43 O ANISOU 5534 O LEU D 67 9565 6580 6814 -1989 576 1834 O ATOM 5535 CB LEU D 67 28.687 46.463 -8.956 1.00 60.58 C ANISOU 5535 CB LEU D 67 9674 6225 7118 -2789 450 1788 C ATOM 5536 CG LEU D 67 29.940 47.341 -8.959 1.00 62.01 C ANISOU 5536 CG LEU D 67 9970 6169 7423 -3145 434 1876 C ATOM 5537 CD1 LEU D 67 30.657 47.258 -7.617 1.00 61.50 C ANISOU 5537 CD1 LEU D 67 9974 5931 7462 -3374 294 1670 C ATOM 5538 CD2 LEU D 67 30.876 46.956 -10.096 1.00 59.34 C ANISOU 5538 CD2 LEU D 67 9339 6107 7102 -3333 488 2011 C ATOM 5539 N HIS D 68 27.114 44.011 -10.383 1.00 55.65 N ANISOU 5539 N HIS D 68 8427 6483 6235 -2291 548 1732 N ATOM 5540 CA HIS D 68 26.111 42.959 -10.279 1.00 51.96 C ANISOU 5540 CA HIS D 68 7792 6278 5674 -2025 550 1598 C ATOM 5541 C HIS D 68 26.160 42.276 -8.917 1.00 49.35 C ANISOU 5541 C HIS D 68 7445 5893 5414 -2034 449 1341 C ATOM 5542 O HIS D 68 27.200 41.761 -8.507 1.00 49.33 O ANISOU 5542 O HIS D 68 7297 5942 5506 -2272 388 1242 O ATOM 5543 CB HIS D 68 26.302 41.925 -11.390 1.00 51.40 C ANISOU 5543 CB HIS D 68 7361 6643 5525 -2040 619 1625 C ATOM 5544 CG HIS D 68 26.061 42.463 -12.766 1.00 55.29 C ANISOU 5544 CG HIS D 68 7854 7247 5907 -1989 719 1871 C ATOM 5545 ND1 HIS D 68 24.832 42.396 -13.386 1.00 55.15 N ANISOU 5545 ND1 HIS D 68 7825 7392 5737 -1702 770 1949 N ATOM 5546 CD2 HIS D 68 26.893 43.074 -13.643 1.00 57.54 C ANISOU 5546 CD2 HIS D 68 8144 7513 6205 -2190 778 2064 C ATOM 5547 CE1 HIS D 68 24.916 42.944 -14.585 1.00 58.17 C ANISOU 5547 CE1 HIS D 68 8209 7858 6034 -1728 848 2185 C ATOM 5548 NE2 HIS D 68 26.156 43.363 -14.766 1.00 58.85 N ANISOU 5548 NE2 HIS D 68 8311 7832 6219 -2020 861 2258 N ATOM 5549 N LEU D 69 25.027 42.273 -8.221 1.00 47.55 N ANISOU 5549 N LEU D 69 7363 5563 5139 -1771 434 1245 N ATOM 5550 CA LEU D 69 24.936 41.630 -6.915 1.00 45.97 C ANISOU 5550 CA LEU D 69 7167 5313 4987 -1749 347 1006 C ATOM 5551 C LEU D 69 24.085 40.373 -6.972 1.00 42.70 C ANISOU 5551 C LEU D 69 6507 5219 4498 -1513 374 878 C ATOM 5552 O LEU D 69 22.883 40.438 -7.226 1.00 43.77 O ANISOU 5552 O LEU D 69 6695 5394 4544 -1231 428 912 O ATOM 5553 CB LEU D 69 24.358 42.590 -5.874 1.00 45.21 C ANISOU 5553 CB LEU D 69 7453 4813 4910 -1653 315 962 C ATOM 5554 CG LEU D 69 24.024 41.961 -4.517 1.00 45.83 C ANISOU 5554 CG LEU D 69 7570 4837 5005 -1577 238 719 C ATOM 5555 CD1 LEU D 69 25.293 41.599 -3.758 1.00 44.62 C ANISOU 5555 CD1 LEU D 69 7341 4667 4947 -1889 124 597 C ATOM 5556 CD2 LEU D 69 23.142 42.882 -3.690 1.00 44.68 C ANISOU 5556 CD2 LEU D 69 7802 4324 4849 -1405 250 689 C ATOM 5557 N VAL D 70 24.715 39.230 -6.736 1.00 39.78 N ANISOU 5557 N VAL D 70 5864 5077 4174 -1631 341 737 N ATOM 5558 CA VAL D 70 23.989 37.976 -6.614 1.00 36.69 C ANISOU 5558 CA VAL D 70 5247 4961 3734 -1432 368 585 C ATOM 5559 C VAL D 70 24.158 37.447 -5.196 1.00 36.58 C ANISOU 5559 C VAL D 70 5259 4845 3795 -1459 275 377 C ATOM 5560 O VAL D 70 25.198 37.652 -4.569 1.00 37.30 O ANISOU 5560 O VAL D 70 5396 4794 3981 -1706 189 347 O ATOM 5561 CB VAL D 70 24.469 36.927 -7.637 1.00 36.09 C ANISOU 5561 CB VAL D 70 4797 5273 3641 -1514 441 596 C ATOM 5562 CG1 VAL D 70 24.216 37.417 -9.057 1.00 37.05 C ANISOU 5562 CG1 VAL D 70 4897 5521 3658 -1477 533 801 C ATOM 5563 CG2 VAL D 70 25.941 36.612 -7.428 1.00 36.38 C ANISOU 5563 CG2 VAL D 70 4686 5329 3807 -1829 397 571 C ATOM 5564 N LEU D 71 23.130 36.779 -4.688 1.00 33.95 N ANISOU 5564 N LEU D 71 4897 4588 3416 -1209 290 238 N ATOM 5565 CA LEU D 71 23.146 36.316 -3.309 1.00 32.16 C ANISOU 5565 CA LEU D 71 4723 4255 3241 -1202 210 47 C ATOM 5566 C LEU D 71 23.380 34.816 -3.204 1.00 31.87 C ANISOU 5566 C LEU D 71 4342 4528 3240 -1205 225 -92 C ATOM 5567 O LEU D 71 23.057 34.056 -4.118 1.00 28.51 O ANISOU 5567 O LEU D 71 3665 4398 2772 -1113 321 -81 O ATOM 5568 CB LEU D 71 21.834 36.682 -2.612 1.00 34.32 C ANISOU 5568 CB LEU D 71 5244 4341 3454 -920 222 -20 C ATOM 5569 CG LEU D 71 21.462 38.164 -2.625 1.00 37.99 C ANISOU 5569 CG LEU D 71 6071 4467 3896 -877 230 111 C ATOM 5570 CD1 LEU D 71 20.250 38.418 -1.745 1.00 38.34 C ANISOU 5570 CD1 LEU D 71 6351 4310 3904 -607 249 19 C ATOM 5571 CD2 LEU D 71 22.643 39.010 -2.181 1.00 40.70 C ANISOU 5571 CD2 LEU D 71 6602 4548 4316 -1185 145 147 C ATOM 5572 N ARG D 72 23.954 34.407 -2.078 1.00 30.79 N ANISOU 5572 N ARG D 72 4202 4319 3179 -1317 134 -221 N ATOM 5573 CA ARG D 72 24.090 32.999 -1.733 1.00 29.16 C ANISOU 5573 CA ARG D 72 3704 4357 3019 -1291 149 -362 C ATOM 5574 C ARG D 72 23.466 32.791 -0.361 1.00 29.68 C ANISOU 5574 C ARG D 72 3928 4274 3074 -1149 89 -523 C ATOM 5575 O ARG D 72 24.153 32.463 0.610 1.00 28.31 O ANISOU 5575 O ARG D 72 3741 4050 2966 -1285 -6 -605 O ATOM 5576 CB ARG D 72 25.556 32.568 -1.741 1.00 32.44 C ANISOU 5576 CB ARG D 72 3903 4871 3552 -1586 101 -337 C ATOM 5577 CG ARG D 72 26.256 32.799 -3.070 1.00 35.00 C ANISOU 5577 CG ARG D 72 4079 5327 3894 -1746 170 -176 C ATOM 5578 CD ARG D 72 25.706 31.891 -4.156 1.00 36.18 C ANISOU 5578 CD ARG D 72 3959 5798 3989 -1598 321 -183 C ATOM 5579 NE ARG D 72 26.056 32.376 -5.488 1.00 39.68 N ANISOU 5579 NE ARG D 72 4349 6331 4396 -1700 396 -16 N ATOM 5580 CZ ARG D 72 27.225 32.162 -6.083 1.00 40.72 C ANISOU 5580 CZ ARG D 72 4282 6579 4612 -1938 428 61 C ATOM 5581 NH1 ARG D 72 28.171 31.466 -5.466 1.00 40.69 N ANISOU 5581 NH1 ARG D 72 4216 6495 4749 -1894 343 -12 N ATOM 5582 NH2 ARG D 72 27.450 32.646 -7.296 1.00 43.41 N ANISOU 5582 NH2 ARG D 72 4614 6976 4905 -1988 497 211 N ATOM 5583 N LEU D 73 22.156 33.003 -0.295 1.00 28.78 N ANISOU 5583 N LEU D 73 3964 4096 2875 -873 145 -557 N ATOM 5584 CA LEU D 73 21.426 32.996 0.965 1.00 29.42 C ANISOU 5584 CA LEU D 73 4249 3997 2932 -715 108 -697 C ATOM 5585 C LEU D 73 21.569 31.679 1.717 1.00 22.84 C ANISOU 5585 C LEU D 73 3199 3333 2147 -695 96 -855 C ATOM 5586 O LEU D 73 21.744 30.618 1.115 1.00 21.33 O ANISOU 5586 O LEU D 73 2678 3434 1991 -689 166 -874 O ATOM 5587 CB LEU D 73 19.944 33.292 0.724 1.00 28.21 C ANISOU 5587 CB LEU D 73 4223 3801 2693 -400 199 -693 C