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| author | Navan Chauhan <navanchauhan@gmail.com> | 2020-09-11 16:18:38 +0530 |
|---|---|---|
| committer | Navan Chauhan <navanchauhan@gmail.com> | 2020-09-11 16:18:38 +0530 |
| commit | 9dadfdb3332b073aaff508d126e90200ad09868d (patch) | |
| tree | 1578ff007b42b2175691f3dab11566611ec44907 /plip/test/pdb/3r0t.pdb | |
| parent | 004f4513c8cd5cfffbf69484fb39a3d7bc98bd49 (diff) | |
removed downloaded plip
Diffstat (limited to 'plip/test/pdb/3r0t.pdb')
| -rw-r--r-- | plip/test/pdb/3r0t.pdb | 6723 |
1 files changed, 0 insertions, 6723 deletions
diff --git a/plip/test/pdb/3r0t.pdb b/plip/test/pdb/3r0t.pdb deleted file mode 100644 index 5088b4f..0000000 --- a/plip/test/pdb/3r0t.pdb +++ /dev/null @@ -1,6723 +0,0 @@ -HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-MAR-11 3R0T -TITLE CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT IN COMPLEX -TITLE 2 WITH THE INHIBITOR CX-5279 -COMPND MOL_ID: 1; -COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA; -COMPND 3 CHAIN: A; -COMPND 4 FRAGMENT: UNP RESIDUES 1-337; -COMPND 5 SYNONYM: CK II ALPHA; -COMPND 6 EC: 2.7.11.1; -COMPND 7 ENGINEERED: YES -SOURCE MOL_ID: 1; -SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; -SOURCE 3 ORGANISM_COMMON: HUMAN; -SOURCE 4 ORGANISM_TAXID: 9606; -SOURCE 5 GENE: CSNK2A1, CK2A1; -SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; -SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; -SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; -SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7-7 -KEYWDS KINASE, CK2-INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR -KEYWDS 2 COMPLEX -EXPDTA X-RAY DIFFRACTION -AUTHOR R.BATTISTUTTA,E.PAPINUTTO,G.LOLLI,F.PIERRE,M.HADDACH,D.M.RYCKMAN -REVDAT 2 29-OCT-14 3R0T 1 AUTHOR -REVDAT 1 07-DEC-11 3R0T 0 -JRNL AUTH R.BATTISTUTTA,G.COZZA,F.PIERRE,E.PAPINUTTO,G.LOLLI,S.SARNO, -JRNL AUTH 2 S.E.O'BRIEN,A.SIDDIQUI-JAIN,M.HADDACH,K.ANDERES,D.M.RYCKMAN, -JRNL AUTH 3 F.MEGGIO,L.A.PINNA -JRNL TITL UNPRECEDENTED SELECTIVITY AND STRUCTURAL DETERMINANTS OF A -JRNL TITL 2 NEW CLASS OF PROTEIN KINASE CK2 INHIBITORS IN CLINICAL -JRNL TITL 3 TRIALS FOR THE TREATMENT OF CANCER. -JRNL REF BIOCHEMISTRY V. 50 8478 2011 -JRNL REFN ISSN 0006-2960 -JRNL PMID 21870818 -JRNL DOI 10.1021/BI2008382 -REMARK 1 -REMARK 1 REFERENCE 1 -REMARK 1 AUTH G.COZZA,M.MAZZORANA,E.PAPINUTTO,J.BAIN,M.ELLIOTT,G.DI MAIRA, -REMARK 1 AUTH 2 A.GIANONCELLI,M.A.PAGANO,S.SARNO,M.RUZZENE,R.BATTISTUTTA, -REMARK 1 AUTH 3 F.MEGGIO,S.MORO,G.ZAGOTTO,L.A.PINNA -REMARK 1 TITL QUINALIZARIN AS A POTENT, SELECTIVE AND CELL-PERMEABLE -REMARK 1 TITL 2 INHIBITOR OF PROTEIN KINASE CK2. -REMARK 1 REF BIOCHEM.J. V. 421 387 2009 -REMARK 1 REFN ISSN 0264-6021 -REMARK 1 PMID 19432557 -REMARK 1 DOI 10.1042/BJ20090069 -REMARK 2 -REMARK 2 RESOLUTION. 