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*** Eutla_projet_1 ***elNémo ID: 23010419095965391Job options:ID = 23010419095965391 JOBID = Eutla_projet_1 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER Eutla_projet_1 HEADER TRANSFERASE 09-APR-19 6OID TITLE REDOX REGULATION OF FN3K FROM ARABIDOPSIS THALIANA COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN-RIBULOSAMINE 3-KINASE, CHLOROPLASTIC; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: FRUCTOSAMINE 3-KINASE-RELATED PROTEIN,ATFN3K-RP; COMPND 5 EC: 2.7.1.172; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: AT3G61080, T27I15_170; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS KINASE, FRUCTOSAMINE-3-KINASE, SMALL MOLECULE KINASE, PROTEIN REPAIR, KEYWDS 2 PHOSPHOTRANSFERASE, DEGLYCATION, PLANT PROTEIN, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR Z.A.WOOD,R.KADIRVELRAJ,S.SHRESTHA REVDAT 2 23-SEP-20 6OID 1 JRNL REVDAT 1 20-MAY-20 6OID 0 JRNL AUTH S.SHRESTHA,S.KATIYAR,C.E.SANZ-RODRIGUEZ,N.R.KEMPPINEN, JRNL AUTH 2 H.W.KIM,R.KADIRVELRAJ,C.PANAGOS,N.KEYHANINEJAD,M.COLONNA, JRNL AUTH 3 P.CHOPRA,D.P.BYRNE,G.J.BOONS,E.VAN DER KNAAP,P.A.EYERS, JRNL AUTH 4 A.S.EDISON,Z.A.WOOD,N.KANNAN JRNL TITL A REDOX-ACTIVE SWITCH IN FRUCTOSAMINE-3-KINASES EXPANDS THE JRNL TITL 2 REGULATORY REPERTOIRE OF THE PROTEIN KINASE SUPERFAMILY. JRNL REF SCI.SIGNAL. V. 13 2020 JRNL REFN ESSN 1937-9145 JRNL PMID 32636308 JRNL DOI 10.1126/SCISIGNAL.AAX6313 REMARK 2 REMARK 2 RESOLUTION. 2.37 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.12_2829: ???) 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) : 2.37 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 37988 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.177 REMARK 3 R VALUE (WORKING SET) : 0.175 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1903 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 53.5177 - 5.6984 1.00 2737 146 0.1755 0.2120 REMARK 3 2 5.6984 - 4.5238 1.00 2631 134 0.1411 0.1555 REMARK 3 3 4.5238 - 3.9521 1.00 2605 136 0.1323 0.1441 REMARK 3 4 3.9521 - 3.5909 1.00 2609 143 0.1498 0.1748 REMARK 3 5 3.5909 - 3.3335 1.00 2579 135 0.1813 0.2273 REMARK 3 6 3.3335 - 3.1370 1.00 2573 133 0.1927 0.2204 REMARK 3 7 3.1370 - 2.9799 1.00 2555 138 0.2118 0.2365 REMARK 3 8 2.9799 - 2.8502 1.00 2553 138 0.2131 0.2710 REMARK 3 9 2.8502 - 2.7405 1.00 2583 127 0.2280 0.2610 REMARK 3 10 2.7405 - 2.6459 1.00 2551 136 0.2230 0.2757 REMARK 3 11 2.6459 - 2.5632 1.00 2558 138 0.2286 0.2572 REMARK 3 12 2.5632 - 2.4899 1.00 2548 135 0.2393 0.2691 REMARK 3 13 2.4899 - 2.4244 1.00 2546 134 0.2479 0.3004 REMARK 3 14 2.4244 - 2.3652 0.97 2457 130 0.2841 0.3296 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) : 0.280 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.210 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 4850 REMARK 3 ANGLE : 1.071 6567 REMARK 3 CHIRALITY : 0.068 650 REMARK 3 PLANARITY : 0.006 834 REMARK 3 DIHEDRAL : 15.996 1741 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.9317 7.0554 35.1953 REMARK 3 T TENSOR REMARK 3 T11: 0.8351 T22: 0.4531 REMARK 3 T33: 0.6129 T12: 0.2789 REMARK 3 T13: 0.2529 T23: 0.2477 REMARK 3 L TENSOR REMARK 3 L11: 0.3761 L22: 1.5675 REMARK 3 L33: 2.3304 L12: -0.0719 REMARK 3 L13: 0.2772 L23: -1.1911 REMARK 3 S TENSOR REMARK 3 S11: -0.4057 S12: -0.4546 S13: -0.6742 REMARK 3 S21: 0.4298 S22: 0.1249 S23: -0.0578 REMARK 3 S31: 0.6753 S32: 0.6338 S33: 0.1822 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 44 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.3595 20.1511 9.0246 REMARK 3 T TENSOR REMARK 3 T11: 0.4097 T22: 0.4611 REMARK 3 T33: 0.3487 T12: -0.0217 REMARK 3 T13: 0.0134 T23: 0.0335 REMARK 3 L TENSOR REMARK 3 L11: 4.1818 L22: 3.0098 REMARK 3 L33: 2.9782 L12: 0.2337 REMARK 3 L13: 0.3545 L23: 0.5394 REMARK 3 S TENSOR REMARK 3 S11: 0.1371 S12: 0.1105 S13: -0.1260 REMARK 3 S21: -0.1320 S22: -0.1104 S23: -0.2539 REMARK 3 S31: -0.0023 S32: -0.0227 S33: -0.0472 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.3738 21.9564 7.9324 REMARK 3 T TENSOR REMARK 3 T11: 0.4471 T22: 0.4889 REMARK 3 T33: 0.4529 T12: 0.0154 REMARK 3 T13: -0.0789 T23: 0.0449 REMARK 3 L TENSOR REMARK 3 L11: 2.5838 L22: 3.2915 REMARK 3 L33: 1.9710 L12: 0.2843 REMARK 3 L13: -0.1292 L23: -0.0359 REMARK 3 S TENSOR REMARK 3 S11: -0.0382 S12: 0.4696 S13: 0.0235 REMARK 3 S21: -0.6829 S22: 0.1268 S23: 0.1613 REMARK 3 S31: 0.2151 S32: -0.1321 S33: 0.0046 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 295 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.5914 23.1197 19.5088 REMARK 3 T TENSOR REMARK 3 T11: 0.3966 T22: 0.3580 REMARK 3 T33: 0.4446 T12: 0.0535 REMARK 3 T13: -0.0112 T23: 0.0723 REMARK 3 L TENSOR REMARK 3 L11: 2.3892 L22: 2.0550 REMARK 3 L33: 2.0557 L12: -0.2604 REMARK 3 L13: -0.2250 L23: -0.5700 REMARK 3 S TENSOR REMARK 3 S11: -0.0131 S12: -0.0743 S13: -0.0544 REMARK 3 S21: 0.1087 S22: 0.1983 S23: 0.3896 REMARK 3 S31: 0.1210 S32: -0.2211 S33: -0.0034 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.7300 12.3302 17.8642 REMARK 3 T TENSOR REMARK 3 T11: 0.4808 T22: 0.4392 REMARK 3 T33: 0.5884 T12: 0.0793 REMARK 3 T13: 0.0833 T23: 0.0219 REMARK 3 L TENSOR REMARK 3 L11: 1.9463 L22: 1.2177 REMARK 3 L33: 1.7715 L12: 0.5689 REMARK 3 L13: -1.1143 L23: -0.3077 REMARK 3 S TENSOR REMARK 3 S11: -0.2913 S12: 0.1910 S13: -0.6194 REMARK 3 S21: 0.0273 S22: -0.0469 S23: -0.1306 REMARK 3 S31: 0.2664 S32: 0.3423 S33: 0.0791 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.7016 14.6744 45.1455 REMARK 3 T TENSOR REMARK 3 T11: 0.6534 T22: 0.5165 REMARK 3 T33: 0.4103 T12: 0.1881 REMARK 3 T13: 0.0636 T23: 0.1341 REMARK 3 L TENSOR REMARK 3 L11: 3.2127 L22: 2.6985 REMARK 3 L33: 2.6185 L12: -0.3181 REMARK 3 L13: -0.1885 L23: 0.6953 REMARK 3 S TENSOR REMARK 3 S11: -0.4857 S12: -0.8347 S13: -0.1388 REMARK 3 S21: 0.4800 S22: 0.2499 S23: 0.0479 REMARK 3 S31: 0.4049 S32: 0.2247 S33: -0.0149 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 107 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.2788 31.4117 47.1904 REMARK 3 T TENSOR REMARK 3 T11: 0.6403 T22: 0.7424 REMARK 3 T33: 0.4932 T12: 0.1505 REMARK 3 T13: -0.0119 T23: -0.0967 REMARK 3 L TENSOR REMARK 3 L11: 3.4413 L22: 1.6750 REMARK 3 L33: 1.9948 L12: -0.1870 REMARK 3 L13: -0.7576 L23: 0.3383 REMARK 3 S TENSOR REMARK 3 S11: -0.2038 S12: -1.0533 S13: -0.0117 REMARK 3 S21: 0.3568 S22: 0.2444 S23: -0.0261 REMARK 3 S31: 0.2416 S32: 0.6140 S33: -0.1262 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 295 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.7677 37.1309 36.0376 REMARK 3 T TENSOR REMARK 3 T11: 0.3804 T22: 0.4581 REMARK 3 T33: 0.4160 T12: 0.0788 REMARK 3 T13: 0.0066 T23: -0.0832 REMARK 3 L TENSOR REMARK 3 L11: 2.6323 L22: 1.8968 REMARK 3 L33: 2.5005 L12: -0.1357 REMARK 3 L13: -1.0298 L23: -0.3515 REMARK 3 S TENSOR REMARK 3 S11: 0.0752 S12: -0.3201 S13: 0.4466 REMARK 3 S21: 0.0164 S22: 0.0913 S23: 0.0179 REMARK 3 S31: -0.0580 S32: 0.4223 S33: -0.1727 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 6OID COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-19. REMARK 100 THE DEPOSITION ID IS D_1000239627. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-NOV-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID 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 : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38000 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350 REMARK 200 RESOLUTION RANGE LOW (A) : 53.504 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 14.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1 REMARK 200 DATA REDUNDANCY IN SHELL : 14.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3F7W, 3JR1, AND 5IGS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M MES PH REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.36000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.36000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 79.43000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 81.82000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 79.43000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 81.82000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 35.36000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 79.43000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.82000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 35.36000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 79.43000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 81.82000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 11070 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24690 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -226.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 SER A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 HIS A -10 REMARK 465 SER A -9 REMARK 465 SER A -8 REMARK 465 GLY A -7 REMARK 465 LEU A -6 REMARK 465 VAL A -5 REMARK 465 PRO A -4 REMARK 465 ARG A -3 REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 MET A 4 REMARK 465 SER A 5 REMARK 465 GLU A 6 REMARK 465 LYS A 296 REMARK 465 ALA A 297 REMARK 465 MET B -19 REMARK 465 GLY B -18 REMARK 465 SER B -17 REMARK 465 SER B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 HIS B -10 REMARK 465 SER B -9 REMARK 465 SER B -8 REMARK 465 GLY B -7 REMARK 465 LEU B -6 REMARK 465 VAL B -5 REMARK 465 PRO B -4 REMARK 465 ARG B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 HIS B 0 REMARK 465 MET B 1 REMARK 465 ALA B 2 REMARK 465 ALA B 3 REMARK 465 MET B 4 REMARK 465 SER B 5 REMARK 465 GLU B 6 REMARK 465 LYS B 296 REMARK 465 ALA B 297 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 15 -72.68 -78.64 REMARK 500 THR A 74 -72.41 -122.96 REMARK 500 ASN A 133 -151.10 -135.78 REMARK 500 ARG A 156 -77.61 -118.42 REMARK 500 ASP A 201 57.81 -155.74 REMARK 500 THR B 15 -80.75 -94.60 REMARK 500 THR B 74 -79.16 -119.89 REMARK 500 ASN B 106 90.22 -164.43 REMARK 500 ASN B 133 -151.61 -136.84 REMARK 500 ARG B 156 -75.25 -114.88 REMARK 500 ASP B 201 58.74 -156.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 307 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 308 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 309 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 310 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 311 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 312 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 313 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 314 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 315 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 316 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 306 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 307 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 308 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 309 DBREF 6OID A 1 297 UNP Q9LEW8 FN3KR_ARATH 30 326 DBREF 6OID B 1 297 UNP Q9LEW8 FN3KR_ARATH 30 326 SEQADV 6OID MET A -19 UNP Q9LEW8 INITIATING METHIONINE SEQADV 6OID GLY A -18 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER A -17 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER A -16 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS A -15 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS A -14 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS A -13 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS A -12 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS A -11 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS A -10 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER A -9 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER A -8 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID GLY A -7 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID LEU A -6 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID VAL A -5 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID PRO A -4 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID ARG A -3 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID GLY A -2 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER A -1 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS A 0 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID MET B -19 UNP Q9LEW8 INITIATING METHIONINE SEQADV 6OID GLY B -18 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER B -17 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER B -16 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS B -15 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS B -14 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS B -13 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS B -12 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS B -11 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS B -10 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER B -9 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER B -8 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID GLY B -7 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID LEU B -6 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID VAL B -5 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID PRO B -4 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID ARG B -3 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID GLY B -2 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID SER B -1 UNP Q9LEW8 EXPRESSION TAG SEQADV 6OID HIS B 0 UNP Q9LEW8 EXPRESSION TAG SEQRES 1 A 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 317 LEU VAL PRO ARG GLY SER HIS MET ALA ALA MET SER GLU SEQRES 3 A 317 ASP PRO ILE ARG GLU TRP ILE LEU THR GLU GLY LYS ALA SEQRES 4 A 317 THR GLN ILE THR LYS ILE GLY SER VAL GLY GLY GLY CYS SEQRES 5 A 317 ILE ASN LEU ALA SER HIS TYR GLN THR ASP ALA GLY SER SEQRES 6 A 317 PHE PHE VAL LYS THR ASN ARG SER ILE GLY PRO ALA MET SEQRES 7 A 317 PHE GLU GLY GLU ALA LEU GLY LEU GLU ALA MET TYR GLU SEQRES 8 A 317 THR ARG THR ILE ARG VAL PRO ASN PRO HIS LYS ALA GLY SEQRES 9 A 317 GLU LEU PRO THR GLY GLY SER TYR ILE ILE MET GLU PHE SEQRES 10 A 317 ILE ASP PHE GLY GLY SER ARG GLY ASN GLN ALA GLU LEU SEQRES 11 A 317 GLY ARG LYS LEU ALA GLU MET HIS LYS ALA GLY LYS THR SEQRES 12 A 317 SER LYS GLY PHE GLY PHE GLU VAL ASP ASN THR ILE GLY SEQRES 13 A 317 SER THR PRO GLN ILE ASN THR TRP SER SER ASP TRP ILE SEQRES 14 A 317 GLU PHE TYR GLY GLU LYS ARG LEU GLY TYR GLN LEU LYS SEQRES 15 A 317 LEU ALA ARG ASP GLN TYR GLY ASP SER ALA ILE TYR GLN SEQRES 16 A 317 LYS GLY HIS THR LEU ILE GLN ASN MET ALA PRO LEU PHE SEQRES 17 A 317 GLU ASN VAL VAL ILE GLU PRO CYS LEU LEU HIS GLY ASP SEQRES 18 A 317 LEU TRP SER GLY ASN ILE ALA TYR ASP LYS ASN ASN GLU SEQRES 19 A 317 PRO VAL ILE LEU ASP PRO ALA CYS TYR TYR GLY HIS ASN SEQRES 20 A 317 GLU ALA ASP PHE GLY MET SER TRP CYS ALA GLY PHE GLY SEQRES 21 A 317 GLU SER PHE TYR ASN ALA TYR PHE LYS VAL MET PRO LYS SEQRES 22 A 317 GLN ALA GLY TYR GLU LYS ARG ARG ASP LEU TYR LEU LEU SEQRES 23 A 317 TYR HIS TYR LEU ASN HIS TYR ASN LEU PHE GLY SER GLY SEQRES 24 A 317 TYR ARG SER SER ALA MET SER ILE ILE ASP ASP TYR LEU SEQRES 25 A 317 ARG MET LEU LYS ALA SEQRES 1 B 317 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 B 317 LEU VAL PRO ARG GLY SER HIS MET ALA ALA MET SER GLU SEQRES 3 B 317 ASP PRO ILE ARG GLU TRP ILE LEU THR GLU GLY LYS ALA SEQRES 4 B 317 THR GLN ILE THR LYS ILE GLY SER VAL GLY GLY GLY CYS SEQRES 5 B 317 ILE ASN LEU ALA SER HIS TYR GLN THR ASP ALA GLY SER SEQRES 6 B 317 PHE PHE VAL LYS THR ASN ARG SER ILE GLY PRO ALA MET SEQRES 7 B 317 PHE GLU GLY GLU ALA LEU GLY LEU GLU ALA MET TYR GLU SEQRES 8 B 317 THR ARG THR ILE ARG VAL PRO ASN PRO HIS LYS ALA GLY SEQRES 9 B 317 GLU LEU PRO THR GLY GLY SER TYR ILE ILE MET GLU PHE SEQRES 10 B 317 ILE ASP PHE GLY GLY SER ARG GLY ASN GLN ALA GLU LEU SEQRES 11 B 317 GLY ARG LYS LEU ALA GLU MET HIS LYS ALA GLY LYS THR SEQRES 12 B 317 SER LYS GLY PHE GLY PHE GLU VAL ASP ASN THR ILE GLY SEQRES 13 B 317 SER THR PRO GLN ILE ASN THR TRP SER SER ASP TRP ILE SEQRES 14 B 317 GLU PHE TYR GLY GLU LYS ARG LEU GLY TYR GLN LEU LYS SEQRES 15 B 317 LEU ALA ARG ASP GLN TYR GLY ASP SER ALA ILE TYR GLN SEQRES 16 B 317 LYS GLY HIS THR LEU ILE GLN ASN MET ALA PRO LEU PHE SEQRES 17 B 317 GLU ASN VAL VAL ILE GLU PRO CYS LEU LEU HIS GLY ASP SEQRES 18 B 317 LEU TRP SER GLY ASN ILE ALA TYR ASP LYS ASN ASN GLU SEQRES 19 B 317 PRO VAL ILE LEU ASP PRO ALA CYS TYR TYR GLY HIS ASN SEQRES 20 B 317 GLU ALA ASP PHE GLY MET SER TRP CYS ALA GLY PHE GLY SEQRES 21 B 317 GLU SER PHE TYR ASN ALA TYR PHE LYS VAL MET PRO LYS SEQRES 22 B 317 GLN ALA GLY TYR GLU LYS ARG ARG ASP LEU TYR LEU LEU SEQRES 23 B 317 TYR HIS TYR LEU ASN HIS TYR ASN LEU PHE GLY SER GLY SEQRES 24 B 317 TYR ARG SER SER ALA MET SER ILE ILE ASP ASP TYR LEU SEQRES 25 B 317 ARG MET LEU LYS ALA HET ADP A 301 27 HET SO4 A 302 5 HET SO4 A 303 5 HET SO4 A 304 5 HET SO4 A 305 5 HET SO4 A 306 5 HET SO4 A 307 5 HET SO4 A 308 5 HET SO4 A 309 5 HET SO4 A 310 5 HET CL A 311 1 HET EDO A 312 4 HET EDO A 313 4 HET EDO A 314 4 HET EDO A 315 4 HET DMS A 316 4 HET ADP B 301 27 HET SO4 B 302 5 HET SO4 B 303 5 HET SO4 B 304 5 HET SO4 B 305 5 HET SO4 B 306 5 HET CL B 307 1 HET EDO B 308 4 HET DMS B 309 4 HETNAM ADP ADENOSINE-5'-DIPHOSPHATE HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION HETNAM EDO 1,2-ETHANEDIOL HETNAM DMS DIMETHYL SULFOXIDE HETSYN EDO ETHYLENE GLYCOL FORMUL 3 ADP 2(C10 H15 N5 O10 P2) FORMUL 4 SO4 14(O4 S 2-) FORMUL 13 CL 2(CL 1-) FORMUL 14 EDO 5(C2 H6 O2) FORMUL 18 DMS 2(C2 H6 O S) FORMUL 28 HOH *89(H2 O) HELIX 1 AA1 ASP A 7 GLU A 16 1 10 HELIX 2 AA2 PRO A 56 THR A 72 1 17 HELIX 3 AA3 ASN A 106 GLY A 121 1 16 HELIX 4 AA4 ASP A 147 ARG A 156 1 10 HELIX 5 AA5 ARG A 156 GLY A 169 1 14 HELIX 6 AA6 ASP A 170 ASN A 183 1 14 HELIX 7 AA7 MET A 184 GLU A 189 5 6 HELIX 8 AA8 TRP A 203 GLY A 205 5 3 HELIX 9 AA9 HIS A 226 GLY A 232 5 7 HELIX 10 AB1 MET A 233 ALA A 237 5 5 HELIX 11 AB2 GLY A 240 MET A 251 1 12 HELIX 12 AB3 ARG A 260 GLY A 277 1 18 HELIX 13 AB4 TYR A 280 LEU A 295 1 16 HELIX 14 AB5 PRO B 8 THR B 15 1 8 HELIX 15 AB6 PRO B 56 THR B 72 1 17 HELIX 16 AB7 ASN B 106 GLY B 121 1 16 HELIX 17 AB8 ASP B 147 ARG B 156 1 10 HELIX 18 AB9 ARG B 156 GLY B 169 1 14 HELIX 19 AC1 ASP B 170 ASN B 183 1 14 HELIX 20 AC2 MET B 184 GLU B 189 5 6 HELIX 21 AC3 TRP B 203 GLY B 205 5 3 HELIX 22 AC4 HIS B 226 GLY B 232 5 7 HELIX 23 AC5 MET B 233 ALA B 237 5 5 HELIX 24 AC6 GLY B 240 MET B 251 1 12 HELIX 25 AC7 GLY B 256 GLY B 277 1 22 HELIX 26 AC8 TYR B 280 LEU B 295 1 16 SHEET 1 AA1 5 ILE A 22 GLY A 29 0 SHEET 2 AA1 5 LEU B 35 THR B 41 -1 O HIS B 38 N GLY A 26 SHEET 3 AA1 5 GLY B 44 ASN B 51 -1 O THR B 50 N LEU B 35 SHEET 4 AA1 5 SER B 91 GLU B 96 -1 O MET B 95 N PHE B 47 SHEET 5 AA1 5 PRO B 80 GLU B 85 -1 N LYS B 82 O ILE B 94 SHEET 1 AA2 5 PRO A 80 GLU A 85 0 SHEET 2 AA2 5 SER A 91 GLU A 96 -1 O ILE A 94 N LYS A 82 SHEET 3 AA2 5 GLY A 44 ASN A 51 -1 N PHE A 47 O MET A 95 SHEET 4 AA2 5 LEU A 35 THR A 41 -1 N SER A 37 O VAL A 48 SHEET 5 AA2 5 ILE B 22 GLY B 29 -1 O GLY B 26 N HIS A 38 SHEET 1 AA3 2 ASN A 133 ILE A 135 0 SHEET 2 AA3 2 THR A 138 GLN A 140 -1 O GLN A 140 N ASN A 133 SHEET 1 AA4 2 CYS A 196 LEU A 198 0 SHEET 2 AA4 2 TYR A 223 GLY A 225 -1 O TYR A 223 N LEU A 198 SHEET 1 AA5 2 ILE A 207 TYR A 209 0 SHEET 2 AA5 2 PRO A 215 ILE A 217 -1 O VAL A 216 N ALA A 208 SHEET 1 AA6 2 ASN B 133 ILE B 135 0 SHEET 2 AA6 2 THR B 138 GLN B 140 -1 O GLN B 140 N ASN B 133 SHEET 1 AA7 2 CYS B 196 LEU B 198 0 SHEET 2 AA7 2 TYR B 223 GLY B 225 -1 O TYR B 223 N LEU B 198 SHEET 1 AA8 2 ILE B 207 TYR B 209 0 SHEET 2 AA8 2 PRO B 215 ILE B 217 -1 O VAL B 216 N ALA B 208 SSBOND 1 CYS A 32 CYS B 32 1555 1555 2.06 SSBOND 2 CYS A 236 CYS B 236 1555 1555 2.06 SITE 1 AC1 15 ASN A 34 PHE A 47 LYS A 49 PRO A 78 SITE 2 AC1 15 GLU A 96 PHE A 97 ILE A 98 PHE A 100 SITE 3 AC1 15 ASP A 219 EDO A 315 DMS A 316 HOH A 402 SITE 4 AC1 15 HOH A 438 PHE B 276 GLY B 277 SITE 1 AC2 4 GLY A 256 TYR A 257 GLU A 258 LYS A 259 SITE 1 AC3 4 ARG A 76 ASP A 99 LYS A 211 HOH A 403 SITE 1 AC4 3 ALA A 172 ARG A 281 SER B 103 SITE 1 AC5 2 ARG A 112 LYS A 113 SITE 1 AC6 2 LYS A 162 ARG A 165 SITE 1 AC7 4 HIS A 38 DMS A 316 HOH A 408 LYS B 24 SITE 1 AC8 4 ASN A 79 HIS A 81 GLU A 96 HOH A 401 SITE 1 AC9 2 SER A 145 SER A 146 SITE 1 AD1 4 ASN A 106 GLN A 107 ALA A 108 SER A 242 SITE 1 AD2 1 HIS A 272 SITE 1 AD3 7 PHE A 276 GLY A 277 SER A 278 GLY A 279 SITE 2 AD3 7 GLY B 205 ILE B 207 ADP B 301 SITE 1 AD4 1 HIS A 81 SITE 1 AD5 3 GLY A 240 GLU A 241 SER A 242 SITE 1 AD6 6 GLY A 205 ILE A 207 ADP A 301 PHE B 276 SITE 2 AD6 6 GLY B 277 GLY B 279 SITE 1 AD7 6 HIS A 38 PHE A 47 PHE A 97 ADP A 301 SITE 2 AD7 6 SO4 A 307 VAL B 28 SITE 1 AD8 14 PHE A 276 GLY A 277 EDO A 312 ASN B 34 SITE 2 AD8 14 PHE B 47 LYS B 49 PRO B 78 MET B 95 SITE 3 AD8 14 GLU B 96 PHE B 97 ILE B 98 PHE B 100 SITE 4 AD8 14 ASP B 219 HOH B 427 SITE 1 AD9 4 GLY B 256 TYR B 257 GLU B 258 LYS B 259 SITE 1 AE1 3 ARG B 76 ASP B 99 LYS B 211 SITE 1 AE2 2 ARG B 112 LYS B 113 SITE 1 AE3 4 SER A 103 ALA B 172 LYS B 176 ARG B 281 SITE 1 AE4 4 LYS A 24 GLY A 26 HIS B 38 GLN B 40 SITE 1 AE5 1 HIS B 272 SITE 1 AE6 3 ASN B 106 GLN B 107 SER B 242 SITE 1 AE7 6 ARG B 10 ILE B 22 THR B 23 LYS B 24 SITE 2 AE7 6 ILE B 25 SER B 27 CRYST1 158.860 163.640 70.720 90.00 90.00 90.00 C 2 2 21 16 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 0.006295 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006111 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014140 0.00000 ATOM 1 N ASP A 7 69.358 -0.958 45.730 1.00105.86 N ANISOU 1 N ASP A 7 15615 12182 12426 4401 2576 3652 N ATOM 2 CA ASP A 7 68.066 -0.411 45.313 1.00104.46 C ANISOU 2 CA ASP A 7 15492 11887 12311 4187 2629 3520 C ATOM 3 C ASP A 7 67.420 0.404 46.429 1.00103.31 C ANISOU 3 C ASP A 7 15396 11812 12046 4103 2559 3526 C ATOM 4 O ASP A 7 66.581 -0.105 47.166 1.00100.42 O ANISOU 4 O ASP A 7 15142 11331 11680 4081 2654 3553 O ATOM 5 CB ASP A 7 67.131 -1.539 44.863 1.00104.04 C ANISOU 5 CB ASP A 7 15559 11573 12400 4129 2815 3478 C ATOM 6 CG ASP A 7 65.916 -1.034 44.092 1.00109.59 C ANISOU 6 CG ASP A 7 16279 12159 13202 3901 2866 3337 C ATOM 7 OD1 ASP A 7 65.719 0.197 43.989 1.00106.91 O ANISOU 7 OD1 ASP A 7 15873 11932 12816 3795 2771 3271 O ATOM 8 OD2 ASP A 7 65.156 -1.880 43.578 1.00112.76 O ANISOU 8 OD2 ASP A 7 16762 12354 13726 3823 2992 3294 O ATOM 9 N PRO A 8 67.807 1.680 46.541 1.00102.65 N ANISOU 9 N PRO A 8 15233 11916 11853 4053 2390 3500 N ATOM 10 CA PRO A 8 67.266 2.520 47.627 1.00 98.33 C ANISOU 10 CA PRO A 8 14752 11441 11168 3980 2310 3499 C ATOM 11 C PRO A 8 65.763 2.768 47.542 1.00 88.43 C ANISOU 11 C PRO A 8 13580 10044 9973 3816 2425 3399 C ATOM 12 O PRO A 8 65.146 3.066 48.572 1.00 91.01 O ANISOU 12 O PRO A 8 13992 10381 10205 3791 2425 3417 O ATOM 13 CB PRO A 8 68.059 3.828 47.493 1.00 97.64 C ANISOU 13 CB PRO A 8 14563 11573 10963 3939 2091 3475 C ATOM 14 CG PRO A 8 69.273 3.475 46.695 1.00 96.21 C ANISOU 14 CG PRO A 8 14244 11477 10835 4051 2046 3524 C ATOM 15 CD PRO A 8 68.821 2.397 45.750 1.00 97.10 C ANISOU 15 CD PRO A 8 14382 11379 11133 4069 2252 3483 C ATOM 16 N ILE A 9 65.152 2.692 46.359 1.00 81.62 N ANISOU 16 N ILE A 9 12691 9058 9263 3702 2519 3296 N ATOM 17 CA ILE A 9 63.710 2.912 46.271 1.00 83.15 C ANISOU 17 CA ILE A 9 12941 9130 9523 3540 2622 3213 C ATOM 18 C ILE A 9 62.958 1.803 47.003 1.00 90.00 C ANISOU 18 C ILE A 9 13908 9854 10434 3572 2772 3287 C ATOM 19 O ILE A 9 62.209 2.065 47.953 1.00 82.85 O ANISOU 19 O ILE A 9 13066 8958 9456 3547 2797 3310 O ATOM 20 CB ILE A 9 63.264 3.033 44.805 1.00 70.41 C ANISOU 20 CB ILE A 9 11271 7414 8069 3398 2673 3091 C ATOM 21 CG1 ILE A 9 63.923 4.247 44.148 1.00 67.06 C ANISOU 21 CG1 ILE A 9 10752 7139 7590 3355 2520 3020 C ATOM 22 CG2 ILE A 9 61.754 3.182 44.725 1.00 70.47 C ANISOU 22 CG2 ILE A 9 11317 7303 8157 3228 2776 3020 C ATOM 23 CD1 ILE A 9 63.906 4.200 42.610 1.00 63.94 C ANISOU 23 CD1 ILE A 9 10291 6655 7348 3263 2558 2919 C ATOM 24 N ARG A 10 63.154 0.545 46.577 1.00 96.12 N ANISOU 24 N ARG A 10 14706 10493 11321 3632 2871 3327 N ATOM 25 CA ARG A 10 62.581 -0.585 47.310 1.00 94.75 C ANISOU 25 CA ARG A 10 14635 10188 11177 3674 2995 3414 C ATOM 26 C ARG A 10 63.051 -0.589 48.756 1.00 90.42 C ANISOU 26 C ARG A 10 14139 9752 10466 3817 2942 3532 C ATOM 27 O ARG A 10 62.256 -0.819 49.673 1.00 88.69 O ANISOU 27 O ARG A 10 13998 9487 10213 3805 3012 3583 O ATOM 28 CB ARG A 10 62.916 -1.910 46.621 1.00103.05 C ANISOU 28 CB ARG A 10 15721 11085 12350 3731 3083 3439 C ATOM 29 CG ARG A 10 62.008 -2.200 45.423 1.00111.66 C ANISOU 29 CG ARG A 10 16814 12000 13612 3552 3168 3333 C ATOM 30 CD ARG A 10 62.227 -3.588 44.799 1.00119.81 C ANISOU 30 CD ARG A 10 17920 12850 14752 3597 3254 3352 C ATOM 31 NE ARG A 10 61.523 -3.697 43.516 1.00118.23 N ANISOU 31 NE ARG A 10 17717 12504 14702 3414 3294 3233 N ATOM 32 CZ ARG A 10 60.550 -4.565 43.249 1.00113.27 C ANISOU 32 CZ ARG A 10 17173 11680 14186 3292 3380 3225 C ATOM 33 NH1 ARG A 10 60.155 -5.438 44.176 1.00113.85 N ANISOU 33 NH1 ARG A 10 17342 11673 14245 3339 3445 3336 N ATOM 34 NH2 ARG A 10 59.976 -4.562 42.049 1.00105.57 N ANISOU 34 NH2 ARG A 10 16186 10589 13336 3116 3388 3111 N ATOM 35 N GLU A 11 64.335 -0.321 48.984 1.00 92.66 N ANISOU 35 N GLU A 11 14373 10187 10645 3950 2812 3582 N ATOM 36 CA GLU A 11 64.841 -0.253 50.351 1.00 99.24 C ANISOU 36 CA GLU A 11 15254 11137 11315 4072 2733 3692 C ATOM 37 C GLU A 11 64.044 0.728 51.212 1.00 93.06 C ANISOU 37 C GLU A 11 14524 10417 10418 3985 2697 3662 C ATOM 38 O GLU A 11 63.593 0.377 52.309 1.00 92.57 O ANISOU 38 O GLU A 11 14558 10325 10289 4028 2751 3736 O ATOM 39 CB GLU A 11 66.314 0.139 50.345 1.00110.78 C ANISOU 39 CB GLU A 11 16625 12783 12683 4188 2561 3739 C ATOM 40 CG GLU A 11 66.893 0.327 51.733 1.00120.04 C ANISOU 40 CG GLU A 11 17841 14088 13678 4290 2443 3848 C ATOM 41 CD GLU A 11 68.394 0.498 51.709 1.00128.88 C ANISOU 41 CD GLU A 11 18854 15389 14727 4407 2274 3922 C ATOM 42 OE1 GLU A 11 69.062 -0.226 50.936 1.00133.18 O ANISOU 42 OE1 GLU A 11 19324 15908 15371 4502 2317 3950 O ATOM 43 OE2 GLU A 11 68.904 1.354 52.464 1.00129.32 O ANISOU 43 OE2 GLU A 11 18900 15611 14624 4401 2093 3953 O ATOM 44 N TRP A 12 63.871 1.974 50.741 1.00 94.22 N ANISOU 44 N TRP A 12 14616 10652 10533 3869 2606 3555 N ATOM 45 CA TRP A 12 63.184 2.983 51.558 1.00 87.75 C ANISOU 45 CA TRP A 12 13858 9898 9586 3800 2564 3519 C ATOM 46 C TRP A 12 61.722 2.610 51.775 1.00 87.96 C ANISOU 46 C TRP A 12 13946 9782 9693 3725 2746 3506 C ATOM 47 O TRP A 12 61.192 2.765 52.885 1.00 72.35 O ANISOU 47 O TRP A 12 12057 7820 7613 3752 2774 3550 O ATOM 48 CB TRP A 12 63.284 4.380 50.932 1.00 77.82 C ANISOU 48 CB TRP A 12 12538 8751 8279 3685 2428 3401 C ATOM 49 CG TRP A 12 62.706 5.470 51.830 1.00 85.73 C ANISOU 49 CG TRP A 12 13622 9827 9123 3631 2367 3362 C ATOM 50 CD1 TRP A 12 63.391 6.244 52.726 1.00 89.03 C ANISOU 50 CD1 TRP A 12 14094 10392 9342 3666 2187 3386 C ATOM 51 CD2 TRP A 12 61.324 5.871 51.935 1.00 83.78 C ANISOU 51 CD2 TRP A 12 13422 9507 8904 3537 2485 3295 C ATOM 52 NE1 TRP A 12 62.527 7.106 53.373 1.00 83.42 N ANISOU 52 NE1 TRP A 12 13477 9693 8527 3605 2192 3329 N ATOM 53 CE2 TRP A 12 61.256 6.894 52.906 1.00 82.74 C ANISOU 53 CE2 TRP A 12 13380 9479 8579 3537 2380 3277 C ATOM 54 CE3 TRP A 12 60.142 5.462 51.301 1.00 81.09 C ANISOU 54 CE3 TRP A 12 13051 9027 8734 3448 2662 3254 C ATOM 55 CZ2 TRP A 12 60.056 7.506 53.265 1.00 83.27 C ANISOU 55 CZ2 TRP A 12 13507 9514 8617 3479 2464 3220 C ATOM 56 CZ3 TRP A 12 58.948 6.082 51.651 1.00 81.80 C ANISOU 56 CZ3 TRP A 12 13180 9099 8802 3379 2735 3208 C ATOM 57 CH2 TRP A 12 58.917 7.092 52.625 1.00 85.15 C ANISOU 57 CH2 TRP A 12 13693 9629 9030 3408 2645 3192 C ATOM 58 N ILE A 13 61.056 2.127 50.720 1.00 78.41 N ANISOU 58 N ILE A 13 12689 8435 8667 3627 2865 3451 N ATOM 59 CA ILE A 13 59.649 1.760 50.811 1.00 81.96 C ANISOU 59 CA ILE A 13 13172 8757 9214 3534 3024 3448 C ATOM 60 C ILE A 13 59.427 0.704 51.898 1.00 91.72 C ANISOU 60 C ILE A 13 14502 9924 10424 3636 3122 3581 C ATOM 61 O ILE A 13 58.356 0.655 52.517 1.00 88.15 O ANISOU 61 O ILE A 13 14093 9427 9972 3598 3222 3611 O ATOM 62 CB ILE A 13 59.154 1.328 49.410 1.00 79.34 C ANISOU 62 CB ILE A 13 12771 8288 9087 3401 3101 3372 C ATOM 63 CG1 ILE A 13 59.119 2.559 48.496 1.00 84.94 C ANISOU 63 CG1 ILE A 13 13396 9071 9806 3284 3013 3239 C ATOM 64 CG2 ILE A 13 57.773 0.705 49.449 1.00 81.54 C ANISOU 64 CG2 ILE A 13 13071 8423 9488 3299 3253 3395 C ATOM 65 CD1 ILE A 13 58.332 2.391 47.190 1.00 83.89 C ANISOU 65 CD1 ILE A 13 13198 8810 9865 3115 3084 3147 C ATOM 66 N LEU A 14 60.432 -0.130 52.175 1.00 97.34 N ANISOU 66 N LEU A 14 15245 10632 11108 3772 3093 3668 N ATOM 67 CA LEU A 14 60.329 -1.122 53.241 1.00100.04 C ANISOU 67 CA LEU A 14 15685 10913 11412 3878 3171 3799 C ATOM 68 C LEU A 14 61.064 -0.708 54.524 1.00104.89 C ANISOU 68 C LEU A 14 16361 11671 11822 4010 3062 3873 C ATOM 69 O LEU A 14 60.752 -1.230 55.596 1.00101.30 O ANISOU 69 O LEU A 14 15998 11185 11305 4079 3126 3971 O ATOM 70 CB LEU A 14 60.812 -2.483 52.722 1.00 92.31 C ANISOU 70 CB LEU A 14 14720 9802 10550 3939 3231 3855 C ATOM 71 CG LEU A 14 60.121 -2.776 51.365 1.00 90.34 C ANISOU 71 CG LEU A 14 14421 9409 10493 3784 3310 3763 C ATOM 72 CD1 LEU A 14 60.551 -4.061 50.716 1.00 92.34 C ANISOU 72 CD1 LEU A 14 14708 9515 10860 3829 3364 3796 C ATOM 73 CD2 LEU A 14 58.611 -2.743 51.390 1.00 93.20 C ANISOU 73 CD2 LEU A 14 14792 9682 10939 3630 3420 3745 C ATOM 74 N THR A 15 61.964 0.275 54.463 1.00116.66 N ANISOU 74 N THR A 15 17806 13319 13201 4031 2891 3828 N ATOM 75 CA THR A 15 62.573 0.796 55.686 1.00126.31 C ANISOU 75 CA THR A 15 19094 14677 14220 4122 2762 3889 C ATOM 76 C THR A 15 61.595 1.744 56.366 1.00123.83 C ANISOU 76 C THR A 15 18848 14397 13806 4051 2780 3839 C ATOM 77 O THR A 15 61.009 1.416 57.402 1.00130.67 O ANISOU 77 O THR A 15 19813 15225 14610 4098 2866 3910 O ATOM 78 CB THR A 15 63.877 1.538 55.362 1.00136.21 C ANISOU 78 CB THR A 15 20272 16093 15390 4147 2551 3865 C ATOM 79 OG1 THR A 15 64.720 0.715 54.551 1.00142.22 O ANISOU 79 OG1 THR A 15 20950 16825 16263 4218 2554 3900 O ATOM 80 CG2 THR A 15 64.613 1.947 56.641 1.00137.59 C ANISOU 80 CG2 THR A 15 20520 16402 15357 4230 2393 3944 C ATOM 81 N GLU A 16 61.415 2.925 55.784 1.00117.62 N ANISOU 81 N GLU A 16 18012 13679 12999 3943 2702 3718 N ATOM 82 CA GLU A 16 60.575 3.972 56.335 1.00111.08 C ANISOU 82 CA GLU A 16 17248 12893 12066 3883 2703 3656 C ATOM 83 C GLU A 16 59.185 4.009 55.718 1.00 95.96 C ANISOU 83 C GLU A 16 15292 10874 10295 3774 2872 3591 C ATOM 84 O GLU A 16 58.278 4.611 56.301 1.00 84.50 O ANISOU 84 O GLU A 16 13897 9432 8777 3754 2929 3569 O ATOM 85 CB GLU A 16 61.262 5.328 56.166 1.00116.61 C ANISOU 85 CB GLU A 16 17935 13739 12633 3830 2491 3566 C ATOM 86 CG GLU A 16 62.595 5.362 56.893 1.00126.57 C ANISOU 86 CG GLU A 16 19233 15117 13740 3920 2301 3644 C ATOM 87 CD GLU A 16 62.983 6.745 57.369 1.00131.14 C ANISOU 87 CD GLU A 16 19873 15832 14122 3864 2095 3582 C ATOM 88 OE1 GLU A 16 63.080 7.659 56.520 1.00128.75 O ANISOU 88 OE1 GLU A 16 19505 15583 13830 3756 2000 3473 O ATOM 89 OE2 GLU A 16 63.185 6.912 58.594 1.00135.87 O ANISOU 89 OE2 GLU A 16 20595 16477 14551 3921 2025 3642 O ATOM 90 N GLY A 17 58.992 3.399 54.553 1.00 93.95 N ANISOU 90 N GLY A 17 14940 10521 10234 3703 2949 3563 N ATOM 91 CA GLY A 17 57.658 3.383 53.995 1.00 94.31 C ANISOU 91 CA GLY A 17 14940 10470 10423 3585 3095 3516 C ATOM 92 C GLY A 17 56.689 2.409 54.637 1.00 98.24 C ANISOU 92 C GLY A 17 15484 10858 10985 3606 3271 3621 C ATOM 93 O GLY A 17 55.499 2.456 54.301 1.00 97.58 O ANISOU 93 O GLY A 17 15356 10710 11011 3505 3385 3599 O ATOM 94 N LYS A 18 57.167 1.527 55.528 1.00 95.64 N ANISOU 94 N LYS A 18 15236 10509 10595 3730 3290 3740 N ATOM 95 CA LYS A 18 56.312 0.629 56.305 1.00 97.15 C ANISOU 95 CA LYS A 18 15487 10607 10819 3760 3445 3854 C ATOM 96 C LYS A 18 55.513 -0.340 55.431 1.00 98.18 C ANISOU 96 C LYS A 18 15556 10579 11171 3647 3573 3871 C ATOM 97 O LYS A 18 54.420 -0.759 55.804 1.00109.17 O ANISOU 97 O LYS A 18 16958 11901 12621 3606 3703 3939 O ATOM 98 CB LYS A 18 55.357 1.417 57.205 1.00 96.08 C ANISOU 98 CB LYS A 18 15400 10528 10578 3768 3504 3859 C ATOM 99 CG LYS A 18 56.020 2.293 58.253 1.00103.48 C ANISOU 99 CG LYS A 18 16440 11600 11280 3876 3383 3853 C ATOM 100 CD LYS A 18 55.105 3.461 58.632 1.00109.18 C ANISOU 100 CD LYS A 18 17187 12382 11916 3850 3413 3790 C ATOM 101 CE LYS A 18 55.203 3.812 60.119 1.00116.38 C ANISOU 101 CE LYS A 18 18250 13361 12609 3977 3394 3848 C ATOM 102 NZ LYS A 18 54.030 4.620 60.580 1.00118.26 N ANISOU 102 NZ LYS A 18 18522 13618 12794 3977 3494 3822 N ATOM 103 N ALA A 19 56.030 -0.727 54.273 1.00 90.38 N ANISOU 103 N ALA A 19 14506 9529 10305 3590 3533 3816 N ATOM 104 CA ALA A 19 55.329 -1.657 53.395 1.00 90.53 C ANISOU 104 CA ALA A 19 14486 9385 10527 3468 3630 3823 C ATOM 105 C ALA A 19 55.976 -3.034 53.472 1.00 89.14 C ANISOU 105 C ALA A 19 14381 9096 10391 3550 3653 3914 C ATOM 106 O ALA A 19 57.092 -3.182 53.983 1.00 91.66 O ANISOU 106 O ALA A 19 14751 9479 10598 3701 3582 3956 O ATOM 107 CB ALA A 19 55.328 -1.154 51.947 1.00 89.15 C ANISOU 107 CB ALA A 19 14207 9194 10471 3331 3578 3687 C ATOM 108 N THR A 20 55.242 -4.065 53.017 1.00 94.47 N ANISOU 108 N THR A 20 15068 9603 11224 3450 3747 3955 N ATOM 109 CA THR A 20 55.833 -5.403 52.906 1.00108.69 C ANISOU 109 CA THR A 20 16950 11271 13076 3516 3766 4026 C ATOM 110 C THR A 20 55.758 -6.039 51.513 1.00110.95 C ANISOU 110 C THR A 20 17216 11403 13537 3393 3770 3958 C ATOM 111 O THR A 20 56.553 -6.946 51.238 1.00111.45 O ANISOU 111 O THR A 20 17346 11378 13623 3475 3759 3984 O ATOM 112 CB THR A 20 55.243 -6.378 53.953 1.00110.43 C ANISOU 112 CB THR A 20 17269 11404 13284 3553 3866 4178 C ATOM 113 OG1 THR A 20 53.829 -6.564 53.759 1.00111.47 O ANISOU 113 OG1 THR A 20 17370 11446 13536 3381 3953 4202 O ATOM 114 CG2 THR A 20 55.515 -5.866 55.376 1.00106.13 C ANISOU 114 CG2 THR A 20 16772 11004 12548 3703 3855 4249 C ATOM 115 N GLN A 21 54.862 -5.595 50.624 1.00111.31 N ANISOU 115 N GLN A 21 17178 11414 13701 3204 3779 3871 N ATOM 116 CA GLN A 21 54.903 -6.082 49.246 1.00111.62 C ANISOU 116 CA GLN A 21 17206 11317 13889 3086 3758 3788 C ATOM 117 C GLN A 21 54.582 -4.953 48.273 1.00104.77 C ANISOU 117 C GLN A 21 16215 10519 13074 2948 3705 3646 C ATOM 118 O GLN A 21 53.710 -4.115 48.522 1.00104.75 O ANISOU 118 O GLN A 21 16139 10598 13064 2864 3721 3631 O ATOM 119 CB GLN A 21 53.941 -7.267 48.955 1.00112.79 C ANISOU 119 CB GLN A 21 17418 11258 14179 2942 3824 3851 C ATOM 120 CG GLN A 21 52.423 -6.977 48.969 1.00107.36 C ANISOU 120 CG GLN A 21 16660 10556 13577 2747 3867 3873 C ATOM 121 CD GLN A 21 51.572 -8.142 48.406 1.00 98.91 C ANISOU 121 CD GLN A 21 15647 9273 12660 2569 3890 3924 C ATOM 122 OE1 GLN A 21 52.071 -9.251 48.177 1.00 91.92 O ANISOU 122 OE1 GLN A 21 14884 8238 11805 2606 3886 3955 O ATOM 123 NE2 GLN A 21 50.283 -7.879 48.179 1.00 95.11 N ANISOU 123 NE2 GLN A 21 15083 8783 12273 2374 3904 3936 N ATOM 124 N ILE A 22 55.307 -4.948 47.164 1.00 98.70 N ANISOU 124 N ILE A 22 15428 9718 12357 2934 3646 3546 N ATOM 125 CA ILE A 22 55.068 -4.046 46.052 1.00 90.81 C ANISOU 125 CA ILE A 22 14324 8753 11427 2791 3592 3405 C ATOM 126 C ILE A 22 54.290 -4.833 45.009 1.00 92.06 C ANISOU 126 C ILE A 22 14501 8720 11759 2599 3611 3369 C ATOM 127 O ILE A 22 54.822 -5.762 44.396 1.00 91.74 O ANISOU 127 O ILE A 22 14541 8546 11771 2620 3607 3358 O ATOM 128 CB ILE A 22 56.386 -3.501 45.488 1.00 86.23 C ANISOU 128 CB ILE A 22 13712 8268 10786 2895 3507 3322 C ATOM 129 CG1 ILE A 22 57.143 -2.714 46.571 1.00 86.05 C ANISOU 129 CG1 ILE A 22 13677 8439 10580 3068 3457 3369 C ATOM 130 CG2 ILE A 22 56.120 -2.671 44.242 1.00 71.97 C ANISOU 130 CG2 ILE A 22 11808 6473 9062 2734 3453 3176 C ATOM 131 CD1 ILE A 22 58.499 -2.190 46.148 1.00 76.77 C ANISOU 131 CD1 ILE A 22 12461 7378 9332 3180 3356 3318 C ATOM 132 N THR A 23 53.043 -4.452 44.769 1.00 98.00 N ANISOU 132 N THR A 23 15180 9460 12595 2412 3622 3349 N ATOM 133 CA THR A 23 52.197 -5.253 43.898 1.00104.23 C ANISOU 133 CA THR A 23 15992 10069 13542 2211 3621 3337 C ATOM 134 C THR A 23 52.259 -4.822 42.442 1.00107.62 C ANISOU 134 C THR A 23 16361 10467 14061 2070 3545 3181 C ATOM 135 O THR A 23 51.970 -5.641 41.561 1.00115.03 O ANISOU 135 O THR A 23 17357 11238 15111 1937 3519 3152 O ATOM 136 CB THR A 23 50.730 -5.188 44.355 1.00103.73 C ANISOU 136 CB THR A 23 15873 10005 13537 2062 3662 3418 C ATOM 137 OG1 THR A 23 50.211 -3.868 44.171 1.00 98.40 O ANISOU 137 OG1 THR A 23 15058 9473 12855 1990 3639 3342 O ATOM 138 CG2 THR A 23 50.592 -5.551 45.823 1.00109.55 C ANISOU 138 CG2 THR A 23 16664 10779 14179 2197 3745 3574 C ATOM 139 N LYS A 24 52.648 -3.577 42.168 1.00100.78 N ANISOU 139 N LYS A 24 15395 9753 13143 2094 3499 3080 N ATOM 140 CA LYS A 24 52.710 -3.079 40.802 1.00 90.74 C ANISOU 140 CA LYS A 24 14063 8464 11951 1960 3426 2930 C ATOM 141 C LYS A 24 53.555 -1.809 40.777 1.00 89.09 C ANISOU 141 C LYS A 24 13777 8433 11638 2062 3379 2850 C ATOM 142 O LYS A 24 53.662 -1.100 41.782 1.00 89.89 O ANISOU 142 O LYS A 24 13852 8681 11623 2172 3391 2901 O ATOM 143 CB LYS A 24 51.300 -2.827 40.261 1.00 85.97 C ANISOU 143 CB LYS A 24 13375 7823 11466 1715 3402 2899 C ATOM 144 CG LYS A 24 51.205 -2.713 38.755 1.00 86.31 C ANISOU 144 CG LYS A 24 13387 7792 11615 1540 3318 2756 C ATOM 145 CD LYS A 24 49.797 -2.339 38.362 1.00 93.10 C ANISOU 145 CD LYS A 24 14145 8653 12575 1308 3280 2742 C ATOM 146 CE LYS A 24 49.718 -1.961 36.905 1.00102.41 C ANISOU 146 CE LYS A 24 15273 9799 13838 1138 3180 2587 C ATOM 147 NZ LYS A 24 48.416 -1.305 36.595 1.00110.18 N ANISOU 147 NZ LYS A 24 16129 10837 14896 936 3131 2571 N ATOM 148 N ILE A 25 54.189 -1.553 39.635 1.00 84.55 N ANISOU 148 N ILE A 25 13182 7844 11100 2026 3318 2729 N ATOM 149 CA ILE A 25 54.925 -0.311 39.388 1.00 76.90 C ANISOU 149 CA ILE A 25 12135 7032 10052 2080 3254 2644 C ATOM 150 C ILE A 25 54.515 0.185 38.010 1.00 76.49 C ANISOU 150 C ILE A 25 12013 6942 10109 1881 3194 2497 C ATOM 151 O ILE A 25 54.858 -0.438 36.996 1.00 80.61 O ANISOU 151 O ILE A 25 12576 7346 10705 1834 3176 2432 O ATOM 152 CB ILE A 25 56.445 -0.498 39.465 1.00 72.54 C ANISOU 152 CB ILE A 25 11627 6529 9406 2288 3235 2663 C ATOM 153 CG1 ILE A 25 56.881 -0.882 40.877 1.00 69.92 C ANISOU 153 CG1 ILE A 25 11356 6259 8952 2485 3274 2806 C ATOM 154 CG2 ILE A 25 57.175 0.754 38.998 1.00 68.65 C ANISOU 154 CG2 ILE A 25 11050 6185 8851 2308 3148 2574 C ATOM 155 CD1 ILE A 25 58.395 -1.008 40.989 1.00 69.30 C ANISOU 155 CD1 ILE A 25 11298 6256 8776 2695 3237 2839 C ATOM 156 N GLY A 26 53.831 1.327 37.963 1.00 65.54 N ANISOU 156 N GLY A 26 10526 5657 8720 1775 3158 2442 N ATOM 157 CA GLY A 26 53.404 1.926 36.712 1.00 64.31 C ANISOU 157 CA GLY A 26 10292 5484 8658 1583 3090 2303 C ATOM 158 C GLY A 26 54.251 3.151 36.396 1.00 68.23 C ANISOU 158 C GLY A 26 10734 6118 9072 1634 3021 2215 C ATOM 159 O GLY A 26 54.378 4.060 37.218 1.00 66.97 O ANISOU 159 O GLY A 26 10550 6100 8797 1721 3008 2248 O ATOM 160 N SER A 27 54.823 3.149 35.192 1.00 66.05 N ANISOU 160 N SER A 27 10450 5794 8851 1578 2971 2106 N ATOM 161 CA SER A 27 55.830 4.115 34.782 1.00 70.09 C ANISOU 161 CA SER A 27 10923 6417 9292 1638 2903 2036 C ATOM 162 C SER A 27 55.444 4.776 33.468 1.00 71.66 C ANISOU 162 C SER A 27 11049 6597 9581 1436 2833 1880 C ATOM 163 O SER A 27 54.991 4.101 32.535 1.00 70.60 O ANISOU 163 O SER A 27 10926 6334 9563 1299 2828 1813 O ATOM 164 CB SER A 27 57.196 3.449 34.617 1.00 72.13 C ANISOU 164 CB SER A 27 11242 6652 9510 1814 2914 2069 C ATOM 165 OG SER A 27 57.698 3.026 35.865 1.00 73.95 O ANISOU 165 OG SER A 27 11525 6936 9635 2014 2955 2210 O ATOM 166 N VAL A 28 55.615 6.104 33.412 1.00 66.59 N ANISOU 166 N VAL A 28 10342 6086 8874 1416 2765 1822 N ATOM 167 CA VAL A 28 55.509 6.879 32.179 1.00 62.11 C ANISOU 167 CA VAL A 28 9706 5524 8368 1249 2686 1671 C ATOM 168 C VAL A 28 56.754 7.750 32.057 1.00 60.18 C ANISOU 168 C VAL A 28 9453 5389 8023 1356 2624 1650 C ATOM 169 O VAL A 28 57.525 7.911 33.007 1.00 64.47 O ANISOU 169 O VAL A 28 10030 6029 8439 1543 2621 1756 O ATOM 170 CB VAL A 28 54.234 7.737 32.122 1.00 59.55 C ANISOU 170 CB VAL A 28 9301 5245 8078 1075 2649 1614 C ATOM 171 CG1 VAL A 28 52.985 6.839 32.219 1.00 58.85 C ANISOU 171 CG1 VAL A 28 9208 5058 8096 970 2696 1657 C ATOM 172 CG2 VAL A 28 54.249 8.770 33.232 1.00 57.28 C ANISOU 172 CG2 VAL A 28 9012 5101 7650 1176 2642 1677 C ATOM 173 N GLY A 29 56.942 8.321 30.870 1.00 58.24 N ANISOU 173 N GLY A 29 9159 5138 7831 1231 2557 1516 N ATOM 174 CA GLY A 29 58.095 9.178 30.630 1.00 59.11 C ANISOU 174 CA GLY A 29 9255 5346 7859 1313 2487 1498 C ATOM 175 C GLY A 29 59.334 8.391 30.235 1.00 70.02 C ANISOU 175 C GLY A 29 10666 6690 9247 1471 2514 1532 C ATOM 176 O GLY A 29 59.228 7.328 29.620 1.00 73.75 O ANISOU 176 O GLY A 29 11174 7033 9816 1444 2573 1499 O ATOM 177 N GLY A 30 60.513 8.918 30.562 1.00 69.27 N ANISOU 177 N GLY A 30 10558 6719 9042 1643 2460 1603 N ATOM 178 CA GLY A 30 61.761 8.208 30.366 1.00 69.77 C ANISOU 178 CA GLY A 30 10625 6790 9094 1845 2483 1668 C ATOM 179 C GLY A 30 62.364 8.249 28.977 1.00 74.15 C ANISOU 179 C GLY A 30 11142 7299 9733 1809 2471 1553 C ATOM 180 O GLY A 30 63.465 7.721 28.789 1.00 77.99 O ANISOU 180 O GLY A 30 11613 7817 10204 2002 2493 1609 O ATOM 181 N GLY A 31 61.698 8.834 27.997 1.00 71.19 N ANISOU 181 N GLY A 31 10744 6865 9442 1576 2438 1393 N ATOM 182 CA GLY A 31 62.295 8.925 26.679 1.00 79.69 C ANISOU 182 CA GLY A 31 11785 7906 10586 1539 2425 1273 C ATOM 183 C GLY A 31 63.494 9.866 26.640 1.00 82.32 C ANISOU 183 C GLY A 31 11975 8495 10807 1625 2296 1262 C ATOM 184 O GLY A 31 63.802 10.576 27.596 1.00 88.15 O ANISOU 184 O GLY A 31 12640 9451 11401 1671 2186 1330 O ATOM 185 N CYS A 32 64.214 9.841 25.518 1.00 74.49 N ANISOU 185 N CYS A 32 10914 7536 9854 1620 2281 1158 N ATOM 186 CA CYS A 32 65.279 10.802 25.272 1.00 71.70 C ANISOU 186 CA CYS A 32 10365 7489 9387 1617 2121 1105 C ATOM 187 C CYS A 32 64.823 11.781 24.194 1.00 66.64 C ANISOU 187 C CYS A 32 9667 6865 8787 1341 2031 900 C ATOM 188 O CYS A 32 64.073 11.423 23.287 1.00 72.24 O ANISOU 188 O CYS A 32 10474 7342 9630 1209 2116 794 O ATOM 189 CB CYS A 32 66.593 10.111 24.891 1.00 81.03 C ANISOU 189 CB CYS A 32 11477 8751 10560 1849 2167 1169 C ATOM 190 SG CYS A 32 67.138 8.925 26.190 1.00106.02 S ANISOU 190 SG CYS A 32 14715 11892 13675 2192 2272 1425 S ATOM 191 N ILE A 33 65.233 13.034 24.354 1.00 60.56 N ANISOU 191 N ILE A 33 8755 6359 7895 1241 1848 851 N ATOM 192 CA ILE A 33 64.847 14.095 23.437 1.00 62.10 C ANISOU 192 CA ILE A 33 8894 6593 8108 978 1742 665 C ATOM 193 C ILE A 33 65.708 14.083 22.191 1.00 64.29 C ANISOU 193 C ILE A 33 9057 6966 8405 969 1714 571 C ATOM 194 O ILE A 33 66.701 13.360 22.115 1.00 63.80 O ANISOU 194 O ILE A 33 8935 6981 8325 1179 1765 663 O ATOM 195 CB ILE A 33 64.949 15.480 24.104 1.00 76.52 C ANISOU 195 CB ILE A 33 10660 8628 9784 865 1559 653 C ATOM 196 CG1 ILE A 33 66.225 15.576 24.943 1.00 89.58 C ANISOU 196 CG1 ILE A 33 12444 10164 11427 854 1609 722 C ATOM 197 CG2 ILE A 33 63.721 15.751 24.959 1.00 83.21 C ANISOU 197 CG2 ILE A 33 11442 9539 10634 611 1435 466 C ATOM 198 CD1 ILE A 33 66.234 16.740 25.909 1.00 96.41 C ANISOU 198 CD1 ILE A 33 13276 11248 12106 806 1432 735 C ATOM 199 N ASN A 34 65.323 14.890 21.211 1.00 58.76 N ANISOU 199 N ASN A 34 8332 6243 7749 735 1652 394 N ATOM 200 CA ASN A 34 66.083 14.954 19.970 1.00 63.92 C ANISOU 200 CA ASN A 34 8897 6960 8429 707 1643 294 C ATOM 201 C ASN A 34 67.438 15.638 20.133 1.00 53.74 C ANISOU 201 C ASN A 34 7401 6018 7001 777 1498 349 C ATOM 202 O ASN A 34 67.558 16.676 20.788 1.00 48.09 O ANISOU 202 O ASN A 34 6604 5507 6162 689 1324 365 O ATOM 203 CB ASN A 34 65.268 15.702 18.918 1.00 59.86 C ANISOU 203 CB ASN A 34 8406 6358 7981 419 1586 95 C ATOM 204 CG ASN A 34 64.121 14.879 18.397 1.00 64.79 C ANISOU 204 CG ASN A 34 9216 6638 8764 342 1733 38 C ATOM 205 OD1 ASN A 34 64.085 13.647 18.538 1.00 72.27 O ANISOU 205 OD1 ASN A 34 10285 7395 9781 506 1891 126 O ATOM 206 ND2 ASN A 34 63.166 15.549 17.813 1.00 61.95 N ANISOU 206 ND2 ASN A 34 8885 6193 8458 89 1675 -100 N ATOM 207 N LEU A 35 68.441 15.082 19.457 1.00 42.12 N ANISOU 207 N LEU A 35 5850 4608 5547 923 1568 376 N ATOM 208 CA LEU A 35 69.703 15.777 19.237 1.00 47.03 C ANISOU 208 CA LEU A 35 6247 5560 6062 942 1435 408 C ATOM 209 C LEU A 35 69.540 16.705 18.038 1.00 47.44 C ANISOU 209 C LEU A 35 6245 5650 6129 684 1346 216 C ATOM 210 O LEU A 35 69.078 16.284 16.972 1.00 51.87 O ANISOU 210 O LEU A 35 6906 6000 6801 621 1461 90 O ATOM 211 CB LEU A 35 70.827 14.774 18.981 1.00 48.05 C ANISOU 211 CB LEU A 35 6305 5747 6206 1226 1568 530 C ATOM 212 CG LEU A 35 72.284 15.239 19.040 1.00 53.06 C ANISOU 212 CG LEU A 35 6678 6755 6729 1322 1453 646 C ATOM 213 CD1 LEU A 35 72.661 15.565 20.453 1.00 48.27 C ANISOU 213 CD1 LEU A 35 5992 6348 6000 1393 1314 816 C ATOM 214 CD2 LEU A 35 73.218 14.177 18.488 1.00 52.31 C ANISOU 214 CD2 LEU A 35 6532 6666 6677 1603 1631 738 C ATOM 215 N ALA A 36 69.893 17.972 18.218 1.00 44.41 N ANISOU 215 N ALA A 36 5721 5523 5628 524 1132 194 N ATOM 216 CA ALA A 36 69.790 18.980 17.170 1.00 43.62 C ANISOU 216 CA ALA A 36 5563 5487 5524 268 1020 23 C ATOM 217 C ALA A 36 71.191 19.453 16.769 1.00 48.93 C ANISOU 217 C ALA A 36 6001 6485 6107 295 917 81 C ATOM 218 O ALA A 36 71.978 19.875 17.627 1.00 48.45 O ANISOU 218 O ALA A 36 5805 6681 5923 351 778 223 O ATOM 219 CB ALA A 36 68.931 20.146 17.662 1.00 37.67 C ANISOU 219 CB ALA A 36 4865 4744 4705 34 849 -60 C ATOM 220 N SER A 37 71.494 19.405 15.467 1.00 41.83 N ANISOU 220 N SER A 37 5053 5577 5263 245 979 -20 N ATOM 221 CA SER A 37 72.852 19.601 14.979 1.00 46.81 C ANISOU 221 CA SER A 37 5454 6499 5831 316 938 59 C ATOM 222 C SER A 37 72.929 20.637 13.859 1.00 48.89 C ANISOU 222 C SER A 37 5637 6865 6074 55 823 -95 C ATOM 223 O SER A 37 72.096 20.671 12.946 1.00 42.13 O ANISOU 223 O SER A 37 4919 5788 5302 -93 883 -276 O ATOM 224 CB SER A 37 73.459 18.287 14.487 1.00 49.46 C ANISOU 224 CB SER A 37 5791 6761 6241 606 1175 138 C ATOM 225 OG SER A 37 73.595 17.375 15.559 1.00 47.51 O ANISOU 225 OG SER A 37 5588 6467 5995 862 1264 308 O ATOM 226 N HIS A 38 73.949 21.485 13.954 1.00 41.73 N ANISOU 226 N HIS A 38 4505 6300 5050 -8 645 -10 N ATOM 227 CA HIS A 38 74.315 22.421 12.903 1.00 45.92 C ANISOU 227 CA HIS A 38 4916 6985 5546 -224 536 -113 C ATOM 228 C HIS A 38 75.495 21.833 12.132 1.00 43.88 C ANISOU 228 C HIS A 38 4478 6893 5302 -35 667 -16 C ATOM 229 O HIS A 38 76.586 21.702 12.690 1.00 38.54 O ANISOU 229 O HIS A 38 3600 6486 4557 126 630 189 O ATOM 230 CB HIS A 38 74.704 23.759 13.515 1.00 40.02 C ANISOU 230 CB HIS A 38 4040 6513 4650 -429 244 -67 C ATOM 231 CG HIS A 38 75.080 24.777 12.491 1.00 52.47 C ANISOU 231 CG HIS A 38 5498 8255 6182 -671 113 -163 C ATOM 232 ND1 HIS A 38 75.611 26.004 12.814 1.00 53.60 N ANISOU 232 ND1 HIS A 38 5511 8669 6186 -874 -157 -117 N ATOM 233 CD2 HIS A 38 74.965 24.758 11.144 1.00 51.57 C ANISOU 233 CD2 HIS A 38 5395 8059 6140 -753 210 -305 C ATOM 234 CE1 HIS A 38 75.821 26.691 11.709 1.00 49.99 C ANISOU 234 CE1 HIS A 38 4977 8296 5721 -1069 -217 -221 C ATOM 235 NE2 HIS A 38 75.425 25.962 10.684 1.00 50.02 N ANISOU 235 NE2 HIS A 38 5064 8090 5850 -998 5 -339 N ATOM 236 N TYR A 39 75.284 21.469 10.864 1.00 47.15 N ANISOU 236 N TYR A 39 4967 7149 5799 -46 822 -152 N ATOM 237 CA TYR A 39 76.347 20.939 10.005 1.00 44.39 C ANISOU 237 CA TYR A 39 4470 6941 5455 139 970 -77 C ATOM 238 C TYR A 39 76.870 22.048 9.108 1.00 49.83 C ANISOU 238 C TYR A 39 4986 7868 6079 -94 829 -137 C ATOM 239 O TYR A 39 76.115 22.585 8.294 1.00 49.31 O ANISOU 239 O TYR A 39 5045 7649 6042 -332 792 -340 O ATOM 240 CB TYR A 39 75.862 19.797 9.110 1.00 47.21 C ANISOU 240 CB TYR A 39 5045 6969 5925 289 1240 -185 C ATOM 241 CG TYR A 39 75.783 18.426 9.729 1.00 38.81 C ANISOU 241 CG TYR A 39 4114 5713 4921 606 1441 -78 C ATOM 242 CD1 TYR A 39 74.953 18.177 10.815 1.00 39.57 C ANISOU 242 CD1 TYR A 39 4355 5633 5045 606 1409 -60 C ATOM 243 CD2 TYR A 39 76.484 17.370 9.189 1.00 43.52 C ANISOU 243 CD2 TYR A 39 4712 6282 5541 906 1671 0 C ATOM 244 CE1 TYR A 39 74.859 16.928 11.364 1.00 40.55 C ANISOU 244 CE1 TYR A 39 4612 5573 5222 883 1588 38 C ATOM 245 CE2 TYR A 39 76.396 16.112 9.723 1.00 46.59 C ANISOU 245 CE2 TYR A 39 5246 6475 5980 1195 1853 93 C ATOM 246 CZ TYR A 39 75.583 15.893 10.811 1.00 47.71 C ANISOU 246 CZ TYR A 39 5524 6450 6152 1175 1806 113 C ATOM 247 OH TYR A 39 75.497 14.635 11.347 1.00 55.04 O ANISOU 247 OH TYR A 39 6605 7180 7129 1456 1984 211 O ATOM 248 N GLN A 40 78.146 22.327 9.182 1.00 53.60 N ANISOU 248 N GLN A 40 5180 8710 6476 -21 763 44 N ATOM 249 CA GLN A 40 78.735 23.322 8.344 1.00 53.00 C ANISOU 249 CA GLN A 40 4921 8880 6336 -230 637 16 C ATOM 250 C GLN A 40 79.482 22.588 7.266 1.00 56.09 C ANISOU 250 C GLN A 40 5228 9322 6763 -17 872 55 C ATOM 251 O GLN A 40 80.240 21.729 7.542 1.00 57.35 O ANISOU 251 O GLN A 40 5282 9580 6930 290 1018 234 O ATOM 252 CB GLN A 40 79.686 24.119 9.178 1.00 71.31 C ANISOU 252 CB GLN A 40 6972 11587 8537 -299 398 217 C ATOM 253 CG GLN A 40 79.107 25.354 9.792 1.00 84.84 C ANISOU 253 CG GLN A 40 8747 13318 10169 -623 106 136 C ATOM 254 CD GLN A 40 80.066 26.515 9.798 1.00103.57 C ANISOU 254 CD GLN A 40 10861 16076 12415 -832 -151 250 C ATOM 255 OE1 GLN A 40 80.670 26.781 10.806 1.00114.29 O ANISOU 255 OE1 GLN A 40 12085 17656 13684 -817 -316 434 O ATOM 256 NE2 GLN A 40 80.203 27.206 8.692 1.00106.44 N ANISOU 256 NE2 GLN A 40 11243 16435 12765 -1006 -187 144 N ATOM 257 N THR A 41 79.251 22.921 6.019 1.00 54.49 N ANISOU 257 N THR A 41 5083 9044 6577 -170 914 -113 N ATOM 258 CA THR A 41 79.906 22.263 4.891 1.00 61.07 C ANISOU 258 CA THR A 41 5870 9905 7430 27 1150 -95 C ATOM 259 C THR A 41 80.452 23.309 3.919 1.00 66.87 C ANISOU 259 C THR A 41 6420 10889 8096 -205 1039 -130 C ATOM 260 O THR A 41 80.211 24.509 4.063 1.00 68.26 O ANISOU 260 O THR A 41 6545 11172 8220 -531 781 -193 O ATOM 261 CB THR A 41 78.948 21.301 4.149 1.00 62.05 C ANISOU 261 CB THR A 41 6337 9588 7651 119 1384 -290 C ATOM 262 OG1 THR A 41 78.102 22.039 3.266 1.00 58.59 O ANISOU 262 OG1 THR A 41 6048 8987 7227 -201 1298 -528 O ATOM 263 CG2 THR A 41 78.067 20.509 5.122 1.00 49.24 C ANISOU 263 CG2 THR A 41 4943 7667 6101 231 1435 -302 C ATOM 264 N ASP A 42 81.204 22.844 2.911 1.00 67.90 N ANISOU 264 N ASP A 42 6464 11114 8222 -26 1241 -85 N ATOM 265 CA ASP A 42 81.678 23.751 1.864 1.00 65.70 C ANISOU 265 CA ASP A 42 6032 11048 7883 -237 1169 -127 C ATOM 266 C ASP A 42 80.561 24.183 0.925 1.00 67.37 C ANISOU 266 C ASP A 42 6515 10956 8127 -512 1143 -421 C ATOM 267 O ASP A 42 80.808 24.989 0.031 1.00 68.76 O ANISOU 267 O ASP A 42 6603 11270 8254 -719 1071 -483 O ATOM 268 CB ASP A 42 82.839 23.136 1.063 1.00 67.05 C ANISOU 268 CB ASP A 42 6021 11426 8028 53 1408 24 C ATOM 269 CG ASP A 42 82.487 21.805 0.411 1.00 80.26 C ANISOU 269 CG ASP A 42 7974 12756 9765 354 1738 -72 C ATOM 270 OD1 ASP A 42 81.706 21.031 0.990 1.00 85.16 O ANISOU 270 OD1 ASP A 42 8843 13060 10454 465 1807 -136 O ATOM 271 OD2 ASP A 42 83.023 21.512 -0.682 1.00 87.05 O ANISOU 271 OD2 ASP A 42 8812 13666 10598 487 1933 -72 O ATOM 272 N ALA A 43 79.347 23.664 1.095 1.00 67.15 N ANISOU 272 N ALA A 43 6807 10524 8181 -523 1199 -591 N ATOM 273 CA ALA A 43 78.191 24.088 0.317 1.00 58.04 C ANISOU 273 CA ALA A 43 5909 9077 7066 -799 1149 -858 C ATOM 274 C ALA A 43 77.156 24.813 1.176 1.00 58.91 C ANISOU 274 C ALA A 43 6122 9066 7196 -1058 914 -951 C ATOM 275 O ALA A 43 75.980 24.884 0.800 1.00 67.67 O ANISOU 275 O ALA A 43 7482 9863 8366 -1228 901 -1155 O ATOM 276 CB ALA A 43 77.557 22.882 -0.371 1.00 56.24 C ANISOU 276 CB ALA A 43 5990 8460 6919 -620 1412 -986 C ATOM 277 N GLY A 44 77.562 25.345 2.324 1.00 62.56 N ANISOU 277 N GLY A 44 6720 8904 8145 -807 1847 618 N ATOM 278 CA GLY A 44 76.638 25.992 3.235 1.00 55.92 C ANISOU 278 CA GLY A 44 6057 7882 7309 -839 1635 684 C ATOM 279 C GLY A 44 76.159 25.073 4.343 1.00 56.30 C ANISOU 279 C GLY A 44 6102 7874 7415 -710 1388 563 C ATOM 280 O GLY A 44 76.589 23.924 4.478 1.00 61.69 O ANISOU 280 O GLY A 44 6646 8624 8170 -595 1354 442 O ATOM 281 N SER A 45 75.221 25.594 5.135 1.00 48.27 N ANISOU 281 N SER A 45 5249 6727 6366 -727 1218 602 N ATOM 282 CA SER A 45 74.805 24.926 6.364 1.00 45.86 C ANISOU 282 CA SER A 45 4942 6372 6110 -652 988 519 C ATOM 283 C SER A 45 73.619 23.997 6.143 1.00 41.44 C ANISOU 283 C SER A 45 4539 5824 5384 -505 920 485 C ATOM 284 O SER A 45 72.838 24.162 5.207 1.00 51.37 O ANISOU 284 O SER A 45 5947 7103 6467 -471 1002 529 O ATOM 285 CB SER A 45 74.440 25.955 7.431 1.00 49.17 C ANISOU 285 CB SER A 45 5435 6670 6578 -753 851 546 C ATOM 286 OG SER A 45 75.597 26.631 7.869 1.00 50.95 O ANISOU 286 OG SER A 45 5486 6877 6994 -897 862 538 O ATOM 287 N PHE A 46 73.485 23.013 7.039 1.00 47.60 N ANISOU 287 N PHE A 46 5277 6588 6219 -428 756 415 N ATOM 288 CA PHE A 46 72.282 22.182 7.127 1.00 42.46 C ANISOU 288 CA PHE A 46 4769 5918 5445 -329 660 388 C ATOM 289 C PHE A 46 71.887 21.977 8.585 1.00 44.97 C ANISOU 289 C PHE A 46 5104 6181 5801 -342 458 389 C ATOM 290 O PHE A 46 72.735 21.973 9.481 1.00 45.11 O ANISOU 290 O PHE A 46 4994 6197 5949 -380 368 383 O ATOM 291 CB PHE A 46 72.466 20.810 6.457 1.00 43.47 C ANISOU 291 CB PHE A 46 4847 6086 5584 -206 699 299 C ATOM 292 CG PHE A 46 72.732 20.892 4.996 1.00 47.90 C ANISOU 292 CG PHE A 46 5409 6740 6050 -183 905 271 C ATOM 293 CD1 PHE A 46 71.700 21.097 4.101 1.00 55.04 C ANISOU 293 CD1 PHE A 46 6489 7682 6741 -165 957 291 C ATOM 294 CD2 PHE A 46 74.023 20.785 4.513 1.00 53.17 C ANISOU 294 CD2 PHE A 46 5891 7481 6829 -181 1048 226 C ATOM 295 CE1 PHE A 46 71.955 21.180 2.737 1.00 52.29 C ANISOU 295 CE1 PHE A 46 6157 7452 6258 -148 1145 274 C ATOM 296 CE2 PHE A 46 74.290 20.874 3.151 1.00 52.66 C ANISOU 296 CE2 PHE A 46 5830 7539 6641 -171 1265 199 C ATOM 297 CZ PHE A 46 73.250 21.067 2.266 1.00 51.46 C ANISOU 297 CZ PHE A 46 5880 7431 6242 -156 1310 228 C ATOM 298 N PHE A 47 70.582 21.824 8.815 1.00 39.25 N ANISOU 298 N PHE A 47 4531 5435 4947 -316 388 398 N ATOM 299 CA PHE A 47 70.045 21.569 10.139 1.00 40.83 C ANISOU 299 CA PHE A 47 4765 5614 5133 -335 226 406 C ATOM 300 C PHE A 47 69.548 20.127 10.200 1.00 43.30 C ANISOU 300 C PHE A 47 5103 5914 5436 -258 157 393 C ATOM 301 O PHE A 47 68.821 19.660 9.317 1.00 43.29 O ANISOU 301 O PHE A 47 5174 5912 5361 -206 214 362 O ATOM 302 CB PHE A 47 68.931 22.563 10.509 1.00 42.35 C ANISOU 302 CB PHE A 47 5086 5795 5209 -379 208 419 C ATOM 303 CG PHE A 47 68.398 22.348 11.886 1.00 48.91 C ANISOU 303 CG PHE A 47 5944 6643 5995 -409 72 414 C ATOM 304 CD1 PHE A 47 69.160 22.687 12.995 1.00 53.77 C ANISOU 304 CD1 PHE A 47 6492 7274 6665 -476 -22 404 C ATOM 305 CD2 PHE A 47 67.157 21.760 12.087 1.00 46.90 C ANISOU 305 CD2 PHE A 47 5774 6412 5633 -382 36 417 C ATOM 306 CE1 PHE A 47 68.692 22.446 14.289 1.00 49.71 C ANISOU 306 CE1 PHE A 47 6013 6810 6064 -508 -145 405 C ATOM 307 CE2 PHE A 47 66.688 21.522 13.361 1.00 44.67 C ANISOU 307 CE2 PHE A 47 5514 6172 5287 -424 -65 426 C ATOM 308 CZ PHE A 47 67.458 21.858 14.468 1.00 46.79 C ANISOU 308 CZ PHE A 47 5734 6469 5575 -484 -153 425 C ATOM 309 N VAL A 48 69.974 19.418 11.220 1.00 36.63 N ANISOU 309 N VAL A 48 4198 5049 4669 -254 26 419 N ATOM 310 CA VAL A 48 69.741 17.992 11.337 1.00 45.27 C ANISOU 310 CA VAL A 48 5306 6086 5810 -187 -49 429 C ATOM 311 C VAL A 48 69.226 17.693 12.737 1.00 49.58 C ANISOU 311 C VAL A 48 5906 6633 6299 -242 -202 514 C ATOM 312 O VAL A 48 69.747 18.225 13.726 1.00 48.33 O ANISOU 312 O VAL A 48 5703 6524 6135 -294 -288 550 O ATOM 313 CB VAL A 48 71.034 17.213 11.068 1.00 44.92 C ANISOU 313 CB VAL A 48 5113 6001 5955 -99 -58 401 C ATOM 314 CG1 VAL A 48 70.836 15.734 11.329 1.00 40.11 C ANISOU 314 CG1 VAL A 48 4527 5280 5432 -23 -163 424 C ATOM 315 CG2 VAL A 48 71.543 17.489 9.667 1.00 42.00 C ANISOU 315 CG2 VAL A 48 4683 5666 5608 -54 125 309 C ATOM 316 N LYS A 49 68.198 16.849 12.818 1.00 48.55 N ANISOU 316 N LYS A 49 5870 6461 6116 -244 -232 542 N ATOM 317 CA LYS A 49 67.734 16.280 14.080 1.00 45.70 C ANISOU 317 CA LYS A 49 5563 6100 5703 -301 -360 650 C ATOM 318 C LYS A 49 67.787 14.765 14.007 1.00 43.61 C ANISOU 318 C LYS A 49 5309 5696 5566 -249 -430 704 C ATOM 319 O LYS A 49 67.449 14.166 12.980 1.00 47.31 O ANISOU 319 O LYS A 49 5796 6082 6098 -201 -362 625 O ATOM 320 CB LYS A 49 66.325 16.748 14.428 1.00 48.22 C ANISOU 320 CB LYS A 49 5980 6497 5844 -387 -323 651 C ATOM 321 CG LYS A 49 66.283 18.203 14.737 1.00 49.01 C ANISOU 321 CG LYS A 49 6078 6700 5843 -428 -282 599 C ATOM 322 CD LYS A 49 64.955 18.629 15.332 1.00 44.91 C ANISOU 322 CD LYS A 49 5631 6272 5161 -496 -258 590 C ATOM 323 CE LYS A 49 63.885 18.790 14.266 1.00 48.02 C ANISOU 323 CE LYS A 49 6056 6660 5530 -465 -158 523 C ATOM 324 NZ LYS A 49 62.592 19.266 14.837 1.00 55.90 N ANISOU 324 NZ LYS A 49 7084 7760 6394 -514 -129 496 N ATOM 325 N THR A 50 68.256 14.151 15.084 1.00 44.38 N ANISOU 325 N THR A 50 5397 5760 5706 -254 -578 837 N ATOM 326 CA THR A 50 68.332 12.701 15.183 1.00 47.44 C ANISOU 326 CA THR A 50 5809 5975 6242 -204 -671 924 C ATOM 327 C THR A 50 67.684 12.256 16.486 1.00 53.71 C ANISOU 327 C THR A 50 6703 6785 6919 -312 -784 1115 C ATOM 328 O THR A 50 67.605 13.012 17.459 1.00 49.72 O ANISOU 328 O THR A 50 6215 6443 6234 -393 -822 1175 O ATOM 329 CB THR A 50 69.799 12.154 15.117 1.00 45.42 C ANISOU 329 CB THR A 50 5425 5623 6212 -61 -764 933 C ATOM 330 OG1 THR A 50 70.625 12.842 16.059 1.00 50.82 O ANISOU 330 OG1 THR A 50 6028 6435 6847 -77 -869 1002 O ATOM 331 CG2 THR A 50 70.375 12.327 13.772 1.00 44.68 C ANISOU 331 CG2 THR A 50 5231 5509 6237 41 -626 747 C ATOM 332 N ASN A 51 67.180 11.032 16.480 1.00 53.53 N ANISOU 332 N ASN A 51 6755 6593 6991 -326 -826 1203 N ATOM 333 CA ASN A 51 66.722 10.410 17.719 1.00 61.46 C ANISOU 333 CA ASN A 51 7857 7587 7909 -432 -937 1433 C ATOM 334 C ASN A 51 66.949 8.916 17.561 1.00 69.50 C ANISOU 334 C ASN A 51 8912 8321 9172 -370 -1035 1537 C ATOM 335 O ASN A 51 66.310 8.285 16.711 1.00 68.02 O ANISOU 335 O ASN A 51 8761 7982 9102 -382 -960 1444 O ATOM 336 CB ASN A 51 65.268 10.719 18.013 1.00 57.90 C ANISOU 336 CB ASN A 51 7488 7260 7250 -600 -833 1445 C ATOM 337 CG ASN A 51 64.898 10.331 19.413 1.00 67.37 C ANISOU 337 CG ASN A 51 8777 8526 8294 -728 -920 1687 C ATOM 338 OD1 ASN A 51 65.165 9.198 19.833 1.00 73.60 O ANISOU 338 OD1 ASN A 51 9624 9140 9201 -727 -1042 1883 O ATOM 339 ND2 ASN A 51 64.296 11.265 20.163 1.00 58.03 N ANISOU 339 ND2 ASN A 51 7611 7595 6842 -836 -857 1680 N ATOM 340 N ARG A 52 67.849 8.360 18.380 1.00 73.35 N ANISOU 340 N ARG A 52 9393 8731 9745 -301 -1215 1723 N ATOM 341 CA ARG A 52 68.263 6.969 18.236 1.00 85.96 C ANISOU 341 CA ARG A 52 11016 10018 11628 -199 -1333 1824 C ATOM 342 C ARG A 52 67.191 5.989 18.688 1.00 95.17 C ANISOU 342 C ARG A 52 12342 11026 12792 -353 -1353 2017 C ATOM 343 O ARG A 52 67.297 4.800 18.369 1.00 98.59 O ANISOU 343 O ARG A 52 12817 11146 13495 -291 -1422 2064 O ATOM 344 CB ARG A 52 69.558 6.713 19.020 1.00 94.18 C ANISOU 344 CB ARG A 52 11988 11030 12765 -63 -1546 1988 C ATOM 345 CG ARG A 52 70.804 7.402 18.456 1.00105.63 C ANISOU 345 CG ARG A 52 13238 12573 14322 106 -1538 1793 C ATOM 346 CD ARG A 52 72.037 7.206 19.356 1.00118.50 C ANISOU 346 CD ARG A 52 14773 14216 16034 228 -1777 1961 C ATOM 347 NE ARG A 52 73.161 8.066 18.967 1.00126.56 N ANISOU 347 NE ARG A 52 15577 15392 17119 337 -1758 1777 N ATOM 348 CZ ARG A 52 74.359 8.069 19.556 1.00129.69 C ANISOU 348 CZ ARG A 52 15824 15840 17614 456 -1953 1855 C ATOM 349 NH1 ARG A 52 74.612 7.254 20.572 1.00131.74 N ANISOU 349 NH1 ARG A 52 16142 16009 17905 504 -2203 2129 N ATOM 350 NH2 ARG A 52 75.310 8.891 19.128 1.00126.75 N ANISOU 350 NH2 ARG A 52 15235 15614 17310 521 -1906 1669 N ATOM 351 N SER A 53 66.157 6.455 19.394 1.00 96.63 N ANISOU 351 N SER A 53 12607 11411 12698 -554 -1285 2115 N ATOM 352 CA SER A 53 65.167 5.547 19.955 1.00101.36 C ANISOU 352 CA SER A 53 13343 11890 13280 -733 -1295 2333 C ATOM 353 C SER A 53 63.967 5.310 19.046 1.00102.61 C ANISOU 353 C SER A 53 13515 11973 13500 -849 -1135 2166 C ATOM 354 O SER A 53 63.408 4.207 19.067 1.00 94.73 O ANISOU 354 O SER A 53 12604 10731 12657 -950 -1160 2288 O ATOM 355 CB SER A 53 64.656 6.091 21.297 1.00104.26 C ANISOU 355 CB SER A 53 13777 12542 13295 -905 -1294 2539 C ATOM 356 OG SER A 53 63.753 7.185 21.132 1.00100.63 O ANISOU 356 OG SER A 53 13273 12358 12602 -1011 -1110 2354 O ATOM 357 N ILE A 54 63.614 6.284 18.197 1.00102.90 N ANISOU 357 N ILE A 54 13465 12190 13443 -829 -988 1891 N ATOM 358 CA ILE A 54 62.318 6.344 17.521 1.00 97.47 C ANISOU 358 CA ILE A 54 12772 11540 12721 -961 -846 1742 C ATOM 359 C ILE A 54 62.463 5.970 16.053 1.00 99.39 C ANISOU 359 C ILE A 54 12973 11603 13189 -844 -813 1480 C ATOM 360 O ILE A 54 63.472 6.294 15.417 1.00103.93 O ANISOU 360 O ILE A 54 13483 12166 13839 -657 -822 1337 O ATOM 361 CB ILE A 54 61.691 7.744 17.621 1.00 83.53 C ANISOU 361 CB ILE A 54 10946 10120 10672 -1015 -717 1626 C ATOM 362 CG1 ILE A 54 61.545 8.195 19.068 1.00 82.51 C ANISOU 362 CG1 ILE A 54 10857 10207 10288 -1125 -732 1833 C ATOM 363 CG2 ILE A 54 60.333 7.747 16.981 1.00 84.28 C ANISOU 363 CG2 ILE A 54 11013 10262 10747 -1140 -597 1492 C ATOM 364 CD1 ILE A 54 60.791 9.539 19.168 1.00 77.94 C ANISOU 364 CD1 ILE A 54 10215 9941 9457 -1175 -593 1687 C ATOM 365 N GLY A 55 61.457 5.263 15.526 1.00 92.14 N ANISOU 365 N GLY A 55 12084 10555 12372 -967 -772 1411 N ATOM 366 CA GLY A 55 61.342 4.992 14.112 1.00 79.37 C ANISOU 366 CA GLY A 55 10431 8824 10901 -892 -730 1126 C ATOM 367 C GLY A 55 60.916 6.227 13.336 1.00 71.24 C ANISOU 367 C GLY A 55 9320 8083 9665 -861 -611 909 C ATOM 368 O GLY A 55 60.446 7.223 13.902 1.00 72.14 O ANISOU 368 O GLY A 55 9404 8457 9551 -927 -552 970 O ATOM 369 N PRO A 56 61.033 6.158 12.006 1.00 68.03 N ANISOU 369 N PRO A 56 8884 7632 9334 -758 -576 649 N ATOM 370 CA PRO A 56 60.999 7.377 11.172 1.00 61.62 C ANISOU 370 CA PRO A 56 8006 7072 8332 -674 -480 470 C ATOM 371 C PRO A 56 59.640 8.041 10.978 1.00 61.79 C ANISOU 371 C PRO A 56 7994 7308 8175 -796 -419 412 C ATOM 372 O PRO A 56 59.600 9.126 10.384 1.00 63.54 O ANISOU 372 O PRO A 56 8174 7731 8238 -719 -355 306 O ATOM 373 CB PRO A 56 61.559 6.887 9.830 1.00 58.91 C ANISOU 373 CB PRO A 56 7658 6607 8120 -534 -467 226 C ATOM 374 CG PRO A 56 61.351 5.411 9.835 1.00 65.54 C ANISOU 374 CG PRO A 56 8556 7136 9212 -594 -549 215 C ATOM 375 CD PRO A 56 61.507 4.980 11.260 1.00 66.48 C ANISOU 375 CD PRO A 56 8719 7134 9405 -674 -630 518 C ATOM 376 N ALA A 57 58.539 7.474 11.476 1.00 60.29 N ANISOU 376 N ALA A 57 7809 7087 8011 -982 -435 489 N ATOM 377 CA ALA A 57 57.211 8.011 11.169 1.00 59.89 C ANISOU 377 CA ALA A 57 7687 7240 7828 -1085 -384 399 C ATOM 378 C ALA A 57 57.057 9.459 11.611 1.00 55.93 C ANISOU 378 C ALA A 57 7135 7018 7100 -1041 -314 441 C ATOM 379 O ALA A 57 56.445 10.269 10.903 1.00 57.67 O ANISOU 379 O ALA A 57 7294 7411 7206 -998 -278 307 O ATOM 380 CB ALA A 57 56.127 7.153 11.825 1.00 56.60 C ANISOU 380 CB ALA A 57 7258 6755 7492 -1317 -397 505 C ATOM 381 N MET A 58 57.578 9.807 12.785 1.00 55.11 N ANISOU 381 N MET A 58 7057 6955 6927 -1048 -307 623 N ATOM 382 CA MET A 58 57.406 11.174 13.271 1.00 54.89 C ANISOU 382 CA MET A 58 6986 7170 6700 -1014 -242 635 C ATOM 383 C MET A 58 58.145 12.184 12.377 1.00 53.44 C ANISOU 383 C MET A 58 6795 7043 6467 -833 -221 507 C ATOM 384 O MET A 58 57.561 13.194 11.960 1.00 59.04 O ANISOU 384 O MET A 58 7458 7911 7063 -791 -173 417 O ATOM 385 CB MET A 58 57.850 11.277 14.738 1.00 54.97 C ANISOU 385 CB MET A 58 7035 7222 6630 -1070 -252 835 C ATOM 386 CG MET A 58 57.886 12.720 15.264 1.00 76.85 C ANISOU 386 CG MET A 58 9775 10215 9210 -1016 -194 810 C ATOM 387 SD MET A 58 58.731 13.022 16.852 1.00 95.91 S ANISOU 387 SD MET A 58 12243 12705 11494 -1044 -231 987 S ATOM 388 CE MET A 58 60.468 13.022 16.399 1.00 86.56 C ANISOU 388 CE MET A 58 11084 11364 10439 -880 -326 980 C ATOM 389 N PHE A 59 59.425 11.925 12.047 1.00 52.32 N ANISOU 389 N PHE A 59 6691 6768 6419 -725 -254 503 N ATOM 390 CA PHE A 59 60.164 12.868 11.197 1.00 50.85 C ANISOU 390 CA PHE A 59 6492 6645 6185 -581 -211 400 C ATOM 391 C PHE A 59 59.601 12.919 9.785 1.00 48.15 C ANISOU 391 C PHE A 59 6140 6338 5815 -534 -182 231 C ATOM 392 O PHE A 59 59.553 13.997 9.184 1.00 54.44 O ANISOU 392 O PHE A 59 6926 7262 6497 -461 -134 177 O ATOM 393 CB PHE A 59 61.659 12.516 11.119 1.00 53.20 C ANISOU 393 CB PHE A 59 6796 6814 6603 -481 -237 419 C ATOM 394 CG PHE A 59 62.440 12.891 12.350 1.00 51.46 C ANISOU 394 CG PHE A 59 6569 6617 6367 -488 -277 565 C ATOM 395 CD1 PHE A 59 62.130 14.038 13.057 1.00 46.79 C ANISOU 395 CD1 PHE A 59 5969 6190 5620 -529 -248 604 C ATOM 396 CD2 PHE A 59 63.502 12.106 12.780 1.00 61.46 C ANISOU 396 CD2 PHE A 59 7832 7742 7778 -442 -357 648 C ATOM 397 CE1 PHE A 59 62.840 14.385 14.211 1.00 49.35 C ANISOU 397 CE1 PHE A 59 6289 6555 5906 -546 -300 712 C ATOM 398 CE2 PHE A 59 64.225 12.450 13.916 1.00 52.64 C ANISOU 398 CE2 PHE A 59 6701 6671 6628 -449 -424 781 C ATOM 399 CZ PHE A 59 63.885 13.591 14.631 1.00 45.02 C ANISOU 399 CZ PHE A 59 5736 5890 5481 -511 -395 805 C ATOM 400 N GLU A 60 59.115 11.792 9.262 1.00 50.47 N ANISOU 400 N GLU A 60 6444 6525 6207 -584 -223 150 N ATOM 401 CA GLU A 60 58.520 11.807 7.929 1.00 55.14 C ANISOU 401 CA GLU A 60 7027 7181 6743 -549 -218 -29 C ATOM 402 C GLU A 60 57.269 12.680 7.904 1.00 53.37 C ANISOU 402 C GLU A 60 6747 7154 6377 -589 -212 -37 C ATOM 403 O GLU A 60 57.059 13.449 6.957 1.00 56.18 O ANISOU 403 O GLU A 60 7099 7638 6610 -501 -200 -119 O ATOM 404 CB GLU A 60 58.225 10.378 7.474 1.00 57.59 C ANISOU 404 CB GLU A 60 7356 7320 7205 -614 -278 -139 C ATOM 405 CG GLU A 60 59.514 9.627 7.097 1.00 70.43 C ANISOU 405 CG GLU A 60 9027 8758 8976 -509 -277 -201 C ATOM 406 CD GLU A 60 59.349 8.118 6.933 1.00 77.75 C ANISOU 406 CD GLU A 60 9987 9438 10116 -572 -346 -291 C ATOM 407 OE1 GLU A 60 58.214 7.602 7.058 1.00 76.38 O ANISOU 407 OE1 GLU A 60 9802 9237 9982 -725 -395 -307 O ATOM 408 OE2 GLU A 60 60.378 7.442 6.694 1.00 83.45 O ANISOU 408 OE2 GLU A 60 10736 9983 10991 -469 -350 -351 O ATOM 409 N GLY A 61 56.466 12.630 8.968 1.00 47.39 N ANISOU 409 N GLY A 61 5943 6436 5627 -710 -216 60 N ATOM 410 CA GLY A 61 55.312 13.519 9.049 1.00 46.85 C ANISOU 410 CA GLY A 61 5792 6563 5445 -725 -200 43 C ATOM 411 C GLY A 61 55.712 14.979 9.159 1.00 47.08 C ANISOU 411 C GLY A 61 5831 6699 5357 -601 -151 81 C ATOM 412 O GLY A 61 55.088 15.851 8.545 1.00 51.57 O ANISOU 412 O GLY A 61 6362 7394 5839 -524 -154 23 O ATOM 413 N GLU A 62 56.778 15.261 9.914 1.00 46.85 N ANISOU 413 N GLU A 62 5854 6608 5338 -579 -119 179 N ATOM 414 CA GLU A 62 57.313 16.619 9.989 1.00 45.38 C ANISOU 414 CA GLU A 62 5687 6481 5074 -477 -76 202 C ATOM 415 C GLU A 62 57.764 17.126 8.617 1.00 48.34 C ANISOU 415 C GLU A 62 6099 6857 5409 -357 -65 138 C ATOM 416 O GLU A 62 57.499 18.279 8.250 1.00 48.90 O ANISOU 416 O GLU A 62 6172 7005 5402 -279 -46 136 O ATOM 417 CB GLU A 62 58.485 16.667 10.990 1.00 43.72 C ANISOU 417 CB GLU A 62 5513 6200 4898 -493 -67 299 C ATOM 418 CG GLU A 62 59.071 18.086 11.140 1.00 53.48 C ANISOU 418 CG GLU A 62 6763 7477 6079 -418 -27 307 C ATOM 419 CD GLU A 62 60.148 18.220 12.225 1.00 63.51 C ANISOU 419 CD GLU A 62 8048 8711 7372 -448 -41 382 C ATOM 420 OE1 GLU A 62 60.520 17.208 12.845 1.00 64.73 O ANISOU 420 OE1 GLU A 62 8209 8809 7578 -508 -89 452 O ATOM 421 OE2 GLU A 62 60.603 19.360 12.477 1.00 62.65 O ANISOU 421 OE2 GLU A 62 7945 8624 7236 -415 -17 373 O ATOM 422 N ALA A 63 58.487 16.289 7.860 1.00 44.43 N ANISOU 422 N ALA A 63 5640 6274 4966 -337 -71 91 N ATOM 423 CA ALA A 63 58.987 16.711 6.555 1.00 43.96 C ANISOU 423 CA ALA A 63 5621 6247 4834 -236 -36 34 C ATOM 424 C ALA A 63 57.841 17.023 5.594 1.00 50.93 C ANISOU 424 C ALA A 63 6497 7255 5598 -201 -78 -36 C ATOM 425 O ALA A 63 57.883 18.025 4.867 1.00 47.62 O ANISOU 425 O ALA A 63 6113 6914 5068 -114 -57 -11 O ATOM 426 CB ALA A 63 59.908 15.636 5.965 1.00 43.64 C ANISOU 426 CB ALA A 63 5604 6105 4871 -217 -22 -41 C ATOM 427 N LEU A 64 56.812 16.170 5.562 1.00 49.82 N ANISOU 427 N LEU A 64 6309 7136 5487 -273 -149 -116 N ATOM 428 CA LEU A 64 55.685 16.443 4.672 1.00 54.75 C ANISOU 428 CA LEU A 64 6898 7901 6002 -240 -219 -192 C ATOM 429 C LEU A 64 54.883 17.657 5.132 1.00 51.68 C ANISOU 429 C LEU A 64 6452 7616 5568 -193 -227 -118 C ATOM 430 O LEU A 64 54.338 18.383 4.294 1.00 48.72 O ANISOU 430 O LEU A 64 6075 7352 5085 -97 -277 -128 O ATOM 431 CB LEU A 64 54.777 15.219 4.553 1.00 58.08 C ANISOU 431 CB LEU A 64 7257 8318 6495 -351 -299 -313 C ATOM 432 CG LEU A 64 55.335 14.013 3.791 1.00 58.92 C ANISOU 432 CG LEU A 64 7421 8319 6647 -374 -316 -448 C ATOM 433 CD1 LEU A 64 54.412 12.830 3.928 1.00 62.94 C ANISOU 433 CD1 LEU A 64 7865 8774 7277 -519 -397 -553 C ATOM 434 CD2 LEU A 64 55.566 14.334 2.321 1.00 50.33 C ANISOU 434 CD2 LEU A 64 6397 7347 5381 -262 -328 -549 C ATOM 435 N GLY A 65 54.811 17.903 6.446 1.00 47.81 N ANISOU 435 N GLY A 65 5919 7095 5152 -247 -185 -48 N ATOM 436 CA GLY A 65 54.169 19.122 6.920 1.00 44.97 C ANISOU 436 CA GLY A 65 5507 6816 4763 -181 -175 -8 C ATOM 