ATOM 5588 CG LEU D 73 19.591 34.702 0.250 1.00 32.16 C ANISOU 5588 CG LEU D 73 5005 4066 3148 -365 215 -538 C ATOM 5589 CD1 LEU D 73 18.083 34.885 0.208 1.00 31.40 C ANISOU 5589 CD1 LEU D 73 5017 3928 2984 -31 301 -542 C ATOM 5590 CD2 LEU D 73 20.238 35.754 1.140 1.00 32.79 C ANISOU 5590 CD2 LEU D 73 5413 3787 3258 -551 117 -535 C ATOM 5591 N ARG D 74 21.499 31.770 3.041 1.00 22.91 N ANISOU 5591 N ARG D 74 3403 3149 2154 -686 15 -966 N ATOM 5592 CA ARG D 74 21.557 30.602 3.908 1.00 29.05 C ANISOU 5592 CA ARG D 74 4019 4051 2969 -648 -1 -1109 C ATOM 5593 C ARG D 74 20.376 30.594 4.867 1.00 28.26 C ANISOU 5593 C ARG D 74 4130 3805 2803 -396 23 -1237 C ATOM 5594 O ARG D 74 19.813 31.643 5.187 1.00 26.69 O ANISOU 5594 O ARG D 74 4259 3339 2543 -323 13 -1224 O ATOM 5595 CB ARG D 74 22.861 30.577 4.706 1.00 30.04 C ANISOU 5595 CB ARG D 74 4139 4117 3159 -931 -145 -1115 C ATOM 5596 CG ARG D 74 24.132 30.629 3.876 1.00 30.05 C ANISOU 5596 CG ARG D 74 3936 4239 3244 -1202 -175 -985 C ATOM 5597 CD ARG D 74 25.340 30.825 4.783 1.00 33.97 C ANISOU 5597 CD ARG D 74 4475 4624 3807 -1451 -333 -960 C ATOM 5598 NE ARG D 74 26.543 31.180 4.035 1.00 37.81 N ANISOU 5598 NE ARG D 74 4836 5154 4379 -1691 -362 -808 N ATOM 5599 CZ ARG D 74 27.702 31.503 4.599 1.00 41.74 C ANISOU 5599 CZ ARG D 74 5348 5550 4961 -1827 -472 -720 C ATOM 5600 NH1 ARG D 74 27.819 31.520 5.921 1.00 40.97 N ANISOU 5600 NH1 ARG D 74 5374 5325 4867 -1782 -571 -774 N ATOM 5601 NH2 ARG D 74 28.746 31.813 3.840 1.00 44.46 N ANISOU 5601 NH2 ARG D 74 5575 5934 5385 -1989 -474 -584 N ATOM 5602 N GLY D 75 20.009 29.405 5.332 1.00 22.60 N ANISOU 5602 N GLY D 75 3213 3186 2187 -218 51 -1184 N ATOM 5603 CA GLY D 75 18.939 29.268 6.302 1.00 21.38 C ANISOU 5603 CA GLY D 75 3241 2847 2034 -2 69 -1118 C ATOM 5604 C GLY D 75 19.436 28.610 7.573 1.00 20.09 C ANISOU 5604 C GLY D 75 3067 2639 1927 -54 -6 -1095 C ATOM 5605 O GLY D 75 20.065 27.557 7.528 1.00 23.43 O ANISOU 5605 O GLY D 75 3191 3251 2461 -115 3 -1077 O HETATM 5606 N NEH D 76 19.173 29.208 8.708 1.00 24.09 N ANISOU 5606 N NEH D 76 3870 2914 2369 -35 -62 -1081 N HETATM 5607 CA NEH D 76 19.612 28.639 9.938 1.00 25.44 C ANISOU 5607 CA NEH D 76 4043 3056 2567 -83 -128 -1047 C HETATM 5608 CB NEH D 76 18.412 28.502 10.843 1.00 24.96 C ANISOU 5608 CB NEH D 76 4011 2950 2521 -48 50 -1047 C TER 5609 NEH D 76 HETATM 5610 C1 GOL A 501 85.825 36.887 -23.098 1.00 42.11 C HETATM 5611 O1 GOL A 501 85.101 37.037 -24.301 1.00 42.69 O HETATM 5612 C2 GOL A 501 87.182 36.250 -23.380 1.00 41.44 C HETATM 5613 O2 GOL A 501 88.057 37.249 -23.849 1.00 44.68 O HETATM 5614 C3 GOL A 501 87.755 35.643 -22.103 1.00 39.44 C HETATM 5615 O3 GOL A 501 88.680 34.614 -22.395 1.00 35.00 O HETATM 5616 C1 GOL C 501 8.764 13.715 7.810 1.00 48.40 C HETATM 5617 O1 GOL C 501 7.485 14.312 7.836 1.00 46.78 O HETATM 5618 C2 GOL C 501 8.730 12.387 7.056 1.00 49.80 C HETATM 5619 O2 GOL C 501 10.015 11.813 7.085 1.00 54.53 O HETATM 5620 C3 GOL C 501 7.779 11.406 7.736 1.00 48.40 C HETATM 5621 O3 GOL C 501 6.940 10.792 6.778 1.00 47.23 O HETATM 5622 O HOH A 601 75.459 36.154 -1.753 1.00 47.32 O HETATM 5623 O HOH A 602 42.323 30.476 -5.707 1.00 47.93 O HETATM 5624 O HOH A 603 71.246 35.312 16.457 1.00 16.47 O HETATM 5625 O HOH A 604 78.937 15.441 3.235 1.00 34.97 O HETATM 5626 O HOH A 605 71.074 16.003 -16.581 1.00 19.86 O HETATM 5627 O HOH A 606 72.547 38.587 11.585 1.00 39.55 O HETATM 5628 O HOH A 607 87.266 16.551 -20.942 1.00 47.18 O HETATM 5629 O HOH A 608 68.736 25.092 8.046 1.00 52.03 O HETATM 5630 O HOH A 609 69.181 15.307 -27.285 1.00 45.06 O HETATM 5631 O HOH A 610 61.393 21.495 3.824 1.00 42.63 O HETATM 5632 O HOH A 611 89.939 26.212 -15.277 1.00 33.81 O HETATM 5633 O HOH A 612 61.324 42.443 -12.392 1.00 26.56 O HETATM 5634 O HOH A 613 54.767 9.990 -23.850 1.00 25.45 O HETATM 5635 O HOH A 614 74.484 36.029 2.262 1.00 35.07 O HETATM 5636 O HOH A 615 72.925 17.550 -21.948 1.00 20.30 O HETATM 5637 O HOH A 616 82.829 28.706 -3.890 1.00 17.53 O HETATM 5638 O HOH A 617 49.841 16.177 -12.598 1.00 24.85 O HETATM 5639 O HOH A 618 43.661 9.570 -23.939 1.00 32.68 O HETATM 5640 O HOH A 619 37.609 13.093 -20.958 1.00 30.97 O HETATM 5641 O HOH A 620 72.779 33.149 -7.854 1.00 8.24 O HETATM 5642 O HOH A 621 73.981 8.055 -15.382 1.00 46.52 O HETATM 5643 O HOH A 622 42.597 10.447 -26.143 1.00 33.71 O HETATM 5644 O HOH A 623 62.245 22.806 -24.564 1.00 33.40 O HETATM 5645 O HOH A 624 76.844 3.725 -3.809 1.00 28.04 O HETATM 5646 O HOH A 625 61.759 26.858 -42.308 1.00 33.67 O HETATM 5647 O HOH A 626 68.514 39.440 -17.444 1.00 37.37 O HETATM 5648 O HOH A 627 72.683 6.429 -13.510 1.00 36.73 O HETATM 5649 O HOH A 628 50.383 11.875 -30.293 1.00 26.36 O HETATM 5650 O HOH A 629 64.500 37.910 4.929 1.00 27.24 O HETATM 5651 O HOH A 630 41.944 27.168 -13.040 1.00 41.15 O HETATM 5652 O HOH A 631 83.705 39.089 -23.705 1.00 47.60 O HETATM 5653 O HOH A 632 39.402 18.696 -13.688 1.00 26.40 O HETATM 5654 O HOH A 633 53.268 9.364 -32.402 1.00 32.09 O HETATM 5655 O HOH A 634 55.353 38.764 -19.312 1.00 40.72 O HETATM 5656 O HOH A 635 63.857 46.029 -16.301 1.00 44.66 O HETATM 5657 O HOH A 636 70.923 0.840 -17.209 1.00 54.29 O HETATM 5658 O HOH A 637 59.606 10.291 -16.768 1.00 21.43 O HETATM 5659 O HOH A 638 47.636 35.136 -20.279 1.00 32.33 O HETATM 5660 O HOH A 639 76.347 19.422 -15.524 1.00 20.29 O HETATM 5661 O HOH A 640 71.185 25.105 10.337 1.00 25.51 O HETATM 5662 O HOH A 641 65.770 34.636 -6.357 1.00 28.02 O HETATM 5663 O HOH A 642 74.564 40.645 -14.734 1.00 42.33 O HETATM 5664 O HOH A 643 41.494 22.428 -23.677 1.00 36.50 O HETATM 5665 O HOH A 644 52.379 14.067 -11.029 1.00 21.26 O HETATM 5666 O HOH A 645 67.937 36.630 -16.292 1.00 16.10 O HETATM 5667 O HOH A 646 68.492 12.651 -10.304 1.00 14.30 O HETATM 5668 O HOH A 647 70.980 37.594 -26.614 1.00 26.42 O HETATM 5669 O HOH A 648 90.455 21.401 -24.052 1.00 45.37 O HETATM 5670 O HOH A 649 45.093 12.187 -15.380 1.00 34.86 O HETATM 5671 O HOH A 650 48.928 17.045 -15.184 1.00 