HEADER MEMBRANE PROTEIN 06-SEP-17 5YC8 TITLE CRYSTAL STRUCTURE OF RATIONALLY THERMOSTABILIZED M2 MUSCARINIC TITLE 2 ACETYLCHOLINE RECEPTOR BOUND WITH NMS (HG-DERIVATIVE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M2,REDESIGNED APO- COMPND 3 CYTOCHROME B562,MUSCARINIC ACETYLCHOLINE RECEPTOR M2; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP RESIDUES 10-214,UNP RESIDUES 377-466; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CHRM2; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR CRYSTALLOGRAPHY, RATIONALLY THERMOSTABILIZED MUTANT, MEMBRANE KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR R.SUNO,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA,M.S.TAWARAMOTO, AUTHOR 2 H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO,B.K.KOBILKA,S.IWATA, AUTHOR 3 T.KOBAYASHI REVDAT 3 26-FEB-20 5YC8 1 REMARK REVDAT 2 28-NOV-18 5YC8 1 JRNL REVDAT 1 21-NOV-18 5YC8 0 JRNL AUTH R.SUNO,S.LEE,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA, JRNL AUTH 2 M.S.TAWARAMOTO,H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO, JRNL AUTH 3 B.K.KOBILKA,N.VAIDEHI,S.IWATA,T.KOBAYASHI JRNL TITL STRUCTURAL INSIGHTS INTO THE SUBTYPE-SELECTIVE ANTAGONIST JRNL TITL 2 BINDING TO THE M2MUSCARINIC RECEPTOR JRNL REF NAT. CHEM. BIOL. V. 14 1150 2018 JRNL REFN ESSN 1552-4469 JRNL PMID 30420692 JRNL DOI 10.1038/S41589-018-0152-Y REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.03 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 32414 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.239 REMARK 3 R VALUE (WORKING SET) : 0.237 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.330 REMARK 3 FREE R VALUE TEST SET COUNT : 1728 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 49.0399 - 5.7211 1.00 2557 135 0.2053 0.2002 REMARK 3 2 5.7211 - 4.5421 1.00 2544 153 0.2342 0.3491 REMARK 3 3 4.5421 - 3.9682 1.00 2539 149 0.2067 0.2385 REMARK 3 4 3.9682 - 3.6055 1.00 2577 139 0.2147 0.2167 REMARK 3 5 3.6055 - 3.3471 1.00 2541 149 0.2437 0.2909 REMARK 3 6 3.3471 - 3.1498 1.00 2563 138 0.2499 0.3040 REMARK 3 7 3.1498 - 2.9921 1.00 2587 152 0.2534 0.2868 REMARK 3 8 2.9921 - 2.8619 1.00 2581 140 0.2538 0.2405 REMARK 3 9 2.8619 - 2.7517 1.00 2517 143 0.2668 0.2925 REMARK 3 10 2.7517 - 2.6568 1.00 2575 140 0.2811 0.3251 REMARK 3 11 2.6568 - 2.5737 1.00 2544 141 0.2976 0.3626 REMARK 3 12 2.5737 - 2.5001 1.00 2561 149 0.3151 0.2953 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) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.230 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 36.98 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.55 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 3144 REMARK 3 ANGLE : 0.491 4291 REMARK 3 CHIRALITY : 0.036 511 REMARK 3 PLANARITY : 0.004 518 REMARK 3 DIHEDRAL : 11.470 1887 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 92 ) REMARK 3 ORIGIN FOR THE GROUP (A): 171.2794 35.5983 533.1464 REMARK 3 T TENSOR REMARK 3 T11: 0.2299 T22: 0.1279 REMARK 3 T33: 0.3072 T12: -0.0063 REMARK 3 T13: 0.0419 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 2.9517 L22: 1.9012 REMARK 3 L33: 5.0678 L12: -1.3240 REMARK 3 L13: -0.0509 L23: -0.9372 REMARK 3 S TENSOR REMARK 3 S11: -0.0339 S12: -0.0197 S13: 0.0379 REMARK 3 S21: 0.1806 S22: 0.0876 S23: 0.0369 REMARK 3 S31: -0.0855 S32: -0.0135 S33: -0.0491 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 195 ) REMARK 3 ORIGIN FOR THE GROUP (A): 189.3543 31.5579 531.8703 REMARK 3 T TENSOR REMARK 3 T11: 0.1814 T22: 0.3444 REMARK 3 T33: 0.3042 T12: -0.0266 REMARK 3 T13: -0.0093 T23: -0.0306 REMARK 3 L TENSOR REMARK 3 L11: 1.0286 L22: 3.1597 REMARK 3 L33: 2.2668 L12: -0.0534 REMARK 3 L13: -0.5354 L23: -1.5175 REMARK 3 S TENSOR REMARK 3 S11: -0.0450 S12: -0.1159 S13: -0.0089 REMARK 3 S21: 0.1431 S22: -0.0691 S23: -0.1798 REMARK 3 S31: -0.0775 S32: 0.4821 S33: 0.1247 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 196 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 187.2912 14.5998 542.8896 REMARK 3 T TENSOR REMARK 3 T11: 0.3128 T22: 0.2423 REMARK 3 T33: 0.4094 T12: 0.2139 REMARK 3 T13: -0.0414 T23: -0.0464 REMARK 3 L TENSOR REMARK 3 L11: 9.2411 L22: 4.9400 REMARK 3 L33: 3.9767 L12: 0.2672 REMARK 3 L13: 2.3510 L23: 4.1478 REMARK 3 S TENSOR REMARK 3 S11: -0.5545 S12: -1.4465 S13: -0.1992 REMARK 3 S21: 0.8484 S22: -0.2629 S23: -0.3691 REMARK 3 S31: 0.5828 S32: -0.1705 S33: 0.4097 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 214 OR (RESID 1001 THROUGH 1018 REMARK 3 )) REMARK 3 ORIGIN FOR THE GROUP (A): 171.4089 15.6593 564.9558 REMARK 3 T TENSOR REMARK 3 T11: 1.0357 T22: 1.2940 REMARK 3 T33: 0.6365 T12: 0.1233 REMARK 3 T13: -0.0956 T23: 0.2048 REMARK 3 L TENSOR REMARK 3 L11: 2.5351 L22: 2.5431 REMARK 3 L33: 6.9746 L12: 0.3312 REMARK 3 L13: -3.1885 L23: 2.3119 REMARK 3 S TENSOR REMARK 3 S11: -0.4781 S12: 0.1843 S13: 0.6829 REMARK 3 S21: -0.0044 S22: 0.5962 S23: -0.6168 REMARK 3 S31: 0.3429 S32: 0.9740 S33: -0.1149 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1019 THROUGH 1055 ) REMARK 3 ORIGIN FOR THE GROUP (A): 170.8885 12.1420 572.0083 REMARK 3 T TENSOR REMARK 3 T11: 1.1523 T22: 1.0724 REMARK 3 T33: 0.6809 T12: 0.1194 REMARK 3 T13: 0.0159 T23: 0.1335 REMARK 3 L TENSOR REMARK 3 L11: 5.8933 L22: 3.9776 REMARK 3 L33: 5.0177 L12: -0.8819 REMARK 3 L13: 1.3870 L23: -0.7141 REMARK 3 S TENSOR REMARK 3 S11: -0.5176 S12: -1.0348 S13: -1.0520 REMARK 3 S21: -0.2423 S22: 0.9351 S23: -0.1027 REMARK 3 S31: 0.0596 S32: 0.0059 S33: -0.3913 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1056 THROUGH 1080 ) REMARK 3 ORIGIN FOR THE GROUP (A): 166.2800 13.0564 579.2525 REMARK 3 T TENSOR REMARK 3 T11: 1.2812 T22: 2.0207 REMARK 3 T33: 0.8937 T12: -0.2015 REMARK 3 T13: -0.2933 T23: 0.6049 REMARK 3 L TENSOR REMARK 3 L11: 3.5510 L22: 1.1517 REMARK 3 L33: 1.0496 L12: -0.1404 REMARK 3 L13: 0.1627 L23: 0.8748 REMARK 3 S TENSOR REMARK 3 S11: 0.1989 S12: 0.1491 S13: -0.1460 REMARK 3 S21: -0.3501 S22: 0.4398 S23: 0.3519 REMARK 3 S31: 1.2204 S32: -0.6321 S33: -0.2912 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 1081 THROUGH 1106) OR (RESID REMARK 3 380 THROUGH 380) ) REMARK 3 ORIGIN FOR THE GROUP (A): 163.9257 20.7694 573.7725 REMARK 3 T TENSOR REMARK 3 T11: 1.0513 T22: 1.1839 REMARK 3 T33: 0.8708 T12: -0.0653 REMARK 3 T13: -0.0272 T23: 0.0382 REMARK 3 L TENSOR REMARK 3 L11: 2.6101 L22: 2.2436 REMARK 3 L33: 2.8567 L12: -0.0290 REMARK 3 L13: 2.6263 L23: 0.6209 REMARK 3 S TENSOR REMARK 3 S11: 0.1238 S12: -1.5875 S13: -0.2652 REMARK 3 S21: 0.5571 S22: -0.0435 S23: 0.1469 REMARK 3 S31: -0.2252 S32: -0.4471 S33: -0.1339 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 381 THROUGH 411 ) REMARK 3 ORIGIN FOR THE GROUP (A): 179.2281 19.6999 536.7767 REMARK 3 T TENSOR REMARK 3 T11: 0.1757 T22: 0.1305 REMARK 3 T33: 0.3089 T12: 0.0157 REMARK 3 T13: -0.0222 T23: 0.0132 REMARK 3 L TENSOR REMARK 3 L11: 4.7166 L22: 4.7700 REMARK 3 L33: 6.7199 L12: 0.1995 REMARK 3 L13: -1.1294 L23: -0.4819 REMARK 3 S TENSOR REMARK 3 S11: -0.0327 S12: -0.4238 S13: -0.0982 REMARK 3 S21: 0.2461 S22: 0.0583 S23: 0.0064 REMARK 3 S31: -0.2774 S32: -0.1065 S33: -0.0170 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 458 ) REMARK 3 ORIGIN FOR THE GROUP (A): 171.2249 28.8013 536.3583 REMARK 3 T TENSOR REMARK 3 T11: 0.2861 T22: 0.2906 REMARK 3 T33: 0.3238 T12: -0.0422 REMARK 3 T13: -0.0504 T23: 0.0640 REMARK 3 L TENSOR REMARK 3 L11: 1.9880 L22: 3.9672 REMARK 3 L33: 7.7310 L12: -0.5002 REMARK 3 L13: -2.0777 L23: 3.5509 REMARK 3 S TENSOR REMARK 3 S11: 0.0086 S12: -0.2813 S13: 0.0312 REMARK 3 S21: 0.3112 S22: -0.0882 S23: 0.1573 REMARK 3 S31: -0.0459 S32: -0.0488 S33: 0.1104 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 5YC8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-SEP-17. REMARK 100 THE DEPOSITION ID IS D_1300005015. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-OCT-15 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 : SPRING-8 REMARK 200 BEAMLINE : BL32XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225-HS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32428 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 49.030 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 12.49 REMARK 200 R MERGE (I) : 0.48700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 12.10 REMARK 200 R MERGE FOR SHELL (I) : 4.97900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.060 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: PHENIX 1.11.1_2575 REMARK 200 STARTING MODEL: 5XBB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES-NAOH PH 6.2-7.0, 26-32% REMARK 280 PEG300, 300~500MM AMMONIUM FLUORIDE, 1% 1,2,3-HEPTANETRIOL, REMARK 280 0.5MM NMS AND 5% DMSO, 1MM HGCL2, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.50000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 330 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20850 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 GLY A -1 REMARK 465 PRO A 0 REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 ASP A 3 REMARK 465 SER A 4 REMARK 465 THR A 5 REMARK 465 ASP A 6 REMARK 465 SER A 7 REMARK 465 SER A 8 REMARK 465 ASP A 9 REMARK 465 ASN A 10 REMARK 465 SER A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 LEU A 14 REMARK 465 THR A 15 REMARK 465 SER A 998 REMARK 465 ARG A 999 REMARK 465 ILE A 1000 REMARK 465 PRO A 377 REMARK 465 PRO A 378 REMARK 465 PRO A 379 REMARK 465 TYR A 459 REMARK 465 LYS A 460 REMARK 465 ASN A 461 REMARK 465 ILE A 462 REMARK 465 GLY A 463 REMARK 465 ALA A 464 REMARK 465 THR A 465 REMARK 465 ARG A 466 REMARK 465 LEU A 467 REMARK 465 GLU A 468 REMARK 465 VAL A 469 REMARK 465 LEU A 470 REMARK 465 PHE A 471 REMARK 465 GLN A 472 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 A1057 CG CD OE1 OE2 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 THR A 130 -50.58 -135.34 REMARK 500 PHE A 195 -57.48 -129.59 REMARK 500 PRO A1046 76.80 -61.80 REMARK 500 CYS A 413 87.25 -153.59 REMARK 500 TYR A 440 -36.81 -137.91 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 622 DISTANCE = 6.58 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HG A 504 HG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ILE A 435 O REMARK 620 2 CYS A 439 SG 79.2 REMARK 620 N 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5XBA RELATED DB: PDB REMARK 900 RELATED ID: 5XB9 RELATED DB: PDB REMARK 900 RELATED ID: 5XBG RELATED DB: PDB REMARK 900 RELATED ID: 5XBB RELATED DB: PDB DBREF 5YC8 A 10 214 UNP P08172 ACM2_HUMAN 10 214 DBREF 5YC8 A 998 1106 PDB 5YC8 5YC8 998 1106 DBREF 5YC8 A 326 466 UNP P08172 ACM2_HUMAN 377 466 SEQADV 5YC8 GLY A -1 UNP P08172 EXPRESSION TAG SEQADV 5YC8 PRO A 0 UNP P08172 EXPRESSION TAG SEQADV 5YC8 MET A 1 UNP P08172 EXPRESSION TAG SEQADV 5YC8 ASP A 2 UNP P08172 EXPRESSION TAG SEQADV 5YC8 ASP A 3 UNP P08172 EXPRESSION TAG SEQADV 5YC8 SER A 4 UNP P08172 EXPRESSION TAG SEQADV 5YC8 THR A 5 UNP P08172 EXPRESSION TAG SEQADV 5YC8 ASP A 6 UNP P08172 EXPRESSION TAG SEQADV 5YC8 SER A 7 UNP P08172 EXPRESSION TAG SEQADV 5YC8 SER A 8 UNP P08172 EXPRESSION TAG SEQADV 5YC8 ASP A 9 UNP P08172 EXPRESSION TAG SEQADV 5YC8 ARG A 110 UNP P08172 SER 110 ENGINEERED MUTATION SEQADV 5YC8 LEU A 467 UNP P08172 EXPRESSION TAG SEQADV 5YC8 GLU A 468 UNP P08172 EXPRESSION TAG SEQADV 5YC8 VAL A 469 UNP P08172 EXPRESSION TAG SEQADV 5YC8 LEU A 470 UNP P08172 EXPRESSION TAG SEQADV 5YC8 PHE A 471 UNP P08172 EXPRESSION TAG SEQADV 5YC8 GLN A 472 UNP P08172 EXPRESSION TAG SEQRES 1 A 421 GLY PRO MET ASP ASP SER THR ASP SER SER ASP ASN SER SEQRES 2 A 421 LEU ALA LEU THR SER PRO TYR LYS THR PHE GLU VAL VAL SEQRES 3 A 421 PHE ILE VAL LEU VAL ALA GLY SER LEU SER LEU VAL THR SEQRES 4 A 421 ILE ILE GLY ASN ILE LEU VAL MET VAL SER ILE LYS VAL SEQRES 5 A 421 ASN ARG HIS LEU GLN THR VAL ASN ASN TYR PHE LEU PHE SEQRES 6 A 421 SER LEU ALA CYS ALA ASP LEU ILE ILE GLY VAL PHE SER SEQRES 7 A 421 MET ASN LEU TYR THR LEU TYR THR VAL ILE GLY TYR TRP SEQRES 8 A 421 PRO LEU GLY PRO VAL VAL CYS ASP LEU TRP LEU ALA LEU SEQRES 9 A 421 ASP TYR VAL VAL SER ASN ALA ARG VAL MET ASN LEU LEU SEQRES 10 A 421 ILE ILE SER PHE ASP ARG TYR PHE CYS VAL THR LYS PRO SEQRES 11 A 421 LEU THR TYR PRO VAL LYS ARG THR THR LYS MET ALA GLY SEQRES 12 A 421 MET MET ILE ALA ALA ALA TRP VAL LEU SER PHE ILE LEU SEQRES 13 A 421 TRP ALA PRO ALA ILE LEU PHE TRP GLN PHE ILE VAL GLY SEQRES 14 A 421 VAL ARG THR VAL GLU ASP GLY GLU CYS TYR ILE GLN PHE SEQRES 15 A 421 PHE SER ASN ALA ALA VAL THR PHE GLY THR ALA ILE ALA SEQRES 16 A 421 ALA PHE TYR LEU PRO VAL ILE ILE MET THR VAL LEU TYR SEQRES 17 A 421 TRP HIS ILE SER ARG ALA SER LYS SER ARG ILE ALA ASP SEQRES 18 A 421 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 19 A 421 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 20 A 421 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 21 A 421 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 22 A 421 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 23 A 421 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 24 A 421 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 25 A 421 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 26 A 421 PRO PRO PRO SER ARG GLU LYS LYS VAL THR ARG THR ILE SEQRES 27 A 421 LEU ALA ILE LEU LEU ALA PHE ILE ILE THR TRP ALA PRO SEQRES 28 A 421 TYR ASN VAL MET VAL LEU ILE ASN THR PHE CYS ALA PRO SEQRES 29 A 421 CYS ILE PRO ASN THR VAL TRP THR ILE GLY TYR TRP LEU SEQRES 30 A 421 CYS TYR ILE ASN SER THR ILE ASN PRO ALA CYS TYR ALA SEQRES 31 A 421 LEU CYS ASN ALA THR PHE LYS LYS THR PHE LYS HIS LEU SEQRES 32 A 421 LEU MET CYS HIS TYR LYS ASN ILE GLY ALA THR ARG LEU SEQRES 33 A 421 GLU VAL LEU PHE GLN HET 3C0 A 501 23 HET HG A 502 1 HET HG A 503 1 HET HG A 504 1 HETNAM 3C0 N-METHYL SCOPOLAMINE HETNAM HG MERCURY (II) ION HETSYN 3C0 (1R,2R,4S,5S,7S)-7-{[(2S)-3-HYDROXY-2- HETSYN 2 3C0 PHENYLPROPANOYL]OXY}-9,9-DIMETHYL-3-OXA-9- HETSYN 3 3C0 AZONIATRICYCLO[3.3.1.0~2,4~]NONANE FORMUL 2 3C0 C18 H24 N O4 1+ FORMUL 3 HG 3(HG 2+) FORMUL 6 HOH *22(H2 O) HELIX 1 AA1 SER A 16 ASN A 51 1 36 HELIX 2 AA2 ARG A 52 GLN A 55 5 4 HELIX 3 AA3 THR A 56 PHE A 75 1 20 HELIX 4 AA4 PHE A 75 GLY A 87 1 13 HELIX 5 AA5 GLY A 92 LYS A 127 1 36 HELIX 6 AA6 TYR A 131 ARG A 135 5 5 HELIX 7 AA7 THR A 136 GLY A 167 1 32 HELIX 8 AA8 ILE A 178 SER A 182 5 5 HELIX 9 AA9 ASN A 183 PHE A 195 1 13 HELIX 10 AB1 PHE A 195 LYS A 214 1 20 HELIX 11 AB2 ASP A 1002 LYS A 1019 1 18 HELIX 12 AB3 ALA A 1023 LYS A 1042 1 20 HELIX 13 AB4 SER A 1055 GLY A 1082 1 28 HELIX 14 AB5 LYS A 1083 TYR A 1101 1 19 HELIX 15 AB6 ARG A 381 THR A 411 1 31 HELIX 16 AB7 PHE A 412 ILE A 417 5 6 HELIX 17 AB8 PRO A 418 ASN A 436 1 19 HELIX 18 AB9 PRO A 437 CYS A 443 5 7 HELIX 19 AC1 ASN A 444 MET A 456 1 13 SSBOND 1 CYS A 96 CYS A 176 1555 1555 2.03 SSBOND 2 CYS A 413 CYS A 416 1555 1555 2.03 LINK SG CYS A 67 HG HG A 502 1555 1555 2.64 LINK SG CYS A 67 HG HG A 503 1555 1555 2.68 LINK O ILE A 435 HG HG A 504 1555 1555 2.98 LINK SG CYS A 439 HG HG A 504 1555 1555 2.63 CRYST1 46.520 59.000 89.220 90.00 98.89 90.00 P 1 21 1 2 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 0.021496 0.000000 0.003364 0.00000 SCALE2 0.000000 0.016949 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011345 0.00000 ATOM 1 N SER A 16 152.412 30.543 507.343 1.00 97.56 N ANISOU 1 N SER A 16 9859 16616 10593 -503 -2595 -1664 N ATOM 2 CA SER A 16 153.280 29.818 508.263 1.00 94.86 C ANISOU 2 CA SER A 16 9745 15827 10469 -714 -2543 -1782 C ATOM 3 C SER A 16 153.030 30.238 509.709 1.00 92.26 C ANISOU 3 C SER A 16 9231 15421 10401 -810 -2363 -1557 C ATOM 4 O SER A 16 153.798 31.018 510.274 1.00 89.65 O ANISOU 4 O SER A 16 8939 15016 10107 -582 -2156 -1415 O ATOM 5 CB SER A 16 154.748 30.041 507.898 1.00 92.14 C ANISOU 5 CB SER A 16 9695 15325 9988 -419 -2436 -1864 C ATOM 6 OG SER A 16 155.605 29.373 508.806 1.00 90.76 O ANISOU 6 OG SER A 16 9752 14702 10029 -590 -2358 -1965 O ATOM 7 N PRO A 17 151.954 29.720 510.311 1.00103.09 N ANISOU 7 N PRO A 17 10413 16799 11958 -1139 -2432 -1510 N ATOM 8 CA PRO A 17 151.640 30.081 511.700 1.00101.10 C ANISOU 8 CA PRO A 17 9985 16488 11940 -1216 -2245 -1282 C ATOM 9 C PRO A 17 152.471 29.348 512.738 1.00 98.81 C ANISOU 9 C PRO A 17 9918 15738 11885 -1444 -2164 -1363 C ATOM 10 O PRO A 17 152.396 29.700 513.923 1.00 97.25 O ANISOU 10 O PRO A 17 9612 15473 11866 -1467 -1982 -1172 O ATOM 11 CB PRO A 17 150.160 29.703 511.824 1.00105.03 C ANISOU 11 CB PRO A 17 10203 17185 12519 -1470 -2356 -1208 C ATOM 12 CG PRO A 17 150.009 28.551 510.891 1.00108.66 C ANISOU 12 CG PRO A 17 10813 17547 12925 -1727 -2636 -1487 C ATOM 13 CD PRO A 17 150.941 28.819 509.732 1.00107.86 C ANISOU 13 CD PRO A 17 10944 17482 12556 -1435 -2683 -1645 C ATOM 14 N TYR A 18 153.254 28.347 512.343 1.00137.13 N ANISOU 14 N TYR A 18 15102 20265 16737 -1585 -2280 -1632 N ATOM 15 CA TYR A 18 154.032 27.584 513.310 1.00135.77 C ANISOU 15 CA TYR A 18 15176 19624 16785 -1786 -2193 -1707 C ATOM 16 C TYR A 18 155.459 28.104 513.444 1.00134.26 C ANISOU 16 C TYR A 18 15280 19157 16575 -1440 -1966 -1661 C ATOM 17 O TYR A 18 155.981 28.194 514.560 1.00132.82 O ANISOU 17 O TYR A 18 15194 18685 16587 -1435 -1761 -1527 O ATOM 18 CB TYR A 18 154.044 26.103 512.921 1.00138.09 C ANISOU 18 CB TYR A 18 15758 19574 17136 -2086 -2395 -1955 C ATOM 19 CG TYR A 18 154.257 25.161 514.084 1.00137.61 C ANISOU 19 CG TYR A 18 15873 19050 17363 -2372 -2324 -1941 C ATOM 20 CD1 TYR A 18 155.519 24.975 514.631 1.00134.97 C ANISOU 20 CD1 TYR A 18 15835 18355 17094 -2282 -2170 -2002 C ATOM 21 CD2 TYR A 18 153.195 24.450 514.630 1.00140.40 C ANISOU 21 CD2 TYR A 18 16088 19331 17927 -2701 -2400 -1859 C ATOM 22 CE1 TYR A 18 155.718 24.115 515.693 1.00134.49 C ANISOU 22 CE1 TYR A 18 15952 17868 17280 -2502 -2092 -1958 C ATOM 23 CE2 TYR A 18 153.385 23.586 515.692 1.00140.22 C ANISOU 23 CE2 TYR A 18 16224 18886 18167 -2917 -2317 -1824 C ATOM 24 CZ TYR A 18 154.649 23.423 516.219 1.00137.15 C ANISOU 24 CZ TYR A 18 16154 18138 17821 -2808 -2165 -1863 C ATOM 25 OH TYR A 18 154.849 22.566 517.277 1.00137.10 O ANISOU 25 OH TYR A 18 16308 17721 18063 -2975 -2067 -1810 O ATOM 26 N LYS A 19 156.099 28.451 512.324 1.00 95.18 N ANISOU 26 N LYS A 19 10469 14308 11388 -1147 -1994 -1754 N ATOM 27 CA LYS A 19 157.459 28.977 512.378 1.00 94.05 C ANISOU 27 CA LYS A 19 10574 13939 11222 -827 -1773 -1681 C ATOM 28 C LYS A 19 157.516 30.320 513.094 1.00 92.87 C ANISOU 28 C LYS A 19 10274 13865 11146 -599 -1523 -1364 C ATOM 29 O LYS A 19 158.554 30.671 513.668 1.00 91.76 O ANISOU 29 O LYS A 19 10309 13458 11097 -458 -1320 -1269 O ATOM 30 CB LYS A 19 158.030 29.106 510.965 1.00 94.93 C ANISOU 30 CB LYS A 19 10822 14207 11039 -556 -1850 -1815 C ATOM 31 CG LYS A 19 158.086 27.796 510.192 1.00 96.14 C ANISOU 31 CG LYS A 19 11190 14259 11081 -728 -2101 -2165 C ATOM 32 CD LYS A 19 159.030 26.799 510.847 1.00 95.41 C ANISOU 32 CD LYS A 19 11433 13663 11155 -843 -2038 -2293 C ATOM 33 CE LYS A 19 159.115 25.511 510.042 1.00 96.75 C ANISOU 33 CE LYS A 19 11874 13689 11197 -975 -2283 -2657 C ATOM 34 NZ LYS A 19 160.061 24.532 510.644 1.00 96.03 N ANISOU 34 NZ LYS A 19 12141 13098 11248 -1033 -2212 -2772 N ATOM 35 N THR A 20 156.421 31.082 513.072 1.00 57.75 N ANISOU 35 N THR A 20 5510 9780 6652 -554 -1539 -1202 N ATOM 36 CA THR A 20 156.379 32.341 513.807 1.00 56.55 C ANISOU 36 CA THR A 20 5248 9671 6568 -332 -1307 -914 C ATOM 37 C THR A 20 156.206 32.107 515.303 1.00 55.47 C ANISOU 37 C THR A 20 5080 9303 6692 -531 -1190 -821 C ATOM 38 O THR A 20 156.788 32.831 516.118 1.00 54.13 O ANISOU 38 O THR A 20 5000 8946 6621 -376 -976 -665 O ATOM 39 CB THR A 20 155.252 33.228 513.276 1.00 57.07 C ANISOU 39 CB THR A 20 4999 10213 6472 -161 -1354 -764 C ATOM 40 OG1 THR A 20 153.998 32.548 513.419 1.00 58.03 O ANISOU 40 OG1 THR A 20 4843 10577 6630 -458 -1540 -823 O ATOM 41 CG2 THR A 20 155.480 33.559 511.807 1.00 57.94 C ANISOU 41 CG2 THR A 20 5150 10566 6298 85 -1447 -824 C ATOM 42 N PHE A 21 155.411 31.101 515.680 1.00 74.06 N ANISOU 42 N PHE A 21 7313 11672 9154 -882 -1331 -913 N ATOM 43 CA PHE A 21 155.233 30.794 517.095 1.00 73.08 C ANISOU 43 CA PHE A 21 7161 11344 9264 -1074 -1214 -809 C ATOM 44 C PHE A 21 156.514 30.257 517.718 1.00 71.89 C ANISOU 44 C PHE A 21 7354 10716 9244 -1103 -1106 -884 C ATOM 45 O PHE A 21 156.759 30.477 518.909 1.00 70.57 O ANISOU 45 O PHE A 21 7222 10368 9225 -1092 -932 -748 O ATOM 46 CB PHE A 21 154.092 29.792 517.279 1.00 74.24 C ANISOU 46 CB PHE A 21 7091 11620 9496 -1475 -1392 -870 C ATOM 47 CG PHE A 21 153.776 29.491 518.718 1.00 73.45 C ANISOU 47 CG PHE A 21 6920 11370 9617 -1668 -1261 -723 C ATOM 48 CD1 PHE A 21 152.911 30.301 519.436 1.00 73.22 C ANISOU 48 CD1 PHE A 21 6590 11625 9606 -1566 -1133 -477 C ATOM 49 CD2 PHE A 21 154.342 28.396 519.353 1.00 72.98 C ANISOU 49 CD2 PHE A 21 7105 10896 9727 -1918 -1255 -820 C ATOM 50 CE1 PHE A 21 152.619 30.028 520.759 1.00 72.67 C ANISOU 50 CE1 PHE A 21 6453 11448 9712 -1717 -1001 -332 C ATOM 51 CE2 PHE A 21 154.054 28.118 520.677 1.00 72.31 C ANISOU 51 CE2 PHE A 21 6958 10691 9826 -2078 -1123 -664 C ATOM 52 CZ PHE A 21 153.191 28.935 521.380 1.00 72.24 C ANISOU 52 CZ PHE A 21 6636 10987 9825 -1981 -996 -420 C ATOM 53 N GLU A 22 157.337 29.551 516.938 1.00 73.49 N ANISOU 53 N GLU A 22 7812 10735 9375 -1116 -1206 -1098 N ATOM 54 CA GLU A 22 158.609 29.063 517.462 1.00 72.29 C ANISOU 54 CA GLU A 22 7975 10172 9320 -1091 -1099 -1158 C ATOM 55 C GLU A 22 159.528 30.220 517.832 1.00 71.19 C ANISOU 55 C GLU A 22 7900 9977 9173 -782 -878 -991 C ATOM 56 O GLU A 22 160.208 30.176 518.864 1.00 69.74 O ANISOU 56 O GLU A 22 7839 9533 9126 -781 -738 -926 O ATOM 57 CB GLU A 22 159.288 28.148 516.442 1.00 73.11 C ANISOU 57 CB GLU A 22 8333 10137 9306 -1101 -1245 -1417 C ATOM 58 CG GLU A 22 158.523 26.870 516.134 1.00 74.26 C ANISOU 58 CG GLU A 22 8500 10238 9480 -1448 -1480 -1625 C ATOM 59 CD GLU A 22 159.308 25.928 515.241 1.00 74.94 C ANISOU 59 CD GLU A 22 8913 10116 9444 -1420 -1608 -1902 C ATOM 60 OE1 GLU A 22 160.546 26.071 515.167 1.00 74.00 O ANISOU 60 OE1 GLU A 22 9013 9831 9272 -1159 -1478 -1908 O ATOM 61 OE2 GLU A 22 158.688 25.046 514.610 1.00 76.51 O ANISOU 61 OE2 GLU A 22 9149 10328 9593 -1655 -1843 -2117 O ATOM 62 N VAL A 23 159.562 31.265 517.002 1.00 46.86 N ANISOU 62 N VAL A 23 4741 7134 5928 -525 -850 -916 N ATOM 63 CA VAL A 23 160.370 32.438 517.315 1.00 45.98 C ANISOU 63 CA VAL A 23 4692 6959 5821 -266 -649 -746 C ATOM 64 C VAL A 23 159.841 33.135 518.562 1.00 44.62 C ANISOU 64 C VAL A 23 4394 6774 5783 -266 -513 -558 C ATOM 65 O VAL A 23 160.614 33.540 519.438 1.00 43.24 O ANISOU 65 O VAL A 23 4342 6379 5709 -202 -363 -480 O ATOM 66 CB VAL A 23 160.415 33.390 516.106 1.00 46.85 C ANISOU 66 CB VAL A 23 4752 7325 5725 -1 -648 -682 C ATOM 67 CG1 VAL A 23 160.977 34.744 516.510 1.00 45.45 C ANISOU 67 CG1 VAL A 23 4610 7083 5575 225 -441 -469 C ATOM 68 CG2 VAL A 23 161.246 32.781 514.987 1.00 48.17 C ANISOU 68 CG2 VAL A 23 5089 7471 5740 60 -732 -853 C ATOM 69 N VAL A 24 158.518 33.278 518.667 1.00 49.24 N ANISOU 69 N VAL A 24 4730 7619 6359 -330 -569 -487 N ATOM 70 CA VAL A 24 157.931 33.900 519.850 1.00 48.17 C ANISOU 70 CA VAL A 24 4470 7508 6324 -297 -435 -309 C ATOM 71 C VAL A 24 158.179 33.042 521.084 1.00 47.27 C ANISOU 71 C VAL A 24 4444 7126 6392 -516 -389 -337 C ATOM 72 O VAL A 24 158.472 33.560 522.168 1.00 45.99 O ANISOU 72 O VAL A 24 4338 6825 6310 -431 -233 -227 O ATOM 73 CB VAL A 24 156.430 34.158 519.627 1.00 49.08 C ANISOU 73 CB VAL A 24 4260 8020 6367 -301 -507 -217 C ATOM 74 CG1 VAL A 24 155.803 34.770 520.871 1.00 48.19 C ANISOU 74 CG1 VAL A 24 4020 7956 6334 -228 -353 -29 C ATOM 75 CG2 VAL A 24 156.221 35.061 518.422 1.00 49.68 C ANISOU 75 CG2 VAL A 24 4263 8370 6242 -37 -542 -167 C ATOM 76 N PHE A 25 158.075 31.718 520.940 1.00 47.90 N ANISOU 76 N PHE A 25 4558 7116 6527 -792 -525 -485 N ATOM 77 CA PHE A 25 158.327 30.828 522.069 1.00 46.85 C ANISOU 77 CA PHE A 25 4531 6710 6559 -993 -477 -494 C ATOM 78 C PHE A 25 159.782 30.902 522.520 1.00 45.24 C ANISOU 78 C PHE A 25 4605 6191 6394 -863 -363 -521 C ATOM 79 O PHE A 25 160.065 30.889 523.723 1.00 43.77 O ANISOU 79 O PHE A 25 4478 5842 6310 -872 -243 -438 O ATOM 80 CB PHE A 25 157.948 29.394 521.698 1.00 47.79 C ANISOU 80 CB PHE A 25 4675 6756 6728 -1317 -656 -653 C ATOM 81 CG PHE A 25 158.116 28.408 522.821 1.00 46.80 C ANISOU 81 CG PHE A 25 4668 6340 6773 -1533 -606 -637 C ATOM 82 CD1 PHE A 25 157.103 28.213 523.745 1.00 47.08 C ANISOU 82 CD1 PHE A 25 4496 6479 6914 -1719 -563 -486 C ATOM 83 CD2 PHE A 25 159.283 27.671 522.946 1.00 45.69 C ANISOU 83 CD2 PHE A 25 4840 5847 6673 -1530 -592 -753 C ATOM 84 CE1 PHE A 25 157.253 27.306 524.777 1.00 46.36 C ANISOU 84 CE1 PHE A 25 4521 6124 6971 -1910 -503 -443 C ATOM 85 CE2 PHE A 25 159.440 26.763 523.976 1.00 44.75 C ANISOU 85 CE2 PHE A 25 4846 5459 6698 -1700 -539 -718 C ATOM 86 CZ PHE A 25 158.423 26.580 524.893 1.00 45.15 C ANISOU 86 CZ PHE A 25 4701 5596 6858 -1897 -493 -559 C ATOM 87 N ILE A 26 160.717 30.985 521.570 1.00 43.87 N ANISOU 87 N ILE A 26 4586 5959 6122 -731 -398 -628 N ATOM 88 CA ILE A 26 162.132 31.043 521.925 1.00 42.57 C ANISOU 88 CA ILE A 26 4644 5547 5983 -612 -297 -644 C ATOM 89 C ILE A 26 162.462 32.364 522.610 1.00 41.48 C ANISOU 89 C ILE A 26 4481 5418 5860 -426 -137 -484 C ATOM 90 O ILE A 26 163.216 32.398 523.589 1.00 39.75 O ANISOU 90 O ILE A 26 4374 5010 5721 -408 -41 -450 O ATOM 91 CB ILE A 26 163.004 30.815 520.676 1.00 43.75 C ANISOU 91 CB ILE A 26 4932 5687 6004 -503 -365 -779 C ATOM 92 CG1 ILE A 26 162.933 29.350 520.238 1.00 44.11 C ANISOU 92 CG1 ILE A 26 5102 5611 6046 -680 -515 -975 C ATOM 93 CG2 ILE A 26 164.447 31.225 520.940 1.00 42.89 C ANISOU 93 CG2 ILE A 26 4974 5425 5897 -337 -240 -742 C ATOM 94 CD1 ILE A 26 163.367 28.370 521.307 1.00 42.26 C ANISOU 94 CD1 ILE A 26 5028 5075 5956 -811 -476 -998 C ATOM 95 N VAL A 27 161.900 33.469 522.116 1.00 38.33 N ANISOU 95 N VAL A 27 3952 5234 5378 -279 -114 -387 N ATOM 96 CA VAL A 27 162.161 34.772 522.723 1.00 37.02 C ANISOU 96 CA VAL A 27 3804 5038 5225 -101 30 -247 C ATOM 97 C VAL A 27 161.632 34.814 524.152 1.00 35.85 C ANISOU 97 C VAL A 27 3610 4836 5174 -151 110 -167 C ATOM 98 O VAL A 27 162.290 35.339 525.059 1.00 34.24 O ANISOU 98 O VAL A 27 3520 4470 5018 -81 213 -124 O ATOM 99 CB VAL A 27 161.556 35.895 521.858 1.00 37.85 C ANISOU 99 CB VAL A 27 3801 5370 5210 89 40 -147 C ATOM 100 CG1 VAL A 27 161.572 37.218 522.606 1.00 36.66 C ANISOU 100 CG1 VAL A 27 3690 5157 5081 263 184 -3 C ATOM 101 CG2 VAL A 27 162.319 36.018 520.550 1.00 38.59 C ANISOU 101 CG2 VAL A 27 3972 5498 5191 181 0 -194 C ATOM 102 N LEU A 28 160.442 34.252 524.378 1.00 34.25 N ANISOU 102 N LEU A 28 3232 4788 4992 -279 60 -145 N ATOM 103 CA LEU A 28 159.869 34.256 525.721 1.00 33.54 C ANISOU 103 CA LEU A 28 3075 4694 4975 -311 152 -46 C ATOM 104 C LEU A 28 160.640 33.334 526.659 1.00 32.12 C ANISOU 104 C LEU A 28 3052 4254 4897 -449 178 -97 C ATOM 105 O LEU A 28 160.845 33.667 527.832 1.00 31.00 O ANISOU 105 O LEU A 28 2967 4023 4787 -382 288 -28 O ATOM 106 CB LEU A 28 158.394 33.856 525.664 1.00 35.17 C ANISOU 106 CB LEU A 28 3012 5175 5175 -432 96 19 C ATOM 107 CG LEU A 28 157.460 34.844 524.962 1.00 36.36 C ANISOU 107 CG LEU A 28 2964 5645 5207 -247 90 111 C ATOM 108 CD1 LEU A 28 156.029 34.326 524.955 1.00 37.69 C ANISOU 108 CD1 LEU A 28 2820 6128 5371 -400 22 179 C ATOM 109 CD2 LEU A 28 157.537 36.214 525.618 1.00 35.19 C ANISOU 109 CD2 LEU A 28 2879 5477 5014 48 250 233 C ATOM 110 N VAL A 29 161.075 32.174 526.165 1.00 40.16 N ANISOU 110 N VAL A 29 4159 5149 5951 -617 77 -220 N ATOM 111 CA VAL A 29 161.834 31.256 527.007 1.00 38.70 C ANISOU 111 CA VAL A 29 4141 4712 5850 -714 105 -255 C ATOM 112 C VAL A 29 163.219 31.821 527.305 1.00 37.09 C ANISOU 112 C VAL A 29 4113 4352 5626 -546 176 -276 C ATOM 113 O VAL A 29 163.709 31.732 528.437 1.00 35.68 O ANISOU 113 O VAL A 29 4020 4047 5490 -526 253 -236 O ATOM 114 CB VAL A 29 161.911 29.865 526.349 1.00 39.24 C ANISOU 114 CB VAL A 29 4294 4663 5951 -912 -23 -388 C ATOM 115 CG1 VAL A 29 162.955 29.000 527.039 1.00 37.57 C ANISOU 115 CG1 VAL A 29 4307 4168 5798 -933 12 -428 C ATOM 116 CG2 VAL A 29 160.552 29.188 526.397 1.00 40.69 C ANISOU 116 CG2 VAL A 29 4302 4966 6190 -1153 -92 -351 C ATOM 117 N ALA A 30 163.867 32.420 526.302 1.00 36.94 N ANISOU 117 N ALA A 30 4136 4364 5536 -428 150 -327 N ATOM 118 CA ALA A 30 165.190 32.998 526.522 1.00 35.64 C ANISOU 118 CA ALA A 30 4100 4081 5358 -304 212 -330 C ATOM 119 C ALA A 30 165.121 34.198 527.459 1.00 34.94 C ANISOU 119 C ALA A 30 4002 3995 5279 -199 312 -230 C ATOM 120 O ALA A 30 165.960 34.338 528.358 1.00 33.36 O ANISOU 120 O ALA A 30 3900 3670 5104 -173 361 -229 O ATOM 121 CB ALA A 30 165.822 33.394 525.188 1.00 36.94 C ANISOU 121 CB ALA A 30 4288 4307 5440 -213 176 -374 C ATOM 122 N GLY A 31 164.133 35.075 527.264 1.00 34.30 N ANISOU 122 N GLY A 31 3811 4060 5161 -121 338 -154 N ATOM 123 CA GLY A 31 163.984 36.218 528.149 1.00 33.72 C ANISOU 123 CA GLY A 31 3767 3967 5080 8 433 -74 C ATOM 124 C GLY A 31 163.622 35.832 529.568 1.00 33.50 C ANISOU 124 C GLY A 31 3738 3906 5086 -23 488 -42 C ATOM 125 O GLY A 31 164.020 36.513 530.519 1.00 33.07 O ANISOU 125 O GLY A 31 3784 3760 5020 68 552 -29 O ATOM 126 N SER A 32 162.871 34.741 529.736 1.00 37.75 N ANISOU 126 N SER A 32 4169 4515 5658 -159 461 -27 N ATOM 127 CA SER A 32 162.533 34.275 531.076 1.00 37.70 C ANISOU 127 CA SER A 32 4156 4490 5678 -193 528 34 C ATOM 128 C SER A 32 163.753 33.700 531.783 1.00 36.46 C ANISOU 128 C SER A 32 4170 4131 5551 -227 531 -23 C ATOM 129 O SER A 32 163.975 33.973 532.968 1.00 36.52 O ANISOU 129 O SER A 32 4243 4097 5534 -149 600 11 O ATOM 130 CB SER A 32 161.417 33.234 531.006 1.00 38.63 C ANISOU 130 CB SER A 32 4107 4731 5841 -370 500 90 C ATOM 131 OG SER A 32 160.249 33.776 530.415 1.00 39.89 O ANISOU 131 OG SER A 32 4065 5135 5955 -328 491 156 O ATOM 132 N LEU A 33 164.551 32.897 531.074 1.00 36.04 N ANISOU 132 N LEU A 33 4192 3972 5531 -317 454 -110 N ATOM 133 CA LEU A 33 165.751 32.325 531.676 1.00 34.28 C ANISOU 133 CA LEU A 33 4115 3589 5320 -314 456 -153 C ATOM 134 C LEU A 33 166.747 33.411 532.059 1.00 33.03 C ANISOU 134 C LEU A 33 4035 3397 5118 -187 482 -176 C ATOM 135 O LEU A 33 167.376 33.340 533.121 1.00 32.11 O ANISOU 135 O LEU A 33 3997 3219 4985 -147 509 -173 O ATOM 136 CB LEU A 33 166.391 31.322 530.717 1.00 33.59 C ANISOU 136 CB LEU A 33 4098 3414 5253 -386 375 -244 C ATOM 137 CG LEU A 33 165.701 29.962 530.614 1.00 34.41 C ANISOU 137 CG LEU A 33 4206 3455 5414 -549 335 -246 C ATOM 138 CD1 LEU A 33 166.197 29.197 529.399 1.00 34.52 C ANISOU 138 CD1 LEU A 33 4308 3392 5417 -586 239 -370 C ATOM 139 CD2 LEU A 33 165.930 29.156 531.883 1.00 33.98 C ANISOU 139 CD2 LEU A 33 4245 3274 5393 -572 393 -180 C ATOM 140 N SER A 34 166.905 34.425 531.204 1.00 34.34 N ANISOU 140 N SER A 34 4183 3602 5262 -131 468 -195 N ATOM 141 CA SER A 34 167.798 35.531 531.530 1.00 33.03 C ANISOU 141 CA SER A 34 4096 3381 5073 -55 484 -211 C ATOM 142 C SER A 34 167.316 36.281 532.765 1.00 33.38 C ANISOU 142 C SER A 34 4181 3418 5084 27 544 -179 C ATOM 143 O SER A 34 168.122 36.665 533.621 1.00 32.31 O ANISOU 143 O SER A 34 4142 3211 4926 53 542 -217 O ATOM 144 CB SER A 34 167.914 36.480 530.338 1.00 33.59 C ANISOU 144 CB SER A 34 4149 3481 5133 -20 474 -203 C ATOM 145 OG SER A 34 168.646 37.643 530.683 1.00 32.68 O ANISOU 145 OG SER A 34 4122 3283 5012 18 492 -205 O ATOM 146 N LEU A 35 166.003 36.491 532.878 1.00 38.41 N ANISOU 146 N LEU A 35 4740 4152 5701 81 593 -113 N ATOM 147 CA LEU A 35 165.468 37.230 534.017 1.00 38.93 C ANISOU 147 CA LEU A 35 4852 4234 5706 209 665 -81 C ATOM 148 C LEU A 35 165.628 36.445 535.313 1.00 38.94 C ANISOU 148 C LEU A 35 4885 4227 5684 196 691 -72 C ATOM 149 O LEU A 35 165.946 37.023 536.359 1.00 38.49 O ANISOU 149 O LEU A 35 4939 4129 5558 295 716 -103 O ATOM 150 CB LEU A 35 164.001 37.575 533.771 1.00 40.95 C ANISOU 150 CB LEU A 35 4980 4649 5930 300 722 11 C ATOM 151 CG LEU A 35 163.340 38.490 534.802 1.00 41.28 C ANISOU 151 CG LEU A 35 5074 4733 5879 499 814 50 C ATOM 152 CD1 LEU A 35 164.103 39.801 534.914 1.00 40.04 C ANISOU 152 CD1 LEU A 35 5125 4399 5689 604 804 -32 C ATOM 153 CD2 LEU A 35 161.886 38.740 534.436 1.00 42.66 C ANISOU 153 CD2 LEU A 35 5076 5122 6013 608 874 163 C ATOM 154 N VAL A 36 165.413 35.129 535.265 1.00 32.78 N ANISOU 154 N VAL A 36 4029 3475 4950 79 684 -29 N ATOM 155 CA VAL A 36 165.592 34.301 536.454 1.00 33.05 C ANISOU 155 CA VAL A 36 4105 3491 4961 73 721 10 C ATOM 156 C VAL A 36 167.058 34.268 536.867 1.00 30.93 C ANISOU 156 C VAL A 36 3969 3114 4668 90 667 -77 C ATOM 157 O VAL A 36 167.382 34.306 538.061 1.00 31.32 O ANISOU 157 O VAL A 36 4092 3168 4640 171 691 -74 O ATOM 158 CB VAL A 36 165.037 32.886 536.207 1.00 33.79 C ANISOU 158 CB VAL A 36 4116 3594 5129 -80 723 85 C ATOM 159 CG1 VAL A 36 165.365 31.967 537.374 1.00 34.02 C ANISOU 159 CG1 VAL A 36 4219 3571 5136 -80 768 147 C ATOM 160 CG2 VAL A 36 163.537 32.941 535.981 1.00 35.63 C ANISOU 160 CG2 VAL A 36 4175 3989 5376 -115 772 187 C ATOM 161 N THR A 37 167.967 34.205 535.891 1.00 31.09 N ANISOU 161 N THR A 37 4005 3070 4737 27 591 -149 N ATOM 162 CA THR A 37 169.394 34.197 536.202 1.00 30.00 C ANISOU 162 CA THR A 37 3945 2880 4572 40 537 -216 C ATOM 163 C THR A 37 169.820 35.504 536.860 1.00 30.09 C ANISOU 163 C THR A 37 4027 2884 4521 106 521 -276 C ATOM 164 O THR A 37 170.675 35.509 537.753 1.00 30.60 O ANISOU 164 O THR A 37 4150 2951 4523 136 485 -318 O ATOM 165 CB THR A 37 170.210 33.951 534.931 1.00 28.87 C ANISOU 165 CB THR A 37 3777 2713 4480 -22 477 -261 C ATOM 166 OG1 THR A 37 169.753 32.755 534.289 1.00 29.01 O ANISOU 166 OG1 THR A 37 3769 2709 4543 -79 477 -237 O ATOM 167 CG2 THR A 37 171.691 33.807 535.263 1.00 28.76 C ANISOU 167 CG2 THR A 37 3798 2699 4431 -1 426 -305 C ATOM 168 N ILE A 38 169.230 36.622 536.436 1.00 25.73 N ANISOU 168 N ILE A 38 3482 2318 3975 134 540 -284 N ATOM 169 CA ILE A 38 169.594 37.917 537.001 1.00 26.00 C ANISOU 169 CA ILE A 38 3632 2289 3958 186 519 -356 C ATOM 170 C ILE A 38 169.090 38.035 538.435 1.00 27.30 C ANISOU 170 C ILE A 38 3874 2488 4011 313 562 -363 C ATOM 171 O ILE A 38 169.841 38.405 539.344 1.00 27.98 O ANISOU 171 O ILE A 38 4062 2548 4023 336 508 -448 O ATOM 172 CB ILE A 38 169.058 39.057 536.117 1.00 25.92 C ANISOU 172 CB ILE A 38 3645 2223 3981 212 541 -346 C ATOM 173 CG1 ILE A 38 169.793 39.082 534.776 1.00 25.06 C ANISOU 173 CG1 ILE A 38 3477 2090 3953 98 496 -339 C ATOM 174 CG2 ILE A 38 169.192 40.396 536.824 1.00 26.60 C ANISOU 174 CG2 ILE A 38 3904 2195 4008 285 531 -422 C ATOM 175 CD1 ILE A 38 169.245 40.096 533.797 1.00 25.47 C ANISOU 175 CD1 ILE A 38 3547 2101 4030 138 528 -296 C ATOM 176 N ILE A 39 167.815 37.714 538.659 1.00 35.52 N ANISOU 176 N ILE A 39 4853 3616 5026 399 656 -269 N ATOM 177 CA ILE A 39 167.221 37.898 539.980 1.00 36.94 C ANISOU 177 CA ILE A 39 5095 3864 5076 557 724 -253 C ATOM 178 C ILE A 39 167.855 36.955 540.994 1.00 37.57 C ANISOU 178 C ILE A 39 5193 3987 5093 552 708 -244 C ATOM 179 O ILE A 39 168.181 37.358 542.117 1.00 38.51 O ANISOU 179 O ILE A 39 5427 4123 5080 663 694 -309 O ATOM 180 CB ILE A 39 165.695 37.708 539.910 1.00 38.13 C ANISOU 180 CB ILE A 39 5122 4151 5216 640 841 -118 C ATOM 181 CG1 ILE A 39 165.070 38.740 538.969 1.00 37.98 C ANISOU 181 CG1 ILE A 39 5091 4114 5225 698 856 -120 C ATOM 182 CG2 ILE A 39 165.080 37.812 541.296 1.00 39.54 C ANISOU 182 CG2 ILE A 39 5345 4441 5239 828 934 -74 C ATOM 183 CD1 ILE A 39 163.583 38.558 538.768 1.00 39.49 C ANISOU 183 CD1 ILE A 39 5109 4492 5402 778 958 21 C ATOM 184 N GLY A 40 168.045 35.690 540.616 1.00 34.67 N ANISOU 184 N GLY A 40 4733 3634 4806 442 707 -167 N ATOM 185 CA GLY A 40 168.565 34.716 541.562 1.00 35.62 C ANISOU 185 CA GLY A 40 4882 3791 4862 468 711 -125 C ATOM 186 C GLY A 40 169.970 35.037 542.033 1.00 35.71 C ANISOU 186 C GLY A 40 4981 3783 4804 484 601 -247 C ATOM 187 O GLY A 40 170.291 34.875 543.213 1.00 37.17 O ANISOU 187 O GLY A 40 5229 4039 4854 590 598 -250 O ATOM 188 N ASN A 41 170.827 35.504 541.123 1.00 32.23 N ANISOU 188 N ASN A 41 4529 3275 4443 378 508 -338 N ATOM 189 CA ASN A 41 172.208 35.791 541.492 1.00 33.23 C ANISOU 189 CA ASN A 41 4690 3419 4515 356 392 -441 C ATOM 190 C ASN A 41 172.352 37.133 542.198 1.00 34.33 C ANISOU 190 C ASN A 41 4948 3535 4561 391 332 -571 C ATOM 191 O ASN A 41 173.241 37.287 543.042 1.00 36.23 O ANISOU 191 O ASN A 41 5233 3836 4696 407 238 -656 O ATOM 192 CB ASN A 41 173.105 35.739 540.257 1.00 32.19 C ANISOU 192 CB ASN A 41 4477 3256 4498 223 328 -463 C ATOM 193 CG ASN A 41 173.324 34.324 539.765 1.00 31.74 C ANISOU 193 CG ASN A 41 4351 3219 4488 223 356 -375 C ATOM 194 OD1 ASN A 41 174.085 33.562 540.362 1.00 33.24 O ANISOU 194 OD1 ASN A 41 4542 3477 4612 285 329 -355 O ATOM 195 ND2 ASN A 41 172.656 33.963 538.675 1.00 29.99 N ANISOU 195 ND2 ASN A 41 4087 2938 4370 167 405 -327 N ATOM 196 N ILE A 42 171.502 38.109 541.872 1.00 36.91 N ANISOU 196 N ILE A 42 5337 3773 4913 414 377 -595 N ATOM 197 CA ILE A 42 171.520 39.369 542.608 1.00 38.03 C ANISOU 197 CA ILE A 42 5649 3848 4953 477 328 -730 C ATOM 198 C ILE A 42 171.089 39.145 544.052 1.00 39.53 C ANISOU 198 C ILE A 42 5920 4147 4952 669 367 -737 C ATOM 199 O ILE A 42 171.682 39.700 544.984 1.00 41.04 O ANISOU 199 O ILE A 42 6240 4345 5009 710 271 -877 O ATOM 200 CB ILE A 42 170.638 40.417 541.905 1.00 37.01 C ANISOU 200 CB ILE A 42 5592 3589 4883 510 387 -732 C ATOM 201 CG1 ILE A 42 171.304 40.894 540.614 1.00 35.86 C ANISOU 201 CG1 ILE A 42 5407 3328 4891 323 328 -743 C ATOM 202 CG2 ILE A 42 170.364 41.597 542.825 1.00 38.30 C ANISOU 202 CG2 ILE A 42 5980 3664 4909 648 369 -864 C ATOM 203 CD1 ILE A 42 170.517 41.957 539.881 1.00 35.26 C ANISOU 203 CD1 ILE A 42 5416 3115 4864 372 386 -728 C ATOM 204 N LEU A 43 170.061 38.317 544.261 1.00 31.45 N ANISOU 204 N LEU A 43 4818 3224 3906 780 506 -584 N ATOM 205 CA LEU A 43 169.600 38.032 545.617 1.00 32.84 C ANISOU 205 CA LEU A 43 5052 3536 3890 977 572 -548 C ATOM 206 C LEU A 43 170.698 37.390 546.455 1.00 34.18 C ANISOU 206 C LEU A 43 5233 3798 3955 980 481 -581 C ATOM 207 O LEU A 43 170.805 37.656 547.657 1.00 35.58 O ANISOU 207 O LEU A 43 5523 4067 3928 1135 457 -650 O ATOM 208 CB LEU A 43 168.364 37.134 545.572 1.00 32.69 C ANISOU 208 CB LEU A 43 4902 3620 3898 1039 742 -335 C ATOM 209 CG LEU A 43 167.061 37.798 545.123 1.00 32.29 C ANISOU 209 CG LEU A 43 4822 3576 3873 1120 850 -282 C ATOM 210 CD1 LEU A 43 165.983 36.753 544.886 1.00 32.65 C ANISOU 210 CD1 LEU A 43 4676 3743 3986 1093 989 -60 C ATOM 211 CD2 LEU A 43 166.603 38.817 546.153 1.00 33.29 C ANISOU 211 CD2 LEU A 43 5112 3747 3790 1372 889 -367 C ATOM 212 N VAL A 44 171.527 36.546 545.840 1.00 34.09 N ANISOU 212 N VAL A 44 5112 3783 4059 840 429 -533 N ATOM 213 CA VAL A 44 172.627 35.924 546.572 1.00 35.69 C ANISOU 213 CA VAL A 44 5307 4099 4154 870 341 -549 C ATOM 214 C VAL A 44 173.694 36.958 546.908 1.00 36.98 C ANISOU 214 C VAL A 44 5544 4269 4239 811 159 -760 C ATOM 215 O VAL A 44 174.174 37.034 548.045 1.00 38.68 O ANISOU 215 O VAL A 44 5826 4611 4259 917 81 -836 O ATOM 216 CB VAL A 44 173.213 34.749 545.770 1.00 35.23 C ANISOU 216 CB VAL A 44 5122 4033 4230 773 343 -438 C ATOM 217 CG1 VAL A 44 174.426 34.170 546.486 1.00 37.23 C ANISOU 217 CG1 VAL A 44 5358 4428 4359 839 248 -449 C ATOM 218 CG2 VAL A 44 172.157 33.677 545.551 1.00 34.30 C ANISOU 218 CG2 VAL A 44 4962 3884 4185 801 503 -243 C ATOM 219 N MET A 45 174.077 37.776 545.924 1.00 36.07 N ANISOU 219 N MET A 45 5415 4021 4269 629 85 -853 N ATOM 220 CA MET A 45 175.137 38.755 546.143 1.00 37.44 C ANISOU 220 CA MET A 45 5644 4178 4402 506 -97 -1041 C ATOM 221 C MET A 45 174.715 39.822 547.145 1.00 38.19 C ANISOU 221 C MET A 45 5959 4220 4332 612 -140 -1205 C ATOM 222 O MET A 45 175.520 40.251 547.980 1.00 39.93 O ANISOU 222 O MET A 45 6250 4510 4411 591 -299 -1363 O ATOM 223 CB MET A 45 175.538 39.398 544.815 1.00 36.36 C ANISOU 223 CB MET A 45 5450 3896 4470 280 -137 -1064 C ATOM 224 CG MET A 45 176.125 38.426 543.806 1.00 35.81 C ANISOU 224 CG MET A 45 5177 3896 4532 191 -114 -933 C ATOM 225 SD MET A 45 176.373 39.178 542.187 0.70 33.97 S ANISOU 225 SD MET A 45 4880 3514 4514 -28 -118 -922 S ATOM 226 CE MET A 45 177.531 40.481 542.597 1.00 35.85 C ANISOU 226 CE MET A 45 5173 3722 4726 -232 -312 -1098 C ATOM 227 N VAL A 46 173.458 40.265 547.080 1.00 36.90 N ANISOU 227 N VAL A 46 5905 3948 4166 740 -8 -1176 N ATOM 228 CA VAL A 46 172.994 41.304 547.994 1.00 37.71 C ANISOU 228 CA VAL A 46 6248 3987 4093 891 -32 -1336 C ATOM 229 C VAL A 46 172.849 40.751 549.407 1.00 39.02 C ANISOU 229 C VAL A 46 6459 4368 3999 1126 -13 -1333 C ATOM 230 O VAL A 46 173.134 41.445 550.391 1.00 40.44 O ANISOU 230 O VAL A 46 6825 4563 3978 1213 -126 -1526 O ATOM 231 CB VAL A 46 171.677 41.916 547.477 1.00 36.35 C ANISOU 231 CB VAL A 46 6161 3673 3977 1008 122 -1282 C ATOM 232 CG1 VAL A 46 171.078 42.864 548.505 1.00 37.38 C ANISOU 232 CG1 VAL A 46 6557 3760 3887 1248 130 -1431 C ATOM 233 CG2 VAL A 46 171.917 42.646 546.163 1.00 35.26 C ANISOU 233 CG2 VAL A 46 6021 3316 4061 796 84 -1302 C ATOM 234 N SER A 47 172.419 39.492 549.532 1.00 44.16 N ANISOU 234 N SER A 47 6957 5180 4643 1227 126 -1114 N ATOM 235 CA SER A 47 172.234 38.901 550.855 1.00 45.38 C ANISOU 235 CA SER A 47 7148 5550 4547 1464 173 -1063 C ATOM 236 C SER A 47 173.552 38.810 551.614 1.00 47.17 C ANISOU 236 C SER A 47 7389 5911 4623 1435 -24 -1197 C ATOM 237 O SER A 47 173.598 39.061 552.824 1.00 48.43 O ANISOU 237 O SER A 47 7683 6205 4515 1624 -75 -1300 O ATOM 238 CB SER A 47 171.596 37.519 550.728 1.00 44.76 C ANISOU 238 CB SER A 47 6901 5577 4528 1525 359 -775 C ATOM 239 OG SER A 47 170.296 37.613 550.178 1.00 43.46 O ANISOU 239 OG SER A 47 6700 5346 4465 1560 532 -652 O ATOM 240 N ILE A 48 174.633 38.449 550.921 1.00 37.80 N ANISOU 240 N ILE A 48 6054 4722 3586 1219 -138 -1194 N ATOM 241 CA ILE A 48 175.935 38.358 551.573 1.00 39.69 C ANISOU 241 CA ILE A 48 6258 5137 3686 1182 -337 -1308 C ATOM 242 C ILE A 48 176.413 39.738 552.006 1.00 40.65 C ANISOU 242 C ILE A 48 6551 5187 3707 1087 -541 -1605 C ATOM 243 O ILE A 48 177.052 39.889 553.054 1.00 42.24 O ANISOU 243 O ILE A 48 6812 5564 3675 1157 -698 -1748 O ATOM 244 CB ILE A 48 176.948 37.669 550.639 1.00 39.88 C ANISOU 244 CB ILE A 48 6058 5199 3894 992 -393 -1217 C ATOM 245 CG1 ILE A 48 176.446 36.279 550.242 1.00 39.04 C ANISOU 245 CG1 ILE A 48 5840 5115 3878 1094 -200 -947 C ATOM 246 CG2 ILE A 48 178.314 37.570 551.304 1.00 41.96 C ANISOU 246 CG2 ILE A 48 6239 5700 4003 966 -602 -1317 C ATOM 247 CD1 ILE A 48 177.359 35.549 549.283 1.00 39.30 C ANISOU 247 CD1 ILE A 48 5687 5171 4073 963 -233 -858 C ATOM 248 N LYS A 49 176.097 40.770 551.220 1.00 41.72 N ANISOU 248 N LYS A 49 6786 5057 4009 930 -547 -1704 N ATOM 249 CA LYS A 49 176.578 42.111 551.535 1.00 42.76 C ANISOU 249 CA LYS A 49 7117 5051 4079 797 -746 -1988 C ATOM 250 C LYS A 49 175.855 42.703 552.739 1.00 43.91 C ANISOU 250 C LYS A 49 7544 5194 3944 1069 -740 -2144 C ATOM 251 O LYS A 49 176.473 43.387 553.563 1.00 46.86 O ANISOU 251 O LYS A 49 8078 5592 4136 1039 -948 -2395 O ATOM 252 CB LYS A 49 176.424 43.021 550.317 1.00 41.58 C ANISOU 252 CB LYS A 49 7019 4589 4190 569 -733 -2017 C ATOM 253 CG LYS A 49 177.496 42.819 549.261 1.00 41.49 C ANISOU 253 CG LYS A 49 6769 4587 4407 253 -818 -1950 C ATOM 254 CD LYS A 49 178.870 43.148 549.821 1.00 43.34 C ANISOU 254 CD LYS A 49 6957 4958 4554 50 -1082 -2129 C ATOM 255 CE LYS A 49 179.970 42.852 548.816 1.00 43.72 C ANISOU 255 CE LYS A 49 6717 5090 4804 -233 -1148 -2027 C ATOM 256 NZ LYS A 49 181.316 43.142 549.384 1.00 45.58 N ANISOU 256 NZ LYS A 49 6852 5518 4947 -441 -1412 -2182 N ATOM 257 N VAL A 50 174.547 42.451 552.865 1.00 51.74 N ANISOU 257 N VAL A 50 8595 6179 4884 1339 -508 -2001 N ATOM 258 CA VAL A 50 173.750 43.094 553.904 1.00 52.39 C ANISOU 258 CA VAL A 50 8934 6263 4708 1628 -465 -2120 C ATOM 259 C VAL A 50 173.677 42.281 555.189 1.00 53.35 C ANISOU 259 C VAL A 50 9028 6710 4532 1905 -427 -2050 C ATOM 260 O VAL A 50 173.104 42.757 556.179 1.00 54.95 O ANISOU 260 O VAL A 50 9360 6967 4553 2111 -390 -2079 O ATOM 261 CB VAL A 50 172.319 43.380 553.402 1.00 50.93 C ANISOU 261 CB VAL A 50 8778 5946 4627 1775 -223 -1961 C ATOM 262 CG1 VAL A 50 172.360 44.187 552.112 1.00 49.93 C ANISOU 262 CG1 VAL A 50 8672 5514 4787 1525 -246 -1996 C ATOM 263 CG2 VAL A 50 171.554 42.079 553.206 1.00 49.76 C ANISOU 263 CG2 VAL A 50 8427 5984 4495 1932 7 -1672 C ATOM 264 N ASN A 51 174.237 41.073 555.212 1.00 55.77 N ANISOU 264 N ASN A 51 9112 7235 4843 1882 -420 -1883 N ATOM 265 CA ASN A 51 174.169 40.200 556.380 1.00 56.61 C ANISOU 265 CA ASN A 51 9190 7653 4666 2160 -361 -1770 C ATOM 266 C ASN A 51 175.571 39.699 556.696 1.00 57.89 C ANISOU 266 C ASN A 51 9220 8013 4761 2043 -573 -1820 C ATOM 267 O ASN A 51 176.152 38.939 555.914 1.00 57.53 O ANISOU 267 O ASN A 51 8950 7981 4929 1865 -570 -1667 O ATOM 268 CB ASN A 51 173.209 39.033 556.139 1.00 55.43 C ANISOU 268 CB ASN A 51 8876 7582 4603 2294 -74 -1410 C ATOM 269 CG ASN A 51 173.031 38.159 557.366 1.00 56.30 C ANISOU 269 CG ASN A 51 8978 7994 4419 2596 21 -1251 C ATOM 270 OD1 ASN A 51 173.426 38.529 558.471 1.00 57.81 O ANISOU 270 OD1 ASN A 51 9304 8350 4309 2762 -107 -1416 O ATOM 271 ND2 ASN A 51 172.426 36.992 557.177 1.00 55.56 N ANISOU 271 ND2 ASN A 51 8727 7965 4419 2653 244 -919 N ATOM 272 N ARG A 52 176.111 40.120 557.843 1.00 73.44 N ANISOU 272 N ARG A 52 11329 10158 6416 2163 -759 -2039 N ATOM 273 CA ARG A 52 177.433 39.666 558.255 1.00 74.75 C ANISOU 273 CA ARG A 52 11350 10579 6472 2086 -975 -2088 C ATOM 274 C ARG A 52 177.458 38.181 558.589 1.00 74.65 C ANISOU 274 C ARG A 52 11153 10828 6381 2295 -823 -1766 C ATOM 275 O ARG A 52 178.529 37.567 558.541 1.00 75.34 O ANISOU 275 O ARG A 52 11053 11099 6472 2218 -947 -1716 O ATOM 276 CB ARG A 52 177.927 40.470 559.461 1.00 77.94 C ANISOU 276 CB ARG A 52 11875 11085 6656 2106 -1179 -2317 C ATOM 277 CG ARG A 52 178.282 41.919 559.160 1.00 79.43 C ANISOU 277 CG ARG A 52 12204 10996 6980 1792 -1368 -2608 C ATOM 278 CD ARG A 52 177.080 42.836 559.314 1.00 80.06 C ANISOU 278 CD ARG A 52 12529 10811 7079 1910 -1220 -2655 C ATOM 279 NE ARG A 52 177.360 43.945 