437 C GLY A 65 54.919 20.365 6.480 1.00 49.51 C ANISOU 437 C GLY A 65 6173 7355 5283 -56 -142 63 C ATOM 438 O GLY A 65 54.328 21.319 5.964 1.00 51.26 O ANISOU 438 O GLY A 65 6386 7637 5453 54 -180 78 O ATOM 439 N LEU A 66 56.240 20.361 6.666 1.00 44.71 N ANISOU 439 N LEU A 66 5647 6641 4702 -74 -76 116 N ATOM 440 CA LEU A 66 57.052 21.493 6.236 1.00 45.28 C ANISOU 440 CA LEU A 66 5799 6663 4742 8 -29 193 C ATOM 441 C LEU A 66 56.798 21.699 4.755 1.00 47.45 C ANISOU 441 C LEU A 66 6124 7008 4896 95 -64 197 C ATOM 442 O LEU A 66 56.450 22.808 4.333 1.00 56.45 O ANISOU 442 O LEU A 66 7296 8164 5986 190 -85 265 O ATOM 443 CB LEU A 66 58.533 21.277 6.598 1.00 39.37 C ANISOU 443 CB LEU A 66 5092 5811 4055 -44 43 232 C ATOM 444 CG LEU A 66 58.901 21.309 8.084 1.00 42.38 C ANISOU 444 CG LEU A 66 5440 6140 4523 -118 57 250 C ATOM 445 CD1 LEU A 66 60.296 20.766 8.328 1.00 44.56 C ANISOU 445 CD1 LEU A 66 5725 6335 4869 -163 89 276 C ATOM 446 CD2 LEU A 66 58.748 22.729 8.663 1.00 42.88 C ANISOU 446 CD2 LEU A 66 5512 6185 4594 -79 75 274 C ATOM 447 N GLU A 67 56.980 20.643 3.951 1.00 46.70 N ANISOU 447 N GLU A 67 6044 6951 4748 68 -78 124 N ATOM 448 CA GLU A 67 56.819 20.781 2.507 1.00 52.72 C ANISOU 448 CA GLU A 67 6868 7815 5347 143 -111 116 C ATOM 449 C GLU A 67 55.510 21.437 2.079 1.00 55.35 C ANISOU 449 C GLU A 67 7169 8261 5599 229 -227 133 C ATOM 450 O GLU A 67 55.507 22.338 1.226 1.00 53.68 O ANISOU 450 O GLU A 67 7035 8095 5265 327 -245 232 O ATOM 451 CB GLU A 67 57.007 19.428 1.822 1.00 48.41 C ANISOU 451 CB GLU A 67 6328 7303 4762 96 -122 -26 C ATOM 452 CG GLU A 67 56.990 19.521 0.290 1.00 50.04 C ANISOU 452 CG GLU A 67 6614 7648 4752 167 -143 -55 C ATOM 453 CD GLU A 67 58.082 20.470 -0.287 1.00 71.52 C ANISOU 453 CD GLU A 67 9437 10368 7370 220 -21 84 C ATOM 454 OE1 GLU A 67 59.240 20.477 0.195 1.00 74.87 O ANISOU 454 OE1 GLU A 67 9862 10685 7899 181 102 120 O ATOM 455 OE2 GLU A 67 57.785 21.215 -1.245 1.00 76.14 O ANISOU 455 OE2 GLU A 67 10097 11066 7768 294 -52 170 O ATOM 456 N ALA A 68 54.391 21.010 2.676 1.00 46.58 N ANISOU 456 N ALA A 68 5936 7199 4564 194 -306 50 N ATOM 457 CA ALA A 68 53.099 21.622 2.371 1.00 47.52 C ANISOU 457 CA ALA A 68 5977 7435 4642 288 -425 51 C ATOM 458 C ALA A 68 53.090 23.112 2.712 1.00 49.97 C ANISOU 458 C ALA A 68 6316 7680 4989 406 -405 181 C ATOM 459 O ALA A 68 52.621 23.933 1.918 1.00 52.78 O ANISOU 459 O ALA A 68 6703 8089 5261 539 -491 258 O ATOM 460 CB ALA A 68 51.985 20.897 3.126 1.00 47.43 C ANISOU 460 CB ALA A 68 5795 7488 4739 203 -478 -65 C ATOM 461 N MET A 69 53.573 23.483 3.908 1.00 46.33 N ANISOU 461 N MET A 69 5850 7097 4657 363 -306 204 N ATOM 462 CA MET A 69 53.599 24.902 4.266 1.00 48.23 C ANISOU 462 CA MET A 69 6125 7242 4958 468 -286 294 C ATOM 463 C MET A 69 54.571 25.667 3.389 1.00 51.78 C ANISOU 463 C MET A 69 6735 7601 5336 517 -249 441 C ATOM 464 O MET A 69 54.296 26.810 2.988 1.00 54.32 O ANISOU 464 O MET A 69 7111 7869 5658 642 -294 549 O ATOM 465 CB MET A 69 53.938 25.103 5.742 1.00 42.44 C ANISOU 465 CB MET A 69 5355 6416 4355 397 -194 253 C ATOM 466 CG MET A 69 52.897 24.515 6.695 1.00 46.60 C ANISOU 466 CG MET A 69 5720 7050 4936 345 -205 133 C ATOM 467 SD MET A 69 53.317 24.855 8.415 1.00 55.14 S ANISOU 467 SD MET A 69 6784 8062 6106 268 -95 90 S ATOM 468 CE MET A 69 54.918 24.049 8.485 1.00 51.14 C ANISOU 468 CE MET A 69 6392 7459 5581 129 -39 152 C ATOM 469 N TYR A 70 55.699 25.039 3.059 1.00 51.60 N ANISOU 469 N TYR A 70 6786 7560 5260 422 -165 453 N ATOM 470 CA TYR A 70 56.690 25.692 2.216 1.00 53.18 C ANISOU 470 CA TYR A 70 7121 7701 5383 438 -96 594 C ATOM 471 C TYR A 70 56.112 26.053 0.849 1.00 55.68 C ANISOU 471 C TYR A 70 7511 8129 5517 549 -187 687 C ATOM 472 O TYR A 70 56.342 27.159 0.341 1.00 60.85 O ANISOU 472 O TYR A 70 8273 8711 6138 616 -178 861 O ATOM 473 CB TYR A 70 57.908 24.788 2.067 1.00 49.18 C ANISOU 473 CB TYR A 70 6636 7197 4852 327 14 553 C ATOM 474 CG TYR A 70 59.101 25.482 1.467 1.00 47.14 C ANISOU 474 CG TYR A 70 6481 6876 4554 307 132 691 C ATOM 475 CD1 TYR A 70 59.276 25.536 0.098 1.00 41.68 C ANISOU 475 CD1 TYR A 70 5882 6293 3660 343 154 770 C ATOM 476 CD2 TYR A 70 60.040 26.121 2.279 1.00 49.18 C ANISOU 476 CD2 TYR A 70 6739 6982 4967 241 222 742 C ATOM 477 CE1 TYR A 70 60.379 26.188 -0.460 1.00 49.09 C ANISOU 477 CE1 TYR A 70 6907 7190 4554 302 290 914 C ATOM 478 CE2 TYR A 70 61.132 26.781 1.732 1.00 50.40 C ANISOU 478 CE2 TYR A 70 6965 7078 5106 196 341 873 C ATOM 479 CZ TYR A 70 61.297 26.803 0.363 1.00 53.05 C ANISOU 479 CZ TYR A 70 7388 7525 5243 223 386 967 C ATOM 480 OH TYR A 70 62.384 27.431 -0.182 1.00 64.05 O ANISOU 480 OH TYR A 70 8843 8880 6612 157 529 1109 O ATOM 481 N GLU A 71 55.333 25.150 0.251 1.00 50.84 N ANISOU 481 N GLU A 71 6844 7688 4785 563 -289 581 N ATOM 482 CA GLU A 71 54.828 25.378 -1.102 1.00 55.03 C ANISOU 482 CA GLU A 71 7446 8366 5097 661 -397 656 C ATOM 483 C GLU A 71 53.735 26.443 -1.180 1.00 59.06 C ANISOU 483 C GLU A 71 7934 8873 5634 820 -544 761 C ATOM 484 O GLU A 71 53.438 26.906 -2.285 1.00 66.24 O ANISOU 484 O GLU A 71 8931 9876 6360 921 -642 890 O ATOM 485 CB GLU A 71 54.323 24.073 -1.716 1.00 55.12 C ANISOU 485 CB GLU A 71 7399 8566 4978 620 -480 475 C ATOM 486 CG GLU A 71 55.446 23.155 -2.200 1.00 64.86 C ANISOU 486 CG GLU A 71 8703 9827 6116 519 -352 394 C ATOM 487 CD GLU A 71 54.985 21.731 -2.491 1.00 74.55 C ANISOU 487 CD GLU A 71 9857 11168 7299 455 -425 161 C ATOM 488 OE1 GLU A 71 53.801 21.413 -2.242 1.00 81.44 O ANISOU 488 OE1 GLU A 71 10611 12104 8229 460 -570 66 O ATOM 489 OE2 GLU A 71 55.806 20.925 -2.973 1.00 77.12 O ANISOU 489 OE2 GLU A 71 10234 11517 7551 397 -334 58 O ATOM 490 N THR A 72 53.093 26.819 -0.065 1.00 53.54 N ANISOU 490 N THR A 72 7114 8082 5147 857 -568 705 N ATOM 491 CA THR A 72 52.123 27.913 -0.155 1.00 56.86 C ANISOU 491 CA THR A 72 7504 8475 5624 1039 -701 798 C ATOM 492 C THR A 72 52.785 29.244 -0.462 1.00 60.67 C ANISOU 492 C THR A 72 8160 8765 6126 1113 -657 1030 C ATOM 493 O THR A 72 52.090 30.179 -0.870 1.00 59.22 O ANISOU 493 O THR A 72 8000 8543 5957 1287 -787 1159 O ATOM 494 CB THR A 72 51.310 28.085 1.131 1.00 52.85 C ANISOU 494 CB THR A 72 6818 7919 5342 1072 -708 662 C ATOM 495 OG1 THR A 72 52.180 28.497 2.203 1.00 50.01 O ANISOU 495 OG1 THR A 72 6502 7363 5134 993 -551 656 O ATOM 496 CG2 THR A 72 50.540 26.811 1.494 1.00 44.53 C ANISOU 496 CG2 THR A 72 5578 7049 4293 979 -746 456 C ATOM 497 N ARG A 73 54.094 29.369 -0.222 1.00 56.69 N ANISOU 497 N ARG A 73 7765 8123 5651 986 -484 1087 N ATOM 498 CA ARG A 73 54.818 30.605 -0.500 1.00 57.07 C ANISOU 498 CA ARG A 73 7976 7969 5740 1011 -423 1312 C ATOM 499 C ARG A 73 54.210 31.798 0.255 1.00 55.76 C ANISOU 499 C ARG A 73 7784 7589 5813 1146 -485 1339 C ATOM 500 O ARG A 73 53.961 32.860 -0.307 1.00 59.93 O ANISOU 500 O ARG A 73 8418 7994 6360 1278 -564 1536 O ATOM 501 CB ARG A 73 54.892 30.861 -2.008 1.00 53.89 C ANISOU 501 CB ARG A 73 7726 7670 5081 1068 -479 1531 C ATOM 502 CG ARG A 73 55.705 29.811 -2.780 1.00 67.56 C ANISOU 502 CG ARG A 73 9503 9594 6571 932 -375 1490 C ATOM 503 CD ARG A 73 56.129 30.300 -4.178 1.00 89.81 C ANISOU 503 CD ARG A 73 12511 12491 9121 951 -359 1744 C ATOM 504 NE ARG A 73 57.076 31.422 -4.142 1.00105.15 N ANISOU 504 NE ARG A 73 14589 14203 11162 894 -222 1979 N ATOM 505 CZ ARG A 73 57.067 32.450 -4.996 1.00111.30 C ANISOU 505 CZ ARG A 73 15537 14918 11832 961 -260 2283 C ATOM 506 NH1 ARG A 73 56.158 32.511 -5.967 1.00112.07 N ANISOU 506 NH1 ARG A 73 15696 15190 11697 1108 -447 2394 N ATOM 507 NH2 ARG A 73 57.964 33.424 -4.876 1.00111.96 N ANISOU 507 NH2 ARG A 73 15732 14762 12046 875 -121 2485 N ATOM 508 N THR A 74 53.945 31.597 1.544 1.00 53.50 N ANISOU 508 N THR A 74 7357 7263 5708 1117 -449 1132 N ATOM 509 CA THR A 74 53.474 32.663 2.418 1.00 56.34 C ANISOU 509 CA THR A 74 7680 7422 6304 1231 -473 1092 C ATOM 510 C THR A 74 54.280 32.985 3.672 1.00 59.35 C ANISOU 510 C THR A 74 8063 7624 6865 1112 -334 980 C ATOM 511 O THR A 74 54.963 34.009 3.722 1.00 70.66 O ANISOU 511 O THR A 74 9620 8810 8418 1100 -287 1089 O ATOM 512 CB THR A 74 52.059 32.357 2.918 1.00 53.69 C ANISOU 512 CB THR A 74 7139 7233 6027 1358 -580 911 C ATOM 513 OG1 THR A 74 52.036 31.063 3.549 1.00 55.27 O ANISOU 513 OG1 THR A 74 7207 7621 6170 1205 -514 721 O ATOM 514 CG2 THR A 74 51.061 32.373 1.763 1.00 50.82 C ANISOU 514 CG2 THR A 74 6750 7018 5541 1527 -768 1015 C ATOM 515 N ILE A 75 54.229 32.106 4.681 1.00 53.82 N ANISOU 515 N ILE A 75 7229 7044 6175 1008 -276 771 N ATOM 516 CA ILE A 75 54.969 32.315 5.925 1.00 47.31 C ANISOU 516 CA ILE A 75 6399 6097 5479 890 -166 652 C ATOM 517 C ILE A 75 56.250 31.516 5.714 1.00 49.76 C ANISOU 517 C ILE A 75 6764 6452 5691 698 -73 703 C ATOM 518 O ILE A 75 56.252 30.466 5.052 1.00 46.14 O ANISOU 518 O ILE A 75 6284 6170 5078 655 -82 722 O ATOM 519 CB ILE A 75 54.201 31.827 7.170 1.00 52.49 C ANISOU 519 CB ILE A 75 6888 6880 6177 886 -155 420 C ATOM 520 CG1 ILE A 75 54.917 32.221 8.459 1.00 49.14 C ANISOU 520 CG1 ILE A 75 6476 6336 5859 784 -63 295 C ATOM 521 CG2 ILE A 75 53.965 30.293 7.142 1.00 48.31 C ANISOU 521 CG2 ILE A 75 6256 6601 5499 779 -152 360 C ATOM 522 CD1 ILE A 75 53.978 32.223 9.636 1.00 55.35 C ANISOU 522 CD1 ILE A 75 7121 7219 6691 834 -49 79 C ATOM 523 N ARG A 76 57.361 32.025 6.250 1.00 52.10 N ANISOU 523 N ARG A 76 7121 6583 6090 585 13 711 N ATOM 524 CA ARG A 76 58.642 31.344 6.065 1.00 49.85 C ANISOU 524 CA ARG A 76 6860 6337 5744 417 103 755 C ATOM 525 C ARG A 76 58.747 30.087 6.934 1.00 45.97 C ANISOU 525 C ARG A 76 6253 6004 5208 321 120 600 C ATOM 526 O ARG A 76 58.471 30.127 8.139 1.00 49.38 O ANISOU 526 O ARG A 76 6620 6436 5707 303 113 460 O ATOM 527 CB ARG A 76 59.790 32.289 6.382 1.00 46.72 C ANISOU 527 CB ARG A 76 6534 5725 5492 316 177 806 C ATOM 528 CG ARG A 76 61.129 31.630 6.198 1.00 44.42 C ANISOU 528 CG ARG A 76 6228 5487 5161 154 271 843 C ATOM 529 CD ARG A 76 62.263 32.627 6.157 1.00 41.60 C ANISOU 529 CD ARG A 76 5933 4928 4944 42 348 937 C ATOM 530 NE ARG A 76 63.439 31.936 5.681 1.00 47.88 N ANISOU 530 NE ARG A 76 6690 5820 5681 -85 447 992 N ATOM 531 CZ ARG A 76 64.685 32.368 5.785 1.00 53.67 C ANISOU 531 CZ ARG A 76 7406 6454 6532 -233 534 1034 C ATOM 532 NH1 ARG A 76 64.950 33.531 6.360 1.00 42.64 N ANISOU 532 NH1 ARG A 76 6046 4833 5323 -293 527 1027 N ATOM 533 NH2 ARG A 76 65.668 31.617 5.308 1.00 47.59 N ANISOU 533 NH2 ARG A 76 6568 5810 5705 -322 630 1064 N ATOM 534 N VAL A 77 59.116 28.963 6.317 1.00 43.31 N ANISOU 534 N VAL A 77 5900 5802 4753 264 141 625 N ATOM 535 CA VAL A 77 59.433 27.736 7.049 1.00 44.86 C ANISOU 535 CA VAL A 77 6011 6101 4932 164 155 519 C ATOM 536 C VAL A 77 60.717 27.147 6.474 1.00 39.66 C ANISOU 536 C VAL A 77 5371 5451 4248 77 229 576 C ATOM 537 O VAL A 77 61.057 27.383 5.307 1.00 45.84 O ANISOU 537 O VAL A 77 6221 6235 4961 100 271 681 O ATOM 538 CB VAL A 77 58.271 26.710 6.995 1.00 47.71 C ANISOU 538 CB VAL A 77 6295 6622 5208 202 89 441 C ATOM 539 CG1 VAL A 77 56.934 27.375 7.295 1.00 53.83 C ANISOU 539 CG1 VAL A 77 7025 7418 6011 313 26 391 C ATOM 540 CG2 VAL A 77 58.227 25.990 5.674 1.00 40.05 C ANISOU 540 CG2 VAL A 77 5354 5747 4116 224 74 485 C ATOM 541 N PRO A 78 61.448 26.360 7.261 1.00 39.64 N ANISOU 541 N PRO A 78 5303 5465 4292 -16 246 511 N ATOM 542 CA PRO A 78 62.657 25.726 6.722 1.00 43.33 C ANISOU 542 CA PRO A 78 5754 5948 4760 -74 316 541 C ATOM 543 C PRO A 78 62.290 24.788 5.589 1.00 46.84 C ANISOU 543 C PRO A 78 6214 6504 5079 -24 318 531 C ATOM 544 O PRO A 78 61.353 23.999 5.702 1.00 51.36 O ANISOU 544 O PRO A 78 6761 7148 5607 2 246 459 O ATOM 545 CB PRO A 78 63.227 24.936 7.911 1.00 43.09 C ANISOU 545 CB PRO A 78 5641 5922 4810 -150 287 468 C ATOM 546 CG PRO A 78 62.434 25.345 9.122 1.00 41.97 C ANISOU 546 CG PRO A 78 5490 5773 4685 -156 221 410 C ATOM 547 CD PRO A 78 61.153 25.930 8.644 1.00 35.22 C ANISOU 547 CD PRO A 78 4676 4933 3771 -62 199 412 C ATOM 548 N ASN A 79 63.049 24.858 4.508 1.00 46.41 N ANISOU 548 N ASN A 79 6195 6473 4966 -25 408 592 N ATOM 549 CA ASN A 79 62.865 23.930 3.401 1.00 42.77 C ANISOU 549 CA ASN A 79 5751 6133 4367 18 421 547 C ATOM 550 C ASN A 79 63.335 22.537 3.814 1.00 49.38 C ANISOU 550 C ASN A 79 6505 6982 5277 -14 417 424 C ATOM 551 O ASN A 79 64.498 22.380 4.202 1.00 48.91 O ANISOU 551 O ASN A 79 6381 6874 5328 -60 479 422 O ATOM 552 CB ASN A 79 63.635 24.428 2.192 1.00 48.31 C ANISOU 552 CB ASN A 79 6512 6879 4963 17 544 643 C ATOM 553 CG ASN A 79 63.345 23.613 0.951 1.00 51.08 C ANISOU 553 CG ASN A 79 6903 7386 5120 70 557 580 C ATOM 554 OD1 ASN A 79 62.316 22.946 0.866 1.00 51.19 O ANISOU 554 OD1 ASN A 79 6918 7460 5073 116 444 485 O ATOM 555 ND2 ASN A 79 64.243 23.674 -0.020 1.00 45.07 N ANISOU 555 ND2 ASN A 79 6167 6702 4254 54 698 619 N ATOM 556 N PRO A 80 62.477 21.521 3.800 1.00 49.52 N ANISOU 556 N PRO A 80 6510 7045 5262 6 333 325 N ATOM 557 CA PRO A 80 62.906 20.182 4.228 1.00 47.59 C ANISOU 557 CA PRO A 80 6201 6761 5119 -22 317 226 C ATOM 558 C PRO A 80 63.607 19.446 3.101 1.00 47.18 C ANISOU 558 C PRO A 80 6151 6757 5017 15 398 140 C ATOM 559 O PRO A 80 63.254 19.586 1.934 1.00 52.94 O ANISOU 559 O PRO A 80 6944 7595 5577 57 426 116 O ATOM 560 CB PRO A 80 61.588 19.484 4.575 1.00 44.39 C ANISOU 560 CB PRO A 80 5790 6373 4705 -35 203 162 C ATOM 561 CG PRO A 80 60.611 20.085 3.553 1.00 47.32 C ANISOU 561 CG PRO A 80 6215 6854 4908 23 174 167 C ATOM 562 CD PRO A 80 61.044 21.561 3.451 1.00 45.75 C ANISOU 562 CD PRO A 80 6063 6640 4679 51 237 302 C ATOM 563 N HIS A 81 64.589 18.623 3.463 1.00 49.50 N ANISOU 563 N HIS A 81 6372 6981 5453 10 428 83 N ATOM 564 CA HIS A 81 65.401 17.917 2.474 1.00 46.87 C ANISOU 564 CA HIS A 81 6016 6689 5103 61 528 -30 C ATOM 565 C HIS A 81 65.226 16.407 2.497 1.00 51.03 C ANISOU 565 C HIS A 81 6522 7138 5728 89 462 -187 C ATOM 566 O HIS A 81 65.070 15.789 1.443 1.00 48.99 O ANISOU 566 O HIS A 81 6298 6941 5375 134 494 -335 O ATOM 567 CB HIS A 81 66.884 18.260 2.676 1.00 46.08 C ANISOU 567 CB HIS A 81 5818 6570 5119 57 642 13 C ATOM 568 CG HIS A 81 67.207 19.691 2.401 1.00 51.69 C ANISOU 568 CG HIS A 81 6553 7341 5746 13 736 153 C ATOM 569 ND1 HIS A 81 66.806 20.329 1.246 1.00 57.78 N ANISOU 569 ND1 HIS A 81 7424 8229 6302 25 809 197 N ATOM 570 CD2 HIS A 81 67.889 20.610 3.123 1.00 51.72 C ANISOU 570 CD2 HIS A 81 6501 7292 5858 -52 760 264 C ATOM 571 CE1 HIS A 81 67.236 21.578 1.265 1.00 55.25 C ANISOU 571 CE1 HIS A 81 7115 7900 5976 -32 883 349 C ATOM 572 NE2 HIS A 81 67.893 21.776 2.393 1.00 51.06 N ANISOU 572 NE2 HIS A 81 6487 7263 5650 -85 856 376 N ATOM 573 N LYS A 82 65.295 15.781 3.666 1.00 44.44 N ANISOU 573 N LYS A 82 5640 6164 5080 61 369 -160 N ATOM 574 CA LYS A 82 65.214 14.331 3.714 1.00 46.72 C ANISOU 574 CA LYS A 82 5919 6330 5503 84 304 -285 C ATOM 575 C LYS A 82 64.938 13.883 5.144 1.00 46.29 C ANISOU 575 C LYS A 82 5847 6138 5602 21 178 -178 C ATOM 576 O LYS A 82 65.440 14.482 6.100 1.00 48.37 O ANISOU 576 O LYS A 82 6069 6395 5913 -5 163 -44 O ATOM 577 CB LYS A 82 66.494 13.670 3.188 1.00 55.60 C ANISOU 577 CB LYS A 82 6969 7413 6743 180 396 -406 C ATOM 578 CG LYS A 82 66.337 12.162 3.124 1.00 64.12 C ANISOU 578 CG LYS A 82 8056 8327 7981 219 322 -559 C ATOM 579 CD LYS A 82 67.148 11.548 2.029 1.00 67.79 C ANISOU 579 CD LYS A 82 8481 8807 8468 332 438 -774 C ATOM 580 CE LYS A 82 66.887 10.057 1.925 1.00 72.84 C ANISOU 580 CE LYS A 82 9146 9244 9285 372 353 -954 C ATOM 581 NZ LYS A 82 67.738 9.465 0.859 1.00 78.86 N ANISOU 581 NZ LYS A 82 9860 10027 10077 505 481 -1206 N ATOM 582 N ALA A 83 64.099 12.863 5.277 1.00 45.57 N ANISOU 582 N ALA A 83 5794 5948 5571 -20 87 -234 N ATOM 583 CA ALA A 83 63.853 12.193 6.542 1.00 52.14 C ANISOU 583 CA ALA A 83 6624 6639 6548 -90 -22 -123 C ATOM 584 C ALA A 83 63.993 10.700 6.313 1.00 56.52 C ANISOU 584 C ALA A 83 7190 6993 7291 -63 -74 -233 C ATOM 585 O ALA A 83 63.830 10.218 5.192 1.00 57.32 O ANISOU 585 O ALA A 83 7314 7091 7375 -20 -40 -426 O ATOM 586 CB ALA A 83 62.477 12.530 7.100 1.00 46.88 C ANISOU 586 CB ALA A 83 5991 6041 5780 -208 -76 -47 C ATOM 587 N GLY A 84 64.346 9.976 7.362 1.00 58.68 N ANISOU 587 N GLY A 84 7456 7096 7745 -81 -162 -113 N ATOM 588 CA GLY A 84 64.503 8.543 7.222 1.00 53.66 C ANISOU 588 CA GLY A 84 6841 6215 7333 -48 -225 -197 C ATOM 589 C GLY A 84 65.015 7.907 8.488 1.00 58.84 C ANISOU 589 C GLY A 84 7493 6689 8176 -53 -336 0 C ATOM 590 O GLY A 84 64.959 8.498 9.571 1.00 60.55 O ANISOU 590 O GLY A 84 7706 6990 8310 -123 -376 203 O ATOM 591 N GLU A 85 65.490 6.673 8.338 1.00 66.35 N ANISOU 591 N GLU A 85 8452 7382 9377 27 -395 -67 N ATOM 592 CA GLU A 85 65.867 5.823 9.459 1.00 73.32 C ANISOU 592 CA GLU A 85 9355 8035 10468 28 -532 135 C ATOM 593 C GLU A 85 67.384 5.727 9.556 1.00 67.75 C ANISOU 593 C GLU A 85 8544 7272 9927 223 -554 137 C ATOM 594 O GLU A 85 68.076 5.636 8.538 1.00 69.31 O ANISOU 594 O GLU A 85 8667 7471 10198 370 -465 -89 O ATOM 595 CB GLU A 85 65.257 4.420 9.324 1.00 85.20 C ANISOU 595 CB GLU A 85 10948 9233 12191 -26 -610 88 C ATOM 596 CG GLU A 85 65.761 3.669 8.091 1.00101.13 C ANISOU 596 CG GLU A 85 12944 11091 14390 129 -567 -219 C ATOM 597 CD GLU A 85 65.092 2.322 7.853 1.00110.06 C ANISOU 597 CD GLU A 85 14170 11897 15751 61 -645 -316 C ATOM 598 OE1 GLU A 85 64.476 1.776 8.796 1.00109.41 O ANISOU 598 OE1 GLU A 85 14166 11647 15759 -90 -749 -86 O ATOM 599 OE2 GLU A 85 65.217 1.798 6.722 1.00112.70 O ANISOU 599 OE2 GLU A 85 14502 12141 16178 154 -596 -627 O ATOM 600 N LEU A 86 67.891 5.722 10.780 1.00 70.11 N ANISOU 600 N LEU A 86 8826 7536 10278 225 -675 385 N ATOM 601 CA LEU A 86 69.320 5.533 11.019 1.00 73.86 C ANISOU 601 CA LEU A 86 9177 7946 10943 413 -739 411 C ATOM 602 C LEU A 86 69.638 4.044 11.029 1.00 80.29 C ANISOU 602 C LEU A 86 10018 8395 12092 531 -855 406 C ATOM 603 O LEU A 86 68.945 3.278 11.712 1.00 79.97 O ANISOU 603 O LEU A 86 10107 8155 12121 424 -971 585 O ATOM 604 CB LEU A 86 69.701 6.152 12.362 1.00 72.96 C ANISOU 604 CB LEU A 86 9035 7962 10726 363 -853 679 C ATOM 605 CG LEU A 86 69.699 7.674 12.403 1.00 67.20 C ANISOU 605 CG LEU A 86 8251 7558 9726 285 -751 661 C ATOM 606 CD1 LEU A 86 69.796 8.175 13.825 1.00 61.32 C ANISOU 606 CD1 LEU A 86 7519 6928 8852 198 -879 906 C ATOM 607 CD2 LEU A 86 70.863 8.180 11.566 1.00 62.98 C ANISOU 607 CD2 LEU A 86 7545 7120 9264 432 -647 481 C ATOM 608 N PRO A 87 70.687 3.596 10.319 1.00 90.24 N ANISOU 608 N PRO A 87 11156 9550 13581 751 -825 211 N ATOM 609 CA PRO A 87 70.975 2.150 10.314 1.00101.09 C ANISOU 609 CA PRO A 87 12561 10533 15315 887 -944 186 C ATOM 610 C PRO A 87 71.265 1.615 11.703 1.00115.88 C ANISOU 610 C PRO A 87 14473 12226 17330 897 -1174 538 C ATOM 611 O PRO A 87 70.878 0.483 12.019 1.00120.34 O ANISOU 611 O PRO A 87 15164 12449 18110 882 -1297 644 O ATOM 612 CB PRO A 87 72.180 2.033 9.368 1.00 93.32 C ANISOU 612 CB PRO A 87 11391 9553 14513 1141 -845 -98 C ATOM 613 CG PRO A 87 72.108 3.246 8.504 1.00 85.59 C ANISOU 613 CG PRO A 87 10347 8942 13232 1079 -628 -276 C ATOM 614 CD PRO A 87 71.590 4.329 9.414 1.00 83.88 C ANISOU 614 CD PRO A 87 10180 8961 12728 881 -664 -13 C ATOM 615 N THR A 88 71.912 2.413 12.555 1.00123.22 N ANISOU 615 N THR A 88 15309 13378 18134 907 -1243 730 N ATOM 616 CA THR A 88 72.134 2.009 13.940 1.00131.13 C ANISOU 616 CA THR A 88 16362 14270 19193 897 -1476 1089 C ATOM 617 C THR A 88 70.832 1.824 14.711 1.00125.81 C ANISOU 617 C THR A 88 15905 13557 18339 639 -1521 1333 C ATOM 618 O THR A 88 70.823 1.125 15.729 1.00128.95 O ANISOU 618 O THR A 88 16400 13774 18821 616 -1709 1640 O ATOM 619 CB THR A 88 73.004 3.048 14.652 1.00137.41 C ANISOU 619 CB THR A 88 17008 15370 19831 928 -1535 1203 C ATOM 620 OG1 THR A 88 72.183 4.129 15.119 1.00135.58 O ANISOU 620 OG1 THR A 88 16858 15433 19223 692 -1463 1290 O ATOM 621 CG2 THR A 88 74.057 3.600 13.696 1.00137.83 C ANISOU 621 CG2 THR A 88 16826 15572 19972 1101 -1400 915 C ATOM 622 N GLY A 89 69.742 2.438 14.259 1.00116.38 N ANISOU 622 N GLY A 89 14780 12541 16899 446 -1354 1217 N ATOM 623 CA GLY A 89 68.473 2.413 14.984 1.00108.62 C ANISOU 623 CA GLY A 89 13961 11589 15722 187 -1363 1425 C ATOM 624 C GLY A 89 68.096 3.851 15.283 1.00103.35 C ANISOU 624 C GLY A 89 13259 11328 14682 58 -1258 1427 C ATOM 625 O GLY A 89 68.915 4.661 15.718 1.00105.48 O ANISOU 625 O GLY A 89 13428 11802 14846 129 -1293 1468 O ATOM 626 N GLY A 90 66.834 4.174 15.026 1.00 94.61 N ANISOU 626 N GLY A 90 12224 10330 13395 -132 -1135 1366 N ATOM 627 CA GLY A 90 66.324 5.526 15.162 1.00 82.03 C ANISOU 627 CA GLY A 90 10601 9088 11478 -241 -1021 1326 C ATOM 628 C GLY A 90 66.130 6.209 13.819 1.00 74.88 C ANISOU 628 C GLY A 90 9628 8307 10517 -196 -856 1018 C ATOM 629 O GLY A 90 66.187 5.594 12.751 1.00 69.19 O ANISOU 629 O GLY A 90 8897 7426 9965 -114 -814 818 O ATOM 630 N SER A 91 65.955 7.528 13.878 1.00 66.81 N ANISOU 630 N SER A 91 8563 7574 9247 -242 -767 979 N ATOM 631 CA SER A 91 65.547 8.273 12.698 1.00 61.60 C ANISOU 631 CA SER A 91 7868 7052 8484 -231 -618 744 C ATOM 632 C SER A 91 66.200 9.649 12.687 1.00 58.84 C ANISOU 632 C SER A 91 7436 6934 7988 -181 -554 706 C ATOM 633 O SER A 91 66.721 10.131 13.701 1.00 55.95 O ANISOU 633 O SER A 91 7043 6655 7561 -194 -623 846 O ATOM 634 CB SER A 91 64.027 8.427 12.653 1.00 59.75 C ANISOU 634 CB SER A 91 7699 6903 8100 -400 -560 732 C ATOM 635 OG SER A 91 63.559 9.007 13.866 1.00 69.82 O ANISOU 635 OG SER A 91 8999 8334 9195 -523 -580 915 O ATOM 636 N TYR A 92 66.118 10.298 11.526 1.00 55.40 N ANISOU 636 N TYR A 92 6966 6599 7483 -138 -425 517 N ATOM 637 CA TYR A 92 66.703 11.615 11.332 1.00 52.84 C ANISOU 637 CA TYR A 92 6572 6462 7044 -105 -346 477 C ATOM 638 C TYR A 92 65.851 12.447 10.391 1.00 48.85 C ANISOU 638 C TYR A 92 6100 6092 6369 -140 -224 358 C ATOM 639 O TYR A 92 65.067 11.921 9.598 1.00 47.36 O ANISOU 639 O TYR A 92 5958 5865 6171 -151 -196 254 O ATOM 640 CB TYR A 92 68.097 11.525 10.731 1.00 48.04 C ANISOU 640 CB TYR A 92 5850 5819 6586 40 -311 387 C ATOM 641 CG TYR A 92 68.090 11.005 9.309 1.00 55.67 C ANISOU 641 CG TYR A 92 6812 6731 7609 125 -207 184 C ATOM 642 CD1 TYR A 92 68.158 9.633 9.047 1.00 56.63 C ANISOU 642 CD1 TYR A 92 6951 6640 7927 197 -261 113 C ATOM 643 CD2 TYR A 92 68.017 11.879 8.224 1.00 52.92 C ANISOU 643 CD2 TYR A 92 6455 6541 7112 134 -58 61 C ATOM 644 CE1 TYR A 92 68.160 9.146 7.745 1.00 58.26 C ANISOU 644 CE1 TYR A 92 7158 6809 8170 277 -165 -114 C ATOM 645 CE2 TYR A 92 68.005 11.397 6.916 1.00 54.82 C ANISOU 645 CE2 TYR A 92 6703 6769 7356 208 38 -134 C ATOM 646 CZ TYR A 92 68.083 10.032 6.682 1.00 61.06 C ANISOU 646 CZ TYR A 92 7503 7364 8332 280 -13 -241 C ATOM 647 OH TYR A 92 68.071 9.564 5.379 1.00 66.35 O ANISOU 647 OH TYR A 92 8183 8037 8988 354 83 -475 O ATOM 648 N ILE A 93 66.094 13.752 10.418 1.00 43.95 N ANISOU 648 N ILE A 93 5449 5622 5628 -149 -162 367 N ATOM 649 CA ILE A 93 65.595 14.654 9.391 1.00 44.10 C ANISOU 649 CA ILE A 93 5490 5757 5508 -144 -50 274 C ATOM 650 C ILE A 93 66.662 15.696 9.082 1.00 49.21 C ANISOU 650 C ILE A 93 6070 6479 6148 -104 33 268 C ATOM 651 O ILE A 93 67.382 16.151 9.984 1.00 47.11 O ANISOU 651 O ILE A 93 5748 6224 5927 -128 -12 345 O ATOM 652 CB ILE A 93 64.278 15.324 9.824 1.00 43.08 C ANISOU 652 CB ILE A 93 5421 5721 5226 -234 -60 316 C ATOM 653 CG1 ILE A 93 63.735 16.179 8.681 1.00 40.63 C ANISOU 653 CG1 ILE A 93 5138 5513 4788 -203 27 237 C ATOM 654 CG2 ILE A 93 64.463 16.103 11.125 1.00 36.71 C ANISOU 654 CG2 ILE A 93 4601 4970 4376 -292 -102 422 C ATOM 655 CD1 ILE A 93 62.348 16.668 8.930 1.00 45.82 C ANISOU 655 CD1 ILE A 93 5827 6251 5329 -257 8 249 C ATOM 656 N ILE A 94 66.764 16.062 7.798 1.00 47.64 N ANISOU 656 N ILE A 94 5875 6340 5884 -57 151 177 N ATOM 657 CA ILE A 94 67.652 17.111 7.307 1.00 40.43 C ANISOU 657 CA ILE A 94 4909 5505 4948 -46 262 185 C ATOM 658 C ILE A 94 66.803 18.225 6.699 1.00 45.88 C ANISOU 658 C ILE A 94 5688 6284 5460 -77 323 207 C ATOM 659 O ILE A 94 65.942 17.956 5.853 1.00 46.73 O ANISOU 659 O ILE A 94 5867 6431 5456 -51 337 149 O ATOM 660 CB ILE A 94 68.643 16.570 6.258 1.00 46.23 C ANISOU 660 CB ILE A 94 5566 6248 5749 40 372 79 C ATOM 661 CG1 ILE A 94 69.345 15.297 6.763 1.00 43.93 C ANISOU 661 CG1 ILE A 94 5189 5837 5668 109 292 39 C ATOM 662 CG2 ILE A 94 69.668 17.653 5.878 1.00 38.65 C ANISOU 662 CG2 ILE A 94 4524 5375 4786 19 503 113 C ATOM 663 CD1 ILE A 94 70.284 14.705 5.725 1.00 48.03 C ANISOU 663 CD1 ILE A 94 5614 6365 6271 218 412 -107 C ATOM 664 N MET A 95 67.079 19.474 7.087 1.00 41.36 N ANISOU 664 N MET A 95 5109 5734 4872 -127 349 286 N ATOM 665 CA MET A 95 66.351 20.615 6.544 1.00 47.54 C ANISOU 665 CA MET A 95 5979 6564 5520 -139 396 329 C ATOM 666 C MET A 95 67.272 21.829 6.437 1.00 46.00 C ANISOU 666 C MET A 95 5754 6361 5362 -185 485 397 C ATOM 667 O MET A 95 68.420 21.821 6.883 1.00 48.12 O ANISOU 667 O MET A 95 5916 6607 5760 -221 501 398 O ATOM 668 CB MET A 95 65.111 20.941 7.394 1.00 44.85 C ANISOU 668 CB MET A 95 5695 6215 5130 -164 296 350 C ATOM 669 CG MET A 95 65.427 21.586 8.712 1.00 45.86 C ANISOU 669 CG MET A 95 5792 6306 5327 -227 245 387 C ATOM 670 SD MET A 95 63.996 21.816 9.803 1.00 45.02 S ANISOU 670 SD MET A 95 5730 6227 5149 -252 157 377 S ATOM 671 CE MET A 95 63.657 20.119 10.241 1.00 44.44 C ANISOU 671 CE MET A 95 5633 6159 5094 -270 83 366 C ATOM 672 N GLU A 96 66.733 22.877 5.825 1.00 47.18 N ANISOU 672 N GLU A 96 5994 6522 5409 -187 532 461 N ATOM 673 CA GLU A 96 67.399 24.164 5.726 1.00 43.30 C ANISOU 673 CA GLU A 96 5505 5985 4964 -251 610 548 C ATOM 674 C GLU A 96 67.796 24.720 7.093 1.00 45.22 C ANISOU 674 C GLU A 96 5691 6143 5346 -327 536 541 C ATOM 675 O GLU A 96 67.031 24.661 8.062 1.00 45.72 O ANISOU 675 O GLU A 96 5781 6189 5402 -320 425 503 O ATOM 676 CB GLU A 96 66.476 25.161 5.022 1.00 44.68 C ANISOU 676 CB GLU A 96 5813 6147 5017 -220 625 636 C ATOM 677 CG GLU A 96 67.065 26.583 4.904 1.00 45.54 C ANISOU 677 CG GLU A 96 5953 6157 5194 -297 702 752 C ATOM 678 CD GLU A 96 66.058 27.602 4.344 1.00 56.58 C ANISOU 678 CD GLU A 96 7495 7500 6502 -242 681 860 C ATOM 679 OE1 GLU A 96 64.892 27.220 4.082 1.00 52.24 O ANISOU 679 OE1 GLU A 96 7001 7017 5833 -141 599 832 O ATOM 680 OE2 GLU A 96 66.428 28.791 4.192 1.00 56.23 O ANISOU 680 OE2 GLU A 96 7503 7336 6526 -301 735 974 O ATOM 681 N PHE A 97 69.002 25.281 7.161 1.00 40.05 N ANISOU 681 N PHE A 97 4951 5456 4810 -411 602 568 N ATOM 682 CA PHE A 97 69.458 25.985 8.348 1.00 41.78 C ANISOU 682 CA PHE A 97 5119 5601 5155 -501 528 546 C ATOM 683 C PHE A 97 69.114 27.461 8.247 1.00 46.99 C ANISOU 683 C PHE A 97 5878 6144 5831 -552 559 603 C ATOM 684 O PHE A 97 69.447 28.113 7.254 1.00 51.24 O ANISOU 684 O PHE A 97 6451 6646 6371 -586 681 701 O ATOM 685 CB PHE A 97 70.968 25.830 8.550 1.00 41.34 C ANISOU 685 CB PHE A 97 4888 5566 5253 -577 560 528 C ATOM 686 CG PHE A 97 71.441 26.414 9.845 1.00 41.62 C ANISOU 686 CG PHE A 97 4858 5551 5403 -674 447 478 C ATOM 687 CD1 PHE A 97 71.777 27.750 9.939 1.00 46.35 C ANISOU 687 CD1 PHE A 97 5470 6046 6094 -790 482 494 C ATOM 688 CD2 PHE A 97 71.452 25.643 10.994 1.00 46.13 C ANISOU 688 CD2 PHE A 97 5378 6173 5978 -651 293 416 C ATOM 689 CE1 PHE A 97 72.177 28.298 11.151 1.00 52.82 C ANISOU 689 CE1 PHE A 97 6235 6824 7009 -885 363 410 C ATOM 690 CE2 PHE A 97 71.841 26.185 12.214 1.00 46.63 C ANISOU 690 CE2 PHE A 97 5393 6222 6102 -740 171 356 C ATOM 691 CZ PHE A 97 72.212 27.518 12.280 1.00 48.19 C ANISOU 691 CZ PHE A 97 5591 6327 6393 -857 206 334 C ATOM 692 N ILE A 98 68.466 27.990 9.281 1.00 46.90 N ANISOU 692 N ILE A 98 5917 6070 5835 -557 454 542 N ATOM 693 CA ILE A 98 68.069 29.393 9.334 1.00 52.42 C ANISOU 693 CA ILE A 98 6714 6618 6585 -585 461 564 C ATOM 694 C ILE A 98 68.667 30.035 10.579 1.00 53.27 C ANISOU 694 C ILE A 98 6764 6651 6824 -694 386 457 C ATOM 695 O ILE A 98 68.627 29.457 11.673 1.00 56.67 O ANISOU 695 O ILE A 98 7142 7168 7223 -696 281 353 O ATOM 696 CB ILE A 98 66.535 29.555 9.353 1.00 53.20 C ANISOU 696 CB ILE A 98 6927 6708 6576 -461 408 547 C ATOM 697 CG1 ILE A 98 65.893 28.883 8.139 1.00 49.24 C ANISOU 697 CG1 ILE A 98 6474 6303 5931 -358 451 631 C ATOM 698 CG2 ILE A 98 66.154 31.038 9.446 1.00 44.74 C ANISOU 698 CG2 ILE A 98 5953 5448 5599 -462 406 557 C ATOM 699 CD1 ILE A 98 64.399 29.144 8.063 1.00 47.64 C ANISOU 699 CD1 ILE A 98 6355 6100 5647 -236 389 620 C ATOM 700 N ASP A 99 69.199 31.243 10.420 1.00 49.70 N ANISOU 700 N ASP A 99 6334 6036 6514 -794 434 487 N ATOM 701 CA ASP A 99 69.782 31.977 11.537 1.00 63.03 C ANISOU 701 CA ASP A 99 7972 7635 8340 -916 356 359 C ATOM 702 C ASP A 99 68.701 32.788 12.249 1.00 57.63 C ANISOU 702 C ASP A 99 7411 6840 7647 -855 286 246 C ATOM 703 O ASP A 99 68.187 33.765 11.705 1.00 61.30 O ANISOU 703 O ASP A 99 7991 7124 8177 -821 331 304 O ATOM 704 CB ASP A 99 70.901 32.899 11.050 1.00 77.17 C ANISOU 704 CB ASP A 99 9715 9282 10324 -1079 444 427 C ATOM 705 CG ASP A 99 71.556 33.667 12.181 1.00102.96 C ANISOU 705 CG ASP A 99 12918 12452 13752 -1226 348 269 C ATOM 706 OD1 ASP A 99 72.189 33.028 13.047 1.00112.17 O ANISOU 706 OD1 ASP A 99 13946 13764 14910 -1271 247 160 O ATOM 707 OD2 ASP A 99 71.439 34.911 12.203 1.00114.69 O ANISOU 707 OD2 ASP A 99 14495 13707 15375 -1295 360 249 O ATOM 708 N PHE A 100 68.346 32.324 13.444 1.00 50.81 N ANISOU 708 N PHE A 100 6518 6096 6691 -831 178 94 N ATOM 709 CA PHE A 100 67.353 32.955 14.302 1.00 54.81 C ANISOU 709 CA PHE A 100 7108 6553 7163 -771 121 -61 C ATOM 710 C PHE A 100 67.998 34.070 15.116 1.00 60.37 C ANISOU 710 C PHE A 100 7809 7108 8022 -900 68 -221 C ATOM 711 O PHE A 100 69.222 34.133 15.226 1.00 79.46 O ANISOU 711 O PHE A 100 10130 9514 10547 -1049 46 -220 O ATOM 712 CB PHE A 100 66.714 31.923 15.233 1.00 50.92 C ANISOU 712 CB PHE A 100 6586 6288 6474 -712 50 -145 C ATOM 713 CG PHE A 100 65.948 30.850 14.514 1.00 48.16 C ANISOU 713 CG PHE A 100 6243 6062 5995 -598 90 -20 C ATOM 714 CD1 PHE A 100 65.236 31.141 13.362 1.00 44.43 C ANISOU 714 CD1 PHE A 100 5840 5506 5535 -497 162 84 C ATOM 715 CD2 PHE A 100 65.939 29.549 14.990 1.00 53.00 C ANISOU 715 CD2 PHE A 100 6797 6865 6478 -597 41 -3 C ATOM 716 CE1 PHE A 100 64.531 30.156 12.698 1.00 46.51 C ANISOU 716 CE1 PHE A 100 6102 5890 5678 -405 183 171 C ATOM 717 CE2 PHE A 100 65.236 28.559 14.331 1.00 50.50 C ANISOU 717 CE2 PHE A 100 6485 6633 6067 -512 73 91 C ATOM 718 CZ PHE A 100 64.530 28.863 13.183 1.00 50.91 C ANISOU 718 CZ PHE A 100 6597 6620 6129 -420 142 162 C ATOM 719 N GLY A 101 67.179 34.946 15.689 1.00 67.29 N ANISOU 719 N GLY A 101 8775 7871 8921 -843 43 -379 N ATOM 720 CA GLY A 101 67.704 36.033 16.494 1.00 85.92 C ANISOU 720 CA GLY A 101 11145 10069 11431 -962 -14 -576 C ATOM 721 C GLY A 101 67.237 37.417 16.095 1.00 98.28 C ANISOU 721 C GLY A 101 12834 11309 13199 -921 28 -608 C ATOM 722 O GLY A 101 68.016 38.369 16.113 1.00101.43 O ANISOU 722 O GLY A 101 13244 11477 13816 -1064 19 -656 O ATOM 723 N GLY A 102 65.963 37.535 15.738 1.00103.44 N ANISOU 723 N GLY A 102 13573 11929 13801 -727 65 -581 N ATOM 724 CA GLY A 102 65.419 38.822 15.350 1.00110.37 C ANISOU 724 CA GLY A 102 14572 12480 14883 -645 87 -597 C ATOM 725 C GLY A 102 65.477 39.778 16.525 1.00118.63 C ANISOU 725 C GLY A 102 15645 13379 16052 -696 24 -917 C ATOM 726 O GLY A 102 65.194 39.399 17.662 1.00123.83 O ANISOU 726 O GLY A 102 16254 14251 16544 -682 -25 -1151 O ATOM 727 N SER A 103 65.933 41.002 16.273 1.00122.40 N ANISOU 727 N SER A 103 16201 13492 16813 -778 24 -931 N ATOM 728 CA SER A 103 66.111 41.987 17.342 1.00128.84 C ANISOU 728 CA SER A 103 17048 14123 17783 -851 -43 -1266 C ATOM 729 C SER A 103 64.869 42.462 18.097 1.00134.75 C ANISOU 729 C SER A 103 17854 14840 18506 -644 -58 -1550 C ATOM 730 O SER A 103 64.886 42.544 19.325 1.00138.43 O ANISOU 730 O SER A 103 18289 15425 18883 -684 -112 -1879 O ATOM 731 CB SER A 103 66.875 43.204 16.808 1.00127.42 C ANISOU 731 CB SER A 103 16947 13511 17956 -1002 -34 -1197 C ATOM 732 OG SER A 103 67.291 44.050 17.866 1.00124.48 O ANISOU 732 OG SER A 103 16584 12971 17740 -1128 -114 -1543 O ATOM 733 N ARG A 104 63.799 42.776 17.377 1.00134.08 N ANISOU 733 N ARG A 104 17841 14616 18488 -418 -14 -1433 N ATOM 734 CA ARG A 104 62.581 43.244 18.031 1.00134.45 C ANISOU 734 CA ARG A 104 17910 14635 18539 -195 -15 -1708 C ATOM 735 C ARG A 104 61.510 42.168 18.129 1.00126.68 C ANISOU 735 C ARG A 104 16835 14038 17260 -23 25 -1682 C ATOM 736 O ARG A 104 60.806 42.059 19.133 1.00133.67 O ANISOU 736 O ARG A 104 17669 15114 18007 66 38 -1968 O ATOM 737 CB ARG A 104 62.024 44.470 17.303 1.00140.56 C ANISOU 737 CB ARG A 104 18810 14958 19639 -32 -15 -1644 C ATOM 738 CG ARG A 104 62.829 45.740 17.522 1.00145.70 C ANISOU 738 CG ARG A 104 19563 15169 20628 -183 -56 -1781 C ATOM 739 CD ARG A 104 63.064 46.477 16.213 1.00148.51 C ANISOU 739 CD ARG A 104 20046 15119 21263 -188 -45 -1424 C ATOM 740 NE ARG A 104 64.365 47.139 16.184 1.00153.19 N ANISOU 740 NE ARG A 104 20685 15427 22092 -481 -58 -1401 N ATOM 741 CZ ARG A 104 65.444 46.639 15.591 1.00152.48 C ANISOU 741 CZ ARG A 104 20546 15442 21947 -717 -20 -1133 C ATOM 742 NH1 ARG A 104 65.382 45.467 14.974 1.00147.68 N ANISOU 742 NH1 ARG A 104 19859 15199 21054 -681 30 -878 N ATOM 743 NH2 ARG A 104 66.587 47.311 15.614 1.00155.24 N ANISOU 743 NH2 ARG A 104 20913 15528 22542 -993 -27 -1137 N ATOM 744 N GLY A 105 61.393 41.381 17.067 1.00111.28 N ANISOU 744 N GLY A 105 14862 12207 15213 12 51 -1345 N ATOM 745 CA GLY A 105 60.402 40.328 16.990 1.00100.67 C ANISOU 745 CA GLY A 105 13427 11199 13623 152 83 -1287 C ATOM 746 C GLY A 105 59.175 40.960 16.369 1.00 98.57 C ANISOU 746 C GLY A 105 13190 10767 13496 416 88 -1255 C ATOM 747 O GLY A 105 58.983 42.171 16.478 1.00104.06 O ANISOU 747 O GLY A 105 13963 11132 14443 509 67 -1390 O ATOM 748 N ASN A 106 58.326 40.255 15.626 1.00 92.94 N ANISOU 748 N ASN A 106 12419 10233 12662 556 97 -1071 N ATOM 749 CA ASN A 106 57.203 40.935 14.927 1.00 85.98 C ANISOU 749 CA ASN A 106 11554 9176 11937 822 69 -1013 C ATOM 750 C ASN A 106 55.786 40.285 14.883 1.00 82.28 C ANISOU 750 C ASN A 106 10941 8991 11331 1027 79 -1052 C ATOM 751 O ASN A 106 55.454 39.572 13.969 1.00 70.63 O ANISOU 751 O ASN A 106 9431 7662 9745 1065 56 -817 O ATOM 752 CB ASN A 106 57.687 41.186 13.497 1.00 83.96 C ANISOU 752 CB ASN A 106 11416 8705 11781 804 33 -642 C ATOM 753 CG ASN A 106 56.993 42.332 12.814 1.00 88.88 C ANISOU 753 CG ASN A 106 12128 8987 12656 1032 -28 -554 C ATOM 754 OD1 ASN A 106 56.000 42.863 13.295 1.00 92.10 O ANISOU 754 OD1 ASN A 106 12483 9333 13178 1248 -49 -768 O ATOM 755 ND2 ASN A 106 57.516 42.715 11.676 1.00 86.96 N ANISOU 755 ND2 ASN A 106 12016 8524 12500 991 -54 -229 N ATOM 756 N GLN A 107 54.956 40.571 15.875 1.00 73.32 N ANISOU 756 N GLN A 107 8047 8305 11508 54 185 460 N ATOM 757 CA GLN A 107 53.612 39.997 16.017 1.00 73.87 C ANISOU 757 CA GLN A 107 8165 8440 11464 170 114 479 C ATOM 758 C GLN A 107 52.577 40.162 14.935 1.00 69.94 C ANISOU 758 C GLN A 107 7743 7904 10926 233 101 673 C ATOM 759 O GLN A 107 51.941 39.231 14.548 1.00 67.59 O ANISOU 759 O GLN A 107 7476 7731 10473 287 50 726 O ATOM 760 CB GLN A 107 53.008 40.467 17.303 1.00 79.54 C ANISOU 760 CB GLN A 107 8861 9089 12270 211 77 323 C ATOM 761 CG GLN A 107 53.640 39.821 18.492 1.00 87.25 C ANISOU 761 CG GLN A 107 9789 10179 13184 184 37 133 C ATOM 762 CD GLN A 107 52.804 38.712 19.019 1.00 90.05 C ANISOU 762 CD GLN A 107 10162 10680 13374 266 -18 97 C ATOM 763 OE1 GLN A 107 51.968 38.199 18.330 1.00 95.44 O ANISOU 763 OE1 GLN A 107 10876 11409 13978 326 -29 216 O ATOM 764 NE2 GLN A 107 53.014 38.354 20.251 1.00 91.53 N ANISOU 764 NE2 GLN A 107 10333 10936 13508 262 -57 -64 N ATOM 765 N ALA A 108 52.383 41.361 14.472 1.00 67.69 N ANISOU 765 N ALA A 108 7488 7440 10789 224 134 780 N ATOM 766 CA ALA A 108 51.429 41.595 13.401 1.00 62.38 C ANISOU 766 CA ALA A 108 6890 6729 10083 287 97 988 C ATOM 767 C ALA A 108 51.844 40.852 12.143 1.00 63.52 C ANISOU 767 C ALA A 108 7107 7003 10026 246 115 1131 C ATOM 768 O ALA A 108 50.999 40.308 11.423 1.00 69.81 O ANISOU 768 O ALA A 108 7962 7884 10680 304 39 1243 O ATOM 769 CB ALA A 108 51.310 43.093 13.124 1.00 60.37 C ANISOU 769 CB ALA A 108 6663 6229 10044 280 134 1094 C ATOM 770 N GLU A 109 53.141 40.825 11.852 1.00 56.13 N ANISOU 770 N GLU A 109 6163 6086 9078 144 219 1120 N ATOM 771 CA GLU A 109 53.600 40.065 10.698 1.00 57.59 C ANISOU 771 CA GLU A 109 6419 6402 9059 108 268 1227 C ATOM 772 C GLU A 109 53.336 38.570 10.866 1.00 57.81 C ANISOU 772 C GLU A 109 6443 6626 8895 159 203 1131 C ATOM 773 O GLU A 109 53.069 37.868 9.883 1.00 63.55 O ANISOU 773 O GLU A 109 7264 7457 9427 172 188 1223 O ATOM 774 CB GLU A 109 55.075 40.334 10.457 1.00 59.06 C ANISOU 774 CB GLU A 109 6566 6571 9305 -9 417 1217 C ATOM 775 CG GLU A 109 55.574 39.765 9.170 1.00 70.33 C ANISOU 775 CG GLU A 109 8080 8108 10535 -49 511 1339 C ATOM 776 CD GLU A 109 55.021 40.475 7.953 1.00 82.74 C ANISOU 776 CD GLU A 109 9802 9603 12032 -56 522 1584 C ATOM 777 OE1 GLU A 109 54.173 41.381 8.089 1.00 85.93 O ANISOU 777 OE1 GLU A 109 10233 9861 12557 -12 439 1671 O ATOM 778 OE2 GLU A 109 55.448 40.124 6.837 1.00 89.38 O ANISOU 778 OE2 GLU A 109 10742 10530 12689 -100 616 1693 O ATOM 779 N LEU A 110 53.424 38.060 12.095 1.00 48.55 N ANISOU 779 N LEU A 110 5177 5502 7769 183 164 945 N ATOM 780 CA LEU A 110 53.093 36.663 12.319 1.00 47.61 C ANISOU 780 CA LEU A 110 5060 5539 7488 233 100 867 C ATOM 781 C LEU A 110 51.616 36.395 12.020 1.00 47.16 C ANISOU 781 C LEU A 110 5060 5506 7353 307 -12 946 C ATOM 782 O LEU A 110 51.275 35.375 11.410 1.00 48.10 O ANISOU 782 O LEU A 110 5239 5737 7299 322 -55 974 O ATOM 783 CB LEU A 110 53.465 36.261 13.749 1.00 46.63 C ANISOU 783 CB LEU A 110 4838 5451 7428 242 74 677 C ATOM 784 CG LEU A 110 52.948 34.887 14.174 1.00 50.71 C ANISOU 784 CG LEU A 110 5363 6100 7805 298 -1 607 C ATOM 785 CD1 LEU A 110 53.561 33.784 13.305 1.00 45.27 C ANISOU 785 CD1 LEU A 110 4718 5517 6965 286 37 631 C ATOM 786 CD2 LEU A 110 53.203 34.640 15.671 1.00 44.90 C ANISOU 786 CD2 LEU A 110 4551 5388 7121 309 -36 444 C ATOM 787 N GLY A 111 50.725 37.291 12.453 1.00 52.40 N ANISOU 787 N GLY A 111 5696 6059 8156 353 -60 971 N ATOM 788 CA GLY A 111 49.304 37.099 12.192 1.00 43.14 C ANISOU 788 CA GLY A 111 4537 4905 6948 427 -170 1049 C ATOM 789 C GLY A 111 48.959 37.226 10.719 1.00 43.51 C ANISOU 789 C GLY A 111 4688 4961 6883 422 -216 1248 C ATOM 790 O GLY A 111 48.192 36.426 10.175 1.00 47.05 O ANISOU 790 O GLY A 111 5175 5511 7191 445 -315 1295 O ATOM 791 N ARG A 112 49.541 38.213 10.051 1.00 49.11 N ANISOU 791 N ARG A 112 5453 5565 7643 381 -148 1369 N ATOM 792 CA ARG A 112 49.340 38.376 8.619 1.00 52.77 C ANISOU 792 CA ARG A 112 6044 6042 7966 366 -181 1575 C ATOM 793 C ARG A 112 49.744 37.070 7.937 1.00 57.37 C ANISOU 793 C ARG A 112 6708 6803 8288 323 -170 1541 C ATOM 794 O ARG A 112 48.918 36.406 7.291 1.00 57.48 O ANISOU 794 O ARG A 112 6788 6911 8142 347 -290 1598 O ATOM 795 CB ARG A 112 50.112 39.613 8.143 1.00 53.52 C ANISOU 795 CB ARG A 112 6188 5986 8162 310 -71 1701 C ATOM 796 CG ARG A 112 49.807 40.004 6.714 1.00 45.97 C ANISOU 796 CG ARG A 112 5382 5019 7067 300 -111 1950 C ATOM 797 CD ARG A 112 50.507 41.272 6.329 1.00 53.30 C ANISOU 797 CD ARG A 112 6357 5774 8119 240 7 2091 C ATOM 798 NE ARG A 112 51.932 41.059 6.105 1.00 70.05 N ANISOU 798 NE ARG A 112 8496 7943 10177 125 194 2040 N ATOM 799 CZ ARG A 112 52.454 40.556 4.987 1.00 77.09 C ANISOU 799 CZ ARG A 112 9515 8954 10823 63 273 2132 C ATOM 800 NH1 ARG A 112 51.674 40.200 3.970 1.00 80.73 N ANISOU 800 NH1 ARG A 112 10120 9504 11048 96 160 2277 N ATOM 801 NH2 ARG A 112 53.766 40.406 4.886 1.00 80.97 N ANISOU 801 NH2 ARG A 112 9984 9478 11302 -33 465 2071 N ATOM 802 N LYS A 113 51.016 36.685 8.072 1.00 55.37 N ANISOU 802 N LYS A 113 6444 6591 8002 260 -29 1441 N ATOM 803 CA LYS A 113 51.561 35.583 7.285 1.00 49.91 C ANISOU 803 CA LYS A 113 5843 6041 7081 223 23 1415 C ATOM 804 C LYS A 113 50.810 34.292 7.551 1.00 49.46 C ANISOU 804 C LYS A 113 5782 6098 6913 267 -95 1311 C ATOM 805 O LYS A 113 50.625 33.472 6.642 1.00 48.00 O ANISOU 805 O LYS A 113 5713 6011 6513 253 -128 1333 O ATOM 806 CB LYS A 113 53.041 35.401 7.606 1.00 54.41 C ANISOU 806 CB LYS A 113 6348 6624 7700 168 194 1304 C ATOM 807 CG LYS A 113 53.928 36.527 7.062 1.00 60.55 C ANISOU 807 CG LYS A 113 7144 7307 8556 93 342 1420 C ATOM 808 CD LYS A 113 54.140 36.394 5.582 1.00 60.38 C ANISOU 808 CD LYS A 113 7289 7349 8303 48 421 1563 C ATOM 809 CE LYS A 113 55.432 37.051 5.145 1.00 71.60 C ANISOU 809 CE LYS A 113 8700 8723 9783 -47 637 1621 C ATOM 810 NZ LYS A 113 55.690 36.747 3.705 1.00 78.49 N ANISOU 810 NZ LYS A 113 9751 9687 10383 -91 745 1741 N ATOM 811 N LEU A 114 50.375 34.096 8.796 1.00 40.63 N ANISOU 811 N LEU A 114 4542 4962 5933 312 -154 1193 N ATOM 812 CA LEU A 114 49.655 32.887 9.147 1.00 40.79 C ANISOU 812 CA LEU A 114 4550 5072 5874 342 -253 1102 C ATOM 813 C LEU A 114 48.294 32.859 8.469 1.00 43.41 C ANISOU 813 C LEU A 114 4931 5426 6135 364 -410 1215 C ATOM 814 O LEU A 114 47.877 31.817 7.948 1.00 48.75 O ANISOU 814 O LEU A 114 5675 6195 6652 349 -486 1194 O ATOM 815 CB LEU A 114 49.516 32.779 10.673 1.00 42.53 C ANISOU 815 CB LEU A 114 4639 5269 6252 377 -260 968 C ATOM 816 CG LEU A 114 48.789 31.512 11.140 1.00 44.76 C ANISOU 816 CG LEU A 114 4906 5633 6467 397 -344 885 C ATOM 817 CD1 LEU A 114 49.683 30.263 10.983 1.00 43.55 C ANISOU 817 CD1 LEU A 114 4805 5555 6187 373 -290 792 C ATOM 818 CD2 LEU A 114 48.269 31.641 12.573 1.00 46.68 C ANISOU 818 CD2 LEU A 114 5036 5848 6853 434 -361 799 C ATOM 819 N ALA A 115 47.587 33.992 8.473 1.00 42.08 N ANISOU 819 N ALA A 115 4723 5167 6100 402 -468 1331 N ATOM 820 CA ALA A 115 46.289 34.057 7.806 1.00 45.36 C ANISOU 820 CA ALA A 115 5159 5601 6474 433 -640 1457 C ATOM 821 C ALA A 115 46.433 33.826 6.311 1.00 47.35 C ANISOU 821 C ALA A 115 5585 5924 6481 384 -683 1577 C ATOM 822 O ALA A 115 45.621 33.117 5.712 1.00 51.39 O ANISOU 822 O ALA A 115 6147 6524 6856 375 -831 1601 O ATOM 823 CB ALA A 115 45.610 35.395 8.093 1.00 48.33 C ANISOU 823 CB ALA A 115 5450 5843 7069 501 -682 1565 C ATOM 824 N GLU A 116 47.488 34.376 5.701 1.00 45.39 N ANISOU 824 N GLU A 116 5437 5644 6167 342 -549 1645 N ATOM 825 CA GLU A 116 47.769 34.100 4.290 1.00 47.79 C ANISOU 825 CA GLU A 116 5932 6030 6197 286 -549 1744 C ATOM 826 C GLU A 116 48.001 32.616 4.037 1.00 49.53 C ANISOU 826 C GLU A 116 6224 6382 6215 248 -540 1592 C ATOM 827 O GLU A 116 47.634 32.101 2.973 1.00 53.88 O ANISOU 827 O GLU A 116 6924 7021 6524 215 -631 1639 O ATOM 828 CB GLU A 116 48.988 34.896 3.810 1.00 48.11 C ANISOU 828 CB GLU A 116 6048 6013 6218 236 -355 1826 C ATOM 829 CG GLU A 116 48.880 36.442 3.867 1.00 58.82 C ANISOU 829 CG GLU A 116 7373 7208 7766 257 -347 1999 C ATOM 830 CD GLU A 116 47.975 37.053 2.805 1.00 80.06 C ANISOU 830 CD GLU A 116 10186 9883 10351 278 -507 2240 C ATOM 831 OE1 GLU A 116 47.886 38.309 2.752 1.00 89.32 O ANISOU 831 OE1 GLU A 116 11352 10905 11680 301 -503 2404 O ATOM 832 OE2 GLU A 116 47.368 36.295 2.011 1.00 86.00 O ANISOU 832 OE2 GLU A 116 11046 10764 10867 270 -646 2268 O ATOM 833 N MET A 117 48.651 31.914 4.976 1.00 44.74 N ANISOU 833 N MET A 117 5524 5782 5694 253 -434 1409 N ATOM 834 CA MET A 117 48.873 30.480 4.784 1.00 43.71 C ANISOU 834 CA MET A 117 5459 5747 5403 229 -423 1263 C ATOM 835 C MET A 117 47.552 29.719 4.843 1.00 47.44 C ANISOU 835 C MET A 117 5919 6264 5841 235 -629 1236 C ATOM 836 O MET A 117 47.319 28.806 4.044 1.00 53.95 O ANISOU 836 O MET A 117 6872 7166 6460 194 -694 1195 O ATOM 837 CB MET A 117 49.844 29.923 5.832 1.00 46.92 C ANISOU 837 CB MET A 117 5758 6137 5934 245 -284 1096 C ATOM 838 CG MET A 117 50.217 28.449 5.584 1.00 49.79 C ANISOU 838 CG MET A 117 6197 6570 6151 233 -249 950 C ATOM 839 SD MET A 117 51.220 27.626 6.864 1.00 55.15 S ANISOU 839 SD MET A 117 6744 7227 6984 273 -135 771 S ATOM 840 CE MET A 117 50.013 27.256 8.162 1.00 45.23 C ANISOU 840 CE MET A 117 5370 5946 5870 303 -300 730 C ATOM 841 N HIS A 118 46.684 30.070 5.797 1.00 51.77 N ANISOU 841 N HIS A 118 6311 6764 6596 279 -723 1246 N ATOM 842 CA HIS A 118 45.341 29.494 5.844 1.00 54.24 C ANISOU 842 CA HIS A 118 6579 7116 6915 278 -916 1243 C ATOM 843 C HIS A 118 44.598 29.731 4.537 1.00 56.18 C ANISOU 843 C HIS A 118 6940 7412 6994 251 -1086 1385 C ATOM 844 O HIS A 118 43.898 28.847 4.042 1.00 56.80 O ANISOU 844 O HIS A 118 7070 7562 6948 207 -1232 1349 O ATOM 845 CB HIS A 118 44.546 30.092 7.003 1.00 43.57 C ANISOU 845 CB HIS A 118 5031 5699 5824 337 -957 1255 C ATOM 846 CG HIS A 118 45.054 29.711 8.348 1.00 47.08 C ANISOU 846 CG HIS A 118 5376 6116 6398 355 -833 1111 C ATOM 847 ND1 HIS A 118 44.652 30.349 9.497 1.00 48.49 N ANISOU 847 ND1 HIS A 118 5403 6232 6789 408 -808 1095 N ATOM 848 CD2 HIS A 118 45.927 28.748 8.734 1.00 47.60 C ANISOU 848 CD2 HIS A 118 5476 6206 6402 332 -733 977 C ATOM 849 CE1 HIS A 118 45.246 29.790 10.537 1.00 46.32 C ANISOU 849 CE1 HIS A 118 5088 5958 6553 407 -709 963 C ATOM 850 NE2 HIS A 118 46.026 28.817 10.100 1.00 45.76 N ANISOU 850 NE2 HIS A 118 5121 5936 6329 366 -670 899 N ATOM 851 N LYS A 119 44.734 30.926 3.972 1.00 55.98 N ANISOU 851 N LYS A 119 6960 7344 6966 273 -1079 1553 N ATOM 852 CA LYS A 119 43.980 31.271 2.777 1.00 54.14 C ANISOU 852 CA LYS A 119 6836 7156 6577 259 -1266 1721 C ATOM 853 C LYS A 119 44.546 30.574 1.543 1.00 55.65 C ANISOU 853 C LYS A 119 7268 7449 6426 180 -1244 1700 C ATOM 854 O LYS A 119 43.792 30.039 0.726 1.00 59.95 O ANISOU 854 O LYS A 119 7910 8081 6786 137 -1437 1721 O ATOM 855 CB LYS A 119 43.984 32.785 2.615 1.00 51.44 C ANISOU 855 CB LYS A 119 6477 6715 6354 313 -1256 1923 C ATOM 856 CG LYS A 119 43.096 33.311 1.539 1.00 56.46 C ANISOU 856 CG LYS A 119 7196 7376 6879 323 -1478 2134 C ATOM 857 CD LYS A 119 43.198 34.829 1.478 1.00 63.44 C ANISOU 857 CD LYS A 119 8064 8125 7916 386 -1443 2338 C ATOM 858 CE LYS A 119 42.499 35.386 0.244 1.00 69.21 C ANISOU 858 CE LYS A 119 8923 8882 8492 395 -1660 2587 C ATOM 859 NZ LYS A 119 42.544 36.875 0.184 1.00 71.01 N ANISOU 859 NZ LYS A 119 9139 8948 8893 464 -1636 2807 N ATOM 860 N ALA A 120 45.873 30.535 1.406 1.00 55.46 N ANISOU 860 N ALA A 120 7338 7419 6315 156 -1009 1643 N ATOM 861 CA ALA A 120 46.482 29.930 0.227 1.00 56.76 C ANISOU 861 CA ALA A 120 7737 7678 6152 88 -943 1612 C ATOM 862 C ALA A 120 46.457 28.409 0.259 1.00 57.88 C ANISOU 862 C ALA A 120 7924 7885 6183 50 -958 1395 C ATOM 863 O ALA A 120 46.367 27.778 -0.796 1.00 64.52 O ANISOU 863 O ALA A 120 8964 8813 6738 -9 -1015 1362 O ATOM 864 CB ALA A 120 47.931 30.393 0.077 1.00 48.53 C ANISOU 864 CB ALA A 120 6751 6605 5082 76 -658 1620 C ATOM 865 N GLY A 121 46.545 27.801 1.436 1.00 56.66 N ANISOU 865 N GLY A 121 7606 7683 6240 81 -908 1245 N ATOM 866 CA GLY A 121 46.616 26.355 1.503 1.00 59.49 C ANISOU 866 CA GLY A 121 8013 8072 6518 48 -904 1047 C ATOM 867 C GLY A 121 45.291 25.637 1.367 1.00 62.29 C ANISOU 867 C GLY A 121 8364 8463 6841 4 -1157 1016 C ATOM 868 O GLY A 121 44.515 25.590 2.318 1.00 69.41 O ANISOU 868 O GLY A 121 9080 9325 7967 26 -1253 1012 O ATOM 869 N LYS A 122 45.044 25.036 0.204 1.00 65.23 N ANISOU 869 N LYS A 122 8939 8912 6935 -66 -1257 981 N ATOM 870 CA LYS A 122 43.751 24.461 -0.136 1.00 65.65 C ANISOU 870 CA LYS A 122 9000 9010 6934 -130 -1533 966 C ATOM 871 C LYS A 122 43.906 23.015 -0.587 1.00 68.12 C ANISOU 871 C LYS A 122 9473 9342 7069 -205 -1531 754 C ATOM 872 O LYS A 122 44.998 22.557 -0.941 1.00 65.85 O ANISOU 872 O LYS A 122 9334 9050 6637 -202 -1324 639 O ATOM 873 CB LYS A 122 43.031 25.273 -1.231 1.00 71.92 C ANISOU 873 CB LYS A 122 9894 9884 7549 -156 -1744 1155 C ATOM 874 CG LYS A 122 42.728 26.707 -0.821 1.00 83.58 C ANISOU 874 CG LYS A 122 11211 11315 9229 -75 -1773 1374 C ATOM 875 CD LYS A 122 42.105 27.505 -1.954 1.00 90.85 C ANISOU 875 CD LYS A 122 12249 12304 9967 -88 -1983 1584 C ATOM 876 CE LYS A 122 41.752 28.911 -1.490 1.00 95.05 C ANISOU 876 CE LYS A 122 12611 12758 10747 7 -2015 1800 C ATOM 877 NZ LYS A 122 41.165 29.737 -2.577 1.00102.71 N ANISOU 877 NZ LYS A 122 13694 13776 11554 9 -2228 2035 N ATOM 878 N THR A 123 42.782 22.301 -0.571 1.00 66.99 N ANISOU 878 N THR A 123 9288 9210 6957 -275 -1762 698 N ATOM 879 CA THR A 123 42.737 20.905 -0.975 1.00 65.21 C ANISOU 879 CA THR A 123 9208 8977 6591 -362 -1799 490 C ATOM 880 C THR A 123 41.363 20.586 -1.539 1.00 71.40 C ANISOU 880 C THR A 123 9999 9821 7309 -468 -2129 503 C ATOM 881 O THR A 123 40.346 21.132 -1.099 1.00 75.54 O ANISOU 881 O THR A 123 10316 10357 8030 -461 -2308 635 O ATOM 882 CB THR A 123 43.036 19.950 0.188 1.00 68.80 C ANISOU 882 CB THR A 123 9543 9318 7279 -342 -1667 340 C ATOM 883 OG1 THR A 123 43.140 18.611 -0.315 1.00 66.76 O ANISOU 883 OG1 THR A 123 9462 9028 6877 -420 -1676 133 O ATOM 884 CG2 THR A 123 41.928 20.025 1.266 1.00 48.32 C ANISOU 884 CG2 THR A 123 6685 6688 4986 -348 -1809 408 C ATOM 885 N SER A 124 41.351 19.687 -2.519 1.00 69.29 N ANISOU 885 N SER A 124 9968 9590 6771 -566 -2207 352 N ATOM 886 CA SER A 124 40.127 19.153 -3.103 1.00 71.82 C ANISOU 886 CA SER A 124 10317 9963 7010 -693 -2532 313 C ATOM 887 C SER A 124 39.641 17.884 -2.416 1.00 70.98 C ANISOU 887 C SER A 124 10115 9754 7101 -772 -2577 133 C ATOM 888 O SER A 124 38.581 17.371 -2.784 1.00 75.84 O ANISOU 888 O SER A 124 10716 10397 7701 -895 -2850 88 O ATOM 889 CB SER A 124 40.344 18.885 -4.592 1.00 77.99 C ANISOU 889 CB SER A 124 11433 10840 7358 -774 -2609 234 C ATOM 890 OG SER A 124 41.647 18.363 -4.814 1.00 84.16 O ANISOU 890 OG SER A 124 12417 11578 7983 -741 -2304 72 O ATOM 891 N LYS A 125 40.390 17.367 -1.435 1.00 69.71 N ANISOU 891 N LYS A 125 9886 9472 7128 -710 -2326 39 N ATOM 892 CA LYS A 125 40.110 16.083 -0.806 1.00 68.66 C ANISOU 892 CA LYS A 125 9706 9217 7162 -781 -2328 -128 C ATOM 893 C LYS A 125 39.329 16.189 0.501 1.00 69.90 C ANISOU 893 C LYS A 125 9554 9322 7684 -772 -2368 -31 C ATOM 894 O LYS A 125 38.980 15.156 1.081 1.00 74.99 O ANISOU 894 O LYS A 125 10145 9862 8486 -844 -2378 -139 O ATOM 895 CB LYS A 125 41.421 15.329 -0.582 1.00 73.23 C ANISOU 895 CB LYS A 125 10424 9687 7711 -717 -2037 -291 C ATOM 896 CG LYS A 125 42.245 15.233 -1.845 1.00 81.56 C ANISOU 896 CG LYS A 125 11778 10796 8413 -717 -1948 -398 C ATOM 897 CD LYS A 125 43.549 14.496 -1.655 1.00 87.66 C ANISOU 897 CD LYS A 125 12663 11459 9184 -637 -1651 -564 C ATOM 898 CE LYS A 125 44.341 14.487 -2.954 1.00 95.03 C ANISOU 898 CE LYS A 125 13888 12462 9757 -636 -1535 -669 C ATOM 899 NZ LYS A 125 45.767 14.133 -2.726 1.00 96.10 N ANISOU 899 NZ LYS A 125 14074 12515 9926 -517 -1199 -778 N ATOM 900 N GLY A 126 39.032 17.396 0.972 1.00 66.38 N ANISOU 900 N GLY A 126 8912 8935 7373 -688 -2380 167 N ATOM 901 CA GLY A 126 38.283 17.561 2.205 1.00 52.94 C ANISOU 901 CA GLY A 126 6921 7193 6000 -673 -2392 251 C ATOM 902 C GLY A 126 39.164 17.821 3.411 1.00 59.36 C ANISOU 902 C GLY A 126 7643 7933 6977 -550 -2119 274 C ATOM 903 O GLY A 126 40.254 18.390 3.281 1.00 60.74 O ANISOU 903 O GLY A 126 7912 8119 7050 -451 -1949 295 O ATOM 904 N PHE A 127 38.704 17.409 4.588 1.00 55.97 N ANISOU 904 N PHE A 127 7033 7436 6799 -563 -2077 273 N ATOM 905 CA PHE A 127 39.438 17.626 5.831 1.00 55.68 C ANISOU 905 CA PHE A 127 6906 7338 6912 -456 -1847 298 C ATOM 906 C PHE A 127 40.311 16.416 6.139 1.00 54.82 C ANISOU 906 C PHE A 127 6933 7117 6777 -463 -1703 152 C ATOM 907 O PHE A 127 39.878 15.271 5.986 1.00 62.77 O ANISOU 907 O PHE A 127 8000 8055 7794 -571 -1779 49 O ATOM 908 CB PHE A 127 38.462 17.910 6.978 1.00 50.95 C ANISOU 908 CB PHE A 127 6046 6735 6578 -459 -1864 389 C ATOM 909 CG PHE A 127 37.513 19.046 6.683 1.00 55.20 C ANISOU 909 CG PHE A 127 6424 7365 7183 -441 -2013 528 C ATOM 910 CD1 PHE A 127 37.938 20.368 6.783 1.00 52.47 C ANISOU 910 CD1 PHE A 127 6036 7055 6844 -316 -1937 637 C ATOM 911 CD2 PHE A 127 36.212 18.796 6.279 1.00 60.21 C ANISOU 911 CD2 PHE A 127 6947 8039 7890 -547 -2238 551 C ATOM 912 CE1 PHE A 127 37.084 21.418 6.511 1.00 54.79 C ANISOU 912 CE1 PHE A 127 6187 7409 7221 -282 -2073 773 C ATOM 913 CE2 PHE A 127 35.338 19.848 5.992 1.00 63.43 C ANISOU 913 CE2 PHE A 127 7191 8528 8383 -512 -2389 689 C ATOM 914 CZ PHE A 127 35.776 21.161 6.110 1.00 60.31 C ANISOU 914 CZ PHE A 127 6763 8153 7997 -371 -2303 804 C ATOM 915 N GLY A 128 41.553 16.670 6.528 1.00 50.32 N ANISOU 915 N GLY A 128 6412 6522 6186 -348 -1503 143 N ATOM 916 CA GLY A 128 42.489 15.590 6.764 1.00 42.85 C ANISOU 916 CA GLY A 128 5588 5466 5225 -326 -1367 15 C ATOM 917 C GLY A 128 43.842 15.928 6.178 1.00 50.19 C ANISOU 917 C GLY A 128 6650 6416 6003 -230 -1216 -28 C ATOM 918 O GLY A 128 44.185 17.109 6.052 1.00 54.70 O ANISOU 918 O GLY A 128 7174 7070 6539 -165 -1171 70 O ATOM 919 N PHE A 129 44.600 14.905 5.788 1.00 51.92 N ANISOU 919 N PHE A 129 7030 6551 6143 -222 -1130 -174 N ATOM 920 CA PHE A 129 45.949 15.089 5.266 1.00 53.59 C ANISOU 920 CA PHE A 129 7352 6775 6236 -128 -952 -231 C ATOM 921 C PHE A 129 46.365 13.831 4.503 1.00 56.18 C ANISOU 921 C PHE A 129 7886 7011 6450 -154 -908 -422 C ATOM 922 O PHE A 129 45.739 12.774 4.609 1.00 62.29 O ANISOU 922 O PHE A 129 8706 7684 7277 -234 -1001 -507 O ATOM 923 CB PHE A 129 46.945 15.421 6.399 1.00 44.63 C ANISOU 923 CB PHE A 129 6085 5609 5265 -3 -787 -180 C ATOM 924 CG PHE A 129 48.202 16.152 5.923 1.00 47.99 C ANISOU 924 CG PHE A 129 6539 6091 5604 87 -617 -178 C ATOM 925 CD1 PHE A 129 48.107 17.384 5.270 1.00 43.53 C ANISOU 925 CD1 PHE A 129 5973 5640 4927 74 -632 -76 C ATOM 926 CD2 PHE A 129 49.467 15.617 6.141 1.00 50.85 C ANISOU 926 CD2 PHE A 129 6918 6387 6018 183 -443 -265 C ATOM 927 CE1 PHE A 129 49.254 18.065 4.849 1.00 49.24 C ANISOU 927 CE1 PHE A 129 6716 6408 5585 139 -460 -63 C ATOM 928 CE2 PHE A 129 50.619 16.295 5.717 1.00 50.53 C ANISOU 928 CE2 PHE A 129 6874 6401 5924 255 -275 -261 C ATOM 929 CZ PHE A 129 50.509 17.515 5.067 1.00 45.66 C ANISOU 929 CZ PHE A 129 6262 5897 5189 224 -276 -160 C ATOM 930 N GLU A 130 47.450 13.962 3.738 1.00 60.27 N ANISOU 930 N GLU A 130 8526 7556 6820 -87 -749 -494 N ATOM 931 CA GLU A 130 47.949 12.865 2.912 1.00 65.33 C ANISOU 931 CA GLU A 130 9377 8114 7334 -94 -670 -695 C ATOM 932 C GLU A 130 48.357 11.647 3.740 1.00 66.83 C ANISOU 932 C GLU A 130 9548 8120 7724 -39 -596 -792 C ATOM 933 O GLU A 130 48.182 10.507 3.294 1.00 69.24 O ANISOU 933 O GLU A 130 10009 8306 7992 -90 -621 -955 O ATOM 934 CB GLU A 130 49.152 13.373 2.117 1.00 88.42 C ANISOU 934 CB GLU A 130 12390 11110 10097 -11 -460 -732 C ATOM 935 CG GLU A 130 48.859 14.429 1.063 1.00113.59 C ANISOU 935 CG GLU A 130 15664 14461 13033 -71 -512 -647 C ATOM 936 CD GLU A 130 50.128 14.940 0.361 1.00131.05 C ANISOU 936 CD GLU A 130 17952 16738 15102 6 -263 -667 C ATOM 937 OE1 GLU A 130 51.253 14.619 0.813 1.00132.22 O ANISOU 937 OE1 GLU A 130 18033 16817 15390 117 -54 -731 O ATOM 938 OE2 GLU A 130 49.995 15.651 -0.659 1.00136.67 O ANISOU 938 OE2 GLU A 130 18790 17572 15564 -48 -278 -612 O ATOM 939 N VAL A 131 48.898 11.860 4.942 1.00 57.69 N ANISOU 939 N VAL A 131 8214 6929 6778 64 -516 -695 N ATOM 940 CA VAL A 131 49.318 10.786 5.833 1.00 65.70 C ANISOU 940 CA VAL A 131 9201 7772 7990 131 -460 -745 C ATOM 941 C VAL A 131 48.888 11.110 7.259 1.00 62.53 C ANISOU 941 C VAL A 131 8606 7371 7783 139 -531 -579 C ATOM 942 O VAL A 131 48.664 12.267 7.619 1.00 56.25 O ANISOU 942 O VAL A 131 7677 6705 6989 139 -561 -445 O ATOM 943 CB VAL A 131 50.853 10.549 5.794 1.00 70.51 C ANISOU 943 CB VAL A 131 9817 8329 8644 292 -242 -824 C ATOM 944 CG1 VAL A 131 51.290 10.072 4.420 1.00 76.37 C ANISOU 944 CG1 VAL A 131 10767 9053 9196 289 -135 -1013 C ATOM 945 CG2 VAL A 131 51.623 11.820 6.204 1.00 66.99 C ANISOU 945 CG2 VAL A 131 9200 8018 8233 378 -149 -694 C ATOM 946 N ASP A 132 48.744 10.063 8.070 1.00 63.88 N ANISOU 946 N ASP A 132 8774 7385 8111 142 -553 -591 N ATOM 947 CA ASP A 132 48.682 10.271 9.507 1.00 58.99 C ANISOU 947 CA ASP A 132 7995 6760 7660 183 -568 -443 C ATOM 948 C ASP A 132 50.034 10.783 9.992 1.00 58.76 C ANISOU 948 C ASP A 132 7872 6769 7686 343 -435 -408 C ATOM 949 O ASP A 132 51.078 10.434 9.441 1.00 63.04 O ANISOU 949 O ASP A 132 8476 7264 8214 438 -315 -512 O ATOM 950 CB ASP A 132 48.306 8.983 10.230 1.00 61.81 C ANISOU 950 CB ASP A 132 8395 6931 8160 151 -609 -448 C ATOM 951 CG ASP A 132 46.885 8.528 9.917 1.00 75.87 C ANISOU 951 CG ASP A 132 10225 8676 9927 -31 -752 -466 C ATOM 952 OD1 ASP A 132 46.161 9.248 9.192 1.00 80.66 O ANISOU 952 OD1 ASP A 132 10817 9415 10414 -122 -839 -465 O ATOM 953 OD2 ASP A 132 46.478 7.461 10.424 1.00 78.61 O ANISOU 953 OD2 ASP A 132 10615 8859 10395 -87 -785 -468 O ATOM 954 N ASN A 133 50.005 11.663 10.998 1.00 49.30 N ANISOU 954 N ASN A 133 6518 5662 6552 369 -453 -270 N ATOM 955 CA ASN A 133 51.232 12.180 11.597 1.00 44.49 C ANISOU 955 CA ASN A 133 5799 5093 6014 502 -359 -231 C ATOM 956 C ASN A 133 51.074 12.168 13.114 1.00 47.57 C ANISOU 956 C ASN A 133 6085 5467 6521 524 -414 -110 C ATOM 957 O ASN A 133 50.355 11.328 13.663 1.00 53.69 O ANISOU 957 O ASN A 133 6906 6146 7348 470 -479 -78 O ATOM 958 CB ASN A 133 51.586 13.584 11.067 1.00 43.56 C ANISOU 958 CB ASN A 133 5610 5132 5810 509 -307 -205 C ATOM 959 CG ASN A 133 50.410 14.599 11.121 1.00 48.65 C ANISOU 959 CG ASN A 133 6201 5884 6398 405 -408 -110 C ATOM 960 OD1 ASN A 133 49.466 14.462 11.896 1.00 54.29 O ANISOU 960 OD1 ASN A 133 6874 6585 7169 347 -499 -43 O ATOM 961 ND2 ASN A 133 50.481 15.620 10.265 1.00 48.34 N ANISOU 961 ND2 ASN A 133 6163 5949 6256 385 -380 -98 N ATOM 962 N THR A 134 51.738 13.068 13.814 1.00 40.89 N ANISOU 962 N THR A 134 5112 4713 5713 593 -387 -45 N ATOM 963 CA THR A 134 51.715 13.015 15.266 1.00 51.15 C ANISOU 963 CA THR A 134 6337 6004 7091 621 -437 57 C ATOM 964 C THR A 134 51.622 14.430 15.802 1.00 54.04 C ANISOU 964 C THR A 134 6582 6516 7436 606 -447 123 C ATOM 965 O THR A 134 52.095 15.371 15.166 1.00 56.47 O ANISOU 965 O THR A 134 6840 6905 7712 620 -396 94 O ATOM 966 CB THR A 134 52.966 12.312 15.852 1.00 54.62 C ANISOU 966 CB THR A 134 6756 6361 7635 759 -411 54 C ATOM 967 OG1 THR A 134 54.160 12.931 15.354 1.00 50.84 O ANISOU 967 OG1 THR A 134 6195 5946 7177 846 -329 -2 O ATOM 968 CG2 THR A 134 52.994 10.825 15.477 1.00 53.74 C ANISOU 968 CG2 THR A 134 6774 6067 7577 784 -402 -5 C ATOM 969 N ILE A 135 50.985 14.575 16.963 1.00 46.96 N ANISOU 969 N ILE A 135 5647 5643 6554 572 -500 210 N ATOM 970 CA ILE A 135 50.923 15.838 17.684 1.00 48.59 C ANISOU 970 CA ILE A 135 5747 5965 6749 568 -505 258 C ATOM 971 C ILE A 135 51.670 15.612 18.991 1.00 59.12 C ANISOU 971 C ILE A 135 7048 7294 8120 642 -531 304 C ATOM 972 O ILE A 135 51.177 14.915 19.895 1.00 58.18 O ANISOU 972 O ILE A 135 6977 7132 7996 622 -567 371 O ATOM 973 CB ILE A 135 49.478 16.331 17.901 1.00 48.45 C ANISOU 973 CB ILE A 135 5710 5995 6703 465 -532 306 C ATOM 974 CG1 ILE A 135 49.464 17.560 18.795 1.00 49.89 C ANISOU 974 CG1 ILE A 135 5796 6274 6886 476 -522 339 C ATOM 975 CG2 ILE A 135 48.564 15.238 18.456 1.00 41.23 C ANISOU 975 CG2 ILE A 135 4857 5006 5803 402 -564 356 C ATOM 976 CD1 ILE A 135 50.316 18.641 18.273 1.00 52.62 C ANISOU 976 CD1 ILE A 135 6080 6674 7239 518 -490 299 C ATOM 977 N GLY A 136 52.877 16.165 19.078 1.00 57.77 N ANISOU 977 N GLY A 136 6798 7168 7985 721 -516 274 N ATOM 978 CA GLY A 136 53.800 15.668 20.086 1.00 53.88 C ANISOU 978 CA GLY A 136 6282 6653 7538 810 -567 309 C ATOM 979 C GLY A 136 54.185 14.262 19.661 1.00 60.26 C ANISOU 979 C GLY A 136 7165 7325 8405 874 -562 297 C ATOM 980 O GLY A 136 54.485 14.009 18.486 1.00 66.68 O ANISOU 980 O GLY A 136 7998 8093 9245 893 -494 216 O ATOM 981 N SER A 137 54.107 13.315 20.581 1.00 62.22 N ANISOU 981 N SER A 137 7476 7497 8669 904 -626 376 N ATOM 982 CA SER A 137 54.325 11.924 20.209 1.00 66.68 C ANISOU 982 CA SER A 137 8131 7897 9308 961 -621 370 C ATOM 983 C SER A 137 53.031 11.153 19.933 1.00 61.28 C ANISOU 983 C SER A 137 7576 7115 8591 849 -612 387 C ATOM 984 O SER A 137 53.097 9.987 19.536 1.00 60.29 O ANISOU 984 O SER A 137 7544 6830 8533 877 -603 365 O ATOM 985 CB SER A 137 55.154 11.215 21.295 1.00 67.74 C ANISOU 985 CB SER A 137 8260 7971 9507 1076 -706 461 C ATOM 986 OG SER A 137 54.334 10.757 22.358 1.00 75.21 O ANISOU 986 OG SER A 137 9300 8889 10389 1016 -765 586 O ATOM 987 N THR A 138 51.857 11.768 20.146 1.00 55.57 N ANISOU 987 N THR A 138 6852 6477 7787 724 -613 420 N ATOM 988 CA THR A 138 50.575 11.082 19.968 1.00 54.68 C ANISOU 988 CA THR A 138 6827 6284 7665 602 -614 444 C ATOM 989 C THR A 138 50.216 10.998 18.485 1.00 58.27 C ANISOU 989 C THR A 138 7317 6706 8116 547 -585 327 C ATOM 990 O THR A 138 50.328 12.002 17.778 1.00 56.96 O ANISOU 990 O THR A 138 7089 6653 7902 543 -560 266 O ATOM 991 CB THR A 138 49.471 11.830 20.699 1.00 53.83 C ANISOU 991 CB THR A 138 6673 6289 7493 498 -614 515 C ATOM 992 OG1 THR A 138 49.905 12.135 22.026 1.00 58.55 O ANISOU 992 OG1 THR A 138 7246 6950 8051 551 -635 601 O ATOM 993 CG2 THR A 138 48.178 11.011 20.749 1.00 49.27 C ANISOU 993 CG2 THR A 138 6161 5623 6935 367 -613 564 C ATOM 994 N PRO A 139 49.754 9.845 17.986 1.00 58.60 N ANISOU 994 N PRO A 139 7471 6596 8199 493 -593 293 N ATOM 995 CA PRO A 139 49.269 9.787 16.603 1.00 52.42 C ANISOU 995 CA PRO A 139 6740 5799 7380 417 -588 174 C ATOM 996 C PRO A 139 48.148 10.791 16.364 1.00 55.91 C ANISOU 996 C PRO A 139 7107 6383 7752 298 -619 195 C ATOM 997 O PRO A 139 47.316 11.058 17.239 1.00 55.51 O ANISOU 997 O PRO A 139 6997 6381 7715 231 -638 292 O ATOM 998 CB PRO A 139 48.759 8.348 16.464 1.00 48.99 C ANISOU 998 CB PRO A 139 6435 5163 7014 350 -612 154 C ATOM 999 CG PRO A 139 49.462 7.591 17.501 1.00 50.83 C ANISOU 999 CG PRO A 139 6696 5280 7335 452 -607 242 C ATOM 1000 CD PRO A 139 49.600 8.540 18.656 1.00 58.47 C ANISOU 1000 CD PRO A 139 7551 6404 8260 487 -616 365 C ATOM 1001 N GLN A 140 48.146 11.357 15.163 1.00 51.59 N ANISOU 1001 N GLN A 140 6566 5903 7131 280 -616 106 N ATOM 1002 CA GLN A 140 47.116 12.288 14.726 1.00 48.66 C ANISOU 1002 CA GLN A 140 6130 5655 6705 183 -664 125 C ATOM 1003 C GLN A 140 46.509 11.689 13.462 1.00 51.87 C ANISOU 1003 C GLN A 140 6641 6008 7060 85 -722 28 C ATOM 1004 O GLN A 140 47.165 11.642 12.417 1.00 53.48 O ANISOU 1004 O GLN A 140 6931 6207 7182 124 -692 -74 O ATOM 1005 CB GLN A 140 47.697 13.693 14.496 1.00 46.89 C ANISOU 1005 CB GLN A 140 5820 5572 6424 251 -625 134 C ATOM 1006 CG GLN A 140 46.651 14.752 14.059 1.00 52.10 C ANISOU 1006 CG GLN A 140 6406 6346 7044 171 -681 173 C ATOM 1007 CD GLN A 140 47.123 16.191 14.247 1.00 53.01 C ANISOU 1007 CD GLN A 140 6422 6573 7147 236 -638 215 C ATOM 1008 OE1 GLN A 140 46.787 16.830 15.244 1.00 48.77 O ANISOU 1008 OE1 GLN A 140 5785 6082 6662 242 -631 282 O ATOM 1009 NE2 GLN A 140 47.865 16.720 13.267 1.00 45.30 N ANISOU 1009 NE2 GLN A 140 5480 5633 6098 275 -599 172 N ATOM 1010 N ILE A 141 45.258 11.234 13.570 1.00 52.10 N ANISOU 1010 N ILE A 141 6661 6002 7134 -48 -803 55 N ATOM 1011 CA ILE A 141 44.578 10.506 12.499 1.00 54.33 C ANISOU 1011 CA ILE A 141 7044 6218 7382 -166 -889 -44 C ATOM 1012 C ILE A 141 44.021 11.501 11.485 1.00 57.44 C ANISOU 1012 C ILE A 141 7400 6758 7666 -216 -969 -58 C ATOM 1013 O ILE A 141 43.303 12.438 11.853 1.00 52.73 O ANISOU 1013 O ILE A 141 6659 6275 7100 -241 -1007 41 O ATOM 1014 CB ILE A 141 43.455 9.630 13.077 1.00 56.24 C ANISOU 1014 CB ILE A 141 7266 6360 7744 -304 -949 0 C ATOM 1015 CG1 ILE A 141 43.971 8.769 14.229 1.00 58.03 C ANISOU 1015 CG1 ILE A 141 7529 6448 8074 -249 -869 61 C ATOM 1016 CG2 ILE A 141 42.855 8.759 12.001 1.00 55.60 C ANISOU 1016 CG2 ILE A 141 7299 6185 7641 -436 -1049 -124 C ATOM 1017 CD1 ILE A 141 45.199 7.973 13.874 1.00 60.32 C ANISOU 1017 CD1 ILE A 141 7964 6600 8355 -137 -811 -36 C ATOM 1018 N ASN A 142 44.343 11.297 10.201 1.00 52.99 N ANISOU 1018 N ASN A 142 6975 6189 6970 -227 -993 -179 N ATOM 1019 CA ASN A 142 44.094 12.306 9.179 1.00 46.36 C ANISOU 1019 CA ASN A 142 6133 5493 5988 -247 -1058 -177 C ATOM 1020 C ASN A 142 43.274 11.760 8.011 1.00 59.63 C ANISOU 1020 C ASN A 142 7928 7163 7566 -385 -1207 -276 C ATOM 1021 O ASN A 142 43.334 12.289 6.893 1.00 56.68 O ANISOU 1021 O ASN A 142 7637 6884 7016 -395 -1255 -312 O ATOM 1022 CB ASN A 142 45.411 12.914 8.698 1.00 49.82 C ANISOU 1022 CB ASN A 142 6630 5985 6314 -119 -929 -209 C ATOM 1023 CG ASN A 142 46.038 13.819 9.750 1.00 55.36 C ANISOU 1023 CG ASN A 142 7185 6742 7108 -7 -830 -98 C ATOM 1024 OD1 ASN A 142 45.330 14.393 10.589 1.00 53.21 O ANISOU 1024 OD1 ASN A 142 6771 6517 6929 -29 -873 10 O ATOM 1025 ND2 ASN A 142 47.361 13.953 9.712 1.00 57.13 N ANISOU 1025 ND2 ASN A 142 7437 6960 7312 108 -695 -135 N ATOM 1026 N THR A 143 42.469 10.733 8.275 1.00 54.35 N ANISOU 1026 N THR A 143 7265 6381 7002 -503 -1289 -312 N ATOM 1027 CA THR A 143 41.635 10.123 7.253 1.00 54.88 C ANISOU 1027 CA THR A 143 7433 6425 6994 -657 -1453 -420 C ATOM 1028 C THR A 143 40.699 11.163 6.648 1.00 60.67 C ANISOU 1028 C THR A 143 8066 7333 7653 -720 -1618 -341 C ATOM 1029 O THR A 143 39.985 11.870 7.367 1.00 62.02 O ANISOU 1029 O THR A 143 8030 7579 7957 -725 -1653 -198 O ATOM 1030 CB THR A 143 40.822 8.983 7.887 1.00 61.04 C ANISOU 1030 CB THR A 143 8181 7052 7959 -788 -1510 -435 C ATOM 1031 OG1 THR A 143 41.714 7.972 8.366 1.00 70.63 O ANISOU 1031 OG1 THR A 143 9512 8083 9241 -720 -1370 -501 O ATOM 1032 CG2 THR A 143 39.849 8.367 6.891 1.00 50.09 C ANISOU 1032 CG2 THR A 143 6872 5640 6521 -974 -1708 -551 C ATOM 1033 N TRP A 144 40.693 11.234 5.318 1.00 58.32 N ANISOU 1033 N TRP A 144 7921 7096 7141 -766 -1720 -434 N ATOM 1034 CA TRP A 144 39.951 12.280 4.629 1.00 57.11 C ANISOU 1034 CA TRP A 144 7699 7112 6890 -803 -1888 -342 C ATOM 1035 C TRP A 144 38.466 12.198 4.943 1.00 61.38 C ANISOU 1035 C TRP A 144 8048 7672 7602 -939 -2084 -274 C ATOM 1036 O TRP A 144 37.850 11.135 4.832 1.00 65.35 O ANISOU 1036 O TRP A 144 8584 8078 8166 -1083 -2187 -374 O ATOM 1037 CB TRP A 144 40.161 12.192 3.119 1.00 54.14 C ANISOU 1037 CB TRP A 144 7557 6792 6221 -849 -1979 -462 C ATOM 1038 CG TRP A 144 41.534 12.496 2.668 1.00 59.97 C ANISOU 1038 CG TRP A 144 8457 7549 6779 -719 -1779 -508 C ATOM 1039 CD1 TRP A 144 42.438 11.621 2.140 1.00 62.92 C ANISOU 1039 CD1 TRP A 144 9052 7829 7026 -698 -1651 -692 C ATOM 1040 CD2 TRP A 144 42.182 13.778 2.695 1.00 62.93 C ANISOU 1040 CD2 TRP A 144 8776 8036 7098 -592 -1668 -372 C ATOM 1041 NE1 TRP A 144 43.607 12.282 1.821 1.00 67.11 N ANISOU 1041 NE1 TRP A 144 9653 8422 7423 -567 -1460 -675 N ATOM 1042 CE2 TRP A 144 43.479 13.603 2.160 1.00 64.16 C ANISOU 1042 CE2 TRP A 144 9114 8171 7091 -508 -1471 -477 C ATOM 1043 CE3 TRP A 144 41.785 15.058 3.099 1.00 59.54 C ANISOU 1043 CE3 TRP A 144 8158 7711 6752 -542 -1711 -178 C ATOM 1044 CZ2 TRP A 144 44.381 14.659 2.022 1.00 60.25 C ANISOU 1044 CZ2 TRP A 144 8611 7762 6519 -395 -1318 -385 C ATOM 1045 CZ3 TRP A 144 42.680 16.104 2.961 1.00 53.33 C ANISOU 1045 CZ3 TRP A 144 7384 6994 5887 -428 -1568 -92 C ATOM 1046 CH2 TRP A 144 43.966 15.898 2.429 1.00 56.44 C ANISOU 1046 CH2 TRP A 144 7954 7371 6122 -363 -1375 -191 C ATOM 1047 N SER A 145 37.886 13.350 5.269 1.00 65.21 N ANISOU 1047 N SER A 145 8328 8278 8170 -896 -2137 -108 N ATOM 1048 CA SER A 145 36.466 13.490 5.537 1.00 68.22 C ANISOU 1048 CA SER A 145 8482 8704 8733 -1001 -2313 -24 C ATOM 1049 C SER A 145 35.939 14.763 4.882 1.00 68.83 C ANISOU 1049 C SER A 145 8465 8941 8745 -962 -2470 101 C ATOM 1050 O SER A 145 36.684 15.723 4.656 1.00 69.89 O ANISOU 1050 O SER A 145 8658 9139 8759 -831 -2383 169 O ATOM 1051 CB SER A 145 36.204 13.534 7.033 1.00 68.51 C ANISOU 1051 CB SER A 145 8306 8693 9033 -967 -2167 70 C ATOM 1052 OG SER A 145 34.837 13.799 7.265 1.00 83.67 O ANISOU 1052 OG SER A 145 9980 10672 11140 -1055 -2311 158 O ATOM 1053 N SER A 146 34.642 14.763 4.574 1.00 69.80 N ANISOU 1053 N SER A 146 8434 9120 8966 -1079 -2708 140 N ATOM 1054 CA SER A 146 34.010 15.890 3.892 1.00 69.53 C ANISOU 1054 CA SER A 146 8301 9229 8889 -1046 -2903 271 C ATOM 1055 C SER A 146 33.177 16.770 4.816 1.00 71.06 C ANISOU 1055 C SER A 146 8166 9463 9369 -981 -2890 433 C ATOM 1056 O SER A 146 32.745 17.846 4.388 1.00 74.96 O ANISOU 1056 O SER A 146 8560 10056 9867 -913 -3020 564 O ATOM 1057 CB SER A 146 33.116 15.400 2.748 1.00 67.86 C ANISOU 1057 CB SER A 146 8136 9073 8574 -1210 -3225 208 C ATOM 1058 OG SER A 146 31.891 14.914 3.254 1.00 72.30 O ANISOU 1058 OG SER A 146 8445 9615 9410 -1339 -3351 217 O ATOM 1059 N ASP A 147 32.919 16.333 6.048 1.00 70.01 N ANISOU 1059 N ASP A 147 7871 9254 9474 -999 -2736 430 N ATOM 1060 CA ASP A 147 32.184 17.107 7.042 1.00 69.57 C ANISOU 1060 CA ASP A 147 7513 9230 9689 -933 -2669 560 C ATOM 1061 C ASP A 147 33.125 17.412 8.199 1.00 59.77 C ANISOU 1061 C ASP A 147 6298 7933 8481 -801 -2364 575 C ATOM 1062 O ASP A 147 33.749 16.498 8.749 1.00 59.03 O ANISOU 1062 O ASP A 147 6323 7744 8361 -834 -2215 489 O ATOM 1063 CB ASP A 147 30.949 16.334 7.537 1.00 77.32 C ANISOU 1063 CB ASP A 147 8267 10188 10924 -1089 -2744 549 C ATOM 1064 CG ASP A 147 30.146 17.096 8.599 1.00 90.60 C ANISOU 1064 CG ASP A 147 9624 11906 12894 -1020 -2641 672 C ATOM 1065 OD1 ASP A 147 30.100 18.342 8.556 1.00 97.95 O ANISOU 1065 OD1 ASP A 147 10457 12904 13854 -874 -2644 777 O ATOM 1066 OD2 ASP A 147 29.568 16.444 9.496 1.00 98.22 O ANISOU 1066 OD2 ASP A 147 10437 12822 14060 -1111 -2539 662 O ATOM 1067 N TRP A 148 33.237 18.697 8.557 1.00 57.97 N ANISOU 1067 N TRP A 148 6634 7231 8159 -544 -1493 906 N ATOM 1068 CA TRP A 148 34.189 19.091 9.597 1.00 54.53 C ANISOU 1068 CA TRP A 148 6286 6723 7708 -406 -1299 902 C ATOM 1069 C TRP A 148 33.721 18.656 10.980 1.00 52.78 C ANISOU 1069 C TRP A 148 5992 6424 7639 -423 -1175 980 C ATOM 1070 O TRP A 148 34.520 18.146 11.774 1.00 53.53 O ANISOU 1070 O TRP A 148 6211 6414 7716 -385 -1071 927 O ATOM 1071 CB TRP A 148 34.421 20.602 9.564 1.00 51.16 C ANISOU 1071 CB TRP A 148 5813 6387 7238 -256 -1221 979 C ATOM 1072 CG TRP A 148 35.193 21.101 10.738 1.00 54.52 C ANISOU 1072 CG TRP A 148 6296 6748 7670 -131 -1033 983 C ATOM 1073 CD1 TRP A 148 34.720 21.874 11.759 1.00 54.74 C ANISOU 1073 CD1 TRP A 148 6216 6787 7796 -49 -901 1089 C ATOM 1074 CD2 TRP A 148 36.575 20.847 11.035 1.00 49.39 C ANISOU 1074 CD2 TRP A 148 5825 6021 6920 -72 -959 870 C ATOM 1075 NE1 TRP A 148 35.719 22.119 12.670 1.00 48.46 N ANISOU 1075 NE1 TRP A 148 5531 5926 6955 46 -762 1038 N ATOM 1076 CE2 TRP A 148 36.867 21.499 12.248 1.00 46.39 C ANISOU 1076 CE2 TRP A 148 5434 5614 6577 31 -801 912 C ATOM 1077 CE3 TRP A 148 37.594 20.132 10.390 1.00 46.85 C ANISOU 1077 CE3 TRP A 148 5666 5656 6479 -92 -1011 735 C ATOM 1078 CZ2 TRP A 148 38.144 21.470 12.825 1.00 47.64 C ANISOU 1078 CZ2 TRP A 148 5727 5714 6659 105 -712 830 C ATOM 1079 CZ3 TRP A 148 38.843 20.091 10.967 1.00 44.34 C ANISOU 1079 CZ3 TRP A 148 5470 5277 6101 -7 -908 666 C ATOM 1080 CH2 TRP A 148 39.112 20.758 12.175 1.00 42.24 C ANISOU 1080 CH2 TRP A 148 5178 4995 5875 84 -769 716 C ATOM 1081 N ILE A 149 32.432 18.852 11.282 1.00 55.87 N ANISOU 1081 N ILE A 149 6176 6877 8174 -472 -1181 1117 N ATOM 1082 CA ILE A 149 31.879 18.476 12.583 1.00 59.96 C ANISOU 1082 CA ILE A 149 6606 7342 8834 -488 -1049 1213 C ATOM 1083 C ILE A 149 32.153 17.010 12.860 1.00 58.06 C ANISOU 1083 C ILE A 149 6480 6958 8622 -608 -1068 1140 C ATOM 1084 O ILE A 149 32.426 16.610 13.998 1.00 60.66 O ANISOU 1084 O ILE A 149 6855 7204 8988 -574 -928 1172 O ATOM 1085 CB ILE A 149 30.363 18.772 12.617 1.00 65.99 C ANISOU 1085 CB ILE A 149 7107 8208 9759 -547 -1079 1371 C ATOM 1086 CG1 ILE A 149 30.087 20.271 12.468 1.00 64.22 C ANISOU 1086 CG1 ILE A 149 6771 8107 9525 -397 -1033 1460 C ATOM 1087 CG2 ILE A 149 29.720 18.240 13.898 1.00 56.74 C ANISOU 1087 CG2 ILE A 149 5835 6988 8735 -583 -938 1480 C ATOM 1088 CD1 ILE A 149 28.611 20.621 12.473 1.00 60.50 C ANISOU 1088 CD1 ILE A 149 6022 7747 9218 -429 -1057 1627 C ATOM 1089 N GLU A 150 32.099 16.198 11.808 1.00 61.87 N ANISOU 1089 N GLU A 150 7020 7406 9082 -744 -1245 1040 N ATOM 1090 CA GLU A 150 32.340 14.765 11.895 1.00 63.60 C ANISOU 1090 CA GLU A 150 7363 7463 9341 -867 -1283 955 C ATOM 1091 C GLU A 150 33.825 14.474 12.065 1.00 63.93 C ANISOU 1091 C GLU A 150 7641 7400 9248 -758 -1209 829 C ATOM 1092 O GLU A 150 34.222 13.716 12.956 1.00 67.65 O ANISOU 1092 O GLU A 150 8196 7742 9765 -751 -1111 836 O ATOM 1093 CB GLU A 150 31.759 14.122 10.641 1.00 72.69 C ANISOU 1093 CB GLU A 150 8499 8619 10501 -1044 -1506 871 C ATOM 1094 CG GLU A 150 31.370 12.684 10.728 1.00 90.37 C ANISOU 1094 CG GLU A 150 10773 10696 12867 -1233 -1574 829 C ATOM 1095 CD GLU A 150 30.281 12.358 9.709 1.00105.58 C ANISOU 1095 CD GLU A 150 12574 12683 14857 -1431 -1797 810 C ATOM 1096 OE1 GLU A 150 29.219 13.028 9.740 1.00109.71 O ANISOU 1096 OE1 GLU A 150 12855 13356 15474 -1459 -1827 956 O ATOM 1097 OE2 GLU A 150 30.489 11.459 8.866 1.00111.28 O ANISOU 1097 OE2 GLU A 150 13438 13310 15535 -1553 -1945 644 O ATOM 1098 N PHE A 151 34.664 15.106 11.245 1.00 60.66 N ANISOU 1098 N PHE A 151 7326 7051 8671 -663 -1247 730 N ATOM 1099 CA PHE A 151 36.104 14.899 11.349 1.00 56.56 C ANISOU 1099 CA PHE A 151 7005 6455 8029 -552 -1175 617 C ATOM 1100 C PHE A 151 36.616 15.305 12.730 1.00 56.52 C ANISOU 1100 C PHE A 151 7001 6432 8041 -423 -992 697 C ATOM 1101 O PHE A 151 37.360 14.556 13.379 1.00 57.81 O ANISOU 1101 O PHE A 151 7284 6481 8200 -389 -923 663 O ATOM 1102 CB PHE A 151 36.835 15.686 10.255 1.00 49.18 C ANISOU 1102 CB PHE A 151 6140 5623 6924 -470 -1228 529 C ATOM 1103 CG PHE A 151 38.320 15.513 10.296 1.00 51.85 C ANISOU 1103 CG PHE A 151 6655 5900 7143 -356 -1153 421 C ATOM 1104 CD1 PHE A 151 39.111 16.326 11.108 1.00 54.98 C ANISOU 1104 CD1 PHE A 151 7057 6327 7507 -214 -1014 465 C ATOM 1105 CD2 PHE A 151 38.933 14.502 9.563 1.00 49.06 C ANISOU 1105 CD2 PHE A 151 6464 5457 6721 -390 -1219 270 C ATOM 1106 CE1 PHE A 151 40.493 16.156 11.171 1.00 51.47 C ANISOU 1106 CE1 PHE A 151 6750 5841 6966 -113 -951 375 C ATOM 1107 CE2 PHE A 151 40.311 14.326 9.614 1.00 51.50 C ANISOU 1107 CE2 PHE A 151 6917 5718 6934 -271 -1140 181 C ATOM 1108 CZ PHE A 151 41.093 15.153 10.419 1.00 47.99 C ANISOU 1108 CZ PHE A 151 6451 5319 6462 -135 -1009 240 C ATOM 1109 N TYR A 152 36.233 16.494 13.196 1.00 56.19 N ANISOU 1109 N TYR A 152 6833 6503 8013 -344 -915 802 N ATOM 1110 CA TYR A 152 36.771 16.977 14.460 1.00 53.24 C ANISOU 1110 CA TYR A 152 6477 6125 7625 -218 -751 852 C ATOM 1111 C TYR A 152 36.246 16.154 15.630 1.00 55.60 C ANISOU 1111 C TYR A 152 6743 6347 8035 -265 -666 945 C ATOM 1112 O TYR A 152 36.987 15.878 16.582 1.00 55.23 O ANISOU 1112 O TYR A 152 6789 6245 7949 -189 -565 946 O ATOM 1113 CB TYR A 152 36.444 18.461 14.644 1.00 55.93 C ANISOU 1113 CB TYR A 152 6704 6587 7959 -123 -687 926 C ATOM 1114 CG TYR A 152 37.203 19.075 15.796 1.00 55.05 C ANISOU 1114 CG TYR A 152 6645 6474 7796 11 -537 933 C ATOM 1115 CD1 TYR A 152 38.573 19.357 15.691 1.00 43.29 C ANISOU 1115 CD1 TYR A 152 5290 4973 6186 96 -521 832 C ATOM 1116 CD2 TYR A 152 36.560 19.375 16.988 1.00 53.36 C ANISOU 1116 CD2 TYR A 152 6346 6282 7648 50 -411 1037 C ATOM 1117 CE1 TYR A 152 39.280 19.915 16.765 1.00 44.54 C ANISOU 1117 CE1 TYR A 152 5492 5137 6294 204 -404 828 C ATOM 1118 CE2 TYR A 152 37.256 19.930 18.052 1.00 50.35 C ANISOU 1118 CE2 TYR A 152 6027 5907 7198 168 -285 1025 C ATOM 1119 CZ TYR A 152 38.602 20.196 17.938 1.00 46.91 C ANISOU 1119 CZ TYR A 152 5721 5456 6646 237 -293 918 C ATOM 1120 OH TYR A 152 39.253 20.746 19.012 1.00 53.54 O ANISOU 1120 OH TYR A 152 6614 6310 7418 339 -187 902 O ATOM 1121 N GLY A 153 34.970 15.751 15.570 1.00 56.58 N ANISOU 1121 N GLY A 153 6728 6474 8295 -393 -710 1035 N ATOM 1122 CA GLY A 153 34.382 14.969 16.654 1.00 47.55 C ANISOU 1122 CA GLY A 153 5536 5262 7270 -450 -618 1148 C ATOM 1123 C GLY A 153 34.972 13.578 16.783 1.00 53.14 C ANISOU 1123 C GLY A 153 6399 5800 7991 -512 -639 1093 C ATOM 1124 O GLY A 153 35.154 13.076 17.892 1.00 60.57 O ANISOU 1124 O GLY A 153 7381 6675 8956 -480 -523 1170 O ATOM 1125 N GLU A 154 35.289 12.940 15.661 1.00 51.42 N ANISOU 1125 N GLU A 154 6278 5506 7751 -591 -783 961 N ATOM 1126 CA GLU A 154 35.771 11.564 15.691 1.00 61.17 C ANISOU 1126 CA GLU A 154 7665 6553 9022 -653 -808 900 C ATOM 1127 C GLU A 154 37.291 11.513 15.740 1.00 61.15 C ANISOU 1127 C GLU A 154 7849 6507 8878 -502 -766 792 C ATOM 1128 O GLU A 154 37.865 10.994 16.699 1.00 64.85 O ANISOU 1128 O GLU A 154 8398 6892 9350 -433 -667 840 O ATOM 1129 CB GLU A 154 35.262 10.801 14.460 1.00 69.89 C ANISOU 1129 CB GLU A 154 8786 7584 10185 -826 -986 796 C ATOM 1130 CG GLU A 154 33.747 10.684 14.402 1.00 87.59 C ANISOU 1130 CG GLU A 154 10827 9860 12592 -1002 -1049 907 C ATOM 1131 CD GLU A 154 33.253 10.226 13.044 1.00104.48 C ANISOU 1131 CD GLU A 154 12967 11979 14750 -1168 -1257 784 C ATOM 1132 OE1 GLU A 154 34.101 9.889 12.183 1.00110.49 O ANISOU 1132 OE1 GLU A 154 13910 12679 15392 -1143 -1338 607 O ATOM 1133 OE2 GLU A 154 32.020 10.238 12.827 1.00108.85 O ANISOU 1133 OE2 GLU A 154 13335 12593 15430 -1317 -1341 864 O ATOM 1134 N LYS A 155 37.951 12.090 14.735 1.00 62.67 N ANISOU 1134 N LYS A 155 8099 6770 8943 -443 -836 663 N ATOM 1135 CA LYS A 155 39.394 11.958 14.572 1.00 56.77 C ANISOU 1135 CA LYS A 155 7514 5984 8072 -315 -810 550 C ATOM 1136 C LYS A 155 40.209 12.935 15.416 1.00 54.05 C ANISOU 1136 C LYS A 155 7159 5741 7635 -151 -692 595 C ATOM 1137 O LYS A 155 41.441 12.864 15.379 1.00 58.31 O ANISOU 1137 O LYS A 155 7809 6263 8083 -42 -666 517 O ATOM 1138 CB LYS A 155 39.732 12.086 13.086 1.00 56.13 C ANISOU 1138 CB LYS A 155 7497 5937 7891 -332 -928 396 C ATOM 1139 CG LYS A 155 39.084 10.948 12.277 1.00 64.53 C ANISOU 1139 CG LYS A 155 8612 6876 9029 -496 -1057 315 C ATOM 1140 CD LYS A 155 38.956 11.221 10.799 1.00 73.26 C ANISOU 1140 CD LYS A 155 9739 8064 10034 -548 -1195 189 C ATOM 1141 CE LYS A 155 37.784 10.402 10.217 1.00 82.08 C ANISOU 1141 CE LYS A 155 10821 9107 11257 -756 -1342 158 C ATOM 1142 NZ LYS A 155 37.482 10.685 8.771 1.00 77.37 N ANISOU 1142 NZ LYS A 155 10231 8618 10547 -824 -1503 45 N ATOM 1143 N ARG A 156 39.575 13.845 16.163 1.00 51.18 N ANISOU 1143 N ARG A 156 6666 5483 7296 -130 -620 709 N ATOM 1144 CA ARG A 156 40.320 14.698 17.086 1.00 50.95 C ANISOU 1144 CA ARG A 156 6643 5533 7183 12 -511 739 C ATOM 1145 C ARG A 156 39.869 14.468 18.528 1.00 50.33 C ANISOU 1145 C ARG A 156 6525 5442 7158 28 -398 873 C ATOM 1146 O ARG A 156 40.537 13.749 19.273 1.00 53.91 O ANISOU 1146 O ARG A 156 7072 5824 7590 79 -350 892 O ATOM 1147 CB ARG A 156 40.190 16.173 16.691 1.00 49.77 C ANISOU 1147 CB ARG A 156 6406 5524 6981 59 -510 731 C ATOM 1148 CG ARG A 156 40.906 16.528 15.392 1.00 48.47 C ANISOU 1148 CG ARG A 156 6297 5392 6727 76 -594 613 C ATOM 1149 CD ARG A 156 42.418 16.484 15.547 1.00 49.48 C ANISOU 1149 CD ARG A 156 6540 5506 6755 185 -557 532 C ATOM 1150 NE ARG A 156 43.157 16.782 14.313 1.00 49.99 N ANISOU 1150 NE ARG A 156 6655 5609 6729 207 -616 429 N ATOM 1151 CZ ARG A 156 43.486 15.863 13.406 1.00 49.58 C ANISOU 1151 CZ ARG A 156 6697 5492 6649 176 -684 335 C ATOM 1152 NH1 ARG A 156 43.138 14.595 13.603 1.00 44.12 N ANISOU 1152 NH1 ARG A 156 6060 4673 6030 113 -709 328 N ATOM 1153 NH2 ARG A 156 44.179 16.197 12.317 1.00 43.78 N ANISOU 1153 NH2 ARG A 156 6008 4812 5814 209 -717 248 N ATOM 1154 N LEU A 157 38.721 15.025 18.919 1.00 51.22 N ANISOU 1154 N LEU A 157 6497 5625 7338 -11 -351 977 N ATOM 1155 CA LEU A 157 38.216 14.837 20.281 1.00 54.93 C ANISOU 1155 CA LEU A 157 6924 6101 7845 7 -225 1113 C ATOM 1156 C LEU A 157 37.991 13.360 20.618 1.00 61.04 C ANISOU 1156 C LEU A 157 7747 6732 8712 -81 -224 1181 C ATOM 1157 O LEU A 157 38.415 12.884 21.678 1.00 64.78 O ANISOU 1157 O LEU A 157 8291 7171 9151 -19 -136 1251 O ATOM 1158 CB LEU A 157 36.902 15.592 20.456 1.00 46.21 C ANISOU 1158 CB LEU A 157 5644 5093 6821 -27 -174 1213 C ATOM 1159 CG LEU A 157 36.962 17.089 20.254 1.00 48.99 C ANISOU 1159 CG LEU A 157 5940 5566 7109 67 -153 1172 C ATOM 1160 CD1 LEU A 157 35.551 17.644 20.511 1.00 44.93 C ANISOU 1160 CD1 LEU A 157 5240 5130 6701 41 -89 1293 C ATOM 1161 CD2 LEU A 157 38.001 17.693 21.217 1.00 42.62 C ANISOU 1161 CD2 LEU A 157 5232 4796 6164 210 -59 1131 C ATOM 1162 N GLY A 158 37.301 12.625 19.739 1.00 57.61 N ANISOU 1162 N GLY A 158 7280 6212 8397 -230 -325 1168 N ATOM 1163 CA GLY A 158 36.924 11.250 20.061 1.00 55.92 C ANISOU 1163 CA GLY A 158 7100 5840 8306 -339 -321 1244 C ATOM 1164 C GLY A 158 38.120 10.330 20.223 1.00 57.52 C ANISOU 1164 C GLY A 158 7492 5905 8460 -272 -324 1187 C ATOM 1165 O GLY A 158 38.152 9.480 21.118 1.00 59.88 O ANISOU 1165 O GLY A 158 7841 6105 8808 -271 -249 1298 O ATOM 1166 N TYR A 159 39.111 10.471 19.346 1.00 58.19 N ANISOU 1166 N TYR A 159 7678 5981 8451 -210 -405 1025 N ATOM 1167 CA TYR A 159 40.343 9.706 19.486 1.00 56.10 C ANISOU 1167 CA TYR A 159 7577 5603 8134 -115 -399 969 C ATOM 1168 C TYR A 159 41.032 9.995 20.816 1.00 54.48 C ANISOU 1168 C TYR A 159 7397 5467 7835 34 -283 1064 C ATOM 1169 O TYR A 159 41.511 9.072 21.495 1.00 55.92 O ANISOU 1169 O TYR A 159 7672 5540 8035 80 -241 1132 O ATOM 1170 CB TYR A 159 41.262 10.021 18.320 1.00 57.18 C ANISOU 1170 CB TYR A 159 7790 5764 8174 -58 -485 787 C ATOM 1171 CG TYR A 159 42.564 9.291 18.357 1.00 60.73 C ANISOU 1171 CG TYR A 159 8389 6111 8575 56 -476 722 C ATOM 1172 CD1 TYR A 159 42.676 8.005 17.842 1.00 62.50 C ANISOU 1172 CD1 TYR A 159 8731 6133 8884 4 -524 662 C ATOM 1173 CD2 TYR A 159 43.693 9.892 18.877 1.00 54.12 C ANISOU 1173 CD2 TYR A 159 7574 5376 7615 217 -422 715 C ATOM 1174 CE1 TYR A 159 43.875 7.341 17.850 1.00 63.70 C ANISOU 1174 CE1 TYR A 159 9015 6187 9001 130 -506 605 C ATOM 1175 CE2 TYR A 159 44.899 9.231 18.897 1.00 58.55 C ANISOU 1175 CE2 TYR A 159 8250 5858 8140 332 -416 666 C ATOM 1176 CZ TYR A 159 44.988 7.962 18.374 1.00 65.50 C ANISOU 1176 CZ TYR A 159 9243 6538 9108 299 -452 615 C ATOM 1177 OH TYR A 159 46.196 7.307 18.387 1.00 72.82 O ANISOU 1177 OH TYR A 159 10279 7382 10009 435 -435 571 O ATOM 1178 N GLN A 160 41.098 11.270 21.202 1.00 52.41 N ANISOU 1178 N GLN A 160 7059 5383 7471 111 -236 1069 N ATOM 1179 CA GLN A 160 41.747 11.631 22.461 1.00 51.01 C ANISOU 1179 CA GLN A 160 6908 5290 7182 245 -142 1137 C ATOM 1180 C GLN A 160 40.982 11.079 23.668 1.00 56.89 C ANISOU 1180 C GLN A 160 7626 6011 7978 218 -37 1322 C ATOM 1181 O GLN A 160 41.594 10.682 24.669 1.00 50.53 O ANISOU 1181 O GLN A 160 6894 5202 7102 311 22 1400 O ATOM 1182 CB GLN A 160 41.897 13.148 22.554 1.00 44.62 C ANISOU 1182 CB GLN A 160 6031 4657 6266 315 -119 1083 C ATOM 1183 CG GLN A 160 42.943 13.737 21.630 1.00 43.32 C ANISOU 1183 CG GLN A 160 5905 4531 6025 372 -195 929 C ATOM 1184 CD GLN A 160 44.340 13.519 22.156 1.00 54.43 C ANISOU 1184 CD GLN A 160 7406 5945 7332 496 -189 899 C ATOM 1185 OE1 GLN A 160 44.527 13.313 23.357 1.00 51.51 O ANISOU 1185 OE1 GLN A 160 7060 5600 6911 559 -126 991 O ATOM 1186 NE2 GLN A 160 45.332 13.541 21.264 1.00 48.49 N ANISOU 1186 NE2 GLN A 160 6698 5181 6543 536 -254 780 N ATOM 1187 N LEU A 161 39.644 11.069 23.599 1.00 61.83 N ANISOU 1187 N LEU A 161 8137 6635 8721 94 -11 1404 N ATOM 1188 CA LEU A 161 38.827 10.543 24.693 1.00 59.53 C ANISOU 1188 CA LEU A 161 7802 6327 8490 56 104 1596 C ATOM 1189 C LEU A 161 39.027 9.040 24.875 1.00 63.48 C ANISOU 1189 C LEU A 161 8404 6630 9084 8 98 1676 C ATOM 1190 O LEU A 161 39.122 8.555 26.009 1.00 65.83 O ANISOU 1190 O LEU A 161 8746 6917 9351 62 198 1827 O ATOM 1191 CB LEU A 161 37.348 10.849 24.442 1.00 53.57 C ANISOU 1191 CB LEU A 161 6875 5615 7866 -75 127 1666 C ATOM 1192 CG LEU A 161 36.933 12.316 24.557 1.00 53.79 C ANISOU 1192 CG LEU A 161 6786 5831 7821 -10 178 1641 C ATOM 1193 CD1 LEU A 161 35.486 12.471 24.173 1.00 57.43 C ANISOU 1193 CD1 LEU A 161 7063 6321 8436 -139 183 1718 C ATOM 1194 CD2 LEU A 161 37.158 12.829 25.970 1.00 54.05 C ANISOU 1194 CD2 LEU A 161 6843 5981 7714 126 327 1724 C ATOM 1195 N LYS A 162 39.037 8.282 23.774 1.00 61.68 N ANISOU 1195 N LYS A 162 8222 6241 8973 -94 -16 1581 N ATOM 1196 CA LYS A 162 39.267 6.843 23.863 1.00 62.73 C ANISOU 1196 CA LYS A 162 8470 6150 9213 -137 -25 1638 C ATOM 1197 C LYS A 162 40.628 6.554 24.478 1.00 65.26 C ANISOU 1197 C LYS A 162 8932 6453 9411 43 2 1643 C ATOM 1198 O LYS A 162 40.755 5.736 25.397 1.00 64.32 O ANISOU 1198 O LYS A 162 8877 6246 9316 79 76 1800 O ATOM 1199 CB LYS A 162 39.175 6.227 22.464 1.00 65.37 C ANISOU 1199 CB LYS A 162 8850 6324 9664 -261 -164 1483 C ATOM 1200 CG LYS A 162 39.627 4.790 22.370 1.00 74.45 C ANISOU 1200 CG LYS A 162 10154 7214 10920 -281 -186 1488 C ATOM 1201 CD LYS A 162 39.065 4.096 21.150 1.00 84.11 C ANISOU 1201 CD LYS A 162 11400 8265 12294 -462 -309 1363 C ATOM 1202 CE LYS A 162 39.323 2.598 21.226 1.00 93.71 C ANISOU 1202 CE LYS A 162 12768 9185 13652 -499 -308 1394 C ATOM 1203 NZ LYS A 162 38.603 1.863 20.155 1.00100.25 N ANISOU 1203 NZ LYS A 162 13617 9828 14645 -709 -427 1278 N ATOM 1204 N LEU A 163 41.647 7.273 24.020 1.00 68.50 N ANISOU 1204 N LEU A 163 9379 6962 9687 162 -54 1488 N ATOM 1205 CA LEU A 163 42.994 7.102 24.539 1.00 63.17 C ANISOU 1205 CA LEU A 163 8809 6299 8894 336 -43 1484 C ATOM 1206 C LEU A 163 42.986 7.406 26.027 1.00 63.92 C ANISOU 1206 C LEU A 163 8883 6524 8878 424 64 1652 C ATOM 1207 O LEU A 163 43.619 6.688 26.806 1.00 71.99 O ANISOU 1207 O LEU A 163 9992 7494 9868 521 97 1761 O ATOM 1208 CB LEU A 163 43.953 7.918 23.681 1.00 62.08 C ANISOU 1208 CB LEU A 163 8679 6258 8650 417 -121 1290 C ATOM 1209 CG LEU A 163 45.429 8.044 23.954 1.00 69.09 C ANISOU 1209 CG LEU A 163 9634 7206 9413 593 -133 1243 C ATOM 1210 CD1 LEU A 163 46.071 6.671 24.065 1.00 71.34 C ANISOU 1210 CD1 LEU A 163 10039 7299 9768 657 -136 1294 C ATOM 1211 CD2 LEU A 163 46.002 8.820 22.786 1.00 64.68 C ANISOU 1211 CD2 LEU A 163 9054 6719 8803 608 -206 1051 C ATOM 1212 N ALA A 164 42.278 8.460 26.449 1.00 62.47 N ANISOU 1212 N ALA A 164 8591 6515 8630 403 122 1677 N ATOM 1213 CA ALA A 164 42.255 8.792 27.873 1.00 61.13 C ANISOU 1213 CA ALA A 164 8415 6484 8329 493 231 1819 C ATOM 1214 C ALA A 164 41.537 7.718 28.685 1.00 70.69 C ANISOU 1214 C ALA A 164 9641 7589 9628 438 327 2042 C ATOM 1215 O ALA A 164 41.899 7.457 29.837 1.00 70.82 O ANISOU 1215 O ALA A 164 9716 7660 9534 539 399 2182 O ATOM 1216 CB ALA A 164 41.591 10.146 28.096 1.00 59.94 C ANISOU 1216 CB ALA A 164 8152 6522 8100 486 286 1784 C ATOM 1217 N ARG A 165 40.496 7.111 28.115 1.00 75.36 N ANISOU 1217 N ARG A 165 10177 8039 10417 272 326 2086 N ATOM 1218 CA ARG A 165 39.800 6.041 28.815 1.00 72.32 C ANISOU 1218 CA ARG A 165 9800 7530 10148 197 419 2307 C ATOM 1219 C ARG A 165 40.713 4.841 29.013 1.00 72.97 C ANISOU 1219 C ARG A 165 10038 7430 10259 267 393 2370 C ATOM 1220 O ARG A 165 40.701 4.209 30.072 1.00 74.24 O ANISOU 1220 O ARG A 165 10246 7564 10397 313 488 2579 O ATOM 1221 CB ARG A 165 38.550 5.641 28.041 1.00 72.26 C ANISOU 1221 CB ARG A 165 9689 7398 10367 -17 399 2320 C ATOM 1222 CG ARG A 165 37.498 4.927 28.873 1.00 78.98 C ANISOU 1222 CG ARG A 165 10479 8189 11339 -121 528 2570 C ATOM 1223 CD ARG A 165 36.509 4.249 27.952 1.00 81.27 C ANISOU 1223 CD ARG A 165 10692 8299 11887 -349 464 2561 C ATOM 1224 NE ARG A 165 37.243 3.565 26.894 1.00 85.34 N ANISOU 1224 NE ARG A 165 11338 8610 12476 -373 315 2389 N ATOM 1225 CZ ARG A 165 36.675 2.921 25.884 1.00 86.29 C ANISOU 1225 CZ ARG A 165 11443 8549 12796 -560 214 2310 C ATOM 1226 NH1 ARG A 165 35.351 2.865 25.796 1.00 91.72 N ANISOU 1226 NH1 ARG A 165 11969 9237 13644 -751 234 2402 N ATOM 1227 NH2 ARG A 165 37.436 2.337 24.965 1.00 81.02 N ANISOU 1227 NH2 ARG A 165 10917 7705 12163 -553 92 2136 N ATOM 1228 N ASP A 166 41.554 4.550 28.024 1.00 75.62 N ANISOU 1228 N ASP A 166 10453 7647 10630 294 272 2198 N ATOM 1229 CA ASP A 166 42.396 3.360 28.067 1.00 77.15 C ANISOU 1229 CA ASP A 166 10793 7638 10884 367 247 2244 C ATOM 1230 C ASP A 166 43.598 3.532 28.994 1.00 76.35 C ANISOU 1230 C ASP A 166 10760 7663 10586 583 266 2304 C ATOM 1231 O ASP A 166 43.998 2.584 29.671 1.00 83.89 O ANISOU 1231 O ASP A 166 11807 8505 11562 660 304 2468 O ATOM 1232 CB ASP A 166 42.863 3.010 26.654 1.00 76.34 C ANISOU 1232 CB ASP A 166 10751 7373 10880 333 124 2025 C ATOM 1233 CG ASP A 166 41.714 2.644 25.724 1.00 82.68 C ANISOU 1233 CG ASP A 166 11506 8029 11880 109 81 1967 C ATOM 1234 OD1 ASP A 166 40.571 2.439 26.196 1.00 82.67 O ANISOU 1234 OD1 ASP A 166 11423 8006 11982 -28 150 2122 O ATOM 1235 OD2 ASP A 166 41.963 2.563 24.504 1.00 87.63 O ANISOU 1235 OD2 ASP A 166 12173 8569 12554 69 -24 1764 O ATOM 1236 N GLN A 167 44.190 4.718 29.037 1.00 74.10 N ANISOU 1236 N GLN A 167 10429 7608 10117 680 233 2179 N ATOM 1237 CA GLN A 167 45.379 4.934 29.854 1.00 66.53 C ANISOU 1237 CA GLN A 167 9521 6786 8971 872 223 2214 C ATOM 1238 C GLN A 167 45.053 5.077 31.333 1.00 67.59 C ANISOU 1238 C GLN A 167 9650 7069 8964 925 329 2421 C ATOM 1239 O GLN A 167 45.854 4.676 32.180 1.00 72.75 O ANISOU 1239 O GLN A 167 10374 7761 9506 1067 332 2541 O ATOM 1240 CB GLN A 167 46.090 6.207 29.415 1.00 69.36 C ANISOU 1240 CB GLN A 167 9826 7338 9190 935 150 2007 C ATOM 1241 CG GLN A 167 46.640 6.181 28.032 1.00 85.94 C ANISOU 1241 CG GLN A 167 11937 9340 11375 920 53 1805 C ATOM 1242 CD GLN A 167 47.629 7.294 27.814 1.00 98.82 C ANISOU 1242 CD GLN A 167 13527 11162 12858 1015 -9 1649 C ATOM 1243 OE1 GLN A 167 48.578 7.150 27.059 1.00113.06 O ANISOU 1243 OE1 GLN A 167 15356 12923 14678 1080 -77 1531 O ATOM 1244 NE2 GLN A 167 47.401 8.426 28.467 1.00 94.14 N ANISOU 1244 NE2 GLN A 167 12868 10775 12127 1019 20 1644 N ATOM 1245 N TYR A 168 43.902 5.648 31.662 1.00 67.66 N ANISOU 1245 N TYR A 168 9573 7173 8964 825 418 2470 N ATOM 1246 CA TYR A 168 43.604 6.047 33.025 1.00 63.39 C ANISOU 1246 CA TYR A 168 9021 6821 8243 889 528 2627 C ATOM 1247 C TYR A 168 42.328 5.445 33.580 1.00 65.26 C ANISOU 1247 C TYR A 168 9223 6991 8582 779 669 2848 C ATOM 1248 O TYR A 168 41.960 5.771 34.718 1.00 67.79 O ANISOU 1248 O TYR A 168 9532 7478 8747 829 786 2988 O ATOM 1249 CB TYR A 168 43.485 7.573 33.119 1.00 58.54 C ANISOU 1249 CB TYR A 168 8329 6444 7470 909 534 2473 C ATOM 1250 CG TYR A 168 44.673 8.366 32.618 1.00 63.58 C ANISOU 1250 CG TYR A 168 8979 7173 8004 998 406 2256 C ATOM 1251 CD1 TYR A 168 45.791 8.559 33.422 1.00 62.75 C ANISOU 1251 CD1 TYR A 168 8935 7207 7698 1149 363 2264 C ATOM 1252 CD2 TYR A 168 44.653 8.978 31.367 1.00 59.64 C ANISOU 1252 CD2 TYR A 168 8421 6640 7601 926 329 2052 C ATOM 1253 CE1 TYR A 168 46.869 9.308 32.981 1.00 61.39 C ANISOU 1253 CE1 TYR A 168 8754 7124 7446 1215 249 2073 C ATOM 1254 CE2 TYR A 168 45.721 9.735 30.920 1.00 53.16 C ANISOU 1254 CE2 TYR A 168 7601 5906 6692 999 228 1870 C ATOM 1255 CZ TYR A 168 46.827 9.893 31.727 1.00 60.43 C ANISOU 1255 CZ TYR A 168 8572 6954 7435 1138 190 1881 C ATOM 1256 OH TYR A 168 47.889 10.644 31.287 1.00 62.88 O ANISOU 1256 OH TYR A 168 8865 7352 7675 1195 90 1709 O ATOM 1257 N GLY A 169 41.631 4.600 32.820 1.00 60.87 N ANISOU 1257 N GLY A 169 8645 6204 8279 626 665 2881 N ATOM 1258 CA GLY A 169 40.300 4.192 33.234 1.00 65.09 C ANISOU 1258 CA GLY A 169 9105 6691 8935 489 797 3076 C ATOM 1259 C GLY A 169 39.363 5.353 33.476 1.00 69.53 C ANISOU 1259 C GLY A 169 9528 7468 9423 449 885 3047 C ATOM 1260 O GLY A 169 38.478 5.257 34.333 1.00 76.69 O ANISOU 1260 O GLY A 169 10377 8442 10320 415 1039 3246 O ATOM 1261 N ASP A 170 39.553 6.466 32.759 1.00 67.54 N ANISOU 1261 N ASP A 170 9220 7327 9116 463 803 2813 N ATOM 1262 CA ASP A 170 38.751 7.677 32.951 1.00 70.77 C ANISOU 1262 CA ASP A 170 9504 7933 9453 453 883 2766 C ATOM 1263 C ASP A 170 37.482 7.572 32.109 1.00 72.01 C ANISOU 1263 C ASP A 170 9512 7998 9851 263 890 2772 C ATOM 1264 O ASP A 170 37.319 8.223 31.077 1.00 66.72 O ANISOU 1264 O ASP A 170 8769 7336 9246 209 796 2593 O ATOM 1265 CB ASP A 170 39.553 8.921 32.591 1.00 63.88 C ANISOU 1265 CB ASP A 170 8643 7204 8424 555 792 2528 C ATOM 1266 CG ASP A 170 38.891 10.204 33.076 1.00 68.22 C ANISOU 1266 CG ASP A 170 9100 7961 8859 592 896 2493 C ATOM 1267 OD1 ASP A 170 37.662 10.202 33.349 1.00 67.72 O ANISOU 1267 OD1 ASP A 170 8925 7924 8883 516 1024 2621 O ATOM 1268 OD2 ASP A 170 39.606 11.224 33.171 1.00 66.49 O ANISOU 1268 OD2 ASP A 170 8917 7874 8474 697 852 2335 O ATOM 1269 N SER A 171 36.546 6.753 32.587 1.00 73.46 N ANISOU 1269 N SER A 171 9640 8105 10165 160 1004 2995 N ATOM 1270 CA SER A 171 35.301 6.607 31.859 1.00 72.22 C ANISOU 1270 CA SER A 171 9321 7872 10247 -34 1006 3019 C ATOM 1271 C SER A 171 34.393 7.818 32.027 1.00 74.52 C ANISOU 1271 C SER A 171 9445 8377 10494 -23 1101 3002 C ATOM 1272 O SER A 171 33.517 8.035 31.185 1.00 80.04 O ANISOU 1272 O SER A 171 9991 9055 11366 -157 1056 2956 O ATOM 1273 CB SER A 171 34.588 5.333 32.304 1.00 77.62 C ANISOU 1273 CB SER A 171 9986 8396 11110 -166 1099 3271 C ATOM 1274 OG SER A 171 34.404 5.353 33.701 1.00 81.31 O ANISOU 1274 OG SER A 171 10463 8999 11430 -68 1289 3487 O ATOM 1275 N ALA A 172 34.593 8.627 33.069 1.00 69.05 N ANISOU 1275 N ALA A 172 8777 7888 9570 139 1225 3029 N ATOM 1276 CA ALA A 172 33.778 9.830 33.223 1.00 66.46 C ANISOU 1276 CA ALA A 172 8304 7749 9199 173 1325 2995 C ATOM 1277 C ALA A 172 34.058 10.836 32.110 1.00 71.95 C ANISOU 1277 C ALA A 172 8965 8470 9905 185 1178 2743 C ATOM 1278 O ALA A 172 33.123 11.327 31.464 1.00 75.95 O ANISOU 1278 O ALA A 172 9303 9004 10551 103 1175 2718 O ATOM 1279 CB ALA A 172 34.010 10.472 34.590 1.00 62.66 C ANISOU 1279 CB ALA A 172 7890 7470 8448 353 1487 3050 C ATOM 1280 N ILE A 173 35.338 11.154 31.863 1.00 70.88 N ANISOU 1280 N ILE A 173 8975 8329 9625 285 1056 2568 N ATOM 1281 CA ILE A 173 35.639 12.104 30.793 1.00 63.53 C ANISOU 1281 CA ILE A 173 8015 7419 8704 293 925 2346 C ATOM 1282 C ILE A 173 35.191 11.533 29.457 1.00 62.11 C ANISOU 1282 C ILE A 173 7758 7087 8753 124 791 2306 C ATOM 1283 O ILE A 173 34.691 12.268 28.600 1.00 60.68 O ANISOU 1283 O ILE A 173 7464 6944 8646 79 733 2211 O ATOM 1284 CB ILE A 173 37.137 12.489 30.781 1.00 61.45 C ANISOU 1284 CB ILE A 173 7911 7178 8257 420 824 2180 C ATOM 1285 CG1 ILE A 173 37.332 13.860 30.138 1.00 58.57 C ANISOU 1285 CG1 ILE A 173 7507 6902 7845 469 765 1986 C ATOM 1286 CG2 ILE A 173 37.965 11.514 29.973 1.00 62.11 C ANISOU 1286 CG2 ILE A 173 8091 7089 8419 369 673 2123 C ATOM 1287 CD1 ILE A 173 38.663 14.510 30.465 1.00 49.83 C ANISOU 1287 CD1 ILE A 173 6529 5869 6537 603 712 1844 C ATOM 1288 N TYR A 174 35.274 10.212 29.291 1.00 61.45 N ANISOU 1288 N TYR A 174 7732 6829 8788 24 745 2387 N ATOM 1289 CA TYR A 174 34.852 9.595 28.038 1.00 66.91 C ANISOU 1289 CA TYR A 174 8369 7365 9688 -148 608 2332 C ATOM 1290 C TYR A 174 33.352 9.739 27.811 1.00 71.92 C ANISOU 1290 C TYR A 174 8789 8040 10499 -290 654 2432 C ATOM 1291 O TYR A 174 32.911 9.943 26.672 1.00 68.32 O ANISOU 1291 O TYR A 174 8240 7561 10159 -395 528 2331 O ATOM 1292 CB TYR A 174 35.250 8.124 28.026 1.00 62.54 C ANISOU 1292 CB TYR A 174 7939 6594 9230 -220 565 2400 C ATOM 1293 CG TYR A 174 34.852 7.373 26.772 1.00 70.07 C ANISOU 1293 CG TYR A 174 8867 7364 10393 -406 419 2324 C ATOM 1294 CD1 TYR A 174 33.592 6.783 26.656 1.00 69.62 C ANISOU 1294 CD1 TYR A 174 8669 7234 10551 -599 441 2455 C ATOM 1295 CD2 TYR A 174 35.747 7.227 25.712 1.00 73.65 C ANISOU 1295 CD2 TYR A 174 9436 7720 10826 -393 260 2121 C ATOM 1296 CE1 TYR A 174 33.232 6.091 25.517 1.00 71.12 C ANISOU 1296 CE1 TYR A 174 8843 7256 10923 -782 291 2368 C ATOM 1297 CE2 TYR A 174 35.397 6.533 24.570 1.00 75.61 C ANISOU 1297 CE2 TYR A 174 9682 7805 11241 -560 124 2033 C ATOM 1298 CZ TYR A 174 34.138 5.961 24.479 1.00 79.90 C ANISOU 1298 CZ TYR A 174 10093 8273 11991 -759 131 2150 C ATOM 1299 OH TYR A 174 33.783 5.260 23.346 1.00 84.16 O ANISOU 1299 OH TYR A 174 10637 8649 12690 -940 -21 2046 O ATOM 1300 N GLN A 175 32.550 9.609 28.871 1.00 71.38 N ANISOU 1300 N GLN A 175 8630 8040 10452 -293 833 2638 N ATOM 1301 CA GLN A 175 31.102 9.667 28.691 1.00 72.61 C ANISOU 1301 CA GLN A 175 8554 8237 10796 -431 887 2756 C ATOM 1302 C GLN A 175 30.632 11.101 28.502 1.00 70.60 C ANISOU 1302 C GLN A 175 8161 8176 10488 -344 919 2681 C ATOM 1303 O GLN A 175 29.850 11.384 27.591 1.00 68.53 O ANISOU 1303 O GLN A 175 7735 7929 10374 -449 832 2648 O ATOM 1304 CB GLN A 175 30.373 9.020 29.870 1.00 73.67 C ANISOU 1304 CB GLN A 175 8624 8384 10984 -467 1087 3020 C ATOM 1305 CG GLN A 175 30.539 7.519 29.974 1.00 83.82 C ANISOU 1305 CG GLN A 175 10005 9448 12395 -594 1061 3138 C ATOM 1306 CD GLN A 175 29.825 6.955 31.192 1.00 98.16 C ANISOU 1306 CD GLN A 175 11755 11291 14251 -621 1279 3424 C ATOM 1307 OE1 GLN A 175 28.783 7.470 31.609 1.00102.53 O ANISOU 1307 OE1 GLN A 175 12113 11997 14847 -633 1424 3546 O ATOM 1308 NE2 GLN A 175 30.397 5.912 31.786 1.00101.16 N ANISOU 1308 NE2 GLN A 175 12295 11528 14612 -615 1315 3544 N ATOM 1309 N LYS A 176 31.068 12.009 29.380 1.00 67.78 N ANISOU 1309 N LYS A 176 7868 7964 9921 -151 1044 2658 N ATOM 1310 CA LYS A 176 30.757 13.421 29.191 1.00 69.44 C ANISOU 1310 CA LYS A 176 7980 8328 10077 -48 1073 2564 C ATOM 1311 C LYS A 176 31.308 13.923 27.859 1.00 65.36 C ANISOU 1311 C LYS A 176 7495 7767 9571 -64 867 2355 C ATOM 1312 O LYS A 176 30.691 14.764 27.193 1.00 58.73 O ANISOU 1312 O LYS A 176 6514 6999 8803 -68 831 2311 O ATOM 1313 CB LYS A 176 31.328 14.252 30.337 1.00 75.39 C ANISOU 1313 CB LYS A 176 8845 9214 10586 158 1220 2535 C ATOM 1314 CG LYS A 176 30.635 14.093 31.665 1.00 78.55 C ANISOU 1314 CG LYS A 176 9192 9715 10938 209 1456 2733 C ATOM 1315 CD LYS A 176 30.955 15.298 32.521 1.00 79.77 C ANISOU 1315 CD LYS A 176 9418 10027 10864 412 1584 2650 C ATOM 1316 CE LYS A 176 30.611 15.086 33.967 1.00 85.52 C ANISOU 1316 CE LYS A 176 10168 10866 11461 496 1815 2819 C ATOM 1317 NZ LYS A 176 31.311 16.111 34.797 1.00 88.16 N ANISOU 1317 NZ LYS A 176 10650 11327 11520 692 1889 2685 N ATOM 1318 N GLY A 177 32.488 13.437 27.471 1.00 61.07 N ANISOU 1318 N GLY A 177 7137 7114 8952 -60 737 2235 N ATOM 1319 CA GLY A 177 33.058 13.835 26.200 1.00 59.26 C ANISOU 1319 CA GLY A 177 6947 6846 8722 -75 554 2047 C ATOM 1320 C GLY A 177 32.177 13.459 25.025 1.00 65.29 C ANISOU 1320 C GLY A 177 7571 7552 9685 -251 425 2051 C ATOM 1321 O GLY A 177 31.930 14.277 24.132 1.00 64.72 O ANISOU 1321 O GLY A 177 7415 7543 9635 -252 337 1964 O ATOM 1322 N HIS A 178 31.690 12.216 24.999 1.00 68.84 N ANISOU 1322 N HIS A 178 7994 7879 10284 -409 403 2154 N ATOM 1323 CA AHIS A 178 30.870 11.797 23.869 0.50 74.43 C ANISOU 1323 CA AHIS A 178 8574 8529 11178 -597 256 2141 C ATOM 1324 CA BHIS A 178 30.872 11.801 23.867 0.50 74.43 C ANISOU 1324 CA BHIS A 178 8574 8528 11177 -597 256 2141 C ATOM 1325 C HIS A 178 29.480 12.409 23.908 1.00 77.62 C ANISOU 1325 C HIS A 178 8715 9069 11709 -644 319 2265 C ATOM 1326 O HIS A 178 28.821 12.470 22.867 1.00 78.15 O ANISOU 1326 O HIS A 178 8650 9148 11897 -765 177 2232 O ATOM 1327 CB AHIS A 178 30.787 10.274 23.796 0.50 76.00 C ANISOU 1327 CB AHIS A 178 8832 8530 11515 -767 204 2198 C ATOM 1328 CB BHIS A 178 30.799 10.278 23.783 0.50 76.01 C ANISOU 1328 CB BHIS A 178 8834 8530 11514 -766 202 2196 C ATOM 1329 CG AHIS A 178 31.930 9.661 23.051 0.50 79.43 C ANISOU 1329 CG AHIS A 178 9480 8810 11888 -770 58 2025 C ATOM 1330 CG BHIS A 178 31.963 9.676 23.060 0.50 79.48 C ANISOU 1330 CG BHIS A 178 9491 8818 11889 -764 59 2022 C ATOM 1331 ND1AHIS A 178 32.061 9.760 21.682 0.50 79.74 N ANISOU 1331 ND1AHIS A 178 9534 8822 11940 -839 -131 1853 N ATOM 1332 ND1BHIS A 178 32.106 9.752 21.692 0.50 79.71 N ANISOU 1332 ND1BHIS A 178 9538 8816 11932 -835 -130 1850 N ATOM 1333 CD2AHIS A 178 33.014 8.974 23.483 0.50 80.30 C ANISOU 1333 CD2AHIS A 178 9796 8799 11915 -695 80 1999 C ATOM 1334 CD2BHIS A 178 33.058 9.024 23.517 0.50 80.36 C ANISOU 1334 CD2BHIS A 178 9807 8814 11912 -683 85 1997 C ATOM 1335 CE1AHIS A 178 33.167 9.145 21.301 0.50 78.42 C ANISOU 1335 CE1AHIS A 178 9575 8519 11704 -807 -206 1722 C ATOM 1336 CE1BHIS A 178 33.229 9.155 21.334 0.50 78.49 C ANISOU 1336 CE1BHIS A 178 9591 8527 11703 -797 -202 1720 C ATOM 1337 NE2AHIS A 178 33.765 8.661 22.375 0.50 79.11 N ANISOU 1337 NE2AHIS A 178 9773 8542 11741 -717 -83 1810 N ATOM 1338 NE2BHIS A 178 33.827 8.707 22.422 0.50 79.01 N ANISOU 1338 NE2BHIS A 178 9767 8537 11716 -703 -77 1809 N ATOM 1339 N THR A 179 29.029 12.873 25.078 1.00 76.17 N ANISOU 1339 N THR A 179 8450 8998 11491 -541 529 2406 N ATOM 1340 CA THR A 179 27.799 13.655 25.137 1.00 73.33 C ANISOU 1340 CA THR A 179 7838 8790 11235 -534 611 2512 C ATOM 1341 C THR A 179 27.990 14.990 24.424 1.00 70.57 C ANISOU 1341 C THR A 179 7465 8543 10807 -414 539 2374 C ATOM 1342 O THR A 179 27.137 15.415 23.639 1.00 72.35 O ANISOU 1342 O THR A 179 7498 8836 11157 -473 458 2395 O ATOM 1343 CB THR A 179 27.364 13.861 26.596 1.00 68.69 C ANISOU 1343 CB THR A 179 7195 8303 10603 -426 875 2681 C ATOM 1344 OG1 THR A 179 27.146 12.591 27.220 1.00 78.88 O ANISOU 1344 OG1 THR A 179 8500 9494 11976 -548 943 2837 O ATOM 1345 CG2 THR A 179 26.086 14.661 26.686 1.00 70.04 C ANISOU 1345 CG2 THR A 179 7095 8630 10888 -399 982 2796 C ATOM 1346 N LEU A 180 29.115 15.662 24.690 1.00 65.54 N ANISOU 1346 N LEU A 180 7018 7917 9969 -247 565 2243 N ATOM 1347 CA LEU A 180 29.430 16.916 24.012 1.00 61.70 C ANISOU 1347 CA LEU A 180 6536 7500 9409 -137 499 2112 C ATOM 1348 C LEU A 180 29.533 16.718 22.504 1.00 62.81 C ANISOU 1348 C LEU A 180 6669 7587 9610 -256 263 2009 C ATOM 1349 O LEU A 180 28.958 17.486 21.729 1.00 70.08 O ANISOU 1349 O LEU A 180 7451 8586 10590 -251 193 2004 O ATOM 1350 CB LEU A 180 30.724 17.503 24.577 1.00 59.30 C ANISOU 1350 CB LEU A 180 6448 7194 8889 29 553 1985 C ATOM 1351 CG LEU A 180 31.231 18.769 23.890 1.00 60.36 C ANISOU 1351 CG LEU A 180 6617 7371 8947 135 485 1844 C ATOM 1352 CD1 LEU A 180 30.138 19.820 23.874 1.00 62.86 C ANISOU 1352 CD1 LEU A 180 6735 7796 9353 202 569 1920 C ATOM 1353 CD2 LEU A 180 32.433 19.305 24.624 1.00 60.91 C ANISOU 1353 CD2 LEU A 180 6880 7443 8822 280 553 1735 C ATOM 1354 N ILE A 181 30.279 15.697 22.070 1.00 64.12 N ANISOU 1354 N ILE A 181 6989 7621 9753 -353 142 1926 N ATOM 1355 CA ILE A 181 30.457 15.428 20.644 1.00 61.67 C ANISOU 1355 CA ILE A 181 6704 7259 9470 -462 -77 1809 C ATOM 1356 C ILE A 181 29.118 15.227 19.951 1.00 70.40 C ANISOU 1356 C ILE A 181 7580 8407 10760 -621 -174 1897 C ATOM 1357 O ILE A 181 28.917 15.676 18.815 1.00 75.65 O ANISOU 1357 O ILE A 181 8186 9125 11433 -654 -328 1831 O ATOM 1358 CB ILE A 181 31.360 14.203 20.453 1.00 59.95 C ANISOU 1358 CB ILE A 181 6685 6875 9217 -538 -159 1720 C ATOM 1359 CG1 ILE A 181 32.783 14.510 20.917 1.00 57.90 C ANISOU 1359 CG1 ILE A 181 6634 6596 8770 -374 -102 1618 C ATOM 1360 CG2 ILE A 181 31.294 13.701 19.012 1.00 56.11 C ANISOU 1360 CG2 ILE A 181 6211 6327 8781 -683 -377 1609 C ATOM 1361 CD1 ILE A 181 33.707 13.317 20.834 1.00 57.47 C ANISOU 1361 CD1 ILE A 181 6768 6381 8686 -416 -160 1548 C ATOM 1362 N GLN A 182 28.177 14.553 20.619 1.00 64.48 N ANISOU 1362 N GLN A 182 6691 7647 10163 -724 -88 2057 N ATOM 1363 CA GLN A 182 26.894 14.278 19.987 1.00 70.50 C ANISOU 1363 CA GLN A 182 7214 8452 11120 -897 -191 2148 C ATOM 1364 C GLN A 182 26.004 15.513 19.937 1.00 69.29 C ANISOU 1364 C GLN A 182 6831 8483 11015 -800 -138 2238 C ATOM 1365 O GLN A 182 25.160 15.607 19.046 1.00 69.02 O ANISOU 1365 O GLN A 182 6611 8517 11098 -907 -284 2268 O ATOM 1366 CB GLN A 182 26.191 13.124 20.696 1.00 76.02 C ANISOU 1366 CB GLN A 182 7827 9070 11986 -1055 -115 2302 C ATOM 1367 CG GLN A 182 26.823 11.775 20.382 1.00 82.32 C ANISOU 1367 CG GLN A 182 8817 9659 12800 -1201 -228 2213 C ATOM 1368 CD GLN A 182 26.361 10.696 21.333 1.00 94.74 C ANISOU 1368 CD GLN A 182 10355 11128 14515 -1317 -103 2381 C ATOM 1369 OE1 GLN A 182 25.210 10.702 21.771 1.00101.22 O ANISOU 1369 OE1 GLN A 182 10936 12030 15494 -1392 -14 2562 O ATOM 1370 NE2 GLN A 182 27.262 9.770 21.678 1.00 96.26 N ANISOU 1370 NE2 GLN A 182 10779 11141 14656 -1323 -86 2336 N ATOM 1371 N ASN A 183 26.191 16.468 20.857 1.00 71.09 N ANISOU 1371 N ASN A 183 7071 8789 11151 -595 61 2276 N ATOM 1372 CA ASN A 183 25.437 17.719 20.904 1.00 73.27 C ANISOU 1372 CA ASN A 183 7154 9219 11468 -463 142 2353 C ATOM 1373 C ASN A 183 26.230 18.919 20.373 1.00 77.81 C ANISOU 1373 C ASN A 183 7849 9823 11893 -297 98 2216 C ATOM 1374 O ASN A 183 25.951 20.061 20.755 1.00 80.90 O ANISOU 1374 O ASN A 183 8163 10302 12272 -129 226 2256 O ATOM 1375 CB ASN A 183 24.968 18.010 22.330 1.00 73.07 C ANISOU 1375 CB ASN A 183 7050 9258 11456 -343 417 2492 C ATOM 1376 CG ASN A 183 24.124 16.884 22.922 1.00 82.56 C ANISOU 1376 CG ASN A 183 8112 10441 12816 -503 491 2662 C ATOM 1377 OD1 ASN A 183 23.655 15.996 22.207 1.00 83.36 O ANISOU 1377 OD1 ASN A 183 8121 10491 13061 -716 329 2690 O ATOM 1378 ND2 ASN A 183 23.894 16.946 24.234 1.00 83.38 N ANISOU 1378 ND2 ASN A 183 8196 10590 12894 -403 742 2780 N ATOM 1379 N MET A 184 27.196 18.686 19.479 1.00 75.47 N ANISOU 1379 N MET A 184 7736 9448 11489 -341 -75 2058 N ATOM 1380 CA MET A 184 28.191 19.701 19.129 1.00 72.29 C ANISOU 1380 CA MET A 184 7488 9050 10928 -190 -91 1927 C ATOM 1381 C MET A 184 27.681 20.731 18.117 1.00 69.29 C ANISOU 1381 C MET A 184 6972 8769 10587 -144 -193 1945 C ATOM 1382 O MET A 184 28.059 21.904 18.207 1.00 70.47 O ANISOU 1382 O MET A 184 7165 8945 10664 21 -120 1913 O ATOM 1383 CB MET A 184 29.431 19.008 18.562 1.00 68.55 C ANISOU 1383 CB MET A 184 7252 8466 10329 -250 -220 1766 C ATOM 1384 CG MET A 184 30.738 19.609 18.958 1.00 71.44 C ANISOU 1384 CG MET A 184 7825 8797 10521 -100 -146 1649 C ATOM 1385 SD MET A 184 32.117 18.571 18.416 1.00 71.20 S ANISOU 1385 SD MET A 184 8042 8639 10372 -171 -273 1487 S ATOM 1386 CE MET A 184 31.985 18.543 16.640 1.00 75.84 C ANISOU 1386 CE MET A 184 8603 9247 10964 -276 -508 1411 C ATOM 1387 N ALA A 185 26.807 20.325 17.193 1.00 66.22 N ANISOU 1387 N ALA A 185 6415 8430 10314 -288 -359 2003 N ATOM 1388 CA ALA A 185 26.432 21.156 16.046 1.00 65.56 C ANISOU 1388 CA ALA A 185 6224 8442 10242 -261 -502 2017 C ATOM 1389 C ALA A 185 26.003 22.587 16.368 1.00 71.00 C ANISOU 1389 C ALA A 185 6794 9217 10967 -60 -368 2108 C ATOM 1390 O ALA A 185 26.366 23.490 15.595 1.00 67.80 O ANISOU 1390 O ALA A 185 6433 8838 10492 29 -441 2069 O ATOM 1391 CB ALA A 185 25.313 20.464 15.259 1.00 59.14 C ANISOU 1391 CB ALA A 185 5200 7698 9575 -452 -685 2100 C ATOM 1392 N PRO A 186 25.223 22.872 17.418 1.00 66.06 N ANISOU 1392 N PRO A 186 6015 8634 10449 21 -173 2233 N ATOM 1393 CA PRO A 186 24.856 24.281 17.678 1.00 64.73 C ANISOU 1393 CA PRO A 186 5752 8527 10315 232 -40 2301 C ATOM 1394 C PRO A 186 26.036 25.227 17.829 1.00 65.82 C ANISOU 1394 C PRO A 186 6125 8587 10295 391 31 2168 C ATOM 1395 O PRO A 186 25.885 26.432 17.573 1.00 62.56 O ANISOU 1395 O PRO A 186 5666 8199 9904 541 66 2199 O ATOM 1396 CB PRO A 186 24.039 24.198 18.976 1.00 68.41 C ANISOU 1396 CB PRO A 186 6074 9032 10886 290 192 2423 C ATOM 1397 CG PRO A 186 23.459 22.810 18.962 1.00 63.65 C ANISOU 1397 CG PRO A 186 5360 8439 10384 68 113 2493 C ATOM 1398 CD PRO A 186 24.506 21.943 18.309 1.00 60.59 C ANISOU 1398 CD PRO A 186 5204 7945 9872 -76 -69 2337 C ATOM 1399 N LEU A 187 27.211 24.728 18.230 1.00 60.26 N ANISOU 1399 N LEU A 187 5665 7785 9444 362 50 2027 N ATOM 1400 CA LEU A 187 28.378 25.595 18.358 1.00 55.44 C ANISOU 1400 CA LEU A 187 5266 7105 8693 491 102 1898 C ATOM 1401 C LEU A 187 28.839 26.115 17.004 1.00 59.99 C ANISOU 1401 C LEU A 187 5889 7682 9221 483 -72 1851 C ATOM 1402 O LEU A 187 29.566 27.118 16.939 1.00 59.24 O ANISOU 1402 O LEU A 187 5911 7543 9056 601 -30 1786 O ATOM 1403 CB LEU A 187 29.526 24.839 19.046 1.00 53.24 C ANISOU 1403 CB LEU A 187 5213 6740 8274 451 140 1772 C ATOM 1404 CG LEU A 187 29.233 24.328 20.462 1.00 57.59 C ANISOU 1404 CG LEU A 187 5757 7292 8834 470 323 1820 C ATOM 1405 CD1 LEU A 187 30.443 23.647 21.122 1.00 55.16 C ANISOU 1405 CD1 LEU A 187 5677 6906 8374 449 347 1705 C ATOM 1406 CD2 LEU A 187 28.718 25.459 21.320 1.00 59.48 C ANISOU 1406 CD2 LEU A 187 5927 7571 9103 650 524 1867 C ATOM 1407 N PHE A 188 28.420 25.460 15.927 1.00 55.92 N ANISOU 1407 N PHE A 188 5287 7218 8740 343 -267 1886 N ATOM 1408 CA PHE A 188 28.848 25.810 14.589 1.00 56.04 C ANISOU 1408 CA PHE A 188 5357 7255 8682 323 -442 1846 C ATOM 1409 C PHE A 188 27.856 26.698 13.831 1.00 62.33 C ANISOU 1409 C PHE A 188 5949 8154 9580 386 -508 1989 C ATOM 1410 O PHE A 188 28.222 27.252 12.783 1.00 68.01 O ANISOU 1410 O PHE A 188 6716 8895 10227 409 -625 1979 O ATOM 1411 CB PHE A 188 29.164 24.522 13.830 1.00 51.53 C ANISOU 1411 CB PHE A 188 4861 6674 8046 135 -625 1764 C ATOM 1412 CG PHE A 188 30.423 23.874 14.322 1.00 56.83 C ANISOU 1412 CG PHE A 188 5767 7234 8593 114 -575 1616 C ATOM 1413 CD1 PHE A 188 31.660 24.246 13.803 1.00 55.23 C ANISOU 1413 CD1 PHE A 188 5751 6990 8243 161 -608 1499 C ATOM 1414 CD2 PHE A 188 30.384 22.952 15.356 1.00 59.30 C ANISOU 1414 CD2 PHE A 188 6103 7490 8939 60 -482 1610 C ATOM 1415 CE1 PHE A 188 32.838 23.676 14.292 1.00 53.90 C ANISOU 1415 CE1 PHE A 188 5778 6731 7971 154 -559 1373 C ATOM 1416 CE2 PHE A 188 31.552 22.372 15.838 1.00 53.71 C ANISOU 1416 CE2 PHE A 188 5603 6686 8119 57 -440 1490 C ATOM 1417 CZ PHE A 188 32.781 22.743 15.304 1.00 55.09 C ANISOU 1417 CZ PHE A 188 5950 6827 8154 108 -481 1369 C ATOM 1418 N GLU A 189 26.636 26.876 14.346 1.00 56.68 N ANISOU 1418 N GLU A 189 5004 7505 9026 426 -428 2133 N ATOM 1419 CA GLU A 189 25.710 27.908 13.862 1.00 65.41 C ANISOU 1419 CA GLU A 189 5906 8701 10247 541 -444 2286 C ATOM 1420 C GLU A 189 25.532 27.844 12.347 1.00 63.51 C ANISOU 1420 C GLU A 189 5610 8552 9969 454 -699 2323 C ATOM 1421 O GLU A 189 25.333 28.871 11.684 1.00 59.48 O ANISOU 1421 O GLU A 189 5040 8086 9474 570 -739 2412 O ATOM 1422 CB GLU A 189 26.175 29.301 14.302 1.00 68.91 C ANISOU 1422 CB GLU A 189 6441 9066 10676 757 -274 2273 C ATOM 1423 CG GLU A 189 26.563 29.357 15.780 1.00 80.95 C ANISOU 1423 CG GLU A 189 8075 10500 12184 838 -37 2193 C ATOM 1424 CD GLU A 189 26.687 30.768 16.332 1.00 81.85 C ANISOU 1424 CD GLU A 189 8231 10541 12326 1055 145 2194 C ATOM 1425 OE1 GLU A 189 27.096 30.924 17.509 1.00 79.69 O ANISOU 1425 OE1 GLU A 189 8076 10194 12011 1129 330 2106 O ATOM 1426 OE2 GLU A 189 26.386 31.722 15.590 1.00 80.56 O ANISOU 1426 OE2 GLU A 189 7994 10390 12226 1153 99 2281 O ATOM 1427 N ASN A 190 25.634 26.629 11.802 1.00 63.63 N ANISOU 1427 N ASN A 190 5662 8589 9926 252 -871 2252 N ATOM 1428 CA ASN A 190 25.405 26.284 10.400 1.00 69.44 C ANISOU 1428 CA ASN A 190 6355 9426 10605 130 -1134 2261 C ATOM 1429 C ASN A 190 26.390 26.925 9.434 1.00 72.31 C ANISOU 1429 C ASN A 190 6906 9777 10791 193 -1213 2194 C ATOM 1430 O ASN A 190 26.135 26.919 8.223 1.00 76.32 O ANISOU 1430 O ASN A 190 7368 10394 11235 135 -1419 2230 O ATOM 1431 CB ASN A 190 23.985 26.618 9.954 1.00 76.11 C ANISOU 1431 CB ASN A 190 6888 10427 11605 135 -1234 2455 C ATOM 1432 CG ASN A 190 23.005 25.560 10.346 1.00 88.31 C ANISOU 1432 CG ASN A 190 8236 12020 13296 -31 -1275 2507 C ATOM 1433 OD1 ASN A 190 23.267 24.373 10.147 1.00 87.82 O ANISOU 1433 OD1 ASN A 190 8267 11918 13182 -225 -1387 2392 O ATOM 1434 ND2 ASN A 190 21.857 25.969 10.885 1.00 93.38 N ANISOU 1434 ND2 ASN A 190 8602 12745 14135 43 -1182 2683 N ATOM 1435 N VAL A 191 27.512 27.468 9.918 1.00 62.90 N ANISOU 1435 N VAL A 191 5921 8467 9513 303 -1060 2100 N ATOM 1436 CA VAL A 191 28.441 28.109 9.005 1.00 64.77 C ANISOU 1436 CA VAL A 191 6319 8695 9596 357 -1120 2056 C ATOM 1437 C VAL A 191 29.121 27.059 8.143 1.00 68.36 C ANISOU 1437 C VAL A 191 6926 9163 9883 200 -1286 1916 C ATOM 1438 O VAL A 191 29.321 25.911 8.553 1.00 68.37 O ANISOU 1438 O VAL A 191 6994 9111 9874 77 -1293 1805 O ATOM 1439 CB VAL A 191 29.472 28.976 9.749 1.00 58.14 C ANISOU 1439 CB VAL A 191 5646 7722 8724 499 -919 1991 C ATOM 1440 CG1 VAL A 191 28.756 29.979 10.656 1.00 55.64 C ANISOU 1440 CG1 VAL A 191 5192 7376 8572 660 -743 2107 C ATOM 1441 CG2 VAL A 191 30.468 28.104 10.527 1.00 50.63 C ANISOU 1441 CG2 VAL A 191 4881 6665 7692 430 -839 1817 C ATOM 1442 N VAL A 192 29.467 27.457 6.943 1.00 68.32 N ANISOU 1442 N VAL A 192 6984 9229 9746 211 -1413 1926 N ATOM 1443 CA VAL A 192 30.200 26.617 6.009 1.00 67.17 C ANISOU 1443 CA VAL A 192 7005 9104 9412 91 -1557 1786 C ATOM 1444 C VAL A 192 31.686 26.792 6.300 1.00 65.54 C ANISOU 1444 C VAL A 192 7031 8778 9091 153 -1421 1657 C ATOM 1445 O VAL A 192 32.156 27.905 6.557 1.00 63.46 O ANISOU 1445 O VAL A 192 6802 8469 8842 289 -1292 1709 O ATOM 1446 CB VAL A 192 29.840 26.994 4.556 1.00 69.45 C ANISOU 1446 CB VAL A 192 7246 9550 9591 82 -1755 1870 C ATOM 1447 CG1 VAL A 192 30.858 26.444 3.559 1.00 60.99 C ANISOU 1447 CG1 VAL A 192 6393 8497 8282 13 -1854 1721 C ATOM 1448 CG2 VAL A 192 28.419 26.527 4.224 1.00 67.26 C ANISOU 1448 CG2 VAL A 192 6738 9405 9414 -23 -1933 1966 C ATOM 1449 N ILE A 193 32.425 25.687 6.279 1.00 58.26 N ANISOU 1449 N ILE A 193 6265 7801 8071 52 -1448 1490 N ATOM 1450 CA ILE A 193 33.803 25.644 6.745 1.00 55.76 C ANISOU 1450 CA ILE A 193 6144 7372 7672 99 -1315 1365 C ATOM 1451 C ILE A 193 34.675 25.188 5.586 1.00 54.31 C ANISOU 1451 C ILE A 193 6123 7227 7287 51 -1418 1253 C ATOM 1452 O ILE A 193 34.451 24.113 5.017 1.00 54.43 O ANISOU 1452 O ILE A 193 6171 7271 7240 -70 -1556 1166 O ATOM 1453 CB ILE A 193 33.955 24.737 7.977 1.00 60.03 C ANISOU 1453 CB ILE A 193 6719 7798 8293 54 -1216 1279 C ATOM 1454 CG1 ILE A 193 33.254 25.410 9.163 1.00 59.48 C ANISOU 1454 CG1 ILE A 193 6509 7699 8391 137 -1073 1391 C ATOM 1455 CG2 ILE A 193 35.433 24.496 8.301 1.00 55.21 C ANISOU 1455 CG2 ILE A 193 6309 7092 7576 88 -1120 1140 C ATOM 1456 CD1 ILE A 193 33.164 24.595 10.386 1.00 61.09 C ANISOU 1456 CD1 ILE A 193 6716 7820 8675 97 -976 1350 C ATOM 1457 N GLU A 194 35.622 26.044 5.189 1.00 55.37 N ANISOU 1457 N GLU A 194 6352 7363 7321 146 -1351 1259 N ATOM 1458 CA GLU A 194 36.526 25.696 4.102 1.00 65.64 C ANISOU 1458 CA GLU A 194 7808 8712 8420 121 -1416 1163 C ATOM 1459 C GLU A 194 37.810 25.077 4.648 1.00 63.67 C ANISOU 1459 C GLU A 194 7717 8352 8121 127 -1306 1007 C ATOM 1460 O GLU A 194 38.377 25.574 5.627 1.00 61.68 O ANISOU 1460 O GLU A 194 7477 8011 7948 198 -1156 1010 O ATOM 1461 CB GLU A 194 36.870 26.923 3.266 1.00 74.05 C ANISOU 1461 CB GLU A 194 8883 9854 9398 214 -1403 1275 C ATOM 1462 CG GLU A 194 35.739 27.326 2.346 1.00101.57 C ANISOU 1462 CG GLU A 194 12242 13482 12866 204 -1559 1419 C ATOM 1463 CD GLU A 194 35.519 26.312 1.230 1.00119.41 C ANISOU 1463 CD GLU A 194 14559 15858 14954 90 -1752 1328 C ATOM 1464 OE1 GLU A 194 36.521 25.751 0.726 1.00125.95 O ANISOU 1464 OE1 GLU A 194 15560 16681 15613 69 -1743 1188 O ATOM 1465 OE2 GLU A 194 34.344 26.056 0.879 1.00122.81 O ANISOU 1465 OE2 GLU A 194 14859 16382 15420 20 -1912 1390 O ATOM 1466 N PRO A 195 38.298 24.009 4.031 1.00 62.51 N ANISOU 1466 N PRO A 195 7696 8212 7844 58 -1378 865 N ATOM 1467 CA PRO A 195 39.566 23.427 4.490 1.00 56.90 C ANISOU 1467 CA PRO A 195 7128 7404 7089 84 -1272 729 C ATOM 1468 C PRO A 195 40.715 24.412 4.319 1.00 54.24 C ANISOU 1468 C PRO A 195 6848 7081 6681 187 -1154 755 C ATOM 1469 O PRO A 195 40.898 25.002 3.259 1.00 58.84 O ANISOU 1469 O PRO A 195 7451 7764 7143 213 -1189 806 O ATOM 1470 CB PRO A 195 39.732 22.187 3.605 1.00 55.29 C ANISOU 1470 CB PRO A 195 7044 7215 6749 2 -1386 582 C ATOM 1471 CG PRO A 195 38.322 21.909 3.043 1.00 60.88 C ANISOU 1471 CG PRO A 195 7651 8002 7480 -105 -1565 629 C ATOM 1472 CD PRO A 195 37.686 23.249 2.922 1.00 57.13 C ANISOU 1472 CD PRO A 195 7031 7622 7054 -44 -1565 816 C ATOM 1473 N CYS A 196 41.493 24.585 5.379 1.00 51.74 N ANISOU 1473 N CYS A 196 6552 6669 6440 240 -1018 726 N ATOM 1474 CA CYS A 196 42.678 25.432 5.355 1.00 47.67 C ANISOU 1474 CA CYS A 196 6081 6149 5881 318 -904 737 C ATOM 1475 C CYS A 196 43.876 24.617 5.824 1.00 45.31 C ANISOU 1475 C CYS A 196 5884 5786 5546 332 -834 601 C ATOM 1476 O CYS A 196 43.757 23.769 6.712 1.00 45.92 O ANISOU 1476 O CYS A 196 5971 5783 5693 309 -826 538 O ATOM 1477 CB CYS A 196 42.502 26.691 6.251 1.00 46.49 C ANISOU 1477 CB CYS A 196 5843 5949 5873 376 -808 843 C ATOM 1478 SG CYS A 196 41.220 27.924 5.715 1.00 58.91 S ANISOU 1478 SG CYS A 196 7286 7584 7512 403 -860 1034 S ATOM 1479 N LEU A 197 45.020 24.846 5.204 1.00 46.87 N ANISOU 1479 N LEU A 197 6149 6024 5636 374 -780 570 N ATOM 1480 CA LEU A 197 46.257 24.249 5.683 1.00 45.23 C ANISOU 1480 CA LEU A 197 6010 5765 5409 409 -699 464 C ATOM 1481 C LEU A 197 46.590 24.815 7.062 1.00 46.32 C ANISOU 1481 C LEU A 197 6093 5826 5681 439 -609 489 C ATOM 1482 O LEU A 197 46.846 26.014 7.192 1.00 53.22 O ANISOU 1482 O LEU A 197 6919 6706 6598 466 -550 565 O ATOM 1483 CB LEU A 197 47.391 24.504 4.689 1.00 45.56 C ANISOU 1483 CB LEU A 197 6108 5886 5316 452 -647 447 C ATOM 1484 CG LEU A 197 48.674 23.789 5.168 1.00 47.01 C ANISOU 1484 CG LEU A 197 6345 6027 5489 498 -566 339 C ATOM 1485 CD1 LEU A 197 48.427 22.298 5.330 1.00 45.73 C ANISOU 1485 CD1 LEU A 197 6260 5801 5314 480 -623 219 C ATOM 1486 CD2 LEU A 197 49.816 24.044 4.254 1.00 43.03 C ANISOU 1486 CD2 LEU A 197 5876 5609 4866 546 -494 330 C ATOM 1487 N LEU A 198 46.580 23.957 8.086 1.00 44.65 N ANISOU 1487 N LEU A 198 5897 5538 5531 434 -601 425 N ATOM 1488 CA LEU A 198 46.885 24.325 9.466 1.00 43.01 C ANISOU 1488 CA LEU A 198 5653 5268 5420 464 -527 432 C ATOM 1489 C LEU A 198 48.291 23.881 9.865 1.00 46.69 C ANISOU 1489 C LEU A 198 6167 5721 5853 509 -471 352 C ATOM 1490 O LEU A 198 48.750 22.807 9.475 1.00 41.58 O ANISOU 1490 O LEU A 198 5587 5069 5143 521 -489 277 O ATOM 1491 CB LEU A 198 45.869 23.693 10.433 1.00 47.57 C ANISOU 1491 CB LEU A 198 6207 5785 6084 434 -550 442 C ATOM 1492 CG LEU A 198 44.371 23.900 10.167 1.00 44.81 C ANISOU 1492 CG LEU A 198 5784 5451 5790 385 -612 524 C ATOM 1493 CD1 LEU A 198 43.525 23.307 11.272 1.00 43.69 C ANISOU 1493 CD1 LEU A 198 5605 5252 5743 360 -603 543 C ATOM 1494 CD2 LEU A 198 44.071 25.369 10.021 1.00 35.66 C ANISOU 1494 CD2 LEU A 198 4553 4325 4672 416 -579 619 C ATOM 1495 N HIS A 199 48.956 24.701 10.680 1.00 49.41 N ANISOU 1495 N HIS A 199 6473 6054 6245 538 -405 365 N ATOM 1496 CA HIS A 199 50.203 24.282 11.308 1.00 41.31 C ANISOU 1496 CA HIS A 199 5467 5024 5207 579 -365 301 C ATOM 1497 C HIS A 199 49.954 23.157 12.316 1.00 40.11 C ANISOU 1497 C HIS A 199 5347 4812 5079 592 -383 266 C ATOM 1498 O HIS A 199 50.684 22.152 12.342 1.00 44.19 O ANISOU 1498 O HIS A 199 5910 5318 5562 630 -383 210 O ATOM 1499 CB HIS A 199 50.881 25.493 11.980 1.00 33.82 C ANISOU 1499 CB HIS A 199 4463 4079 4309 586 -312 319 C ATOM 1500 CG HIS A 199 52.153 25.153 12.701 1.00 41.85 C ANISOU 1500 CG HIS A 199 5474 5109 5318 622 -288 262 C ATOM 1501 ND1 HIS A 199 52.176 24.506 13.922 1.00 43.72 N ANISOU 1501 ND1 HIS A 199 5726 5316 5569 647 -299 231 N ATOM 1502 CD2 HIS A 199 53.449 25.365 12.366 1.00 42.89 C ANISOU 1502 CD2 HIS A 199 5575 5294 5429 641 -256 242 C ATOM 1503 CE1 HIS A 199 53.429 24.326 14.300 1.00 41.56 C ANISOU 1503 CE1 HIS A 199 5432 5078 5281 683 -288 194 C ATOM 1504 NE2 HIS A 199 54.222 24.847 13.376 1.00 40.80 N ANISOU 1504 NE2 HIS A 199 5298 5032 5171 677 -260 198 N ATOM 1505 N GLY A 200 48.950 23.313 13.178 1.00 40.26 N ANISOU 1505 N GLY A 200 5343 4793 5162 569 -387 307 N ATOM 1506 CA GLY A 200 48.497 22.229 14.039 1.00 41.62 C ANISOU 1506 CA GLY A 200 5546 4910 5359 569 -398 302 C ATOM 1507 C GLY A 200 49.105 22.165 15.436 1.00 47.37 C ANISOU 1507 C GLY A 200 6277 5628 6093 615 -359 293 C ATOM 1508 O GLY A 200 48.616 21.389 16.275 1.00 44.70 O ANISOU 1508 O GLY A 200 5961 5248 5775 618 -357 316 O ATOM 1509 N ASP A 201 50.155 22.936 15.722 1.00 43.43 N ANISOU 1509 N ASP A 201 5756 5173 5575 646 -333 265 N ATOM 1510 CA ASP A 201 50.766 22.906 17.053 1.00 44.93 C ANISOU 1510 CA ASP A 201 5947 5373 5752 686 -316 250 C ATOM 1511 C ASP A 201 51.489 24.223 17.310 1.00 46.24 C ANISOU 1511 C ASP A 201 6068 5580 5921 681 -297 223 C ATOM 1512 O ASP A 201 52.692 24.243 17.597 1.00 48.03 O ANISOU 1512 O ASP A 201 6276 5849 6122 706 -306 185 O ATOM 1513 CB ASP A 201 51.748 21.729 17.186 1.00 45.75 C ANISOU 1513 CB ASP A 201 6085 5480 5820 742 -334 223 C ATOM 1514 CG ASP A 201 52.247 21.523 18.633 1.00 55.54 C ANISOU 1514 CG ASP A 201 7329 6742 7033 789 -333 228 C ATOM 1515 OD1 ASP A 201 51.538 21.895 19.601 1.00 59.05 O ANISOU 1515 OD1 ASP A 201 7777 7182 7475 776 -315 254 O ATOM 1516 OD2 ASP A 201 53.348 20.974 18.805 1.00 56.86 O ANISOU 1516 OD2 ASP A 201 7494 6938 7173 846 -350 210 O ATOM 1517 N LEU A 202 50.771 25.329 17.236 1.00 42.93 N ANISOU 1517 N LEU A 202 5625 5142 5544 647 -272 244 N ATOM 1518 CA LEU A 202 51.403 26.643 17.142 1.00 46.07 C ANISOU 1518 CA LEU A 202 5987 5548 5968 625 -253 221 C ATOM 1519 C LEU A 202 51.496 27.256 18.535 1.00 46.37 C ANISOU 1519 C LEU A 202 6035 5579 6006 632 -238 177 C ATOM 1520 O LEU A 202 50.527 27.828 19.035 1.00 49.03 O ANISOU 1520 O LEU A 202 6383 5875 6371 634 -202 189 O ATOM 1521 CB LEU A 202 50.601 27.529 16.201 1.00 43.67 C ANISOU 1521 CB LEU A 202 5662 5214 5718 595 -233 275 C ATOM 1522 CG LEU A 202 51.265 28.796 15.716 1.00 49.84 C ANISOU 1522 CG LEU A 202 6410 5985 6540 565 -210 277 C ATOM 1523 CD1 LEU A 202 52.577 28.442 15.020 1.00 47.72 C ANISOU 1523 CD1 LEU A 202 6119 5778 6233 559 -221 259 C ATOM 1524 CD2 LEU A 202 50.301 29.418 14.753 1.00 53.28 C ANISOU 1524 CD2 LEU A 202 6832 6393 7019 554 -197 358 C ATOM 1525 N TRP A 203 52.671 27.148 19.157 1.00 48.06 N ANISOU 1525 N TRP A 203 6240 5840 6180 640 -266 122 N ATOM 1526 CA TRP A 203 52.941 27.786 20.445 1.00 43.65 C ANISOU 1526 CA TRP A 203 5696 5290 5597 637 -271 59 C ATOM 1527 C TRP A 203 54.345 28.403 20.384 1.00 48.03 C ANISOU 1527 C TRP A 203 6199 5885 6167 597 -308 3 C ATOM 1528 O TRP A 203 55.013 28.364 19.342 1.00 51.78 O ANISOU 1528 O TRP A 203 6621 6378 6674 579 -310 28 O ATOM 1529 CB TRP A 203 52.745 26.785 21.593 1.00 41.93 C ANISOU 1529 CB TRP A 203 5524 5111 5296 691 -286 63 C ATOM 1530 CG TRP A 203 53.783 25.723 21.648 1.00 49.08 C ANISOU 1530 CG TRP A 203 6414 6080 6155 728 -338 69 C ATOM 1531 CD1 TRP A 203 53.900 24.662 20.808 1.00 52.07 C ANISOU 1531 CD1 TRP A 203 6788 6452 6544 756 -344 114 C ATOM 1532 CD2 TRP A 203 54.844 25.597 22.606 1.00 45.74 C ANISOU 1532 CD2 TRP A 203 5978 5737 5667 751 -395 28 C ATOM 1533 NE1 TRP A 203 54.981 23.894 21.157 1.00 45.82 N ANISOU 1533 NE1 TRP A 203 5979 5720 5711 807 -388 110 N ATOM 1534 CE2 TRP A 203 55.584 24.441 22.255 1.00 48.13 C ANISOU 1534 CE2 TRP A 203 6256 6076 5957 804 -426 66 C ATOM 1535 CE3 TRP A 203 55.255 26.356 23.712 1.00 45.77 C ANISOU 1535 CE3 TRP A 203 5988 5786 5617 732 -429 -44 C ATOM 1536 CZ2 TRP A 203 56.710 24.015 22.978 1.00 48.21 C ANISOU 1536 CZ2 TRP A 203 6232 6174 5912 849 -490 56 C ATOM 1537 CZ3 TRP A 203 56.385 25.932 24.440 1.00 48.36 C ANISOU 1537 CZ3 TRP A 203 6285 6214 5875 761 -508 -64 C ATOM 1538 CH2 TRP A 203 57.099 24.776 24.060 1.00 48.64 C ANISOU 1538 CH2 TRP A 203 6279 6291 5909 822 -538 -4 C ATOM 1539 N SER A 204 54.783 29.010 21.496 1.00 45.94 N ANISOU 1539 N SER A 204 5945 5637 5875 578 -335 -74 N ATOM 1540 CA SER A 204 56.009 29.823 21.500 1.00 48.30 C ANISOU 1540 CA SER A 204 6182 5959 6211 511 -377 -135 C ATOM 1541 C SER A 204 57.242 29.038 21.076 1.00 52.05 C ANISOU 1541 C SER A 204 6575 6530 6673 525 -423 -111 C ATOM 1542 O SER A 204 58.128 29.585 20.417 1.00 53.10 O ANISOU 1542 O SER A 204 6627 6678 6872 469 -426 -112 O ATOM 1543 CB SER A 204 56.258 30.414 22.888 1.00 48.59 C ANISOU 1543 CB SER A 204 6255 6012 6195 487 -421 -240 C ATOM 1544 OG SER A 204 55.456 31.563 23.072 1.00 66.58 O ANISOU 1544 OG SER A 204 8591 8182 8524 456 -367 -285 O ATOM 1545 N GLY A 205 57.356 27.780 21.510 1.00 52.89 N ANISOU 1545 N GLY A 205 6696 6700 6701 604 -453 -85 N ATOM 1546 CA GLY A 205 58.515 26.986 21.158 1.00 52.22 C ANISOU 1546 CA GLY A 205 6532 6701 6610 642 -488 -60 C ATOM 1547 C GLY A 205 58.640 26.650 19.678 1.00 54.77 C ANISOU 1547 C GLY A 205 6819 7008 6982 656 -433 -5 C ATOM 1548 O GLY A 205 59.707 26.197 19.266 1.00 51.99 O ANISOU 1548 O GLY A 205 6387 6727 6638 687 -442 9 O ATOM 1549 N ASN A 206 57.595 26.877 18.878 1.00 51.73 N ANISOU 1549 N ASN A 206 6489 6543 6622 638 -376 26 N ATOM 1550 CA ASN A 206 57.575 26.558 17.454 1.00 49.38 C ANISOU 1550 CA ASN A 206 6181 6240 6342 651 -328 73 C ATOM 1551 C ASN A 206 57.586 27.801 16.576 1.00 45.91 C ANISOU 1551 C ASN A 206 5704 5773 5965 574 -285 94 C ATOM 1552 O ASN A 206 57.344 27.695 15.369 1.00 47.12 O ANISOU 1552 O ASN A 206 5866 5924 6115 580 -243 141 O ATOM 1553 CB ASN A 206 56.339 25.715 17.111 1.00 46.59 C ANISOU 1553 CB ASN A 206 5917 5829 5957 689 -313 104 C ATOM 1554 CG ASN A 206 56.453 24.287 17.577 1.00 53.89 C ANISOU 1554 CG ASN A 206 6878 6764 6834 769 -338 106 C ATOM 1555 OD1 ASN A 206 57.551 23.772 17.734 1.00 58.36 O ANISOU 1555 OD1 ASN A 206 7398 7389 7386 819 -356 96 O ATOM 1556 ND2 ASN A 206 55.316 23.636 17.812 1.00 49.55 N ANISOU 1556 ND2 ASN A 206 6404 6152 6270 781 -338 129 N ATOM 1557 N ILE A 207 57.808 28.975 17.158 1.00 48.17 N ANISOU 1557 N ILE A 207 5962 6033 6307 502 -296 62 N ATOM 1558 CA ILE A 207 57.797 30.245 16.446 1.00 48.45 C ANISOU 1558 CA ILE A 207 5970 6014 6423 425 -252 92 C ATOM 1559 C ILE A 207 59.157 30.900 16.639 1.00 50.01 C ANISOU 1559 C ILE A 207 6065 6255 6681 354 -270 64 C ATOM 1560 O ILE A 207 59.714 30.864 17.738 1.00 49.05 O ANISOU 1560 O ILE A 207 5919 6169 6549 340 -335 -8 O ATOM 1561 CB ILE A 207 56.677 31.169 16.966 1.00 50.04 C ANISOU 1561 CB ILE A 207 6241 6105 6667 396 -240 76 C ATOM 1562 CG1 ILE A 207 55.305 30.518 16.804 1.00 48.32 C ANISOU 1562 CG1 ILE A 207 6097 5858 6404 459 -225 116 C ATOM 1563 CG2 ILE A 207 56.726 32.530 16.273 1.00 48.08 C ANISOU 1563 CG2 ILE A 207 5968 5779 6522 321 -193 118 C ATOM 1564 CD1 ILE A 207 54.203 31.207 17.596 1.00 48.86 C ANISOU 1564 CD1 ILE A 207 6223 5838 6503 460 -208 94 C ATOM 1565 N ALA A 208 59.688 31.508 15.582 1.00 50.13 N ANISOU 1565 N ALA A 208 6015 6275 6758 304 -215 127 N ATOM 1566 CA ALA A 208 60.992 32.154 15.655 1.00 46.84 C ANISOU 1566 CA ALA A 208 5477 5900 6420 219 -224 117 C ATOM 1567 C ALA A 208 61.011 33.305 14.665 1.00 46.16 C ANISOU 1567 C ALA A 208 5364 5745 6428 137 -149 198 C ATOM 1568 O ALA A 208 60.077 33.480 13.878 1.00 52.59 O ANISOU 1568 O ALA A 208 6251 6503 7228 164 -96 267 O ATOM 1569 CB ALA A 208 62.120 31.147 15.391 1.00 44.23 C ANISOU 1569 CB ALA A 208 5044 5713 6049 278 -227 132 C ATOM 1570 N TYR A 209 62.073 34.118 14.717 1.00 53.01 N ANISOU 1570 N TYR A 209 6122 6618 7400 30 -149 200 N ATOM 1571 CA TYR A 209 62.201 35.267 13.817 1.00 56.90 C ANISOU 1571 CA TYR A 209 6583 7034 8001 -62 -70 294 C ATOM 1572 C TYR A 209 63.591 35.283 13.200 1.00 57.27 C ANISOU 1572 C TYR A 209 6468 7193 8100 -114 -27 359 C ATOM 1573 O TYR A 209 64.576 35.004 13.881 1.00 62.65 O ANISOU 1573 O TYR A 209 7041 7961 8803 -143 -89 297 O ATOM 1574 CB TYR A 209 61.907 36.604 14.553 1.00 55.02 C ANISOU 1574 CB TYR A 209 6388 6627 7888 -173 -98 237 C ATOM 1575 CG TYR A 209 60.460 36.715 14.973 1.00 55.74 C ANISOU 1575 CG TYR A 209 6631 6607 7942 -108 -105 200 C ATOM 1576 CD1 TYR A 209 60.010 36.107 16.144 1.00 56.37 C ANISOU 1576 CD1 TYR A 209 6777 6704 7937 -50 -178 82 C ATOM 1577 CD2 TYR A 209 59.534 37.391 14.182 1.00 53.27 C ANISOU 1577 CD2 TYR A 209 6385 6183 7674 -94 -33 299 C ATOM 1578 CE1 TYR A 209 58.678 36.167 16.522 1.00 49.51 C ANISOU 1578 CE1 TYR A 209 6029 5747 7035 16 -168 60 C ATOM 1579 CE2 TYR A 209 58.195 37.456 14.545 1.00 53.64 C ANISOU 1579 CE2 TYR A 209 6545 6141 7694 -23 -35 278 C ATOM 1580 CZ TYR A 209 57.776 36.851 15.709 1.00 54.37 C ANISOU 1580 CZ TYR A 209 6693 6254 7710 29 -96 157 C ATOM 1581 OH TYR A 209 56.462 36.931 16.062 1.00 54.43 O ANISOU 1581 OH TYR A 209 6797 6184 7701 100 -82 146 O ATOM 1582 N ASP A 210 63.668 35.593 11.910 1.00 55.38 N ANISOU 1582 N ASP A 210 6204 6967 7873 -120 80 492 N ATOM 1583 CA ASP A 210 64.927 35.531 11.185 1.00 60.30 C ANISOU 1583 CA ASP A 210 6668 7713 8529 -151 152 574 C ATOM 1584 C ASP A 210 65.610 36.905 11.215 1.00 71.46 C ANISOU 1584 C ASP A 210 7983 9040 10128 -326 175 623 C ATOM 1585 O ASP A 210 65.238 37.788 11.993 1.00 71.70 O ANISOU 1585 O ASP A 210 8068 8917 10257 -420 114 555 O ATOM 1586 CB ASP A 210 64.699 34.987 9.766 1.00 50.37 C ANISOU 1586 CB ASP A 210 5442 6541 7153 -50 264 690 C ATOM 1587 CG ASP A 210 63.957 35.961 8.843 1.00 58.87 C ANISOU 1587 CG ASP A 210 6595 7517 8255 -91 340 816 C ATOM 1588 OD1 ASP A 210 63.673 37.118 9.232 1.00 60.08 O ANISOU 1588 OD1 ASP A 210 6770 7515 8542 -197 322 828 O ATOM 1589 OD2 ASP A 210 63.673 35.566 7.687 1.00 61.25 O ANISOU 1589 OD2 ASP A 210 6940 7895 8437 -10 418 908 O ATOM 1590 N LYS A 211 66.625 37.091 10.360 1.00 73.33 N ANISOU 1590 N LYS A 211 8074 9372 10417 -373 272 740 N ATOM 1591 CA LYS A 211 67.442 38.308 10.371 1.00 78.17 C ANISOU 1591 CA LYS A 211 8562 9914 11226 -557 297 798 C ATOM 1592 C LYS A 211 66.660 39.555 9.950 1.00 75.45 C ANISOU 1592 C LYS A 211 8325 9366 10976 -638 350 884 C ATOM 1593 O LYS A 211 66.969 40.656 10.423 1.00 76.11 O ANISOU 1593 O LYS A 211 8372 9305 11240 -799 323 867 O ATOM 1594 CB LYS A 211 68.661 38.122 9.460 1.00 85.90 C ANISOU 1594 CB LYS A 211 9349 11060 12229 -572 413 929 C ATOM 1595 CG LYS A 211 68.315 37.960 7.966 1.00 90.73 C ANISOU 1595 CG LYS A 211 10015 11731 12727 -478 570 1092 C ATOM 1596 CD LYS A 211 69.551 37.771 7.080 1.00 93.37 C ANISOU 1596 CD LYS A 211 10157 12244 13074 -482 708 1222 C ATOM 1597 CE LYS A 211 69.171 37.527 5.611 1.00 94.22 C ANISOU 1597 CE LYS A 211 10343 12432 13023 -371 862 1368 C ATOM 1598 NZ LYS A 211 68.370 36.272 5.411 1.00 93.59 N ANISOU 1598 NZ LYS A 211 10417 12423 12719 -177 833 1279 N ATOM 1599 N ASN A 212 65.665 39.418 9.060 1.00 71.92 N ANISOU 1599 N ASN A 212 8008 8901 10418 -530 420 978 N ATOM 1600 CA ASN A 212 64.781 40.528 8.693 1.00 70.76 C ANISOU 1600 CA ASN A 212 7974 8561 10352 -573 461 1069 C ATOM 1601 C ASN A 212 63.599 40.708 9.662 1.00 69.61 C ANISOU 1601 C ASN A 212 7984 8258 10208 -536 362 937 C ATOM 1602 O ASN A 212 62.664 41.447 9.328 1.00 69.61 O ANISOU 1602 O ASN A 212 8090 8110 10249 -524 396 1013 O ATOM 1603 CB ASN A 212 64.232 40.348 7.270 1.00 72.64 C ANISOU 1603 CB ASN A 212 8271 8867 10460 -471 571 1245 C ATOM 1604 CG ASN A 212 65.309 39.999 6.245 1.00 85.71 C ANISOU 1604 CG ASN A 212 9792 10710 12064 -469 690 1372 C ATOM 1605 OD1 ASN A 212 66.302 40.708 6.095 1.00 88.68 O ANISOU 1605 OD1 ASN A 212 10031 11076 12588 -601 754 1456 O ATOM 1606 ND2 ASN A 212 65.113 38.888 5.538 1.00 89.45 N ANISOU 1606 ND2 ASN A 212 10304 11356 12329 -321 723 1382 N ATOM 1607 N ASN A 213 63.623 40.071 10.839 1.00 68.97 N ANISOU 1607 N ASN A 213 7913 8211 10083 -512 250 754 N ATOM 1608 CA ASN A 213 62.490 40.097 11.777 1.00 67.99 C ANISOU 1608 CA ASN A 213 7933 7968 9930 -457 172 630 C ATOM 1609 C ASN A 213 61.191 39.630 11.131 1.00 63.11 C ANISOU 1609 C ASN A 213 7435 7358 9187 -313 204 700 C ATOM 1610 O ASN A 213 60.117 40.155 11.412 1.00 69.34 O ANISOU 1610 O ASN A 213 8333 8005 10009 -284 196 688 O ATOM 1611 CB ASN A 213 62.310 41.481 12.413 1.00 77.13 C ANISOU 1611 CB ASN A 213 9142 8895 11270 -578 157 580 C ATOM 1612 CG ASN A 213 63.416 41.824 13.373 1.00 91.35 C ANISOU 1612 CG ASN A 213 10848 10686 13175 -724 78 450 C ATOM 1613 OD1 ASN A 213 63.347 41.484 14.553 1.00 97.77 O ANISOU 1613 OD1 ASN A 213 11699 11513 13937 -712 -26 278 O ATOM 1614 ND2 ASN A 213 64.455 42.480 12.872 1.00 92.68 N ANISOU 1614 ND2 ASN A 213 10887 10842 13485 -865 124 539 N ATOM 1615 N GLU A 214 61.302 38.646 10.235 1.00 51.95 N ANISOU 1615 N GLU A 214 5995 6114 7631 -223 242 772 N ATOM 1616 CA GLU A 214 60.147 37.958 9.674 1.00 55.14 C ANISOU 1616 CA GLU A 214 6500 6558 7892 -94 243 811 C ATOM 1617 C GLU A 214 59.885 36.646 10.417 1.00 52.86 C ANISOU 1617 C GLU A 214 6245 6359 7479 -3 163 676 C ATOM 1618 O GLU A 214 60.829 35.993 10.879 1.00 48.87 O ANISOU 1618 O GLU A 214 5664 5953 6952 -7 133 600 O ATOM 1619 CB GLU A 214 60.361 37.670 8.180 1.00 58.55 C ANISOU 1619 CB GLU A 214 6907 7113 8225 -51 331 964 C ATOM 1620 CG GLU A 214 60.266 38.915 7.288 1.00 65.11 C ANISOU 1620 CG GLU A 214 7737 7854 9148 -112 417 1142 C ATOM 1621 CD GLU A 214 58.868 39.526 7.235 1.00 75.29 C ANISOU 1621 CD GLU A 214 9138 9004 10463 -69 397 1195 C ATOM 1622 OE1 GLU A 214 57.923 38.789 6.904 1.00 77.64 O ANISOU 1622 OE1 GLU A 214 9507 9371 10624 36 360 1196 O ATOM 1623 OE2 GLU A 214 58.716 40.746 7.493 1.00 80.26 O ANISOU 1623 OE2 GLU A 214 9781 9452 11260 -139 420 1241 O ATOM 1624 N PRO A 215 58.625 36.240 10.575 1.00 53.13 N ANISOU 1624 N PRO A 215 6383 6361 7443 80 126 653 N ATOM 1625 CA PRO A 215 58.338 35.003 11.315 1.00 50.20 C ANISOU 1625 CA PRO A 215 6047 6058 6969 157 57 538 C ATOM 1626 C PRO A 215 58.729 33.736 10.561 1.00 48.72 C ANISOU 1626 C PRO A 215 5841 6022 6647 232 69 552 C ATOM 1627 O PRO A 215 58.701 33.668 9.329 1.00 53.75 O ANISOU 1627 O PRO A 215 6481 6718 7222 256 126 649 O ATOM 1628 CB PRO A 215 56.824 35.063 11.528 1.00 50.17 C ANISOU 1628 CB PRO A 215 6143 5970 6951 211 33 541 C ATOM 1629 CG PRO A 215 56.324 35.961 10.420 1.00 45.69 C ANISOU 1629 CG PRO A 215 5588 5348 6423 200 91 687 C ATOM 1630 CD PRO A 215 57.404 36.977 10.215 1.00 47.11 C ANISOU 1630 CD PRO A 215 5699 5485 6717 101 145 735 C ATOM 1631 N VAL A 216 59.092 32.722 11.339 1.00 43.18 N ANISOU 1631 N VAL A 216 5130 5381 5895 277 17 451 N ATOM 1632 CA VAL A 216 59.403 31.381 10.864 1.00 43.52 C ANISOU 1632 CA VAL A 216 5175 5539 5822 365 22 434 C ATOM 1633 C VAL A 216 58.687 30.415 11.793 1.00 47.25 C ANISOU 1633 C VAL A 216 5722 5988 6243 427 -52 347 C ATOM 1634 O VAL A 216 58.786 30.562 13.013 1.00 49.10 O ANISOU 1634 O VAL A 216 5947 6188 6522 405 -104 280 O ATOM 1635 CB VAL A 216 60.920 31.092 10.898 1.00 43.17 C ANISOU 1635 CB VAL A 216 5010 5599 5795 363 47 419 C ATOM 1636 CG1 VAL A 216 61.218 29.737 10.264 1.00 36.87 C ANISOU 1636 CG1 VAL A 216 4226 4903 4880 476 74 405 C ATOM 1637 CG2 VAL A 216 61.734 32.217 10.260 1.00 37.59 C ANISOU 1637 CG2 VAL A 216 4202 4902 5177 272 121 508 C ATOM 1638 N ILE A 217 57.985 29.418 11.241 1.00 42.44 N ANISOU 1638 N ILE A 217 5188 5400 5538 498 -59 348 N ATOM 1639 CA ILE A 217 57.326 28.454 12.116 1.00 43.47 C ANISOU 1639 CA ILE A 217 5383 5501 5634 547 -120 282 C ATOM 1640 C ILE A 217 57.877 27.061 11.832 1.00 46.83 C ANISOU 1640 C ILE A 217 5820 5992 5982 631 -119 245 C ATOM 1641 O ILE A 217 58.284 26.766 10.702 1.00 47.21 O ANISOU 1641 O ILE A 217 5865 6100 5974 661 -69 268 O ATOM 1642 CB ILE A 217 55.784 28.510 12.003 1.00 43.41 C ANISOU 1642 CB ILE A 217 5456 5423 5615 544 -144 308 C ATOM 1643 CG1 ILE A 217 55.296 28.200 10.597 1.00 49.36 C ANISOU 1643 CG1 ILE A 217 6249 6211 6294 562 -129 360 C ATOM 1644 CG2 ILE A 217 55.266 29.912 12.409 1.00 38.05 C ANISOU 1644 CG2 ILE A 217 4764 4662 5029 484 -134 341 C ATOM 1645 CD1 ILE A 217 53.759 28.359 10.470 1.00 42.43 C ANISOU 1645 CD1 ILE A 217 5422 5278 5421 550 -166 400 C ATOM 1646 N LEU A 218 57.902 26.211 12.883 1.00 46.07 N ANISOU 1646 N LEU A 218 5743 5881 5879 675 -168 191 N ATOM 1647 CA LEU A 218 58.665 24.956 12.925 1.00 47.96 C ANISOU 1647 CA LEU A 218 5979 6167 6078 765 -168 156 C ATOM 1648 C LEU A 218 57.835 23.825 13.531 1.00 48.09 C ANISOU 1648 C LEU A 218 6089 6117 6064 813 -214 128 C ATOM 1649 O LEU A 218 56.833 24.059 14.219 1.00 45.67 O ANISOU 1649 O LEU A 218 5827 5751 5776 774 -249 134 O ATOM 1650 CB LEU A 218 59.940 25.112 13.778 1.00 50.51 C ANISOU 1650 CB LEU A 218 6192 6555 6444 776 -184 141 C ATOM 1651 CG LEU A 218 60.733 26.412 13.637 1.00 52.80 C ANISOU 1651 CG LEU A 218 6370 6890 6802 691 -159 167 C ATOM 1652 CD1 LEU A 218 61.611 26.683 14.861 1.00 51.83 C ANISOU 1652 CD1 LEU A 218 6154 6810 6728 667 -221 134 C ATOM 1653 CD2 LEU A 218 61.555 26.384 12.367 1.00 48.12 C ANISOU 1653 CD2 LEU A 218 5713 6375 6195 715 -74 207 C ATOM 1654 N ASP A 219 58.317 22.591 13.352 1.00 44.94 N ANISOU 1654 N ASP A 219 5717 5727 5633 903 -207 102 N ATOM 1655 CA ASP A 219 57.743 21.405 13.984 1.00 52.98 C ANISOU 1655 CA ASP A 219 6819 6671 6640 952 -245 86 C ATOM 1656 C ASP A 219 56.224 21.294 13.808 1.00 50.10 C ANISOU 1656 C ASP A 219 6544 6222 6270 894 -270 94 C ATOM 1657 O ASP A 219 55.484 21.264 14.792 1.00 47.56 O ANISOU 1657 O ASP A 219 6245 5854 5972 870 -302 114 O ATOM 1658 CB ASP A 219 58.084 21.347 15.468 1.00 58.86 C ANISOU 1658 CB ASP A 219 7528 7426 7409 973 -289 97 C ATOM 1659 CG ASP A 219 59.551 21.256 15.727 1.00 76.32 C ANISOU 1659 CG ASP A 219 9639 9728 9632 1037 -286 95 C ATOM 1660 OD1 ASP A 219 60.200 20.368 15.137 1.00 89.64 O ANISOU 1660 OD1 ASP A 219 11324 11425 11308 1130 -251 85 O ATOM 1661 OD2 ASP A 219 60.054 22.083 16.520 1.00 79.50 O ANISOU 1661 OD2 ASP A 219 9960 10191 10056 995 -320 99 O ATOM 1662 N PRO A 220 55.728 21.237 12.578 1.00 51.04 N ANISOU 1662 N PRO A 220 6709 6334 6352 871 -257 84 N ATOM 1663 CA PRO A 220 54.278 21.223 12.402 1.00 49.70 C ANISOU 1663 CA PRO A 220 6596 6102 6186 806 -295 101 C ATOM 1664 C PRO A 220 53.679 19.876 12.785 1.00 50.07 C ANISOU 1664 C PRO A 220 6725 6057 6245 825 -330 79 C ATOM 1665 O PRO A 220 54.369 18.867 12.940 1.00 55.02 O ANISOU 1665 O PRO A 220 7385 6653 6865 900 -319 45 O ATOM 1666 CB PRO A 220 54.099 21.504 10.910 1.00 47.86 C ANISOU 1666 CB PRO A 220 6384 5910 5891 782 -284 95 C ATOM 1667 CG PRO A 220 55.321 20.912 10.300 1.00 56.17 C ANISOU 1667 CG PRO A 220 7445 7008 6891 863 -234 46 C ATOM 1668 CD PRO A 220 56.431 21.217 11.283 1.00 53.35 C ANISOU 1668 CD PRO A 220 6997 6687 6587 903 -207 61 C ATOM 1669 N ALA A 221 52.356 19.906 12.959 1.00 52.67 N ANISOU 1669 N ALA A 221 7074 6335 6603 756 -367 110 N ATOM 1670 CA ALA A 221 51.470 18.743 13.001 1.00 45.11 C ANISOU 1670 CA ALA A 221 6190 5282 5670 731 -406 100 C ATOM 1671 C ALA A 221 50.310 19.003 12.032 1.00 46.64 C ANISOU 1671 C ALA A 221 6390 5477 5852 646 -452 106 C ATOM 1672 O ALA A 221 49.157 19.105 12.440 1.00 42.84 O ANISOU 1672 O ALA A 221 5886 4967 5427 583 -481 158 O ATOM 1673 CB ALA A 221 50.957 18.514 14.423 1.00 38.78 C ANISOU 1673 CB ALA A 221 5377 4430 4928 725 -405 157 C ATOM 1674 N CYS A 222 50.642 19.155 10.746 1.00 44.46 N ANISOU 1674 N CYS A 222 6138 5254 5498 650 -457 63 N ATOM 1675 CA CYS A 222 49.757 19.753 9.744 1.00 47.71 C ANISOU 1675 CA CYS A 222 6538 5716 5874 581 -504 86 C ATOM 1676 C CYS A 222 48.545 18.903 9.421 1.00 50.97 C ANISOU 1676 C CYS A 222 6996 6067 6304 504 -588 67 C ATOM 1677 O CYS A 222 48.569 17.673 9.520 1.00 47.58 O ANISOU 1677 O CYS A 222 6644 5545 5888 505 -608 2 O ATOM 1678 CB CYS A 222 50.477 19.978 8.416 1.00 51.16 C ANISOU 1678 CB CYS A 222 7007 6236 6195 612 -485 45 C ATOM 