1.75 ANGSTROMS. -REMARK 3 -REMARK 3 REFINEMENT. -REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486) -REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN -REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- -REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, -REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL -REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE -REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM -REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, -REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER -REMARK 3 : ZWART -REMARK 3 -REMARK 3 REFINEMENT TARGET : ML -REMARK 3 -REMARK 3 DATA USED IN REFINEMENT. -REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 -REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.18 -REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 -REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4 -REMARK 3 NUMBER OF REFLECTIONS : 28526 -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT. -REMARK 3 R VALUE (WORKING + TEST SET) : 0.163 -REMARK 3 R VALUE (WORKING SET) : 0.160 -REMARK 3 FREE R VALUE : 0.211 -REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 -REMARK 3 FREE R VALUE TEST SET COUNT : 1420 -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 35.1842 - 3.7690 0.99 3103 165 0.1437 0.1687 -REMARK 3 2 3.7690 - 2.9920 0.99 3026 162 0.1456 0.1894 -REMARK 3 3 2.9920 - 2.6140 1.00 3033 153 0.1662 0.2429 -REMARK 3 4 2.6140 - 2.3750 0.99 2975 179 0.1725 0.2541 -REMARK 3 5 2.3750 - 2.2048 0.99 3009 152 0.1654 0.2217 -REMARK 3 6 2.2048 - 2.0749 0.97 2927 145 0.1638 0.2257 -REMARK 3 7 2.0749 - 1.9710 0.92 2782 140 0.1662 0.2278 -REMARK 3 8 1.9710 - 1.8852 0.85 2580 129 0.1825 0.2350 -REMARK 3 9 1.8852 - 1.8126 0.71 2123 113 0.2041 0.2279 -REMARK 3 10 1.8126 - 1.7500 0.51 1548 82 0.2385 0.3005 -REMARK 3 -REMARK 3 BULK SOLVENT MODELLING. -REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL -REMARK 3 SOLVENT RADIUS : 1.10 -REMARK 3 SHRINKAGE RADIUS : 0.83 -REMARK 3 K_SOL : 0.37 -REMARK 3 B_SOL : 38.79 -REMARK 3 -REMARK 3 ERROR ESTIMATES. -REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200 -REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.080 -REMARK 3 -REMARK 3 B VALUES. -REMARK 3 FROM WILSON PLOT (A**2) : 17.83 -REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.07 -REMARK 3 OVERALL ANISOTROPIC B VALUE. -REMARK 3 B11 (A**2) : -6.30980 -REMARK 3 B22 (A**2) : 3.47990 -REMARK 3 B33 (A**2) : 2.82990 -REMARK 3 B12 (A**2) : 0.00000 -REMARK 3 B13 (A**2) : -1.16510 -REMARK 3 B23 (A**2) : -0.00000 -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 : 0.007 2946 -REMARK 3 ANGLE : 1.036 3976 -REMARK 3 CHIRALITY : 0.075 406 -REMARK 3 PLANARITY : 0.005 501 -REMARK 3 DIHEDRAL : 13.608 1109 -REMARK 3 -REMARK 3 TLS DETAILS -REMARK 3 NUMBER OF TLS GROUPS : 9 -REMARK 3 TLS GROUP : 1 -REMARK 3 SELECTION: (chain A and resid 