560.221 1.00 84.03 N ANISOU 279 NE ARG A 52 13229 11259 7440 1864 -1390 -2911 N ATOM 280 CZ ARG A 52 177.177 43.898 561.536 1.00 87.05 C ANISOU 280 CZ ARG A 52 13699 11844 7533 2135 -1397 -2940 C ATOM 281 NH1 ARG A 52 176.712 42.793 562.104 1.00 86.30 N ANISOU 281 NH1 ARG A 52 13497 12020 7271 2464 -1234 -2702 N ATOM 282 NH2 ARG A 52 177.459 44.954 562.286 1.00 91.12 N ANISOU 282 NH2 ARG A 52 14413 12285 7924 2073 -1562 -3200 N ATOM 283 N HIS A 53 176.308 37.593 558.929 1.00 56.00 N ANISOU 283 N HIS A 53 8840 8490 3947 2561 -553 -1535 N ATOM 284 CA HIS A 53 176.266 36.161 559.208 1.00 55.93 C ANISOU 284 CA HIS A 53 8688 8672 3891 2738 -388 -1201 C ATOM 285 C HIS A 53 176.576 35.338 557.963 1.00 55.17 C ANISOU 285 C HIS A 53 8383 8431 4147 2514 -320 -1004 C ATOM 286 O HIS A 53 177.063 34.208 558.075 1.00 55.53 O ANISOU 286 O HIS A 53 8308 8619 4172 2600 -280 -794 O ATOM 287 CB HIS A 53 174.899 35.773 559.774 1.00 55.44 C ANISOU 287 CB HIS A 53 8712 8648 3704 3021 -102 -978 C ATOM 288 CG HIS A 53 174.591 36.400 561.098 1.00 57.82 C ANISOU 288 CG HIS A 53 9149 9084 3736 3246 -144 -1085 C ATOM 289 ND1 HIS A 53 175.120 35.935 562.283 1.00 60.34 N ANISOU 289 ND1 HIS A 53 9440 9673 3814 3443 -211 -1030 N ATOM 290 CD2 HIS A 53 173.803 37.452 561.425 1.00 58.98 C ANISOU 290 CD2 HIS A 53 9437 9112 3860 3298 -125 -1221 C ATOM 291 CE1 HIS A 53 174.675 36.675 563.283 1.00 63.04 C ANISOU 291 CE1 HIS A 53 9906 10059 3987 3604 -235 -1144 C ATOM 292 NE2 HIS A 53 173.874 37.602 562.789 1.00 62.28 N ANISOU 292 NE2 HIS A 53 9920 9729 4015 3524 -184 -1258 N ATOM 293 N LEU A 54 176.304 35.882 556.779 1.00 51.99 N ANISOU 293 N LEU A 54 7954 7748 4052 2253 -305 -1067 N ATOM 294 CA LEU A 54 176.613 35.218 555.520 1.00 51.30 C ANISOU 294 CA LEU A 54 7687 7520 4283 2041 -257 -920 C ATOM 295 C LEU A 54 177.986 35.590 554.978 1.00 52.14 C ANISOU 295 C LEU A 54 7670 7658 4481 1804 -499 -1089 C ATOM 296 O LEU A 54 178.331 35.178 553.867 1.00 51.71 O ANISOU 296 O LEU A 54 7470 7498 4679 1631 -474 -997 O ATOM 297 CB LEU A 54 175.543 35.542 554.474 1.00 49.55 C ANISOU 297 CB LEU A 54 7481 7015 4330 1904 -99 -869 C ATOM 298 CG LEU A 54 174.198 34.828 554.604 1.00 48.58 C ANISOU 298 CG LEU A 54 7372 6864 4221 2061 173 -609 C ATOM 299 CD1 LEU A 54 173.201 35.381 553.599 1.00 46.87 C ANISOU 299 CD1 LEU A 54 7155 6415 4237 1923 281 -608 C ATOM 300 CD2 LEU A 54 174.373 33.328 554.419 1.00 48.72 C ANISOU 300 CD2 LEU A 54 7271 6920 4320 2089 285 -330 C ATOM 301 N GLN A 55 178.774 36.358 555.726 1.00 52.23 N ANISOU 301 N GLN A 55 7731 7828 4287 1788 -735 -1333 N ATOM 302 CA GLN A 55 180.093 36.788 555.264 1.00 53.16 C ANISOU 302 CA GLN A 55 7700 8012 4487 1527 -977 -1489 C ATOM 303 C GLN A 55 181.172 35.812 555.737 1.00 54.33 C ANISOU 303 C GLN A 55 7661 8503 4478 1655 -1066 -1378 C ATOM 304 O GLN A 55 182.058 36.136 556.526 1.00 55.60 O ANISOU 304 O GLN A 55 7784 8928 4415 1666 -1295 -1540 O ATOM 305 CB GLN A 55 180.374 38.211 555.729 1.00 53.91 C ANISOU 305 CB GLN A 55 7947 8066 4471 1380 -1207 -1828 C ATOM 306 CG GLN A 55 179.438 39.240 555.115 1.00 52.75 C ANISOU 306 CG GLN A 55 7990 7554 4500 1253 -1127 -1934 C ATOM 307 CD GLN A 55 179.689 40.643 555.625 1.00 53.74 C ANISOU 307 CD GLN A 55 8329 7582 4506 1125 -1353 -2279 C ATOM 308 OE1 GLN A 55 180.473 40.848 556.551 1.00 55.31 O ANISOU 308 OE1 GLN A 55 8545 8007 4463 1139 -1577 -2457 O ATOM 309 NE2 GLN A 55 179.022 41.620 555.020 1.00 52.86 N ANISOU 309 NE2 GLN A 55 8398 7129 4558 1005 -1303 -2378 N ATOM 310 N THR A 56 181.076 34.591 555.224 1.00 45.02 N ANISOU 310 N THR A 56 6373 7315 3417 1760 -886 -1099 N ATOM 311 CA THR A 56 182.022 33.527 555.522 1.00 46.12 C ANISOU 311 CA THR A 56 6349 7739 3433 1929 -924 -944 C ATOM 312 C THR A 56 182.951 33.297 554.334 1.00 45.39 C ANISOU 312 C THR A 56 6030 7645 3571 1733 -978 -905 C ATOM 313 O THR A 56 182.744 33.822 553.238 1.00 44.42 O ANISOU 313 O THR A 56 5883 7280 3713 1477 -951 -958 O ATOM 314 CB THR A 56 181.283 32.232 555.875 1.00 45.58 C ANISOU 314 CB THR A 56 6362 7647 3308 2227 -672 -642 C ATOM 315 OG1 THR A 56 180.459 31.835 554.770 1.00 43.52 O ANISOU 315 OG1 THR A 56 6123 7061 3351 2114 -465 -498 O ATOM 316 CG2 THR A 56 180.410 32.433 557.104 1.00 47.19 C ANISOU 316 CG2 THR A 56 6761 7916 3252 2449 -603 -649 C ATOM 317 N VAL A 57 183.989 32.491 554.568 1.00 47.99 N ANISOU 317 N VAL A 57 6187 8273 3774 1887 -1049 -795 N ATOM 318 CA VAL A 57 184.941 32.177 553.506 1.00 48.12 C ANISOU 318 CA VAL A 57 5968 8352 3963 1766 -1087 -734 C ATOM 319 C VAL A 57 184.254 31.408 552.384 1.00 47.18 C ANISOU 319 C VAL A 57 5905 7916 4107 1772 -843 -544 C ATOM 320 O VAL A 57 184.525 31.636 551.198 1.00 46.97 O ANISOU 320 O VAL A 57 5764 7776 4306 1565 -840 -563 O ATOM 321 CB VAL A 57 186.142 31.400 554.078 1.00 49.19 C ANISOU 321 CB VAL A 57 5912 8908 3869 2004 -1196 -633 C ATOM 322 CG1 VAL A 57 187.023 30.868 552.958 1.00 48.95 C ANISOU 322 CG1 VAL A 57 5649 8950 4000 1967 -1178 -518 C ATOM 323 CG2 VAL A 57 186.948 32.291 555.010 1.00 51.53 C ANISOU 323 CG2 VAL A 57 6104 9549 3928 1919 -1488 -861 C ATOM 324 N ASN A 58 183.345 30.495 552.737 1.00 50.27 N ANISOU 324 N ASN A 58 6471 8163 4465 1999 -639 -357 N ATOM 325 CA ASN A 58 182.621 29.741 551.719 1.00 49.48 C ANISOU 325 CA ASN A 58 6444 7747 4608 1979 -425 -195 C ATOM 326 C ASN A 58 181.790 30.662 550.834 1.00 48.62 C ANISOU 326 C ASN A 58 6384 7353 4738 1688 -388 -319 C ATOM 327 O ASN A 58 181.750 30.488 549.610 1.00 48.20 O ANISOU 327 O ASN A 58 6279 7127 4909 1557 -325 -286 O ATOM 328 CB ASN A 58 181.726 28.689 552.375 1.00 49.05 C ANISOU 328 CB ASN A 58 6576 7584 4475 2225 -224 28 C ATOM 329 CG ASN A 58 182.517 27.579 553.038 1.00 49.53 C ANISOU 329 CG ASN A 58 6618 7869 4333 2545 -219 208 C ATOM 330 OD1 ASN A 58 183.675 27.338 552.699 1.00 49.83 O ANISOU 330 OD1 ASN A 58 6492 8100 4341 2602 -324 204 O ATOM 331 ND2 ASN A 58 181.889 26.890 553.983 1.00 49.44 N ANISOU 331 ND2 ASN A 58 6767 7846 4172 2774 -84 388 N ATOM 332 N ASN A 59 181.125 31.651 551.433 1.00 45.72 N ANISOU 332 N ASN A 59 6124 6941 4305 1614 -425 -463 N ATOM 333 CA ASN A 59 180.259 32.539 550.669 1.00 44.33 C ANISOU 333 CA ASN A 59 6015 6497 4331 1388 -377 -563 C ATOM 334 C ASN A 59 181.033 33.582 549.874 1.00 44.59 C ANISOU 334 C ASN A 59 5927 6525 4490 1112 -540 -743 C ATOM 335 O ASN A 59 180.477 34.153 548.930 1.00 43.25 O ANISOU 335 O ASN A 59 5785 6123 4524 929 -485 -782 O ATOM 336 CB ASN A 59 179.257 33.224 551.598 1.00 43.62 C ANISOU 336 CB ASN A 59 6105 6362 4108 1455 -343 -644 C ATOM 337 CG ASN A 59 178.303 32.240 552.250 1.00 43.14 C ANISOU 337 CG ASN A 59 6149 6285 3958 1691 -140 -426 C ATOM 338 OD1 ASN A 59 178.030 31.169 551.706 1.00 42.62 O ANISOU 338 OD1 ASN A 59 6061 6109 4021 1725 5 -224 O ATOM 339 ND2 ASN A 59 177.789 32.599 553.420 1.00 43.34 N ANISOU 339 ND2 ASN A 59 6298 6416 3755 1854 -128 -464 N ATOM 340 N TYR A 60 182.291 33.852 550.232 1.00 56.56 N ANISOU 340 N TYR A 60 7298 8305 5888 1072 -738 -838 N ATOM 341 CA TYR A 60 183.133 34.666 549.362 1.00 56.78 C ANISOU 341 CA TYR A 60 7166 8349 6061 786 -874 -951 C ATOM 342 C TYR A 60 183.359 33.969 548.028 1.00 56.57 C ANISOU 342 C TYR A 60 7005 8255 6236 755 -758 -797 C ATOM 343 O TYR A 60 183.364 34.613 546.972 1.00 55.92 O ANISOU 343 O TYR A 60 6872 8028 6348 527 -755 -837 O ATOM 344 CB TYR A 60 184.467 34.968 550.043 1.00 58.14 C ANISOU 344 CB TYR A 60 7163 8872 6055 742 -1114 -1058 C ATOM 345 CG TYR A 60 184.489 36.268 550.815 1.00 58.44 C ANISOU 345 CG TYR A 60 7310 8905 5991 570 -1306 -1314 C ATOM 346 CD1 TYR A 60 183.803 36.397 552.015 1.00 58.54 C ANISOU 346 CD1 TYR A 60 7542 8916 5787 756 -1309 -1397 C ATOM 347 CD2 TYR A 60 185.205 37.363 550.348 1.00 58.70 C ANISOU 347 CD2 TYR A 60 7241 8929 6134 223 -1482 -1471 C ATOM 348 CE1 TYR A 60 183.822 37.582 552.727 1.00 59.01 C ANISOU 348 CE1 TYR A 60 7741 8951 5728 624 -1493 -1659 C ATOM 349 CE2 TYR A 60 185.231 38.553 551.054 1.00 59.20 C ANISOU 349 CE2 TYR A 60 7448 8939 6106 50 -1672 -1725 C ATOM 350 CZ TYR A 60 184.537 38.656 552.244 1.00 59.40 C ANISOU 350 CZ TYR A 60 7717 8951 5903 264 -1681 -1833 C ATOM 351 OH TYR A 60 184.556 39.836 552.954 1.00 60.09 O ANISOU 351 OH TYR A 60 7988 8967 5877 118 -1877 -2112 O ATOM 352 N PHE A 61 183.540 32.647 548.057 1.00 39.76 N ANISOU 352 N PHE A 61 4840 6217 4050 1003 -658 -616 N ATOM 353 CA PHE A 61 183.658 31.885 546.820 1.00 39.53 C ANISOU 353 CA PHE A 61 4739 6096 4186 1021 -538 -483 C ATOM 354 C PHE A 61 182.325 31.823 546.084 1.00 38.12 C ANISOU 354 C PHE A 61 4728 5563 4193 955 -368 -446 C ATOM 355 O PHE A 61 182.290 31.831 544.848 1.00 37.16 O ANISOU 355 O PHE A 61 4555 5319 4244 843 -314 -425 O ATOM 356 CB PHE A 61 184.173 30.478 547.121 1.00 39.55 C ANISOU 356 CB PHE A 61 4714 6251 4063 1332 -478 -310 C ATOM 357 CG PHE A 61 185.503 30.454 547.821 1.00 40.36 C ANISOU 357 CG PHE A 61 4616 6757 3961 1437 -644 -323 C ATOM 358 CD1 PHE A 61 186.475 31.396 547.526 1.00 40.84 C ANISOU 358 CD1 PHE A 61 4444 7035 4039 1210 -819 -443 C ATOM 359 CD2 PHE A 61 185.779 29.490 548.777 1.00 40.60 C ANISOU 359 CD2 PHE A 61 4683 6965 3777 1757 -627 -200 C ATOM 360 CE1 PHE A 61 187.698 31.375 548.169 1.00 41.79 C ANISOU 360 CE1 PHE A 61 4340 7571 3966 1286 -988 -452 C ATOM 361 CE2 PHE A 61 187.000 29.464 549.424 1.00 42.27 C ANISOU 361 CE2 PHE A 61 4688 7593 3780 1875 -791 -207 C ATOM 362 CZ PHE A 61 187.961 30.407 549.120 1.00 43.42 C ANISOU 362 CZ PHE A 61 4572 7982 3943 1632 -979 -339 C ATOM 363 N LEU A 62 181.217 31.759 546.827 1.00 38.15 N ANISOU 363 N LEU A 62 4916 5432 4146 1033 -284 -429 N ATOM 364 CA LEU A 62 179.904 31.757 546.191 1.00 34.95 C ANISOU 364 CA LEU A 62 4634 4741 3906 960 -135 -390 C ATOM 365 C LEU A 62 179.540 33.135 545.655 1.00 33.98 C ANISOU 365 C LEU A 62 4517 4497 3897 728 -184 -538 C ATOM 366 O LEU A 62 178.818 33.237 544.656 1.00 31.54 O ANISOU 366 O LEU A 62 4231 3996 3758 628 -94 -513 O ATOM 367 CB LEU A 62 178.841 31.270 547.176 1.00 34.05 C ANISOU 367 CB LEU A 62 4678 4566 3694 1117 -17 -297 C ATOM 368 CG LEU A 62 179.069 29.881 547.778 1.00 34.85 C ANISOU 368 CG LEU A 62 4819 4740 3682 1355 57 -115 C ATOM 369 CD1 LEU A 62 177.887 29.465 548.641 1.00 34.17 C ANISOU 369 CD1 LEU A 62 4879 4576 3527 1468 201 9 C ATOM 370 CD2 LEU A 62 179.331 28.853 546.687 1.00 33.26 C ANISOU 370 CD2 LEU A 62 4594 4417 3625 1368 128 -8 C ATOM 371 N PHE A 63 180.022 34.200 546.301 1.00 37.42 N ANISOU 371 N PHE A 63 4949 5033 4236 643 -333 -695 N ATOM 372 CA PHE A 63 179.790 35.547 545.790 1.00 36.27 C ANISOU 372 CA PHE A 63 4841 4738 4201 422 -387 -833 C ATOM 373 C PHE A 63 180.433 35.724 544.421 1.00 36.08 C ANISOU 373 C PHE A 63 4664 4687 4356 239 -403 -809 C ATOM 374 O PHE A 63 179.819 36.269 543.496 1.00 33.89 O ANISOU 374 O PHE A 63 4428 4215 4232 120 -337 -811 O ATOM 375 CB PHE A 63 180.330 36.582 546.779 1.00 37.56 C ANISOU 375 CB PHE A 63 5052 4999 4219 350 -569 -1021 C ATOM 376 CG PHE A 63 179.924 37.997 546.466 1.00 36.25 C ANISOU 376 CG PHE A 63 5011 4616 4146 157 -613 -1170 C ATOM 377 CD1 PHE A 63 180.617 38.744 545.526 1.00 36.04 C ANISOU 377 CD1 PHE A 63 4888 4531 4276 -104 -694 -1214 C ATOM 378 CD2 PHE A 63 178.855 38.583 547.122 1.00 35.31 C ANISOU 378 CD2 PHE A 63 5116 4353 3948 257 -564 -1250 C ATOM 379 CE1 PHE A 63 180.244 40.043 545.239 1.00 34.88 C ANISOU 379 CE1 PHE A 63 4891 4146 4217 -274 -726 -1332 C ATOM 380 CE2 PHE A 63 178.480 39.883 546.842 1.00 34.37 C ANISOU 380 CE2 PHE A 63 5148 4009 3902 119 -598 -1384 C ATOM 381 CZ PHE A 63 179.175 40.614 545.898 1.00 34.14 C ANISOU 381 CZ PHE A 63 5047 3883 4041 -152 -681 -1424 C ATOM 382 N SER A 64 181.681 35.272 544.277 1.00 36.18 N ANISOU 382 N SER A 64 4489 4925 4332 238 -485 -773 N ATOM 383 CA SER A 64 182.350 35.343 542.983 1.00 36.18 C ANISOU 383 CA SER A 64 4321 4952 4475 103 -480 -722 C ATOM 384 C SER A 64 181.661 34.448 541.962 1.00 34.85 C ANISOU 384 C SER A 64 4188 4636 4417 204 -310 -597 C ATOM 385 O SER A 64 181.588 34.787 540.775 1.00 33.48 O ANISOU 385 O SER A 64 3968 4370 4382 83 -266 -577 O ATOM 386 CB SER A 64 183.820 34.955 543.133 1.00 38.09 C ANISOU 386 CB SER A 64 4328 5522 4622 130 -591 -689 C ATOM 387 OG SER A 64 184.453 34.839 541.869 1.00 37.73 O ANISOU 387 OG SER A 64 4106 5543 4689 57 -553 -605 O ATOM 388 N LEU A 65 181.151 33.298 542.406 1.00 32.86 N ANISOU 388 N LEU A 65 4029 4356 4100 419 -218 -511 N ATOM 389 CA LEU A 65 180.433 32.411 541.498 1.00 29.60 C ANISOU 389 CA LEU A 65 3679 3776 3792 487 -77 -414 C ATOM 390 C LEU A 65 179.120 33.038 541.046 1.00 26.68 C ANISOU 390 C LEU A 65 3419 3176 3541 369 -5 -445 C ATOM 391 O LEU A 65 178.772 32.979 539.861 1.00 24.56 O ANISOU 391 O LEU A 65 3136 2802 3394 305 54 -420 O ATOM 392 CB LEU A 65 180.191 31.061 542.173 1.00 28.96 C ANISOU 392 CB LEU A 65 3695 3688 3622 714 -2 -306 C ATOM 393 CG LEU A 65 179.819 29.892 541.261 1.00 26.51 C ANISOU 393 CG LEU A 65 3451 3224 3399 795 112 -211 C ATOM 394 CD1 LEU A 65 180.866 29.709 540.171 1.00 26.96 C ANISOU 394 CD1 LEU A 65 3375 3388 3482 813 85 -210 C ATOM 395 CD2 LEU A 65 179.660 28.616 542.073 1.00 26.71 C ANISOU 395 CD2 LEU A 65 3602 3214 3334 1005 181 -92 C ATOM 396 N ALA A 66 178.380 33.650 541.974 1.00 30.92 N ANISOU 396 N ALA A 66 4065 3659 4024 365 -8 -497 N ATOM 397 CA ALA A 66 177.172 34.374 541.600 1.00 28.43 C ANISOU 397 CA ALA A 66 3837 3166 3799 284 58 -523 C ATOM 398 C ALA A 66 177.487 35.631 540.802 1.00 27.79 C ANISOU 398 C ALA A 66 3717 3032 3810 104 -4 -606 C ATOM 399 O ALA A 66 176.637 36.092 540.032 1.00 25.30 O ANISOU 399 O ALA A 66 3441 2577 3594 48 61 -596 O ATOM 400 CB ALA A 66 176.363 34.733 542.847 1.00 28.78 C ANISOU 400 CB ALA A 66 4008 3196 3730 372 79 -554 C ATOM 401 N CYS A 67 178.686 36.195 540.970 1.00 42.51 N ANISOU 401 N CYS A 67 5497 5013 5641 6 -129 -675 N ATOM 402 CA CYS A 67 179.068 37.367 540.189 1.00 41.92 C ANISOU 402 CA CYS A 67 5387 4873 5669 -197 -182 -725 C ATOM 403 C CYS A 67 179.279 37.006 538.725 1.00 40.79 C ANISOU 403 C CYS A 67 5123 4734 5640 -238 -114 -627 C ATOM 404 O CYS A 67 178.861 37.750 537.830 1.00 38.72 O ANISOU 404 O CYS A 67 4887 4343 5481 -339 -75 -616 O ATOM 405 CB CYS A 67 180.329 37.999 540.776 1.00 44.58 C ANISOU 405 CB CYS A 67 5640 5354 5945 -332 -344 -813 C ATOM 406 SG CYS A 67 180.987 39.378 539.814 1.00 43.90 S ANISOU 406 SG CYS A 67 5490 5189 6002 -634 -410 -839 S ATOM 407 N ALA A 68 179.926 35.869 538.462 1.00 33.79 N ANISOU 407 N ALA A 68 4119 4000 4720 -133 -97 -553 N ATOM 408 CA ALA A 68 180.110 35.427 537.084 1.00 33.08 C ANISOU 408 CA ALA A 68 3937 3926 4704 -125 -29 -473 C ATOM 409 C ALA A 68 178.789 34.986 536.467 1.00 29.29 C ANISOU 409 C ALA A 68 3575 3269 4286 -62 79 -444 C ATOM 410 O ALA A 68 178.549 35.208 535.274 1.00 27.78 O ANISOU 410 O ALA A 68 3356 3031 4168 -110 124 -414 O ATOM 411 CB ALA A 68 181.135 34.294 537.032 1.00 35.76 C ANISOU 411 CB ALA A 68 4153 4469 4965 19 -36 -412 C ATOM 412 N ASP A 69 177.919 34.363 537.266 1.00 35.82 N ANISOU 412 N ASP A 69 4516 4018 5074 40 118 -443 N ATOM 413 CA ASP A 69 176.614 33.949 536.763 1.00 32.87 C ANISOU 413 CA ASP A 69 4224 3503 4761 64 206 -410 C ATOM 414 C ASP A 69 175.738 35.146 536.420 1.00 31.20 C ANISOU 414 C ASP A 69 4052 3191 4612 -29 225 -437 C ATOM 415 O ASP A 69 174.881 35.052 535.534 1.00 29.39 O ANISOU 415 O ASP A 69 3828 2896 4444 -39 280 -407 O ATOM 416 CB ASP A 69 175.916 33.061 537.791 1.00 32.88 C ANISOU 416 CB ASP A 69 4317 3465 4710 169 251 -373 C ATOM 417 CG ASP A 69 176.664 31.772 538.047 1.00 34.23 C ANISOU 417 CG ASP A 69 4489 3695 4822 294 251 -322 C ATOM 418 OD1 ASP A 69 177.642 31.501 537.321 1.00 34.94 O ANISOU 418 OD1 ASP A 69 4502 3866 4909 320 223 -323 O ATOM 419 OD2 ASP A 69 176.281 31.033 538.977 1.00 34.73 O ANISOU 419 OD2 ASP A 69 4634 3732 4831 385 290 -268 O ATOM 420 N LEU A 70 175.931 36.272 537.110 1.00 36.11 N ANISOU 420 N LEU A 70 4715 3797 5208 -85 174 -499 N ATOM 421 CA LEU A 70 175.152 37.465 536.803 1.00 34.85 C ANISOU 421 CA LEU A 70 4629 3515 5096 -139 197 -521 C ATOM 422 C LEU A 70 175.556 38.056 535.458 1.00 34.31 C ANISOU 422 C LEU A 70 4495 3427 5114 -242 198 -488 C ATOM 423 O LEU A 70 174.698 38.509 534.691 1.00 33.01 O ANISOU 423 O LEU A 70 4361 3184 4997 -235 255 -453 O ATOM 424 CB LEU A 70 175.317 38.497 537.918 1.00 36.26 C ANISOU 424 CB LEU A 70 4918 3645 5213 -162 133 -617 C ATOM 425 CG LEU A 70 174.500 39.782 537.782 1.00 35.51 C ANISOU 425 CG LEU A 70 4957 3388 5147 -170 161 -650 C ATOM 426 CD1 LEU A 70 173.015 39.464 537.720 1.00 34.27 C ANISOU 426 CD1 LEU A 70 4829 3212 4979 -28 273 -588 C ATOM 427 CD2 LEU A 70 174.803 40.736 538.928 1.00 37.29 C ANISOU 427 CD2 LEU A 70 5331 3543 5293 -189 78 -778 C ATOM 428 N ILE A 71 176.856 38.056 535.153 1.00 34.20 N ANISOU 428 N ILE A 71 4373 3515 5106 -326 142 -481 N ATOM 429 CA ILE A 71 177.322 38.582 533.874 1.00 34.25 C ANISOU 429 CA ILE A 71 4297 3535 5180 -420 159 -418 C ATOM 430 C ILE A 71 176.814 37.723 532.723 1.00 33.19 C ANISOU 430 C ILE A 71 4116 3438 5056 -324 233 -356 C ATOM 431 O ILE A 71 176.502 38.240 531.643 1.00 32.74 O ANISOU 431 O ILE A 71 4050 3351 5040 -348 277 -303 O ATOM 432 CB ILE A 71 178.859 38.684 533.869 1.00 36.73 C ANISOU 432 CB ILE A 71 4464 4005 5486 -529 89 -403 C ATOM 433 CG1 ILE A 71 179.338 39.536 535.046 1.00 37.96 C ANISOU 433 CG1 ILE A 71 4673 4127 5625 -654 -16 -492 C ATOM 434 CG2 ILE A 71 179.359 39.265 532.554 1.00 37.02 C ANISOU 434 CG2 ILE A 71 4402 4079 5587 -630 127 -306 C ATOM 435 CD1 ILE A 71 180.843 39.625 535.162 1.00 40.51 C ANISOU 435 CD1 ILE A 71 4812 4646 5932 -788 -107 -477 C ATOM 436 N ILE A 72 176.715 36.409 532.931 1.00 35.99 N ANISOU 436 N ILE A 72 4460 3848 5366 -212 244 -364 N ATOM 437 CA ILE A 72 176.179 35.530 531.898 1.00 35.09 C ANISOU 437 CA ILE A 72 4339 3740 5254 -134 292 -338 C ATOM 438 C ILE A 72 174.710 35.844 531.638 1.00 33.32 C ANISOU 438 C ILE A 72 4183 3412 5066 -135 331 -336 C ATOM 439 O ILE A 72 174.258 35.860 530.486 1.00 33.28 O ANISOU 439 O ILE A 72 4154 3421 5071 -124 355 -312 O ATOM 440 CB ILE A 72 176.387 34.057 532.297 1.00 35.33 C ANISOU 440 CB ILE A 72 4389 3798 5235 -25 290 -352 C ATOM 441 CG1 ILE A 72 177.878 33.711 532.317 1.00 37.89 C ANISOU 441 CG1 ILE A 72 4617 4277 5504 26 261 -335 C ATOM 442 CG2 ILE A 72 175.631 33.129 531.360 1.00 34.28 C ANISOU 442 CG2 ILE A 72 4300 3614 5110 28 321 -358 C ATOM 443 CD1 ILE A 72 178.569 33.892 530.983 1.00 39.25 C ANISOU 443 CD1 ILE A 72 4683 4565 5667 33 282 -294 C ATOM 444 N GLY A 73 173.944 36.114 532.697 1.00 35.35 N ANISOU 444 N GLY A 73 4514 3597 5322 -128 338 -356 N ATOM 445 CA GLY A 73 172.526 36.377 532.525 1.00 34.65 C ANISOU 445 CA GLY A 73 4456 3459 5252 -105 382 -336 C ATOM 446 C GLY A 73 172.232 37.737 531.924 1.00 34.91 C ANISOU 446 C GLY A 73 4507 3449 5307 -120 401 -311 C ATOM 447 O GLY A 73 171.226 37.905 531.227 1.00 35.16 O ANISOU 447 O GLY A 73 4520 3493 5344 -81 435 -273 O ATOM 448 N VAL A 74 173.093 38.719 532.180 1.00 34.84 N ANISOU 448 N VAL A 74 4538 3390 5310 -182 374 -325 N ATOM 449 CA VAL A 74 172.894 40.077 531.679 1.00 35.33 C ANISOU 449 CA VAL A 74 4664 3358 5402 -203 397 -289 C ATOM 450 C VAL A 74 173.437 40.237 530.265 1.00 36.10 C ANISOU 450 C VAL A 74 4679 3512 5525 -247 413 -212 C ATOM 451 O VAL A 74 172.732 40.698 529.365 1.00 36.62 O ANISOU 451 O VAL A 74 4753 3570 5591 -191 459 -146 O ATOM 452 CB VAL A 74 173.546 41.090 532.645 1.00 35.94 C ANISOU 452 CB VAL A 74 4853 3315 5486 -282 350 -348 C ATOM 453 CG1 VAL A 74 173.500 42.494 532.058 1.00 36.68 C ANISOU 453 CG1 VAL A 74 5049 3261 5628 -327 374 -301 C ATOM 454 CG2 VAL A 74 172.860 41.055 534.006 1.00 35.82 C ANISOU 454 CG2 VAL A 74 4942 3258 5410 -191 347 -424 C ATOM 455 N PHE A 75 174.695 39.856 530.041 1.00 35.72 N ANISOU 455 N PHE A 75 4539 3552 5479 -323 382 -204 N ATOM 456 CA PHE A 75 175.345 40.093 528.755 1.00 37.08 C ANISOU 456 CA PHE A 75 4623 3807 5659 -357 412 -111 C ATOM 457 C PHE A 75 175.257 38.882 527.828 1.00 37.63 C ANISOU 457 C PHE A 75 4603 4025 5668 -252 428 -107 C ATOM 458 O PHE A 75 174.769 38.992 526.700 1.00 38.51 O ANISOU 458 O PHE A 75 4698 4183 5751 -192 466 -53 O ATOM 459 CB PHE A 75 176.812 40.483 528.970 1.00 38.29 C ANISOU 459 CB PHE A 75 4700 4011 5840 -501 377 -84 C ATOM 460 CG PHE A 75 176.997 41.803 529.663 1.00 38.44 C ANISOU 460 CG PHE A 75 4827 3856 5922 -646 345 -95 C ATOM 461 CD1 PHE A 75 177.092 42.978 528.934 1.00 39.25 C ANISOU 461 CD1 PHE A 75 4978 3854 6083 -738 387 9 C ATOM 462 CD2 PHE A 75 177.089 41.867 531.042 1.00 38.17 C ANISOU 462 CD2 PHE A 75 4870 3753 5881 -687 270 -211 C ATOM 463 CE1 PHE A 75 177.270 44.194 529.572 1.00 39.73 C ANISOU 463 CE1 PHE A 75 5184 3702 6210 -886 349 -15 C ATOM 464 CE2 PHE A 75 177.267 43.079 531.685 1.00 38.79 C ANISOU 464 CE2 PHE A 75 5084 3650 6005 -822 222 -253 C ATOM 465 CZ PHE A 75 177.357 44.244 530.949 1.00 39.52 C ANISOU 465 CZ PHE A 75 5247 3599 6172 -931 259 -162 C ATOM 466 N SER A 76 175.726 37.722 528.294 1.00 32.23 N ANISOU 466 N SER A 76 3881 3412 4951 -215 395 -169 N ATOM 467 CA SER A 76 175.932 36.589 527.395 1.00 33.41 C ANISOU 467 CA SER A 76 3980 3680 5035 -113 404 -178 C ATOM 468 C SER A 76 174.611 36.042 526.865 1.00 32.54 C ANISOU 468 C SER A 76 3925 3532 4906 -49 403 -220 C ATOM 469 O SER A 76 174.482 35.766 525.666 1.00 33.68 O ANISOU 469 O SER A 76 4045 3761 4992 17 413 -212 O ATOM 470 CB SER A 76 176.723 35.494 528.110 1.00 33.61 C ANISOU 470 CB SER A 76 3988 3755 5027 -62 373 -229 C ATOM 471 OG SER A 76 177.997 35.972 528.506 1.00 35.60 O ANISOU 471 OG SER A 76 4142 4103 5280 -124 359 -185 O ATOM 472 N MET A 77 173.619 35.872 527.742 1.00 32.33 N ANISOU 472 N MET A 77 3962 3407 4916 -68 389 -262 N ATOM 473 CA MET A 77 172.348 35.296 527.310 1.00 32.38 C ANISOU 473 CA MET A 77 3984 3408 4911 -44 377 -293 C ATOM 474 C MET A 77 171.626 36.206 526.323 1.00 33.79 C ANISOU 474 C MET A 77 4128 3639 5070 -20 396 -237 C ATOM 475 O MET A 77 171.107 35.736 525.304 1.00 35.20 O ANISOU 475 O MET A 77 4279 3899 5196 18 371 -259 O ATOM 476 CB MET A 77 171.456 35.017 528.518 1.00 31.07 C ANISOU 476 CB MET A 77 3858 3162 4787 -76 376 -311 C ATOM 477 CG MET A 77 171.851 33.799 529.331 1.00 30.24 C ANISOU 477 CG MET A 77 3799 3006 4684 -77 359 -353 C ATOM 478 SD MET A 77 170.685 33.515 530.676 0.81 29.64 S ANISOU 478 SD MET A 77 3754 2866 4643 -111 383 -332 S ATOM 479 CE MET A 77 171.289 31.968 531.339 1.00 29.42 C ANISOU 479 CE MET A 77 3805 2764 4610 -98 370 -353 C ATOM 480 N ASN A 78 171.580 37.509 526.608 1.00 33.13 N ANISOU 480 N ASN A 78 4064 3505 5018 -31 435 -169 N ATOM 481 CA ASN A 78 170.820 38.421 525.759 1.00 34.47 C ANISOU 481 CA ASN A 78 4224 3711 5163 27 465 -94 C ATOM 482 C ASN A 78 171.486 38.610 524.402 1.00 35.85 C ANISOU 482 C ASN A 78 4353 3988 5278 63 483 -32 C ATOM 483 O ASN A 78 170.804 38.642 523.371 1.00 36.70 O ANISOU 483 O ASN A 78 4426 4203 5317 143 480 -3 O ATOM 484 CB ASN A 78 170.636 39.762 526.468 1.00 33.93 C ANISOU 484 CB ASN A 78 4238 3513 5140 28 508 -39 C ATOM 485 CG ASN A 78 169.686 39.669 527.645 1.00 33.01 C ANISOU 485 CG ASN A 78 4159 3344 5039 54 509 -83 C ATOM 486 OD1 ASN A 78 168.628 39.046 527.555 1.00 33.71 O ANISOU 486 OD1 ASN A 78 4182 3524 5102 94 498 -93 O ATOM 487 ND2 ASN A 78 170.064 40.282 528.760 1.00 31.94 N ANISOU 487 ND2 ASN A 78 4122 3078 4935 26 517 -107 N ATOM 488 N LEU A 79 172.816 38.737 524.376 1.00 37.19 N ANISOU 488 N LEU A 79 4507 4161 5461 14 502 -1 N ATOM 489 CA LEU A 79 173.509 38.891 523.102 1.00 38.27 C ANISOU 489 CA LEU A 79 4582 4431 5527 61 539 82 C ATOM 490 C LEU A 79 173.414 37.629 522.254 1.00 38.47 C ANISOU 490 C LEU A 79 4573 4599 5445 160 501 -1 C ATOM 491 O LEU A 79 173.376 37.715 521.021 1.00 39.48 O ANISOU 491 O LEU A 79 4668 4863 5470 254 521 48 O ATOM 492 CB LEU A 79 174.973 39.266 523.337 1.00 38.67 C ANISOU 492 CB LEU A 79 4585 4493 5616 -30 570 149 C ATOM 493 CG LEU A 79 175.231 40.662 523.911 1.00 38.58 C ANISOU 493 CG LEU A 79 4626 4328 5705 -160 599 237 C ATOM 494 CD1 LEU A 79 176.721 40.924 524.048 1.00 38.87 C ANISOU 494 CD1 LEU A 79 4570 4421 5777 -290 611 304 C ATOM 495 CD2 LEU A 79 174.577 41.730 523.051 1.00 39.48 C ANISOU 495 CD2 LEU A 79 4796 4400 5807 -109 662 365 C ATOM 496 N TYR A 80 173.371 36.455 522.889 1.00 21.62 N ANISOU 496 N TYR A 80 2468 2424 3321 149 445 -128 N ATOM 497 CA TYR A 80 173.245 35.211 522.139 1.00 22.51 C ANISOU 497 CA TYR A 80 2601 2615 3338 235 395 -233 C ATOM 498 C TYR A 80 171.827 34.996 521.627 1.00 23.61 C ANISOU 498 C TYR A 80 2752 2776 3442 240 335 -290 C ATOM 499 O TYR A 80 171.642 34.394 520.563 1.00 25.35 O ANISOU 499 O TYR A 80 2983 3102 3548 318 289 -358 O ATOM 500 CB TYR A 80 173.678 34.028 523.006 1.00 21.72 C ANISOU 500 CB TYR A 80 2560 2426 3267 222 360 -333 C ATOM 501 CG TYR A 80 173.859 32.741 522.236 1.00 22.83 C ANISOU 501 CG TYR A 80 2768 2604 3302 329 317 -447 C ATOM 502 CD1 TYR A 80 174.887 32.604 521.313 1.00 23.95 C ANISOU 502 CD1 TYR A 80 2884 2895 3322 473 355 -427 C ATOM 503 CD2 TYR A 80 173.010 31.659 522.436 1.00 22.86 C ANISOU 503 CD2 TYR A 80 2873 2491 3321 289 241 -572 C ATOM 504 CE1 TYR A 80 175.063 31.431 520.605 1.00 25.09 C ANISOU 504 CE1 TYR A 80 3127 3061 3345 609 316 -550 C ATOM 505 CE2 TYR A 80 173.178 30.480 521.732 1.00 23.91 C ANISOU 505 CE2 TYR A 80 3118 2610 3356 383 190 -698 C ATOM 506 CZ TYR A 80 174.207 30.372 520.818 1.00 25.01 C ANISOU 506 CZ TYR A 80 3257 2889 3358 561 226 -698 C ATOM 507 OH TYR A 80 174.385 29.205 520.114 1.00 26.00 O ANISOU 507 OH TYR A 80 3529 2989 3362 693 176 -842 O ATOM 508 N THR A 81 170.820 35.470 522.366 1.00 29.62 N ANISOU 508 N THR A 81 3504 3464 4285 168 329 -267 N ATOM 509 CA THR A 81 169.445 35.383 521.885 1.00 31.11 C ANISOU 509 CA THR A 81 3654 3730 4437 171 273 -294 C ATOM 510 C THR A 81 169.235 36.278 520.672 1.00 32.22 C ANISOU 510 C THR A 81 3744 4025 4474 282 296 -202 C ATOM 511 O THR A 81 168.585 35.876 519.699 1.00 34.19 O ANISOU 511 O THR A 81 3957 4418 4616 330 226 -256 O ATOM 512 CB THR A 81 168.470 35.760 523.000 1.00 30.27 C ANISOU 512 CB THR A 81 3525 3552 4425 105 286 -260 C ATOM 513 OG1 THR A 81 168.662 34.888 524.119 1.00 29.46 O ANISOU 513 OG1 THR A 81 3471 3320 4401 14 273 -326 O ATOM 514 CG2 THR A 81 167.033 35.641 522.511 1.00 31.99 C ANISOU 514 CG2 THR A 81 3651 3904 4598 105 225 -270 C ATOM 515 N LEU A 82 169.782 37.495 520.713 1.00 39.82 N ANISOU 515 N LEU A 82 4712 4954 5462 318 389 -62 N ATOM 516 CA LEU A 82 169.706 38.387 519.561 1.00 40.60 C ANISOU 516 CA LEU A 82 4783 5181 5462 436 434 63 C ATOM 517 C LEU A 82 170.421 37.787 518.357 1.00 41.78 C ANISOU 517 C LEU A 82 4915 5490 5471 521 422 35 C ATOM 518 O LEU A 82 169.977 37.952 517.214 1.00 43.00 O ANISOU 518 O LEU A 82 5036 5819 5483 641 406 70 O ATOM 519 CB LEU A 82 170.307 39.745 519.920 1.00 39.71 C ANISOU 519 CB LEU A 82 4716 4945 5428 420 540 223 C ATOM 520 CG LEU A 82 170.315 40.809 518.824 1.00 40.66 C ANISOU 520 CG LEU A 82 4835 5150 5464 537 615 401 C ATOM 521 CD1 LEU A 82 168.896 41.245 518.507 1.00 41.18 C ANISOU 521 CD1 LEU A 82 4885 5293 5467 660 594 438 C ATOM 522 CD2 LEU A 82 171.171 41.996 519.236 1.00 40.84 C ANISOU 522 CD2 LEU A 82 4930 4996 5592 459 714 548 C ATOM 523 N TYR A 83 171.526 37.080 518.598 1.00 36.14 N ANISOU 523 N TYR A 83 4222 4739 4770 490 430 -25 N ATOM 524 CA TYR A 83 172.291 36.481 517.509 1.00 37.15 C ANISOU 524 CA TYR A 83 4342 5029 4743 612 434 -53 C ATOM 525 C TYR A 83 171.478 35.411 516.788 1.00 38.99 C ANISOU 525 C TYR A 83 4613 5354 4849 675 313 -229 C ATOM 526 O TYR A 83 171.394 35.404 515.555 1.00 40.27 O ANISOU 526 O TYR A 83 4763 5705 4834 815 299 -227 O ATOM 527 CB TYR A 83 173.592 35.893 518.061 1.00 36.46 C ANISOU 527 CB TYR A 83 4263 4894 4695 591 468 -81 C ATOM 528 CG TYR A 83 174.528 35.317 517.020 1.00 37.28 C ANISOU 528 CG TYR A 83 4353 5183 4626 757 499 -90 C ATOM 529 CD1 TYR A 83 174.556 35.815 515.723 1.00 38.12 C ANISOU 529 CD1 TYR A 83 4417 5493 4572 896 548 10 C ATOM 530 CD2 TYR A 83 175.384 34.270 517.337 1.00 37.21 C ANISOU 530 CD2 TYR A 83 4381 5161 4594 811 490 -189 C ATOM 531 CE1 TYR A 83 175.413 35.287 514.774 1.00 38.88 C ANISOU 531 CE1 TYR A 83 4501 5788 4483 1082 590 6 C ATOM 532 CE2 TYR A 83 176.243 33.736 516.395 1.00 37.91 C ANISOU 532 CE2 TYR A 83 4464 5437 4502 1010 531 -197 C ATOM 533 CZ TYR A 83 176.253 34.248 515.115 1.00 38.75 C ANISOU 533 CZ TYR A 83 4521 5758 4444 1144 582 -103 C ATOM 534 OH TYR A 83 177.108 33.718 514.175 1.00 39.50 O ANISOU 534 OH TYR A 83 4609 6067 4331 1374 635 -107 O ATOM 535 N THR A 84 170.867 34.498 517.545 1.00 39.83 N ANISOU 535 N THR A 84 4769 5326 5037 563 220 -381 N ATOM 536 CA THR A 84 170.175 33.368 516.936 1.00 42.01 C ANISOU 536 CA THR A 84 5102 5646 5214 569 86 -571 C ATOM 537 C THR A 84 168.811 33.753 516.373 1.00 43.94 C ANISOU 537 C THR A 84 5264 6030 5400 555 5 -569 C ATOM 538 O THR A 84 168.401 33.210 515.341 1.00 46.22 O ANISOU 538 O THR A 84 5570 6462 5529 616 -100 -688 O ATOM 539 CB THR A 84 170.021 32.239 517.955 1.00 41.64 C ANISOU 539 CB THR A 84 5145 5387 5289 428 22 -708 C ATOM 540 OG1 THR A 84 169.334 32.730 519.113 1.00 40.68 O ANISOU 540 OG1 THR A 84 4961 5163 5334 285 45 -630 O ATOM 541 CG2 THR A 84 171.386 31.708 518.372 1.00 39.92 C ANISOU 541 CG2 THR A 84 5011 5072 5085 495 88 -721 C ATOM 542 N VAL A 85 168.100 34.675 517.026 1.00 38.46 N ANISOU 542 N VAL A 85 4483 5316 4815 494 47 -443 N ATOM 543 CA VAL A 85 166.773 35.063 516.553 1.00 39.75 C ANISOU 543 CA VAL A 85 4538 5650 4914 509 -23 -420 C ATOM 544 C VAL A 85 166.870 35.818 515.233 1.00 40.29 C ANISOU 544 C VAL A 85 4570 5944 4794 708 5 -320 C ATOM 545 O VAL A 85 166.098 35.566 514.300 1.00 42.39 O ANISOU 545 O VAL A 85 4780 6422 4904 765 -108 -389 O ATOM 546 CB VAL A 85 166.045 35.888 517.631 1.00 37.87 C ANISOU 546 CB VAL A 85 4230 5340 4820 450 37 -297 C ATOM 547 CG1 VAL A 85 165.009 36.806 517.001 1.00 38.05 C ANISOU 547 CG1 VAL A 85 4136 5577 4746 573 31 -181 C ATOM 548 CG2 VAL A 85 165.388 34.963 518.642 1.00 38.16 C ANISOU 548 CG2 VAL A 85 4251 5268 4982 261 -34 -404 C ATOM 549 N ILE A 86 167.818 36.751 515.128 1.00 47.17 N ANISOU 549 N ILE A 86 5470 6784 5670 805 150 -148 N ATOM 550 CA ILE A 86 167.968 37.511 513.891 1.00 47.74 C ANISOU 550 CA ILE A 86 5514 7063 5563 999 204 -10 C ATOM 551 C ILE A 86 168.558 36.641 512.787 1.00 49.67 C ANISOU 551 C ILE A 86 5799 7466 5606 1109 150 -131 C ATOM 552 O ILE A 86 168.197 36.787 511.612 1.00 51.45 O ANISOU 552 O ILE A 86 5993 7937 5620 1270 111 -114 O ATOM 553 CB ILE A 86 168.812 38.775 514.151 1.00 45.73 C ANISOU 553 CB ILE A 86 5283 6698 5394 1030 381 229 C ATOM 554 CG1 ILE A 86 167.977 39.818 514.899 1.00 44.72 C ANISOU 554 CG1 ILE A 86 5145 6457 5388 1007 424 352 C ATOM 555 CG2 ILE A 86 169.354 39.356 512.856 1.00 46.56 C ANISOU 555 CG2 ILE A 86 5377 6998 5314 1217 466 390 C ATOM 556 CD1 ILE A 86 168.578 41.206 514.897 1.00 43.99 C ANISOU 556 CD1 ILE A 86 5111 6254 5348 1056 581 594 C ATOM 557 N GLY A 87 169.446 35.712 513.135 1.00 54.97 N ANISOU 557 N GLY A 87 6551 8018 6319 1054 146 -259 N ATOM 558 CA GLY A 87 170.055 34.823 512.170 1.00 56.26 C ANISOU 558 CA GLY A 87 6786 8309 6281 1192 103 -393 C ATOM 559 C GLY A 87 171.479 35.170 511.798 1.00 54.90 C ANISOU 559 C GLY A 87 6613 8206 6042 1330 262 -246 C ATOM 560 O GLY A 87 172.160 34.344 511.178 1.00 55.46 O ANISOU 560 O GLY A 87 6753 8368 5953 1469 250 -358 O ATOM 561 N TYR A 88 171.944 36.365 512.151 1.00 39.61 N ANISOU 561 N TYR A 88 4601 6230 4218 1296 410 4 N ATOM 562 CA TYR A 88 173.318 36.778 511.904 1.00 38.71 C ANISOU 562 CA TYR A 88 4444 6188 4074 1369 567 179 C ATOM 563 C TYR A 88 173.731 37.729 513.019 1.00 36.94 C ANISOU 563 C TYR A 88 4178 5761 4098 1179 664 348 C ATOM 564 O TYR A 88 172.938 38.056 513.907 1.00 36.25 O ANISOU 564 O TYR A 88 4114 5487 4173 1038 616 320 O ATOM 565 CB TYR A 88 173.465 37.419 510.519 1.00 39.82 C ANISOU 565 CB TYR A 88 4538 6605 3987 1580 652 354 C ATOM 566 CG TYR A 88 172.541 38.593 510.277 1.00 40.15 C ANISOU 566 CG TYR A 88 4550 6661 4042 1584 676 527 C ATOM 567 CD1 TYR A 88 171.265 38.403 509.762 1.00 41.71 C ANISOU 567 CD1 TYR A 88 4760 6972 4116 1663 543 415 C ATOM 568 CD2 TYR A 88 172.947 39.892 510.559 1.00 39.27 C ANISOU 568 CD2 TYR A 88 4406 6451 4063 1513 828 806 C ATOM 569 CE1 TYR A 88 170.418 39.472 509.537 1.00 42.07 C ANISOU 569 CE1 TYR A 88 4772 7058 4154 1714 570 588 C ATOM 570 CE2 TYR A 88 172.106 40.967 510.338 1.00 39.76 C ANISOU 570 CE2 TYR A 88 4479 6499 4129 1556 860 972 C ATOM 571 CZ TYR A 88 170.842 40.751 509.829 1.00 40.95 C ANISOU 571 CZ TYR A 88 4630 6790 4141 1678 737 869 C ATOM 572 OH TYR A 88 170.001 41.816 509.608 1.00 41.47 O ANISOU 572 OH TYR A 88 4698 6867 4190 1766 774 1048 O ATOM 573 N TRP A 89 174.987 38.167 512.978 1.00 36.40 N ANISOU 573 N TRP A 89 4041 5744 4048 1175 797 520 N ATOM 574 CA TRP A 89 175.490 39.097 513.979 1.00 35.38 C ANISOU 574 CA TRP A 89 3876 5426 4142 971 873 669 C ATOM 575 C TRP A 89 175.228 40.524 513.522 1.00 35.98 C ANISOU 575 C TRP A 89 3947 5490 4236 962 972 920 C ATOM 576 O TRP A 89 175.768 40.939 512.487 1.00 36.92 O ANISOU 576 O TRP A 89 4006 5803 4219 1077 1081 1109 O ATOM 577 CB TRP A 89 176.974 38.889 514.223 1.00 35.13 C ANISOU 577 CB TRP A 89 3747 5466 4135 930 952 739 C ATOM 578 CG TRP A 89 177.483 39.717 515.358 1.00 34.51 C ANISOU 578 CG TRP A 89 3635 5190 4286 685 987 842 C ATOM 579 CD1 TRP A 89 178.223 40.858 515.273 1.00 35.05 C ANISOU 579 CD1 TRP A 89 3628 5259 4432 560 1101 1088 C ATOM 580 CD2 TRP A 89 177.262 39.484 516.754 1.00 33.49 C ANISOU 580 CD2 TRP A 89 3563 4832 4332 524 899 696 C ATOM 581 NE1 TRP A 89 178.488 41.345 516.530 1.00 34.54 N ANISOU 581 NE1 TRP A 89 3578 4969 4577 321 1070 1077 N ATOM 582 CE2 TRP A 89 177.908 40.519 517.457 1.00 33.53 C ANISOU 582 CE2 TRP A 89 3529 4712 4500 315 950 839 C ATOM 583 CE3 TRP A 89 176.585 38.497 517.477 1.00 32.75 C ANISOU 583 CE3 TRP A 89 3552 4624 4266 529 783 466 C ATOM 584 CZ2 TRP A 89 177.898 40.595 518.849 1.00 32.76 C ANISOU 584 CZ2 TRP A 89 3477 4403 4566 142 881 740 C ATOM 585 CZ3 TRP A 89 176.577 38.574 518.858 1.00 31.85 C ANISOU 585 CZ3 TRP A 89 3472 4309 4320 364 737 400 C ATOM 586 CH2 TRP A 89 177.229 39.616 519.529 1.00 31.85 C ANISOU 586 CH2 TRP A 89 3436 4210 4456 187 782 527 C ATOM 587 N PRO A 90 174.410 41.296 514.236 1.00 35.42 N ANISOU 587 N PRO A 90 3948 5196 4313 855 950 943 N ATOM 588 CA PRO A 90 174.046 42.633 513.754 1.00 36.43 C ANISOU 588 CA PRO A 90 4117 5282 4442 891 1044 1179 C ATOM 589 C PRO A 90 174.800 43.768 514.432 1.00 36.62 C ANISOU 589 C PRO A 90 4173 5078 4662 687 1142 1362 C ATOM 590 O PRO A 90 174.659 44.925 514.027 1.00 37.62 O ANISOU 590 O PRO A 90 4365 5125 4805 703 1239 1584 O ATOM 591 CB PRO A 90 172.552 42.702 514.079 1.00 36.25 C ANISOU 591 CB PRO A 90 4167 5175 4432 947 950 1071 C ATOM 592 CG PRO A 90 172.448 41.923 515.364 1.00 34.82 C ANISOU 592 CG PRO A 90 4000 4835 4394 795 849 846 C ATOM 593 CD PRO A 90 173.533 40.859 515.337 1.00 34.41 C ANISOU 593 CD PRO A 90 3884 4885 4307 763 832 742 C ATOM 594 N LEU A 91 175.593 43.463 515.458 1.00 36.91 N ANISOU 594 N LEU A 91 4178 5000 4844 493 1112 1271 N ATOM 595 CA LEU A 91 176.195 44.492 516.296 1.00 36.90 C ANISOU 595 CA LEU A 91 4225 4752 5042 257 1158 1385 C ATOM 596 C LEU A 91 177.604 44.887 515.867 1.00 37.41 C ANISOU 596 C LEU A 91 4162 4928 5124 132 1266 1597 C ATOM 597 O LEU A 91 178.194 45.777 516.488 1.00 37.49 O ANISOU 597 O LEU A 91 4202 4740 5304 -108 1295 1701 O ATOM 598 CB LEU A 91 176.210 44.033 517.757 1.00 35.70 C ANISOU 598 CB LEU A 91 4106 4427 5032 107 1049 1169 C ATOM 599 CG LEU A 91 174.840 43.713 518.359 1.00 35.22 C ANISOU 599 CG LEU A 91 4153 4252 4978 194 956 987 C ATOM 600 CD1 LEU A 91 174.973 43.394 519.836 1.00 34.03 C ANISOU 600 CD1 LEU A 91 4039 3932 4959 44 874 817 C ATOM 601 CD2 LEU A 91 173.865 44.863 518.138 1.00 36.11 C ANISOU 601 CD2 LEU A 91 4402 4217 5101 273 1003 1107 C ATOM 602 N GLY A 92 178.158 44.259 514.833 1.00 34.09 N ANISOU 602 N GLY A 92 3598 4827 4527 283 1325 1663 N ATOM 603 CA GLY A 92 179.455 44.641 514.329 1.00 36.34 C ANISOU 603 CA GLY A 92 3724 5279 4805 189 1450 1903 C ATOM 604 C GLY A 92 180.581 43.762 514.838 1.00 36.01 C ANISOU 604 C GLY A 92 3506 5406 4773 118 1419 1811 C ATOM 605 O GLY A 92 180.408 42.955 515.756 1.00 33.99 O ANISOU 605 O GLY A 92 3279 5073 4562 105 1297 1564 O ATOM 606 N PRO A 93 181.769 43.914 514.246 1.00 36.16 N ANISOU 606 N PRO A 93 4515 4477 4745 -695 -263 253 N ATOM 607 CA PRO A 93 182.890 43.043 514.633 1.00 35.64 C ANISOU 607 CA PRO A 93 4439 4476 4626 -704 -192 144 C ATOM 608 C PRO A 93 183.490 43.382 515.987 1.00 33.53 C ANISOU 608 C PRO A 93 4070 4217 4455 -720 -94 88 C ATOM 609 O PRO A 93 183.983 42.476 516.671 1.00 32.54 O ANISOU 609 O PRO A 93 3891 4142 4331 -713 -79 13 O ATOM 610 CB PRO A 93 183.901 43.257 513.499 1.00 37.92 C ANISOU 610 CB PRO A 93 4839 4791 4776 -717 -117 153 C ATOM 611 CG PRO A 93 183.616 44.638 513.012 1.00 38.54 C ANISOU 611 CG PRO A 93 4955 4814 4874 -732 -97 246 C ATOM 612 CD PRO A 93 182.128 44.830 513.149 1.00 38.15 C ANISOU 612 CD PRO A 93 4872 4711 4911 -708 -225 319 C ATOM 613 N VAL A 94 183.473 44.653 516.394 1.00 38.92 N ANISOU 613 N VAL A 94 4740 4843 5206 -743 -32 122 N ATOM 614 CA VAL A 94 184.062 45.029 517.676 1.00 37.32 C ANISOU 614 CA VAL A 94 4479 4633 5068 -779 44 62 C ATOM 615 C VAL A 94 183.249 44.449 518.827 1.00 36.04 C ANISOU 615 C VAL A 94 4255 4452 4985 -737 6 32 C ATOM 616 O VAL A 94 183.800 43.846 519.756 1.00 34.83 O ANISOU 616 O VAL A 94 4054 4345 4836 -748 23 -42 O ATOM 617 CB VAL A 94 184.184 46.559 517.786 1.00 37.53 C ANISOU 617 CB VAL A 94 4553 4574 5134 -824 120 103 C ATOM 618 CG1 VAL A 94 184.691 46.952 519.164 1.00 36.16 C ANISOU 618 CG1 VAL A 94 4357 4373 5009 -878 174 34 C ATOM 619 CG2 VAL A 94 185.106 47.094 516.705 1.00 38.72 C ANISOU 619 CG2 VAL A 94 4755 4746 5211 -873 174 139 C ATOM 620 N VAL A 95 181.926 44.623 518.784 1.00 35.59 N ANISOU 620 N VAL A 95 4192 4330 5001 -683 -41 105 N ATOM 621 CA VAL A 95 181.073 44.073 519.833 1.00 34.46 C ANISOU 621 CA VAL A 95 3982 4163 4947 -633 -57 99 C ATOM 622 C VAL A 95 181.111 42.550 519.813 1.00 33.95 C ANISOU 622 C VAL A 95 3874 4174 4850 -623 -133 50 C ATOM 623 O VAL A 95 180.965 41.904 520.858 1.00 32.86 O ANISOU 623 O VAL A 95 3686 4042 4756 -599 -120 8 O ATOM 624 CB VAL A 95 179.636 44.608 519.684 1.00 34.94 C ANISOU 624 CB VAL A 95 4017 4142 5116 -570 -81 222 C ATOM 625 CG1 VAL A 95 178.763 44.142 520.843 1.00 34.07 C ANISOU 625 CG1 VAL A 95 3831 3998 5117 -509 -59 235 C ATOM 626 CG2 VAL A 95 179.645 46.126 519.598 1.00 35.68 C ANISOU 626 CG2 VAL A 95 4178 4145 5234 -567 12 277 C ATOM 627 N CYS A 96 181.315 41.951 518.637 1.00 31.24 N ANISOU 627 N CYS A 96 3575 3878 4419 -639 -205 54 N ATOM 628 CA CYS A 96 181.447 40.500 518.564 1.00 31.08 C ANISOU 628 CA CYS A 96 3551 3907 4350 -631 -263 -1 C ATOM 629 C CYS A 96 182.678 40.019 519.322 1.00 30.40 C ANISOU 629 C CYS A 96 3441 3883 4227 -634 -179 -93 C ATOM 630 O CYS A 96 182.617 39.022 520.051 1.00 29.51 O ANISOU 630 O CYS A 96 3287 3790 4138 -608 -190 -136 O ATOM 631 CB CYS A 96 181.508 40.048 517.106 1.00 32.84 C ANISOU 631 CB CYS A 96 3877 4146 4454 -648 -339 15 C ATOM 632 SG CYS A 96 182.130 38.366 516.901 1.00 33.33 S ANISOU 632 SG CYS A 96 3999 4252 4413 -636 -354 -75 S ATOM 633 N ASP A 97 183.806 40.715 519.163 1.00 40.70 N ANISOU 633 N ASP A 97 4761 5221 5484 -668 -98 -110 N ATOM 634 CA ASP A 97 185.019 40.320 519.870 1.00 39.94 C ANISOU 634 CA ASP A 97 4612 5195 5367 -678 -35 -171 C ATOM 635 C ASP A 97 184.879 40.541 521.371 1.00 38.28 C ANISOU 635 C ASP A 97 4345 4968 5231 -686 -21 -202 C ATOM 636 O ASP A 97 185.313 39.702 522.170 1.00 37.55 O ANISOU 636 O ASP A 97 4204 4927 5137 -666 -18 -245 O ATOM 637 CB ASP A 97 186.220 41.089 519.320 1.00 40.79 C ANISOU 637 CB ASP A 97 4727 5343 5429 -728 41 -156 C ATOM 638 CG ASP A 97 186.487 40.787 517.857 1.00 43.07 C ANISOU 638 CG ASP A 97 5096 5647 5620 -705 57 -127 C ATOM 639 OD1 ASP A 97 186.125 39.681 517.400 1.00 44.06 O ANISOU 639 OD1 ASP A 97 5274 5774 5691 -655 14 -145 O ATOM 640 OD2 ASP A 97 187.061 41.654 517.164 1.00 44.11 O ANISOU 640 OD2 ASP A 97 5259 5780 5722 -742 118 -85 O ATOM 641 N LEU A 98 184.272 41.661 521.774 1.00 31.93 N ANISOU 641 N LEU A 98 3565 4084 4482 -705 -4 -175 N ATOM 642 CA LEU A 98 184.077 41.926 523.196 1.00 31.10 C ANISOU 642 CA LEU A 98 3454 3939 4423 -706 25 -206 C ATOM 643 C LEU A 98 183.147 40.897 523.827 1.00 30.58 C ANISOU 643 C LEU A 98 3353 3862 4406 -632 -3 -206 C ATOM 644 O LEU A 98 183.363 40.473 524.968 1.00 30.08 O ANISOU 644 O LEU A 98 3274 3813 4341 -621 14 -250 O ATOM 645 CB LEU A 98 183.527 43.339 523.396 1.00 31.64 C ANISOU 645 CB LEU A 98 3592 3896 4534 -723 76 -170 C ATOM 646 CG LEU A 98 184.404 44.496 522.914 1.00 32.19 C ANISOU 646 CG LEU A 98 3711 3951 4568 -811 113 -167 C ATOM 647 CD1 LEU A 98 183.694 45.826 523.114 1.00 32.89 C ANISOU 647 CD1 LEU A 98 3892 3900 4703 -809 175 -126 C ATOM 648 CD2 LEU A 98 185.745 44.486 523.631 1.00 31.74 C ANISOU 648 CD2 LEU A 98 3633 3961 4467 -901 116 -231 C ATOM 649 N TRP A 99 182.105 40.485 523.101 1.00 25.64 N ANISOU 649 N TRP A 99 2713 3208 3822 -590 -55 -149 N ATOM 650 CA TRP A 99 181.181 39.488 523.632 1.00 25.18 C ANISOU 650 CA TRP A 99 2605 3133 3828 -535 -86 -133 C ATOM 651 C TRP A 99 181.850 38.126 523.763 1.00 24.75 C ANISOU 651 C TRP A 99 2532 3153 3718 -527 -113 -194 C ATOM 652 O TRP A 99 181.668 37.434 524.771 1.00 24.23 O ANISOU 652 O TRP A 99 2436 3087 3683 -491 -95 -213 O ATOM 653 CB TRP A 99 179.940 39.398 522.743 1.00 25.68 C ANISOU 653 CB TRP A 99 2646 3154 3959 -518 -163 -40 C ATOM 654 CG TRP A 99 179.077 38.209 523.031 1.00 25.24 C ANISOU 654 CG TRP A 99 2529 3090 3972 -489 -221 -14 C ATOM 655 CD1 TRP A 99 178.427 37.930 524.197 1.00 24.77 C ANISOU 655 CD1 TRP A 99 2414 2992 4005 -440 -168 8 C ATOM 656 CD2 TRP A 99 178.759 37.140 522.130 1.00 25.52 C ANISOU 656 CD2 TRP A 99 2571 3142 3985 -516 -338 -4 C ATOM 657 NE1 TRP A 99 177.729 36.752 524.081 1.00 24.55 N ANISOU 657 NE1 TRP A 99 2333 2962 4033 -439 -245 40 N ATOM 658 CE2 TRP A 99 177.917 36.247 522.822 1.00 24.98 C ANISOU 658 CE2 TRP A 99 2431 3044 4014 -494 -359 27 C ATOM 659 CE3 TRP A 99 179.108 36.851 520.807 1.00 26.52 C ANISOU 659 CE3 TRP A 99 2778 3293 4006 -561 -422 -19 C ATOM 660 CZ2 TRP A 99 177.418 35.085 522.236 1.00 25.19 C ANISOU 660 CZ2 TRP A 99 2461 3063 4046 -532 -477 41 C ATOM 661 CZ3 TRP A 99 178.612 35.697 520.227 1.00 26.87 C ANISOU 661 CZ3 TRP A 99 2852 3324 4034 -591 -537 -15 C ATOM 662 CH2 TRP A 99 177.775 34.829 520.941 1.00 26.12 C ANISOU 662 CH2 TRP A 99 2681 3197 4048 -585 -572 13 C ATOM 663 N LEU A 100 182.627 37.724 522.755 1.00 29.34 N ANISOU 663 N LEU A 100 3142 3790 4216 -548 -138 -217 N ATOM 664 CA LEU A 100 183.331 36.447 522.829 1.00 29.42 C ANISOU 664 CA LEU A 100 3147 3858 4172 -521 -137 -267 C ATOM 665 C LEU A 100 184.388 36.460 523.927 1.00 28.76 C ANISOU 665 C LEU A 100 3017 3837 4074 -519 -78 -307 C ATOM 666 O LEU A 100 184.547 35.473 524.654 1.00 28.51 O ANISOU 666 O LEU A 100 2957 3830 4044 -476 -73 -330 O ATOM 667 CB LEU A 100 183.967 36.120 521.478 1.00 30.98 C ANISOU 667 CB LEU A 100 3411 4085 4274 -528 -143 -273 C ATOM 668 CG LEU A 100 183.013 35.797 520.328 1.00 32.18 C ANISOU 668 CG LEU A 100 3644 4181 4403 -540 -233 -242 C ATOM 669 CD1 LEU A 100 183.754 35.838 519.004 1.00 34.22 C ANISOU 669 CD1 LEU A 100 4006 4459 4536 -548 -213 -247 C ATOM 670 CD2 LEU A 100 182.362 34.438 520.538 1.00 32.20 C ANISOU 670 CD2 LEU A 100 3660 4149 4426 -520 -294 -258 C ATOM 671 N ALA A 101 185.119 37.569 524.063 1.00 30.42 N ANISOU 671 N ALA A 101 3222 4070 4267 -573 -43 -309 N ATOM 672 CA ALA A 101 186.140 37.658 525.102 1.00 30.09 C ANISOU 672 CA ALA A 101 3134 4091 4207 -598 -21 -338 C ATOM 673 C ALA A 101 185.515 37.656 526.492 1.00 29.66 C ANISOU 673 C ALA A 101 3094 3992 4185 -581 -23 -355 C ATOM 674 O ALA A 101 186.006 36.973 527.398 1.00 29.68 O ANISOU 674 O ALA A 101 3065 4045 4165 -559 -28 -375 O ATOM 675 CB ALA A 101 186.993 38.909 524.897 1.00 30.36 C ANISOU 675 CB ALA A 101 3168 4144 4224 -689 -1 -329 C ATOM 676 N LEU A 102 184.431 38.413 526.677 1.00 33.92 N ANISOU 676 N LEU A 102 3686 4431 4772 -578 -5 -336 N ATOM 677 CA LEU A 102 183.746 38.423 527.965 1.00 34.23 C ANISOU 677 CA LEU A 102 3760 4409 4838 -541 27 -342 C ATOM 678 C LEU A 102 183.172 37.052 528.293 1.00 34.02 C ANISOU 678 C LEU A 102 3691 4391 4845 -464 17 -331 C ATOM 679 O LEU A 102 183.179 36.628 529.454 1.00 34.49 O ANISOU 679 O LEU A 102 3764 4450 4889 -431 41 -347 O ATOM 680 CB LEU A 102 182.638 39.476 527.959 1.00 34.79 C ANISOU 680 CB LEU A 102 3888 4361 4970 -527 78 -299 C ATOM 681 CG LEU A 102 181.807 39.593 529.237 1.00 35.76 C ANISOU 681 CG LEU A 102 4066 4396 5124 -467 152 -289 C ATOM 682 CD1 LEU A 102 182.644 40.170 530.368 1.00 36.72 C ANISOU 682 CD1 LEU A 102 4293 4511 5147 -520 175 -356 C ATOM 683 CD2 LEU A 102 180.563 40.432 528.998 1.00 36.35 C ANISOU 683 CD2 LEU A 102 4164 4355 5293 -417 220 -211 C ATOM 684 N ASP A 103 182.678 36.340 527.279 1.00 37.34 N ANISOU 684 N ASP A 103 4075 4811 5302 -441 -22 -302 N ATOM 685 CA ASP A 103 182.059 35.041 527.516 1.00 37.26 C ANISOU 685 CA ASP A 103 4036 4789 5334 -386 -37 -287 C ATOM 686 C ASP A 103 183.084 34.010 527.973 1.00 37.35 C ANISOU 686 C ASP A 103 4033 4877 5280 -360 -35 -330 C ATOM 687 O ASP A 103 182.803 33.202 528.866 1.00 37.55 O ANISOU 687 O ASP A 103 4051 4891 5326 -311 -16 -326 O ATOM 688 CB ASP A 103 181.350 34.568 526.249 1.00 37.30 C ANISOU 688 CB ASP A 103 4032 4765 5375 -397 -105 -251 C ATOM 689 CG ASP A 103 179.956 34.060 526.522 1.00 37.27 C ANISOU 689 CG ASP A 103 3988 4688 5485 -371 -123 -185 C ATOM 690 OD1 ASP A 103 179.584 33.962 527.710 1.00 37.31 O ANISOU 690 OD1 ASP A 103 3974 4665 5539 -326 -57 -170 O ATOM 691 OD2 ASP A 103 179.232 33.758 525.551 1.00 37.44 O ANISOU 691 OD2 ASP A 103 4001 4679 5547 -401 -206 -141 O ATOM 692 N TYR A 104 184.278 34.023 527.378 1.00 23.90 N ANISOU 692 N TYR A 104 2319 3252 3508 -384 -44 -355 N ATOM 693 CA TYR A 104 185.284 33.019 527.706 1.00 24.27 C ANISOU 693 CA TYR A 104 2334 3377 3509 -341 -33 -370 C ATOM 694 C TYR A 104 186.054 33.361 528.975 1.00 24.36 C ANISOU 694 C TYR A 104 2319 3450 3488 -355 -28 -378 C ATOM 695 O TYR A 104 186.468 32.452 529.702 1.00 24.75 O ANISOU 695 O TYR A 104 2343 3543 3519 -301 -25 -372 O ATOM 696 CB TYR A 104 186.246 32.840 526.532 1.00 24.93 C ANISOU 696 CB TYR A 104 2410 3520 3545 -343 -21 -370 C ATOM 697 CG TYR A 104 185.720 31.913 525.460 1.00 25.93 C ANISOU 697 CG TYR A 104 2601 3590 3661 -309 -29 -373 C ATOM 698 CD1 TYR A 104 184.641 32.278 524.665 1.00 25.93 C ANISOU 698 CD1 TYR A 104 2656 3512 3685 -350 -79 -364 C ATOM 699 CD2 TYR A 104 186.302 30.671 525.244 1.00 27.23 C ANISOU 699 CD2 TYR A 104 2784 3773 3789 -237 9 -379 C ATOM 700 CE1 TYR A 104 184.156 31.431 523.685 1.00 27.21 C ANISOU 700 CE1 TYR A 104 2901 3617 3821 -343 -116 -369 C ATOM 701 CE2 TYR A 104 185.825 29.818 524.267 1.00 28.94 C ANISOU 701 CE2 TYR A 104 3106 3915 3976 -219 -2 -394 C ATOM 702 CZ TYR A 104 184.752 30.202 523.491 1.00 28.88 C ANISOU 702 CZ TYR A 104 3162 3832 3979 -283 -77 -393 C ATOM 703 OH TYR A 104 184.274 29.355 522.517 1.00 30.50 O ANISOU 703 OH TYR A 104 3494 3958 4137 -289 -116 -410 O ATOM 704 N VAL A 105 186.254 34.649 529.262 1.00 22.11 N ANISOU 704 N VAL A 105 2054 3160 3186 -431 -37 -388 N ATOM 705 CA VAL A 105 186.937 35.034 530.493 1.00 22.73 C ANISOU 705 CA VAL A 105 2141 3282 3215 -470 -59 -401 C ATOM 706 C VAL A 105 186.058 34.740 531.703 1.00 23.38 C ANISOU 706 C VAL A 105 2293 3295 3294 -418 -34 -408 C ATOM 707 O VAL A 105 186.516 34.167 532.700 1.00 24.31 O ANISOU 707 O VAL A 105 2412 3462 3364 -393 -53 -406 O ATOM 708 CB VAL A 105 187.350 36.516 530.439 1.00 23.15 C ANISOU 708 CB VAL A 105 2231 3322 3243 -583 -76 -417 C ATOM 709 CG1 VAL A 105 187.756 37.007 531.819 1.00 24.18 C ANISOU 709 CG1 VAL A 105 2427 3456 3305 -643 -115 -441 C ATOM 710 CG2 VAL A 105 188.491 36.711 529.451 1.00 23.12 C ANISOU 710 CG2 VAL A 105 2137 3410 3240 -636 -93 -393 C ATOM 711 N VAL A 106 184.781 35.121 531.632 1.00 35.79 N ANISOU 711 N VAL A 106 3921 4755 4922 -395 15 -399 N ATOM 712 CA VAL A 106 183.869 34.885 532.748 1.00 37.04 C ANISOU 712 CA VAL A 106 4144 4836 5091 -332 72 -387 C ATOM 713 C VAL A 106 183.649 33.390 532.956 1.00 36.86 C ANISOU 713 C VAL A 106 4070 4835 5098 -250 77 -362 C ATOM 714 O VAL A 106 183.543 32.917 534.094 1.00 38.18 O ANISOU 714 O VAL A 106 4282 4993 5232 -201 108 -355 O ATOM 715 CB VAL A 106 182.544 35.636 532.515 1.00 37.14 C ANISOU 715 CB VAL A 106 4197 4728 5188 -312 141 -354 C ATOM 716 CG1 VAL A 106 181.497 35.211 533.529 1.00 38.41 C ANISOU 716 CG1 VAL A 106 4397 4807 5391 -226 228 -314 C ATOM 717 CG2 VAL A 106 182.771 37.140 532.588 1.00 37.78 C ANISOU 717 CG2 VAL A 106 4369 4761 5225 -381 159 -380 C ATOM 718 N SER A 107 183.590 32.621 531.866 1.00 32.13 N ANISOU 718 N SER A 107 3402 4255 4550 -236 51 -349 N ATOM 719 CA SER A 107 183.442 31.175 531.997 1.00 32.06 C ANISOU 719 CA SER A 107 3367 4248 4565 -167 58 -329 C ATOM 720 C SER A 107 184.703 30.539 532.566 1.00 32.58 C ANISOU 720 C SER A 107 3413 4416 4552 -137 40 -338 C ATOM 721 O SER A 107 184.623 29.604 533.371 1.00 33.12 O ANISOU 721 O SER A 107 3490 4480 4615 -70 64 -317 O ATOM 722 CB SER A 107 183.098 30.555 530.645 1.00 31.34 C ANISOU 722 CB SER A 107 3250 4132 4525 -173 28 -323 C ATOM 723 OG SER A 107 181.888 31.081 530.132 1.00 31.01 O ANISOU 723 OG SER A 107 3207 4008 4568 -203 20 -291 O ATOM 724 N ASN A 108 185.876 31.025 532.155 1.00 30.66 N ANISOU 724 N ASN A 108 3129 4264 4256 -184 1 -353 N ATOM 725 CA ASN A 108 187.121 30.482 532.686 1.00 31.30 C ANISOU 725 CA ASN A 108 3155 4455 4281 -156 -25 -333 C ATOM 726 C ASN A 108 187.270 30.810 534.165 1.00 32.84 C ANISOU 726 C ASN A 108 3399 4668 4409 -170 -53 -331 C ATOM 727 O ASN A 108 187.798 30.000 534.937 1.00 33.76 O ANISOU 727 O ASN A 108 3495 4844 4488 -113 -68 -297 O ATOM 728 CB ASN A 108 188.310 31.019 531.889 1.00 31.00 C ANISOU 728 CB ASN A 108 3039 4513 4226 -211 -55 -325 C ATOM 729 CG ASN A 108 189.576 30.216 532.117 1.00 31.59 C ANISOU 729 CG ASN A 108 3014 4706 4280 -155 -66 -270 C ATOM 730 OD1 ASN A 108 189.890 29.299 531.357 1.00 31.47 O ANISOU 730 OD1 ASN A 108 2965 4704 4290 -74 -12 -245 O ATOM 731 ND2 ASN A 108 190.310 30.556 533.170 1.00 32.54 N ANISOU 731 ND2 ASN A 108 3100 4910 4354 -197 -136 -244 N ATOM 732 N ALA A 109 186.807 31.993 534.578 1.00 30.98 N ANISOU 732 N ALA A 109 3248 4374 4147 -241 -55 -363 N ATOM 733 CA ALA A 109 186.836 32.347 535.992 1.00 33.25 C ANISOU 733 CA ALA A 109 3639 4650 4344 -257 -72 -373 C ATOM 734 C ALA A 109 185.913 31.453 536.808 1.00 34.52 C ANISOU 734 C ALA A 109 3862 4741 4514 -151 3 -348 C ATOM 735 O ALA A 109 186.218 31.146 537.966 1.00 36.76 O ANISOU 735 O ALA A 109 4209 5050 4708 -125 -16 -335 O ATOM 736 CB ALA A 109 186.459 33.818 536.177 1.00 33.86 C ANISOU 736 CB ALA A 109 3833 4645 4387 -346 -62 -417 C ATOM 737 N ARG A 110 184.789 31.027 536.225 1.00 50.79 N ANISOU 737 N ARG A 110 5903 6712 6682 -96 80 -332 N ATOM 738 CA ARG A 110 183.885 30.117 536.923 1.00 50.88 C ANISOU 738 CA ARG A 110 5949 6653 6729 -3 159 -292 C ATOM 739 C ARG A 110 184.559 28.780 537.196 1.00 50.75 C ANISOU 739 C ARG A 110 5885 6707 6690 65 136 -260 C ATOM 740 O ARG A 110 184.478 28.243 538.307 1.00 52.06 O ANISOU 740 O ARG A 110 6112 6864 6804 126 167 -230 O ATOM 741 CB ARG A 110 182.612 29.911 536.103 1.00 48.95 C ANISOU 741 CB ARG A 110 5661 6311 6627 15 217 -264 C ATOM 742 CG ARG A 110 181.843 28.659 536.497 1.00 48.24 C ANISOU 742 CG ARG A 110 5559 6162 6608 95 279 -208 C ATOM 743 CD ARG A 110 180.945 28.171 535.372 1.00 46.71 C ANISOU 743 CD ARG A 110 5289 5904 6554 78 273 -179 C ATOM 744 NE ARG A 110 180.018 29.207 534.930 1.00 46.56 N ANISOU 744 NE ARG A 110 5253 5822 6614 39 293 -158 N ATOM 745 CZ ARG A 110 178.886 29.507 535.556 1.00 46.77 C ANISOU 745 CZ ARG A 110 5288 5760 6721 77 390 -92 C ATOM 746 NH1 ARG A 110 178.542 28.853 536.657 1.00 46.99 N ANISOU 746 NH1 ARG A 110 5353 5750 6751 149 478 -48 N ATOM 747 NH2 ARG A 110 178.101 30.469 535.089 1.00 46.75 N ANISOU 747 NH2 ARG A 110 5256 5704 6801 54 411 -57 N ATOM 748 N VAL A 111 185.228 28.225 536.184 1.00 30.98 N ANISOU 748 N VAL A 111 3285 4265 4220 65 95 -260 N ATOM 749 CA VAL A 111 185.851 26.912 536.326 1.00 30.87 C ANISOU 749 CA VAL A 111 3230 4301 4198 150 97 -220 C ATOM 750 C VAL A 111 186.928 26.948 537.401 1.00 32.82 C ANISOU 750 C VAL A 111 3477 4658 4337 162 38 -191 C ATOM 751 O VAL A 111 186.992 26.073 538.273 1.00 33.73 O ANISOU 751 O VAL A 111 3619 4779 4419 244 57 -144 O ATOM 752 CB VAL A 111 186.414 26.440 534.975 1.00 29.53 C ANISOU 752 CB VAL A 111 2986 4163 4072 157 88 -225 C ATOM 753 CG1 VAL A 111 187.189 25.148 535.149 1.00 29.82 C ANISOU 753 CG1 VAL A 111 2988 4246 4095 261 110 -175 C ATOM 754 CG2 VAL A 111 185.287 26.258 533.971 1.00 28.39 C ANISOU 754 CG2 VAL A 111 2868 3903 4016 135 120 -248 C ATOM 755 N MET A 112 187.789 27.968 537.361 1.00 31.51 N ANISOU 755 N MET A 112 3280 4578 4113 72 -46 -210 N ATOM 756 CA MET A 112 188.816 28.098 538.386 1.00 33.57 C ANISOU 756 CA MET A 112 3538 4950 4269 52 -140 -174 C ATOM 757 C MET A 112 188.233 28.489 539.737 1.00 36.49 C ANISOU 757 C MET A 112 4072 5257 4534 40 -139 -191 C ATOM 758 O MET A 112 188.868 28.241 540.766 1.00 38.40 O ANISOU 758 O MET A 112 4347 5570 4672 52 -211 -150 O ATOM 759 CB MET A 112 189.876 29.106 537.943 1.00 33.12 C ANISOU 759 CB MET A 112 3399 4994 4192 -68 -241 -181 C ATOM 760 CG MET A 112 190.643 28.660 536.709 1.00 31.23 C ANISOU 760 CG MET A 112 2998 4829 4040 -37 -224 -142 C ATOM 761 SD MET A 112 192.277 29.404 536.569 0.53 31.38 S ANISOU 761 SD MET A 112 2860 5017 4045 -144 -348 -83 S ATOM 762 CE MET A 112 191.846 31.134 536.450 1.00 31.16 C ANISOU 762 CE MET A 112 2940 4918 3983 -323 -392 -177 C ATOM 763 N ASN A 113 187.040 29.089 539.758 1.00 38.84 N ANISOU 763 N ASN A 113 4480 5424 4855 26 -52 -239 N ATOM 764 CA ASN A 113 186.346 29.306 541.023 1.00 41.24 C ANISOU 764 CA ASN A 113 4961 5643 5065 53 2 -243 C ATOM 765 C ASN A 113 185.905 27.981 541.632 1.00 40.62 C ANISOU 765 C ASN A 113 4895 5536 5003 183 79 -180 C ATOM 766 O ASN A 113 186.044 27.768 542.842 1.00 42.57 O ANISOU 766 O ASN A 113 5259 5791 5126 220 72 -152 O ATOM 767 CB ASN A 113 185.146 30.230 540.812 1.00 39.85 C ANISOU 767 CB ASN A 113 4876 5326 4939 32 109 -284 C ATOM 768 CG ASN A 113 184.598 30.792 542.112 1.00 40.85 C ANISOU 768 CG ASN A 113 5221 5358 4941 49 180 -296 C ATOM 769 OD1 ASN A 113 184.856 30.267 543.196 1.00 42.22 O ANISOU 769 OD1 ASN A 113 5489 5553 4999 95 168 -268 O ATOM 770 ND2 ASN A 113 183.828 31.868 542.006 1.00 40.00 N ANISOU 770 ND2 ASN A 113 5210 5137 4851 22 265 -330 N ATOM 771 N LEU A 114 185.370 27.076 540.806 1.00 37.25 N ANISOU 771 N LEU A 114 4367 5069 4718 247 150 -154 N ATOM 772 CA LEU A 114 185.015 25.748 541.294 1.00 36.56 C ANISOU 772 CA LEU A 114 4285 4945 4659 360 222 -89 C ATOM 773 C LEU A 114 186.245 24.975 541.746 1.00 37.92 C ANISOU 773 C LEU A 114 4415 5241 4751 410 139 -37 C ATOM 774 O LEU A 114 186.164 24.170 542.681 1.00 38.84 O ANISOU 774 O LEU A 114 4594 5345 4818 499 177 22 O ATOM 775 CB LEU A 114 184.268 24.972 540.209 1.00 33.61 C ANISOU 775 CB LEU A 114 3826 4495 4451 387 288 -79 C ATOM 776 CG LEU A 114 182.976 25.606 539.695 1.00 32.04 C ANISOU 776 CG LEU A 114 3632 4181 4359 342 356 -98 C ATOM 777 CD1 LEU A 114 182.366 24.756 538.592 1.00 29.75 C ANISOU 777 CD1 LEU A 114 3260 3828 4217 343 374 -83 C ATOM 778 CD2 LEU A 114 181.989 25.809 540.833 1.00 32.43 C ANISOU 778 CD2 LEU A 114 3790 4137 4396 389 471 -58 C ATOM 779 N LEU A 115 187.389 25.200 541.095 1.00 35.23 N ANISOU 779 N LEU A 115 3959 5021 4406 363 35 -42 N ATOM 780 CA LEU A 115 188.630 24.582 541.548 1.00 36.35 C ANISOU 780 CA LEU A 115 4031 5296 4486 412 -51 33 C ATOM 781 C LEU A 115 189.048 25.126 542.909 1.00 39.99 C ANISOU 781 C LEU A 115 4599 5815 4779 370 -151 51 C ATOM 782 O LEU A 115 189.537 24.375 543.760 1.00 41.09 O ANISOU 782 O LEU A 115 4750 6015 4847 447 -188 133 O ATOM 783 CB LEU A 115 189.735 24.804 540.516 1.00 34.81 C ANISOU 783 CB LEU A 115 3670 5216 4342 370 -123 43 C ATOM 784 CG LEU A 115 189.576 24.102 539.165 1.00 31.99 C ANISOU 784 CG LEU A 115 3231 4810 4114 428 -29 36 C ATOM 785 CD1 LEU A 115 190.651 24.561 538.192 1.00 31.14 C ANISOU 785 CD1 LEU A 115 2982 4809 4039 382 -80 46 C ATOM 786 CD2 LEU A 115 189.623 22.593 539.335 1.00 31.48 C ANISOU 786 CD2 LEU A 115 3161 4716 4082 578 48 109 C ATOM 787 N ILE A 116 188.861 26.429 543.132 1.00 29.54 N ANISOU 787 N ILE A 116 3376 4467 3382 247 -198 -22 N ATOM 788 CA ILE A 116 189.194 27.018 544.427 1.00 30.82 C ANISOU 788 CA ILE A 116 3696 4657 3356 188 -298 -22 C ATOM 789 C ILE A 116 188.325 26.412 545.522 1.00 31.94 C ANISOU 789 C ILE A 116 4016 4700 3420 296 -188 5 C ATOM 790 O ILE A 116 188.817 26.040 546.594 1.00 32.77 O ANISOU 790 O ILE A 116 4204 4863 3383 327 -263 63 O ATOM 791 CB ILE A 116 189.054 28.550 544.374 1.00 30.39 C ANISOU 791 CB ILE A 116 3754 4554 3239 36 -342 -118 C ATOM 792 CG1 ILE A 116 190.152 29.158 543.498 1.00 29.50 C ANISOU 792 CG1 ILE A 116 3468 4561 3178 -86 -478 -122 C ATOM 793 CG2 ILE A 116 189.102 29.141 545.773 1.00 31.72 C ANISOU 793 CG2 ILE A 116 4169 4694 3188 -20 -410 -139 C ATOM 794 CD1 ILE A 116 190.023 30.654 543.305 1.00 29.23 C ANISOU 794 CD1 ILE A 116 3538 4465 3102 -241 -512 -215 C ATOM 795 N ILE A 117 187.020 26.293 545.262 1.00 28.82 N ANISOU 795 N ILE A 117 3672 4156 3121 356 -8 -23 N ATOM 796 CA ILE A 117 186.111 25.705 546.243 1.00 28.96 C ANISOU 796 CA ILE A 117 3842 4069 3093 465 129 19 C ATOM 797 C ILE A 117 186.492 24.257 546.524 1.00 29.49 C ANISOU 797 C ILE A 117 3836 4189 3179 584 132 118 C ATOM 798 O ILE A 117 186.431 23.794 547.670 1.00 30.42 O ANISOU 798 O ILE A 117 4090 4294 3173 657 157 176 O ATOM 799 CB ILE A 117 184.654 25.820 545.757 1.00 27.76 C ANISOU 799 CB ILE A 117 3699 3758 3089 498 318 -1 C ATOM 800 CG1 ILE A 117 184.290 27.281 545.490 1.00 27.57 C ANISOU 800 CG1 ILE A 117 3752 3676 3048 399 327 -84 C ATOM 801 CG2 ILE A 117 183.700 25.210 546.773 1.00 28.47 C ANISOU 801 CG2 ILE A 117 3928 3737 3152 613 483 64 C ATOM 802 CD1 ILE A 117 182.900 27.470 544.925 1.00 26.74 C ANISOU 802 CD1 ILE A 117 3618 3432 3111 432 497 -79 C ATOM 803 N SER A 118 186.896 23.523 545.486 1.00 31.09 N ANISOU 803 N SER A 118 3843 4442 3527 613 118 143 N ATOM 804 CA SER A 118 187.225 22.113 545.664 1.00 30.86 C ANISOU 804 CA SER A 118 3755 4440 3532 739 146 239 C ATOM 805 C SER A 118 188.526 21.938 546.439 1.00 32.73 C ANISOU 805 C SER A 118 3976 4832 3627 757 -10 315 C ATOM 806 O SER A 118 188.610 21.089 547.334 1.00 33.40 O ANISOU 806 O SER A 118 4127 4922 3641 862 10 404 O ATOM 807 CB SER A 118 187.309 21.421 544.305 1.00 28.29 C ANISOU 807 CB SER A 118 3262 4102 3383 767 186 237 C ATOM 808 OG SER A 118 186.080 21.522 543.609 1.00 26.60 O ANISOU 808 OG SER A 118 3062 3748 3297 738 300 181 O ATOM 809 N PHE A 119 189.551 22.728 546.109 1.00 33.14 N ANISOU 809 N PHE A 119 3932 5016 3644 651 -171 297 N ATOM 810 CA PHE A 119 190.821 22.617 546.821 1.00 33.75 C ANISOU 810 CA PHE A 119 3962 5258 3604 647 -349 391 C ATOM 811 C PHE A 119 190.710 23.154 548.243 1.00 35.24 C ANISOU 811 C PHE A 119 4381 5440 3569 598 -431 387 C ATOM 812 O PHE A 119 191.255 22.556 549.178 1.00 36.36 O ANISOU 812 O PHE A 119 4561 5658 3596 661 -514 491 O ATOM 813 CB PHE A 119 191.925 23.348 546.055 1.00 33.24 C ANISOU 813 CB PHE A 119 3713 5332 3584 530 -499 388 C ATOM 814 CG PHE A 119 192.518 22.545 544.931 1.00 32.08 C ANISOU 814 CG PHE A 119 3337 5243 3610 620 -446 452 C ATOM 815 CD1 PHE A 119 193.388 21.500 545.194 1.00 33.34 C ANISOU 815 CD1 PHE A 119 3376 5505 3787 748 -476 599 C ATOM 816 CD2 PHE A 119 192.212 22.841 543.613 1.00 30.60 C ANISOU 816 CD2 PHE A 119 3070 4998 3557 585 -359 373 C ATOM 817 CE1 PHE A 119 193.937 20.760 544.162 1.00 33.15 C ANISOU 817 CE1 PHE A 119 3168 5514 3914 851 -395 662 C ATOM 818 CE2 PHE A 119 192.759 22.106 542.577 1.00 30.40 C ANISOU 818 CE2 PHE A 119 2878 5008 3666 675 -292 427 C ATOM 819 CZ PHE A 119 193.622 21.064 542.852 1.00 31.70 C ANISOU 819 CZ PHE A 119 2934 5263 3848 813 -299 570 C ATOM 820 N ASP A 120 190.012 24.279 548.425 1.00 48.92 N ANISOU 820 N ASP A 120 6286 7074 5227 491 -404 273 N ATOM 821 CA ASP A 120 189.838 24.838 549.763 1.00 49.91 C ANISOU 821 CA ASP A 120 6687 7161 5115 448 -456 254 C ATOM 822 C ASP A 120 189.160 23.842 550.694 1.00 50.33 C ANISOU 822 C ASP A 120 6887 7134 5104 607 -316 326 C ATOM 823 O ASP A 120 189.539 23.714 551.864 1.00 51.27 O ANISOU 823 O ASP A 120 7169 7294 5016 621 -411 382 O ATOM 824 CB ASP A 120 189.034 26.136 549.688 1.00 49.60 C ANISOU 824 CB ASP A 120 6823 6988 5033 343 -383 122 C ATOM 825 CG ASP A 120 188.592 26.630 551.049 1.00 50.18 C ANISOU 825 CG ASP A 120 7240 6967 4859 333 -361 94 C ATOM 826 OD1 ASP A 120 189.430 27.200 551.778 1.00 50.95 O ANISOU 826 OD1 ASP A 120 7467 7141 4752 217 -567 87 O ATOM 827 OD2 ASP A 120 187.403 26.450 551.388 1.00 49.60 O ANISOU 827 OD2 ASP A 120 7314 6739 4795 439 -136 85 O ATOM 828 N ARG A 121 188.153 23.126 550.190 1.00 42.94 N ANISOU 828 N ARG A 121 5899 6078 4338 720 -98 332 N ATOM 829 CA ARG A 121 187.509 22.091 550.989 1.00 43.05 C ANISOU 829 CA ARG A 121 6025 6009 4324 872 50 416 C ATOM 830 C ARG A 121 188.427 20.893 551.196 1.00 43.58 C ANISOU 830 C ARG A 121 5973 6195 4392 974 -35 546 C ATOM 831 O ARG A 121 188.335 20.212 552.224 1.00 44.09 O ANISOU 831 O ARG A 121 6172 6241 4338 1076 2 635 O ATOM 832 CB ARG A 121 186.203 21.658 550.320 1.00 41.88 C ANISOU 832 CB ARG A 121 5828 5701 4383 938 286 398 C ATOM 833 CG ARG A 121 185.413 20.609 551.083 1.00 41.69 C ANISOU 833 CG ARG A 121 5908 5569 4362 1082 465 492 C ATOM 834 CD ARG A 121 184.937 21.134 552.425 1.00 41.91 C ANISOU 834 CD ARG A 121 6226 5526 4172 1104 534 496 C ATOM 835 NE ARG A 121 184.114 20.154 553.127 1.00 41.61 N ANISOU 835 NE ARG A 121 6285 5375 4151 1246 735 597 N ATOM 836 CZ ARG A 121 183.572 20.351 554.324 1.00 41.74 C ANISOU 836 CZ ARG A 121 6565 5305 3989 1305 853 629 C ATOM 837 NH1 ARG A 121 182.837 19.401 554.884 1.00 41.45 N ANISOU 837 NH1 ARG A 121 6590 5165 3992 1436 1049 735 N ATOM 838 NH2 ARG A 121 183.765 21.498 554.961 1.00 42.15 N ANISOU 838 NH2 ARG A 121 6837 5362 3818 1232 786 556 N ATOM 839 N TYR A 122 189.324 20.630 550.241 1.00 44.03 N ANISOU 839 N TYR A 122 5783 6367 4578 959 -134 571 N ATOM 840 CA TYR A 122 190.216 19.481 550.362 1.00 44.04 C ANISOU 840 CA TYR A 122 5654 6475 4604 1078 -191 712 C ATOM 841 C TYR A 122 191.235 19.680 551.477 1.00 45.17 C ANISOU 841 C TYR A 122 5860 6770 4533 1051 -409 801 C ATOM 842 O TYR A 122 191.580 18.726 552.185 1.00 45.64 O ANISOU 842 O TYR A 122 5937 6871 4532 1178 -422 935 O ATOM 843 CB TYR A 122 190.918 19.219 549.030 1.00 42.73 C ANISOU 843 CB TYR A 122 5222 6385 4630 1081 -215 721 C ATOM 844 CG TYR A 122 191.995 18.162 549.107 1.00 42.41 C ANISOU 844 CG TYR A 122 5029 6465 4619 1211 -273 882 C ATOM 845 CD1 TYR A 122 191.670 16.815 549.192 1.00 41.79 C ANISOU 845 CD1 TYR A 122 4966 6300 4613 1385 -118 967 C ATOM 846 CD2 TYR A 122 193.339 18.512 549.091 1.00 42.58 C ANISOU 846 CD2 TYR A 122 4883 6683 4611 1161 -477 963 C ATOM 847 CE1 TYR A 122 192.654 15.845 549.263 1.00 41.50 C ANISOU 847 CE1 TYR A 122 4798 6363 4609 1525 -151 1126 C ATOM 848 CE2 TYR A 122 194.329 17.550 549.161 1.00 42.37 C ANISOU 848 CE2 TYR A 122 4695 6772 4631 1299 -518 1136 C ATOM 849 CZ TYR A 122 193.981 16.219 549.247 1.00 41.89 C ANISOU 849 CZ TYR A 122 4668 6616 4634 1491 -347 1215 C ATOM 850 OH TYR A 122 194.965 15.260 549.318 1.00 42.05 O ANISOU 850 OH TYR A 122 4534 6738 4704 1648 -369 1399 O ATOM 851 N PHE A 123 191.727 20.906 551.652 1.00 42.77 N ANISOU 851 N PHE A 123 5598 6544 4108 879 -593 735 N ATOM 852 CA PHE A 123 192.712 21.172 552.691 1.00 43.96 C ANISOU 852 CA PHE A 123 5816 6840 4045 815 -843 818 C ATOM 853 C PHE A 123 192.088 21.371 554.067 1.00 45.08 C ANISOU 853 C PHE A 123 6310 6889 3928 821 -825 800 C ATOM 854 O PHE A 123 192.818 21.369 555.064 1.00 46.53 O ANISOU 854 O PHE A 123 6592 7181 3906 792 -1027 887 O ATOM 855 CB PHE A 123 193.556 22.394 552.317 1.00 43.90 C ANISOU 855 CB PHE A 123 5717 6949 4013 604 -1067 762 C ATOM 856 CG PHE A 123 194.363 22.208 551.063 1.00 42.65 C ANISOU 856 CG PHE A 123 5211 6905 4087 603 -1098 811 C ATOM 857 CD1 PHE A 123 195.311 21.202 550.979 1.00 42.97 C ANISOU 857 CD1 PHE A 123 5023 7089 4215 726 -1157 989 C ATOM 858 CD2 PHE A 123 194.179 23.041 549.972 1.00 41.52 C ANISOU 858 CD2 PHE A 123 4980 6723 4072 494 -1053 692 C ATOM 859 CE1 PHE A 123 196.055 21.025 549.828 1.00 42.01 C ANISOU 859 CE1 PHE A 123 4598 7062 4303 746 -1152 1044 C ATOM 860 CE2 PHE A 123 194.921 22.870 548.819 1.00 40.27 C ANISOU 860 CE2 PHE A 123 4525 6663 4112 503 -1060 742 C ATOM 861 CZ PHE A 123 195.861 21.861 548.747 1.00 40.64 C ANISOU 861 CZ PHE A 123 4353 6845 4243 632 -1102 917 C ATOM 862 N CYS A 124 190.767 21.542 554.148 1.00 57.44 N ANISOU 862 N CYS A 124 8068 8259 5496 860 -587 702 N ATOM 863 CA CYS A 124 190.096 21.574 555.441 1.00 58.01 C ANISOU 863 CA CYS A 124 8482 8224 5335 909 -508 705 C ATOM 864 C CYS A 124 189.901 20.183 556.027 1.00 58.18 C ANISOU 864 C CYS A 124 8522 8226 5357 1107 -392 849 C ATOM 865 O CYS A 124 189.766 20.054 557.249 1.00 58.93 O ANISOU 865 O CYS A 124 8883 8292 5217 1154 -396 900 O ATOM 866 CB CYS A 124 188.740 22.273 555.324 1.00 57.05 C ANISOU 866 CB CYS A 124 8540 7898 5237 896 -268 575 C ATOM 867 SG CYS A 124 188.826 24.074 555.217 1.00 56.91 S ANISOU 867 SG CYS A 124 8677 7851 5093 675 -385 408 S ATOM 868 N VAL A 125 189.883 19.146 555.189 1.00 67.94 N ANISOU 868 N VAL A 125 9508 9465 6840 1221 -284 915 N ATOM 869 CA VAL A 125 189.710 17.780 555.667 1.00 67.99 C ANISOU 869 CA VAL A 125 9528 9437 6869 1410 -162 1055 C ATOM 870 C VAL A 125 191.021 17.000 555.711 1.00 68.52 C ANISOU 870 C VAL A 125 9405 9687 6943 1478 -347 1212 C ATOM 871 O VAL A 125 191.078 15.948 556.365 1.00 68.87 O ANISOU 871 O VAL A 125 9499 9724 6943 1632 -294 1351 O ATOM 872 CB VAL A 125 188.678 17.021 554.806 1.00 66.74 C ANISOU 872 CB VAL A 125 9267 9119 6974 1503 110 1035 C ATOM 873 CG1 VAL A 125 187.384 17.814 554.705 1.00 66.12 C ANISOU 873 CG1 VAL A 125 9327 8873 6922 1438 288 908 C ATOM 874 CG2 VAL A 125 189.246 16.732 553.427 1.00 65.96 C ANISOU 874 CG2 VAL A 125 8865 9086 7110 1488 70 1023 C ATOM 875 N THR A 126 192.069 17.478 555.038 1.00 49.20 N ANISOU 875 N THR A 126 6734 7400 4560 1377 -550 1209 N ATOM 876 CA THR A 126 193.360 16.807 555.040 1.00 49.50 C ANISOU 876 CA THR A 126 6555 7624 4629 1447 -721 1382 C ATOM 877 C THR A 126 194.437 17.572 555.795 1.00 50.83 C ANISOU 877 C THR A 126 6743 7981 4589 1309 -1051 1440 C ATOM 878 O THR A 126 195.478 16.985 556.113 1.00 51.37 O ANISOU 878 O THR A 126 6662 8214 4643 1377 -1215 1623 O ATOM 879 CB THR A 126 193.837 16.557 553.601 1.00 48.13 C ANISOU 879 CB THR A 126 6061 7496 4729 1466 -678 1382 C ATOM 880 OG1 THR A 126 193.956 17.805 552.909 1.00 47.76 O ANISOU 880 OG1 THR A 126 5949 7483 4714 1273 -770 1243 O ATOM 881 CG2 THR A 126 192.853 15.664 552.864 1.00 46.86 C ANISOU 881 CG2 THR A 126 5895 7147 4763 1596 -382 1340 C ATOM 882 N LYS A 127 194.226 18.857 556.081 1.00 55.89 N ANISOU 882 N LYS A 127 7564 8600 5072 1113 -1158 1299 N ATOM 883 CA LYS A 127 195.164 19.653 556.875 1.00 57.27 C ANISOU 883 CA LYS A 127 7814 8927 5018 945 -1492 1337 C ATOM 884 C LYS A 127 194.389 20.482 557.895 1.00 58.31 C ANISOU 884 C LYS A 127 8372 8925 4859 847 -1485 1209 C ATOM 885 O LYS A 127 194.389 21.716 557.848 1.00 58.55 O ANISOU 885 O LYS A 127 8520 8933 4795 649 -1591 1072 O ATOM 886 CB LYS A 127 196.015 20.546 555.971 1.00 56.62 C ANISOU 886 CB LYS A 127 7478 8973 5061 760 -1675 1297 C ATOM 887 CG LYS A 127 196.826 19.793 554.926 1.00 55.41 C ANISOU 887 CG LYS A 127 6914 8949 5192 865 -1659 1429 C ATOM 888 CD LYS A 127 197.538 20.746 553.980 1.00 54.50 C ANISOU 888 CD LYS A 127 6565 8936 5208 683 -1794 1382 C ATOM 889 CE LYS A 127 198.316 19.987 552.916 1.00 53.23 C ANISOU 889 CE LYS A 127 6014 8886 5324 811 -1734 1519 C ATOM 890 NZ LYS A 127 198.911 20.901 551.901 1.00 52.27 N ANISOU 890 NZ LYS A 127 5669 8845 5347 648 -1816 1472 N ATOM 891 N PRO A 128 193.714 19.827 558.847 1.00 63.00 N ANISOU 891 N PRO A 128 9224 9414 5300 992 -1343 1256 N ATOM 892 CA PRO A 128 192.895 20.583 559.808 1.00 63.36 C ANISOU 892 CA PRO A 128 9703 9306 5065 930 -1280 1138 C ATOM 893 C PRO A 128 193.711 21.356 560.829 1.00 64.82 C ANISOU 893 C PRO A 128 10118 9594 4917 753 -1619 1150 C ATOM 894 O PRO A 128 193.195 22.323 561.403 1.00 64.50 O ANISOU 894 O PRO A 128 10437 9425 4645 642 -1604 1011 O ATOM 895 CB PRO A 128 192.047 19.495 560.488 1.00 63.10 C ANISOU 895 CB PRO A 128 9838 9147 4989 1156 -1022 1224 C ATOM 896 CG PRO A 128 192.256 18.242 559.670 1.00 62.40 C ANISOU 896 CG PRO A 128 9395 9112 5202 1321 -917 1347 C ATOM 897 CD PRO A 128 193.620 18.378 559.084 1.00 62.83 C ANISOU 897 CD PRO A 128 9130 9389 5353 1227 -1204 1419 C ATOM 898 N LEU A 129 194.958 20.963 561.076 1.00 73.28 N ANISOU 898 N LEU A 129 11004 10885 5955 723 -1923 1317 N ATOM 899 CA LEU A 129 195.805 21.627 562.057 1.00 74.21 C ANISOU 899 CA LEU A 129 11323 11118 5756 534 -2295 1352 C ATOM 900 C LEU A 129 196.599 22.787 561.472 1.00 73.48 C ANISOU 900 C LEU A 129 11080 11128 5710 262 -2562 1273 C ATOM 901 O LEU A 129 197.380 23.410 562.199 1.00 74.02 O ANISOU 901 O LEU A 129 11292 11299 5534 62 -2911 1301 O ATOM 902 CB LEU A 129 196.772 20.617 562.686 1.00 75.66 C ANISOU 902 CB LEU A 129 11366 11499 5880 632 -2517 1606 C ATOM 903 CG LEU A 129 196.161 19.355 563.294 1.00 76.47 C ANISOU 903 CG LEU A 129 11591 11522 5943 907 -2280 1723 C ATOM 904 CD1 LEU A 129 197.250 18.453 563.854 1.00 77.76 C ANISOU 904 CD1 LEU A 129 11588 11900 6057 992 -2535 1990 C ATOM 905 CD2 LEU A 129 195.149 19.712 564.371 1.00 76.33 C ANISOU 905 CD2 LEU A 129 12105 11301 5594 918 -2133 1612 C ATOM 906 N THR A 130 196.421 23.095 560.188 1.00 80.02 N ANISOU 906 N THR A 130 11637 11929 6838 240 -2417 1181 N ATOM 907 CA THR A 130 197.235 24.115 559.539 1.00 79.15 C ANISOU 907 CA THR A 130 11339 11926 6809 -6 -2656 1132 C ATOM 908 C THR A 130 196.400 25.057 558.681 1.00 77.82 C ANISOU 908 C THR A 130 11232 11581 6755 -83 -2439 911 C ATOM 909 O THR A 130 196.512 26.280 558.805 1.00 77.38 O ANISOU 909 O THR A 130 11363 11479 6561 -313 -2583 783 O ATOM 910 CB THR A 130 198.318 23.459 558.677 1.00 78.74 C ANISOU 910 CB THR A 130 10766 12096 7055 42 -2768 1316 C ATOM 911 OG1 THR A 130 199.218 22.722 559.513 1.00 79.85 O ANISOU 911 OG1 THR A 130 10835 12421 7085 91 -3016 1543 O ATOM 912 CG2 THR A 130 199.096 24.513 557.900 1.00 77.80 C ANISOU 912 CG2 THR A 130 10427 12076 7056 -204 -2970 1272 C ATOM 913 N TYR A 131 195.565 24.500 557.810 1.00 58.45 N ANISOU 913 N TYR A 131 8632 9024 4552 100 -2103 872 N ATOM 914 CA TYR A 131 194.853 25.288 556.810 1.00 57.15 C ANISOU 914 CA TYR A 131 8442 8722 4549 42 -1910 698 C ATOM 915 C TYR A 131 193.759 26.190 557.385 1.00 56.80 C ANISOU 915 C TYR A 131 8834 8450 4297 -9 -1758 522 C ATOM 916 O TYR A 131 193.652 27.346 556.955 1.00 55.89 O ANISOU 916 O TYR A 131 8787 8265 4184 -174 -1779 383 O ATOM 917 CB TYR A 131 194.259 24.368 555.739 1.00 56.63 C ANISOU 917 CB TYR A 131 8109 8611 4797 247 -1617 720 C ATOM 918 CG TYR A 131 193.639 25.118 554.584 1.00 55.32 C ANISOU 918 CG TYR A 131 7864 8335 4819 185 -1452 568 C ATOM 919 CD1 TYR A 131 194.422 25.879 553.726 1.00 54.19 C ANISOU 919 CD1 TYR A 131 7503 8294 4794 18 -1608 541 C ATOM 920 CD2 TYR A 131 192.272 25.065 554.348 1.00 54.88 C ANISOU 920 CD2 TYR A 131 7944 8078 4831 294 -1142 470 C ATOM 921 CE1 TYR A 131 193.862 26.569 552.669 1.00 53.01 C ANISOU 921 CE1 TYR A 131 7293 8044 4805 -34 -1461 411 C ATOM 922 CE2 TYR A 131 191.703 25.749 553.292 1.00 53.73 C ANISOU 922 CE2 TYR A 131 7720 7839 4855 240 -1009 349 C ATOM 923 CZ TYR A 131 192.502 26.500 552.456 1.00 52.96 C ANISOU 923 CZ TYR A 131 7426 7842 4853 79 -1169 316 C ATOM 924 OH TYR A 131 191.941 27.185 551.403 1.00 51.82 O ANISOU 924 OH TYR A 131 7215 7605 4868 30 -1039 204 O ATOM 925 N PRO A 132 192.917 25.725 558.321 1.00 63.15 N ANISOU 925 N PRO A 132 9943 9123 4928 138 -1581 527 N ATOM 926 CA PRO A 132 191.832 26.599 558.805 1.00 62.44 C ANISOU 926 CA PRO A 132 10260 8801 4662 116 -1386 371 C ATOM 927 C PRO A 132 192.302 27.923 559.385 1.00 62.52 C ANISOU 927 C PRO A 132 10577 8783 4393 -131 -1623 262 C ATOM 928 O PRO A 132 191.599 28.930 559.236 1.00 61.62 O ANISOU 928 O PRO A 132 10682 8491 4240 -195 -1476 109 O ATOM 929 CB PRO A 132 191.139 25.736 559.867 1.00 62.93 C ANISOU 929 CB PRO A 132 10580 8771 4559 316 -1206 446 C ATOM 930 CG PRO A 132 191.382 24.351 559.422 1.00 63.32 C ANISOU 930 CG PRO A 132 10277 8941 4842 487 -1162 603 C ATOM 931 CD PRO A 132 192.774 24.358 558.861 1.00 63.99 C ANISOU 931 CD PRO A 132 10025 9260 5030 358 -1484 678 C ATOM 932 N VAL A 133 193.465 27.964 560.039 1.00 71.30 N ANISOU 932 N VAL A 133 11719 10060 5314 -277 -1989 342 N ATOM 933 CA VAL A 133 193.928 29.230 560.600 1.00 71.37 C ANISOU 933 CA VAL A 133 12044 10029 5045 -544 -2240 234 C ATOM 934 C VAL A 133 194.414 30.163 559.496 1.00 70.39 C ANISOU 934 C VAL A 133 11671 9949 5126 -744 -2351 154 C ATOM 935 O VAL A 133 194.397 31.389 559.659 1.00 70.25 O ANISOU 935 O VAL A 133 11885 9808 4997 -930 -2398 10 O ATOM 936 CB VAL A 133 195.014 28.987 561.667 1.00 73.20 C ANISOU 936 CB VAL A 133 12295 10419 5099 -636 -2563 346 C ATOM 937 CG1 VAL A 133 196.322 28.549 561.025 1.00 73.40 C ANISOU 937 CG1 VAL A 133 11824 10723 5343 -712 -2855 506 C ATOM 938 CG2 VAL A 133 195.218 30.233 562.519 1.00 75.21 C ANISOU 938 CG2 VAL A 133 12863 10551 5163 -843 -2663 204 C ATOM 939 N LYS A 134 194.840 29.612 558.359 1.00 77.36 N ANISOU 939 N LYS A 134 12053 10984 6355 -688 -2342 244 N ATOM 940 CA LYS A 134 195.263 30.404 557.211 1.00 76.32 C ANISOU 940 CA LYS A 134 11658 10895 6445 -849 -2407 185 C ATOM 941 C LYS A 134 194.104 30.770 556.296 1.00 75.12 C ANISOU 941 C LYS A 134 11503 10556 6482 -749 -2052 51 C ATOM 942 O LYS A 134 194.331 31.320 555.212 1.00 74.15 O ANISOU 942 O LYS A 134 11144 10460 6570 -843 -2055 9 O ATOM 943 CB LYS A 134 196.323 29.644 556.408 1.00 76.30 C ANISOU 943 CB LYS A 134 11129 11144 6715 -827 -2555 359 C ATOM 944 CG LYS A 134 197.395 28.981 557.252 1.00 77.80 C ANISOU 944 CG LYS A 134 11241 11541 6778 -854 -2866 547 C ATOM 945 CD LYS A 134 198.300 28.101 556.402 1.00 77.54 C ANISOU 945 CD LYS A 134 10676 11735 7051 -765 -2927 738 C ATOM 946 CE LYS A 134 199.084 28.924 555.392 1.00 76.09 C ANISOU 946 CE LYS A 134 10198 11647 7066 -966 -3064 731 C ATOM 947 NZ LYS A 134 200.019 28.083 554.594 1.00 75.71 N ANISOU 947 NZ LYS A 134 9643 11817 7308 -866 -3105 934 N ATOM 948 N ARG A 135 192.876 30.482 556.715 1.00 63.39 N ANISOU 948 N ARG A 135 10268 8887 4929 -563 -1750 -1 N ATOM 949 CA ARG A 135 191.687 30.595 555.878 1.00 62.38 C ANISOU 949 CA ARG A 135 10093 8599 5011 -430 -1402 -83 C ATOM 950 C ARG A 135 190.915 31.844 556.297 1.00 61.87 C ANISOU 950 C ARG A 135 10447 8302 4760 -508 -1277 -242 C ATOM 951 O ARG A 135 189.978 31.784 557.092 1.00 61.98 O ANISOU 951 O ARG A 135 10788 8148 4616 -380 -1060 -271 O ATOM 952 CB ARG A 135 190.848 29.315 556.019 1.00 62.65 C ANISOU 952 CB ARG A 135 10068 8594 5141 -160 -1141 4 C ATOM 953 CG ARG A 135 189.751 29.138 554.996 1.00 61.64 C ANISOU 953 CG ARG A 135 9774 8353 5294 -23 -827 -33 C ATOM 954 CD ARG A 135 189.225 27.712 555.030 1.00 61.86 C ANISOU 954 CD ARG A 135 9666 8388 5450 204 -645 82 C ATOM 955 NE ARG A 135 188.122 27.520 554.098 1.00 60.76 N ANISOU 955 NE ARG A 135 9382 8133 5573 315 -366 55 N ATOM 956 CZ ARG A 135 186.841 27.591 554.439 1.00 59.98 C ANISOU 956 CZ ARG A 135 9475 7846 5467 428 -89 31 C ATOM 957 NH1 ARG A 135 186.501 27.847 555.695 1.00 60.24 N ANISOU 957 NH1 ARG A 135 9879 7775 5234 462 -25 23 N ATOM 958 NH2 ARG A 135 185.902 27.404 553.524 1.00 58.86 N ANISOU 958 NH2 ARG A 135 9158 7621 5586 508 125 26 N ATOM 959 N THR A 136 191.324 32.985 555.753 1.00 65.53 N ANISOU 959 N THR A 136 10904 8748 5245 -713 -1400 -336 N ATOM 960 CA THR A 136 190.699 34.270 556.034 1.00 65.05 C ANISOU 960 CA THR A 136 11234 8458 5022 -802 -1289 -489 C ATOM 961 C THR A 136 190.022 34.810 554.780 1.00 63.82 C ANISOU 961 C THR A 136 10892 8212 5144 -767 -1071 -553 C ATOM 962 O THR A 136 190.184 34.283 553.676 1.00 63.36 O ANISOU 962 O THR A 136 10416 8281 5378 -718 -1056 -491 O ATOM 963 CB THR A 136 191.729 35.283 556.553 1.00 65.51 C ANISOU 963 CB THR A 136 11514 8538 4837 -1099 -1628 -554 C ATOM 964 OG1 THR A 136 192.661 35.593 555.509 1.00 65.03 O ANISOU 964 OG1 THR A 136 11075 8636 4996 -1268 -1833 -529 O ATOM 965 CG2 THR A 136 192.482 34.712 557.749 1.00 66.87 C ANISOU 965 CG2 THR A 136 11818 8826 4762 -1141 -1880 -467 C ATOM 966 N THR A 137 189.249 35.883 554.968 1.00 73.00 N ANISOU 966 N THR A 137 12393 9145 6201 -788 -896 -673 N ATOM 967 CA THR A 137 188.592 36.525 553.837 1.00 71.89 C ANISOU 967 CA THR A 137 12109 8905 6300 -763 -700 -727 C ATOM 968 C THR A 137 189.580 37.264 552.946 1.00 71.48 C ANISOU 968 C THR A 137 11847 8956 6356 -993 -937 -761 C ATOM 969 O THR A 137 189.295 37.460 551.760 1.00 70.58 O ANISOU 969 O THR A 137 11471 8845 6500 -965 -829 -764 O ATOM 970 CB THR A 137 187.511 37.490 554.324 1.00 71.56 C ANISOU 970 CB THR A 137 12493 8580 6117 -704 -432 -828 C ATOM 971 OG1 THR A 137 188.109 38.529 555.109 1.00 72.14 O ANISOU 971 OG1 THR A 137 12969 8558 5881 -917 -613 -933 O ATOM 972 CG2 THR A 137 186.476 36.755 555.164 1.00 71.68 C ANISOU 972 CG2 THR A 137 12694 8488 6052 -459 -158 -773 C ATOM 973 N LYS A 138 190.727 37.680 553.487 1.00 67.86 N ANISOU 973 N LYS A 138 11497 8581 5705 -1226 -1261 -777 N ATOM 974 CA LYS A 138 191.748 38.309 552.657 1.00 67.41 C ANISOU 974 CA LYS A 138 11202 8640 5771 -1455 -1495 -782 C ATOM 975 C LYS A 138 192.407 37.292 551.733 1.00 67.11 C ANISOU 975 C LYS A 138 10634 8854 6009 -1397 -1581 -646 C ATOM 976 O LYS A 138 192.666 37.587 550.559 1.00 66.19 O ANISOU 976 O LYS A 138 10232 8796 6123 -1448 -1577 -639 O ATOM 977 CB LYS A 138 192.791 38.996 553.539 1.00 68.22 C ANISOU 977 CB LYS A 138 11527 8761 5630 -1719 -1817 -809 C ATOM 978 CG LYS A 138 193.959 39.593 552.773 1.00 68.06 C ANISOU 978 CG LYS A 138 11190 8874 5798 -1938 -2045 -770 C ATOM 979 CD LYS A 138 194.876 40.375 553.699 1.00 70.68 C ANISOU 979 CD LYS A 138 11675 9179 6002 -2134 -2266 -770 C ATOM 980 CE LYS A 138 196.134 40.836 552.980 1.00 71.32 C ANISOU 980 CE LYS A 138 11406 9410 6283 -2335 -2488 -698 C ATOM 981 NZ LYS A 138 196.959 39.684 552.522 1.00 70.52 N ANISOU 981 NZ LYS A 138 10849 9595 6351 -2290 -2640 -537 N ATOM 982 N MET A 139 192.685 36.090 552.243 1.00 56.97 N ANISOU 982 N MET A 139 9231 7714 4700 -1280 -1646 -534 N ATOM 983 CA MET A 139 193.212 35.032 551.388 1.00 56.74 C ANISOU 983 CA MET A 139 8732 7896 4931 -1182 -1677 -401 C ATOM 984 C MET A 139 192.185 34.609 550.347 1.00 55.94 C ANISOU 984 C MET A 139 8452 7724 5080 -977 -1366 -411 C ATOM 985 O MET A 139 192.540 34.318 549.198 1.00 55.23 O ANISOU 985 O MET A 139 8011 7743 5229 -960 -1361 -360 O ATOM 986 CB MET A 139 193.638 33.832 552.233 1.00 57.86 C ANISOU 986 CB MET A 139 8827 8178 4979 -1080 -1786 -274 C ATOM 987 CG MET A 139 194.281 32.712 551.430 1.00 57.72 C ANISOU 987 CG MET A 139 8348 8371 5213 -972 -1818 -125 C ATOM 988 SD MET A 139 193.872 31.070 552.054 0.35 58.92 S ANISOU 988 SD MET A 139 8470 8565 5353 -696 -1692 -7 S ATOM 989 CE MET A 139 192.115 31.006 551.708 1.00 58.51 C ANISOU 989 CE MET A 139 8574 8270 5386 -502 -1287 -113 C ATOM 990 N ALA A 140 190.907 34.569 550.731 1.00 41.82 N ANISOU 990 N ALA A 140 6904 5749 3238 -823 -1106 -468 N ATOM 991 CA ALA A 140 189.858 34.219 549.780 1.00 40.21 C ANISOU 991 CA ALA A 140 6538 5470 3271 -649 -831 -468 C ATOM 992 C ALA A 140 189.725 35.277 548.693 1.00 39.06 C ANISOU 992 C ALA A 140 6318 5260 3264 -750 -788 -542 C ATOM 993 O ALA A 140 189.461 34.951 547.530 1.00 38.35 O ANISOU 993 O ALA A 140 5955 5205 3411 -676 -689 -515 O ATOM 994 CB ALA A 140 188.529 34.028 550.511 1.00 40.36 C ANISOU 994 CB ALA A 140 6824 5302 3207 -475 -566 -489 C ATOM 995 N GLY A 141 189.910 36.549 549.050 1.00 44.62 N ANISOU 995 N GLY A 141 7282 5860 3812 -921 -863 -636 N ATOM 996 CA GLY A 141 189.826 37.603 548.054 1.00 43.59 C ANISOU 996 CA GLY A 141 7099 5660 3805 -1022 -824 -700 C ATOM 997 C GLY A 141 190.988 37.584 547.081 1.00 42.96 C ANISOU 997 C GLY A 141 6673 5770 3880 -1154 -1019 -647 C ATOM 998 O GLY A 141 190.822 37.890 545.897 1.00 41.90 O ANISOU 998 O GLY A 141 6352 5631 3938 -1150 -936 -653 O ATOM 999 N MET A 142 192.181 37.222 547.562 1.00 48.66 N ANISOU 999 N MET A 142 7302 6664 4522 -1268 -1277 -581 N ATOM 1000 CA MET A 142 193.347 37.182 546.684 1.00 47.95 C ANISOU 1000 CA MET A 142 6864 6763 4592 -1385 -1449 -503 C ATOM 1001 C MET A 142 193.275 36.007 545.715 1.00 47.35 C ANISOU 1001 C MET A 142 6436 6807 4749 -1193 -1330 -409 C ATOM 1002 O MET A 142 193.655 36.138 544.546 1.00 46.17 O ANISOU 1002 O MET A 142 6035 6725 4784 -1220 -1317 -379 O ATOM 1003 CB MET A 142 194.632 37.120 547.510 1.00 48.80 C ANISOU 1003 CB MET A 142 6951 7026 4564 -1558 -1764 -431 C ATOM 1004 CG MET A 142 194.970 38.419 548.221 1.00 49.20 C ANISOU 1004 CG MET A 142 7319 6972 4404 -1819 -1941 -524 C ATOM 1005 SD MET A 142 196.653 38.462 548.870 0.31 50.07 S ANISOU 1005 SD MET A 142 7304 7297 4422 -2079 -2364 -410 S ATOM 1006 CE MET A 142 196.577 37.185 550.123 1.00 51.28 C ANISOU 1006 CE MET A 142 7555 7534 4394 -1918 -2425 -329 C ATOM 1007 N MET A 143 192.795 34.851 546.179 1.00 40.20 N ANISOU 1007 N MET A 143 5529 5916 3830 -1000 -1236 -360 N ATOM 1008 CA MET A 143 192.671 33.700 545.289 1.00 39.73 C ANISOU 1008 CA MET A 143 5181 5939 3975 -820 -1115 -281 C ATOM 1009 C MET A 143 191.624 33.945 544.209 1.00 38.68 C ANISOU 1009 C MET A 143 5022 5679 3996 -740 -894 -345 C ATOM 1010 O MET A 143 191.782 33.493 543.069 1.00 37.56 O ANISOU 1010 O MET A 143 4634 5603 4034 -682 -840 -303 O ATOM 1011 CB MET A 143 192.329 32.445 546.092 1.00 41.02 C ANISOU 1011 CB MET A 143 5384 6120 4082 -643 -1059 -217 C ATOM 1012 CG MET A 143 193.428 31.999 547.043 1.00 41.99 C ANISOU 1012 CG MET A 143 5480 6398 4074 -694 -1287 -119 C ATOM 1013 SD MET A 143 193.032 30.449 547.877 0.48 43.40 S ANISOU 1013 SD MET A 143 5690 6594 4205 -464 -1200 -26 S ATOM 1014 CE MET A 143 192.970 29.324 546.485 1.00 42.24 C ANISOU 1014 CE MET A 143 5201 6504 4343 -289 -1038 44 C ATOM 1015 N ILE A 144 190.550 34.658 544.551 1.00 51.72 N ANISOU 1015 N ILE A 144 6932 7144 5576 -731 -761 -436 N ATOM 1016 CA ILE A 144 189.529 34.983 543.561 1.00 50.78 C ANISOU 1016 CA ILE A 144 6782 6906 5605 -663 -569 -479 C ATOM 1017 C ILE A 144 190.042 36.039 542.590 1.00 49.39 C ANISOU 1017 C ILE A 144 6521 6742 5501 -813 -632 -513 C ATOM 1018 O ILE A 144 189.813 35.951 541.377 1.00 48.15 O ANISOU 1018 O ILE A 144 6187 6595 5511 -770 -552 -500 O ATOM 1019 CB ILE A 144 188.235 35.433 544.262 1.00 51.31 C ANISOU 1019 CB ILE A 144 7135 6773 5589 -589 -392 -537 C ATOM 1020 CG1 ILE A 144 187.603 34.258 545.009 1.00 52.34 C ANISOU 1020 CG1 ILE A 144 7304 6888 5695 -416 -287 -482 C ATOM 1021 CG2 ILE A 144 187.253 36.028 543.262 1.00 50.27 C ANISOU 1021 CG2 ILE A 144 6972 6520 5608 -549 -224 -566 C ATOM 1022 CD1 ILE A 144 186.375 34.627 545.803 1.00 52.40 C ANISOU 1022 CD1 ILE A 144 7585 6704 5621 -326 -91 -513 C ATOM 1023 N ALA A 145 190.743 37.053 543.104 1.00 40.69 N ANISOU 1023 N ALA A 145 5559 5633 4269 -1000 -779 -555 N ATOM 1024 CA ALA A 145 191.297 38.083 542.231 1.00 39.56 C ANISOU 1024 CA ALA A 145 5338 5496 4195 -1159 -842 -579 C ATOM 1025 C ALA A 145 192.309 37.493 541.259 1.00 38.56 C ANISOU 1025 C ALA A 145 4865 5563 4224 -1171 -926 -485 C ATOM 1026 O ALA A 145 192.334 37.859 540.078 1.00 37.26 O ANISOU 1026 O ALA A 145 4564 5398 4194 -1188 -866 -482 O ATOM 1027 CB ALA A 145 191.935 39.193 543.066 1.00 40.19 C ANISOU 1027 CB ALA A 145 5643 5528 4097 -1380 -1009 -635 C ATOM 1028 N ALA A 146 193.150 36.571 541.736 1.00 45.69 N ANISOU 1028 N ALA A 146 5628 6626 5106 -1151 -1052 -397 N ATOM 1029 CA ALA A 146 194.111 35.921 540.852 1.00 44.79 C ANISOU 1029 CA ALA A 146 5184 6689 5144 -1127 -1098 -288 C ATOM 1030 C ALA A 146 193.415 35.074 539.796 1.00 43.68 C ANISOU 1030 C ALA A 146 4916 6527 5152 -933 -901 -275 C ATOM 1031 O ALA A 146 193.930 34.925 538.682 1.00 42.41 O ANISOU 1031 O ALA A 146 4546 6444 5124 -921 -871 -223 O ATOM 1032 CB ALA A 146 195.080 35.065 541.668 1.00 45.85 C ANISOU 1032 CB ALA A 146 5202 6991 5229 -1119 -1259 -177 C ATOM 1033 N ALA A 147 192.247 34.518 540.122 1.00 38.75 N ANISOU 1033 N ALA A 147 4427 5792 4504 -788 -766 -317 N ATOM 1034 CA ALA A 147 191.517 33.711 539.151 1.00 37.71 C ANISOU 1034 CA ALA A 147 4197 5626 4506 -629 -604 -307 C ATOM 1035 C ALA A 147 190.964 34.570 538.022 1.00 36.19 C ANISOU 1035 C ALA A 147 4011 5342 4398 -671 -516 -362 C ATOM 1036 O ALA A 147 191.028 34.180 536.850 1.00 34.66 O ANISOU 1036 O ALA A 147 3671 5181 4319 -617 -456 -335 O ATOM 1037 CB ALA A 147 190.393 32.944 539.847 1.00 38.99 C ANISOU 1037 CB ALA A 147 4492 5690 4634 -487 -493 -322 C ATOM 1038 N TRP A 148 190.420 35.743 538.351 1.00 40.91 N ANISOU 1038 N TRP A 148 4796 5816 4932 -761 -502 -435 N ATOM 1039 CA TRP A 148 189.904 36.628 537.313 1.00 39.62 C ANISOU 1039 CA TRP A 148 4644 5564 4848 -797 -423 -473 C ATOM 1040 C TRP A 148 191.026 37.222 536.471 1.00 38.54 C ANISOU 1040 C TRP A 148 4363 5522 4759 -925 -506 -446 C ATOM 1041 O TRP A 148 190.848 37.432 535.266 1.00 37.17 O ANISOU 1041 O TRP A 148 4109 5333 4682 -910 -437 -440 O ATOM 1042 CB TRP A 148 189.061 37.740 537.937 1.00 40.50 C ANISOU 1042 CB TRP A 148 5004 5505 4879 -843 -366 -545 C ATOM 1043 CG TRP A 148 187.712 37.277 538.400 1.00 41.39 C ANISOU 1043 CG TRP A 148 5228 5501 4998 -693 -222 -552 C ATOM 1044 CD1 TRP A 148 187.374 36.850 539.652 1.00 43.04 C ANISOU 1044 CD1 TRP A 148 5581 5670 5101 -631 -199 -556 C ATOM 1045 CD2 TRP A 148 186.520 37.186 537.610 1.00 40.72 C ANISOU 1045 CD2 TRP A 148 5108 5325 5038 -588 -82 -537 C ATOM 1046 NE1 TRP A 148 186.044 36.503 539.691 1.00 43.40 N ANISOU 1046 NE1 TRP A 148 5672 5605 5214 -491 -35 -540 N ATOM 1047 CE2 TRP A 148 185.498 36.701 538.449 1.00 42.08 C ANISOU 1047 CE2 TRP A 148 5385 5407 5194 -469 27 -524 C ATOM 1048 CE3 TRP A 148 186.218 37.471 536.275 1.00 39.04 C ANISOU 1048 CE3 TRP A 148 4786 5101 4948 -588 -46 -523 C ATOM 1049 CZ2 TRP A 148 184.196 36.494 537.997 1.00 41.81 C ANISOU 1049 CZ2 TRP A 148 5321 5280 5286 -359 163 -487 C ATOM 1050 CZ3 TRP A 148 184.926 37.266 535.828 1.00 38.81 C ANISOU 1050 CZ3 TRP A 148 4745 4980 5023 -482 70 -493 C ATOM 1051 CH2 TRP A 148 183.931 36.781 536.686 1.00 40.28 C ANISOU 1051 CH2 TRP A 148 5007 5084 5212 -374 169 -470 C ATOM 1052 N VAL A 149 192.181 37.497 537.077 1.00 41.38 N ANISOU 1052 N VAL A 149 4687 5980 5055 -1056 -659 -418 N ATOM 1053 CA VAL A 149 193.297 38.044 536.313 1.00 40.72 C ANISOU 1053 CA VAL A 149 4439 5994 5040 -1186 -734 -368 C ATOM 1054 C VAL A 149 193.870 36.988 535.376 1.00 39.87 C ANISOU 1054 C VAL A 149 4079 6021 5050 -1071 -688 -274 C ATOM 1055 O VAL A 149 194.146 37.267 534.204 1.00 38.95 O ANISOU 1055 O VAL A 149 3852 5923 5023 -1083 -628 -247 O ATOM 1056 CB VAL A 149 194.369 38.613 537.261 1.00 41.90 C ANISOU 1056 CB VAL A 149 4605 6215 5100 -1377 -932 -345 C ATOM 1057 CG1 VAL A 149 195.610 39.013 536.474 1.00 41.49 C ANISOU 1057 CG1 VAL A 149 4326 6288 5152 -1505 -1009 -258 C ATOM 1058 CG2 VAL A 149 193.819 39.808 538.019 1.00 42.64 C ANISOU 1058 CG2 VAL A 149 4998 6140 5064 -1505 -959 -452 C ATOM 1059 N LEU A 150 194.051 35.759 535.870 1.00 40.70 N ANISOU 1059 N LEU A 150 4108 6209 5147 -948 -699 -221 N ATOM 1060 CA LEU A 150 194.546 34.687 535.012 1.00 40.06 C ANISOU 1060 CA LEU A 150 3823 6229 5167 -815 -626 -134 C ATOM 1061 C LEU A 150 193.570 34.386 533.883 1.00 38.75 C ANISOU 1061 C LEU A 150 3701 5961 5061 -700 -465 -182 C ATOM 1062 O LEU A 150 193.984 34.109 532.752 1.00 38.11 O ANISOU 1062 O LEU A 150 3501 5923 5056 -652 -391 -137 O ATOM 1063 CB LEU A 150 194.808 33.427 535.836 1.00 40.94 C ANISOU 1063 CB LEU A 150 3880 6421 5253 -694 -657 -70 C ATOM 1064 CG LEU A 150 196.152 33.339 536.559 1.00 42.01 C ANISOU 1064 CG LEU A 150 3862 6724 5377 -769 -819 45 C ATOM 1065 CD1 LEU A 150 196.246 32.038 537.339 1.00 42.88 C ANISOU 1065 CD1 LEU A 150 3939 6895 5457 -620 -828 112 C ATOM 1066 CD2 LEU A 150 197.302 33.458 535.570 1.00 41.62 C ANISOU 1066 CD2 LEU A 150 3564 6798 5451 -799 -809 155 C ATOM 1067 N SER A 151 192.267 34.431 534.171 1.00 30.78 N ANISOU 1067 N SER A 151 2866 4814 4016 -656 -409 -264 N ATOM 1068 CA SER A 151 191.276 34.166 533.135 1.00 29.57 C ANISOU 1068 CA SER A 151 2749 4565 3922 -568 -289 -298 C ATOM 1069 C SER A 151 191.318 35.231 532.048 1.00 28.74 C ANISOU 1069 C SER A 151 2640 4428 3854 -655 -265 -314 C ATOM 1070 O SER A 151 191.175 34.921 530.859 1.00 27.98 O ANISOU 1070 O SER A 151 2503 4321 3807 -598 -192 -302 O ATOM 1071 CB SER A 151 189.882 34.082 533.755 1.00 29.84 C ANISOU 1071 CB SER A 151 2940 4466 3931 -515 -242 -354 C ATOM 1072 OG SER A 151 189.821 33.059 534.733 1.00 30.89 O ANISOU 1072 OG SER A 151 3085 4623 4029 -428 -250 -331 O ATOM 1073 N PHE A 152 191.520 36.492 532.435 1.00 39.00 N ANISOU 1073 N PHE A 152 4003 5699 5118 -797 -324 -341 N ATOM 1074 CA PHE A 152 191.607 37.565 531.450 1.00 38.44 C ANISOU 1074 CA PHE A 152 3934 5589 5082 -886 -297 -347 C ATOM 1075 C PHE A 152 192.833 37.392 530.559 1.00 38.45 C ANISOU 1075 C PHE A 152 3754 5717 5139 -905 -294 -268 C ATOM 1076 O PHE A 152 192.738 37.479 529.331 1.00 37.99 O ANISOU 1076 O PHE A 152 3672 5641 5121 -873 -213 -253 O ATOM 1077 CB PHE A 152 191.637 38.922 532.156 1.00 39.11 C ANISOU 1077 CB PHE A 152 4146 5602 5112 -1041 -360 -392 C ATOM 1078 CG PHE A 152 191.684 40.098 531.218 1.00 38.72 C ANISOU 1078 CG PHE A 152 4119 5493 5099 -1135 -326 -395 C ATOM 1079 CD1 PHE A 152 190.515 40.676 530.753 1.00 38.25 C ANISOU 1079 CD1 PHE A 152 4187 5293 5053 -1095 -240 -434 C ATOM 1080 CD2 PHE A 152 192.897 40.631 530.811 1.00 39.04 C ANISOU 1080 CD2 PHE A 152 4042 5620 5170 -1262 -377 -342 C ATOM 1081 CE1 PHE A 152 190.554 41.759 529.894 1.00 38.09 C ANISOU 1081 CE1 PHE A 152 4195 5214 5063 -1173 -205 -427 C ATOM 1082 CE2 PHE A 152 192.942 41.713 529.951 1.00 38.91 C ANISOU 1082 CE2 PHE A 152 4055 5542 5188 -1349 -335 -338 C ATOM 1083 CZ PHE A 152 191.769 42.277 529.493 1.00 38.43 C ANISOU 1083 CZ PHE A 152 4140 5335 5127 -1301 -249 -384 C ATOM 1084 N ILE A 153 193.995 37.136 531.166 1.00 38.26 N ANISOU 1084 N ILE A 153 3600 5822 5116 -953 -379 -202 N ATOM 1085 CA ILE A 153 195.234 37.016 530.400 1.00 38.63 C ANISOU 1085 CA ILE A 153 3446 5997 5236 -967 -361 -97 C ATOM 1086 C ILE A 153 195.183 35.826 529.448 1.00 38.42 C ANISOU 1086 C ILE A 153 3356 5995 5248 -783 -229 -59 C ATOM 1087 O ILE A 153 195.745 35.877 528.347 1.00 38.72 O ANISOU 1087 O ILE A 153 3307 6069 5334 -761 -140 0 O ATOM 1088 CB ILE A 153 196.437 36.923 531.362 1.00 39.67 C ANISOU 1088 CB ILE A 153 3429 6270 5374 -1053 -497 -10 C ATOM 1089 CG1 ILE A 153 196.542 38.196 532.204 1.00 40.13 C ANISOU 1089 CG1 ILE A 153 3588 6283 5375 -1268 -640 -57 C ATOM 1090 CG2 ILE A 153 197.731 36.685 530.598 1.00 40.21 C ANISOU 1090 CG2 ILE A 153 3250 6481 5548 -1042 -457 132 C ATOM 1091 CD1 ILE A 153 197.714 38.200 533.159 1.00 41.24 C ANISOU 1091 CD1 ILE A 153 3595 6563 5512 -1391 -817 32 C ATOM 1092 N LEU A 154 194.501 34.747 529.840 1.00 41.01 N ANISOU 1092 N LEU A 154 3748 6288 5546 -650 -204 -92 N ATOM 1093 CA LEU A 154 194.475 33.550 529.004 1.00 41.06 C ANISOU 1093 CA LEU A 154 3729 6299 5575 -483 -85 -63 C ATOM 1094 C LEU A 154 193.607 33.744 527.766 1.00 40.63 C ANISOU 1094 C LEU A 154 3796 6130 5510 -457 3 -122 C ATOM 1095 O LEU A 154 193.969 33.293 526.673 1.00 41.26 O ANISOU 1095 O LEU A 154 3856 6221 5600 -378 107 -85 O ATOM 1096 CB LEU A 154 193.983 32.349 529.812 1.00 41.04 C ANISOU 1096 CB LEU A 154 3770 6277 5546 -365 -90 -78 C ATOM 1097 CG LEU A 154 194.946 31.747 530.837 1.00 41.86 C ANISOU 1097 CG LEU A 154 3740 6507 5657 -334 -155 11 C ATOM 1098 CD1 LEU A 154 194.306 30.554 531.532 1.00 41.90 C ANISOU 1098 CD1 LEU A 154 3820 6466 5632 -206 -138 -8 C ATOM 1099 CD2 LEU A 154 196.259 31.348 530.180 1.00 42.52 C ANISOU 