1679 SG CYS A 222 51.729 21.247 8.422 1.00 56.08 S ANISOU 1679 SG CYS A 222 7549 6954 6803 665 -392 93 S ATOM 1680 N TYR A 223 47.493 19.589 8.982 1.00 45.69 N ANISOU 1680 N TYR A 223 6272 5446 5642 436 -642 128 N ATOM 1681 CA TYR A 223 46.367 18.980 8.288 1.00 48.70 C ANISOU 1681 CA TYR A 223 6677 5811 6016 347 -746 108 C ATOM 1682 C TYR A 223 45.482 20.095 7.765 1.00 43.33 C ANISOU 1682 C TYR A 223 5907 5225 5332 306 -791 202 C ATOM 1683 O TYR A 223 45.711 21.276 8.040 1.00 49.08 O ANISOU 1683 O TYR A 223 6566 6002 6079 348 -731 281 O ATOM 1684 CB TYR A 223 45.576 18.015 9.178 1.00 46.39 C ANISOU 1684 CB TYR A 223 6385 5404 5838 289 -775 115 C ATOM 1685 CG TYR A 223 44.861 18.637 10.336 1.00 48.92 C ANISOU 1685 CG TYR A 223 6596 5721 6270 275 -738 228 C ATOM 1686 CD1 TYR A 223 45.549 19.012 11.485 1.00 47.42 C ANISOU 1686 CD1 TYR A 223 6388 5519 6111 350 -644 259 C ATOM 1687 CD2 TYR A 223 43.482 18.822 10.302 1.00 48.03 C ANISOU 1687 CD2 TYR A 223 6396 5624 6228 191 -799 302 C ATOM 1688 CE1 TYR A 223 44.873 19.558 12.585 1.00 49.80 C ANISOU 1688 CE1 TYR A 223 6606 5819 6495 346 -601 349 C ATOM 1689 CE2 TYR A 223 42.800 19.369 11.385 1.00 40.94 C ANISOU 1689 CE2 TYR A 223 5398 4726 5432 193 -746 405 C ATOM 1690 CZ TYR A 223 43.494 19.734 12.527 1.00 48.12 C ANISOU 1690 CZ TYR A 223 6311 5619 6355 273 -641 423 C ATOM 1691 OH TYR A 223 42.807 20.265 13.608 1.00 48.09 O ANISOU 1691 OH TYR A 223 6223 5618 6430 283 -579 511 O ATOM 1692 N TYR A 224 44.472 19.704 6.995 1.00 43.22 N ANISOU 1692 N TYR A 224 5893 5231 5296 222 -904 194 N ATOM 1693 CA TYR A 224 43.500 20.630 6.434 1.00 43.48 C ANISOU 1693 CA TYR A 224 5832 5361 5329 184 -969 296 C ATOM 1694 C TYR A 224 42.270 20.656 7.336 1.00 48.88 C ANISOU 1694 C TYR A 224 6401 6005 6168 127 -992 384 C ATOM 1695 O TYR A 224 41.588 19.636 7.498 1.00 52.22 O ANISOU 1695 O TYR A 224 6829 6365 6648 43 -1059 350 O ATOM 1696 CB TYR A 224 43.132 20.222 5.007 1.00 42.52 C ANISOU 1696 CB TYR A 224 5767 5313 5074 126 -1095 239 C ATOM 1697 CG TYR A 224 44.289 20.372 4.055 1.00 45.07 C ANISOU 1697 CG TYR A 224 6193 5704 5227 195 -1052 173 C ATOM 1698 CD1 TYR A 224 44.550 21.598 3.424 1.00 47.45 C ANISOU 1698 CD1 TYR A 224 6455 6122 5453 245 -1020 270 C ATOM 1699 CD2 TYR A 224 45.125 19.310 3.781 1.00 50.56 C ANISOU 1699 CD2 TYR A 224 7021 6345 5844 219 -1030 26 C ATOM 1700 CE1 TYR A 224 45.630 21.756 2.561 1.00 44.65 C ANISOU 1700 CE1 TYR A 224 6184 5840 4943 308 -961 228 C ATOM 1701 CE2 TYR A 224 46.217 19.461 2.918 1.00 58.49 C ANISOU 1701 CE2 TYR A 224 8108 7424 6690 296 -967 -29 C ATOM 1702 CZ TYR A 224 46.461 20.680 2.317 1.00 52.65 C ANISOU 1702 CZ TYR A 224 7320 6813 5873 335 -931 76 C ATOM 1703 OH TYR A 224 47.537 20.811 1.472 1.00 49.43 O ANISOU 1703 OH TYR A 224 6984 6485 5310 408 -855 37 O ATOM 1704 N GLY A 225 41.979 21.818 7.903 1.00 45.56 N ANISOU 1704 N GLY A 225 5877 5614 5820 173 -930 498 N ATOM 1705 CA GLY A 225 40.917 21.896 8.876 1.00 47.43 C ANISOU 1705 CA GLY A 225 6003 5817 6202 145 -915 583 C ATOM 1706 C GLY A 225 40.329 23.285 8.972 1.00 49.85 C ANISOU 1706 C GLY A 225 6191 6183 6567 194 -881 710 C ATOM 1707 O GLY A 225 40.594 24.157 8.142 1.00 51.26 O ANISOU 1707 O GLY A 225 6370 6428 6678 232 -894 748 O ATOM 1708 N HIS A 226 39.512 23.471 10.001 1.00 43.20 N ANISOU 1708 N HIS A 226 5251 5311 5854 199 -829 784 N ATOM 1709 CA HIS A 226 38.957 24.781 10.294 1.00 41.03 C ANISOU 1709 CA HIS A 226 4869 5066 5656 267 -769 897 C ATOM 1710 C HIS A 226 40.071 25.726 10.711 1.00 45.31 C ANISOU 1710 C HIS A 226 5476 5572 6168 358 -658 870 C ATOM 1711 O HIS A 226 40.851 25.408 11.619 1.00 46.18 O ANISOU 1711 O HIS A 226 5656 5623 6268 379 -582 797 O ATOM 1712 CB HIS A 226 37.924 24.675 11.414 1.00 43.46 C ANISOU 1712 CB HIS A 226 5067 5346 6100 264 -711 967 C ATOM 1713 CG HIS A 226 37.067 25.892 11.562 1.00 41.95 C ANISOU 1713 CG HIS A 226 4745 5190 6003 335 -664 1090 C ATOM 1714 ND1 HIS A 226 36.234 26.083 12.643 1.00 45.61 N ANISOU 1714 ND1 HIS A 226 5108 5637 6585 370 -569 1157 N ATOM 1715 CD2 HIS A 226 36.884 26.962 10.747 1.00 41.12 C ANISOU 1715 CD2 HIS A 226 4593 5135 5896 387 -694 1168 C ATOM 1716 CE1 HIS A 226 35.588 27.231 12.499 1.00 43.64 C ANISOU 1716 CE1 HIS A 226 4754 5417 6408 449 -538 1261 C ATOM 1717 NE2 HIS A 226 35.973 27.786 11.362 1.00 45.03 N ANISOU 1717 NE2 HIS A 226 4962 5628 6518 460 -616 1274 N ATOM 1718 N ASN A 227 40.148 26.894 10.057 1.00 45.18 N ANISOU 1718 N ASN A 227 5435 5590 6141 408 -652 937 N ATOM 1719 CA ASN A 227 41.249 27.807 10.367 1.00 43.54 C ANISOU 1719 CA ASN A 227 5289 5338 5917 472 -555 909 C ATOM 1720 C ASN A 227 41.279 28.166 11.857 1.00 44.94 C ANISOU 1720 C ASN A 227 5458 5439 6179 520 -439 886 C ATOM 1721 O ASN A 227 42.361 28.304 12.436 1.00 46.10 O ANISOU 1721 O ASN A 227 5679 5543 6295 540 -378 807 O ATOM 1722 CB ASN A 227 41.168 29.063 9.495 1.00 40.43 C ANISOU 1722 CB ASN A 227 4861 4973 5528 515 -558 1011 C ATOM 1723 CG ASN A 227 39.979 29.957 9.849 1.00 47.21 C ANISOU 1723 CG ASN A 227 5603 5815 6519 570 -527 1131 C ATOM 1724 OD1 ASN A 227 38.870 29.487 10.052 1.00 53.30 O ANISOU 1724 OD1 ASN A 227 6284 6618 7350 551 -568 1175 O ATOM 1725 ND2 ASN A 227 40.221 31.248 9.928 1.00 46.67 N ANISOU 1725 ND2 ASN A 227 5533 5691 6509 640 -450 1186 N ATOM 1726 N GLU A 228 40.114 28.257 12.511 1.00 43.99 N ANISOU 1726 N GLU A 228 5245 5311 6158 537 -411 951 N ATOM 1727 CA GLU A 228 40.110 28.613 13.926 1.00 38.31 C ANISOU 1727 CA GLU A 228 4530 4531 5493 593 -292 924 C ATOM 1728 C GLU A 228 40.812 27.570 14.797 1.00 42.96 C ANISOU 1728 C GLU A 228 5201 5099 6021 564 -271 826 C ATOM 1729 O GLU A 228 41.205 27.891 15.921 1.00 45.11 O ANISOU 1729 O GLU A 228 5513 5334 6293 610 -182 778 O ATOM 1730 CB GLU A 228 38.669 28.805 14.427 1.00 46.95 C ANISOU 1730 CB GLU A 228 5500 5638 6701 624 -251 1021 C ATOM 1731 CG GLU A 228 37.829 29.930 13.775 1.00 45.87 C ANISOU 1731 CG GLU A 228 5259 5517 6651 683 -254 1141 C ATOM 1732 CD GLU A 228 36.356 29.921 14.267 1.00 51.66 C ANISOU 1732 CD GLU A 228 5842 6282 7505 716 -215 1245 C ATOM 1733 OE1 GLU A 228 36.031 29.138 15.180 1.00 50.29 O ANISOU 1733 OE1 GLU A 228 5654 6112 7344 691 -168 1223 O ATOM 1734 OE2 GLU A 228 35.516 30.686 13.738 1.00 59.54 O ANISOU 1734 OE2 GLU A 228 6728 7305 8588 770 -228 1362 O ATOM 1735 N ALA A 229 40.974 26.330 14.327 1.00 43.40 N ANISOU 1735 N ALA A 229 5289 5176 6024 495 -353 794 N ATOM 1736 CA ALA A 229 41.627 25.342 15.183 1.00 47.04 C ANISOU 1736 CA ALA A 229 5828 5606 6440 484 -329 721 C ATOM 1737 C ALA A 229 43.118 25.613 15.353 1.00 49.36 C ANISOU 1737 C ALA A 229 6213 5884 6656 519 -304 631 C ATOM 1738 O ALA A 229 43.724 25.055 16.269 1.00 44.89 O ANISOU 1738 O ALA A 229 5701 5299 6054 534 -271 581 O ATOM 1739 CB ALA A 229 41.414 23.919 14.650 1.00 35.39 C ANISOU 1739 CB ALA A 229 4373 4128 4947 404 -417 706 C ATOM 1740 N ASP A 230 43.707 26.487 14.566 1.00 46.19 N ANISOU 1740 N ASP A 230 5820 5497 6234 532 -314 623 N ATOM 1741 CA ASP A 230 45.097 26.787 14.732 1.00 42.84 C ANISOU 1741 CA ASP A 230 5457 5066 5756 553 -288 549 C ATOM 1742 C ASP A 230 45.397 27.642 15.941 1.00 46.43 C ANISOU 1742 C ASP A 230 5919 5485 6237 596 -210 517 C ATOM 1743 O ASP A 230 46.516 27.846 16.246 1.00 46.13 O ANISOU 1743 O ASP A 230 5919 5446 6161 603 -198 452 O ATOM 1744 CB ASP A 230 45.690 27.398 13.482 1.00 44.39 C ANISOU 1744 CB ASP A 230 5656 5289 5920 544 -314 560 C ATOM 1745 CG ASP A 230 46.868 26.623 12.948 1.00 55.35 C ANISOU 1745 CG ASP A 230 7102 6709 7221 534 -342 493 C ATOM 1746 OD1 ASP A 230 47.320 25.700 13.598 1.00 47.00 O ANISOU 1746 OD1 ASP A 230 6082 5639 6137 542 -343 435 O ATOM 1747 OD2 ASP A 230 47.343 26.938 11.872 1.00 47.19 O ANISOU 1747 OD2 ASP A 230 6074 5712 6143 527 -356 506 O ATOM 1748 N PHE A 231 44.395 28.141 16.623 1.00 41.84 N ANISOU 1748 N PHE A 231 5298 4881 5718 624 -156 559 N ATOM 1749 CA PHE A 231 44.591 28.906 17.848 1.00 42.89 C ANISOU 1749 CA PHE A 231 5457 4979 5860 670 -77 509 C ATOM 1750 C PHE A 231 44.467 28.044 19.105 1.00 45.64 C ANISOU 1750 C PHE A 231 5836 5345 6159 686 -46 483 C ATOM 1751 O PHE A 231 44.519 28.574 20.218 1.00 46.30 O ANISOU 1751 O PHE A 231 5950 5417 6225 728 21 437 O ATOM 1752 CB PHE A 231 43.589 30.065 17.929 1.00 47.89 C ANISOU 1752 CB PHE A 231 6039 5570 6587 715 -12 564 C ATOM 1753 CG PHE A 231 43.620 31.011 16.749 1.00 52.29 C ANISOU 1753 CG PHE A 231 6566 6100 7200 711 -34 618 C ATOM 1754 CD1 PHE A 231 44.805 31.357 16.142 1.00 53.35 C ANISOU 1754 CD1 PHE A 231 6740 6227 7303 678 -65 579 C ATOM 1755 CD2 PHE A 231 42.442 31.578 16.267 1.00 59.11 C ANISOU 1755 CD2 PHE A 231 7351 6954 8153 747 -20 724 C ATOM 1756 CE1 PHE A 231 44.829 32.245 15.061 1.00 49.07 C ANISOU 1756 CE1 PHE A 231 6174 5662 6809 675 -74 650 C ATOM 1757 CE2 PHE A 231 42.464 32.463 15.199 1.00 59.02 C ANISOU 1757 CE2 PHE A 231 7316 6920 8188 753 -40 794 C ATOM 1758 CZ PHE A 231 43.671 32.793 14.594 1.00 52.68 C ANISOU 1758 CZ PHE A 231 6568 6105 7344 715 -65 760 C ATOM 1759 N GLY A 232 44.327 26.727 18.953 1.00 48.31 N ANISOU 1759 N GLY A 232 6177 5709 6470 654 -91 510 N ATOM 1760 CA GLY A 232 44.143 25.838 20.089 1.00 40.48 C ANISOU 1760 CA GLY A 232 5213 4729 5438 669 -57 516 C ATOM 1761 C GLY A 232 45.323 25.721 21.040 1.00 42.17 C ANISOU 1761 C GLY A 232 5503 4961 5558 699 -52 438 C ATOM 1762 O GLY A 232 45.156 25.136 22.109 1.00 45.82 O ANISOU 1762 O GLY A 232 5995 5443 5973 725 -15 455 O ATOM 1763 N MET A 233 46.506 26.225 20.690 1.00 46.81 N ANISOU 1763 N MET A 233 6115 5554 6117 696 -91 365 N ATOM 1764 CA MET A 233 47.628 26.237 21.623 1.00 46.45 C ANISOU 1764 CA MET A 233 6120 5541 5989 720 -101 291 C ATOM 1765 C MET A 233 47.912 27.636 22.168 1.00 48.27 C ANISOU 1765 C MET A 233 6363 5758 6217 731 -66 216 C ATOM 1766 O MET A 233 48.975 27.860 22.755 1.00 43.36 O ANISOU 1766 O MET A 233 5772 5168 5535 731 -97 138 O ATOM 1767 CB MET A 233 48.895 25.667 20.967 1.00 50.64 C ANISOU 1767 CB MET A 233 6657 6094 6491 706 -173 259 C ATOM 1768 CG MET A 233 48.987 24.134 20.893 1.00 53.04 C ANISOU 1768 CG MET A 233 6985 6401 6768 718 -206 300 C ATOM 1769 SD MET A 233 49.017 23.372 22.539 1.00 54.04 S ANISOU 1769 SD MET A 233 7163 6560 6812 770 -184 323 S ATOM 1770 CE MET A 233 50.616 23.917 23.152 1.00 46.39 C ANISOU 1770 CE MET A 233 6201 5663 5763 797 -232 233 C ATOM 1771 N SER A 234 46.970 28.570 22.022 1.00 47.73 N ANISOU 1771 N SER A 234 6271 5642 6221 741 -6 236 N ATOM 1772 CA SER A 234 47.236 29.972 22.341 1.00 53.26 C ANISOU 1772 CA SER A 234 6993 6295 6948 747 28 158 C ATOM 1773 C SER A 234 47.527 30.193 23.820 1.00 53.21 C ANISOU 1773 C SER A 234 7056 6314 6845 779 57 65 C ATOM 1774 O SER A 234 48.167 31.190 24.175 1.00 52.45 O ANISOU 1774 O SER A 234 6997 6184 6747 764 53 -37 O ATOM 1775 CB SER A 234 46.048 30.854 21.933 1.00 54.62 C ANISOU 1775 CB SER A 234 7127 6400 7227 775 99 213 C ATOM 1776 OG SER A 234 44.901 30.576 22.737 1.00 52.54 O ANISOU 1776 OG SER A 234 6857 6154 6953 831 177 254 O ATOM 1777 N TRP A 235 47.078 29.286 24.689 1.00 43.14 N ANISOU 1777 N TRP A 235 5805 5099 5487 819 85 99 N ATOM 1778 CA TRP A 235 47.345 29.435 26.113 1.00 44.18 C ANISOU 1778 CA TRP A 235 6013 5280 5495 857 110 18 C ATOM 1779 C TRP A 235 48.832 29.354 26.460 1.00 51.29 C ANISOU 1779 C TRP A 235 6946 6233 6309 824 9 -72 C ATOM 1780 O TRP A 235 49.195 29.656 27.598 1.00 57.84 O ANISOU 1780 O TRP A 235 7843 7110 7025 844 6 -161 O ATOM 1781 CB TRP A 235 46.571 28.368 26.892 1.00 43.85 C ANISOU 1781 CB TRP A 235 5984 5301 5377 905 165 106 C ATOM 1782 CG TRP A 235 46.886 26.967 26.478 1.00 55.69 C ANISOU 1782 CG TRP A 235 7458 6832 6869 881 99 195 C ATOM 1783 CD1 TRP A 235 46.248 26.236 25.514 1.00 64.08 C ANISOU 1783 CD1 TRP A 235 8460 7859 8029 852 93 297 C ATOM 1784 CD2 TRP A 235 47.906 26.111 27.021 1.00 53.87 C ANISOU 1784 CD2 TRP A 235 7269 6669 6532 890 27 188 C ATOM 1785 NE1 TRP A 235 46.814 24.983 25.418 1.00 62.16 N ANISOU 1785 NE1 TRP A 235 8230 7637 7751 841 30 341 N ATOM 1786 CE2 TRP A 235 47.828 24.881 26.337 1.00 57.98 C ANISOU 1786 CE2 TRP A 235 7758 7171 7102 873 -7 286 C ATOM 1787 CE3 TRP A 235 48.873 26.267 28.017 1.00 54.56 C ANISOU 1787 CE3 TRP A 235 7414 6832 6486 912 -20 108 C ATOM 1788 CZ2 TRP A 235 48.686 23.817 26.614 1.00 64.19 C ANISOU 1788 CZ2 TRP A 235 8571 7996 7822 892 -71 315 C ATOM 1789 CZ3 TRP A 235 49.726 25.211 28.290 1.00 57.96 C ANISOU 1789 CZ3 TRP A 235 7855 7323 6843 930 -95 148 C ATOM 1790 CH2 TRP A 235 49.629 24.005 27.590 1.00 63.41 C ANISOU 1790 CH2 TRP A 235 8515 7979 7599 927 -113 254 C ATOM 1791 N CYS A 236 49.695 28.938 25.521 1.00 47.51 N ANISOU 1791 N CYS A 236 6417 5760 5874 778 -74 -49 N ATOM 1792 CA CYS A 236 51.142 28.956 25.694 1.00 46.72 C ANISOU 1792 CA CYS A 236 6313 5714 5724 744 -170 -123 C ATOM 1793 C CYS A 236 51.815 29.644 24.519 1.00 48.38 C ANISOU 1793 C CYS A 236 6462 5873 6046 679 -203 -141 C ATOM 1794 O CYS A 236 52.927 29.275 24.130 1.00 48.87 O ANISOU 1794 O CYS A 236 6479 5984 6106 652 -274 -145 O ATOM 1795 CB CYS A 236 51.707 27.539 25.854 1.00 44.20 C ANISOU 1795 CB CYS A 236 5984 5477 5332 775 -229 -59 C ATOM 1796 SG CYS A 236 53.378 27.549 26.613 1.00 63.90 S ANISOU 1796 SG CYS A 236 8471 8080 7728 763 -346 -146 S ATOM 1797 N ALA A 237 51.156 30.627 23.922 1.00 46.62 N ANISOU 1797 N ALA A 237 6233 5555 5926 660 -145 -138 N ATOM 1798 CA ALA A 237 51.669 31.229 22.706 1.00 45.29 C ANISOU 1798 CA ALA A 237 6009 5337 5863 602 -162 -120 C ATOM 1799 C ALA A 237 52.024 32.697 22.846 1.00 54.14 C ANISOU 1799 C ALA A 237 7145 6373 7054 549 -150 -207 C ATOM 1800 O ALA A 237 52.825 33.190 22.048 1.00 54.14 O ANISOU 1800 O ALA A 237 7095 6348 7128 485 -176 -202 O ATOM 1801 CB ALA A 237 50.657 31.080 21.558 1.00 40.75 C ANISOU 1801 CB ALA A 237 5401 4717 5365 618 -117 -8 C ATOM 1802 N GLY A 238 51.474 33.404 23.827 1.00 59.83 N ANISOU 1802 N GLY A 238 7936 7042 7756 574 -104 -288 N ATOM 1803 CA GLY A 238 51.714 34.832 23.897 1.00 69.54 C ANISOU 1803 CA GLY A 238 9195 8154 9074 524 -85 -377 C ATOM 1804 C GLY A 238 51.282 35.604 22.661 1.00 69.70 C ANISOU 1804 C GLY A 238 9177 8059 9249 508 -33 -288 C ATOM 1805 O GLY A 238 52.056 36.406 22.131 1.00 67.81 O ANISOU 1805 O GLY A 238 8913 7752 9101 429 -54 -305 O ATOM 1806 N PHE A 239 50.078 35.349 22.157 1.00 66.79 N ANISOU 1806 N PHE A 239 8791 7674 8911 579 30 -178 N ATOM 1807 CA PHE A 239 49.565 36.110 21.023 1.00 63.86 C ANISOU 1807 CA PHE A 239 8384 7205 8675 580 74 -78 C ATOM 1808 C PHE A 239 49.101 37.475 21.517 1.00 65.80 C ANISOU 1808 C PHE A 239 8691 7295 9016 604 149 -144 C ATOM 1809 O PHE A 239 48.158 37.553 22.312 1.00 70.28 O ANISOU 1809 O PHE A 239 9301 7842 9559 688 218 -176 O ATOM 1810 CB PHE A 239 48.397 35.380 20.355 1.00 58.89 C ANISOU 1810 CB PHE A 239 7705 6622 8047 644 98 60 C ATOM 1811 CG PHE A 239 48.781 34.123 19.613 1.00 54.54 C ANISOU 1811 CG PHE A 239 7106 6190 7428 618 29 127 C ATOM 1812 CD1 PHE A 239 49.999 34.018 18.956 1.00 50.25 C ANISOU 1812 CD1 PHE A 239 6537 5682 6875 552 -26 121 C ATOM 1813 CD2 PHE A 239 47.897 33.041 19.559 1.00 58.50 C ANISOU 1813 CD2 PHE A 239 7584 6760 7881 661 26 195 C ATOM 1814 CE1 PHE A 239 50.351 32.834 18.266 1.00 50.67 C ANISOU 1814 CE1 PHE A 239 6555 5836 6860 545 -77 170 C ATOM 1815 CE2 PHE A 239 48.226 31.868 18.868 1.00 54.77 C ANISOU 1815 CE2 PHE A 239 7084 6373 7352 638 -37 240 C ATOM 1816 CZ PHE A 239 49.454 31.763 18.221 1.00 52.58 C ANISOU 1816 CZ PHE A 239 6795 6128 7054 588 -84 222 C ATOM 1817 N GLY A 240 49.707 38.551 21.002 1.00 67.90 N ANISOU 1817 N GLY A 240 8960 7441 9397 538 150 -155 N ATOM 1818 CA GLY A 240 49.297 39.892 21.364 1.00 75.58 C ANISOU 1818 CA GLY A 240 10000 8231 10485 561 225 -216 C ATOM 1819 C GLY A 240 48.037 40.332 20.631 1.00 79.69 C ANISOU 1819 C GLY A 240 10492 8671 11115 658 308 -71 C ATOM 1820 O GLY A 240 47.473 39.620 19.800 1.00 78.03 O ANISOU 1820 O GLY A 240 10206 8556 10888 693 295 75 O ATOM 1821 N GLU A 241 47.560 41.528 20.985 1.00 76.22 N ANISOU 1821 N GLU A 241 10117 8051 10791 706 392 -119 N ATOM 1822 CA GLU A 241 46.400 42.063 20.278 1.00 71.62 C ANISOU 1822 CA GLU A 241 9497 7383 10333 810 470 31 C ATOM 1823 C GLU A 241 46.752 42.412 18.838 1.00 64.04 C ANISOU 1823 C GLU A 241 8474 6388 9470 756 437 196 C ATOM 1824 O GLU A 241 45.901 42.322 17.950 1.00 61.16 O ANISOU 1824 O GLU A 241 8037 6052 9147 826 451 369 O ATOM 1825 CB GLU A 241 45.839 43.289 20.992 1.00 82.71 C ANISOU 1825 CB GLU A 241 10992 8584 11851 892 580 -59 C ATOM 1826 CG GLU A 241 44.484 43.710 20.452 1.00 95.15 C ANISOU 1826 CG GLU A 241 12512 10096 13546 1036 670 101 C ATOM 1827 CD GLU A 241 44.087 45.101 20.885 1.00111.12 C ANISOU 1827 CD GLU A 241 14625 11872 15724 1119 784 34 C ATOM 1828 OE1 GLU A 241 44.784 46.064 20.493 1.00117.72 O ANISOU 1828 OE1 GLU A 241 15513 12531 16685 1046 779 22 O ATOM 1829 OE2 GLU A 241 43.089 45.232 21.627 1.00115.99 O ANISOU 1829 OE2 GLU A 241 15261 12466 16343 1257 888 -6 O ATOM 1830 N SER A 242 47.999 42.802 18.588 1.00 56.43 N ANISOU 1830 N SER A 242 7528 5376 8537 630 392 152 N ATOM 1831 CA SER A 242 48.421 43.043 17.224 1.00 61.95 C ANISOU 1831 CA SER A 242 8166 6069 9303 575 370 317 C ATOM 1832 C SER A 242 48.444 41.757 16.400 1.00 62.19 C ANISOU 1832 C SER A 242 8110 6320 9200 569 301 426 C ATOM 1833 O SER A 242 48.402 41.823 15.166 1.00 67.58 O ANISOU 1833 O SER A 242 8741 7031 9905 565 293 591 O ATOM 1834 CB SER A 242 49.789 43.724 17.218 1.00 67.51 C ANISOU 1834 CB SER A 242 8895 6679 10077 431 348 245 C ATOM 1835 OG SER A 242 50.735 42.900 17.860 1.00 84.43 O ANISOU 1835 OG SER A 242 11028 8960 12091 349 270 109 O ATOM 1836 N PHE A 243 48.562 40.598 17.043 1.00 58.33 N ANISOU 1836 N PHE A 243 7615 5982 8566 567 252 335 N ATOM 1837 CA PHE A 243 48.472 39.345 16.306 1.00 53.70 C ANISOU 1837 CA PHE A 243 6963 5578 7863 572 192 423 C ATOM 1838 C PHE A 243 47.079 39.177 15.708 1.00 50.07 C ANISOU 1838 C PHE A 243 6458 5144 7421 669 210 564 C ATOM 1839 O PHE A 243 46.920 39.025 14.493 1.00 51.19 O ANISOU 1839 O PHE A 243 6551 5345 7555 667 180 705 O ATOM 1840 CB PHE A 243 48.826 38.166 17.221 1.00 50.02 C ANISOU 1840 CB PHE A 243 6509 5239 7259 559 144 302 C ATOM 1841 CG PHE A 243 48.572 36.823 16.598 1.00 46.90 C ANISOU 1841 CG PHE A 243 6063 5000 6756 575 90 376 C ATOM 1842 CD1 PHE A 243 49.507 36.256 15.733 1.00 48.53 C ANISOU 1842 CD1 PHE A 243 6237 5297 6905 516 39 409 C ATOM 1843 CD2 PHE A 243 47.411 36.124 16.872 1.00 44.93 C ANISOU 1843 CD2 PHE A 243 5799 4802 6469 645 96 408 C ATOM 1844 CE1 PHE A 243 49.275 35.033 15.139 1.00 43.20 C ANISOU 1844 CE1 PHE A 243 5535 4746 6133 532 -8 458 C ATOM 1845 CE2 PHE A 243 47.169 34.894 16.280 1.00 49.61 C ANISOU 1845 CE2 PHE A 243 6354 5517 6978 643 40 466 C ATOM 1846 CZ PHE A 243 48.111 34.342 15.415 1.00 49.94 C ANISOU 1846 CZ PHE A 243 6384 5635 6958 588 -15 481 C ATOM 1847 N TYR A 244 46.054 39.240 16.550 1.00 50.88 N ANISOU 1847 N TYR A 244 6573 5213 7547 755 259 530 N ATOM 1848 CA TYR A 244 44.691 39.027 16.083 1.00 54.47 C ANISOU 1848 CA TYR A 244 6960 5709 8029 845 271 665 C ATOM 1849 C TYR A 244 44.215 40.149 15.159 1.00 57.01 C ANISOU 1849 C TYR A 244 7254 5924 8485 893 305 815 C ATOM 1850 O TYR A 244 43.419 39.900 14.248 1.00 55.40 O ANISOU 1850 O TYR A 244 6973 5796 8282 935 269 968 O ATOM 1851 CB TYR A 244 43.763 38.883 17.282 1.00 49.44 C ANISOU 1851 CB TYR A 244 6330 5062 7393 930 337 596 C ATOM 1852 CG TYR A 244 43.921 37.582 18.038 1.00 52.03 C ANISOU 1852 CG TYR A 244 6665 5522 7580 900 301 509 C ATOM 1853 CD1 TYR A 244 43.453 36.377 17.503 1.00 49.71 C ANISOU 1853 CD1 TYR A 244 6302 5368 7219 886 236 593 C ATOM 1854 CD2 TYR A 244 44.546 37.549 19.286 1.00 56.34 C ANISOU 1854 CD2 TYR A 244 7294 6052 8060 883 325 346 C ATOM 1855 CE1 TYR A 244 43.599 35.173 18.187 1.00 51.79 C ANISOU 1855 CE1 TYR A 244 6578 5730 7370 860 208 528 C ATOM 1856 CE2 TYR A 244 44.689 36.343 19.993 1.00 59.23 C ANISOU 1856 CE2 TYR A 244 7669 6541 8295 866 293 290 C ATOM 1857 CZ TYR A 244 44.220 35.161 19.437 1.00 61.62 C ANISOU 1857 CZ TYR A 244 7903 6961 8551 856 241 387 C ATOM 1858 OH TYR A 244 44.352 33.969 20.130 1.00 55.90 O ANISOU 1858 OH TYR A 244 7192 6333 7714 841 216 346 O ATOM 1859 N ASN A 245 44.694 41.380 15.352 1.00 61.71 N ANISOU 1859 N ASN A 245 7910 6341 9195 886 365 780 N ATOM 1860 CA ASN A 245 44.270 42.471 14.479 1.00 63.88 C ANISOU 1860 CA ASN A 245 8166 6495 9609 939 404 941 C ATOM 1861 C ASN A 245 44.781 42.271 13.061 1.00 61.58 C ANISOU 1861 C ASN A 245 7833 6296 9270 875 336 1091 C ATOM 1862 O ASN A 245 44.079 42.585 12.090 1.00 64.21 O ANISOU 1862 O ASN A 245 8111 6641 9643 937 326 1277 O ATOM 1863 CB ASN A 245 44.746 43.814 15.034 1.00 71.80 C ANISOU 1863 CB ASN A 245 9260 7261 10759 931 487 859 C ATOM 1864 CG ASN A 245 43.919 44.282 16.217 1.00 84.28 C ANISOU 1864 CG ASN A 245 10888 8727 12409 1041 580 750 C ATOM 1865 OD1 ASN A 245 42.739 43.943 16.342 1.00 86.41 O ANISOU 1865 OD1 ASN A 245 11093 9063 12674 1156 606 815 O ATOM 1866 ND2 ASN A 245 44.533 45.065 17.092 1.00 95.76 N ANISOU 1866 ND2 ASN A 245 12450 10011 13925 1004 631 581 N ATOM 1867 N ALA A 246 46.002 41.753 12.923 1.00 57.24 N ANISOU 1867 N ALA A 246 7303 5820 8626 759 290 1017 N ATOM 1868 CA ALA A 246 46.566 41.513 11.607 1.00 47.91 C ANISOU 1868 CA ALA A 246 6088 4739 7376 703 242 1146 C ATOM 1869 C ALA A 246 45.947 40.280 10.964 1.00 54.48 C ANISOU 1869 C ALA A 246 6863 5775 8062 729 160 1206 C ATOM 1870 O ALA A 246 45.724 40.260 9.747 1.00 56.96 O ANISOU 1870 O ALA A 246 7143 6168 8332 741 124 1362 O ATOM 1871 CB ALA A 246 48.082 41.354 11.724 1.00 38.46 C ANISOU 1871 CB ALA A 246 4917 3560 6136 581 234 1043 C ATOM 1872 N TYR A 247 45.668 39.251 11.775 1.00 50.29 N ANISOU 1872 N TYR A 247 6328 5326 7453 735 129 1084 N ATOM 1873 CA TYR A 247 45.040 38.031 11.276 1.00 45.06 C ANISOU 1873 CA TYR A 247 5617 4832 6671 745 48 1122 C ATOM 1874 C TYR A 247 43.681 38.329 10.642 1.00 48.58 C ANISOU 1874 C TYR A 247 5994 5296 7168 827 28 1284 C ATOM 1875 O TYR A 247 43.424 37.959 9.489 1.00 51.74 O ANISOU 1875 O TYR A 247 6357 5812 7489 820 -46 1397 O ATOM 1876 CB TYR A 247 44.900 36.999 12.409 1.00 36.54 C ANISOU 1876 CB TYR A 247 4548 3801 5533 740 36 977 C ATOM 1877 CG TYR A 247 44.400 35.687 11.873 1.00 47.57 C ANISOU 1877 CG TYR A 247 5906 5349 6820 726 -50 1004 C ATOM 1878 CD1 TYR A 247 43.032 35.450 11.707 1.00 47.61 C ANISOU 1878 CD1 TYR A 247 5839 5397 6854 776 -80 1093 C ATOM 1879 CD2 TYR A 247 45.299 34.694 11.471 1.00 44.69 C ANISOU 1879 CD2 TYR A 247 5571 5079 6330 662 -104 944 C ATOM 1880 CE1 TYR A 247 42.565 34.246 11.165 1.00 48.48 C ANISOU 1880 CE1 TYR A 247 5913 5634 6871 743 -174 1111 C ATOM 1881 CE2 TYR A 247 44.842 33.484 10.935 1.00 42.37 C ANISOU 1881 CE2 TYR A 247 5259 4900 5940 644 -186 954 C ATOM 1882 CZ TYR A 247 43.474 33.269 10.778 1.00 47.64 C ANISOU 1882 CZ TYR A 247 5861 5602 6639 675 -227 1033 C ATOM 1883 OH TYR A 247 43.010 32.087 10.227 1.00 48.62 O ANISOU 1883 OH TYR A 247 5966 5828 6678 638 -320 1035 O ATOM 1884 N PHE A 248 42.793 38.991 11.383 1.00 41.38 N ANISOU 1884 N PHE A 248 5060 4281 6383 912 92 1295 N ATOM 1885 CA PHE A 248 41.438 39.206 10.882 1.00 45.93 C ANISOU 1885 CA PHE A 248 5542 4889 7019 1002 70 1453 C ATOM 1886 C PHE A 248 41.352 40.268 9.799 1.00 56.16 C ANISOU 1886 C PHE A 248 6823 6132 8383 1045 73 1637 C ATOM 1887 O PHE A 248 40.269 40.453 9.232 1.00 63.22 O ANISOU 1887 O PHE A 248 7629 7074 9318 1123 36 1793 O ATOM 1888 CB PHE A 248 40.502 39.444 12.055 1.00 44.09 C ANISOU 1888 CB PHE A 248 5277 4583 6892 1092 151 1407 C ATOM 1889 CG PHE A 248 40.248 38.180 12.837 1.00 47.16 C ANISOU 1889 CG PHE A 248 5647 5078 7193 1057 126 1295 C ATOM 1890 CD1 PHE A 248 39.735 37.055 12.188 1.00 54.01 C ANISOU 1890 CD1 PHE A 248 6442 6108 7972 1015 17 1352 C ATOM 1891 CD2 PHE A 248 40.613 38.063 14.167 1.00 49.68 C ANISOU 1891 CD2 PHE A 248 6033 5339 7504 1054 201 1132 C ATOM 1892 CE1 PHE A 248 39.522 35.850 12.875 1.00 50.69 C ANISOU 1892 CE1 PHE A 248 6009 5768 7485 972 -4 1263 C ATOM 1893 CE2 PHE A 248 40.390 36.864 14.861 1.00 52.42 C ANISOU 1893 CE2 PHE A 248 6366 5786 7767 1024 181 1055 C ATOM 1894 CZ PHE A 248 39.845 35.757 14.209 1.00 47.17 C ANISOU 1894 CZ PHE A 248 5623 5261 7038 981 83 1126 C ATOM 1895 N LYS A 249 42.452 40.965 9.496 1.00 54.48 N ANISOU 1895 N LYS A 249 6685 5827 8187 994 113 1637 N ATOM 1896 CA LYS A 249 42.497 41.780 8.281 1.00 50.90 C ANISOU 1896 CA LYS A 249 6222 5355 7762 1016 106 1836 C ATOM 1897 C LYS A 249 42.524 40.904 7.023 1.00 54.01 C ANISOU 1897 C LYS A 249 6584 5965 7973 973 -8 1927 C ATOM 1898 O LYS A 249 41.932 41.263 6.005 1.00 59.25 O ANISOU 1898 O LYS A 249 7202 6687 8624 1027 -54 2119 O ATOM 1899 CB LYS A 249 43.726 42.686 8.292 1.00 50.89 C ANISOU 1899 CB LYS A 249 6304 5202 7832 952 186 1815 C ATOM 1900 CG LYS A 249 43.608 43.995 9.041 1.00 54.95 C ANISOU 1900 CG LYS A 249 6860 5463 8556 1007 295 1803 C ATOM 1901 CD LYS A 249 44.966 44.730 9.062 1.00 58.67 C ANISOU 1901 CD LYS A 249 7408 5793 9090 901 355 1758 C ATOM 1902 CE LYS A 249 44.809 46.184 9.470 1.00 77.99 C ANISOU 1902 CE LYS A 249 9907 7962 11762 953 458 1791 C ATOM 1903 NZ LYS A 249 45.959 46.746 10.240 1.00 86.42 N ANISOU 1903 NZ LYS A 249 11058 8859 12917 840 514 1624 N ATOM 1904 N VAL A 250 43.202 39.752 7.071 1.00 55.96 N ANISOU 1904 N VAL A 250 6860 6333 8069 884 -57 1789 N ATOM 1905 CA VAL A 250 43.298 38.857 5.915 1.00 56.33 C ANISOU 1905 CA VAL A 250 6900 6576 7928 843 -159 1838 C ATOM 1906 C VAL A 250 42.107 37.903 5.830 1.00 54.41 C ANISOU 1906 C VAL A 250 6585 6463 7624 864 -267 1839 C ATOM 1907 O VAL A 250 41.631 37.604 4.733 1.00 52.81 O ANISOU 1907 O VAL A 250 6352 6402 7314 867 -367 1950 O ATOM 1908 CB VAL A 250 44.634 38.066 5.959 1.00 53.31 C ANISOU 1908 CB VAL A 250 6584 6249 7422 748 -150 1688 C ATOM 1909 CG1 VAL A 250 44.733 37.042 4.802 1.00 38.37 C ANISOU 1909 CG1 VAL A 250 4703 4554 5322 715 -246 1707 C ATOM 1910 CG2 VAL A 250 45.814 38.994 5.902 1.00 48.22 C ANISOU 1910 CG2 VAL A 250 5984 5498 6840 710 -54 1708 C ATOM 1911 N MET A 251 41.591 37.447 6.971 1.00 53.03 N ANISOU 1911 N MET A 251 6382 6249 7519 874 -252 1725 N ATOM 1912 CA MET A 251 40.558 36.419 7.062 1.00 60.07 C ANISOU 1912 CA MET A 251 7200 7253 8371 868 -344 1707 C ATOM 1913 C MET A 251 39.296 36.943 7.733 1.00 59.61 C ANISOU 1913 C MET A 251 7040 7136 8474 959 -309 1780 C ATOM 1914 O MET A 251 39.381 37.524 8.823 1.00 60.53 O ANISOU 1914 O MET A 251 7177 7112 8708 1005 -193 1714 O ATOM 1915 CB MET A 251 41.042 35.182 7.862 1.00 58.54 C ANISOU 1915 CB MET A 251 7052 7083 8107 794 -349 1515 C ATOM 1916 CG MET A 251 42.123 34.348 7.188 1.00 71.03 C ANISOU 1916 CG MET A 251 8717 8750 9523 715 -396 1433 C ATOM 1917 SD MET A 251 41.460 33.321 5.854 1.00 68.53 S ANISOU 1917 SD MET A 251 8374 8617 9047 671 -559 1483 S ATOM 1918 CE MET A 251 40.281 32.291 6.737 1.00 66.91 C ANISOU 1918 CE MET A 251 8090 8425 8909 646 -614 1421 C ATOM 1919 N PRO A 252 38.129 36.824 7.095 1.00 55.82 N ANISOU 1919 N PRO A 252 6446 6760 8003 995 -402 1916 N ATOM 1920 CA PRO A 252 36.885 37.269 7.748 1.00 58.65 C ANISOU 1920 CA PRO A 252 6682 7077 8525 1093 -360 1994 C ATOM 1921 C PRO A 252 36.497 36.331 8.884 1.00 58.62 C ANISOU 1921 C PRO A 252 6646 7084 8542 1059 -333 1861 C ATOM 1922 O PRO A 252 36.454 35.110 8.719 1.00 59.73 O ANISOU 1922 O PRO A 252 6780 7334 8580 962 -428 1794 O ATOM 1923 CB PRO A 252 35.846 37.239 6.614 1.00 57.38 C ANISOU 1923 CB PRO A 252 6394 7063 8344 1119 -498 2181 C ATOM 1924 CG PRO A 252 36.343 36.157 5.701 1.00 59.92 C ANISOU 1924 CG PRO A 252 6772 7534 8461 996 -636 2121 C ATOM 1925 CD PRO A 252 37.884 36.152 5.807 1.00 51.43 C ANISOU 1925 CD PRO A 252 5863 6381 7297 940 -559 1988 C ATOM 1926 N LYS A 253 36.174 36.929 10.027 1.00 56.21 N ANISOU 1926 N LYS A 253 6325 6660 8372 1145 -197 1831 N ATOM 1927 CA LYS A 253 35.767 36.204 11.221 1.00 48.17 C ANISOU 1927 CA LYS A 253 5278 5646 7380 1134 -139 1726 C ATOM 1928 C LYS A 253 34.345 35.671 11.052 1.00 54.38 C ANISOU 1928 C LYS A 253 5883 6555 8226 1148 -207 1842 C ATOM 1929 O LYS A 253 33.449 36.418 10.632 1.00 57.84 O ANISOU 1929 O LYS A 253 6199 7006 8772 1245 -212 2002 O ATOM 1930 CB LYS A 253 35.839 37.137 12.431 1.00 54.44 C ANISOU 1930 CB LYS A 253 6119 6281 8285 1236 35 1661 C ATOM 1931 CG LYS A 253 35.395 36.515 13.750 1.00 55.89 C ANISOU 1931 CG LYS A 253 6279 6473 8483 1246 121 1566 C ATOM 1932 CD LYS A 253 35.517 37.477 14.949 1.00 48.02 C ANISOU 1932 CD LYS A 253 5354 5324 7566 1352 295 1478 C ATOM 1933 CE LYS A 253 36.948 37.871 15.242 1.00 50.53 C ANISOU 1933 CE LYS A 253 5849 5532 7817 1301 322 1329 C ATOM 1934 NZ LYS A 253 36.994 38.821 16.378 1.00 48.53 N ANISOU 1934 NZ LYS A 253 5671 5129 7637 1397 476 1230 N ATOM 1935 N GLN A 254 34.134 34.380 11.347 1.00 56.28 N ANISOU 1935 N GLN A 254 6095 6882 8406 1047 -263 1773 N ATOM 1936 CA GLN A 254 32.829 33.750 11.179 1.00 51.64 C ANISOU 1936 CA GLN A 254 5325 6416 7881 1026 -341 1876 C ATOM 1937 C GLN A 254 32.078 33.658 12.496 1.00 54.30 C ANISOU 1937 C GLN A 254 5577 6724 8331 1084 -201 1867 C ATOM 1938 O GLN A 254 32.679 33.486 13.556 1.00 49.19 O ANISOU 1938 O GLN A 254 5041 5999 7652 1085 -86 1737 O ATOM 1939 CB GLN A 254 32.922 32.350 10.584 1.00 47.26 C ANISOU 1939 CB GLN A 254 4780 5970 7209 866 -499 1822 C ATOM 1940 CG GLN A 254 33.468 32.299 9.172 1.00 55.90 C ANISOU 1940 CG GLN A 254 5940 7131 8171 808 -649 1839 C ATOM 1941 CD GLN A 254 33.601 30.871 8.653 1.00 60.11 C ANISOU 1941 CD GLN A 254 6507 7750 8583 654 -794 1751 C ATOM 1942 OE1 GLN A 254 34.584 30.169 8.932 1.00 64.03 O ANISOU 1942 OE1 GLN A 254 7147 8197 8983 590 -772 1603 O ATOM 1943 NE2 GLN A 254 32.601 30.438 7.880 1.00 55.95 N ANISOU 1943 NE2 GLN A 254 5846 7349 8065 595 -949 1841 N ATOM 1944 N ALA A 255 30.744 33.705 12.392 1.00 52.66 N ANISOU 1944 N ALA A 255 5162 6600 8246 1129 -220 2014 N ATOM 1945 CA ALA A 255 29.854 33.659 13.549 1.00 53.21 C ANISOU 1945 CA ALA A 255 5114 6667 8435 1199 -76 2041 C ATOM 1946 C ALA A 255 30.117 32.444 14.429 1.00 56.78 C ANISOU 1946 C ALA A 255 5624 7129 8820 1087 -42 1922 C ATOM 1947 O ALA A 255 30.250 31.310 13.946 1.00 51.74 O ANISOU 1947 O ALA A 255 4994 6557 8108 935 -181 1891 O ATOM 1948 CB ALA A 255 28.382 33.659 13.093 1.00 47.37 C ANISOU 1948 CB ALA A 255 4109 6055 7835 1230 -141 2232 C ATOM 1949 N GLY A 256 30.126 32.690 15.737 1.00 58.41 N ANISOU 1949 N GLY A 256 5871 7268 9054 1172 147 1862 N ATOM 1950 CA GLY A 256 30.449 31.688 16.729 1.00 54.95 C ANISOU 1950 CA GLY A 256 5508 6827 8542 1095 208 1761 C ATOM 1951 C GLY A 256 31.924 31.534 17.011 1.00 54.88 C ANISOU 1951 C GLY A 256 5736 6735 8382 1051 209 1589 C ATOM 1952 O GLY A 256 32.309 30.572 17.683 1.00 55.26 O ANISOU 1952 O GLY A 256 5856 6789 8353 975 226 1513 O ATOM 1953 N TYR A 257 32.762 32.450 16.514 1.00 49.07 N ANISOU 1953 N TYR A 257 5113 5923 7610 1095 191 1538 N ATOM 1954 CA TYR A 257 34.201 32.340 16.723 1.00 47.24 C ANISOU 1954 CA TYR A 257 5080 5622 7246 1047 183 1384 C ATOM 1955 C TYR A 257 34.560 32.358 18.209 1.00 51.17 C ANISOU 1955 C TYR A 257 5675 6068 7700 1096 333 1272 C ATOM 1956 O TYR A 257 35.357 31.527 18.675 1.00 47.64 O ANISOU 1956 O TYR A 257 5333 5626 7140 1022 314 1173 O ATOM 1957 CB TYR A 257 34.933 33.458 15.977 1.00 48.67 C ANISOU 1957 CB TYR A 257 5340 5726 7425 1089 159 1372 C ATOM 1958 CG TYR A 257 36.301 33.720 16.551 1.00 50.54 C ANISOU 1958 CG TYR A 257 5758 5874 7571 1076 206 1214 C ATOM 1959 CD1 TYR A 257 37.365 32.872 16.270 1.00 52.62 C ANISOU 1959 CD1 TYR A 257 6119 6165 7710 967 116 1127 C ATOM 1960 CD2 TYR A 257 36.529 34.792 17.391 1.00 48.85 C ANISOU 1960 CD2 TYR A 257 5614 5549 7397 1173 338 1147 C ATOM 1961 CE1 TYR A 257 38.603 33.098 16.794 1.00 48.51 C ANISOU 1961 CE1 TYR A 257 5736 5580 7115 954 150 994 C ATOM 1962 CE2 TYR A 257 37.787 35.021 17.935 1.00 44.44 C ANISOU 1962 CE2 TYR A 257 5211 4919 6757 1144 363 996 C ATOM 1963 CZ TYR A 257 38.816 34.172 17.625 1.00 48.44 C ANISOU 1963 CZ TYR A 257 5788 5471 7147 1034 265 929 C ATOM 1964 OH TYR A 257 40.068 34.385 18.147 1.00 52.64 O ANISOU 1964 OH TYR A 257 6447 5948 7605 1004 278 792 O ATOM 1965 N GLU A 258 34.003 33.314 18.968 1.00 50.06 N ANISOU 1965 N GLU A 258 5507 5878 7637 1230 485 1283 N ATOM 1966 CA GLU A 258 34.304 33.389 20.400 1.00 54.49 C ANISOU 1966 CA GLU A 258 6171 6402 8131 1285 630 1168 C ATOM 1967 C GLU A 258 33.788 32.169 21.134 1.00 55.63 C ANISOU 1967 C GLU A 258 6261 6642 8235 1236 664 1200 C ATOM 1968 O GLU A 258 34.453 31.645 22.037 1.00 52.86 O ANISOU 1968 O GLU A 258 6028 6293 7762 1210 702 1102 O ATOM 1969 CB GLU A 258 33.708 34.648 21.019 1.00 57.17 C ANISOU 1969 CB GLU A 258 6494 6667 8561 1449 795 1168 C ATOM 1970 CG GLU A 258 34.572 35.876 20.840 1.00 75.48 C ANISOU 1970 CG GLU A 258 8946 8844 10888 1495 806 1071 C ATOM 1971 CD GLU A 258 35.895 35.784 21.593 1.00 87.48 C ANISOU 1971 CD GLU A 258 10659 10317 12261 1439 806 883 C ATOM 1972 OE1 GLU A 258 36.017 34.945 22.531 1.00 77.62 O ANISOU 1972 OE1 GLU A 258 9452 9140 10901 1410 841 824 O ATOM 1973 OE2 GLU A 258 36.809 36.577 21.250 1.00 95.66 O ANISOU 1973 OE2 GLU A 258 11799 11248 13300 1422 770 805 O ATOM 1974 N LYS A 259 32.610 31.701 20.737 1.00 50.65 N ANISOU 1974 N LYS A 259 5444 6092 7709 1218 644 1349 N ATOM 1975 CA LYS A 259 31.971 30.568 21.382 1.00 52.64 C ANISOU 1975 CA LYS A 259 5616 6427 7958 1162 685 1410 C ATOM 1976 C LYS A 259 32.772 29.274 21.211 1.00 52.69 C ANISOU 1976 C LYS A 259 5716 6446 7859 1011 561 1357 C ATOM 1977 O LYS A 259 32.746 28.412 22.090 1.00 56.65 O ANISOU 1977 O LYS A 259 6243 6975 8306 977 622 1357 O ATOM 1978 CB LYS A 259 30.552 30.438 20.809 1.00 53.04 C ANISOU 1978 CB LYS A 259 5424 6560 8171 1158 664 1588 C ATOM 1979 CG LYS A 259 29.817 29.151 21.110 1.00 64.02 C ANISOU 1979 CG LYS A 259 6693 8034 9596 1052 659 1682 C ATOM 1980 CD LYS A 259 28.521 29.106 20.306 1.00 71.36 C ANISOU 1980 CD LYS A 259 7369 9050 10696 1025 591 1851 C ATOM 1981 CE LYS A 259 27.546 30.172 20.798 1.00 74.54 C ANISOU 1981 CE LYS A 259 7627 9476 11218 1205 766 1942 C ATOM 1982 NZ LYS A 259 26.291 30.174 20.000 1.00 86.07 N ANISOU 1982 NZ LYS A 259 8816 11035 12853 1190 689 2121 N ATOM 1983 N ARG A 260 33.499 29.131 20.107 1.00 52.46 N ANISOU 1983 N ARG A 260 5743 6393 7795 930 399 1317 N ATOM 1984 CA ARG A 260 34.203 27.901 19.785 1.00 48.12 C ANISOU 1984 CA ARG A 260 5273 5847 7162 798 279 1269 C ATOM 1985 C ARG A 260 35.646 27.871 20.267 1.00 43.92 C ANISOU 1985 C ARG A 260 4936 5262 6489 804 284 1124 C ATOM 1986 O ARG A 260 36.322 26.862 20.059 1.00 46.41 O ANISOU 1986 O ARG A 260 5326 5573 6736 716 198 1081 O ATOM 1987 CB ARG A 260 34.182 27.658 18.274 1.00 50.58 C ANISOU 1987 CB ARG A 260 5539 6180 7500 708 100 1300 C ATOM 1988 CG ARG A 260 32.835 27.233 17.696 1.00 48.33 C ANISOU 1988 CG ARG A 260 5057 5968 7338 648 35 1438 C ATOM 1989 CD ARG A 260 32.944 26.894 16.208 1.00 49.98 C ANISOU 1989 CD ARG A 260 5254 6207 7529 549 -162 1442 C ATOM 1990 NE ARG A 260 33.276 28.060 15.365 1.00 52.07 N ANISOU 1990 NE ARG A 260 5539 6469 7778 623 -200 1446 N ATOM 1991 CZ ARG A 260 32.374 28.890 14.833 1.00 55.97 C ANISOU 1991 CZ ARG A 260 5886 7010 8369 685 -216 1567 C ATOM 1992 NH1 ARG A 260 31.082 28.697 15.062 1.00 54.59 N ANISOU 1992 NH1 ARG A 260 5520 6901 8319 683 -198 1687 N ATOM 1993 NH2 ARG A 260 32.760 29.917 14.082 1.00 47.73 N ANISOU 1993 NH2 ARG A 260 4879 5949 7307 752 -245 1581 N ATOM 1994 N ARG A 261 36.158 28.951 20.857 1.00 48.91 N ANISOU 1994 N ARG A 261 5651 5850 7084 903 375 1045 N ATOM 1995 CA ARG A 261 37.584 28.991 21.175 1.00 44.56 C ANISOU 1995 CA ARG A 261 5264 5259 6409 893 352 909 C ATOM 1996 C ARG A 261 37.983 27.856 22.111 1.00 49.54 C ANISOU 1996 C ARG A 261 5966 5919 6940 858 369 880 C ATOM 1997 O ARG A 261 38.986 27.169 21.877 1.00 53.52 O ANISOU 1997 O ARG A 261 6554 6415 7367 799 280 821 O ATOM 1998 CB ARG A 261 37.956 30.349 21.768 1.00 42.83 C ANISOU 1998 CB ARG A 261 5116 4981 6178 993 447 822 C ATOM 1999 CG ARG A 261 38.118 31.438 20.735 1.00 54.71 C ANISOU 1999 CG ARG A 261 6604 6425 7758 1011 403 829 C ATOM 2000 CD ARG A 261 38.175 32.794 21.381 1.00 60.82 C ANISOU 2000 CD ARG A 261 7433 7115 8562 1114 517 760 C ATOM 2001 NE ARG A 261 39.498 33.061 21.926 1.00 76.28 N ANISOU 2001 NE ARG A 261 9538 9028 10416 1091 507 608 N ATOM 2002 CZ ARG A 261 39.755 34.054 22.768 1.00 77.62 C ANISOU 2002 CZ ARG A 261 9794 9123 10575 1159 598 500 C ATOM 2003 NH1 ARG A 261 38.763 34.848 23.149 1.00 73.94 N ANISOU 2003 NH1 ARG A 261 9289 8612 10194 1270 723 529 N ATOM 2004 NH2 ARG A 261 40.987 34.244 23.233 1.00 76.18 N ANISOU 2004 NH2 ARG A 261 9733 8913 10299 1118 564 360 N ATOM 2005 N ASP A 262 37.202 27.632 23.173 1.00 46.98 N ANISOU 2005 N ASP A 262 5605 5631 6616 903 491 932 N ATOM 2006 CA ASP A 262 37.518 26.562 24.125 1.00 46.70 C ANISOU 2006 CA ASP A 262 5637 5626 6481 879 520 932 C ATOM 2007 C ASP A 262 37.418 25.178 23.502 1.00 48.63 C ANISOU 2007 C ASP A 262 5847 5869 6762 764 416 1003 C ATOM 2008 O ASP A 262 38.176 24.275 23.869 1.00 52.57 O ANISOU 2008 O ASP A 262 6439 6359 7176 731 380 976 O ATOM 2009 CB ASP A 262 36.606 26.671 25.346 1.00 52.22 C ANISOU 2009 CB ASP A 262 6297 6375 7171 957 691 993 C ATOM 2010 CG ASP A 262 37.096 27.716 26.338 1.00 66.39 C ANISOU 2010 CG ASP A 262 8202 8166 8855 1068 793 874 C ATOM 2011 OD1 ASP A 262 38.226 28.245 26.156 1.00 67.01 O ANISOU 2011 OD1 ASP A 262 8389 8202 8869 1066 718 746 O ATOM 2012 OD2 ASP A 262 36.346 28.029 27.284 1.00 70.28 O ANISOU 2012 OD2 ASP A 262 8673 8701 9331 1155 949 904 O ATOM 2013 N LEU A 263 36.518 24.995 22.540 1.00 49.12 N ANISOU 2013 N LEU A 263 5779 5935 6950 702 357 1089 N ATOM 2014 CA LEU A 263 36.411 23.702 21.882 1.00 48.35 C ANISOU 2014 CA LEU A 263 5660 5820 6891 580 246 1133 C ATOM 2015 C LEU A 263 37.719 23.302 21.203 1.00 45.88 C ANISOU 2015 C LEU A 263 5475 5462 6495 541 124 1025 C ATOM 2016 O LEU A 263 38.062 22.114 21.167 1.00 46.07 O ANISOU 2016 O LEU A 263 5554 5450 6501 475 70 1024 O ATOM 2017 CB LEU A 263 35.280 23.754 20.867 1.00 51.66 C ANISOU 2017 CB LEU A 263 5917 6263 7448 518 179 1222 C ATOM 2018 CG LEU A 263 34.852 22.433 20.245 1.00 59.83 C ANISOU 2018 CG LEU A 263 6905 7278 8548 374 69 1273 C ATOM 2019 CD1 LEU A 263 34.113 21.571 21.252 1.00 62.94 C ANISOU 2019 CD1 LEU A 263 7242 7676 8998 336 167 1379 C ATOM 2020 CD2 LEU A 263 33.999 22.722 19.009 1.00 59.92 C ANISOU 2020 CD2 LEU A 263 6775 7329 8661 316 -43 1325 C ATOM 2021 N TYR A 264 38.463 24.271 20.665 1.00 43.94 N ANISOU 2021 N TYR A 264 5276 5211 6208 585 89 941 N ATOM 2022 CA TYR A 264 39.734 23.971 20.009 1.00 45.96 C ANISOU 2022 CA TYR A 264 5637 5439 6387 559 -9 846 C ATOM 2023 C TYR A 264 40.895 23.930 20.988 1.00 42.19 C ANISOU 2023 C TYR A 264 5276 4956 5798 613 33 766 C ATOM 2024 O TYR A 264 41.859 23.204 20.746 1.00 45.39 O ANISOU 2024 O TYR A 264 5758 5341 6147 590 -33 715 O ATOM 2025 CB TYR A 264 40.029 24.981 18.875 1.00 42.36 C ANISOU 2025 CB TYR A 264 5167 4987 5942 568 -68 811 C ATOM 2026 CG TYR A 264 39.022 24.870 17.740 1.00 47.74 C ANISOU 2026 CG TYR A 264 5741 5690 6707 508 -148 889 C ATOM 2027 CD1 TYR A 264 38.751 23.642 17.151 1.00 43.91 C ANISOU 2027 CD1 TYR A 264 5249 5200 6234 412 -241 903 C ATOM 2028 CD2 TYR A 264 38.271 25.980 17.323 1.00 43.62 C ANISOU 2028 CD2 TYR A 264 5122 5193 6257 550 -131 953 C ATOM 2029 CE1 TYR A 264 37.794 23.525 16.125 1.00 42.55 C ANISOU 2029 CE1 TYR A 264 4975 5063 6130 343 -335 966 C ATOM 2030 CE2 TYR A 264 37.313 25.871 16.312 1.00 42.57 C ANISOU 2030 CE2 TYR A 264 4877 5103 6194 497 -219 1036 C ATOM 2031 CZ TYR A 264 37.080 24.636 15.718 1.00 47.76 C ANISOU 2031 CZ TYR A 264 5528 5771 6849 387 -328 1037 C ATOM 2032 OH TYR A 264 36.142 24.499 14.708 1.00 51.83 O ANISOU 2032 OH TYR A 264 5932 6339 7422 321 -438 1108 O ATOM 2033 N LEU A 265 40.826 24.671 22.095 1.00 36.86 N ANISOU 2033 N LEU A 265 4617 4303 5087 688 137 753 N ATOM 2034 CA LEU A 265 41.780 24.437 23.176 1.00 45.52 C ANISOU 2034 CA LEU A 265 5817 5415 6064 730 165 692 C ATOM 2035 C LEU A 265 41.657 23.014 23.708 1.00 49.18 C ANISOU 2035 C LEU A 265 6304 5877 6504 701 167 763 C ATOM 2036 O LEU A 265 42.663 22.382 24.055 1.00 46.95 O ANISOU 2036 O LEU A 265 6105 5594 6138 712 128 727 O ATOM 2037 CB LEU A 265 41.560 25.434 24.319 1.00 39.96 C ANISOU 2037 CB LEU A 265 5133 4741 5310 813 281 660 C ATOM 2038 CG LEU A 265 41.872 26.898 24.028 1.00 48.09 C ANISOU 2038 CG LEU A 265 6171 5742 6358 850 289 572 C ATOM 2039 CD1 LEU A 265 41.315 27.792 25.124 1.00 50.15 C ANISOU 2039 CD1 LEU A 265 6448 6015 6593 935 421 545 C ATOM 2040 CD2 LEU A 265 43.346 27.113 23.882 1.00 52.30 C ANISOU 2040 CD2 LEU A 265 6784 6267 6819 834 208 463 C ATOM 2041 N LEU A 266 40.426 22.491 23.742 1.00 43.53 N ANISOU 2041 N LEU A 266 5505 5158 5875 663 211 874 N ATOM 2042 CA LEU A 266 40.132 21.230 24.416 1.00 42.14 C ANISOU 2042 CA LEU A 266 5345 4970 5696 633 242 967 C ATOM 2043 C LEU A 266 40.913 20.074 23.820 1.00 43.59 C ANISOU 2043 C LEU A 266 5597 5088 5879 578 134 946 C ATOM 2044 O LEU A 266 41.403 19.207 24.553 1.00 54.51 O ANISOU 2044 O LEU A 266 7054 6454 7203 597 147 978 O ATOM 2045 CB LEU A 266 38.628 20.955 24.342 1.00 40.04 C ANISOU 2045 CB LEU A 266 4948 4707 5557 578 297 1094 C ATOM 2046 CG LEU A 266 38.119 19.613 24.849 1.00 46.38 C ANISOU 2046 CG LEU A 266 5741 5478 6403 515 329 1215 C ATOM 2047 CD1 LEU A 266 38.464 19.444 26.348 1.00 37.65 C ANISOU 2047 CD1 LEU A 266 4720 4420 5167 599 445 1254 C ATOM 2048 CD2 LEU A 266 36.601 19.512 24.611 1.00 44.62 C ANISOU 2048 CD2 LEU A 266 5353 5268 6332 444 372 1337 C ATOM 2049 N TYR A 267 41.047 20.042 22.493 1.00 42.64 N ANISOU 2049 N TYR A 267 5457 4928 5816 521 29 895 N ATOM 2050 CA TYR A 267 41.838 18.989 21.855 1.00 44.16 C ANISOU 2050 CA TYR A 267 5726 5051 6002 484 -64 853 C ATOM 2051 C TYR A 267 43.248 18.928 22.425 1.00 42.15 C ANISOU 2051 C TYR A 267 5572 4811 5632 566 -68 789 C ATOM 2052 O TYR A 267 43.769 17.847 22.701 1.00 43.41 O ANISOU 2052 O TYR A 267 5801 4919 5775 575 -86 809 O ATOM 2053 CB TYR A 267 41.908 19.227 20.353 1.00 41.91 C ANISOU 2053 CB TYR A 267 5418 4751 5753 433 -164 785 C ATOM 2054 CG TYR A 267 42.836 18.294 19.601 1.00 47.43 C ANISOU 2054 CG TYR A 267 6208 5386 6428 417 -249 713 C ATOM 2055 CD1 TYR A 267 42.551 16.925 19.496 1.00 45.77 C ANISOU 2055 CD1 TYR A 267 6036 5079 6277 353 -281 744 C ATOM 2056 CD2 TYR A 267 43.986 18.782 18.965 1.00 43.47 C ANISOU 2056 CD2 TYR A 267 5752 4912 5854 464 -288 615 C ATOM 2057 CE1 TYR A 267 43.398 16.063 18.784 1.00 49.06 C ANISOU 2057 CE1 TYR A 267 6547 5421 6674 353 -347 665 C ATOM 2058 CE2 TYR A 267 44.846 17.925 18.240 1.00 44.22 C ANISOU 2058 CE2 TYR A 267 5924 4953 5923 467 -348 546 C ATOM 2059 CZ TYR A 267 44.545 16.569 18.159 1.00 51.68 C ANISOU 2059 CZ TYR A 267 6919 5796 6921 419 -376 565 C ATOM 2060 OH TYR A 267 45.367 15.714 17.435 1.00 50.88 O ANISOU 2060 OH TYR A 267 6906 5626 6799 434 -424 485 O ATOM 2061 N HIS A 268 43.884 20.088 22.598 1.00 41.71 N ANISOU 2061 N HIS A 268 5521 4820 5505 626 -55 715 N ATOM 2062 CA HIS A 268 45.237 20.130 23.117 1.00 42.92 C ANISOU 2062 CA HIS A 268 5747 5006 5556 693 -75 651 C ATOM 2063 C HIS A 268 45.293 19.866 24.614 1.00 46.53 C ANISOU 2063 C HIS A 268 6247 5506 5927 751 -10 704 C ATOM 2064 O HIS A 268 46.245 19.235 25.084 1.00 49.88 O ANISOU 2064 O HIS A 268 6732 5939 6280 797 -42 702 O ATOM 2065 CB HIS A 268 45.869 21.475 22.764 1.00 40.14 C ANISOU 2065 CB HIS A 268 5378 4700 5173 714 -90 553 C ATOM 2066 CG HIS A 268 46.083 21.638 21.299 1.00 43.28 C ANISOU 2066 CG HIS A 268 5750 5069 5624 671 -156 511 C ATOM 2067 ND1 HIS A 268 47.068 20.951 20.620 1.00 37.85 N ANISOU 2067 ND1 HIS A 268 5100 4363 4917 675 -218 468 N ATOM 2068 CD2 HIS A 268 45.407 22.356 20.366 1.00 42.51 C ANISOU 2068 CD2 HIS A 268 5595 4966 5590 632 -164 515 C ATOM 2069 CE1 HIS A 268 47.013 21.265 19.338 1.00 37.07 C ANISOU 2069 CE1 HIS A 268 4977 4256 4853 636 -257 439 C ATOM 2070 NE2 HIS A 268 46.010 22.112 19.156 1.00 42.73 N ANISOU 2070 NE2 HIS A 268 5635 4982 5619 607 -233 473 N ATOM 2071 N TYR A 269 44.274 20.278 25.370 1.00 41.29 N ANISOU 2071 N TYR A 269 5551 4876 5261 758 83 762 N ATOM 2072 CA TYR A 269 44.231 19.892 26.777 1.00 43.99 C ANISOU 2072 CA TYR A 269 5942 5268 5504 813 155 831 C ATOM 2073 C TYR A 269 44.120 18.379 26.932 1.00 51.24 C ANISOU 2073 C TYR A 269 6891 6123 6456 790 149 946 C ATOM 2074 O TYR A 269 44.772 17.788 27.803 1.00 54.60 O ANISOU 2074 O TYR A 269 7386 6575 6783 848 150 988 O ATOM 2075 CB TYR A 269 43.072 20.597 27.477 1.00 45.73 C ANISOU 2075 CB TYR A 269 6117 5539 5721 830 278 876 C ATOM 2076 CG TYR A 269 43.364 22.057 27.744 1.00 60.21 C ANISOU 2076 CG TYR A 269 7962 7427 7487 882 302 755 C ATOM 2077 CD1 TYR A 269 44.667 22.495 27.979 1.00 66.88 C ANISOU 2077 CD1 TYR A 269 8876 8308 8228 916 231 641 C ATOM 2078 CD2 TYR A 269 42.345 23.008 27.736 1.00 59.74 C ANISOU 2078 CD2 TYR A 269 7839 7375 7484 895 391 755 C ATOM 2079 CE1 TYR A 269 44.943 23.849 28.221 1.00 66.83 C ANISOU 2079 CE1 TYR A 269 8887 8331 8175 946 247 520 C ATOM 2080 CE2 TYR A 269 42.615 24.361 27.963 1.00 54.65 C ANISOU 2080 CE2 TYR A 269 7220 6751 6795 943 417 636 C ATOM 2081 CZ TYR A 269 43.908 24.772 28.203 1.00 60.70 C ANISOU 2081 CZ TYR A 269 8067 7538 7459 960 342 515 C ATOM 2082 OH TYR A 269 44.166 26.105 28.442 1.00 62.86 O ANISOU 2082 OH TYR A 269 8372 7811 7702 992 363 391 O ATOM 2083 N LEU A 270 43.308 17.727 26.096 1.00 46.49 N ANISOU 2083 N LEU A 270 6238 5432 5995 704 134 1002 N ATOM 2084 CA LEU A 270 43.246 16.272 26.154 1.00 45.57 C ANISOU 2084 CA LEU A 270 6161 5220 5933 669 122 1099 C ATOM 2085 C LEU A 270 44.584 15.653 25.762 1.00 46.91 C ANISOU 2085 C LEU A 270 6413 5340 6070 712 29 1035 C ATOM 2086 O LEU A 270 45.045 14.699 26.393 1.00 49.83 O ANISOU 2086 O LEU A 270 6851 5673 6410 755 34 1110 O ATOM 2087 CB LEU A 270 42.116 15.747 25.259 1.00 47.93 C ANISOU 2087 CB LEU A 270 6387 5427 6397 548 106 1147 C ATOM 2088 CG LEU A 270 40.674 16.024 25.703 1.00 52.93 C ANISOU 2088 CG LEU A 270 6914 6098 7098 500 207 1257 C ATOM 2089 CD1 LEU A 270 39.679 15.580 24.629 1.00 53.64 C ANISOU 2089 CD1 LEU A 270 6914 6110 7358 367 151 1283 C ATOM 2090 CD2 LEU A 270 40.341 15.375 27.057 1.00 50.08 C ANISOU 2090 CD2 LEU A 270 6579 5754 6695 530 322 1408 C ATOM 2091 N ASN A 271 45.215 16.157 24.706 1.00 46.42 N ANISOU 2091 N ASN A 271 6342 5277 6018 706 -49 909 N ATOM 2092 CA ASN A 271 46.510 15.601 24.321 1.00 43.10 C ANISOU 2092 CA ASN A 271 5985 4823 5569 760 -121 849 C ATOM 2093 C ASN A 271 47.539 15.772 25.435 1.00 44.79 C ANISOU 2093 C ASN A 271 6238 5130 5652 866 -116 857 C ATOM 2094 O ASN A 271 48.342 14.865 25.690 1.00 53.11 O ANISOU 2094 O ASN A 271 7346 6148 6686 929 -145 893 O ATOM 2095 CB ASN A 271 47.022 16.251 23.035 1.00 43.33 C ANISOU 2095 CB ASN A 271 5987 4861 5614 742 -185 720 C ATOM 2096 CG ASN A 271 48.180 15.482 22.426 1.00 48.44 C ANISOU 2096 CG ASN A 271 6689 5455 6260 791 -244 666 C ATOM 2097 OD1 ASN A 271 48.149 14.251 22.347 1.00 49.81 O ANISOU 2097 OD1 ASN A 271 6921 5517 6489 792 -252 709 O ATOM 2098 ND2 ASN A 271 49.200 16.194 21.999 1.00 41.61 N ANISOU 2098 ND2 ASN A 271 5805 4663 5343 834 -276 574 N ATOM 2099 N HIS A 272 47.528 16.930 26.106 1.00 44.26 N ANISOU 2099 N HIS A 272 6144 5179 5493 890 -85 821 N ATOM 2100 CA HIS A 272 48.482 17.194 27.181 1.00 49.60 C ANISOU 2100 CA HIS A 272 6855 5963 6027 977 -99 811 C ATOM 2101 C HIS A 272 48.197 16.303 28.384 1.00 49.44 C ANISOU 2101 C HIS A 272 6889 5952 5942 1023 -48 954 C ATOM 2102 O HIS A 272 49.125 15.767 28.999 1.00 54.81 O ANISOU 2102 O HIS A 272 7614 6671 6540 1103 -90 992 O ATOM 2103 CB HIS A 272 48.446 18.680 27.550 1.00 46.36 C ANISOU 2103 CB HIS A 272 6418 5654 5542 976 -79 717 C ATOM 2104 CG HIS A 272 49.397 19.510 26.752 1.00 50.75 C ANISOU 2104 CG HIS A 272 6939 6232 6111 966 -152 587 C ATOM 2105 ND1 HIS A 272 49.321 19.611 25.380 1.00 53.90 N ANISOU 2105 ND1 HIS A 272 7297 6562 6621 912 -177 543 N ATOM 2106 CD2 HIS A 272 50.462 20.260 27.126 1.00 55.60 C ANISOU 2106 CD2 HIS A 272 7550 6935 6641 996 -205 498 C ATOM 2107 CE1 HIS A 272 50.293 20.391 24.942 1.00 52.32 C ANISOU 2107 CE1 HIS A 272 7069 6405 6407 914 -228 446 C ATOM 2108 NE2 HIS A 272 51.008 20.789 25.979 1.00 54.85 N ANISOU 2108 NE2 HIS A 272 7404 6815 6620 958 -249 415 N ATOM 2109 N TYR A 273 46.914 16.105 28.695 1.00 46.45 N ANISOU 2109 N TYR A 273 6499 5542 5608 976 44 1050 N ATOM 2110 CA TYR A 273 46.484 15.085 29.648 1.00 50.16 C ANISOU 2110 CA TYR A 273 7016 5992 6051 1000 110 1218 C ATOM 2111 C TYR A 273 47.067 13.709 29.301 1.00 53.96 C ANISOU 2111 C TYR A 273 7547 6348 6608 1018 55 1287 C ATOM 2112 O TYR A 273 47.667 13.042 30.152 1.00 56.61 O ANISOU 2112 O TYR A 273 7944 6707 6860 1102 50 1384 O ATOM 2113 CB TYR A 273 44.951 15.075 29.676 1.00 50.09 C ANISOU 2113 CB TYR A 273 6952 5947 6133 919 216 1305 C ATOM 2114 CG TYR A 273 44.249 14.049 30.552 1.00 54.47 C ANISOU 2114 CG TYR A 273 7533 6468 6696 914 310 1502 C ATOM 2115 CD1 TYR A 273 44.878 13.442 31.645 1.00 59.17 C ANISOU 2115 CD1 TYR A 273 8212 7112 7158 1006 323 1608 C ATOM 2116 CD2 TYR A 273 42.943 13.694 30.280 1.00 49.02 C ANISOU 2116 CD2 TYR A 273 6774 5702 6150 814 384 1596 C ATOM 2117 CE1 TYR A 273 44.201 12.494 32.427 1.00 61.46 C ANISOU 2117 CE1 TYR A 273 8528 7365 7461 999 421 1812 C ATOM 2118 CE2 TYR A 273 42.265 12.773 31.046 1.00 54.09 C ANISOU 2118 CE2 TYR A 273 7427 6306 6819 793 480 1790 C ATOM 2119 CZ TYR A 273 42.885 12.174 32.115 1.00 58.40 C ANISOU 2119 CZ TYR A 273 8067 6891 7232 886 506 1902 C ATOM 2120 OH TYR A 273 42.167 11.253 32.841 1.00 59.59 O ANISOU 2120 OH TYR A 273 8226 6996 7417 860 613 2116 O ATOM 2121 N ASN A 274 46.910 13.273 28.046 1.00 53.22 N ANISOU 2121 N ASN A 274 7436 6119 6668 947 11 1237 N ATOM 2122 CA ASN A 274 47.390 11.951 27.647 1.00 52.79 C ANISOU 2122 CA ASN A 274 7442 5916 6700 965 -30 1284 C ATOM 2123 C ASN A 274 48.911 11.850 27.653 1.00 54.66 C ANISOU 2123 C ASN A 274 7711 6194 6862 1084 -106 1227 C ATOM 2124 O ASN A 274 49.443 10.775 27.938 1.00 55.01 O ANISOU 2124 O ASN A 274 7817 6158 6926 1155 -118 1316 O ATOM 2125 CB ASN A 274 46.853 11.591 26.259 1.00 53.19 C ANISOU 2125 CB ASN A 274 7476 5822 6913 858 -64 1212 C ATOM 2126 CG ASN A 274 45.442 11.002 26.310 1.00 56.31 C ANISOU 2126 CG ASN A 274 7849 6115 7430 740 -4 1324 C ATOM 2127 OD1 ASN A 274 45.137 10.190 27.178 1.00 53.61 O ANISOU 2127 OD1 ASN A 274 7545 5721 7104 749 56 1480 O ATOM 2128 ND2 ASN A 274 44.576 11.435 25.402 1.00 53.45 N ANISOU 2128 ND2 ASN A 274 7417 5736 7157 627 -20 1257 N ATOM 2129 N LEU A 275 49.621 12.947 27.369 1.00 53.60 N ANISOU 2129 N LEU A 275 7529 6182 6653 1108 -155 1092 N ATOM 2130 CA LEU A 275 51.080 12.958 27.305 1.00 52.58 C ANISOU 2130 CA LEU A 275 7399 6113 6467 1209 -229 1034 C ATOM 2131 C LEU A 275 51.758 13.255 28.641 1.00 56.45 C ANISOU 2131 C LEU A 275 7895 6761 6794 1301 -249 1088 C ATOM 2132 O LEU A 275 52.768 12.620 28.963 1.00 59.07 O ANISOU 2132 O LEU A 275 8243 7109 7093 1405 -300 1137 O ATOM 2133 CB LEU A 275 51.565 13.980 26.277 1.00 49.55 C ANISOU 2133 CB LEU A 275 6950 5781 6096 1175 -274 870 C ATOM 2134 CG LEU A 275 51.503 13.637 24.793 1.00 49.47 C ANISOU 2134 CG LEU A 275 6939 5650 6207 1128 -289 791 C ATOM 2135 CD1 LEU A 275 52.033 14.818 24.022 1.00 45.59 C ANISOU 2135 CD1 LEU A 275 6380 5250 5694 1105 -320 659 C ATOM 2136 CD2 LEU A 275 52.345 12.391 24.491 1.00 51.03 C ANISOU 2136 CD2 LEU A 275 7188 5747 6455 1218 -314 816 C ATOM 2137 N PHE A 276 51.261 14.222 29.417 1.00 57.75 N ANISOU 2137 N PHE A 276 8046 7046 6849 1272 -215 1072 N ATOM 2138 CA PHE A 276 52.000 14.707 30.575 1.00 48.44 C ANISOU 2138 CA PHE A 276 6875 6038 5492 1348 -257 1075 C ATOM 2139 C PHE A 276 51.296 14.488 31.903 1.00 58.71 C ANISOU 2139 C PHE A 276 8236 7404 6668 1375 -185 1207 C ATOM 2140 O PHE A 276 51.839 14.909 32.929 1.00 73.46 O ANISOU 2140 O PHE A 276 10125 9430 8359 1436 -222 1204 O ATOM 2141 CB PHE A 276 52.343 16.199 30.422 1.00 42.26 C ANISOU 2141 CB PHE A 276 6038 5367 4652 1306 -295 905 C ATOM 2142 CG PHE A 276 53.077 16.515 29.151 1.00 42.36 C ANISOU 2142 CG PHE A 276 5985 5338 4773 1279 -354 788 C ATOM 2143 CD1 PHE A 276 54.338 15.997 28.920 1.00 44.47 C ANISOU 2143 CD1 PHE A 276 6222 5626 5049 1353 -434 789 C ATOM 2144 CD2 PHE A 276 52.480 17.290 28.165 1.00 43.14 C ANISOU 2144 CD2 PHE A 276 6047 5380 4964 1187 -322 694 C ATOM 2145 CE1 PHE A 276 55.002 16.245 27.720 1.00 49.57 C ANISOU 2145 CE1 PHE A 276 6804 6240 5791 1334 -467 692 C ATOM 2146 CE2 PHE A 276 53.134 17.553 26.974 1.00 47.03 C ANISOU 2146 CE2 PHE A 276 6485 5843 5542 1165 -365 603 C ATOM 2147 CZ PHE A 276 54.399 17.027 26.745 1.00 50.15 C ANISOU 2147 CZ PHE A 276 6853 6262 5941 1237 -431 599 C ATOM 2148 N GLY A 277 50.119 13.875 31.930 1.00 54.66 N ANISOU 2148 N GLY A 277 7750 6787 6234 1328 -84 1322 N ATOM 2149 CA GLY A 277 49.510 13.433 33.173 1.00 54.24 C ANISOU 2149 CA GLY A 277 7753 6786 6070 1364 1 1487 C ATOM 2150 C GLY A 277 48.232 14.188 33.547 1.00 57.52 C ANISOU 2150 C GLY A 277 8153 7249 6454 1301 122 1484 C ATOM 2151 O GLY A 277 47.874 15.221 32.976 1.00 55.69 O ANISOU 2151 O GLY A 277 7868 7028 6265 1241 131 1342 O ATOM 2152 N SER A 278 47.565 13.644 34.574 1.00 59.33 N ANISOU 2152 N SER A 278 8428 7511 6603 1328 224 1657 N ATOM 2153 CA SER A 278 46.232 14.065 34.983 1.00 68.04 C ANISOU 2153 CA SER A 278 9508 8645 7698 1279 371 1706 C ATOM 2154 C SER A 278 46.184 15.465 35.582 1.00 68.11 C ANISOU 2154 C SER A 278 9522 8821 7535 1311 400 1565 C ATOM 2155 O SER A 278 45.084 15.971 35.832 1.00 63.37 O ANISOU 2155 O SER A 278 8891 8249 6937 1284 531 1579 O ATOM 2156 CB SER A 278 45.652 13.071 35.990 1.00 70.80 C ANISOU 2156 CB SER A 278 9907 9000 7992 1310 482 1947 C ATOM 2157 OG SER A 278 46.531 12.910 37.079 1.00 77.20 O ANISOU 2157 OG SER A 278 10805 9951 8578 1427 440 2005 O ATOM 2158 N GLY A 279 47.320 16.120 35.806 1.00 63.42 N ANISOU 2158 N GLY A 279 8960 8333 6805 1365 286 1426 N ATOM 2159 CA GLY A 279 47.241 17.524 36.168 1.00 58.14 C ANISOU 2159 CA GLY A 279 8297 7778 6015 1372 306 1257 C ATOM 2160 C GLY A 279 46.493 18.346 35.133 1.00 60.09 C ANISOU 2160 C GLY A 279 8463 7930 6440 1289 350 1145 C ATOM 2161 O GLY A 279 45.907 19.377 35.459 1.00 63.13 O ANISOU 2161 O GLY A 279 8849 8370 6769 1295 432 1057 O ATOM 2162 N TYR A 280 46.476 17.886 33.879 1.00 63.63 N ANISOU 2162 N TYR A 280 8845 8234 7099 1220 298 1151 N ATOM 2163 CA TYR A 280 45.759 18.568 32.809 1.00 57.68 C ANISOU 2163 CA TYR A 280 8009 7394 6514 1143 324 1069 C ATOM 2164 C TYR A 280 44.301 18.132 32.695 1.00 59.50 C ANISOU 2164 C TYR A 280 8180 7561 6865 1092 452 1204 C ATOM 2165 O TYR A 280 43.545 18.723 31.913 1.00 55.47 O ANISOU 2165 O TYR A 280 7590 7000 6487 1036 482 1157 O ATOM 2166 CB TYR A 280 46.473 18.337 31.471 1.00 54.69 C ANISOU 2166 CB TYR A 280 7589 6911 6278 1093 201 999 C ATOM 2167 CG TYR A 280 47.711 19.188 31.264 1.00 53.62 C ANISOU 2167 CG TYR A 280 7461 6833 6079 1114 91 837 C ATOM 2168 CD1 TYR A 280 47.602 20.519 30.867 1.00 48.41 C ANISOU 2168 CD1 TYR A 280 6769 6184 5443 1083 96 697 C ATOM 2169 CD2 TYR A 280 48.985 18.660 31.447 1.00 53.11 C ANISOU 2169 CD2 TYR A 280 7426 6806 5947 1163 -14 834 C ATOM 2170 CE1 TYR A 280 48.719 21.303 30.679 1.00 49.30 C ANISOU 2170 CE1 TYR A 280 6880 6337 5515 1084 0 557 C ATOM 2171 CE2 TYR A 280 50.120 19.435 31.252 1.00 50.62 C ANISOU 2171 CE2 TYR A 280 7094 6551 5589 1168 -115 695 C ATOM 2172 CZ TYR A 280 49.979 20.761 30.874 1.00 60.39 C ANISOU 2172 CZ TYR A 280 8301 7792 6853 1120 -107 555 C ATOM 2173 OH TYR A 280 51.095 21.552 30.665 1.00 65.57 O ANISOU 2173 OH TYR A 280 8932 8495 7486 1107 -204 424 O ATOM 2174 N ARG A 281 43.875 17.130 33.460 1.00 59.23 N ANISOU 2174 N ARG A 281 8175 7532 6795 1109 528 1382 N ATOM 2175 CA ARG A 281 42.508 16.649 33.305 1.00 58.65 C ANISOU 2175 CA ARG A 281 8026 7395 6865 1041 645 1522 C ATOM 2176 C ARG A 281 41.482 17.700 33.715 1.00 58.82 C ANISOU 2176 C ARG A 281 7991 7501 6856 1060 783 1497 C ATOM 2177 O ARG A 281 40.397 17.760 33.126 1.00 58.45 O ANISOU 2177 O ARG A 281 7834 7399 6976 991 843 1544 O ATOM 2178 CB ARG A 281 42.303 15.368 34.108 1.00 56.15 C ANISOU 2178 CB ARG A 281 7754 7062 6518 1053 709 1735 C ATOM 2179 CG ARG A 281 40.900 14.796 34.013 1.00 59.59 C ANISOU 2179 CG ARG A 281 8098 7429 7113 966 833 1898 C ATOM 2180 CD ARG A 281 40.680 13.754 35.080 1.00 59.04 C ANISOU 2180 CD ARG A 281 8083 7375 6975 993 932 2121 C ATOM 2181 NE ARG A 281 39.434 13.010 34.890 1.00 65.98 N ANISOU 2181 NE ARG A 281 8865 8158 8046 882 1034 2296 N ATOM 2182 CZ ARG A 281 38.288 13.302 35.492 1.00 68.18 C ANISOU 2182 CZ ARG A 281 9063 8522 8321 875 1207 2404 C ATOM 2183 NH1 ARG A 281 38.224 14.326 36.328 1.00 70.07 N ANISOU 2183 NH1 ARG A 281 9326 8937 8360 984 1304 2343 N ATOM 2184 NH2 ARG A 281 37.209 12.570 35.261 1.00 66.80 N ANISOU 2184 NH2 ARG A 281 8780 8256 8343 758 1285 2568 N ATOM 2185 N SER A 282 41.807 18.546 34.700 1.00 56.31 N ANISOU 2185 N SER A 282 7747 7319 6331 1155 830 1416 N ATOM 2186 CA SER A 282 40.832 19.519 35.198 1.00 60.88 C ANISOU 2186 CA SER A 282 8289 7974 6870 1197 984 1389 C ATOM 2187 C SER A 282 40.504 20.595 34.162 1.00 58.11 C ANISOU 2187 C SER A 282 7852 7560 6668 1162 957 1250 C ATOM 2188 O SER A 282 39.339 20.979 34.017 1.00 64.17 O ANISOU 2188 O SER A 282 8520 8323 7540 1155 1076 1297 O ATOM 2189 CB SER A 282 41.334 20.150 36.504 1.00 65.22 C ANISOU 2189 CB SER A 282 8963 8676 7142 1309 1031 1310 C ATOM 2190 OG SER A 282 42.703 20.477 36.451 1.00 79.65 O ANISOU 2190 OG SER A 282 10873 10523 8866 1326 867 1159 O ATOM 2191 N SER A 283 41.514 21.101 33.447 1.00 50.21 N ANISOU 2191 N SER A 283 6881 6516 5681 1144 808 1092 N ATOM 2192 CA SER A 283 41.271 22.029 32.344 1.00 49.98 C ANISOU 2192 CA SER A 283 6773 6415 5804 1105 771 985 C ATOM 2193 C SER A 283 40.345 21.423 31.289 1.00 49.17 C ANISOU 2193 C SER A 283 6541 6221 5921 1014 767 1099 C ATOM 2194 O SER A 283 39.428 22.088 30.797 1.00 52.33 O ANISOU 2194 O SER A 283 6841 6602 6440 1004 824 1099 O ATOM 2195 CB SER A 283 42.599 22.445 31.718 1.00 57.07 C ANISOU 2195 CB SER A 283 7719 7280 6684 1088 609 833 C ATOM 2196 OG SER A 283 43.383 23.157 32.651 1.00 64.35 O ANISOU 2196 OG SER A 283 8742 8288 7418 1155 600 711 O ATOM 2197 N ALA A 284 40.563 20.160 30.929 1.00 49.65 N ANISOU 2197 N ALA A 284 6603 6219 6041 949 696 1194 N ATOM 2198 CA ALA A 284 39.703 19.523 29.935 1.00 51.06 C ANISOU 2198 CA ALA A 284 6670 6307 6423 845 674 1285 C ATOM 2199 C ALA A 284 38.282 19.345 30.457 1.00 55.85 C ANISOU 2199 C ALA A 284 7174 6948 7097 832 829 1437 C ATOM 2200 O ALA A 284 37.312 19.601 29.738 1.00 56.75 O ANISOU 2200 O ALA A 284 7156 7038 7369 776 844 1470 O ATOM 2201 CB ALA A 284 40.282 18.165 29.522 1.00 48.12 C ANISOU 2201 CB ALA A 284 6344 5843 6097 782 571 1340 C ATOM 2202 N MET A 285 38.133 18.886 31.681 1.00 60.81 N ANISOU 2202 N MET A 285 7853 7643 7610 882 945 1544 N ATOM 2203 CA MET A 285 36.817 18.642 32.222 1.00 61.19 C ANISOU 2203 CA MET A 285 7796 7733 7722 870 1110 1709 C ATOM 2204 C MET A 285 36.042 19.914 32.428 1.00 59.52 C ANISOU 2204 C MET A 285 7506 7601 7506 945 1233 1658 C ATOM 2205 O MET A 285 34.877 19.965 32.188 1.00 56.27 O ANISOU 2205 O MET A 285 6944 7197 7241 910 1317 1756 O ATOM 2206 CB MET A 285 36.900 17.815 33.492 1.00 69.62 C ANISOU 2206 CB MET A 285 8946 8858 8649 911 1214 1851 C ATOM 2207 CG MET A 285 35.566 17.380 34.043 1.00 80.86 C ANISOU 2207 CG MET A 285 10253 10320 10150 883 1395 2054 C ATOM 2208 SD MET A 285 34.795 16.076 33.112 1.00 87.72 S ANISOU 2208 SD MET A 285 10989 11040 11303 695 1336 2216 S ATOM 2209 CE MET A 285 36.051 14.837 33.196 1.00 84.53 C ANISOU 2209 CE MET A 285 10756 10527 10833 674 1207 2238 C ATOM 2210 N SER A 286 36.709 20.943 32.873 1.00 57.70 N ANISOU 2210 N SER A 286 7377 7429 7117 1050 1240 1502 N ATOM 2211 CA SER A 286 36.048 22.229 33.046 1.00 59.44 C ANISOU 2211 CA SER A 286 7545 7700 7340 1136 1358 1431 C ATOM 2212 C SER A 286 35.439 22.713 31.728 1.00 63.02 C ANISOU 2212 C SER A 286 7850 8077 8017 1077 1293 1416 C ATOM 2213 O SER A 286 34.274 23.127 31.682 1.00 59.12 O ANISOU 2213 O SER A 286 7216 7612 7636 1103 1412 1491 O ATOM 2214 CB SER A 286 37.047 23.237 33.621 1.00 63.44 C ANISOU 2214 CB SER A 286 8209 8247 7650 1236 1338 1234 C ATOM 2215 OG SER A 286 36.548 24.549 33.534 1.00 72.06 O ANISOU 2215 OG SER A 286 9263 9338 8779 1312 1421 1134 O ATOM 2216 N ILE A 287 36.199 22.622 30.630 1.00 62.68 N ANISOU 2216 N ILE A 287 7829 7948 8040 1002 1106 1332 N ATOM 2217 CA ILE A 287 35.675 23.032 29.329 1.00 56.55 C ANISOU 2217 CA ILE A 287 6922 7112 7451 944 1028 1326 C ATOM 2218 C ILE A 287 34.497 22.157 28.916 1.00 54.89 C ANISOU 2218 C ILE A 287 6546 6893 7416 845 1047 1501 C ATOM 2219 O ILE A 287 33.493 22.655 28.397 1.00 59.61 O ANISOU 2219 O ILE A 287 6987 7505 8157 841 1079 1554 O ATOM 2220 CB ILE A 287 36.786 23.011 28.264 1.00 50.66 C ANISOU 2220 CB ILE A 287 6246 6289 6713 884 834 1209 C ATOM 2221 CG1 ILE A 287 37.771 24.160 28.472 1.00 45.78 C ANISOU 2221 CG1 ILE A 287 5742 5674 5977 967 815 1038 C ATOM 2222 CG2 ILE A 287 36.187 23.061 26.868 1.00 47.41 C ANISOU 2222 CG2 ILE A 287 5703 5828 6483 801 737 1240 C ATOM 2223 CD1 ILE A 287 38.972 24.152 27.473 1.00 42.66 C ANISOU 2223 CD1 ILE A 287 5410 5217 5582 912 639 931 C ATOM 2224 N ILE A 288 34.604 20.841 29.116 1.00 55.39 N ANISOU 2224 N ILE A 288 6636 6929 7483 759 1018 1598 N ATOM 2225 CA ILE A 288 33.508 19.954 28.731 1.00 63.12 C ANISOU 2225 CA ILE A 288 7458 7884 8643 639 1025 1760 C ATOM 2226 C ILE A 288 32.265 20.253 29.559 1.00 66.10 C ANISOU 2226 C ILE A 288 7697 8357 9060 694 1231 1896 C ATOM 2227 O ILE A 288 31.139 20.208 29.050 1.00 67.46 O ANISOU 2227 O ILE A 288 7676 8543 9415 628 1246 2001 O ATOM 2228 CB ILE A 288 33.930 18.476 28.857 1.00 63.81 C ANISOU 2228 CB ILE A 288 7622 7893 8731 540 965 1835 C ATOM 2229 CG1 ILE A 288 35.003 18.117 27.823 1.00 58.89 C ANISOU 2229 CG1 ILE A 288 7101 7168 8107 482 763 1707 C ATOM 2230 CG2 ILE A 288 32.725 17.555 28.674 1.00 62.94 C ANISOU 2230 CG2 ILE A 288 7350 7753 8812 405 997 2014 C ATOM 2231 CD1 ILE A 288 35.545 16.676 27.968 1.00 50.16 C ANISOU 2231 CD1 ILE A 288 6095 5963 7001 410 708 1765 C ATOM 2232 N ASP A 289 32.448 20.554 30.852 1.00 69.61 N ANISOU 2232 N ASP A 289 8235 8883 9331 817 1391 1899 N ATOM 2233 CA ASP A 289 31.311 20.864 31.718 1.00 72.01 C ANISOU 2233 CA ASP A 289 8421 9292 9649 892 1616 2024 C ATOM 2234 C ASP A 289 30.609 22.145 31.281 1.00 71.28 C ANISOU 2234 C ASP A 289 8200 9233 9650 975 1668 1970 C ATOM 2235 O ASP A 289 29.374 22.210 31.264 1.00 69.70 O ANISOU 2235 O ASP A 289 7798 9086 9597 973 1780 2107 O ATOM 2236 CB ASP A 289 31.763 20.989 33.175 1.00 73.77 C ANISOU 2236 CB ASP A 289 8801 9603 9624 1020 1770 2010 C ATOM 2237 CG ASP A 289 31.995 19.646 33.845 1.00 76.45 C ANISOU 2237 CG ASP A 289 9210 9940 9898 955 1791 2155 C ATOM 2238 OD1 ASP A 289 31.453 18.628 33.364 1.00 78.56 O ANISOU 2238 OD1 ASP A 289 9364 10141 10343 813 1751 2303 O ATOM 2239 OD2 ASP A 289 32.736 19.616 34.856 1.00 76.58 O ANISOU 2239 OD2 ASP A 289 9398 10018 9683 1045 1842 2121 O ATOM 2240 N ASP A 290 31.378 23.183 30.952 1.00 70.12 N ANISOU 2240 N ASP A 290 8161 9053 9427 1055 1593 1783 N ATOM 2241 CA ASP A 290 30.771 24.447 30.541 1.00 74.92 C ANISOU 2241 CA ASP A 290 8667 9671 10130 1149 1645 1736 C ATOM 2242 C ASP A 290 29.939 24.282 29.277 1.00 63.70 C ANISOU 2242 C ASP A 290 7034 8223 8948 1045 1536 1833 C ATOM 2243 O ASP A 290 28.852 24.849 29.163 1.00 63.68 O ANISOU 2243 O ASP A 290 6849 8270 9078 1103 1635 1917 O ATOM 2244 CB ASP A 290 31.845 25.509 30.330 1.00 80.97 C ANISOU 2244 CB ASP A 290 9597 10379 10788 1225 1564 1523 C ATOM 2245 CG ASP A 290 32.547 25.880 31.602 1.00 89.46 C ANISOU 2245 CG ASP A 290 10865 11496 11629 1337 1671 1410 C ATOM 2246 OD1 ASP A 290 32.088 25.444 32.678 1.00 97.36 O ANISOU 2246 OD1 ASP A 290 11868 12585 12538 1383 1834 1502 O ATOM 2247 OD2 ASP A 290 33.553 26.614 31.526 1.00 93.50 O ANISOU 2247 OD2 ASP A 290 11523 11958 12044 1373 1591 1232 O ATOM 2248 N TYR A 291 30.442 23.531 28.305 1.00 61.34 N ANISOU 2248 N TYR A 291 6755 7851 8701 898 1329 1818 N ATOM 2249 CA TYR A 291 29.684 23.347 27.075 1.00 61.77 C ANISOU 2249 CA TYR A 291 6622 7891 8959 790 1202 1896 C ATOM 2250 C TYR A 291 28.415 22.526 27.307 1.00 71.60 C ANISOU 2250 C TYR A 291 7657 9192 10354 703 1283 2098 C ATOM 2251 O TYR A 291 27.383 22.786 26.676 1.00 73.17 O ANISOU 2251 O TYR A 291 7639 9434 10729 676 1266 2191 O ATOM 2252 CB TYR A 291 30.562 22.697 26.013 1.00 50.52 C ANISOU 2252 CB TYR A 291 5291 6375 7528 657 970 1813 C ATOM 2253 CG TYR A 291 31.434 23.668 25.259 1.00 50.10 C ANISOU 2253 CG TYR A 291 5341 6280 7416 715 861 1656 C ATOM 2254 CD1 TYR A 291 30.917 24.845 24.724 1.00 49.29 C ANISOU 2254 CD1 TYR A 291 5135 6198 7394 796 872 1653 C ATOM 2255 CD2 TYR A 291 32.779 23.390 25.059 1.00 47.63 C ANISOU 2255 CD2 TYR A 291 5219 5903 6977 688 749 1526 C ATOM 2256 CE1 TYR A 291 31.743 25.738 24.012 1.00 52.11 C ANISOU 2256 CE1 TYR A 291 5590 6504 7704 841 777 1526 C ATOM 2257 CE2 TYR A 291 33.602 24.258 24.373 1.00 49.19 C ANISOU 2257 CE2 TYR A 291 5499 6063 7127 730 660 1397 C ATOM 2258 CZ TYR A 291 33.088 25.428 23.842 1.00 53.81 C ANISOU 2258 CZ TYR A 291 5992 6661 7792 800 673 1399 C ATOM 2259 OH TYR A 291 33.950 26.266 23.161 1.00 50.73 O ANISOU 2259 OH TYR A 291 5692 6223 7359 832 589 1284 O ATOM 2260 N LEU A 292 28.472 21.519 28.186 1.00 70.39 N ANISOU 2260 N LEU A 292 7558 9043 10146 652 1367 2180 N ATOM 2261 CA LEU A 292 27.275 20.730 28.465 1.00 67.40 C ANISOU 2261 CA LEU A 292 6974 8713 9921 558 1461 2387 C ATOM 2262 C LEU A 292 26.193 21.591 29.107 1.00 68.59 C ANISOU 2262 C LEU A 292 6951 8986 10124 698 1684 2484 C ATOM 2263 O LEU A 292 25.019 21.503 28.738 1.00 68.58 O ANISOU 2263 O LEU A 292 6694 9041 10323 639 1705 2629 O ATOM 2264 CB LEU A 292 27.634 19.535 29.342 1.00 69.82 C ANISOU 2264 CB LEU A 292 7394 8988 10145 491 1522 2466 C ATOM 2265 CG LEU A 292 28.456 18.461 28.619 1.00 71.86 C ANISOU 2265 CG LEU A 292 7777 9111 10416 334 1308 2410 C ATOM 2266 CD1 LEU A 292 28.760 17.318 29.551 1.00 72.58 C ANISOU 2266 CD1 LEU A 292 7976 9163 10439 289 1386 2513 C ATOM 2267 CD2 LEU A 292 27.697 17.927 27.405 1.00 75.45 C ANISOU 2267 CD2 LEU A 292 8049 9517 11100 149 1145 2466 C ATOM 2268 N ARG A 293 26.584 22.462 30.036 1.00 68.73 N ANISOU 2268 N ARG A 293 7102 9048 9964 887 1846 2396 N ATOM 2269 CA ARG A 293 25.683 23.474 30.580 1.00 70.91 C ANISOU 2269 CA ARG A 293 7247 9424 10273 1057 2062 2442 C ATOM 2270 C ARG A 293 25.146 24.381 29.473 1.00 73.32 C ANISOU 2270 C ARG A 293 7386 9720 10750 1089 1968 2424 C ATOM 2271 O ARG A 293 23.937 24.422 29.216 1.00 78.24 O ANISOU 2271 O ARG A 293 7744 10417 11569 1079 2025 2580 O ATOM 2272 CB ARG A 293 26.450 24.278 31.636 1.00 79.81 C ANISOU 2272 CB ARG A 293 8605 10568 11150 1244 2204 2290 C ATOM 2273 CG ARG A 293 25.704 25.391 32.340 1.00 92.28 C ANISOU 2273 CG ARG A 293 10114 12231 12717 1452 2449 2291 C ATOM 2274 CD ARG A 293 26.417 25.775 33.641 1.00 99.36 C ANISOU 2274 CD ARG A 293 11258 13163 13331 1596 2603 2162 C ATOM 2275 NE ARG A 293 26.125 27.150 34.050 1.00108.00 N ANISOU 2275 NE ARG A 293 12373 14276 14385 1809 2771 2053 N ATOM 2276 CZ ARG A 293 25.143 27.514 34.872 1.00112.57 C ANISOU 2276 CZ ARG A 293 12844 14961 14966 1957 3043 2141 C ATOM 2277 NH1 ARG A 293 24.327 26.604 35.393 1.00116.51 N ANISOU 2277 NH1 ARG A 293 13190 15572 15507 1906 3185 2357 N ATOM 2278 NH2 ARG A 293 24.975 28.797 35.168 1.00109.87 N ANISOU 2278 NH2 ARG A 293 12546 14606 14591 2158 3182 2013 N ATOM 2279 N MET A 294 26.052 25.086 28.779 1.00 70.24 N ANISOU 2279 N MET A 294 7145 9244 10297 1122 1815 2247 N ATOM 2280 CA MET A 294 25.678 26.026 27.721 1.00 70.61 C ANISOU 2280 CA MET A 294 7069 9275 10484 1168 1720 2229 C ATOM 2281 C MET A 294 24.721 25.400 26.716 1.00 74.61 C ANISOU 2281 C MET A 294 7315 9820 11213 1015 1585 2388 C ATOM 2282 O MET A 294 23.798 26.064 26.230 1.00 83.19 O ANISOU 2282 O MET A 294 8189 10962 12458 1079 1600 2476 O ATOM 2283 CB MET A 294 26.940 26.543 27.020 1.00 70.16 C ANISOU 2283 CB MET A 294 7224 9111 10324 1168 1543 2037 C ATOM 2284 CG MET A 294 26.683 27.288 25.712 1.00 73.33 C ANISOU 2284 CG MET A 294 7514 9486 10863 1173 1395 2039 C ATOM 2285 SD MET A 294 28.168 27.683 24.751 1.00 79.76 S ANISOU 2285 SD MET A 294 8557 10183 11566 1133 1178 1848 S ATOM 2286 CE MET A 294 29.167 28.543 25.965 1.00 75.90 C ANISOU 2286 CE MET A 294 8322 9639 10879 1291 1337 1668 C ATOM 2287 N LEU A 295 24.926 24.130 26.385 1.00 73.27 N ANISOU 2287 N LEU A 295 7159 9619 11061 813 1443 2424 N ATOM 2288 CA LEU A 295 23.989 23.400 25.533 1.00 69.04 C ANISOU 2288 CA LEU A 295 6381 9118 10731 640 1311 2567 C ATOM 2289 C LEU A 295 22.845 22.870 26.401 1.00 69.17 C ANISOU 2289 C LEU A 295 6186 9231 10864 618 1506 2768 C ATOM 2290 O LEU A 295 21.991 22.120 25.938 1.00 75.66 O ANISOU 2290 O LEU A 295 6791 10089 11869 454 1427 2909 O ATOM 2291 CB LEU A 295 24.702 22.256 24.798 1.00 60.11 C ANISOU 2291 CB LEU A 295 5371 7892 9577 430 1080 2504 C ATOM 2292 CG LEU A 295 25.938 22.688 23.991 1.00 64.86 C ANISOU 2292 CG LEU A 295 6192 8407 10046 450 905 2309 C ATOM 