19.76 O HETATM 5672 O HOH A 651 48.428 19.834 -28.422 1.00 26.15 O HETATM 5673 O HOH A 652 58.046 28.179 5.260 1.00 24.21 O HETATM 5674 O HOH A 653 68.570 10.221 -9.352 1.00 32.58 O HETATM 5675 O HOH A 654 67.233 5.065 -10.569 1.00 41.18 O HETATM 5676 O HOH A 655 65.093 21.603 0.142 1.00 24.58 O HETATM 5677 O HOH A 656 49.983 33.604 -31.278 1.00 24.87 O HETATM 5678 O HOH A 657 52.648 30.148 -34.556 1.00 28.28 O HETATM 5679 O HOH A 658 81.924 24.251 -9.249 1.00 24.13 O HETATM 5680 O HOH A 659 68.347 42.897 16.362 1.00 13.68 O HETATM 5681 O HOH A 660 55.331 18.038 2.360 1.00 43.77 O HETATM 5682 O HOH A 661 46.679 30.463 -25.763 1.00 28.75 O HETATM 5683 O HOH A 662 74.717 5.278 -6.345 1.00 41.92 O HETATM 5684 O HOH A 663 37.863 13.074 -23.683 1.00 28.77 O HETATM 5685 O HOH A 664 71.233 38.919 15.566 1.00 21.70 O HETATM 5686 O HOH A 665 52.647 16.123 -35.610 1.00 49.99 O HETATM 5687 O HOH A 666 74.240 6.697 -8.526 1.00 23.73 O HETATM 5688 O HOH A 667 76.972 32.811 -1.765 1.00 16.75 O HETATM 5689 O HOH A 668 68.575 11.851 -2.322 1.00 24.57 O HETATM 5690 O HOH A 669 77.585 30.461 5.475 1.00 30.55 O HETATM 5691 O HOH A 670 63.701 28.478 2.875 1.00 18.33 O HETATM 5692 O HOH A 671 68.160 14.847 4.952 1.00 48.98 O HETATM 5693 O HOH A 672 71.841 21.619 11.541 1.00 37.59 O HETATM 5694 O HOH A 673 71.347 34.314 -5.682 1.00 31.88 O HETATM 5695 O HOH A 674 82.584 29.433 8.722 1.00 18.72 O HETATM 5696 O HOH A 675 71.962 27.040 -4.419 1.00 16.65 O HETATM 5697 O HOH A 676 66.462 16.492 -18.365 1.00 30.82 O HETATM 5698 O HOH A 677 72.226 7.431 -2.298 1.00 20.52 O HETATM 5699 O HOH A 678 70.099 42.176 -1.020 1.00 46.96 O HETATM 5700 O HOH A 679 41.958 17.014 -13.205 1.00 22.18 O HETATM 5701 O HOH A 680 56.403 17.877 -0.906 1.00 24.37 O HETATM 5702 O HOH A 681 45.247 28.860 -15.643 1.00 32.05 O HETATM 5703 O HOH A 682 83.439 22.818 -2.063 1.00 16.88 O HETATM 5704 O HOH A 683 78.602 34.022 -14.496 1.00 14.45 O HETATM 5705 O HOH A 684 56.684 42.754 -17.744 1.00 28.41 O HETATM 5706 O HOH A 685 74.209 14.930 6.630 1.00 30.10 O HETATM 5707 O HOH A 686 75.385 17.052 -14.933 1.00 16.03 O HETATM 5708 O HOH A 687 46.852 28.918 -23.307 1.00 22.21 O HETATM 5709 O HOH A 688 50.337 34.958 -21.676 1.00 15.85 O HETATM 5710 O HOH A 689 58.684 34.958 -24.518 1.00 20.68 O HETATM 5711 O HOH A 690 86.575 32.929 -22.872 1.00 26.89 O HETATM 5712 O HOH A 691 80.768 35.533 -22.319 1.00 17.84 O HETATM 5713 O HOH A 692 75.838 35.265 -21.554 1.00 13.04 O HETATM 5714 O HOH A 693 87.706 26.111 -28.423 1.00 25.28 O HETATM 5715 O HOH A 694 86.089 29.646 -10.574 1.00 39.44 O HETATM 5716 O HOH A 695 74.166 33.627 -15.294 1.00 14.88 O HETATM 5717 O HOH A 696 57.835 16.007 -16.835 1.00 44.00 O HETATM 5718 O HOH A 697 69.326 7.646 -6.894 1.00 28.52 O HETATM 5719 O HOH A 698 66.907 21.845 -24.979 1.00 21.83 O HETATM 5720 O HOH A 699 63.859 27.045 -19.831 1.00 15.68 O HETATM 5721 O HOH A 700 80.735 12.732 -10.805 1.00 18.00 O HETATM 5722 O HOH A 701 52.328 17.314 -17.821 1.00 26.82 O HETATM 5723 O HOH A 702 51.557 16.325 -15.592 1.00 25.22 O HETATM 5724 O HOH A 703 59.316 18.523 1.194 1.00 37.52 O HETATM 5725 O HOH A 704 56.301 37.767 -22.576 1.00 27.30 O HETATM 5726 O HOH A 705 76.441 15.087 -16.603 1.00 25.68 O HETATM 5727 O HOH A 706 79.202 3.987 -2.169 1.00 49.30 O HETATM 5728 O HOH A 707 53.780 31.087 10.833 1.00 37.33 O HETATM 5729 O HOH A 708 64.978 33.124 -2.277 1.00 40.27 O HETATM 5730 O HOH A 709 67.121 14.960 -15.788 1.00 14.05 O HETATM 5731 O HOH A 710 69.572 7.841 -11.018 1.00 42.58 O HETATM 5732 O HOH A 711 69.332 40.467 -22.366 1.00 33.77 O HETATM 5733 O HOH A 712 67.171 30.260 -2.442 1.00 23.30 O HETATM 5734 O HOH A 713 62.568 12.448 2.929 1.00 61.97 O HETATM 5735 O HOH A 714 47.620 32.375 -4.665 1.00 29.64 O HETATM 5736 O HOH A 715 73.156 14.186 -20.370 1.00 22.99 O HETATM 5737 O HOH A 716 75.975 34.202 -13.329 1.00 12.12 O HETATM 5738 O HOH A 717 57.436 24.234 -24.778 1.00 11.53 O HETATM 5739 O HOH A 718 63.568 10.133 -8.660 1.00 19.24 O HETATM 5740 O HOH A 719 62.342 9.443 -1.750 1.00 36.73 O HETATM 5741 O HOH A 720 52.639 35.443 -8.420 1.00 21.66 O HETATM 5742 O HOH A 721 71.918 42.133 10.823 1.00 25.69 O HETATM 5743 O HOH A 722 66.822 19.988 0.762 1.00 47.53 O HETATM 5744 O HOH A 723 48.745 13.370 -8.819 1.00 43.48 O HETATM 5745 O HOH A 724 66.108 37.944 -5.785 1.00 31.15 O HETATM 5746 O HOH A 725 62.729 28.566 -28.389 1.00 21.29 O HETATM 5747 O HOH A 726 79.655 23.215 6.944 1.00 13.78 O HETATM 5748 O HOH A 727 45.907 7.930 -30.057 1.00 48.60 O HETATM 5749 O HOH A 728 70.536 45.876 8.388 1.00 27.50 O HETATM 5750 O HOH A 729 79.800 10.436 -3.428 1.00 35.40 O HETATM 5751 O HOH A 730 66.061 9.711 -8.559 1.00 22.82 O HETATM 5752 O HOH A 731 42.780 17.820 -28.638 1.00 37.54 O HETATM 5753 O HOH A 732 85.692 27.953 -13.335 1.00 30.72 O HETATM 5754 O HOH A 733 76.250 12.970 -19.525 1.00 31.58 O HETATM 5755 O HOH A 734 78.726 36.661 -19.449 1.00 29.52 O HETATM 5756 O HOH A 735 50.383 24.664 -26.981 1.00 19.26 O HETATM 5757 O HOH A 736 88.656 21.875 -8.917 1.00 33.18 O HETATM 5758 O HOH A 737 61.204 31.811 -25.590 1.00 17.88 O HETATM 5759 O HOH A 738 55.030 4.329 -24.411 1.00 43.65 O HETATM 5760 O HOH A 739 86.107 21.813 -4.024 1.00 25.43 O HETATM 5761 O HOH A 740 81.610 23.447 -26.801 1.00 28.69 O HETATM 5762 O HOH A 741 71.895 20.194 -26.280 1.00 37.61 O HETATM 5763 O HOH A 742 58.892 30.827 -30.701 1.00 21.26 O HETATM 5764 O HOH A 743 63.766 36.187 -6.725 1.00 31.94 O HETATM 5765 O HOH A 744 55.371 19.053 -15.506 1.00 13.66 O HETATM 5766 O HOH A 745 71.825 38.244 -10.748 1.00 25.00 O HETATM 5767 O HOH A 746 58.116 34.512 11.004 1.00 24.83 O HETATM 5768 O HOH A 747 82.111 35.208 1.708 1.00 34.12 O HETATM 5769 O HOH A 748 83.010 23.697 9.814 1.00 28.59 O HETATM 5770 O HOH A 749 75.169 13.812 -23.731 1.00 30.25 O HETATM 5771 O HOH A 750 67.965 22.820 0.109 1.00 16.09 O HETATM 5772 O HOH A 751 42.458 24.651 -12.796 1.00 26.34 O HETATM 5773 O HOH A 752 76.751 35.306 -9.254 1.00 21.54 O HETATM 