1099 CD2 LEU A 154 3631 6713 5810 -271 -88 139 C ATOM 1100 N TRP A 155 192.465 34.413 527.909 1.00 32.10 N ANISOU 1100 N TRP A 155 2852 4939 4406 -516 -33 -203 N ATOM 1101 CA TRP A 155 191.463 34.466 526.850 1.00 31.80 C ANISOU 1101 CA TRP A 155 2931 4793 4359 -484 21 -248 C ATOM 1102 C TRP A 155 191.328 35.822 526.177 1.00 31.66 C ANISOU 1102 C TRP A 155 2953 4732 4345 -589 21 -256 C ATOM 1103 O TRP A 155 191.172 35.877 524.955 1.00 32.19 O ANISOU 1103 O TRP A 155 3064 4767 4400 -565 78 -248 O ATOM 1104 CB TRP A 155 190.096 34.044 527.402 1.00 31.11 C ANISOU 1104 CB TRP A 155 2950 4603 4266 -443 -5 -305 C ATOM 1105 CG TRP A 155 189.982 32.573 527.645 1.00 31.42 C ANISOU 1105 CG TRP A 155 2988 4646 4303 -325 20 -299 C ATOM 1106 CD1 TRP A 155 189.944 31.938 528.853 1.00 31.39 C ANISOU 1106 CD1 TRP A 155 2968 4662 4298 -284 -7 -295 C ATOM 1107 CD2 TRP A 155 189.900 31.548 526.650 1.00 32.20 C ANISOU 1107 CD2 TRP A 155 3128 4715 4391 -233 85 -295 C ATOM 1108 NE1 TRP A 155 189.838 30.579 528.670 1.00 31.78 N ANISOU 1108 NE1 TRP A 155 3032 4694 4350 -170 40 -284 N ATOM 1109 CE2 TRP A 155 189.810 30.315 527.326 1.00 32.34 C ANISOU 1109 CE2 TRP A 155 3147 4727 4412 -141 97 -289 C ATOM 1110 CE3 TRP A 155 189.892 31.553 525.251 1.00 33.20 C ANISOU 1110 CE3 TRP A 155 3318 4806 4490 -222 135 -298 C ATOM 1111 CZ2 TRP A 155 189.713 29.101 526.651 1.00 33.29 C ANISOU 1111 CZ2 TRP A 155 3334 4798 4517 -44 160 -291 C ATOM 1112 CZ3 TRP A 155 189.797 30.348 524.585 1.00 34.49 C ANISOU 1112 CZ3 TRP A 155 3562 4922 4621 -127 192 -305 C ATOM 1113 CH2 TRP A 155 189.708 29.140 525.284 1.00 34.44 C ANISOU 1113 CH2 TRP A 155 3560 4901 4626 -42 205 -304 C ATOM 1114 N ALA A 156 191.378 36.922 526.930 1.00 29.25 N ANISOU 1114 N ALA A 156 2658 4414 4042 -706 -40 -272 N ATOM 1115 CA ALA A 156 191.080 38.228 526.342 1.00 29.15 C ANISOU 1115 CA ALA A 156 2712 4329 4034 -798 -31 -283 C ATOM 1116 C ALA A 156 192.061 38.639 525.249 1.00 29.97 C ANISOU 1116 C ALA A 156 2740 4491 4154 -837 24 -221 C ATOM 1117 O ALA A 156 191.601 39.039 524.166 1.00 30.24 O ANISOU 1117 O ALA A 156 2846 4464 4179 -826 74 -219 O ATOM 1118 CB ALA A 156 190.996 39.287 527.446 1.00 29.05 C ANISOU 1118 CB ALA A 156 2758 4269 4009 -916 -96 -317 C ATOM 1119 N PRO A 157 193.388 38.580 525.440 1.00 41.92 N ANISOU 1119 N PRO A 157 4108 6123 5697 -880 19 -155 N ATOM 1120 CA PRO A 157 194.278 39.001 524.343 1.00 42.92 C ANISOU 1120 CA PRO A 157 4157 6299 5854 -909 100 -77 C ATOM 1121 C PRO A 157 194.180 38.117 523.113 1.00 43.79 C ANISOU 1121 C PRO A 157 4299 6405 5934 -764 219 -56 C ATOM 1122 O PRO A 157 194.289 38.617 521.986 1.00 44.67 O ANISOU 1122 O PRO A 157 4451 6490 6032 -771 299 -25 O ATOM 1123 CB PRO A 157 195.676 38.932 524.978 1.00 43.54 C ANISOU 1123 CB PRO A 157 4037 6516 5990 -973 61 11 C ATOM 1124 CG PRO A 157 195.440 38.963 526.445 1.00 42.91 C ANISOU 1124 CG PRO A 157 3980 6435 5890 -1037 -75 -41 C ATOM 1125 CD PRO A 157 194.159 38.227 526.644 1.00 42.06 C ANISOU 1125 CD PRO A 157 4015 6238 5729 -915 -63 -128 C ATOM 1126 N ALA A 158 193.977 36.811 523.295 1.00 38.24 N ANISOU 1126 N ALA A 158 3604 5718 5210 -634 236 -71 N ATOM 1127 CA ALA A 158 193.920 35.910 522.150 1.00 39.49 C ANISOU 1127 CA ALA A 158 3834 5853 5320 -501 350 -60 C ATOM 1128 C ALA A 158 192.645 36.117 521.343 1.00 39.72 C ANISOU 1128 C ALA A 158 4052 5755 5283 -497 334 -128 C ATOM 1129 O ALA A 158 192.675 36.089 520.108 1.00 41.23 O ANISOU 1129 O ALA A 158 4335 5915 5417 -457 416 -110 O ATOM 1130 CB ALA A 158 194.035 34.459 522.617 1.00 39.61 C ANISOU 1130 CB ALA A 158 3826 5897 5329 -371 372 -60 C ATOM 1131 N ILE A 159 191.515 36.332 522.018 1.00 31.96 N ANISOU 1131 N ILE A 159 3134 4701 4308 -536 231 -194 N ATOM 1132 CA ILE A 159 190.257 36.519 521.303 1.00 32.28 C ANISOU 1132 CA ILE A 159 3322 4634 4310 -535 198 -232 C ATOM 1133 C ILE A 159 190.225 37.871 520.601 1.00 32.60 C ANISOU 1133 C ILE A 159 3399 4642 4347 -618 209 -205 C ATOM 1134 O ILE A 159 189.737 37.987 519.471 1.00 34.04 O ANISOU 1134 O ILE A 159 3692 4768 4472 -601 222 -196 O ATOM 1135 CB ILE A 159 189.069 36.357 522.268 1.00 30.70 C ANISOU 1135 CB ILE A 159 3149 4369 4145 -539 107 -281 C ATOM 1136 CG1 ILE A 159 189.007 34.923 522.792 1.00 30.78 C ANISOU 1136 CG1 ILE A 159 3148 4395 4153 -450 105 -302 C ATOM 1137 CG2 ILE A 159 187.764 36.741 521.582 1.00 30.82 C ANISOU 1137 CG2 ILE A 159 3273 4284 4153 -552 58 -289 C ATOM 1138 CD1 ILE A 159 187.951 34.703 523.841 1.00 29.33 C ANISOU 1138 CD1 ILE A 159 2975 4156 4014 -448 39 -334 C ATOM 1139 N LEU A 160 190.746 38.911 521.248 1.00 41.14 N ANISOU 1139 N LEU A 160 4402 5749 5479 -716 197 -188 N ATOM 1140 CA LEU A 160 190.566 40.260 520.725 1.00 41.31 C ANISOU 1140 CA LEU A 160 4476 5713 5507 -800 205 -165 C ATOM 1141 C LEU A 160 191.639 40.651 519.717 1.00 42.80 C ANISOU 1141 C LEU A 160 4631 5951 5679 -822 303 -95 C ATOM 1142 O LEU A 160 191.390 41.508 518.861 1.00 43.56 O ANISOU 1142 O LEU A 160 4807 5990 5753 -855 332 -67 O ATOM 1143 CB LEU A 160 190.545 41.269 521.876 1.00 40.01 C ANISOU 1143 CB LEU A 160 4288 5519 5394 -908 152 -187 C ATOM 1144 CG LEU A 160 189.464 41.091 522.941 1.00 38.76 C ANISOU 1144 CG LEU A 160 4181 5294 5251 -884 86 -244 C ATOM 1145 CD1 LEU A 160 189.805 41.914 524.170 1.00 38.28 C ANISOU 1145 CD1 LEU A 160 4117 5217 5210 -988 49 -270 C ATOM 1146 CD2 LEU A 160 188.090 41.476 522.409 1.00 38.73 C ANISOU 1146 CD2 LEU A 160 4284 5180 5252 -845 78 -242 C ATOM 1147 N PHE A 161 192.820 40.034 519.785 1.00 36.15 N ANISOU 1147 N PHE A 161 3666 5213 4854 -794 365 -51 N ATOM 1148 CA PHE A 161 193.984 40.510 519.048 1.00 37.39 C ANISOU 1148 CA PHE A 161 3747 5429 5031 -826 474 41 C ATOM 1149 C PHE A 161 194.613 39.450 518.151 1.00 38.99 C ANISOU 1149 C PHE A 161 3947 5682 5185 -690 609 92 C ATOM 1150 O PHE A 161 195.673 39.707 517.569 1.00 40.06 O ANISOU 1150 O PHE A 161 3996 5876 5348 -692 730 189 O ATOM 1151 CB PHE A 161 195.033 41.051 520.025 1.00 36.77 C ANISOU 1151 CB PHE A 161 3484 5435 5051 -947 437 89 C ATOM 1152 CG PHE A 161 194.514 42.132 520.938 1.00 35.52 C ANISOU 1152 CG PHE A 161 3370 5206 4919 -1088 319 33 C ATOM 1153 CD1 PHE A 161 193.717 43.153 520.442 1.00 35.48 C ANISOU 1153 CD1 PHE A 161 3507 5084 4890 -1135 321 10 C ATOM 1154 CD2 PHE A 161 194.820 42.126 522.291 1.00 34.68 C ANISOU 1154 CD2 PHE A 161 3183 5142 4851 -1166 213 9 C ATOM 1155 CE1 PHE A 161 193.238 44.147 521.275 1.00 34.58 C ANISOU 1155 CE1 PHE A 161 3460 4882 4796 -1245 243 -39 C ATOM 1156 CE2 PHE A 161 194.343 43.119 523.131 1.00 33.93 C ANISOU 1156 CE2 PHE A 161 3175 4960 4757 -1290 123 -50 C ATOM 1157 CZ PHE A 161 193.550 44.131 522.621 1.00 33.88 C ANISOU 1157 CZ PHE A 161 3316 4823 4732 -1324 150 -75 C ATOM 1158 N TRP A 162 193.998 38.273 518.015 1.00 37.55 N ANISOU 1158 N TRP A 162 3865 5468 4934 -571 603 35 N ATOM 1159 CA TRP A 162 194.568 37.261 517.130 1.00 39.16 C ANISOU 1159 CA TRP A 162 4118 5690 5072 -433 750 75 C ATOM 1160 C TRP A 162 194.519 37.700 515.672 1.00 40.80 C ANISOU 1160 C TRP A 162 4485 5838 5179 -412 852 106 C ATOM 1161 O TRP A 162 195.417 37.359 514.893 1.00 41.88 O ANISOU 1161 O TRP A 162 4626 6006 5282 -325 1026 182 O ATOM 1162 CB TRP A 162 193.844 35.925 517.304 1.00 39.26 C ANISOU 1162 CB TRP A 162 4242 5652 5022 -328 711 -3 C ATOM 1163 CG TRP A 162 194.373 34.839 516.416 1.00 40.73 C ANISOU 1163 CG TRP A 162 4529 5826 5122 -179 871 25 C ATOM 1164 CD1 TRP A 162 193.760 34.303 515.321 1.00 42.02 C ANISOU 1164 CD1 TRP A 162 4943 5883 5137 -115 905 -23 C ATOM 1165 CD2 TRP A 162 195.633 34.165 516.539 1.00 40.88 C ANISOU 1165 CD2 TRP A 162 4414 5930 5189 -71 1027 114 C ATOM 1166 NE1 TRP A 162 194.556 33.335 514.758 1.00 42.58 N ANISOU 1166 NE1 TRP A 162 5078 5953 5148 30 1089 17 N ATOM 1167 CE2 TRP A 162 195.712 33.232 515.487 1.00 41.85 C ANISOU 1167 CE2 TRP A 162 4738 5978 5184 72 1178 110 C ATOM 1168 CE3 TRP A 162 196.701 34.260 517.438 1.00 40.03 C ANISOU 1168 CE3 TRP A 162 4038 5952 5220 -82 1048 208 C ATOM 1169 CZ2 TRP A 162 196.815 32.399 515.309 1.00 41.85 C ANISOU 1169 CZ2 TRP A 162 4678 6022 5200 227 1380 200 C ATOM 1170 CZ3 TRP A 162 197.795 33.432 517.259 1.00 40.19 C ANISOU 1170 CZ3 TRP A 162 3965 6035 5271 63 1227 312 C ATOM 1171 CH2 TRP A 162 197.843 32.514 516.203 1.00 41.07 C ANISOU 1171 CH2 TRP A 162 4280 6063 5262 227 1406 310 C ATOM 1172 N GLN A 163 193.487 38.456 515.290 1.00 38.77 N ANISOU 1172 N GLN A 163 4362 5496 4874 -482 756 62 N ATOM 1173 CA GLN A 163 193.382 38.939 513.917 1.00 40.35 C ANISOU 1173 CA GLN A 163 4728 5638 4965 -469 834 99 C ATOM 1174 C GLN A 163 194.548 39.846 513.548 1.00 40.61 C ANISOU 1174 C GLN A 163 4648 5728 5054 -512 976 209 C ATOM 1175 O GLN A 163 194.970 39.872 512.386 1.00 41.85 O ANISOU 1175 O GLN A 163 4915 5866 5119 -451 1124 270 O ATOM 1176 CB GLN A 163 192.055 39.673 513.728 1.00 40.48 C ANISOU 1176 CB GLN A 163 4868 5565 4948 -541 685 55 C ATOM 1177 CG GLN A 163 191.815 40.763 514.757 1.00 38.67 C ANISOU 1177 CG GLN A 163 4506 5338 4849 -660 591 51 C ATOM 1178 CD GLN A 163 190.367 41.199 514.824 1.00 38.41 C ANISOU 1178 CD GLN A 163 4572 5215 4809 -692 448 11 C ATOM 1179 OE1 GLN A 163 189.779 41.600 513.820 1.00 39.87 O ANISOU 1179 OE1 GLN A 163 4897 5338 4912 -687 432 39 O ATOM 1180 NE2 GLN A 163 189.781 41.119 516.013 1.00 36.49 N ANISOU 1180 NE2 GLN A 163 4252 4962 4649 -719 348 -40 N ATOM 1181 N PHE A 164 195.084 40.592 514.516 1.00 35.71 N ANISOU 1181 N PHE A 164 3822 5169 4579 -624 934 242 N ATOM 1182 CA PHE A 164 196.213 41.471 514.236 1.00 36.09 C ANISOU 1182 CA PHE A 164 3738 5270 4705 -694 1052 359 C ATOM 1183 C PHE A 164 197.534 40.713 514.214 1.00 36.46 C ANISOU 1183 C PHE A 164 3617 5426 4810 -608 1209 460 C ATOM 1184 O PHE A 164 198.477 41.145 513.542 1.00 37.05 O ANISOU 1184 O PHE A 164 3620 5537 4920 -609 1371 583 O ATOM 1185 CB PHE A 164 196.269 42.600 515.266 1.00 34.73 C ANISOU 1185 CB PHE A 164 3434 5105 4658 -872 929 355 C ATOM 1186 CG PHE A 164 194.972 43.340 515.423 1.00 33.96 C ANISOU 1186 CG PHE A 164 3487 4892 4522 -935 797 269 C ATOM 1187 CD1 PHE A 164 194.528 44.206 514.437 1.00 34.88 C ANISOU 1187 CD1 PHE A 164 3749 4924 4580 -953 836 299 C ATOM 1188 CD2 PHE A 164 194.199 43.174 516.560 1.00 32.28 C ANISOU 1188 CD2 PHE A 164 3269 4656 4339 -963 646 176 C ATOM 1189 CE1 PHE A 164 193.334 44.889 514.580 1.00 34.25 C ANISOU 1189 CE1 PHE A 164 3790 4741 4482 -993 724 244 C ATOM 1190 CE2 PHE A 164 193.004 43.855 516.710 1.00 31.56 C ANISOU 1190 CE2 PHE A 164 3303 4457 4230 -1000 552 120 C ATOM 1191 CZ PHE A 164 192.572 44.714 515.718 1.00 32.57 C ANISOU 1191 CZ PHE A 164 3559 4505 4313 -1012 589 158 C ATOM 1192 N ILE A 165 197.623 39.592 514.932 1.00 42.36 N ANISOU 1192 N ILE A 165 4294 6223 5577 -526 1177 426 N ATOM 1193 CA ILE A 165 198.843 38.790 514.906 1.00 42.43 C ANISOU 1193 CA ILE A 165 4141 6334 5649 -415 1339 539 C ATOM 1194 C ILE A 165 199.004 38.117 513.549 1.00 43.58 C ANISOU 1194 C ILE A 165 4474 6425 5659 -241 1557 573 C ATOM 1195 O ILE A 165 200.083 38.148 512.945 1.00 44.05 O ANISOU 1195 O ILE A 165 4440 6537 5760 -175 1768 714 O ATOM 1196 CB ILE A 165 198.838 37.760 516.050 1.00 41.50 C ANISOU 1196 CB ILE A 165 3916 6272 5579 -362 1245 498 C ATOM 1197 CG1 ILE A 165 198.621 38.451 517.396 1.00 40.22 C ANISOU 1197 CG1 ILE A 165 3617 6147 5516 -535 1028 455 C ATOM 1198 CG2 ILE A 165 200.141 36.976 516.062 1.00 41.60 C ANISOU 1198 CG2 ILE A 165 3733 6395 5678 -237 1416 643 C ATOM 1199 CD1 ILE A 165 199.691 39.454 517.745 1.00 40.07 C ANISOU 1199 CD1 ILE A 165 3365 6221 5639 -686 1020 576 C ATOM 1200 N VAL A 166 197.934 37.493 513.052 1.00 35.14 N ANISOU 1200 N VAL A 166 3681 5245 4424 -168 1513 452 N ATOM 1201 CA VAL A 166 197.974 36.906 511.718 1.00 36.27 C ANISOU 1201 CA VAL A 166 4073 5309 4397 -22 1698 464 C ATOM 1202 C VAL A 166 197.815 37.959 510.630 1.00 37.07 C ANISOU 1202 C VAL A 166 4319 5355 4413 -78 1753 499 C ATOM 1203 O VAL A 166 198.133 37.689 509.466 1.00 38.46 O ANISOU 1203 O VAL A 166 4682 5478 4451 36 1948 546 O ATOM 1204 CB VAL A 166 196.895 35.820 511.564 1.00 35.95 C ANISOU 1204 CB VAL A 166 4295 5162 4202 52 1606 323 C ATOM 1205 CG1 VAL A 166 197.169 34.664 512.515 1.00 35.34 C ANISOU 1205 CG1 VAL A 166 4099 5129 4199 138 1602 306 C ATOM 1206 CG2 VAL A 166 195.513 36.404 511.812 1.00 35.17 C ANISOU 1206 CG2 VAL A 166 4291 5000 4073 -84 1353 213 C ATOM 1207 N GLY A 167 197.332 39.152 510.976 1.00 41.02 N ANISOU 1207 N GLY A 167 4755 5851 4978 -244 1597 482 N ATOM 1208 CA GLY A 167 197.241 40.249 510.038 1.00 41.74 C ANISOU 1208 CA GLY A 167 4956 5891 5010 -303 1648 534 C ATOM 1209 C GLY A 167 195.981 40.297 509.204 1.00 42.53 C ANISOU 1209 C GLY A 167 5367 5873 4919 -295 1545 447 C ATOM 1210 O GLY A 167 195.845 41.205 508.374 1.00 43.19 O ANISOU 1210 O GLY A 167 5563 5909 4937 -335 1581 497 O ATOM 1211 N VAL A 168 195.056 39.360 509.391 1.00 35.37 N ANISOU 1211 N VAL A 168 4597 4916 3926 -252 1409 331 N ATOM 1212 CA VAL A 168 193.818 39.323 508.623 1.00 35.66 C ANISOU 1212 CA VAL A 168 4913 4847 3790 -260 1275 261 C ATOM 1213 C VAL A 168 192.701 38.809 509.521 1.00 34.61 C ANISOU 1213 C VAL A 168 4758 4693 3701 -304 1043 151 C ATOM 1214 O VAL A 168 192.914 37.921 510.354 1.00 33.96 O ANISOU 1214 O VAL A 168 4568 4647 3688 -263 1037 108 O ATOM 1215 CB VAL A 168 193.963 38.453 507.354 1.00 36.84 C ANISOU 1215 CB VAL A 168 5363 4925 3709 -130 1415 258 C ATOM 1216 CG1 VAL A 168 194.269 37.004 507.718 1.00 36.66 C ANISOU 1216 CG1 VAL A 168 5359 4901 3668 -16 1479 202 C ATOM 1217 CG2 VAL A 168 192.714 38.545 506.489 1.00 37.28 C ANISOU 1217 CG2 VAL A 168 5711 4878 3577 -167 1246 204 C ATOM 1218 N ARG A 169 191.511 39.385 509.364 1.00 38.78 N ANISOU 1218 N ARG A 169 5375 5161 4198 -382 860 123 N ATOM 1219 CA ARG A 169 190.319 38.940 510.076 1.00 38.53 C ANISOU 1219 CA ARG A 169 5333 5097 4208 -421 646 41 C ATOM 1220 C ARG A 169 189.510 38.050 509.140 1.00 39.27 C ANISOU 1220 C ARG A 169 5703 5107 4113 -385 558 -7 C ATOM 1221 O ARG A 169 188.879 38.539 508.198 1.00 39.94 O ANISOU 1221 O ARG A 169 5960 5137 4081 -416 481 23 O ATOM 1222 CB ARG A 169 189.489 40.129 510.556 1.00 38.30 C ANISOU 1222 CB ARG A 169 5209 5055 4290 -523 506 62 C ATOM 1223 CG ARG A 169 188.195 39.731 511.247 1.00 38.24 C ANISOU 1223 CG ARG A 169 5179 5011 4340 -553 306 5 C ATOM 1224 CD ARG A 169 187.368 40.945 511.631 1.00 37.75 C ANISOU 1224 CD ARG A 169 5040 4920 4384 -625 205 46 C ATOM 1225 NE ARG A 169 186.106 40.563 512.258 1.00 37.23 N ANISOU 1225 NE ARG A 169 4938 4820 4386 -640 36 17 N ATOM 1226 CZ ARG A 169 185.940 40.399 513.566 1.00 34.54 C ANISOU 1226 CZ ARG A 169 4443 4498 4182 -649 13 -23 C ATOM 1227 NH1 ARG A 169 186.958 40.587 514.395 1.00 33.05 N ANISOU 1227 NH1 ARG A 169 4127 4365 4065 -658 120 -43 N ATOM 1228 NH2 ARG A 169 184.756 40.048 514.046 1.00 32.96 N ANISOU 1228 NH2 ARG A 169 4215 4262 4048 -655 -121 -31 N ATOM 1229 N THR A 170 189.537 36.742 509.396 1.00 34.43 N ANISOU 1229 N THR A 170 5143 4476 3463 -326 561 -76 N ATOM 1230 CA THR A 170 188.781 35.799 508.583 1.00 34.64 C ANISOU 1230 CA THR A 170 5451 4404 3306 -313 462 -134 C ATOM 1231 C THR A 170 187.302 35.762 508.944 1.00 34.37 C ANISOU 1231 C THR A 170 5404 4331 3324 -411 192 -165 C ATOM 1232 O THR A 170 186.510 35.196 508.183 1.00 34.33 O ANISOU 1232 O THR A 170 5628 4244 3171 -443 55 -194 O ATOM 1233 CB THR A 170 189.375 34.394 508.712 1.00 34.47 C ANISOU 1233 CB THR A 170 5513 4357 3228 -212 582 -193 C ATOM 1234 OG1 THR A 170 189.246 33.939 510.064 1.00 33.44 O ANISOU 1234 OG1 THR A 170 5157 4273 3277 -221 524 -229 O ATOM 1235 CG2 THR A 170 190.845 34.405 508.328 1.00 35.10 C ANISOU 1235 CG2 THR A 170 5585 4478 3273 -95 872 -134 C ATOM 1236 N VAL A 171 186.913 36.345 510.076 1.00 37.81 N ANISOU 1236 N VAL A 171 5584 4818 3962 -462 115 -150 N ATOM 1237 CA VAL A 171 185.508 36.404 510.468 1.00 37.16 C ANISOU 1237 CA VAL A 171 5455 4703 3961 -540 -111 -150 C ATOM 1238 C VAL A 171 184.804 37.394 509.544 1.00 37.90 C ANISOU 1238 C VAL A 171 5641 4767 3991 -595 -219 -74 C ATOM 1239 O VAL A 171 185.015 38.606 509.642 1.00 38.65 O ANISOU 1239 O VAL A 171 5632 4894 4161 -606 -164 -10 O ATOM 1240 CB VAL A 171 185.351 36.806 511.938 1.00 36.20 C ANISOU 1240 CB VAL A 171 5061 4632 4061 -559 -123 -148 C ATOM 1241 CG1 VAL A 171 183.899 36.669 512.376 1.00 34.20 C ANISOU 1241 CG1 VAL A 171 4755 4339 3902 -616 -323 -137 C ATOM 1242 CG2 VAL A 171 186.266 35.967 512.819 1.00 35.84 C ANISOU 1242 CG2 VAL A 171 4918 4633 4067 -497 1 -204 C ATOM 1243 N GLU A 172 183.968 36.881 508.645 1.00 62.44 N ANISOU 1243 N GLU A 172 8957 7810 6959 -635 -383 -75 N ATOM 1244 CA GLU A 172 183.308 37.726 507.664 1.00 63.22 C ANISOU 1244 CA GLU A 172 9165 7884 6973 -682 -504 12 C ATOM 1245 C GLU A 172 182.196 38.545 508.321 1.00 62.78 C ANISOU 1245 C GLU A 172 8896 7842 7115 -734 -655 93 C ATOM 1246 O GLU A 172 181.813 38.324 509.474 1.00 61.33 O ANISOU 1246 O GLU A 172 8514 7676 7113 -739 -681 74 O ATOM 1247 CB GLU A 172 182.747 36.879 506.524 1.00 63.16 C ANISOU 1247 CB GLU A 172 9458 7800 6741 -725 -662 -10 C ATOM 1248 CG GLU A 172 183.773 35.958 505.883 1.00 63.44 C ANISOU 1248 CG GLU A 172 9747 7792 6565 -656 -493 -95 C ATOM 1249 CD GLU A 172 183.169 35.044 504.838 1.00 63.40 C ANISOU 1249 CD GLU A 172 10082 7686 6319 -714 -662 -137 C ATOM 1250 OE1 GLU A 172 182.602 35.556 503.849 1.00 63.89 O ANISOU 1250 OE1 GLU A 172 10312 7723 6242 -771 -808 -72 O ATOM 1251 OE2 GLU A 172 183.253 33.809 505.011 1.00 62.91 O ANISOU 1251 OE2 GLU A 172 10136 7565 6204 -707 -656 -231 O ATOM 1252 N ASP A 173 181.677 39.509 507.561 1.00 55.27 N ANISOU 1252 N ASP A 173 7996 6879 6124 -759 -739 197 N ATOM 1253 CA ASP A 173 180.614 40.368 508.063 1.00 55.06 C ANISOU 1253 CA ASP A 173 7781 6857 6284 -785 -859 301 C ATOM 1254 C ASP A 173 179.350 39.559 508.327 1.00 53.44 C ANISOU 1254 C ASP A 173 7518 6631 6154 -844 -1089 320 C ATOM 1255 O ASP A 173 178.949 38.718 507.518 1.00 53.35 O ANISOU 1255 O ASP A 173 7690 6587 5993 -902 -1251 305 O ATOM 1256 CB ASP A 173 180.326 41.490 507.063 1.00 56.50 C ANISOU 1256 CB ASP A 173 8053 7024 6391 -790 -905 424 C ATOM 1257 CG ASP A 173 179.164 42.367 507.487 1.00 56.42 C ANISOU 1257 CG ASP A 173 7856 7007 6573 -797 -1023 556 C ATOM 1258 OD1 ASP A 173 179.273 43.034 508.538 1.00 56.14 O ANISOU 1258 OD1 ASP A 173 7630 6975 6724 -761 -899 562 O ATOM 1259 OD2 ASP A 173 178.144 42.392 506.767 1.00 56.48 O ANISOU 1259 OD2 ASP A 173 7916 7002 6543 -837 -1238 662 O ATOM 1260 N GLY A 174 178.722 39.819 509.470 1.00 33.86 N ANISOU 1260 N GLY A 174 4795 4164 3908 -835 -1099 359 N ATOM 1261 CA GLY A 174 177.555 39.074 509.889 1.00 33.10 C ANISOU 1261 CA GLY A 174 4595 4052 3928 -885 -1285 394 C ATOM 1262 C GLY A 174 177.850 37.796 510.642 1.00 31.75 C ANISOU 1262 C GLY A 174 4409 3876 3777 -891 -1247 271 C ATOM 1263 O GLY A 174 176.910 37.141 511.109 1.00 31.09 O ANISOU 1263 O GLY A 174 4225 3776 3813 -936 -1382 301 O ATOM 1264 N GLU A 175 179.118 37.417 510.770 1.00 44.15 N ANISOU 1264 N GLU A 175 6068 5460 5247 -843 -1064 149 N ATOM 1265 CA GLU A 175 179.526 36.240 511.518 1.00 42.92 C ANISOU 1265 CA GLU A 175 5898 5300 5110 -826 -1001 41 C ATOM 1266 C GLU A 175 180.159 36.656 512.838 1.00 41.76 C ANISOU 1266 C GLU A 175 5554 5199 5112 -759 -818 10 C ATOM 1267 O GLU A 175 180.610 37.793 513.008 1.00 42.16 O ANISOU 1267 O GLU A 175 5536 5279 5203 -730 -709 43 O ATOM 1268 CB GLU A 175 180.515 35.389 510.714 1.00 44.21 C ANISOU 1268 CB GLU A 175 6309 5439 5049 -806 -921 -59 C ATOM 1269 CG GLU A 175 179.941 34.787 509.444 1.00 44.92 C ANISOU 1269 CG GLU A 175 6657 5461 4949 -883 -1107 -56 C ATOM 1270 CD GLU A 175 180.970 33.988 508.668 1.00 45.94 C ANISOU 1270 CD GLU A 175 7067 5546 4841 -839 -983 -156 C ATOM 1271 OE1 GLU A 175 182.181 34.208 508.884 1.00 46.59 O ANISOU 1271 OE1 GLU A 175 7123 5670 4909 -741 -744 -192 O ATOM 1272 OE2 GLU A 175 180.570 33.137 507.846 1.00 46.08 O ANISOU 1272 OE2 GLU A 175 7337 5482 4690 -903 -1121 -193 O ATOM 1273 N CYS A 176 180.191 35.715 513.779 1.00 42.80 N ANISOU 1273 N CYS A 176 5613 5331 5319 -744 -791 -53 N ATOM 1274 CA CYS A 176 180.806 35.967 515.079 1.00 41.57 C ANISOU 1274 CA CYS A 176 5295 5218 5280 -688 -639 -87 C ATOM 1275 C CYS A 176 181.302 34.643 515.641 1.00 41.26 C ANISOU 1275 C CYS A 176 5274 5181 5222 -657 -588 -176 C ATOM 1276 O CYS A 176 180.497 33.792 516.032 1.00 40.29 O ANISOU 1276 O CYS A 176 5127 5019 5164 -681 -682 -176 O ATOM 1277 CB CYS A 176 179.824 36.635 516.036 1.00 39.78 C ANISOU 1277 CB CYS A 176 4887 4982 5245 -690 -673 -12 C ATOM 1278 SG CYS A 176 180.609 37.188 517.559 0.94 38.30 S ANISOU 1278 SG CYS A 176 4560 4834 5158 -636 -494 -56 S ATOM 1279 N TYR A 177 182.621 34.477 515.681 1.00 30.70 N ANISOU 1279 N TYR A 177 3970 3886 3808 -601 -435 -234 N ATOM 1280 CA TYR A 177 183.232 33.283 516.247 1.00 30.82 C ANISOU 1280 CA TYR A 177 3992 3908 3810 -549 -361 -302 C ATOM 1281 C TYR A 177 184.698 33.577 516.523 1.00 31.87 C ANISOU 1281 C TYR A 177 4070 4119 3921 -485 -184 -319 C ATOM 1282 O TYR A 177 185.279 34.511 515.963 1.00 33.02 O ANISOU 1282 O TYR A 177 4224 4297 4023 -492 -121 -288 O ATOM 1283 CB TYR A 177 183.080 32.072 515.318 1.00 31.96 C ANISOU 1283 CB TYR A 177 4351 3977 3815 -555 -414 -346 C ATOM 1284 CG TYR A 177 183.667 32.274 513.938 1.00 33.83 C ANISOU 1284 CG TYR A 177 4790 4197 3867 -544 -368 -351 C ATOM 1285 CD1 TYR A 177 182.925 32.871 512.928 1.00 34.11 C ANISOU 1285 CD1 TYR A 177 4934 4197 3830 -616 -501 -305 C ATOM 1286 CD2 TYR A 177 184.960 31.862 513.645 1.00 35.25 C ANISOU 1286 CD2 TYR A 177 5052 4396 3944 -454 -184 -386 C ATOM 1287 CE1 TYR A 177 183.456 33.058 511.667 1.00 35.72 C ANISOU 1287 CE1 TYR A 177 5349 4380 3845 -602 -451 -306 C ATOM 1288 CE2 TYR A 177 185.499 32.043 512.387 1.00 36.57 C ANISOU 1288 CE2 TYR A 177 5418 4539 3937 -430 -112 -381 C ATOM 1289 CZ TYR A 177 184.744 32.641 511.401 1.00 36.81 C ANISOU 1289 CZ TYR A 177 5579 4529 3878 -507 -246 -347 C ATOM 1290 OH TYR A 177 185.280 32.823 510.147 1.00 37.98 O ANISOU 1290 OH TYR A 177 5949 4648 3832 -478 -166 -339 O ATOM 1291 N ILE A 178 185.286 32.770 517.406 1.00 31.25 N ANISOU 1291 N ILE A 178 3923 4072 3881 -428 -110 -354 N ATOM 1292 CA ILE A 178 186.699 32.918 517.731 1.00 32.63 C ANISOU 1292 CA ILE A 178 4014 4332 4053 -370 40 -348 C ATOM 1293 C ILE A 178 187.537 32.496 516.532 1.00 34.89 C ANISOU 1293 C ILE A 178 4451 4608 4198 -312 151 -349 C ATOM 1294 O ILE A 178 187.376 31.391 515.999 1.00 35.00 O ANISOU 1294 O ILE A 178 4629 4550 4119 -270 155 -387 O ATOM 1295 CB ILE A 178 187.051 32.102 518.981 1.00 31.77 C ANISOU 1295 CB ILE A 178 3793 4260 4018 -317 75 -367 C ATOM 1296 CG1 ILE A 178 186.396 32.720 520.217 1.00 28.21 C ANISOU 1296 CG1 ILE A 178 3205 3823 3690 -367 2 -360 C ATOM 1297 CG2 ILE A 178 188.554 32.020 519.155 1.00 31.78 C ANISOU 1297 CG2 ILE A 178 3709 4353 4011 -250 218 -341 C ATOM 1298 CD1 ILE A 178 186.830 32.082 521.514 1.00 26.97 C ANISOU 1298 CD1 ILE A 178 2943 3713 3591 -318 36 -369 C ATOM 1299 N GLN A 179 188.446 33.378 516.109 1.00 32.69 N ANISOU 1299 N GLN A 179 4130 4389 3901 -309 253 -303 N ATOM 1300 CA GLN A 179 189.144 33.174 514.843 1.00 33.48 C ANISOU 1300 CA GLN A 179 4390 4468 3860 -250 377 -286 C ATOM 1301 C GLN A 179 190.125 32.010 514.913 1.00 33.17 C ANISOU 1301 C GLN A 179 4372 4444 3789 -126 533 -289 C ATOM 1302 O GLN A 179 190.205 31.209 513.974 1.00 33.76 O ANISOU 1302 O GLN A 179 4669 4439 3720 -59 604 -313 O ATOM 1303 CB GLN A 179 189.860 34.459 514.426 1.00 33.62 C ANISOU 1303 CB GLN A 179 4337 4546 3890 -281 461 -217 C ATOM 1304 CG GLN A 179 190.539 34.375 513.067 1.00 34.53 C ANISOU 1304 CG GLN A 179 4628 4636 3856 -217 609 -184 C ATOM 1305 CD GLN A 179 190.858 35.741 512.493 1.00 34.90 C ANISOU 1305 CD GLN A 179 4646 4711 3903 -273 654 -114 C ATOM 1306 OE1 GLN A 179 190.228 36.738 512.848 1.00 34.74 O ANISOU 1306 OE1 GLN A 179 4548 4692 3960 -369 537 -105 O ATOM 1307 NE2 GLN A 179 191.841 35.794 511.601 1.00 35.35 N ANISOU 1307 NE2 GLN A 179 4774 4781 3876 -204 843 -55 N ATOM 1308 N PHE A 180 190.884 31.893 516.004 1.00 51.16 N ANISOU 1308 N PHE A 180 6435 6814 6189 -90 589 -258 N ATOM 1309 CA PHE A 180 191.851 30.802 516.050 1.00 51.02 C ANISOU 1309 CA PHE A 180 6419 6814 6154 47 750 -235 C ATOM 1310 C PHE A 180 191.205 29.444 516.306 1.00 51.02 C ANISOU 1310 C PHE A 180 6551 6719 6115 98 705 -305 C ATOM 1311 O PHE A 180 191.926 28.442 516.369 1.00 50.88 O ANISOU 1311 O PHE A 180 6558 6694 6080 226 844 -287 O ATOM 1312 CB PHE A 180 192.936 31.078 517.097 1.00 49.86 C ANISOU 1312 CB PHE A 180 5989 6806 6149 68 811 -157 C ATOM 1313 CG PHE A 180 192.408 31.396 518.466 1.00 48.33 C ANISOU 1313 CG PHE A 180 5637 6656 6071 -19 651 -183 C ATOM 1314 CD1 PHE A 180 192.055 30.383 519.342 1.00 47.68 C ANISOU 1314 CD1 PHE A 180 5544 6554 6019 28 605 -218 C ATOM 1315 CD2 PHE A 180 192.289 32.710 518.886 1.00 47.31 C ANISOU 1315 CD2 PHE A 180 5391 6576 6011 -144 565 -169 C ATOM 1316 CE1 PHE A 180 191.577 30.674 520.604 1.00 46.04 C ANISOU 1316 CE1 PHE A 180 5214 6379 5900 -41 479 -236 C ATOM 1317 CE2 PHE A 180 191.814 33.007 520.147 1.00 45.51 C ANISOU 1317 CE2 PHE A 180 5057 6370 5866 -214 440 -195 C ATOM 1318 CZ PHE A 180 191.459 31.988 521.009 1.00 44.87 C ANISOU 1318 CZ PHE A 180 4967 6274 5806 -159 400 -227 C ATOM 1319 N PHE A 181 189.882 29.381 516.446 1.00 48.10 N ANISOU 1319 N PHE A 181 6261 6272 5741 4 524 -370 N ATOM 1320 CA PHE A 181 189.162 28.117 516.514 1.00 48.13 C ANISOU 1320 CA PHE A 181 6419 6164 5703 24 468 -434 C ATOM 1321 C PHE A 181 188.798 27.576 515.137 1.00 48.86 C ANISOU 1321 C PHE A 181 6830 6122 5611 25 471 -482 C ATOM 1322 O PHE A 181 187.999 26.638 515.045 1.00 48.73 O ANISOU 1322 O PHE A 181 6979 5990 5548 -4 381 -542 O ATOM 1323 CB PHE A 181 187.895 28.269 517.360 1.00 47.53 C ANISOU 1323 CB PHE A 181 6259 6070 5732 -84 274 -460 C ATOM 1324 CG PHE A 181 188.143 28.219 518.840 1.00 46.52 C ANISOU 1324 CG PHE A 181 5906 6026 5746 -59 279 -437 C ATOM 1325 CD1 PHE A 181 189.374 27.826 519.338 1.00 45.88 C ANISOU 1325 CD1 PHE A 181 5720 6023 5690 51 421 -396 C ATOM 1326 CD2 PHE A 181 187.141 28.555 519.735 1.00 45.84 C ANISOU 1326 CD2 PHE A 181 5716 5936 5763 -138 146 -442 C ATOM 1327 CE1 PHE A 181 189.604 27.777 520.700 1.00 44.37 C ANISOU 1327 CE1 PHE A 181 5339 5911 5609 66 404 -369 C ATOM 1328 CE2 PHE A 181 187.365 28.507 521.098 1.00 44.64 C ANISOU 1328 CE2 PHE A 181 5396 5851 5713 -113 155 -423 C ATOM 1329 CZ PHE A 181 188.598 28.117 521.581 1.00 43.53 C ANISOU 1329 CZ PHE A 181 5167 5793 5580 -18 271 -391 C ATOM 1330 N SER A 182 189.360 28.147 514.067 1.00 64.57 N ANISOU 1330 N SER A 182 8926 8119 7490 48 570 -455 N ATOM 1331 CA SER A 182 189.099 27.643 512.724 1.00 65.10 C ANISOU 1331 CA SER A 182 9338 8050 7346 55 584 -502 C ATOM 1332 C SER A 182 189.610 26.221 512.538 1.00 65.09 C ANISOU 1332 C SER A 182 9537 7945 7249 185 739 -540 C ATOM 1333 O SER A 182 189.118 25.505 511.660 1.00 65.35 O ANISOU 1333 O SER A 182 9900 7825 7105 166 702 -609 O ATOM 1334 CB SER A 182 189.730 28.568 511.683 1.00 65.72 C ANISOU 1334 CB SER A 182 9486 8162 7322 76 697 -451 C ATOM 1335 OG SER A 182 189.191 29.875 511.770 1.00 65.85 O ANISOU 1335 OG SER A 182 9356 8250 7416 -45 555 -416 O ATOM 1336 N ASN A 183 190.586 25.802 513.339 1.00 59.12 N ANISOU 1336 N ASN A 183 8601 7261 6600 315 906 -491 N ATOM 1337 CA ASN A 183 191.066 24.428 513.333 1.00 59.04 C ANISOU 1337 CA ASN A 183 8752 7151 6531 460 1067 -512 C ATOM 1338 C ASN A 183 190.309 23.644 514.400 1.00 58.58 C ANISOU 1338 C ASN A 183 8625 7055 6578 413 926 -557 C ATOM 1339 O ASN A 183 190.331 24.012 515.579 1.00 58.00 O ANISOU 1339 O ASN A 183 8251 7106 6682 391 863 -514 O ATOM 1340 CB ASN A 183 192.573 24.385 513.583 1.00 58.78 C ANISOU 1340 CB ASN A 183 8543 7222 6568 642 1335 -403 C ATOM 1341 CG ASN A 183 193.125 22.975 513.590 1.00 58.71 C ANISOU 1341 CG ASN A 183 8692 7107 6510 822 1532 -403 C ATOM 1342 OD1 ASN A 183 193.389 22.406 514.648 1.00 58.10 O ANISOU 1342 OD1 ASN A 183 8433 7077 6566 889 1551 -366 O ATOM 1343 ND2 ASN A 183 193.303 22.403 512.406 1.00 59.34 N ANISOU 1343 ND2 ASN A 183 9133 7030 6384 908 1688 -440 N ATOM 1344 N ALA A 184 189.634 22.569 513.981 1.00 44.39 N ANISOU 1344 N ALA A 184 7125 5077 4663 392 876 -642 N ATOM 1345 CA ALA A 184 188.801 21.807 514.905 1.00 44.04 C ANISOU 1345 CA ALA A 184 7037 4977 4718 329 736 -681 C ATOM 1346 C ALA A 184 189.623 21.161 516.013 1.00 43.54 C ANISOU 1346 C ALA A 184 6785 4975 4783 482 890 -623 C ATOM 1347 O ALA A 184 189.126 20.988 517.132 1.00 43.06 O ANISOU 1347 O ALA A 184 6546 4953 4863 437 782 -615 O ATOM 1348 CB ALA A 184 188.009 20.744 514.144 1.00 44.42 C ANISOU 1348 CB ALA A 184 7468 4803 4608 264 660 -778 C ATOM 1349 N ALA A 185 190.875 20.797 515.727 1.00 39.08 N ANISOU 1349 N ALA A 185 6254 4422 4174 672 1147 -568 N ATOM 1350 CA ALA A 185 191.720 20.206 516.759 1.00 38.42 C ANISOU 1350 CA ALA A 185 5970 4412 4218 828 1287 -487 C ATOM 1351 C ALA A 185 192.106 21.227 517.821 1.00 37.63 C ANISOU 1351 C ALA A 185 5465 4536 4298 795 1220 -399 C ATOM 1352 O ALA A 185 192.279 20.866 518.991 1.00 36.87 O ANISOU 1352 O ALA A 185 5177 4507 4325 840 1206 -352 O ATOM 1353 CB ALA A 185 192.970 19.590 516.131 1.00 38.63 C ANISOU 1353 CB ALA A 185 6117 4395 4165 1053 1593 -423 C ATOM 1354 N VAL A 186 192.245 22.499 517.438 1.00 38.36 N ANISOU 1354 N VAL A 186 5444 4736 4396 712 1174 -375 N ATOM 1355 CA VAL A 186 192.553 23.541 518.415 1.00 37.61 C ANISOU 1355 CA VAL A 186 5004 4831 4454 651 1092 -305 C ATOM 1356 C VAL A 186 191.405 23.697 519.404 1.00 37.18 C ANISOU 1356 C VAL A 186 4867 4776 4483 515 870 -359 C ATOM 1357 O VAL A 186 191.621 23.861 520.611 1.00 36.18 O ANISOU 1357 O VAL A 186 4512 4757 4476 516 826 -311 O ATOM 1358 CB VAL A 186 192.871 24.866 517.698 1.00 38.00 C ANISOU 1358 CB VAL A 186 4992 4962 4483 580 1096 -274 C ATOM 1359 CG1 VAL A 186 192.991 26.004 518.702 1.00 37.23 C ANISOU 1359 CG1 VAL A 186 4589 5026 4530 477 976 -226 C ATOM 1360 CG2 VAL A 186 194.150 24.733 516.884 1.00 38.29 C ANISOU 1360 CG2 VAL A 186 5058 5021 4469 734 1349 -187 C ATOM 1361 N THR A 187 190.165 23.640 518.910 1.00 38.76 N ANISOU 1361 N THR A 187 5252 4854 4619 396 729 -447 N ATOM 1362 CA THR A 187 189.010 23.748 519.795 1.00 38.37 C ANISOU 1362 CA THR A 187 5121 4794 4663 278 543 -478 C ATOM 1363 C THR A 187 188.944 22.571 520.760 1.00 37.83 C ANISOU 1363 C THR A 187 5039 4682 4654 353 570 -474 C ATOM 1364 O THR A 187 188.546 22.730 521.920 1.00 36.96 O ANISOU 1364 O THR A 187 4763 4627 4652 316 487 -454 O ATOM 1365 CB THR A 187 187.726 23.838 518.971 1.00 39.04 C ANISOU 1365 CB THR A 187 5395 4757 4681 140 387 -546 C ATOM 1366 OG1 THR A 187 187.897 24.800 517.923 1.00 39.50 O ANISOU 1366 OG1 THR A 187 5511 4842 4655 97 386 -543 O ATOM 1367 CG2 THR A 187 186.558 24.263 519.848 1.00 38.40 C ANISOU 1367 CG2 THR A 187 5173 4691 4725 20 211 -544 C ATOM 1368 N PHE A 188 189.336 21.380 520.300 1.00 35.62 N ANISOU 1368 N PHE A 188 4950 4290 4294 466 700 -489 N ATOM 1369 CA PHE A 188 189.296 20.208 521.168 1.00 35.18 C ANISOU 1369 CA PHE A 188 4901 4176 4291 547 740 -477 C ATOM 1370 C PHE A 188 190.379 20.274 522.238 1.00 34.03 C ANISOU 1370 C PHE A 188 4501 4188 4242 673 835 -376 C ATOM 1371 O PHE A 188 190.142 19.897 523.391 1.00 33.24 O ANISOU 1371 O PHE A 188 4291 4112 4227 685 789 -350 O ATOM 1372 CB PHE A 188 189.434 18.934 520.337 1.00 35.91 C ANISOU 1372 CB PHE A 188 5300 4081 4262 639 867 -521 C ATOM 1373 CG PHE A 188 189.324 17.671 521.142 1.00 35.66 C ANISOU 1373 CG PHE A 188 5311 3958 4279 719 915 -511 C ATOM 1374 CD1 PHE A 188 188.261 17.479 522.009 1.00 35.47 C ANISOU 1374 CD1 PHE A 188 5224 3904 4349 608 760 -528 C ATOM 1375 CD2 PHE A 188 190.277 16.672 521.025 1.00 35.64 C ANISOU 1375 CD2 PHE A 188 5414 3892 4234 916 1132 -471 C ATOM 1376 CE1 PHE A 188 188.155 16.319 522.752 1.00 35.27 C ANISOU 1376 CE1 PHE A 188 5244 3788 4370 681 812 -511 C ATOM 1377 CE2 PHE A 188 190.175 15.508 521.763 1.00 35.46 C ANISOU 1377 CE2 PHE A 188 5441 3775 4257 997 1183 -454 C ATOM 1378 CZ PHE A 188 189.114 15.332 522.628 1.00 35.27 C ANISOU 1378 CZ PHE A 188 5357 3722 4321 873 1019 -477 C ATOM 1379 N GLY A 189 191.575 20.743 521.874 1.00 37.81 N ANISOU 1379 N GLY A 189 4880 4777 4710 764 963 -306 N ATOM 1380 CA GLY A 189 192.613 20.933 522.873 1.00 36.76 C ANISOU 1380 CA GLY A 189 4475 4815 4679 853 1013 -191 C ATOM 1381 C GLY A 189 192.205 21.928 523.941 1.00 35.87 C ANISOU 1381 C GLY A 189 4152 4825 4653 718 835 -186 C ATOM 1382 O GLY A 189 192.545 21.770 525.116 1.00 34.96 O ANISOU 1382 O GLY A 189 3873 4800 4610 757 808 -123 O ATOM 1383 N THR A 190 191.468 22.967 523.545 1.00 43.82 N ANISOU 1383 N THR A 190 5179 5828 5644 564 716 -249 N ATOM 1384 CA THR A 190 190.902 23.891 524.521 1.00 42.72 C ANISOU 1384 CA THR A 190 4894 5764 5574 440 563 -258 C ATOM 1385 C THR A 190 189.908 23.184 525.433 1.00 42.13 C ANISOU 1385 C THR A 190 4861 5610 5537 425 489 -289 C ATOM 1386 O THR A 190 189.899 23.408 526.649 1.00 40.95 O ANISOU 1386 O THR A 190 4580 5535 5443 413 432 -257 O ATOM 1387 CB THR A 190 190.237 25.063 523.798 1.00 42.91 C ANISOU 1387 CB THR A 190 4958 5772 5575 300 474 -310 C ATOM 1388 OG1 THR A 190 191.242 25.978 523.343 1.00 42.98 O ANISOU 1388 OG1 THR A 190 4864 5888 5578 295 529 -259 O ATOM 1389 CG2 THR A 190 189.268 25.786 524.715 1.00 41.66 C ANISOU 1389 CG2 THR A 190 4726 5623 5480 185 333 -334 C ATOM 1390 N ALA A 191 189.069 22.314 524.864 1.00 36.99 N ANISOU 1390 N ALA A 191 4403 4801 4850 420 488 -347 N ATOM 1391 CA ALA A 191 188.101 21.581 525.673 1.00 36.64 C ANISOU 1391 CA ALA A 191 4395 4670 4856 399 429 -363 C ATOM 1392 C ALA A 191 188.786 20.666 526.678 1.00 35.95 C ANISOU 1392 C ALA A 191 4243 4616 4799 535 513 -299 C ATOM 1393 O ALA A 191 188.269 20.461 527.783 1.00 35.11 O ANISOU 1393 O ALA A 191 4080 4510 4749 524 465 -280 O ATOM 1394 CB ALA A 191 187.165 20.774 524.771 1.00 38.12 C ANISOU 1394 CB ALA A 191 4808 4674 5001 349 402 -428 C ATOM 1395 N ILE A 192 189.946 20.114 526.321 1.00 40.03 N ANISOU 1395 N ILE A 192 4768 5160 5279 675 650 -251 N ATOM 1396 CA ILE A 192 190.667 19.240 527.241 1.00 39.40 C ANISOU 1396 CA ILE A 192 4615 5121 5234 822 733 -166 C ATOM 1397 C ILE A 192 191.293 20.049 528.369 1.00 38.43 C ANISOU 1397 C ILE A 192 4251 5189 5162 812 666 -89 C ATOM 1398 O ILE A 192 191.252 19.646 529.538 1.00 37.85 O ANISOU 1398 O ILE A 192 4114 5146 5120 852 637 -41 O ATOM 1399 CB ILE A 192 191.724 18.420 526.478 1.00 39.99 C ANISOU 1399 CB ILE A 192 4766 5162 5266 993 918 -117 C ATOM 1400 CG1 ILE A 192 191.054 17.531 525.429 1.00 41.09 C ANISOU 1400 CG1 ILE A 192 5204 5081 5326 993 978 -208 C ATOM 1401 CG2 ILE A 192 192.549 17.582 527.440 1.00 39.42 C ANISOU 1401 CG2 ILE A 192 4586 5150 5243 1161 1005 0 C ATOM 1402 CD1 ILE A 192 192.034 16.771 524.561 1.00 41.74 C ANISOU 1402 CD1 ILE A 192 5418 5098 5343 1169 1190 -171 C ATOM 1403 N ALA A 193 191.872 21.206 528.045 1.00 32.48 N ANISOU 1403 N ALA A 193 3376 4557 4406 749 633 -73 N ATOM 1404 CA ALA A 193 192.572 21.995 529.052 1.00 31.88 C ANISOU 1404 CA ALA A 193 3089 4655 4367 718 555 0 C ATOM 1405 C ALA A 193 191.624 22.832 529.901 1.00 31.23 C ANISOU 1405 C ALA A 193 2999 4577 4291 575 410 -57 C ATOM 1406 O ALA A 193 191.898 23.053 531.086 1.00 30.94 O ANISOU 1406 O ALA A 193 2864 4632 4262 566 340 -10 O ATOM 1407 CB ALA A 193 193.607 22.900 528.384 1.00 32.17 C ANISOU 1407 CB ALA A 193 2998 4812 4411 695 580 51 C ATOM 1408 N ALA A 194 190.515 23.301 529.329 1.00 30.50 N ANISOU 1408 N ALA A 194 3017 4383 4190 470 367 -150 N ATOM 1409 CA ALA A 194 189.620 24.207 530.037 1.00 29.59 C ANISOU 1409 CA ALA A 194 2892 4262 4089 350 261 -191 C ATOM 1410 C ALA A 194 188.406 23.523 530.647 1.00 29.33 C ANISOU 1410 C ALA A 194 2949 4112 4083 354 249 -215 C ATOM 1411 O ALA A 194 187.735 24.132 531.487 1.00 28.77 O ANISOU 1411 O ALA A 194 2865 4039 4028 291 193 -225 O ATOM 1412 CB ALA A 194 189.143 25.325 529.100 1.00 29.35 C ANISOU 1412 CB ALA A 194 2893 4206 4054 234 221 -248 C ATOM 1413 N PHE A 195 188.102 22.286 530.258 1.00 25.88 N ANISOU 1413 N PHE A 195 2613 3567 3654 424 311 -220 N ATOM 1414 CA PHE A 195 186.930 21.621 530.814 1.00 25.68 C ANISOU 1414 CA PHE A 195 2661 3424 3673 412 300 -230 C ATOM 1415 C PHE A 195 187.246 20.227 531.342 1.00 25.99 C ANISOU 1415 C PHE A 195 2743 3420 3714 538 378 -183 C ATOM 1416 O PHE A 195 187.013 19.942 532.520 1.00 25.60 O ANISOU 1416 O PHE A 195 2666 3378 3683 572 377 -141 O ATOM 1417 CB PHE A 195 185.810 21.538 529.773 1.00 26.34 C ANISOU 1417 CB PHE A 195 2853 3372 3783 320 264 -287 C ATOM 1418 CG PHE A 195 184.601 20.785 530.253 1.00 26.46 C ANISOU 1418 CG PHE A 195 2923 3261 3868 294 251 -278 C ATOM 1419 CD1 PHE A 195 183.761 21.336 531.205 1.00 25.55 C ANISOU 1419 CD1 PHE A 195 2740 3152 3817 249 220 -250 C ATOM 1420 CD2 PHE A 195 184.312 19.524 529.761 1.00 27.61 C ANISOU 1420 CD2 PHE A 195 3200 3273 4020 314 282 -290 C ATOM 1421 CE1 PHE A 195 182.653 20.644 531.655 1.00 25.72 C ANISOU 1421 CE1 PHE A 195 2790 3060 3922 228 226 -220 C ATOM 1422 CE2 PHE A 195 183.203 18.828 530.206 1.00 27.87 C ANISOU 1422 CE2 PHE A 195 3269 3185 4134 273 266 -269 C ATOM 1423 CZ PHE A 195 182.373 19.390 531.154 1.00 26.90 C ANISOU 1423 CZ PHE A 195 3046 3083 4091 231 240 -226 C ATOM 1424 N TYR A 196 187.776 19.353 530.484 1.00 32.22 N ANISOU 1424 N TYR A 196 4106 2845 5293 655 -574 -210 N ATOM 1425 CA TYR A 196 187.915 17.948 530.860 1.00 30.88 C ANISOU 1425 CA TYR A 196 3882 2823 5030 713 -271 -265 C ATOM 1426 C TYR A 196 188.921 17.759 531.990 1.00 30.95 C ANISOU 1426 C TYR A 196 3783 2858 5118 708 -266 -211 C ATOM 1427 O TYR A 196 188.663 17.002 532.933 1.00 30.61 O ANISOU 1427 O TYR A 196 3709 2890 5033 737 -202 -270 O ATOM 1428 CB TYR A 196 188.297 17.114 529.639 1.00 31.51 C ANISOU 1428 CB TYR A 196 3935 2889 5148 766 -72 -278 C ATOM 1429 CG TYR A 196 187.134 16.864 528.703 1.00 31.58 C ANISOU 1429 CG TYR A 196 4030 2932 5036 808 -31 -417 C ATOM 1430 CD1 TYR A 196 186.166 15.915 529.008 1.00 30.70 C ANISOU 1430 CD1 TYR A 196 3902 2972 4791 797 79 -539 C ATOM 1431 CD2 TYR A 196 186.999 17.579 527.520 1.00 33.74 C ANISOU 1431 CD2 TYR A 196 4363 3015 5444 845 -210 -435 C ATOM 1432 CE1 TYR A 196 185.099 15.684 528.162 1.00 31.21 C ANISOU 1432 CE1 TYR A 196 3987 3085 4786 808 92 -687 C ATOM 1433 CE2 TYR A 196 185.935 17.354 526.667 1.00 34.25 C ANISOU 1433 CE2 TYR A 196 4499 3150 5362 918 -228 -641 C ATOM 1434 CZ TYR A 196 184.989 16.405 526.994 1.00 32.43 C ANISOU 1434 CZ TYR A 196 4227 3155 4939 870 -4 -740 C ATOM 1435 OH TYR A 196 183.928 16.177 526.149 1.00 33.21 O ANISOU 1435 OH TYR A 196 4340 3344 4935 896 -30 -924 O ATOM 1436 N LEU A 197 190.068 18.431 531.922 1.00 33.06 N ANISOU 1436 N LEU A 197 3984 3030 5547 671 -356 -91 N ATOM 1437 CA LEU A 197 191.053 18.303 532.992 1.00 33.29 C ANISOU 1437 CA LEU A 197 3908 3101 5641 687 -368 -67 C ATOM 1438 C LEU A 197 190.547 18.901 534.306 1.00 33.45 C ANISOU 1438 C LEU A 197 3916 3140 5652 678 -583 -174 C ATOM 1439 O LEU A 197 190.736 18.281 535.360 1.00 33.53 O ANISOU 1439 O LEU A 197 3905 3219 5617 752 -540 -202 O ATOM 1440 CB LEU A 197 192.386 18.940 532.586 1.00 35.62 C ANISOU 1440 CB LEU A 197 3997 3221 6314 601 -472 52 C ATOM 1441 CG LEU A 197 193.223 18.149 531.579 1.00 36.94 C ANISOU 1441 CG LEU A 197 3952 3336 6747 596 -219 118 C ATOM 1442 CD1 LEU A 197 194.575 18.812 531.368 1.00 39.79 C ANISOU 1442 CD1 LEU A 197 4016 3510 7593 492 -266 281 C ATOM 1443 CD2 LEU A 197 193.389 16.707 532.033 1.00 35.95 C ANISOU 1443 CD2 LEU A 197 3818 3406 6436 704 -11 -9 C ATOM 1444 N PRO A 198 189.918 20.087 534.310 1.00 34.04 N ANISOU 1444 N PRO A 198 4008 3152 5774 605 -849 -255 N ATOM 1445 CA PRO A 198 189.340 20.576 535.576 1.00 34.36 C ANISOU 1445 CA PRO A 198 4018 3237 5799 613 -1081 -457 C ATOM 1446 C PRO A 198 188.292 19.649 536.169 1.00 33.37 C ANISOU 1446 C PRO A 198 3940 3249 5492 690 -950 -566 C ATOM 1447 O PRO A 198 188.300 19.419 537.384 1.00 33.66 O ANISOU 1447 O PRO A 198 3967 3355 5469 763 -966 -638 O ATOM 1448 CB PRO A 198 188.741 21.931 535.181 1.00 35.46 C ANISOU 1448 CB PRO A 198 4157 3272 6046 526 -1424 -560 C ATOM 1449 CG PRO A 198 189.574 22.382 534.048 1.00 36.38 C ANISOU 1449 CG PRO A 198 4292 3240 6291 458 -1395 -314 C ATOM 1450 CD PRO A 198 189.897 21.140 533.275 1.00 35.07 C ANISOU 1450 CD PRO A 198 4184 3140 6000 520 -1008 -162 C ATOM 1451 N VAL A 199 187.386 19.111 535.347 1.00 28.48 N ANISOU 1451 N VAL A 199 3371 2661 4789 686 -817 -575 N ATOM 1452 CA VAL A 199 186.344 18.225 535.864 1.00 28.00 C ANISOU 1452 CA VAL A 199 3328 2701 4609 734 -677 -667 C ATOM 1453 C VAL A 199 186.963 16.985 536.498 1.00 27.96 C ANISOU 1453 C VAL A 199 3365 2696 4561 820 -394 -514 C ATOM 1454 O VAL A 199 186.492 16.498 537.533 1.00 28.27 O ANISOU 1454 O VAL A 199 3431 2779 4531 893 -319 -545 O ATOM 1455 CB VAL A 199 185.349 17.859 534.746 1.00 27.63 C ANISOU 1455 CB VAL A 199 3301 2671 4524 705 -595 -717 C ATOM 1456 CG1 VAL A 199 184.410 16.750 535.200 1.00 27.56 C ANISOU 1456 CG1 VAL A 199 3297 2728 4449 727 -383 -780 C ATOM 1457 CG2 VAL A 199 184.551 19.083 534.329 1.00 28.31 C ANISOU 1457 CG2 VAL A 199 3344 2770 4644 683 -949 -878 C ATOM 1458 N ILE A 200 188.033 16.462 535.894 1.00 26.08 N ANISOU 1458 N ILE A 200 3133 2409 4369 837 -255 -354 N ATOM 1459 CA ILE A 200 188.726 15.312 536.471 1.00 26.73 C ANISOU 1459 CA ILE A 200 3245 2487 4425 952 -92 -232 C ATOM 1460 C ILE A 200 189.319 15.674 537.827 1.00 27.68 C ANISOU 1460 C ILE A 200 3338 2630 4549 1048 -203 -187 C ATOM 1461 O ILE A 200 189.267 14.883 538.776 1.00 28.50 O ANISOU 1461 O ILE A 200 3501 2744 4584 1193 -97 -96 O ATOM 1462 CB ILE A 200 189.802 14.794 535.499 1.00 27.07 C ANISOU 1462 CB ILE A 200 3225 2500 4560 935 -23 -169 C ATOM 1463 CG1 ILE A 200 189.151 14.164 534.266 1.00 26.57 C ANISOU 1463 CG1 ILE A 200 3157 2440 4498 863 106 -237 C ATOM 1464 CG2 ILE A 200 190.718 13.792 536.187 1.00 28.46 C ANISOU 1464 CG2 ILE A 200 3379 2656 4780 1050 16 -90 C ATOM 1465 CD1 ILE A 200 190.144 13.661 533.243 1.00 27.17 C ANISOU 1465 CD1 ILE A 200 3113 2508 4704 833 205 -223 C ATOM 1466 N ILE A 201 189.879 16.879 537.944 1.00 25.94 N ANISOU 1466 N ILE A 201 3033 2408 4415 987 -438 -252 N ATOM 1467 CA ILE A 201 190.470 17.303 539.209 1.00 27.23 C ANISOU 1467 CA ILE A 201 3148 2617 4583 1078 -603 -274 C ATOM 1468 C ILE A 201 189.394 17.471 540.277 1.00 27.35 C ANISOU 1468 C ILE A 201 3198 2725 4470 1143 -677 -416 C ATOM 1469 O ILE A 201 189.562 17.027 541.419 1.00 28.50 O ANISOU 1469 O ILE A 201 3341 2950 4539 1301 -655 -346 O ATOM 1470 CB ILE A 201 191.282 18.594 539.009 1.00 27.94 C ANISOU 1470 CB ILE A 201 3138 2646 4831 978 -857 -365 C ATOM 1471 CG1 ILE A 201 192.470 18.334 538.081 1.00 28.23 C ANISOU 1471 CG1 ILE A 201 3100 2616 5010 941 -753 -222 C ATOM 1472 CG2 ILE A 201 191.755 19.144 540.347 1.00 29.62 C ANISOU 1472 CG2 ILE A 201 3298 2915 5040 1075 -1072 -479 C ATOM 1473 CD1 ILE A 201 193.249 19.575 537.723 1.00 29.15 C ANISOU 1473 CD1 ILE A 201 3102 2625 5348 824 -953 -261 C ATOM 1474 N MET A 202 188.272 18.105 539.925 1.00 37.45 N ANISOU 1474 N MET A 202 4488 4019 5724 1042 -786 -624 N ATOM 1475 CA MET A 202 187.198 18.299 540.896 1.00 37.87 C ANISOU 1475 CA MET A 202 4537 4203 5649 1111 -869 -842 C ATOM 1476 C MET A 202 186.552 16.979 541.298 1.00 37.80 C ANISOU 1476 C MET A 202 4594 4218 5551 1211 -527 -707 C ATOM 1477 O MET A 202 186.096 16.837 542.438 1.00 39.63 O ANISOU 1477 O MET A 202 4804 4588 5664 1382 -584 -875 O ATOM 1478 CB MET A 202 186.143 19.252 540.334 1.00 37.58 C ANISOU 1478 CB MET A 202 4442 4191 5647 986 -1109 -1116 C ATOM 1479 CG MET A 202 186.693 20.597 539.895 1.00 38.20 C ANISOU 1479 CG MET A 202 4467 4154 5893 878 -1447 -1234 C ATOM 1480 SD MET A 202 185.416 21.705 539.268 0.66 38.73 S ANISOU 1480 SD MET A 202 4481 4243 5994 808 -1580 -1340 S ATOM 1481 CE MET A 202 184.567 20.633 538.113 1.00 37.31 C ANISOU 1481 CE MET A 202 4288 4102 5786 783 -1463 -1290 C ATOM 1482 N THR A 203 186.502 16.009 540.382 1.00 30.70 N ANISOU 1482 N THR A 203 3761 3190 4713 1160 -255 -524 N ATOM 1483 CA THR A 203 185.925 14.709 540.711 1.00 31.14 C ANISOU 1483 CA THR A 203 3897 3170 4765 1234 101 -400 C ATOM 1484 C THR A 203 186.801 13.952 541.701 1.00 33.36 C ANISOU 1484 C THR A 203 4138 3377 5162 1427 91 -210 C ATOM 1485 O THR A 203 186.295 13.371 542.669 1.00 36.03 O ANISOU 1485 O THR A 203 4550 3757 5383 1644 84 -284 O ATOM 1486 CB THR A 203 185.725 13.888 539.437 1.00 30.46 C ANISOU 1486 CB THR A 203 3930 3008 4637 1179 254 -335 C ATOM 1487 OG1 THR A 203 184.858 14.597 538.544 1.00 29.61 O ANISOU 1487 OG1 THR A 203 3740 2949 4561 1009 123 -554 O ATOM 1488 CG2 THR A 203 185.112 12.534 539.763 1.00 31.42 C ANISOU 1488 CG2 THR A 203 4153 3156 4628 1263 235 -423 C ATOM 1489 N VAL A 204 188.116 13.943 541.474 1.00 26.25 N ANISOU 1489 N VAL A 204 3199 2456 4318 1415 40 20 N ATOM 1490 CA VAL A 204 189.023 13.277 542.403 1.00 28.97 C ANISOU 1490 CA VAL A 204 3495 2736 4777 1575 -128 202 C ATOM 1491 C VAL A 204 189.050 14.011 543.738 1.00 31.16 C ANISOU 1491 C VAL A 204 3835 3277 4728 1838 -438 83 C ATOM 1492 O VAL A 204 189.110 13.387 544.804 1.00 34.55 O ANISOU 1492 O VAL A 204 4417 3813 4899 2127 -530 255 O ATOM 1493 CB VAL A 204 190.429 13.164 541.787 1.00 28.73 C ANISOU 1493 CB VAL A 204 3452 2753 4712 1520 -28 393 C ATOM 1494 CG1 VAL A 204 191.385 12.482 542.755 1.00 32.01 C ANISOU 1494 CG1 VAL A 204 3771 3073 5317 1635 -251 578 C ATOM 1495 CG2 VAL A 204 190.367 12.405 540.472 1.00 27.90 C ANISOU 1495 CG2 VAL A 204 3644 2635 4320 1574 -104 144 C ATOM 1496 N LEU A 205 188.997 15.345 543.703 1.00 30.67 N ANISOU 1496 N LEU A 205 3688 3371 4593 1752 -616 -195 N ATOM 1497 CA LEU A 205 188.972 16.112 544.944 1.00 33.06 C ANISOU 1497 CA LEU A 205 3957 3972 4631 1962 -941 -446 C ATOM 1498 C LEU A 205 187.726 15.794 545.762 1.00 35.36 C ANISOU 1498 C LEU A 205 4302 4556 4576 2247 -917 -648 C ATOM 1499 O LEU A 205 187.813 15.588 546.978 1.00 41.98 O ANISOU 1499 O LEU A 205 5175 5775 4999 2466 -1021 -585 O ATOM 1500 CB LEU A 205 189.057 17.609 544.641 1.00 31.82 C ANISOU 1500 CB LEU A 205 3696 3827 4567 1763 -1143 -764 C ATOM 1501 CG LEU A 205 190.456 18.134 544.300 1.00 31.66 C ANISOU 1501 CG LEU A 205 3607 