2293 CD1 LEU A 295 26.756 21.487 23.517 1.00 61.57 C ANISOU 2293 CD1 LEU A 295 5928 7889 9576 276 730 2235 C ATOM 2294 CD2 LEU A 295 25.589 23.605 22.816 1.00 58.91 C ANISOU 2294 CD2 LEU A 295 5320 7685 9379 486 774 2299 C TER 2295 LEU A 295 ATOM 2296 N ASP B 7 76.297 6.041 7.118 1.00 74.75 N ANISOU 2296 N ASP B 7 8702 8975 10725 875 2289 -1053 N ATOM 2297 CA ASP B 7 75.920 7.366 7.604 1.00 77.92 C ANISOU 2297 CA ASP B 7 9112 9537 10956 809 2019 -911 C ATOM 2298 C ASP B 7 75.020 8.067 6.571 1.00 74.10 C ANISOU 2298 C ASP B 7 8684 9205 10263 605 1921 -1075 C ATOM 2299 O ASP B 7 75.494 8.770 5.673 1.00 75.28 O ANISOU 2299 O ASP B 7 8795 9549 10258 525 1872 -1108 O ATOM 2300 CB ASP B 7 77.162 8.196 7.932 1.00 87.61 C ANISOU 2300 CB ASP B 7 10233 10925 12130 886 1910 -708 C ATOM 2301 CG ASP B 7 76.846 9.399 8.804 1.00 95.64 C ANISOU 2301 CG ASP B 7 11269 12043 13028 853 1661 -531 C ATOM 2302 OD1 ASP B 7 75.645 9.649 9.056 1.00 82.93 O ANISOU 2302 OD1 ASP B 7 9751 10389 11368 772 1573 -569 O ATOM 2303 OD2 ASP B 7 77.802 10.075 9.251 1.00109.44 O ANISOU 2303 OD2 ASP B 7 12935 13912 14736 904 1564 -358 O ATOM 2304 N PRO B 8 73.712 7.830 6.671 1.00 67.30 N ANISOU 2304 N PRO B 8 7909 8261 9401 519 1902 -1174 N ATOM 2305 CA PRO B 8 72.796 8.411 5.677 1.00 70.16 C ANISOU 2305 CA PRO B 8 8309 8779 9569 330 1811 -1321 C ATOM 2306 C PRO B 8 72.743 9.938 5.712 1.00 65.77 C ANISOU 2306 C PRO B 8 7738 8429 8822 276 1571 -1175 C ATOM 2307 O PRO B 8 72.479 10.557 4.670 1.00 61.25 O ANISOU 2307 O PRO B 8 7165 8039 8068 143 1506 -1260 O ATOM 2308 CB PRO B 8 71.446 7.770 6.042 1.00 70.59 C ANISOU 2308 CB PRO B 8 8441 8682 9700 276 1842 -1421 C ATOM 2309 CG PRO B 8 71.539 7.551 7.543 1.00 65.10 C ANISOU 2309 CG PRO B 8 7756 7810 9169 434 1825 -1227 C ATOM 2310 CD PRO B 8 72.999 7.220 7.812 1.00 65.93 C ANISOU 2310 CD PRO B 8 7791 7878 9382 592 1923 -1113 C ATOM 2311 N ILE B 9 72.998 10.567 6.869 1.00 58.96 N ANISOU 2311 N ILE B 9 6867 7545 7991 370 1444 -956 N ATOM 2312 CA ILE B 9 73.055 12.027 6.926 1.00 55.95 C ANISOU 2312 CA ILE B 9 6479 7338 7443 320 1241 -819 C ATOM 2313 C ILE B 9 74.238 12.538 6.104 1.00 59.13 C ANISOU 2313 C ILE B 9 6812 7912 7744 301 1248 -804 C ATOM 2314 O ILE B 9 74.079 13.360 5.190 1.00 59.48 O ANISOU 2314 O ILE B 9 6859 8128 7612 186 1169 -840 O ATOM 2315 CB ILE B 9 73.112 12.507 8.387 1.00 53.63 C ANISOU 2315 CB ILE B 9 6197 6971 7207 412 1129 -609 C ATOM 2316 CG1 ILE B 9 71.823 12.132 9.114 1.00 48.96 C ANISOU 2316 CG1 ILE B 9 5681 6230 6691 409 1115 -629 C ATOM 2317 CG2 ILE B 9 73.298 14.010 8.432 1.00 46.40 C ANISOU 2317 CG2 ILE B 9 5280 6218 6130 355 948 -478 C ATOM 2318 CD1 ILE B 9 71.951 12.098 10.616 1.00 48.23 C ANISOU 2318 CD1 ILE B 9 5606 6017 6703 522 1076 -454 C ATOM 2319 N ARG B 10 75.442 12.043 6.418 1.00 60.77 N ANISOU 2319 N ARG B 10 6948 8077 8064 419 1348 -741 N ATOM 2320 CA ARG B 10 76.626 12.354 5.618 1.00 65.01 C ANISOU 2320 CA ARG B 10 7405 8766 8530 409 1389 -741 C ATOM 2321 C ARG B 10 76.413 11.990 4.156 1.00 65.13 C ANISOU 2321 C ARG B 10 7434 8857 8455 295 1501 -962 C ATOM 2322 O ARG B 10 76.704 12.791 3.262 1.00 64.31 O ANISOU 2322 O ARG B 10 7312 8941 8180 198 1446 -977 O ATOM 2323 CB ARG B 10 77.838 11.605 6.185 1.00 70.15 C ANISOU 2323 CB ARG B 10 7964 9335 9353 570 1513 -656 C ATOM 2324 CG ARG B 10 79.203 12.163 5.808 1.00 85.72 C ANISOU 2324 CG ARG B 10 9828 11475 11268 586 1510 -574 C ATOM 2325 CD ARG B 10 80.328 11.458 6.588 1.00 94.34 C ANISOU 2325 CD ARG B 10 10810 12493 12543 765 1607 -446 C ATOM 2326 NE ARG B 10 81.437 12.363 6.912 1.00 98.33 N ANISOU 2326 NE ARG B 10 11210 13168 12984 779 1498 -270 N ATOM 2327 CZ ARG B 10 81.583 13.001 8.078 1.00 97.53 C ANISOU 2327 CZ ARG B 10 11092 13094 12871 808 1339 -77 C ATOM 2328 NH1 ARG B 10 80.686 12.849 9.056 1.00 89.69 N ANISOU 2328 NH1 ARG B 10 10183 11968 11926 836 1270 -27 N ATOM 2329 NH2 ARG B 10 82.630 13.804 8.268 1.00 97.71 N ANISOU 2329 NH2 ARG B 10 11014 13285 12826 797 1252 58 N ATOM 2330 N GLU B 11 75.852 10.806 3.900 1.00 70.63 N ANISOU 2330 N GLU B 11 8170 9411 9256 293 1660 -1137 N ATOM 2331 CA GLU B 11 75.594 10.363 2.532 1.00 70.59 C ANISOU 2331 CA GLU B 11 8185 9476 9159 165 1780 -1373 C ATOM 2332 C GLU B 11 74.776 11.384 1.744 1.00 62.36 C ANISOU 2332 C GLU B 11 7181 8638 7877 -4 1616 -1407 C ATOM 2333 O GLU B 11 75.137 11.733 0.615 1.00 69.51 O ANISOU 2333 O GLU B 11 8066 9720 8624 -102 1634 -1487 O ATOM 2334 CB GLU B 11 74.903 8.998 2.559 1.00 91.45 C ANISOU 2334 CB GLU B 11 10883 11913 11952 167 1959 -1555 C ATOM 2335 CG GLU B 11 74.494 8.457 1.193 1.00109.94 C ANISOU 2335 CG GLU B 11 13259 14321 14193 7 2090 -1829 C ATOM 2336 CD GLU B 11 74.046 6.998 1.250 1.00126.46 C ANISOU 2336 CD GLU B 11 15403 16180 16465 15 2314 -2019 C ATOM 2337 OE1 GLU B 11 73.012 6.663 0.627 1.00131.05 O ANISOU 2337 OE1 GLU B 11 16042 16782 16967 -145 2338 -2217 O ATOM 2338 OE2 GLU B 11 74.716 6.191 1.936 1.00132.21 O ANISOU 2338 OE2 GLU B 11 16111 16706 17417 180 2467 -1963 O ATOM 2339 N TRP B 12 73.655 11.862 2.312 1.00 58.84 N ANISOU 2339 N TRP B 12 6786 8172 7400 -37 1462 -1342 N ATOM 2340 CA TRP B 12 72.810 12.816 1.593 1.00 53.36 C ANISOU 2340 CA TRP B 12 6117 7667 6492 -181 1307 -1353 C ATOM 2341 C TRP B 12 73.545 14.135 1.363 1.00 58.94 C ANISOU 2341 C TRP B 12 6791 8551 7054 -191 1179 -1191 C ATOM 2342 O TRP B 12 73.553 14.672 0.247 1.00 63.02 O ANISOU 2342 O TRP B 12 7300 9260 7383 -304 1147 -1239 O ATOM 2343 CB TRP B 12 71.491 13.066 2.353 1.00 48.80 C ANISOU 2343 CB TRP B 12 5587 7016 5937 -191 1179 -1296 C ATOM 2344 CG TRP B 12 70.561 13.983 1.562 1.00 56.28 C ANISOU 2344 CG TRP B 12 6545 8163 6676 -327 1030 -1300 C ATOM 2345 CD1 TRP B 12 69.602 13.595 0.672 1.00 59.30 C ANISOU 2345 CD1 TRP B 12 6936 8636 6960 -462 1046 -1473 C ATOM 2346 CD2 TRP B 12 70.536 15.424 1.566 1.00 54.19 C ANISOU 2346 CD2 TRP B 12 6280 8037 6275 -340 852 -1117 C ATOM 2347 NE1 TRP B 12 68.986 14.691 0.120 1.00 57.26 N ANISOU 2347 NE1 TRP B 12 6669 8577 6512 -546 881 -1393 N ATOM 2348 CE2 TRP B 12 69.550 15.826 0.638 1.00 55.18 C ANISOU 2348 CE2 TRP B 12 6405 8333 6228 -469 769 -1174 C ATOM 2349 CE3 TRP B 12 71.271 16.408 2.238 1.00 54.60 C ANISOU 2349 CE3 TRP B 12 6327 8087 6330 -264 763 -914 C ATOM 2350 CZ2 TRP B 12 69.267 17.167 0.379 1.00 50.95 C ANISOU 2350 CZ2 TRP B 12 5870 7948 5541 -502 607 -1018 C ATOM 2351 CZ3 TRP B 12 70.987 17.736 1.986 1.00 48.37 C ANISOU 2351 CZ3 TRP B 12 5551 7434 5393 -313 613 -780 C ATOM 2352 CH2 TRP B 12 69.990 18.106 1.064 1.00 53.06 C ANISOU 2352 CH2 TRP B 12 6149 8181 5833 -421 540 -824 C ATOM 2353 N ILE B 13 74.200 14.649 2.409 1.00 56.39 N ANISOU 2353 N ILE B 13 6448 8167 6812 -81 1112 -998 N ATOM 2354 CA ILE B 13 74.885 15.938 2.345 1.00 59.19 C ANISOU 2354 CA ILE B 13 6778 8666 7045 -98 992 -837 C ATOM 2355 C ILE B 13 75.993 15.954 1.299 1.00 58.53 C ANISOU 2355 C ILE B 13 6636 8726 6878 -136 1087 -894 C ATOM 2356 O ILE B 13 76.208 16.978 0.640 1.00 56.40 O ANISOU 2356 O ILE B 13 6363 8628 6439 -219 1004 -834 O ATOM 2357 CB ILE B 13 75.426 16.292 3.748 1.00 56.97 C ANISOU 2357 CB ILE B 13 6482 8283 6881 17 926 -646 C ATOM 2358 CG1 ILE B 13 74.248 16.571 4.691 1.00 52.21 C ANISOU 2358 CG1 ILE B 13 5950 7572 6315 29 813 -578 C ATOM 2359 CG2 ILE B 13 76.401 17.478 3.678 1.00 45.21 C ANISOU 2359 CG2 ILE B 13 4956 6935 5288 -8 841 -501 C ATOM 2360 CD1 ILE B 13 74.633 17.203 5.997 1.00 55.67 C ANISOU 2360 CD1 ILE B 13 6393 7949 6811 101 718 -388 C ATOM 2361 N LEU B 14 76.644 14.812 1.050 1.00 63.03 N ANISOU 2361 N LEU B 14 7163 9227 7560 -84 1274 -1019 N ATOM 2362 CA LEU B 14 77.750 14.780 0.093 1.00 66.12 C ANISOU 2362 CA LEU B 14 7491 9746 7885 -111 1386 -1077 C ATOM 2363 C LEU B 14 77.321 14.398 -1.312 1.00 73.79 C ANISOU 2363 C LEU B 14 8492 10828 8715 -247 1478 -1291 C ATOM 2364 O LEU B 14 78.106 14.575 -2.250 1.00 78.73 O ANISOU 2364 O LEU B 14 9080 11598 9236 -302 1551 -1340 O ATOM 2365 CB LEU B 14 78.841 13.810 0.554 1.00 64.92 C ANISOU 2365 CB LEU B 14 7262 9470 7935 32 1557 -1080 C ATOM 2366 CG LEU B 14 79.362 14.043 1.969 1.00 66.02 C ANISOU 2366 CG LEU B 14 7354 9518 8213 169 1476 -868 C ATOM 2367 CD1 LEU B 14 80.333 12.958 2.344 1.00 63.72 C ANISOU 2367 CD1 LEU B 14 6976 9109 8125 320 1656 -870 C ATOM 2368 CD2 LEU B 14 80.026 15.426 2.059 1.00 61.00 C ANISOU 2368 CD2 LEU B 14 6680 9049 7448 126 1325 -695 C ATOM 2369 N THR B 15 76.142 13.804 -1.477 1.00 79.11 N ANISOU 2369 N THR B 15 9229 11443 9387 -309 1490 -1431 N ATOM 2370 CA THR B 15 75.582 13.642 -2.812 1.00 72.89 C ANISOU 2370 CA THR B 15 8472 10807 8417 -473 1533 -1622 C ATOM 2371 C THR B 15 74.629 14.786 -3.151 1.00 64.40 C ANISOU 2371 C THR B 15 7430 9904 7136 -582 1320 -1532 C ATOM 2372 O THR B 15 74.984 15.723 -3.871 1.00 64.82 O ANISOU 2372 O THR B 15 7469 10152 7007 -651 1249 -1460 O ATOM 2373 CB THR B 15 74.865 12.296 -2.936 1.00 73.28 C ANISOU 2373 CB THR B 15 8561 10717 8566 -505 1684 -1850 C ATOM 2374 OG1 THR B 15 73.763 12.257 -2.022 1.00 72.88 O ANISOU 2374 OG1 THR B 15 8549 10542 8599 -477 1575 -1794 O ATOM 2375 CG2 THR B 15 75.821 11.151 -2.613 1.00 66.08 C ANISOU 2375 CG2 THR B 15 7618 9613 7876 -380 1916 -1925 C ATOM 2376 N GLU B 16 73.410 14.704 -2.671 1.00 71.06 N ANISOU 2376 N GLU B 16 8312 10679 8010 -596 1229 -1533 N ATOM 2377 CA GLU B 16 72.366 15.691 -2.955 1.00 71.54 C ANISOU 2377 CA GLU B 16 8394 10890 7900 -684 1038 -1446 C ATOM 2378 C GLU B 16 72.494 17.094 -2.410 1.00 69.57 C ANISOU 2378 C GLU B 16 8146 10681 7606 -632 864 -1190 C ATOM 2379 O GLU B 16 72.013 18.013 -3.011 1.00 68.02 O ANISOU 2379 O GLU B 16 7956 10653 7233 -709 742 -1113 O ATOM 2380 CB GLU B 16 71.014 15.161 -2.554 1.00 77.87 C ANISOU 2380 CB GLU B 16 9223 11601 8764 -709 1002 -1521 C ATOM 2381 CG GLU B 16 70.533 13.965 -3.333 1.00 89.74 C ANISOU 2381 CG GLU B 16 10734 13118 10245 -824 1144 -1792 C ATOM 2382 CD GLU B 16 70.462 14.248 -4.795 1.00112.19 C ANISOU 2382 CD GLU B 16 13564 16232 12829 -989 1133 -1893 C ATOM 2383 OE1 GLU B 16 70.045 15.352 -5.153 1.00119.39 O ANISOU 2383 OE1 GLU B 16 14464 17330 13569 -1036 961 -1751 O ATOM 2384 OE2 GLU B 16 70.830 13.365 -5.583 1.00119.79 O ANISOU 2384 OE2 GLU B 16 14532 17222 13762 -1071 1305 -2111 O ATOM 2385 N GLY B 17 73.105 17.256 -1.261 1.00 65.03 N ANISOU 2385 N GLY B 17 7567 9951 7190 -504 854 -1057 N ATOM 2386 CA GLY B 17 73.322 18.579 -0.706 1.00 63.19 C ANISOU 2386 CA GLY B 17 7344 9743 6921 -468 710 -830 C ATOM 2387 C GLY B 17 74.398 19.363 -1.411 1.00 73.37 C ANISOU 2387 C GLY B 17 8606 11190 8082 -509 713 -760 C ATOM 2388 O GLY B 17 74.598 20.539 -1.084 1.00 71.09 O ANISOU 2388 O GLY B 17 8333 10933 7746 -503 604 -580 O ATOM 2389 N LYS B 18 75.082 18.705 -2.367 1.00 75.68 N ANISOU 2389 N LYS B 18 8861 11570 8322 -557 852 -908 N ATOM 2390 CA LYS B 18 76.110 19.281 -3.241 1.00 77.81 C ANISOU 2390 CA LYS B 18 9099 12009 8456 -614 888 -878 C ATOM 2391 C LYS B 18 77.370 19.704 -2.488 1.00 75.11 C ANISOU 2391 C LYS B 18 8710 11611 8216 -528 899 -738 C ATOM 2392 O LYS B 18 78.089 20.604 -2.921 1.00 68.02 O ANISOU 2392 O LYS B 18 7795 10841 7207 -575 872 -641 O ATOM 2393 CB LYS B 18 75.549 20.465 -4.035 1.00 76.38 C ANISOU 2393 CB LYS B 18 8953 12017 8053 -720 755 -780 C ATOM 2394 CG LYS B 18 74.420 20.089 -4.975 1.00 79.11 C ANISOU 2394 CG LYS B 18 9320 12483 8256 -826 739 -914 C ATOM 2395 CD LYS B 18 73.499 21.285 -5.168 1.00 89.83 C ANISOU 2395 CD LYS B 18 10710 13951 9472 -870 561 -748 C ATOM 2396 CE LYS B 18 72.936 21.372 -6.571 1.00 99.02 C ANISOU 2396 CE LYS B 18 11869 15362 10391 -1009 539 -820 C ATOM 2397 NZ LYS B 18 72.405 22.736 -6.835 1.00100.72 N ANISOU 2397 NZ LYS B 18 12105 15700 10463 -1032 381 -603 N ATOM 2398 N ALA B 19 77.683 19.033 -1.386 1.00 72.09 N ANISOU 2398 N ALA B 19 8301 11050 8039 -408 944 -726 N ATOM 2399 CA ALA B 19 78.878 19.336 -0.621 1.00 62.82 C ANISOU 2399 CA ALA B 19 7065 9843 6961 -329 950 -595 C ATOM 2400 C ALA B 19 79.931 18.269 -0.880 1.00 65.91 C ANISOU 2400 C ALA B 19 7369 10215 7458 -266 1138 -703 C ATOM 2401 O ALA B 19 79.622 17.147 -1.279 1.00 69.34 O ANISOU 2401 O ALA B 19 7810 10586 7950 -254 1270 -877 O ATOM 2402 CB ALA B 19 78.562 19.406 0.875 1.00 55.12 C ANISOU 2402 CB ALA B 19 6110 8701 6133 -233 860 -475 C ATOM 2403 N THR B 20 81.186 18.612 -0.607 1.00 62.14 N ANISOU 2403 N THR B 20 6807 9785 7018 -226 1159 -599 N ATOM 2404 CA THR B 20 82.270 17.641 -0.674 1.00 65.33 C ANISOU 2404 CA THR B 20 7107 10162 7555 -135 1337 -663 C ATOM 2405 C THR B 20 82.950 17.434 0.665 1.00 65.31 C ANISOU 2405 C THR B 20 7025 10055 7735 3 1318 -521 C ATOM 2406 O THR B 20 83.641 16.423 0.838 1.00 61.98 O ANISOU 2406 O THR B 20 6518 9562 7471 117 1466 -560 O ATOM 2407 CB THR B 20 83.341 18.039 -1.717 1.00 69.15 C ANISOU 2407 CB THR B 20 7520 10829 7923 -206 1420 -682 C ATOM 2408 OG1 THR B 20 83.940 19.289 -1.352 1.00 71.52 O ANISOU 2408 OG1 THR B 20 7791 11230 8154 -246 1291 -498 O ATOM 2409 CG2 THR B 20 82.745 18.165 -3.113 1.00 69.42 C ANISOU 2409 CG2 THR B 20 7626 10990 7758 -347 1453 -826 C ATOM 2410 N GLN B 21 82.790 18.356 1.611 1.00 67.30 N ANISOU 2410 N GLN B 21 7302 10299 7969 -5 1146 -354 N ATOM 2411 CA GLN B 21 83.360 18.141 2.929 1.00 64.95 C ANISOU 2411 CA GLN B 21 6933 9921 7825 113 1115 -219 C ATOM 2412 C GLN B 21 82.501 18.777 4.014 1.00 61.00 C ANISOU 2412 C GLN B 21 6524 9337 7318 102 945 -109 C ATOM 2413 O GLN B 21 81.898 19.837 3.818 1.00 59.50 O ANISOU 2413 O GLN B 21 6421 9198 6990 -6 827 -74 O ATOM 2414 CB GLN B 21 84.810 18.635 2.945 1.00 70.88 C ANISOU 2414 CB GLN B 21 7551 10816 8566 112 1126 -112 C ATOM 2415 CG GLN B 21 84.985 20.115 2.741 1.00 87.90 C ANISOU 2415 CG GLN B 21 9737 13111 10550 -30 996 -18 C ATOM 2416 CD GLN B 21 86.433 20.523 2.888 1.00102.00 C ANISOU 2416 CD GLN B 21 11377 15034 12343 -35 1009 87 C ATOM 2417 OE1 GLN B 21 87.328 19.667 2.921 1.00103.69 O ANISOU 2417 OE1 GLN B 21 11456 15261 12680 70 1131 77 O ATOM 2418 NE2 GLN B 21 86.677 21.833 2.981 1.00105.94 N ANISOU 2418 NE2 GLN B 21 11900 15634 12719 -159 893 190 N ATOM 2419 N ILE B 22 82.431 18.086 5.145 1.00 58.68 N ANISOU 2419 N ILE B 22 6210 8908 7177 222 946 -53 N ATOM 2420 CA ILE B 22 81.774 18.561 6.356 1.00 51.08 C ANISOU 2420 CA ILE B 22 5319 7860 6229 228 804 58 C ATOM 2421 C ILE B 22 82.865 19.112 7.270 1.00 52.51 C ANISOU 2421 C ILE B 22 5407 8121 6422 245 731 227 C ATOM 2422 O ILE B 22 83.766 18.373 7.670 1.00 50.48 O ANISOU 2422 O ILE B 22 5027 7869 6283 355 803 276 O ATOM 2423 CB ILE B 22 80.982 17.428 7.026 1.00 50.48 C ANISOU 2423 CB ILE B 22 5285 7594 6303 338 857 14 C ATOM 2424 CG1 ILE B 22 79.925 16.900 6.042 1.00 49.44 C ANISOU 2424 CG1 ILE B 22 5236 7406 6145 292 932 -171 C ATOM 2425 CG2 ILE B 22 80.360 17.906 8.351 1.00 48.10 C ANISOU 2425 CG2 ILE B 22 5054 7208 6013 346 720 135 C ATOM 2426 CD1 ILE B 22 79.149 15.710 6.530 1.00 55.46 C ANISOU 2426 CD1 ILE B 22 6039 7976 7057 381 1013 -243 C ATOM 2427 N THR B 23 82.836 20.427 7.536 1.00 49.94 N ANISOU 2427 N THR B 23 5132 7870 5972 131 596 315 N ATOM 2428 CA THR B 23 83.889 21.104 8.287 1.00 53.03 C ANISOU 2428 CA THR B 23 5439 8368 6343 101 522 457 C ATOM 2429 C THR B 23 83.572 21.312 9.770 1.00 59.33 C ANISOU 2429 C THR B 23 6280 9090 7174 122 411 568 C ATOM 2430 O THR B 23 84.496 21.540 10.556 1.00 63.67 O ANISOU 2430 O THR B 23 6734 9728 7730 120 361 683 O ATOM 2431 CB THR B 23 84.236 22.446 7.629 1.00 50.51 C ANISOU 2431 CB THR B 23 5143 8184 5864 -57 467 480 C ATOM 2432 OG1 THR B 23 83.095 23.311 7.657 1.00 54.56 O ANISOU 2432 OG1 THR B 23 5816 8625 6288 -142 379 477 O ATOM 2433 CG2 THR B 23 84.681 22.229 6.201 1.00 51.24 C ANISOU 2433 CG2 THR B 23 5182 8374 5912 -80 580 382 C ATOM 2434 N LYS B 24 82.309 21.244 10.180 1.00 58.61 N ANISOU 2434 N LYS B 24 6321 8851 7096 133 373 537 N ATOM 2435 CA LYS B 24 81.990 21.392 11.592 1.00 56.69 C ANISOU 2435 CA LYS B 24 6125 8535 6881 151 283 634 C ATOM 2436 C LYS B 24 80.620 20.789 11.876 1.00 56.28 C ANISOU 2436 C LYS B 24 6186 8301 6895 212 299 571 C ATOM 2437 O LYS B 24 79.710 20.853 11.043 1.00 61.33 O ANISOU 2437 O LYS B 24 6908 8893 7504 178 323 468 O ATOM 2438 CB LYS B 24 82.015 22.865 12.023 1.00 49.03 C ANISOU 2438 CB LYS B 24 5227 7624 5780 4 165 707 C ATOM 2439 CG LYS B 24 82.070 23.037 13.519 1.00 57.43 C ANISOU 2439 CG LYS B 24 6307 8661 6854 4 80 813 C ATOM 2440 CD LYS B 24 81.988 24.485 13.887 1.00 64.02 C ANISOU 2440 CD LYS B 24 7236 9527 7563 -155 -12 855 C ATOM 2441 CE LYS B 24 81.835 24.653 15.367 1.00 63.69 C ANISOU 2441 CE LYS B 24 7240 9445 7516 -170 -87 934 C ATOM 2442 NZ LYS B 24 81.441 26.061 15.656 1.00 66.75 N ANISOU 2442 NZ LYS B 24 7762 9806 7792 -326 -149 943 N ATOM 2443 N ILE B 25 80.487 20.229 13.080 1.00 53.40 N ANISOU 2443 N ILE B 25 5822 7851 6615 295 280 643 N ATOM 2444 CA ILE B 25 79.228 19.693 13.600 1.00 52.89 C ANISOU 2444 CA ILE B 25 5865 7612 6620 348 290 605 C ATOM 2445 C ILE B 25 79.081 20.182 15.035 1.00 47.88 C ANISOU 2445 C ILE B 25 5283 6950 5960 328 190 722 C ATOM 2446 O ILE B 25 79.933 19.881 15.878 1.00 52.08 O ANISOU 2446 O ILE B 25 5728 7539 6521 378 170 832 O ATOM 2447 CB ILE B 25 79.181 18.162 13.559 1.00 50.18 C ANISOU 2447 CB ILE B 25 5468 7163 6435 494 416 558 C ATOM 2448 CG1 ILE B 25 79.266 17.645 12.129 1.00 49.61 C ANISOU 2448 CG1 ILE B 25 5358 7111 6381 498 533 416 C ATOM 2449 CG2 ILE B 25 77.889 17.664 14.178 1.00 45.44 C ANISOU 2449 CG2 ILE B 25 4978 6383 5902 533 425 526 C ATOM 2450 CD1 ILE B 25 79.198 16.127 12.031 1.00 47.14 C ANISOU 2450 CD1 ILE B 25 5008 6669 6235 631 685 349 C ATOM 2451 N GLY B 26 78.060 20.999 15.290 1.00 46.27 N ANISOU 2451 N GLY B 26 5214 6676 5691 247 128 705 N ATOM 2452 CA GLY B 26 77.715 21.452 16.635 1.00 44.34 C ANISOU 2452 CA GLY B 26 5047 6380 5419 218 52 789 C ATOM 2453 C GLY B 26 76.355 20.904 17.044 1.00 51.43 C ANISOU 2453 C GLY B 26 6047 7101 6392 275 82 742 C ATOM 2454 O GLY B 26 75.377 21.065 16.308 1.00 47.08 O ANISOU 2454 O GLY B 26 5563 6485 5840 251 103 649 O ATOM 2455 N SER B 27 76.305 20.262 18.228 1.00 48.05 N ANISOU 2455 N SER B 27 5622 6607 6025 346 82 815 N ATOM 2456 CA SER B 27 75.136 19.492 18.678 1.00 53.04 C ANISOU 2456 CA SER B 27 6332 7068 6753 417 133 778 C ATOM 2457 C SER B 27 74.664 19.925 20.059 1.00 50.64 C ANISOU 2457 C SER B 27 6123 6709 6409 385 74 857 C ATOM 2458 O SER B 27 75.469 20.028 20.996 1.00 44.83 O ANISOU 2458 O SER B 27 5350 6054 5628 379 23 969 O ATOM 2459 CB SER B 27 75.444 17.993 18.726 1.00 50.05 C ANISOU 2459 CB SER B 27 5871 6629 6517 560 232 785 C ATOM 2460 OG SER B 27 75.651 17.507 17.420 1.00 54.00 O ANISOU 2460 OG SER B 27 6309 7147 7063 584 314 679 O ATOM 2461 N VAL B 28 73.345 20.102 20.195 1.00 47.78 N ANISOU 2461 N VAL B 28 5873 6215 6064 365 87 797 N ATOM 2462 CA VAL B 28 72.692 20.373 21.470 1.00 49.34 C ANISOU 2462 CA VAL B 28 6174 6331 6242 344 61 850 C ATOM 2463 C VAL B 28 71.541 19.380 21.651 1.00 56.29 C ANISOU 2463 C VAL B 28 7098 7044 7244 426 141 799 C ATOM 2464 O VAL B 28 71.185 18.628 20.740 1.00 52.54 O ANISOU 2464 O VAL B 28 6585 6520 6857 478 210 709 O ATOM 2465 CB VAL B 28 72.171 21.821 21.559 1.00 44.66 C ANISOU 2465 CB VAL B 28 5688 5737 5544 221 5 834 C ATOM 2466 CG1 VAL B 28 73.305 22.803 21.362 1.00 39.23 C ANISOU 2466 CG1 VAL B 28 4962 5202 4740 123 -60 876 C ATOM 2467 CG2 VAL B 28 71.081 22.045 20.509 1.00 44.09 C ANISOU 2467 CG2 VAL B 28 5652 5592 5506 214 38 731 C ATOM 2468 N GLY B 29 70.979 19.357 22.863 1.00 53.44 N ANISOU 2468 N GLY B 29 6821 6601 6884 428 138 852 N ATOM 2469 CA GLY B 29 69.836 18.488 23.115 1.00 45.41 C ANISOU 2469 CA GLY B 29 5852 5422 5979 492 218 806 C ATOM 2470 C GLY B 29 70.256 17.071 23.459 1.00 48.26 C ANISOU 2470 C GLY B 29 6151 5733 6452 612 291 857 C ATOM 2471 O GLY B 29 71.346 16.833 23.965 1.00 54.11 O ANISOU 2471 O GLY B 29 6827 6561 7170 653 264 969 O ATOM 2472 N GLY B 30 69.380 16.117 23.167 1.00 50.54 N ANISOU 2472 N GLY B 30 6454 5880 6868 668 389 777 N ATOM 2473 CA GLY B 30 69.717 14.725 23.399 1.00 51.53 C ANISOU 2473 CA GLY B 30 6530 5925 7122 787 486 818 C ATOM 2474 C GLY B 30 69.566 14.216 24.827 1.00 57.33 C ANISOU 2474 C GLY B 30 7316 6582 7885 844 507 945 C ATOM 2475 O GLY B 30 69.801 13.026 25.064 1.00 68.07 O ANISOU 2475 O GLY B 30 8642 7857 9365 954 600 996 O ATOM 2476 N GLY B 31 69.205 15.058 25.794 1.00 58.73 N ANISOU 2476 N GLY B 31 7578 6782 7955 773 434 1002 N ATOM 2477 CA GLY B 31 69.044 14.568 27.151 1.00 64.62 C ANISOU 2477 CA GLY B 31 8377 7465 8709 817 456 1123 C ATOM 2478 C GLY B 31 67.869 13.614 27.269 1.00 70.11 C ANISOU 2478 C GLY B 31 9132 7962 9547 866 580 1063 C ATOM 2479 O GLY B 31 66.990 13.555 26.411 1.00 70.54 O ANISOU 2479 O GLY B 31 9199 7935 9668 835 630 916 O ATOM 2480 N CYS B 32 67.818 12.879 28.378 1.00 71.80 N ANISOU 2480 N CYS B 32 9380 8103 9798 933 628 1184 N ATOM 2481 CA CYS B 32 66.714 11.956 28.605 1.00 73.59 C ANISOU 2481 CA CYS B 32 9669 8132 10161 971 756 1138 C ATOM 2482 C CYS B 32 65.775 12.478 29.682 1.00 66.81 C ANISOU 2482 C CYS B 32 8927 7226 9231 903 743 1161 C ATOM 2483 O CYS B 32 66.204 13.091 30.661 1.00 67.90 O ANISOU 2483 O CYS B 32 9102 7464 9232 869 663 1276 O ATOM 2484 CB CYS B 32 67.225 10.555 28.940 1.00 89.46 C ANISOU 2484 CB CYS B 32 11637 10050 12303 1111 862 1248 C ATOM 2485 SG CYS B 32 68.290 9.884 27.599 1.00110.14 S ANISOU 2485 SG CYS B 32 14118 12700 15030 1198 914 1200 S ATOM 2486 N ILE B 33 64.485 12.220 29.474 1.00 65.23 N ANISOU 2486 N ILE B 33 8780 6880 9123 875 828 1044 N ATOM 2487 CA ILE B 33 63.428 12.731 30.331 1.00 59.15 C ANISOU 2487 CA ILE B 33 8117 6051 8308 809 837 1037 C ATOM 2488 C ILE B 33 63.306 11.855 31.577 1.00 58.49 C ANISOU 2488 C ILE B 33 8092 5873 8260 870 916 1168 C ATOM 2489 O ILE B 33 63.664 10.680 31.577 1.00 56.52 O ANISOU 2489 O ILE B 33 7804 5545 8125 969 999 1230 O ATOM 2490 CB ILE B 33 62.114 12.749 29.527 1.00 52.64 C ANISOU 2490 CB ILE B 33 7298 5125 7577 759 899 864 C ATOM 2491 CG1 ILE B 33 62.220 13.757 28.395 1.00 68.28 C ANISOU 2491 CG1 ILE B 33 9229 7221 9495 696 808 764 C ATOM 2492 CG2 ILE B 33 60.922 13.029 30.390 1.00 61.42 C ANISOU 2492 CG2 ILE B 33 8505 6146 8685 711 944 855 C ATOM 2493 CD1 ILE B 33 61.082 13.671 27.378 1.00 78.59 C ANISOU 2493 CD1 ILE B 33 10504 8467 10889 656 854 602 C ATOM 2494 N ASN B 34 62.772 12.432 32.651 1.00 60.09 N ANISOU 2494 N ASN B 34 8392 6073 8366 810 902 1214 N ATOM 2495 CA ASN B 34 62.622 11.677 33.885 1.00 57.79 C ANISOU 2495 CA ASN B 34 8166 5706 8085 857 974 1348 C ATOM 2496 C ASN B 34 61.632 10.546 33.676 1.00 58.05 C ANISOU 2496 C ASN B 34 8213 5534 8309 902 1130 1283 C ATOM 2497 O ASN B 34 60.679 10.673 32.901 1.00 60.73 O ANISOU 2497 O ASN B 34 8544 5799 8730 852 1172 1119 O ATOM 2498 CB ASN B 34 62.152 12.572 35.026 1.00 59.94 C ANISOU 2498 CB ASN B 34 8550 6017 8207 765 942 1383 C ATOM 2499 CG ASN B 34 63.260 13.432 35.588 1.00 63.29 C ANISOU 2499 CG ASN B 34 8976 6641 8432 717 808 1486 C ATOM 2500 OD1 ASN B 34 64.440 13.162 35.380 1.00 64.98 O ANISOU 2500 OD1 ASN B 34 9101 6968 8620 774 743 1579 O ATOM 2501 ND2 ASN B 34 62.882 14.466 36.317 1.00 62.65 N ANISOU 2501 ND2 ASN B 34 8992 6603 8207 607 776 1466 N ATOM 2502 N LEU B 35 61.908 9.406 34.302 1.00 49.76 N ANISOU 2502 N LEU B 35 7172 4399 7336 997 1218 1415 N ATOM 2503 CA LEU B 35 60.918 8.352 34.429 1.00 52.65 C ANISOU 2503 CA LEU B 35 7581 4556 7869 1023 1382 1377 C ATOM 2504 C LEU B 35 60.070 8.641 35.659 1.00 59.77 C ANISOU 2504 C LEU B 35 8597 5418 8697 966 1415 1429 C ATOM 2505 O LEU B 35 60.613 8.831 36.755 1.00 57.31 O ANISOU 2505 O LEU B 35 8333 5193 8249 979 1366 1595 O ATOM 2506 CB LEU B 35 61.608 6.990 34.548 1.00 55.08 C ANISOU 2506 CB LEU B 35 7855 4768 8304 1159 1482 1507 C ATOM 2507 CG LEU B 35 60.810 5.695 34.410 1.00 57.04 C ANISOU 2507 CG LEU B 35 8131 4775 8764 1197 1678 1456 C ATOM 2508 CD1 LEU B 35 60.332 5.549 33.000 1.00 60.45 C ANISOU 2508 CD1 LEU B 35 8505 5146 9318 1147 1723 1226 C ATOM 2509 CD2 LEU B 35 61.691 4.522 34.764 1.00 53.42 C ANISOU 2509 CD2 LEU B 35 7651 4240 8405 1348 1767 1640 C ATOM 2510 N ALA B 36 58.748 8.648 35.480 1.00 57.01 N ANISOU 2510 N ALA B 36 8284 4947 8431 899 1501 1288 N ATOM 2511 CA ALA B 36 57.792 8.897 36.552 1.00 55.05 C ANISOU 2511 CA ALA B 36 8140 4641 8135 840 1559 1311 C ATOM 2512 C ALA B 36 57.009 7.621 36.857 1.00 58.45 C ANISOU 2512 C ALA B 36 8605 4867 8735 874 1738 1321 C ATOM 2513 O ALA B 36 56.403 7.032 35.957 1.00 62.21 O ANISOU 2513 O ALA B 36 9033 5230 9376 864 1823 1180 O ATOM 2514 CB ALA B 36 56.825 10.019 36.154 1.00 54.51 C ANISOU 2514 CB ALA B 36 8079 4602 8032 735 1524 1149 C ATOM 2515 N SER B 37 56.996 7.205 38.123 1.00 56.85 N ANISOU 2515 N SER B 37 8492 4622 8488 902 1799 1482 N ATOM 2516 CA SER B 37 56.474 5.893 38.487 1.00 57.66 C ANISOU 2516 CA SER B 37 8633 4526 8751 950 1977 1532 C ATOM 2517 C SER B 37 55.539 5.951 39.688 1.00 60.26 C ANISOU 2517 C SER B 37 9075 4791 9032 894 2064 1582 C ATOM 2518 O SER B 37 55.815 6.629 40.682 1.00 61.67 O ANISOU 2518 O SER B 37 9322 5089 9022 869 1993 1694 O ATOM 2519 CB SER B 37 57.606 4.904 38.802 1.00 60.45 C ANISOU 2519 CB SER B 37 8972 4858 9139 1086 2004 1735 C ATOM 2520 OG SER B 37 58.426 4.686 37.670 1.00 57.84 O ANISOU 2520 OG SER B 37 8535 4558 8884 1146 1960 1682 O ATOM 2521 N HIS B 38 54.456 5.188 39.591 1.00 57.18 N ANISOU 2521 N HIS B 38 8684 4249 8791 859 2208 1479 N ATOM 2522 CA HIS B 38 53.525 4.924 40.681 1.00 62.59 C ANISOU 2522 CA HIS B 38 9443 4886 9452 807 2307 1506 C ATOM 2523 C HIS B 38 53.858 3.566 41.307 1.00 68.54 C ANISOU 2523 C HIS B 38 10207 5575 10261 885 2400 1645 C ATOM 2524 O HIS B 38 53.776 2.532 40.638 1.00 67.92 O ANISOU 2524 O HIS B 38 10061 5403 10342 912 2482 1573 O ATOM 2525 CB HIS B 38 52.095 4.953 40.134 1.00 65.10 C ANISOU 2525 CB HIS B 38 9718 5133 9885 706 2387 1287 C ATOM 2526 CG HIS B 38 51.033 4.700 41.158 1.00 73.78 C ANISOU 2526 CG HIS B 38 10879 6178 10977 648 2502 1294 C ATOM 2527 ND1 HIS B 38 49.697 4.597 40.827 1.00 76.48 N ANISOU 2527 ND1 HIS B 38 11174 6460 11426 561 2591 1125 N ATOM 2528 CD2 HIS B 38 51.101 4.517 42.499 1.00 78.04 C ANISOU 2528 CD2 HIS B 38 11519 6721 11413 663 2546 1454 C ATOM 2529 CE1 HIS B 38 48.990 4.379 41.922 1.00 77.52 C ANISOU 2529 CE1 HIS B 38 11376 6553 11526 529 2691 1176 C ATOM 2530 NE2 HIS B 38 49.816 4.324 42.950 1.00 75.86 N ANISOU 2530 NE2 HIS B 38 11260 6377 11185 588 2667 1372 N ATOM 2531 N TYR B 39 54.230 3.578 42.583 1.00 72.58 N ANISOU 2531 N TYR B 39 10804 6138 10633 915 2391 1844 N ATOM 2532 CA TYR B 39 54.573 2.352 43.293 1.00 73.66 C ANISOU 2532 CA TYR B 39 10954 6225 10807 999 2473 2006 C ATOM 2533 C TYR B 39 53.376 1.810 44.066 1.00 78.14 C ANISOU 2533 C TYR B 39 11580 6694 11414 935 2618 1972 C ATOM 2534 O TYR B 39 52.836 2.483 44.944 1.00 77.26 O ANISOU 2534 O TYR B 39 11555 6625 11174 865 2618 1996 O ATOM 2535 CB TYR B 39 55.748 2.594 44.243 1.00 77.47 C ANISOU 2535 CB TYR B 39 11482 6847 11105 1074 2371 2269 C ATOM 2536 CG TYR B 39 57.104 2.402 43.602 1.00 80.63 C ANISOU 2536 CG TYR B 39 11793 7316 11526 1190 2279 2367 C ATOM 2537 CD1 TYR B 39 57.499 3.180 42.522 1.00 76.65 C ANISOU 2537 CD1 TYR B 39 11229 6860 11032 1180 2183 2256 C ATOM 2538 CD2 TYR B 39 57.989 1.444 44.078 1.00 84.78 C ANISOU 2538 CD2 TYR B 39 12287 7861 12066 1316 2293 2575 C ATOM 2539 CE1 TYR B 39 58.737 3.008 41.933 1.00 76.97 C ANISOU 2539 CE1 TYR B 39 11183 6968 11095 1288 2107 2345 C ATOM 2540 CE2 TYR B 39 59.230 1.265 43.495 1.00 84.39 C ANISOU 2540 CE2 TYR B 39 12140 7881 12044 1429 2216 2667 C ATOM 2541 CZ TYR B 39 59.598 2.050 42.424 1.00 81.32 C ANISOU 2541 CZ TYR B 39 11694 7540 11663 1413 2126 2549 C ATOM 2542 OH TYR B 39 60.832 1.876 41.840 1.00 81.86 O ANISOU 2542 OH TYR B 39 11660 7683 11762 1527 2057 2639 O ATOM 2543 N GLN B 40 52.869 0.641 43.741 1.00 86.18 N ANISOU 2543 N GLN B 40 12559 7580 12607 944 2754 1902 N ATOM 2544 CA GLN B 40 51.725 0.150 44.500 1.00 88.71 C ANISOU 2544 CA GLN B 40 12934 7811 12960 880 2895 1876 C ATOM 2545 C GLN B 40 52.174 -0.903 45.492 1.00 96.55 C ANISOU 2545 C GLN B 40 13976 8763 13945 969 2971 2090 C ATOM 2546 O GLN B 40 52.774 -1.890 45.137 1.00102.92 O ANISOU 2546 O GLN B 40 14736 9508 14864 1058 3018 2147 O ATOM 2547 CB GLN B 40 50.627 -0.354 43.606 1.00 92.94 C ANISOU 2547 CB GLN B 40 13403 8234 13678 798 3009 1647 C ATOM 2548 CG GLN B 40 49.986 0.742 42.803 1.00103.58 C ANISOU 2548 CG GLN B 40 14702 9633 15018 702 2938 1451 C ATOM 2549 CD GLN B 40 48.932 0.228 41.851 1.00112.70 C ANISOU 2549 CD GLN B 40 15774 10702 16345 614 3037 1234 C ATOM 2550 OE1 GLN B 40 48.957 -0.921 41.437 1.00124.77 O ANISOU 2550 OE1 GLN B 40 17267 12134 18007 629 3138 1204 O ATOM 2551 NE2 GLN B 40 47.993 1.091 41.500 1.00108.95 N ANISOU 2551 NE2 GLN B 40 15264 10263 15867 517 3015 1084 N ATOM 2552 N THR B 41 51.876 -0.648 46.744 1.00 95.10 N ANISOU 2552 N THR B 41 13890 8620 13624 942 2986 2210 N ATOM 2553 CA THR B 41 52.244 -1.443 47.909 1.00 98.07 C ANISOU 2553 CA THR B 41 14329 8990 13944 1015 3040 2441 C ATOM 2554 C THR B 41 51.060 -1.613 48.855 1.00 96.47 C ANISOU 2554 C THR B 41 14211 8723 13719 930 3169 2423 C ATOM 2555 O THR B 41 50.102 -0.842 48.810 1.00101.98 O ANISOU 2555 O THR B 41 14931 9424 14393 819 3187 2265 O ATOM 2556 CB THR B 41 53.417 -0.808 48.679 1.00 94.43 C ANISOU 2556 CB THR B 41 13908 8710 13260 1072 2883 2673 C ATOM 2557 OG1 THR B 41 52.923 0.224 49.542 1.00 87.31 O ANISOU 2557 OG1 THR B 41 13107 7902 12164 967 2846 2678 O ATOM 2558 CG2 THR B 41 54.429 -0.213 47.712 1.00 88.93 C ANISOU 2558 CG2 THR B 41 13131 8106 12553 1121 2735 2652 C ATOM 2559 N ASP B 42 51.132 -2.628 49.710 1.00 98.90 N ANISOU 2559 N ASP B 42 14564 8973 14041 989 3265 2590 N ATOM 2560 CA ASP B 42 50.067 -2.899 50.665 1.00100.29 C ANISOU 2560 CA ASP B 42 14824 9085 14198 918 3400 2594 C ATOM 2561 C ASP B 42 49.891 -1.781 51.683 1.00 96.48 C ANISOU 2561 C ASP B 42 14442 8737 13479 841 3329 2655 C ATOM 2562 O ASP B 42 48.936 -1.823 52.462 1.00101.16 O ANISOU 2562 O ASP B 42 15108 9288 14041 766 3440 2635 O ATOM 2563 CB ASP B 42 50.336 -4.215 51.397 1.00104.67 C ANISOU 2563 CB ASP B 42 15409 9557 14803 1010 3507 2791 C ATOM 2564 CG ASP B 42 51.692 -4.237 52.080 1.00113.82 C ANISOU 2564 CG ASP B 42 16585 10855 15808 1124 3380 3073 C ATOM 2565 OD1 ASP B 42 52.658 -3.682 51.520 1.00117.60 O ANISOU 2565 OD1 ASP B 42 17005 11444 16235 1173 3230 3098 O ATOM 2566 OD2 ASP B 42 51.791 -4.784 53.196 1.00121.39 O ANISOU 2566 OD2 ASP B 42 17611 11825 16687 1161 3425 3277 O ATOM 2567 N ALA B 43 50.769 -0.780 51.681 1.00 92.85 N ANISOU 2567 N ALA B 43 13990 8439 12849 847 3159 2721 N ATOM 2568 CA ALA B 43 50.681 0.360 52.583 1.00 86.26 C ANISOU 2568 CA ALA B 43 13257 7745 11771 757 3093 2765 C ATOM 2569 C ALA B 43 50.371 1.657 51.845 1.00 85.06 C ANISOU 2569 C ALA B 43 13088 7636 11594 672 3025 2562 C ATOM 2570 O ALA B 43 50.733 2.737 52.321 1.00 91.27 O ANISOU 2570 O ALA B 43 13945 8566 12168 615 2930 2605 O ATOM 2571 CB ALA B 43 51.971 0.503 53.390 1.00 86.14 C ANISOU 2571 CB ALA B 43 13281 7915 11534 814 2954 3032 C ATOM 2572 N GLY B 44 49.746 1.571 50.675 1.00 85.16 N ANISOU 2572 N GLY B 44 13142 9360 9853 1400 3487 3423 N ATOM 2573 CA GLY B 44 49.430 2.738 49.877 1.00 74.88 C ANISOU 2573 CA GLY B 44 11699 8135 8616 1314 3393 3225 C ATOM 2574 C GLY B 44 50.463 2.995 48.798 1.00 76.94 C ANISOU 2574 C GLY B 44 11955 8318 8962 1368 3158 3099 C ATOM 2575 O GLY B 44 51.407 2.226 48.584 1.00 77.91 O ANISOU 2575 O GLY B 44 12164 8319 9118 1461 3079 3145 O ATOM 2576 N SER B 45 50.264 4.116 48.110 1.00 72.85 N ANISOU 2576 N SER B 45 11330 7874 8477 1309 3055 2939 N ATOM 2577 CA SER B 45 51.064 4.483 46.953 1.00 71.42 C ANISOU 2577 CA SER B 45 11127 7614 8395 1312 2846 2804 C ATOM 2578 C SER B 45 52.246 5.372 47.345 1.00 71.55 C ANISOU 2578 C SER B 45 11154 7864 8168 1557 2628 2781 C ATOM 2579 O SER B 45 52.238 6.035 48.381 1.00 71.84 O ANISOU 2579 O SER B 45 11188 8149 7957 1700 2620 2820 O ATOM 2580 CB SER B 45 50.196 5.199 45.925 1.00 76.00 C ANISOU 2580 CB SER B 45 11585 8129 9163 1100 2833 2641 C ATOM 2581 OG SER B 45 49.266 4.311 45.334 1.00 78.30 O ANISOU 2581 OG SER B 45 11859 8177 9715 860 3001 2634 O ATOM 2582 N PHE B 46 53.278 5.366 46.493 1.00 71.30 N ANISOU 2582 N PHE B 46 11126 7758 8207 1601 2452 2703 N ATOM 2583 CA PHE B 46 54.380 6.321 46.548 1.00 61.00 C ANISOU 2583 CA PHE B 46 9794 6646 6737 1781 2225 2638 C ATOM 2584 C PHE B 46 54.699 6.797 45.140 1.00 64.63 C ANISOU 2584 C PHE B 46 10170 7006 7381 1655 2066 2446 C ATOM 2585 O PHE B 46 54.558 6.045 44.172 1.00 67.26 O ANISOU 2585 O PHE B 46 10545 7095 7917 1521 2139 2442 O ATOM 2586 CB PHE B 46 55.652 5.729 47.155 1.00 68.17 C ANISOU 2586 CB PHE B 46 10759 7627 7516 2003 2143 2724 C ATOM 2587 CG PHE B 46 55.522 5.351 48.594 1.00 70.29 C ANISOU 2587 CG PHE B 46 11094 8040 7573 2145 2237 2879 C ATOM 2588 CD1 PHE B 46 55.621 6.314 49.584 1.00 71.93 C ANISOU 2588 CD1 PHE B 46 11280 8545 7506 2295 2154 2868 C ATOM 2589 CD2 PHE B 46 55.328 4.034 48.962 1.00 72.16 C ANISOU 2589 CD2 PHE B 46 11425 8119 7874 2133 2400 3029 C ATOM 2590 CE1 PHE B 46 55.517 5.972 50.920 1.00 74.19 C ANISOU 2590 CE1 PHE B 46 11633 8983 7571 2428 2235 3003 C ATOM 2591 CE2 PHE B 46 55.221 3.681 50.304 1.00 75.88 C ANISOU 2591 CE2 PHE B 46 11971 8723 8136 2264 2485 3189 C ATOM 2592 CZ PHE B 46 55.319 4.653 51.281 1.00 71.95 C ANISOU 2592 CZ PHE B 46 11449 8537 7353 2411 2402 3174 C ATOM 2593 N PHE B 47 55.159 8.042 45.028 1.00 59.25 N ANISOU 2593 N PHE B 47 9366 6520 6629 1689 1838 2265 N ATOM 2594 CA PHE B 47 55.541 8.603 43.738 1.00 55.62 C ANISOU 2594 CA PHE B 47 8818 5999 6318 1569 1671 2079 C ATOM 2595 C PHE B 47 57.059 8.739 43.668 1.00 58.55 C ANISOU 2595 C PHE B 47 9188 6452 6605 1733 1522 2075 C ATOM 2596 O PHE B 47 57.688 9.275 44.590 1.00 58.88 O ANISOU 2596 O PHE B 47 9202 6711 6461 1906 1417 2082 O ATOM 2597 CB PHE B 47 54.867 9.958 43.489 1.00 48.20 C ANISOU 2597 CB PHE B 47 7731 5174 5410 1450 1529 1874 C ATOM 2598 CG PHE B 47 55.151 10.507 42.133 1.00 51.31 C ANISOU 2598 CG PHE B 47 8059 5491 5947 1313 1375 1716 C ATOM 2599 CD1 PHE B 47 54.551 9.947 41.014 1.00 50.32 C ANISOU 2599 CD1 PHE B 47 7951 5165 6005 1128 1440 1685 C ATOM 2600 CD2 PHE B 47 56.049 11.557 41.958 1.00 51.52 C ANISOU 2600 CD2 PHE B 47 8011 5645 5919 1363 1169 1600 C ATOM 2601 CE1 PHE B 47 54.827 10.429 39.743 1.00 54.10 C ANISOU 2601 CE1 PHE B 47 8388 5589 6578 1009 1301 1552 C ATOM 2602 CE2 PHE B 47 56.325 12.051 40.680 1.00 47.22 C ANISOU 2602 CE2 PHE B 47 7423 5027 5493 1228 1047 1481 C ATOM 2603 CZ PHE B 47 55.716 11.482 39.576 1.00 51.47 C ANISOU 2603 CZ PHE B 47 7993 5382 6179 1060 1114 1464 C ATOM 2604 N VAL B 48 57.638 8.241 42.578 1.00 60.45 N ANISOU 2604 N VAL B 48 9452 6534 6984 1677 1514 2048 N ATOM 2605 CA VAL B 48 59.082 8.128 42.404 1.00 51.57 C ANISOU 2605 CA VAL B 48 8317 5459 5819 1828 1417 2054 C ATOM 2606 C VAL B 48 59.454 8.654 41.026 1.00 56.63 C ANISOU 2606 C VAL B 48 8877 6049 6591 1673 1310 1878 C ATOM 2607 O VAL B 48 58.802 8.324 40.029 1.00 61.89 O ANISOU 2607 O VAL B 48 9574 6538 7403 1491 1380 1825 O ATOM 2608 CB VAL B 48 59.557 6.664 42.569 1.00 58.83 C ANISOU 2608 CB VAL B 48 9378 6214 6762 1970 1572 2246 C ATOM 2609 CG1 VAL B 48 61.017 6.509 42.173 1.00 58.36 C ANISOU 2609 CG1 VAL B 48 9279 6189 6707 2114 1477 2222 C ATOM 2610 CG2 VAL B 48 59.378 6.219 44.003 1.00 54.92 C ANISOU 2610 CG2 VAL B 48 8941 5821 6105 2125 1643 2406 C ATOM 2611 N LYS B 49 60.515 9.455 40.961 1.00 57.85 N ANISOU 2611 N LYS B 49 8927 6364 6689 1741 1144 1788 N ATOM 2612 CA LYS B 49 61.099 9.846 39.688 1.00 57.68 C ANISOU 2612 CA LYS B 49 8840 6304 6769 1618 1069 1656 C ATOM 2613 C LYS B 49 62.585 9.535 39.597 1.00 68.88 C ANISOU 2613 C LYS B 49 10213 7789 8170 1772 1034 1667 C ATOM 2614 O LYS B 49 63.354 9.852 40.513 1.00 68.75 O ANISOU 2614 O LYS B 49 10126 7957 8040 1946 937 1690 O ATOM 2615 CB LYS B 49 60.972 11.350 39.447 1.00 49.60 C ANISOU 2615 CB LYS B 49 7702 5404 5740 1494 896 1503 C ATOM 2616 CG LYS B 49 59.513 11.779 39.322 1.00 51.12 C ANISOU 2616 CG LYS B 49 7910 5532 5981 1336 907 1460 C ATOM 2617 CD LYS B 49 59.358 13.202 38.800 1.00 45.53 C ANISOU 2617 CD LYS B 49 7110 4882 5308 1203 738 1313 C ATOM 2618 CE LYS B 49 59.613 14.244 39.880 1.00 55.46 C ANISOU 2618 CE LYS B 49 8282 6324 6466 1305 607 1255 C ATOM 2619 NZ LYS B 49 59.417 15.631 39.377 1.00 52.18 N ANISOU 2619 NZ LYS B 49 7792 5921 6114 1175 449 1117 N ATOM 2620 N THR B 50 62.976 8.865 38.510 1.00 67.82 N ANISOU 2620 N THR B 50 10111 7511 8146 1718 1117 1642 N ATOM 2621 CA THR B 50 64.354 8.436 38.317 1.00 63.10 C ANISOU 2621 CA THR B 50 9457 6958 7559 1869 1115 1644 C ATOM 2622 C THR B 50 64.883 9.035 37.028 1.00 61.97 C ANISOU 2622 C THR B 50 9228 6832 7487 1706 1073 1491 C ATOM 2623 O THR B 50 64.127 9.307 36.089 1.00 54.07 O ANISOU 2623 O THR B 50 8273 5732 6540 1492 1094 1417 O ATOM 2624 CB THR B 50 64.525 6.890 38.252 1.00 59.46 C ANISOU 2624 CB THR B 50 9125 6302 7166 2005 1288 1762 C ATOM 2625 OG1 THR B 50 63.644 6.334 37.268 1.00 64.24 O ANISOU 2625 OG1 THR B 50 9842 6677 7888 1815 1416 1720 O ATOM 2626 CG2 THR B 50 64.234 6.256 39.592 1.00 60.62 C ANISOU 2626 CG2 THR B 50 9366 6443 7225 2199 1336 1954 C ATOM 2627 N ASN B 51 66.197 9.231 37.000 1.00 57.23 N ANISOU 2627 N ASN B 51 8496 6370 6878 1814 1015 1448 N ATOM 2628 CA ASN B 51 66.888 9.615 35.779 1.00 54.20 C ANISOU 2628 CA ASN B 51 8029 6007 6557 1681 1021 1324 C ATOM 2629 C ASN B 51 68.301 9.047 35.839 1.00 58.27 C ANISOU 2629 C ASN B 51 8434 6608 7099 1881 1050 1322 C ATOM 2630 O ASN B 51 69.070 9.395 36.737 1.00 58.43 O ANISOU 2630 O ASN B 51 8320 6811 7069 2036 936 1335 O ATOM 2631 CB ASN B 51 66.880 11.135 35.623 1.00 51.72 C ANISOU 2631 CB ASN B 51 7605 5827 6218 1510 871 1227 C ATOM 2632 CG ASN B 51 67.359 11.569 34.268 1.00 56.47 C ANISOU 2632 CG ASN B 51 8160 6425 6870 1329 901 1126 C ATOM 2633 OD1 ASN B 51 68.442 11.180 33.839 1.00 69.62 O ANISOU 2633 OD1 ASN B 51 9740 8142 8569 1394 968 1091 O ATOM 2634 ND2 ASN B 51 66.554 12.350 33.573 1.00 46.15 N ANISOU 2634 ND2 ASN B 51 6909 5062 5564 1109 860 1085 N ATOM 2635 N ARG B 52 68.629 8.126 34.927 1.00 63.11 N ANISOU 2635 N ARG B 52 9098 7091 7791 1894 1200 1296 N ATOM 2636 CA ARG B 52 69.936 7.469 34.962 1.00 74.35 C ANISOU 2636 CA ARG B 52 10410 8577 9261 2112 1245 1289 C ATOM 2637 C ARG B 52 71.066 8.348 34.429 1.00 76.72 C ANISOU 2637 C ARG B 52 10488 9083 9579 2043 1189 1159 C ATOM 2638 O ARG B 52 72.237 8.035 34.664 1.00 75.98 O ANISOU 2638 O ARG B 52 10238 9108 9524 2235 1185 1142 O ATOM 2639 CB ARG B 52 69.895 6.157 34.171 1.00 85.97 C ANISOU 2639 CB ARG B 52 12014 9825 10826 2161 1439 1283 C ATOM 2640 CG ARG B 52 69.881 6.352 32.652 1.00102.90 C ANISOU 2640 CG ARG B 52 14171 11924 13003 1932 1534 1130 C ATOM 2641 CD ARG B 52 69.770 5.032 31.878 1.00117.76 C ANISOU 2641 CD ARG B 52 16197 13575 14972 1976 1723 1090 C ATOM 2642 NE ARG B 52 69.645 5.247 30.433 1.00126.54 N ANISOU 2642 NE ARG B 52 17342 14665 16072 1747 1806 936 N ATOM 2643 CZ ARG B 52 68.492 5.446 29.792 1.00129.56 C ANISOU 2643 CZ ARG B 52 17867 14943 16417 1513 1806 898 C ATOM 2644 NH1 ARG B 52 67.345 5.462 30.464 1.00128.45 N ANISOU 2644 NH1 ARG B 52 17830 14703 16273 1466 1742 993 N ATOM 2645 NH2 ARG B 52 68.484 5.633 28.475 1.00130.08 N ANISOU 2645 NH2 ARG B 52 17964 15018 16440 1330 1870 762 N ATOM 2646 N SER B 53 70.751 9.438 33.725 1.00 71.69 N ANISOU 2646 N SER B 53 9827 8487 8923 1776 1146 1075 N ATOM 2647 CA SER B 53 71.779 10.258 33.100 1.00 76.41 C ANISOU 2647 CA SER B 53 10230 9251 9550 1669 1129 964 C ATOM 2648 C SER B 53 72.252 11.409 33.982 1.00 76.17 C ANISOU 2648 C SER B 53 10018 9423 9501 1666 940 940 C ATOM 2649 O SER B 53 73.347 11.925 33.755 1.00 84.22 O ANISOU 2649 O SER B 53 10827 10603 10570 1637 920 854 O ATOM 2650 CB SER B 53 71.286 10.793 31.754 1.00 82.79 C ANISOU 2650 CB SER B 53 11124 9986 10347 1380 1199 899 C ATOM 2651 OG SER B 53 70.340 11.838 31.912 1.00 91.12 O ANISOU 2651 OG SER B 53 12244 11021 11356 1201 1072 919 O ATOM 2652 N ILE B 54 71.447 11.850 34.947 1.00 71.67 N ANISOU 2652 N ILE B 54 9515 8851 8865 1679 808 995 N ATOM 2653 CA ILE B 54 71.690 13.072 35.711 1.00 75.37 C ANISOU 2653 CA ILE B 54 9842 9485 9309 1635 621 940 C ATOM 2654 C ILE B 54 72.116 12.710 37.130 1.00 77.48 C ANISOU 2654 C ILE B 54 10033 9894 9512 1913 508 985 C ATOM 2655 O ILE B 54 71.552 11.800 37.747 1.00 77.63 O ANISOU 2655 O ILE B 54 10199 9833 9466 2086 547 1105 O ATOM 2656 CB ILE B 54 70.431 13.963 35.723 1.00 79.31 C ANISOU 2656 CB ILE B 54 10473 9890 9773 1443 549 943 C ATOM 2657 CG1 ILE B 54 70.017 14.305 34.287 1.00 88.53 C ANISOU 2657 CG1 ILE B 54 11726 10929 10984 1186 642 915 C ATOM 2658 CG2 ILE B 54 70.643 15.220 36.545 1.00 79.65 C ANISOU 2658 CG2 ILE B 54 10384 10076 9802 1404 358 864 C ATOM 2659 CD1 ILE B 54 68.849 15.284 34.186 1.00 91.85 C ANISOU 2659 CD1 ILE B 54 12252 11258 11388 1003 552 914 C ATOM 2660 N GLY B 55 73.087 13.451 37.660 1.00 74.57 N ANISOU 2660 N GLY B 55 9438 9739 9155 1946 363 890 N ATOM 2661 CA GLY B 55 73.516 13.309 39.032 1.00 65.34 C ANISOU 2661 CA GLY B 55 8180 8749 7896 2198 211 909 C ATOM 2662 C GLY B 55 72.513 13.852 40.028 1.00 68.06 C ANISOU 2662 C GLY B 55 8644 9102 8113 2196 93 933 C ATOM 2663 O GLY B 55 71.567 14.556 39.670 1.00 67.89 O ANISOU 2663 O GLY B 55 8729 8963 8103 1984 103 907 O ATOM 2664 N PRO B 56 72.726 13.555 41.316 1.00 71.30 N ANISOU 2664 N PRO B 56 9033 9669 8391 2448 -25 980 N ATOM 2665 CA PRO B 56 71.653 13.740 42.314 1.00 64.59 C ANISOU 2665 CA PRO B 56 8340 8817 7382 2495 -81 1039 C ATOM 2666 C PRO B 56 71.358 15.185 42.695 1.00 68.97 C ANISOU 2666 C PRO B 56 8826 9462 7916 2330 -239 876 C ATOM 2667 O PRO B 56 70.404 15.408 43.450 1.00 75.28 O ANISOU 2667 O PRO B 56 9753 10259 8592 2355 -268 901 O ATOM 2668 CB PRO B 56 72.169 12.959 43.530 1.00 65.50 C ANISOU 2668 CB PRO B 56 8444 9103 7341 2832 -160 1142 C ATOM 2669 CG PRO B 56 73.665 12.924 43.357 1.00 65.35 C ANISOU 2669 CG PRO B 56 8169 9253 7407 2931 -248 1053 C ATOM 2670 CD PRO B 56 73.895 12.847 41.875 1.00 69.25 C ANISOU 2670 CD PRO B 56 8624 9583 8105 2730 -88 1008 C ATOM 2671 N ALA B 57 72.122 16.169 42.218 1.00 67.12 N ANISOU 2671 N ALA B 57 8397 9298 7806 2163 -330 708 N ATOM 2672 CA ALA B 57 71.926 17.539 42.690 1.00 66.22 C ANISOU 2672 CA ALA B 57 8216 9256 7687 2027 -494 540 C ATOM 2673 C ALA B 57 70.519 18.055 42.382 1.00 64.88 C ANISOU 2673 C ALA B 57 8237 8887 7529 1854 -434 557 C ATOM 2674 O ALA B 57 69.904 18.729 43.215 1.00 67.38 O ANISOU 2674 O ALA B 57 8590 9252 7758 1866 -538 482 O ATOM 2675 CB ALA B 57 72.986 18.457 42.084 1.00 61.02 C ANISOU 2675 CB ALA B 57 7324 8659 7200 1841 -569 374 C ATOM 2676 N MET B 58 69.987 17.735 41.196 1.00 60.03 N ANISOU 2676 N MET B 58 7737 8059 7014 1704 -271 644 N ATOM 2677 CA MET B 58 68.686 18.262 40.774 1.00 58.94 C ANISOU 2677 CA MET B 58 7751 7737 6908 1534 -231 652 C ATOM 2678 C MET B 58 67.546 17.760 41.661 1.00 51.81 C ANISOU 2678 C MET B 58 7004 6819 5863 1673 -195 739 C ATOM 2679 O MET B 58 66.688 18.539 42.090 1.00 62.98 O ANISOU 2679 O MET B 58 8463 8214 7254 1620 -259 671 O ATOM 2680 CB MET B 58 68.429 17.892 39.312 1.00 67.54 C ANISOU 2680 CB MET B 58 8925 8632 8106 1367 -76 728 C ATOM 2681 CG MET B 58 67.014 18.149 38.849 1.00 81.98 C ANISOU 2681 CG MET B 58 10919 10277 9954 1234 -31 764 C ATOM 2682 SD MET B 58 66.647 17.331 37.281 1.00 97.73 S ANISOU 2682 SD MET B 58 13039 12078 12015 1100 153 864 S ATOM 2683 CE MET B 58 66.393 15.644 37.813 1.00 97.70 C ANISOU 2683 CE MET B 58 13138 12055 11928 1323 295 998 C ATOM 2684 N PHE B 59 67.491 16.455 41.909 1.00 52.19 N ANISOU 2684 N PHE B 59 7140 6861 5830 1845 -77 893 N ATOM 2685 CA PHE B 59 66.435 15.912 42.756 1.00 53.13 C ANISOU 2685 CA PHE B 59 7408 6964 5816 1964 -11 999 C ATOM 2686 C PHE B 59 66.586 16.373 44.201 1.00 59.60 C ANISOU 2686 C PHE B 59 8178 8009 6459 2130 -153 935 C ATOM 2687 O PHE B 59 65.587 16.509 44.916 1.00 60.85 O ANISOU 2687 O PHE B 59 8430 8179 6510 2163 -131 950 O ATOM 2688 CB PHE B 59 66.413 14.385 42.651 1.00 54.09 C ANISOU 2688 CB PHE B 59 7644 6994 5912 2100 159 1191 C ATOM 2689 CG PHE B 59 65.742 13.856 41.386 1.00 53.23 C ANISOU 2689 CG PHE B 59 7643 6639 5942 1930 321 1246 C ATOM 2690 CD1 PHE B 59 64.604 14.467 40.874 1.00 51.37 C ANISOU 2690 CD1 PHE B 59 7465 6282 5770 1732 336 1196 C ATOM 2691 CD2 PHE B 59 66.263 12.755 40.714 1.00 52.09 C ANISOU 2691 CD2 PHE B 59 7535 6394 5865 1981 446 1332 C ATOM 2692 CE1 PHE B 59 63.980 13.978 39.736 1.00 53.31 C ANISOU 2692 CE1 PHE B 59 7803 6327 6124 1582 460 1233 C ATOM 2693 CE2 PHE B 59 65.644 12.266 39.561 1.00 48.52 C ANISOU 2693 CE2 PHE B 59 7184 5727 5524 1823 585 1353 C ATOM 2694 CZ PHE B 59 64.503 12.886 39.073 1.00 53.00 C ANISOU 2694 CZ PHE B 59 7807 6195 6136 1619 584 1303 C ATOM 2695 N GLU B 60 67.819 16.606 44.654 1.00 63.04 N ANISOU 2695 N GLU B 60 8458 8640 6854 2238 -298 853 N ATOM 2696 CA GLU B 60 68.021 17.113 46.007 1.00 57.79 C ANISOU 2696 CA GLU B 60 7737 8215 6004 2390 -461 759 C ATOM 2697 C GLU B 60 67.479 18.525 46.165 1.00 62.03 C ANISOU 2697 C GLU B 60 8237 8751 6580 2230 -573 554 C ATOM 2698 O GLU B 60 66.880 18.852 47.199 1.00 66.51 O ANISOU 2698 O GLU B 60 8857 9430 6982 2321 -622 501 O ATOM 2699 CB GLU B 60 69.501 17.054 46.380 1.00 55.75 C ANISOU 2699 CB GLU B 60 7293 8175 5714 2533 -612 695 C ATOM 2700 CG GLU B 60 69.976 15.649 46.701 1.00 66.66 C ANISOU 2700 CG GLU B 60 8727 9609 6991 2790 -540 902 C ATOM 2701 CD GLU B 60 71.486 15.557 46.814 1.00 84.41 C ANISOU 2701 CD GLU B 60 10756 12053 9263 2921 -684 834 C ATOM 2702 OE1 GLU B 60 72.166 16.601 46.679 1.00 90.12 O ANISOU 2702 OE1 GLU B 60 11276 12882 10083 2791 -837 617 O ATOM 2703 OE2 GLU B 60 71.989 14.442 47.060 1.00 92.46 O ANISOU 2703 OE2 GLU B 60 11799 13117 10217 3157 -647 997 O ATOM 2704 N GLY B 61 67.675 19.374 45.153 1.00 58.68 N ANISOU 2704 N GLY B 61 7730 8196 6368 1996 -606 440 N ATOM 2705 CA GLY B 61 67.117 20.714 45.214 1.00 56.02 C ANISOU 2705 CA GLY B 61 7377 7806 6103 1844 -705 259 C ATOM 2706 C GLY B 61 65.602 20.715 45.162 1.00 56.39 C ANISOU 2706 C GLY B 61 7586 7703 6136 1802 -594 319 C ATOM 2707 O GLY B 61 64.946 21.525 45.828 1.00 61.25 O ANISOU 2707 O GLY B 61 8215 8351 6706 1807 -666 187 O ATOM 2708 N GLU B 62 65.028 19.826 44.350 1.00 51.11 N ANISOU 2708 N GLU B 62 7029 6871 5521 1757 -419 498 N ATOM 2709 CA GLU B 62 63.582 19.656 44.334 1.00 51.88 C ANISOU 2709 CA GLU B 62 7257 6846 5608 1727 -304 563 C ATOM 2710 C GLU B 62 63.064 19.221 45.704 1.00 59.67 C ANISOU 2710 C GLU B 62 8307 7993 6372 1929 -266 603 C ATOM 2711 O GLU B 62 62.059 19.752 46.195 1.00 54.29 O ANISOU 2711 O GLU B 62 7660 7314 5654 1924 -259 530 O ATOM 2712 CB GLU B 62 63.196 18.638 43.251 1.00 49.19 C ANISOU 2712 CB GLU B 62 7011 6320 5358 1648 -131 736 C ATOM 2713 CG GLU B 62 61.680 18.411 43.122 1.00 64.45 C ANISOU 2713 CG GLU B 62 9054 8123 7313 1592 -12 795 C ATOM 2714 CD GLU B 62 61.288 17.497 41.952 1.00 72.05 C ANISOU 2714 CD GLU B 62 10099 8894 8383 1483 134 924 C ATOM 2715 OE1 GLU B 62 62.185 17.007 41.235 1.00 73.92 O ANISOU 2715 OE1 GLU B 62 10324 9096 8667 1460 159 970 O ATOM 2716 OE2 GLU B 62 60.076 17.251 41.759 1.00 74.37 O ANISOU 2716 OE2 GLU B 62 10460 9081 8716 1421 227 964 O ATOM 2717 N ALA B 63 63.741 18.255 46.339 1.00 52.33 N ANISOU 2717 N ALA B 63 7395 7202 5285 2118 -235 724 N ATOM 2718 CA ALA B 63 63.288 17.769 47.637 1.00 55.21 C ANISOU 2718 CA ALA B 63 7844 7728 5406 2316 -183 800 C ATOM 2719 C ALA B 63 63.306 18.881 48.671 1.00 61.89 C ANISOU 2719 C ALA B 63 8623 8775 6119 2378 -346 586 C ATOM 2720 O ALA B 63 62.356 19.030 49.449 1.00 67.56 O ANISOU 2720 O ALA B 63 9410 9557 6703 2435 -285 566 O ATOM 2721 CB ALA B 63 64.154 16.590 48.111 1.00 47.07 C ANISOU 2721 CB ALA B 63 6847 6808 4229 2528 -151 981 C ATOM 2722 N LEU B 64 64.382 19.669 48.703 1.00 60.02 N ANISOU 2722 N LEU B 64 8243 8642 5921 2362 -548 408 N ATOM 2723 CA LEU B 64 64.461 20.760 49.669 1.00 58.10 C ANISOU 2723 CA LEU B 64 7930 8580 5566 2410 -720 165 C ATOM 2724 C LEU B 64 63.466 21.872 49.343 1.00 58.82 C ANISOU 2724 C LEU B 64 8026 8514 5810 2243 -725 0 C ATOM 2725 O LEU B 64 62.933 22.510 50.256 1.00 60.25 O ANISOU 2725 O LEU B 64 8218 8809 5865 2313 -773 -157 O ATOM 2726 CB LEU B 64 65.895 21.285 49.723 1.00 56.91 C ANISOU 2726 CB LEU B 64 7606 8565 5454 2411 -935 7 C ATOM 2727 CG LEU B 64 66.870 20.287 50.357 1.00 63.62 C ANISOU 2727 CG LEU B 64 8430 9636 6105 2641 -974 135 C ATOM 2728 CD1 LEU B 64 68.302 20.723 50.172 1.00 64.18 C ANISOU 2728 CD1 LEU B 64 8291 9819 6276 2614 -1170 -14 C ATOM 2729 CD2 LEU B 64 66.553 20.132 51.837 1.00 58.60 C ANISOU 2729 CD2 LEU B 64 7875 9260 5128 2873 -1012 126 C ATOM 2730 N GLY B 65 63.185 22.099 48.057 1.00 56.38 N ANISOU 2730 N GLY B 65 7714 7946 5761 2039 -676 33 N ATOM 2731 CA GLY B 65 62.143 23.052 47.689 1.00 54.72 C ANISOU 2731 CA GLY B 65 7522 7566 5702 1905 -677 -85 C ATOM 2732 C GLY B 65 60.760 22.599 48.123 1.00 49.94 C ANISOU 2732 C GLY B 65 7021 6956 5000 1976 -512 -1 C ATOM 2733 O GLY B 65 60.023 23.353 48.763 1.00 59.21 O ANISOU 2733 O GLY B 65 8190 8171 6135 2012 -539 -161 O ATOM 2734 N LEU B 66 60.401 21.347 47.813 1.00 53.33 N ANISOU 2734 N LEU B 66 7536 7333 5393 1998 -329 238 N ATOM 2735 CA LEU B 66 59.114 20.819 48.266 1.00 58.99 C ANISOU 2735 CA LEU B 66 8337 8053 6022 2051 -148 330 C ATOM 2736 C LEU B 66 59.012 20.870 49.783 1.00 62.55 C ANISOU 2736 C LEU B 66 8809 8766 6190 2248 -145 266 C ATOM 2737 O LEU B 66 57.945 21.156 50.333 1.00 62.54 O ANISOU 2737 O LEU B 66 8825 8804 6132 2277 -60 201 O ATOM 2738 CB LEU B 66 58.907 19.385 47.774 1.00 57.54 C ANISOU 2738 CB LEU B 66 8245 7770 5845 2042 46 596 C ATOM 2739 CG LEU B 66 58.652 19.097 46.292 1.00 49.55 C ANISOU 2739 CG LEU B 66 7244 6505 5078 1852 100 675 C ATOM 2740 CD1 LEU B 66 58.876 17.641 46.013 1.00 49.22 C ANISOU 2740 CD1 LEU B 66 7290 6403 5008 1884 258 904 C ATOM 2741 CD2 LEU B 66 57.235 19.483 45.897 1.00 54.12 C ANISOU 2741 CD2 LEU B 66 7818 6954 5789 1738 164 628 C ATOM 2742 N GLU B 67 60.116 20.595 50.477 1.00 67.63 N ANISOU 2742 N GLU B 67 9446 9608 6644 2392 -238 279 N ATOM 2743 CA GLU B 67 60.086 20.592 51.934 1.00 65.14 C ANISOU 2743 CA GLU B 67 9167 9573 6011 2595 -247 229 C ATOM 2744 C GLU B 67 59.804 21.989 52.490 1.00 64.76 C ANISOU 2744 C GLU B 67 9045 9609 5950 2590 -387 -90 C ATOM 2745 O GLU B 67 58.955 22.155 53.376 1.00 67.68 O ANISOU 2745 O GLU B 67 9458 10109 6148 2682 -299 -156 O ATOM 2746 CB GLU B 67 61.400 20.046 52.473 1.00 58.33 C ANISOU 2746 CB GLU B 67 8297 8907 4957 2758 -358 302 C ATOM 2747 CG GLU B 67 61.457 19.948 53.996 1.00 70.68 C ANISOU 2747 CG GLU B 67 9918 10793 6142 2990 -384 276 C ATOM 2748 CD GLU B 67 60.373 19.050 54.576 1.00 79.55 C ANISOU 2748 CD GLU B 67 11198 11948 7081 3076 -119 499 C ATOM 2749 OE1 GLU B 67 60.092 17.983 53.998 1.00 84.07 O ANISOU 2749 OE1 GLU B 67 11852 12345 7746 3035 64 765 O ATOM 2750 OE2 GLU B 67 59.800 19.402 55.625 1.00 90.26 O ANISOU 2750 OE2 GLU B 67 12595 13504 8196 3180 -82 402 O ATOM 2751 N ALA B 68 60.485 23.011 51.965 1.00 59.22 N ANISOU 2751 N ALA B 68 8233 8825 5443 2476 -590 -296 N ATOM 2752 CA ALA B 68 60.264 24.370 52.452 1.00 55.02 C ANISOU 2752 CA ALA B 68 7637 8331 4936 2464 -731 -616 C ATOM 2753 C ALA B 68 58.860 24.923 52.172 1.00 58.82 C ANISOU 2753 C ALA B 68 8136 8644 5570 2389 -624 -689 C ATOM 2754 O ALA B 68 58.308 25.676 52.985 1.00 65.72 O ANISOU 2754 O ALA B 68 8998 9617 6354 2467 -648 -910 O ATOM 2755 CB ALA B 68 61.257 25.318 51.783 1.00 53.68 C ANISOU 2755 CB ALA B 68 7351 8044 5001 2318 -948 -792 C ATOM 2756 N MET B 69 58.248 24.527 51.042 1.00 61.80 N ANISOU 2756 N MET B 69 8536 8778 6168 2250 -505 -514 N ATOM 2757 CA MET B 69 56.886 24.977 50.729 1.00 59.08 C ANISOU 2757 CA MET B 69 8187 8283 5978 2191 -413 -569 C ATOM 2758 C MET B 69 55.914 24.156 51.571 1.00 58.23 C ANISOU 2758 C MET B 69 8139 8334 5653 2315 -187 -458 C ATOM 2759 O MET B 69 54.883 24.672 52.005 1.00 56.74 O ANISOU 2759 O MET B 69 7923 8170 5465 2355 -120 -594 O ATOM 2760 CB MET B 69 56.558 24.789 49.247 1.00 53.15 C ANISOU 2760 CB MET B 69 7435 7248 5510 2007 -379 -422 C ATOM 2761 CG MET B 69 57.358 25.671 48.271 1.00 58.69 C ANISOU 2761 CG MET B 69 8089 7762 6448 1855 -570 -509 C ATOM 2762 SD MET B 69 56.875 25.441 46.531 1.00 57.34 S ANISOU 2762 SD MET B 69 7943 7289 6557 1653 -524 -329 S ATOM 2763 CE MET B 69 57.214 23.704 46.315 1.00 53.86 C ANISOU 2763 CE MET B 69 7570 6917 5979 1671 -344 -41 C ATOM 2764 N TYR B 70 56.210 22.866 51.792 1.00 58.17 N ANISOU 2764 N TYR B 70 8211 8422 5469 2377 -52 -203 N ATOM 2765 CA TYR B 70 55.329 22.029 52.607 1.00 60.94 C ANISOU 2765 CA TYR B 70 8633 8912 5609 2480 187 -64 C ATOM 2766 C TYR B 70 55.207 22.586 54.014 1.00 69.20 C ANISOU 2766 C TYR B 70 9684 10239 6370 2654 171 -255 C ATOM 2767 O TYR B 70 54.120 22.572 54.608 1.00 68.63 O ANISOU 2767 O TYR B 70 9617 10254 6207 2703 348 -282 O ATOM 2768 CB TYR B 70 55.836 20.580 52.645 1.00 65.41 C ANISOU 2768 CB TYR B 70 9304 9512 6036 2529 313 249 C ATOM 2769 CG TYR B 70 54.877 19.555 53.268 1.00 62.78 C ANISOU 2769 CG TYR B 70 9063 9251 5541 2587 601 458 C ATOM 2770 CD1 TYR B 70 53.924 18.896 52.487 1.00 60.98 C ANISOU 2770 CD1 TYR B 70 8838 8815 5518 2442 792 610 C ATOM 2771 CD2 TYR B 70 54.960 19.214 54.627 1.00 62.12 C ANISOU 2771 CD2 TYR B 70 9065 9447 5092 2779 683 512 C ATOM 2772 CE1 TYR B 70 53.052 17.955 53.040 1.00 58.74 C ANISOU 2772 CE1 TYR B 70 8626 8580 5114 2466 1071 801 C ATOM 2773 CE2 TYR B 70 54.093 18.263 55.194 1.00 63.47 C ANISOU 2773 CE2 TYR B 70 9329 9674 5113 2816 973 730 C ATOM 2774 CZ TYR B 70 53.142 17.642 54.388 1.00 67.99 C ANISOU 2774 CZ TYR B 70 9889 10015 5930 2648 1172 872 C ATOM 2775 OH TYR B 70 52.280 16.704 54.915 1.00 71.32 O ANISOU 2775 OH TYR B 70 10390 10471 6239 2654 1472 1085 O ATOM 2776 N GLU B 71 56.317 23.078 54.567 1.00 66.49 N ANISOU 2776 N GLU B 71 9328 10057 5880 2746 -37 -403 N ATOM 2777 CA GLU B 71 56.304 23.537 55.947 1.00 69.25 C ANISOU 2777 CA GLU B 71 9695 10706 5912 2924 -68 -594 C ATOM 2778 C GLU B 71 55.562 24.856 56.143 1.00 69.11 C ANISOU 2778 C GLU B 71 9596 10657 6007 2907 -124 -933 C ATOM 2779 O GLU B 71 55.146 25.143 57.268 1.00 77.21 O ANISOU 2779 O GLU B 71 10643 11920 6772 3051 -67 -1087 O ATOM 2780 CB GLU B 71 57.730 23.638 56.465 1.00 73.13 C ANISOU 2780 CB GLU B 71 10182 11389 6215 3026 -297 -667 C ATOM 2781 CG GLU B 71 58.321 22.295 56.847 1.00 82.40 C ANISOU 2781 CG GLU B 71 11460 12712 7135 3153 -216 -352 C ATOM 2782 CD GLU B 71 59.825 22.357 57.013 1.00 94.49 C ANISOU 2782 CD GLU B 71 12943 14378 8580 3227 -472 -406 C ATOM 2783 OE1 GLU B 71 60.403 23.427 56.719 1.00101.40 O ANISOU 2783 OE1 GLU B 71 13695 15203 9629 3139 -696 -683 O ATOM 2784 OE2 GLU B 71 60.425 21.352 57.456 1.00 93.15 O ANISOU 2784 OE2 GLU B 71 12852 14364 8179 3374 -450 -175 O ATOM 2785 N THR B 72 55.353 25.660 55.098 1.00 63.44 N ANISOU 2785 N THR B 72 8793 9653 5659 2748 -224 -1050 N ATOM 2786 CA THR B 72 54.546 26.853 55.330 1.00 67.03 C ANISOU 2786 CA THR B 72 9180 10061 6228 2761 -258 -1356 C ATOM 2787 C THR B 72 53.115 26.488 55.684 1.00 67.48 C ANISOU 2787 C THR B 72 9238 10174 6227 2814 8 -1300 C ATOM 2788 O THR B 72 52.397 27.320 56.242 1.00 66.95 O ANISOU 2788 O THR B 72 9120 10166 6153 2891 27 -1561 O ATOM 2789 CB THR B 72 54.541 27.791 54.119 1.00 63.42 C ANISOU 2789 CB THR B 72 8647 9264 6185 2592 -416 -1463 C ATOM 2790 OG1 THR B 72 53.870 27.165 53.011 1.00 56.29 O ANISOU 2790 OG1 THR B 72 7743 8145 5500 2464 -287 -1216 O ATOM 2791 CG2 THR B 72 55.967 28.185 53.731 1.00 57.25 C ANISOU 2791 CG2 THR B 72 7849 8421 5485 2510 -657 -1519 C ATOM 2792 N ARG B 73 52.692 25.265 55.368 1.00 71.71 N ANISOU 2792 N ARG B 73 9821 10688 6737 2770 221 -979 N ATOM 2793 CA ARG B 73 51.339 24.790 55.654 1.00 76.41 C ANISOU 2793 CA ARG B 73 10400 11334 7299 2790 501 -897 C ATOM 2794 C ARG B 73 50.276 25.685 55.007 1.00 70.11 C ANISOU 2794 C ARG B 73 9471 10334 6835 2716 489 -1083 C ATOM 2795 O ARG B 73 49.285 26.059 55.634 1.00 67.70 O ANISOU 2795 O ARG B 73 9101 10138 6484 2800 623 -1239 O ATOM 2796 CB ARG B 73 51.112 24.658 57.162 1.00 80.84 C ANISOU 2796 CB ARG B 73 11016 12245 7454 2979 646 -968 C ATOM 2797 CG ARG B 73 52.033 23.630 57.828 1.00 87.38 C ANISOU 2797 CG ARG B 73 11988 13283 7929 3075 678 -729 C ATOM 2798 CD ARG B 73 51.467 23.181 59.162 1.00 98.70 C ANISOU 2798 CD ARG B 73 13501 15038 8964 3234 918 -685 C ATOM 2799 NE ARG B 73 50.244 22.412 58.954 1.00108.50 N ANISOU 2799 NE ARG B 73 14725 16206 10295 3151 1238 -477 N ATOM 2800 CZ ARG B 73 49.159 22.492 59.720 1.00114.84 C ANISOU 2800 CZ ARG B 73 15495 17182 10959 3212 1483 -552 C ATOM 2801 NH1 ARG B 73 49.130 23.320 60.759 1.00111.36 N ANISOU 2801 NH1 ARG B 73 15049 17001 10260 3373 1445 -839 N ATOM 2802 NH2 ARG B 73 48.096 21.750 59.434 1.00119.29 N ANISOU 2802 NH2 ARG B 73 16019 17659 11647 3106 1771 -355 N ATOM 2803 N THR B 74 50.485 26.037 53.736 1.00 65.96 N ANISOU 2803 N THR B 74 8904 9517 6641 2569 328 -1062 N ATOM 2804 CA THR B 74 49.494 26.816 53.012 1.00 60.20 C ANISOU 2804 CA THR B 74 8061 8578 6236 2508 295 -1194 C ATOM 2805 C THR B 74 48.967 26.101 51.783 1.00 61.19 C ANISOU 2805 C THR B 74 8159 8493 6598 2347 365 -955 C ATOM 2806 O THR B 74 47.874 25.535 51.833 1.00 70.19 O ANISOU 2806 O THR B 74 9236 9669 7763 2335 575 -874 O ATOM 2807 CB THR B 74 50.039 28.190 52.595 1.00 62.11 C ANISOU 2807 CB THR B 74 8275 8639 6686 2489 12 -1441 C ATOM 2808 OG1 THR B 74 51.197 28.033 51.778 1.00 56.61 O ANISOU 2808 OG1 THR B 74 7639 7803 6068 2365 -148 -1306 O ATOM 2809 CG2 THR B 74 50.405 29.044 53.841 1.00 57.59 C ANISOU 2809 CG2 THR B 74 7709 8264 5910 2648 -67 -1751 C ATOM 2810 N ILE B 75 49.725 26.110 50.678 1.00 59.76 N ANISOU 2810 N ILE B 75 8016 8102 6586 2216 199 -852 N ATOM 2811 CA ILE B 75 49.240 25.544 49.425 1.00 57.60 C ANISOU 2811 CA ILE B 75 7722 7627 6538 2062 234 -662 C ATOM 2812 C ILE B 75 49.724 24.103 49.519 1.00 60.06 C ANISOU 2812 C ILE B 75 8130 8024 6668 2026 392 -392 C ATOM 2813 O ILE B 75 50.816 23.824 50.035 1.00 56.52 O ANISOU 2813 O ILE B 75 7769 7691 6016 2084 355 -345 O ATOM 2814 CB ILE B 75 49.785 26.243 48.161 1.00 59.60 C ANISOU 2814 CB ILE B 75 7983 7621 7039 1939 -3 -674 C ATOM 2815 CG1 ILE B 75 49.048 25.759 46.912 1.00 53.51 C ANISOU 2815 CG1 ILE B 75 7179 6670 6481 1801 29 -518 C ATOM 2816 CG2 ILE B 75 51.262 25.927 47.941 1.00 47.13 C ANISOU 2816 CG2 ILE B 75 6503 6040 5364 1887 -98 -569 C ATOM 2817 CD1 ILE B 75 49.182 26.699 45.708 1.00 52.72 C ANISOU 2817 CD1 ILE B 75 7075 6321 6636 1708 -198 -561 C ATOM 2818 N ARG B 76 48.910 23.177 49.014 1.00 52.33 N ANISOU 2818 N ARG B 76 7128 6979 5776 1932 563 -220 N ATOM 2819 CA ARG B 76 49.265 21.771 49.083 1.00 55.72 C ANISOU 2819 CA ARG B 76 7657 7447 6067 1896 732 38 C ATOM 2820 C ARG B 76 50.402 21.436 48.113 1.00 59.86 C ANISOU 2820 C ARG B 76 8265 7823 6656 1803 595 162 C ATOM 2821 O ARG B 76 50.376 21.826 46.940 1.00 62.22 O ANISOU 2821 O ARG B 76 8533 7931 7179 1682 462 140 O ATOM 2822 CB ARG B 76 48.057 20.900 48.785 1.00 57.71 C ANISOU 2822 CB ARG B 76 7852 7646 6428 1799 953 162 C ATOM 2823 CG ARG B 76 48.416 19.418 48.856 1.00 60.76 C ANISOU 2823 CG ARG B 76 8360 8031 6697 1756 1138 434 C ATOM 2824 CD ARG B 76 47.203 18.538 48.886 1.00 59.24 C ANISOU 2824 CD ARG B 76 8111 7819 6578 1666 1399 543 C ATOM 2825 NE ARG B 76 47.577 17.162 49.191 1.00 64.14 N ANISOU 2825 NE ARG B 76 8872 8437 7063 1653 1594 803 N ATOM 2826 CZ ARG B 76 46.795 16.117 48.945 1.00 67.63 C ANISOU 2826 CZ ARG B 76 9304 8783 7609 1523 1815 952 C ATOM 2827 NH1 ARG B 76 45.601 16.297 48.388 1.00 67.88 N ANISOU 2827 NH1 ARG B 76 9171 8743 7876 1395 1857 854 N ATOM 2828 NH2 ARG B 76 47.203 14.897 49.252 1.00 62.21 N ANISOU 2828 NH2 ARG B 76 8766 8065 6807 1524 1988 1195 N ATOM 2829 N VAL B 77 51.422 20.750 48.625 1.00 56.41 N ANISOU 2829 N VAL B 77 7932 7489 6010 1874 626 289 N ATOM 2830 CA VAL B 77 52.507 20.206 47.810 1.00 51.04 C ANISOU 2830 CA VAL B 77 7324 6697 5372 1806 547 425 C ATOM 2831 C VAL B 77 52.755 18.773 48.257 1.00 51.33 C ANISOU 2831 C VAL B 77 7467 6792 5243 1857 742 666 C ATOM 2832 O VAL B 77 52.442 18.400 49.398 1.00 56.63 O ANISOU 2832 O VAL B 77 8176 7636 5704 1977 889 718 O ATOM 2833 CB VAL B 77 53.809 21.046 47.922 1.00 52.94 C ANISOU 2833 CB VAL B 77 7562 6992 5560 1859 319 300 C ATOM 2834 CG1 VAL B 77 53.553 22.509 47.790 1.00 54.99 C ANISOU 2834 CG1 VAL B 77 7736 7202 5956 1838 145 54 C ATOM 2835 CG2 VAL B 77 54.520 20.766 49.218 1.00 57.52 C ANISOU 2835 CG2 VAL B 77 8193 7816 5846 2039 337 314 C ATOM 2836 N PRO B 78 53.309 17.942 47.378 1.00 52.44 N ANISOU 2836 N PRO B 78 7668 6786 5471 1774 756 821 N ATOM 2837 CA PRO B 78 53.654 16.572 47.776 1.00 49.81 C ANISOU 2837 CA PRO B 78 7452 6472 5003 1840 928 1056 C ATOM 2838 C PRO B 78 54.701 16.560 48.884 1.00 53.33 C ANISOU 2838 C PRO B 78 7953 7133 5176 2043 868 1083 C ATOM 2839 O PRO B 78 55.719 17.251 48.815 1.00 55.27 O ANISOU 2839 O PRO B 78 8158 7440 5401 2086 661 966 O ATOM 2840 CB PRO B 78 54.197 15.948 46.482 1.00 48.85 C ANISOU 2840 CB PRO B 78 7366 6141 5055 1718 901 1149 C ATOM 2841 CG PRO B 78 53.849 16.876 45.395 1.00 51.73 C ANISOU 2841 CG PRO B 78 7639 6381 5635 1567 757 991 C ATOM 2842 CD PRO B 78 53.621 18.220 45.964 1.00 49.21 C ANISOU 2842 CD PRO B 78 7232 6181 5285 1622 623 788 C ATOM 2843 N ASN B 79 54.450 15.752 49.899 1.00 54.91 N ANISOU 2843 N ASN B 79 8245 7452 5167 2162 1049 1244 N ATOM 2844 CA ASN B 79 55.401 15.577 50.985 1.00 58.71 C ANISOU 2844 CA ASN B 79 8797 8154 5354 2375 996 1305 C ATOM 2845 C ASN B 79 56.606 14.795 50.484 1.00 63.01 C ANISOU 2845 C ASN B 79 9400 8614 5925 2419 932 1454 C ATOM 2846 O ASN B 79 56.445 13.643 50.065 1.00 64.17 O ANISOU 2846 O ASN B 79 9638 8591 6152 2378 1098 1665 O ATOM 2847 CB ASN B 79 54.734 14.837 52.122 1.00 60.99 C ANISOU 2847 CB ASN B 79 9193 8574 5407 2483 1232 1479 C ATOM 2848 CG ASN B 79 55.605 14.742 53.346 1.00 69.48 C ANISOU 2848 CG ASN B 79 10350 9918 6131 2725 1164 1537 C ATOM 2849 OD1 ASN B 79 56.530 15.538 53.539 1.00 71.61 O ANISOU 2849 OD1 ASN B 79 10555 10329 6322 2812 919 1362 O ATOM 2850 ND2 ASN B 79 55.311 13.761 54.191 1.00 66.51 N ANISOU 2850 ND2 ASN B 79 10118 9616 5537 2833 1378 1786 N ATOM 2851 N PRO B 80 57.811 15.363 50.497 1.00 61.05 N ANISOU 2851 N PRO B 80 9094 8472 5631 2499 704 1340 N ATOM 2852 CA PRO B 80 58.972 14.627 49.993 1.00 56.09 C ANISOU 2852 CA PRO B 80 8492 7775 5046 2550 650 1466 C ATOM 2853 C PRO B 80 59.533 13.695 51.055 1.00 58.48 C ANISOU 2853 C PRO B 80 8909 8232 5077 2791 704 1676 C ATOM 2854 O PRO B 80 59.512 13.993 52.250 1.00 61.38 O ANISOU 2854 O PRO B 80 9302 8847 5174 2946 670 1651 O ATOM 2855 CB PRO B 80 59.968 15.740 49.643 1.00 51.92 C ANISOU 2855 CB PRO B 80 7821 7321 4586 2525 386 1235 C ATOM 2856 CG PRO B 80 59.674 16.810 50.675 1.00 57.43 C ANISOU 2856 CG PRO B 80 8470 8238 5113 2594 284 1038 C ATOM 2857 CD PRO B 80 58.156 16.758 50.853 1.00 57.41 C ANISOU 2857 CD PRO B 80 8518 8173 5124 2521 482 1064 C ATOM 2858 N HIS B 81 60.047 12.553 50.597 1.00 60.04 N ANISOU 2858 N HIS B 81 9186 8282 5346 2833 784 1883 N ATOM 2859 CA HIS B 81 60.565 11.517 51.485 1.00 62.30 C ANISOU 2859 CA HIS B 81 9605 8660 5407 3073 846 2131 C ATOM 2860 C HIS B 81 62.063 11.294 51.347 1.00 64.55 C ANISOU 2860 C HIS B 81 9834 9012 5680 3232 664 2143 C ATOM 2861 O HIS B 81 62.762 11.229 52.356 1.00 66.42 O ANISOU 2861 O HIS B 81 10089 9490 5659 3467 551 2196 O ATOM 2862 CB HIS B 81 59.802 10.213 51.245 1.00 66.83 C ANISOU 2862 CB HIS B 81 10340 8984 6070 3022 1129 2396 C ATOM 2863 CG HIS B 81 58.352 10.300 51.611 1.00 71.47 C ANISOU 2863 CG HIS B 81 10972 9550 6633 2898 1331 2414 C ATOM 2864 ND1 HIS B 81 57.346 9.830 50.793 1.00 70.24 N ANISOU 2864 ND1 HIS B 81 10836 9127 6723 2679 1524 2455 N ATOM 2865 CD2 HIS B 81 57.740 10.814 52.703 1.00 71.81 C ANISOU 2865 CD2 HIS B 81 11028 9820 6437 2962 1371 2378 C ATOM 2866 CE1 HIS B 81 56.177 10.044 51.371 1.00 70.97 C ANISOU 2866 CE1 HIS B 81 10935 9284 6746 2611 1677 2450 C ATOM 2867 NE2 HIS B 81 56.387 10.647 52.526 1.00 72.48 N ANISOU 2867 NE2 HIS B 81 11126 9773 6641 2783 1598 2403 N ATOM 2868 N LYS B 82 62.590 11.166 50.130 1.00 62.87 N ANISOU 2868 N LYS B 82 9546 8612 5730 3118 630 2092 N ATOM 2869 CA LYS B 82 64.016 10.891 49.987 1.00 68.83 C ANISOU 2869 CA LYS B 82 10224 9437 6491 3275 480 2103 C ATOM 2870 C LYS B 82 64.471 11.197 48.561 1.00 69.55 C ANISOU 2870 C LYS B 82 10188 9362 6876 3084 434 1955 C ATOM 2871 O LYS B 82 63.772 10.878 47.593 1.00 67.40 O ANISOU 2871 O LYS B 82 9969 8839 6802 2894 585 1977 O ATOM 2872 CB LYS B 82 64.322 9.429 50.341 1.00 69.01 C ANISOU 2872 CB LYS B 82 10392 9371 6459 3465 610 2381 C ATOM 2873 CG LYS B 82 65.791 9.047 50.326 1.00 71.92 C ANISOU 2873 CG LYS B 82 10658 9826 6842 3645 461 2379 C ATOM 2874 CD LYS B 82 66.072 7.850 51.222 1.00 68.69 C ANISOU 2874 CD LYS B 82 10346 9421 6331 3811 537 2560 C ATOM 2875 CE LYS B 82 67.550 7.493 51.208 1.00 76.21 C ANISOU 2875 CE LYS B 82 11182 10471 7301 4008 376 2552 C ATOM 2876 NZ LYS B 82 67.880 6.250 51.992 1.00 80.54 N ANISOU 2876 NZ LYS B 82 11837 10992 7771 4186 443 2747 N ATOM 2877 N ALA B 83 65.654 11.805 48.446 1.00 68.46 N ANISOU 2877 N ALA B 83 9878 9380 6755 3133 226 1802 N ATOM 2878 CA ALA B 83 66.332 11.986 47.174 1.00 66.77 C ANISOU 2878 CA ALA B 83 9538 9046 6785 2990 191 1690 C ATOM 2879 C ALA B 83 67.751 11.468 47.319 1.00 71.56 C ANISOU 2879 C ALA B 83 10046 9774 7369 3207 90 1731 C ATOM 2880 O ALA B 83 68.323 11.498 48.406 1.00 76.64 O ANISOU 2880 O ALA B 83 10653 10660 7808 3431 -49 1752 O ATOM 2881 CB ALA B 83 66.360 13.456 46.724 1.00 57.25 C ANISOU 2881 CB ALA B 83 8177 7897 5678 2776 45 1427 C ATOM 2882 N GLY B 84 68.327 11.004 46.222 1.00 71.73 N ANISOU 2882 N GLY B 84 10016 9645 7594 3151 153 1731 N ATOM 2883 CA GLY B 84 69.678 10.498 46.304 1.00 75.97 C ANISOU 2883 CA GLY B 84 10432 10295 8137 3366 66 1757 C ATOM 2884 C GLY B 84 70.168 9.919 45.001 1.00 75.67 C ANISOU 2884 C GLY B 84 10354 10064 8333 3291 184 1750 C ATOM 2885 O GLY B 84 69.588 10.140 43.937 1.00 75.19 O ANISOU 2885 O GLY B 84 10329 9815 8424 3037 295 1682 O ATOM 2886 N GLU B 85 71.233 9.139 45.118 1.00 77.74 N ANISOU 2886 N GLU B 85 10547 10383 8609 3533 157 1823 N ATOM 2887 CA GLU B 85 71.999 8.650 43.988 1.00 77.60 C ANISOU 2887 CA GLU B 85 10436 10250 8800 3512 242 1777 C ATOM 2888 C GLU B 85 71.607 7.206 43.710 1.00 71.08 C ANISOU 2888 C GLU B 85 9825 9146 8037 3627 454 1979 C ATOM 2889 O GLU B 85 71.317 6.450 44.638 1.00 69.38 O ANISOU 2889 O GLU B 85 9767 8902 7691 3842 479 2184 O ATOM 2890 CB GLU B 85 73.492 8.767 44.310 1.00 86.63 C ANISOU 2890 CB GLU B 85 11323 11650 9943 3719 66 1696 C ATOM 2891 CG GLU B 85 74.441 8.723 43.126 1.00 97.70 C ANISOU 2891 CG GLU B 85 12535 13023 11562 3644 122 1563 C ATOM 2892 CD GLU B 85 75.848 9.206 43.478 1.00104.11 C ANISOU 2892 CD GLU B 85 13029 14142 12388 3778 -81 1425 C ATOM 2893 OE1 GLU B 85 76.189 9.276 44.678 1.00106.95 O ANISOU 2893 OE1 GLU B 85 13334 14724 12580 4003 -271 1463 O ATOM 2894 OE2 GLU B 85 76.613 9.529 42.547 1.00106.52 O ANISOU 2894 OE2 GLU B 85 13130 14478 12864 3651 -48 1272 O ATOM 2895 N LEU B 86 71.517 6.848 42.428 1.00 71.01 N ANISOU 2895 N LEU B 86 9842 8918 8221 3466 614 1920 N ATOM 2896 CA LEU B 86 71.277 5.439 42.126 1.00 74.07 C ANISOU 2896 CA LEU B 86 10418 9026 8698 3583 809 2079 C ATOM 2897 C LEU B 86 72.604 4.684 42.061 1.00 84.38 C ANISOU 2897 C LEU B 86 11604 10373 10082 3868 790 2098 C ATOM 2898 O LEU B 86 73.565 5.175 41.461 1.00 83.04 O ANISOU 2898 O LEU B 86 11203 10350 10001 3834 726 1923 O ATOM 2899 CB LEU B 86 70.545 5.262 40.800 1.00 66.27 C ANISOU 2899 CB LEU B 86 9531 7779 7871 3304 991 1995 C ATOM 2900 CG LEU B 86 69.081 5.660 40.762 1.00 63.66 C ANISOU 2900 CG LEU B 86 9350 7334 7503 3051 1050 2006 C ATOM 2901 CD1 LEU B 86 68.520 5.570 39.343 1.00 66.64 C ANISOU 2901 CD1 LEU B 86 9786 7501 8034 2782 1187 1889 C ATOM 2902 CD2 LEU B 86 68.290 4.819 41.734 1.00 56.46 C ANISOU 2902 CD2 LEU B 86 8647 6297 6507 3184 1138 2233 C ATOM 2903 N PRO B 87 72.703 3.500 42.675 1.00 97.05 N ANISOU 2903 N PRO B 87 13349 11858 11667 4132 846 2299 N ATOM 2904 CA PRO B 87 73.978 2.770 42.602 1.00102.73 C ANISOU 2904 CA PRO B 87 13934 12620 12479 4379 816 2286 C ATOM 2905 C PRO B 87 74.332 2.396 41.178 1.00105.18 C ANISOU 2905 C PRO B 87 14204 12740 13022 4345 983 2172 C ATOM 2906 O PRO B 87 75.503 2.470 40.792 1.00104.08 O ANISOU 2906 O PRO B 87 13827 12746 12973 4457 930 2044 O ATOM 2907 CB PRO B 87 73.728 1.544 43.486 1.00102.48 C ANISOU 2907 CB PRO B 87 14096 12457 12387 4487 865 2470 C ATOM 2908 CG PRO B 87 72.260 1.317 43.387 1.00103.97 C ANISOU 2908 CG PRO B 87 14530 12407 12569 4240 1035 2542 C ATOM 2909 CD PRO B 87 71.626 2.677 43.257 1.00100.42 C ANISOU 2909 CD PRO B 87 14029 12092 12035 4046 970 2451 C ATOM 2910 N THR B 88 73.328 2.038 40.372 1.00107.85 N ANISOU 2910 N THR B 88 14742 12786 13450 4111 1178 2161 N ATOM 2911 CA THR B 88 73.544 1.749 38.960 1.00110.25 C ANISOU 2911 CA THR B 88 15016 12936 13939 3970 1336 1988 C ATOM 2912 C THR B 88 74.040 2.967 38.182 1.00104.66 C ANISOU 2912 C THR B 88 14065 12464 13237 3737 1265 1751 C ATOM 2913 O THR B 88 74.653 2.801 37.122 1.00103.84 O ANISOU 2913 O THR B 88 13861 12334 13259 3691 1368 1599 O ATOM 2914 CB THR B 88 72.245 1.219 38.337 1.00115.30 