5774 O HOH A 753 66.384 40.012 5.767 1.00 24.08 O HETATM 5775 O HOH A 754 71.931 29.108 -6.071 1.00 24.42 O HETATM 5776 O HOH A 755 52.947 35.904 -21.716 1.00 28.52 O HETATM 5777 O HOH A 756 60.044 21.206 -38.334 1.00 38.20 O HETATM 5778 O HOH A 757 74.111 41.644 3.284 1.00 49.62 O HETATM 5779 O HOH A 758 69.054 41.964 -15.911 1.00 53.05 O HETATM 5780 O HOH A 759 59.930 22.693 -24.874 1.00 37.47 O HETATM 5781 O HOH A 760 68.001 -5.383 -6.522 1.00 41.44 O HETATM 5782 O HOH A 761 62.551 39.399 -8.472 1.00 36.94 O HETATM 5783 O HOH A 762 64.251 5.863 -3.689 1.00 59.26 O HETATM 5784 O HOH A 763 71.252 7.551 -16.337 1.00 43.21 O HETATM 5785 O HOH A 764 60.431 34.638 12.514 1.00 32.39 O HETATM 5786 O HOH A 765 66.740 40.862 2.481 1.00 24.61 O HETATM 5787 O HOH A 766 46.422 16.437 -28.390 1.00 24.46 O HETATM 5788 O HOH A 767 72.585 20.440 -14.774 1.00 26.94 O HETATM 5789 O HOH A 768 72.464 -6.494 -11.857 1.00 48.88 O HETATM 5790 O HOH A 769 50.350 28.314 -0.695 1.00 66.79 O HETATM 5791 O HOH A 770 77.697 33.857 9.886 1.00 19.67 O HETATM 5792 O HOH A 771 85.523 15.063 -10.868 1.00 34.63 O HETATM 5793 O HOH A 772 43.135 30.021 -14.755 1.00 42.21 O HETATM 5794 O HOH A 773 73.121 -1.621 -14.804 1.00 43.08 O HETATM 5795 O HOH A 774 52.707 10.716 -22.231 1.00 26.33 O HETATM 5796 O HOH A 775 55.456 27.598 4.965 1.00 30.17 O HETATM 5797 O HOH A 776 45.185 24.203 -23.576 1.00 27.99 O HETATM 5798 O HOH A 777 53.369 19.793 -32.547 1.00 33.72 O HETATM 5799 O HOH A 778 72.309 41.826 7.200 1.00 20.87 O HETATM 5800 O HOH A 779 37.185 17.107 -25.439 1.00 31.14 O HETATM 5801 O HOH A 780 55.795 15.389 -15.358 1.00 28.17 O HETATM 5802 O HOH A 781 83.758 15.394 -18.308 1.00 39.81 O HETATM 5803 O HOH A 782 60.618 16.416 -19.996 1.00 35.49 O HETATM 5804 O HOH A 783 70.199 20.739 8.201 1.00 28.07 O HETATM 5805 O HOH A 784 68.522 26.389 6.106 1.00 50.61 O HETATM 5806 O HOH A 785 69.473 19.370 -25.051 1.00 51.45 O HETATM 5807 O HOH A 786 87.921 30.697 0.454 1.00 37.13 O HETATM 5808 O HOH A 787 50.281 35.261 -24.385 1.00 25.54 O HETATM 5809 O HOH A 788 83.590 36.535 -1.753 1.00 34.07 O HETATM 5810 O HOH A 789 66.379 25.856 -27.885 1.00 30.44 O HETATM 5811 O HOH A 790 59.159 30.530 -28.002 1.00 20.47 O HETATM 5812 O HOH A 791 75.937 36.797 -12.716 1.00 23.82 O HETATM 5813 O HOH A 792 66.782 38.513 -0.056 1.00 40.10 O HETATM 5814 O HOH A 793 38.446 17.305 -28.047 1.00 21.61 O HETATM 5815 O HOH A 794 83.082 35.624 -4.530 1.00 16.96 O HETATM 5816 O HOH A 795 42.266 22.723 -10.314 1.00 21.10 O HETATM 5817 O HOH A 796 74.850 35.785 14.503 1.00 37.65 O HETATM 5818 O HOH A 797 68.773 16.409 -18.093 1.00 29.99 O HETATM 5819 O HOH A 798 79.709 11.869 4.884 1.00 43.68 O HETATM 5820 O HOH A 799 50.693 39.262 -13.965 1.00 32.83 O HETATM 5821 O HOH A 800 84.408 30.839 -8.633 1.00 29.08 O HETATM 5822 O HOH A 801 42.987 32.426 -23.503 1.00 46.50 O HETATM 5823 O HOH A 802 70.623 11.671 2.999 1.00 24.76 O HETATM 5824 O HOH A 803 75.212 21.383 -14.324 1.00 19.47 O HETATM 5825 O HOH A 804 71.103 40.404 -12.473 1.00 28.23 O HETATM 5826 O HOH A 805 74.412 31.644 15.661 1.00 20.39 O HETATM 5827 O HOH A 806 56.720 37.238 -13.126 1.00 33.24 O HETATM 5828 O HOH A 807 60.911 22.285 -40.126 1.00 37.33 O HETATM 5829 O HOH A 808 72.324 17.658 -14.686 1.00 19.78 O HETATM 5830 O HOH A 809 48.487 14.753 -27.404 1.00 19.36 O HETATM 5831 O HOH A 810 81.177 33.980 8.798 1.00 46.35 O HETATM 5832 O HOH A 811 73.902 40.680 9.597 1.00 25.55 O HETATM 5833 O HOH A 812 77.699 36.965 3.560 1.00 22.75 O HETATM 5834 O HOH A 813 55.150 18.953 -20.711 1.00 37.35 O HETATM 5835 O HOH A 814 36.205 19.975 -21.856 1.00 52.15 O HETATM 5836 O HOH A 815 70.825 25.687 13.289 1.00 32.08 O HETATM 5837 O HOH A 816 53.191 22.934 3.605 1.00 48.11 O HETATM 5838 O HOH A 817 67.465 18.481 -38.200 1.00 44.00 O HETATM 5839 O HOH A 818 66.373 27.210 6.162 1.00 44.91 O HETATM 5840 O HOH A 819 72.509 40.164 -22.746 1.00 36.48 O HETATM 5841 O HOH A 820 83.851 22.189 6.958 1.00 33.21 O HETATM 5842 O HOH A 821 70.396 40.772 -10.164 1.00 45.34 O HETATM 5843 O HOH A 822 55.900 25.131 5.449 1.00 45.88 O HETATM 5844 O HOH A 823 54.756 23.596 0.923 1.00 24.43 O HETATM 5845 O HOH A 824 79.226 38.757 -15.195 1.00 35.21 O HETATM 5846 O HOH A 825 46.309 16.255 -6.265 1.00 27.90 O HETATM 5847 O HOH A 826 48.922 36.641 -10.952 1.00 37.73 O HETATM 5848 O HOH A 827 50.304 14.161 -29.352 1.00 26.39 O HETATM 5849 O HOH A 828 51.051 17.688 -32.690 1.00 33.11 O HETATM 5850 O HOH A 829 80.130 36.175 -13.667 1.00 41.48 O HETATM 5851 O HOH A 830 71.023 38.505 -7.889 1.00 44.40 O HETATM 5852 O HOH A 831 69.234 22.617 10.186 1.00 45.97 O HETATM 5853 O HOH A 832 75.459 21.143 -27.590 1.00 15.06 O HETATM 5854 O HOH A 833 71.557 12.842 4.958 1.00 32.23 O HETATM 5855 O HOH A 834 74.237 42.390 -2.175 1.00 32.90 O HETATM 5856 O HOH A 835 70.690 14.913 6.130 1.00 55.86 O HETATM 5857 O HOH A 836 48.068 35.187 -24.990 1.00 54.00 O HETATM 5858 O HOH A 837 74.398 8.529 2.039 1.00 32.03 O HETATM 5859 O HOH A 838 83.431 11.098 -5.527 1.00 38.92 O HETATM 5860 O HOH A 839 50.731 35.318 -3.986 1.00 42.66 O HETATM 5861 O HOH A 840 52.617 36.329 -24.500 1.00 21.73 O HETATM 5862 O HOH A 841 68.654 22.256 -28.532 1.00 46.24 O HETATM 5863 O HOH A 842 55.962 38.950 -17.125 1.00 32.20 O HETATM 5864 O HOH A 843 42.544 17.904 -10.713 1.00 32.35 O HETATM 5865 O HOH A 844 76.550 39.324 -28.487 1.00 30.74 O HETATM 5866 O HOH A 845 50.481 22.100 -28.725 1.00 34.50 O HETATM 5867 O HOH A 846 46.741 19.638 -30.443 1.00 34.63 O HETATM 5868 O HOH A 847 71.000 42.487 -17.036 1.00 46.99 O HETATM 5869 O HOH A 848 70.706 5.586 -5.275 1.00 36.75 O HETATM 5870 O HOH A 849 75.146 5.493 -11.101 1.00 49.13 O HETATM 5871 O HOH A 850 36.281 14.513 -25.111 1.00 21.59 O HETATM 5872 O HOH A 851 38.954 19.936 -11.332 1.00 45.11 O HETATM 5873 O HOH A 852 76.916 37.607 -21.890 1.00 28.09 O HETATM 5874 O HOH A 853 48.847 39.230 -11.972 1.00 44.61 O HETATM 5875 O HOH A 854 67.256 35.640 -3.886 1.00 44.66 O HETATM 5876 O HOH