3687 4735 1642 -1212 -638 C ATOM 1502 CD1 LEU A 205 190.414 19.613 543.949 1.00 31.07 C ANISOU 1502 CD1 LEU A 205 3488 3539 4780 1471 -1416 -942 C ATOM 1503 CD2 LEU A 205 191.423 17.881 545.449 1.00 34.81 C ANISOU 1503 CD2 LEU A 205 3956 4239 5033 1860 -1374 -561 C ATOM 1504 N TYR A 206 186.558 15.738 545.112 1.00 29.75 N ANISOU 1504 N TYR A 206 3596 3765 3944 2101 -686 -858 N ATOM 1505 CA TYR A 206 185.347 15.353 545.830 1.00 32.07 C ANISOU 1505 CA TYR A 206 3927 4394 3866 2068 -431 -1044 C ATOM 1506 C TYR A 206 185.424 13.917 546.328 1.00 38.48 C ANISOU 1506 C TYR A 206 4992 5201 4428 1981 -89 -498 C ATOM 1507 O TYR A 206 184.875 13.601 547.390 1.00 46.54 O ANISOU 1507 O TYR A 206 6091 6632 4960 1877 76 -450 O ATOM 1508 CB TYR A 206 184.109 15.527 544.948 1.00 29.91 C ANISOU 1508 CB TYR A 206 3578 3986 3798 1883 -241 -1414 C ATOM 1509 CG TYR A 206 182.842 15.077 545.642 1.00 32.72 C ANISOU 1509 CG TYR A 206 3930 4706 3795 1715 110 -1640 C ATOM 1510 CD1 TYR A 206 182.208 15.896 546.565 1.00 35.25 C ANISOU 1510 CD1 TYR A 206 4058 5533 3802 1696 -23 -2122 C ATOM 1511 CD2 TYR A 206 182.294 13.822 545.396 1.00 33.46 C ANISOU 1511 CD2 TYR A 206 4180 4644 3890 1511 582 -1366 C ATOM 1512 CE1 TYR A 206 181.059 15.488 547.215 1.00 38.50 C ANISOU 1512 CE1 TYR A 206 4430 6322 3876 1447 334 -2304 C ATOM 1513 CE2 TYR A 206 181.144 13.404 546.043 1.00 36.70 C ANISOU 1513 CE2 TYR A 206 4568 5396 3982 1270 950 -1546 C ATOM 1514 CZ TYR A 206 180.531 14.243 546.951 1.00 39.25 C ANISOU 1514 CZ TYR A 206 4690 6288 3935 1248 852 -2049 C ATOM 1515 OH TYR A 206 179.386 13.840 547.602 1.00 43.09 O ANISOU 1515 OH TYR A 206 5117 7170 4087 956 1254 -2253 O ATOM 1516 N TRP A 207 186.091 13.038 545.577 1.00 34.24 N ANISOU 1516 N TRP A 207 4577 4209 4226 2008 15 -92 N ATOM 1517 CA TRP A 207 186.232 11.651 546.007 1.00 42.08 C ANISOU 1517 CA TRP A 207 5815 5074 5098 1949 267 453 C ATOM 1518 C TRP A 207 186.968 11.567 547.338 1.00 49.54 C ANISOU 1518 C TRP A 207 6887 6341 5595 2100 30 780 C ATOM 1519 O TRP A 207 186.644 10.727 548.185 1.00 57.82 O ANISOU 1519 O TRP A 207 8167 7539 6264 1984 227 1163 O ATOM 1520 CB TRP A 207 186.958 10.846 544.930 1.00 34.83 C ANISOU 1520 CB TRP A 207 4923 3601 4708 2015 321 714 C ATOM 1521 CG TRP A 207 186.822 9.360 545.069 1.00 39.31 C ANISOU 1521 CG TRP A 207 5710 3880 5347 1918 610 1182 C ATOM 1522 CD1 TRP A 207 186.049 8.682 545.968 1.00 49.65 C ANISOU 1522 CD1 TRP A 207 7224 5345 6295 1718 873 1445 C ATOM 1523 CD2 TRP A 207 187.481 8.366 544.277 1.00 37.73 C ANISOU 1523 CD2 TRP A 207 5503 3209 5624 1938 633 1385 C ATOM 1524 NE1 TRP A 207 186.188 7.327 545.784 1.00 48.22 N ANISOU 1524 NE1 TRP A 207 7217 4699 6404 1663 1057 1897 N ATOM 1525 CE2 TRP A 207 187.062 7.108 544.751 1.00 41.93 C ANISOU 1525 CE2 TRP A 207 6284 3489 6160 1851 904 1845 C ATOM 1526 CE3 TRP A 207 188.385 8.420 543.211 1.00 34.99 C ANISOU 1526 CE3 TRP A 207 4907 2830 5559 1783 350 1050 C ATOM 1527 CZ2 TRP A 207 187.518 5.912 544.197 1.00 43.37 C ANISOU 1527 CZ2 TRP A 207 6401 3376 6702 1695 840 1878 C ATOM 1528 CZ3 TRP A 207 188.836 7.233 542.662 1.00 36.36 C ANISOU 1528 CZ3 TRP A 207 5079 2772 5963 1691 342 1107 C ATOM 1529 CH2 TRP A 207 188.401 5.996 543.155 1.00 40.45 C ANISOU 1529 CH2 TRP A 207 5780 3022 6567 1670 558 1482 C ATOM 1530 N HIS A 208 187.955 12.441 547.545 1.00 40.42 N ANISOU 1530 N HIS A 208 5583 5306 4469 2346 -402 637 N ATOM 1531 CA HIS A 208 188.655 12.486 548.822 1.00 44.81 C ANISOU 1531 CA HIS A 208 6216 6235 4575 2536 -693 848 C ATOM 1532 C HIS A 208 187.849 13.216 549.888 1.00 48.70 C ANISOU 1532 C HIS A 208 6636 7398 4470 2460 -707 500 C ATOM 1533 O HIS A 208 188.045 12.968 551.082 1.00 53.07 O ANISOU 1533 O HIS A 208 7329 8385 4452 2527 -801 740 O ATOM 1534 CB HIS A 208 190.022 13.150 548.651 1.00 43.58 C ANISOU 1534 CB HIS A 208 5866 5969 4724 2827 -1151 742 C ATOM 1535 CG HIS A 208 190.932 12.422 547.712 1.00 41.94 C ANISOU 1535 CG HIS A 208 5632 5202 5102 2698 -1078 967 C ATOM 1536 ND1 HIS A 208 191.374 11.138 547.949 1.00 45.10 N ANISOU 1536 ND1 HIS A 208 6228 5369 5539 2709 -1035 1439 N ATOM 1537 CD2 HIS A 208 191.488 12.798 546.536 1.00 38.14 C ANISOU 1537 CD2 HIS A 208 4891 4418 5181 2414 -1010 752 C ATOM 1538 CE1 HIS A 208 192.157 10.753 546.958 1.00 43.13 C ANISOU 1538 CE1 HIS A 208 5777 4720 5891 2499 -1013 1381 C ATOM 1539 NE2 HIS A 208 192.244 11.743 546.087 1.00 38.93 N ANISOU 1539 NE2 HIS A 208 4968 4192 5633 2318 -951 1016 N ATOM 1540 N ILE A 209 186.947 14.112 549.482 1.00 52.94 N ANISOU 1540 N ILE A 209 6944 8055 5117 2336 -639 -88 N ATOM 1541 CA ILE A 209 186.100 14.806 550.447 1.00 54.52 C ANISOU 1541 CA ILE A 209 6997 8916 4800 2263 -641 -549 C ATOM 1542 C ILE A 209 185.091 13.842 551.058 1.00 58.07 C ANISOU 1542 C ILE A 209 7660 9663 4740 1963 -151 -293 C ATOM 1543 O ILE A 209 184.944 13.765 552.284 1.00 61.03 O ANISOU 1543 O ILE A 209 8099 10657 4433 1923 -127 -222 O ATOM 1544 CB ILE A 209 185.397 16.005 549.787 1.00 47.41 C ANISOU 1544 CB ILE A 209 5773 7981 4259 2237 -758 -1284 C ATOM 1545 CG1 ILE A 209 186.419 17.057 549.364 1.00 41.90 C ANISOU 1545 CG1 ILE A 209 4868 7035 4016 2487 -1263 -1501 C ATOM 1546 CG2 ILE A 209 184.378 16.612 550.739 1.00 47.98 C ANISOU 1546 CG2 ILE A 209 5639 8743 3848 2147 -717 -1861 C ATOM 1547 CD1 ILE A 209 187.247 17.561 550.503 1.00 45.48 C ANISOU 1547 CD1 ILE A 209 5208 7925 4148 2722 -1649 -1591 C ATOM 1548 N SER A 210 184.377 13.095 550.212 1.00 49.83 N ANISOU 1548 N SER A 210 6716 8211 4007 1725 257 -162 N ATOM 1549 CA SER A 210 183.357 12.181 550.714 1.00 53.97 C ANISOU 1549 CA SER A 210 7408 8960 4137 1376 769 57 C ATOM 1550 C SER A 210 183.966 11.000 551.459 1.00 59.02 C ANISOU 1550 C SER A 210 8440 9557 4427 1344 850 907 C ATOM 1551 O SER A 210 183.317 10.430 552.343 1.00 64.68 O ANISOU 1551 O SER A 210 9327 10677 4571 1062 1181 1166 O ATOM 1552 CB SER A 210 182.477 11.691 549.564 1.00 50.73 C ANISOU 1552 CB SER A 210 6960 8075 4240 1151 1149 -78 C ATOM 1553 OG SER A 210 183.240 10.989 548.600 1.00 47.72 O ANISOU 1553 OG SER A 210 6724 6995 4413 1267 1105 341 O ATOM 1554 N ARG A 211 185.199 10.614 551.120 1.00 99.87 N ANISOU 1554 N ARG A 211 13756 14249 9939 1618 544 1347 N ATOM 1555 CA ARG A 211 185.860 9.540 551.852 1.00103.25 C ANISOU 1555 CA ARG A 211 14560 14587 10084 1659 496 2147 C ATOM 1556 C ARG A 211 186.357 10.003 553.216 1.00105.88 C ANISOU 1556 C ARG A 211 14952 15613 9664 1832 169 2227 C ATOM 1557 O ARG A 211 186.407 9.202 554.156 1.00109.82 O ANISOU 1557 O ARG A 211 15795 16322 9611 1740 235 2852 O ATOM 1558 CB ARG A 211 187.014 8.963 551.029 1.00 99.82 C ANISOU 1558 CB ARG A 211 14196 13417 10312 1927 241 2489 C ATOM 1559 CG ARG A 211 186.557 8.002 549.941 1.00 97.63 C ANISOU 1559 CG ARG A 211 13974 12472 10648 1729 609 2641 C ATOM 1560 CD ARG A 211 187.709 7.186 549.373 1.00 92.60 C ANISOU 1560 CD ARG A 211 13429 11178 10577 1984 369 3042 C ATOM 1561 NE ARG A 211 188.184 7.707 548.095 1.00 85.11 N ANISOU 1561 NE ARG A 211 12171 9912 10256 2144 252 2585 N ATOM 1562 CZ ARG A 211 189.311 8.392 547.935 1.00 79.59 C ANISOU 1562 CZ ARG A 211 11290 9234 9716 2452 -165 2408 C ATOM 1563 NH1 ARG A 211 190.092 8.641 548.977 1.00 81.64 N ANISOU 1563 NH1 ARG A 211 11613 9805 9602 2656 -545 2573 N ATOM 1564 NH2 ARG A 211 189.660 8.822 546.730 1.00 71.48 N ANISOU 1564 NH2 ARG A 211 9959 7978 9223 2406 -206 1957 N ATOM 1565 N ALA A 212 186.723 11.280 553.345 1.00 65.85 N ANISOU 1565 N ALA A 212 9556 10903 4563 2079 -203 1612 N ATOM 1566 CA ALA A 212 187.051 11.817 554.661 1.00 71.02 C ANISOU 1566 CA ALA A 212 10187 12322 4474 2240 -502 1526 C ATOM 1567 C ALA A 212 185.806 11.964 555.525 1.00 75.60 C ANISOU 1567 C ALA A 212 10735 13681 4308 1900 -122 1283 C ATOM 1568 O ALA A 212 185.883 11.826 556.751 1.00 82.43 O ANISOU 1568 O ALA A 212 11754 15219 4345 1893 -178 1522 O ATOM 1569 CB ALA A 212 187.765 13.161 554.520 1.00 67.54 C ANISOU 1569 CB ALA A 212 9348 11998 4317 2584 -1009 860 C ATOM 1570 N SER A 213 184.655 12.244 554.908 1.00 95.98 N ANISOU 1570 N SER A 213 13098 16227 7143 1617 258 780 N ATOM 1571 CA SER A 213 183.402 12.305 555.650 1.00 96.36 C ANISOU 1571 CA SER A 213 13060 17007 6545 1247 687 482 C ATOM 1572 C SER A 213 182.883 10.916 555.997 1.00101.20 C ANISOU 1572 C SER A 213 14093 17566 6794 836 1214 1273 C ATOM 1573 O SER A 213 182.139 10.760 556.971 1.00105.96 O ANISOU 1573 O SER A 213 14739 18781 6740 494 1527 1264 O ATOM 1574 CB SER A 213 182.351 13.071 554.843 1.00 90.24 C ANISOU 1574 CB SER A 213 11875 16173 6240 1115 865 -382 C ATOM 1575 OG SER A 213 182.828 14.351 554.461 1.00 85.57 O ANISOU 1575 OG SER A 213 10927 15515 6068 1471 349 -1045 O ATOM 1576 N LYS A 214 183.264 9.907 555.220 1.00120.97 N ANISOU 1576 N LYS A 214 13760 21123 11079 1091 1254 669 N ATOM 1577 CA LYS A 214 182.830 8.535 555.457 1.00116.51 C ANISOU 1577 CA LYS A 214 13626 20372 10270 1563 1351 767 C ATOM 1578 C LYS A 214 183.932 7.718 556.122 1.00121.25 C ANISOU 1578 C LYS A 214 14000 21274 10794 2250 1343 492 C ATOM 1579 O LYS A 214 184.159 7.828 557.327 1.00123.17 O ANISOU 1579 O LYS A 214 14093 21653 11052 2694 1073 382 O ATOM 1580 CB LYS A 214 182.406 7.878 554.142 1.00112.28 C ANISOU 1580 CB LYS A 214 13431 19655 9574 1232 1697 925 C ATOM 1581 CG LYS A 214 182.343 6.361 554.191 1.00109.77 C ANISOU 1581 CG LYS A 214 13510 19196 9000 1691 1932 923 C ATOM 1582 CD LYS A 214 182.020 5.784 552.823 1.00106.41 C ANISOU 1582 CD LYS A 214 13369 18642 8419 1279 2306 1023 C ATOM 1583 CE LYS A 214 182.173 4.273 552.808 1.00105.92 C ANISOU 1583 CE LYS A 214 13688 18442 8115 1726 2624 962 C ATOM 1584 NZ LYS A 214 181.301 3.616 553.819 1.00104.30 N ANISOU 1584 NZ LYS A 214 13969 17916 7743 2111 2565 1076 N ATOM 1585 N ALA A1001 184.097 12.142 565.212 1.00130.93 N ANISOU 1585 N ALA A1001 13814 23481 12452 3618 -973 -367 N ATOM 1586 CA ALA A1001 183.650 11.279 564.125 1.00128.69 C ANISOU 1586 CA ALA A1001 13955 22857 12085 3586 -691 -93 C ATOM 1587 C ALA A1001 182.220 10.803 564.364 1.00119.96 C ANISOU 1587 C ALA A1001 13547 21159 10873 3637 -667 273 C ATOM 1588 O ALA A1001 181.304 11.173 563.628 1.00116.34 O ANISOU 1588 O ALA A1001 13351 20325 10528 3130 -533 511 O ATOM 1589 CB ALA A1001 184.589 10.090 563.972 1.00132.34 C ANISOU 1589 CB ALA A1001 14325 23640 12319 4198 -600 -223 C ATOM 1590 N ASP A1002 182.039 9.983 565.403 1.00142.48 N ANISOU 1590 N ASP A1002 16695 23956 13484 4258 -791 302 N ATOM 1591 CA ASP A1002 180.729 9.450 565.760 1.00134.63 C ANISOU 1591 CA ASP A1002 16369 22428 12355 4327 -742 587 C ATOM 1592 C ASP A1002 179.919 10.401 566.630 1.00131.10 C ANISOU 1592 C ASP A1002 15959 21804 12051 4084 -965 625 C ATOM 1593 O ASP A1002 178.683 10.351 566.605 1.00125.16 O ANISOU 1593 O ASP A1002 15655 20607 11294 3867 -895 856 O ATOM 1594 CB ASP A1002 180.883 8.112 566.491 1.00133.18 C ANISOU 1594 CB ASP A1002 16583 22202 11818 5103 -715 608 C ATOM 1595 CG ASP A1002 179.548 7.478 566.840 1.00125.46 C ANISOU 1595 CG ASP A1002 16339 20657 10671 5133 -592 860 C ATOM 1596 OD1 ASP A1002 178.826 7.070 565.910 1.00121.83 O ANISOU 1596 OD1 ASP A1002 16228 19867 10193 4798 -309 1035 O ATOM 1597 OD2 ASP A1002 179.222 7.387 568.043 1.00123.04 O ANISOU 1597 OD2 ASP A1002 16256 20262 10233 5467 -766 860 O ATOM 1598 N LEU A1003 180.585 11.256 567.410 1.00147.25 N ANISOU 1598 N LEU A1003 17528 24211 14212 4106 -1218 376 N ATOM 1599 CA LEU A1003 179.858 12.176 568.277 1.00144.30 C ANISOU 1599 CA LEU A1003 17190 23661 13975 3878 -1407 388 C ATOM 1600 C LEU A1003 179.109 13.230 567.475 1.00143.75 C ANISOU 1600 C LEU A1003 17120 23296 14202 3166 -1300 541 C ATOM 1601 O LEU A1003 178.018 13.655 567.875 1.00139.32 O ANISOU 1601 O LEU A1003 16838 22379 13718 2982 -1349 698 O ATOM 1602 CB LEU A1003 180.820 12.844 569.259 1.00148.50 C ANISOU 1602 CB LEU A1003 17190 24693 14541 4029 -1671 39 C ATOM 1603 CG LEU A1003 181.469 11.934 570.302 1.00148.52 C ANISOU 1603 CG LEU A1003 17192 25031 14210 4810 -1856 -104 C ATOM 1604 CD1 LEU A1003 182.456 12.714 571.155 1.00152.65 C ANISOU 1604 CD1 LEU A1003 17080 26157 14761 4869 -2124 -496 C ATOM 1605 CD2 LEU A1003 180.403 11.291 571.169 1.00141.95 C ANISOU 1605 CD2 LEU A1003 17011 23754 13168 5131 -1895 124 C ATOM 1606 N GLU A1004 179.671 13.660 566.343 1.00145.06 N ANISOU 1606 N GLU A1004 16992 23606 14519 2784 -1143 501 N ATOM 1607 CA GLU A1004 179.016 14.680 565.533 1.00145.22 C ANISOU 1607 CA GLU A1004 17047 23348 14783 2157 -1029 673 C ATOM 1608 C GLU A1004 177.782 14.130 564.828 1.00138.88 C ANISOU 1608 C GLU A1004 16752 22126 13890 2050 -881 1026 C ATOM 1609 O GLU A1004 176.845 14.884 564.546 1.00136.65 O ANISOU 1609 O GLU A1004 16617 21556 13749 1684 -866 1223 O ATOM 1610 CB GLU A1004 180.002 15.250 564.514 1.00152.46 C ANISOU 1610 CB GLU A1004 17554 24530 15843 1780 -870 525 C ATOM 1611 CG GLU A1004 181.377 15.571 565.085 1.00158.94 C ANISOU 1611 CG GLU A1004 17803 25891 16696 1897 -973 98 C ATOM 1612 CD GLU A1004 181.338 16.650 566.149 1.00159.78 C ANISOU 1612 CD GLU A1004 17717 26038 16955 1744 -1151 -87 C ATOM 1613 OE1 GLU A1004 180.501 17.571 566.037 1.00159.09 O ANISOU 1613 OE1 GLU A1004 17829 25562 17057 1333 -1102 90 O ATOM 1614 OE2 GLU A1004 182.143 16.576 567.101 1.00161.14 O ANISOU 1614 OE2 GLU A1004 17536 26648 17040 2051 -1336 -415 O ATOM 1615 N ASP A1005 177.761 12.826 564.541 1.00115.29 N ANISOU 1615 N ASP A1005 14036 19117 10653 2369 -756 1093 N ATOM 1616 CA ASP A1005 176.629 12.230 563.842 1.00109.27 C ANISOU 1616 CA ASP A1005 13732 18018 9767 2220 -580 1367 C ATOM 1617 C ASP A1005 175.415 12.067 564.747 1.00102.99 C ANISOU 1617 C ASP A1005 13323 16912 8896 2337 -674 1478 C ATOM 1618 O ASP A1005 174.278 12.164 564.273 1.00 98.54 O ANISOU 1618 O ASP A1005 13009 16101 8330 2046 -595 1679 O ATOM 1619 CB ASP A1005 177.034 10.879 563.251 1.00108.79 C ANISOU 1619 CB ASP A1005 13868 18013 9455 2484 -353 1362 C ATOM 1620 CG ASP A1005 177.790 11.018 561.942 1.00113.34 C ANISOU 1620 CG ASP A1005 14173 18790 10100 2187 -172 1336 C ATOM 1621 OD1 ASP A1005 177.147 11.308 560.911 1.00110.27 O ANISOU 1621 OD1 ASP A1005 13895 18255 9745 1737 -37 1526 O ATOM 1622 OD2 ASP A1005 179.029 10.854 561.947 1.00120.09 O ANISOU 1622 OD2 ASP A1005 14691 19979 10960 2408 -166 1114 O ATOM 1623 N ASN A1006 175.628 11.819 566.041 1.00128.45 N ANISOU 1623 N ASN A1006 16592 20176 12038 2757 -839 1338 N ATOM 1624 CA ASN A1006 174.502 11.685 566.959 1.00122.97 C ANISOU 1624 CA ASN A1006 16273 19182 11270 2847 -909 1416 C ATOM 1625 C ASN A1006 173.930 13.043 567.344 1.00123.29 C ANISOU 1625 C ASN A1006 16132 19127 11587 2514 -1080 1439 C ATOM 1626 O ASN A1006 172.711 13.190 567.480 1.00118.99 O ANISOU 1626 O ASN A1006 15850 18303 11058 2350 -1067 1576 O ATOM 1627 CB ASN A1006 174.929 10.915 568.209 1.00122.44 C ANISOU 1627 CB ASN A1006 16376 19172 10974 3435 -1009 1275 C ATOM 1628 CG ASN A1006 175.231 9.457 567.922 1.00121.46 C ANISOU 1628 CG ASN A1006 16604 19011 10532 3825 -783 1300 C ATOM 1629 OD1 ASN A1006 176.341 8.982 568.164 1.00125.24 O ANISOU 1629 OD1 ASN A1006 16932 19766 10887 4273 -822 1166 O ATOM 1630 ND2 ASN A1006 174.241 8.738 567.407 1.00116.69 N ANISOU 1630 ND2 ASN A1006 16472 18083 9783 3663 -527 1452 N ATOM 1631 N TRP A1007 174.794 14.046 567.522 1.00 89.89 N ANISOU 1631 N TRP A1007 11452 15130 7571 2401 -1213 1282 N ATOM 1632 CA TRP A1007 174.318 15.368 567.915 1.00 91.05 C ANISOU 1632 CA TRP A1007 11464 15147 7984 2090 -1327 1287 C ATOM 1633 C TRP A1007 173.639 16.090 566.759 1.00 91.24 C ANISOU 1633 C TRP A1007 11510 14980 8175 1628 -1198 1523 C ATOM 1634 O TRP A1007 172.728 16.895 566.982 1.00 89.94 O ANISOU 1634 O TRP A1007 11434 14576 8164 1438 -1243 1637 O ATOM 1635 CB TRP A1007 175.478 16.201 568.461 1.00 97.32 C ANISOU 1635 CB TRP A1007 11795 16254 8929 2064 -1455 1002 C ATOM 1636 CG TRP A1007 175.052 17.504 569.062 1.00 98.88 C ANISOU 1636 CG TRP A1007 11900 16290 9378 1779 -1539 962 C ATOM 1637 CD1 TRP A1007 175.361 18.754 568.613 1.00104.45 C ANISOU 1637 CD1 TRP A1007 12352 16986 10347 1347 -1463 918 C ATOM 1638 CD2 TRP A1007 174.231 17.685 570.221 1.00 95.37 C ANISOU 1638 CD2 TRP A1007 11661 15634 8940 1896 -1673 955 C ATOM 1639 NE1 TRP A1007 174.787 19.704 569.424 1.00104.72 N ANISOU 1639 NE1 TRP A1007 12427 16804 10557 1206 -1532 887 N ATOM 1640 CE2 TRP A1007 174.087 19.072 570.419 1.00 99.13 C ANISOU 1640 CE2 TRP A1007 11977 15985 9702 1535 -1674 905 C ATOM 1641 CE3 TRP A1007 173.604 16.808 571.113 1.00 89.85 C ANISOU 1641 CE3 TRP A1007 11301 14816 8022 2258 -1757 978 C ATOM 1642 CZ2 TRP A1007 173.343 19.603 571.470 1.00 97.53 C ANISOU 1642 CZ2 TRP A1007 11905 15562 9588 1534 -1771 872 C ATOM 1643 CZ3 TRP A1007 172.866 17.337 572.155 1.00 88.16 C ANISOU 1643 CZ3 TRP A1007 11212 14396 7887 2237 -1860 941 C ATOM 1644 CH2 TRP A1007 172.742 18.721 572.325 1.00 91.94 C ANISOU 1644 CH2 TRP A1007 11491 14775 8669 1882 -1875 886 C ATOM 1645 N GLU A1008 174.065 15.820 565.522 1.00122.62 N ANISOU 1645 N GLU A1008 15417 19066 12107 1471 -1034 1602 N ATOM 1646 CA GLU A1008 173.419 16.440 564.370 1.00122.41 C ANISOU 1646 CA GLU A1008 15447 18886 12177 1073 -915 1851 C ATOM 1647 C GLU A1008 172.045 15.831 564.118 1.00115.40 C ANISOU 1647 C GLU A1008 14926 17793 11126 1079 -871 2071 C ATOM 1648 O GLU A1008 171.107 16.539 563.733 1.00113.97 O ANISOU 1648 O GLU A1008 14815 17454 11035 853 -878 2270 O ATOM 1649 CB GLU A1008 174.307 16.300 563.133 1.00126.20 C ANISOU 1649 CB GLU A1008 15756 19565 12628 887 -741 1851 C ATOM 1650 CG GLU A1008 173.776 17.009 561.898 1.00126.40 C ANISOU 1650 CG GLU A1008 15842 19464 12720 484 -618 2115 C ATOM 1651 CD GLU A1008 174.688 16.845 560.697 1.00130.11 C ANISOU 1651 CD GLU A1008 16165 20127 13142 279 -426 2096 C ATOM 1652 OE1 GLU A1008 175.619 16.016 560.766 1.00131.92 O ANISOU 1652 OE1 GLU A1008 16261 20590 13272 479 -377 1888 O ATOM 1653 OE2 GLU A1008 174.475 17.547 559.686 1.00131.26 O ANISOU 1653 OE2 GLU A1008 16343 20194 13337 -61 -315 2293 O ATOM 1654 N THR A1009 171.908 14.520 564.331 1.00103.86 N ANISOU 1654 N THR A1009 13708 16345 9407 1342 -805 2022 N ATOM 1655 CA THR A1009 170.613 13.871 564.155 1.00 97.73 C ANISOU 1655 CA THR A1009 13280 15406 8449 1299 -721 2157 C ATOM 1656 C THR A1009 169.599 14.383 565.171 1.00 95.34 C ANISOU 1656 C THR A1009 13082 14906 8238 1333 -866 2163 C ATOM 1657 O THR A1009 168.422 14.576 564.845 1.00 92.33 O ANISOU 1657 O THR A1009 12813 14430 7838 1150 -847 2304 O ATOM 1658 CB THR A1009 170.770 12.353 564.267 1.00 94.90 C ANISOU 1658 CB THR A1009 13221 15051 7786 1563 -555 2063 C ATOM 1659 OG1 THR A1009 171.695 11.891 563.275 1.00 97.41 O ANISOU 1659 OG1 THR A1009 13433 15547 8029 1530 -398 2052 O ATOM 1660 CG2 THR A1009 169.434 11.654 564.066 1.00 89.21 C ANISOU 1660 CG2 THR A1009 12865 14178 6853 1438 -409 2142 C ATOM 1661 N LEU A1010 170.043 14.618 566.409 1.00 77.56 N ANISOU 1661 N LEU A1010 10769 12628 6072 1569 -1014 1995 N ATOM 1662 CA LEU A1010 169.141 15.122 567.440 1.00 75.68 C ANISOU 1662 CA LEU A1010 10630 12195 5928 1595 -1138 1974 C ATOM 1663 C LEU A1010 168.665 16.533 567.117 1.00 78.13 C ANISOU 1663 C LEU A1010 10746 12419 6522 1311 -1208 2111 C ATOM 1664 O LEU A1010 167.491 16.861 567.325 1.00 75.71 O ANISOU 1664 O LEU A1010 10554 11954 6257 1240 -1234 2199 O ATOM 1665 CB LEU A1010 169.837 15.080 568.802 1.00 77.09 C ANISOU 1665 CB LEU A1010 10775 12408 6110 1903 -1281 1752 C ATOM 1666 CG LEU A1010 169.062 15.510 570.051 1.00 75.42 C ANISOU 1666 CG LEU A1010 10683 12002 5970 1963 -1403 1680 C ATOM 1667 CD1 LEU A1010 169.445 14.628 571.225 1.00 75.36 C ANISOU 1667 CD1 LEU A1010 10889 12015 5731 2359 -1455 1503 C ATOM 1668 CD2 LEU A1010 169.317 16.973 570.388 1.00 80.02 C ANISOU 1668 CD2 LEU A1010 10953 12575 6877 1782 -1533 1633 C ATOM 1669 N ASN A1011 169.560 17.382 566.606 1.00 82.27 N ANISOU 1669 N ASN A1011 10991 13037 7232 1155 -1211 2119 N ATOM 1670 CA ASN A1011 169.183 18.760 566.308 1.00 85.43 C ANISOU 1670 CA ASN A1011 11279 13292 7887 909 -1226 2261 C ATOM 1671 C ASN A1011 168.316 18.842 565.058 1.00 83.10 C ANISOU 1671 C ASN A1011 11080 12972 7523 730 -1138 2549 C ATOM 1672 O ASN A1011 167.412 19.682 564.979 1.00 83.00 O ANISOU 1672 O ASN A1011 11103 12802 7630 654 -1170 2716 O ATOM 1673 CB ASN A1011 170.434 19.623 566.152 1.00 92.60 C ANISOU 1673 CB ASN A1011 11908 14289 8986 751 -1196 2148 C ATOM 1674 CG ASN A1011 171.215 19.754 567.444 1.00 95.31 C ANISOU 1674 CG ASN A1011 12093 14722 9400 900 -1310 1836 C ATOM 1675 OD1 ASN A1011 170.636 19.845 568.527 1.00 93.24 O ANISOU 1675 OD1 ASN A1011 11934 14327 9166 1036 -1420 1763 O ATOM 1676 ND2 ASN A1011 172.538 19.762 567.337 1.00100.06 N ANISOU 1676 ND2 ASN A1011 12421 15588 10011 869 -1284 1629 N ATOM 1677 N ASP A1012 168.575 17.982 564.071 1.00 93.00 N ANISOU 1677 N ASP A1012 12370 14398 8566 679 -1025 2607 N ATOM 1678 CA ASP A1012 167.787 18.016 562.843 1.00 90.58 C ANISOU 1678 CA ASP A1012 12135 14139 8143 499 -950 2864 C ATOM 1679 C ASP A1012 166.361 17.539 563.087 1.00 85.12 C ANISOU 1679 C ASP A1012 11617 13425 7301 559 -986 2910 C ATOM 1680 O ASP A1012 165.405 18.152 562.597 1.00 84.14 O ANISOU 1680 O ASP A1012 11484 13297 7187 477 -1024 3109 O ATOM 1681 CB ASP A1012 168.461 17.174 561.760 1.00 90.30 C ANISOU 1681 CB ASP A1012 12096 14309 7905 398 -797 2874 C ATOM 1682 CG ASP A1012 169.752 17.793 561.260 1.00 96.46 C ANISOU 1682 CG ASP A1012 12671 15147 8831 259 -730 2846 C ATOM 1683 OD1 ASP A1012 169.876 19.035 561.308 1.00100.72 O ANISOU 1683 OD1 ASP A1012 13117 15554 9596 139 -758 2917 O ATOM 1684 OD2 ASP A1012 170.643 17.038 560.818 1.00 97.56 O ANISOU 1684 OD2 ASP A1012 12756 15456 8855 260 -617 2735 O ATOM 1685 N ASN A1013 166.194 16.452 563.843 1.00 96.41 N ANISOU 1685 N ASN A1013 13212 14851 8568 713 -959 2718 N ATOM 1686 CA ASN A1013 164.854 15.962 564.145 1.00 92.09 C ANISOU 1686 CA ASN A1013 12836 14288 7867 718 -948 2696 C ATOM 1687 C ASN A1013 164.111 16.869 565.117 1.00 92.81 C ANISOU 1687 C ASN A1013 12888 14204 8171 798 -1094 2686 C ATOM 1688 O ASN A1013 162.878 16.811 565.177 1.00 90.41 O ANISOU 1688 O ASN A1013 12636 13926 7788 761 -1100 2701 O ATOM 1689 CB ASN A1013 164.923 14.541 564.704 1.00 89.08 C ANISOU 1689 CB ASN A1013 12726 13888 7234 842 -813 2483 C ATOM 1690 CG ASN A1013 165.297 13.519 563.649 1.00 87.76 C ANISOU 1690 CG ASN A1013 12658 13879 6809 735 -608 2493 C ATOM 1691 OD1 ASN A1013 164.430 12.948 562.987 1.00 84.89 O ANISOU 1691 OD1 ASN A1013 12403 13632 6219 546 -476 2512 O ATOM 1692 ND2 ASN A1013 166.593 13.284 563.486 1.00 90.27 N ANISOU 1692 ND2 ASN A1013 12918 14230 7149 844 -568 2453 N ATOM 1693 N LEU A1014 164.827 17.699 565.878 1.00 81.62 N ANISOU 1693 N LEU A1014 11364 12635 7013 889 -1194 2629 N ATOM 1694 CA LEU A1014 164.156 18.661 566.746 1.00 82.92 C ANISOU 1694 CA LEU A1014 11497 12609 7401 940 -1303 2622 C ATOM 1695 C LEU A1014 163.508 19.772 565.931 1.00 84.67 C ANISOU 1695 C LEU A1014 11607 12807 7757 840 -1327 2886 C ATOM 1696 O LEU A1014 162.438 20.276 566.296 1.00 84.19 O ANISOU 1696 O LEU A1014 11551 12662 7774 896 -1383 2931 O ATOM 1697 CB LEU A1014 165.147 19.239 567.756 1.00 86.86 C ANISOU 1697 CB LEU A1014 11911 12978 8113 1022 -1375 2457 C ATOM 1698 CG LEU A1014 164.561 20.158 568.829 1.00 88.50 C ANISOU 1698 CG LEU A1014 12116 12961 8547 1068 -1459 2393 C ATOM 1699 CD1 LEU A1014 163.566 19.401 569.695 1.00 84.19 C ANISOU 1699 CD1 LEU A1014 11766 12368 7854 1183 -1472 2259 C ATOM 1700 CD2 LEU A1014 165.664 20.766 569.680 1.00 93.16 C ANISOU 1700 CD2 LEU A1014 12586 13488 9321 1082 -1509 2204 C ATOM 1701 N LYS A1015 164.140 20.165 564.823 1.00106.55 N ANISOU 1701 N LYS A1015 14292 15652 10540 715 -1272 3067 N ATOM 1702 CA LYS A1015 163.542 21.164 563.945 1.00108.06 C ANISOU 1702 CA LYS A1015 14442 15819 10796 666 -1277 3362 C ATOM 1703 C LYS A1015 162.359 20.593 563.175 1.00103.65 C ANISOU 1703 C LYS A1015 13897 15517 9967 663 -1293 3488 C ATOM 1704 O LYS A1015 161.400 21.318 562.890 1.00103.97 O ANISOU 1704 O LYS A1015 13899 15570 10035 743 -1357 3680 O ATOM 1705 CB LYS A1015 164.593 21.707 562.977 1.00112.08 C ANISOU 1705 CB LYS A1015 14905 16322 11358 509 -1180 3507 C ATOM 1706 CG LYS A1015 165.844 22.247 563.652 1.00117.60 C ANISOU 1706 CG LYS A1015 15536 16852 12295 447 -1136 3321 C ATOM 1707 CD LYS A1015 166.891 22.651 562.627 1.00122.06 C ANISOU 1707 CD LYS A1015 16051 17450 12875 235 -994 3413 C ATOM 1708 CE LYS A1015 168.171 23.121 563.299 1.00128.48 C ANISOU 1708 CE LYS A1015 16736 18184 13898 128 -933 3151 C ATOM 1709 NZ LYS A1015 169.213 23.497 562.303 1.00133.65 N ANISOU 1709 NZ LYS A1015 17331 18889 14562 -127 -756 3190 N ATOM 1710 N VAL A1016 162.407 19.302 562.834 1.00 86.66 N ANISOU 1710 N VAL A1016 11798 13591 7539 579 -1221 3367 N ATOM 1711 CA VAL A1016 161.303 18.675 562.112 1.00 83.03 C ANISOU 1711 CA VAL A1016 11332 13431 6785 507 -1205 3416 C ATOM 1712 C VAL A1016 160.037 18.684 562.961 1.00 81.67 C ANISOU 1712 C VAL A1016 11150 13261 6621 609 -1275 3294 C ATOM 1713 O VAL A1016 158.927 18.866 562.446 1.00 80.94 O ANISOU 1713 O VAL A1016 10946 13412 6397 613 -1330 3392 O ATOM 1714 CB VAL A1016 161.690 17.247 561.682 1.00 80.11 C ANISOU 1714 CB VAL A1016 11071 13243 6123 359 -1047 3258 C ATOM 1715 CG1 VAL A1016 160.516 16.549 561.012 1.00 77.58 C ANISOU 1715 CG1 VAL A1016 10740 13262 5473 217 -993 3234 C ATOM 1716 CG2 VAL A1016 162.892 17.283 560.751 1.00 81.82 C ANISOU 1716 CG2 VAL A1016 11263 13492 6333 253 -968 3376 C ATOM 1717 N ILE A1017 160.184 18.496 564.275 1.00 77.40 N ANISOU 1717 N ILE A1017 10710 12485 6216 700 -1277 3065 N ATOM 1718 CA ILE A1017 159.029 18.541 565.168 1.00 76.73 C ANISOU 1718 CA ILE A1017 10627 12369 6157 775 -1319 2919 C ATOM 1719 C ILE A1017 158.421 19.938 565.181 1.00 79.70 C ANISOU 1719 C ILE A1017 10846 12662 6774 921 -1449 3120 C ATOM 1720 O ILE A1017 157.195 20.099 565.231 1.00 79.43 O ANISOU 1720 O ILE A1017 10707 12785 6687 980 -1497 3107 O ATOM 1721 CB ILE A1017 159.431 18.086 566.583 1.00 76.44 C ANISOU 1721 CB ILE A1017 10774 12072 6200 848 -1286 2647 C ATOM 1722 CG1 ILE A1017 159.904 16.633 566.562 1.00 73.41 C ANISOU 1722 CG1 ILE A1017 10611 11752 5530 770 -1124 2468 C ATOM 1723 CG2 ILE A1017 158.273 18.257 567.554 1.00 76.60 C ANISOU 1723 CG2 ILE A1017 10806 12024 6276 905 -1313 2489 C ATOM 1724 CD1 ILE A1017 160.315 16.111 567.917 1.00 72.84 C ANISOU 1724 CD1 ILE A1017 10769 11439 5466 901 -1089 2231 C ATOM 1725 N GLU A1018 159.267 20.968 565.123 1.00119.75 N ANISOU 1725 N GLU A1018 15906 17491 12104 982 -1481 3292 N ATOM 1726 CA GLU A1018 158.770 22.339 565.181 1.00123.21 C ANISOU 1726 CA GLU A1018 16277 17759 12780 1142 -1547 3492 C ATOM 1727 C GLU A1018 157.968 22.695 563.935 1.00123.13 C ANISOU 1727 C GLU A1018 16156 18027 12599 1216 -1597 3787 C ATOM 1728 O GLU A1018 156.969 23.419 564.020 1.00124.66 O ANISOU 1728 O GLU A1018 16267 18239 12861 1420 -1670 3899 O ATOM 1729 CB GLU A1018 159.936 23.310 565.366 1.00127.72 C ANISOU 1729 CB GLU A1018 16909 17986 13634 1124 -1500 3572 C ATOM 1730 CG GLU A1018 159.522 24.766 565.481 1.00132.08 C ANISOU 1730 CG GLU A1018 17478 18262 14445 1281 -1498 3774 C ATOM 1731 CD GLU A1018 160.703 25.694 565.681 1.00137.45 C ANISOU 1731 CD GLU A1018 18247 18592 15385 1179 -1384 3791 C ATOM 1732 OE1 GLU A1018 161.828 25.192 565.889 1.00137.94 O ANISOU 1732 OE1 GLU A1018 18297 18675 15441 1004 -1345 3601 O ATOM 1733 OE2 GLU A1018 160.506 26.926 565.630 1.00141.72 O ANISOU 1733 OE2 GLU A1018 18873 18848 16124 1275 -1313 3979 O ATOM 1734 N LYS A1019 158.380 22.194 562.772 1.00125.78 N ANISOU 1734 N LYS A1019 20106 16144 11540 219 -1683 1942 N ATOM 1735 CA LYS A1019 157.718 22.488 561.505 1.00126.20 C ANISOU 1735 CA LYS A1019 20383 16052 11516 2 -1930 2028 C ATOM 1736 C LYS A1019 157.055 21.246 560.912 1.00128.52 C ANISOU 1736 C LYS A1019 20462 16396 11971 -278 -2050 2204 C ATOM 1737 O LYS A1019 157.093 21.018 559.702 1.00129.65 O ANISOU 1737 O LYS A1019 20862 16362 12036 -632 -2189 2130 O ATOM 1738 CB LYS A1019 158.703 23.097 560.509 1.00125.46 C ANISOU 1738 CB LYS A1019 20797 15645 11226 -301 -1917 1765 C ATOM 1739 CG LYS A1019 159.922 22.235 560.214 1.00126.22 C ANISOU 1739 CG LYS A1019 20981 15629 11347 -640 -1706 1519 C ATOM 1740 CD LYS A1019 160.740 22.813 559.071 1.00125.93 C ANISOU 1740 CD LYS A1019 21413 15349 11087 -967 -1690 1320 C ATOM 1741 CE LYS A1019 161.890 21.895 558.694 1.00127.31 C ANISOU 1741 CE LYS A1019 21637 15458 11276 -1277 -1467 1068 C ATOM 1742 NZ LYS A1019 162.646 22.411 557.520 1.00127.28 N ANISOU 1742 NZ LYS A1019 22057 15285 11019 -1607 -1417 906 N ATOM 1743 N ALA A1020 156.428 20.435 561.759 1.00 99.84 N ANISOU 1743 N ALA A1020 16363 13013 8561 -130 -2010 2445 N ATOM 1744 CA ALA A1020 155.730 19.241 561.305 1.00102.61 C ANISOU 1744 CA ALA A1020 16470 13385 9131 -407 -2154 2639 C ATOM 1745 C ALA A1020 154.295 19.580 560.926 1.00103.53 C ANISOU 1745 C ALA A1020 16402 13667 9270 -328 -2446 2937 C ATOM 1746 O ALA A1020 153.603 20.307 561.645 1.00102.72 O ANISOU 1746 O ALA A1020 16072 13817 9141 76 -2446 3129 O ATOM 1747 CB ALA A1020 155.746 18.159 562.383 1.00103.94 C ANISOU 1747 CB ALA A1020 16205 13721 9565 -330 -1979 2818 C ATOM 1748 N ASP A1021 153.852 19.042 559.789 1.00 92.07 N ANISOU 1748 N ASP A1021 15037 12087 7859 -700 -2704 2956 N ATOM 1749 CA ASP A1021 152.522 19.329 559.268 1.00 93.53 C ANISOU 1749 CA ASP A1021 15054 12421 8062 -677 -3035 3225 C ATOM 1750 C ASP A1021 151.466 18.343 559.748 1.00 96.30 C ANISOU 1750 C ASP A1021 14817 13015 8757 -718 -3132 3586 C ATOM 1751 O ASP A1021 150.291 18.713 559.856 1.00 97.68 O ANISOU 1751 O ASP A1021 14662 13458 8992 -525 -3315 3891 O ATOM 1752 CB ASP A1021 152.547 19.330 557.737 1.00 95.07 C ANISOU 1752 CB ASP A1021 15660 12386 8076 -1064 -3314 3059 C ATOM 1753 CG ASP A1021 153.644 20.208 557.171 1.00 92.72 C ANISOU 1753 CG ASP A1021 15939 11851 7440 -1101 -3196 2745 C ATOM 1754 OD1 ASP A1021 154.021 21.196 557.836 1.00 91.02 O ANISOU 1754 OD1 ASP A1021 15808 11650 7124 -773 -3024 2714 O ATOM 1755 OD2 ASP A1021 154.132 19.910 556.060 1.00 94.15 O ANISOU 1755 OD2 ASP A1021 16484 11836 7450 -1464 -3276 2526 O ATOM 1756 N ASN A1022 151.849 17.103 560.035 1.00139.04 N ANISOU 1756 N ASN A1022 20075 18335 14419 -963 -3019 3578 N ATOM 1757 CA ASN A1022 150.893 16.071 560.419 1.00142.16 C ANISOU 1757 CA ASN A1022 19926 18899 15188 -1092 -3127 3950 C ATOM 1758 C ASN A1022 151.402 15.366 561.675 1.00141.61 C ANISOU 1758 C ASN A1022 19578 18910 15316 -964 -2793 4073 C ATOM 1759 O ASN A1022 152.263 15.869 562.408 1.00138.66 O ANISOU 1759 O ASN A1022 19343 18575 14764 -670 -2500 3919 O ATOM 1760 CB ASN A1022 150.663 15.100 559.254 1.00146.47 C ANISOU 1760 CB ASN A1022 20585 19173 15895 -1623 -3450 3855 C ATOM 1761 CG ASN A1022 151.920 14.345 558.866 1.00147.53 C ANISOU 1761 CG ASN A1022 21114 18915 16026 -1900 -3318 3458 C ATOM 1762 OD1 ASN A1022 153.035 14.825 559.072 1.00144.66 O ANISOU 1762 OD1 ASN A1022 21068 18459 15438 -1742 -3042 3183 O ATOM 1763 ND2 ASN A1022 151.745 13.157 558.301 1.00152.26 N ANISOU 1763 ND2 ASN A1022 21681 19278 16892 -2310 -3526 3414 N ATOM 1764 N ALA A1023 150.865 14.174 561.935 1.00102.56 N ANISOU 1764 N ALA A1023 14231 13984 10754 -1201 -2860 4371 N ATOM 1765 CA ALA A1023 151.234 13.386 563.102 1.00102.52 C ANISOU 1765 CA ALA A1023 13929 14058 10967 -1111 -2578 4580 C ATOM 1766 C ALA A1023 152.281 12.321 562.804 1.00104.60 C ANISOU 1766 C ALA A1023 14467 13875 11403 -1435 -2529 4314 C ATOM 1767 O ALA A1023 152.795 11.703 563.741 1.00104.45 O ANISOU 1767 O ALA A1023 14280 13869 11536 -1338 -2290 4446 O ATOM 1768 CB ALA A1023 149.991 12.719 563.706 1.00105.01 C ANISOU 1768 CB ALA A1023 13586 14681 11633 -1158 -2650 5158 C ATOM 1769 N ALA A1024 152.605 12.087 561.531 1.00124.07 N ANISOU 1769 N ALA A1024 17345 15965 13832 -1788 -2750 3944 N ATOM 1770 CA ALA A1024 153.631 11.107 561.198 1.00126.69 C ANISOU 1770 CA ALA A1024 17955 15872 14310 -2043 -2692 3632 C ATOM 1771 C ALA A1024 155.032 11.690 561.319 1.00123.77 C ANISOU 1771 C ALA A1024 17976 15423 13626 -1832 -2395 3232 C ATOM 1772 O ALA A1024 155.975 10.964 561.656 1.00125.03 O ANISOU 1772 O ALA A1024 18202 15378 13927 -1850 -2213 3092 O ATOM 1773 CB ALA A1024 153.405 10.566 559.786 1.00131.21 C ANISOU 1773 CB ALA A1024 18806 16106 14942 -2489 -3045 3364 C ATOM 1774 N GLN A1025 155.187 12.989 561.056 1.00120.73 N ANISOU 1774 N GLN A1025 17838 15186 12846 -1635 -2356 3062 N ATOM 1775 CA GLN A1025 156.491 13.632 561.135 1.00118.19 C ANISOU 1775 CA GLN A1025 17869 14795 12243 -1478 -2097 2699 C ATOM 1776 C GLN A1025 156.938 13.884 562.569 1.00115.60 C ANISOU 1776 C GLN A1025 17301 14708 11913 -1092 -1803 2842 C ATOM 1777 O GLN A1025 158.141 14.033 562.810 1.00114.81 O ANISOU 1777 O GLN A1025 17402 14523 11697 -1006 -1585 2563 O ATOM 1778 CB GLN A1025 156.469 14.948 560.353 1.00115.51 C ANISOU 1778 CB GLN A1025 17884 14490 11515 -1435 -2184 2509 C ATOM 1779 CG GLN A1025 156.414 14.757 558.846 1.00118.11 C ANISOU 1779 CG GLN A1025 18573 14579 11725 -1813 -2425 2265 C ATOM 1780 CD GLN A1025 155.957 16.002 558.112 1.00115.76 C ANISOU 1780 CD GLN A1025 18527 14369 11090 -1767 -2598 2258 C ATOM 1781 OE1 GLN A1025 156.568 16.419 557.128 1.00115.56 O ANISOU 1781 OE1 GLN A1025 18943 14192 10773 -1934 -2609 1968 O ATOM 1782 NE2 GLN A1025 154.869 16.596 558.583 1.00114.33 N ANISOU 1782 NE2 GLN A1025 18054 14443 10942 -1527 -2729 2600 N ATOM 1783 N VAL A1026 156.006 13.941 563.522 1.00137.96 N ANISOU 1783 N VAL A1026 19696 17875 14849 -851 -1794 3268 N ATOM 1784 CA VAL A1026 156.403 14.093 564.918 1.00136.07 C ANISOU 1784 CA VAL A1026 19225 17909 14567 -472 -1522 3409 C ATOM 1785 C VAL A1026 156.763 12.745 565.531 1.00138.58 C ANISOU 1785 C VAL A1026 19307 18136 15211 -569 -1414 3593 C ATOM 1786 O VAL A1026 157.633 12.672 566.406 1.00137.85 O ANISOU 1786 O VAL A1026 19187 18124 15065 -348 -1188 3546 O ATOM 1787 CB VAL A1026 155.301 14.797 565.729 1.00134.13 C ANISOU 1787 CB VAL A1026 18615 18121 14226 -108 -1515 3772 C ATOM 1788 CG1 VAL A1026 155.233 16.271 565.370 1.00131.65 C ANISOU 1788 CG1 VAL A1026 18585 17864 13571 108 -1573 3539 C ATOM 1789 CG2 VAL A1026 153.957 14.128 565.499 1.00136.41 C ANISOU 1789 CG2 VAL A1026 18515 18514 14802 -301 -1719 4195 C ATOM 1790 N LYS A1027 156.114 11.664 565.090 1.00118.99 N ANISOU 1790 N LYS A1027 16658 15469 13084 -901 -1597 3809 N ATOM 1791 CA LYS A1027 156.429 10.346 565.631 1.00121.79 C ANISOU 1791 CA LYS A1027 16814 15659 13803 -1012 -1525 4013 C ATOM 1792 C LYS A1027 157.792 9.863 565.154 1.00123.91 C ANISOU 1792 C LYS A1027 17459 15519 14100 -1137 -1448 3557 C ATOM 1793 O LYS A1027 158.581 9.335 565.946 1.00124.54 O ANISOU 1793 O LYS A1027 17458 15577 14285 -988 -1262 3604 O ATOM 1794 CB LYS A1027 155.343 9.342 565.244 1.00125.43 C ANISOU 1794 CB LYS A1027 17007 15971 14679 -1371 -1781 4355 C ATOM 1795 CG LYS A1027 153.994 9.588 565.897 1.00124.32 C ANISOU 1795 CG LYS A1027 16358 16287 14593 -1247 -1815 4908 C ATOM 1796 CD LYS A1027 152.991 8.517 565.496 1.00128.79 C ANISOU 1796 CD LYS A1027 16632 16672 15629 -1671 -2090 5253 C ATOM 1797 CE LYS A1027 151.647 8.732 566.170 1.00128.37 C ANISOU 1797 CE LYS A1027 15997 17128 15650 -1555 -2096 5845 C ATOM 1798 NZ LYS A1027 150.668 7.672 565.801 1.00133.39 N ANISOU 1798 NZ LYS A1027 16302 17588 16791 -2020 -2383 6212 N ATOM 1799 N ASP A1028 158.086 10.033 563.863 1.00119.64 N ANISOU 1799 N ASP A1028 17319 14687 13452 -1391 -1586 3124 N ATOM 1800 CA ASP A1028 159.364 9.573 563.330 1.00122.27 C ANISOU 1800 CA ASP A1028 17990 14671 13795 -1497 -1491 2671 C ATOM 1801 C ASP A1028 160.524 10.387 563.889 1.00119.53 C ANISOU 1801 C ASP A1028 17768 14498 13151 -1195 -1213 2436 C ATOM 1802 O ASP A1028 161.605 9.844 564.146 1.00121.69 O ANISOU 1802 O ASP A1028 18092 14622 13521 -1136 -1054 2255 O ATOM 1803 CB ASP A1028 159.350 9.640 561.803 1.00124.48 C ANISOU 1803 CB ASP A1028 18665 14681 13952 -1821 -1686 2273 C ATOM 1804 CG ASP A1028 160.656 9.178 561.188 1.00127.87 C ANISOU 1804 CG ASP A1028 19430 14798 14358 -1908 -1558 1782 C ATOM 1805 OD1 ASP A1028 160.908 7.954 561.174 1.00132.28 O ANISOU 1805 OD1 ASP A1028 19949 15040 15270 -2020 -1592 1746 O ATOM 1806 OD2 ASP A1028 161.433 10.037 560.720 1.00126.28 O ANISOU 1806 OD2 ASP A1028 19521 14663 13797 -1858 -1420 1440 O ATOM 1807 N ALA A1029 160.319 11.691 564.088 1.00 82.38 N ANISOU 1807 N ALA A1029 13105 10092 8103 -995 -1173 2431 N ATOM 1808 CA ALA A1029 161.392 12.532 564.605 1.00 79.73 C ANISOU 1808 CA ALA A1029 12895 9898 7501 -744 -953 2190 C ATOM 1809 C ALA A1029 161.647 12.261 566.082 1.00 79.47 C ANISOU 1809 C ALA A1029 12528 10121 7547 -416 -787 2453 C ATOM 1810 O ALA A1029 162.798 12.283 566.530 1.00 79.15 O ANISOU 1810 O ALA A1029 12538 10086 7448 -281 -619 2246 O ATOM 1811 CB ALA A1029 161.062 14.006 564.376 1.00 78.46 C ANISOU 1811 CB ALA A1029 12908 9916 6988 -632 -997 2103 C ATOM 1812 N LEU A1030 160.589 12.001 566.855 1.00106.41 N ANISOU 1812 N LEU A1030 15577 13780 11074 -283 -830 2927 N ATOM 1813 CA LEU A1030 160.764 11.725 568.278 1.00105.70 C ANISOU 1813 CA LEU A1030 15164 13991 11005 40 -666 3227 C ATOM 1814 C LEU A1030 161.519 10.421 568.504 1.00109.40 C ANISOU 1814 C LEU A1030 15562 14210 11795 -50 -606 3277 C ATOM 1815 O LEU A1030 162.371 10.337 569.397 1.00109.24 O ANISOU 1815 O LEU A1030 15460 14332 11712 200 -452 3270 O ATOM 1816 CB LEU A1030 159.406 11.684 568.978 1.00103.90 C ANISOU 1816 CB LEU A1030 14536 14119 10822 181 -701 3762 C ATOM 1817 CG LEU A1030 158.809 13.020 569.425 1.00 99.98 C ANISOU 1817 CG LEU A1030 13990 14035 9962 515 -673 3783 C ATOM 1818 CD1 LEU A1030 157.378 12.832 569.899 1.00 99.41 C ANISOU 1818 CD1 LEU A1030 13484 14305 9983 604 -709 4319 C ATOM 1819 CD2 LEU A1030 159.657 13.640 570.523 1.00 97.58 C ANISOU 1819 CD2 LEU A1030 13695 14018 9361 916 -484 3641 C ATOM 1820 N THR A1031 161.224 9.392 567.707 1.00 98.51 N ANISOU 1820 N THR A1031 14220 12443 10767 -392 -749 3315 N ATOM 1821 CA THR A1031 161.881 8.103 567.894 1.00102.60 C ANISOU 1821 CA THR A1031 14685 12653 11644 -460 -719 3368 C ATOM 1822 C THR A1031 163.325 8.139 567.407 1.00105.09 C ANISOU 1822 C THR A1031 15309 12738 11883 -451 -613 2827 C ATOM 1823 O THR A1031 164.227 7.632 568.085 1.00107.02 O ANISOU 1823 O THR A1031 15464 12967 12232 -266 -489 2837 O ATOM 1824 CB THR A1031 161.101 7.004 567.173 1.00106.08 C ANISOU 1824 CB THR A1031 15094 12701 12510 -833 -939 3533 C ATOM 1825 OG1 THR A1031 160.990 7.329 565.781 1.00107.13 O ANISOU 1825 OG1 THR A1031 15569 12592 12546 -1115 -1092 3108 O ATOM 1826 CG2 THR A1031 159.707 6.861 567.769 1.00104.33 C ANISOU 1826 CG2 THR A1031 14475 12744 12422 -855 -1026 4142 C ATOM 1827 N LYS A1032 163.564 8.732 566.235 1.00102.86 N ANISOU 1827 N LYS A1032 15368 12303 11410 -644 -656 2375 N ATOM 1828 CA LYS A1032 164.920 8.781 565.697 1.00105.33 C ANISOU 1828 CA LYS A1032 15941 12440 11639 -657 -526 1872 C ATOM 1829 C LYS A1032 165.813 9.708 566.512 1.00102.72 C ANISOU 1829 C LYS A1032 15568 12443 11020 -362 -340 1756 C ATOM 1830 O LYS A1032 167.029 9.490 566.583 1.00105.49 O ANISOU 1830 O LYS A1032 15956 12728 11398 -281 -205 1490 O ATOM 1831 CB LYS A1032 164.882 9.210 564.230 1.00105.71 C ANISOU 1831 CB LYS A1032 16358 12297 11509 -950 -606 1472 C ATOM 1832 CG LYS A1032 166.213 9.097 563.504 1.00109.34 C ANISOU 1832 CG LYS A1032 17070 12572 11901 -1008 -454 963 C ATOM 1833 CD LYS A1032 166.008 8.967 562.002 1.00111.85 C ANISOU 1833 CD LYS A1032 17726 12633 12138 -1331 -566 639 C ATOM 1834 CE LYS A1032 165.145 10.093 561.456 1.00106.96 C ANISOU 1834 CE LYS A1032 17262 12188 11190 -1461 -694 694 C ATOM 1835 NZ LYS A1032 164.854 9.915 560.006 1.00109.68 N ANISOU 1835 NZ LYS A1032 17932 12316 11423 -1773 -841 420 N ATOM 1836 N MET A1033 165.235 10.737 567.136 1.00116.57 N ANISOU 1836 N MET A1033 17232 14554 12508 -188 -346 1935 N ATOM 1837 CA MET A1033 166.016 11.600 568.016 1.00114.28 C ANISOU 1837 CA MET A1033 16894 14571 11955 101 -214 1822 C ATOM 1838 C MET A1033 166.328 10.904 569.334 1.00115.36 C ANISOU 1838 C MET A1033 16709 14901 12220 390 -139 2121 C ATOM 1839 O MET A1033 167.450 11.001 569.844 1.00115.99 O ANISOU 1839 O MET A1033 16759 15078 12234 557 -38 1933 O ATOM 1840 CB MET A1033 165.265 12.906 568.271 1.00109.24 C ANISOU 1840 CB MET A1033 16289 14219 10998 232 -265 1884 C ATOM 1841 CG MET A1033 165.968 13.864 569.211 1.00106.55 C ANISOU 1841 CG MET A1033 15923 14178 10382 532 -177 1738 C ATOM 1842 SD MET A1033 164.839 15.101 569.874 1.00101.46 S ANISOU 1842 SD MET A1033 15225 13894 9432 818 -247 1919 S ATOM 1843 CE MET A1033 163.886 15.493 568.413 1.00101.01 C ANISOU 1843 CE MET A1033 15423 13569 9387 493 -400 1878 C ATOM 1844 N ARG A1034 165.343 10.204 569.903 1.00145.09 N ANISOU 1844 N ARG A1034 20215 18748 16165 444 -195 2615 N ATOM 1845 CA ARG A1034 165.569 9.486 571.152 1.00144.97 C ANISOU 1845 CA ARG A1034 19896 18929 16258 710 -126 2981 C ATOM 1846 C ARG A1034 166.597 8.378 570.968 1.00150.21 C ANISOU 1846 C ARG A1034 20580 19247 17246 652 -97 2863 C ATOM 1847 O ARG A1034 167.403 8.113 571.867 1.00150.56 O ANISOU 1847 O ARG A1034 20473 19451 17281 913 -22 2934 O ATOM 1848 CB ARG A1034 164.249 8.920 571.675 1.00143.47 C ANISOU 1848 CB ARG A1034 19414 18878 16220 717 -179 3584 C ATOM 1849 CG ARG A1034 164.371 8.124 572.965 1.00143.31 C ANISOU 1849 CG ARG A1034 19072 19079 16301 972 -102 4063 C ATOM 1850 CD ARG A1034 163.008 7.687 573.486 1.00141.83 C ANISOU 1850 CD ARG A1034 18562 19098 16230 958 -124 4704 C ATOM 1851 NE ARG A1034 162.325 6.770 572.576 1.00145.08 N ANISOU 1851 NE ARG A1034 18985 19045 17095 550 -274 4852 N ATOM 1852 CZ ARG A1034 161.384 7.134 571.710 1.00144.73 C ANISOU 1852 CZ ARG A1034 19006 18917 17070 297 -398 4791 C ATOM 1853 NH1 ARG A1034 160.819 6.229 570.922 1.00148.12 N ANISOU 1853 NH1 ARG A1034 19441 18916 17922 -84 -571 4908 N ATOM 1854 NH2 ARG A1034 161.008 8.402 571.630 1.00141.23 N ANISOU 1854 NH2 ARG A1034 18626 18801 16232 432 -375 4606 N ATOM 1855 N ALA A1035 166.585 7.720 569.806 1.00122.60 N ANISOU 1855 N ALA A1035 17274 15282 14028 338 -171 2665 N ATOM 1856 CA ALA A1035 167.615 6.731 569.512 1.00128.32 C ANISOU 1856 CA ALA A1035 18054 15647 15055 318 -137 2460 C ATOM 1857 C ALA A1035 168.989 7.380 569.418 1.00129.28 C ANISOU 1857 C ALA A1035 18287 15882 14953 443 0 1979 C ATOM 1858 O ALA A1035 169.980 6.827 569.907 1.00132.21 O ANISOU 1858 O ALA A1035 18538 16231 15464 638 68 1940 O ATOM 1859 CB ALA A1035 167.279 5.989 568.218 1.00132.38 C ANISOU 1859 CB ALA A1035 18788 15651 15858 -30 -254 2269 C ATOM 1860 N ALA A1036 169.071 8.557 568.796 1.00105.66 N ANISOU 1860 N ALA A1036 15505 13010 11630 328 33 1634 N ATOM 1861 CA ALA A1036 170.348 9.255 568.708 1.00106.20 C ANISOU 1861 CA ALA A1036 15651 13203 11499 396 160 1209 C ATOM 1862 C ALA A1036 170.752 9.888 570.032 1.00102.77 C ANISOU 1862 C ALA A1036 15003 13199 10846 718 191 1332 C ATOM 1863 O ALA A1036 171.947 10.110 570.258 1.00104.46 O ANISOU 1863 O ALA A1036 15166 13518 11006 823 271 1065 O ATOM 1864 CB ALA A1036 170.296 10.321 567.612 1.00103.60 C ANISOU 1864 CB ALA A1036 15626 12839 10900 138 176 851 C ATOM 1865 N ALA A1037 169.790 10.178 570.911 1.00112.10 N ANISOU 1865 N ALA A1037 16043 14658 11890 883 126 1717 N ATOM 1866 CA ALA A1037 170.125 10.745 572.213 1.00108.89 C ANISOU 1866 CA ALA A1037 15451 14694 11229 1222 140 1816 C ATOM 1867 C ALA A1037 170.755 9.700 573.126 1.00111.58 C ANISOU 1867 C ALA A1037 15528 15105 11764 1465 160 2063 C ATOM 1868 O ALA A1037 171.650 10.019 573.918 1.00111.57 O ANISOU 1868 O ALA A1037 15407 15383 11601 1702 172 1952 O ATOM 1869 CB ALA A1037 168.879 11.345 572.865 1.00103.59 C ANISOU 1869 CB ALA A1037 14703 14338 10318 1369 90 2143 C ATOM 1870 N LEU A1038 170.299 8.449 573.034 1.00102.86 N ANISOU 1870 N LEU A1038 14330 13735 11017 1406 136 2409 N ATOM 1871 CA LEU A1038 170.877 7.394 573.861 1.00105.49 C ANISOU 1871 CA LEU A1038 14433 14074 11576 1639 137 2693 C ATOM 1872 C LEU A1038 172.279 7.030 573.386 1.00111.20 C ANISOU 1872 C LEU A1038 15199 14567 12485 1643 184 2278 C ATOM 1873 O LEU A1038 173.167 6.765 574.205 1.00112.60 O ANISOU 1873 O LEU A1038 15184 14932 12667 1919 186 2329 O ATOM 1874 CB LEU A1038 169.965 6.168 573.857 1.00106.56 C ANISOU 1874 CB LEU A1038 14473 13922 12094 1541 79 3199 C ATOM 1875 CG LEU A1038 168.545 6.389 574.386 1.00101.81 C ANISOU 1875 CG LEU A1038 13739 13592 11353 1542 53 3693 C ATOM 1876 CD1 LEU A1038 167.750 5.091 574.367 1.00103.76 C ANISOU 1876 CD1 LEU A1038 13859 13516 12050 1389 -16 4216 C ATOM 1877 CD2 LEU A1038 168.572 6.985 575.786 1.00 97.65 C ANISOU 1877 CD2 LEU A1038 12997 13688 10418 1925 104 3942 C ATOM 1878 N ASP A1039 172.498 7.014 572.068 1.00122.33 N ANISOU 1878 N ASP A1039 16845 15607 14028 1356 222 1868 N ATOM 1879 CA ASP A1039 173.836 6.782 571.536 1.00128.24 C ANISOU 1879 CA ASP A1039 17618 16199 14910 1366 309 1431 C ATOM 1880 C ASP A1039 174.772 7.948 571.820 1.00126.93 C ANISOU 1880 C ASP A1039 17408 16410 14408 1445 368 1092 C ATOM 1881 O ASP A1039 175.992 7.753 571.872 1.00131.41 O ANISOU 1881 O ASP A1039 17848 17014 15069 1563 428 851 O ATOM 1882 CB ASP A1039 173.775 6.520 570.030 1.00132.51 C ANISOU 1882 CB ASP A1039 18434 16308 15606 1046 356 1071 C ATOM 1883 CG ASP A1039 173.260 5.132 569.698 1.00136.09 C ANISOU 1883 CG ASP A1039 18920 16291 16498 989 275 1283 C ATOM 1884 OD1 ASP A1039 172.030 4.923 569.730 1.00133.41 O ANISOU 1884 OD1 ASP A1039 18612 15854 16223 850 160 1630 O ATOM 1885 OD2 ASP A1039 174.089 4.245 569.413 1.00141.63 O ANISOU 1885 OD2 ASP A1039 19601 16711 17502 1086 316 1099 O ATOM 1886 N ALA A1040 174.235 9.157 571.996 1.00111.61 N ANISOU 1886 N ALA A1040 15562 14737 12107 1382 338 1063 N ATOM 1887 CA ALA A1040 175.059 10.286 572.405 1.00109.58 C ANISOU 1887 CA ALA A1040 15264 14815 11556 1452 345 772 C ATOM 1888 C ALA A1040 175.265 10.342 573.912 1.00107.55 C ANISOU 1888 C ALA A1040 14746 14976 11143 1821 254 1024 C ATOM 1889 O ALA A1040 176.148 11.070 574.376 1.00107.39 O ANISOU 1889 O ALA A1040 14640 15228 10937 1914 221 770 O ATOM 1890 CB ALA A1040 174.440 11.598 571.923 1.00104.25 C ANISOU 1890 CB ALA A1040 14842 14191 10579 1240 327 598 C ATOM 1891 N GLN A1041 174.468 9.602 574.682 1.00102.92 N ANISOU 1891 N GLN A1041 14028 14463 10615 2020 202 1525 N ATOM 1892 CA GLN A1041 174.644 9.588 576.129 