C ANISOU 2914 CB THR B 88 15922 13244 14645 3742 1527 2013 C ATOM 2915 OG1 THR B 88 71.397 2.318 37.972 1.00119.47 O ANISOU 2915 OG1 THR B 88 16441 13852 15102 3399 1487 1906 O ATOM 2916 CG2 THR B 88 71.499 0.338 39.325 1.00114.90 C ANISOU 2916 CG2 THR B 88 16084 13035 14539 3808 1562 2224 C ATOM 2917 N GLY B 89 73.796 4.177 38.681 1.00 97.24 N ANISOU 2917 N GLY B 89 13034 11744 12168 3588 1104 1716 N ATOM 2918 CA GLY B 89 74.137 5.429 37.997 1.00 88.67 C ANISOU 2918 CA GLY B 89 11747 10849 11094 3333 1038 1515 C ATOM 2919 C GLY B 89 72.869 6.240 37.811 1.00 82.51 C ANISOU 2919 C GLY B 89 11101 10003 10246 3021 1032 1497 C ATOM 2920 O GLY B 89 71.832 5.731 37.391 1.00 85.54 O ANISOU 2920 O GLY B 89 11702 10147 10654 2904 1165 1547 O ATOM 2921 N GLY B 90 72.954 7.522 38.132 1.00 74.27 N ANISOU 2921 N GLY B 90 9917 9173 9131 2889 871 1413 N ATOM 2922 CA GLY B 90 71.800 8.394 38.114 1.00 70.06 C ANISOU 2922 CA GLY B 90 9487 8599 8535 2634 834 1395 C ATOM 2923 C GLY B 90 71.287 8.734 39.503 1.00 68.53 C ANISOU 2923 C GLY B 90 9338 8510 8192 2737 696 1488 C ATOM 2924 O GLY B 90 71.970 8.565 40.521 1.00 65.44 O ANISOU 2924 O GLY B 90 8861 8286 7717 2986 582 1544 O ATOM 2925 N SER B 91 70.045 9.222 39.536 1.00 67.05 N ANISOU 2925 N SER B 91 9284 8234 7959 2548 705 1497 N ATOM 2926 CA SER B 91 69.451 9.802 40.736 1.00 61.36 C ANISOU 2926 CA SER B 91 8592 7631 7090 2590 584 1539 C ATOM 2927 C SER B 91 67.956 9.507 40.787 1.00 57.51 C ANISOU 2927 C SER B 91 8317 6953 6581 2480 699 1631 C ATOM 2928 O SER B 91 67.336 9.161 39.778 1.00 57.64 O ANISOU 2928 O SER B 91 8430 6764 6706 2311 831 1618 O ATOM 2929 CB SER B 91 69.681 11.302 40.751 1.00 60.26 C ANISOU 2929 CB SER B 91 8288 7668 6940 2429 415 1367 C ATOM 2930 OG SER B 91 69.222 11.840 39.520 1.00 68.55 O ANISOU 2930 OG SER B 91 9357 8584 8104 2148 477 1276 O ATOM 2931 N TYR B 92 67.372 9.694 41.971 1.00 58.40 N ANISOU 2931 N TYR B 92 8488 7155 6545 2569 644 1706 N ATOM 2932 CA TYR B 92 65.959 9.411 42.200 1.00 58.32 C ANISOU 2932 CA TYR B 92 8652 6998 6508 2481 762 1798 C ATOM 2933 C TYR B 92 65.393 10.402 43.208 1.00 62.38 C ANISOU 2933 C TYR B 92 9139 7688 6874 2472 646 1754 C ATOM 2934 O TYR B 92 66.132 11.080 43.929 1.00 65.61 O ANISOU 2934 O TYR B 92 9426 8329 7173 2584 477 1682 O ATOM 2935 CB TYR B 92 65.730 7.972 42.714 1.00 62.31 C ANISOU 2935 CB TYR B 92 9332 7360 6985 2665 922 2021 C ATOM 2936 CG TYR B 92 66.256 7.732 44.123 1.00 65.86 C ANISOU 2936 CG TYR B 92 9789 7999 7235 2955 842 2157 C ATOM 2937 CD1 TYR B 92 67.585 7.353 44.340 1.00 65.16 C ANISOU 2937 CD1 TYR B 92 9611 8023 7125 3194 754 2186 C ATOM 2938 CD2 TYR B 92 65.426 7.890 45.239 1.00 63.09 C ANISOU 2938 CD2 TYR B 92 9531 7734 6706 3000 853 2252 C ATOM 2939 CE1 TYR B 92 68.080 7.155 45.630 1.00 64.63 C ANISOU 2939 CE1 TYR B 92 9549 8153 6853 3476 651 2311 C ATOM 2940 CE2 TYR B 92 65.905 7.703 46.526 1.00 62.48 C ANISOU 2940 CE2 TYR B 92 9476 7858 6407 3270 772 2376 C ATOM 2941 CZ TYR B 92 67.230 7.329 46.714 1.00 69.59 C ANISOU 2941 CZ TYR B 92 10283 8872 7288 3490 660 2392 C ATOM 2942 OH TYR B 92 67.696 7.138 47.990 1.00 74.12 O ANISOU 2942 OH TYR B 92 10847 9662 7653 3695 561 2456 O ATOM 2943 N ILE B 93 64.063 10.470 43.262 1.00 60.88 N ANISOU 2943 N ILE B 93 9052 7392 6686 2341 739 1779 N ATOM 2944 CA ILE B 93 63.361 11.129 44.359 1.00 60.68 C ANISOU 2944 CA ILE B 93 9035 7514 6504 2372 686 1767 C ATOM 2945 C ILE B 93 62.099 10.332 44.679 1.00 61.27 C ANISOU 2945 C ILE B 93 9270 7444 6564 2345 885 1920 C ATOM 2946 O ILE B 93 61.444 9.799 43.774 1.00 57.20 O ANISOU 2946 O ILE B 93 8819 6704 6211 2187 1019 1942 O ATOM 2947 CB ILE B 93 63.029 12.599 44.023 1.00 50.31 C ANISOU 2947 CB ILE B 93 7607 6266 5243 2186 547 1553 C ATOM 2948 CG1 ILE B 93 62.386 13.306 45.228 1.00 55.02 C ANISOU 2948 CG1 ILE B 93 8201 7031 5672 2247 489 1509 C ATOM 2949 CG2 ILE B 93 62.102 12.681 42.840 1.00 45.57 C ANISOU 2949 CG2 ILE B 93 7042 5452 4820 1944 631 1510 C ATOM 2950 CD1 ILE B 93 62.256 14.817 45.038 1.00 50.21 C ANISOU 2950 CD1 ILE B 93 7472 6489 5117 2108 324 1283 C ATOM 2951 N ILE B 94 61.767 10.244 45.969 1.00 59.18 N ANISOU 2951 N ILE B 94 9066 7320 6099 2494 910 2020 N ATOM 2952 CA ILE B 94 60.546 9.600 46.451 1.00 61.18 C ANISOU 2952 CA ILE B 94 9455 7474 6317 2463 1113 2168 C ATOM 2953 C ILE B 94 59.696 10.654 47.143 1.00 61.83 C ANISOU 2953 C ILE B 94 9482 7723 6289 2410 1068 2050 C ATOM 2954 O ILE B 94 60.187 11.391 48.005 1.00 64.04 O ANISOU 2954 O ILE B 94 9701 8248 6382 2543 919 1971 O ATOM 2955 CB ILE B 94 60.819 8.451 47.444 1.00 60.90 C ANISOU 2955 CB ILE B 94 9570 7452 6117 2699 1230 2432 C ATOM 2956 CG1 ILE B 94 61.882 7.482 46.939 1.00 60.90 C ANISOU 2956 CG1 ILE B 94 9582 7329 6227 2791 1230 2497 C ATOM 2957 CG2 ILE B 94 59.515 7.688 47.750 1.00 53.95 C ANISOU 2957 CG2 ILE B 94 8807 6421 5271 2590 1476 2563 C ATOM 2958 CD1 ILE B 94 62.173 6.385 47.959 1.00 64.59 C ANISOU 2958 CD1 ILE B 94 10128 7822 6589 2958 1303 2659 C ATOM 2959 N MET B 95 58.416 10.691 46.813 1.00 60.83 N ANISOU 2959 N MET B 95 9368 7470 6273 2228 1198 2027 N ATOM 2960 CA MET B 95 57.542 11.652 47.464 1.00 59.12 C ANISOU 2960 CA MET B 95 9090 7403 5969 2191 1175 1907 C ATOM 2961 C MET B 95 56.151 11.046 47.602 1.00 63.61 C ANISOU 2961 C MET B 95 9721 7855 6592 2083 1415 2010 C ATOM 2962 O MET B 95 55.858 9.966 47.077 1.00 68.88 O ANISOU 2962 O MET B 95 10473 8304 7392 2003 1579 2151 O ATOM 2963 CB MET B 95 57.513 12.983 46.688 1.00 55.65 C ANISOU 2963 CB MET B 95 8504 6973 5667 2046 985 1651 C ATOM 2964 CG MET B 95 56.735 12.928 45.374 1.00 57.62 C ANISOU 2964 CG MET B 95 8729 6992 6172 1812 1036 1600 C ATOM 2965 SD MET B 95 56.774 14.442 44.356 1.00 59.19 S ANISOU 2965 SD MET B 95 8789 7171 6528 1653 809 1349 S ATOM 2966 CE MET B 95 58.472 14.443 43.792 1.00 51.49 C ANISOU 2966 CE MET B 95 7794 6211 5559 1702 671 1339 C ATOM 2967 N GLU B 96 55.300 11.776 48.319 1.00 63.25 N ANISOU 2967 N GLU B 96 9621 7958 6454 2076 1436 1919 N ATOM 2968 CA GLU B 96 53.886 11.452 48.451 1.00 55.91 C ANISOU 2968 CA GLU B 96 8693 6956 5594 1951 1653 1964 C ATOM 2969 C GLU B 96 53.198 11.333 47.094 1.00 53.52 C ANISOU 2969 C GLU B 96 8326 6413 5596 1712 1674 1888 C ATOM 2970 O GLU B 96 53.369 12.183 46.218 1.00 53.17 O ANISOU 2970 O GLU B 96 8184 6338 5680 1624 1487 1707 O ATOM 2971 CB GLU B 96 53.198 12.547 49.272 1.00 51.72 C ANISOU 2971 CB GLU B 96 8067 6645 4941 1986 1623 1802 C ATOM 2972 CG GLU B 96 51.704 12.382 49.406 1.00 58.33 C ANISOU 2972 CG GLU B 96 8854 7442 5866 1856 1839 1807 C ATOM 2973 CD GLU B 96 51.017 13.573 50.068 1.00 68.54 C ANISOU 2973 CD GLU B 96 10025 8940 7077 1892 1795 1600 C ATOM 2974 OE1 GLU B 96 51.701 14.578 50.393 1.00 68.79 O ANISOU 2974 OE1 GLU B 96 10018 9126 6992 2008 1583 1436 O ATOM 2975 OE2 GLU B 96 49.775 13.497 50.252 1.00 68.57 O ANISOU 2975 OE2 GLU B 96 9959 8943 7150 1801 1979 1587 O ATOM 2976 N PHE B 97 52.360 10.305 46.946 1.00 57.06 N ANISOU 2976 N PHE B 97 8830 6696 6156 1598 1904 2024 N ATOM 2977 CA PHE B 97 51.508 10.155 45.770 1.00 59.85 C ANISOU 2977 CA PHE B 97 9108 6847 6783 1364 1934 1936 C ATOM 2978 C PHE B 97 50.183 10.879 45.991 1.00 64.28 C ANISOU 2978 C PHE B 97 9522 7496 7405 1266 1974 1802 C ATOM 2979 O PHE B 97 49.497 10.639 46.994 1.00 63.90 O ANISOU 2979 O PHE B 97 9479 7546 7255 1302 2166 1885 O ATOM 2980 CB PHE B 97 51.236 8.680 45.453 1.00 58.72 C ANISOU 2980 CB PHE B 97 9080 6464 6766 1268 2155 2117 C ATOM 2981 CG PHE B 97 50.459 8.483 44.180 1.00 65.03 C ANISOU 2981 CG PHE B 97 9803 7065 7841 1025 2158 2001 C ATOM 2982 CD1 PHE B 97 49.065 8.537 44.181 1.00 63.54 C ANISOU 2982 CD1 PHE B 97 9498 6864 7783 863 2273 1938 C ATOM 2983 CD2 PHE B 97 51.120 8.296 42.969 1.00 66.64 C ANISOU 2983 CD2 PHE B 97 10036 7120 8163 962 2033 1935 C ATOM 2984 CE1 PHE B 97 48.344 8.406 42.994 1.00 63.30 C ANISOU 2984 CE1 PHE B 97 9378 6677 7997 645 2239 1810 C ATOM 2985 CE2 PHE B 97 50.408 8.150 41.770 1.00 60.67 C ANISOU 2985 CE2 PHE B 97 9215 6208 7629 744 2012 1811 C ATOM 2986 CZ PHE B 97 49.021 8.206 41.780 1.00 57.68 C ANISOU 2986 CZ PHE B 97 8718 5820 7378 587 2102 1747 C ATOM 2987 N ILE B 98 49.814 11.743 45.038 1.00 61.15 N ANISOU 2987 N ILE B 98 8995 7066 7175 1149 1801 1601 N ATOM 2988 CA ILE B 98 48.578 12.516 45.098 1.00 61.84 C ANISOU 2988 CA ILE B 98 8917 7224 7356 1071 1801 1448 C ATOM 2989 C ILE B 98 47.738 12.195 43.871 1.00 64.78 C ANISOU 2989 C ILE B 98 9207 7412 7994 853 1800 1384 C ATOM 2990 O ILE B 98 48.252 12.093 42.752 1.00 67.10 O ANISOU 2990 O ILE B 98 9539 7571 8385 777 1666 1354 O ATOM 2991 CB ILE B 98 48.834 14.035 45.189 1.00 62.66 C ANISOU 2991 CB ILE B 98 8928 7472 7408 1164 1561 1250 C ATOM 2992 CG1 ILE B 98 49.689 14.362 46.409 1.00 63.32 C ANISOU 2992 CG1 ILE B 98 9083 7754 7220 1374 1541 1281 C ATOM 2993 CG2 ILE B 98 47.516 14.804 45.278 1.00 61.18 C ANISOU 2993 CG2 ILE B 98 8564 7348 7335 1111 1567 1090 C ATOM 2994 CD1 ILE B 98 49.847 15.844 46.650 1.00 61.28 C ANISOU 2994 CD1 ILE B 98 8732 7631 6921 1459 1330 1065 C ATOM 2995 N ASP B 99 46.441 12.043 44.096 1.00 68.86 N ANISOU 2995 N ASP B 99 9601 7941 8620 753 1950 1353 N ATOM 2996 CA ASP B 99 45.474 11.724 43.058 1.00 76.41 C ANISOU 2996 CA ASP B 99 10446 8754 9831 542 1953 1273 C ATOM 2997 C ASP B 99 44.991 13.024 42.435 1.00 72.18 C ANISOU 2997 C ASP B 99 9746 8283 9397 532 1710 1059 C ATOM 2998 O ASP B 99 44.209 13.753 43.051 1.00 73.78 O ANISOU 2998 O ASP B 99 9803 8626 9605 585 1727 959 O ATOM 2999 CB ASP B 99 44.309 10.952 43.664 1.00 90.49 C ANISOU 2999 CB ASP B 99 12149 10535 11698 437 2239 1339 C ATOM 3000 CG ASP B 99 43.318 10.506 42.634 1.00110.10 C ANISOU 3000 CG ASP B 99 14503 12875 14456 206 2247 1247 C ATOM 3001 OD1 ASP B 99 43.564 10.791 41.441 1.00114.31 O ANISOU 3001 OD1 ASP B 99 15030 13320 15084 143 2021 1140 O ATOM 3002 OD2 ASP B 99 42.296 9.887 43.013 1.00118.10 O ANISOU 3002 OD2 ASP B 99 15416 13874 15583 82 2478 1278 O ATOM 3003 N PHE B 100 45.455 13.320 41.221 1.00 72.03 N ANISOU 3003 N PHE B 100 9754 8160 9453 473 1491 992 N ATOM 3004 CA PHE B 100 45.091 14.558 40.543 1.00 67.63 C ANISOU 3004 CA PHE B 100 9075 7637 8985 474 1241 821 C ATOM 3005 C PHE B 100 43.850 14.382 39.698 1.00 70.84 C ANISOU 3005 C PHE B 100 9325 7980 9612 309 1215 725 C ATOM 3006 O PHE B 100 43.427 13.269 39.389 1.00 77.81 O ANISOU 3006 O PHE B 100 10209 8763 10592 161 1361 773 O ATOM 3007 CB PHE B 100 46.214 15.055 39.633 1.00 57.51 C ANISOU 3007 CB PHE B 100 7906 6289 7656 491 1015 809 C ATOM 3008 CG PHE B 100 47.498 15.291 40.340 1.00 57.55 C ANISOU 3008 CG PHE B 100 8034 6362 7469 642 1003 877 C ATOM 3009 CD1 PHE B 100 47.516 15.894 41.583 1.00 59.42 C ANISOU 3009 CD1 PHE B 100 8237 6755 7585 794 1039 851 C ATOM 3010 CD2 PHE B 100 48.693 14.916 39.764 1.00 58.29 C ANISOU 3010 CD2 PHE B 100 8265 6379 7501 636 953 950 C ATOM 3011 CE1 PHE B 100 48.698 16.112 42.234 1.00 55.04 C ANISOU 3011 CE1 PHE B 100 7781 6281 6850 931 1005 895 C ATOM 3012 CE2 PHE B 100 49.888 15.134 40.413 1.00 58.69 C ANISOU 3012 CE2 PHE B 100 8400 6510 7389 777 928 1000 C ATOM 3013 CZ PHE B 100 49.887 15.735 41.650 1.00 58.71 C ANISOU 3013 CZ PHE B 100 8364 6670 7271 922 943 971 C ATOM 3014 N GLY B 101 43.245 15.511 39.355 1.00 76.18 N ANISOU 3014 N GLY B 101 9857 8712 10377 341 1020 579 N ATOM 3015 CA GLY B 101 42.143 15.529 38.421 1.00 83.21 C ANISOU 3015 CA GLY B 101 10585 9561 11469 210 921 470 C ATOM 3016 C GLY B 101 40.862 16.096 38.985 1.00 91.17 C ANISOU 3016 C GLY B 101 11349 10690 12602 251 953 348 C ATOM 3017 O GLY B 101 39.783 15.671 38.567 1.00100.06 O ANISOU 3017 O GLY B 101 12304 11807 13907 121 985 279 O ATOM 3018 N GLY B 102 40.941 17.038 39.922 1.00 89.52 N ANISOU 3018 N GLY B 102 11105 10599 12311 428 947 301 N ATOM 3019 CA GLY B 102 39.712 17.622 40.412 1.00 95.46 C ANISOU 3019 CA GLY B 102 11611 11469 13192 483 978 162 C ATOM 3020 C GLY B 102 39.012 18.303 39.262 1.00104.62 C ANISOU 3020 C GLY B 102 12626 12581 14544 453 705 35 C ATOM 3021 O GLY B 102 39.565 19.228 38.670 1.00109.08 O ANISOU 3021 O GLY B 102 13276 13087 15082 534 449 11 O ATOM 3022 N SER B 103 37.848 17.817 38.903 1.00110.82 N ANISOU 3022 N SER B 103 13202 13386 15520 331 751 -34 N ATOM 3023 CA SER B 103 37.140 18.335 37.763 1.00119.96 C ANISOU 3023 CA SER B 103 14214 14513 16851 302 478 -147 C ATOM 3024 C SER B 103 36.773 19.813 37.743 1.00131.31 C ANISOU 3024 C SER B 103 15537 15994 18360 498 244 -272 C ATOM 3025 O SER B 103 36.650 20.412 36.694 1.00135.78 O ANISOU 3025 O SER B 103 16094 16497 19000 514 -43 -309 O ATOM 3026 CB SER B 103 35.908 17.461 37.508 1.00124.20 C ANISOU 3026 CB SER B 103 14512 15087 17593 125 591 -218 C ATOM 3027 OG SER B 103 36.232 16.135 37.134 1.00130.12 O ANISOU 3027 OG SER B 103 15384 15735 18320 -80 731 -121 O ATOM 3028 N ARG B 104 36.568 20.419 38.884 1.00136.25 N ANISOU 3028 N ARG B 104 16079 16723 18966 655 360 -340 N ATOM 3029 CA ARG B 104 36.136 21.807 38.835 1.00137.25 C ANISOU 3029 CA ARG B 104 16085 16864 19199 847 137 -479 C ATOM 3030 C ARG B 104 37.340 22.722 38.660 1.00125.85 C ANISOU 3030 C ARG B 104 14891 15308 17619 959 -57 -427 C ATOM 3031 O ARG B 104 37.346 23.592 37.780 1.00133.05 O ANISOU 3031 O ARG B 104 15823 16118 18611 1020 -346 -450 O ATOM 3032 CB ARG B 104 35.319 22.166 40.089 1.00142.28 C ANISOU 3032 CB ARG B 104 16504 17662 19892 980 336 -617 C ATOM 3033 CG ARG B 104 34.142 21.204 40.381 1.00142.99 C ANISOU 3033 CG ARG B 104 16331 17878 20121 845 585 -660 C ATOM 3034 CD ARG B 104 33.168 21.745 41.444 1.00145.28 C ANISOU 3034 CD ARG B 104 16354 18344 20502 993 749 -829 C ATOM 3035 NE ARG B 104 32.213 20.744 41.928 1.00148.42 N ANISOU 3035 NE ARG B 104 16525 18872 20994 843 1063 -841 N ATOM 3036 CZ ARG B 104 32.256 20.171 43.130 1.00148.68 C ANISOU 3036 CZ ARG B 104 16583 19025 20883 821 1425 -785 C ATOM 3037 NH1 ARG B 104 33.188 20.526 44.006 1.00148.64 N ANISOU 3037 NH1 ARG B 104 16807 19049 20621 960 1498 -732 N ATOM 3038 NH2 ARG B 104 31.349 19.263 43.469 1.00148.21 N ANISOU 3038 NH2 ARG B 104 16314 19065 20936 659 1713 -783 N ATOM 3039 N GLY B 105 38.375 22.538 39.470 1.00107.08 N ANISOU 3039 N GLY B 105 12704 12945 15038 984 94 -350 N ATOM 3040 CA GLY B 105 39.455 23.500 39.457 1.00 97.06 C ANISOU 3040 CA GLY B 105 11625 11587 13667 1092 -76 -337 C ATOM 3041 C GLY B 105 39.046 24.781 40.150 1.00 86.59 C ANISOU 3041 C GLY B 105 10189 10293 12419 1301 -152 -509 C ATOM 3042 O GLY B 105 37.865 24.980 40.425 1.00 78.99 O ANISOU 3042 O GLY B 105 8989 9415 11609 1370 -110 -639 O ATOM 3043 N ASN B 106 40.003 25.666 40.419 1.00 82.82 N ANISOU 3043 N ASN B 106 9870 9744 11855 1400 -263 -529 N ATOM 3044 CA ASN B 106 39.723 26.848 41.237 1.00 81.50 C ANISOU 3044 CA ASN B 106 9621 9599 11747 1603 -307 -717 C ATOM 3045 C ASN B 106 40.870 27.853 41.050 1.00 78.03 C ANISOU 3045 C ASN B 106 9382 9002 11265 1655 -509 -715 C ATOM 3046 O ASN B 106 41.855 27.812 41.783 1.00 67.59 O ANISOU 3046 O ASN B 106 8192 7725 9762 1666 -427 -710 O ATOM 3047 CB ASN B 106 39.537 26.472 42.692 1.00 76.91 C ANISOU 3047 CB ASN B 106 8971 9223 11028 1675 -22 -800 C ATOM 3048 CG ASN B 106 38.540 27.371 43.391 1.00 84.75 C ANISOU 3048 CG ASN B 106 9757 10292 12154 1866 -7 -1032 C ATOM 3049 OD1 ASN B 106 38.289 28.507 42.949 1.00 72.35 O ANISOU 3049 OD1 ASN B 106 8144 8584 10762 1984 -241 -1144 O ATOM 3050 ND2 ASN B 106 37.961 26.874 44.487 1.00 90.93 N ANISOU 3050 ND2 ASN B 106 10413 11286 12849 1905 277 -1102 N ATOM 3051 N GLN B 107 40.724 28.743 40.059 1.00 75.41 N ANISOU 3051 N GLN B 107 9812 7983 10857 169 583 -313 N ATOM 3052 CA GLN B 107 41.776 29.720 39.769 1.00 69.70 C ANISOU 3052 CA GLN B 107 9143 7322 10019 234 472 -383 C ATOM 3053 C GLN B 107 41.947 30.733 40.904 1.00 62.72 C ANISOU 3053 C GLN B 107 8225 6568 9038 329 525 -422 C ATOM 3054 O GLN B 107 43.069 31.157 41.203 1.00 57.56 O ANISOU 3054 O GLN B 107 7636 5991 8242 397 497 -457 O ATOM 3055 CB GLN B 107 41.478 30.439 38.460 1.00 69.35 C ANISOU 3055 CB GLN B 107 9054 7229 10067 176 316 -457 C ATOM 3056 CG GLN B 107 42.736 30.910 37.766 1.00 84.11 C ANISOU 3056 CG GLN B 107 11016 9111 11832 203 208 -496 C ATOM 3057 CD GLN B 107 42.470 31.559 36.412 1.00 94.99 C ANISOU 3057 CD GLN B 107 12362 10451 13280 148 61 -537 C ATOM 3058 OE1 GLN B 107 41.583 32.436 36.250 1.00 90.63 O ANISOU 3058 OE1 GLN B 107 11707 9900 12829 147 16 -556 O ATOM 3059 NE2 GLN B 107 43.245 31.129 35.422 1.00 97.24 N ANISOU 3059 NE2 GLN B 107 12732 10710 13505 113 -14 -544 N ATOM 3060 N ALA B 108 40.843 31.163 41.521 1.00 54.81 N ANISOU 3060 N ALA B 108 7110 5601 8115 330 600 -439 N ATOM 3061 CA ALA B 108 40.944 32.075 42.652 1.00 56.51 C ANISOU 3061 CA ALA B 108 7289 5945 8237 417 667 -502 C ATOM 3062 C ALA B 108 41.570 31.387 43.858 1.00 55.12 C ANISOU 3062 C ALA B 108 7181 5890 7870 487 789 -428 C ATOM 3063 O ALA B 108 42.400 31.978 44.552 1.00 57.88 O ANISOU 3063 O ALA B 108 7561 6370 8061 565 789 -492 O ATOM 3064 CB ALA B 108 39.564 32.645 42.999 1.00 47.78 C ANISOU 3064 CB ALA B 108 6037 4849 7271 408 731 -543 C ATOM 3065 N GLU B 109 41.209 30.131 44.111 1.00 54.02 N ANISOU 3065 N GLU B 109 7068 5713 7746 459 894 -290 N ATOM 3066 CA GLU B 109 41.830 29.406 45.216 1.00 59.71 C ANISOU 3066 CA GLU B 109 7862 6547 8280 541 1009 -178 C ATOM 3067 C GLU B 109 43.338 29.268 45.033 1.00 58.66 C ANISOU 3067 C GLU B 109 7840 6452 7995 607 919 -175 C ATOM 3068 O GLU B 109 44.098 29.356 46.005 1.00 59.40 O ANISOU 3068 O GLU B 109 7966 6718 7884 709 955 -159 O ATOM 3069 CB GLU B 109 41.191 28.029 45.350 1.00 62.13 C ANISOU 3069 CB GLU B 109 8184 6751 8670 489 1141 -8 C ATOM 3070 CG GLU B 109 41.665 27.205 46.518 1.00 64.97 C ANISOU 3070 CG GLU B 109 8617 7216 8852 582 1282 157 C ATOM 3071 CD GLU B 109 41.237 27.757 47.849 1.00 70.58 C ANISOU 3071 CD GLU B 109 9262 8136 9418 650 1405 153 C ATOM 3072 OE1 GLU B 109 40.642 28.849 47.888 1.00 74.69 O ANISOU 3072 OE1 GLU B 109 9681 8714 9986 632 1380 -1 O ATOM 3073 OE2 GLU B 109 41.486 27.089 48.874 1.00 75.84 O ANISOU 3073 OE2 GLU B 109 9979 8917 9921 729 1534 310 O ATOM 3074 N LEU B 110 43.787 29.073 43.795 1.00 50.97 N ANISOU 3074 N LEU B 110 6915 5343 7110 553 799 -200 N ATOM 3075 CA LEU B 110 45.216 29.010 43.515 1.00 53.22 C ANISOU 3075 CA LEU B 110 7287 5666 7270 611 713 -215 C ATOM 3076 C LEU B 110 45.897 30.329 43.858 1.00 52.95 C ANISOU 3076 C LEU B 110 7220 5778 7119 661 641 -358 C ATOM 3077 O LEU B 110 46.963 30.338 44.481 1.00 54.64 O ANISOU 3077 O LEU B 110 7468 6135 7155 748 634 -362 O ATOM 3078 CB LEU B 110 45.442 28.676 42.038 1.00 46.88 C ANISOU 3078 CB LEU B 110 6526 4697 6589 531 606 -239 C ATOM 3079 CG LEU B 110 46.866 28.805 41.502 1.00 51.02 C ANISOU 3079 CG LEU B 110 7119 5252 7014 572 506 -285 C ATOM 3080 CD1 LEU B 110 47.826 27.778 42.159 1.00 43.67 C ANISOU 3080 CD1 LEU B 110 6263 4378 5951 678 570 -169 C ATOM 3081 CD2 LEU B 110 46.837 28.616 40.023 1.00 47.32 C ANISOU 3081 CD2 LEU B 110 6675 4639 6665 479 412 -326 C ATOM 3082 N GLY B 111 45.289 31.453 43.462 1.00 47.70 N ANISOU 3082 N GLY B 111 6482 5076 6565 608 587 -481 N ATOM 3083 CA GLY B 111 45.888 32.747 43.740 1.00 45.89 C ANISOU 3083 CA GLY B 111 6220 4945 6269 640 531 -632 C ATOM 3084 C GLY B 111 45.918 33.057 45.224 1.00 50.35 C ANISOU 3084 C GLY B 111 6748 5709 6675 721 627 -677 C ATOM 3085 O GLY B 111 46.909 33.579 45.732 1.00 54.25 O ANISOU 3085 O GLY B 111 7246 6344 7021 772 594 -773 O ATOM 3086 N ARG B 112 44.821 32.758 45.930 1.00 46.95 N ANISOU 3086 N ARG B 112 6269 5306 6266 729 749 -620 N ATOM 3087 CA ARG B 112 44.782 32.902 47.383 1.00 51.27 C ANISOU 3087 CA ARG B 112 6784 6068 6629 810 860 -644 C ATOM 3088 C ARG B 112 45.831 32.025 48.071 1.00 52.28 C ANISOU 3088 C ARG B 112 6988 6354 6521 899 881 -531 C ATOM 3089 O ARG B 112 46.586 32.497 48.927 1.00 52.97 O ANISOU 3089 O ARG B 112 7064 6657 6407 973 872 -623 O ATOM 3090 CB ARG B 112 43.391 32.552 47.916 1.00 48.87 C ANISOU 3090 CB ARG B 112 6415 5756 6397 794 1007 -569 C ATOM 3091 CG ARG B 112 43.258 32.842 49.402 1.00 52.14 C ANISOU 3091 CG ARG B 112 6787 6414 6609 876 1132 -614 C ATOM 3092 CD ARG B 112 41.887 32.525 49.952 1.00 61.51 C ANISOU 3092 CD ARG B 112 7900 7608 7865 857 1296 -540 C ATOM 3093 NE ARG B 112 41.670 31.085 50.094 1.00 69.48 N ANISOU 3093 NE ARG B 112 8966 8580 8853 850 1396 -294 N ATOM 3094 CZ ARG B 112 42.157 30.347 51.091 1.00 77.01 C ANISOU 3094 CZ ARG B 112 9981 9707 9573 935 1490 -149 C ATOM 3095 NH1 ARG B 112 42.912 30.896 52.038 1.00 84.94 N ANISOU 3095 NH1 ARG B 112 10990 10969 10315 1035 1483 -241 N ATOM 3096 NH2 ARG B 112 41.901 29.051 51.140 1.00 77.12 N ANISOU 3096 NH2 ARG B 112 10049 9638 9614 923 1592 88 N ATOM 3097 N LYS B 113 45.858 30.729 47.751 1.00 51.94 N ANISOU 3097 N LYS B 113 7016 6215 6505 900 914 -333 N ATOM 3098 CA LYS B 113 46.802 29.842 48.432 1.00 53.40 C ANISOU 3098 CA LYS B 113 7270 6538 6481 1008 943 -193 C ATOM 3099 C LYS B 113 48.245 30.181 48.089 1.00 56.67 C ANISOU 3099 C LYS B 113 7711 7025 6796 1051 804 -284 C ATOM 3100 O LYS B 113 49.124 30.063 48.950 1.00 49.25 O ANISOU 3100 O LYS B 113 6777 6307 5628 1160 800 -264 O ATOM 3101 CB LYS B 113 46.508 28.378 48.106 1.00 50.95 C ANISOU 3101 CB LYS B 113 7033 6062 6265 999 1021 36 C ATOM 3102 CG LYS B 113 45.278 27.825 48.797 1.00 51.04 C ANISOU 3102 CG LYS B 113 7018 6059 6317 980 1195 171 C ATOM 3103 CD LYS B 113 45.575 27.530 50.233 1.00 59.37 C ANISOU 3103 CD LYS B 113 8086 7366 7104 1110 1303 291 C ATOM 3104 CE LYS B 113 44.626 26.467 50.771 1.00 72.11 C ANISOU 3104 CE LYS B 113 9716 8916 8765 1099 1498 522 C ATOM 3105 NZ LYS B 113 45.022 26.047 52.148 1.00 79.58 N ANISOU 3105 NZ LYS B 113 10695 10121 9422 1244 1606 689 N ATOM 3106 N LEU B 114 48.509 30.618 46.857 1.00 52.75 N ANISOU 3106 N LEU B 114 7220 6365 6457 968 690 -383 N ATOM 3107 CA LEU B 114 49.873 30.990 46.497 1.00 50.56 C ANISOU 3107 CA LEU B 114 6955 6157 6101 993 571 -476 C ATOM 3108 C LEU B 114 50.325 32.206 47.296 1.00 53.68 C ANISOU 3108 C LEU B 114 7275 6762 6360 1018 538 -671 C ATOM 3109 O LEU B 114 51.440 32.229 47.827 1.00 53.59 O ANISOU 3109 O LEU B 114 7252 6947 6164 1094 492 -709 O ATOM 3110 CB LEU B 114 49.961 31.281 44.996 1.00 46.47 C ANISOU 3110 CB LEU B 114 6455 5425 5775 889 474 -537 C ATOM 3111 CG LEU B 114 51.379 31.634 44.546 1.00 53.47 C ANISOU 3111 CG LEU B 114 7347 6375 6594 902 367 -625 C ATOM 3112 CD1 LEU B 114 52.268 30.367 44.496 1.00 51.11 C ANISOU 3112 CD1 LEU B 114 7110 6101 6208 991 371 -481 C ATOM 3113 CD2 LEU B 114 51.411 32.402 43.224 1.00 48.69 C ANISOU 3113 CD2 LEU B 114 6739 5608 6153 790 280 -725 C ATOM 3114 N ALA B 115 49.450 33.209 47.412 1.00 52.22 N ANISOU 3114 N ALA B 115 7030 6541 6272 956 564 -806 N ATOM 3115 CA ALA B 115 49.745 34.416 48.178 1.00 52.02 C ANISOU 3115 CA ALA B 115 6929 6684 6152 966 550 -1025 C ATOM 3116 C ALA B 115 49.958 34.106 49.649 1.00 49.22 C ANISOU 3116 C ALA B 115 6552 6625 5522 1076 621 -1009 C ATOM 3117 O ALA B 115 50.816 34.713 50.299 1.00 59.60 O ANISOU 3117 O ALA B 115 7820 8155 6671 1111 574 -1169 O ATOM 3118 CB ALA B 115 48.606 35.425 48.014 1.00 51.85 C ANISOU 3118 CB ALA B 115 6849 6533 6318 896 588 -1149 C ATOM 3119 N GLU B 116 49.173 33.183 50.203 1.00 50.10 N ANISOU 3119 N GLU B 116 6692 6764 5580 1126 739 -821 N ATOM 3120 CA GLU B 116 49.433 32.729 51.570 1.00 53.30 C ANISOU 3120 CA GLU B 116 7091 7468 5693 1246 810 -750 C ATOM 3121 C GLU B 116 50.825 32.119 51.704 1.00 53.08 C ANISOU 3121 C GLU B 116 7096 7594 5479 1342 723 -670 C ATOM 3122 O GLU B 116 51.482 32.290 52.735 1.00 58.96 O ANISOU 3122 O GLU B 116 7799 8646 5955 1434 708 -729 O ATOM 3123 CB GLU B 116 48.376 31.716 52.018 1.00 54.58 C ANISOU 3123 CB GLU B 116 7288 7596 5853 1275 967 -513 C ATOM 3124 CG GLU B 116 46.942 32.246 52.105 1.00 63.67 C ANISOU 3124 CG GLU B 116 8381 8653 7158 1200 1074 -584 C ATOM 3125 CD GLU B 116 46.734 33.176 53.288 1.00 89.04 C ANISOU 3125 CD GLU B 116 11513 12128 10188 1240 1135 -776 C ATOM 3126 OE1 GLU B 116 47.711 33.442 54.027 1.00 98.48 O ANISOU 3126 OE1 GLU B 116 12698 13591 11131 1316 1083 -870 O ATOM 3127 OE2 GLU B 116 45.588 33.639 53.489 1.00100.51 O ANISOU 3127 OE2 GLU B 116 12905 13535 11750 1198 1237 -847 O ATOM 3128 N MET B 117 51.289 31.382 50.689 1.00 52.15 N ANISOU 3128 N MET B 117 7043 7283 5490 1330 666 -540 N ATOM 3129 CA MET B 117 52.639 30.818 50.771 1.00 55.74 C ANISOU 3129 CA MET B 117 7513 7877 5789 1433 584 -469 C ATOM 3130 C MET B 117 53.704 31.909 50.699 1.00 51.28 C ANISOU 3130 C MET B 117 6868 7455 5161 1405 453 -728 C ATOM 3131 O MET B 117 54.662 31.895 51.473 1.00 56.07 O ANISOU 3131 O MET B 117 7425 8347 5531 1505 400 -761 O ATOM 3132 CB MET B 117 52.870 29.778 49.671 1.00 50.35 C ANISOU 3132 CB MET B 117 6915 6941 5276 1427 569 -293 C ATOM 3133 CG MET B 117 54.259 29.113 49.757 1.00 50.99 C ANISOU 3133 CG MET B 117 7003 7158 5212 1557 496 -206 C ATOM 3134 SD MET B 117 54.683 27.987 48.410 1.00 58.28 S ANISOU 3134 SD MET B 117 8016 7787 6341 1554 477 -55 S ATOM 3135 CE MET B 117 55.019 29.096 47.038 1.00 48.61 C ANISOU 3135 CE MET B 117 6756 6414 5302 1389 359 -308 C ATOM 3136 N HIS B 118 53.553 32.870 49.794 1.00 56.44 N ANISOU 3136 N HIS B 118 7498 7921 6024 1269 402 -909 N ATOM 3137 CA HIS B 118 54.495 33.983 49.775 1.00 55.61 C ANISOU 3137 CA HIS B 118 7310 7931 5886 1222 301 -1164 C ATOM 3138 C HIS B 118 54.537 34.678 51.119 1.00 53.81 C ANISOU 3138 C HIS B 118 6999 8004 5441 1263 319 -1339 C ATOM 3139 O HIS B 118 55.615 35.008 51.621 1.00 60.53 O ANISOU 3139 O HIS B 118 7776 9103 6120 1299 239 -1476 O ATOM 3140 CB HIS B 118 54.110 34.985 48.696 1.00 48.27 C ANISOU 3140 CB HIS B 118 6376 6737 5228 1071 274 -1308 C ATOM 3141 CG HIS B 118 54.270 34.467 47.311 1.00 46.55 C ANISOU 3141 CG HIS B 118 6225 6270 5189 1020 233 -1184 C ATOM 3142 ND1 HIS B 118 53.768 35.127 46.209 1.00 51.66 N ANISOU 3142 ND1 HIS B 118 6888 6665 6074 899 215 -1238 N ATOM 3143 CD2 HIS B 118 54.864 33.348 46.845 1.00 47.59 C ANISOU 3143 CD2 HIS B 118 6414 6376 5293 1079 211 -1012 C ATOM 3144 CE1 HIS B 118 54.043 34.429 45.122 1.00 48.49 C ANISOU 3144 CE1 HIS B 118 6549 6114 5760 879 180 -1112 C ATOM 3145 NE2 HIS B 118 54.710 33.348 45.482 1.00 47.29 N ANISOU 3145 NE2 HIS B 118 6422 6084 5461 985 183 -986 N ATOM 3146 N LYS B 119 53.368 34.880 51.727 1.00 52.47 N ANISOU 3146 N LYS B 119 6830 7836 5269 1260 427 -1347 N ATOM 3147 CA LYS B 119 53.280 35.651 52.960 1.00 55.27 C ANISOU 3147 CA LYS B 119 7104 8467 5430 1286 460 -1554 C ATOM 3148 C LYS B 119 53.818 34.870 54.151 1.00 57.93 C ANISOU 3148 C LYS B 119 7429 9172 5411 1439 467 -1438 C ATOM 3149 O LYS B 119 54.497 35.437 55.006 1.00 58.31 O ANISOU 3149 O LYS B 119 7391 9529 5237 1472 414 -1637 O ATOM 3150 CB LYS B 119 51.835 36.077 53.199 1.00 59.82 C ANISOU 3150 CB LYS B 119 7678 8930 6122 1242 587 -1594 C ATOM 3151 CG LYS B 119 51.654 37.006 54.385 1.00 68.04 C ANISOU 3151 CG LYS B 119 8632 10226 6995 1255 635 -1855 C ATOM 3152 CD LYS B 119 50.187 37.370 54.568 1.00 65.38 C ANISOU 3152 CD LYS B 119 8285 9763 6794 1223 774 -1884 C ATOM 3153 CE LYS B 119 49.944 38.082 55.886 1.00 69.86 C ANISOU 3153 CE LYS B 119 8771 10622 7149 1259 852 -2121 C ATOM 3154 NZ LYS B 119 48.500 38.451 56.011 1.00 77.97 N ANISOU 3154 NZ LYS B 119 9775 11514 8335 1233 997 -2155 N ATOM 3155 N ALA B 120 53.510 33.577 54.238 1.00 63.21 N ANISOU 3155 N ALA B 120 8179 9816 6021 1535 535 -1116 N ATOM 3156 CA ALA B 120 53.948 32.779 55.375 1.00 63.89 C ANISOU 3156 CA ALA B 120 8264 10242 5769 1701 555 -952 C ATOM 3157 C ALA B 120 55.416 32.390 55.286 1.00 67.09 C ANISOU 3157 C ALA B 120 8640 10809 6041 1791 415 -917 C ATOM 3158 O ALA B 120 56.060 32.220 56.323 1.00 71.73 O ANISOU 3158 O ALA B 120 9174 11771 6310 1920 377 -906 O ATOM 3159 CB ALA B 120 53.086 31.522 55.511 1.00 59.36 C ANISOU 3159 CB ALA B 120 7790 9556 5208 1771 696 -600 C ATOM 3160 N GLY B 121 55.955 32.217 54.079 1.00 68.02 N ANISOU 3160 N GLY B 121 8785 10674 6384 1735 339 -892 N ATOM 3161 CA GLY B 121 57.335 31.780 53.913 1.00 64.46 C ANISOU 3161 CA GLY B 121 8297 10358 5835 1826 218 -848 C ATOM 3162 C GLY B 121 58.350 32.895 54.088 1.00 65.59 C ANISOU 3162 C GLY B 121 8304 10723 5894 1771 87 -1174 C ATOM 3163 O GLY B 121 58.515 33.738 53.199 1.00 65.08 O ANISOU 3163 O GLY B 121 8213 10459 6056 1619 42 -1375 O ATOM 3164 N LYS B 122 59.051 32.889 55.225 1.00 66.58 N ANISOU 3164 N LYS B 122 8339 11267 5692 1892 27 -1223 N ATOM 3165 CA LYS B 122 59.906 33.988 55.654 1.00 70.79 C ANISOU 3165 CA LYS B 122 8720 12071 6104 1833 -87 -1571 C ATOM 3166 C LYS B 122 61.306 33.469 55.967 1.00 74.93 C ANISOU 3166 C LYS B 122 9148 12910 6413 1974 -221 -1518 C ATOM 3167 O LYS B 122 61.505 32.277 56.215 1.00 73.73 O ANISOU 3167 O LYS B 122 9045 12842 6127 2157 -212 -1202 O ATOM 3168 CB LYS B 122 59.317 34.651 56.901 1.00 76.66 C ANISOU 3168 CB LYS B 122 9415 13094 6619 1835 -37 -1753 C ATOM 3169 CG LYS B 122 57.906 35.163 56.706 1.00 79.17 C ANISOU 3169 CG LYS B 122 9808 13133 7140 1718 103 -1808 C ATOM 3170 CD LYS B 122 57.284 35.610 58.031 1.00 87.71 C ANISOU 3170 CD LYS B 122 10847 14518 7961 1754 179 -1948 C ATOM 3171 CE LYS B 122 55.859 36.109 57.822 1.00 88.92 C ANISOU 3171 CE LYS B 122 11060 14390 8337 1649 326 -2001 C ATOM 3172 NZ LYS B 122 55.194 36.452 59.098 1.00 97.85 N ANISOU 3172 NZ LYS B 122 12152 15813 9214 1694 424 -2122 N ATOM 3173 N THR B 123 62.280 34.380 55.972 1.00 78.62 N ANISOU 3173 N THR B 123 9466 13550 6857 1891 -343 -1831 N ATOM 3174 CA THR B 123 63.663 34.027 56.280 1.00 78.39 C ANISOU 3174 CA THR B 123 9304 13854 6627 2013 -486 -1829 C ATOM 3175 C THR B 123 64.358 35.249 56.869 1.00 82.69 C ANISOU 3175 C THR B 123 9663 14708 7048 1907 -592 -2249 C ATOM 3176 O THR B 123 64.051 36.397 56.519 1.00 78.17 O ANISOU 3176 O THR B 123 9069 13953 6679 1702 -563 -2544 O ATOM 3177 CB THR B 123 64.437 33.494 55.039 1.00 72.10 C ANISOU 3177 CB THR B 123 8518 12814 6062 2012 -530 -1702 C ATOM 3178 OG1 THR B 123 65.725 32.983 55.425 1.00 71.15 O ANISOU 3178 OG1 THR B 123 8262 13037 5733 2172 -660 -1653 O ATOM 3179 CG2 THR B 123 64.638 34.583 53.995 1.00 66.85 C ANISOU 3179 CG2 THR B 123 7813 11884 5703 1774 -545 -1978 C ATOM 3180 N SER B 124 65.286 34.985 57.786 1.00 84.81 N ANISOU 3180 N SER B 124 9792 15448 6985 2053 -713 -2272 N ATOM 3181 CA SER B 124 66.139 36.019 58.358 1.00 91.72 C ANISOU 3181 CA SER B 124 10459 16668 7721 1962 -838 -2679 C ATOM 3182 C SER B 124 67.426 36.209 57.565 1.00 90.64 C ANISOU 3182 C SER B 124 10182 16514 7742 1894 -956 -2798 C ATOM 3183 O SER B 124 68.205 37.122 57.870 1.00 89.24 O ANISOU 3183 O SER B 124 9817 16576 7516 1780 -1058 -3162 O ATOM 3184 CB SER B 124 66.477 35.670 59.809 1.00 97.95 C ANISOU 3184 CB SER B 124 11146 18034 8035 2155 -923 -2662 C ATOM 3185 OG SER B 124 66.732 34.278 59.934 1.00102.62 O ANISOU 3185 OG SER B 124 11795 18726 8469 2409 -939 -2228 O ATOM 3186 N LYS B 125 67.654 35.389 56.543 1.00 83.87 N ANISOU 3186 N LYS B 125 9406 15377 7084 1950 -935 -2520 N ATOM 3187 CA LYS B 125 68.921 35.380 55.837 1.00 81.46 C ANISOU 3187 CA LYS B 125 8961 15095 6893 1925 -1037 -2586 C ATOM 3188 C LYS B 125 68.913 36.248 54.590 1.00 83.70 C ANISOU 3188 C LYS B 125 9264 14970 7567 1670 -983 -2773 C ATOM 3189 O LYS B 125 69.965 36.419 53.971 1.00 84.25 O ANISOU 3189 O LYS B 125 9205 15055 7752 1609 -1051 -2873 O ATOM 3190 CB LYS B 125 69.290 33.943 55.476 1.00 81.16 C ANISOU 3190 CB LYS B 125 8985 15022 6830 2155 -1043 -2184 C ATOM 3191 CG LYS B 125 69.218 32.989 56.653 1.00 88.09 C ANISOU 3191 CG LYS B 125 9872 16256 7343 2429 -1075 -1926 C ATOM 3192 CD LYS B 125 69.597 31.587 56.247 1.00 94.50 C ANISOU 3192 CD LYS B 125 10748 16981 8179 2657 -1067 -1529 C ATOM 3193 CE LYS B 125 69.489 30.628 57.417 1.00104.81 C ANISOU 3193 CE LYS B 125 12075 18617 9132 2939 -1084 -1229 C ATOM 3194 NZ LYS B 125 69.497 29.214 56.941 1.00109.67 N ANISOU 3194 NZ LYS B 125 12818 19004 9847 3146 -1017 -801 N ATOM 3195 N GLY B 126 67.767 36.825 54.224 1.00 82.89 N ANISOU 3195 N GLY B 126 9309 14521 7666 1522 -860 -2820 N ATOM 3196 CA GLY B 126 67.708 37.689 53.061 1.00 72.60 C ANISOU 3196 CA GLY B 126 8030 12834 6722 1291 -806 -2972 C ATOM 3197 C GLY B 126 67.203 37.009 51.807 1.00 71.75 C ANISOU 3197 C GLY B 126 8101 12304 6858 1295 -717 -2680 C ATOM 3198 O GLY B 126 66.378 36.098 51.878 1.00 75.71 O ANISOU 3198 O GLY B 126 8753 12701 7311 1426 -651 -2398 O ATOM 3199 N PHE B 127 67.714 37.422 50.651 1.00 65.93 N ANISOU 3199 N PHE B 127 7341 11333 6377 1149 -709 -2747 N ATOM 3200 CA PHE B 127 67.303 36.853 49.378 1.00 62.83 C ANISOU 3200 CA PHE B 127 7105 10560 6206 1136 -631 -2508 C ATOM 3201 C PHE B 127 68.269 35.756 48.955 1.00 63.64 C ANISOU 3201 C PHE B 127 7168 10755 6258 1284 -679 -2317 C ATOM 3202 O PHE B 127 69.485 35.937 49.013 1.00 66.67 O ANISOU 3202 O PHE B 127 7373 11367 6590 1281 -763 -2453 O ATOM 3203 CB PHE B 127 67.228 37.956 48.330 1.00 58.89 C ANISOU 3203 CB PHE B 127 6617 9751 6006 897 -581 -2672 C ATOM 3204 CG PHE B 127 66.385 39.120 48.761 1.00 64.38 C ANISOU 3204 CG PHE B 127 7330 10351 6782 759 -534 -2884 C ATOM 3205 CD1 PHE B 127 64.994 39.035 48.732 1.00 61.96 C ANISOU 3205 CD1 PHE B 127 7186 9815 6540 773 -447 -2756 C ATOM 3206 CD2 PHE B 127 66.974 40.286 49.225 1.00 59.83 C ANISOU 3206 CD2 PHE B 127 6596 9913 6223 619 -572 -3223 C ATOM 3207 CE1 PHE B 127 64.211 40.090 49.128 1.00 62.18 C ANISOU 3207 CE1 PHE B 127 7222 9750 6653 665 -396 -2951 C ATOM 3208 CE2 PHE B 127 66.191 41.354 49.630 1.00 63.11 C ANISOU 3208 CE2 PHE B 127 7029 10218 6731 500 -516 -3433 C ATOM 3209 CZ PHE B 127 64.808 41.255 49.582 1.00 67.44 C ANISOU 3209 CZ PHE B 127 7742 10537 7346 532 -427 -3292 C ATOM 3210 N GLY B 128 67.720 34.622 48.533 1.00 58.75 N ANISOU 3210 N GLY B 128 6705 9953 5664 1412 -620 -2015 N ATOM 3211 CA GLY B 128 68.511 33.461 48.192 1.00 56.93 C ANISOU 3211 CA GLY B 128 6457 9780 5394 1582 -646 -1815 C ATOM 3212 C GLY B 128 67.864 32.183 48.685 1.00 63.81 C ANISOU 3212 C GLY B 128 7459 10640 6145 1795 -602 -1507 C ATOM 3213 O GLY B 128 66.637 32.119 48.846 1.00 61.04 O ANISOU 3213 O GLY B 128 7254 10115 5824 1769 -522 -1416 O ATOM 3214 N PHE B 129 68.682 31.166 48.942 1.00 58.02 N ANISOU 3214 N PHE B 129 6668 10089 5288 2007 -649 -1341 N ATOM 3215 CA PHE B 129 68.192 29.867 49.383 1.00 67.20 C ANISOU 3215 CA PHE B 129 7952 11223 6358 2224 -597 -1020 C ATOM 3216 C PHE B 129 69.350 29.125 50.033 1.00 70.13 C ANISOU 3216 C PHE B 129 8184 11934 6529 2468 -690 -912 C ATOM 3217 O PHE B 129 70.520 29.497 49.870 1.00 66.71 O ANISOU 3217 O PHE B 129 7568 11699 6079 2458 -786 -1077 O ATOM 3218 CB PHE B 129 67.597 29.051 48.215 1.00 56.55 C ANISOU 3218 CB PHE B 129 6783 9448 5254 2208 -484 -830 C ATOM 3219 CG PHE B 129 66.633 27.969 48.654 1.00 56.81 C ANISOU 3219 CG PHE B 129 6978 9352 5254 2347 -390 -536 C ATOM 3220 CD1 PHE B 129 65.498 28.284 49.386 1.00 66.29 C ANISOU 3220 CD1 PHE B 129 8255 10554 6378 2298 -337 -518 C ATOM 3221 CD2 PHE B 129 66.861 26.641 48.345 1.00 63.16 C ANISOU 3221 CD2 PHE B 129 7854 10027 6118 2524 -341 -282 C ATOM 3222 CE1 PHE B 129 64.611 27.283 49.809 1.00 66.96 C ANISOU 3222 CE1 PHE B 129 8480 10523 6441 2414 -234 -239 C ATOM 3223 CE2 PHE B 129 65.974 25.638 48.766 1.00 68.26 C ANISOU 3223 CE2 PHE B 129 8647 10531 6757 2639 -238 -5 C ATOM 3224 CZ PHE B 129 64.848 25.964 49.502 1.00 57.80 C ANISOU 3224 CZ PHE B 129 7393 9220 5350 2579 -184 21 C ATOM 3225 N GLU B 130 69.007 28.070 50.781 1.00 68.68 N ANISOU 3225 N GLU B 130 8079 11816 6198 2690 -657 -622 N ATOM 3226 CA GLU B 130 70.030 27.306 51.493 1.00 71.93 C ANISOU 3226 CA GLU B 130 8365 12563 6403 2959 -747 -471 C ATOM 3227 C GLU B 130 70.982 26.582 50.540 1.00 75.57 C ANISOU 3227 C GLU B 130 8781 12897 7034 3055 -752 -393 C ATOM 3228 O GLU B 130 72.174 26.448 50.842 1.00 75.64 O ANISOU 3228 O GLU B 130 8600 13216 6923 3201 -865 -419 O ATOM 3229 CB GLU B 130 69.379 26.310 52.454 1.00 86.41 C ANISOU 3229 CB GLU B 130 10316 14454 8060 3178 -687 -136 C ATOM 3230 CG GLU B 130 68.648 26.995 53.602 1.00113.79 C ANISOU 3230 CG GLU B 130 13784 18164 11286 3126 -695 -219 C ATOM 3231 CD GLU B 130 67.931 26.033 54.532 1.00134.74 C ANISOU 3231 CD GLU B 130 16563 20869 13763 3326 -611 129 C ATOM 3232 OE1 GLU B 130 67.834 24.832 54.191 1.00142.70 O ANISOU 3232 OE1 GLU B 130 17687 21639 14892 3478 -525 443 O ATOM 3233 OE2 GLU B 130 67.461 26.490 55.602 1.00138.24 O ANISOU 3233 OE2 GLU B 130 16988 21585 13952 3325 -620 83 O ATOM 3234 N VAL B 131 70.493 26.127 49.386 1.00 72.78 N ANISOU 3234 N VAL B 131 8586 12113 6955 2978 -635 -314 N ATOM 3235 CA VAL B 131 71.337 25.470 48.396 1.00 69.47 C ANISOU 3235 CA VAL B 131 8134 11553 6710 3053 -620 -271 C ATOM 3236 C VAL B 131 71.019 26.049 47.026 1.00 72.17 C ANISOU 3236 C VAL B 131 8549 11562 7310 2791 -552 -451 C ATOM 3237 O VAL B 131 69.921 26.567 46.786 1.00 58.18 O ANISOU 3237 O VAL B 131 6910 9577 5619 2603 -490 -506 O ATOM 3238 CB VAL B 131 71.154 23.930 48.369 1.00 68.17 C ANISOU 3238 CB VAL B 131 8102 11192 6609 3297 -528 76 C ATOM 3239 CG1 VAL B 131 71.604 23.309 49.685 1.00 68.83 C ANISOU 3239 CG1 VAL B 131 8103 11620 6430 3589 -598 295 C ATOM 3240 CG2 VAL B 131 69.696 23.553 48.052 1.00 69.06 C ANISOU 3240 CG2 VAL B 131 8461 10912 6869 3195 -382 208 C ATOM 3241 N ASP B 132 72.005 25.980 46.132 1.00 66.57 N ANISOU 3241 N ASP B 132 7741 10832 6721 2786 -565 -542 N ATOM 3242 CA ASP B 132 71.749 26.211 44.718 1.00 65.68 C ANISOU 3242 CA ASP B 132 7720 10388 6847 2588 -481 -644 C ATOM 3243 C ASP B 132 70.875 25.094 44.189 1.00 65.92 C ANISOU 3243 C ASP B 132 7969 10056 7023 2652 -358 -426 C ATOM 3244 O ASP B 132 70.973 23.947 44.638 1.00 58.42 O ANISOU 3244 O ASP B 132 7056 9098 6041 2888 -329 -197 O ATOM 3245 CB ASP B 132 73.052 26.259 43.921 1.00 65.13 C ANISOU 3245 CB ASP B 132 7489 10400 6855 2594 -505 -769 C ATOM 3246 CG ASP B 132 73.894 27.484 44.248 1.00 76.44 C ANISOU 3246 CG ASP B 132 8698 12149 8197 2468 -612 -1028 C ATOM 3247 OD1 ASP B 132 73.409 28.369 44.994 1.00 72.44 O ANISOU 3247 OD1 ASP B 132 8176 11762 7584 2355 -663 -1137 O ATOM 3248 OD2 ASP B 132 75.056 27.544 43.782 1.00 81.48 O ANISOU 3248 OD2 ASP B 132 9165 12920 8876 2485 -640 -1132 O ATOM 3249 N ASN B 133 69.988 25.441 43.258 1.00 56.12 N ANISOU 3249 N ASN B 133 6867 8514 5941 2439 -284 -495 N ATOM 3250 CA ASN B 133 69.170 24.427 42.605 1.00 62.00 C ANISOU 3250 CA ASN B 133 7805 8908 6846 2463 -169 -337 C ATOM 3251 C ASN B 133 69.120 24.727 41.113 1.00 59.41 C ANISOU 3251 C ASN B 133 7527 8353 6695 2273 -120 -481 C ATOM 3252 O ASN B 133 70.055 25.329 40.577 1.00 55.02 O ANISOU 3252 O ASN B 133 6843 7918 6143 2206 -159 -643 O ATOM 3253 CB ASN B 133 67.769 24.333 43.236 1.00 58.07 C ANISOU 3253 CB ASN B 133 7453 8282 6327 2425 -121 -213 C ATOM 3254 CG ASN B 133 67.090 25.694 43.431 1.00 61.66 C ANISOU 3254 CG ASN B 133 7896 8793 6739 2206 -161 -383 C ATOM 3255 OD1 ASN B 133 67.444 26.693 42.792 1.00 58.72 O ANISOU 3255 OD1 ASN B 133 7454 8447 6412 2038 -201 -589 O ATOM 3256 ND2 ASN B 133 66.072 25.720 44.301 1.00 56.27 N ANISOU 3256 ND2 ASN B 133 7286 8110 5983 2209 -135 -290 N ATOM 3257 N THR B 134 68.050 24.342 40.426 1.00 59.86 N ANISOU 3257 N THR B 134 7758 8098 6889 2178 -36 -430 N ATOM 3258 CA THR B 134 68.020 24.508 38.978 1.00 60.48 C ANISOU 3258 CA THR B 134 7887 7985 7108 2020 7 -552 C ATOM 3259 C THR B 134 66.657 25.007 38.510 1.00 64.46 C ANISOU 3259 C THR B 134 8524 8279 7689 1815 33 -581 C ATOM 3260 O THR B 134 65.617 24.728 39.119 1.00 59.87 O ANISOU 3260 O THR B 134 8034 7602 7111 1825 59 -468 O ATOM 3261 CB THR B 134 68.359 23.202 38.251 1.00 60.83 C ANISOU 3261 CB THR B 134 7992 7849 7271 2148 91 -479 C ATOM 3262 OG1 THR B 134 67.515 22.161 38.747 1.00 62.31 O ANISOU 3262 OG1 THR B 134 8310 7853 7513 2255 156 -289 O ATOM 3263 CG2 THR B 134 69.855 22.802 38.441 1.00 52.62 C ANISOU 3263 CG2 THR B 134 6794 7017 6183 2346 67 -481 C ATOM 3264 N ILE B 135 66.678 25.755 37.417 1.00 59.70 N ANISOU 3264 N ILE B 135 7922 7615 7146 1632 30 -724 N ATOM 3265 CA ILE B 135 65.466 26.207 36.753 1.00 51.78 C ANISOU 3265 CA ILE B 135 7035 6415 6225 1447 48 -752 C ATOM 3266 C ILE B 135 65.467 25.514 35.394 1.00 58.95 C ANISOU 3266 C ILE B 135 8025 7138 7236 1408 109 -777 C ATOM 3267 O ILE B 135 66.229 25.874 34.482 1.00 57.49 O ANISOU 3267 O ILE B 135 7790 7001 7053 1344 111 -885 O ATOM 3268 CB ILE B 135 65.415 27.737 36.646 1.00 55.71 C ANISOU 3268 CB ILE B 135 7469 7002 6696 1269 -8 -882 C ATOM 3269 CG1 ILE B 135 64.181 28.203 35.864 1.00 49.34 C ANISOU 3269 CG1 ILE B 135 6773 5994 5980 1097 4 -894 C ATOM 3270 CG2 ILE B 135 66.733 28.296 36.127 1.00 52.73 C ANISOU 3270 CG2 ILE B 135 6965 6776 6294 1234 -27 -1006 C ATOM 3271 CD1 ILE B 135 62.877 27.738 36.486 1.00 44.05 C ANISOU 3271 CD1 ILE B 135 6196 5200 5341 1121 25 -784 C ATOM 3272 N GLY B 136 64.643 24.481 35.261 1.00 59.03 N ANISOU 3272 N GLY B 136 8155 6941 7332 1447 167 -686 N ATOM 3273 CA GLY B 136 64.868 23.551 34.167 1.00 57.80 C ANISOU 3273 CA GLY B 136 8062 6634 7266 1463 234 -721 C ATOM 3274 C GLY B 136 66.152 22.798 34.445 1.00 62.04 C ANISOU 3274 C GLY B 136 8519 7267 7787 1666 263 -695 C ATOM 3275 O GLY B 136 66.339 22.248 35.536 1.00 66.63 O ANISOU 3275 O GLY B 136 9075 7899 8342 1840 266 -563 O ATOM 3276 N SER B 137 67.058 22.777 33.467 1.00 61.99 N ANISOU 3276 N SER B 137 8464 7301 7788 1655 287 -811 N ATOM 3277 CA SER B 137 68.402 22.244 33.680 1.00 64.42 C ANISOU 3277 CA SER B 137 8659 7740 8079 1846 307 -808 C ATOM 3278 C SER B 137 69.413 23.323 34.029 1.00 60.53 C ANISOU 3278 C SER B 137 7991 7536 7472 1827 233 -883 C ATOM 3279 O SER B 137 70.575 23.002 34.292 1.00 56.61 O ANISOU 3279 O SER B 137 7365 7194 6949 1985 233 -887 O ATOM 3280 CB SER B 137 68.927 21.536 32.420 1.00 60.17 C ANISOU 3280 CB SER B 137 8145 7097 7621 1860 394 -912 C ATOM 3281 OG SER B 137 67.949 20.747 31.806 1.00 63.78 O ANISOU 3281 OG SER B 137 8759 7287 8187 1808 458 -912 O ATOM 3282 N THR B 138 69.032 24.569 33.970 1.00 54.97 N ANISOU 3282 N THR B 138 7272 6899 6717 1638 178 -951 N ATOM 3283 CA THR B 138 70.047 25.581 34.184 1.00 53.57 C ANISOU 3283 CA THR B 138 6922 6970 6461 1596 124 -1049 C ATOM 3284 C THR B 138 70.294 25.744 35.677 1.00 63.93 C ANISOU 3284 C THR B 138 8133 8476 7680 1720 47 -987 C ATOM 3285 O THR B 138 69.339 25.795 36.458 1.00 64.56 O ANISOU 3285 O THR B 138 8291 8505 7736 1719 21 -902 O ATOM 3286 CB THR B 138 69.612 26.913 33.593 1.00 52.60 C ANISOU 3286 CB THR B 138 6815 6834 6337 1350 103 -1144 C ATOM 3287 OG1 THR B 138 69.067 26.700 32.288 1.00 60.30 O ANISOU 3287 OG1 THR B 138 7916 7623 7371 1240 163 -1166 O ATOM 3288 CG2 THR B 138 70.797 27.875 33.503 1.00 49.69 C ANISOU 3288 CG2 THR B 138 6267 6684 5927 1280 82 -1267 C ATOM 3289 N PRO B 139 71.552 25.824 36.098 1.00 64.30 N ANISOU 3289 N PRO B 139 7998 8768 7665 1827 10 -1034 N ATOM 3290 CA PRO B 139 71.828 26.138 37.504 1.00 54.03 C ANISOU 3290 CA PRO B 139 6580 7708 6242 1925 -83 -1005 C ATOM 3291 C PRO B 139 71.170 27.457 37.889 1.00 59.02 C ANISOU 3291 C PRO B 139 7214 8377 6833 1725 -136 -1094 C ATOM 3292 O PRO B 139 71.077 28.388 37.083 1.00 59.60 O ANISOU 3292 O PRO B 139 7293 8386 6966 1517 -119 -1213 O ATOM 3293 CB PRO B 139 73.356 26.236 37.551 1.00 52.72 C ANISOU 3293 CB PRO B 139 6190 7808 6034 2012 -117 -1098 C ATOM 3294 CG PRO B 139 73.833 25.432 36.358 1.00 57.02 C ANISOU 3294 CG PRO B 139 6762 8214 6687 2061 -19 -1105 C ATOM 3295 CD PRO B 139 72.787 25.678 35.304 1.00 58.50 C ANISOU 3295 CD PRO B 139 7140 8129 6960 1858 49 -1130 C ATOM 3296 N GLN B 140 70.688 27.519 39.126 1.00 51.47 N ANISOU 3296 N GLN B 140 6260 7520 5777 1797 -191 -1028 N ATOM 3297 CA GLN B 140 70.098 28.729 39.690 1.00 50.56 C ANISOU 3297 CA GLN B 140 6132 7461 5617 1639 -240 -1126 C ATOM 3298 C GLN B 140 70.906 29.068 40.935 1.00 54.02 C ANISOU 3298 C GLN B 140 6385 8244 5895 1736 -335 -1190 C ATOM 3299 O GLN B 140 70.898 28.303 41.905 1.00 63.23 O ANISOU 3299 O GLN B 140 7546 9535 6944 1937 -364 -1054 O ATOM 3300 CB GLN B 140 68.607 28.528 39.998 1.00 48.36 C ANISOU 3300 CB GLN B 140 6031 6985 5357 1616 -206 -1010 C ATOM 3301 CG GLN B 140 67.943 29.753 40.585 1.00 62.45 C ANISOU 3301 CG GLN B 140 7803 8815 7109 1468 -244 -1117 C ATOM 3302 CD GLN B 140 66.421 29.717 40.510 1.00 57.56 C ANISOU 3302 CD GLN B 140 7354 7958 6559 1397 -194 -1031 C ATOM 3303 OE1 GLN B 140 65.813 30.329 39.626 1.00 54.04 O ANISOU 3303 OE1 GLN B 140 6977 7324 6233 1228 -168 -1085 O ATOM 3304 NE2 GLN B 140 65.801 29.009 41.449 1.00 53.79 N ANISOU 3304 NE2 GLN B 140 6933 7500 6003 1530 -180 -888 N ATOM 3305 N ILE B 141 71.646 30.179 40.883 1.00 58.21 N ANISOU 3305 N ILE B 141 6759 8937 6423 1596 -382 -1394 N ATOM 3306 CA ILE B 141 72.560 30.565 41.963 1.00 61.37 C ANISOU 3306 CA ILE B 141 6946 9696 6673 1665 -484 -1505 C ATOM 3307 C ILE B 141 71.778 31.258 43.075 1.00 66.45 C ANISOU 3307 C ILE B 141 7609 10429 7210 1615 -532 -1561 C ATOM 3308 O ILE B 141 71.060 32.235 42.827 1.00 69.81 O ANISOU 3308 O ILE B 141 8100 10701 7724 1414 -502 -1669 O ATOM 3309 CB ILE B 141 73.676 31.485 41.439 1.00 65.91 C ANISOU 3309 CB ILE B 141 7331 10399 7311 1510 -502 -1724 C ATOM 3310 CG1 ILE B 141 74.358 30.912 40.190 1.00 70.53 C ANISOU 3310 CG1 ILE B 141 7909 10876 8014 1527 -429 -1686 C ATOM 3311 CG2 ILE B 141 74.713 31.687 42.506 1.00 60.60 C ANISOU 3311 CG2 ILE B 141 6417 10123 6485 1603 -617 -1840 C ATOM 3312 CD1 ILE B 141 74.850 29.497 40.338 1.00 66.59 C ANISOU 3312 CD1 ILE B 141 7395 10445 7461 1805 -430 -1518 C ATOM 3313 N ASN B 142 71.948 30.778 44.315 1.00 67.22 N ANISOU 3313 N ASN B 142 7640 10792 7110 1808 -603 -1490 N ATOM 3314 CA ASN B 142 71.094 31.170 45.433 1.00 60.83 C ANISOU 3314 CA ASN B 142 6873 10074 6166 1804 -630 -1503 C ATOM 3315 C ASN B 142 71.870 31.705 46.638 1.00 68.55 C ANISOU 3315 C ASN B 142 7638 11475 6931 1852 -751 -1666 C ATOM 3316 O ASN B 142 71.349 31.689 47.766 1.00 63.42 O ANISOU 3316 O ASN B 142 7006 10993 6097 1933 -784 -1633 O ATOM 3317 CB ASN B 142 70.224 29.986 45.863 1.00 64.35 C ANISOU 3317 CB ASN B 142 7487 10415 6547 1993 -579 -1218 C ATOM 3318 CG ASN B 142 69.132 29.674 44.868 1.00 60.71 C ANISOU 3318 CG ASN B 142 7240 9543 6284 1898 -465 -1107 C ATOM 3319 OD1 ASN B 142 68.662 30.558 44.147 1.00 59.24 O ANISOU 3319 OD1 ASN B 142 7100 9170 6239 1684 -433 -1239 O ATOM 3320 ND2 ASN B 142 68.718 28.412 44.823 1.00 60.65 N ANISOU 3320 ND2 ASN B 142 7359 9392 6293 2059 -403 -860 N ATOM 3321 N THR B 143 73.085 32.203 46.430 1.00 71.65 N ANISOU 3321 N THR B 143 7823 12061 7339 1794 -816 -1855 N ATOM 3322 CA THR B 143 73.870 32.734 47.536 1.00 71.90 C ANISOU 3322 CA THR B 143 7629 12519 7172 1823 -944 -2045 C ATOM 3323 C THR B 143 73.168 33.932 48.182 1.00 70.37 C ANISOU 3323 C THR B 143 7443 12352 6943 1638 -952 -2267 C ATOM 3324 O THR B 143 72.684 34.842 47.495 1.00 68.03 O ANISOU 3324 O THR B 143 7216 11783 6849 1405 -880 -2401 O ATOM 3325 CB THR B 143 75.270 33.093 47.041 1.00 78.24 C ANISOU 3325 CB THR B 143 8197 13485 8045 1758 -996 -2224 C ATOM 3326 OG1 THR B 143 75.176 34.148 46.085 1.00 83.78 O ANISOU 3326 OG1 THR B 143 8917 13937 8980 1472 -921 -2410 O ATOM 3327 CG2 THR B 143 75.893 31.879 46.351 1.00 72.83 C ANISOU 3327 CG2 THR B 143 7513 12745 7412 1952 -969 -2006 C ATOM 3328 N TRP B 144 73.098 33.905 49.514 1.00 65.40 N ANISOU 3328 N TRP B 144 6745 12054 6051 1757 -1036 -2297 N ATOM 3329 CA TRP B 144 72.334 34.884 50.278 1.00 67.98 C ANISOU 3329 CA TRP B 144 7092 12427 6311 1623 -1034 -2495 C ATOM 3330 C TRP B 144 72.825 36.301 50.015 1.00 73.41 C ANISOU 3330 C TRP B 144 7632 13114 7145 1352 -1051 -2865 C ATOM 3331 O TRP B 144 74.026 36.552 49.910 1.00 70.76 O ANISOU 3331 O TRP B 144 7083 12987 6814 1314 -1128 -3025 O ATOM 3332 CB TRP B 144 72.427 34.560 51.770 1.00 66.80 C ANISOU 3332 CB TRP B 144 6854 12718 5808 1814 -1134 -2480 C ATOM 3333 CG TRP B 144 71.754 33.254 52.133 1.00 74.79 C ANISOU 3333 CG TRP B 144 8036 13695 6684 2065 -1088 -2099 C ATOM 3334 CD1 TRP B 144 72.368 32.087 52.486 1.00 72.42 C ANISOU 3334 CD1 TRP B 144 7690 13607 6218 2337 -1146 -1847 C ATOM 3335 CD2 TRP B 144 70.337 32.992 52.192 1.00 71.29 C ANISOU 3335 CD2 TRP B 144 7827 12983 6278 2064 -966 -1924 C ATOM 3336 NE1 TRP B 144 71.426 31.111 52.743 1.00 76.55 N ANISOU 3336 NE1 TRP B 144 8416 13984 6684 2497 -1058 -1519 N ATOM 3337 CE2 TRP B 144 70.175 31.641 52.568 1.00 70.05 C ANISOU 3337 CE2 TRP B 144 7760 12875 5981 2327 -947 -1567 C ATOM 3338 CE3 TRP B 144 69.195 33.764 51.943 1.00 66.96 C ANISOU 3338 CE3 TRP B 144 7410 12148 5882 1871 -867 -2030 C ATOM 3339 CZ2 TRP B 144 68.923 31.050 52.717 1.00 66.39 C ANISOU 3339 CZ2 TRP B 144 7509 12191 5526 2381 -827 -1326 C ATOM 3340 CZ3 TRP B 144 67.946 33.176 52.088 1.00 62.80 C ANISOU 3340 CZ3 TRP B 144 7084 11423 5355 1936 -759 -1795 C ATOM 3341 CH2 TRP B 144 67.819 31.832 52.478 1.00 63.34 C ANISOU 3341 CH2 TRP B 144 7234 11552 5282 2179 -737 -1452 C ATOM 3342 N SER B 145 71.874 37.216 49.827 1.00 78.58 N ANISOU 3342 N SER B 145 8402 13501 7953 1159 -967 -2990 N ATOM 3343 CA SER B 145 72.159 38.634 49.650 1.00 84.25 C ANISOU 3343 CA SER B 145 9008 14164 8840 894 -959 -3336 C ATOM 3344 C SER B 145 71.073 39.441 50.354 1.00 82.32 C ANISOU 3344 C SER B 145 8846 13853 8580 806 -915 -3488 C ATOM 3345 O SER B 145 69.941 38.977 50.514 1.00 77.90 O ANISOU 3345 O SER B 145 8472 13148 7979 899 -851 -3290 O ATOM 3346 CB SER B 145 72.256 39.011 48.165 1.00 85.34 C ANISOU 3346 CB SER B 145 9210 13913 9303 717 -863 -3308 C ATOM 3347 OG SER B 145 72.447 40.406 48.008 1.00 91.01 O ANISOU 3347 OG SER B 145 9836 14536 10207 458 -835 -3617 O ATOM 3348 N SER B 146 71.416 40.677 50.738 1.00 76.84 N ANISOU 3348 N SER B 146 8006 13249 7943 614 -938 -3855 N ATOM 3349 CA SER B 146 70.527 41.531 51.520 1.00 77.66 C ANISOU 3349 CA SER B 146 8149 13333 8025 531 -900 -4065 C ATOM 3350 C SER B 146 69.794 42.592 50.701 1.00 76.89 C ANISOU 3350 C SER B 146 8164 12773 8278 309 -772 -4162 C ATOM 3351 O SER B 146 68.867 43.219 51.225 1.00 79.89 O ANISOU 3351 O SER B 146 8611 13065 8680 261 -716 -4290 O ATOM 3352 CB SER B 146 71.321 42.241 52.625 1.00 86.80 C ANISOU 3352 CB SER B 146 9066 14907 9005 469 -1007 -4449 C ATOM 3353 OG SER B 146 72.065 43.335 52.097 1.00 88.78 O ANISOU 3353 OG SER B 146 9175 15044 9513 217 -996 -4746 O ATOM 3354 N ASP B 147 70.184 42.820 49.449 1.00 75.53 N ANISOU 3354 N ASP B 147 8009 12315 8375 181 -721 -4100 N ATOM 3355 CA ASP B 147 69.513 43.770 48.572 1.00 75.67 C ANISOU 3355 CA ASP B 147 8140 11886 8724 -9 -601 -4136 C ATOM 3356 C ASP B 147 68.908 43.031 47.379 1.00 76.51 C ANISOU 3356 C ASP B 147 8446 11673 8951 54 -532 -3770 C ATOM 3357 O ASP B 147 69.610 42.276 46.693 1.00 71.06 O ANISOU 3357 O ASP B 147 7739 11017 8243 111 -555 -3601 O ATOM 3358 CB ASP B 147 70.487 44.848 48.101 1.00 82.61 C ANISOU 3358 CB ASP B 147 8862 12698 9830 -247 -585 -4399 C ATOM 3359 CG ASP B 147 69.834 45.861 47.182 1.00 98.25 C ANISOU 3359 CG ASP B 147 10960 14207 12162 -435 -454 -4408 C ATOM 3360 OD1 ASP B 147 68.621 46.126 47.339 1.00105.50 O ANISOU 3360 OD1 ASP B 147 12026 14920 13141 -411 -392 -4365 O ATOM 3361 OD2 ASP B 147 70.536 46.399 46.304 1.00105.52 O ANISOU 3361 OD2 ASP B 147 11820 14969 13301 -601 -408 -4449 O ATOM 3362 N TRP B 148 67.608 43.257 47.123 1.00 70.49 N ANISOU 3362 N TRP B 148 7576 11088 8121 -264 -54 -3004 N ATOM 3363 CA TRP B 148 66.934 42.524 46.052 1.00 61.23 C ANISOU 3363 CA TRP B 148 6502 9705 7058 -91 -17 -2714 C ATOM 3364 C TRP B 148 67.427 42.969 44.682 1.00 64.46 C ANISOU 3364 C TRP B 148 6872 9928 7691 -171 32 -2635 C ATOM 3365 O TRP B 148 67.682 42.129 43.816 1.00 69.80 O ANISOU 3365 O TRP B 148 7537 10620 8365 -46 -4 -2420 O ATOM 3366 CB TRP B 148 65.412 42.676 46.153 1.00 60.76 C ANISOU 3366 CB TRP B 148 6621 9376 7089 -20 92 -2667 C ATOM 3367 CG TRP B 148 64.694 42.088 44.959 1.00 56.99 C ANISOU 3367 CG TRP B 148 6236 8670 6749 116 127 -2395 C ATOM 3368 CD1 TRP B 148 63.994 42.765 43.995 1.00 55.31 C ANISOU 3368 CD1 TRP B 148 6102 8129 6783 82 232 -2329 C ATOM 3369 CD2 TRP B 148 64.664 40.702 44.581 1.00 53.69 C ANISOU 3369 CD2 TRP B 148 5836 8346 6220 302 52 -2159 C ATOM 3370 NE1 TRP B 148 63.507 41.881 43.059 1.00 52.59 N ANISOU 3370 NE1 TRP B 148 5820 7693 6469 226 212 -2077 N ATOM 3371 CE2 TRP B 148 63.916 40.611 43.388 1.00 55.93 C ANISOU 3371 CE2 TRP B 148 6212 8357 6683 354 109 -1980 C ATOM 3372 CE3 TRP B 148 65.196 39.525 45.144 1.00 53.04 C ANISOU 3372 CE3 TRP B 148 5703 8548 5903 434 -53 -2079 C ATOM 3373 CZ2 TRP B 148 63.679 39.389 42.747 1.00 54.17 C ANISOU 3373 CZ2 TRP B 148 6042 8130 6411 511 64 -1754 C ATOM 3374 CZ3 TRP B 148 64.975 38.321 44.508 1.00 49.91 C ANISOU 3374 CZ3 TRP B 148 5364 8121 5477 603 -81 -1841 C ATOM 3375 CH2 TRP B 148 64.217 38.259 43.315 1.00 53.75 C ANISOU 3375 CH2 TRP B 148 5952 8325 6146 630 -22 -1694 C ATOM 3376 N ILE B 149 67.561 44.283 44.462 1.00 71.13 N ANISOU 3376 N ILE B 149 7709 10586 8732 -375 127 -2804 N ATOM 3377 CA ILE B 149 68.090 44.783 43.191 1.00 70.39 C ANISOU 3377 CA ILE B 149 7575 10323 8849 -464 188 -2726 C ATOM 3378 C ILE B 149 69.483 44.224 42.927 1.00 73.46 C ANISOU 3378 C ILE B 149 7778 11000 9133 -473 86 -2687 C ATOM 3379 O ILE B 149 69.842 43.931 41.779 1.00 76.37 O ANISOU 3379 O ILE B 149 8127 11304 9587 -424 107 -2508 O ATOM 3380 CB ILE B 149 68.071 46.323 43.182 1.00 72.77 C ANISOU 3380 CB ILE B 149 7894 10382 9372 -696 320 -2933 C ATOM 3381 CG1 ILE B 149 66.629 46.810 43.257 1.00 74.85 C ANISOU 3381 CG1 ILE B 149 8342 10333 9765 -640 440 -2919 C ATOM 3382 CG2 ILE B 149 68.757 46.875 41.941 1.00 65.77 C ANISOU 3382 CG2 ILE B 149 6951 9348 8691 -804 391 -2853 C ATOM 3383 CD1 ILE B 149 66.492 48.306 43.263 1.00 79.31 C ANISOU 3383 CD1 ILE B 149 8953 10616 10566 -837 594 -3108 C ATOM 3384 N GLU B 150 70.277 44.038 43.979 1.00 70.92 N ANISOU 3384 N GLU B 150 7314 11018 8616 -522 -25 -2846 N ATOM 3385 CA GLU B 150 71.593 43.439 43.810 1.00 74.28 C ANISOU 3385 CA GLU B 150 7537 11754 8932 -504 -129 -2795 C ATOM 3386 C GLU B 150 71.464 41.966 43.460 1.00 70.01 C ANISOU 3386 C GLU B 150 7033 11313 8253 -225 -193 -2523 C ATOM 3387 O GLU B 150 72.145 41.466 42.557 1.00 72.37 O ANISOU 3387 O GLU B 150 7258 11658 8583 -155 -198 -2368 O ATOM 3388 CB GLU B 150 72.404 43.586 45.096 1.00 89.79 C ANISOU 3388 CB GLU B 150 9331 14087 10700 -615 -250 -3026 C ATOM 3389 CG GLU B 150 73.910 43.482 44.929 1.00105.20 C ANISOU 3389 CG GLU B 150 11019 16345 12609 -694 -337 -3050 C ATOM 3390 CD GLU B 150 74.664 44.075 46.117 1.00118.85 C ANISOU 3390 CD GLU B 150 12571 18385 14203 -899 -440 -3347 C ATOM 3391 OE1 GLU B 150 74.404 45.248 46.478 1.00117.41 O ANISOU 3391 OE1 GLU B 150 12439 18039 14132 -1135 -368 -3600 O ATOM 3392 OE2 GLU B 150 75.529 43.363 46.678 1.00125.75 O ANISOU 3392 OE2 GLU B 150 13254 19670 14857 -821 -592 -3326 O ATOM 3393 N PHE B 151 70.610 41.249 44.189 1.00 66.30 N ANISOU 3393 N PHE B 151 6682 10879 7632 -65 -231 -2467 N ATOM 3394 CA PHE B 151 70.459 39.820 43.954 1.00 61.46 C ANISOU 3394 CA PHE B 151 6117 10344 6891 192 -281 -2219 C ATOM 3395 C PHE B 151 69.933 39.540 42.549 1.00 61.06 C ANISOU 3395 C PHE B 151 6194 9995 7009 272 -195 -2017 C ATOM 3396 O PHE B 151 70.483 38.706 41.822 1.00 65.35 O ANISOU 3396 O PHE B 151 6703 10601 7525 398 -214 -1852 O ATOM 3397 CB PHE B 151 69.538 39.207 45.012 1.00 56.99 C ANISOU 3397 CB PHE B 151 5666 9833 6153 323 -312 -2199 C ATOM 3398 CG PHE B 151 69.369 37.721 44.864 1.00 61.80 C ANISOU 3398 CG PHE B 151 6336 10505 6638 578 -351 -1950 C ATOM 3399 CD1 PHE B 151 70.261 36.846 45.488 1.00 58.83 C ANISOU 3399 CD1 PHE B 151 5834 10473 6046 709 -458 -1891 C ATOM 3400 CD2 PHE B 151 68.341 37.192 44.082 1.00 53.09 C ANISOU 3400 CD2 PHE B 151 5412 9119 5639 686 -281 -1773 C ATOM 3401 CE1 PHE B 151 70.122 35.464 45.354 1.00 53.64 C ANISOU 3401 CE1 PHE B 151 5247 9844 5290 952 -474 -1655 C ATOM 3402 CE2 PHE B 151 68.206 35.809 43.933 1.00 57.09 C ANISOU 3402 CE2 PHE B 151 5986 9661 6045 903 -306 -1559 C ATOM 3403 CZ PHE B 151 69.097 34.942 44.572 1.00 50.48 C ANISOU 3403 CZ PHE B 151 5041 9135 5005 1040 -392 -1498 C ATOM 3404 N TYR B 152 68.860 40.230 42.152 1.00 57.50 N ANISOU 3404 N TYR B 152 5892 9227 6729 207 -98 -2027 N ATOM 3405 CA TYR B 152 68.214 39.918 40.884 1.00 54.46 C ANISOU 3405 CA TYR B 152 5638 8583 6473 291 -35 -1830 C ATOM 3406 C TYR B 152 69.085 40.324 39.702 1.00 55.24 C ANISOU 3406 C TYR B 152 5659 8632 6698 212 11 -1786 C ATOM 3407 O TYR B 152 69.148 39.611 38.696 1.00 60.59 O ANISOU 3407 O TYR B 152 6384 9257 7379 328 20 -1607 O ATOM 3408 CB TYR B 152 66.845 40.597 40.821 1.00 53.86 C ANISOU 3408 CB TYR B 152 5713 8210 6541 250 50 -1844 C ATOM 3409 CG TYR B 152 66.010 40.112 39.670 1.00 53.15 C ANISOU 3409 CG TYR B 152 5757 7899 6539 357 85 -1632 C ATOM 3410 CD1 TYR B 152 65.384 38.855 39.717 1.00 49.76 C ANISOU 3410 CD1 TYR B 152 5417 7492 5996 531 37 -1483 C ATOM 3411 CD2 TYR B 152 65.856 40.891 38.520 1.00 49.92 C ANISOU 3411 CD2 TYR B 152 5385 7262 6321 280 165 -1577 C ATOM 3412 CE1 TYR B 152 64.611 38.400 38.654 1.00 47.71 C ANISOU 3412 CE1 TYR B 152 5277 7043 5809 607 57 -1310 C ATOM 3413 CE2 TYR B 152 65.081 40.443 37.457 1.00 54.32 C ANISOU 3413 CE2 TYR B 152 6061 7648 6932 375 179 -1387 C ATOM 3414 CZ TYR B 152 64.472 39.198 37.528 1.00 50.57 C ANISOU 3414 CZ TYR B 152 5667 7211 6339 529 119 -1267 C ATOM 3415 OH TYR B 152 63.720 38.766 36.471 1.00 55.68 O ANISOU 3415 OH TYR B 152 6423 7700 7032 598 123 -1102 O ATOM 3416 N GLY B 153 69.775 41.459 39.807 1.00 58.87 N ANISOU 3416 N GLY B 153 6003 9105 7259 10 49 -1954 N ATOM 3417 CA GLY B 153 70.632 41.890 38.715 1.00 57.28 C ANISOU 3417 CA GLY B 153 5718 8860 7184 -78 110 -1907 C ATOM 3418 C GLY B 153 71.820 40.971 38.509 1.00 62.82 C ANISOU 3418 C GLY B 153 6271 9844 7755 20 43 -1827 C ATOM 3419 O GLY B 153 72.218 40.705 37.370 1.00 66.62 O ANISOU 3419 O GLY B 153 6750 10274 8287 70 94 -1684 O ATOM 3420 N GLU B 154 72.389 40.452 39.598 1.00 65.43 N ANISOU 3420 N GLU B 154 6474 10482 7905 65 -67 -1907 N ATOM 3421 CA GLU B 154 73.602 39.644 39.491 1.00 62.94 C ANISOU 3421 CA GLU B 154 5982 10459 7472 167 -128 -1832 C ATOM 3422 C GLU B 154 73.302 38.151 39.391 1.00 66.45 C ANISOU 3422 C GLU B 154 6525 10954 7768 447 -171 -1632 C ATOM 3423 O GLU B 154 73.738 37.493 38.445 1.00 67.48 O ANISOU 3423 O GLU B 154 6655 11079 7906 567 -134 -1479 O ATOM 3424 CB GLU B 154 74.534 39.945 40.660 1.00 67.07 C ANISOU 3424 CB GLU B 154 6280 11321 7884 59 -230 -2019 C ATOM 3425 CG GLU B 154 75.019 41.379 40.648 1.00 79.63 C ANISOU 3425 CG GLU B 154 7755 12863 9638 -241 -177 -2227 C ATOM 3426 CD GLU B 154 75.732 41.761 41.934 1.00101.81 C ANISOU 3426 CD GLU B 154 10365 15995 12322 -382 -291 -2457 C ATOM 3427 OE1 GLU B 154 75.953 40.865 42.782 1.00106.00 O ANISOU 3427 OE1 GLU B 154 10828 16823 12625 -224 -418 -2425 O ATOM 3428 OE2 GLU B 154 76.046 42.960 42.110 1.00110.86 O ANISOU 3428 OE2 GLU B 154 11432 17095 13595 -653 -252 -2671 O ATOM 3429 N LYS B 155 72.581 37.594 40.357 1.00 66.76 N ANISOU 3429 N LYS B 155 6653 11039 7672 551 -236 -1631 N ATOM 3430 CA LYS B 155 72.372 36.150 40.344 1.00 63.93 C ANISOU 3430 CA LYS B 155 6382 10729 7179 809 -267 -1442 C ATOM 3431 C LYS B 155 71.197 35.707 39.472 1.00 67.23 C ANISOU 3431 C LYS B 155 7042 10824 7679 892 -196 -1302 C ATOM 3432 O LYS B 155 71.020 34.500 39.276 1.00 65.50 O ANISOU 3432 O LYS B 155 6914 10597 7376 1088 -202 -1148 O ATOM 3433 CB LYS B 155 72.203 35.658 41.780 1.00 63.38 C ANISOU 3433 CB LYS B 155 6292 10877 6914 895 -362 -1479 C ATOM 3434 CG LYS B 155 73.468 35.951 42.593 1.00 75.26 C ANISOU 3434 CG LYS B 155 7536 12757 8303 832 -457 -1602 C ATOM 3435 CD LYS B 155 73.221 36.898 43.730 1.00 91.25 C ANISOU 3435 CD LYS B 155 9520 14871 10278 650 -505 -1830 C ATOM 3436 CE LYS B 155 74.489 37.660 44.127 1.00103.58 C ANISOU 3436 CE LYS B 155 10813 16726 11815 472 -576 -2011 C ATOM 3437 NZ LYS B 155 74.214 38.694 45.176 1.00103.74 N ANISOU 3437 NZ LYS B 155 10817 16800 11799 260 -609 -2275 N ATOM 3438 N ARG B 156 70.428 36.635 38.897 1.00 59.76 N ANISOU 3438 N ARG B 156 6196 9613 6898 749 -127 -1347 N ATOM 3439 CA ARG B 156 69.358 36.237 37.995 1.00 55.78 C ANISOU 3439 CA ARG B 156 5893 8835 6464 820 -76 -1211 C ATOM 3440 C ARG B 156 69.625 36.721 36.571 1.00 56.63 C ANISOU 3440 C ARG B 156 6017 8791 6708 753 2 -1154 C ATOM 3441 O ARG B 156 69.957 35.911 35.700 1.00 53.92 O ANISOU 3441 O ARG B 156 5714 8446 6326 871 21 -1028 O ATOM 3442 CB ARG B 156 67.999 36.738 38.506 1.00 49.31 C ANISOU 3442 CB ARG B 156 5196 7834 5706 759 -63 -1263 C ATOM 3443 CG ARG B 156 67.547 36.014 39.769 1.00 55.52 C ANISOU 3443 CG ARG B 156 6011 8745 6340 861 -121 -1270 C ATOM 3444 CD ARG B 156 67.156 34.563 39.484 1.00 58.72 C ANISOU 3444 CD ARG B 156 6536 9116 6658 1056 -135 -1088 C ATOM 3445 NE ARG B 156 66.789 33.845 40.701 1.00 55.54 N ANISOU 3445 NE ARG B 156 6158 8835 6108 1160 -176 -1071 N ATOM 3446 CZ ARG B 156 67.655 33.190 41.468 1.00 56.92 C ANISOU 3446 CZ ARG B 156 6237 9274 6117 1270 -233 -1053 C ATOM 3447 NH1 ARG B 156 68.933 33.145 41.127 1.00 53.01 N ANISOU 3447 NH1 ARG B 156 5600 8950 5593 1291 -257 -1055 N ATOM 3448 NH2 ARG B 156 67.243 32.574 42.576 1.00 53.35 N ANISOU 3448 NH2 ARG B 156 5821 8925 5524 1367 -260 -1020 N ATOM 3449 N LEU B 157 69.442 38.013 36.297 1.00 57.57 N ANISOU 3449 N LEU B 157 6123 8769 6983 574 60 -1238 N ATOM 3450 CA LEU B 157 69.689 38.506 34.945 1.00 56.45 C ANISOU 3450 CA LEU B 157 6002 8486 6961 515 145 -1163 C ATOM 3451 C LEU B 157 71.153 38.334 34.550 1.00 59.22 C ANISOU 3451 C LEU B 157 6188 9036 7275 518 163 -1154 C ATOM 3452 O LEU B 157 71.453 37.869 33.443 1.00 57.61 O ANISOU 3452 O LEU B 157 6028 8800 7063 596 213 -1028 O ATOM 3453 CB LEU B 157 69.273 39.965 34.818 1.00 52.42 C ANISOU 3453 CB LEU B 157 5502 7781 6636 328 218 -1245 C ATOM 3454 CG LEU B 157 67.813 40.323 35.076 1.00 49.09 C ANISOU 3454 CG LEU B 157 5225 7141 6286 324 226 -1243 C ATOM 3455 CD1 LEU B 157 67.582 41.832 34.846 1.00 48.38 C ANISOU 3455 CD1 LEU B 157 5135 6845 6400 152 325 -1311 C ATOM 3456 CD2 LEU B 157 66.854 39.465 34.254 1.00 45.13 C ANISOU 3456 CD2 LEU B 157 4887 6513 5749 467 208 -1065 C ATOM 3457 N GLY B 158 72.078 38.717 35.447 1.00 57.53 N ANISOU 3457 N GLY B 158 5778 9043 7036 428 126 -1293 N ATOM 3458 CA GLY B 158 73.496 38.728 35.097 1.00 56.94 C ANISOU 3458 CA GLY B 158 5506 9172 6956 402 150 -1294 C ATOM 3459 C GLY B 158 74.038 37.348 34.767 1.00 61.43 C ANISOU 3459 C GLY B 158 6062 9895 7382 631 128 -1154 C ATOM 3460 O GLY B 158 74.739 37.173 33.770 1.00 63.54 O ANISOU 3460 O GLY B 158 6288 10182 7673 669 203 -1066 O ATOM 3461 N TYR B 159 73.675 36.339 35.566 1.00 58.89 N ANISOU 3461 N TYR B 159 5794 9665 6916 797 42 -1122 N ATOM 3462 CA TYR B 159 74.090 34.969 35.277 1.00 60.35 C ANISOU 3462 CA TYR B 159 5998 9952 6978 1035 38 -980 C ATOM 3463 C TYR B 159 73.578 34.509 33.918 1.00 60.49 C ANISOU 3463 C TYR B 159 6216 9735 7034 1115 124 -849 C ATOM 3464 O TYR B 159 74.327 33.925 33.129 1.00 58.61 O ANISOU 3464 O TYR B 159 5949 9555 6763 1226 186 -762 O ATOM 3465 CB TYR B 159 73.596 34.036 36.380 1.00 61.34 C ANISOU 3465 CB TYR B 159 6184 10161 6961 1188 -53 -956 C ATOM 3466 CG TYR B 159 73.966 32.572 36.236 1.00 62.62 C ANISOU 3466 CG TYR B 159 6384 10406 7004 1449 -49 -806 C ATOM 3467 CD1 TYR B 159 75.171 32.082 36.723 1.00 63.80 C ANISOU 3467 CD1 TYR B 159 6327 10858 7057 1570 -84 -778 C ATOM 3468 CD2 TYR B 159 73.094 31.676 35.640 1.00 64.75 C ANISOU 3468 CD2 TYR B 159 6891 10449 7261 1575 -8 -693 C ATOM 3469 CE1 TYR B 159 75.496 30.741 36.604 1.00 67.22 C ANISOU 3469 CE1 TYR B 159 6803 11343 7395 1831 -62 -629 C ATOM 3470 CE2 TYR B 159 73.404 30.344 35.518 1.00 64.52 C ANISOU 3470 CE2 TYR B 159 6919 10458 7139 1808 15 -567 C ATOM 3471 CZ TYR B 159 74.605 29.879 35.998 1.00 69.33 C ANISOU 3471 CZ TYR B 159 7333 11346 7662 1946 -4 -529 C ATOM 3472 OH TYR B 159 74.895 28.542 35.872 1.00 70.14 O ANISOU 3472 OH TYR B 159 7504 11461 7687 2200 37 -392 O ATOM 3473 N GLN B 160 72.302 34.773 33.617 1.00 59.19 N ANISOU 3473 N GLN B 160 6249 9313 6928 1060 131 -838 N ATOM 3474 CA GLN B 160 71.741 34.316 32.346 1.00 53.87 C ANISOU 3474 CA GLN B 160 5766 8437 6265 1125 192 -722 C ATOM 3475 C GLN B 160 72.385 35.025 31.155 1.00 53.81 C ANISOU 3475 C GLN B 160 5711 8395 6338 1036 292 -695 C ATOM 3476 O GLN B 160 72.643 34.397 30.119 1.00 52.86 O ANISOU 3476 O GLN B 160 5670 8246 6169 1139 356 -601 O ATOM 3477 CB GLN B 160 70.223 34.516 32.345 1.00 54.45 C ANISOU 3477 CB GLN B 160 6025 8277 6387 1075 163 -714 C ATOM 3478 CG GLN B 160 69.463 33.558 33.255 1.00 46.29 C ANISOU 3478 CG GLN B 160 5082 7240 5264 1190 91 -699 C ATOM 3479 CD GLN B 160 69.310 32.180 32.647 1.00 52.42 C ANISOU 3479 CD GLN B 160 6007 7961 5951 1362 105 -588 C ATOM 3480 OE1 GLN B 160 69.376 32.019 31.436 1.00 59.64 O ANISOU 3480 OE1 GLN B 160 7007 8782 6871 1377 159 -530 O ATOM 3481 NE2 GLN B 160 69.130 31.174 33.489 1.00 50.19 N ANISOU 3481 NE2 GLN B 160 5761 7731 5578 1492 64 -559 N ATOM 3482 N LEU B 161 72.669 36.325 31.287 1.00 53.19 N ANISOU 3482 N LEU B 161 5511 8317 6382 844 320 -778 N ATOM 3483 CA LEU B 161 73.294 37.069 30.194 1.00 56.23 C ANISOU 3483 CA LEU B 161 5846 8663 6856 746 433 -739 C ATOM 3484 C LEU B 161 74.688 36.544 29.901 1.00 64.12 C ANISOU 3484 C LEU B 161 6682 9886 7794 831 484 -708 C ATOM 3485 O LEU B 161 75.053 36.321 28.739 1.00 64.10 O ANISOU 3485 O LEU B 161 6727 9854 7774 885 583 -611 O ATOM 3486 CB LEU B 161 73.386 38.550 30.543 1.00 51.71 C ANISOU 3486 CB LEU B 161 5166 8038 6444 515 463 -846 C ATOM 3487 CG LEU B 161 72.091 39.356 30.591 1.00 52.91 C ANISOU 3487 CG LEU B 161 5466 7934 6702 418 460 -861 C ATOM 3488 CD1 LEU B 161 72.433 40.771 31.033 1.00 54.43 C ANISOU 3488 CD1 LEU B 161 5533 8089 7059 194 511 -988 C ATOM 3489 CD2 LEU B 161 71.384 39.342 29.224 1.00 41.18 C ANISOU 3489 CD2 LEU B 161 4168 6246 5232 463 522 -705 C ATOM 3490 N LYS B 162 75.484 36.348 30.953 1.00 67.06 N ANISOU 3490 N LYS B 162 6854 10502 8124 848 420 -788 N ATOM 3491 CA LYS B 162 76.828 35.819 30.778 1.00 64.70 C ANISOU 3491 CA LYS B 162 6365 10447 7771 948 461 -750 C ATOM 3492 C LYS B 162 76.770 34.435 30.141 1.00 63.17 C ANISOU 3492 C LYS B 162 6318 10230 7453 1202 496 -621 C ATOM 3493 O LYS B 162 77.564 34.110 29.247 1.00 58.59 O ANISOU 3493 O LYS B 162 5694 9711 6855 1285 603 -546 O ATOM 3494 CB LYS B 162 77.557 35.821 32.121 1.00 68.32 C ANISOU 3494 CB LYS B 162 6581 11189 8188 931 357 -853 C ATOM 3495 CG LYS B 162 78.944 35.223 32.089 1.00 83.56 C ANISOU 3495 CG LYS B 162 8278 13411 10059 1057 381 -804 C ATOM 3496 CD LYS B 162 79.808 35.835 33.191 1.00 91.50 C ANISOU 3496 CD LYS B 162 8980 14707 11078 920 291 -937 C ATOM 3497 CE LYS B 162 81.290 35.512 32.985 1.00 99.82 C ANISOU 3497 CE LYS B 162 9748 16064 12115 999 333 -886 C ATOM 3498 NZ LYS B 162 82.163 36.313 33.898 1.00102.24 N ANISOU 3498 NZ LYS B 162 9734 16656 12458 804 248 -1033 N ATOM 3499 N LEU B 163 75.796 33.627 30.552 1.00 59.95 N ANISOU 3499 N LEU B 163 6097 9714 6966 1320 421 -598 N ATOM 3500 CA LEU B 163 75.636 32.299 29.975 1.00 64.88 C ANISOU 3500 CA LEU B 163 6892 10276 7486 1543 459 -495 C ATOM 3501 C LEU B 163 75.275 32.361 28.485 1.00 71.63 C ANISOU 3501 C LEU B 163 7930 10935 8353 1526 563 -431 C ATOM 3502 O LEU B 163 75.716 31.510 27.702 1.00 70.45 O ANISOU 3502 O LEU B 163 7848 10793 8128 1682 650 -363 O ATOM 3503 CB LEU B 163 74.572 31.545 30.771 1.00 64.07 C ANISOU 3503 CB LEU B 163 6950 10074 7319 1629 363 -491 C ATOM 3504 CG LEU B 163 74.134 30.153 30.342 1.00 61.58 C ANISOU 3504 CG LEU B 163 6850 9635 6911 1831 392 -403 C ATOM 3505 CD1 LEU B 163 75.351 29.199 30.271 1.00 56.82 C ANISOU 3505 CD1 LEU B 163 6144 9209 6234 2050 460 -337 C ATOM 3506 CD2 LEU B 163 73.034 29.655 31.282 1.00 55.50 C ANISOU 3506 CD2 LEU B 163 6209 8770 6110 1860 296 -408 C ATOM 3507 N ALA B 164 74.481 33.358 28.066 1.00 65.71 N ANISOU 3507 N ALA B 164 7266 10012 7687 1348 562 -450 N ATOM 3508 CA ALA B 164 74.173 33.484 26.638 1.00 64.87 C ANISOU 3508 CA ALA B 164 7323 9754 7573 1331 652 -376 C ATOM 3509 C ALA B 164 75.375 33.986 25.834 1.00 64.54 C ANISOU 3509 C ALA B 164 7136 9827 7560 1295 788 -342 C ATOM 3510 O ALA B 164 75.555 33.588 24.676 1.00 62.13 O ANISOU 3510 O ALA B 164 6942 9484 7182 1373 888 -269 O ATOM 3511 CB ALA B 164 72.967 34.399 26.428 1.00 61.53 C ANISOU 3511 CB ALA B 164 7022 9126 7231 1174 611 -378 C ATOM 3512 N ARG B 165 76.198 34.858 26.424 1.00 65.89 N ANISOU 3512 N ARG B 165 7060 10142 7834 1168 798 -399 N ATOM 3513 CA ARG B 165 77.410 35.321 25.749 1.00 70.22 C ANISOU 3513 CA ARG B 165 7435 10819 8425 1122 934 -366 C ATOM 3514 C ARG B 165 78.380 34.169 25.488 1.00 71.56 C ANISOU 3514 C ARG B 165 7539 11166 8485 1342 1002 -315 C ATOM 3515 O ARG B 165 79.080 34.163 24.471 1.00 74.21 O ANISOU 3515 O ARG B 165 7849 11544 8804 1377 1148 -247 O ATOM 3516 CB ARG B 165 78.093 36.411 26.578 1.00 67.69 C ANISOU 3516 CB ARG B 165 6847 10630 8244 925 916 -461 C ATOM 3517 CG ARG B 165 79.093 37.260 25.804 1.00 66.47 C ANISOU 3517 CG ARG B 165 6529 10539 8186 794 1069 -426 C ATOM 3518 CD ARG B 165 80.012 38.040 26.763 1.00 69.67 C ANISOU 3518 CD ARG B 165 6622 11140 8709 620 1039 -543 C ATOM 3519 NE ARG B 165 80.485 37.167 27.838 1.00 79.11 N ANISOU 3519 NE ARG B 165 7667 12579 9810 759 919 -599 N ATOM 3520 CZ ARG B 165 81.250 37.550 28.858 1.00 82.46 C ANISOU 3520 CZ ARG B 165 7815 13235 10280 