A 855 34.489 13.265 -21.094 1.00 42.71 O HETATM 5877 O HOH A 856 67.016 43.106 -11.887 1.00 47.00 O HETATM 5878 O HOH A 857 71.118 28.504 -36.339 1.00 32.74 O HETATM 5879 O HOH A 858 41.811 12.191 -30.116 1.00 39.25 O HETATM 5880 O HOH A 859 87.280 31.154 -12.644 1.00 51.35 O HETATM 5881 O HOH A 860 85.593 14.204 -3.405 1.00 37.36 O HETATM 5882 O HOH A 861 80.202 2.047 -3.030 1.00 48.44 O HETATM 5883 O HOH A 862 55.487 18.632 -18.136 1.00 35.44 O HETATM 5884 O HOH A 863 86.267 36.782 -1.325 1.00 31.90 O HETATM 5885 O HOH A 864 62.165 7.970 -5.525 1.00 36.05 O HETATM 5886 O HOH A 865 65.888 18.619 -41.161 1.00 44.80 O HETATM 5887 O HOH A 866 46.980 26.050 -24.313 1.00 22.66 O HETATM 5888 O HOH A 867 71.320 23.509 14.519 1.00 38.77 O HETATM 5889 O HOH A 868 63.873 26.372 -29.345 1.00 29.18 O HETATM 5890 O HOH A 869 71.106 -6.388 -6.814 1.00 41.58 O HETATM 5891 O HOH A 870 57.852 15.810 -21.666 1.00 39.73 O HETATM 5892 O HOH A 871 59.843 12.442 -18.631 1.00 32.24 O HETATM 5893 O HOH A 872 41.157 17.624 -30.230 1.00 40.64 O HETATM 5894 O HOH A 873 35.551 19.189 -24.815 1.00 28.60 O HETATM 5895 O HOH A 874 74.576 38.781 -10.958 1.00 33.27 O HETATM 5896 O HOH A 875 66.165 23.601 -27.015 1.00 44.09 O HETATM 5897 O HOH A 876 75.437 38.120 14.299 1.00 44.56 O HETATM 5898 O HOH A 877 47.857 35.265 -4.109 1.00 44.38 O HETATM 5899 O HOH A 878 66.751 3.248 -6.860 1.00 43.70 O HETATM 5900 O HOH A 879 66.063 16.742 -38.924 1.00 56.24 O HETATM 5901 O HOH A 880 75.584 11.780 -22.426 1.00 49.28 O HETATM 5902 O HOH A 881 71.397 6.587 -8.936 1.00 31.22 O HETATM 5903 O HOH A 882 47.577 25.702 -26.801 1.00 32.62 O HETATM 5904 O HOH A 883 81.019 37.859 1.883 1.00 27.22 O HETATM 5905 O HOH A 884 61.801 13.822 -19.874 1.00 31.05 O HETATM 5906 O HOH A 885 45.016 30.035 1.665 1.00 49.18 O HETATM 5907 O HOH A 886 61.296 8.485 -7.980 1.00 33.88 O HETATM 5908 O HOH A 887 71.753 41.724 -3.190 1.00 46.45 O HETATM 5909 O HOH A 888 32.844 15.167 -19.042 1.00 46.91 O HETATM 5910 O HOH A 889 70.838 29.394 -3.057 1.00 31.68 O HETATM 5911 O HOH A 890 69.026 18.431 8.441 1.00 39.87 O HETATM 5912 O HOH A 891 73.044 5.521 -4.168 1.00 18.05 O HETATM 5913 O HOH A 892 71.576 41.962 -14.473 1.00 44.73 O HETATM 5914 O HOH A 893 41.329 14.389 -13.457 1.00 43.05 O HETATM 5915 O HOH A 894 82.300 9.003 -6.194 1.00 53.16 O HETATM 5916 O HOH A 895 46.465 36.350 -6.320 1.00 49.61 O HETATM 5917 O HOH A 896 83.375 33.058 -12.669 1.00 45.50 O HETATM 5918 O HOH A 897 65.735 -3.777 -18.959 1.00 53.83 O HETATM 5919 O HOH A 898 76.478 13.992 -26.207 1.00 49.23 O HETATM 5920 O HOH A 899 39.268 26.746 -20.618 1.00 38.96 O HETATM 5921 O HOH A 900 61.597 36.064 -4.853 1.00 37.82 O HETATM 5922 O HOH A 901 54.000 35.670 5.675 1.00 40.23 O HETATM 5923 O HOH A 902 82.588 38.942 -0.697 1.00 44.98 O HETATM 5924 O HOH A 903 68.807 16.292 7.770 1.00 27.43 O HETATM 5925 O HOH A 904 46.817 27.931 -28.743 1.00 54.59 O HETATM 5926 O HOH A 905 76.082 41.567 11.362 1.00 35.76 O HETATM 5927 O HOH A 906 75.978 44.297 -0.833 1.00 50.94 O HETATM 5928 O HOH A 907 73.108 2.595 -7.619 1.00 57.37 O HETATM 5929 O HOH A 908 80.810 39.832 -2.796 1.00 48.94 O HETATM 5930 O HOH A 909 49.581 24.384 -30.436 1.00 44.66 O HETATM 5931 O HOH A 910 66.697 15.399 -22.511 1.00 34.65 O HETATM 5932 O HOH A 911 65.450 12.968 -23.986 1.00 51.27 O HETATM 5933 O HOH A 912 67.976 -4.465 -21.016 1.00 52.29 O HETATM 5934 O HOH A 913 69.128 14.169 10.645 1.00 47.07 O HETATM 5935 O HOH B 101 50.659 -1.076 -3.183 1.00 49.37 O HETATM 5936 O HOH B 102 40.334 -4.128 -28.625 1.00 41.34 O HETATM 5937 O HOH B 103 50.502 10.507 -20.147 1.00 36.22 O HETATM 5938 O HOH B 104 41.217 -0.726 -25.599 1.00 39.23 O HETATM 5939 O HOH B 105 53.446 11.756 -19.933 1.00 31.45 O HETATM 5940 O HOH B 106 55.997 11.550 -18.994 1.00 28.10 O HETATM 5941 O HOH B 107 42.710 -10.131 -28.113 1.00 46.20 O HETATM 5942 O HOH B 108 39.208 11.961 -19.218 1.00 39.43 O HETATM 5943 O HOH B 109 52.710 11.230 -5.162 1.00 30.84 O HETATM 5944 O HOH B 110 58.130 5.391 -19.148 1.00 30.60 O HETATM 5945 O HOH B 111 46.391 2.765 -6.512 1.00 39.75 O HETATM 5946 O HOH B 112 49.259 -0.145 -25.394 1.00 50.35 O HETATM 5947 O HOH B 113 42.263 -14.678 -14.579 1.00 53.56 O HETATM 5948 O HOH B 114 62.205 -5.819 -19.432 1.00 42.30 O HETATM 5949 O HOH B 115 46.495 6.793 -16.426 1.00 19.13 O HETATM 5950 O HOH B 116 57.628 16.125 -13.764 1.00 16.80 O HETATM 5951 O HOH B 117 53.097 6.599 -2.666 1.00 38.06 O HETATM 5952 O HOH B 118 49.732 13.845 -11.583 1.00 29.74 O HETATM 5953 O HOH B 119 41.754 2.464 -28.901 1.00 29.29 O HETATM 5954 O HOH B 120 43.293 9.580 -17.413 1.00 36.42 O HETATM 5955 O HOH B 121 57.629 2.017 -26.294 1.00 57.17 O HETATM 5956 O HOH B 122 47.501 11.864 -10.956 1.00 43.21 O HETATM 5957 O HOH B 123 43.669 3.281 -31.127 1.00 39.10 O HETATM 5958 O HOH B 124 58.179 12.334 -15.203 1.00 18.58 O HETATM 5959 O HOH B 125 42.524 8.823 -14.205 1.00 41.43 O HETATM 5960 O HOH B 126 49.219 8.027 -5.522 1.00 30.03 O HETATM 5961 O HOH B 127 44.572 6.228 -8.636 1.00 54.37 O HETATM 5962 O HOH B 128 57.504 12.261 -4.933 1.00 44.75 O HETATM 5963 O HOH B 129 58.983 10.953 -7.308 1.00 30.87 O HETATM 5964 O HOH B 130 55.700 3.505 -22.142 1.00 31.35 O HETATM 5965 O HOH B 131 46.334 7.461 -9.267 1.00 39.09 O HETATM 5966 O HOH B 132 43.383 -6.398 -26.467 1.00 34.30 O HETATM 5967 O HOH B 133 45.482 8.965 -14.630 1.00 46.95 O HETATM 5968 O HOH B 134 36.247 -2.129 -24.577 1.00 36.23 O HETATM 5969 O HOH B 135 58.145 8.230 -18.606 1.00 7.01 O HETATM 5970 O HOH B 136 45.423 5.229 -6.815 1.00 40.00 O HETATM 5971 O HOH B 137 51.234 -8.366 -9.662 1.00 38.78 O HETATM 5972 O HOH B 138 33.012 -0.994 -22.381 1.00 45.47 O HETATM 5973 O HOH B 139 58.055 9.436 -4.751 1.00 28.11 O HETATM 5974 O HOH B 140 56.359 10.116 -3.058 1.00 41.01 O HETATM 5975 O HOH B 141 32.351 8.191 -16.663 1.00 39.26 O HETATM 5976 O HOH B 142 54.737 -15.034 -14.560 1.00 48.16 O HETATM 5977 O HOH B 143 41.781 11.270 -15.935 1.00 46.51 O HETATM 5978 O HOH B 144 