1.00100.85 C ANISOU 1892 CA GLN A1041 13522 14644 10152 2394 123 1804 C ATOM 1893 C GLN A1041 175.684 8.561 576.556 1.00105.58 C ANISOU 1893 C GLN A1041 13888 15214 11012 2602 106 1896 C ATOM 1894 O GLN A1041 176.469 8.815 577.477 1.00105.62 O ANISOU 1894 O GLN A1041 13707 15590 10832 2863 28 1856 O ATOM 1895 CB GLN A1041 173.307 9.311 576.816 1.00 96.60 C ANISOU 1895 CB GLN A1041 12918 14271 9513 2525 102 2355 C ATOM 1896 CG GLN A1041 173.383 9.255 578.332 1.00 94.58 C ANISOU 1896 CG GLN A1041 12421 14533 8985 2932 40 2697 C ATOM 1897 CD GLN A1041 172.140 8.650 578.945 1.00 92.41 C ANISOU 1897 CD GLN A1041 12020 14393 8698 3044 67 3340 C ATOM 1898 OE1 GLN A1041 171.714 9.043 580.029 1.00 91.07 O ANISOU 1898 OE1 GLN A1041 11727 14732 8144 3332 56 3591 O ATOM 1899 NE2 GLN A1041 171.553 7.681 578.252 1.00 94.00 N ANISOU 1899 NE2 GLN A1041 12244 14152 9318 2812 100 3608 N ATOM 1900 N LYS A1042 175.712 7.404 575.891 1.00 88.50 N ANISOU 1900 N LYS A1042 11739 12604 9284 2505 154 1999 N ATOM 1901 CA LYS A1042 176.644 6.343 576.251 1.00 91.74 C ANISOU 1901 CA LYS A1042 11938 12920 9999 2737 129 2110 C ATOM 1902 C LYS A1042 178.088 6.687 575.909 1.00 94.51 C ANISOU 1902 C LYS A1042 12206 13329 10374 2754 166 1590 C ATOM 1903 O LYS A1042 179.004 6.035 576.423 1.00 97.07 O ANISOU 1903 O LYS A1042 12293 13716 10871 3022 119 1654 O ATOM 1904 CB LYS A1042 176.245 5.040 575.556 1.00 94.31 C ANISOU 1904 CB LYS A1042 12342 12677 10815 2624 153 2307 C ATOM 1905 CG LYS A1042 174.840 4.562 575.887 1.00 93.67 C ANISOU 1905 CG LYS A1042 12285 12512 10794 2567 105 2877 C ATOM 1906 CD LYS A1042 174.459 3.352 575.050 1.00 95.44 C ANISOU 1906 CD LYS A1042 12625 12099 11537 2379 91 2984 C ATOM 1907 CE LYS A1042 173.029 2.919 575.325 1.00 96.37 C ANISOU 1907 CE LYS A1042 12735 12134 11749 2253 31 3561 C ATOM 1908 NZ LYS A1042 172.631 1.761 574.477 1.00 98.53 N ANISOU 1908 NZ LYS A1042 13140 11738 12558 2024 -29 3630 N ATOM 1909 N ALA A1043 178.313 7.685 575.062 1.00 89.31 N ANISOU 1909 N ALA A1043 11715 12660 9559 2474 246 1111 N ATOM 1910 CA ALA A1043 179.653 8.066 574.642 1.00 89.83 C ANISOU 1910 CA ALA A1043 11676 12797 9657 2426 311 632 C ATOM 1911 C ALA A1043 180.150 9.265 575.444 1.00 89.48 C ANISOU 1911 C ALA A1043 11519 13238 9242 2492 204 465 C ATOM 1912 O ALA A1043 179.372 10.009 576.046 1.00 88.20 O ANISOU 1912 O ALA A1043 11456 13303 8753 2517 111 601 O ATOM 1913 CB ALA A1043 179.681 8.385 573.146 1.00 88.19 C ANISOU 1913 CB ALA A1043 11718 12273 9516 2046 479 225 C ATOM 1914 N THR A1044 181.477 9.443 575.441 1.00113.10 N ANISOU 1914 N THR A1044 14287 16388 12300 2527 209 145 N ATOM 1915 CA THR A1044 182.121 10.507 576.202 1.00111.05 C ANISOU 1915 CA THR A1044 13883 16565 11747 2572 64 -58 C ATOM 1916 C THR A1044 182.440 11.683 575.295 1.00108.83 C ANISOU 1916 C THR A1044 13761 16226 11362 2169 152 -513 C ATOM 1917 O THR A1044 183.076 11.495 574.247 1.00111.51 O ANISOU 1917 O THR A1044 14083 16363 11924 1957 335 -772 O ATOM 1918 CB THR A1044 183.405 10.000 576.855 1.00115.30 C ANISOU 1918 CB THR A1044 14019 17356 12433 2852 -29 -92 C ATOM 1919 OG1 THR A1044 184.344 9.625 575.839 1.00120.13 O ANISOU 1919 OG1 THR A1044 14514 17760 13371 2712 152 -399 O ATOM 1920 CG2 THR A1044 183.113 8.792 577.733 1.00113.97 C ANISOU 1920 CG2 THR A1044 13708 17212 12384 3257 -122 413 C ATOM 1921 N PRO A1045 182.024 12.894 575.651 1.00117.88 N ANISOU 1921 N PRO A1045 15069 17542 12178 2064 32 -614 N ATOM 1922 CA PRO A1045 182.332 14.062 574.825 1.00115.34 C ANISOU 1922 CA PRO A1045 14915 17130 11779 1663 91 -1002 C ATOM 1923 C PRO A1045 183.740 14.558 575.096 1.00118.26 C ANISOU 1923 C PRO A1045 14983 17760 12190 1604 12 -1319 C ATOM 1924 O PRO A1045 184.356 14.176 576.102 1.00121.50 O ANISOU 1924 O PRO A1045 15079 18480 12606 1911 -147 -1248 O ATOM 1925 CB PRO A1045 181.283 15.087 575.274 1.00109.15 C ANISOU 1925 CB PRO A1045 14414 16406 10654 1654 -51 -951 C ATOM 1926 CG PRO A1045 181.060 14.750 576.708 1.00108.97 C ANISOU 1926 CG PRO A1045 14216 16736 10454 2090 -239 -686 C ATOM 1927 CD PRO A1045 181.194 13.247 576.817 1.00113.49 C ANISOU 1927 CD PRO A1045 14569 17255 11296 2322 -155 -364 C ATOM 1928 N PRO A1046 184.293 15.405 574.217 1.00109.28 N ANISOU 1928 N PRO A1046 13913 16524 11086 1201 112 -1647 N ATOM 1929 CA PRO A1046 185.616 15.985 574.487 1.00112.16 C ANISOU 1929 CA PRO A1046 13959 17151 11507 1084 17 -1939 C ATOM 1930 C PRO A1046 185.626 16.833 575.749 1.00110.53 C ANISOU 1930 C PRO A1046 13718 17237 11040 1226 -325 -2004 C ATOM 1931 O PRO A1046 185.613 18.067 575.679 1.00107.75 O ANISOU 1931 O PRO A1046 13546 16842 10550 949 -439 -2233 O ATOM 1932 CB PRO A1046 185.892 16.833 573.238 1.00110.53 C ANISOU 1932 CB PRO A1046 13921 16731 11345 570 205 -2195 C ATOM 1933 CG PRO A1046 185.034 16.232 572.175 1.00108.80 C ANISOU 1933 CG PRO A1046 14001 16170 11168 493 456 -2052 C ATOM 1934 CD PRO A1046 183.796 15.763 572.877 1.00106.48 C ANISOU 1934 CD PRO A1046 13892 15824 10742 821 325 -1734 C ATOM 1935 N LYS A1047 185.648 16.180 576.907 1.00126.05 N ANISOU 1935 N LYS A1047 15471 19493 12928 1665 -502 -1803 N ATOM 1936 CA LYS A1047 185.613 16.888 578.176 1.00124.33 C ANISOU 1936 CA LYS A1047 15232 19609 12398 1866 -838 -1869 C ATOM 1937 C LYS A1047 187.003 17.365 578.573 1.00128.42 C ANISOU 1937 C LYS A1047 15385 20414 12994 1765 -1040 -2187 C ATOM 1938 O LYS A1047 188.019 16.754 578.230 1.00133.69 O ANISOU 1938 O LYS A1047 15685 21152 13957 1731 -938 -2229 O ATOM 1939 CB LYS A1047 185.040 15.995 579.277 1.00124.14 C ANISOU 1939 CB LYS A1047 15131 19833 12202 2383 -943 -1481 C ATOM 1940 CG LYS A1047 183.546 15.768 579.172 1.00119.35 C ANISOU 1940 CG LYS A1047 14868 19032 11446 2487 -821 -1161 C ATOM 1941 CD LYS A1047 183.019 15.013 580.378 1.00118.30 C ANISOU 1941 CD LYS A1047 14630 19216 11103 2976 -933 -748 C ATOM 1942 CE LYS A1047 181.503 14.964 580.367 1.00113.21 C ANISOU 1942 CE LYS A1047 14286 18449 10280 3057 -828 -436 C ATOM 1943 NZ LYS A1047 180.908 16.329 580.372 1.00108.91 N ANISOU 1943 NZ LYS A1047 14046 17897 9437 2927 -915 -709 N ATOM 1944 N LEU A1048 187.036 18.472 579.307 1.00137.17 N ANISOU 1944 N LEU A1048 16584 21691 13842 1726 -1343 -2428 N ATOM 1945 CA LEU A1048 188.297 19.021 579.780 1.00141.03 C ANISOU 1945 CA LEU A1048 16731 22461 14393 1602 -1607 -2748 C ATOM 1946 C LEU A1048 188.862 18.164 580.907 1.00144.57 C ANISOU 1946 C LEU A1048 16781 23372 14777 2068 -1816 -2594 C ATOM 1947 O LEU A1048 188.124 17.534 581.670 1.00142.42 O ANISOU 1947 O LEU A1048 16593 23256 14265 2505 -1862 -2278 O ATOM 1948 CB LEU A1048 188.111 20.464 580.258 1.00138.18 C ANISOU 1948 CB LEU A1048 16632 22092 13776 1429 -1916 -3083 C ATOM 1949 CG LEU A1048 187.984 21.582 579.215 1.00136.14 C ANISOU 1949 CG LEU A1048 16684 21400 13643 882 -1815 -3317 C ATOM 1950 CD1 LEU A1048 186.671 21.504 578.445 1.00131.27 C ANISOU 1950 CD1 LEU A1048 16519 20405 12954 867 -1537 -3089 C ATOM 1951 CD2 LEU A1048 188.120 22.940 579.885 1.00135.48 C ANISOU 1951 CD2 LEU A1048 16762 21335 13378 746 -2212 -3697 C ATOM 1952 N GLU A1049 190.192 18.136 580.992 1.00166.99 N ANISOU 1952 N GLU A1049 19160 26448 17842 1965 -1939 -2789 N ATOM 1953 CA GLU A1049 190.986 17.437 582.002 1.00170.74 C ANISOU 1953 CA GLU A1049 19183 27391 18300 2360 -2188 -2693 C ATOM 1954 C GLU A1049 190.918 15.918 581.886 1.00172.62 C ANISOU 1954 C GLU A1049 19241 27614 18733 2736 -1959 -2271 C ATOM 1955 O GLU A1049 191.533 15.228 582.710 1.00174.55 O ANISOU 1955 O GLU A1049 19118 28223 18981 3112 -2158 -2122 O ATOM 1956 CB GLU A1049 190.597 17.838 583.434 1.00167.82 C ANISOU 1956 CB GLU A1049 18925 27396 17442 2710 -2596 -2703 C ATOM 1957 CG GLU A1049 190.599 19.338 583.692 1.00166.10 C ANISOU 1957 CG GLU A1049 18934 27166 17010 2407 -2886 -3157 C ATOM 1958 CD GLU A1049 191.890 20.008 583.261 1.00170.79 C ANISOU 1958 CD GLU A1049 19190 27767 17934 1932 -3013 -3544 C ATOM 1959 OE1 GLU A1049 191.964 20.476 582.105 1.00170.67 O ANISOU 1959 OE1 GLU A1049 19283 27360 18202 1446 -2756 -3666 O ATOM 1960 OE2 GLU A1049 192.834 20.061 584.077 1.00174.55 O ANISOU 1960 OE2 GLU A1049 19274 28664 18381 2036 -3376 -3706 O ATOM 1961 N ASP A1050 190.208 15.374 580.897 1.00159.94 N ANISOU 1961 N ASP A1050 17885 25585 17299 2651 -1577 -2079 N ATOM 1962 CA ASP A1050 190.078 13.929 580.693 1.00161.57 C ANISOU 1962 CA ASP A1050 17977 25670 17740 2975 -1365 -1704 C ATOM 1963 C ASP A1050 189.619 13.236 581.979 1.00158.62 C ANISOU 1963 C ASP A1050 17576 25582 17109 3509 -1588 -1302 C ATOM 1964 O ASP A1050 190.348 12.476 582.616 1.00160.54 O ANISOU 1964 O ASP A1050 17443 26103 17452 3854 -1739 -1139 O ATOM 1965 CB ASP A1050 191.393 13.332 580.181 1.00167.00 C ANISOU 1965 CB ASP A1050 18176 26424 18854 2961 -1256 -1827 C ATOM 1966 CG ASP A1050 191.808 13.899 578.837 1.00170.07 C ANISOU 1966 CG ASP A1050 18581 26561 19477 2445 -965 -2159 C ATOM 1967 OD1 ASP A1050 190.919 14.321 578.068 1.00168.04 O ANISOU 1967 OD1 ASP A1050 18767 25947 19135 2160 -761 -2181 O ATOM 1968 OD2 ASP A1050 193.023 13.920 578.549 1.00174.06 O ANISOU 1968 OD2 ASP A1050 18639 27254 20243 2328 -937 -2377 O ATOM 1969 N LYS A1051 188.374 13.525 582.339 1.00138.80 N ANISOU 1969 N LYS A1051 15466 23015 14258 3578 -1598 -1121 N ATOM 1970 CA LYS A1051 187.823 13.108 583.618 1.00135.51 C ANISOU 1970 CA LYS A1051 15063 22940 13487 4045 -1801 -742 C ATOM 1971 C LYS A1051 187.211 11.714 583.528 1.00134.54 C ANISOU 1971 C LYS A1051 14961 22598 13559 4318 -1600 -193 C ATOM 1972 O LYS A1051 186.693 11.303 582.486 1.00134.64 O ANISOU 1972 O LYS A1051 15163 22137 13858 4116 -1302 -121 O ATOM 1973 CB LYS A1051 186.778 14.117 584.096 1.00130.49 C ANISOU 1973 CB LYS A1051 14812 22400 12370 4018 -1896 -816 C ATOM 1974 CG LYS A1051 187.280 15.555 584.079 1.00130.90 C ANISOU 1974 CG LYS A1051 14922 22536 12277 3701 -2102 -1385 C ATOM 1975 CD LYS A1051 186.215 16.539 584.532 1.00125.69 C ANISOU 1975 CD LYS A1051 14670 21926 11161 3731 -2196 -1487 C ATOM 1976 CE LYS A1051 185.976 16.451 586.030 1.00124.14 C ANISOU 1976 CE LYS A1051 14423 22288 10455 4231 -2475 -1314 C ATOM 1977 NZ LYS A1051 184.929 17.408 586.481 1.00119.60 N ANISOU 1977 NZ LYS A1051 14236 21790 9415 4317 -2543 -1447 N ATOM 1978 N SER A1052 187.280 10.988 584.644 1.00116.70 N ANISOU 1978 N SER A1052 12512 20687 11141 4775 -1789 203 N ATOM 1979 CA SER A1052 186.777 9.628 584.727 1.00116.02 C ANISOU 1979 CA SER A1052 12417 20406 11259 5057 -1655 785 C ATOM 1980 C SER A1052 185.249 9.627 584.680 1.00112.91 C ANISOU 1980 C SER A1052 12407 19828 10666 5012 -1484 1105 C ATOM 1981 O SER A1052 184.612 10.668 584.853 1.00111.10 O ANISOU 1981 O SER A1052 12417 19743 10055 4884 -1515 910 O ATOM 1982 CB SER A1052 187.289 8.965 586.007 1.00120.98 C ANISOU 1982 CB SER A1052 12740 21503 11724 5553 -1934 1153 C ATOM 1983 OG SER A1052 186.883 9.687 587.156 1.00122.37 O ANISOU 1983 OG SER A1052 13003 22211 11281 5736 -2169 1191 O ATOM 1984 N PRO A1053 184.628 8.468 584.432 1.00113.57 N ANISOU 1984 N PRO A1053 12548 19575 11030 5112 -1311 1594 N ATOM 1985 CA PRO A1053 183.156 8.419 584.427 1.00110.25 C ANISOU 1985 CA PRO A1053 12430 19016 10443 5060 -1160 1947 C ATOM 1986 C PRO A1053 182.522 8.768 585.763 1.00112.18 C ANISOU 1986 C PRO A1053 12694 19829 10098 5370 -1313 2255 C ATOM 1987 O PRO A1053 181.351 9.170 585.787 1.00110.16 O ANISOU 1987 O PRO A1053 12677 19586 9593 5298 -1200 2386 O ATOM 1988 CB PRO A1053 182.851 6.967 584.025 1.00111.06 C ANISOU 1988 CB PRO A1053 12510 18661 11027 5129 -1013 2431 C ATOM 1989 CG PRO A1053 184.116 6.212 584.296 1.00114.88 C ANISOU 1989 CG PRO A1053 12657 19201 11791 5396 -1150 2460 C ATOM 1990 CD PRO A1053 185.215 7.184 584.012 1.00116.17 C ANISOU 1990 CD PRO A1053 12679 19565 11895 5239 -1236 1805 C ATOM 1991 N ASP A1054 183.246 8.632 586.873 1.00140.06 N ANISOU 1991 N ASP A1054 15974 23864 13376 5732 -1566 2373 N ATOM 1992 CA ASP A1054 182.721 8.995 588.184 1.00137.23 C ANISOU 1992 CA ASP A1054 15637 24127 12379 6062 -1718 2626 C ATOM 1993 C ASP A1054 182.769 10.495 588.449 1.00135.98 C ANISOU 1993 C ASP A1054 15619 24300 11747 5974 -1867 2032 C ATOM 1994 O ASP A1054 182.292 10.936 589.501 1.00133.82 O ANISOU 1994 O ASP A1054 15402 24557 10885 6258 -1987 2140 O ATOM 1995 CB ASP A1054 183.492 8.261 589.286 1.00139.43 C ANISOU 1995 CB ASP A1054 15606 24846 12526 6502 -1965 2990 C ATOM 1996 CG ASP A1054 183.351 6.755 589.195 1.00140.55 C ANISOU 1996 CG ASP A1054 15635 24658 13110 6649 -1851 3662 C ATOM 1997 OD1 ASP A1054 182.747 6.269 588.216 1.00140.15 O ANISOU 1997 OD1 ASP A1054 15735 24009 13505 6383 -1594 3776 O ATOM 1998 OD2 ASP A1054 183.843 6.056 590.106 1.00142.13 O ANISOU 1998 OD2 ASP A1054 15605 25182 13214 7033 -2041 4078 O ATOM 1999 N SER A1055 183.321 11.281 587.530 1.00115.58 N ANISOU 1999 N SER A1055 13100 21413 9400 5594 -1860 1418 N ATOM 2000 CA SER A1055 183.505 12.702 587.769 1.00115.58 C ANISOU 2000 CA SER A1055 13231 21655 9028 5485 -2049 832 C ATOM 2001 C SER A1055 182.166 13.438 587.735 1.00113.11 C ANISOU 2001 C SER A1055 13277 21314 8387 5439 -1911 822 C ATOM 2002 O SER A1055 181.212 12.983 587.099 1.00110.20 O ANISOU 2002 O SER A1055 13055 20597 8221 5320 -1633 1139 O ATOM 2003 CB SER A1055 184.445 13.295 586.724 1.00117.40 C ANISOU 2003 CB SER A1055 13422 21528 9656 5045 -2054 253 C ATOM 2004 OG SER A1055 183.913 13.144 585.419 1.00116.83 O ANISOU 2004 OG SER A1055 13547 20866 9977 4689 -1733 255 O ATOM 2005 N PRO A1056 182.069 14.581 588.421 1.00111.77 N ANISOU 2005 N PRO A1056 13119 19658 9689 2253 -1633 2485 N ATOM 2006 CA PRO A1056 180.837 15.382 588.338 1.00109.94 C ANISOU 2006 CA PRO A1056 12586 19642 9542 2014 -1531 2768 C ATOM 2007 C PRO A1056 180.533 15.883 586.937 1.00109.94 C ANISOU 2007 C PRO A1056 12542 19598 9632 1855 -1467 2832 C ATOM 2008 O PRO A1056 179.371 16.191 586.645 1.00108.67 O ANISOU 2008 O PRO A1056 12249 19553 9487 1591 -1466 3127 O ATOM 2009 CB PRO A1056 181.109 16.546 589.302 1.00109.05 C ANISOU 2009 CB PRO A1056 12033 19789 9613 2243 -1306 2601 C ATOM 2010 CG PRO A1056 182.148 16.024 590.242 1.00109.90 C ANISOU 2010 CG PRO A1056 12266 19855 9637 2536 -1359 2345 C ATOM 2011 CD PRO A1056 183.012 15.118 589.417 1.00111.71 C ANISOU 2011 CD PRO A1056 12898 19772 9776 2601 -1501 2184 C ATOM 2012 N GLU A1057 181.538 15.978 586.063 1.00 95.56 N ANISOU 2012 N GLU A1057 10819 17629 7861 2007 -1414 2569 N ATOM 2013 CA GLU A1057 181.289 16.387 584.685 1.00 95.33 C ANISOU 2013 CA GLU A1057 10772 17571 7876 1857 -1362 2643 C ATOM 2014 C GLU A1057 180.635 15.270 583.882 1.00 96.93 C ANISOU 2014 C GLU A1057 11340 17624 7864 1571 -1603 2850 C ATOM 2015 O GLU A1057 179.717 15.525 583.095 1.00 97.19 O ANISOU 2015 O GLU A1057 11312 17728 7888 1323 -1615 3093 O ATOM 2016 CB GLU A1057 182.595 16.829 584.023 1.00 94.52 C ANISOU 2016 CB GLU A1057 10652 17379 7881 2106 -1216 2291 C ATOM 2017 N MET A1058 181.094 14.029 584.064 1.00107.42 N ANISOU 2017 N MET A1058 13042 18742 9032 1606 -1804 2750 N ATOM 2018 CA MET A1058 180.487 12.905 583.359 1.00108.57 C ANISOU 2018 CA MET A1058 13531 18722 9000 1336 -2045 2919 C ATOM 2019 C MET A1058 179.123 12.547 583.936 1.00107.07 C ANISOU 2019 C MET A1058 13327 18614 8740 1050 -2163 3295 C ATOM 2020 O MET A1058 178.234 12.113 583.195 1.00107.18 O ANISOU 2020 O MET A1058 13461 18594 8669 759 -2293 3509 O ATOM 2021 CB MET A1058 181.415 11.690 583.403 1.00111.48 C ANISOU 2021 CB MET A1058 14288 18812 9257 1470 -2227 2684 C ATOM 2022 CG MET A1058 182.552 11.730 582.393 1.00113.69 C ANISOU 2022 CG MET A1058 14673 18973 9552 1644 -2176 2339 C ATOM 2023 SD MET A1058 181.994 11.451 580.700 1.00115.00 S ANISOU 2023 SD MET A1058 14991 19098 9605 1357 -2266 2431 S ATOM 2024 CE MET A1058 181.280 9.814 580.843 1.00117.07 C ANISOU 2024 CE MET A1058 15654 19123 9706 1106 -2609 2604 C ATOM 2025 N LYS A1059 178.939 12.716 585.248 1.00105.26 N ANISOU 2025 N LYS A1059 12944 18510 8541 1126 -2118 3371 N ATOM 2026 CA LYS A1059 177.649 12.411 585.857 1.00104.03 C ANISOU 2026 CA LYS A1059 12750 18458 8317 853 -2209 3727 C ATOM 2027 C LYS A1059 176.575 13.392 585.404 1.00102.17 C ANISOU 2027 C LYS A1059 12189 18450 8180 648 -2091 3947 C ATOM 2028 O LYS A1059 175.454 12.986 585.078 1.00102.18 O ANISOU 2028 O LYS A1059 12252 18463 8108 335 -2214 4226 O ATOM 2029 CB LYS A1059 177.769 12.413 587.381 1.00103.46 C ANISOU 2029 CB LYS A1059 12569 18508 8234 1001 -2171 3738 C ATOM 2030 CG LYS A1059 178.310 11.120 587.967 1.00105.56 C ANISOU 2030 CG LYS A1059 13209 18547 8354 1078 -2371 3697 C ATOM 2031 CD LYS A1059 178.351 11.183 589.486 1.00104.95 C ANISOU 2031 CD LYS A1059 12997 18644 8236 1216 -2328 3744 C ATOM 2032 CE LYS A1059 178.679 9.828 590.091 1.00107.19 C ANISOU 2032 CE LYS A1059 13662 18703 8363 1244 -2550 3799 C ATOM 2033 NZ LYS A1059 177.623 8.821 589.796 1.00108.23 N ANISOU 2033 NZ LYS A1059 14044 18682 8394 874 -2749 4138 N ATOM 2034 N ASP A1060 176.896 14.687 585.377 1.00 99.20 N ANISOU 2034 N ASP A1060 11456 18248 7988 822 -1858 3822 N ATOM 2035 CA ASP A1060 175.927 15.685 584.946 1.00 98.62 C ANISOU 2035 CA ASP A1060 11053 18376 8041 655 -1745 4026 C ATOM 2036 C ASP A1060 175.746 15.704 583.434 1.00 98.92 C ANISOU 2036 C ASP A1060 11198 18337 8051 507 -1791 4080 C ATOM 2037 O ASP A1060 174.712 16.181 582.954 1.00 99.13 O ANISOU 2037 O ASP A1060 11046 18499 8119 291 -1783 4323 O ATOM 2038 CB ASP A1060 176.341 17.072 585.447 1.00 96.86 C ANISOU 2038 CB ASP A1060 10398 18342 8060 897 -1481 3872 C ATOM 2039 CG ASP A1060 177.028 17.900 584.381 1.00 95.80 C ANISOU 2039 CG ASP A1060 10157 18168 8073 1028 -1330 3709 C ATOM 2040 OD1 ASP A1060 176.330 18.668 583.687 1.00 95.61 O ANISOU 2040 OD1 ASP A1060 9917 18250 8159 890 -1259 3887 O ATOM 2041 OD2 ASP A1060 178.263 17.784 584.237 1.00 95.31 O ANISOU 2041 OD2 ASP A1060 10222 17972 8018 1268 -1283 3409 O ATOM 2042 N PHE A1061 176.723 15.200 582.676 1.00 99.11 N ANISOU 2042 N PHE A1061 11497 18165 7996 622 -1843 3852 N ATOM 2043 CA PHE A1061 176.550 15.073 581.232 1.00 99.80 C ANISOU 2043 CA PHE A1061 11717 18197 8004 470 -1909 3896 C ATOM 2044 C PHE A1061 175.517 14.004 580.904 1.00101.73 C ANISOU 2044 C PHE A1061 12211 18370 8070 141 -2160 4131 C ATOM 2045 O PHE A1061 174.618 14.224 580.084 1.00102.33 O ANISOU 2045 O PHE A1061 12215 18547 8120 -88 -2201 4337 O ATOM 2046 CB PHE A1061 177.890 14.754 580.568 1.00 99.72 C ANISOU 2046 CB PHE A1061 11932 18011 7945 680 -1898 3561 C ATOM 2047 CG PHE A1061 177.786 14.464 579.096 1.00100.78 C ANISOU 2047 CG PHE A1061 12240 18102 7951 528 -1985 3574 C ATOM 2048 CD1 PHE A1061 177.802 13.158 578.631 1.00102.55 C ANISOU 2048 CD1 PHE A1061 12846 18133 7983 401 -2224 3518 C ATOM 2049 CD2 PHE A1061 177.675 15.494 578.178 1.00100.24 C ANISOU 2049 CD2 PHE A1061 11942 18188 7956 513 -1831 3642 C ATOM 2050 CE1 PHE A1061 177.706 12.887 577.279 1.00103.71 C ANISOU 2050 CE1 PHE A1061 13138 18271 7998 265 -2307 3501 C ATOM 2051 CE2 PHE A1061 177.580 15.230 576.824 1.00101.44 C ANISOU 2051 CE2 PHE A1061 12247 18339 7958 377 -1913 3658 C ATOM 2052 CZ PHE A1061 177.597 13.924 576.374 1.00103.17 C ANISOU 2052 CZ PHE A1061 12839 18391 7968 254 -2150 3573 C ATOM 2053 N ARG A1062 175.634 12.832 581.534 1.00102.89 N ANISOU 2053 N ARG A1062 12650 18339 8105 114 -2335 4103 N ATOM 2054 CA ARG A1062 174.612 11.805 581.376 1.00104.91 C ANISOU 2054 CA ARG A1062 13121 18511 8229 -208 -2566 4333 C ATOM 2055 C ARG A1062 173.279 12.254 581.957 1.00105.00 C ANISOU 2055 C ARG A1062 12863 18739 8292 -429 -2537 4662 C ATOM 2056 O ARG A1062 172.220 11.889 581.432 1.00106.36 O ANISOU 2056 O ARG A1062 13078 18934 8399 -730 -2671 4881 O ATOM 2057 CB ARG A1062 175.061 10.505 582.042 1.00106.29 C ANISOU 2057 CB ARG A1062 13645 18431 8310 -172 -2744 4251 C ATOM 2058 CG ARG A1062 176.358 9.931 581.501 1.00106.52 C ANISOU 2058 CG ARG A1062 13955 18223 8293 41 -2802 3908 C ATOM 2059 CD ARG A1062 176.786 8.720 582.313 1.00108.27 C ANISOU 2059 CD ARG A1062 14489 18192 8458 102 -2975 3850 C ATOM 2060 NE ARG A1062 178.026 8.130 581.818 1.00110.34 N ANISOU 2060 NE ARG A1062 15016 18215 8693 313 -3045 3503 N ATOM 2061 CZ ARG A1062 178.650 7.113 582.402 1.00112.93 C ANISOU 2061 CZ ARG A1062 15625 18290 8994 430 -3195 3388 C ATOM 2062 NH1 ARG A1062 178.151 6.573 583.506 1.00112.89 N ANISOU 2062 NH1 ARG A1062 15679 18243 8972 351 -3286 3618 N ATOM 2063 NH2 ARG A1062 179.774 6.635 581.886 1.00116.03 N ANISOU 2063 NH2 ARG A1062 16233 18476 9378 628 -3254 3049 N ATOM 2064 N HIS A1063 173.310 13.045 583.033 1.00103.69 N ANISOU 2064 N HIS A1063 12406 18745 8247 -283 -2367 4679 N ATOM 2065 CA HIS A1063 172.071 13.518 583.640 1.00103.83 C ANISOU 2065 CA HIS A1063 12137 18991 8324 -478 -2325 4962 C ATOM 2066 C HIS A1063 171.328 14.478 582.721 1.00103.36 C ANISOU 2066 C HIS A1063 11805 19107 8362 -606 -2249 5099 C ATOM 2067 O HIS A1063 170.093 14.517 582.737 1.00104.25 O ANISOU 2067 O HIS A1063 11787 19349 8473 -870 -2308 5362 O ATOM 2068 CB HIS A1063 172.364 14.184 584.984 1.00102.65 C ANISOU 2068 CB HIS A1063 11716 19005 8281 -266 -2152 4899 C ATOM 2069 CG HIS A1063 171.136 14.567 585.747 1.00103.05 C ANISOU 2069 CG HIS A1063 11478 19298 8377 -458 -2113 5161 C ATOM 2070 ND1 HIS A1063 170.107 13.683 585.992 1.00104.95 N ANISOU 2070 ND1 HIS A1063 11860 19524 8492 -765 -2280 5422 N ATOM 2071 CD2 HIS A1063 170.770 15.738 586.321 1.00101.94 C ANISOU 2071 CD2 HIS A1063 10903 19422 8407 -389 -1924 5188 C ATOM 2072 CE1 HIS A1063 169.160 14.293 586.681 1.00104.97 C ANISOU 2072 CE1 HIS A1063 11527 19787 8569 -879 -2190 5600 C ATOM 2073 NE2 HIS A1063 169.538 15.541 586.895 1.00103.16 N ANISOU 2073 NE2 HIS A1063 10944 19731 8521 -651 -1978 5455 N ATOM 2074 N GLY A1064 172.057 15.255 581.918 1.00102.16 N ANISOU 2074 N GLY A1064 11559 18962 8295 -424 -2120 4934 N ATOM 2075 CA GLY A1064 171.402 16.127 580.959 1.00102.02 C ANISOU 2075 CA GLY A1064 11308 19095 8359 -537 -2062 5086 C ATOM 2076 C GLY A1064 170.652 15.357 579.888 1.00103.83 C ANISOU 2076 C GLY A1064 11765 19272 8415 -827 -2277 5239 C ATOM 2077 O GLY A1064 169.577 15.773 579.450 1.00104.42 O ANISOU 2077 O GLY A1064 11652 19504 8519 -1032 -2305 5474 O ATOM 2078 N PHE A1065 171.206 14.222 579.454 1.00104.90 N ANISOU 2078 N PHE A1065 12294 19187 8377 -845 -2438 5093 N ATOM 2079 CA PHE A1065 170.501 13.390 578.486 1.00106.90 C ANISOU 2079 CA PHE A1065 12768 19382 8466 -1125 -2659 5201 C ATOM 2080 C PHE A1065 169.358 12.619 579.133 1.00108.42 C ANISOU 2080 C PHE A1065 13014 19565 8615 -1410 -2819 5429 C ATOM 2081 O PHE A1065 168.367 12.308 578.465 1.00109.95 O ANISOU 2081 O PHE A1065 13228 19810 8739 -1685 -2962 5599 O ATOM 2082 CB PHE A1065 171.477 12.432 577.801 1.00107.75 C ANISOU 2082 CB PHE A1065 13260 19253 8426 -1047 -2779 4938 C ATOM 2083 CG PHE A1065 172.321 13.085 576.742 1.00107.00 C ANISOU 2083 CG PHE A1065 13129 19205 8321 -869 -2660 4759 C ATOM 2084 CD1 PHE A1065 173.474 13.771 577.084 1.00105.20 C ANISOU 2084 CD1 PHE A1065 12799 18964 8208 -552 -2453 4546 C ATOM 2085 CD2 PHE A1065 171.960 13.014 575.406 1.00108.29 C ANISOU 2085 CD2 PHE A1065 13351 19439 8354 -1023 -2753 4803 C ATOM 2086 CE1 PHE A1065 174.249 14.376 576.115 1.00104.71 C ANISOU 2086 CE1 PHE A1065 12696 18946 8141 -402 -2329 4395 C ATOM 2087 CE2 PHE A1065 172.733 13.617 574.432 1.00107.85 C ANISOU 2087 CE2 PHE A1065 13260 19449 8268 -868 -2633 4660 C ATOM 2088 CZ PHE A1065 173.880 14.298 574.787 1.00106.06 C ANISOU 2088 CZ PHE A1065 12933 19196 8167 -562 -2416 4462 C ATOM 2089 N ASP A1066 169.475 12.305 580.425 1.00131.57 N ANISOU 2089 N ASP A1066 15962 22446 11584 -1351 -2795 5438 N ATOM 2090 CA ASP A1066 168.378 11.643 581.123 1.00132.68 C ANISOU 2090 CA ASP A1066 16123 22599 11690 -1626 -2918 5679 C ATOM 2091 C ASP A1066 167.173 12.564 581.263 1.00132.42 C ANISOU 2091 C ASP A1066 15701 22816 11798 -1780 -2814 5889 C ATOM 2092 O ASP A1066 166.029 12.097 581.230 1.00134.09 O ANISOU 2092 O ASP A1066 15910 23021 12018 -2073 -2916 6052 O ATOM 2093 CB ASP A1066 168.846 11.160 582.496 1.00132.62 C ANISOU 2093 CB ASP A1066 16209 22502 11680 -1503 -2896 5643 C ATOM 2094 CG ASP A1066 167.902 10.143 583.111 1.00134.83 C ANISOU 2094 CG ASP A1066 16626 22716 11887 -1796 -3057 5876 C ATOM 2095 OD1 ASP A1066 166.979 9.684 582.407 1.00136.45 O ANISOU 2095 OD1 ASP A1066 16894 22874 12075 -2086 -3189 5995 O ATOM 2096 OD2 ASP A1066 168.086 9.802 584.299 1.00135.09 O ANISOU 2096 OD2 ASP A1066 16696 22726 11906 -1732 -3034 5915 O ATOM 2097 N ILE A1067 167.407 13.869 581.420 1.00112.70 N ANISOU 2097 N ILE A1067 12859 20524 9438 -1585 -2608 5869 N ATOM 2098 CA ILE A1067 166.304 14.823 581.466 1.00112.53 C ANISOU 2098 CA ILE A1067 12446 20724 9587 -1709 -2508 6040 C ATOM 2099 C ILE A1067 165.670 14.969 580.089 1.00113.45 C ANISOU 2099 C ILE A1067 12553 20852 9702 -1879 -2589 6111 C ATOM 2100 O ILE A1067 164.450 15.134 579.964 1.00114.47 O ANISOU 2100 O ILE A1067 12500 21087 9907 -2109 -2624 6280 O ATOM 2101 CB ILE A1067 166.795 16.176 582.014 1.00110.43 C ANISOU 2101 CB ILE A1067 11807 20674 9476 -1439 -2282 6004 C ATOM 2102 CG1 ILE A1067 167.355 16.011 583.428 1.00109.77 C ANISOU 2102 CG1 ILE A1067 11715 20588 9403 -1270 -2196 5893 C ATOM 2103 CG2 ILE A1067 165.672 17.203 582.006 1.00110.39 C ANISOU 2103 CG2 ILE A1067 11380 20904 9659 -1557 -2196 6189 C ATOM 2104 CD1 ILE A1067 167.927 17.285 584.011 1.00107.98 C ANISOU 2104 CD1 ILE A1067 11125 20508 9394 -980 -1948 5746 C ATOM 2105 N LEU A1068 166.484 14.901 579.032 1.00108.16 N ANISOU 2105 N LEU A1068 12070 20096 8930 -1766 -2624 5979 N ATOM 2106 CA LEU A1068 165.959 15.062 577.680 1.00109.20 C ANISOU 2106 CA LEU A1068 12192 20268 9032 -1904 -2697 6035 C ATOM 2107 C LEU A1068 165.060 13.895 577.291 1.00111.59 C ANISOU 2107 C LEU A1068 12720 20465 9213 -2219 -2926 6101 C ATOM 2108 O LEU A1068 163.986 14.099 576.714 1.00112.75 O ANISOU 2108 O LEU A1068 12719 20718 9401 -2422 -2982 6239 O ATOM 2109 CB LEU A1068 167.110 15.212 576.686 1.00108.66 C ANISOU 2109 CB LEU A1068 12278 20159 8850 -1708 -2674 5871 C ATOM 2110 CG LEU A1068 166.755 15.807 575.322 1.00109.37 C ANISOU 2110 CG LEU A1068 12261 20361 8933 -1765 -2673 5936 C ATOM 2111 CD1 LEU A1068 166.277 17.242 575.476 1.00108.31 C ANISOU 2111 CD1 LEU A1068 11688 20427 9037 -1697 -2489 6103 C ATOM 2112 CD2 LEU A1068 167.944 15.735 574.380 1.00109.21 C ANISOU 2112 CD2 LEU A1068 12445 20304 8748 -1592 -2665 5761 C ATOM 2113 N VAL A1069 165.480 12.664 577.599 1.00112.51 N ANISOU 2113 N VAL A1069 13186 20378 9183 -2263 -3073 6012 N ATOM 2114 CA VAL A1069 164.650 11.499 577.305 1.00114.98 C ANISOU 2114 CA VAL A1069 13713 20583 9391 -2573 -3304 6088 C ATOM 2115 C VAL A1069 163.355 11.546 578.105 1.00115.75 C ANISOU 2115 C VAL A1069 13589 20778 9613 -2804 -3295 6303 C ATOM 2116 O VAL A1069 162.300 11.115 577.622 1.00117.68 O ANISOU 2116 O VAL A1069 13829 21052 9832 -3087 -3439 6420 O ATOM 2117 CB VAL A1069 165.438 10.200 577.574 1.00115.89 C ANISOU 2117 CB VAL A1069 14240 20446 9348 -2559 -3467 5968 C ATOM 2118 CG1 VAL A1069 164.572 8.978 577.307 1.00118.68 C ANISOU 2118 CG1 VAL A1069 14806 20679 9609 -2898 -3720 6065 C ATOM 2119 CG2 VAL A1069 166.695 10.158 576.719 1.00115.30 C ANISOU 2119 CG2 VAL A1069 14366 20309 9133 -2343 -3488 5742 C ATOM 2120 N GLY A1070 163.406 12.075 579.329 1.00114.41 N ANISOU 2120 N GLY A1070 13217 20685 9567 -2692 -3130 6351 N ATOM 2121 CA GLY A1070 162.190 12.213 580.113 1.00115.16 C ANISOU 2121 CA GLY A1070 13065 20920 9771 -2904 -3104 6550 C ATOM 2122 C GLY A1070 161.205 13.188 579.496 1.00115.19 C ANISOU 2122 C GLY A1070 12718 21152 9898 -3006 -3057 6670 C ATOM 2123 O GLY A1070 159.990 12.982 579.562 1.00116.77 O ANISOU 2123 O GLY A1070 12795 21444 10128 -3282 -3138 6835 O ATOM 2124 N GLN A1071 161.713 14.263 578.889 1.00113.62 N ANISOU 2124 N GLN A1071 12348 21051 9772 -2789 -2932 6604 N ATOM 2125 CA GLN A1071 160.841 15.212 578.207 1.00113.84 C ANISOU 2125 CA GLN A1071 12054 21280 9920 -2865 -2901 6732 C ATOM 2126 C GLN A1071 160.416 14.708 576.833 1.00115.69 C ANISOU 2126 C GLN A1071 12453 21474 10029 -3038 -3082 6737 C ATOM 2127 O GLN A1071 159.355 15.102 576.335 1.00116.77 O ANISOU 2127 O GLN A1071 12372 21767 10230 -3203 -3129 6878 O ATOM 2128 CB GLN A1071 161.537 16.568 578.077 1.00111.75 C ANISOU 2128 CB GLN A1071 11534 21133 9793 -2573 -2701 6694 C ATOM 2129 CG GLN A1071 161.839 17.251 579.401 1.00110.05 C ANISOU 2129 CG GLN A1071 11070 21027 9718 -2401 -2520 6698 C ATOM 2130 CD GLN A1071 162.605 18.548 579.223 1.00108.17 C ANISOU 2130 CD GLN A1071 10586 20896 9619 -2110 -2336 6662 C ATOM 2131 OE1 GLN A1071 162.664 19.378 580.130 1.00106.97 O ANISOU 2131 OE1 GLN A1071 10123 20902 9617 -1975 -2189 6696 O ATOM 2132 NE2 GLN A1071 163.201 18.727 578.050 1.00108.09 N ANISOU 2132 NE2 GLN A1071 10700 20817 9554 -2014 -2346 6600 N ATOM 2133 N ILE A1072 161.224 13.847 576.209 1.00116.21 N ANISOU 2133 N ILE A1072 12889 21355 9909 -2998 -3195 6580 N ATOM 2134 CA ILE A1072 160.838 13.260 574.929 1.00118.25 C ANISOU 2134 CA ILE A1072 13315 21598 10016 -3171 -3387 6563 C ATOM 2135 C ILE A1072 159.667 12.302 575.115 1.00120.58 C ANISOU 2135 C ILE A1072 13669 21878 10268 -3519 -3581 6687 C ATOM 2136 O ILE A1072 158.703 12.320 574.339 1.00122.26 O ANISOU 2136 O ILE A1072 13778 22215 10460 -3717 -3695 6778 O ATOM 2137 CB ILE A1072 162.045 12.561 574.275 1.00118.33 C ANISOU 2137 CB ILE A1072 13695 21438 9827 -3039 -3465 6348 C ATOM 2138 CG1 ILE A1072 163.032 13.595 573.728 1.00116.56 C ANISOU 2138 CG1 ILE A1072 13377 21283 9625 -2740 -3289 6252 C ATOM 2139 CG2 ILE A1072 161.591 11.618 573.170 1.00120.93 C ANISOU 2139 CG2 ILE A1072 14243 21741 9965 -3267 -3712 6313 C ATOM 2140 CD1 ILE A1072 164.268 12.988 573.103 1.00116.61 C ANISOU 2140 CD1 ILE A1072 13718 21159 9428 -2598 -3350 6031 C ATOM 2141 N ASP A1073 159.726 11.457 576.147 1.00120.90 N ANISOU 2141 N ASP A1073 13870 21775 10290 -3602 -3625 6704 N ATOM 2142 CA ASP A1073 158.635 10.523 576.401 1.00123.28 C ANISOU 2142 CA ASP A1073 14227 22057 10558 -3952 -3805 6848 C ATOM 2143 C ASP A1073 157.386 11.237 576.902 1.00123.47 C ANISOU 2143 C ASP A1073 13859 22313 10742 -4105 -3729 7052 C ATOM 2144 O ASP A1073 156.270 10.744 576.699 1.00125.66 O ANISOU 2144 O ASP A1073 14093 22657 10995 -4415 -3885 7185 O ATOM 2145 CB ASP A1073 159.081 9.452 577.396 1.00123.76 C ANISOU 2145 CB ASP A1073 14568 21893 10562 -3992 -3862 6841 C ATOM 2146 CG ASP A1073 160.112 8.507 576.808 1.00124.36 C ANISOU 2146 CG ASP A1073 15057 21732 10462 -3918 -4015 6660 C ATOM 2147 OD1 ASP A1073 159.966 8.130 575.626 1.00125.83 O ANISOU 2147 OD1 ASP A1073 15364 21919 10527 -4029 -4187 6592 O ATOM 2148 OD2 ASP A1073 161.068 8.145 577.525 1.00123.49 O ANISOU 2148 OD2 ASP A1073 15141 21451 10329 -3746 -3973 6579 O ATOM 2149 N ASP A1074 157.546 12.391 577.555 1.00121.36 N ANISOU 2149 N ASP A1074 13290 22186 10636 -3902 -3505 7077 N ATOM 2150 CA ASP A1074 156.382 13.195 577.909 1.00121.58 C ANISOU 2150 CA ASP A1074 12910 22466 10817 -4029 -3441 7260 C ATOM 2151 C ASP A1074 155.769 13.853 576.678 1.00122.27 C ANISOU 2151 C ASP A1074 12815 22708 10934 -4073 -3495 7307 C ATOM 2152 O ASP A1074 154.554 14.084 576.641 1.00123.58 O ANISOU 2152 O ASP A1074 12729 23059 11168 -4287 -3553 7470 O ATOM 2153 CB ASP A1074 156.763 14.250 578.949 1.00119.29 C ANISOU 2153 CB ASP A1074 12339 22298 10689 -3795 -3202 7265 C ATOM 2154 CG ASP A1074 157.023 13.652 580.322 1.00119.13 C ANISOU 2154 CG ASP A1074 12416 22204 10643 -3803 -3149 7269 C ATOM 2155 OD1 ASP A1074 156.985 12.410 580.450 1.00120.74 O ANISOU 2155 OD1 ASP A1074 12931 22227 10716 -3978 -3295 7277 O ATOM 2156 OD2 ASP A1074 157.262 14.425 581.274 1.00117.57 O ANISOU 2156 OD2 ASP A1074 11979 22139 10553 -3635 -2968 7271 O ATOM 2157 N ALA A1075 156.587 14.157 575.667 1.00121.58 N ANISOU 2157 N ALA A1075 12845 22562 10786 -3874 -3480 7175 N ATOM 2158 CA ALA A1075 156.063 14.676 574.409 1.00122.61 C ANISOU 2158 CA ALA A1075 12847 22832 10909 -3912 -3545 7221 C ATOM 2159 C ALA A1075 155.472 13.567 573.549 1.00125.33 C ANISOU 2159 C ALA A1075 13416 23139 11066 -4182 -3801 7209 C ATOM 2160 O ALA A1075 154.477 13.792 572.850 1.00126.98 O ANISOU 2160 O ALA A1075 13453 23515 11279 -4341 -3901 7314 O ATOM 2161 CB ALA A1075 157.165 15.411 573.642 1.00121.14 C ANISOU 2161 CB ALA A1075 12699 22619 10710 -3608 -3425 7101 C ATOM 2162 N LEU A1076 156.069 12.372 573.584 1.00138.58 N ANISOU 2162 N LEU A1076 15470 24606 12579 -4236 -3923 7082 N ATOM 2163 CA LEU A1076 155.496 11.239 572.866 1.00141.40 C ANISOU 2163 CA LEU A1076 16036 24925 12762 -4518 -4190 7069 C ATOM 2164 C LEU A1076 154.141 10.849 573.444 1.00143.18 C ANISOU 2164 C LEU A1076 16107 25246 13051 -4854 -4299 7264 C ATOM 2165 O LEU A1076 153.246 10.436 572.697 1.00145.58 O ANISOU 2165 O LEU A1076 16391 25648 13276 -5101 -4496 7311 O ATOM 2166 CB LEU A1076 156.465 10.054 572.901 1.00141.77 C ANISOU 2166 CB LEU A1076 16510 24713 12643 -4502 -4304 6903 C ATOM 2167 CG LEU A1076 156.416 9.005 571.781 1.00144.35 C ANISOU 2167 CG LEU A1076 17113 24986 12749 -4677 -4577 6787 C ATOM 2168 CD1 LEU A1076 157.719 8.225 571.749 1.00143.96 C ANISOU 2168 CD1 LEU A1076 17442 24697 12560 -4534 -4628 6583 C ATOM 2169 CD2 LEU A1076 155.242 8.048 571.931 1.00147.14 C ANISOU 2169 CD2 LEU A1076 17491 25343 13073 -5075 -4812 6916 C ATOM 2170 N LYS A1077 153.972 10.975 574.762 1.00129.60 N ANISOU 2170 N LYS A1077 14263 23518 11460 -4873 -4177 7374 N ATOM 2171 CA LYS A1077 152.685 10.675 575.379 1.00131.32 C ANISOU 2171 CA LYS A1077 14303 23857 11735 -5196 -4258 7575 C ATOM 2172 C LYS A1077 151.608 11.629 574.880 1.00131.87 C ANISOU 2172 C LYS A1077 13985 24211 11909 -5266 -4250 7697 C ATOM 2173 O LYS A1077 150.568 11.197 574.370 1.00134.32 O ANISOU 2173 O LYS A1077 14241 24629 12166 -5552 -4442 7783 O ATOM 2174 CB LYS A1077 152.806 10.743 576.902 1.00130.11 C ANISOU 2174 CB LYS A1077 14072 23677 11686 -5163 -4095 7659 C ATOM 2175 CG LYS A1077 151.480 10.591 577.635 1.00131.79 C ANISOU 2175 CG LYS A1077 14048 24063 11963 -5483 -4139 7883 C ATOM 2176 CD LYS A1077 151.651 10.786 579.134 1.00130.59 C ANISOU 2176 CD LYS A1077 13787 23931 11898 -5416 -3949 7954 C ATOM 2177 CE LYS A1077 150.318 10.689 579.863 1.00132.39 C ANISOU 2177 CE LYS A1077 13754 24373 12176 -5740 -3976 8182 C ATOM 2178 NZ LYS A1077 149.336 11.689 579.358 1.00132.60 N ANISOU 2178 NZ LYS A1077 13376 24699 12308 -5794 -3978 8269 N ATOM 2179 N LEU A1078 151.851 12.938 575.006 1.00129.75 N ANISOU 2179 N LEU A1078 13439 24068 11794 -5007 -4041 7707 N ATOM 2180 CA LEU A1078 150.864 13.928 574.585 1.00130.29 C ANISOU 2180 CA LEU A1078 13123 24396 11984 -5048 -4027 7840 C ATOM 2181 C LEU A1078 150.548 13.818 573.100 1.00132.11 C ANISOU 2181 C LEU A1078 13419 24679 12098 -5107 -4195 7800 C ATOM 2182 O LEU A1078 149.436 14.154 572.678 1.00133.74 O ANISOU 2182 O LEU A1078 13377 25087 12351 -5263 -4281 7923 O ATOM 2183 CB LEU A1078 151.360 15.335 574.921 1.00127.76 C ANISOU 2183 CB LEU A1078 12528 24163 11852 -4735 -3783 7851 C ATOM 2184 CG LEU A1078 151.502 15.666 576.408 1.00126.13 C ANISOU 2184 CG LEU A1078 12156 23992 11776 -4669 -3610 7900 C ATOM 2185 CD1 LEU A1078 152.181 17.013 576.599 1.00123.69 C ANISOU 2185 CD1 LEU A1078 11610 23748 11639 -4337 -3388 7876 C ATOM 2186 CD2 LEU A1078 150.142 15.648 577.089 1.00127.67 C ANISOU 2186 CD2 LEU A1078 12062 24402 12044 -4953 -3662 8091 C ATOM 2187 N ALA A1079 151.506 13.353 572.294 1.00147.65 N ANISOU 2187 N ALA A1079 15708 26487 13904 -4980 -4245 7623 N ATOM 2188 CA ALA A1079 151.236 13.146 570.876 1.00149.70 C ANISOU 2188 CA ALA A1079 16046 26820 14012 -5043 -4414 7566 C ATOM 2189 C ALA A1079 150.234 12.020 570.655 1.00152.72 C ANISOU 2189 C ALA A1079 16516 27235 14277 -5416 -4682 7599 C ATOM 2190 O ALA A1079 149.495 12.035 569.664 1.00154.86 O ANISOU 2190 O ALA A1079 16701 27664 14475 -5533 -4830 7614 O ATOM 2191 CB ALA A1079 152.537 12.856 570.129 1.00149.03 C ANISOU 2191 CB ALA A1079 16285 26579 13762 -4828 -4406 7355 C ATOM 2192 N ASN A1080 150.192 11.043 571.561 1.00161.14 N ANISOU 2192 N ASN A1080 17746 28158 15321 -5609 -4754 7618 N ATOM 2193 CA ASN A1080 149.239 9.945 571.461 1.00164.15 C ANISOU 2193 CA ASN A1080 18202 28557 15609 -5995 -5017 7671 C ATOM 2194 C ASN A1080 147.927 10.225 572.180 1.00165.07 C ANISOU 2194 C ASN A1080 17980 28869 15870 -6236 -5021 7891 C ATOM 2195 O ASN A1080 146.907 9.620 571.832 1.00167.84 O ANISOU 2195 O ASN A1080 18284 29321 16168 -6553 -5241 7946 O ATOM 2196 CB ASN A1080 149.856 8.655 572.012 1.00164.61 C ANISOU 2196 CB ASN A1080 18637 28345 15562 -6111 -5122 7605 C ATOM 2197 CG ASN A1080 150.884 8.053 571.074 1.00164.91 C ANISOU 2197 CG ASN A1080 19026 28219 15412 -5984 -5229 7370 C ATOM 2198 OD1 ASN A1080 152.058 8.421 571.100 1.00162.66 O ANISOU 2198 OD1 ASN A1080 18867 27818 15119 -5671 -5066 7248 O ATOM 2199 ND2 ASN A1080 150.445 7.119 570.238 1.00167.84 N ANISOU 2199 ND2 ASN A1080 19545 28596 15630 -6234 -5513 7290 N ATOM 2200 N GLU A1081 147.925 11.120 573.172 1.00158.10 N ANISOU 2200 N GLU A1081 17302 22954 19813 -2039 405 3835 N ATOM 2201 CA GLU A1081 146.683 11.476 573.847 1.00161.22 C ANISOU 2201 CA GLU A1081 17326 23955 19975 -2105 696 3796 C ATOM 2202 C GLU A1081 145.760 12.298 572.958 1.00161.50 C ANISOU 2202 C GLU A1081 17268 23840 20254 -1833 787 3359 C ATOM 2203 O GLU A1081 144.560 12.384 573.241 1.00163.84 O ANISOU 2203 O GLU A1081 17217 24538 20498 -1889 972 3358 O ATOM 2204 CB GLU A1081 146.973 12.259 575.131 1.00163.31 C ANISOU 2204 CB GLU A1081 17530 24857 19665 -2082 960 3616 C ATOM 2205 CG GLU A1081 148.009 11.638 576.062 1.00162.99 C ANISOU 2205 CG GLU A1081 17626 24967 19335 -2308 868 3973 C ATOM 2206 CD GLU A1081 147.510 10.395 576.775 1.00164.24 C ANISOU 2206 CD GLU A1081 17564 25437 19404 -2729 832 4606 C ATOM 2207 OE1 GLU A1081 147.287 9.364 576.107 1.00163.08 O ANISOU 2207 OE1 GLU A1081 17421 24885 19658 -2895 585 4967 O ATOM 2208 OE2 GLU A1081 147.344 10.450 578.012 1.00166.29 O ANISOU 2208 OE2 GLU A1081 17653 26348 19181 -2901 1037 4747 O ATOM 2209 N GLY A1082 146.289 12.896 571.894 1.00152.93 N ANISOU 2209 N GLY A1082 16479 22198 19427 -1547 653 2992 N ATOM 2210 CA GLY A1082 145.548 13.814 571.054 1.00153.05 C ANISOU 2210 CA GLY A1082 16473 22035 19645 -1260 709 2530 C ATOM 2211 C GLY A1082 146.074 15.230 571.086 1.00153.36 C ANISOU 2211 C GLY A1082 16709 22093 19469 -955 810 1973 C ATOM 2212 O GLY A1082 145.602 16.069 570.307 1.00153.21 O ANISOU 2212 O GLY A1082 16742 21840 19628 -697 804 1560 O ATOM 2213 N LYS A1083 147.035 15.524 571.960 1.00108.97 N ANISOU 2213 N LYS A1083 11206 16722 13476 -983 874 1951 N ATOM 2214 CA LYS A1083 147.637 16.853 572.052 1.00109.01 C ANISOU 2214 CA LYS A1083 11417 16730 13270 -716 934 1445 C ATOM 2215 C LYS A1083 148.909 16.922 571.204 1.00106.07 C ANISOU 2215 C LYS A1083 11445 15755 13101 -638 711 1379 C ATOM 2216 O LYS A1083 150.014 17.150 571.694 1.00105.41 O ANISOU 2216 O LYS A1083 11542 15717 12794 -651 690 1352 O ATOM 2217 CB LYS A1083 147.924 17.200 573.509 1.00110.73 C ANISOU 2217 CB LYS A1083 11526 17589 12958 -777 1127 1426 C ATOM 2218 CG LYS A1083 146.695 17.554 574.328 1.00113.74 C ANISOU 2218 CG LYS A1083 11522 18630 13064 -758 1391 1306 C ATOM 2219 CD LYS A1083 146.181 18.939 573.974 1.00114.48 C ANISOU 2219 CD LYS A1083 11629 18708 13161 -397 1452 680 C ATOM 2220 CE LYS A1083 145.073 19.375 574.918 1.00117.52 C ANISOU 2220 CE LYS A1083 11617 19824 13212 -337 1722 495 C ATOM 2221 NZ LYS A1083 144.627 20.769 574.641 1.00118.14 N ANISOU 2221 NZ LYS A1083 11723 19884 13279 48 1741 -157 N ATOM 2222 N VAL A1084 148.728 16.710 569.898 1.00112.95 N ANISOU 2222 N VAL A1084 12445 16069 14401 -558 543 1351 N ATOM 2223 CA VAL A1084 149.859 16.779 568.979 1.00109.91 C ANISOU 2223 CA VAL A1084 12416 15130 14214 -478 347 1273 C ATOM 2224 C VAL A1084 150.405 18.199 568.906 1.00110.20 C ANISOU 2224 C VAL A1084 12673 15115 14083 -256 388 783 C ATOM 2225 O VAL A1084 151.610 18.400 568.710 1.00108.54 O ANISOU 2225 O VAL A1084 12718 14679 13842 -244 294 729 O ATOM 2226 CB VAL A1084 149.450 16.256 567.589 1.00107.04 C ANISOU 2226 CB VAL A1084 12136 14214 14321 -429 162 1336 C ATOM 2227 CG1 VAL A1084 150.672 16.093 566.698 1.00103.24 C ANISOU 2227 CG1 VAL A1084 11987 13224 14016 -384 -33 1328 C ATOM 2228 CG2 VAL A1084 148.699 14.939 567.719 1.00107.00 C ANISOU 2228 CG2 VAL A1084 11880 14286 14489 -646 108 1798 C ATOM 2229 N LYS A1085 149.539 19.203 569.068 1.00 96.70 N ANISOU 2229 N LYS A1085 10860 13612 12269 -80 510 415 N ATOM 2230 CA LYS A1085 150.008 20.583 569.105 1.00 96.68 C ANISOU 2230 CA LYS A1085 11066 13574 12093 125 515 -52 C ATOM 2231 C LYS A1085 150.783 20.873 570.384 1.00 97.14 C ANISOU 2231 C LYS A1085 11115 14067 11725 65 615 -58 C ATOM 2232 O LYS A1085 151.701 21.701 570.377 1.00 95.57 O ANISOU 2232 O LYS A1085 11164 13733 11414 152 551 -307 O ATOM 2233 CB LYS A1085 148.830 21.550 568.972 1.00 98.38 C ANISOU 2233 CB LYS A1085 11168 13892 12320 353 578 -462 C ATOM 2234 CG LYS A1085 147.597 20.964 568.297 1.00 98.81 C ANISOU 2234 CG LYS A1085 11019 13828 12695 355 565 -350 C ATOM 2235 CD LYS A1085 146.609 20.425 569.323 1.00101.47 C ANISOU 2235 CD LYS A1085 10923 14782 12850 238 769 -156 C ATOM 2236 CE LYS A1085 145.404 19.787 568.654 1.00101.63 C ANISOU 2236 CE LYS A1085 10719 14680 13214 211 741 -15 C ATOM 2237 NZ LYS A1085 144.442 19.246 569.653 1.00104.39 N ANISOU 2237 NZ LYS A1085 10618 15665 13379 59 951 201 N ATOM 2238 N GLU A1086 150.428 20.207 571.485 1.00127.03 N ANISOU 2238 N GLU A1086 14623 18377 15267 -97 762 222 N ATOM 2239 CA GLU A1086 151.166 20.374 572.731 1.00127.22 C ANISOU 2239 CA GLU A1086 14643 18823 14870 -168 845 253 C ATOM 2240 C GLU A1086 152.495 19.632 572.703 1.00125.16 C ANISOU 2240 C GLU A1086 14576 18327 14651 -342 702 567 C ATOM 2241 O GLU A1086 153.457 20.068 573.346 1.00124.03 O ANISOU 2241 O GLU A1086 14567 18308 14251 -337 689 472 O ATOM 2242 CB GLU A1086 150.315 19.900 573.912 1.00129.68 C ANISOU 2242 CB GLU A1086 14595 19799 14877 -298 1053 462 C ATOM 2243 CG GLU A1086 150.903 20.215 575.277 1.00130.00 C ANISOU 2243 CG GLU A1086 14620 20350 14426 -335 1158 434 C ATOM 2244 CD GLU A1086 149.999 19.782 576.414 1.00132.59 C ANISOU 2244 CD GLU A1086 14584 21377 14418 -470 1384 634 C ATOM 2245 OE1 GLU A1086 148.864 19.340 576.137 1.00134.19 O ANISOU 2245 OE1 GLU A1086 14524 21683 14778 -523 1470 757 O ATOM 2246 OE2 GLU A1086 150.423 19.882 577.585 1.00132.99 O ANISOU 2246 OE2 GLU A1086 14605 21886 14038 -531 1475 673 O ATOM 2247 N ALA A1087 152.569 18.516 571.973 1.00 90.98 N ANISOU 2247 N ALA A1087 10260 13659 10648 -482 573 923 N ATOM 2248 CA ALA A1087 153.849 17.840 571.788 1.00 88.77 C ANISOU 2248 CA ALA A1087 10170 13101 10457 -600 402 1162 C ATOM 2249 C ALA A1087 154.819 18.718 571.007 1.00 86.24 C ANISOU 2249 C ALA A1087 10151 12377 10238 -443 298 826 C ATOM 2250 O ALA A1087 156.025 18.722 571.281 1.00 84.52 O ANISOU 2250 O ALA A1087 10077 12119 9915 -492 221 854 O ATOM 2251 CB ALA A1087 153.642 16.501 571.081 1.00 88.03 C ANISOU 2251 CB ALA A1087 10031 12700 10718 -741 254 1563 C ATOM 2252 N GLN A1088 154.308 19.470 570.028 1.00118.06 N ANISOU 2252 N GLN A1088 14278 16108 14472 -268 284 514 N ATOM 2253 CA GLN A1088 155.135 20.468 569.359 1.00115.43 C ANISOU 2253 CA GLN A1088 14230 15442 14186 -140 198 179 C ATOM 2254 C GLN A1088 155.523 21.592 570.309 1.00115.59 C ANISOU 2254 C GLN A1088 14300 15773 13846 -64 268 -121 C ATOM 2255 O GLN A1088 156.625 22.142 570.201 1.00113.23 O ANISOU 2255 O GLN A1088 14213 15312 13498 -57 183 -261 O ATOM 2256 CB GLN A1088 154.404 21.029 568.138 1.00115.01 C ANISOU 2256 CB GLN A1088 14281 15006 14412 20 147 -74 C ATOM 2257 CG GLN A1088 154.238 20.035 566.999 1.00113.92 C ANISOU 2257 CG GLN A1088 14170 14462 14652 -26 30 168 C ATOM 2258 CD GLN A1088 153.546 20.641 565.793 1.00113.18 C ANISOU 2258 CD GLN A1088 14208 13981 14814 137 -36 -94 C ATOM 2259 OE1 GLN A1088 152.684 21.509 565.928 1.00115.01 O ANISOU 2259 OE1 GLN A1088 14392 14324 14982 274 24 -381 O ATOM 2260 NE2 GLN A1088 153.927 20.190 564.603 1.00109.22 N ANISOU 2260 NE2 GLN A1088 13877 13025 14596 135 -174 -11 N ATOM 2261 N ALA A1089 154.636 21.947 571.242 1.00148.89 N ANISOU 2261 N ALA A1089 18315 20447 17808 -6 416 -231 N ATOM 2262 CA ALA A1089 154.988 22.910 572.277 1.00149.14 C ANISOU 2262 CA ALA A1089 18376 20823 17466 75 471 -503 C ATOM 2263 C ALA A1089 155.998 22.340 573.263 1.00148.59 C ANISOU 2263 C ALA A1089 18296 21011 17148 -95 471 -238 C ATOM 2264 O ALA A1089 156.723 23.107 573.905 1.00147.83 O ANISOU 2264 O ALA A1089 18315 21050 16802 -44 446 -449 O ATOM 2265 CB ALA A1089 153.733 23.373 573.018 1.00152.06 C ANISOU 2265 CB ALA A1089 18505 21661 17612 202 635 -703 C ATOM 2266 N ALA A1090 156.059 21.013 573.394 1.00 87.70 N ANISOU 2266 N ALA A1090 10460 13349 9512 -293 467 216 N ATOM 2267 CA ALA A1090 157.072 20.376 574.224 1.00 88.46 C ANISOU 2267 CA ALA A1090 10573 13619 9418 -458 417 490 C ATOM 2268 C ALA A1090 158.449 20.399 573.576 1.00 85.55 C ANISOU 2268 C ALA A1090 10447 12829 9229 -476 237 470 C ATOM 2269 O ALA A1090 159.449 20.181 574.269 1.00 86.13 O ANISOU 2269 O ALA A1090 10569 13025 9132 -567 172 583 O ATOM 2270 CB ALA A1090 156.669 18.933 574.533 1.00 89.85 C ANISOU 2270 CB ALA A1090 10555 13945 9639 -671 424 991 C ATOM 2271 N ALA A1091 158.524 20.649 572.266 1.00120.95 N ANISOU 2271 N ALA A1091 15074 16838 14044 -395 156 328 N ATOM 2272 CA ALA A1091 159.822 20.771 571.613 1.00117.96 C ANISOU 2272 CA ALA A1091 14904 16104 13812 -412 11 275 C ATOM 2273 C ALA A1091 160.561 22.020 572.074 1.00116.96 C ANISOU 2273 C ALA A1091 14926 16057 13458 -343 -3 -60 C ATOM 2274 O ALA A1091 161.796 22.022 572.129 1.00115.20 O ANISOU 2274 O ALA A1091 14808 15742 13220 -410 -104 -41 O ATOM 2275 CB ALA A1091 159.649 20.782 570.095 1.00116.12 C ANISOU 2275 CB ALA A1091 14790 15382 13949 -346 -58 200 C ATOM 2276 N GLU A1092 159.828 23.086 572.403 1.00144.88 N ANISOU 2276 N GLU A1092 18465 19757 16824 -203 75 -380 N ATOM 2277 CA GLU A1092 160.463 24.274 572.962 1.00144.41 C ANISOU 2277 CA GLU A1092 18547 19789 16532 -132 28 -702 C ATOM 2278 C GLU A1092 161.041 23.995 574.343 1.00145.27 C ANISOU 2278 C GLU A1092 18573 20317 16305 -212 48 -571 C ATOM 2279 O GLU A1092 162.074 24.566 574.708 1.00144.18 O ANISOU 2279 O GLU A1092 18568 20168 16045 -225 -50 -706 O ATOM 2280 CB GLU A1092 159.461 25.427 