652 845 -711 C ATOM 3521 NH1 ARG B 165 81.664 38.813 28.957 1.00 85.41 N ANISOU 3521 NH1 ARG B 165 8028 13614 10810 381 886 -801 N ATOM 3522 NH2 ARG B 165 81.604 36.660 29.782 1.00 77.40 N ANISOU 3522 NH2 ARG B 165 7060 12824 9526 815 730 -730 N ATOM 3523 N ASP B 166 78.464 33.204 26.414 1.00 67.61 N ANISOU 3523 N ASP B 166 7003 10774 7913 1502 911 -339 N ATOM 3524 CA ASP B 166 79.383 32.077 26.265 1.00 68.10 C ANISOU 3524 CA ASP B 166 6996 10996 7883 1740 981 -281 C ATOM 3525 C ASP B 166 78.838 31.017 25.312 1.00 68.60 C ANISOU 3525 C ASP B 166 7352 10883 7832 1916 1051 -217 C ATOM 3526 O ASP B 166 79.608 30.386 24.581 1.00 74.57 O ANISOU 3526 O ASP B 166 8099 11707 8527 2073 1186 -162 O ATOM 3527 CB ASP B 166 79.684 31.446 27.624 1.00 71.63 C ANISOU 3527 CB ASP B 166 7299 11624 8293 1860 862 -308 C ATOM 3528 CG ASP B 166 80.420 32.391 28.571 1.00 81.81 C ANISOU 3528 CG ASP B 166 8270 13147 9668 1696 790 -387 C ATOM 3529 OD1 ASP B 166 80.907 33.457 28.127 1.00 88.63 O ANISOU 3529 OD1 ASP B 166 8996 14042 10636 1501 859 -418 O ATOM 3530 OD2 ASP B 166 80.509 32.064 29.772 1.00 83.35 O ANISOU 3530 OD2 ASP B 166 8354 13496 9819 1755 665 -422 O ATOM 3531 N GLN B 167 77.525 30.779 25.325 1.00 64.35 N ANISOU 3531 N GLN B 167 7067 10123 7259 1893 966 -233 N ATOM 3532 CA GLN B 167 76.943 29.726 24.493 1.00 60.88 C ANISOU 3532 CA GLN B 167 6909 9516 6707 2036 1015 -199 C ATOM 3533 C GLN B 167 76.765 30.146 23.040 1.00 66.52 C ANISOU 3533 C GLN B 167 7767 10123 7385 1963 1121 -166 C ATOM 3534 O GLN B 167 76.778 29.288 22.149 1.00 63.49 O ANISOU 3534 O GLN B 167 7563 9674 6888 2097 1213 -145 O ATOM 3535 CB GLN B 167 75.595 29.268 25.048 1.00 56.52 C ANISOU 3535 CB GLN B 167 6559 8783 6134 2028 882 -228 C ATOM 3536 CG GLN B 167 75.721 28.594 26.386 1.00 73.09 C ANISOU 3536 CG GLN B 167 8568 10974 8228 2145 798 -237 C ATOM 3537 CD GLN B 167 74.556 27.687 26.696 1.00 77.83 C ANISOU 3537 CD GLN B 167 9406 11384 8782 2207 726 -239 C ATOM 3538 OE1 GLN B 167 74.730 26.650 27.353 1.00 89.42 O ANISOU 3538 OE1 GLN B 167 10891 12879 10206 2385 721 -210 O ATOM 3539 NE2 GLN B 167 73.364 28.058 26.227 1.00 64.47 N ANISOU 3539 NE2 GLN B 167 7892 9501 7103 2065 674 -262 N ATOM 3540 N TYR B 168 76.517 31.428 22.791 1.00 62.85 N ANISOU 3540 N TYR B 168 7251 9624 7006 1754 1111 -162 N ATOM 3541 CA TYR B 168 76.180 31.899 21.462 1.00 62.51 C ANISOU 3541 CA TYR B 168 7359 9473 6918 1680 1194 -109 C ATOM 3542 C TYR B 168 77.071 33.035 20.977 1.00 61.45 C ANISOU 3542 C TYR B 168 7040 9439 6869 1554 1317 -62 C ATOM 3543 O TYR B 168 76.820 33.568 19.896 1.00 65.11 O ANISOU 3543 O TYR B 168 7617 9822 7299 1483 1394 4 O ATOM 3544 CB TYR B 168 74.717 32.380 21.408 1.00 59.99 C ANISOU 3544 CB TYR B 168 7218 8957 6618 1549 1072 -111 C ATOM 3545 CG TYR B 168 73.668 31.402 21.865 1.00 57.61 C ANISOU 3545 CG TYR B 168 7097 8536 6255 1626 948 -154 C ATOM 3546 CD1 TYR B 168 73.195 30.406 21.017 1.00 51.21 C ANISOU 3546 CD1 TYR B 168 6528 7630 5300 1728 968 -150 C ATOM 3547 CD2 TYR B 168 73.090 31.518 23.127 1.00 56.77 C ANISOU 3547 CD2 TYR B 168 6930 8405 6235 1579 816 -203 C ATOM 3548 CE1 TYR B 168 72.183 29.520 21.425 1.00 49.94 C ANISOU 3548 CE1 TYR B 168 6533 7343 5101 1772 859 -193 C ATOM 3549 CE2 TYR B 168 72.094 30.636 23.549 1.00 56.49 C ANISOU 3549 CE2 TYR B 168 7056 8254 6153 1638 715 -230 C ATOM 3550 CZ TYR B 168 71.647 29.641 22.700 1.00 58.19 C ANISOU 3550 CZ TYR B 168 7499 8365 6244 1728 737 -223 C ATOM 3551 OH TYR B 168 70.666 28.783 23.140 1.00 59.05 O ANISOU 3551 OH TYR B 168 7757 8352 6326 1764 645 -253 O ATOM 3552 N GLY B 169 78.071 33.446 21.749 1.00 69.64 N ANISOU 3552 N GLY B 169 7794 10652 8013 1513 1334 -91 N ATOM 3553 CA GLY B 169 78.794 34.669 21.437 1.00 68.12 C ANISOU 3553 CA GLY B 169 7414 10528 7941 1341 1437 -60 C ATOM 3554 C GLY B 169 77.907 35.889 21.329 1.00 71.28 C ANISOU 3554 C GLY B 169 7889 10748 8445 1128 1395 -49 C ATOM 3555 O GLY B 169 78.261 36.848 20.637 1.00 70.65 O ANISOU 3555 O GLY B 169 7758 10649 8438 999 1516 16 O ATOM 3556 N ASP B 170 76.779 35.901 22.041 1.00 70.69 N ANISOU 3556 N ASP B 170 7926 10541 8391 1094 1238 -102 N ATOM 3557 CA ASP B 170 75.804 36.986 21.940 1.00 62.63 C ANISOU 3557 CA ASP B 170 6995 9330 7470 926 1199 -82 C ATOM 3558 C ASP B 170 76.251 38.110 22.866 1.00 65.43 C ANISOU 3558 C ASP B 170 7124 9722 8014 737 1192 -160 C ATOM 3559 O ASP B 170 75.716 38.314 23.957 1.00 70.16 O ANISOU 3559 O ASP B 170 7694 10285 8679 679 1070 -256 O ATOM 3560 CB ASP B 170 74.410 36.482 22.294 1.00 61.75 C ANISOU 3560 CB ASP B 170 7085 9071 7304 977 1047 -106 C ATOM 3561 CG ASP B 170 73.307 37.440 21.871 1.00 65.12 C ANISOU 3561 CG ASP B 170 7641 9299 7802 855 1023 -45 C ATOM 3562 OD1 ASP B 170 73.594 38.639 21.645 1.00 61.40 O ANISOU 3562 OD1 ASP B 170 7084 8783 7463 710 1110 -6 O ATOM 3563 OD2 ASP B 170 72.137 36.984 21.778 1.00 66.03 O ANISOU 3563 OD2 ASP B 170 7938 9300 7850 907 920 -30 O ATOM 3564 N SER B 171 77.272 38.845 22.418 1.00 69.18 N ANISOU 3564 N SER B 171 7436 10275 8575 631 1336 -126 N ATOM 3565 CA SER B 171 77.778 39.980 23.180 1.00 70.13 C ANISOU 3565 CA SER B 171 7339 10422 8887 417 1350 -213 C ATOM 3566 C SER B 171 76.868 41.195 23.097 1.00 69.75 C ANISOU 3566 C SER B 171 7398 10123 8982 248 1358 -195 C ATOM 3567 O SER B 171 76.988 42.100 23.930 1.00 78.01 O ANISOU 3567 O SER B 171 8313 11137 10189 69 1342 -304 O ATOM 3568 CB SER B 171 79.176 40.370 22.697 1.00 74.60 C ANISOU 3568 CB SER B 171 7683 11145 9515 343 1514 -178 C ATOM 3569 OG SER B 171 79.161 40.634 21.308 1.00 71.92 O ANISOU 3569 OG SER B 171 7473 10709 9143 353 1671 -22 O ATOM 3570 N ALA B 172 75.994 41.262 22.096 1.00 63.11 N ANISOU 3570 N ALA B 172 6785 9108 8084 299 1390 -61 N ATOM 3571 CA ALA B 172 75.055 42.376 22.023 1.00 60.45 C ANISOU 3571 CA ALA B 172 6552 8530 7885 172 1396 -20 C ATOM 3572 C ALA B 172 74.041 42.323 23.164 1.00 64.32 C ANISOU 3572 C ALA B 172 7091 8934 8413 171 1232 -137 C ATOM 3573 O ALA B 172 73.811 43.329 23.845 1.00 73.00 O ANISOU 3573 O ALA B 172 8134 9916 9687 17 1236 -215 O ATOM 3574 CB ALA B 172 74.353 42.384 20.668 1.00 59.77 C ANISOU 3574 CB ALA B 172 6687 8319 7703 250 1451 168 C ATOM 3575 N ILE B 173 73.401 41.164 23.376 1.00 60.80 N ANISOU 3575 N ILE B 173 6760 8532 7810 336 1102 -153 N ATOM 3576 CA ILE B 173 72.443 41.059 24.480 1.00 61.99 C ANISOU 3576 CA ILE B 173 6950 8614 7989 340 960 -254 C ATOM 3577 C ILE B 173 73.156 41.214 25.812 1.00 64.19 C ANISOU 3577 C ILE B 173 7023 9031 8334 257 918 -428 C ATOM 3578 O ILE B 173 72.593 41.763 26.767 1.00 69.27 O ANISOU 3578 O ILE B 173 7652 9594 9073 171 858 -533 O ATOM 3579 CB ILE B 173 71.630 39.747 24.410 1.00 60.18 C ANISOU 3579 CB ILE B 173 6883 8397 7584 522 842 -228 C ATOM 3580 CG1 ILE B 173 70.286 39.926 25.135 1.00 60.82 C ANISOU 3580 CG1 ILE B 173 7055 8334 7720 508 731 -266 C ATOM 3581 CG2 ILE B 173 72.391 38.579 25.009 1.00 49.74 C ANISOU 3581 CG2 ILE B 173 5474 7281 6143 642 795 -304 C ATOM 3582 CD1 ILE B 173 69.220 38.867 24.774 1.00 54.93 C ANISOU 3582 CD1 ILE B 173 6497 7540 6835 646 632 -205 C ATOM 3583 N TYR B 174 74.413 40.771 25.889 1.00 62.10 N ANISOU 3583 N TYR B 174 6590 8987 8018 281 953 -462 N ATOM 3584 CA TYR B 174 75.184 40.908 27.118 1.00 60.69 C ANISOU 3584 CA TYR B 174 6190 8988 7883 200 899 -622 C ATOM 3585 C TYR B 174 75.441 42.370 27.459 1.00 68.32 C ANISOU 3585 C TYR B 174 7040 9866 9053 -51 968 -715 C ATOM 3586 O TYR B 174 75.381 42.761 28.632 1.00 71.39 O ANISOU 3586 O TYR B 174 7339 10289 9496 -153 892 -878 O ATOM 3587 CB TYR B 174 76.510 40.159 26.986 1.00 64.00 C ANISOU 3587 CB TYR B 174 6431 9674 8211 289 933 -610 C ATOM 3588 CG TYR B 174 77.373 40.264 28.215 1.00 67.24 C ANISOU 3588 CG TYR B 174 6585 10317 8645 212 862 -763 C ATOM 3589 CD1 TYR B 174 78.263 41.323 28.377 1.00 66.08 C ANISOU 3589 CD1 TYR B 174 6223 10239 8648 -10 933 -846 C ATOM 3590 CD2 TYR B 174 77.284 39.309 29.231 1.00 63.62 C ANISOU 3590 CD2 TYR B 174 6099 10017 8058 353 721 -822 C ATOM 3591 CE1 TYR B 174 79.054 41.424 29.516 1.00 69.51 C ANISOU 3591 CE1 TYR B 174 6407 10915 9087 -97 849 -1001 C ATOM 3592 CE2 TYR B 174 78.065 39.399 30.372 1.00 62.71 C ANISOU 3592 CE2 TYR B 174 5743 10148 7936 289 640 -955 C ATOM 3593 CZ TYR B 174 78.952 40.457 30.508 1.00 72.56 C ANISOU 3593 CZ TYR B 174 6768 11483 9320 60 695 -1052 C ATOM 3594 OH TYR B 174 79.730 40.550 31.638 1.00 82.51 O ANISOU 3594 OH TYR B 174 7776 13015 10559 -18 598 -1197 O ATOM 3595 N GLN B 175 75.728 43.195 26.453 1.00 67.75 N ANISOU 3595 N GLN B 175 6975 9674 9091 -155 1120 -617 N ATOM 3596 CA GLN B 175 76.036 44.592 26.727 1.00 67.79 C ANISOU 3596 CA GLN B 175 6876 9568 9313 -405 1211 -702 C ATOM 3597 C GLN B 175 74.767 45.385 27.012 1.00 69.49 C ANISOU 3597 C GLN B 175 7259 9499 9643 -465 1197 -723 C ATOM 3598 O GLN B 175 74.701 46.129 27.997 1.00 65.25 O ANISOU 3598 O GLN B 175 6654 8909 9228 -621 1177 -894 O ATOM 3599 CB GLN B 175 76.791 45.209 25.548 1.00 73.61 C ANISOU 3599 CB GLN B 175 7567 10262 10141 -494 1400 -569 C ATOM 3600 CG GLN B 175 77.285 46.629 25.798 1.00 96.02 C ANISOU 3600 CG GLN B 175 10277 12984 13221 -774 1520 -658 C ATOM 3601 CD GLN B 175 78.175 47.150 24.676 1.00110.85 C ANISOU 3601 CD GLN B 175 12081 14852 15185 -865 1721 -518 C ATOM 3602 OE1 GLN B 175 78.507 46.419 23.739 1.00115.00 O ANISOU 3602 OE1 GLN B 175 12636 15490 15570 -712 1771 -365 O ATOM 3603 NE2 GLN B 175 78.580 48.412 24.778 1.00112.20 N ANISOU 3603 NE2 GLN B 175 12158 14884 15587 -1121 1851 -576 N ATOM 3604 N LYS B 176 73.759 45.260 26.142 1.00 69.20 N ANISOU 3604 N LYS B 176 7439 9285 9568 -345 1211 -552 N ATOM 3605 CA LYS B 176 72.502 45.961 26.382 1.00 66.55 C ANISOU 3605 CA LYS B 176 7251 8691 9343 -371 1198 -548 C ATOM 3606 C LYS B 176 71.865 45.511 27.686 1.00 66.65 C ANISOU 3606 C LYS B 176 7269 8754 9303 -327 1047 -709 C ATOM 3607 O LYS B 176 71.351 46.338 28.446 1.00 65.07 O ANISOU 3607 O LYS B 176 7079 8406 9239 -433 1055 -823 O ATOM 3608 CB LYS B 176 71.551 45.785 25.199 1.00 61.64 C ANISOU 3608 CB LYS B 176 6836 7924 8661 -233 1215 -324 C ATOM 3609 CG LYS B 176 72.024 46.584 23.989 1.00 68.44 C ANISOU 3609 CG LYS B 176 7713 8683 9610 -305 1392 -157 C ATOM 3610 CD LYS B 176 70.925 46.893 22.992 1.00 76.24 C ANISOU 3610 CD LYS B 176 8899 9475 10595 -215 1419 57 C ATOM 3611 CE LYS B 176 70.877 45.880 21.869 1.00 86.05 C ANISOU 3611 CE LYS B 176 10245 10844 11605 -48 1386 214 C ATOM 3612 NZ LYS B 176 69.693 46.101 20.977 1.00 89.97 N ANISOU 3612 NZ LYS B 176 10927 11189 12067 45 1371 412 N ATOM 3613 N GLY B 177 71.942 44.214 27.991 1.00 66.15 N ANISOU 3613 N GLY B 177 7195 8895 9043 -171 923 -724 N ATOM 3614 CA GLY B 177 71.417 43.735 29.260 1.00 62.16 C ANISOU 3614 CA GLY B 177 6687 8459 8472 -125 790 -863 C ATOM 3615 C GLY B 177 72.093 44.375 30.459 1.00 65.32 C ANISOU 3615 C GLY B 177 6913 8958 8949 -294 780 -1082 C ATOM 3616 O GLY B 177 71.433 44.711 31.448 1.00 69.43 O ANISOU 3616 O GLY B 177 7461 9414 9505 -337 732 -1211 O ATOM 3617 N HIS B 178 73.418 44.557 30.394 1.00 68.65 N ANISOU 3617 N HIS B 178 7144 9549 9391 -398 828 -1134 N ATOM 3618 CA HIS B 178 74.128 45.133 31.531 1.00 71.00 C ANISOU 3618 CA HIS B 178 7255 9978 9743 -578 800 -1360 C ATOM 3619 C HIS B 178 73.930 46.629 31.642 1.00 69.29 C ANISOU 3619 C HIS B 178 7053 9514 9759 -809 916 -1461 C ATOM 3620 O HIS B 178 74.096 47.176 32.735 1.00 72.37 O ANISOU 3620 O HIS B 178 7355 9947 10195 -961 882 -1681 O ATOM 3621 CB HIS B 178 75.624 44.812 31.486 1.00 73.03 C ANISOU 3621 CB HIS B 178 7270 10528 9949 -620 801 -1389 C ATOM 3622 CG HIS B 178 75.990 43.600 32.286 1.00 81.58 C ANISOU 3622 CG HIS B 178 8255 11919 10822 -461 649 -1429 C ATOM 3623 ND1 HIS B 178 76.084 42.338 31.733 1.00 83.05 N ANISOU 3623 ND1 HIS B 178 8488 12217 10852 -222 618 -1269 N ATOM 3624 CD2 HIS B 178 76.240 43.448 33.608 1.00 83.96 C ANISOU 3624 CD2 HIS B 178 8430 12432 11038 -495 525 -1604 C ATOM 3625 CE1 HIS B 178 76.396 41.465 32.674 1.00 81.28 C ANISOU 3625 CE1 HIS B 178 8165 12245 10471 -109 490 -1328 C ATOM 3626 NE2 HIS B 178 76.493 42.113 33.822 1.00 84.97 N ANISOU 3626 NE2 HIS B 178 8523 12793 10968 -268 424 -1524 N ATOM 3627 N THR B 179 73.565 47.304 30.555 1.00 70.63 N ANISOU 3627 N THR B 179 7342 9423 10070 -836 1055 -1306 N ATOM 3628 CA THR B 179 73.083 48.674 30.689 1.00 72.37 C ANISOU 3628 CA THR B 179 7632 9346 10521 -1010 1173 -1376 C ATOM 3629 C THR B 179 71.791 48.702 31.494 1.00 72.02 C ANISOU 3629 C THR B 179 7730 9166 10467 -934 1103 -1448 C ATOM 3630 O THR B 179 71.623 49.530 32.399 1.00 77.91 O ANISOU 3630 O THR B 179 8465 9810 11329 -1082 1132 -1648 O ATOM 3631 CB THR B 179 72.862 49.300 29.320 1.00 70.01 C ANISOU 3631 CB THR B 179 7446 8800 10356 -1010 1334 -1149 C ATOM 3632 OG1 THR B 179 74.076 49.216 28.566 1.00 74.52 O ANISOU 3632 OG1 THR B 179 7880 9513 10921 -1071 1412 -1074 O ATOM 3633 CG2 THR B 179 72.429 50.783 29.483 1.00 61.80 C ANISOU 3633 CG2 THR B 179 6474 7423 9582 -1187 1481 -1214 C ATOM 3634 N LEU B 180 70.870 47.786 31.178 1.00 62.95 N ANISOU 3634 N LEU B 180 6717 8020 9181 -709 1017 -1296 N ATOM 3635 CA LEU B 180 69.626 47.682 31.932 1.00 61.63 C ANISOU 3635 CA LEU B 180 6668 7754 8994 -621 950 -1347 C ATOM 3636 C LEU B 180 69.904 47.408 33.402 1.00 60.31 C ANISOU 3636 C LEU B 180 6400 7789 8727 -671 846 -1590 C ATOM 3637 O LEU B 180 69.412 48.127 34.275 1.00 63.91 O ANISOU 3637 O LEU B 180 6885 8128 9271 -761 873 -1755 O ATOM 3638 CB LEU B 180 68.738 46.578 31.348 1.00 59.13 C ANISOU 3638 CB LEU B 180 6481 7458 8528 -388 861 -1151 C ATOM 3639 CG LEU B 180 67.453 46.244 32.119 1.00 54.94 C ANISOU 3639 CG LEU B 180 6052 6869 7954 -280 780 -1183 C ATOM 3640 CD1 LEU B 180 66.605 47.492 32.299 1.00 52.06 C ANISOU 3640 CD1 LEU B 180 5764 6214 7802 -356 889 -1216 C ATOM 3641 CD2 LEU B 180 66.669 45.172 31.395 1.00 60.79 C ANISOU 3641 CD2 LEU B 180 6907 7627 8565 -84 699 -986 C ATOM 3642 N ILE B 181 70.730 46.395 33.692 1.00 61.07 N ANISOU 3642 N ILE B 181 6372 8196 8635 -610 735 -1615 N ATOM 3643 CA ILE B 181 71.004 46.035 35.082 1.00 64.98 C ANISOU 3643 CA ILE B 181 6767 8924 8998 -632 620 -1817 C ATOM 3644 C ILE B 181 71.520 47.240 35.850 1.00 71.45 C ANISOU 3644 C ILE B 181 7484 9715 9948 -887 678 -2068 C ATOM 3645 O ILE B 181 71.180 47.438 37.025 1.00 74.32 O ANISOU 3645 O ILE B 181 7852 10121 10266 -935 629 -2260 O ATOM 3646 CB ILE B 181 71.993 44.857 35.154 1.00 67.34 C ANISOU 3646 CB ILE B 181 6925 9565 9097 -526 511 -1779 C ATOM 3647 CG1 ILE B 181 71.358 43.581 34.588 1.00 68.10 C ANISOU 3647 CG1 ILE B 181 7151 9670 9052 -273 453 -1569 C ATOM 3648 CG2 ILE B 181 72.487 44.657 36.582 1.00 56.28 C ANISOU 3648 CG2 ILE B 181 5383 8439 7562 -576 396 -1988 C ATOM 3649 CD1 ILE B 181 72.279 42.378 34.582 1.00 63.22 C ANISOU 3649 CD1 ILE B 181 6419 9348 8254 -137 371 -1510 C ATOM 3650 N GLN B 182 72.329 48.080 35.192 1.00 72.65 N ANISOU 3650 N GLN B 182 7551 9786 10266 -1063 793 -2074 N ATOM 3651 CA GLN B 182 72.902 49.247 35.859 1.00 79.88 C ANISOU 3651 CA GLN B 182 8364 10660 11324 -1339 858 -2327 C ATOM 3652 C GLN B 182 71.903 50.389 36.027 1.00 75.60 C ANISOU 3652 C GLN B 182 7992 9746 10986 -1426 987 -2403 C ATOM 3653 O GLN B 182 72.059 51.190 36.946 1.00 76.03 O ANISOU 3653 O GLN B 182 8009 9766 11111 -1620 1015 -2665 O ATOM 3654 CB GLN B 182 74.117 49.763 35.086 1.00 87.77 C ANISOU 3654 CB GLN B 182 9208 11686 12453 -1514 956 -2301 C ATOM 3655 CG GLN B 182 75.361 48.902 35.183 1.00 94.01 C ANISOU 3655 CG GLN B 182 9765 12876 13077 -1493 845 -2305 C ATOM 3656 CD GLN B 182 76.397 49.285 34.135 1.00108.61 C ANISOU 3656 CD GLN B 182 11485 14724 15059 -1613 969 -2203 C ATOM 3657 OE1 GLN B 182 76.544 50.463 33.793 1.00112.76 O ANISOU 3657 OE1 GLN B 182 12019 15009 15816 -1829 1126 -2251 O ATOM 3658 NE2 GLN B 182 77.100 48.287 33.598 1.00112.50 N ANISOU 3658 NE2 GLN B 182 11864 15470 15411 -1464 919 -2052 N ATOM 3659 N ASN B 183 70.895 50.505 35.156 1.00 76.96 N ANISOU 3659 N ASN B 183 8346 9641 11254 -1288 1071 -2183 N ATOM 3660 CA ASN B 183 69.911 51.583 35.231 1.00 79.07 C ANISOU 3660 CA ASN B 183 8769 9542 11730 -1334 1208 -2217 C ATOM 3661 C ASN B 183 68.551 51.113 35.748 1.00 77.67 C ANISOU 3661 C ASN B 183 8734 9311 11466 -1136 1144 -2184 C ATOM 3662 O ASN B 183 67.525 51.736 35.471 1.00 76.18 O ANISOU 3662 O ASN B 183 8689 8823 11434 -1080 1250 -2101 O ATOM 3663 CB ASN B 183 69.758 52.234 33.860 1.00 79.80 C ANISOU 3663 CB ASN B 183 8948 9350 12022 -1331 1367 -1979 C ATOM 3664 CG ASN B 183 71.088 52.664 33.286 1.00 86.46 C ANISOU 3664 CG ASN B 183 9649 10245 12956 -1523 1450 -1984 C ATOM 3665 OD1 ASN B 183 72.081 52.725 34.004 1.00 88.68 O ANISOU 3665 OD1 ASN B 183 9763 10731 13202 -1700 1405 -2207 O ATOM 3666 ND2 ASN B 183 71.120 52.951 31.993 1.00 84.74 N ANISOU 3666 ND2 ASN B 183 9489 9863 12846 -1490 1569 -1735 N ATOM 3667 N MET B 184 68.542 50.032 36.525 1.00 72.34 N ANISOU 3667 N MET B 184 8010 8927 10549 -1028 980 -2243 N ATOM 3668 CA MET B 184 67.326 49.296 36.862 1.00 70.11 C ANISOU 3668 CA MET B 184 7844 8643 10153 -818 906 -2158 C ATOM 3669 C MET B 184 66.534 49.939 37.995 1.00 76.42 C ANISOU 3669 C MET B 184 8714 9318 11003 -861 956 -2362 C ATOM 3670 O MET B 184 65.310 49.769 38.066 1.00 72.77 O ANISOU 3670 O MET B 184 8370 8728 10552 -710 968 -2268 O ATOM 3671 CB MET B 184 67.712 47.881 37.270 1.00 66.81 C ANISOU 3671 CB MET B 184 7347 8576 9460 -690 731 -2134 C ATOM 3672 CG MET B 184 66.826 46.804 36.811 1.00 63.48 C ANISOU 3672 CG MET B 184 7026 8164 8930 -459 660 -1912 C ATOM 3673 SD MET B 184 67.621 45.229 37.186 1.00 74.01 S ANISOU 3673 SD MET B 184 8255 9890 9976 -335 488 -1884 S ATOM 3674 CE MET B 184 67.733 45.252 38.969 1.00 77.71 C ANISOU 3674 CE MET B 184 8655 10568 10305 -397 416 -2153 C ATOM 3675 N ALA B 185 67.222 50.621 38.909 1.00 73.85 N ANISOU 3675 N ALA B 185 8311 9053 10695 -1065 980 -2647 N ATOM 3676 CA ALA B 185 66.617 51.064 40.162 1.00 71.54 C ANISOU 3676 CA ALA B 185 8078 8720 10385 -1107 1008 -2885 C ATOM 3677 C ALA B 185 65.310 51.847 40.025 1.00 77.25 C ANISOU 3677 C ALA B 185 8968 9070 11313 -1038 1165 -2835 C ATOM 3678 O ALA B 185 64.376 51.550 40.788 1.00 79.83 O ANISOU 3678 O ALA B 185 9366 9413 11553 -918 1148 -2876 O ATOM 3679 CB ALA B 185 67.661 51.882 40.934 1.00 65.42 C ANISOU 3679 CB ALA B 185 7196 8025 9635 -1383 1033 -3210 C ATOM 3680 N PRO B 186 65.152 52.811 39.105 1.00 73.98 N ANISOU 3680 N PRO B 186 8618 8325 11165 -1089 1324 -2731 N ATOM 3681 CA PRO B 186 63.864 53.536 39.025 1.00 66.00 C ANISOU 3681 CA PRO B 186 7757 6970 10350 -991 1474 -2667 C ATOM 3682 C PRO B 186 62.658 52.629 38.819 1.00 67.60 C ANISOU 3682 C PRO B 186 8019 7211 10454 -727 1397 -2436 C ATOM 3683 O PRO B 186 61.533 53.043 39.125 1.00 67.83 O ANISOU 3683 O PRO B 186 8142 7043 10588 -630 1492 -2429 O ATOM 3684 CB PRO B 186 64.056 54.478 37.828 1.00 64.25 C ANISOU 3684 CB PRO B 186 7574 6442 10397 -1056 1630 -2508 C ATOM 3685 CG PRO B 186 65.518 54.667 37.721 1.00 63.41 C ANISOU 3685 CG PRO B 186 7343 6467 10282 -1283 1614 -2634 C ATOM 3686 CD PRO B 186 66.138 53.357 38.148 1.00 65.61 C ANISOU 3686 CD PRO B 186 7495 7181 10252 -1238 1395 -2667 C ATOM 3687 N LEU B 187 62.847 51.418 38.277 1.00 67.98 N ANISOU 3687 N LEU B 187 8015 7496 10317 -610 1238 -2246 N ATOM 3688 CA LEU B 187 61.726 50.496 38.121 1.00 63.61 C ANISOU 3688 CA LEU B 187 7513 6990 9666 -386 1157 -2048 C ATOM 3689 C LEU B 187 61.178 50.035 39.458 1.00 70.96 C ANISOU 3689 C LEU B 187 8452 8064 10446 -333 1110 -2209 C ATOM 3690 O LEU B 187 60.056 49.517 39.507 1.00 70.13 O ANISOU 3690 O LEU B 187 8395 7939 10312 -168 1088 -2078 O ATOM 3691 CB LEU B 187 62.124 49.268 37.312 1.00 56.21 C ANISOU 3691 CB LEU B 187 6530 6269 8557 -292 1006 -1845 C ATOM 3692 CG LEU B 187 62.578 49.517 35.880 1.00 53.25 C ANISOU 3692 CG LEU B 187 6156 5791 8285 -308 1042 -1645 C ATOM 3693 CD1 LEU B 187 62.890 48.202 35.193 1.00 51.55 C ANISOU 3693 CD1 LEU B 187 5914 5801 7873 -200 898 -1474 C ATOM 3694 CD2 LEU B 187 61.527 50.319 35.123 1.00 54.15 C ANISOU 3694 CD2 LEU B 187 6366 5594 8614 -232 1161 -1466 C ATOM 3695 N PHE B 188 61.936 50.210 40.539 1.00 68.19 N ANISOU 3695 N PHE B 188 8049 7870 9992 -474 1094 -2487 N ATOM 3696 CA PHE B 188 61.485 49.726 41.828 1.00 70.71 C ANISOU 3696 CA PHE B 188 8378 8360 10129 -420 1047 -2634 C ATOM 3697 C PHE B 188 60.810 50.791 42.681 1.00 83.41 C ANISOU 3697 C PHE B 188 10067 9763 11864 -472 1208 -2845 C ATOM 3698 O PHE B 188 60.152 50.434 43.661 1.00 85.40 O ANISOU 3698 O PHE B 188 10350 10114 11984 -392 1202 -2927 O ATOM 3699 CB PHE B 188 62.659 49.081 42.555 1.00 67.44 C ANISOU 3699 CB PHE B 188 7854 8303 9466 -506 905 -2790 C ATOM 3700 CG PHE B 188 63.032 47.758 41.962 1.00 67.50 C ANISOU 3700 CG PHE B 188 7804 8534 9310 -382 751 -2570 C ATOM 3701 CD1 PHE B 188 63.948 47.679 40.928 1.00 68.54 C ANISOU 3701 CD1 PHE B 188 7867 8688 9488 -432 719 -2460 C ATOM 3702 CD2 PHE B 188 62.402 46.595 42.386 1.00 63.82 C ANISOU 3702 CD2 PHE B 188 7363 8227 8659 -209 660 -2461 C ATOM 3703 CE1 PHE B 188 64.264 46.459 40.356 1.00 67.85 C ANISOU 3703 CE1 PHE B 188 7742 8784 9255 -306 597 -2266 C ATOM 3704 CE2 PHE B 188 62.713 45.376 41.827 1.00 63.65 C ANISOU 3704 CE2 PHE B 188 7308 8373 8504 -93 537 -2265 C ATOM 3705 CZ PHE B 188 63.647 45.303 40.809 1.00 64.84 C ANISOU 3705 CZ PHE B 188 7396 8545 8694 -137 506 -2174 C ATOM 3706 N GLU B 189 60.902 52.069 42.295 1.00 90.26 N ANISOU 3706 N GLU B 189 10977 10328 12988 -590 1369 -2917 N ATOM 3707 CA GLU B 189 60.105 53.161 42.876 1.00 93.21 C ANISOU 3707 CA GLU B 189 11453 10420 13541 -607 1564 -3074 C ATOM 3708 C GLU B 189 60.198 53.214 44.400 1.00 91.20 C ANISOU 3708 C GLU B 189 11210 10334 13109 -686 1565 -3404 C ATOM 3709 O GLU B 189 59.242 53.604 45.084 1.00 91.73 O ANISOU 3709 O GLU B 189 11363 10269 13221 -613 1690 -3497 O ATOM 3710 CB GLU B 189 58.642 53.072 42.432 1.00 93.68 C ANISOU 3710 CB GLU B 189 11582 10287 13723 -378 1634 -2826 C ATOM 3711 CG GLU B 189 58.484 52.900 40.934 1.00 96.18 C ANISOU 3711 CG GLU B 189 11888 10492 14165 -284 1604 -2488 C ATOM 3712 CD GLU B 189 57.070 53.136 40.466 1.00101.28 C ANISOU 3712 CD GLU B 189 12590 10909 14983 -88 1698 -2267 C ATOM 3713 OE1 GLU B 189 56.804 52.946 39.260 1.00101.50 O ANISOU 3713 OE1 GLU B 189 12609 10871 15087 7 1659 -1979 O ATOM 3714 OE2 GLU B 189 56.221 53.507 41.304 1.00105.85 O ANISOU 3714 OE2 GLU B 189 13216 11391 15612 -25 1810 -2379 O ATOM 3715 N ASN B 190 61.352 52.820 44.936 1.00 84.84 N ANISOU 3715 N ASN B 190 10309 9836 12090 -830 1428 -3579 N ATOM 3716 CA ASN B 190 61.682 52.956 46.349 1.00 88.44 C ANISOU 3716 CA ASN B 190 10761 10491 12352 -947 1411 -3918 C ATOM 3717 C ASN B 190 60.809 52.099 47.259 1.00 86.94 C ANISOU 3717 C ASN B 190 10607 10495 11932 -764 1362 -3894 C ATOM 3718 O ASN B 190 60.755 52.343 48.475 1.00 86.75 O ANISOU 3718 O ASN B 190 10618 10581 11760 -826 1395 -4168 O ATOM 3719 CB ASN B 190 61.612 54.424 46.787 1.00 98.50 C ANISOU 3719 CB ASN B 190 12128 11464 13833 -1121 1620 -4214 C ATOM 3720 CG ASN B 190 62.821 55.219 46.332 1.00111.87 C ANISOU 3720 CG ASN B 190 13759 13075 15673 -1383 1643 -4352 C ATOM 3721 OD1 ASN B 190 63.962 54.771 46.470 1.00114.60 O ANISOU 3721 OD1 ASN B 190 13968 13730 15844 -1513 1481 -4430 O ATOM 3722 ND2 ASN B 190 62.579 56.402 45.785 1.00117.27 N ANISOU 3722 ND2 ASN B 190 14534 13339 16683 -1458 1852 -4370 N ATOM 3723 N VAL B 191 60.103 51.111 46.700 1.00 80.19 N ANISOU 3723 N VAL B 191 9748 9680 11041 -548 1293 -3577 N ATOM 3724 CA VAL B 191 59.302 50.216 47.525 1.00 78.98 C ANISOU 3724 CA VAL B 191 9619 9713 10675 -382 1251 -3529 C ATOM 3725 C VAL B 191 60.230 49.322 48.349 1.00 78.69 C ANISOU 3725 C VAL B 191 9498 10100 10299 -422 1070 -3629 C ATOM 3726 O VAL B 191 61.358 48.996 47.943 1.00 80.94 O ANISOU 3726 O VAL B 191 9681 10556 10517 -505 937 -3607 O ATOM 3727 CB VAL B 191 58.328 49.380 46.665 1.00 75.03 C ANISOU 3727 CB VAL B 191 9129 9139 10239 -167 1221 -3168 C ATOM 3728 CG1 VAL B 191 57.515 50.287 45.768 1.00 77.63 C ANISOU 3728 CG1 VAL B 191 9517 9081 10896 -124 1379 -3047 C ATOM 3729 CG2 VAL B 191 59.063 48.301 45.828 1.00 65.23 C ANISOU 3729 CG2 VAL B 191 7804 8089 8893 -131 1035 -2950 C ATOM 3730 N VAL B 192 59.764 48.940 49.517 1.00 75.22 N ANISOU 3730 N VAL B 192 9096 9841 9644 -354 1071 -3730 N ATOM 3731 CA VAL B 192 60.485 48.029 50.390 1.00 72.47 C ANISOU 3731 CA VAL B 192 8676 9909 8951 -350 906 -3790 C ATOM 3732 C VAL B 192 60.085 46.612 50.020 1.00 76.82 C ANISOU 3732 C VAL B 192 9208 10587 9394 -140 801 -3460 C ATOM 3733 O VAL B 192 58.908 46.330 49.758 1.00 84.72 O ANISOU 3733 O VAL B 192 10276 11420 10495 7 881 -3276 O ATOM 3734 CB VAL B 192 60.183 48.341 51.867 1.00 84.65 C ANISOU 3734 CB VAL B 192 10282 11592 10291 -381 971 -4064 C ATOM 3735 CG1 VAL B 192 60.826 49.659 52.261 1.00 79.52 C ANISOU 3735 CG1 VAL B 192 9643 10859 9712 -626 1047 -4432 C ATOM 3736 CG2 VAL B 192 58.676 48.404 52.098 1.00 91.79 C ANISOU 3736 CG2 VAL B 192 11301 12288 11286 -222 1141 -3979 C ATOM 3737 N ILE B 193 61.070 45.722 49.964 1.00 75.17 N ANISOU 3737 N ILE B 193 8899 10666 8994 -129 626 -3381 N ATOM 3738 CA ILE B 193 60.889 44.388 49.419 1.00 65.43 C ANISOU 3738 CA ILE B 193 7650 9519 7692 50 528 -3068 C ATOM 3739 C ILE B 193 61.303 43.384 50.479 1.00 69.83 C ANISOU 3739 C ILE B 193 8168 10455 7908 131 410 -3069 C ATOM 3740 O ILE B 193 62.474 43.335 50.871 1.00 74.86 O ANISOU 3740 O ILE B 193 8704 11363 8378 50 294 -3191 O ATOM 3741 CB ILE B 193 61.690 44.199 48.117 1.00 68.72 C ANISOU 3741 CB ILE B 193 7992 9882 8236 22 449 -2919 C ATOM 3742 CG1 ILE B 193 61.074 45.058 47.006 1.00 73.86 C ANISOU 3742 CG1 ILE B 193 8700 10150 9213 -14 573 -2850 C ATOM 3743 CG2 ILE B 193 61.733 42.737 47.692 1.00 58.17 C ANISOU 3743 CG2 ILE B 193 6639 8683 6781 196 337 -2642 C ATOM 3744 CD1 ILE B 193 61.885 45.086 45.753 1.00 70.50 C ANISOU 3744 CD1 ILE B 193 8211 9663 8913 -65 523 -2735 C ATOM 3745 N GLU B 194 60.351 42.582 50.931 1.00 73.72 N ANISOU 3745 N GLU B 194 8733 10976 8301 293 441 -2920 N ATOM 3746 CA GLU B 194 60.511 41.513 51.908 1.00 81.05 C ANISOU 3746 CA GLU B 194 9651 12228 8915 411 357 -2855 C ATOM 3747 C GLU B 194 60.759 40.189 51.192 1.00 73.89 C ANISOU 3747 C GLU B 194 8717 11381 7979 555 253 -2556 C ATOM 3748 O GLU B 194 60.133 39.911 50.166 1.00 77.30 O ANISOU 3748 O GLU B 194 9191 11566 8613 612 291 -2366 O ATOM 3749 CB GLU B 194 59.267 41.382 52.786 1.00 91.12 C ANISOU 3749 CB GLU B 194 11030 13473 10118 505 481 -2846 C ATOM 3750 CG GLU B 194 59.105 42.463 53.858 1.00108.90 C ANISOU 3750 CG GLU B 194 13323 15762 12292 394 582 -3163 C ATOM 3751 CD GLU B 194 60.114 42.338 54.987 1.00120.59 C ANISOU 3751 CD GLU B 194 14746 17642 13429 342 466 -3346 C ATOM 3752 OE1 GLU B 194 60.451 41.196 55.365 1.00124.92 O ANISOU 3752 OE1 GLU B 194 15262 18464 13740 470 355 -3175 O ATOM 3753 OE2 GLU B 194 60.573 43.380 55.497 1.00124.09 O ANISOU 3753 OE2 GLU B 194 15179 18130 13839 172 486 -3659 O ATOM 3754 N PRO B 195 61.679 39.374 51.689 1.00 69.58 N ANISOU 3754 N PRO B 195 8100 11156 7183 618 123 -2512 N ATOM 3755 CA PRO B 195 61.894 38.054 51.078 1.00 64.19 C ANISOU 3755 CA PRO B 195 7408 10513 6467 775 46 -2227 C ATOM 3756 C PRO B 195 60.653 37.182 51.233 1.00 61.99 C ANISOU 3756 C PRO B 195 7247 10121 6187 923 126 -2020 C ATOM 3757 O PRO B 195 60.082 37.085 52.321 1.00 62.36 O ANISOU 3757 O PRO B 195 7343 10275 6076 968 182 -2057 O ATOM 3758 CB PRO B 195 63.085 37.487 51.864 1.00 63.34 C ANISOU 3758 CB PRO B 195 7195 10803 6067 823 -91 -2247 C ATOM 3759 CG PRO B 195 63.713 38.689 52.570 1.00 64.19 C ANISOU 3759 CG PRO B 195 7224 11066 6098 635 -114 -2573 C ATOM 3760 CD PRO B 195 62.571 39.624 52.837 1.00 61.26 C ANISOU 3760 CD PRO B 195 6967 10450 5858 552 41 -2721 C ATOM 3761 N CYS B 196 60.231 36.553 50.133 1.00 54.34 N ANISOU 3761 N CYS B 196 6319 8938 5391 989 135 -1807 N ATOM 3762 CA CYS B 196 59.126 35.602 50.151 1.00 53.55 C ANISOU 3762 CA CYS B 196 6314 8726 5306 1113 198 -1596 C ATOM 3763 C CYS B 196 59.563 34.276 49.548 1.00 57.71 C ANISOU 3763 C CYS B 196 6852 9280 5793 1236 123 -1365 C ATOM 3764 O CYS B 196 60.268 34.250 48.536 1.00 58.55 O ANISOU 3764 O CYS B 196 6919 9332 5996 1214 60 -1336 O ATOM 3765 CB CYS B 196 57.924 36.130 49.360 1.00 60.24 C ANISOU 3765 CB CYS B 196 7215 9247 6429 1062 298 -1565 C ATOM 3766 SG CYS B 196 57.171 37.611 50.063 1.00 67.34 S ANISOU 3766 SG CYS B 196 8124 10054 7409 956 431 -1805 S ATOM 3767 N LEU B 197 59.116 33.174 50.148 1.00 59.52 N ANISOU 3767 N LEU B 197 7147 9577 5892 1369 148 -1197 N ATOM 3768 CA LEU B 197 59.337 31.864 49.543 1.00 56.95 C ANISOU 3768 CA LEU B 197 6863 9211 5564 1490 110 -970 C ATOM 3769 C LEU B 197 58.576 31.789 48.225 1.00 59.71 C ANISOU 3769 C LEU B 197 7269 9246 6174 1443 143 -884 C ATOM 3770 O LEU B 197 57.342 31.823 48.215 1.00 64.22 O ANISOU 3770 O LEU B 197 7894 9648 6857 1418 226 -840 O ATOM 3771 CB LEU B 197 58.906 30.724 50.481 1.00 51.46 C ANISOU 3771 CB LEU B 197 6241 8615 4696 1634 156 -797 C ATOM 3772 CG LEU B 197 59.174 29.278 50.017 1.00 51.98 C ANISOU 3772 CG LEU B 197 6369 8635 4745 1776 137 -559 C ATOM 3773 CD1 LEU B 197 60.658 29.025 49.759 1.00 48.67 C ANISOU 3773 CD1 LEU B 197 5869 8399 4225 1847 27 -555 C ATOM 3774 CD2 LEU B 197 58.605 28.249 50.986 1.00 53.25 C ANISOU 3774 CD2 LEU B 197 6615 8854 4762 1904 213 -381 C ATOM 3775 N LEU B 198 59.314 31.689 47.121 1.00 51.37 N ANISOU 3775 N LEU B 198 6188 8129 5201 1432 78 -859 N ATOM 3776 CA LEU B 198 58.787 31.585 45.772 1.00 49.81 C ANISOU 3776 CA LEU B 198 6041 7672 5213 1390 86 -782 C ATOM 3777 C LEU B 198 58.806 30.135 45.301 1.00 54.21 C ANISOU 3777 C LEU B 198 6684 8169 5746 1503 76 -587 C ATOM 3778 O LEU B 198 59.679 29.350 45.677 1.00 51.52 O ANISOU 3778 O LEU B 198 6339 7985 5253 1620 43 -520 O ATOM 3779 CB LEU B 198 59.608 32.436 44.795 1.00 50.05 C ANISOU 3779 CB LEU B 198 6003 7670 5345 1300 37 -882 C ATOM 3780 CG LEU B 198 59.797 33.904 45.149 1.00 48.91 C ANISOU 3780 CG LEU B 198 5777 7563 5245 1173 54 -1088 C ATOM 3781 CD1 LEU B 198 60.563 34.617 44.050 1.00 46.32 C ANISOU 3781 CD1 LEU B 198 5392 7168 5038 1085 22 -1147 C ATOM 3782 CD2 LEU B 198 58.457 34.569 45.382 1.00 37.09 C ANISOU 3782 CD2 LEU B 198 4319 5899 3873 1116 142 -1126 C ATOM 3783 N HIS B 199 57.809 29.775 44.492 1.00 52.01 N ANISOU 3783 N HIS B 199 6482 7659 5621 1469 107 -497 N ATOM 3784 CA HIS B 199 57.861 28.494 43.797 1.00 49.52 C ANISOU 3784 CA HIS B 199 6261 7240 5314 1544 99 -347 C ATOM 3785 C HIS B 199 58.983 28.497 42.768 1.00 51.78 C ANISOU 3785 C HIS B 199 6528 7537 5609 1558 39 -368 C ATOM 3786 O HIS B 199 59.774 27.550 42.700 1.00 52.43 O ANISOU 3786 O HIS B 199 6644 7678 5599 1676 28 -286 O ATOM 3787 CB HIS B 199 56.511 28.179 43.147 1.00 40.60 C ANISOU 3787 CB HIS B 199 5205 5877 4345 1474 134 -272 C ATOM 3788 CG HIS B 199 56.514 26.918 42.331 1.00 51.20 C ANISOU 3788 CG HIS B 199 6658 7084 5710 1517 129 -151 C ATOM 3789 ND1 HIS B 199 57.042 26.857 41.058 1.00 46.38 N ANISOU 3789 ND1 HIS B 199 6075 6394 5151 1498 78 -166 N ATOM 3790 CD2 HIS B 199 56.083 25.664 42.620 1.00 53.08 C ANISOU 3790 CD2 HIS B 199 6998 7245 5925 1578 180 -21 C ATOM 3791 CE1 HIS B 199 56.905 25.630 40.586 1.00 47.23 C ANISOU 3791 CE1 HIS B 199 6302 6378 5264 1541 96 -67 C ATOM 3792 NE2 HIS B 199 56.339 24.884 41.517 1.00 49.19 N ANISOU 3792 NE2 HIS B 199 6598 6616 5477 1587 159 23 N ATOM 3793 N GLY B 200 59.082 29.570 41.976 1.00 38.90 N ANISOU 3793 N GLY B 200 4841 5850 4090 1448 12 -470 N ATOM 3794 CA GLY B 200 60.220 29.800 41.104 1.00 40.04 C ANISOU 3794 CA GLY B 200 4942 6036 4235 1448 -30 -506 C ATOM 3795 C GLY B 200 60.079 29.314 39.669 1.00 45.37 C ANISOU 3795 C GLY B 200 5704 6536 5000 1437 -38 -436 C ATOM 3796 O GLY B 200 60.927 29.661 38.837 1.00 48.17 O ANISOU 3796 O GLY B 200 6023 6911 5369 1422 -59 -469 O ATOM 3797 N ASP B 201 59.051 28.521 39.350 1.00 40.65 N ANISOU 3797 N ASP B 201 5217 5774 4453 1437 -21 -345 N ATOM 3798 CA ASP B 201 58.852 28.024 37.988 1.00 47.99 C ANISOU 3798 CA ASP B 201 6241 6546 5447 1412 -36 -296 C ATOM 3799 C ASP B 201 57.388 27.664 37.765 1.00 45.44 C ANISOU 3799 C ASP B 201 5991 6053 5219 1340 -31 -241 C ATOM 3800 O ASP B 201 57.073 26.511 37.453 1.00 50.44 O ANISOU 3800 O ASP B 201 6738 6584 5845 1367 -19 -169 O ATOM 3801 CB ASP B 201 59.742 26.794 37.701 1.00 50.41 C ANISOU 3801 CB ASP B 201 6629 6866 5657 1541 -21 -232 C ATOM 3802 CG ASP B 201 59.725 26.374 36.205 1.00 57.52 C ANISOU 3802 CG ASP B 201 7634 7622 6601 1512 -32 -217 C ATOM 3803 OD1 ASP B 201 59.488 27.232 35.310 1.00 58.03 O ANISOU 3803 OD1 ASP B 201 7671 7640 6737 1408 -65 -261 O ATOM 3804 OD2 ASP B 201 59.927 25.175 35.918 1.00 60.42 O ANISOU 3804 OD2 ASP B 201 8118 7915 6925 1596 0 -160 O ATOM 3805 N LEU B 202 56.484 28.627 37.933 1.00 43.94 N ANISOU 3805 N LEU B 202 5733 5832 5130 1247 -33 -274 N ATOM 3806 CA LEU B 202 55.054 28.342 38.075 1.00 46.80 C ANISOU 3806 CA LEU B 202 6119 6082 5582 1187 -19 -217 C ATOM 3807 C LEU B 202 54.328 28.541 36.740 1.00 48.30 C ANISOU 3807 C LEU B 202 6329 6144 5880 1091 -75 -196 C ATOM 3808 O LEU B 202 54.013 29.667 36.349 1.00 48.61 O ANISOU 3808 O LEU B 202 6291 6171 6007 1033 -95 -225 O ATOM 3809 CB LEU B 202 54.476 29.209 39.184 1.00 42.56 C ANISOU 3809 CB LEU B 202 5486 5604 5080 1168 28 -258 C ATOM 3810 CG LEU B 202 53.094 28.802 39.676 1.00 56.76 C ANISOU 3810 CG LEU B 202 7289 7328 6951 1133 71 -188 C ATOM 3811 CD1 LEU B 202 53.081 27.338 40.183 1.00 46.92 C ANISOU 3811 CD1 LEU B 202 6141 6067 5622 1194 109 -97 C ATOM 3812 CD2 LEU B 202 52.649 29.765 40.764 1.00 55.61 C ANISOU 3812 CD2 LEU B 202 7049 7252 6827 1130 135 -246 C ATOM 3813 N TRP B 203 54.069 27.438 36.039 1.00 44.86 N ANISOU 3813 N TRP B 203 6000 5612 5434 1076 -99 -145 N ATOM 3814 CA TRP B 203 53.309 27.443 34.801 1.00 42.08 C ANISOU 3814 CA TRP B 203 5674 5160 5153 977 -167 -126 C ATOM 3815 C TRP B 203 52.369 26.234 34.799 1.00 47.87 C ANISOU 3815 C TRP B 203 6486 5787 5917 923 -165 -73 C ATOM 3816 O TRP B 203 52.319 25.466 35.764 1.00 54.30 O ANISOU 3816 O TRP B 203 7336 6589 6705 969 -96 -38 O ATOM 3817 CB TRP B 203 54.251 27.479 33.595 1.00 38.64 C ANISOU 3817 CB TRP B 203 5301 4730 4652 991 -207 -157 C ATOM 3818 CG TRP B 203 55.020 26.211 33.395 1.00 43.98 C ANISOU 3818 CG TRP B 203 6111 5374 5225 1061 -179 -157 C ATOM 3819 CD1 TRP B 203 56.088 25.779 34.115 1.00 42.95 C ANISOU 3819 CD1 TRP B 203 5998 5314 5008 1185 -119 -160 C ATOM 3820 CD2 TRP B 203 54.778 25.213 32.390 1.00 43.40 C ANISOU 3820 CD2 TRP B 203 6176 5189 5126 1019 -206 -156 C ATOM 3821 NE1 TRP B 203 56.520 24.566 33.639 1.00 48.24 N ANISOU 3821 NE1 TRP B 203 6809 5906 5614 1241 -93 -146 N ATOM 3822 CE2 TRP B 203 55.738 24.195 32.578 1.00 47.57 C ANISOU 3822 CE2 TRP B 203 6811 5699 5565 1133 -140 -157 C ATOM 3823 CE3 TRP B 203 53.843 25.087 31.345 1.00 38.95 C ANISOU 3823 CE3 TRP B 203 5653 4547 4601 894 -283 -159 C ATOM 3824 CZ2 TRP B 203 55.801 23.062 31.758 1.00 52.30 C ANISOU 3824 CZ2 TRP B 203 7574 6175 6121 1127 -128 -174 C ATOM 3825 CZ3 TRP B 203 53.892 23.955 30.532 1.00 45.56 C ANISOU 3825 CZ3 TRP B 203 6649 5283 5379 867 -289 -189 C ATOM 3826 CH2 TRP B 203 54.874 22.957 30.742 1.00 52.75 C ANISOU 3826 CH2 TRP B 203 7683 6149 6211 984 -202 -202 C ATOM 3827 N SER B 204 51.618 26.067 33.696 1.00 46.85 N ANISOU 3827 N SER B 204 6382 5582 5837 816 -241 -65 N ATOM 3828 CA SER B 204 50.515 25.097 33.642 1.00 50.36 C ANISOU 3828 CA SER B 204 6867 5925 6341 718 -252 -28 C ATOM 3829 C SER B 204 50.967 23.669 33.947 1.00 53.26 C ANISOU 3829 C SER B 204 7390 6203 6644 760 -183 -21 C ATOM 3830 O SER B 204 50.246 22.919 34.611 1.00 57.90 O ANISOU 3830 O SER B 204 7996 6718 7287 720 -130 27 O ATOM 3831 CB SER B 204 49.836 25.146 32.263 1.00 44.95 C ANISOU 3831 CB SER B 204 6188 5206 5685 593 -367 -39 C ATOM 3832 OG SER B 204 48.939 26.233 32.204 1.00 61.18 O ANISOU 3832 OG SER B 204 8082 7319 7844 545 -417 -1 O ATOM 3833 N GLY B 205 52.138 23.267 33.452 1.00 51.35 N ANISOU 3833 N GLY B 205 7261 5954 6296 845 -171 -60 N ATOM 3834 CA GLY B 205 52.664 21.924 33.678 1.00 52.59 C ANISOU 3834 CA GLY B 205 7575 6009 6397 915 -92 -46 C ATOM 3835 C GLY B 205 53.024 21.601 35.118 1.00 51.55 C ANISOU 3835 C GLY B 205 7430 5918 6240 1040 11 25 C ATOM 3836 O GLY B 205 53.320 20.439 35.416 1.00 59.99 O ANISOU 3836 O GLY B 205 8628 6886 7280 1108 91 68 O ATOM 3837 N ASN B 206 53.045 22.593 36.005 1.00 49.86 N ANISOU 3837 N ASN B 206 7073 5847 6026 1081 16 38 N ATOM 3838 CA ASN B 206 53.433 22.391 37.395 1.00 50.66 C ANISOU 3838 CA ASN B 206 7152 6029 6066 1203 101 98 C ATOM 3839 C ASN B 206 52.277 22.571 38.361 1.00 53.36 C ANISOU 3839 C ASN B 206 7415 6377 6481 1141 144 151 C ATOM 3840 O ASN B 206 52.505 22.601 39.574 1.00 54.06 O ANISOU 3840 O ASN B 206 7471 6565 6503 1236 211 196 O ATOM 3841 CB ASN B 206 54.550 23.361 37.770 1.00 47.94 C ANISOU 3841 CB ASN B 206 6710 5873 5631 1306 83 50 C ATOM 3842 CG ASN B 206 55.834 22.981 37.158 1.00 61.77 C ANISOU 3842 CG ASN B 206 8529 7646 7295 1408 78 29 C ATOM 3843 OD1 ASN B 206 56.023 21.823 36.801 1.00 69.38 O ANISOU 3843 OD1 ASN B 206 9631 8489 8241 1454 119 68 O ATOM 3844 ND2 ASN B 206 56.750 23.926 37.050 1.00 63.66 N ANISOU 3844 ND2 ASN B 206 8672 8031 7486 1447 43 -33 N ATOM 3845 N ILE B 207 51.055 22.720 37.853 1.00 49.05 N ANISOU 3845 N ILE B 207 6829 5747 6061 990 106 147 N ATOM 3846 CA ILE B 207 49.878 22.995 38.663 1.00 50.69 C ANISOU 3846 CA ILE B 207 6935 5967 6358 925 151 196 C ATOM 3847 C ILE B 207 48.865 21.886 38.426 1.00 54.19 C ANISOU 3847 C ILE B 207 7443 6248 6899 804 178 255 C ATOM 3848 O ILE B 207 48.699 21.417 37.297 1.00 60.58 O ANISOU 3848 O ILE B 207 8322 6950 7745 706 109 216 O ATOM 3849 CB ILE B 207 49.270 24.379 38.332 1.00 50.04 C ANISOU 3849 CB ILE B 207 6695 5955 6362 856 86 146 C ATOM 3850 CG1 ILE B 207 50.283 25.501 38.575 1.00 50.34 C ANISOU 3850 CG1 ILE B 207 6676 6129 6321 953 73 74 C ATOM 3851 CG2 ILE B 207 48.047 24.646 39.160 1.00 48.69 C ANISOU 3851 CG2 ILE B 207 6411 5798 6291 805 150 198 C ATOM 3852 CD1 ILE B 207 49.893 26.824 37.930 1.00 44.92 C ANISOU 3852 CD1 ILE B 207 5873 5468 5728 894 8 25 C ATOM 3853 N ALA B 208 48.200 21.459 39.497 1.00 56.92 N ANISOU 3853 N ALA B 208 7769 6580 7279 801 285 343 N ATOM 3854 CA ALA B 208 47.205 20.404 39.426 1.00 49.92 C ANISOU 3854 CA ALA B 208 6931 5535 6501 671 333 407 C ATOM 3855 C ALA B 208 46.178 20.642 40.522 1.00 54.46 C ANISOU 3855 C ALA B 208 7382 6161 7147 642 430 489 C ATOM 3856 O ALA B 208 46.343 21.513 41.378 1.00 55.03 O ANISOU 3856 O ALA B 208 7364 6383 7161 740 468 490 O ATOM 3857 CB ALA B 208 47.849 19.018 39.560 1.00 52.63 C ANISOU 3857 CB ALA B 208 7474 5737 6788 735 418 461 C ATOM 3858 N TYR B 209 45.112 19.846 40.493 1.00 55.75 N ANISOU 3858 N TYR B 209 7545 6199 7439 496 478 550 N ATOM 3859 CA TYR B 209 44.032 19.937 41.462 1.00 52.91 C ANISOU 3859 CA TYR B 209 7063 5874 7165 450 588 641 C ATOM 3860 C TYR B 209 43.709 18.552 42.006 1.00 59.00 C ANISOU 3860 C TYR B 209 7952 6489 7974 404 727 757 C ATOM 3861 O TYR B 209 43.645 17.580 41.250 1.00 61.94 O ANISOU 3861 O TYR B 209 8442 6683 8408 294 705 742 O ATOM 3862 CB TYR B 209 42.798 20.590 40.817 1.00 52.07 C ANISOU 3862 CB TYR B 209 6768 5794 7223 288 503 611 C ATOM 3863 CG TYR B 209 43.044 22.048 40.500 1.00 54.03 C ANISOU 3863 CG TYR B 209 6895 6190 7446 359 406 530 C ATOM 3864 CD1 TYR B 209 43.703 22.427 39.335 1.00 56.64 C ANISOU 3864 CD1 TYR B 209 7267 6521 7733 359 259 437 C ATOM 3865 CD2 TYR B 209 42.650 23.047 41.388 1.00 50.23 C ANISOU 3865 CD2 TYR B 209 6269 5834 6980 433 480 548 C ATOM 3866 CE1 TYR B 209 43.950 23.770 39.056 1.00 55.00 C ANISOU 3866 CE1 TYR B 209 6957 6428 7513 425 189 378 C ATOM 3867 CE2 TYR B 209 42.881 24.378 41.124 1.00 47.78 C ANISOU 3867 CE2 TYR B 209 5864 5625 6664 497 413 473 C ATOM 3868 CZ TYR B 209 43.538 24.738 39.958 1.00 55.10 C ANISOU 3868 CZ TYR B 209 6833 6542 7562 491 268 395 C ATOM 3869 OH TYR B 209 43.787 26.068 39.700 1.00 60.32 O ANISOU 3869 OH TYR B 209 7407 7283 8227 554 218 334 O ATOM 3870 N ASP B 210 43.502 18.461 43.320 1.00 58.48 N ANISOU 3870 N ASP B 210 7867 6485 7870 487 881 870 N ATOM 3871 CA ASP B 210 43.286 17.167 43.951 1.00 59.79 C ANISOU 3871 CA ASP B 210 8157 6503 8060 470 1040 1009 C ATOM 3872 C ASP B 210 41.783 16.876 44.014 1.00 68.45 C ANISOU 3872 C ASP B 210 9131 7523 9355 262 1108 1069 C ATOM 3873 O ASP B 210 40.970 17.588 43.419 1.00 70.51 O ANISOU 3873 O ASP B 210 9215 7842 9733 134 1009 998 O ATOM 3874 CB ASP B 210 43.988 17.126 45.317 1.00 54.57 C ANISOU 3874 CB ASP B 210 7558 5959 7216 686 1171 1118 C ATOM 3875 CG ASP B 210 43.331 18.025 46.371 1.00 63.32 C ANISOU 3875 CG ASP B 210 8501 7257 8300 721 1253 1152 C ATOM 3876 OD1 ASP B 210 42.259 18.605 46.122 1.00 69.17 O ANISOU 3876 OD1 ASP B 210 9074 8018 9188 585 1234 1116 O ATOM 3877 OD2 ASP B 210 43.899 18.155 47.473 1.00 69.73 O ANISOU 3877 OD2 ASP B 210 9350 8209 8935 893 1340 1216 O ATOM 3878 N LYS B 211 41.400 15.839 44.768 1.00 78.51 N ANISOU 3878 N LYS B 211 10485 8675 10671 233 1285 1217 N ATOM 3879 CA LYS B 211 40.011 15.378 44.778 1.00 83.56 C ANISOU 3879 CA LYS B 211 11015 9216 11518 9 1363 1280 C ATOM 3880 C LYS B 211 39.063 16.392 45.415 1.00 80.89 C ANISOU 3880 C LYS B 211 10432 9072 11232 -2 1406 1308 C ATOM 3881 O LYS B 211 37.882 16.428 45.058 1.00 80.66 O ANISOU 3881 O LYS B 211 10233 9023 11392 -197 1393 1308 O ATOM 3882 CB LYS B 211 39.901 14.022 45.483 1.00 93.14 C ANISOU 3882 CB LYS B 211 12387 10236 12765 -11 1568 1447 C ATOM 3883 CG LYS B 211 40.209 14.034 46.978 1.00101.46 C ANISOU 3883 CG LYS B 211 13478 11406 13665 195 1754 1612 C ATOM 3884 CD LYS B 211 40.052 12.641 47.583 1.00105.90 C ANISOU 3884 CD LYS B 211 14206 11753 14278 169 1965 1802 C ATOM 3885 CE LYS B 211 40.432 12.637 49.052 1.00110.78 C ANISOU 3885 CE LYS B 211 14874 12511 14706 395 2141 1982 C ATOM 3886 NZ LYS B 211 41.860 13.003 49.252 1.00112.51 N ANISOU 3886 NZ LYS B 211 15200 12874 14676 660 2057 1948 N ATOM 3887 N ASN B 212 39.541 17.196 46.368 1.00 78.39 N ANISOU 3887 N ASN B 212 10089 8944 10751 203 1464 1328 N ATOM 3888 CA ASN B 212 38.756 18.293 46.930 1.00 73.69 C ANISOU 3888 CA ASN B 212 9276 8532 10190 221 1508 1324 C ATOM 3889 C ASN B 212 38.816 19.552 46.077 1.00 74.25 C ANISOU 3889 C ASN B 212 9214 8712 10288 226 1321 1167 C ATOM 3890 O ASN B 212 38.435 20.624 46.558 1.00 66.39 O ANISOU 3890 O ASN B 212 8066 7869 9290 295 1356 1142 O ATOM 3891 CB ASN B 212 39.239 18.629 48.341 1.00 75.15 C ANISOU 3891 CB ASN B 212 9506 8875 10174 431 1657 1393 C ATOM 3892 CG ASN B 212 39.388 17.405 49.206 1.00 86.86 C ANISOU 3892 CG ASN B 212 11150 10266 11588 471 1839 1571 C ATOM 3893 OD1 ASN B 212 38.446 16.632 49.374 1.00 85.73 O ANISOU 3893 OD1 ASN B 212 10975 10000 11597 327 1968 1691 O ATOM 3894 ND2 ASN B 212 40.591 17.196 49.733 1.00 94.54 N ANISOU 3894 ND2 ASN B 212 12291 11294 12336 666 1851 1599 N ATOM 3895 N ASN B 213 39.314 19.446 44.842 1.00 76.49 N ANISOU 3895 N ASN B 213 9562 8913 10587 166 1139 1064 N ATOM 3896 CA ASN B 213 39.488 20.584 43.945 1.00 72.74 C ANISOU 3896 CA ASN B 213 8987 8528 10122 180 962 932 C ATOM 3897 C ASN B 213 40.326 21.693 44.572 1.00 65.37 C ANISOU 3897 C ASN B 213 8055 7754 9028 383 972 871 C ATOM 3898 O ASN B 213 40.117 22.874 44.297 1.00 67.31 O ANISOU 3898 O ASN B 213 8164 8095 9314 409 906 797 O ATOM 3899 CB ASN B 213 38.135 21.120 43.481 1.00 83.78 C ANISOU 3899 CB ASN B 213 10142 9967 11722 35 917 937 C ATOM 3900 CG ASN B 213 37.433 20.160 42.544 1.00 99.41 C ANISOU 3900 CG ASN B 213 12108 11811 13852 -197 839 948 C ATOM 3901 OD1 ASN B 213 37.654 20.190 41.333 1.00104.90 O ANISOU 3901 OD1 ASN B 213 12828 12472 14556 -273 659 855 O ATOM 3902 ND2 ASN B 213 36.582 19.301 43.099 1.00104.37 N ANISOU 3902 ND2 ASN B 213 12699 12364 14593 -319 979 1055 N ATOM 3903 N GLU B 214 41.300 21.320 45.382 1.00 59.72 N ANISOU 3903 N GLU B 214 7495 7066 8131 527 1051 899 N ATOM 3904 CA GLU B 214 42.291 22.238 45.922 1.00 55.54 C ANISOU 3904 CA GLU B 214 6989 6691 7423 702 1039 819 C ATOM 3905 C GLU B 214 43.550 22.198 45.077 1.00 56.20 C ANISOU 3905 C GLU B 214 7194 6748 7412 754 893 730 C ATOM 3906 O GLU B 214 43.906 21.143 44.548 1.00 58.26 O ANISOU 3906 O GLU B 214 7587 6876 7672 718 865 765 O ATOM 3907 CB GLU B 214 42.640 21.886 47.371 1.00 59.75 C ANISOU 3907 CB GLU B 214 7601 7317 7786 837 1202 907 C ATOM 3908 CG GLU B 214 41.502 22.215 48.343 1.00 65.90 C ANISOU 3908 CG GLU B 214 8249 8169 8621 820 1366 974 C ATOM 3909 CD GLU B 214 41.240 23.718 48.411 1.00 75.67 C ANISOU 3909 CD GLU B 214 9334 9532 9884 857 1343 849 C ATOM 3910 OE1 GLU B 214 42.191 24.481 48.692 1.00 78.72 O ANISOU 3910 OE1 GLU B 214 9761 10033 10114 974 1300 737 O ATOM 3911 OE2 GLU B 214 40.094 24.142 48.154 1.00 78.94 O ANISOU 3911 OE2 GLU B 214 9584 9925 10485 766 1369 860 O ATOM 3912 N PRO B 215 44.228 23.339 44.931 1.00 55.74 N ANISOU 3912 N PRO B 215 7093 6805 7281 834 812 611 N ATOM 3913 CA PRO B 215 45.424 23.389 44.075 1.00 48.98 C ANISOU 3913 CA PRO B 215 6329 5937 6345 878 680 527 C ATOM 3914 C PRO B 215 46.623 22.679 44.690 1.00 56.44 C ANISOU 3914 C PRO B 215 7421 6923 7099 1018 719 563 C ATOM 3915 O PRO B 215 46.805 22.644 45.907 1.00 59.56 O ANISOU 3915 O PRO B 215 7828 7432 7371 1120 823 614 O ATOM 3916 CB PRO B 215 45.696 24.890 43.927 1.00 44.75 C ANISOU 3916 CB PRO B 215 5686 5515 5803 916 617 403 C ATOM 3917 CG PRO B 215 45.104 25.496 45.157 1.00 49.51 C ANISOU 3917 CG PRO B 215 6198 6223 6391 962 747 413 C ATOM 3918 CD PRO B 215 43.883 24.657 45.491 1.00 50.14 C ANISOU 3918 CD PRO B 215 6246 6226 6581 878 851 544 C ATOM 3919 N VAL B 216 47.457 22.120 43.815 1.00 51.72 N ANISOU 3919 N VAL B 216 6933 6245 6471 1031 634 541 N ATOM 3920 CA VAL B 216 48.706 21.465 44.180 1.00 45.66 C ANISOU 3920 CA VAL B 216 6294 5517 5539 1181 653 577 C ATOM 3921 C VAL B 216 49.769 21.949 43.210 1.00 49.15 C ANISOU 3921 C VAL B 216 6748 5990 5937 1214 524 463 C ATOM 3922 O VAL B 216 49.530 21.984 41.997 1.00 54.06 O ANISOU 3922 O VAL B 216 7376 6501 6664 1108 439 408 O ATOM 3923 CB VAL B 216 48.575 19.929 44.112 1.00 50.02 C ANISOU 3923 CB VAL B 216 6998 5886 6122 1173 730 704 C ATOM 3924 CG1 VAL B 216 49.852 19.250 44.594 1.00 49.54 C ANISOU 3924 CG1 VAL B 216 7059 5873 5891 1364 766 771 C ATOM 3925 CG2 VAL B 216 47.351 19.442 44.920 1.00 44.70 C ANISOU 3925 CG2 VAL B 216 6300 5152 5532 1098 867 825 C ATOM 3926 N ILE B 217 50.935 22.326 43.720 1.00 45.36 N ANISOU 3926 N ILE B 217 6263 5673 5297 1354 509 428 N ATOM 3927 CA ILE B 217 51.999 22.769 42.823 1.00 48.06 C ANISOU 3927 CA ILE B 217 6605 6052 5602 1384 403 329 C ATOM 3928 C ILE B 217 53.220 21.864 42.974 1.00 55.04 C ANISOU 3928 C ILE B 217 7593 6966 6352 1540 419 390 C ATOM 3929 O ILE B 217 53.477 21.307 44.045 1.00 51.56 O ANISOU 3929 O ILE B 217 7186 6604 5799 1658 496 491 O ATOM 3930 CB ILE B 217 52.352 24.251 43.046 1.00 45.04 C ANISOU 3930 CB ILE B 217 6090 5839 5186 1383 351 204 C ATOM 3931 CG1 ILE B 217 52.795 24.508 44.484 1.00 45.65 C ANISOU 3931 CG1 ILE B 217 6127 6115 5102 1492 408 208 C ATOM 3932 CG2 ILE B 217 51.131 25.141 42.697 1.00 41.24 C ANISOU 3932 CG2 ILE B 217 5510 5295 4866 1245 339 156 C ATOM 3933 CD1 ILE B 217 53.064 25.993 44.722 1.00 46.10 C ANISOU 3933 CD1 ILE B 217 6062 6313 5141 1464 369 57 C ATOM 3934 N LEU B 218 53.968 21.721 41.874 1.00 54.77 N ANISOU 3934 N LEU B 218 7608 6876 6327 1550 353 338 N ATOM 3935 CA LEU B 218 54.984 20.684 41.703 1.00 57.11 C ANISOU 3935 CA LEU B 218 8020 7138 6543 1691 381 403 C ATOM 3936 C LEU B 218 56.246 21.271 41.084 1.00 55.79 C ANISOU 3936 C LEU B 218 7800 7091 6306 1757 303 312 C ATOM 3937 O LEU B 218 56.266 22.409 40.603 1.00 52.12 O ANISOU 3937 O LEU B 218 7233 6694 5876 1668 227 198 O ATOM 3938 CB LEU B 218 54.481 19.545 40.797 1.00 60.26 C ANISOU 3938 CB LEU B 218 8575 7273 7049 1623 416 441 C ATOM 3939 CG LEU B 218 53.062 19.016 40.998 1.00 62.53 C ANISOU 3939 CG LEU B 218 8902 7396 7461 1485 477 502 C ATOM 3940 CD1 LEU B 218 52.542 18.352 39.744 1.00 58.56 C ANISOU 3940 CD1 LEU B 218 8508 6663 7077 1346 455 457 C ATOM 3941 CD2 LEU B 218 53.071 18.040 42.144 1.00 59.29 C ANISOU 3941 CD2 LEU B 218 8571 6961 6995 1602 607 661 C ATOM 3942 N ASP B 219 57.308 20.469 41.094 1.00 58.04 N ANISOU 3942 N ASP B 219 8153 7397 6502 1920 334 375 N ATOM 3943 CA ASP B 219 58.543 20.765 40.374 1.00 59.40 C ANISOU 3943 CA ASP B 219 8288 7659 6622 1992 282 308 C ATOM 3944 C ASP B 219 59.105 22.161 40.659 1.00 60.99 C ANISOU 3944 C ASP B 219 8309 8096 6769 1966 203 201 C ATOM 3945 O ASP B 219 59.323 22.943 39.733 1.00 62.68 O ANISOU 3945 O ASP B 219 8473 8308 7035 1878 145 98 O ATOM 3946 CB ASP B 219 58.325 20.600 38.876 1.00 57.27 C ANISOU 3946 CB ASP B 219 8108 7199 6452 1889 258 239 C ATOM 3947 CG ASP B 219 57.889 19.220 38.502 1.00 70.61 C ANISOU 3947 CG ASP B 219 9987 8647 8196 1900 337 310 C ATOM 3948 OD1 ASP B 219 58.549 18.252 38.932 1.00 78.08 O ANISOU 3948 OD1 ASP B 219 11014 9571 9081 2073 418 411 O ATOM 3949 OD2 ASP B 219 56.885 19.114 37.765 1.00 78.69 O ANISOU 3949 OD2 ASP B 219 11074 9500 9325 1733 317 263 O ATOM 3950 N PRO B 220 59.389 22.481 41.917 1.00 60.81 N ANISOU 3950 N PRO B 220 8193 8277 6635 2038 204 222 N ATOM 3951 CA PRO B 220 59.800 23.848 42.243 1.00 61.33 C ANISOU 3951 CA PRO B 220 8096 8545 6661 1977 136 94 C ATOM 3952 C PRO B 220 61.220 24.161 41.797 1.00 60.25 C ANISOU 3952 C PRO B 220 7870 8558 6463 2045 85 39 C ATOM 3953 O PRO B 220 62.011 23.283 41.452 1.00 66.34 O ANISOU 3953 O PRO B 220 8690 9324 7192 2182 107 117 O ATOM 3954 CB PRO B 220 59.684 23.884 43.767 1.00 59.69 C ANISOU 3954 CB PRO B 220 7839 8517 6324 2043 160 135 C ATOM 3955 CG PRO B 220 59.942 22.473 44.174 1.00 60.07 C ANISOU 3955 CG PRO B 220 7994 8539 6293 2216 224 311 C ATOM 3956 CD PRO B 220 59.274 21.644 43.123 1.00 57.49 C ANISOU 3956 CD PRO B 220 7818 7910 6115 2165 273 362 C ATOM 3957 N ALA B 221 61.514 25.463 41.776 1.00 54.71 N ANISOU 3957 N ALA B 221 7036 7978 5775 1942 29 -98 N ATOM 3958 CA ALA B 221 62.867 26.010 41.725 1.00 51.94 C ANISOU 3958 CA ALA B 221 6547 7835 5352 1979 -21 -169 C ATOM 3959 C ALA B 221 62.990 27.102 42.796 1.00 56.05 C ANISOU 3959 C ALA B 221 6929 8566 5803 1909 -62 -286 C ATOM 3960 O ALA B 221 63.252 28.268 42.499 1.00 57.80 O ANISOU 3960 O ALA B 221 7052 8825 6084 1782 -94 -425 O ATOM 3961 CB ALA B 221 63.176 26.551 40.328 1.00 49.97 C ANISOU 3961 CB ALA B 221 6287 7483 5216 1888 -36 -238 C ATOM 3962 N CYS B 222 62.799 26.712 44.060 1.00 57.24 N ANISOU 3962 N CYS B 222 7081 8848 5821 1990 -51 -233 N ATOM 3963 CA CYS B 222 62.490 27.667 45.125 1.00 56.12 C ANISOU 3963 CA CYS B 222 6858 8851 5614 1905 -66 -352 C ATOM 3964 C CYS B 222 63.641 28.605 45.446 1.00 53.04 C ANISOU 3964 C CYS B 222 6296 8715 5140 1860 -141 -501 C ATOM 3965 O CYS B 222 64.812 28.263 45.312 1.00 56.21 O ANISOU 3965 O CYS B 222 6613 9279 5463 1953 -188 -468 O ATOM 3966 CB CYS B 222 62.113 26.957 46.429 1.00 57.25 C ANISOU 3966 CB CYS B 222 7046 9110 5597 2019 -32 -248 C ATOM 3967 SG CYS B 222 60.569 26.053 46.439 1.00 63.36 S ANISOU 3967 SG CYS B 222 7997 9613 6465 2027 74 -97 S ATOM 3968 N TYR B 223 63.274 29.783 45.940 1.00 53.42 N ANISOU 3968 N TYR B 223 6289 8801 5207 1714 -145 -669 N ATOM 3969 CA TYR B 223 64.176 30.685 46.644 1.00 54.48 C ANISOU 3969 CA TYR B 223 6269 9200 5230 1648 -209 -838 C ATOM 3970 C TYR B 223 63.326 31.783 47.273 1.00 51.57 C ANISOU 3970 C TYR B 223 5910 8787 4898 1502 -169 -1005 C ATOM 3971 O TYR B 223 62.117 31.863 47.049 1.00 51.09 O ANISOU 3971 O TYR B 223 5953 8495 4962 1464 -93 -974 O ATOM 3972 CB TYR B 223 65.252 31.268 45.721 1.00 58.83 C ANISOU 3972 CB TYR B 223 6703 9781 5868 1573 -255 -920 C ATOM 3973 CG TYR B 223 64.769 32.219 44.628 1.00 59.36 C ANISOU 3973 CG TYR B 223 6801 9588 6167 1409 -210 -1005 C ATOM 3974 CD1 TYR B 223 64.157 31.746 43.464 1.00 53.56 C ANISOU 3974 CD1 TYR B 223 6185 8591 5576 1432 -166 -883 C ATOM 3975 CD2 TYR B 223 64.972 33.589 44.748 1.00 59.71 C ANISOU 3975 CD2 TYR B 223 6756 9652 6278 1233 -212 -1205 C ATOM 3976 CE1 TYR B 223 63.739 32.632 42.463 1.00 53.54 C ANISOU 3976 CE1 TYR B 223 6202 8377 5764 1297 -133 -940 C ATOM 3977 CE2 TYR B 223 64.559 34.471 43.770 1.00 53.85 C ANISOU 3977 CE2 TYR B 223 6044 8671 5747 1102 -161 -1257 C ATOM 3978 CZ TYR B 223 63.954 33.994 42.631 1.00 54.35 C ANISOU 3978 CZ TYR B 223 6215 8500 5935 1142 -126 -1115 C ATOM 3979 OH TYR B 223 63.580 34.905 41.673 1.00 52.77 O ANISOU 3979 OH TYR B 223 6035 8089 5925 1022 -83 -1152 O ATOM 3980 N TYR B 224 63.974 32.619 48.078 1.00 50.93 N ANISOU 3980 N TYR B 224 5713 8937 4702 1421 -217 -1187 N ATOM 3981 CA TYR B 224 63.331 33.747 48.734 1.00 53.89 C ANISOU 3981 CA TYR B 224 6094 9283 5098 1280 -170 -1383 C ATOM 3982 C TYR B 224 63.602 34.997 47.919 1.00 55.84 C ANISOU 3982 C TYR B 224 6283 9389 5546 1098 -158 -1550 C ATOM 3983 O TYR B 224 64.766 35.358 47.713 1.00 53.45 O ANISOU 3983 O TYR B 224 5853 9233 5221 1036 -228 -1637 O ATOM 3984 CB TYR B 224 63.846 33.925 50.161 1.00 60.02 C ANISOU 3984 CB TYR B 224 6796 10399 5612 1286 -224 -1507 C ATOM 3985 CG TYR B 224 63.469 32.792 51.073 1.00 60.60 C ANISOU 3985 CG TYR B 224 6940 10610 5478 1467 -214 -1333 C ATOM 3986 CD1 TYR B 224 62.265 32.799 51.757 1.00 62.02 C ANISOU 3986 CD1 TYR B 224 7230 10703 5632 1476 -114 -1324 C ATOM 3987 CD2 TYR B 224 64.310 31.703 51.234 1.00 62.62 C ANISOU 3987 CD2 TYR B 224 7149 11072 5570 1638 -290 -1160 C ATOM 3988 CE1 TYR B 224 61.918 31.763 52.583 1.00 67.52 C ANISOU 3988 CE1 TYR B 224 7994 11517 6143 1637 -88 -1149 C ATOM 3989 CE2 TYR B 224 63.971 30.661 52.063 1.00 63.05 C ANISOU 3989 CE2 TYR B 224 7278 11236 5442 1812 -266 -978 C ATOM 3990 CZ TYR B 224 62.778 30.697 52.737 1.00 67.00 C ANISOU 3990 CZ TYR B 224 7893 11648 5916 1804 -165 -973 C ATOM 3991 OH TYR B 224 62.433 29.658 53.566 1.00 68.95 O ANISOU 3991 OH TYR B 224 8217 11997 5982 1973 -125 -776 O ATOM 3992 N GLY B 225 62.536 35.649 47.458 1.00 56.38 N ANISOU 3992 N GLY B 225 6435 9175 5813 1017 -66 -1581 N ATOM 3993 CA GLY B 225 62.695 36.790 46.589 1.00 50.97 C ANISOU 3993 CA GLY B 225 5715 8313 5337 864 -36 -1696 C ATOM 3994 C GLY B 225 61.506 37.722 46.633 1.00 53.78 C ANISOU 3994 C GLY B 225 6146 8431 5858 782 75 -1779 C ATOM 3995 O GLY B 225 60.636 37.617 47.501 1.00 55.74 O ANISOU 3995 O GLY B 225 6453 8687 6039 825 130 -1791 O ATOM 3996 N HIS B 226 61.501 38.659 45.689 1.00 50.41 N ANISOU 3996 N HIS B 226 5710 7795 5648 671 117 -1827 N ATOM 3997 CA HIS B 226 60.360 39.537 45.512 1.00 52.14 C ANISOU 3997 CA HIS B 226 5996 7754 6062 619 230 -1865 C ATOM 3998 C HIS B 226 59.171 38.706 45.060 1.00 54.61 C ANISOU 3998 C HIS B 226 6394 7922 6435 737 253 -1649 C ATOM 3999 O HIS B 226 59.266 37.968 44.073 1.00 56.00 O ANISOU 3999 O HIS B 226 6588 8045 6646 792 201 -1481 O ATOM 4000 CB HIS B 226 60.673 40.614 44.482 1.00 51.97 C ANISOU 4000 CB HIS B 226 5949 7536 6260 496 270 -1915 C ATOM 4001 CG HIS B 226 59.673 41.723 44.459 1.00 54.45 C ANISOU 4001 CG HIS B 226 6317 7598 6773 440 398 -1985 C ATOM 4002 ND1 HIS B 226 59.666 42.702 43.489 1.00 55.27 N ANISOU 4002 ND1 HIS B 226 6424 7473 7105 358 461 -1984 N ATOM 4003 CD2 HIS B 226 58.640 42.004 45.285 1.00 57.16 C ANISOU 4003 CD2 HIS B 226 6711 7881 7125 470 487 -2046 C ATOM 4004 CE1 HIS B 226 58.684 43.555 43.733 1.00 57.38 C ANISOU 4004 CE1 HIS B 226 6741 7541 7519 346 583 -2040 C ATOM 4005 NE2 HIS B 226 58.037 43.147 44.810 1.00 57.09 N ANISOU 4005 NE2 HIS B 226 6731 7604 7356 414 603 -2083 N ATOM 4006 N ASN B 227 58.075 38.782 45.774 1.00 52.92 N ANISOU 4006 N ASN B 227 6228 7654 6226 772 332 -1659 N ATOM 4007 CA ASN B 227 56.921 37.992 45.446 1.00 49.61 C ANISOU 4007 CA ASN B 227 5868 7118 5865 865 354 -1465 C ATOM 4008 C ASN B 227 56.460 38.101 44.017 1.00 52.03 C ANISOU 4008 C ASN B 227 6190 7202 6378 853 347 -1330 C ATOM 4009 O ASN B 227 55.962 37.170 43.483 1.00 49.86 O ANISOU 4009 O ASN B 227 5951 6883 6112 916 311 -1161 O ATOM 4010 CB ASN B 227 55.792 38.298 46.411 1.00 42.86 C ANISOU 4010 CB ASN B 227 5040 6229 5017 887 465 -1513 C ATOM 4011 CG ASN B 227 55.091 39.576 46.092 1.00 49.10 C ANISOU 4011 CG ASN B 227 5827 6798 6032 825 570 -1593 C ATOM 4012 OD1 ASN B 227 55.651 40.617 46.161 1.00 51.56 O ANISOU 4012 OD1 ASN B 227 6117 7078 6394 734 601 -1764 O ATOM 4013 ND2 ASN B 227 53.867 39.481 45.737 1.00 49.55 N ANISOU 4013 ND2 ASN B 227 5896 6699 6230 874 627 -1462 N ATOM 4014 N GLU B 228 56.611 39.258 43.414 1.00 54.18 N ANISOU 4014 N GLU B 228 6439 7334 6813 767 385 -1406 N ATOM 4015 CA GLU B 228 56.187 39.461 42.030 1.00 47.91 C ANISOU 4015 CA GLU B 228 5658 6344 6201 761 377 -1268 C ATOM 4016 C GLU B 228 56.983 38.629 41.035 1.00 51.65 C ANISOU 4016 C GLU B 228 6140 6872 6613 780 275 -1154 C ATOM 4017 O GLU B 228 56.554 38.503 39.882 1.00 51.39 O ANISOU 4017 O GLU B 228 6134 6710 6682 791 251 -1018 O ATOM 4018 CB GLU B 228 56.312 40.925 41.616 1.00 46.38 C ANISOU 4018 CB GLU B 228 5444 5988 6191 671 454 -1364 C ATOM 4019 CG GLU B 228 55.452 41.935 42.386 1.00 45.10 C ANISOU 4019 CG GLU B 228 5285 5707 6143 657 586 -1477 C ATOM 4020 CD GLU B 228 55.785 43.364 41.951 1.00 56.68 C ANISOU 4020 CD GLU B 228 6745 6995 7796 562 672 -1577 C ATOM 4021 OE1 GLU B 228 56.587 43.514 40.986 1.00 58.93 O ANISOU 4021 OE1 GLU B 228 7016 7252 8122 510 625 -1529 O ATOM 4022 OE2 GLU B 228 55.263 44.331 42.561 1.00 55.55 O ANISOU 4022 OE2 GLU B 228 6615 6731 7761 542 799 -1700 O ATOM 4023 N ALA B 229 58.152 38.110 41.426 1.00 46.55 N ANISOU 4023 N ALA B 229 5467 6419 5800 787 216 -1211 N ATOM 4024 CA ALA B 229 58.944 37.314 40.496 1.00 46.70 C ANISOU 4024 CA ALA B 229 5494 6487 5763 822 140 -1107 C ATOM 4025 C ALA B 229 58.309 35.960 40.225 1.00 43.34 C ANISOU 4025 C ALA B 229 5143 6046 5278 923 99 -942 C ATOM 4026 O ALA B 229 58.663 35.321 39.232 1.00 45.68 O ANISOU 4026 O ALA B 229 5475 6318 5563 952 53 -844 O ATOM 4027 CB ALA B 229 60.380 37.137 41.009 1.00 43.11 C ANISOU 4027 CB ALA B 229 4967 6258 5156 817 94 -1202 C ATOM 4028 N ASP B 230 57.356 35.522 41.058 1.00 45.75 N ANISOU 4028 N ASP B 230 5478 6352 5552 967 128 -913 N ATOM 4029 CA ASP B 230 56.711 34.235 40.809 1.00 42.40 C ANISOU 4029 CA ASP B 230 5126 5890 5093 1040 101 -760 C ATOM 4030 C ASP B 230 55.706 34.278 39.651 1.00 44.27 C ANISOU 4030 C ASP B 230 5396 5937 5486 1007 91 -655 C ATOM 4031 O ASP B 230 55.149 33.235 39.307 1.00 52.52 O ANISOU 4031 O ASP B 230 6501 6936 6517 1038 63 -542 O ATOM 4032 CB ASP B 230 56.021 33.722 42.081 1.00 49.49 C ANISOU 4032 CB ASP B 230 6040 6855 5909 1091 148 -749 C ATOM 4033 CG ASP B 230 56.464 32.281 42.471 1.00 54.94 C ANISOU 4033 CG ASP B 230 6785 7655 6434 1193 118 -653 C ATOM 4034 OD1 ASP B 230 57.269 31.679 41.737 1.00 47.68 O ANISOU 4034 OD1 ASP B 230 5892 6749 5475 1228 65 -604 O ATOM 4035 OD2 ASP B 230 56.013 31.746 43.516 1.00 52.54 O ANISOU 4035 OD2 ASP B 230 6502 7420 6041 1246 161 -619 O ATOM 4036 N PHE B 231 55.453 35.432 39.044 1.00 42.96 N ANISOU 4036 N PHE B 231 5194 5664 5465 943 113 -683 N ATOM 4037 CA PHE B 231 54.626 35.518 37.845 1.00 46.82 C ANISOU 4037 CA PHE B 231 5701 6008 6080 921 84 -569 C ATOM 4038 C PHE B 231 55.439 35.492 36.547 1.00 46.77 C ANISOU 4038 C PHE B 231 5725 5984 6061 903 29 -530 C ATOM 4039 O PHE B 231 54.855 35.630 35.471 1.00 52.75 O ANISOU 4039 O PHE B 231 6500 6644 6898 883 -5 -437 O ATOM 4040 CB PHE B 231 53.772 36.790 37.870 1.00 46.38 C ANISOU 4040 CB PHE B 231 5588 5835 6198 888 149 -586 C ATOM 4041 CG PHE B 231 52.922 36.922 39.092 1.00 51.22 C ANISOU 4041 CG PHE B 231 6170 6459 6834 910 226 -630 C ATOM 4042 CD1 PHE B 231 52.315 35.812 39.648 1.00 54.63 C ANISOU 4042 CD1 PHE B 231 6623 6942 7190 949 217 -567 C ATOM 4043 CD2 PHE B 231 52.729 38.163 39.687 1.00 60.58 C ANISOU 4043 CD2 PHE B 231 7310 7589 8117 892 324 -736 C ATOM 4044 CE1 PHE B 231 51.542 35.927 40.785 1.00 58.52 C ANISOU 4044 CE1 PHE B 231 7086 7455 7692 973 304 -600 C ATOM 4045 CE2 PHE B 231 51.941 38.294 40.827 1.00 64.06 C ANISOU 4045 CE2 PHE B 231 7728 8045 8567 920 412 -785 C ATOM 4046 CZ PHE B 231 51.355 37.171 41.379 1.00 62.65 C ANISOU 4046 CZ PHE B 231 7564 7942 8300 963 402 -712 C ATOM 4047 N GLY B 232 56.753 35.284 36.620 1.00 50.42 N ANISOU 4047 N GLY B 232 6187 6556 6415 916 18 -590 N ATOM 4048 CA GLY B 232 57.631 35.348 35.457 1.00 51.52 C ANISOU 4048 CA GLY B 232 6343 6693 6538 902 -9 -562 C ATOM 4049 C GLY B 232 57.448 34.248 34.419 1.00 46.76 C ANISOU 4049 C GLY B 232 5833 6057 5877 937 -69 -454 C ATOM 4050 O GLY B 232 58.078 34.323 33.364 1.00 49.05 O ANISOU 4050 O GLY B 232 6148 6341 6148 929 -81 -425 O ATOM 4051 N MET B 233 56.610 33.246 34.683 1.00 46.72 N ANISOU 4051 N MET B 233 5883 6027 5843 968 -95 -399 N ATOM 4052 CA MET B 233 56.260 32.212 33.709 1.00 43.00 C ANISOU 4052 CA MET B 233 5510 5499 5330 976 -149 -317 C ATOM 4053 C MET B 233 54.799 32.345 33.278 1.00 52.49 C ANISOU 4053 C MET B 233 6709 6600 6635 920 -187 -245 C ATOM 4054 O MET B 233 54.227 31.386 32.752 1.00 51.32 O ANISOU 4054 O MET B 233 6634 6407 6458 904 -237 -193 O ATOM 4055 CB MET B 233 56.513 30.804 34.274 1.00 45.90 C ANISOU 4055 CB MET B 233 5950 5904 5585 1045 -146 -308 C ATOM 4056 CG MET B 233 57.984 30.347 34.198 1.00 45.13 C ANISOU 4056 CG MET B 233 5874 5904 5370 1124 -129 -338 C ATOM 4057 SD MET B 233 58.561 30.186 32.470 1.00 53.99 S ANISOU 4057 SD MET B 233 7075 6984 6457 1114 -153 -312 S ATOM 4058 CE MET B 233 57.667 28.738 31.961 1.00 53.23 C ANISOU 4058 CE MET B 233 7131 6768 6327 1114 -186 -257 C ATOM 4059 N SER B 234 54.170 33.506 33.524 1.00 43.49 N ANISOU 4059 N SER B 234 5482 5423 5622 889 -160 -245 N ATOM 4060 CA SER B 234 52.732 33.636 33.306 1.00 48.61 C ANISOU 4060 CA SER B 234 6092 5998 6377 855 -190 -167 C ATOM 4061 C SER B 234 52.343 33.483 31.834 1.00 48.46 C ANISOU 4061 C SER B 234 6113 5944 6356 817 -279 -80 C ATOM 4062 O SER B 234 51.192 33.149 31.536 1.00 45.66 O ANISOU 4062 O SER B 234 5737 5560 6050 781 -336 -11 O ATOM 4063 CB SER B 234 52.237 34.987 33.833 1.00 47.38 C ANISOU 4063 CB SER B 234 5836 5802 6366 854 -123 -182 C ATOM 4064 OG SER B 234 52.769 36.048 33.058 1.00 48.16 O ANISOU 4064 OG SER B 234 5920 5864 6515 842 -111 -174 O ATOM 4065 N TRP B 235 53.273 33.703 30.906 1.00 49.10 N ANISOU 4065 N TRP B 235 6244 6042 6371 821 -294 -81 N ATOM 4066 CA TRP B 235 52.967 33.565 29.489 1.00 47.31 C ANISOU 4066 CA TRP B 235 6066 5803 6105 789 -378 -2 C ATOM 4067 C TRP B 235 52.615 32.128 29.102 1.00 57.68 C ANISOU 4067 C TRP B 235 7476 7121 7319 759 -450 -4 C ATOM 4068 O TRP B 235 52.153 31.909 27.981 1.00 59.18 O ANISOU 4068 O TRP B 235 7707 7313 7466 715 -536 47 O ATOM 4069 CB TRP B 235 54.152 34.073 28.659 1.00 46.12 C ANISOU 4069 CB TRP B 235 5955 5678 5889 805 -351 -6 C ATOM 4070 CG TRP B 235 55.436 33.338 28.932 1.00 48.53 C ANISOU 4070 CG TRP B 235 6324 6038 6076 843 -308 -91 C ATOM 4071 CD1 TRP B 235 56.374 33.648 29.867 1.00 56.16 C ANISOU 4071 CD1 TRP B 235 7240 7049 7049 874 -232 -170 C ATOM 4072 CD2 TRP B 235 55.919 32.167 28.252 1.00 52.68 C ANISOU 4072 CD2 TRP B 235 6969 6587 6459 861 -337 -106 C ATOM 4073 NE1 TRP B 235 57.415 32.751 29.821 1.00 58.01 N ANISOU 4073 NE1 TRP B 235 7537 7347 7158 923 -216 -213 N ATOM 4074 CE2 TRP B 235 57.167 31.832 28.834 1.00 58.12 C ANISOU 4074 CE2 TRP B 235 7663 7335 7084 923 -268 -176 C ATOM 4075 CE3 TRP B 235 55.415 31.364 27.211 1.00 52.62 C ANISOU 4075 CE3 TRP B 235 7065 6561 6368 829 -413 -75 C ATOM 4076 CZ2 TRP B 235 57.931 30.722 28.412 1.00 57.11 C ANISOU 4076 CZ2 TRP B 235 7641 7231 6826 976 -256 -201 C ATOM 4077 CZ3 TRP B 235 56.178 30.259 26.785 1.00 53.07 C ANISOU 4077 CZ3 TRP B 235 7248 6629 6289 865 -397 -124 C ATOM 4078 CH2 TRP B 235 57.422 29.951 27.395 1.00 52.92 C ANISOU 4078 CH2 TRP B 235 7231 6652 6224 949 -311 -180 C ATOM 4079 N CYS B 236 52.813 31.146 29.996 1.00 51.28 N ANISOU 4079 N CYS B 236 6708 6308 6467 780 -414 -60 N ATOM 4080 CA CYS B 236 52.358 29.778 29.766 1.00 48.58 C ANISOU 4080 CA CYS B 236 6462 5930 6064 741 -460 -64 C ATOM 4081 C CYS B 236 51.516 29.258 30.934 1.00 45.72 C ANISOU 4081 C CYS B 236 6058 5537 5775 727 -429 -57 C ATOM 4082 O CYS B 236 51.594 28.074 31.284 1.00 58.84 O ANISOU 4082 O CYS B 236 7809 7161 7386 730 -406 -77 O ATOM 4083 CB CYS B 236 53.551 28.844 29.495 1.00 50.82 C ANISOU 4083 CB CYS B 236 6881 6218 6210 795 -427 -121 C ATOM 4084 SG CYS B 236 53.063 27.262 28.632 1.00 64.69 S ANISOU 4084 SG CYS B 236 8804 7894 7882 725 -487 -142 S ATOM 4085 N ALA B 237 50.730 30.132 31.582 1.00 53.09 N ANISOU 4085 N ALA B 237 6860 6479 6833 720 -408 -23 N ATOM 4086 CA ALA B 237 50.001 29.765 32.789 1.00 44.75 C ANISOU 4086 CA ALA B 237 5753 5409 5840 718 -351 -14 C ATOM 4087 C ALA B 237 48.488 29.943 32.710 1.00 55.99 C ANISOU 4087 C ALA B 237 7068 6812 7394 646 -391 57 C ATOM 4088 O ALA B 237 47.772 29.311 33.495 1.00 62.77 O ANISOU 4088 O ALA B 237 7901 7651 8296 619 -351 76 O ATOM 4089 CB ALA B 237 50.523 30.569 33.986 1.00 42.29 C ANISOU 4089 CB ALA B 237 5378 5144 5546 794 -252 -60 C ATOM 4090 N GLY B 238 47.982 30.781 31.815 1.00 57.53 N ANISOU 4090 N GLY B 238 7187 7019 7653 620 -462 110 N ATOM 4091 CA GLY B 238 46.552 31.067 31.798 1.00 64.80 C ANISOU 4091 CA GLY B 238 7967 7944 8708 572 -498 192 C ATOM 4092 C GLY B 238 45.966 31.624 33.083 1.00 65.89 C ANISOU 4092 C GLY B 238 7989 8079 8968 620 -385 202 C ATOM 4093 O GLY B 238 44.870 31.218 33.484 1.00 70.61 O ANISOU 4093 O GLY B 238 8500 8678 9650 573 -378 250 O ATOM 4094 N PHE B 239 46.651 32.572 33.718 1.00 64.23 N ANISOU 4094 N PHE B 239 7770 7867 8768 704 -291 152 N ATOM 4095 CA PHE B 239 46.156 33.222 34.930 1.00 56.65 C ANISOU 4095 CA PHE B 239 6714 6903 7908 755 -169 138 C ATOM 4096 C PHE B 239 45.098 34.270 34.558 1.00 58.69 C ANISOU 4096 C PHE B 239 6824 7141 8336 774 -173 227 C ATOM 4097 O PHE B 239 45.385 35.216 33.810 1.00 52.98 O ANISOU 4097 O PHE B 239 6089 6392 7649 806 -198 253 O ATOM 4098 CB PHE B 239 47.298 33.905 35.693 1.00 48.31 C ANISOU 4098 CB PHE B 239 5706 5855 6795 822 -74 28 C ATOM 4099 CG PHE B 239 48.319 32.968 36.327 1.00 46.12 C ANISOU 4099 CG PHE B 239 5542 5627 6356 834 -53 -48 C ATOM 4100 CD1 PHE B 239 47.963 31.729 36.845 1.00 47.14 C ANISOU 4100 CD1 PHE B 239 5711 5768 6431 816 -44 -19 C ATOM 4101 CD2 PHE B 239 49.651 33.365 36.427 1.00 40.74 C ANISOU 4101 CD2 PHE B 239 4915 4980 5584 869 -35 -137 C ATOM 4102 CE1 PHE B 239 48.928 30.882 37.440 1.00 41.19 C ANISOU 4102 CE1 PHE B 239 5063 5058 5531 855 -17 -65 C ATOM 4103 CE2 PHE B 239 50.630 32.527 37.029 1.00 41.38 C ANISOU 4103 CE2 PHE B 239 5079 5130 5513 903 -20 -192 C ATOM 4104 CZ PHE B 239 50.265 31.302 37.534 1.00 40.14 C ANISOU 4104 CZ PHE B 239 4970 4982 5300 907 -10 -148 C ATOM 4105 N GLY B 240 43.874 34.094 35.074 1.00 64.97 N ANISOU 4105 N GLY B 240 7500 7947 9238 763 -138 287 N ATOM 4106 CA GLY B 240 42.803 35.053 34.900 1.00 66.80 C ANISOU 4106 CA GLY B 240 7568 8169 9645 807 -120 382 C ATOM 4107 C GLY B 240 42.779 36.188 35.923 1.00 65.44 C ANISOU 4107 C GLY B 240 7346 7949 9571 907 50 330 C ATOM 4108 O GLY B 240 43.575 36.260 36.863 1.00 58.96 O ANISOU 4108 O GLY B 240 6613 7119 8671 932 149 207 O ATOM 4109 N GLU B 241 41.790 37.072 35.734 1.00 61.30 N ANISOU 4109 N GLU B 241 6671 7398 9220 969 82 428 N ATOM 4110 CA GLU B 241 41.552 38.162 36.673 1.00 58.79 C ANISOU 4110 CA GLU B 241 6298 7015 9023 1070 261 383 C ATOM 4111 C GLU B 241 41.123 37.637 38.041 1.00 57.26 C ANISOU 4111 C GLU B 241 6082 6862 8814 1071 388 320 C ATOM 4112 O GLU B 241 41.444 38.247 39.068 1.00 52.58 O ANISOU 4112 O GLU B 241 5526 6234 8217 1130 541 203 O ATOM 4113 CB GLU B 241 40.485 39.114 36.108 1.00 59.10 C ANISOU 4113 CB GLU B 241 6170 7018 9266 1155 271 530 C ATOM 4114 CG GLU B 241 40.307 40.412 36.895 1.00 71.79 C ANISOU 4114 CG GLU B 241 7740 8517 11021 1277 471 482 C ATOM 4115 CD GLU B 241 39.037 41.195 36.517 1.00 82.99 C ANISOU 4115 CD GLU B 241 8963 9907 12660 1387 507 653 C ATOM 4116 OE1 GLU B 241 37.913 40.679 36.696 1.00 87.83 O ANISOU 4116 OE1 GLU B 241 9419 10609 13344 1386 495 748 O ATOM 4117 OE2 GLU B 241 39.161 42.345 36.057 1.00 90.79 O ANISOU 4117 OE2 GLU B 241 9950 10784 13763 1481 556 700 O ATOM 4118 N SER B 242 40.422 36.498 38.087 1.00 49.42 N ANISOU 4118 N SER B 242 5035 5943 7801 999 333 389 N ATOM 4119 CA SER B 242 40.074 35.934 39.387 1.00 48.07 C ANISOU 4119 CA SER B 242 4855 5810 7598 998 465 346 C ATOM 4120 C SER B 242 41.302 35.412 40.128 1.00 51.31 C ANISOU 4120 C SER B 242 5448 6241 7806 983 498 211 C ATOM 4121 O SER B 242 41.331 35.455 41.363 1.00 54.70 O ANISOU 4121 O SER B 242 5899 6698 8185 1026 643 138 O ATOM 4122 CB SER B 242 39.035 34.820 39.224 1.00 56.30 C ANISOU 4122 CB SER B 242 5794 6913 8684 906 406 462 C ATOM 4123 OG SER B 242 39.553 33.764 38.433 1.00 80.02 O ANISOU 4123 OG SER B 242 8905 9929 11571 796 248 467 O ATOM 4124 N PHE B 243 42.333 34.950 39.401 1.00 48.78 N ANISOU 4124 N PHE B 243 5256 5920 7361 933 370 179 N ATOM 4125 CA PHE B 243 43.598 34.577 40.042 1.00 46.78 C ANISOU 4125 CA PHE B 243 5155 5699 6920 940 395 59 C ATOM 4126 C PHE B 243 44.262 35.790 40.688 1.00 48.30 C ANISOU 4126 C PHE B 243 5371 5876 7103 1009 499 -73 C ATOM 4127 O PHE B 243 44.643 35.753 41.860 1.00 55.96 O ANISOU 4127 O PHE B 243 6390 6904 7969 1040 600 -172 O ATOM 4128 CB PHE B 243 44.557 33.942 39.018 1.00 43.50 C ANISOU 4128 CB PHE B 243 4852 5281 6394 887 247 58 C ATOM 