58.473 10.370 -20.031 1.00 36.84 O HETATM 5979 O HOH B 145 53.509 9.603 -2.893 1.00 29.48 O HETATM 5980 O HOH C 601 32.194 33.225 -4.609 1.00 67.94 O HETATM 5981 O HOH C 602 19.404 23.963 15.467 1.00 47.13 O HETATM 5982 O HOH C 603 9.850 20.027 -26.357 1.00 46.66 O HETATM 5983 O HOH C 604 22.841 11.052 20.331 1.00 33.35 O HETATM 5984 O HOH C 605 26.960 30.612 8.926 1.00 39.98 O HETATM 5985 O HOH C 606 7.245 10.082 29.096 1.00 20.47 O HETATM 5986 O HOH C 607 -0.762 34.573 9.311 1.00 37.65 O HETATM 5987 O HOH C 608 0.239 13.023 14.002 1.00 32.63 O HETATM 5988 O HOH C 609 9.712 8.719 7.549 1.00 75.17 O HETATM 5989 O HOH C 610 1.236 12.057 22.482 1.00 35.08 O HETATM 5990 O HOH C 611 20.455 25.168 9.077 1.00 14.49 O HETATM 5991 O HOH C 612 26.543 31.328 1.279 1.00 27.41 O HETATM 5992 O HOH C 613 7.973 29.337 -3.927 1.00 34.41 O HETATM 5993 O HOH C 614 -6.917 17.916 -0.724 1.00 35.49 O HETATM 5994 O HOH C 615 8.759 4.004 11.435 1.00 43.11 O HETATM 5995 O HOH C 616 30.285 28.230 -2.605 1.00 26.34 O HETATM 5996 O HOH C 617 2.642 7.205 14.174 1.00 35.83 O HETATM 5997 O HOH C 618 5.757 38.534 -1.260 1.00 43.01 O HETATM 5998 O HOH C 619 6.817 16.188 6.436 1.00 23.52 O HETATM 5999 O HOH C 620 18.964 34.863 -4.267 1.00 30.53 O HETATM 6000 O HOH C 621 1.109 13.488 16.285 1.00 51.55 O HETATM 6001 O HOH C 622 -5.057 22.942 -13.893 1.00 62.04 O HETATM 6002 O HOH C 623 4.592 6.822 -9.283 1.00 28.35 O HETATM 6003 O HOH C 624 5.948 12.439 4.879 1.00 12.56 O HETATM 6004 O HOH C 625 20.765 31.414 -17.805 1.00 35.54 O HETATM 6005 O HOH C 626 28.507 10.399 -8.971 1.00 28.23 O HETATM 6006 O HOH C 627 17.301 3.086 0.440 1.00 32.82 O HETATM 6007 O HOH C 628 10.872 9.082 -3.620 1.00 22.19 O HETATM 6008 O HOH C 629 0.868 15.317 18.720 1.00 25.17 O HETATM 6009 O HOH C 630 28.609 10.127 -1.863 1.00 42.36 O HETATM 6010 O HOH C 631 15.019 43.141 1.253 1.00 44.27 O HETATM 6011 O HOH C 632 9.574 5.066 -9.204 1.00 27.84 O HETATM 6012 O HOH C 633 25.912 34.113 -9.848 1.00 38.83 O HETATM 6013 O HOH C 634 22.231 32.485 9.039 1.00 50.81 O HETATM 6014 O HOH C 635 26.362 10.939 10.896 1.00 34.81 O HETATM 6015 O HOH C 636 23.596 6.818 -6.758 1.00 39.42 O HETATM 6016 O HOH C 637 10.228 23.076 17.042 1.00 41.36 O HETATM 6017 O HOH C 638 7.831 7.705 -13.856 1.00 23.62 O HETATM 6018 O HOH C 639 2.444 26.032 -2.948 1.00 19.93 O HETATM 6019 O HOH C 640 -7.436 16.019 2.638 1.00 35.75 O HETATM 6020 O HOH C 641 4.605 38.793 4.029 1.00 27.85 O HETATM 6021 O HOH C 642 1.684 16.842 27.493 1.00 26.56 O HETATM 6022 O HOH C 643 -9.733 23.442 3.427 1.00 34.31 O HETATM 6023 O HOH C 644 14.202 7.870 17.257 1.00 35.49 O HETATM 6024 O HOH C 645 10.389 6.320 -4.472 1.00 38.45 O HETATM 6025 O HOH C 646 3.399 28.618 -2.182 1.00 16.87 O HETATM 6026 O HOH C 647 21.974 2.567 -5.189 1.00 31.61 O HETATM 6027 O HOH C 648 -0.860 22.282 19.696 1.00 19.97 O HETATM 6028 O HOH C 649 -9.392 15.492 -0.731 1.00 56.40 O HETATM 6029 O HOH C 650 10.186 35.368 3.141 1.00 22.93 O HETATM 6030 O HOH C 651 6.723 8.471 8.043 1.00 54.42 O HETATM 6031 O HOH C 652 20.192 17.691 18.042 1.00 28.50 O HETATM 6032 O HOH C 653 1.614 12.931 11.025 1.00 13.43 O HETATM 6033 O HOH C 654 26.176 10.275 4.225 1.00 17.72 O HETATM 6034 O HOH C 655 11.688 30.622 -3.104 1.00 22.02 O HETATM 6035 O HOH C 656 2.202 10.241 3.597 1.00 16.51 O HETATM 6036 O HOH C 657 -3.174 21.432 3.352 1.00 29.19 O HETATM 6037 O HOH C 658 6.319 25.099 -1.940 1.00 22.77 O HETATM 6038 O HOH C 659 11.602 15.880 10.475 1.00 24.21 O HETATM 6039 O HOH C 660 23.264 29.679 -2.879 1.00 35.85 O HETATM 6040 O HOH C 661 41.115 30.988 -8.797 1.00 35.15 O HETATM 6041 O HOH C 662 -8.687 19.128 -15.963 1.00 28.13 O HETATM 6042 O HOH C 663 14.975 17.172 15.746 1.00 22.11 O HETATM 6043 O HOH C 664 26.412 28.012 -5.764 1.00 28.93 O HETATM 6044 O HOH C 665 -3.817 16.173 21.416 1.00 16.88 O HETATM 6045 O HOH C 666 -12.630 32.308 -4.843 1.00 48.00 O HETATM 6046 O HOH C 667 2.881 11.356 -0.586 1.00 12.09 O HETATM 6047 O HOH C 668 31.679 16.425 -10.665 1.00 23.33 O HETATM 6048 O HOH C 669 -4.154 16.774 8.498 1.00 19.02 O HETATM 6049 O HOH C 670 25.679 9.398 -9.105 1.00 25.70 O HETATM 6050 O HOH C 671 13.680 12.536 10.339 1.00 30.89 O HETATM 6051 O HOH C 672 6.194 38.154 10.201 1.00 31.50 O HETATM 6052 O HOH C 673 5.758 31.184 -7.857 1.00 22.81 O HETATM 6053 O HOH C 674 -9.020 28.922 -8.267 1.00 53.64 O HETATM 6054 O HOH C 675 15.501 7.191 -10.366 1.00 26.91 O HETATM 6055 O HOH C 676 12.744 28.862 -5.722 1.00 32.65 O HETATM 6056 O HOH C 677 6.834 18.500 8.233 1.00 15.28 O HETATM 6057 O HOH C 678 8.409 -0.327 20.812 1.00 31.49 O HETATM 6058 O HOH C 679 15.325 35.219 3.853 1.00 31.42 O HETATM 6059 O HOH C 680 20.130 10.663 -11.793 1.00 15.51 O HETATM 6060 O HOH C 681 7.376 20.828 23.064 1.00 23.63 O HETATM 6061 O HOH C 682 16.527 22.648 -12.178 1.00 43.76 O HETATM 6062 O HOH C 683 -2.713 21.965 -14.262 1.00 38.92 O HETATM 6063 O HOH C 684 21.279 20.992 -12.066 1.00 12.24 O HETATM 6064 O HOH C 685 -4.707 22.777 10.595 1.00 15.26 O HETATM 6065 O HOH C 686 3.388 38.207 -2.287 1.00 37.82 O HETATM 6066 O HOH C 687 2.243 32.245 -7.074 1.00 26.32 O HETATM 6067 O HOH C 688 14.790 18.241 -7.225 1.00 14.76 O HETATM 6068 O HOH C 689 7.640 7.072 9.705 1.00 34.88 O HETATM 6069 O HOH C 690 0.045 11.392 -1.790 1.00 20.12 O HETATM 6070 O HOH C 691 17.561 13.503 -12.970 1.00 18.24 O HETATM 6071 O HOH C 692 3.768 31.534 -11.255 1.00 26.83 O HETATM 6072 O HOH C 693 9.933 4.159 -3.822 1.00 57.91 O HETATM 6073 O HOH C 694 -1.149 19.947 26.117 1.00 20.57 O HETATM 6074 O HOH C 695 33.592 21.476 -10.920 1.00 46.00 O HETATM 6075 O HOH C 696 -4.089 21.844 22.460 1.00 28.81 O HETATM 6076 O HOH C 697 24.203 26.107 -8.180 1.00 39.46 O HETATM 6077 O HOH C 698 5.105 2.886 16.839 1.00 58.39 O HETATM 6078 O HOH C 699 10.096 20.009 20.894 1.00 56.53 O HETATM 6079 O HOH C 700 11.997 23.465 -12.383 1.00 22.83 O HETATM 6080 O HOH C 701 4.730 11.844 -2.516 1.00 14.25 O HETATM 6081 O HOH C 702 24.357 20.285 13.212 1.00 30.92 O HETATM 