573.024 1.00145.91 C ANISOU 2280 CB GLU A1092 18754 20060 16625 67 73 -1091 C ATOM 2281 CG GLU A1092 158.890 25.822 571.671 1.00145.20 C ANISOU 2281 CG GLU A1092 18780 19533 16856 157 20 -1251 C ATOM 2282 CD GLU A1092 157.840 26.910 571.776 1.00147.06 C ANISOU 2282 CD GLU A1092 19018 19851 17007 374 33 -1645 C ATOM 2283 OE1 GLU A1092 157.522 27.324 572.910 1.00148.85 O ANISOU 2283 OE1 GLU A1092 19132 20507 16915 466 102 -1802 O ATOM 2284 OE2 GLU A1092 157.331 27.351 570.724 1.00146.73 O ANISOU 2284 OE2 GLU A1092 19092 19448 17209 464 -39 -1812 O ATOM 2285 N GLN A1093 160.390 23.125 575.120 1.00109.94 N ANISOU 2285 N GLN A1093 13885 16213 11675 -281 162 -301 N ATOM 2286 CA GLN A1093 160.969 22.694 576.388 1.00110.64 C ANISOU 2286 CA GLN A1093 13910 16682 11447 -387 163 -113 C ATOM 2287 C GLN A1093 162.216 21.851 576.155 1.00108.95 C ANISOU 2287 C GLN A1093 13770 16231 11394 -542 8 163 C ATOM 2288 O GLN A1093 163.186 21.941 576.916 1.00108.55 O ANISOU 2288 O GLN A1093 13779 16315 11149 -591 -75 171 O ATOM 2289 CB GLN A1093 159.934 21.914 577.199 1.00113.19 C ANISOU 2289 CB GLN A1093 13988 17454 11567 -461 319 153 C ATOM 2290 CG GLN A1093 158.497 22.391 577.021 1.00115.04 C ANISOU 2290 CG GLN A1093 14080 17842 11789 -322 479 -49 C ATOM 2291 CD GLN A1093 158.259 23.785 577.572 1.00115.69 C ANISOU 2291 CD GLN A1093 14209 18154 11594 -105 525 -528 C ATOM 2292 OE1 GLN A1093 159.012 24.272 578.414 1.00115.31 O ANISOU 2292 OE1 GLN A1093 14253 18294 11264 -84 473 -653 O ATOM 2293 NE2 GLN A1093 157.202 24.435 577.096 1.00116.77 N ANISOU 2293 NE2 GLN A1093 14287 18262 11818 71 595 -814 N ATOM 2294 N LEU A1094 162.205 21.023 575.106 1.00 85.59 N ANISOU 2294 N LEU A1094 10804 12924 8793 -603 -47 373 N ATOM 2295 CA LEU A1094 163.396 20.262 574.746 1.00 84.06 C ANISOU 2295 CA LEU A1094 10673 12480 8786 -708 -212 577 C ATOM 2296 C LEU A1094 164.538 21.191 574.360 1.00 82.57 C ANISOU 2296 C LEU A1094 10663 12069 8641 -661 -305 288 C ATOM 2297 O LEU A1094 165.685 20.988 574.776 1.00 82.85 O ANISOU 2297 O LEU A1094 10732 12128 8619 -733 -421 352 O ATOM 2298 CB LEU A1094 163.074 19.304 573.598 1.00 82.04 C ANISOU 2298 CB LEU A1094 10382 11880 8909 -738 -262 792 C ATOM 2299 CG LEU A1094 162.056 18.193 573.859 1.00 83.48 C ANISOU 2299 CG LEU A1094 10386 12212 9120 -827 -223 1146 C ATOM 2300 CD1 LEU A1094 161.582 17.588 572.547 1.00 81.30 C ANISOU 2300 CD1 LEU A1094 10108 11540 9242 -802 -276 1240 C ATOM 2301 CD2 LEU A1094 162.661 17.123 574.745 1.00 85.26 C ANISOU 2301 CD2 LEU A1094 10551 12617 9228 -987 -343 1508 C ATOM 2302 N LYS A1095 164.239 22.222 573.563 1.00 87.66 N ANISOU 2302 N LYS A1095 11423 12493 9392 -553 -272 -26 N ATOM 2303 CA LYS A1095 165.251 23.191 573.166 1.00 85.66 C ANISOU 2303 CA LYS A1095 11344 12027 9174 -540 -366 -291 C ATOM 2304 C LYS A1095 165.777 23.991 574.353 1.00 86.51 C ANISOU 2304 C LYS A1095 11496 12419 8954 -527 -402 -469 C ATOM 2305 O LYS A1095 166.903 24.493 574.295 1.00 85.16 O ANISOU 2305 O LYS A1095 11433 12129 8794 -573 -516 -588 O ATOM 2306 CB LYS A1095 164.678 24.131 572.102 1.00 84.76 C ANISOU 2306 CB LYS A1095 11364 11616 9225 -441 -345 -568 C ATOM 2307 CG LYS A1095 165.694 24.628 571.089 1.00 82.12 C ANISOU 2307 CG LYS A1095 11197 10921 9085 -494 -448 -691 C ATOM 2308 CD LYS A1095 165.023 25.430 569.981 1.00 81.51 C ANISOU 2308 CD LYS A1095 11267 10530 9173 -414 -444 -912 C ATOM 2309 CE LYS A1095 166.021 25.815 568.898 1.00 79.13 C ANISOU 2309 CE LYS A1095 11125 9888 9054 -506 -533 -982 C ATOM 2310 NZ LYS A1095 166.575 24.619 568.200 1.00 77.12 N ANISOU 2310 NZ LYS A1095 10781 9509 9011 -580 -532 -719 N ATOM 2311 N THR A1096 164.988 24.123 575.423 1.00107.57 N ANISOU 2311 N THR A1096 14075 15474 11323 -465 -309 -495 N ATOM 2312 CA THR A1096 165.469 24.797 576.624 1.00108.37 C ANISOU 2312 CA THR A1096 14218 15874 11083 -436 -355 -658 C ATOM 2313 C THR A1096 166.412 23.899 577.415 1.00108.44 C ANISOU 2313 C THR A1096 14168 16052 10981 -571 -436 -373 C ATOM 2314 O THR A1096 167.483 24.339 577.848 1.00107.80 O ANISOU 2314 O THR A1096 14178 15976 10807 -599 -565 -481 O ATOM 2315 CB THR A1096 164.291 25.232 577.497 1.00110.61 C ANISOU 2315 CB THR A1096 14414 16557 11057 -306 -220 -804 C ATOM 2316 OG1 THR A1096 163.501 26.200 576.793 1.00110.65 O ANISOU 2316 OG1 THR A1096 14491 16381 11169 -151 -193 -1129 O ATOM 2317 CG2 THR A1096 164.795 25.843 578.800 1.00111.36 C ANISOU 2317 CG2 THR A1096 14554 16991 10768 -262 -277 -966 C ATOM 2318 N THR A1097 166.032 22.633 577.601 1.00 88.57 N ANISOU 2318 N THR A1097 11507 13658 8486 -663 -388 -5 N ATOM 2319 CA THR A1097 166.905 21.688 578.288 1.00 89.57 C ANISOU 2319 CA THR A1097 11594 13901 8538 -794 -507 288 C ATOM 2320 C THR A1097 168.175 21.437 577.487 1.00 87.33 C ANISOU 2320 C THR A1097 11376 13249 8556 -851 -673 309 C ATOM 2321 O THR A1097 169.269 21.332 578.056 1.00 88.16 O ANISOU 2321 O THR A1097 11509 13407 8580 -907 -815 339 O ATOM 2322 CB THR A1097 166.161 20.376 578.541 1.00 90.60 C ANISOU 2322 CB THR A1097 11573 14187 8665 -896 -457 695 C ATOM 2323 OG1 THR A1097 164.976 20.636 579.304 1.00 93.08 O ANISOU 2323 OG1 THR A1097 11790 14901 8674 -858 -277 671 O ATOM 2324 CG2 THR A1097 167.042 19.396 579.303 1.00 92.01 C ANISOU 2324 CG2 THR A1097 11734 14470 8756 -1033 -623 1005 C ATOM 2325 N ARG A1098 168.050 21.339 576.161 1.00110.73 N ANISOU 2325 N ARG A1098 14358 15854 11862 -831 -657 283 N ATOM 2326 CA ARG A1098 169.229 21.180 575.317 1.00108.63 C ANISOU 2326 CA ARG A1098 14135 15274 11866 -873 -787 264 C ATOM 2327 C ARG A1098 170.151 22.386 575.432 1.00107.55 C ANISOU 2327 C ARG A1098 14115 15102 11648 -867 -850 -44 C ATOM 2328 O ARG A1098 171.374 22.235 575.526 1.00106.79 O ANISOU 2328 O ARG A1098 14013 14961 11602 -932 -985 -30 O ATOM 2329 CB ARG A1098 168.809 20.966 573.863 1.00107.09 C ANISOU 2329 CB ARG A1098 13950 14732 12007 -840 -739 263 C ATOM 2330 CG ARG A1098 169.973 20.811 572.900 1.00104.68 C ANISOU 2330 CG ARG A1098 13671 14140 11963 -875 -844 225 C ATOM 2331 CD ARG A1098 169.489 20.746 571.462 1.00102.91 C ANISOU 2331 CD ARG A1098 13484 13594 12023 -829 -786 187 C ATOM 2332 NE ARG A1098 168.914 22.013 571.023 1.00102.29 N ANISOU 2332 NE ARG A1098 13540 13420 11907 -779 -690 -91 N ATOM 2333 CZ ARG A1098 169.578 22.934 570.331 1.00100.47 C ANISOU 2333 CZ ARG A1098 13431 13001 11743 -808 -714 -315 C ATOM 2334 NH1 ARG A1098 170.843 22.727 569.993 1.00 98.97 N ANISOU 2334 NH1 ARG A1098 13213 12736 11654 -887 -798 -301 N ATOM 2335 NH2 ARG A1098 168.975 24.060 569.975 1.00100.46 N ANISOU 2335 NH2 ARG A1098 13573 12890 11707 -764 -666 -552 N ATOM 2336 N ASN A1099 169.581 23.593 575.432 1.00138.47 N ANISOU 2336 N ASN A1099 18134 19032 15447 -787 -777 -331 N ATOM 2337 CA ASN A1099 170.389 24.796 575.578 1.00137.86 C ANISOU 2337 CA ASN A1099 18185 18902 15291 -792 -872 -621 C ATOM 2338 C ASN A1099 170.914 24.965 576.997 1.00139.24 C ANISOU 2338 C ASN A1099 18356 19396 15153 -798 -960 -643 C ATOM 2339 O ASN A1099 171.935 25.633 577.194 1.00138.73 O ANISOU 2339 O ASN A1099 18366 19281 15063 -842 -1094 -803 O ATOM 2340 CB ASN A1099 169.576 26.026 575.170 1.00138.03 C ANISOU 2340 CB ASN A1099 18340 18815 15290 -691 -818 -928 C ATOM 2341 CG ASN A1099 170.450 27.172 574.703 1.00137.04 C ANISOU 2341 CG ASN A1099 18373 18453 15241 -742 -945 -1185 C ATOM 2342 OD1 ASN A1099 171.567 26.962 574.232 1.00135.63 O ANISOU 2342 OD1 ASN A1099 18184 18125 15225 -866 -1024 -1116 O ATOM 2343 ND2 ASN A1099 169.943 28.394 574.827 1.00137.89 N ANISOU 2343 ND2 ASN A1099 18624 18531 15235 -648 -981 -1486 N ATOM 2344 N ALA A1100 170.242 24.377 577.989 1.00 88.11 N ANISOU 2344 N ALA A1100 11793 13252 8430 -768 -894 -479 N ATOM 2345 CA ALA A1100 170.720 24.438 579.363 1.00 90.82 C ANISOU 2345 CA ALA A1100 12141 13919 8447 -776 -981 -473 C ATOM 2346 C ALA A1100 171.898 23.507 579.613 1.00 90.95 C ANISOU 2346 C ALA A1100 12102 13911 8544 -895 -1138 -234 C ATOM 2347 O ALA A1100 172.626 23.700 580.592 1.00 92.92 O ANISOU 2347 O ALA A1100 12386 14340 8581 -912 -1267 -273 O ATOM 2348 CB ALA A1100 169.584 24.104 580.333 1.00 93.16 C ANISOU 2348 CB ALA A1100 12359 14618 8420 -722 -844 -361 C ATOM 2349 N TYR A1101 172.101 22.508 578.757 1.00127.56 N ANISOU 2349 N TYR A1101 16656 18326 13485 -960 -1154 -7 N ATOM 2350 CA TYR A1101 173.208 21.567 578.872 1.00127.41 C ANISOU 2350 CA TYR A1101 16570 18250 13588 -1045 -1331 197 C ATOM 2351 C TYR A1101 173.878 21.361 577.521 1.00125.43 C ANISOU 2351 C TYR A1101 16284 17645 13729 -1070 -1369 167 C ATOM 2352 O TYR A1101 174.219 20.238 577.136 1.00125.31 O ANISOU 2352 O TYR A1101 16176 17519 13919 -1098 -1455 386 O ATOM 2353 CB TYR A1101 172.740 20.239 579.459 1.00128.99 C ANISOU 2353 CB TYR A1101 16683 18618 13709 -1093 -1356 571 C ATOM 2354 CG TYR A1101 172.832 20.179 580.967 1.00130.66 C ANISOU 2354 CG TYR A1101 16919 19194 13531 -1122 -1425 658 C ATOM 2355 CD1 TYR A1101 173.872 20.807 581.641 1.00130.58 C ANISOU 2355 CD1 TYR A1101 16977 19258 13380 -1119 -1570 479 C ATOM 2356 CD2 TYR A1101 171.879 19.503 581.717 1.00132.31 C ANISOU 2356 CD2 TYR A1101 17084 19685 13503 -1165 -1350 924 C ATOM 2357 CE1 TYR A1101 173.964 20.758 583.018 1.00131.99 C ANISOU 2357 CE1 TYR A1101 17196 19770 13185 -1136 -1646 550 C ATOM 2358 CE2 TYR A1101 171.962 19.448 583.097 1.00133.67 C ANISOU 2358 CE2 TYR A1101 17288 20217 13282 -1201 -1407 1013 C ATOM 2359 CZ TYR A1101 173.007 20.078 583.741 1.00133.46 C ANISOU 2359 CZ TYR A1101 17348 20247 13114 -1176 -1558 817 C ATOM 2360 OH TYR A1101 173.097 20.030 585.113 1.00134.73 O ANISOU 2360 OH TYR A1101 17559 20766 12868 -1203 -1627 897 O ATOM 2361 N ILE A1102 174.072 22.453 576.775 1.00110.68 N ANISOU 2361 N ILE A1102 14496 15599 11960 -1058 -1321 -111 N ATOM 2362 CA ILE A1102 174.822 22.402 575.523 1.00108.57 C ANISOU 2362 CA ILE A1102 14195 15041 12014 -1101 -1347 -166 C ATOM 2363 C ILE A1102 176.291 22.745 575.724 1.00108.07 C ANISOU 2363 C ILE A1102 14104 14976 11982 -1178 -1504 -281 C ATOM 2364 O ILE A1102 177.089 22.598 574.785 1.00106.47 O ANISOU 2364 O ILE A1102 13831 14597 12027 -1227 -1533 -313 O ATOM 2365 CB ILE A1102 174.197 23.344 574.472 1.00107.17 C ANISOU 2365 CB ILE A1102 14125 14651 11941 -1079 -1213 -368 C ATOM 2366 CG1 ILE A1102 174.538 22.883 573.052 1.00105.03 C ANISOU 2366 CG1 ILE A1102 13805 14108 11995 -1106 -1188 -326 C ATOM 2367 CG2 ILE A1102 174.653 24.778 574.699 1.00107.12 C ANISOU 2367 CG2 ILE A1102 14248 14636 11817 -1115 -1264 -659 C ATOM 2368 CD1 ILE A1102 173.913 23.735 571.968 1.00103.74 C ANISOU 2368 CD1 ILE A1102 13768 13717 11932 -1096 -1074 -495 C ATOM 2369 N GLN A1103 176.680 23.177 576.925 1.00 86.45 N ANISOU 2369 N GLN A1103 11405 12447 8994 -1188 -1609 -347 N ATOM 2370 CA GLN A1103 178.056 23.554 577.230 1.00 87.58 C ANISOU 2370 CA GLN A1103 11517 12601 9159 -1264 -1780 -464 C ATOM 2371 C GLN A1103 179.025 22.379 577.191 1.00 87.86 C ANISOU 2371 C GLN A1103 11386 12628 9368 -1290 -1923 -287 C ATOM 2372 O GLN A1103 180.231 22.594 577.355 1.00 88.85 O ANISOU 2372 O GLN A1103 11445 12761 9552 -1352 -2071 -384 O ATOM 2373 CB GLN A1103 178.111 24.227 578.602 1.00 90.03 C ANISOU 2373 CB GLN A1103 11924 13142 9140 -1244 -1877 -570 C ATOM 2374 CG GLN A1103 177.445 23.423 579.708 1.00 91.60 C ANISOU 2374 CG GLN A1103 12118 13605 9081 -1182 -1878 -356 C ATOM 2375 CD GLN A1103 177.351 24.187 581.014 1.00 94.17 C ANISOU 2375 CD GLN A1103 12556 14187 9036 -1139 -1943 -495 C ATOM 2376 OE1 GLN A1103 176.671 23.761 581.948 1.00 95.81 O ANISOU 2376 OE1 GLN A1103 12780 14658 8966 -1093 -1909 -356 O ATOM 2377 NE2 GLN A1103 178.036 25.323 581.088 1.00 94.78 N ANISOU 2377 NE2 GLN A1103 12713 14197 9100 -1159 -2047 -768 N ATOM 2378 N LYS A1104 178.541 21.154 576.982 1.00101.49 N ANISOU 2378 N LYS A1104 13039 14332 11190 -1241 -1909 -43 N ATOM 2379 CA LYS A1104 179.403 19.985 576.887 1.00101.69 C ANISOU 2379 CA LYS A1104 12915 14318 11405 -1236 -2082 109 C ATOM 2380 C LYS A1104 179.709 19.578 575.452 1.00 99.67 C ANISOU 2380 C LYS A1104 12549 13837 11483 -1218 -2034 81 C ATOM 2381 O LYS A1104 180.560 18.707 575.243 1.00 99.60 O ANISOU 2381 O LYS A1104 12395 13787 11660 -1190 -2191 139 O ATOM 2382 CB LYS A1104 178.772 18.792 577.620 1.00103.58 C ANISOU 2382 CB LYS A1104 13152 14659 11545 -1200 -2164 417 C ATOM 2383 CG LYS A1104 178.980 18.784 579.127 1.00105.63 C ANISOU 2383 CG LYS A1104 13469 15168 11496 -1226 -2307 493 C ATOM 2384 CD LYS A1104 178.034 19.734 579.841 1.00106.24 C ANISOU 2384 CD LYS A1104 13685 15444 11236 -1224 -2146 408 C ATOM 2385 CE LYS A1104 178.261 19.701 581.343 1.00108.05 C ANISOU 2385 CE LYS A1104 13978 15950 11128 -1242 -2289 480 C ATOM 2386 NZ LYS A1104 177.301 20.573 582.074 1.00108.63 N ANISOU 2386 NZ LYS A1104 14170 16261 10844 -1211 -2131 379 N ATOM 2387 N TYR A1105 179.048 20.177 574.469 1.00114.56 N ANISOU 2387 N TYR A1105 14502 15583 13444 -1220 -1837 -20 N ATOM 2388 CA TYR A1105 179.218 19.820 573.067 1.00112.55 C ANISOU 2388 CA TYR A1105 14166 15129 13471 -1197 -1772 -48 C ATOM 2389 C TYR A1105 179.687 21.033 572.269 1.00110.95 C ANISOU 2389 C TYR A1105 13998 14845 13314 -1292 -1664 -293 C ATOM 2390 O TYR A1105 179.870 22.130 572.802 1.00111.47 O ANISOU 2390 O TYR A1105 14157 14979 13219 -1374 -1667 -437 O ATOM 2391 CB TYR A1105 177.918 19.257 572.486 1.00112.22 C ANISOU 2391 CB TYR A1105 14182 14962 13497 -1118 -1655 98 C ATOM 2392 CG TYR A1105 177.975 17.777 572.193 1.00112.34 C ANISOU 2392 CG TYR A1105 14079 14895 13709 -1031 -1785 303 C ATOM 2393 CD1 TYR A1105 178.615 17.300 571.057 1.00110.41 C ANISOU 2393 CD1 TYR A1105 13720 14505 13726 -978 -1814 236 C ATOM 2394 CD2 TYR A1105 177.388 16.855 573.050 1.00114.47 C ANISOU 2394 CD2 TYR A1105 14356 15241 13897 -1004 -1895 561 C ATOM 2395 CE1 TYR A1105 178.672 15.948 570.783 1.00110.35 C ANISOU 2395 CE1 TYR A1105 13615 14403 13910 -870 -1975 394 C ATOM 2396 CE2 TYR A1105 177.439 15.500 572.785 1.00114.58 C ANISOU 2396 CE2 TYR A1105 14284 15142 14108 -931 -2065 754 C ATOM 2397 CZ TYR A1105 178.082 15.052 571.650 1.00112.36 C ANISOU 2397 CZ TYR A1105 13897 14691 14103 -849 -2117 657 C ATOM 2398 OH TYR A1105 178.135 13.704 571.380 1.00112.19 O ANISOU 2398 OH TYR A1105 13798 14539 14289 -748 -2325 821 O ATOM 2399 N LEU A1106 179.877 20.817 570.971 1.00106.65 N ANISOU 2399 N LEU A1106 13387 14150 12986 -1286 -1586 -333 N ATOM 2400 CA LEU A1106 180.339 21.865 570.069 1.00105.50 C ANISOU 2400 CA LEU A1106 13270 13923 12891 -1408 -1484 -526 C ATOM 2401 C LEU A1106 179.159 22.632 569.482 1.00104.84 C ANISOU 2401 C LEU A1106 13396 13681 12758 -1414 -1324 -573 C ATOM 2402 O LEU A1106 178.245 22.040 568.909 1.00104.18 O ANISOU 2402 O LEU A1106 13349 13479 12757 -1312 -1246 -474 O ATOM 2403 CB LEU A1106 181.194 21.276 568.941 1.00104.40 C ANISOU 2403 CB LEU A1106 12945 13743 12978 -1403 -1472 -560 C ATOM 2404 CG LEU A1106 182.485 20.536 569.307 1.00105.11 C ANISOU 2404 CG LEU A1106 12791 13982 13164 -1380 -1642 -566 C ATOM 2405 CD1 LEU A1106 182.213 19.076 569.642 1.00105.48 C ANISOU 2405 CD1 LEU A1106 12759 14019 13298 -1199 -1782 -386 C ATOM 2406 CD2 LEU A1106 183.486 20.632 568.168 1.00104.51 C ANISOU 2406 CD2 LEU A1106 12536 13927 13245 -1444 -1579 -706 C ATOM 2407 N SER A 380 177.778 19.523 563.709 1.00127.73 N ANISOU 2407 N SER A 380 16175 15865 16493 -1005 -1015 -416 N ATOM 2408 CA SER A 380 178.664 19.786 562.582 1.00127.09 C ANISOU 2408 CA SER A 380 16018 15799 16470 -1069 -936 -558 C ATOM 2409 C SER A 380 177.902 19.738 561.261 1.00125.76 C ANISOU 2409 C SER A 380 15982 15420 16381 -1006 -830 -573 C ATOM 2410 O SER A 380 177.409 18.686 560.852 1.00124.66 O ANISOU 2410 O SER A 380 15813 15172 16382 -823 -888 -492 O ATOM 2411 CB SER A 380 179.820 18.782 562.562 1.00127.14 C ANISOU 2411 CB SER A 380 15752 15961 16596 -979 -1051 -580 C ATOM 2412 OG SER A 380 180.599 18.880 563.741 1.00128.54 O ANISOU 2412 OG SER A 380 15812 16325 16703 -1045 -1164 -579 O ATOM 2413 N ARG A 381 177.811 20.890 560.597 1.00113.37 N ANISOU 2413 N ARG A 381 17209 17691 8175 226 374 51 N ATOM 2414 CA ARG A 381 177.116 21.023 559.324 1.00110.46 C ANISOU 2414 CA ARG A 381 16568 17024 8378 358 613 10 C ATOM 2415 C ARG A 381 177.974 20.613 558.133 1.00107.68 C ANISOU 2415 C ARG A 381 15889 16421 8604 292 261 158 C ATOM 2416 O ARG A 381 177.624 20.942 556.993 1.00105.46 O ANISOU 2416 O ARG A 381 15405 15806 8859 333 363 40 O ATOM 2417 CB ARG A 381 176.634 22.464 559.142 1.00110.93 C ANISOU 2417 CB ARG A 381 16799 16884 8463 405 829 -541 C ATOM 2418 CG ARG A 381 177.763 23.484 559.100 1.00111.63 C ANISOU 2418 CG ARG A 381 17071 16890 8454 221 446 -956 C ATOM 2419 CD ARG A 381 177.247 24.902 559.281 1.00112.95 C ANISOU 2419 CD ARG A 381 17499 16867 8551 254 702 -1495 C ATOM 2420 NE ARG A 381 176.368 25.321 558.194 1.00110.68 N ANISOU 2420 NE ARG A 381 17085 16196 8774 466 1014 -1575 N ATOM 2421 CZ ARG A 381 175.759 26.501 558.142 1.00111.34 C ANISOU 2421 CZ ARG A 381 17303 16032 8969 576 1278 -1965 C ATOM 2422 NH1 ARG A 381 174.975 26.801 557.116 1.00109.28 N ANISOU 2422 NH1 ARG A 381 16891 15455 9176 802 1527 -1971 N ATOM 2423 NH2 ARG A 381 175.931 27.381 559.119 1.00115.31 N ANISOU 2423 NH2 ARG A 381 18042 16618 9151 484 1273 -2329 N ATOM 2424 N GLU A 382 179.080 19.903 558.370 1.00 98.20 N ANISOU 2424 N GLU A 382 14628 15391 7291 218 -142 424 N ATOM 2425 CA GLU A 382 180.003 19.565 557.293 1.00 95.87 C ANISOU 2425 CA GLU A 382 14025 14892 7511 175 -464 532 C ATOM 2426 C GLU A 382 179.401 18.590 556.289 1.00 93.29 C ANISOU 2426 C GLU A 382 13420 14280 7745 280 -263 859 C ATOM 2427 O GLU A 382 179.857 18.545 555.141 1.00 91.08 O ANISOU 2427 O GLU A 382 12898 13743 7963 263 -402 837 O ATOM 2428 CB GLU A 382 181.295 18.994 557.878 1.00 97.07 C ANISOU 2428 CB GLU A 382 14147 15346 7389 126 -925 767 C ATOM 2429 CG GLU A 382 181.931 19.894 558.927 1.00100.02 C ANISOU 2429 CG GLU A 382 14790 16025 7188 -27 -1175 437 C ATOM 2430 CD GLU A 382 182.165 21.305 558.420 1.00 99.74 C ANISOU 2430 CD GLU A 382 14812 15822 7264 -206 -1226 -123 C ATOM 2431 OE1 GLU A 382 182.869 21.464 557.401 1.00 97.68 O ANISOU 2431 OE1 GLU A 382 14282 15352 7481 -284 -1425 -179 O ATOM 2432 OE2 GLU A 382 181.636 22.255 559.035 1.00101.70 O ANISOU 2432 OE2 GLU A 382 15394 16064 7182 -250 -1030 -506 O ATOM 2433 N LYS A 383 178.395 17.809 556.690 1.00 75.75 N ANISOU 2433 N LYS A 383 11235 12106 5441 359 67 1152 N ATOM 2434 CA LYS A 383 177.689 16.970 555.726 1.00 73.46 C ANISOU 2434 CA LYS A 383 10698 11532 5681 398 281 1395 C ATOM 2435 C LYS A 383 176.938 17.821 554.709 1.00 71.91 C ANISOU 2435 C LYS A 383 10359 11086 5877 411 481 1064 C ATOM 2436 O LYS A 383 176.976 17.539 553.506 1.00 69.63 O ANISOU 2436 O LYS A 383 9835 10525 6097 402 431 1098 O ATOM 2437 CB LYS A 383 176.729 16.026 556.450 1.00 74.52 C ANISOU 2437 CB LYS A 383 10906 11787 5621 420 616 1763 C ATOM 2438 CG LYS A 383 177.338 14.687 556.838 1.00 74.91 C ANISOU 2438 CG LYS A 383 10993 11870 5598 437 451 2268 C ATOM 2439 CD LYS A 383 177.614 13.832 555.610 1.00 72.16 C ANISOU 2439 CD LYS A 383 10397 11149 5872 441 355 2452 C ATOM 2440 CE LYS A 383 178.075 12.436 555.996 1.00 72.68 C ANISOU 2440 CE LYS A 383 10539 11171 5905 500 265 2981 C ATOM 2441 NZ LYS A 383 178.271 11.567 554.802 1.00 70.07 N ANISOU 2441 NZ LYS A 383 10016 10430 6177 511 227 3127 N ATOM 2442 N LYS A 384 176.252 18.867 555.177 1.00 85.84 N ANISOU 2442 N LYS A 384 12280 12942 7394 455 713 743 N ATOM 2443 CA LYS A 384 175.561 19.775 554.268 1.00 84.60 C ANISOU 2443 CA LYS A 384 12009 12552 7583 523 889 442 C ATOM 2444 C LYS A 384 176.540 20.514 553.363 1.00 83.39 C ANISOU 2444 C LYS A 384 11823 12165 7696 462 573 192 C ATOM 2445 O LYS A 384 176.229 20.776 552.195 1.00 81.54 O ANISOU 2445 O LYS A 384 11405 11673 7903 500 614 118 O ATOM 2446 CB LYS A 384 174.709 20.759 555.074 1.00 86.56 C ANISOU 2446 CB LYS A 384 12473 12938 7479 635 1216 151 C ATOM 2447 CG LYS A 384 174.346 22.050 554.354 1.00 85.85 C ANISOU 2447 CG LYS A 384 12391 12597 7632 747 1313 -241 C ATOM 2448 CD LYS A 384 175.205 23.211 554.842 1.00 87.32 C ANISOU 2448 CD LYS A 384 12927 12746 7505 683 1125 -643 C ATOM 2449 CE LYS A 384 174.935 24.477 554.046 1.00 86.56 C ANISOU 2449 CE LYS A 384 12884 12311 7694 792 1212 -996 C ATOM 2450 NZ LYS A 384 175.822 25.594 554.470 1.00 87.92 N ANISOU 2450 NZ LYS A 384 13425 12382 7598 663 1025 -1400 N ATOM 2451 N VAL A 385 177.725 20.849 553.878 1.00 49.32 N ANISOU 2451 N VAL A 385 7671 7962 3106 351 253 73 N ATOM 2452 CA VAL A 385 178.717 21.549 553.066 1.00 47.18 C ANISOU 2452 CA VAL A 385 7349 7495 3080 242 -31 -153 C ATOM 2453 C VAL A 385 179.210 20.657 551.934 1.00 43.34 C ANISOU 2453 C VAL A 385 6551 6847 3069 228 -189 112 C ATOM 2454 O VAL A 385 179.365 21.108 550.792 1.00 40.34 O ANISOU 2454 O VAL A 385 6050 6210 3069 205 -223 -17 O ATOM 2455 CB VAL A 385 179.880 22.037 553.949 1.00 50.55 C ANISOU 2455 CB VAL A 385 7973 8145 3090 77 -355 -331 C ATOM 2456 CG1 VAL A 385 180.909 22.781 553.110 1.00 48.86 C ANISOU 2456 CG1 VAL A 385 7676 7739 3150 -89 -623 -561 C ATOM 2457 CG2 VAL A 385 179.359 22.921 555.072 1.00 54.87 C ANISOU 2457 CG2 VAL A 385 8889 8833 3127 83 -175 -642 C ATOM 2458 N THR A 386 179.465 19.379 552.226 1.00 43.82 N ANISOU 2458 N THR A 386 6509 7038 3101 253 -270 490 N ATOM 2459 CA THR A 386 179.908 18.459 551.184 1.00 40.79 C ANISOU 2459 CA THR A 386 5869 6471 3160 268 -380 727 C ATOM 2460 C THR A 386 178.806 18.214 550.159 1.00 37.81 C ANISOU 2460 C THR A 386 5351 5839 3174 317 -110 757 C ATOM 2461 O THR A 386 179.075 18.147 548.954 1.00 34.76 O ANISOU 2461 O THR A 386 4801 5231 3177 302 -176 727 O ATOM 2462 CB THR A 386 180.375 17.143 551.809 1.00 42.83 C ANISOU 2462 CB THR A 386 6105 6879 3290 322 -498 1136 C ATOM 2463 OG1 THR A 386 181.514 17.389 552.643 1.00 45.84 O ANISOU 2463 OG1 THR A 386 6555 7541 3322 284 -822 1116 O ATOM 2464 CG2 THR A 386 180.755 16.140 550.731 1.00 40.24 C ANISOU 2464 CG2 THR A 386 5554 6305 3430 371 -555 1361 C ATOM 2465 N ARG A 387 177.556 18.088 550.617 1.00 57.88 N ANISOU 2465 N ARG A 387 7942 8447 5603 367 195 814 N ATOM 2466 CA ARG A 387 176.440 17.934 549.689 1.00 56.35 C ANISOU 2466 CA ARG A 387 7569 8081 5762 394 428 824 C ATOM 2467 C ARG A 387 176.301 19.154 548.787 1.00 55.77 C ANISOU 2467 C ARG A 387 7463 7842 5885 433 424 501 C ATOM 2468 O ARG A 387 176.025 19.023 547.589 1.00 53.97 O ANISOU 2468 O ARG A 387 7057 7426 6022 432 426 506 O ATOM 2469 CB ARG A 387 175.139 17.700 550.457 1.00 57.33 C ANISOU 2469 CB ARG A 387 7705 8374 5703 430 770 929 C ATOM 2470 CG ARG A 387 175.072 16.399 551.234 1.00 57.91 C ANISOU 2470 CG ARG A 387 7819 8562 5622 371 839 1312 C ATOM 2471 CD ARG A 387 173.764 16.317 552.006 1.00 59.28 C ANISOU 2471 CD ARG A 387 7993 8935 5595 381 1225 1393 C ATOM 2472 NE ARG A 387 173.687 15.138 552.864 1.00 60.35 N ANISOU 2472 NE ARG A 387 8223 9181 5528 305 1325 1784 N ATOM 2473 CZ ARG A 387 172.661 14.866 553.663 1.00 61.94 C ANISOU 2473 CZ ARG A 387 8440 9584 5512 274 1681 1934 C ATOM 2474 NH1 ARG A 387 171.624 15.692 553.715 1.00 62.55 N ANISOU 2474 NH1 ARG A 387 8407 9799 5562 344 1970 1707 N ATOM 2475 NH2 ARG A 387 172.669 13.772 554.412 1.00 63.11 N ANISOU 2475 NH2 ARG A 387 8711 9794 5472 189 1768 2329 N ATOM 2476 N THR A 388 176.482 20.351 549.350 1.00 40.22 N ANISOU 2476 N THR A 388 5698 5924 3659 465 420 218 N ATOM 2477 CA THR A 388 176.356 21.574 548.564 1.00 39.48 C ANISOU 2477 CA THR A 388 5638 5620 3740 518 438 -70 C ATOM 2478 C THR A 388 177.401 21.631 547.457 1.00 38.21 C ANISOU 2478 C THR A 388 5390 5261 3868 412 181 -93 C ATOM 2479 O THR A 388 177.089 21.996 546.316 1.00 36.47 O ANISOU 2479 O THR A 388 5074 4838 3944 455 213 -147 O ATOM 2480 CB THR A 388 176.472 22.795 549.477 1.00 41.15 C ANISOU 2480 CB THR A 388 6159 5875 3603 542 485 -385 C ATOM 2481 OG1 THR A 388 175.315 22.878 550.319 1.00 42.37 O ANISOU 2481 OG1 THR A 388 6380 6192 3525 694 807 -399 O ATOM 2482 CG2 THR A 388 176.595 24.073 548.662 1.00 40.08 C ANISOU 2482 CG2 THR A 388 6124 5445 3661 572 468 -666 C ATOM 2483 N ILE A 389 178.645 21.265 547.771 1.00 34.68 N ANISOU 2483 N ILE A 389 4956 4899 3323 284 -73 -35 N ATOM 2484 CA ILE A 389 179.705 21.292 546.767 1.00 33.40 C ANISOU 2484 CA ILE A 389 4672 4591 3426 184 -285 -50 C ATOM 2485 C ILE A 389 179.405 20.309 545.644 1.00 31.66 C ANISOU 2485 C ILE A 389 4230 4239 3560 230 -238 159 C ATOM 2486 O ILE A 389 179.575 20.626 544.461 1.00 30.14 O ANISOU 2486 O ILE A 389 3962 3858 3630 209 -261 88 O ATOM 2487 CB ILE A 389 181.069 21.010 547.425 1.00 33.79 C ANISOU 2487 CB ILE A 389 4709 4833 3297 66 -564 -2 C ATOM 2488 CG1 ILE A 389 181.477 22.188 548.311 1.00 35.79 C ANISOU 2488 CG1 ILE A 389 5195 5185 3217 -55 -655 -296 C ATOM 2489 CG2 ILE A 389 182.130 20.729 546.371 1.00 31.71 C ANISOU 2489 CG2 ILE A 389 4233 4468 3345 -4 -736 54 C ATOM 2490 CD1 ILE A 389 182.822 22.021 548.972 1.00 38.18 C ANISOU 2490 CD1 ILE A 389 5446 5742 3319 -203 -979 -274 C ATOM 2491 N LEU A 390 178.942 19.105 545.993 1.00 38.72 N ANISOU 2491 N LEU A 390 5048 5216 4448 274 -162 414 N ATOM 2492 CA LEU A 390 178.611 18.116 544.971 1.00 35.71 C ANISOU 2492 CA LEU A 390 4499 4681 4387 279 -111 579 C ATOM 2493 C LEU A 390 177.523 18.627 544.036 1.00 34.55 C ANISOU 2493 C LEU A 390 4285 4417 4428 311 38 463 C ATOM 2494 O LEU A 390 177.604 18.440 542.817 1.00 30.50 O ANISOU 2494 O LEU A 390 3670 3747 4171 285 -3 452 O ATOM 2495 CB LEU A 390 178.177 16.805 545.625 1.00 35.48 C ANISOU 2495 CB LEU A 390 4454 4721 4307 287 -19 866 C ATOM 2496 CG LEU A 390 177.705 15.722 544.652 1.00 32.45 C ANISOU 2496 CG LEU A 390 3943 4145 4244 246 58 1008 C ATOM 2497 CD1 LEU A 390 178.833 15.309 543.718 1.00 29.38 C ANISOU 2497 CD1 LEU A 390 3496 3587 4080 249 -106 1012 C ATOM 2498 CD2 LEU A 390 177.150 14.519 545.399 1.00 32.99 C ANISOU 2498 CD2 LEU A 390 4042 4240 4254 213 194 1293 C ATOM 2499 N ALA A 391 176.497 19.280 544.589 1.00 26.14 N ANISOU 2499 N ALA A 391 3268 3446 3219 388 212 378 N ATOM 2500 CA ALA A 391 175.424 19.810 543.753 1.00 25.46 C ANISOU 2500 CA ALA A 391 3076 3292 3304 469 336 294 C ATOM 2501 C ALA A 391 175.946 20.874 542.797 1.00 24.01 C ANISOU 2501 C ALA A 391 2963 2923 3237 495 226 111 C ATOM 2502 O ALA A 391 175.547 20.919 541.628 1.00 22.67 O ANISOU 2502 O ALA A 391 2681 2653 3279 518 215 118 O ATOM 2503 CB ALA A 391 174.305 20.376 544.627 1.00 27.96 C ANISOU 2503 CB ALA A 391 3417 3766 3439 602 569 235 C ATOM 2504 N ILE A 392 176.845 21.738 543.274 1.00 36.83 N ANISOU 2504 N ILE A 392 4783 4506 4706 465 140 -48 N ATOM 2505 CA ILE A 392 177.412 22.771 542.414 1.00 34.82 C ANISOU 2505 CA ILE A 392 4627 4043 4560 442 59 -203 C ATOM 2506 C ILE A 392 178.275 22.144 541.325 1.00 31.63 C ANISOU 2506 C ILE A 392 4096 3556 4365 324 -85 -110 C ATOM 2507 O ILE A 392 178.285 22.607 540.178 1.00 28.17 O ANISOU 2507 O ILE A 392 3657 2963 4085 331 -95 -145 O ATOM 2508 CB ILE A 392 178.202 23.787 543.259 1.00 37.21 C ANISOU 2508 CB ILE A 392 5175 4317 4646 365 1 -413 C ATOM 2509 CG1 ILE A 392 177.283 24.449 544.287 1.00 39.11 C ANISOU 2509 CG1 ILE A 392 5586 4614 4658 512 190 -547 C ATOM 2510 CG2 ILE A 392 178.838 24.842 542.374 1.00 34.75 C ANISOU 2510 CG2 ILE A 392 4985 3755 4466 287 -62 -555 C ATOM 2511 CD1 ILE A 392 177.976 25.465 545.167 1.00 40.86 C ANISOU 2511 CD1 ILE A 392 6106 4790 4628 412 141 -807 C ATOM 2512 N LEU A 393 179.001 21.075 541.659 1.00 36.19 N ANISOU 2512 N LEU A 393 4579 4237 4935 242 -181 21 N ATOM 2513 CA LEU A 393 179.848 20.426 540.664 1.00 32.58 C ANISOU 2513 CA LEU A 393 4002 3701 4677 171 -277 95 C ATOM 2514 C LEU A 393 179.018 19.655 539.644 1.00 28.66 C ANISOU 2514 C LEU A 393 3393 3128 4367 208 -201 189 C ATOM 2515 O LEU A 393 179.340 19.655 538.451 1.00 25.60 O ANISOU 2515 O LEU A 393 2973 2627 4126 176 -227 163 O ATOM 2516 CB LEU A 393 180.854 19.501 541.351 1.00 33.94 C ANISOU 2516 CB LEU A 393 4101 3996 4800 133 -394 223 C ATOM 2517 CG LEU A 393 181.889 20.186 542.247 1.00 37.41 C ANISOU 2517 CG LEU A 393 4598 4568 5048 49 -541 127 C ATOM 2518 CD1 LEU A 393 182.899 19.179 542.778 1.00 37.26 C ANISOU 2518 CD1 LEU A 393 4446 4707 5005 61 -690 304 C ATOM 2519 CD2 LEU A 393 182.589 21.309 541.498 1.00 36.43 C ANISOU 2519 CD2 LEU A 393 4505 4328 5009 -74 -588 -57 C ATOM 2520 N LEU A 394 177.947 18.996 540.091 1.00 30.63 N ANISOU 2520 N LEU A 394 3586 3456 4596 248 -101 289 N ATOM 2521 CA LEU A 394 177.115 18.234 539.163 1.00 28.13 C ANISOU 2521 CA LEU A 394 3150 3089 4449 223 -52 355 C ATOM 2522 C LEU A 394 176.361 19.153 538.210 1.00 26.49 C ANISOU 2522 C LEU A 394 2919 2852 4294 284 -38 254 C ATOM 2523 O LEU A 394 176.209 18.834 537.025 1.00 24.24 O ANISOU 2523 O LEU A 394 2576 2504 4132 239 -81 251 O ATOM 2524 CB LEU A 394 176.142 17.344 539.934 1.00 30.46 C ANISOU 2524 CB LEU A 394 3367 3489 4717 198 63 495 C ATOM 2525 CG LEU A 394 176.776 16.188 540.708 1.00 31.85 C ANISOU 2525 CG LEU A 394 3585 3652 4863 149 54 666 C ATOM 2526 CD1 LEU A 394 175.705 15.304 541.321 1.00 33.95 C ANISOU 2526 CD1 LEU A 394 3793 3984 5121 81 205 828 C ATOM 2527 CD2 LEU A 394 177.697 15.381 539.807 1.00 28.70 C ANISOU 2527 CD2 LEU A 394 3188 3071 4646 110 -33 691 C ATOM 2528 N ALA A 395 175.877 20.294 538.707 1.00 25.11 N ANISOU 2528 N ALA A 395 2810 2720 4011 405 23 173 N ATOM 2529 CA ALA A 395 175.223 21.254 537.824 1.00 23.73 C ANISOU 2529 CA ALA A 395 2636 2493 3888 524 29 112 C ATOM 2530 C ALA A 395 176.185 21.776 536.766 1.00 21.45 C ANISOU 2530 C ALA A 395 2468 2030 3652 472 -70 58 C ATOM 2531 O ALA A 395 175.769 22.083 535.644 1.00 19.94 O ANISOU 2531 O ALA A 395 2258 1798 3521 522 -104 74 O ATOM 2532 CB ALA A 395 174.646 22.412 538.638 1.00 26.08 C ANISOU 2532 CB ALA A 395 3032 2809 4069 706 145 26 C ATOM 2533 N PHE A 396 177.472 21.876 537.103 1.00 31.08 N ANISOU 2533 N PHE A 396 3795 3179 4835 364 -118 9 N ATOM 2534 CA PHE A 396 178.465 22.321 536.132 1.00 29.31 C ANISOU 2534 CA PHE A 396 3653 2817 4667 278 -174 -30 C ATOM 2535 C PHE A 396 178.777 21.226 535.119 1.00 27.26 C ANISOU 2535 C PHE A 396 3280 2564 4512 201 -209 36 C ATOM 2536 O PHE A 396 178.884 21.497 533.917 1.00 25.79 O ANISOU 2536 O PHE A 396 3136 2304 4358 186 -218 31 O ATOM 2537 CB PHE A 396 179.734 22.766 536.860 1.00 31.07 C ANISOU 2537 CB PHE A 396 3963 3014 4829 158 -217 -110 C ATOM 2538 CG PHE A 396 180.916 22.960 535.958 1.00 29.69 C ANISOU 2538 CG PHE A 396 3794 2753 4733 21 -252 -126 C ATOM 2539 CD1 PHE A 396 181.007 24.076 535.144 1.00 28.70 C ANISOU 2539 CD1 PHE A 396 3826 2457 4623 -6 -213 -167 C ATOM 2540 CD2 PHE A 396 181.946 22.033 535.934 1.00 29.92 C ANISOU 2540 CD2 PHE A 396 3671 2871 4826 -65 -301 -79 C ATOM 2541 CE1 PHE A 396 182.096 24.260 534.316 1.00 28.13 C ANISOU 2541 CE1 PHE A 396 3751 2325 4612 -159 -205 -166 C ATOM 2542 CE2 PHE A 396 183.038 22.211 535.108 1.00 29.32 C ANISOU 2542 CE2 PHE A 396 3558 2754 4828 -181 -293 -94 C ATOM 2543 CZ PHE A 396 183.113 23.326 534.298 1.00 28.47 C ANISOU 2543 CZ PHE A 396 3599 2498 4719 -250 -237 -139 C ATOM 2544 N ILE A 397 178.916 19.983 535.584 1.00 28.03 N ANISOU 2544 N ILE A 397 3269 2732 4648 160 -215 100 N ATOM 2545 CA ILE A 397 179.268 18.885 534.688 1.00 26.44 C ANISOU 2545 CA ILE A 397 3008 2485 4554 99 -220 131 C ATOM 2546 C ILE A 397 178.115 18.575 533.740 1.00 25.68 C ANISOU 2546 C ILE A 397 2875 2397 4483 94 -220 129 C ATOM 2547 O ILE A 397 178.311 18.419 532.530 1.00 24.79 O ANISOU 2547 O ILE A 397 2799 2234 4388 51 -235 88 O ATOM 2548 CB ILE A 397 179.674 17.641 535.498 1.00 27.20 C ANISOU 2548 CB ILE A 397 3040 2597 4697 86 -214 221 C ATOM 2549 CG1 ILE A 397 180.941 17.916 536.310 1.00 28.78 C ANISOU 2549 CG1 ILE A 397 3232 2848 4856 94 -266 233 C ATOM 2550 CG2 ILE A 397 179.867 16.445 534.578 1.00 25.95 C ANISOU 2550 CG2 ILE A 397 2865 2329 4664 48 -183 229 C ATOM 2551 CD1 ILE A 397 181.302 16.797 537.261 1.00 30.15 C ANISOU 2551 CD1 ILE A 397 3354 3063 5039 137 -284 372 C ATOM 2552 N ILE A 398 176.896 18.488 534.275 1.00 30.01 N ANISOU 2552 N ILE A 398 3339 3048 5017 127 -205 171 N ATOM 2553 CA ILE A 398 175.759 18.046 533.473 1.00 30.57 C ANISOU 2553 CA ILE A 398 3305 3189 5122 82 -236 174 C ATOM 2554 C ILE A 398 175.405 19.077 532.404 1.00 30.46 C ANISOU 2554 C ILE A 398 3327 3202 5046 167 -305 143 C ATOM 2555 O ILE A 398 175.015 18.719 531.286 1.00 31.11 O ANISOU 2555 O ILE A 398 3381 3323 5116 100 -381 120 O ATOM 2556 CB ILE A 398 174.563 17.733 534.391 1.00 32.72 C ANISOU 2556 CB ILE A 398 3416 3609 5406 85 -180 244 C ATOM 2557 CG1 ILE A 398 174.878 16.518 535.266 1.00 33.51 C ANISOU 2557 CG1 ILE A 398 3520 3656 5558 -26 -110 320 C ATOM 2558 CG2 ILE A 398 173.300 17.494 533.582 1.00 33.80 C ANISOU 2558 CG2 ILE A 398 3375 3888 5581 26 -241 244 C ATOM 2559 CD1 ILE A 398 173.775 16.154 536.234 1.00 35.72 C ANISOU 2559 CD1 ILE A 398 3655 4083 5833 -60 -11 416 C ATOM 2560 N THR A 399 175.542 20.367 532.716 1.00 23.47 N ANISOU 2560 N THR A 399 2535 2281 4102 311 -283 143 N ATOM 2561 CA THR A 399 175.148 21.399 531.763 1.00 23.80 C ANISOU 2561 CA THR A 399 2645 2313 4087 432 -336 163 C ATOM 2562 C THR A 399 176.237 21.727 530.749 1.00 22.90 C ANISOU 2562 C THR A 399 2716 2059 3927 361 -349 142 C ATOM 2563 O THR A 399 175.921 22.235 529.668 1.00 23.91 O ANISOU 2563 O THR A 399 2911 2195 3977 420 -409 189 O ATOM 2564 CB THR A 399 174.733 22.679 532.497 1.00 24.46 C ANISOU 2564 CB THR A 399 2796 2356 4142 641 -274 174 C ATOM 2565 OG1 THR A 399 175.782 23.099 533.377 1.00 24.01 O ANISOU 2565 OG1 THR A 399 2899 2155 4068 588 -202 103 O ATOM 2566 CG2 THR A 399 173.468 22.442 533.300 1.00 25.97 C ANISOU 2566 CG2 THR A 399 2769 2740 4361 751 -229 206 C ATOM 2567 N TRP A 400 177.501 21.441 531.061 1.00 21.76 N ANISOU 2567 N TRP A 400 2635 1816 3817 244 -291 94 N ATOM 2568 CA TRP A 400 178.605 21.768 530.167 1.00 21.48 C ANISOU 2568 CA TRP A 400 2734 1678 3751 161 -256 78 C ATOM 2569 C TRP A 400 179.139 20.574 529.384 1.00 21.37 C ANISOU 2569 C TRP A 400 2679 1688 3753 50 -238 35 C ATOM 2570 O TRP A 400 179.892 20.779 528.426 1.00 22.03 O ANISOU 2570 O TRP A 400 2862 1726 3780 -6 -183 23 O ATOM 2571 CB TRP A 400 179.763 22.401 530.948 1.00 21.32 C ANISOU 2571 CB TRP A 400 2778 1559 3766 97 -196 44 C ATOM 2572 CG TRP A 400 179.533 23.816 531.355 1.00 21.99 C ANISOU 2572 CG TRP A 400 3019 1526 3811 168 -179 45 C ATOM 2573 CD1 TRP A 400 178.372 24.358 531.817 1.00 22.59 C ANISOU 2573 CD1 TRP A 400 3119 1605 3862 346 -191 64 C ATOM 2574 CD2 TRP A 400 180.492 24.881 531.328 1.00 22.64 C ANISOU 2574 CD2 TRP A 400 3268 1445 3889 61 -123 18 C ATOM 2575 NE1 TRP A 400 178.548 25.693 532.087 1.00 23.50 N ANISOU 2575 NE1 TRP A 400 3448 1526 3954 389 -139 38 N ATOM 2576 CE2 TRP A 400 179.841 26.039 531.794 1.00 23.50 C ANISOU 2576 CE2 TRP A 400 3553 1409 3968 185 -104 7 C ATOM 2577 CE3 TRP A 400 181.838 24.965 530.957 1.00 23.04 C ANISOU 2577 CE3 TRP A 400 3325 1458 3972 -138 -69 -2 C ATOM 2578 CZ2 TRP A 400 180.489 27.268 531.901 1.00 24.61 C ANISOU 2578 CZ2 TRP A 400 3925 1358 4068 84 -32 -33 C ATOM 2579 CZ3 TRP A 400 182.481 26.187 531.064 1.00 24.18 C ANISOU 2579 CZ3 TRP A 400 3647 1449 4091 -265 -14 -29 C ATOM 2580 CH2 TRP A 400 181.806 27.321 531.532 1.00 24.88 C ANISOU 2580 CH2 TRP A 400 3961 1375 4116 -167 -4 -50 C ATOM 2581 N ALA A 401 178.778 19.342 529.763 1.00 26.73 N ANISOU 2581 N ALA A 401 3240 2413 4503 14 -254 10 N ATOM 2582 CA ALA A 401 179.207 18.126 529.075 1.00 26.89 C ANISOU 2582 CA ALA A 401 3267 2397 4555 -72 -214 -58 C ATOM 2583 C ALA A 401 178.654 18.028 527.652 1.00 28.53 C ANISOU 2583 C ALA A 401 3559 2653 4628 -122 -264 -112 C ATOM 2584 O ALA A 401 179.413 17.697 526.732 1.00 29.48 O ANISOU 2584 O ALA A 401 3783 2727 4692 -169 -185 -184 O ATOM 2585 CB ALA A 401 178.810 16.884 529.883 1.00 26.56 C ANISOU 2585 CB ALA A 401 3129 2335 4628 -109 -212 -53 C ATOM 2586 N PRO A 402 177.354 18.280 527.417 1.00 26.43 N ANISOU 2586 N PRO A 402 3239 2513 4290 -107 -394 -81 N ATOM 2587 CA PRO A 402 176.838 18.135 526.042 1.00 29.15 C ANISOU 2587 CA PRO A 402 3657 2956 4462 -169 -489 -132 C ATOM 2588 C PRO A 402 177.558 18.993 525.014 1.00 30.66 C ANISOU 2588 C PRO A 402 4041 3126 4481 -128 -442 -101 C ATOM 2589 O PRO A 402 177.839 18.514 523.909 1.00 32.82 O ANISOU 2589 O PRO A 402 4442 3421 4605 -215 -423 -192 O ATOM 2590 CB PRO A 402 175.362 18.535 526.187 1.00 31.48 C ANISOU 2590 CB PRO A 402 3789 3443 4730 -109 -655 -53 C ATOM 2591 CG PRO A 402 175.031 18.198 527.584 1.00 29.77 C ANISOU 2591 CG PRO A 402 3404 3209 4698 -98 -603 -24 C ATOM 2592 CD PRO A 402 176.256 18.577 528.356 1.00 26.60 C ANISOU 2592 CD PRO A 402 3102 2636 4370 -34 -460 -5 C ATOM 2593 N TYR A 403 177.866 20.250 525.337 1.00 22.27 N ANISOU 2593 N TYR A 403 3033 2006 3422 -14 -405 20 N ATOM 2594 CA TYR A 403 178.596 21.087 524.389 1.00 24.12 C ANISOU 2594 CA TYR A 403 3472 2190 3504 -11 -326 81 C ATOM 2595 C TYR A 403 179.987 20.528 524.112 1.00 24.17 C ANISOU 2595 C TYR A 403 3526 2117 3539 -126 -135 -14 C ATOM 2596 O TYR A 403 180.466 20.569 522.972 1.00 26.75 O ANISOU 2596 O TYR A 403 4005 2469 3689 -178 -49 -27 O ATOM 2597 CB TYR A 403 178.695 22.521 524.913 1.00 23.20 C ANISOU 2597 CB TYR A 403 3434 1955 3427 98 -298 218 C ATOM 2598 CG TYR A 403 179.578 23.412 524.069 1.00 25.00 C ANISOU 2598 CG TYR A 403 3888 2078 3532 51 -174 305 C ATOM 2599 CD1 TYR A 403 179.058 24.115 522.989 1.00 27.83 C ANISOU 2599 CD1 TYR A 403 4433 2471 3670 134 -238 450 C ATOM 2600 CD2 TYR A 403 180.933 23.549 524.349 1.00 24.19 C ANISOU 2600 CD2 TYR A 403 3798 1865 3529 -84 7 265 C ATOM 2601 CE1 TYR A 403 179.862 24.928 522.214 1.00 29.48 C ANISOU 2601 CE1 TYR A 403 4879 2569 3752 71 -95 563 C ATOM 2602 CE2 TYR A 403 181.744 24.355 523.576 1.00 25.98 C ANISOU 2602 CE2 TYR A 403 4211 2006 3655 -173 152 356 C ATOM 2603 CZ TYR A 403 181.203 25.044 522.514 1.00 28.54 C ANISOU 2603 CZ TYR A 403 4763 2329 3753 -102 117 510 C ATOM 2604 OH TYR A 403 182.009 25.850 521.747 1.00 30.40 O ANISOU 2604 OH TYR A 403 5214 2462 3874 -210 291 633 O ATOM 2605 N ASN A 404 180.655 20.006 525.141 1.00 23.61 N ANISOU 2605 N ASN A 404 3317 1976 3677 -146 -58 -69 N ATOM 2606 CA ASN A 404 182.030 19.554 524.976 1.00 23.95 C ANISOU 2606 CA ASN A 404 3341 1973 3786 -202 127 -133 C ATOM 2607 C ASN A 404 182.139 18.225 524.243 1.00 25.26 C ANISOU 2607 C ASN A 404 3540 2144 3913 -228 196 -277 C ATOM 2608 O ASN A 404 183.192 17.943 523.661 1.00 26.98 O ANISOU 2608 O ASN A 404 3785 2348 4116 -241 386 -337 O ATOM 2609 CB ASN A 404 182.718 19.464 526.339 1.00 21.86 C ANISOU 2609 CB ASN A 404 2899 1666 3739 -187 149 -118 C ATOM 2610 CG ASN A 404 183.103 20.825 526.879 1.00 21.58 C ANISOU 2610 CG ASN A 404 2881 1597 3721 -221 148 -34 C ATOM 2611 OD1 ASN A 404 184.187 21.334 526.591 1.00 22.99 O ANISOU 2611 OD1 ASN A 404 3058 1766 3912 -312 273 -20 O ATOM 2612 ND2 ASN A 404 182.210 21.430 527.656 1.00 20.17 N ANISOU 2612 ND2 ASN A 404 2723 1394 3548 -162 26 9 N ATOM 2613 N VAL A 405 181.088 17.402 524.251 1.00 32.18 N ANISOU 2613 N VAL A 405 4414 3032 4779 -247 68 -348 N ATOM 2614 CA VAL A 405 181.126 16.207 523.417 1.00 33.85 C ANISOU 2614 CA VAL A 405 4733 3205 4923 -308 135 -525 C ATOM 2615 C VAL A 405 180.844 16.567 521.962 1.00 37.34 C ANISOU 2615 C VAL A 405 5376 3765 5047 -369 114 -575 C ATOM 2616 O VAL A 405 181.273 15.852 521.050 1.00 39.33 O ANISOU 2616 O VAL A 405 5780 3993 5172 -414 244 -739 O ATOM 2617 CB VAL A 405 180.154 15.132 523.937 1.00 32.73 C ANISOU 2617 CB VAL A 405 4538 3008 4892 -375 16 -598 C ATOM 2618 CG1 VAL A 405 180.360 14.904 525.427 1.00 29.82 C ANISOU 2618 CG1 VAL A 405 3997 2550 4784 -303 30 -494 C ATOM 2619 CG2 VAL A 405 178.711 15.504 523.633 1.00 33.98 C ANISOU 2619 CG2 VAL A 405 4672 3333 4907 -454 -217 -571 C ATOM 2620 N MET A 406 180.136 17.674 521.718 1.00 24.18 N ANISOU 2620 N MET A 406 3735 2225 3229 -349 -41 -429 N ATOM 2621 CA MET A 406 179.980 18.162 520.351 1.00 26.51 C ANISOU 2621 CA MET A 406 4239 2650 3183 -378 -66 -413 C ATOM 2622 C MET A 406 181.313 18.640 519.792 1.00 27.53 C ANISOU 2622 C MET A 406 4493 2736 3233 -373 204 -378 C ATOM 2623 O MET A 406 181.618 18.411 518.616 1.00 30.76 O ANISOU 2623 O MET A 406 5099 3219 3370 -425 312 -463 O ATOM 2624 CB MET A 406 178.947 19.287 520.304 1.00 27.17 C ANISOU 2624 CB MET A 406 4313 2856 3152 -296 -290 -211 C ATOM 2625 CG MET A 406 177.578 18.905 520.837 1.00 26.62 C ANISOU 2625 CG MET A 406 4052 2896 3167 -295 -542 -225 C ATOM 2626 SD MET A 406 176.497 20.333 521.053 0.91 28.63 S ANISOU 2626 SD MET A 406 4229 3271 3380 -92 -749 41 S ATOM 2627 CE MET A 406 175.212 19.626 522.082 1.00 27.01 C ANISOU 2627 CE MET A 406 3688 3180 3395 -111 -923 -13 C ATOM 2628 N VAL A 407 182.119 19.308 520.622 1.00 27.90 N ANISOU 2628 N VAL A 407 4420 2683 3496 -336 321 -262 N ATOM 2629 CA VAL A 407 183.456 19.713 520.199 1.00 29.90 C ANISOU 2629 CA VAL A 407 4715 2917 3728 -375 597 -229 C ATOM 2630 C VAL A 407 184.300 18.489 519.870 1.00 30.98 C ANISOU 2630 C VAL A 407 4817 3046 3908 -372 816 -430 C ATOM 2631 O VAL A 407 185.067 18.487 518.899 1.00 34.51 O ANISOU 2631 O VAL A 407 5379 3553 4181 -403 1055 -471 O ATOM 2632 CB VAL A 407 184.116 20.585 521.285 1.00 27.25 C ANISOU 2632 CB VAL A 407 4218 2492 3645 -385 638 -100 C ATOM 2633 CG1 VAL A 407 185.571 20.868 520.938 1.00 29.59 C ANISOU 2633 CG1 VAL A 407 4468 2803 3970 -473 929 -81 C ATOM 2634 CG2 VAL A 407 183.345 21.885 521.463 1.00 26.36 C ANISOU 2634 CG2 VAL A 407 4219 2328 3467 -364 481 83 C ATOM 2635 N LEU A 408 184.163 17.425 520.664 1.00 35.10 N ANISOU 2635 N LEU A 408 5199 3480 4658 -318 763 -549 N ATOM 2636 CA LEU A 408 184.909 16.197 520.406 1.00 35.80 C ANISOU 2636 CA LEU A 408 5281 3500 4822 -260 978 -738 C ATOM 2637 C LEU A 408 184.482 15.558 519.089 1.00 38.26 C ANISOU 2637 C LEU A 408 5875 3841 4820 -316 1024 -936 C ATOM 2638 O LEU A 408 185.326 15.170 518.273 1.00 40.54 O ANISOU 2638 O LEU A 408 6266 4142 4996 -282 1303 -1063 O ATOM 2639 CB LEU A 408 184.724 15.224 521.572 1.00 32.55 C ANISOU 2639 CB LEU A 408 4712 2943 4713 -182 892 -778 C ATOM 2640 CG LEU A 408 185.135 13.760 521.389 1.00 32.97 C ANISOU 2640 CG LEU A 408 4824 2834 4869 -91 1064 -976 C ATOM 2641 CD1 LEU A 408 186.579 13.630 520.926 1.00 35.24 C ANISOU 2641 CD1 LEU A 408 5043 3150 5198 37 1396 -1019 C ATOM 2642 CD2 LEU A 408 184.921 12.996 522.688 1.00 30.25 C ANISOU 2642 CD2 LEU A 408 4336 2330 4826 -14 960 -924 C ATOM 2643 N ILE A 409 183.171 15.438 518.863 1.00 30.92 N ANISOU 2643 N ILE A 409 5064 2951 3733 -408 754 -977 N ATOM 2644 CA ILE A 409 182.684 14.859 517.615 1.00 33.99 C ANISOU 2644 CA ILE A 409 5729 3406 3778 -507 738 -1187 C ATOM 2645 C ILE A 409 183.025 15.759 516.431 1.00 36.13 C ANISOU 2645 C ILE A 409 6195 3865 3666 -531 844 -1108 C ATOM 2646 O ILE A 409 183.261 15.272 515.319 1.00 39.37 O ANISOU 2646 O ILE A 409 6855 4334 3771 -576 996 -1300 O ATOM 2647 CB ILE A 409 181.170 14.589 517.713 1.00 33.91 C ANISOU 2647 CB ILE A 409 5725 3457 3702 -633 382 -1228 C ATOM 2648 CG1 ILE A 409 180.877 13.602 518.846 1.00 32.43 C ANISOU 2648 CG1 ILE A 409 5379 3063 3880 -643 334 -1299 C ATOM 2649 CG2 ILE A 409 180.623 14.053 516.398 1.00 37.66 C ANISOU 2649 CG2 ILE A 409 6484 4049 3775 -785 307 -1461 C ATOM 2650 CD1 ILE A 409 179.401 13.342 519.063 1.00 32.61 C ANISOU 2650 CD1 ILE A 409 5336 3166 3889 -802 13 -1321 C ATOM 2651 N ASN A 410 183.083 17.075 516.652 1.00 34.81 N ANISOU 2651 N ASN A 410 5955 3774 3497 -505 792 -825 N ATOM 2652 CA ASN A 410 183.375 18.013 515.572 1.00 37.18 C ANISOU 2652 CA ASN A 410 6468 4221 3436 -536 898 -686 C ATOM 2653 C ASN A 410 184.778 17.832 515.002 1.00 39.28 C ANISOU 2653 C ASN A 410 6785 4489 3651 -531 1326 -762 C ATOM 2654 O ASN A 410 185.039 18.273 513.877 1.00 42.31 O ANISOU 2654 O ASN A 410 7408 5011 3654 -581 1478 -713 O ATOM 2655 CB ASN A 410 183.187 19.448 516.075 1.00 36.50 C ANISOU 2655 CB ASN A 410 6312 4124 3433 -506 781 -361 C ATOM 2656 CG ASN A 410 183.333 20.481 514.977 1.00 39.19 C ANISOU 2656 CG ASN A 410 6919 4577 3394 -538 864 -156 C ATOM 2657 OD1 ASN A 410 182.453 20.632 514.129 1.00 40.62 O ANISOU 2657 OD1 ASN A 410 7309 4914 3209 -535 660 -109 O ATOM 2658 ND2 ASN A 410 184.443 21.210 514.994 1.00 39.53 N ANISOU 2658 ND2 ASN A 410 6948 4554 3516 -583 1155 -14 N ATOM 2659 N THR A 411 185.682 17.183 515.741 1.00 39.25 N ANISOU 2659 N THR A 411 6549 4358 4005 -456 1531 -864 N ATOM 2660 CA THR A 411 187.050 17.019 515.261 1.00 40.66 C ANISOU 2660 CA THR A 411 6692 4577 4181 -417 1958 -923 C ATOM 2661 C THR A 411 187.131 16.053 514.087 1.00 44.41 C ANISOU 2661 C THR A 411 7450 5096 4330 -398 2162 -1210 C ATOM 2662 O THR A 411 188.038 16.168 513.255 1.00 47.58 O ANISOU 2662 O THR A 411 7932 5610 4535 -390 2528 -1238 O ATOM 2663 CB THR A 411 187.957 16.536 516.393 1.00 39.12 C ANISOU 2663 CB THR A 411 6131 4270 4462 -296 2084 -940 C ATOM 2664 OG1 THR A 411 187.607 15.191 516.748 1.00 38.87 O ANISOU 2664 OG1 THR A 411 6109 4077 4583 -185 2021 -1167 O ATOM 2665 CG2 THR A 411 187.801 17.427 517.608 1.00 36.92 C ANISOU 2665 CG2 THR A 411 5613 3954 4463 -338 1852 -705 C ATOM 2666 N PHE A 412 186.209 15.093 514.003 1.00 41.47 N ANISOU 2666 N PHE A 412 4611 5092 6053 -245 787 -600 N ATOM 2667 CA PHE A 412 186.225 14.117 512.924 1.00 43.24 C ANISOU 2667 CA PHE A 412 4999 5173 6256 -227 926 -660 C ATOM 2668 C PHE A 412 184.938 14.058 512.115 1.00 41.54 C ANISOU 2668 C PHE A 412 5126 4716 5941 -449 930 -514 C ATOM 2669 O PHE A 412 184.915 13.370 511.088 1.00 42.89 O ANISOU 2669 O PHE A 412 5446 4782 6069 -498 1059 -588 O ATOM 2670 CB PHE A 412 186.533 12.712 513.469 1.00 45.59 C ANISOU 2670 CB PHE A 412 5318 5394 6611 183 883 -669 C ATOM 2671 CG PHE A 412 185.601 12.261 514.556 1.00 45.09 C ANISOU 2671 CG PHE A 412 5454 5140 6539 342 719 -445 C ATOM 2672 CD1 PHE A 412 185.888 12.527 515.885 1.00 44.51 C ANISOU 2672 CD1 PHE A 412 5225 5202 6484 571 555 -395 C ATOM 2673 CD2 PHE A 412 184.443 11.565 514.252 1.00 44.83 C ANISOU 2673 CD2 PHE A 412 5765 4807 6462 237 751 -316 C ATOM 2674 CE1 PHE A 412 185.034 12.113 516.889 1.00 43.61 C ANISOU 2674 CE1 PHE A 412 5340 4893 6337 695 442 -192 C ATOM 2675 CE2 PHE A 412 183.586 11.149 515.251 1.00 43.37 C ANISOU 2675 CE2 PHE A 412 5774 4443 6262 323 661 -146 C ATOM 2676 CZ PHE A 412 183.881 11.423 516.571 1.00 42.95 C ANISOU 2676 CZ PHE A 412 5609 4492 6219 554 516 -69 C ATOM 2677 N CYS A 413 183.873 14.744 512.533 1.00 