4129 CG PHE B 243 45.967 33.726 39.537 1.00 40.21 C ANISOU 4129 CG PHE B 243 4567 4910 5800 913 262 -55 C ATOM 4130 CD1 PHE B 243 46.301 32.572 40.252 1.00 40.42 C ANISOU 4130 CD1 PHE B 243 4675 4993 5690 913 283 -59 C ATOM 4131 CD2 PHE B 243 46.961 34.671 39.313 1.00 40.48 C ANISOU 4131 CD2 PHE B 243 4634 4936 5811 938 259 -148 C ATOM 4132 CE1 PHE B 243 47.613 32.365 40.726 1.00 40.27 C ANISOU 4132 CE1 PHE B 243 4757 5043 5503 953 287 -146 C ATOM 4133 CE2 PHE B 243 48.271 34.479 39.784 1.00 43.20 C ANISOU 4133 CE2 PHE B 243 5069 5349 5994 955 263 -252 C ATOM 4134 CZ PHE B 243 48.598 33.329 40.498 1.00 41.12 C ANISOU 4134 CZ PHE B 243 4874 5165 5585 971 271 -248 C ATOM 4135 N TYR B 244 44.442 36.866 39.918 1.00 51.41 N ANISOU 4135 N TYR B 244 5741 6195 7599 1028 475 -79 N ATOM 4136 CA TYR B 244 45.169 38.025 40.428 1.00 52.80 C ANISOU 4136 CA TYR B 244 5954 6330 7778 1067 573 -221 C ATOM 4137 C TYR B 244 44.409 38.728 41.550 1.00 55.38 C ANISOU 4137 C TYR B 244 6216 6635 8190 1132 750 -280 C ATOM 4138 O TYR B 244 45.004 39.132 42.560 1.00 54.39 O ANISOU 4138 O TYR B 244 6150 6538 7976 1145 851 -440 O ATOM 4139 CB TYR B 244 45.466 38.996 39.287 1.00 43.81 C ANISOU 4139 CB TYR B 244 4807 5090 6749 1070 525 -189 C ATOM 4140 CG TYR B 244 46.548 38.502 38.356 1.00 51.11 C ANISOU 4140 CG TYR B 244 5822 6044 7554 1013 387 -184 C ATOM 4141 CD1 TYR B 244 47.875 38.433 38.785 1.00 50.16 C ANISOU 4141 CD1 TYR B 244 5795 5976 7288 988 393 -322 C ATOM 4142 CD2 TYR B 244 46.258 38.126 37.044 1.00 46.33 C ANISOU 4142 CD2 TYR B 244 5201 5430 6974 987 255 -45 C ATOM 4143 CE1 TYR B 244 48.885 37.978 37.946 1.00 51.90 C ANISOU 4143 CE1 TYR B 244 6087 6229 7404 948 285 -314 C ATOM 4144 CE2 TYR B 244 47.263 37.661 36.194 1.00 43.10 C ANISOU 4144 CE2 TYR B 244 4884 5050 6443 942 148 -48 C ATOM 4145 CZ TYR B 244 48.574 37.593 36.648 1.00 49.32 C ANISOU 4145 CZ TYR B 244 5759 5878 7102 929 172 -179 C ATOM 4146 OH TYR B 244 49.579 37.159 35.810 1.00 51.58 O ANISOU 4146 OH TYR B 244 6124 6196 7277 898 84 -179 O ATOM 4147 N ASN B 245 43.098 38.877 41.403 1.00 48.76 N ANISOU 4147 N ASN B 245 5250 5760 7516 1172 793 -158 N ATOM 4148 CA ASN B 245 42.360 39.583 42.432 1.00 50.57 C ANISOU 4148 CA ASN B 245 5416 5962 7836 1249 983 -212 C ATOM 4149 C ASN B 245 42.320 38.793 43.727 1.00 51.38 C ANISOU 4149 C ASN B 245 5558 6183 7783 1244 1068 -278 C ATOM 4150 O ASN B 245 42.360 39.400 44.804 1.00 47.51 O ANISOU 4150 O ASN B 245 5093 5698 7260 1292 1227 -413 O ATOM 4151 CB ASN B 245 40.957 39.936 41.935 1.00 44.38 C ANISOU 4151 CB ASN B 245 4461 5125 7276 1309 1012 -47 C ATOM 4152 CG ASN B 245 40.979 41.118 40.991 1.00 54.19 C ANISOU 4152 CG ASN B 245 5671 6235 8683 1362 999 -2 C ATOM 4153 OD1 ASN B 245 42.056 41.663 40.692 1.00 54.52 O ANISOU 4153 OD1 ASN B 245 5826 6213 8677 1338 975 -98 O ATOM 4154 ND2 ASN B 245 39.806 41.530 40.515 1.00 53.02 N ANISOU 4154 ND2 ASN B 245 5363 6049 8734 1438 1019 157 N ATOM 4155 N ALA B 246 42.291 37.452 43.659 1.00 45.21 N ANISOU 4155 N ALA B 246 4795 5490 6893 1185 975 -190 N ATOM 4156 CA ALA B 246 42.378 36.682 44.900 1.00 48.86 C ANISOU 4156 CA ALA B 246 5313 6064 7188 1189 1062 -235 C ATOM 4157 C ALA B 246 43.785 36.757 45.474 1.00 51.27 C ANISOU 4157 C ALA B 246 5760 6439 7282 1185 1049 -399 C ATOM 4158 O ALA B 246 43.954 36.819 46.694 1.00 55.40 O ANISOU 4158 O ALA B 246 6326 7050 7672 1220 1165 -502 O ATOM 4159 CB ALA B 246 41.949 35.229 44.682 1.00 40.54 C ANISOU 4159 CB ALA B 246 4249 5058 6096 1127 986 -87 C ATOM 4160 N TYR B 247 44.801 36.762 44.602 1.00 48.40 N ANISOU 4160 N TYR B 247 5460 6053 6878 1143 908 -424 N ATOM 4161 CA TYR B 247 46.181 36.948 45.035 1.00 47.50 C ANISOU 4161 CA TYR B 247 5448 6014 6587 1133 884 -580 C ATOM 4162 C TYR B 247 46.364 38.287 45.752 1.00 50.16 C ANISOU 4162 C TYR B 247 5785 6325 6949 1156 1012 -764 C ATOM 4163 O TYR B 247 46.822 38.332 46.900 1.00 51.54 O ANISOU 4163 O TYR B 247 6012 6616 6956 1169 1083 -900 O ATOM 4164 CB TYR B 247 47.134 36.855 43.828 1.00 42.10 C ANISOU 4164 CB TYR B 247 4807 5294 5897 1085 728 -562 C ATOM 4165 CG TYR B 247 48.564 36.967 44.278 1.00 45.43 C ANISOU 4165 CG TYR B 247 5304 5817 6140 1071 699 -711 C ATOM 4166 CD1 TYR B 247 49.156 38.220 44.457 1.00 44.24 C ANISOU 4166 CD1 TYR B 247 5154 5633 6022 1050 750 -876 C ATOM 4167 CD2 TYR B 247 49.314 35.832 44.588 1.00 44.42 C ANISOU 4167 CD2 TYR B 247 5241 5822 5816 1080 630 -688 C ATOM 4168 CE1 TYR B 247 50.436 38.343 44.925 1.00 43.92 C ANISOU 4168 CE1 TYR B 247 5159 5710 5820 1021 718 -1023 C ATOM 4169 CE2 TYR B 247 50.615 35.949 45.041 1.00 40.78 C ANISOU 4169 CE2 TYR B 247 4821 5485 5189 1076 597 -815 C ATOM 4170 CZ TYR B 247 51.163 37.203 45.216 1.00 43.63 C ANISOU 4170 CZ TYR B 247 5163 5833 5581 1038 635 -988 C ATOM 4171 OH TYR B 247 52.431 37.345 45.689 1.00 47.21 O ANISOU 4171 OH TYR B 247 5634 6429 5873 1015 595 -1125 O ATOM 4172 N PHE B 248 45.986 39.396 45.098 1.00 48.08 N ANISOU 4172 N PHE B 248 5470 5907 6892 1164 1049 -770 N ATOM 4173 CA PHE B 248 46.258 40.716 45.677 1.00 49.48 C ANISOU 4173 CA PHE B 248 5669 6018 7114 1174 1178 -962 C ATOM 4174 C PHE B 248 45.410 41.007 46.906 1.00 56.10 C ANISOU 4174 C PHE B 248 6486 6881 7948 1237 1365 -1034 C ATOM 4175 O PHE B 248 45.725 41.944 47.645 1.00 53.64 O ANISOU 4175 O PHE B 248 6220 6546 7615 1237 1484 -1235 O ATOM 4176 CB PHE B 248 45.976 41.843 44.681 1.00 42.53 C ANISOU 4176 CB PHE B 248 4744 4936 6478 1186 1200 -924 C ATOM 4177 CG PHE B 248 46.878 41.840 43.489 1.00 48.14 C ANISOU 4177 CG PHE B 248 5485 5609 7197 1124 1050 -878 C ATOM 4178 CD1 PHE B 248 48.258 41.770 43.634 1.00 46.94 C ANISOU 4178 CD1 PHE B 248 5410 5540 6886 1051 985 -1014 C ATOM 4179 CD2 PHE B 248 46.341 41.923 42.199 1.00 47.62 C ANISOU 4179 CD2 PHE B 248 5360 5441 7293 1143 976 -691 C ATOM 4180 CE1 PHE B 248 49.111 41.767 42.496 1.00 45.40 C ANISOU 4180 CE1 PHE B 248 5237 5314 6701 998 863 -964 C ATOM 4181 CE2 PHE B 248 47.174 41.937 41.066 1.00 47.82 C ANISOU 4181 CE2 PHE B 248 5422 5438 7311 1091 850 -644 C ATOM 4182 CZ PHE B 248 48.559 41.856 41.210 1.00 46.01 C ANISOU 4182 CZ PHE B 248 5272 5278 6931 1019 803 -779 C ATOM 4183 N LYS B 249 44.389 40.196 47.182 1.00 53.61 N ANISOU 4183 N LYS B 249 6109 6622 7640 1281 1400 -889 N ATOM 4184 CA LYS B 249 43.635 40.376 48.414 1.00 50.94 C ANISOU 4184 CA LYS B 249 5753 6333 7268 1345 1591 -953 C ATOM 4185 C LYS B 249 44.487 40.047 49.627 1.00 51.34 C ANISOU 4185 C LYS B 249 5912 6565 7031 1327 1617 -1115 C ATOM 4186 O LYS B 249 44.349 40.692 50.672 1.00 57.11 O ANISOU 4186 O LYS B 249 6674 7327 7697 1361 1778 -1280 O ATOM 4187 CB LYS B 249 42.375 39.521 48.375 1.00 48.16 C ANISOU 4187 CB LYS B 249 5295 6007 6997 1381 1622 -742 C ATOM 4188 CG LYS B 249 41.443 39.725 49.504 1.00 56.46 C ANISOU 4188 CG LYS B 249 6303 7098 8051 1456 1836 -773 C ATOM 4189 CD LYS B 249 40.065 39.323 49.064 1.00 69.20 C ANISOU 4189 CD LYS B 249 7757 8673 9864 1488 1868 -555 C ATOM 4190 CE LYS B 249 39.191 39.000 50.237 1.00 77.67 C ANISOU 4190 CE LYS B 249 8786 9841 10885 1544 2064 -534 C ATOM 4191 NZ LYS B 249 39.353 37.574 50.614 1.00 80.88 N ANISOU 4191 NZ LYS B 249 9237 10389 11104 1487 2003 -432 N ATOM 4192 N VAL B 250 45.362 39.047 49.501 1.00 57.31 N ANISOU 4192 N VAL B 250 6724 7447 7605 1281 1464 -1070 N ATOM 4193 CA VAL B 250 46.302 38.644 50.548 1.00 54.48 C ANISOU 4193 CA VAL B 250 6455 7291 6952 1273 1451 -1194 C ATOM 4194 C VAL B 250 47.616 39.432 50.456 1.00 56.31 C ANISOU 4194 C VAL B 250 6741 7543 7113 1207 1376 -1400 C ATOM 4195 O VAL B 250 48.190 39.809 51.477 1.00 63.13 O ANISOU 4195 O VAL B 250 7657 8539 7790 1195 1426 -1596 O ATOM 4196 CB VAL B 250 46.542 37.113 50.443 1.00 55.91 C ANISOU 4196 CB VAL B 250 6662 7590 6992 1278 1335 -1011 C ATOM 4197 CG1 VAL B 250 47.582 36.588 51.471 1.00 47.15 C ANISOU 4197 CG1 VAL B 250 5637 6714 5565 1293 1301 -1097 C ATOM 4198 CG2 VAL B 250 45.233 36.353 50.574 1.00 51.23 C ANISOU 4198 CG2 VAL B 250 6012 6970 6484 1316 1421 -818 C ATOM 4199 N MET B 251 48.121 39.687 49.245 1.00 50.83 N ANISOU 4199 N MET B 251 6029 6729 6555 1156 1257 -1365 N ATOM 4200 CA MET B 251 49.403 40.373 49.033 1.00 51.61 C ANISOU 4200 CA MET B 251 6162 6841 6608 1077 1184 -1538 C ATOM 4201 C MET B 251 49.138 41.555 48.109 1.00 54.37 C ANISOU 4201 C MET B 251 6481 6945 7231 1048 1229 -1561 C ATOM 4202 O MET B 251 49.277 41.433 46.879 1.00 52.00 O ANISOU 4202 O MET B 251 6155 6547 7055 1030 1125 -1427 O ATOM 4203 CB MET B 251 50.459 39.437 48.423 1.00 45.89 C ANISOU 4203 CB MET B 251 5450 6224 5761 1049 999 -1451 C ATOM 4204 CG MET B 251 50.934 38.297 49.329 1.00 55.92 C ANISOU 4204 CG MET B 251 6756 7738 6752 1091 950 -1422 C ATOM 4205 SD MET B 251 52.144 38.754 50.611 1.00 66.44 S ANISOU 4205 SD MET B 251 8118 9319 7806 1051 944 -1685 S ATOM 4206 CE MET B 251 53.557 39.313 49.649 1.00 50.33 C ANISOU 4206 CE MET B 251 6046 7254 5821 947 808 -1783 C ATOM 4207 N PRO B 252 48.880 42.740 48.669 1.00 48.72 N ANISOU 4207 N PRO B 252 5780 6130 6599 1043 1384 -1741 N ATOM 4208 CA PRO B 252 48.415 43.867 47.851 1.00 48.15 C ANISOU 4208 CA PRO B 252 5682 5797 6815 1048 1464 -1727 C ATOM 4209 C PRO B 252 49.429 44.352 46.825 1.00 52.63 C ANISOU 4209 C PRO B 252 6262 6273 7463 959 1362 -1746 C ATOM 4210 O PRO B 252 50.645 44.281 47.013 1.00 56.54 O ANISOU 4210 O PRO B 252 6790 6889 7805 868 1278 -1878 O ATOM 4211 CB PRO B 252 48.104 44.954 48.891 1.00 51.77 C ANISOU 4211 CB PRO B 252 6182 6185 7304 1057 1669 -1958 C ATOM 4212 CG PRO B 252 47.780 44.174 50.137 1.00 53.25 C ANISOU 4212 CG PRO B 252 6387 6591 7256 1103 1715 -1993 C ATOM 4213 CD PRO B 252 48.719 43.000 50.111 1.00 46.93 C ANISOU 4213 CD PRO B 252 5597 6017 6216 1060 1521 -1930 C ATOM 4214 N LYS B 253 48.889 44.817 45.706 1.00 55.68 N ANISOU 4214 N LYS B 253 6608 6457 8090 993 1370 -1592 N ATOM 4215 CA LYS B 253 49.687 45.240 44.564 1.00 53.44 C ANISOU 4215 CA LYS B 253 6332 6071 7902 925 1286 -1553 C ATOM 4216 C LYS B 253 50.487 46.515 44.869 1.00 50.98 C ANISOU 4216 C LYS B 253 6074 5643 7654 829 1388 -1794 C ATOM 4217 O LYS B 253 49.933 47.552 45.261 1.00 55.61 O ANISOU 4217 O LYS B 253 6681 6052 8397 856 1564 -1895 O ATOM 4218 CB LYS B 253 48.738 45.420 43.372 1.00 50.35 C ANISOU 4218 CB LYS B 253 5883 5512 7737 1005 1280 -1309 C ATOM 4219 CG LYS B 253 49.357 45.888 42.097 1.00 57.11 C ANISOU 4219 CG LYS B 253 6747 6249 8702 959 1212 -1224 C ATOM 4220 CD LYS B 253 48.340 45.845 40.947 1.00 65.67 C ANISOU 4220 CD LYS B 253 7766 7232 9955 1051 1173 -955 C ATOM 4221 CE LYS B 253 47.294 46.926 41.073 1.00 76.25 C ANISOU 4221 CE LYS B 253 9067 8370 11533 1150 1347 -925 C ATOM 4222 NZ LYS B 253 46.466 47.007 39.844 1.00 82.31 N ANISOU 4222 NZ LYS B 253 9758 9055 12461 1238 1291 -654 N ATOM 4223 N GLN B 254 51.790 46.445 44.625 1.00 51.19 N ANISOU 4223 N GLN B 254 6117 5755 7577 715 1285 -1879 N ATOM 4224 CA GLN B 254 52.742 47.493 44.981 1.00 56.02 C ANISOU 4224 CA GLN B 254 6768 6303 8215 583 1356 -2131 C ATOM 4225 C GLN B 254 52.997 48.417 43.801 1.00 53.60 C ANISOU 4225 C GLN B 254 6466 5751 8149 539 1394 -2056 C ATOM 4226 O GLN B 254 52.863 48.019 42.641 1.00 59.65 O ANISOU 4226 O GLN B 254 7203 6483 8978 588 1304 -1818 O ATOM 4227 CB GLN B 254 54.063 46.867 45.423 1.00 58.53 C ANISOU 4227 CB GLN B 254 7074 6887 8278 479 1218 -2260 C ATOM 4228 CG GLN B 254 53.968 46.026 46.678 1.00 67.65 C ANISOU 4228 CG GLN B 254 8234 8302 9170 519 1186 -2342 C ATOM 4229 CD GLN B 254 55.217 45.153 46.876 1.00 78.78 C ANISOU 4229 CD GLN B 254 9609 9998 10327 463 1015 -2375 C ATOM 4230 OE1 GLN B 254 55.309 44.040 46.313 1.00 70.86 O ANISOU 4230 OE1 GLN B 254 8580 9097 9246 531 890 -2170 O ATOM 4231 NE2 GLN B 254 56.182 45.652 47.665 1.00 79.44 N ANISOU 4231 NE2 GLN B 254 9687 10211 10286 339 1011 -2636 N ATOM 4232 N ALA B 255 53.358 49.659 44.114 1.00 51.35 N ANISOU 4232 N ALA B 255 6227 5290 7992 443 1536 -2265 N ATOM 4233 CA ALA B 255 53.676 50.640 43.084 1.00 53.96 C ANISOU 4233 CA ALA B 255 6574 5366 8560 389 1602 -2205 C ATOM 4234 C ALA B 255 54.718 50.098 42.111 1.00 59.63 C ANISOU 4234 C ALA B 255 7253 6201 9203 315 1440 -2089 C ATOM 4235 O ALA B 255 55.705 49.475 42.513 1.00 59.30 O ANISOU 4235 O ALA B 255 7181 6399 8950 225 1322 -2203 O ATOM 4236 CB ALA B 255 54.206 51.911 43.734 1.00 53.32 C ANISOU 4236 CB ALA B 255 6556 5119 8584 247 1766 -2504 C ATOM 4237 N GLY B 256 54.477 50.312 40.819 1.00 60.58 N ANISOU 4237 N GLY B 256 7369 6163 9487 369 1436 -1849 N ATOM 4238 CA GLY B 256 55.367 49.780 39.808 1.00 56.98 C ANISOU 4238 CA GLY B 256 6881 5811 8957 319 1300 -1718 C ATOM 4239 C GLY B 256 55.134 48.330 39.443 1.00 58.92 C ANISOU 4239 C GLY B 256 7090 6281 9014 415 1121 -1536 C ATOM 4240 O GLY B 256 55.960 47.746 38.723 1.00 58.09 O ANISOU 4240 O GLY B 256 6965 6295 8810 378 1007 -1457 O ATOM 4241 N TYR B 257 54.036 47.725 39.907 1.00 54.07 N ANISOU 4241 N TYR B 257 6469 5722 8355 535 1106 -1469 N ATOM 4242 CA TYR B 257 53.807 46.310 39.628 1.00 53.81 C ANISOU 4242 CA TYR B 257 6411 5885 8151 607 948 -1313 C ATOM 4243 C TYR B 257 53.712 46.050 38.126 1.00 55.74 C ANISOU 4243 C TYR B 257 6650 6078 8451 646 863 -1068 C ATOM 4244 O TYR B 257 54.337 45.118 37.604 1.00 57.22 O ANISOU 4244 O TYR B 257 6837 6414 8488 632 734 -1002 O ATOM 4245 CB TYR B 257 52.543 45.812 40.334 1.00 55.39 C ANISOU 4245 CB TYR B 257 6595 6120 8331 716 971 -1270 C ATOM 4246 CG TYR B 257 52.041 44.531 39.696 1.00 55.43 C ANISOU 4246 CG TYR B 257 6577 6240 8244 788 829 -1058 C ATOM 4247 CD1 TYR B 257 52.645 43.300 39.984 1.00 49.76 C ANISOU 4247 CD1 TYR B 257 5869 5736 7302 773 710 -1073 C ATOM 4248 CD2 TYR B 257 51.009 44.559 38.757 1.00 54.72 C ANISOU 4248 CD2 TYR B 257 6456 6043 8291 867 811 -842 C ATOM 4249 CE1 TYR B 257 52.200 42.127 39.377 1.00 54.33 C ANISOU 4249 CE1 TYR B 257 6443 6389 7810 825 594 -895 C ATOM 4250 CE2 TYR B 257 50.563 43.406 38.140 1.00 53.41 C ANISOU 4250 CE2 TYR B 257 6272 5981 8042 906 677 -672 C ATOM 4251 CZ TYR B 257 51.154 42.196 38.445 1.00 59.03 C ANISOU 4251 CZ TYR B 257 7012 6874 8545 878 576 -707 C ATOM 4252 OH TYR B 257 50.681 41.066 37.819 1.00 60.54 O ANISOU 4252 OH TYR B 257 7199 7134 8669 906 458 -552 O ATOM 4253 N GLU B 258 52.911 46.852 37.421 1.00 55.73 N ANISOU 4253 N GLU B 258 6648 5873 8655 707 938 -927 N ATOM 4254 CA GLU B 258 52.749 46.688 35.977 1.00 59.68 C ANISOU 4254 CA GLU B 258 7145 6338 9194 749 858 -687 C ATOM 4255 C GLU B 258 54.046 46.966 35.235 1.00 58.28 C ANISOU 4255 C GLU B 258 6996 6157 8991 651 844 -700 C ATOM 4256 O GLU B 258 54.368 46.292 34.252 1.00 58.24 O ANISOU 4256 O GLU B 258 6998 6243 8885 659 732 -563 O ATOM 4257 CB GLU B 258 51.648 47.619 35.462 1.00 64.77 C ANISOU 4257 CB GLU B 258 7772 6773 10067 847 952 -528 C ATOM 4258 CG GLU B 258 50.258 47.071 35.660 1.00 80.57 C ANISOU 4258 CG GLU B 258 9711 8819 12082 964 914 -411 C ATOM 4259 CD GLU B 258 50.004 45.824 34.835 1.00 98.27 C ANISOU 4259 CD GLU B 258 11931 11231 14176 985 726 -244 C ATOM 4260 OE1 GLU B 258 50.745 45.582 33.843 1.00 99.74 O ANISOU 4260 OE1 GLU B 258 12154 11459 14283 942 639 -169 O ATOM 4261 OE2 GLU B 258 49.060 45.082 35.191 1.00106.67 O ANISOU 4261 OE2 GLU B 258 12942 12383 15205 1038 675 -195 O ATOM 4262 N LYS B 259 54.794 47.967 35.689 1.00 59.67 N ANISOU 4262 N LYS B 259 7187 6225 9259 551 966 -871 N ATOM 4263 CA LYS B 259 56.032 48.370 35.034 1.00 58.43 C ANISOU 4263 CA LYS B 259 7040 6050 9110 441 981 -889 C ATOM 4264 C LYS B 259 57.097 47.280 35.095 1.00 59.37 C ANISOU 4264 C LYS B 259 7134 6426 8999 385 848 -954 C ATOM 4265 O LYS B 259 57.950 47.201 34.201 1.00 61.18 O ANISOU 4265 O LYS B 259 7361 6691 9194 339 819 -881 O ATOM 4266 CB LYS B 259 56.512 49.662 35.690 1.00 63.83 C ANISOU 4266 CB LYS B 259 7738 6558 9955 325 1148 -1093 C ATOM 4267 CG LYS B 259 57.886 50.089 35.359 1.00 77.97 C ANISOU 4267 CG LYS B 259 9518 8352 11754 170 1178 -1178 C ATOM 4268 CD LYS B 259 58.281 51.258 36.245 1.00 88.90 C ANISOU 4268 CD LYS B 259 10915 9579 13282 31 1335 -1432 C ATOM 4269 CE LYS B 259 57.481 52.502 35.919 1.00 89.08 C ANISOU 4269 CE LYS B 259 11003 9260 13584 78 1517 -1349 C ATOM 4270 NZ LYS B 259 57.898 53.614 36.807 1.00 97.11 N ANISOU 4270 NZ LYS B 259 12050 10105 14743 -73 1682 -1628 N ATOM 4271 N ARG B 260 57.073 46.440 36.137 1.00 54.88 N ANISOU 4271 N ARG B 260 6544 6038 8269 399 780 -1079 N ATOM 4272 CA ARG B 260 58.089 45.412 36.356 1.00 47.65 C ANISOU 4272 CA ARG B 260 5598 5368 7137 367 666 -1143 C ATOM 4273 C ARG B 260 57.724 44.044 35.785 1.00 51.42 C ANISOU 4273 C ARG B 260 6096 5972 7469 473 534 -972 C ATOM 4274 O ARG B 260 58.576 43.147 35.806 1.00 51.26 O ANISOU 4274 O ARG B 260 6061 6135 7282 470 450 -994 O ATOM 4275 CB ARG B 260 58.366 45.228 37.854 1.00 42.53 C ANISOU 4275 CB ARG B 260 4921 4865 6373 328 666 -1367 C ATOM 4276 CG ARG B 260 59.100 46.383 38.526 1.00 45.12 C ANISOU 4276 CG ARG B 260 5223 5138 6783 182 768 -1600 C ATOM 4277 CD ARG B 260 59.449 46.043 39.963 1.00 52.37 C ANISOU 4277 CD ARG B 260 6108 6262 7527 147 735 -1817 C ATOM 4278 NE ARG B 260 58.284 45.856 40.836 1.00 55.87 N ANISOU 4278 NE ARG B 260 6593 6690 7946 239 770 -1838 N ATOM 4279 CZ ARG B 260 57.655 46.846 41.481 1.00 60.43 C ANISOU 4279 CZ ARG B 260 7205 7105 8651 213 906 -1971 C ATOM 4280 NH1 ARG B 260 58.048 48.105 41.338 1.00 53.47 N ANISOU 4280 NH1 ARG B 260 6334 6036 7944 93 1022 -2095 N ATOM 4281 NH2 ARG B 260 56.608 46.585 42.255 1.00 59.31 N ANISOU 4281 NH2 ARG B 260 7091 6971 8474 309 944 -1977 N ATOM 4282 N ARG B 261 56.506 43.850 35.266 1.00 45.34 N ANISOU 4282 N ARG B 261 5355 5113 6760 565 514 -806 N ATOM 4283 CA ARG B 261 56.109 42.502 34.863 1.00 52.18 C ANISOU 4283 CA ARG B 261 6243 6096 7485 641 390 -681 C ATOM 4284 C ARG B 261 57.092 41.911 33.860 1.00 55.16 C ANISOU 4284 C ARG B 261 6644 6563 7751 626 320 -614 C ATOM 4285 O ARG B 261 57.474 40.734 33.970 1.00 47.58 O ANISOU 4285 O ARG B 261 5700 5751 6626 658 238 -618 O ATOM 4286 CB ARG B 261 54.699 42.514 34.289 1.00 44.87 C ANISOU 4286 CB ARG B 261 5325 5066 6658 716 373 -511 C ATOM 4287 CG ARG B 261 53.661 42.576 35.369 1.00 55.62 C ANISOU 4287 CG ARG B 261 6656 6401 8075 758 422 -562 C ATOM 4288 CD ARG B 261 52.296 42.853 34.808 1.00 62.79 C ANISOU 4288 CD ARG B 261 7537 7199 9122 829 425 -394 C ATOM 4289 NE ARG B 261 51.651 41.649 34.313 1.00 75.59 N ANISOU 4289 NE ARG B 261 9158 8916 10647 865 298 -266 N ATOM 4290 CZ ARG B 261 50.544 41.654 33.582 1.00 83.18 C ANISOU 4290 CZ ARG B 261 10081 9833 11691 914 251 -98 C ATOM 4291 NH1 ARG B 261 49.977 42.814 33.264 1.00 85.11 N ANISOU 4291 NH1 ARG B 261 10282 9938 12116 958 328 -17 N ATOM 4292 NH2 ARG B 261 50.004 40.505 33.178 1.00 83.56 N ANISOU 4292 NH2 ARG B 261 10130 9976 11644 917 131 -11 N ATOM 4293 N ASP B 262 57.514 42.721 32.877 1.00 51.86 N ANISOU 4293 N ASP B 262 6233 6049 7424 587 366 -546 N ATOM 4294 CA ASP B 262 58.449 42.260 31.857 1.00 52.50 C ANISOU 4294 CA ASP B 262 6336 6210 7402 576 324 -478 C ATOM 4295 C ASP B 262 59.823 41.940 32.443 1.00 53.93 C ANISOU 4295 C ASP B 262 6469 6546 7477 523 325 -626 C ATOM 4296 O ASP B 262 60.529 41.062 31.932 1.00 51.94 O ANISOU 4296 O ASP B 262 6230 6418 7087 553 270 -589 O ATOM 4297 CB ASP B 262 58.565 43.313 30.755 1.00 57.08 C ANISOU 4297 CB ASP B 262 6931 6649 8110 545 397 -362 C ATOM 4298 CG ASP B 262 57.384 43.285 29.798 1.00 68.41 C ANISOU 4298 CG ASP B 262 8411 8003 9580 623 351 -161 C ATOM 4299 OD1 ASP B 262 56.532 42.383 29.925 1.00 77.51 O ANISOU 4299 OD1 ASP B 262 9578 9217 10657 684 254 -123 O ATOM 4300 OD2 ASP B 262 57.305 44.157 28.913 1.00 75.08 O ANISOU 4300 OD2 ASP B 262 9271 8730 10525 622 409 -33 O ATOM 4301 N LEU B 263 60.224 42.651 33.494 1.00 51.55 N ANISOU 4301 N LEU B 263 6107 6246 7234 447 389 -796 N ATOM 4302 CA LEU B 263 61.520 42.404 34.103 1.00 51.64 C ANISOU 4302 CA LEU B 263 6045 6435 7141 391 376 -939 C ATOM 4303 C LEU B 263 61.596 41.004 34.676 1.00 48.50 C ANISOU 4303 C LEU B 263 5652 6227 6549 484 275 -946 C ATOM 4304 O LEU B 263 62.649 40.363 34.615 1.00 51.96 O ANISOU 4304 O LEU B 263 6047 6830 6866 498 236 -964 O ATOM 4305 CB LEU B 263 61.789 43.452 35.182 1.00 56.88 C ANISOU 4305 CB LEU B 263 6649 7069 7895 278 453 -1140 C ATOM 4306 CG LEU B 263 63.237 43.552 35.653 1.00 59.54 C ANISOU 4306 CG LEU B 263 6879 7581 8162 176 447 -1295 C ATOM 4307 CD1 LEU B 263 64.106 44.180 34.542 1.00 51.64 C ANISOU 4307 CD1 LEU B 263 5846 6516 7259 90 513 -1235 C ATOM 4308 CD2 LEU B 263 63.317 44.354 36.940 1.00 62.24 C ANISOU 4308 CD2 LEU B 263 7174 7930 8543 69 494 -1525 C ATOM 4309 N TYR B 264 60.490 40.497 35.201 1.00 50.95 N ANISOU 4309 N TYR B 264 6011 6513 6836 556 242 -917 N ATOM 4310 CA TYR B 264 60.467 39.147 35.745 1.00 50.65 C ANISOU 4310 CA TYR B 264 5993 6625 6628 648 164 -902 C ATOM 4311 C TYR B 264 60.195 38.069 34.686 1.00 46.30 C ANISOU 4311 C TYR B 264 5522 6059 6010 729 102 -742 C ATOM 4312 O TYR B 264 60.632 36.928 34.861 1.00 48.45 O ANISOU 4312 O TYR B 264 5814 6453 6141 800 53 -725 O ATOM 4313 CB TYR B 264 59.439 39.084 36.888 1.00 46.05 C ANISOU 4313 CB TYR B 264 5422 6029 6048 676 175 -951 C ATOM 4314 CG TYR B 264 59.881 39.975 38.021 1.00 50.77 C ANISOU 4314 CG TYR B 264 5952 6681 6659 598 230 -1142 C ATOM 4315 CD1 TYR B 264 61.183 39.901 38.502 1.00 50.10 C ANISOU 4315 CD1 TYR B 264 5792 6783 6462 558 203 -1256 C ATOM 4316 CD2 TYR B 264 59.020 40.905 38.601 1.00 50.31 C ANISOU 4316 CD2 TYR B 264 5899 6494 6722 562 312 -1216 C ATOM 4317 CE1 TYR B 264 61.627 40.718 39.522 1.00 47.77 C ANISOU 4317 CE1 TYR B 264 5431 6558 6163 464 240 -1453 C ATOM 4318 CE2 TYR B 264 59.455 41.730 39.639 1.00 50.32 C ANISOU 4318 CE2 TYR B 264 5854 6541 6724 477 368 -1421 C ATOM 4319 CZ TYR B 264 60.766 41.628 40.087 1.00 50.30 C ANISOU 4319 CZ TYR B 264 5779 6737 6596 417 324 -1545 C ATOM 4320 OH TYR B 264 61.224 42.425 41.107 1.00 54.72 O ANISOU 4320 OH TYR B 264 6288 7365 7138 313 365 -1767 O ATOM 4321 N LEU B 265 59.477 38.388 33.604 1.00 39.29 N ANISOU 4321 N LEU B 265 4685 5028 5215 722 105 -625 N ATOM 4322 CA LEU B 265 59.432 37.496 32.444 1.00 48.19 C ANISOU 4322 CA LEU B 265 5890 6156 6262 772 48 -501 C ATOM 4323 C LEU B 265 60.812 37.336 31.820 1.00 50.67 C ANISOU 4323 C LEU B 265 6191 6563 6497 770 63 -510 C ATOM 4324 O LEU B 265 61.155 36.252 31.334 1.00 46.58 O ANISOU 4324 O LEU B 265 5732 6110 5857 836 25 -465 O ATOM 4325 CB LEU B 265 58.447 38.026 31.391 1.00 44.11 C ANISOU 4325 CB LEU B 265 5415 5498 5847 758 40 -375 C ATOM 4326 CG LEU B 265 56.958 37.993 31.764 1.00 43.44 C ANISOU 4326 CG LEU B 265 5334 5334 5838 777 13 -327 C ATOM 4327 CD1 LEU B 265 56.147 38.869 30.818 1.00 43.15 C ANISOU 4327 CD1 LEU B 265 5295 5173 5925 767 18 -204 C ATOM 4328 CD2 LEU B 265 56.446 36.569 31.700 1.00 47.05 C ANISOU 4328 CD2 LEU B 265 5855 5841 6183 822 -70 -283 C ATOM 4329 N LEU B 266 61.617 38.414 31.829 1.00 46.30 N ANISOU 4329 N LEU B 266 5559 6011 6022 692 131 -572 N ATOM 4330 CA LEU B 266 62.879 38.430 31.099 1.00 46.16 C ANISOU 4330 CA LEU B 266 5509 6071 5958 677 164 -563 C ATOM 4331 C LEU B 266 63.820 37.329 31.581 1.00 49.86 C ANISOU 4331 C LEU B 266 5944 6726 6275 751 130 -613 C ATOM 4332 O LEU B 266 64.522 36.706 30.775 1.00 48.26 O ANISOU 4332 O LEU B 266 5766 6586 5986 804 136 -557 O ATOM 4333 CB LEU B 266 63.544 39.799 31.230 1.00 47.06 C ANISOU 4333 CB LEU B 266 5528 6150 6203 557 252 -638 C ATOM 4334 CG LEU B 266 64.979 39.931 30.681 1.00 49.77 C ANISOU 4334 CG LEU B 266 5795 6598 6516 517 304 -649 C ATOM 4335 CD1 LEU B 266 65.044 39.657 29.186 1.00 39.34 C ANISOU 4335 CD1 LEU B 266 4559 5237 5152 562 324 -495 C ATOM 4336 CD2 LEU B 266 65.574 41.314 31.003 1.00 43.30 C ANISOU 4336 CD2 LEU B 266 4872 5731 5849 366 395 -749 C ATOM 4337 N TYR B 267 63.849 37.073 32.888 1.00 51.00 N ANISOU 4337 N TYR B 267 6034 6965 6378 767 101 -709 N ATOM 4338 CA TYR B 267 64.685 35.989 33.407 1.00 50.09 C ANISOU 4338 CA TYR B 267 5884 7034 6115 863 65 -729 C ATOM 4339 C TYR B 267 64.334 34.646 32.759 1.00 45.94 C ANISOU 4339 C TYR B 267 5488 6476 5492 984 34 -618 C ATOM 4340 O TYR B 267 65.223 33.898 32.348 1.00 48.21 O ANISOU 4340 O TYR B 267 5775 6856 5688 1066 43 -587 O ATOM 4341 CB TYR B 267 64.539 35.910 34.921 1.00 44.74 C ANISOU 4341 CB TYR B 267 5149 6459 5391 872 33 -826 C ATOM 4342 CG TYR B 267 65.245 34.744 35.561 1.00 46.83 C ANISOU 4342 CG TYR B 267 5385 6913 5497 997 -8 -817 C ATOM 4343 CD1 TYR B 267 66.635 34.663 35.569 1.00 50.99 C ANISOU 4343 CD1 TYR B 267 5787 7626 5960 1019 -6 -848 C ATOM 4344 CD2 TYR B 267 64.523 33.737 36.187 1.00 45.66 C ANISOU 4344 CD2 TYR B 267 5320 6759 5267 1098 -41 -765 C ATOM 4345 CE1 TYR B 267 67.289 33.587 36.178 1.00 51.72 C ANISOU 4345 CE1 TYR B 267 5842 7901 5907 1160 -43 -817 C ATOM 4346 CE2 TYR B 267 65.161 32.665 36.799 1.00 50.71 C ANISOU 4346 CE2 TYR B 267 5941 7561 5766 1231 -67 -732 C ATOM 4347 CZ TYR B 267 66.539 32.597 36.791 1.00 48.57 C ANISOU 4347 CZ TYR B 267 5546 7478 5429 1271 -71 -754 C ATOM 4348 OH TYR B 267 67.156 31.539 37.411 1.00 45.49 O ANISOU 4348 OH TYR B 267 5128 7254 4902 1427 -95 -701 O ATOM 4349 N HIS B 268 63.037 34.328 32.650 1.00 40.67 N ANISOU 4349 N HIS B 268 4929 5674 4851 993 2 -561 N ATOM 4350 CA HIS B 268 62.630 33.058 32.061 1.00 44.00 C ANISOU 4350 CA HIS B 268 5481 6047 5189 1079 -27 -478 C ATOM 4351 C HIS B 268 62.748 33.051 30.540 1.00 47.74 C ANISOU 4351 C HIS B 268 6031 6454 5652 1068 -15 -411 C ATOM 4352 O HIS B 268 63.028 31.992 29.972 1.00 51.15 O ANISOU 4352 O HIS B 268 6556 6894 5986 1147 -15 -377 O ATOM 4353 CB HIS B 268 61.208 32.703 32.485 1.00 44.53 C ANISOU 4353 CB HIS B 268 5618 6010 5292 1072 -67 -447 C ATOM 4354 CG HIS B 268 61.087 32.444 33.950 1.00 49.35 C ANISOU 4354 CG HIS B 268 6181 6697 5873 1107 -69 -496 C ATOM 4355 ND1 HIS B 268 61.585 31.301 34.549 1.00 46.14 N ANISOU 4355 ND1 HIS B 268 5800 6382 5350 1216 -72 -481 N ATOM 4356 CD2 HIS B 268 60.575 33.205 34.950 1.00 43.93 C ANISOU 4356 CD2 HIS B 268 5427 6017 5248 1057 -58 -556 C ATOM 4357 CE1 HIS B 268 61.360 31.361 35.851 1.00 49.09 C ANISOU 4357 CE1 HIS B 268 6122 6829 5702 1229 -72 -520 C ATOM 4358 NE2 HIS B 268 60.745 32.503 36.119 1.00 45.31 N ANISOU 4358 NE2 HIS B 268 5589 6302 5326 1130 -62 -576 N ATOM 4359 N TYR B 269 62.555 34.196 29.862 1.00 40.56 N ANISOU 4359 N TYR B 269 5097 5478 4837 979 7 -388 N ATOM 4360 CA TYR B 269 62.860 34.247 28.427 1.00 45.25 C ANISOU 4360 CA TYR B 269 5756 6046 5393 976 30 -318 C ATOM 4361 C TYR B 269 64.346 34.024 28.158 1.00 44.44 C ANISOU 4361 C TYR B 269 5601 6067 5215 1022 95 -342 C ATOM 4362 O TYR B 269 64.707 33.356 27.187 1.00 48.94 O ANISOU 4362 O TYR B 269 6259 6649 5687 1079 116 -299 O ATOM 4363 CB TYR B 269 62.429 35.577 27.808 1.00 47.73 C ANISOU 4363 CB TYR B 269 6046 6267 5823 884 54 -265 C ATOM 4364 CG TYR B 269 60.950 35.689 27.589 1.00 55.80 C ANISOU 4364 CG TYR B 269 7129 7175 6899 863 -11 -198 C ATOM 4365 CD1 TYR B 269 60.187 34.567 27.365 1.00 61.95 C ANISOU 4365 CD1 TYR B 269 8008 7936 7592 903 -87 -172 C ATOM 4366 CD2 TYR B 269 60.321 36.931 27.567 1.00 60.74 C ANISOU 4366 CD2 TYR B 269 7705 7704 7668 803 10 -156 C ATOM 4367 CE1 TYR B 269 58.824 34.668 27.157 1.00 72.83 C ANISOU 4367 CE1 TYR B 269 9415 9234 9025 873 -155 -109 C ATOM 4368 CE2 TYR B 269 58.967 37.045 27.353 1.00 53.40 C ANISOU 4368 CE2 TYR B 269 6807 6690 6794 799 -51 -79 C ATOM 4369 CZ TYR B 269 58.224 35.908 27.160 1.00 66.60 C ANISOU 4369 CZ TYR B 269 8556 8374 8374 829 -140 -57 C ATOM 4370 OH TYR B 269 56.879 36.003 26.947 1.00 66.00 O ANISOU 4370 OH TYR B 269 8484 8237 8355 815 -208 20 O ATOM 4371 N LEU B 270 65.223 34.599 28.985 1.00 46.53 N ANISOU 4371 N LEU B 270 5719 6434 5525 993 131 -415 N ATOM 4372 CA LEU B 270 66.648 34.298 28.852 1.00 48.44 C ANISOU 4372 CA LEU B 270 5878 6826 5701 1046 186 -435 C ATOM 4373 C LEU B 270 66.909 32.823 29.110 1.00 50.41 C ANISOU 4373 C LEU B 270 6187 7144 5821 1197 165 -426 C ATOM 4374 O LEU B 270 67.680 32.181 28.390 1.00 52.01 O ANISOU 4374 O LEU B 270 6419 7399 5942 1284 217 -394 O ATOM 4375 CB LEU B 270 67.493 35.164 29.795 1.00 47.81 C ANISOU 4375 CB LEU B 270 5608 6867 5691 970 208 -530 C ATOM 4376 CG LEU B 270 67.625 36.650 29.424 1.00 51.83 C ANISOU 4376 CG LEU B 270 6046 7306 6341 817 270 -545 C ATOM 4377 CD1 LEU B 270 68.379 37.441 30.474 1.00 50.10 C ANISOU 4377 CD1 LEU B 270 5647 7197 6190 718 283 -673 C ATOM 4378 CD2 LEU B 270 68.285 36.835 28.061 1.00 54.22 C ANISOU 4378 CD2 LEU B 270 6366 7602 6632 811 355 -459 C ATOM 4379 N ASN B 271 66.269 32.262 30.128 1.00 50.37 N ANISOU 4379 N ASN B 271 6207 7130 5801 1237 105 -448 N ATOM 4380 CA ASN B 271 66.495 30.856 30.405 1.00 43.76 C ANISOU 4380 CA ASN B 271 5439 6333 4856 1387 101 -423 C ATOM 4381 C ASN B 271 66.046 29.986 29.236 1.00 47.18 C ANISOU 4381 C ASN B 271 6060 6636 5231 1434 116 -367 C ATOM 4382 O ASN B 271 66.690 28.981 28.915 1.00 52.73 O ANISOU 4382 O ASN B 271 6822 7367 5847 1560 163 -347 O ATOM 4383 CB ASN B 271 65.784 30.442 31.684 1.00 48.66 C ANISOU 4383 CB ASN B 271 6067 6951 5472 1413 46 -437 C ATOM 4384 CG ASN B 271 66.325 29.161 32.224 1.00 51.61 C ANISOU 4384 CG ASN B 271 6463 7402 5743 1579 58 -403 C ATOM 4385 OD1 ASN B 271 67.538 29.008 32.311 1.00 55.12 O ANISOU 4385 OD1 ASN B 271 6804 8003 6138 1664 91 -404 O ATOM 4386 ND2 ASN B 271 65.452 28.198 32.509 1.00 49.57 N ANISOU 4386 ND2 ASN B 271 6342 7032 5462 1632 42 -360 N ATOM 4387 N HIS B 272 64.931 30.338 28.599 1.00 49.68 N ANISOU 4387 N HIS B 272 6472 6813 5590 1338 77 -346 N ATOM 4388 CA HIS B 272 64.433 29.518 27.496 1.00 45.48 C ANISOU 4388 CA HIS B 272 6120 6174 4986 1360 73 -313 C ATOM 4389 C HIS B 272 65.334 29.643 26.281 1.00 50.74 C ANISOU 4389 C HIS B 272 6810 6886 5585 1384 146 -297 C ATOM 4390 O HIS B 272 65.604 28.653 25.598 1.00 51.56 O ANISOU 4390 O HIS B 272 7041 6964 5586 1468 186 -298 O ATOM 4391 CB HIS B 272 62.993 29.900 27.160 1.00 47.94 C ANISOU 4391 CB HIS B 272 6498 6363 5353 1248 -4 -287 C ATOM 4392 CG HIS B 272 61.978 29.157 27.970 1.00 49.79 C ANISOU 4392 CG HIS B 272 6786 6520 5610 1250 -60 -292 C ATOM 4393 ND1 HIS B 272 61.884 29.280 29.340 1.00 49.26 N ANISOU 4393 ND1 HIS B 272 6623 6495 5598 1265 -65 -312 N ATOM 4394 CD2 HIS B 272 61.043 28.247 27.610 1.00 50.64 C ANISOU 4394 CD2 HIS B 272 7032 6520 5689 1232 -103 -283 C ATOM 4395 CE1 HIS B 272 60.918 28.499 29.787 1.00 48.74 C ANISOU 4395 CE1 HIS B 272 6634 6344 5541 1263 -100 -298 C ATOM 4396 NE2 HIS B 272 60.387 27.865 28.756 1.00 56.18 N ANISOU 4396 NE2 HIS B 272 7713 7188 6443 1234 -125 -283 N ATOM 4397 N TYR B 273 65.816 30.856 26.015 1.00 46.63 N ANISOU 4397 N TYR B 273 6171 6424 5123 1311 179 -284 N ATOM 4398 CA TYR B 273 66.869 31.071 25.032 1.00 43.93 C ANISOU 4398 CA TYR B 273 5811 6154 4726 1336 274 -262 C ATOM 4399 C TYR B 273 68.072 30.155 25.307 1.00 51.70 C ANISOU 4399 C TYR B 273 6754 7252 5639 1483 346 -286 C ATOM 4400 O TYR B 273 68.500 29.384 24.436 1.00 49.81 O ANISOU 4400 O TYR B 273 6621 7009 5294 1574 414 -275 O ATOM 4401 CB TYR B 273 67.240 32.561 25.076 1.00 45.60 C ANISOU 4401 CB TYR B 273 5868 6406 5050 1222 307 -249 C ATOM 4402 CG TYR B 273 68.374 33.049 24.197 1.00 53.64 C ANISOU 4402 CG TYR B 273 6824 7509 6048 1217 421 -215 C ATOM 4403 CD1 TYR B 273 68.773 32.365 23.045 1.00 53.26 C ANISOU 4403 CD1 TYR B 273 6893 7478 5867 1299 489 -179 C ATOM 4404 CD2 TYR B 273 69.059 34.203 24.535 1.00 56.52 C ANISOU 4404 CD2 TYR B 273 7012 7936 6529 1123 473 -226 C ATOM 4405 CE1 TYR B 273 69.827 32.833 22.259 1.00 46.86 C ANISOU 4405 CE1 TYR B 273 6016 6754 5036 1297 612 -139 C ATOM 4406 CE2 TYR B 273 70.110 34.675 23.755 1.00 57.61 C ANISOU 4406 CE2 TYR B 273 7076 8150 6662 1105 591 -187 C ATOM 4407 CZ TYR B 273 70.492 33.984 22.629 1.00 55.03 C ANISOU 4407 CZ TYR B 273 6859 7850 6199 1198 663 -136 C ATOM 4408 OH TYR B 273 71.536 34.483 21.879 1.00 58.61 O ANISOU 4408 OH TYR B 273 7230 8389 6651 1180 797 -89 O ATOM 4409 N ASN B 274 68.591 30.185 26.541 1.00 52.46 N ANISOU 4409 N ASN B 274 6696 7454 5781 1518 332 -318 N ATOM 4410 CA ASN B 274 69.788 29.416 26.879 1.00 52.53 C ANISOU 4410 CA ASN B 274 6625 7602 5731 1671 395 -320 C ATOM 4411 C ASN B 274 69.536 27.914 26.862 1.00 51.73 C ANISOU 4411 C ASN B 274 6694 7419 5541 1824 406 -306 C ATOM 4412 O ASN B 274 70.455 27.146 26.576 1.00 61.93 O ANISOU 4412 O ASN B 274 7990 8772 6767 1975 494 -289 O ATOM 4413 CB ASN B 274 70.335 29.843 28.242 1.00 53.80 C ANISOU 4413 CB ASN B 274 6574 7922 5946 1664 355 -356 C ATOM 4414 CG ASN B 274 71.171 31.097 28.162 1.00 55.78 C ANISOU 4414 CG ASN B 274 6627 8295 6272 1547 392 -384 C ATOM 4415 OD1 ASN B 274 71.952 31.274 27.227 1.00 62.70 O ANISOU 4415 OD1 ASN B 274 7470 9217 7135 1556 485 -355 O ATOM 4416 ND2 ASN B 274 71.026 31.972 29.148 1.00 52.02 N ANISOU 4416 ND2 ASN B 274 6020 7868 5875 1432 331 -446 N ATOM 4417 N LEU B 275 68.317 27.476 27.151 1.00 50.47 N ANISOU 4417 N LEU B 275 6674 7113 5390 1788 332 -311 N ATOM 4418 CA LEU B 275 67.989 26.057 27.139 1.00 48.40 C ANISOU 4418 CA LEU B 275 6589 6737 5064 1907 351 -302 C ATOM 4419 C LEU B 275 67.537 25.557 25.770 1.00 56.15 C ANISOU 4419 C LEU B 275 7782 7577 5974 1885 383 -319 C ATOM 4420 O LEU B 275 67.935 24.463 25.360 1.00 56.25 O ANISOU 4420 O LEU B 275 7923 7535 5914 2015 465 -328 O ATOM 4421 CB LEU B 275 66.862 25.758 28.132 1.00 50.69 C ANISOU 4421 CB LEU B 275 6925 6935 5400 1865 265 -299 C ATOM 4422 CG LEU B 275 67.154 25.702 29.626 1.00 54.92 C ANISOU 4422 CG LEU B 275 7322 7586 5958 1934 240 -280 C ATOM 4423 CD1 LEU B 275 65.853 25.430 30.381 1.00 52.00 C ANISOU 4423 CD1 LEU B 275 7031 7098 5628 1872 172 -271 C ATOM 4424 CD2 LEU B 275 68.171 24.637 29.927 1.00 49.78 C ANISOU 4424 CD2 LEU B 275 6667 7005 5240 2145 317 -236 C ATOM 4425 N PHE B 276 66.688 26.315 25.064 1.00 55.75 N ANISOU 4425 N PHE B 276 7777 7466 5938 1729 320 -326 N ATOM 4426 CA PHE B 276 65.981 25.796 23.900 1.00 51.67 C ANISOU 4426 CA PHE B 276 7469 6824 5338 1683 310 -350 C ATOM 4427 C PHE B 276 66.316 26.475 22.580 1.00 58.87 C ANISOU 4427 C PHE B 276 8403 7787 6177 1634 350 -338 C ATOM 4428 O PHE B 276 65.748 26.084 21.557 1.00 62.90 O ANISOU 4428 O PHE B 276 9088 8222 6589 1592 333 -364 O ATOM 4429 CB PHE B 276 64.454 25.872 24.101 1.00 55.29 C ANISOU 4429 CB PHE B 276 7992 7168 5849 1547 184 -354 C ATOM 4430 CG PHE B 276 63.968 25.175 25.341 1.00 50.89 C ANISOU 4430 CG PHE B 276 7433 6546 5358 1581 153 -355 C ATOM 4431 CD1 PHE B 276 64.156 23.811 25.504 1.00 56.16 C ANISOU 4431 CD1 PHE B 276 8234 7124 5980 1693 214 -376 C ATOM 4432 CD2 PHE B 276 63.308 25.875 26.334 1.00 43.52 C ANISOU 4432 CD2 PHE B 276 6375 5632 4530 1505 79 -330 C ATOM 4433 CE1 PHE B 276 63.703 23.158 26.655 1.00 56.43 C ANISOU 4433 CE1 PHE B 276 8273 7093 6074 1729 200 -354 C ATOM 4434 CE2 PHE B 276 62.841 25.237 27.485 1.00 53.40 C ANISOU 4434 CE2 PHE B 276 7628 6835 5827 1537 62 -321 C ATOM 4435 CZ PHE B 276 63.040 23.867 27.639 1.00 56.06 C ANISOU 4435 CZ PHE B 276 8098 7087 6117 1648 122 -324 C ATOM 4436 N GLY B 277 67.202 27.456 22.556 1.00 57.88 N ANISOU 4436 N GLY B 277 8113 7790 6088 1631 405 -301 N ATOM 4437 CA GLY B 277 67.702 27.989 21.306 1.00 53.47 C ANISOU 4437 CA GLY B 277 7578 7287 5451 1609 479 -273 C ATOM 4438 C GLY B 277 67.247 29.419 21.038 1.00 53.25 C ANISOU 4438 C GLY B 277 7463 7274 5495 1463 429 -210 C ATOM 4439 O GLY B 277 66.341 29.963 21.672 1.00 58.45 O ANISOU 4439 O GLY B 277 8073 7879 6258 1371 327 -197 O ATOM 4440 N SER B 278 67.880 29.994 20.020 1.00 54.88 N ANISOU 4440 N SER B 278 7664 7548 5642 1453 520 -161 N ATOM 4441 CA SER B 278 67.798 31.407 19.684 1.00 63.11 C ANISOU 4441 CA SER B 278 8611 8610 6759 1339 525 -78 C ATOM 4442 C SER B 278 66.430 31.854 19.169 1.00 65.82 C ANISOU 4442 C SER B 278 9053 8863 7091 1240 409 -24 C ATOM 4443 O SER B 278 66.249 33.048 18.913 1.00 67.71 O ANISOU 4443 O SER B 278 9224 9097 7407 1158 414 64 O ATOM 4444 CB SER B 278 68.874 31.709 18.650 1.00 56.11 C ANISOU 4444 CB SER B 278 7713 7819 5788 1371 674 -28 C ATOM 4445 OG SER B 278 68.699 30.799 17.589 1.00 66.95 O ANISOU 4445 OG SER B 278 9293 9179 6967 1436 695 -49 O ATOM 4446 N GLY B 279 65.481 30.945 18.963 1.00 62.21 N ANISOU 4446 N GLY B 279 8752 8338 6545 1245 311 -66 N ATOM 4447 CA GLY B 279 64.126 31.389 18.696 1.00 57.76 C ANISOU 4447 CA GLY B 279 8233 7713 6000 1149 179 -13 C ATOM 4448 C GLY B 279 63.539 32.252 19.799 1.00 57.44 C ANISOU 4448 C GLY B 279 8042 7621 6161 1085 118 15 C ATOM 4449 O GLY B 279 62.611 33.027 19.545 1.00 56.51 O ANISOU 4449 O GLY B 279 7910 7465 6095 1015 44 97 O ATOM 4450 N TYR B 280 64.037 32.110 21.027 1.00 52.05 N ANISOU 4450 N TYR B 280 7250 6943 5584 1117 147 -50 N ATOM 4451 CA TYR B 280 63.582 32.900 22.156 1.00 49.07 C ANISOU 4451 CA TYR B 280 6735 6525 5382 1060 106 -50 C ATOM 4452 C TYR B 280 64.345 34.204 22.312 1.00 53.65 C ANISOU 4452 C TYR B 280 7169 7138 6078 1013 194 -15 C ATOM 4453 O TYR B 280 63.969 35.031 23.149 1.00 54.00 O ANISOU 4453 O TYR B 280 7110 7134 6272 953 176 -22 O ATOM 4454 CB TYR B 280 63.711 32.082 23.446 1.00 47.60 C ANISOU 4454 CB TYR B 280 6510 6347 5230 1114 89 -140 C ATOM 4455 CG TYR B 280 62.614 31.060 23.663 1.00 51.08 C ANISOU 4455 CG TYR B 280 7064 6708 5635 1119 -6 -166 C ATOM 4456 CD1 TYR B 280 61.372 31.438 24.166 1.00 48.16 C ANISOU 4456 CD1 TYR B 280 6665 6269 5366 1048 -94 -144 C ATOM 4457 CD2 TYR B 280 62.813 29.722 23.359 1.00 53.30 C ANISOU 4457 CD2 TYR B 280 7481 6975 5795 1192 7 -213 C ATOM 4458 CE1 TYR B 280 60.369 30.508 24.364 1.00 53.23 C ANISOU 4458 CE1 TYR B 280 7393 6844 5987 1036 -173 -164 C ATOM 4459 CE2 TYR B 280 61.810 28.778 23.561 1.00 48.97 C ANISOU 4459 CE2 TYR B 280 7040 6337 5231 1175 -68 -242 C ATOM 4460 CZ TYR B 280 60.598 29.179 24.064 1.00 56.73 C ANISOU 4460 CZ TYR B 280 7973 7265 6314 1090 -161 -216 C ATOM 4461 OH TYR B 280 59.610 28.249 24.278 1.00 62.54 O ANISOU 4461 OH TYR B 280 8797 7917 7047 1058 -228 -241 O ATOM 4462 N ARG B 281 65.391 34.417 21.518 1.00 53.94 N ANISOU 4462 N ARG B 281 7197 7245 6052 1031 301 17 N ATOM 4463 CA ARG B 281 66.212 35.602 21.704 1.00 54.27 C ANISOU 4463 CA ARG B 281 7090 7313 6218 968 399 40 C ATOM 4464 C ARG B 281 65.451 36.890 21.384 1.00 55.02 C ANISOU 4464 C ARG B 281 7175 7303 6430 877 393 140 C ATOM 4465 O ARG B 281 65.702 37.923 22.010 1.00 56.48 O ANISOU 4465 O ARG B 281 7235 7447 6778 800 444 126 O ATOM 4466 CB ARG B 281 67.479 35.490 20.860 1.00 56.19 C ANISOU 4466 CB ARG B 281 7322 7659 6368 1008 529 66 C ATOM 4467 CG ARG B 281 68.372 36.713 20.985 1.00 61.50 C ANISOU 4467 CG ARG B 281 7831 8357 7178 920 642 91 C ATOM 4468 CD ARG B 281 69.417 36.763 19.920 1.00 57.93 C ANISOU 4468 CD ARG B 281 7379 7993 6639 944 782 156 C ATOM 4469 NE ARG B 281 70.380 37.832 20.178 1.00 58.96 N ANISOU 4469 NE ARG B 281 7327 8156 6918 845 898 162 N ATOM 4470 CZ ARG B 281 70.295 39.051 19.648 1.00 64.39 C ANISOU 4470 CZ ARG B 281 8000 8758 7707 741 976 266 C ATOM 4471 NH1 ARG B 281 69.289 39.348 18.833 1.00 59.03 N ANISOU 4471 NH1 ARG B 281 7472 7977 6982 745 939 386 N ATOM 4472 NH2 ARG B 281 71.215 39.970 19.930 1.00 60.00 N ANISOU 4472 NH2 ARG B 281 7276 8221 7301 632 1090 255 N ATOM 4473 N SER B 282 64.526 36.861 20.423 1.00 54.86 N ANISOU 4473 N SER B 282 7281 7237 6328 884 334 240 N ATOM 4474 CA SER B 282 63.818 38.091 20.077 1.00 55.75 C ANISOU 4474 CA SER B 282 7376 7253 6552 824 335 365 C ATOM 4475 C SER B 282 62.968 38.538 21.258 1.00 52.27 C ANISOU 4475 C SER B 282 6857 6714 6288 787 272 318 C ATOM 4476 O SER B 282 62.977 39.719 21.613 1.00 53.35 O ANISOU 4476 O SER B 282 6910 6763 6599 728 338 348 O ATOM 4477 CB SER B 282 62.995 37.907 18.803 1.00 57.48 C ANISOU 4477 CB SER B 282 7734 7483 6622 852 266 491 C ATOM 4478 OG SER B 282 62.323 36.667 18.833 1.00 77.17 O ANISOU 4478 OG SER B 282 10322 10009 8989 889 141 417 O ATOM 4479 N SER B 283 62.244 37.602 21.887 1.00 52.04 N ANISOU 4479 N SER B 283 6860 6691 6221 819 161 240 N ATOM 4480 CA SER B 283 61.432 37.939 23.055 1.00 52.18 C ANISOU 4480 CA SER B 283 6804 6630 6391 793 113 191 C ATOM 4481 C SER B 283 62.263 38.617 24.132 1.00 52.51 C ANISOU 4481 C SER B 283 6718 6666 6568 746 202 90 C ATOM 4482 O SER B 283 61.848 39.627 24.708 1.00 51.99 O ANISOU 4482 O SER B 283 6585 6502 6667 695 232 87 O ATOM 4483 CB SER B 283 60.774 36.687 23.626 1.00 57.40 C ANISOU 4483 CB SER B 283 7514 7316 6979 832 7 116 C ATOM 4484 OG SER B 283 59.864 36.124 22.706 1.00 63.95 O ANISOU 4484 OG SER B 283 8451 8145 7702 845 -89 189 O ATOM 4485 N ALA B 284 63.444 38.074 24.422 1.00 51.28 N ANISOU 4485 N ALA B 284 6521 6620 6342 763 246 0 N ATOM 4486 CA ALA B 284 64.276 38.677 25.454 1.00 49.23 C ANISOU 4486 CA ALA B 284 6122 6391 6191 704 311 -109 C ATOM 4487 C ALA B 284 64.779 40.044 25.010 1.00 52.93 C ANISOU 4487 C ALA B 284 6530 6791 6790 611 426 -60 C ATOM 4488 O ALA B 284 64.691 41.026 25.762 1.00 55.42 O ANISOU 4488 O ALA B 284 6766 7024 7268 528 468 -119 O ATOM 4489 CB ALA B 284 65.431 37.743 25.813 1.00 44.20 C ANISOU 4489 CB ALA B 284 5437 5916 5442 759 323 -195 C ATOM 4490 N MET B 285 65.267 40.138 23.768 1.00 50.35 N ANISOU 4490 N MET B 285 6251 6484 6397 620 490 52 N ATOM 4491 CA MET B 285 65.835 41.393 23.283 1.00 56.45 C ANISOU 4491 CA MET B 285 6968 7186 7293 529 621 118 C ATOM 4492 C MET B 285 64.767 42.479 23.172 1.00 54.29 C ANISOU 4492 C MET B 285 6731 6724 7173 493 632 215 C ATOM 4493 O MET B 285 65.026 43.655 23.469 1.00 56.31 O ANISOU 4493 O MET B 285 6918 6865 7611 396 737 203 O ATOM 4494 CB MET B 285 66.503 41.171 21.932 1.00 62.81 C ANISOU 4494 CB MET B 285 7833 8064 7969 563 693 236 C ATOM 4495 CG MET B 285 67.279 42.374 21.445 1.00 74.90 C ANISOU 4495 CG MET B 285 9297 9539 9624 464 853 310 C ATOM 4496 SD MET B 285 68.816 42.600 22.372 1.00 85.63 S ANISOU 4496 SD MET B 285 10449 11007 11078 359 944 141 S ATOM 4497 CE MET B 285 68.416 43.981 23.424 1.00 88.77 C ANISOU 4497 CE MET B 285 10767 11220 11742 211 978 55 C ATOM 4498 N SER B 286 63.555 42.100 22.769 1.00 55.13 N ANISOU 4498 N SER B 286 6938 6793 7216 570 530 308 N ATOM 4499 CA SER B 286 62.451 43.056 22.705 1.00 59.25 C ANISOU 4499 CA SER B 286 7478 7151 7884 566 531 415 C ATOM 4500 C SER B 286 62.204 43.727 24.057 1.00 60.23 C ANISOU 4500 C SER B 286 7515 7167 8202 507 561 282 C ATOM 4501 O SER B 286 62.018 44.943 24.135 1.00 62.55 O ANISOU 4501 O SER B 286 7786 7297 8683 457 660 326 O ATOM 4502 CB SER B 286 61.193 42.341 22.230 1.00 60.25 C ANISOU 4502 CB SER B 286 7693 7302 7898 654 388 506 C ATOM 4503 OG SER B 286 60.063 43.146 22.462 1.00 77.66 O ANISOU 4503 OG SER B 286 9880 9368 10257 668 376 586 O ATOM 4504 N ILE B 287 62.199 42.944 25.135 1.00 60.10 N ANISOU 4504 N ILE B 287 7460 7236 8138 515 486 119 N ATOM 4505 CA ILE B 287 61.992 43.493 26.471 1.00 54.71 C ANISOU 4505 CA ILE B 287 6704 6483 7602 461 512 -27 C ATOM 4506 C ILE B 287 63.141 44.398 26.882 1.00 55.70 C ANISOU 4506 C ILE B 287 6738 6581 7843 337 637 -137 C ATOM 4507 O ILE B 287 62.922 45.472 27.453 1.00 61.51 O ANISOU 4507 O ILE B 287 7443 7166 8763 265 720 -196 O ATOM 4508 CB ILE B 287 61.795 42.349 27.471 1.00 50.26 C ANISOU 4508 CB ILE B 287 6125 6045 6924 508 405 -156 C ATOM 4509 CG1 ILE B 287 60.445 41.665 27.230 1.00 47.06 C ANISOU 4509 CG1 ILE B 287 5796 5621 6464 597 297 -61 C ATOM 4510 CG2 ILE B 287 61.952 42.860 28.887 1.00 46.30 C ANISOU 4510 CG2 ILE B 287 5540 5527 6526 440 443 -336 C ATOM 4511 CD1 ILE B 287 60.208 40.434 28.123 1.00 46.53 C ANISOU 4511 CD1 ILE B 287 5732 5664 6283 645 203 -161 C ATOM 4512 N ILE B 288 64.384 43.985 26.614 1.00 59.81 N ANISOU 4512 N ILE B 288 7210 7247 8267 306 660 -175 N ATOM 4513 CA ILE B 288 65.533 44.796 27.014 1.00 59.84 C ANISOU 4513 CA ILE B 288 7100 7254 8380 167 770 -289 C ATOM 4514 C ILE B 288 65.521 46.138 26.290 1.00 63.69 C ANISOU 4514 C ILE B 288 7611 7537 9052 86 914 -177 C ATOM 4515 O ILE B 288 65.822 47.181 26.881 1.00 63.61 O ANISOU 4515 O ILE B 288 7539 7406 9222 -44 1015 -282 O ATOM 4516 CB ILE B 288 66.847 44.031 26.757 1.00 59.58 C ANISOU 4516 CB ILE B 288 6993 7437 8206 169 767 -323 C ATOM 4517 CG1 ILE B 288 66.971 42.835 27.708 1.00 53.40 C ANISOU 4517 CG1 ILE B 288 6172 6843 7276 245 645 -448 C ATOM 4518 CG2 ILE B 288 68.055 44.976 26.870 1.00 55.71 C ANISOU 4518 CG2 ILE B 288 6372 6951 7846 6 895 -402 C ATOM 4519 CD1 ILE B 288 68.209 41.959 27.465 1.00 48.42 C ANISOU 4519 CD1 ILE B 288 5466 6430 6502 287 642 -464 C ATOM 4520 N ASP B 289 65.142 46.138 25.009 1.00 67.23 N ANISOU 4520 N ASP B 289 8156 7936 9454 162 931 41 N ATOM 4521 CA ASP B 289 65.100 47.385 24.249 1.00 62.31 C ANISOU 4521 CA ASP B 289 7565 7115 8995 108 1076 190 C ATOM 4522 C ASP B 289 64.078 48.364 24.819 1.00 67.41 C ANISOU 4522 C ASP B 289 8237 7526 9847 98 1118 187 C ATOM 4523 O ASP B 289 64.370 49.559 24.947 1.00 66.93 O ANISOU 4523 O ASP B 289 8155 7278 9996 -11 1270 171 O ATOM 4524 CB ASP B 289 64.792 47.093 22.781 1.00 65.01 C ANISOU 4524 CB ASP B 289 8013 7485 9204 214 1064 436 C ATOM 4525 CG ASP B 289 66.009 46.583 22.012 1.00 71.63 C ANISOU 4525 CG ASP B 289 8829 8492 9896 197 1113 464 C ATOM 4526 OD1 ASP B 289 67.154 46.811 22.485 1.00 70.76 O ANISOU 4526 OD1 ASP B 289 8601 8433 9851 81 1196 333 O ATOM 4527 OD2 ASP B 289 65.815 45.969 20.931 1.00 67.98 O ANISOU 4527 OD2 ASP B 289 8460 8118 9252 298 1070 614 O ATOM 4528 N ASP B 290 62.877 47.880 25.171 1.00 68.82 N ANISOU 4528 N ASP B 290 8461 7704 9983 210 998 199 N ATOM 4529 CA ASP B 290 61.828 48.767 25.678 1.00 67.38 C ANISOU 4529 CA ASP B 290 8300 7306 9996 230 1046 211 C ATOM 4530 C ASP B 290 62.241 49.441 26.981 1.00 70.77 C ANISOU 4530 C ASP B 290 8661 7646 10582 100 1132 -35 C ATOM 4531 O ASP B 290 62.004 50.640 27.171 1.00 77.52 O ANISOU 4531 O ASP B 290 9532 8263 11661 47 1272 -37 O ATOM 4532 CB ASP B 290 60.530 47.990 25.883 1.00 68.50 C ANISOU 4532 CB ASP B 290 8475 7505 10049 367 897 255 C ATOM 4533 CG ASP B 290 59.978 47.438 24.596 1.00 80.81 C ANISOU 4533 CG ASP B 290 10102 9139 11462 480 806 487 C ATOM 4534 OD1 ASP B 290 60.509 47.807 23.530 1.00 90.26 O ANISOU 4534 OD1 ASP B 290 11336 10321 12639 469 875 636 O ATOM 4535 OD2 ASP B 290 59.035 46.615 24.646 1.00 86.77 O ANISOU 4535 OD2 ASP B 290 10875 9980 12115 571 666 517 O ATOM 4536 N TYR B 291 62.850 48.687 27.898 1.00 63.55 N ANISOU 4536 N TYR B 291 7675 6921 9549 49 1052 -247 N ATOM 4537 CA TYR B 291 63.260 49.278 29.168 1.00 60.73 C ANISOU 4537 CA TYR B 291 7250 6521 9304 -83 1114 -500 C ATOM 4538 C TYR B 291 64.356 50.315 28.965 1.00 68.55 C ANISOU 4538 C TYR B 291 8191 7407 10447 -260 1269 -555 C ATOM 4539 O TYR B 291 64.381 51.342 29.653 1.00 66.96 O ANISOU 4539 O TYR B 291 7980 7027 10435 -379 1384 -701 O ATOM 4540 CB TYR B 291 63.734 48.186 30.124 1.00 58.50 C ANISOU 4540 CB TYR B 291 6895 6502 8830 -85 982 -684 C ATOM 4541 CG TYR B 291 62.647 47.505 30.912 1.00 62.67 C ANISOU 4541 CG TYR B 291 7456 7076 9279 29 876 -724 C ATOM 4542 CD1 TYR B 291 61.697 48.244 31.611 1.00 59.96 C ANISOU 4542 CD1 TYR B 291 7146 6554 9083 35 939 -785 C ATOM 4543 CD2 TYR B 291 62.558 46.116 30.947 1.00 66.10 C ANISOU 4543 CD2 TYR B 291 7895 7722 9500 134 731 -695 C ATOM 4544 CE1 TYR B 291 60.707 47.616 32.336 1.00 62.63 C ANISOU 4544 CE1 TYR B 291 7503 6944 9350 137 857 -814 C ATOM 4545 CE2 TYR B 291 61.555 45.474 31.667 1.00 59.42 C ANISOU 4545 CE2 TYR B 291 7077 6911 8589 228 648 -719 C ATOM 4546 CZ TYR B 291 60.640 46.230 32.360 1.00 60.23 C ANISOU 4546 CZ TYR B 291 7196 6855 8834 227 711 -776 C ATOM 4547 OH TYR B 291 59.650 45.607 33.076 1.00 57.19 O ANISOU 4547 OH TYR B 291 6828 6511 8389 317 644 -794 O ATOM 4548 N LEU B 292 65.279 50.062 28.031 1.00 70.87 N ANISOU 4548 N LEU B 292 8455 7806 10666 -288 1287 -450 N ATOM 4549 CA LEU B 292 66.311 51.054 27.744 1.00 73.30 C ANISOU 4549 CA LEU B 292 8707 8010 11133 -466 1450 -477 C ATOM 4550 C LEU B 292 65.690 52.323 27.178 1.00 77.36 C ANISOU 4550 C LEU B 292 9318 8191 11884 -475 1616 -323 C ATOM 4551 O LEU B 292 66.112 53.434 27.508 1.00 82.91 O ANISOU 4551 O LEU B 292 10000 8698 12803 -641 1773 -428 O ATOM 4552 CB LEU B 292 67.349 50.491 26.773 1.00 64.34 C ANISOU 4552 CB LEU B 292 7521 7060 9864 -471 1451 -364 C ATOM 4553 CG LEU B 292 68.245 49.372 27.290 1.00 62.40 C ANISOU 4553 CG LEU B 292 7155 7134 9421 -475 1328 -512 C ATOM 4554 CD1 LEU B 292 69.262 48.984 26.246 1.00 59.42 C ANISOU 4554 CD1 LEU B 292 6730 6902 8947 -474 1372 -387 C ATOM 4555 CD2 LEU B 292 68.917 49.770 28.586 1.00 69.34 C ANISOU 4555 CD2 LEU B 292 7902 8068 10377 -649 1333 -796 C ATOM 4556 N ARG B 293 64.695 52.174 26.307 1.00 74.14 N ANISOU 4556 N ARG B 293 9017 7716 11439 -299 1587 -70 N ATOM 4557 CA ARG B 293 63.944 53.329 25.845 1.00 72.63 C ANISOU 4557 CA ARG B 293 8915 7213 11466 -264 1731 101 C ATOM 4558 C ARG B 293 63.256 54.021 27.023 1.00 71.62 C ANISOU 4558 C ARG B 293 8801 6888 11525 -293 1785 -80 C ATOM 4559 O ARG B 293 63.522 55.192 27.312 1.00 74.78 O ANISOU 4559 O ARG B 293 9213 7035 12164 -423 1967 -159 O ATOM 4560 CB ARG B 293 62.962 52.886 24.753 1.00 76.03 C ANISOU 4560 CB ARG B 293 9434 7675 11779 -54 1647 401 C ATOM 4561 CG ARG B 293 62.214 54.014 24.069 1.00 86.49 C ANISOU 4561 CG ARG B 293 10846 8715 13303 20 1788 645 C ATOM 4562 CD ARG B 293 61.703 53.583 22.694 1.00 94.21 C ANISOU 4562 CD ARG B 293 11889 9792 14115 186 1711 965 C ATOM 4563 NE ARG B 293 60.602 54.418 22.205 1.00106.73 N ANISOU 4563 NE ARG B 293 13544 11159 15849 325 1778 1213 N ATOM 4564 CZ ARG B 293 60.756 55.502 21.441 1.00114.52 C ANISOU 4564 CZ ARG B 293 14589 11926 16998 323 1964 1431 C ATOM 4565 NH1 ARG B 293 61.970 55.899 21.075 1.00118.47 N ANISOU 4565 NH1 ARG B 293 15084 12390 17540 171 2108 1421 N ATOM 4566 NH2 ARG B 293 59.696 56.194 21.043 1.00113.69 N ANISOU 4566 NH2 ARG B 293 14538 11638 17021 479 2013 1671 N ATOM 4567 N MET B 294 62.386 53.295 27.735 1.00 72.44 N ANISOU 4567 N MET B 294 8904 7099 11521 -179 1642 -159 N ATOM 4568 CA MET B 294 61.663 53.857 28.879 1.00 70.45 C ANISOU 4568 CA MET B 294 8666 6684 11416 -185 1695 -332 C ATOM 4569 C MET B 294 62.593 54.521 29.897 1.00 74.17 C ANISOU 4569 C MET B 294 9086 7093 12002 -409 1799 -642 C ATOM 4570 O MET B 294 62.280 55.592 30.425 1.00 76.79 O ANISOU 4570 O MET B 294 9464 7155 12559 -470 1954 -745 O ATOM 4571 CB MET B 294 60.849 52.758 29.564 1.00 69.24 C ANISOU 4571 CB MET B 294 8497 6730 11082 -58 1514 -397 C ATOM 4572 CG MET B 294 60.310 53.156 30.930 1.00 74.89 C ANISOU 4572 CG MET B 294 9211 7348 11895 -82 1561 -630 C ATOM 4573 SD MET B 294 59.615 51.774 31.870 1.00 78.54 S ANISOU 4573 SD MET B 294 9638 8083 12121 30 1362 -732 S ATOM 4574 CE MET B 294 58.470 51.079 30.670 1.00 77.55 C ANISOU 4574 CE MET B 294 9550 7997 11919 245 1248 -388 C ATOM 4575 N LEU B 295 63.738 53.909 30.187 1.00 74.00 N ANISOU 4575 N LEU B 295 8965 7321 11830 -534 1718 -800 N ATOM 4576 CA LEU B 295 64.714 54.525 31.085 1.00 68.65 C ANISOU 4576 CA LEU B 295 8214 6626 11244 -770 1797 -1095 C ATOM 4577 C LEU B 295 65.575 55.516 30.318 1.00 68.77 C ANISOU 4577 C LEU B 295 8221 6455 11452 -933 1978 -1028 C ATOM 4578 O LEU B 295 66.498 56.099 30.874 1.00 75.45 O ANISOU 4578 O LEU B 295 8994 7277 12396 -1161 2057 -1256 O ATOM 4579 CB LEU B 295 65.593 53.463 31.756 1.00 68.35 C ANISOU 4579 CB LEU B 295 8048 6958 10964 -828 1628 -1281 C ATOM 4580 CG LEU B 295 64.877 52.363 32.558 1.00 71.17 C ANISOU 4580 CG LEU B 295 8407 7525 11109 -677 1451 -1344 C ATOM 4581 CD1 LEU B 295 65.808 51.221 32.907 1.00 67.19 C ANISOU 4581 CD1 LEU B 295 7784 7385 10360 -692 1292 -1438 C ATOM 4582 CD2 LEU B 295 64.277 52.924 33.834 1.00 71.37 C ANISOU 4582 CD2 LEU B 295 8464 7436 11216 -721 1497 -1579 C TER 4583 LEU B 295 HETATM 4584 PB ADP A 301 62.776 19.434 18.724 1.00 94.59 P HETATM 4585 O1B ADP A 301 63.058 18.047 18.180 1.00 82.70 O HETATM 4586 O2B ADP A 301 63.470 19.717 20.047 1.00100.17 O HETATM 4587 O3B ADP A 301 61.299 19.774 18.681 1.00 96.19 O HETATM 4588 PA ADP A 301 63.464 22.110 17.891 1.00 76.58 P HETATM 4589 O1A ADP A 301 62.710 22.703 16.710 1.00 72.25 O HETATM 4590 O2A ADP A 301 63.129 22.485 19.323 1.00 73.57 O HETATM 4591 O3A ADP A 301 63.477 20.498 17.713 1.00 84.28 O HETATM 4592 O5' ADP A 301 65.031 22.460 17.685 1.00 75.40 O HETATM 4593 C5' ADP A 301 65.996 22.544 18.737 1.00 69.21 C HETATM 4594 C4' ADP A 301 67.137 23.518 18.401 1.00 68.88 C HETATM 4595 O4' ADP A 301 67.388 23.665 16.991 1.00 70.02 O HETATM 4596 C3' ADP A 301 66.831 24.926 18.877 1.00 73.49 C HETATM 4597 O3' ADP A 301 68.079 25.439 19.370 1.00 73.03 O HETATM 4598 C2' ADP A 301 66.344 25.686 17.643 1.00 66.84 C HETATM 4599 O2' ADP A 301 66.624 27.093 17.703 1.00 61.08 O HETATM 4600 C1' ADP A 301 67.135 25.020 16.539 1.00 62.33 C HETATM 4601 N9 ADP A 301 66.481 24.914 15.213 1.00 50.95 N HETATM 4602 C8 ADP A 301 65.334 24.261 14.923 1.00 52.68 C HETATM 4603 N7 ADP A 301 65.055 24.305 13.595 1.00 48.33 N HETATM 4604 C5 ADP A 301 66.059 24.988 13.024 1.00 48.56 C HETATM 4605 C6 ADP A 301 66.408 25.398 11.655 1.00 41.65 C HETATM 4606 N6 ADP A 301 65.609 25.068 10.612 1.00 40.39 N HETATM 4607 N1 ADP A 301 67.547 26.094 11.487 1.00 44.64 N HETATM 4608 C2 ADP A 301 68.354 26.416 12.504 1.00 45.94 C HETATM 4609 N3 ADP A 301 68.106 26.075 13.769 1.00 52.98 N HETATM 4610 C4 ADP A 301 66.992 25.380 14.084 1.00 47.88 C HETATM 4611 S SO4 A 302 30.666 35.033 18.401 1.00 75.72 S HETATM 4612 O1 SO4 A 302 32.063 35.300 17.998 1.00 75.57 O HETATM 4613 O2 SO4 A 302 29.817 34.914 17.218 1.00 77.61 O HETATM 4614 O3 SO4 A 302 30.523 33.797 19.199 1.00 76.15 O HETATM 4615 O4 SO4 A 302 30.232 36.180 19.189 1.00 72.22 O HETATM 4616 S SO4 A 303 68.898 33.103 6.367 1.00 69.92 S HETATM 4617 O1 SO4 A 303 69.784 33.908 5.526 1.00 74.46 O HETATM 4618 O2 SO4 A 303 68.373 32.001 5.570 1.00 68.50 O HETATM 4619 O3 SO4 A 303 69.568 32.489 7.511 1.00 55.18 O HETATM 4620 O4 SO4 A 303 67.825 33.984 6.845 1.00 67.14 O HETATM 4621 S SO4 A 304 34.784 13.471 37.599 1.00121.49 S HETATM 4622 O1 SO4 A 304 34.038 14.655 37.176 1.00103.79 O HETATM 4623 O2 SO4 A 304 35.064 12.593 36.463 1.00128.01 O HETATM 4624 O3 SO4 A 304 36.048 13.875 38.202 1.00127.81 O HETATM 4625 O4 SO4 A 304 34.007 12.733 38.590 1.00124.96 O HETATM 4626 S SO4 A 305 54.393 39.470 1.422 1.00134.25 S HETATM 4627 O1 SO4 A 305 54.260 38.033 1.663 1.00135.63 O HETATM 4628 O2 SO4 A 305 54.782 39.700 0.035 1.00133.22 O HETATM 4629 O3 SO4 A 305 53.109 40.117 1.674 1.00137.89 O HETATM 4630 O4 SO4 A 305 55.415 40.038 2.302 1.00128.17 O HETATM 4631 S SO4 A 306 35.501 1.271 21.957 1.00164.10 S HETATM 4632 O1 SO4 A 306 35.533 2.561 21.270 1.00163.16 O HETATM 4633 O2 SO4 A 306 35.057 0.225 21.042 1.00162.80 O HETATM 4634 O3 SO4 A 306 34.581 1.344 23.090 1.00162.26 O HETATM 4635 O4 SO4 A 306 36.842 0.943 22.433 1.00164.89 O HETATM 4636 S SO4 A 307 77.177 26.290 16.088 1.00 96.59 S HETATM 4637 O1 SO4 A 307 77.933 25.138 15.589 1.00 79.19 O HETATM 4638 O2 SO4 A 307 76.521 27.016 15.003 1.00100.30 O HETATM 4639 O3 SO4 A 307 76.114 25.831 16.987 1.00101.60 O HETATM 4640 O4 SO4 A 307 78.106 27.181 16.790 1.00102.03 O HETATM 4641 S SO4 A 308 67.368 25.706 0.149 1.00123.86 S HETATM 4642 O1 SO4 A 308 66.942 24.451 -0.473 1.00124.47 O HETATM 4643 O2 SO4 A 308 68.431 26.291 -0.661 1.00132.22 O HETATM 4644 O3 SO4 A 308 67.869 25.471 1.501 1.00118.52 O HETATM 4645 O4 SO4 A 308 66.239 26.629 0.203 1.00122.22 O HETATM 4646 S SO4 A 309 32.874 11.273 3.646 1.00149.27 S HETATM 4647 O1 SO4 A 309 32.057 12.315 3.033 1.00148.20 O HETATM 4648 O2 SO4 A 309 33.647 10.604 2.605 1.00150.97 O HETATM 4649 O3 SO4 A 309 33.773 11.856 4.636 1.00147.97 O HETATM 4650 O4 SO4 A 309 32.006 10.303 4.304 1.00151.48 O HETATM 4651 S SO4 A 310 54.542 43.792 17.378 1.00152.45 S HETATM 4652 O1 SO4 A 310 55.200 43.610 16.085 1.00152.41 O HETATM 4653 O2 SO4 A 310 53.098 43.722 17.186 1.00151.28 O HETATM 4654 O3 SO4 A 310 54.984 42.758 18.314 1.00147.67 O HETATM 4655 O4 SO4 A 310 54.879 45.105 17.921 1.00155.80 O HETATM 4656 CL CL A 311 53.789 23.021 26.149 1.00 86.02 CL HETATM 4657 C1 EDO A 312 51.037 16.811 35.168 1.00 61.73 C HETATM 4658 O1 EDO A 312 50.055 16.027 35.854 1.00 63.55 O HETATM 4659 C2 EDO A 312 51.528 17.896 36.103 1.00 72.29 C HETATM 4660 O2 EDO A 312 50.627 18.999 35.965 1.00 83.25 O HETATM 4661 C1 EDO A 313 65.897 20.185 -2.642 1.00 82.00 C HETATM 4662 O1 EDO A 313 65.566 19.565 -1.389 1.00 73.87 O HETATM 4663 C2 EDO A 313 65.051 21.437 -2.865 1.00 85.13 C HETATM 4664 O2 EDO A 313 64.067 21.184 -3.876 1.00 88.26 O HETATM 4665 C1 EDO A 314 49.758 43.423 23.604 1.00 90.86 C HETATM 4666 O1 EDO A 314 48.382 43.036 23.455 1.00 87.08 O HETATM 4667 C2 EDO A 314 50.596 42.971 22.410 1.00 91.91 C HETATM 4668 O2 EDO A 314 50.079 43.525 21.192 1.00 91.81 O HETATM 4669 C1 EDO A 315 63.526 27.040 19.036 1.00 67.28 C HETATM 4670 O1 EDO A 315 64.662 27.915 19.003 1.00 62.77 O HETATM 4671 C2 EDO A 315 62.413 27.696 19.839 1.00 76.09 C HETATM 4672 O2 EDO A 315 61.723 28.652 19.020 1.00 79.64 O HETATM 4673 S DMS A 316 72.228 23.699 16.587 1.00 96.12 S HETATM 4674 O DMS A 316 73.586 24.295 16.884 1.00102.40 O HETATM 4675 C1 DMS A 316 71.060 24.085 17.933 1.00 93.23 C HETATM 4676 C2 DMS A 316 71.377 24.637 15.281 1.00 93.49 C HETATM 4677 PB ADP B 301 58.956 15.730 35.610 1.00 72.15 P HETATM 4678 O1B ADP B 301 58.855 14.734 34.482 1.00 74.18 O HETATM 4679 O2B ADP B 301 60.204 15.559 36.445 1.00 70.07 O HETATM 4680 O3B ADP B 301 58.665 17.158 35.206 1.00 80.45 O HETATM 4681 PA ADP B 301 56.240 15.874 36.455 1.00 64.13 P HETATM 4682 O1A ADP B 301 56.011 16.477 35.083 1.00 80.42 O HETATM 4683 O2A ADP B 301 55.937 16.643 37.707 1.00 62.82 O HETATM 4684 O3A ADP B 301 57.748 15.330 36.600 1.00 69.76 O HETATM 4685 O5' ADP B 301 55.437 14.496 36.578 1.00 60.75 O HETATM 4686 C5' ADP B 301 55.371 13.492 35.580 1.00 59.97 C HETATM 4687 C4' ADP B 301 54.090 12.683 35.836 1.00 67.53 C HETATM 4688 O4' ADP B 301 53.957 12.338 37.214 1.00 74.42 O HETATM 4689 C3' ADP B 301 52.823 13.451 35.508 1.00 69.10 C HETATM 4690 O3' ADP B 301 51.918 12.480 34.982 1.00 72.37 O HETATM 4691 C2' ADP B 301 52.259 13.938 36.818 1.00 67.53 C HETATM 4692 O2' ADP B 301 50.840 13.892 36.790 1.00 66.76 O HETATM 4693 C1' ADP B 301 52.728 12.862 37.755 1.00 71.63 C HETATM 4694 N9 ADP B 301 53.053 13.329 39.112 1.00 61.40 N HETATM 4695 C8 ADP B 301 53.976 14.259 39.423 1.00 51.85 C HETATM 4696 N7 ADP B 301 54.065 14.408 40.763 1.00 50.54 N HETATM 4697 C5 ADP B 301 53.186 13.549 41.313 1.00 46.71 C HETATM 4698 C6 ADP B 301 52.779 13.190 42.675 1.00 41.04 C HETATM 4699 N6 ADP B 301 53.340 13.807 43.736 1.00 47.28 N HETATM 4700 N1 ADP B 301 51.822 12.248 42.814 1.00 44.64 N HETATM 4701 C2 ADP B 301 51.255 11.627 41.767 1.00 40.24 C HETATM 4702 N3 ADP B 301 51.588 11.905 40.501 1.00 54.44 N HETATM 4703 C4 ADP B 301 52.524 12.837 40.222 1.00 51.54 C HETATM 4704 S SO4 B 302 52.239 50.522 38.094 1.00 81.94 S HETATM 4705 O1 SO4 B 302 53.461 50.153 37.355 1.00 83.86 O HETATM 4706 O2 SO4 B 302 51.373 51.270 37.188 1.00 83.76 O HETATM 4707 O3 SO4 B 302 51.497 49.352 38.589 1.00 69.39 O HETATM 4708 O4 SO4 B 302 52.596 51.374 39.233 1.00 84.26 O HETATM 4709 S SO4 B 303 44.833 12.327 48.268 1.00 81.68 S HETATM 4710 O1 SO4 B 303 45.249 11.667 47.019 1.00 68.62 O HETATM 4711 O2 SO4 B 303 44.312 13.666 47.975 1.00 87.28 O HETATM 4712 O3 SO4 B 303 43.793 11.567 48.954 1.00 85.66 O HETATM 4713 O4 SO4 B 303 45.991 12.421 49.156 1.00 81.11 O HETATM 4714 S SO4 B 304 42.757 27.743 54.254 1.00147.64 S HETATM 4715 O1 SO4 B 304 42.280 26.955 53.120 1.00148.43 O HETATM 4716 O2 SO4 B 304 43.358 28.984 53.772 1.00148.82 O HETATM 4717 O3 SO4 B 304 41.634 28.057 55.131 1.00146.62 O HETATM 4718 O4 SO4 B 304 43.759 26.976 54.986 1.00145.33 O HETATM 4719 S SO4 B 305 70.636 43.078 17.801 1.00133.02 S HETATM 4720 O1 SO4 B 305 70.006 41.842 17.324 1.00131.85 O HETATM 4721 O2 SO4 B 305 70.917 43.961 16.672 1.00134.03 O HETATM 4722 O3 SO4 B 305 71.892 42.748 18.463 1.00131.17 O HETATM 4723 O4 SO4 B 305 69.747 43.775 18.732 1.00134.23 O HETATM 4724 S SO4 B 306 48.666 2.722 37.410 1.00138.41 S HETATM 4725 O1 SO4 B 306 49.931 2.598 36.700 1.00138.10 O HETATM 4726 O2 SO4 B 306 47.732 1.723 36.898 1.00134.76 O HETATM 4727 O3 SO4 B 306 48.910 2.488 38.829 1.00141.84 O HETATM 4728 O4 SO4 B 306 48.111 4.062 37.226 1.00137.59 O HETATM 4729 CL CL B 307 57.529 25.590 28.609 1.00 83.59 CL HETATM 4730 C1 EDO B 308 37.804 31.104 38.275 1.00 81.49 C HETATM 4731 O1 EDO B 308 37.617 30.831 39.679 1.00 78.52 O HETATM 4732 C2 EDO B 308 38.020 29.832 37.449 1.00 79.78 C HETATM 4733 O2 EDO B 308 38.820 28.886 38.169 1.00 78.71 O HETATM 4734 S DMS B 309 83.611 16.682 11.578 1.00 90.95 S HETATM 4735 O DMS B 309 82.817 16.078 10.457 1.00 89.31 O HETATM 4736 C1 DMS B 309 84.145 18.351 11.128 1.00 80.25 C HETATM 4737 C2 DMS B 309 82.617 17.023 13.049 1.00 84.06 C HETATM 4738 O HOH A 401 69.366 24.227 2.665 1.00 57.84 O HETATM 4739 O HOH A 402 63.987 22.954 21.489 1.00 54.39 O HETATM 4740 O HOH A 403 68.113 34.711 9.427 1.00 58.23 O HETATM 4741 O HOH A 404 36.460 31.023 10.348 1.00 55.83 O HETATM 4742 O HOH A 405 43.954 20.729 15.861 1.00 50.99 O HETATM 4743 O HOH A 406 45.592 17.851 -0.670 1.00 71.49 O HETATM 4744 O HOH A 407 55.334 29.314 2.915 1.00 49.40 O HETATM 4745 O HOH A 408 78.255 24.070 13.208 1.00 51.02 O HETATM 4746 O HOH A 409 61.027 9.851 13.505 1.00 64.39 O HETATM 4747 O HOH A 410 45.379 13.126 18.195 1.00 43.52 O HETATM 4748 O HOH A 411 47.773 27.912 18.640 1.00 46.26 O HETATM 4749 O HOH A 412 69.475 29.667 14.250 1.00 55.46 O HETATM 4750 O HOH A 413 35.674 38.135 18.675 1.00 59.69 O HETATM 4751 O HOH A 414 47.951 25.357 16.239 1.00 43.03 O HETATM 4752 O HOH A 415 44.294 18.532 -4.093 1.00 74.42 O HETATM 4753 O HOH A 416 51.090 23.167 -0.238 1.00 58.89 O HETATM 4754 O HOH A 417 51.668 20.095 21.682 1.00 56.20 O HETATM 4755 O HOH A 418 60.641 22.067 11.946 1.00 47.30 O HETATM 4756 O HOH A 419 48.119 33.850 23.426 1.00 57.45 O HETATM 4757 O HOH A 420 47.373 33.797 0.804 1.00 61.22 O HETATM 4758 O HOH A 421 45.974 23.476 16.652 1.00 49.43 O HETATM 4759 O HOH A 422 47.257 41.709 7.941 1.00 63.06 O HETATM 4760 O HOH A 423 38.143 27.420 7.698 1.00 49.57 O HETATM 4761 O HOH A 424 37.185 29.634 17.729 1.00 44.01 O HETATM 4762 O HOH A 425 39.962 29.335 17.973 1.00 49.34 O HETATM 4763 O HOH A 426 71.410 15.659 15.178 1.00 48.94 O HETATM 4764 O HOH A 427 44.027 11.974 16.012 1.00 59.60 O HETATM 4765 O HOH A 428 45.313 34.502 22.715 1.00 61.23 O HETATM 4766 O HOH A 429 57.489 34.794 7.056 1.00 58.76 O HETATM 4767 O HOH A 430 46.499 19.604 15.631 1.00 45.61 O HETATM 4768 O HOH A 431 41.514 32.466 19.625 1.00 65.56 O HETATM 4769 O HOH A 432 30.347 32.160 7.899 1.00 53.65 O HETATM 4770 O HOH A 433 41.022 28.334 20.240 1.00 42.59 O HETATM 4771 O HOH A 434 42.237 30.332 21.681 1.00 47.25 O HETATM 4772 O HOH A 435 39.453 39.608 17.669 1.00 71.37 O HETATM 4773 O HOH A 436 57.645 29.570 1.262 1.00 71.57 O HETATM 4774 O HOH A 437 41.422 31.423 23.822 1.00 58.54 O HETATM 4775 O HOH A 438 62.906 22.334 13.668 1.00 50.62 O HETATM 4776 O HOH A 439 45.449 8.897 6.356 1.00 63.45 O HETATM 4777 O HOH A 440 36.024 28.501 6.785 1.00 54.48 O HETATM 4778 O HOH A 441 35.155 29.645 24.112 1.00 56.88 O HETATM 4779 O HOH A 442 40.644 36.844 19.777 1.00 67.57 O HETATM 4780 O HOH A 443 49.050 19.298 22.194 1.00 42.76 O HETATM 4781 O HOH A 444 31.714 20.713 6.774 1.00 62.14 O HETATM 4782 O HOH A 445 59.200 35.806 4.883 1.00 59.67 O HETATM 4783 O HOH B 401 70.204 13.588 30.257 1.00 64.86 O HETATM 4784 O HOH B 402 71.123 32.102 38.760 1.00 61.33 O HETATM 4785 O HOH B 403 71.746 20.717 24.939 1.00 59.25 O HETATM 4786 O HOH B 404 52.097 24.215 52.270 1.00 57.04 O HETATM 4787 O HOH B 405 62.892 34.222 39.252 1.00 50.80 O HETATM 4788 O HOH B 406 54.676 32.316 36.886 1.00 44.11 O HETATM 4789 O HOH B 407 49.069 31.845 29.639 1.00 63.14 O HETATM 4790 O HOH B 408 43.294 42.690 38.563 1.00 52.35 O HETATM 4791 O HOH B 409 60.714 5.915 38.321 1.00 58.45 O HETATM 4792 O HOH B 410 53.469 38.263 34.392 1.00 48.94 O HETATM 4793 O HOH B 411 69.578 30.927 36.380 1.00 46.85 O HETATM 4794 O HOH B 412 63.135 31.164 39.351 1.00 44.92 O HETATM 4795 O HOH B 413 50.189 33.227 55.196 1.00 67.21 O HETATM 4796 O HOH B 414 59.567 32.504 38.605 1.00 51.46 O HETATM 4797 O HOH B 415 56.131 38.984 35.616 1.00 45.69 O HETATM 4798 O HOH B 416 51.777 39.129 36.155 1.00 52.25 O HETATM 4799 O HOH B 417 52.936 43.736 43.966 1.00 47.45 O HETATM 4800 O HOH B 418 55.784 42.705 38.446 1.00 44.93 O HETATM 4801 O HOH B 419 49.384 36.968 33.030 1.00 60.25 O HETATM 4802 O HOH B 420 57.462 17.810 42.581 1.00 52.52 O HETATM 4803 O HOH B 421 60.891 27.052 32.897 1.00 56.16 O HETATM 4804 O HOH B 422 51.673 21.523 53.727 1.00 68.10 O HETATM 4805 O HOH B 423 57.192 31.153 38.964 1.00 47.42 O HETATM 4806 O HOH B 424 42.001 42.175 45.334 1.00 40.99 O HETATM 4807 O HOH B 425 55.321 40.060 37.840 1.00 45.66 O HETATM 4808 O HOH B 426 63.794 23.843 44.634 1.00 65.72 O HETATM 4809 O HOH B 427 56.411 16.065 40.679 1.00 51.28 O HETATM 4810 O HOH B 428 56.085 45.139 32.104 1.00 49.78 O HETATM 4811 O HOH B 429 62.633 29.293 32.667 1.00 47.74 O HETATM 4812 O HOH B 430 41.857 35.754 48.528 1.00 55.83 O HETATM 4813 O HOH B 431 65.659 31.567 59.199 1.00 72.68 O HETATM 4814 O HOH B 432 51.135 37.106 30.759 1.00 63.25 O HETATM 4815 O HOH B 433 56.174 34.268 24.563 1.00 63.68 O HETATM 4816 O HOH B 434 61.268 35.722 37.589 1.00 50.80 O HETATM 4817 O HOH B 435 51.799 41.647 45.156 1.00 50.78 O HETATM 4818 O HOH B 436 39.009 35.001 35.660 1.00 57.47 O HETATM 4819 O HOH B 437 64.068 34.623 17.250 1.00 66.11 O HETATM 4820 O HOH B 438 75.003 15.929 41.046 1.00 68.57 O HETATM 4821 O HOH B 439 73.106 26.192 23.734 1.00 66.76 O HETATM 4822 O HOH B 440 50.873 20.613 51.770 1.00 62.72 O HETATM 4823 O HOH B 441 57.328 42.954 49.681 1.00 60.56 O HETATM 4824 O HOH B 442 40.597 37.621 32.708 1.00 60.89 O HETATM 4825 O HOH B 443 57.082 47.327 30.223 1.00 74.97 O HETATM 4826 O HOH B 444 39.371 35.855 33.245 1.00 75.39 O CONECT 190 2485 CONECT 1796 4084 CONECT 2485 190 CONECT 4084 1796 CONECT 4584 4585 4586 4587 4591 CONECT 4585 4584 CONECT 4586 4584 CONECT 4587 4584 CONECT 4588 4589 4590 4591 4592 CONECT 4589 4588 CONECT 4590 4588 CONECT 4591 4584 4588 CONECT 4592 4588 4593 CONECT 4593 4592 4594 CONECT 4594 4593 4595 4596 CONECT 4595 4594 4600 CONECT 4596 4594 4597 4598 CONECT 4597 4596 CONECT 4598 4596 4599 4600 CONECT 4599 4598 CONECT 4600 4595 4598 4601 CONECT 4601 4600 4602 4610 CONECT 4602 4601 4603 CONECT 4603 4602 4604 CONECT 4604 4603 4605 4610 CONECT 4605 4604 4606 4607 CONECT 4606 4605 CONECT 4607 4605 4608 CONECT 4608 4607 4609 CONECT 4609 4608 4610 CONECT 4610 4601 4604 4609 CONECT 4611 4612 4613 4614 4615 CONECT 4612 4611 CONECT 4613 4611 CONECT 4614 4611 CONECT 4615 4611 CONECT 4616 4617 4618 4619 4620 CONECT 4617 4616 CONECT 4618 4616 CONECT 4619 4616 CONECT 4620 4616 CONECT 4621 4622 4623 4624 4625 CONECT 4622 4621 CONECT 4623 4621 CONECT 4624 4621 CONECT 4625 4621 CONECT 4626 4627 4628 4629 4630 CONECT 4627 4626 CONECT 4628 4626 CONECT 4629 4626 CONECT 4630 4626 CONECT 4631 4632 4633 4634 4635 CONECT 4632 4631 CONECT 4633 4631 CONECT 4634 4631 CONECT 4635 4631 CONECT 4636 4637 4638 4639 4640 CONECT 4637 4636 CONECT 4638 4636 CONECT 4639 4636 CONECT 4640 4636 CONECT 4641 4642 4643 4644 4645 CONECT 4642 4641 CONECT 4643 4641 CONECT 4644 4641 CONECT 4645 4641 CONECT 4646 4647 4648 4649 4650 CONECT 4647 4646 CONECT 4648 4646 CONECT 4649 4646 CONECT 4650 4646 CONECT 4651 4652 4653 4654 4655 CONECT 4652 4651 CONECT 4653 4651 CONECT 4654 4651 CONECT 4655 4651 CONECT 4657 4658 4659 CONECT 4658 4657 CONECT 4659 4657 4660 CONECT 4660 4659 CONECT 4661 4662 4663 CONECT 4662 4661 CONECT 4663 4661 4664 CONECT 4664 4663 CONECT 4665 4666 4667 CONECT 4666 4665 CONECT 4667 4665 4668 CONECT 4668 4667 CONECT 4669 4670 4671 CONECT 4670 4669 CONECT 4671 4669 4672 CONECT 4672 4671 CONECT 4673 4674 4675 4676 CONECT 4674 4673 CONECT 4675 4673 CONECT 4676 4673 CONECT 4677 4678 4679 4680 4684 CONECT 4678 4677 CONECT 4679 4677 CONECT 4680 4677 CONECT 4681 4682 4683 4684 4685 CONECT 4682 4681 CONECT 4683 4681 CONECT 4684 4677 4681 CONECT 4685 4681 4686 CONECT 4686 4685 4687 CONECT 4687 4686 4688 4689 CONECT 4688 4687 4693 CONECT 4689 4687 4690 4691 CONECT 4690 4689 CONECT 4691 4689 4692 4693 CONECT 4692 4691 CONECT 4693 4688 4691 4694 CONECT 4694 4693 4695 4703 CONECT 4695 4694 4696 CONECT 4696 4695 4697 CONECT 4697 4696 4698 4703 CONECT 4698 4697 4699 4700 CONECT 4699 4698 CONECT 4700 4698 4701 CONECT 4701 4700 4702 CONECT 4702 4701 4703 CONECT 4703 4694 4697 4702 CONECT 4704 4705 4706 4707 4708 CONECT 4705 4704 CONECT 4706 4704 CONECT 4707 4704 CONECT 4708 4704 CONECT 4709 4710 4711 4712 4713 CONECT 4710 4709 CONECT 4711 4709 CONECT 4712 4709 CONECT 4713 4709 CONECT 4714 4715 4716 4717 4718 CONECT 4715 4714 CONECT 4716 4714 CONECT 4717 4714 CONECT 4718 4714 CONECT 4719 4720 4721 4722 4723 CONECT 4720 4719 CONECT 4721 4719 CONECT 4722 4719 CONECT 4723 4719 CONECT 4724 4725 4726 4727 4728 CONECT 4725 4724 CONECT 4726 4724 CONECT 4727 4724 CONECT 4728 4724 CONECT 4730 4731 4732 CONECT 4731 4730 CONECT 4732 4730 4733 CONECT 4733 4732 CONECT 4734 4735 4736 4737 CONECT 4735 4734 CONECT 4736 4734 CONECT 4737 4734 MASTER 533 0 25 26 22 0 35 6 4817 2 156 50 END If you find results from this site helpful for your research, please cite one of our papers:
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