6082 O HOH C 703 10.363 32.979 2.089 1.00 15.76 O HETATM 6083 O HOH C 704 36.434 22.835 1.922 1.00 35.51 O HETATM 6084 O HOH C 705 9.117 4.226 2.605 1.00 39.14 O HETATM 6085 O HOH C 706 37.314 28.470 -1.255 1.00 37.06 O HETATM 6086 O HOH C 707 19.969 14.587 -18.006 1.00 42.65 O HETATM 6087 O HOH C 708 19.639 15.072 -15.522 1.00 24.92 O HETATM 6088 O HOH C 709 21.974 8.591 -0.324 1.00 33.68 O HETATM 6089 O HOH C 710 18.763 23.366 -12.301 1.00 40.32 O HETATM 6090 O HOH C 711 11.715 25.419 -30.900 1.00 44.00 O HETATM 6091 O HOH C 712 2.026 7.342 19.717 1.00 36.08 O HETATM 6092 O HOH C 713 -1.991 32.921 1.943 1.00 39.27 O HETATM 6093 O HOH C 714 12.160 4.626 15.291 1.00 27.60 O HETATM 6094 O HOH C 715 13.967 24.259 12.748 1.00 25.75 O HETATM 6095 O HOH C 716 10.083 26.646 -29.916 1.00 59.36 O HETATM 6096 O HOH C 717 12.605 7.477 6.965 1.00 33.77 O HETATM 6097 O HOH C 718 30.243 25.002 -16.032 1.00 29.46 O HETATM 6098 O HOH C 719 -7.757 12.262 -10.130 1.00 26.14 O HETATM 6099 O HOH C 720 6.926 3.120 23.115 1.00 18.98 O HETATM 6100 O HOH C 721 10.745 33.675 10.210 1.00 29.78 O HETATM 6101 O HOH C 722 2.491 30.259 -4.046 1.00 26.73 O HETATM 6102 O HOH C 723 12.847 17.391 18.046 1.00 51.68 O HETATM 6103 O HOH C 724 6.080 27.640 -9.527 1.00 25.73 O HETATM 6104 O HOH C 725 13.196 10.892 6.543 1.00 44.04 O HETATM 6105 O HOH C 726 8.286 34.221 15.455 1.00 25.81 O HETATM 6106 O HOH C 727 15.855 17.079 -15.835 1.00 31.03 O HETATM 6107 O HOH C 728 -10.877 20.204 -14.446 1.00 32.56 O HETATM 6108 O HOH C 729 33.923 16.813 -2.726 1.00 48.29 O HETATM 6109 O HOH C 730 -4.824 9.378 10.919 1.00 24.33 O HETATM 6110 O HOH C 731 37.118 22.141 -11.813 1.00 32.93 O HETATM 6111 O HOH C 732 18.204 29.071 -7.289 1.00 51.50 O HETATM 6112 O HOH C 733 -5.807 20.167 10.739 1.00 22.49 O HETATM 6113 O HOH C 734 8.588 25.104 20.794 1.00 27.81 O HETATM 6114 O HOH C 735 18.564 11.025 24.914 1.00 28.71 O HETATM 6115 O HOH C 736 -2.596 11.360 21.177 1.00 38.99 O HETATM 6116 O HOH C 737 39.499 35.247 -9.005 1.00 38.69 O HETATM 6117 O HOH C 738 6.543 3.790 19.784 1.00 22.05 O HETATM 6118 O HOH C 739 10.872 22.914 12.816 1.00 22.68 O HETATM 6119 O HOH C 740 -5.074 14.806 4.307 1.00 36.33 O HETATM 6120 O HOH C 741 -0.414 10.792 24.596 1.00 49.35 O HETATM 6121 O HOH C 742 16.814 11.166 -11.633 1.00 23.54 O HETATM 6122 O HOH C 743 4.536 5.055 22.163 1.00 31.03 O HETATM 6123 O HOH C 744 6.868 32.635 17.565 1.00 25.99 O HETATM 6124 O HOH C 745 3.531 4.561 16.879 1.00 38.50 O HETATM 6125 O HOH C 746 -3.720 10.291 14.329 1.00 32.27 O HETATM 6126 O HOH C 747 36.717 22.588 -14.437 1.00 51.83 O HETATM 6127 O HOH C 748 -0.354 8.682 -6.496 1.00 29.07 O HETATM 6128 O HOH C 749 31.184 13.490 8.432 1.00 29.94 O HETATM 6129 O HOH C 750 25.014 30.718 10.848 1.00 35.60 O HETATM 6130 O HOH C 751 0.864 8.778 16.047 1.00 24.22 O HETATM 6131 O HOH C 752 23.278 26.643 -2.998 1.00 16.14 O HETATM 6132 O HOH C 753 14.860 9.547 6.033 1.00 31.13 O HETATM 6133 O HOH C 754 40.365 27.243 -15.889 1.00 40.37 O HETATM 6134 O HOH C 755 9.691 38.078 5.537 1.00 25.20 O HETATM 6135 O HOH C 756 -5.093 30.356 -5.806 1.00 34.67 O HETATM 6136 O HOH C 757 3.537 24.165 -1.953 1.00 22.04 O HETATM 6137 O HOH C 758 28.430 20.792 -14.418 1.00 28.84 O HETATM 6138 O HOH C 759 31.393 10.148 -7.332 1.00 35.41 O HETATM 6139 O HOH C 760 -4.725 23.213 19.493 1.00 41.28 O HETATM 6140 O HOH C 761 12.511 5.480 18.214 1.00 33.30 O HETATM 6141 O HOH C 762 9.780 26.896 -12.355 1.00 40.75 O HETATM 6142 O HOH C 763 12.068 9.706 -14.609 1.00 41.18 O HETATM 6143 O HOH C 764 -1.889 33.620 -2.940 1.00 27.93 O HETATM 6144 O HOH C 765 8.047 39.229 10.268 1.00 47.93 O HETATM 6145 O HOH C 766 21.148 11.088 23.484 1.00 30.99 O HETATM 6146 O HOH C 767 -12.485 18.630 -1.214 1.00 50.45 O HETATM 6147 O HOH C 768 20.627 29.660 -9.383 1.00 34.70 O HETATM 6148 O HOH C 769 13.560 42.214 3.721 1.00 52.34 O HETATM 6149 O HOH C 770 -14.402 26.181 -9.203 1.00 48.38 O HETATM 6150 O HOH C 771 39.144 26.736 -1.148 1.00 39.11 O HETATM 6151 O HOH C 772 23.224 17.940 17.637 1.00 29.14 O HETATM 6152 O HOH C 773 35.826 18.184 -4.791 1.00 40.38 O HETATM 6153 O HOH C 774 -12.155 26.169 3.419 1.00 41.83 O HETATM 6154 O HOH C 775 32.103 17.476 10.691 1.00 51.17 O HETATM 6155 O HOH C 776 -2.623 10.168 3.051 1.00 36.53 O HETATM 6156 O HOH C 777 32.042 14.782 -13.189 1.00 32.01 O HETATM 6157 O HOH C 778 6.369 27.766 -1.963 1.00 19.26 O HETATM 6158 O HOH C 779 -0.414 8.390 25.662 1.00 50.05 O HETATM 6159 O HOH C 780 22.329 7.629 -10.126 1.00 45.15 O HETATM 6160 O HOH C 781 29.525 18.033 9.727 1.00 39.78 O HETATM 6161 O HOH C 782 11.341 40.343 2.383 1.00 43.67 O HETATM 6162 O HOH C 783 28.553 10.087 -11.662 1.00 24.30 O HETATM 6163 O HOH C 784 10.079 37.894 1.527 1.00 36.10 O HETATM 6164 O HOH C 785 7.037 7.229 2.358 1.00 27.34 O HETATM 6165 O HOH C 786 -9.596 20.673 6.935 1.00 47.59 O HETATM 6166 O HOH C 787 14.416 31.823 -7.159 1.00 39.45 O HETATM 6167 O HOH C 788 3.240 24.269 -14.795 1.00 13.53 O HETATM 6168 O HOH C 789 0.004 37.847 -2.456 1.00 48.31 O HETATM 6169 O HOH C 790 30.056 30.574 -15.125 1.00 32.50 O HETATM 6170 O HOH C 791 4.687 4.771 -1.347 1.00 42.44 O HETATM 6171 O HOH C 792 2.508 8.810 -0.034 1.00 30.01 O HETATM 6172 O HOH C 793 22.241 23.110 20.048 1.00 47.37 O HETATM 6173 O HOH C 794 32.292 28.593 -16.336 1.00 31.54 O HETATM 6174 O HOH C 795 16.536 5.918 4.367 1.00 30.59 O HETATM 6175 O HOH C 796 15.424 25.451 -8.722 1.00 37.59 O HETATM 6176 O HOH C 797 -4.296 9.832 8.100 1.00 19.45 O HETATM 6177 O HOH C 798 8.294 30.337 18.291 1.00 36.41 O HETATM 6178 O HOH C 799 7.854 19.944 25.501 1.00 24.40 O HETATM 6179 O HOH C 800 8.494 16.737 9.710 1.00 26.69 O HETATM 6180 O HOH C 801 -10.497 31.493 -6.214 1.00 53.58 O HETATM 6181 O HOH C 802 19.998 31.841 -6.019 1.00 44.01 O HETATM 6182 O HOH C 803 12.529 36.104 3.679 1.00 20.95 O HETATM 6183 O HOH C 804 7.408 7.278 4.954 1.00 38.77 O HETATM 6184 O HOH C 805 0.388 40.177 -0.803 1.00 47.01 O HETATM 6185 O HOH C 806 -2.447 7.521 