42.34 N ANISOU 2677 N CYS A 413 5333 4759 5995 -567 788 -343 N ATOM 2678 CA CYS A 413 182.625 14.756 511.766 1.00 40.21 C ANISOU 2678 CA CYS A 413 5321 4346 5610 -743 754 -259 C ATOM 2679 C CYS A 413 181.892 16.059 512.090 1.00 37.36 C ANISOU 2679 C CYS A 413 4991 4029 5176 -864 623 -138 C ATOM 2680 O CYS A 413 181.053 16.106 512.991 1.00 35.80 O ANISOU 2680 O CYS A 413 4784 3807 5011 -805 472 -23 O ATOM 2681 CB CYS A 413 181.758 13.544 512.072 1.00 40.32 C ANISOU 2681 CB CYS A 413 5474 4190 5655 -654 708 -207 C ATOM 2682 SG CYS A 413 180.200 13.531 511.154 0.84 38.58 S ANISOU 2682 SG CYS A 413 5464 3903 5290 -885 646 -200 S ATOM 2683 N ALA A 414 182.220 17.109 511.341 1.00 52.26 N ANISOU 2683 N ALA A 414 6953 5960 6945 -1032 710 -173 N ATOM 2684 CA ALA A 414 181.504 18.372 511.496 1.00 50.43 C ANISOU 2684 CA ALA A 414 6846 5717 6599 -1112 607 -56 C ATOM 2685 C ALA A 414 180.029 18.279 511.117 1.00 49.85 C ANISOU 2685 C ALA A 414 6950 5587 6403 -1088 435 30 C ATOM 2686 O ALA A 414 179.203 18.869 511.836 1.00 48.55 O ANISOU 2686 O ALA A 414 6774 5441 6231 -1031 273 131 O ATOM 2687 CB ALA A 414 182.210 19.471 510.689 1.00 50.96 C ANISOU 2687 CB ALA A 414 7068 5775 6519 -1304 795 -117 C ATOM 2688 N PRO A 415 179.622 17.592 510.041 1.00 45.89 N ANISOU 2688 N PRO A 415 6586 5053 5797 -1125 455 -37 N ATOM 2689 CA PRO A 415 178.180 17.483 509.760 1.00 46.30 C ANISOU 2689 CA PRO A 415 6723 5137 5732 -1099 265 -22 C ATOM 2690 C PRO A 415 177.402 16.710 510.812 1.00 45.29 C ANISOU 2690 C PRO A 415 6418 5024 5764 -1051 163 -16 C ATOM 2691 O PRO A 415 176.168 16.788 510.821 1.00 45.78 O ANISOU 2691 O PRO A 415 6468 5171 5754 -1047 4 -40 O ATOM 2692 CB PRO A 415 178.138 16.769 508.401 1.00 48.61 C ANISOU 2692 CB PRO A 415 7168 5414 5886 -1177 342 -147 C ATOM 2693 CG PRO A 415 179.454 17.051 507.784 1.00 49.20 C ANISOU 2693 CG PRO A 415 7334 5433 5928 -1252 568 -182 C ATOM 2694 CD PRO A 415 180.424 17.059 508.923 1.00 47.76 C ANISOU 2694 CD PRO A 415 6911 5257 5978 -1210 652 -162 C ATOM 2695 N CYS A 416 178.074 15.967 511.695 1.00 44.46 N ANISOU 2695 N CYS A 416 6192 4851 5851 -1003 257 -5 N ATOM 2696 CA CYS A 416 177.371 15.197 512.715 1.00 43.82 C ANISOU 2696 CA CYS A 416 6040 4725 5884 -974 215 11 C ATOM 2697 C CYS A 416 176.670 16.072 513.748 1.00 42.23 C ANISOU 2697 C CYS A 416 5742 4602 5701 -934 62 111 C ATOM 2698 O CYS A 416 175.835 15.557 514.499 1.00 41.83 O ANISOU 2698 O CYS A 416 5651 4534 5708 -958 36 101 O ATOM 2699 CB CYS A 416 178.337 14.248 513.429 1.00 44.36 C ANISOU 2699 CB CYS A 416 6087 4672 6094 -852 344 24 C ATOM 2700 SG CYS A 416 178.846 12.796 512.474 1.00 46.79 S ANISOU 2700 SG CYS A 416 6545 4828 6405 -862 544 -114 S ATOM 2701 N ILE A 417 176.984 17.359 513.812 1.00 35.92 N ANISOU 2701 N ILE A 417 4933 3868 4848 -895 -2 187 N ATOM 2702 CA ILE A 417 176.378 18.277 514.765 1.00 34.28 C ANISOU 2702 CA ILE A 417 4655 3720 4648 -842 -133 275 C ATOM 2703 C ILE A 417 175.729 19.416 513.989 1.00 35.12 C ANISOU 2703 C ILE A 417 4887 3892 4565 -820 -248 285 C ATOM 2704 O ILE A 417 176.409 20.319 513.501 1.00 35.30 O ANISOU 2704 O ILE A 417 5056 3870 4487 -826 -192 327 O ATOM 2705 CB ILE A 417 177.414 18.815 515.771 1.00 33.01 C ANISOU 2705 CB ILE A 417 4405 3552 4585 -787 -92 350 C ATOM 2706 CG1 ILE A 417 178.253 17.673 516.350 1.00 33.72 C ANISOU 2706 CG1 ILE A 417 4413 3595 4805 -713 1 328 C ATOM 2707 CG2 ILE A 417 176.716 19.570 516.892 1.00 31.21 C ANISOU 2707 CG2 ILE A 417 4113 3368 4377 -738 -213 430 C ATOM 2708 CD1 ILE A 417 177.460 16.690 517.182 1.00 33.24 C ANISOU 2708 CD1 ILE A 417 4369 3457 4802 -675 -16 355 C ATOM 2709 N PRO A 418 174.405 19.401 513.846 1.00 37.98 N ANISOU 2709 N PRO A 418 5216 4366 4850 -784 -400 225 N ATOM 2710 CA PRO A 418 173.719 20.522 513.193 1.00 40.15 C ANISOU 2710 CA PRO A 418 5629 4720 4905 -656 -556 236 C ATOM 2711 C PRO A 418 173.827 21.798 514.014 1.00 38.43 C ANISOU 2711 C PRO A 418 5465 4454 4681 -554 -594 365 C ATOM 2712 O PRO A 418 174.150 21.785 515.204 1.00 35.98 O ANISOU 2712 O PRO A 418 5013 4113 4546 -591 -546 418 O ATOM 2713 CB PRO A 418 172.264 20.048 513.100 1.00 42.76 C ANISOU 2713 CB PRO A 418 5792 5260 5194 -623 -722 77 C ATOM 2714 CG PRO A 418 172.333 18.557 513.230 1.00 41.70 C ANISOU 2714 CG PRO A 418 5531 5097 5218 -821 -582 -35 C ATOM 2715 CD PRO A 418 173.490 18.287 514.140 1.00 38.54 C ANISOU 2715 CD PRO A 418 5139 4504 5002 -864 -412 101 C ATOM 2716 N ASN A 419 173.543 22.922 513.349 1.00 60.59 N ANISOU 2716 N ASN A 419 8528 7240 7254 -407 -679 412 N ATOM 2717 CA ASN A 419 173.607 24.215 514.023 1.00 59.00 C ANISOU 2717 CA ASN A 419 8461 6944 7011 -309 -688 525 C ATOM 2718 C ASN A 419 172.572 24.323 515.135 1.00 58.36 C ANISOU 2718 C ASN A 419 8138 7002 7034 -194 -842 502 C ATOM 2719 O ASN A 419 172.815 24.995 516.144 1.00 56.43 O ANISOU 2719 O ASN A 419 7883 6686 6873 -195 -801 578 O ATOM 2720 CB ASN A 419 173.422 25.346 513.009 1.00 60.42 C ANISOU 2720 CB ASN A 419 9072 7020 6866 -130 -731 587 C ATOM 2721 CG ASN A 419 173.270 26.703 513.671 1.00 59.35 C ANISOU 2721 CG ASN A 419 9142 6757 6652 10 -742 691 C ATOM 2722 OD1 ASN A 419 174.234 27.264 514.192 1.00 57.95 O ANISOU 2722 OD1 ASN A 419 9067 6404 6547 -164 -538 751 O ATOM 2723 ND2 ASN A 419 172.054 27.239 513.651 1.00 60.26 N ANISOU 2723 ND2 ASN A 419 9307 6979 6611 330 -978 680 N ATOM 2724 N THR A 420 171.417 23.675 514.970 1.00 38.50 N ANISOU 2724 N THR A 420 5414 4705 4511 -124 -1000 362 N ATOM 2725 CA THR A 420 170.415 23.670 516.031 1.00 37.96 C ANISOU 2725 CA THR A 420 5074 4796 4553 -66 -1101 289 C ATOM 2726 C THR A 420 170.942 22.969 517.277 1.00 36.18 C ANISOU 2726 C THR A 420 4669 4493 4583 -277 -942 329 C ATOM 2727 O THR A 420 170.682 23.407 518.404 1.00 34.71 O ANISOU 2727 O THR A 420 4391 4316 4479 -245 -950 364 O ATOM 2728 CB THR A 420 169.130 23.000 515.537 1.00 40.13 C ANISOU 2728 CB THR A 420 5113 5365 4771 -21 -1257 55 C ATOM 2729 OG1 THR A 420 168.609 23.731 514.420 1.00 41.61 O ANISOU 2729 OG1 THR A 420 5477 5664 4670 265 -1458 13 O ATOM 2730 CG2 THR A 420 168.081 22.962 516.638 1.00 39.61 C ANISOU 2730 CG2 THR A 420 4733 5492 4825 -11 -1313 -73 C ATOM 2731 N VAL A 421 171.699 21.886 517.092 1.00 37.03 N ANISOU 2731 N VAL A 421 4761 4517 4792 -458 -798 324 N ATOM 2732 CA VAL A 421 172.271 21.175 518.230 1.00 34.08 C ANISOU 2732 CA VAL A 421 4289 4053 4607 -580 -664 374 C ATOM 2733 C VAL A 421 173.352 22.016 518.899 1.00 31.68 C ANISOU 2733 C VAL A 421 4061 3638 4337 -549 -611 512 C ATOM 2734 O VAL A 421 173.496 22.003 520.128 1.00 30.12 O ANISOU 2734 O VAL A 421 3778 3428 4239 -556 -586 559 O ATOM 2735 CB VAL A 421 172.805 19.803 517.779 1.00 33.82 C ANISOU 2735 CB VAL A 421 4269 3941 4639 -712 -530 325 C ATOM 2736 CG1 VAL A 421 173.518 19.097 518.919 1.00 31.82 C ANISOU 2736 CG1 VAL A 421 3996 3567 4525 -744 -406 399 C ATOM 2737 CG2 VAL A 421 171.664 18.944 517.253 1.00 35.98 C ANISOU 2737 CG2 VAL A 421 4453 4332 4884 -811 -548 139 C ATOM 2738 N TRP A 422 174.125 22.766 518.108 1.00 36.26 N ANISOU 2738 N TRP A 422 4817 4145 4816 -538 -575 554 N ATOM 2739 CA TRP A 422 175.130 23.653 518.686 1.00 34.94 C ANISOU 2739 CA TRP A 422 4707 3899 4669 -571 -492 620 C ATOM 2740 C TRP A 422 174.486 24.720 519.562 1.00 34.42 C ANISOU 2740 C TRP A 422 4662 3839 4575 -482 -573 665 C ATOM 2741 O TRP A 422 174.987 25.024 520.651 1.00 33.27 O ANISOU 2741 O TRP A 422 4438 3689 4514 -523 -532 689 O ATOM 2742 CB TRP A 422 175.964 24.309 517.583 1.00 35.98 C ANISOU 2742 CB TRP A 422 5072 3931 4669 -638 -377 619 C ATOM 2743 CG TRP A 422 177.072 23.451 517.051 1.00 36.45 C ANISOU 2743 CG TRP A 422 5067 3989 4794 -758 -236 554 C ATOM 2744 CD1 TRP A 422 177.160 22.908 515.802 1.00 37.85 C ANISOU 2744 CD1 TRP A 422 5350 4143 4890 -791 -186 508 C ATOM 2745 CD2 TRP A 422 178.253 23.038 517.752 1.00 36.21 C ANISOU 2745 CD2 TRP A 422 4839 4009 4909 -824 -136 502 C ATOM 2746 NE1 TRP A 422 178.322 22.185 515.681 1.00 38.32 N ANISOU 2746 NE1 TRP A 422 5292 4217 5051 -881 -41 433 N ATOM 2747 CE2 TRP A 422 179.010 22.248 516.865 1.00 37.64 C ANISOU 2747 CE2 TRP A 422 5005 4194 5102 -880 -21 421 C ATOM 2748 CE3 TRP A 422 178.742 23.261 519.043 1.00 35.57 C ANISOU 2748 CE3 TRP A 422 4586 4000 4930 -814 -148 497 C ATOM 2749 CZ2 TRP A 422 180.230 21.678 517.228 1.00 38.81 C ANISOU 2749 CZ2 TRP A 422 4948 4429 5367 -889 72 324 C ATOM 2750 CZ3 TRP A 422 179.953 22.696 519.401 1.00 36.80 C ANISOU 2750 CZ3 TRP A 422 4541 4261 5182 -820 -78 400 C ATOM 2751 CH2 TRP A 422 180.683 21.914 518.497 1.00 38.52 C ANISOU 2751 CH2 TRP A 422 4725 4495 5416 -840 27 310 C ATOM 2752 N THR A 423 173.376 25.302 519.099 1.00 33.42 N ANISOU 2752 N THR A 423 4638 3744 4315 -330 -698 658 N ATOM 2753 CA THR A 423 172.691 26.325 519.883 1.00 33.16 C ANISOU 2753 CA THR A 423 4638 3716 4247 -197 -776 684 C ATOM 2754 C THR A 423 172.200 25.763 521.211 1.00 32.23 C ANISOU 2754 C THR A 423 4245 3710 4293 -231 -800 653 C ATOM 2755 O THR A 423 172.308 26.423 522.252 1.00 31.32 O ANISOU 2755 O THR A 423 4124 3562 4214 -226 -779 689 O ATOM 2756 CB THR A 423 171.527 26.910 519.080 1.00 35.04 C ANISOU 2756 CB THR A 423 5007 4017 4290 57 -942 649 C ATOM 2757 OG1 THR A 423 172.037 27.656 517.967 1.00 35.93 O ANISOU 2757 OG1 THR A 423 5504 3958 4190 115 -892 714 O ATOM 2758 CG2 THR A 423 170.676 27.828 519.949 1.00 35.02 C ANISOU 2758 CG2 THR A 423 4989 4052 4264 246 -1034 644 C ATOM 2759 N ILE A 424 171.674 24.536 521.198 1.00 32.87 N ANISOU 2759 N ILE A 424 4134 3901 4454 -293 -814 574 N ATOM 2760 CA ILE A 424 171.173 23.925 522.426 1.00 32.65 C ANISOU 2760 CA ILE A 424 3920 3938 4547 -360 -782 540 C ATOM 2761 C ILE A 424 172.316 23.681 523.405 1.00 30.53 C ANISOU 2761 C ILE A 424 3669 3567 4365 -441 -680 637 C ATOM 2762 O ILE A 424 172.205 23.976 524.600 1.00 29.95 O ANISOU 2762 O ILE A 424 3553 3504 4325 -434 -671 663 O ATOM 2763 CB ILE A 424 170.415 22.625 522.106 1.00 34.35 C ANISOU 2763 CB ILE A 424 3999 4248 4805 -468 -753 408 C ATOM 2764 CG1 ILE A 424 169.195 22.925 521.232 1.00 36.34 C ANISOU 2764 CG1 ILE A 424 4153 4701 4955 -363 -895 247 C ATOM 2765 CG2 ILE A 424 169.993 21.921 523.386 1.00 33.72 C ANISOU 2765 CG2 ILE A 424 3820 4171 4822 -586 -646 378 C ATOM 2766 CD1 ILE A 424 168.440 21.693 520.788 1.00 37.84 C ANISOU 2766 CD1 ILE A 424 4180 5023 5172 -525 -851 47 C ATOM 2767 N GLY A 425 173.433 23.142 522.911 1.00 34.17 N ANISOU 2767 N GLY A 425 4179 3958 4846 -493 -612 667 N ATOM 2768 CA GLY A 425 174.578 22.915 523.776 1.00 33.33 C ANISOU 2768 CA GLY A 425 4046 3822 4794 -505 -556 715 C ATOM 2769 C GLY A 425 175.174 24.198 524.319 1.00 33.14 C ANISOU 2769 C GLY A 425 4040 3809 4741 -505 -564 731 C ATOM 2770 O GLY A 425 175.661 24.231 525.452 1.00 33.21 O ANISOU 2770 O GLY A 425 3983 3860 4776 -492 -566 741 O ATOM 2771 N TYR A 426 175.147 25.268 523.522 1.00 29.47 N ANISOU 2771 N TYR A 426 3707 3294 4196 -521 -557 722 N ATOM 2772 CA TYR A 426 175.618 26.562 524.001 1.00 29.77 C ANISOU 2772 CA TYR A 426 3830 3292 4188 -565 -515 715 C ATOM 2773 C TYR A 426 174.708 27.105 525.097 1.00 29.50 C ANISOU 2773 C TYR A 426 3778 3278 4154 -487 -582 737 C ATOM 2774 O TYR A 426 175.183 27.708 526.067 1.00 29.79 O ANISOU 2774 O TYR A 426 3794 3327 4196 -537 -552 718 O ATOM 2775 CB TYR A 426 175.700 27.546 522.835 1.00 30.65 C ANISOU 2775 CB TYR A 426 4207 3270 4168 -591 -448 715 C ATOM 2776 CG TYR A 426 176.915 28.444 522.852 1.00 31.60 C ANISOU 2776 CG TYR A 426 4435 3321 4251 -778 -279 649 C ATOM 2777 CD1 TYR A 426 178.125 28.013 522.325 1.00 32.35 C ANISOU 2777 CD1 TYR A 426 4446 3466 4380 -936 -156 558 C ATOM 2778 CD2 TYR A 426 176.850 29.726 523.379 1.00 32.21 C ANISOU 2778 CD2 TYR A 426 4695 3290 4255 -819 -215 639 C ATOM 2779 CE1 TYR A 426 179.238 28.829 522.330 1.00 33.72 C ANISOU 2779 CE1 TYR A 426 4670 3619 4521 -1167 37 428 C ATOM 2780 CE2 TYR A 426 177.959 30.551 523.388 1.00 33.47 C ANISOU 2780 CE2 TYR A 426 4961 3383 4374 -1064 -11 528 C ATOM 2781 CZ TYR A 426 179.150 30.096 522.862 1.00 34.21 C ANISOU 2781 CZ TYR A 426 4926 3565 4508 -1257 120 407 C ATOM 2782 OH TYR A 426 180.258 30.912 522.869 1.00 35.69 O ANISOU 2782 OH TYR A 426 5171 3731 4658 -1558 359 230 O ATOM 2783 N TRP A 427 173.396 26.891 524.962 1.00 37.94 N ANISOU 2783 N TRP A 427 4823 4381 5211 -373 -667 741 N ATOM 2784 CA TRP A 427 172.453 27.416 525.944 1.00 38.26 C ANISOU 2784 CA TRP A 427 4822 4464 5251 -292 -713 728 C ATOM 2785 C TRP A 427 172.525 26.650 527.258 1.00 37.82 C ANISOU 2785 C TRP A 427 4618 4476 5277 -357 -686 732 C ATOM 2786 O TRP A 427 172.352 27.238 528.331 1.00 38.16 O ANISOU 2786 O TRP A 427 4657 4532 5312 -346 -679 729 O ATOM 2787 CB TRP A 427 171.032 27.377 525.384 1.00 39.45 C ANISOU 2787 CB TRP A 427 4925 4703 5360 -146 -811 664 C ATOM 2788 CG TRP A 427 170.581 28.692 524.861 1.00 40.49 C ANISOU 2788 CG TRP A 427 5258 4769 5355 49 -874 666 C ATOM 2789 CD1 TRP A 427 170.464 29.059 523.554 1.00 41.36 C ANISOU 2789 CD1 TRP A 427 5563 4826 5324 184 -932 675 C ATOM 2790 CD2 TRP A 427 170.198 29.832 525.636 1.00 41.23 C ANISOU 2790 CD2 TRP A 427 5448 4813 5403 166 -876 663 C ATOM 2791 NE1 TRP A 427 170.024 30.358 523.466 1.00 42.54 N ANISOU 2791 NE1 TRP A 427 5963 4875 5325 411 -973 693 N ATOM 2792 CE2 TRP A 427 169.854 30.855 524.732 1.00 42.51 C ANISOU 2792 CE2 TRP A 427 5895 4867 5389 399 -934 680 C ATOM 2793 CE3 TRP A 427 170.110 30.087 527.008 1.00 41.31 C ANISOU 2793 CE3 TRP A 427 5369 4845 5481 112 -829 648 C ATOM 2794 CZ2 TRP A 427 169.428 32.111 525.154 1.00 43.80 C ANISOU 2794 CZ2 TRP A 427 6267 4921 5453 594 -937 683 C ATOM 2795 CZ3 TRP A 427 169.687 31.334 527.426 1.00 42.70 C ANISOU 2795 CZ3 TRP A 427 5708 4939 5577 268 -830 635 C ATOM 2796 CH2 TRP A 427 169.352 32.331 526.502 1.00 43.90 C ANISOU 2796 CH2 TRP A 427 6155 4962 5564 513 -879 652 C ATOM 2797 N LEU A 428 172.768 25.338 527.195 1.00 40.91 N ANISOU 2797 N LEU A 428 4940 4885 5720 -409 -656 743 N ATOM 2798 CA LEU A 428 172.859 24.547 528.419 1.00 40.93 C ANISOU 2798 CA LEU A 428 4909 4900 5743 -431 -613 771 C ATOM 2799 C LEU A 428 173.980 25.048 529.319 1.00 41.00 C ANISOU 2799 C LEU A 428 4925 4931 5721 -415 -629 797 C ATOM 2800 O LEU A 428 173.846 25.043 530.548 1.00 41.49 O ANISOU 2800 O LEU A 428 4995 5022 5749 -396 -626 812 O ATOM 2801 CB LEU A 428 173.059 23.070 528.080 1.00 40.98 C ANISOU 2801 CB LEU A 428 4939 4857 5776 -458 -554 786 C ATOM 2802 CG LEU A 428 171.789 22.293 527.732 1.00 42.06 C ANISOU 2802 CG LEU A 428 5051 4995 5934 -544 -489 711 C ATOM 2803 CD1 LEU A 428 172.126 20.862 527.347 1.00 42.25 C ANISOU 2803 CD1 LEU A 428 5171 4912 5970 -593 -391 721 C ATOM 2804 CD2 LEU A 428 170.818 22.322 528.904 1.00 43.20 C ANISOU 2804 CD2 LEU A 428 5175 5172 6066 -598 -422 671 C ATOM 2805 N CYS A 429 175.092 25.489 528.728 1.00 27.23 N ANISOU 2805 N CYS A 429 3172 3200 3975 -441 -633 769 N ATOM 2806 CA CYS A 429 176.159 26.077 529.530 1.00 28.84 C ANISOU 2806 CA CYS A 429 3321 3490 4145 -464 -645 716 C ATOM 2807 C CYS A 429 175.683 27.348 530.221 1.00 29.07 C ANISOU 2807 C CYS A 429 3408 3503 4136 -509 -636 689 C ATOM 2808 O CYS A 429 176.050 27.614 531.372 1.00 30.35 O ANISOU 2808 O CYS A 429 3527 3750 4254 -511 -659 652 O ATOM 2809 CB CYS A 429 177.379 26.361 528.656 1.00 29.52 C ANISOU 2809 CB CYS A 429 3357 3618 4243 -549 -600 626 C ATOM 2810 SG CYS A 429 178.079 24.914 527.822 0.96 30.04 S ANISOU 2810 SG CYS A 429 3347 3715 4353 -470 -598 627 S ATOM 2811 N TYR A 430 174.865 28.148 529.531 1.00 22.37 N ANISOU 2811 N TYR A 430 2677 2544 3277 -511 -610 699 N ATOM 2812 CA TYR A 430 174.266 29.316 530.166 1.00 23.11 C ANISOU 2812 CA TYR A 430 2867 2589 3326 -499 -594 676 C ATOM 2813 C TYR A 430 173.311 28.915 531.283 1.00 23.31 C ANISOU 2813 C TYR A 430 2817 2678 3360 -429 -626 695 C ATOM 2814 O TYR A 430 173.209 29.622 532.292 1.00 24.56 O ANISOU 2814 O TYR A 430 3005 2849 3479 -441 -609 660 O ATOM 2815 CB TYR A 430 173.532 30.166 529.126 1.00 23.19 C ANISOU 2815 CB TYR A 430 3062 2462 3286 -419 -582 688 C ATOM 2816 CG TYR A 430 174.432 30.909 528.163 1.00 23.70 C ANISOU 2816 CG TYR A 430 3325 2394 3287 -523 -484 666 C ATOM 2817 CD1 TYR A 430 175.764 31.155 528.470 1.00 24.50 C ANISOU 2817 CD1 TYR A 430 3390 2527 3393 -731 -385 577 C ATOM 2818 CD2 TYR A 430 173.945 31.370 526.946 1.00 24.26 C ANISOU 2818 CD2 TYR A 430 3629 2322 3267 -416 -478 706 C ATOM 2819 CE1 TYR A 430 176.586 31.839 527.591 1.00 25.36 C ANISOU 2819 CE1 TYR A 430 3688 2509 3437 -897 -230 515 C ATOM 2820 CE2 TYR A 430 174.756 32.053 526.061 1.00 25.50 C ANISOU 2820 CE2 TYR A 430 4049 2310 3329 -539 -337 691 C ATOM 2821 CZ TYR A 430 176.076 32.284 526.388 1.00 26.00 C ANISOU 2821 CZ TYR A 430 4072 2389 3419 -812 -187 588 C ATOM 2822 OH TYR A 430 176.885 32.964 525.506 1.00 27.71 O ANISOU 2822 OH TYR A 430 4558 2434 3536 -1002 15 532 O ATOM 2823 N ILE A 431 172.614 27.784 531.127 1.00 33.68 N ANISOU 2823 N ILE A 431 4055 4027 4715 -391 -639 726 N ATOM 2824 CA ILE A 431 171.674 27.325 532.149 1.00 34.63 C ANISOU 2824 CA ILE A 431 4132 4194 4832 -384 -606 716 C ATOM 2825 C ILE A 431 172.393 27.060 533.465 1.00 35.17 C ANISOU 2825 C ILE A 431 4234 4294 4835 -405 -595 749 C ATOM 2826 O ILE A 431 171.790 27.156 534.542 1.00 36.57 O ANISOU 2826 O ILE A 431 4437 4493 4967 -413 -549 733 O ATOM 2827 CB ILE A 431 170.916 26.074 531.656 1.00 34.78 C ANISOU 2827 CB ILE A 431 4094 4226 4896 -415 -563 704 C ATOM 2828 CG1 ILE A 431 170.157 26.379 530.363 1.00 35.19 C ANISOU 2828 CG1 ILE A 431 4080 4312 4978 -361 -615 634 C ATOM 2829 CG2 ILE A 431 169.945 25.568 532.715 1.00 36.75 C ANISOU 2829 CG2 ILE A 431 4326 4509 5129 -479 -458 659 C ATOM 2830 CD1 ILE A 431 169.214 27.550 530.471 1.00 36.66 C ANISOU 2830 CD1 ILE A 431 4235 4554 5138 -242 -658 553 C ATOM 2831 N ASN A 432 173.689 26.743 533.406 1.00 27.68 N ANISOU 2831 N ASN A 432 3279 3376 3862 -394 -643 770 N ATOM 2832 CA ASN A 432 174.456 26.522 534.628 1.00 28.86 C ANISOU 2832 CA ASN A 432 3446 3611 3907 -345 -684 775 C ATOM 2833 C ASN A 432 174.396 27.738 535.544 1.00 30.49 C ANISOU 2833 C ASN A 432 3659 3868 4058 -396 -685 701 C ATOM 2834 O ASN A 432 174.361 27.598 536.772 1.00 31.72 O ANISOU 2834 O ASN A 432 3869 4078 4105 -358 -694 708 O ATOM 2835 CB ASN A 432 175.905 26.183 534.280 1.00 29.06 C ANISOU 2835 CB ASN A 432 3386 3738 3918 -291 -763 740 C ATOM 2836 CG ASN A 432 176.723 25.796 535.497 1.00 30.45 C ANISOU 2836 CG ASN A 432 3560 4060 3948 -154 -857 723 C ATOM 2837 OD1 ASN A 432 176.185 25.318 536.496 1.00 30.99 O ANISOU 2837 OD1 ASN A 432 3780 4087 3909 -76 -844 801 O ATOM 2838 ND2 ASN A 432 178.032 26.000 535.418 1.00 31.42 N ANISOU 2838 ND2 ASN A 432 3515 4376 4046 -120 -948 596 N ATOM 2839 N SER A 433 174.374 28.939 534.964 1.00 32.14 N ANISOU 2839 N SER A 433 3867 4032 4314 -476 -657 631 N ATOM 2840 CA SER A 433 174.247 30.151 535.762 1.00 34.26 C ANISOU 2840 CA SER A 433 4190 4298 4528 -534 -622 549 C ATOM 2841 C SER A 433 172.844 30.326 536.327 1.00 34.62 C ANISOU 2841 C SER A 433 4291 4289 4572 -480 -569 569 C ATOM 2842 O SER A 433 172.678 31.017 537.338 1.00 36.68 O ANISOU 2842 O SER A 433 4601 4569 4765 -504 -538 510 O ATOM 2843 CB SER A 433 174.622 31.372 534.922 1.00 34.16 C ANISOU 2843 CB SER A 433 4260 4183 4538 -635 -559 471 C ATOM 2844 OG SER A 433 175.970 31.301 534.492 1.00 34.15 O ANISOU 2844 OG SER A 433 4174 4266 4536 -747 -562 390 O ATOM 2845 N THR A 434 171.837 29.714 535.701 1.00 31.07 N ANISOU 2845 N THR A 434 3808 3804 4192 -421 -549 614 N ATOM 2846 CA THR A 434 170.459 29.887 536.146 1.00 32.86 C ANISOU 2846 CA THR A 434 4014 4040 4429 -380 -485 566 C ATOM 2847 C THR A 434 170.153 29.040 537.375 1.00 34.11 C ANISOU 2847 C THR A 434 4191 4250 4520 -434 -410 581 C ATOM 2848 O THR A 434 169.535 29.525 538.329 1.00 36.53 O ANISOU 2848 O THR A 434 4520 4582 4778 -446 -339 518 O ATOM 2849 CB THR A 434 169.496 29.537 535.010 1.00 32.61 C ANISOU 2849 CB THR A 434 3888 4020 4482 -315 -493 539 C ATOM 2850 OG1 THR A 434 169.887 30.233 533.820 1.00 31.20 O ANISOU 2850 OG1 THR A 434 3774 3765 4316 -241 -562 554 O ATOM 2851 CG2 THR A 434 168.074 29.931 535.374 1.00 35.92 C ANISOU 2851 CG2 THR A 434 4213 4517 4915 -245 -440 415 C ATOM 2852 N ILE A 435 170.580 27.772 537.371 1.00 35.57 N ANISOU 2852 N ILE A 435 4415 4424 4676 -457 -405 665 N ATOM 2853 CA ILE A 435 170.280 26.860 538.470 1.00 36.90 C ANISOU 2853 CA ILE A 435 4714 4575 4731 -499 -296 703 C ATOM 2854 C ILE A 435 171.347 26.872 539.554 1.00 37.44 C ANISOU 2854 C ILE A 435 4918 4681 4628 -429 -373 759 C ATOM 2855 O ILE A 435 171.218 26.137 540.543 1.00 38.74 O ANISOU 2855 O ILE A 435 5277 4807 4636 -419 -293 816 O ATOM 2856 CB ILE A 435 170.096 25.421 537.947 1.00 36.02 C ANISOU 2856 CB ILE A 435 4671 4379 4635 -540 -214 762 C ATOM 2857 CG1 ILE A 435 171.406 24.904 537.348 1.00 33.98 C ANISOU 2857 CG1 ILE A 435 4448 4098 4364 -429 -346 859 C ATOM 2858 CG2 ILE A 435 168.984 25.372 536.914 1.00 36.18 C ANISOU 2858 CG2 ILE A 435 4514 4429 4804 -624 -149 650 C ATOM 2859 CD1 ILE A 435 171.309 23.506 536.777 1.00 33.46 C ANISOU 2859 CD1 ILE A 435 4495 3910 4307 -450 -256 917 C ATOM 2860 N ASN A 436 172.397 27.686 539.406 1.00 42.46 N ANISOU 2860 N ASN A 436 5470 5400 5263 -387 -514 721 N ATOM 2861 CA ASN A 436 173.476 27.669 540.393 1.00 43.51 C ANISOU 2861 CA ASN A 436 5661 5651 5218 -306 -623 715 C ATOM 2862 C ASN A 436 173.029 28.184 541.757 1.00 45.89 C ANISOU 2862 C ASN A 436 6075 5986 5374 -336 -568 671 C ATOM 2863 O ASN A 436 173.368 27.545 542.770 1.00 46.88 O ANISOU 2863 O ASN A 436 6370 6155 5288 -233 -602 725 O ATOM 2864 CB ASN A 436 174.684 28.442 539.857 1.00 43.19 C ANISOU 2864 CB ASN A 436 5450 5736 5222 -325 -748 608 C ATOM 2865 CG ASN A 436 175.995 27.720 540.104 1.00 43.21 C ANISOU 2865 CG ASN A 436 5406 5910 5101 -171 -905 597 C ATOM 2866 OD1 ASN A 436 176.164 27.046 541.120 1.00 44.29 O ANISOU 2866 OD1 ASN A 436 5683 6105 5040 -11 -965 651 O ATOM 2867 ND2 ASN A 436 176.930 27.853 539.169 1.00 42.45 N ANISOU 2867 ND2 ASN A 436 5127 5903 5098 -194 -967 513 N ATOM 2868 N PRO A 437 172.300 29.302 541.877 1.00 40.19 N ANISOU 2868 N PRO A 437 5306 5240 4725 -439 -485 575 N ATOM 2869 CA PRO A 437 171.836 29.712 543.215 1.00 42.62 C ANISOU 2869 CA PRO A 437 5733 5575 4885 -471 -409 524 C ATOM 2870 C PRO A 437 170.970 28.671 543.901 1.00 43.25 C ANISOU 2870 C PRO A 437 5995 5580 4859 -477 -256 606 C ATOM 2871 O PRO A 437 171.040 28.535 545.128 1.00 44.68 O ANISOU 2871 O PRO A 437 6366 5791 4821 -458 -226 616 O ATOM 2872 CB PRO A 437 171.052 31.002 542.937 1.00 44.07 C ANISOU 2872 CB PRO A 437 5837 5705 5202 -542 -323 407 C ATOM 2873 CG PRO A 437 171.642 31.531 541.682 1.00 42.68 C ANISOU 2873 CG PRO A 437 5557 5495 5165 -544 -404 389 C ATOM 2874 CD PRO A 437 171.974 30.322 540.861 1.00 39.93 C ANISOU 2874 CD PRO A 437 5158 5146 4869 -494 -464 503 C ATOM 2875 N ALA A 438 170.160 27.924 543.148 1.00 37.83 N ANISOU 2875 N ALA A 438 5279 4796 4299 -528 -137 644 N ATOM 2876 CA ALA A 438 169.327 26.885 543.742 1.00 38.85 C ANISOU 2876 CA ALA A 438 5609 4827 4324 -612 79 684 C ATOM 2877 C ALA A 438 170.137 25.730 544.316 1.00 38.55 C ANISOU 2877 C ALA A 438 5892 4708 4046 -495 50 843 C ATOM 2878 O ALA A 438 169.574 24.906 545.045 1.00 39.77 O ANISOU 2878 O ALA A 438 6347 4730 4034 -566 263 892 O ATOM 2879 CB ALA A 438 168.334 26.351 542.709 1.00 38.44 C ANISOU 2879 CB ALA A 438 5415 4725 4466 -732 218 628 C ATOM 2880 N CYS A 439 171.433 25.642 544.006 1.00 61.51 N ANISOU 2880 N CYS A 439 8767 7690 6913 -305 -192 907 N ATOM 2881 CA CYS A 439 172.247 24.567 544.563 1.00 61.90 C ANISOU 2881 CA CYS A 439 9129 7690 6701 -90 -263 1047 C ATOM 2882 C CYS A 439 172.546 24.788 546.040 1.00 63.93 C ANISOU 2882 C CYS A 439 9621 8025 6644 22 -311 1054 C ATOM 2883 O CYS A 439 172.788 23.820 546.769 1.00 64.98 O ANISOU 2883 O CYS A 439 10157 8050 6483 200 -286 1186 O ATOM 2884 CB CYS A 439 173.553 24.430 543.780 1.00 60.45 C ANISOU 2884 CB CYS A 439 8770 7630 6568 113 -521 1059 C ATOM 2885 SG CYS A 439 173.382 23.745 542.116 1.00 57.96 S ANISOU 2885 SG CYS A 439 8319 7183 6523 46 -462 1096 S ATOM 2886 N TYR A 440 172.530 26.039 546.502 1.00 54.21 N ANISOU 2886 N TYR A 440 8197 6960 5441 -65 -370 913 N ATOM 2887 CA TYR A 440 172.928 26.330 547.875 1.00 56.07 C ANISOU 2887 CA TYR A 440 8623 7316 5365 42 -450 886 C ATOM 2888 C TYR A 440 172.016 27.346 548.554 1.00 57.29 C ANISOU 2888 C TYR A 440 8744 7478 5546 -176 -282 762 C ATOM 2889 O TYR A 440 171.742 27.229 549.753 1.00 58.85 O ANISOU 2889 O TYR A 440 9235 7655 5470 -165 -189 779 O ATOM 2890 CB TYR A 440 174.379 26.824 547.912 1.00 56.17 C ANISOU 2890 CB TYR A 440 8417 7624 5301 230 -782 782 C ATOM 2891 CG TYR A 440 174.683 27.973 546.975 1.00 55.05 C ANISOU 2891 CG TYR A 440 7853 7602 5463 56 -847 610 C ATOM 2892 CD1 TYR A 440 175.128 27.741 545.679 1.00 53.16 C ANISOU 2892 CD1 TYR A 440 7401 7354 5444 66 -909 622 C ATOM 2893 CD2 TYR A 440 174.538 29.291 547.389 1.00 56.05 C ANISOU 2893 CD2 TYR A 440 7853 7818 5627 -123 -818 436 C ATOM 2894 CE1 TYR A 440 175.410 28.788 544.820 1.00 52.35 C ANISOU 2894 CE1 TYR A 440 7003 7315 5574 -104 -927 475 C ATOM 2895 CE2 TYR A 440 174.817 30.344 546.537 1.00 55.44 C ANISOU 2895 CE2 TYR A 440 7500 7779 5785 -286 -829 289 C ATOM 2896 CZ TYR A 440 175.253 30.087 545.254 1.00 53.63 C ANISOU 2896 CZ TYR A 440 7097 7527 5754 -280 -878 315 C ATOM 2897 OH TYR A 440 175.533 31.132 544.402 1.00 53.26 O ANISOU 2897 OH TYR A 440 6862 7475 5900 -454 -850 178 O ATOM 2898 N ALA A 441 171.541 28.346 547.807 1.00 53.10 N ANISOU 2898 N ALA A 441 7897 6965 5315 -347 -237 635 N ATOM 2899 CA ALA A 441 170.773 29.420 548.431 1.00 54.60 C ANISOU 2899 CA ALA A 441 8046 7172 5528 -495 -102 494 C ATOM 2900 C ALA A 441 169.407 28.933 548.897 1.00 55.63 C ANISOU 2900 C ALA A 441 8342 7162 5631 -630 208 503 C ATOM 2901 O ALA A 441 168.957 29.288 549.993 1.00 57.16 O ANISOU 2901 O ALA A 441 8689 7369 5659 -697 341 434 O ATOM 2902 CB ALA A 441 170.626 30.595 547.465 1.00 54.37 C ANISOU 2902 CB ALA A 441 7711 7158 5791 -574 -130 367 C ATOM 2903 N LEU A 442 168.733 28.120 548.086 1.00 69.89 N ANISOU 2903 N LEU A 442 10112 8851 7592 -702 349 552 N ATOM 2904 CA LEU A 442 167.420 27.598 548.443 1.00 71.03 C ANISOU 2904 CA LEU A 442 10364 8896 7727 -897 686 495 C ATOM 2905 C LEU A 442 167.493 26.389 549.368 1.00 71.56 C ANISOU 2905 C LEU A 442 10916 8805 7467 -913 855 635 C ATOM 2906 O LEU A 442 166.478 25.711 549.559 1.00 72.38 O ANISOU 2906 O LEU A 442 11167 8784 7548 -1133 1193 587 O ATOM 2907 CB LEU A 442 166.634 27.244 547.179 1.00 70.38 C ANISOU 2907 CB LEU A 442 10016 8791 7932 -1002 781 428 C ATOM 2908 CG LEU A 442 166.334 28.417 546.244 1.00 70.51 C ANISOU 2908 CG LEU A 442 9626 8934 8229 -947 649 288 C ATOM 2909 CD1 LEU A 442 165.493 27.965 545.061 1.00 70.19 C ANISOU 2909 CD1 LEU A 442 9338 8915 8416 -1021 727 200 C ATOM 2910 CD2 LEU A 442 165.644 29.543 547.002 1.00 72.56 C ANISOU 2910 CD2 LEU A 442 9806 9279 8485 -973 747 114 C ATOM 2911 N CYS A 443 168.664 26.105 549.939 1.00108.40 N ANISOU 2911 N CYS A 443 15850 13479 11858 -680 638 784 N ATOM 2912 CA CYS A 443 168.821 25.020 550.894 1.00109.40 C ANISOU 2912 CA CYS A 443 16541 13430 11595 -603 767 942 C ATOM 2913 C CYS A 443 169.454 25.475 552.202 1.00110.73 C ANISOU 2913 C CYS A 443 16949 13717 11408 -430 622 956 C ATOM 2914 O CYS A 443 169.567 24.667 553.130 1.00111.98 O ANISOU 2914 O CYS A 443 17648 13727 11171 -322 722 1092 O ATOM 2915 CB CYS A 443 169.667 23.889 550.289 1.00108.40 C ANISOU 2915 CB CYS A 443 16613 13182 11392 -373 626 1133 C ATOM 2916 SG CYS A 443 169.160 23.382 548.629 1.00106.72 S ANISOU 2916 SG CYS A 443 16090 12870 11588 -546 727 1103 S ATOM 2917 N ASN A 444 169.864 26.735 552.301 1.00 65.56 N ANISOU 2917 N ASN A 444 10882 8241 5785 -403 403 810 N ATOM 2918 CA ASN A 444 170.519 27.269 553.487 1.00 66.87 C ANISOU 2918 CA ASN A 444 11207 8576 5625 -262 237 767 C ATOM 2919 C ASN A 444 169.525 28.105 554.283 1.00 67.98 C ANISOU 2919 C ASN A 444 11355 8717 5759 -506 492 610 C ATOM 2920 O ASN A 444 168.798 28.924 553.711 1.00 67.61 O ANISOU 2920 O ASN A 444 10949 8689 6051 -698 606 458 O ATOM 2921 CB ASN A 444 171.734 28.110 553.095 1.00 66.32 C ANISOU 2921 CB ASN A 444 10757 8793 5650 -114 -150 655 C ATOM 2922 CG ASN A 444 172.442 28.704 554.291 1.00 67.91 C ANISOU 2922 CG ASN A 444 11058 9232 5515 4 -339 545 C ATOM 2923 OD1 ASN A 444 172.156 29.829 554.699 1.00 68.44 O ANISOU 2923 OD1 ASN A 444 10975 9388 5641 -175 -281 362 O ATOM 2924 ND2 ASN A 444 173.377 27.953 554.859 1.00 68.89 N ANISOU 2924 ND2 ASN A 444 11446 9468 5262 335 -575 640 N ATOM 2925 N ALA A 445 169.500 27.898 555.602 1.00 52.36 N ANISOU 2925 N ALA A 445 9807 6717 3368 -463 579 643 N ATOM 2926 CA ALA A 445 168.524 28.585 556.441 1.00 53.52 C ANISOU 2926 CA ALA A 445 10008 6851 3474 -700 866 489 C ATOM 2927 C ALA A 445 168.788 30.084 556.517 1.00 52.18 C ANISOU 2927 C ALA A 445 9462 6906 3458 -735 697 270 C ATOM 2928 O ALA A 445 167.842 30.871 556.629 1.00 51.82 O ANISOU 2928 O ALA A 445 9255 6844 3589 -936 927 100 O ATOM 2929 CB ALA A 445 168.516 27.978 557.843 1.00 57.72 C ANISOU 2929 CB ALA A 445 11158 7293 3477 -637 1002 587 C ATOM 2930 N THR A 446 170.055 30.499 556.460 1.00 52.92 N ANISOU 2930 N THR A 446 9415 7212 3479 -546 320 240 N ATOM 2931 CA THR A 446 170.368 31.920 556.571 1.00 53.10 C ANISOU 2931 CA THR A 446 9145 7414 3615 -631 205 6 C ATOM 2932 C THR A 446 170.049 32.667 555.280 1.00 51.93 C ANISOU 2932 C THR A 446 8580 7208 3943 -751 235 -82 C ATOM 2933 O THR A 446 169.588 33.813 555.323 1.00 52.27 O ANISOU 2933 O THR A 446 8480 7241 4139 -883 344 -262 O ATOM 2934 CB THR A 446 171.838 32.111 556.949 1.00 53.66 C ANISOU 2934 CB THR A 446 9178 7773 3437 -443 -178 -65 C ATOM 2935 OG1 THR A 446 172.166 31.248 558.045 1.00 56.18 O ANISOU 2935 OG1 THR A 446 9933 8147 3267 -228 -254 53 O ATOM 2936 CG2 THR A 446 172.098 33.551 557.363 1.00 54.26 C ANISOU 2936 CG2 THR A 446 9063 8015 3540 -602 -219 -348 C ATOM 2937 N PHE A 447 170.284 32.036 554.126 1.00 51.38 N ANISOU 2937 N PHE A 447 8356 7082 4084 -679 143 44 N ATOM 2938 CA PHE A 447 169.937 32.669 552.857 1.00 50.53 C ANISOU 2938 CA PHE A 447 7913 6903 4383 -759 172 -18 C ATOM 2939 C PHE A 447 168.430 32.845 552.722 1.00 51.09 C ANISOU 2939 C PHE A 447 7939 6833 4640 -881 480 -73 C ATOM 2940 O PHE A 447 167.962 33.851 552.177 1.00 51.38 O ANISOU 2940 O PHE A 447 7768 6839 4917 -915 530 -205 O ATOM 2941 CB PHE A 447 170.484 31.851 551.687 1.00 49.07 C ANISOU 2941 CB PHE A 447 7601 6695 4347 -657 20 128 C ATOM 2942 CG PHE A 447 171.850 32.280 551.228 1.00 48.42 C ANISOU 2942 CG PHE A 447 7330 6782 4287 -590 -264 61 C ATOM 2943 CD1 PHE A 447 172.031 33.500 550.598 1.00 48.34 C ANISOU 2943 CD1 PHE A 447 7101 6774 4493 -709 -275 -98 C ATOM 2944 CD2 PHE A 447 172.947 31.455 551.408 1.00 48.16 C ANISOU 2944 CD2 PHE A 447 7355 6901 4042 -402 -497 136 C ATOM 2945 CE1 PHE A 447 173.284 33.896 550.169 1.00 47.85 C ANISOU 2945 CE1 PHE A 447 6864 6869 4448 -723 -473 -206 C ATOM 2946 CE2 PHE A 447 174.203 31.844 550.979 1.00 47.80 C ANISOU 2946 CE2 PHE A 447 7064 7073 4025 -365 -739 9 C ATOM 2947 CZ PHE A 447 174.371 33.066 550.359 1.00 47.56 C ANISOU 2947 CZ PHE A 447 6798 7047 4225 -566 -706 -174 C ATOM 2948 N LYS A 448 167.653 31.874 553.210 1.00 67.47 N ANISOU 2948 N LYS A 448 10220 8825 6591 -940 704 3 N ATOM 2949 CA LYS A 448 166.199 31.974 553.119 1.00 68.24 C ANISOU 2949 CA LYS A 448 10207 8861 6860 -1082 1018 -120 C ATOM 2950 C LYS A 448 165.672 33.145 553.938 1.00 69.43 C ANISOU 2950 C LYS A 448 10341 9063 6977 -1138 1149 -326 C ATOM 2951 O LYS A 448 164.796 33.888 553.480 1.00 70.02 O ANISOU 2951 O LYS A 448 10163 9145 7296 -1142 1260 -491 O ATOM 2952 CB LYS A 448 165.551 30.669 553.580 1.00 68.55 C ANISOU 2952 CB LYS A 448 10517 8796 6732 -1211 1293 -39 C ATOM 2953 CG LYS A 448 165.813 29.481 552.672 1.00 67.41 C ANISOU 2953 CG LYS A 448 10401 8554 6658 -1182 1243 133 C ATOM 2954 CD LYS A 448 165.181 28.220 553.237 1.00 68.02 C ANISOU 2954 CD LYS A 448 10854 8466 6523 -1354 1583 197 C ATOM 2955 CE LYS A 448 165.432 27.026 552.336 1.00 66.90 C ANISOU 2955 CE LYS A 448 10791 8188 6442 -1336 1565 355 C ATOM 2956 NZ LYS A 448 164.856 27.230 550.979 1.00 66.14 N ANISOU 2956 NZ LYS A 448 10209 8168 6753 -1403 1547 230 N ATOM 2957 N LYS A 449 166.190 33.322 555.156 1.00 59.48 N ANISOU 2957 N LYS A 449 9358 7846 5394 -1148 1127 -332 N ATOM 2958 CA LYS A 449 165.735 34.422 556.002 1.00 60.48 C ANISOU 2958 CA LYS A 449 9505 8011 5463 -1213 1265 -539 C ATOM 2959 C LYS A 449 166.114 35.771 555.405 1.00 60.30 C ANISOU 2959 C LYS A 449 9257 8002 5655 -1145 1107 -668 C ATOM 2960 O LYS A 449 165.346 36.736 555.499 1.00 61.04 O ANISOU 2960 O LYS A 449 9259 8061 5871 -1153 1265 -853 O ATOM 2961 CB LYS A 449 166.314 34.275 557.410 1.00 61.13 C ANISOU 2961 CB LYS A 449 9958 8154 5113 -1231 1246 -518 C ATOM 2962 CG LYS A 449 165.893 35.371 558.377 1.00 62.12 C ANISOU 2962 CG LYS A 449 10145 8319 5141 -1317 1402 -741 C ATOM 2963 CD LYS A 449 166.581 35.215 559.725 1.00 62.96 C ANISOU 2963 CD LYS A 449 10624 8518 4779 -1314 1332 -725 C ATOM 2964 CE LYS A 449 166.150 36.302 560.700 1.00 63.91 C ANISOU 2964 CE LYS A 449 10819 8672 4793 -1422 1506 -964 C ATOM 2965 NZ LYS A 449 166.476 37.669 560.202 1.00 63.62 N ANISOU 2965 NZ LYS A 449 10524 8651 4998 -1417 1387 -1149 N ATOM 2966 N THR A 450 167.292 35.859 554.783 1.00 54.05 N ANISOU 2966 N THR A 450 8398 7245 4894 -1078 821 -591 N ATOM 2967 CA THR A 450 167.710 37.118 554.176 1.00 53.96 C ANISOU 2967 CA THR A 450 8249 7195 5060 -1067 726 -719 C ATOM 2968 C THR A 450 166.922 37.403 552.904 1.00 53.94 C ANISOU 2968 C THR A 450 8036 7064 5395 -976 789 -718 C ATOM 2969 O THR A 450 166.609 38.562 552.608 1.00 54.48 O ANISOU 2969 O THR A 450 8081 7027 5590 -928 853 -854 O ATOM 2970 CB THR A 450 169.210 37.093 553.884 1.00 53.20 C ANISOU 2970 CB THR A 450 8120 7205 4889 -1072 444 -686 C ATOM 2971 OG1 THR A 450 169.904 36.506 554.992 1.00 53.52 O ANISOU 2971 OG1 THR A 450 8331 7425 4579 -1067 329 -665 O ATOM 2972 CG2 THR A 450 169.729 38.505 553.672 1.00 53.45 C ANISOU 2972 CG2 THR A 450 8121 7190 4997 -1165 429 -885 C ATOM 2973 N PHE A 451 166.595 36.358 552.136 1.00 52.58 N ANISOU 2973 N PHE A 451 7741 6893 5344 -929 771 -574 N ATOM 2974 CA PHE A 451 165.759 36.545 550.954 1.00 52.92 C ANISOU 2974 CA PHE A 451 7566 6870 5671 -816 812 -598 C ATOM 2975 C PHE A 451 164.391 37.094 551.336 1.00 54.24 C ANISOU 2975 C PHE A 451 7657 7049 5905 -767 1046 -791 C ATOM 2976 O PHE A 451 163.872 38.004 550.678 1.00 54.90 O ANISOU 2976 O PHE A 451 7637 7070 6153 -594 1050 -899 O ATOM 2977 CB PHE A 451 165.607 35.226 550.195 1.00 52.26 C ANISOU 2977 CB PHE A 451 7366 6815 5674 -818 776 -448 C ATOM 2978 CG PHE A 451 166.853 34.782 549.481 1.00 50.86 C ANISOU 2978 CG PHE A 451 7198 6626 5501 -797 537 -282 C ATOM 2979 CD1 PHE A 451 167.941 35.628 549.354 1.00 50.39 C ANISOU 2979 CD1 PHE A 451 7179 6552 5415 -795 380 -309 C ATOM 2980 CD2 PHE A 451 166.929 33.514 548.927 1.00 49.86 C ANISOU 2980 CD2 PHE A 451 7036 6504 5404 -801 500 -133 C ATOM 2981 CE1 PHE A 451 169.084 35.214 548.695 1.00 49.05 C ANISOU 2981 CE1 PHE A 451 6967 6416 5255 -790 182 -206 C ATOM 2982 CE2 PHE A 451 168.068 33.097 548.266 1.00 48.30 C ANISOU 2982 CE2 PHE A 451 6829 6310 5213 -756 288 -2 C ATOM 2983 CZ PHE A 451 169.147 33.948 548.150 1.00 47.96 C ANISOU 2983 CZ PHE A 451 6777 6295 5150 -746 125 -47 C ATOM 2984 N LYS A 452 163.791 36.549 552.397 1.00 72.85 N ANISOU 2984 N LYS A 452 10087 9482 8111 -895 1253 -849 N ATOM 2985 CA LYS A 452 162.506 37.054 552.869 1.00 74.13 C ANISOU 2985 CA LYS A 452 10142 9699 8323 -871 1506 -1083 C ATOM 2986 C LYS A 452 162.609 38.513 553.292 1.00 74.71 C ANISOU 2986 C LYS A 452 10325 9693 8370 -768 1513 -1228 C ATOM 2987 O LYS A 452 161.697 39.309 553.037 1.00 75.74 O ANISOU 2987 O LYS A 452 10316 9821 8641 -585 1611 -1413 O ATOM 2988 CB LYS A 452 162.004 36.195 554.031 1.00 74.47 C ANISOU 2988 CB LYS A 452 10319 9814 8161 -1092 1769 -1120 C ATOM 2989 CG LYS A 452 160.712 36.688 554.660 1.00 75.84 C ANISOU 2989 CG LYS A 452 10369 10082 8365 -1112 2074 -1406 C ATOM 2990 CD LYS A 452 160.561 36.177 556.085 1.00 76.24 C ANISOU 2990 CD LYS A 452 10706 10145 8116 -1358 2340 -1435 C ATOM 2991 CE LYS A 452 161.669 36.716 556.980 1.00 75.87 C ANISOU 2991 CE LYS A 452 11008 10022 7798 -1362 2195 -1338 C ATOM 2992 NZ LYS A 452 161.521 36.271 558.395 1.00 76.49 N ANISOU 2992 NZ LYS A 452 11420 10111 7532 -1561 2438 -1362 N ATOM 2993 N HIS A 453 163.717 38.885 553.935 1.00 53.64 N ANISOU 2993 N HIS A 453 7907 6968 5507 -869 1411 -1173 N ATOM 2994 CA HIS A 453 163.880 40.261 554.393 1.00 54.21 C ANISOU 2994 CA HIS A 453 8129 6938 5529 -834 1455 -1336 C ATOM 2995 C HIS A 453 164.110 41.211 553.224 1.00 54.19 C ANISOU 2995 C HIS A 453 8110 6760 5721 -654 1343 -1343 C ATOM 2996 O HIS A 453 163.636 42.353 553.243 1.00 55.12 O ANISOU 2996 O HIS A 453 8319 6740 5884 -509 1454 -1502 O ATOM 2997 CB HIS A 453 165.031 40.342 555.396 1.00 53.79 C ANISOU 2997 CB HIS A 453 8317 6926 5196 -1026 1372 -1325 C ATOM 2998 CG HIS A 453 165.274 41.720 555.927 1.00 54.43 C ANISOU 2998 CG HIS A 453 8576 6901 5203 -1061 1443 -1525 C ATOM 2999 ND1 HIS A 453 166.503 42.339 555.855 1.00 54.02 N ANISOU 2999 ND1 HIS A 453 8642 6809 5076 -1180 1299 -1564 N ATOM 3000 CD2 HIS A 453 164.444 42.601 556.533 1.00 55.56 C ANISOU 3000 CD2 HIS A 453 8805 6969 5335 -1009 1670 -1728 C ATOM 3001 CE1 HIS A 453 166.421 43.541 556.397 1.00 54.90 C ANISOU 3001 CE1 HIS A 453 8938 6797 5126 -1228 1447 -1777 C ATOM 3002 NE2 HIS A 453 165.182 43.724 556.817 1.00 55.79 N ANISOU 3002 NE2 HIS A 453 9048 6875 5275 -1100 1664 -1866 N ATOM 3003 N LEU A 454 164.831 40.759 552.194 1.00 50.32 N ANISOU 3003 N LEU A 454 7551 6247 5323 -648 1143 -1171 N ATOM 3004 CA LEU A 454 165.076 41.600 551.028 1.00 50.27 C ANISOU 3004 CA LEU A 454 7596 6043 5464 -494 1064 -1159 C ATOM 3005 C LEU A 454 163.817 41.834 550.204 1.00 51.25 C ANISOU 3005 C LEU A 454 7571 6131 5769 -171 1113 -1211 C ATOM 3006 O LEU A 454 163.742 42.833 549.480 1.00 51.69 O ANISOU 3006 O LEU A 454 7780 5975 5885 43 1106 -1246 O ATOM 3007 CB LEU A 454 166.157 40.977 550.142 1.00 48.98 C ANISOU 3007 CB LEU A 454 7381 5888 5341 -586 858 -978 C ATOM 3008 CG LEU A 454 167.598 40.997 550.652 1.00 48.17 C ANISOU 3008 CG LEU A 454 7388 5840 5073 -842 758 -982 C ATOM 3009 CD1 LEU A 454 168.514 40.289 549.668 1.00 46.95 C ANISOU 3009 CD1 LEU A 454 7116 5732 4989 -882 568 -829 C ATOM 3010 CD2 LEU A 454 168.063 42.425 550.884 1.00 48.67 C ANISOU 3010 CD2 LEU A 454 7699 5720 5075 -940 860 -1164 C ATOM 3011 N LEU A 455 162.827 40.946 550.298 1.00 52.46 N ANISOU 3011 N LEU A 455 7451 6495 5988 -127 1172 -1242 N ATOM 3012 CA LEU A 455 161.632 41.047 549.473 1.00 53.54 C ANISOU 3012 CA LEU A 455 7347 6703 6290 189 1180 -1346 C ATOM 3013 C LEU A 455 160.445 41.675 550.188 1.00 55.12 C ANISOU 3013 C LEU A 455 7466 6989 6489 360 1380 -1613 C ATOM 3014 O LEU A 455 159.501 42.105 549.517 1.00 56.36 O ANISOU 3014 O LEU A 455 7452 7205 6759 723 1360 -1753 O ATOM 3015 CB LEU A 455 161.228 39.661 548.957 1.00 53.16 C ANISOU 3015 CB LEU A 455 6982 6877 6340 108 1136 -1285 C ATOM 3016 CG LEU A 455 162.252 38.954 548.067 1.00 51.82 C ANISOU 3016 CG LEU A 455 6846 6643 6199 4 935 -1039 C ATOM 3017 CD1 LEU A 455 161.775 37.557 547.700 1.00 51.60 C ANISOU 3017 CD1 LEU A 455 6549 6809 6247 -107 947 -1009 C ATOM 3018 CD2 LEU A 455 162.536 39.774 546.819 1.00 51.75 C ANISOU 3018 CD2 LEU A 455 6934 6457 6271 267 774 -980 C ATOM 3019 N MET A 456 160.460 41.736 551.517 1.00 79.29 N ANISOU 3019 N MET A 456 10638 10081 9407 141 1563 -1704 N ATOM 3020 CA MET A 456 159.342 42.326 552.238 1.00 80.84 C ANISOU 3020 CA MET A 456 10749 10368 9599 289 1783 -1982 C ATOM 3021 C MET A 456 159.358 43.845 552.098 1.00 81.87 C ANISOU 3021 C MET A 456 11149 10242 9718 598 1784 -2074 C ATOM 3022 O MET A 456 160.409 44.466 551.915 1.00 81.16 O ANISOU 3022 O MET A 456 11403 9878 9555 532 1699 -1943 O ATOM 3023 CB MET A 456 159.378 41.933 553.716 1.00 80.66 C ANISOU 3023 CB MET A 456 10822 10432 9391 -53 2000 -2047 C ATOM 3024 CG MET A 456 160.503 42.571 554.516 1.00 79.99 C ANISOU 3024 CG MET A 456 11135 10151 9105 -235 1981 -1975 C ATOM 3025 SD MET A 456 160.322 42.309 556.292 1.00 80.24 S ANISOU 3025 SD MET A 456 11314 10301 8874 -538 2246 -2104 S ATOM 3026 CE MET A 456 158.730 43.075 556.590 1.00 82.28 C ANISOU 3026 CE MET A 456 11371 10647 9243 -281 2529 -2460 C ATOM 3027 N CYS A 457 158.171 44.441 552.182 1.00101.97 N ANISOU 3027 N CYS A 457 13544 12877 12324 937 1905 -2331 N ATOM 3028 CA CYS A 457 158.009 45.883 552.032 1.00103.46 C ANISOU 3028 CA CYS A 457 14031 12794 12485 1320 1933 -2437 C ATOM 3029 C CYS A 457 158.175 46.544 553.396 1.00103.78 C ANISOU 3029 C CYS A 457 14343 12720 12371 1122 2167 -2574 C ATOM 3030 O CYS A 457 157.342 46.360 554.289 1.00104.63 O ANISOU 3030 O CYS A 457 14240 13053 12460 1081 2368 -2795 O ATOM 3031 CB CYS A 457 156.647 46.211 551.425 1.00105.66 C ANISOU 3031 CB CYS A 457 14007 13257 12882 1875 1914 -2670 C ATOM 3032 SG CYS A 457 156.352 45.476 549.798 1.00105.40 S ANISOU 3032 SG CYS A 457 13633 13414 13000 2147 1618 -2563 S ATOM 3033 N HIS A 458 159.249 47.311 553.556 1.00 79.34 N ANISOU 3033 N HIS A 458 11706 9284 9154 969 2164 -2475 N ATOM 3034 CA HIS A 458 159.503 48.026 554.803 1.00 79.70 C ANISOU 3034 CA HIS A 458 12046 9205 9032 766 2375 -2625 C ATOM 3035 C HIS A 458 158.590 49.241 554.934 1.00 81.99 C ANISOU 3035 C HIS A 458 12502 9324 9327 1205 2548 -2869 C ATOM 3036 O HIS A 458 158.120 49.788 553.937 1.00 83.24 O ANISOU 3036 O HIS A 458 12716 9338 9574 1686 2465 -2870 O ATOM 3037 CB HIS A 458 160.970 48.459 554.888 1.00 78.50 C ANISOU 3037 CB HIS A 458 12293 8786 8747 424 2325 -2504 C ATOM 3038 CG HIS A 458 161.905 47.359 555.289 1.00 76.63 C ANISOU 3038 CG HIS A 458 11920 8770 8425 -22 2198 -2351 C ATOM 3039 ND1 HIS A 458 162.036 46.192 554.568 1.00 75.48 N ANISOU 3039 ND1 HIS A 458 11482 8814 8383 -54 2005 -2147 N ATOM 3040 CD2 HIS A 458 162.755 47.252 556.337 1.00 75.93 C ANISOU 3040 CD2 HIS A 458 11968 8751 8131 -410 2224 -2384 C ATOM 3041 CE1 HIS A 458 162.927 45.413 555.155 1.00 74.20 C ANISOU 3041 CE1 HIS A 458 11307 8804 8082 -411 1922 -2046 C ATOM 3042 NE2 HIS A 458 163.379 46.032 556.230 1.00 74.50 N ANISOU 3042 NE2 HIS A 458 11588 8794 7922 -616 2034 -2190 N TER 3043 HIS A 458 HETATM 3044 C10 3C0 A 501 185.728 24.189 526.979 1.00 39.51 C HETATM 3045 C13 3C0 A 501 181.593 26.645 526.135 1.00 39.51 C HETATM 3046 C15 3C0 A 501 181.087 29.107 525.572 1.00 39.51 C HETATM 3047 C17 3C0 A 501 182.542 29.105 527.490 1.00 39.51 C HETATM 3048 C20 3C0 A 501 180.001 30.709 527.113 1.00 39.51 C HETATM 3049 C21 3C0 A 501 178.906 28.738 526.614 1.00 39.51 C HETATM 3050 C22 3C0 A 501 181.105 28.586 527.755 1.00 39.51 C HETATM 3051 N19 3C0 A 501 180.260 29.296 526.774 1.00 39.51 N HETATM 3052 C14 3C0 A 501 181.042 27.638 525.091 1.00 39.51 C HETATM 3053 C16 3C0 A 501 182.529 29.466 526.027 1.00 39.51 C HETATM 3054 O18 3C0 A 501 182.776 30.480 527.053 1.00 39.51 O HETATM 3055 C23 3C0 A 501 181.087 27.061 527.537 1.00 39.51 C HETATM 3056 O12 3C0 A 501 183.037 26.539 526.031 1.00 39.51 O HETATM 3057 C02 3C0 A 501 183.613 25.522 526.725 1.00 39.51 C HETATM 3058 O01 3C0 A 501 183.001 24.610 527.281 1.00 39.51 O HETATM 3059 C03 3C0 A 501 185.143 25.582 526.741 1.00 39.51 C HETATM 3060 O11 3C0 A 501 185.358 23.332 525.895 1.00 39.51 O HETATM 3061 C04 3C0 A 501 185.565 26.466 527.731 1.00 39.51 C HETATM 3062 C05 3C0 A 501 186.071 27.710 527.372 1.00 39.51 C HETATM 3063 C06 3C0 A 501 186.492 28.600 528.352 1.00 39.51 C HETATM 3064 C07 3C0 A 501 186.408 28.247 529.693 1.00 39.51 C HETATM 3065 C08 3C0 A 501 185.901 27.003 530.054 1.00 39.51 C HETATM 3066 C09 3C0 A 501 185.479 26.112 529.073 1.00 39.51 C HETATM 3067 HG HG A 502 179.240 41.022 538.717 0.49 71.50 HG ANISOU 3067 HG HG A 502 7177 8901 11087 -343 437 760 HG HETATM 3068 HG HG A 503 182.843 38.949 537.927 0.28 89.49 HG ANISOU 3068 HG HG A 503 15291 9264 9446 -1724 -3018 4738 HG HETATM 3069 HG HG A 504 170.872 23.320 541.454 0.69 57.71 HG ANISOU 3069 HG HG A 504 11739 5317 4872 -485 1718 -378 HG HETATM 3070 O HOH A 601 180.378 33.127 523.282 1.00 39.51 O HETATM 3071 O HOH A 602 179.125 26.952 537.940 1.00 39.51 O HETATM 3072 O HOH A 603 178.870 11.620 548.251 1.00 39.51 O HETATM 3073 O HOH A 604 177.296 29.331 532.586 1.00 39.51 O HETATM 3074 O HOH A 605 178.004 24.914 539.133 1.00 39.51 O HETATM 3075 O HOH A 606 195.215 35.303 525.610 1.00 39.51 O HETATM 3076 O HOH A 607 188.791 38.045 514.585 1.00 39.51 O HETATM 3077 O HOH A 608 175.405 31.290 541.433 1.00 39.51 O HETATM 3078 O HOH A 609 179.905 20.978 513.450 1.00 39.51 O HETATM 3079 O HOH A 610 194.361 12.918 550.497 1.00 39.51 O HETATM 3080 O HOH A 611 194.585 20.035 512.428 1.00 39.51 O HETATM 3081 O HOH A 612 186.157 20.559 517.443 1.00 39.51 O HETATM 3082 O HOH A 613 191.423 41.622 507.738 1.00 39.51 O HETATM 3083 O HOH A 614 185.347 25.157 550.049 1.00 39.51 O HETATM 3084 O HOH A 615 176.054 21.787 526.814 1.00 39.51 O HETATM 3085 O HOH A 616 176.572 34.360 511.486 1.00 39.51 O HETATM 3086 O HOH A 617 156.108 24.890 569.803 1.00 39.51 O HETATM 3087 O HOH A 618 191.130 38.123 516.973 1.00 39.51 O HETATM 3088 O HOH A 619 169.345 32.508 539.291 1.00 39.51 O HETATM 3089 O HOH A 620 186.374 24.755 523.537 1.00 39.51 O HETATM 3090 O HOH A 621 187.079 36.985 516.593 1.00 39.51 O HETATM 3091 O HOH A 622 181.583 43.575 539.223 1.00 39.51 O CONECT 406 3067 3068 CONECT 632 1278 CONECT 1278 632 CONECT 2682 2700 CONECT 2700 2682 CONECT 2855 3069 CONECT 2885 3069 CONECT 3044 3059 3060 CONECT 3045 3052 3055 3056 CONECT 3046 3051 3052 3053 CONECT 3047 3050 3053 3054 CONECT 3048 3051 CONECT 3049 3051 CONECT 3050 3047 3051 3055 CONECT 3051 3046 3048 3049 3050 CONECT 3052 3045 3046 CONECT 3053 3046 3047 3054 CONECT 3054 3047 3053 CONECT 3055 3045 3050 CONECT 3056 3045 3057 CONECT 3057 3056 3058 3059 CONECT 3058 3057 CONECT 3059 3044 3057 3061 CONECT 3060 3044 CONECT 3061 3059 3062 3066 CONECT 3062 3061 3063 CONECT 3063 3062 3064 CONECT 3064 3063 3065 CONECT 3065 3064 3066 CONECT 3066 3061 3065 CONECT 3067 406 CONECT 3068 406 CONECT 3069 2855 2885 MASTER 437 0 4 19 0 0 0 6 3090 1 33 33 END