7.403 1.00 32.03 O HETATM 6186 O HOH C 807 7.904 4.739 0.576 1.00 34.84 O HETATM 6187 O HOH C 808 1.720 5.178 18.994 1.00 49.28 O HETATM 6188 O HOH C 809 23.506 20.728 16.120 1.00 44.36 O HETATM 6189 O HOH C 810 22.848 27.175 -5.738 1.00 33.03 O HETATM 6190 O HOH C 811 14.878 25.432 -11.100 1.00 33.50 O HETATM 6191 O HOH C 812 34.329 13.812 -12.633 1.00 35.63 O HETATM 6192 O HOH C 813 28.615 10.519 8.651 1.00 49.73 O HETATM 6193 O HOH C 814 -2.193 34.359 12.301 1.00 28.67 O HETATM 6194 O HOH C 815 6.785 2.542 12.237 1.00 33.47 O HETATM 6195 O HOH C 816 2.114 6.172 -15.789 1.00 29.40 O HETATM 6196 O HOH C 817 28.534 20.430 -20.698 1.00 43.60 O HETATM 6197 O HOH C 818 26.127 8.916 -11.990 1.00 34.50 O HETATM 6198 O HOH C 819 11.717 9.219 9.094 1.00 38.66 O HETATM 6199 O HOH C 820 6.349 5.199 -15.566 1.00 39.02 O HETATM 6200 O HOH C 821 -0.568 14.247 21.219 1.00 41.88 O HETATM 6201 O HOH C 822 2.377 31.700 -13.596 1.00 35.19 O HETATM 6202 O HOH C 823 10.361 18.808 18.927 1.00 39.15 O HETATM 6203 O HOH C 824 -0.158 7.641 -11.412 1.00 33.19 O HETATM 6204 O HOH C 825 24.195 18.125 20.214 1.00 34.84 O HETATM 6205 O HOH C 826 5.459 39.824 8.265 1.00 27.96 O HETATM 6206 O HOH C 827 27.885 9.122 2.354 1.00 35.64 O HETATM 6207 O HOH C 828 31.703 19.458 -11.428 1.00 27.20 O HETATM 6208 O HOH C 829 1.291 8.107 -9.499 1.00 25.17 O HETATM 6209 O HOH C 830 25.402 7.246 -8.225 1.00 53.58 O HETATM 6210 O HOH C 831 -7.191 15.600 -1.008 1.00 37.81 O HETATM 6211 O HOH C 832 2.191 38.461 -4.787 1.00 47.21 O HETATM 6212 O HOH C 833 39.969 25.384 1.109 1.00 34.32 O HETATM 6213 O HOH C 834 4.128 6.734 1.194 1.00 32.07 O HETATM 6214 O HOH C 835 8.906 27.911 -27.523 1.00 40.18 O HETATM 6215 O HOH C 836 17.889 22.091 20.237 1.00 45.61 O HETATM 6216 O HOH C 837 23.115 4.150 -7.491 1.00 41.72 O HETATM 6217 O HOH C 838 -0.948 9.277 -0.994 1.00 35.13 O HETATM 6218 O HOH C 839 -4.447 11.511 3.241 1.00 47.69 O HETATM 6219 O HOH C 840 27.047 8.917 6.684 1.00 40.44 O HETATM 6220 O HOH C 841 12.863 38.682 4.570 1.00 33.34 O HETATM 6221 O HOH C 842 9.997 29.552 20.055 1.00 41.55 O HETATM 6222 O HOH C 843 9.976 26.900 20.986 1.00 27.60 O HETATM 6223 O HOH C 844 13.811 40.378 5.708 1.00 39.12 O HETATM 6224 O HOH C 845 -2.706 9.178 1.119 1.00 48.40 O HETATM 6225 O HOH C 846 6.138 34.840 18.856 1.00 39.84 O HETATM 6226 O HOH C 847 18.429 35.053 -12.709 1.00 44.11 O HETATM 6227 O HOH D 101 14.961 41.457 -7.435 1.00 50.72 O HETATM 6228 O HOH D 102 38.396 34.167 -13.772 1.00 57.30 O HETATM 6229 O HOH D 103 37.969 46.750 5.462 1.00 44.44 O HETATM 6230 O HOH D 104 26.304 34.548 6.958 1.00 31.73 O HETATM 6231 O HOH D 105 35.249 34.962 -11.703 1.00 33.10 O HETATM 6232 O HOH D 106 21.141 29.243 -1.168 1.00 20.83 O HETATM 6233 O HOH D 107 28.819 31.877 0.855 1.00 38.11 O HETATM 6234 O HOH D 108 32.334 38.462 -4.622 1.00 32.49 O HETATM 6235 O HOH D 109 20.666 36.823 -6.031 1.00 29.06 O HETATM 6236 O HOH D 110 44.595 50.638 -9.557 1.00 40.31 O HETATM 6237 O HOH D 111 20.677 32.680 -3.178 1.00 30.93 O HETATM 6238 O HOH D 112 37.614 44.640 4.216 1.00 49.11 O HETATM 6239 O HOH D 113 42.166 42.526 -8.586 1.00 53.96 O HETATM 6240 O HOH D 114 44.368 43.173 -8.447 1.00 55.30 O HETATM 6241 O HOH D 115 39.576 43.301 3.767 1.00 44.05 O HETATM 6242 O HOH D 116 16.254 34.871 -10.708 1.00 44.47 O CONECT 547 2850 CONECT 2846 2848 CONECT 2848 2846 2849 CONECT 2849 2848 2850 CONECT 2850 547 2849 CONECT 3408 5608 CONECT 5604 5606 CONECT 5606 5604 5607 CONECT 5607 5606 5608 CONECT 5608 3408 5607 CONECT 5610 5611 5612 CONECT 5611 5610 CONECT 5612 5610 5613 5614 CONECT 5613 5612 CONECT 5614 5612 5615 CONECT 5615 5614 CONECT 5616 5617 5618 CONECT 5617 5616 CONECT 5618 5616 5619 5620 CONECT 5619 5618 CONECT 5620 5618 5621 CONECT 5621 5620 MASTER 466 0 4 32 30 0 12 6 6150 4 22 58 END
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Check Database
Protein Sequence Similarity
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RCSB PDB
PDBbind
76aa, >1CMX_2|Chains... at 100%
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PDBbind
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2hd5
RCSB PDB
PDBbind
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PDBbind
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2y5b
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PDBbind
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RCSB PDB
PDBbind
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3dvn
RCSB PDB
PDBbind
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3kw5
RCSB PDB
PDBbind
75aa, >3KW5_2|Chain... at 100%
3olm
RCSB PDB
PDBbind
79aa, >3OLM_2|Chain... at 92%
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RCSB PDB
PDBbind
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3znz
RCSB PDB
PDBbind
152aa, >3ZNZ_2|Chain... at 100%
4i6l
RCSB PDB
PDBbind
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4m0w
RCSB PDB
PDBbind
76aa, >4M0W_2|Chain... at 100%
5e6j
RCSB PDB
PDBbind
76aa, >5E6J_2|Chains... at 97%
5gvi
RCSB PDB
PDBbind
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5l6h
RCSB PDB
PDBbind
76aa, >5L6H_2|Chains... at 96%
5l6i
RCSB PDB
PDBbind
76aa, >5L6I_2|Chains... at 96%
5l6j
RCSB PDB
PDBbind
76aa, >5L6J_2|Chains... at 96%
5ohp
RCSB PDB
PDBbind
76aa, >5OHP_2|Chains... at 100%
5ydr
RCSB PDB
PDBbind
75aa, >5YDR_1|Chains... at 97%
5yij
RCSB PDB
PDBbind
78aa, >5YIJ_2|Chains... at 97%
6isu
RCSB PDB
PDBbind
76aa, >6ISU_3|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
5lrw
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Cezanne/OTUD7B OTU domain
Ligand Name
Mono-ubiquitin
EC.Number
E.C.3.4.19.12
Resolution
2(Å)
Affinity (Kd/Ki/IC50)
Kd=9.3uM
Release Year
2016
Protein/NA Sequence
Check fasta file
Primary Reference
(2016) Nature Vol. 538: pp. 402-405
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q6GQQ9
P0CG47
Entrez Gene ID
NCBI Entrez Gene ID:
56957
7314
ASD
Information of known allosteric effects of PDB entries
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