3:13) -REMARK 3 ORIGIN FOR THE GROUP (A): 1.4641 -55.6146 14.6268 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1667 T22: 0.1553 -REMARK 3 T33: 0.2001 T12: -0.0541 -REMARK 3 T13: 0.0353 T23: -0.0565 -REMARK 3 L TENSOR -REMARK 3 L11: 0.0564 L22: 0.0078 -REMARK 3 L33: 0.0150 L12: 0.0243 -REMARK 3 L13: 0.0083 L23: -0.0003 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0120 S12: 0.0526 S13: -0.0471 -REMARK 3 S21: -0.0062 S22: 0.0860 S23: -0.0703 -REMARK 3 S31: -0.0106 S32: -0.0466 S33: 0.0000 -REMARK 3 TLS GROUP : 2 -REMARK 3 SELECTION: (chain A and resid 14:32) -REMARK 3 ORIGIN FOR THE GROUP (A): 20.9593 -56.5547 8.8193 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2184 T22: 0.1470 -REMARK 3 T33: 0.3446 T12: 0.0235 -REMARK 3 T13: 0.0536 T23: -0.0858 -REMARK 3 L TENSOR -REMARK 3 L11: 0.0139 L22: 0.0999 -REMARK 3 L33: 0.0686 L12: -0.0127 -REMARK 3 L13: 0.0311 L23: -0.0074 -REMARK 3 S TENSOR -REMARK 3 S11: -0.2488 S12: 0.1931 S13: -0.1999 -REMARK 3 S21: -0.0211 S22: 0.0957 S23: -0.1243 -REMARK 3 S31: 0.1808 S32: 0.1616 S33: -0.0000 -REMARK 3 TLS GROUP : 3 -REMARK 3 SELECTION: (chain A and resid 33:51) -REMARK 3 ORIGIN FOR THE GROUP (A): 33.0192 -34.0681 15.6464 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1317 T22: 0.2292 -REMARK 3 T33: 0.2319 T12: -0.0256 -REMARK 3 T13: 0.0088 T23: -0.0750 -REMARK 3 L TENSOR -REMARK 3 L11: 0.0751 L22: 0.1045 -REMARK 3 L33: 0.1087 L12: -0.0117 -REMARK 3 L13: 0.0879 L23: 0.0255 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0732 S12: 0.0348 S13: -0.0756 -REMARK 3 S21: -0.0804 S22: -0.1905 S23: 0.2135 -REMARK 3 S31: -0.0276 S32: 0.0701 S33: -0.0001 -REMARK 3 TLS GROUP : 4 -REMARK 3 SELECTION: (chain A and resid 52:71) -REMARK 3 ORIGIN FOR THE GROUP (A): 32.1118 -31.5914 11.3104 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1156 T22: 0.2072 -REMARK 3 T33: 0.1295 T12: -0.0180 -REMARK 3 T13: -0.0353 T23: -0.0043 -REMARK 3 L TENSOR -REMARK 3 L11: 0.0728 L22: 0.0127 -REMARK 3 L33: 0.0385 L12: -0.0320 -REMARK 3 L13: -0.0050 L23: 0.0035 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0461 S12: 0.1432 S13: 0.2397 -REMARK 3 S21: -0.1383 S22: 0.0626 S23: 0.0589 -REMARK 3 S31: 0.0279 S32: -0.0798 S33: 0.0007 -REMARK 3 TLS GROUP : 5 -REMARK 3 SELECTION: (chain A and resid 72:102) -REMARK 3 ORIGIN FOR THE GROUP (A): 24.7116 -44.4796 11.8194 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1217 T22: 0.1772 -REMARK 3 T33: 0.1597 T12: 0.0066 -REMARK 3 T13: -0.0140 T23: -0.0266 -REMARK 3 L TENSOR -REMARK 3 L11: 0.1791 L22: 0.2326 -REMARK 3 L33: 0.1170 L12: 0.1641 -REMARK 3 L13: 0.0026 L23: 0.1089 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0039 S12: -0.1009 S13: -0.1852 -REMARK 3 S21: 0.0915 S22: 0.0280 S23: -0.1044 -REMARK 3 S31: 0.0618 S32: 0.0149 S33: -0.0000 -REMARK 3 TLS GROUP : 6 -REMARK 3 SELECTION: (chain A and resid 103:139) -REMARK 3 ORIGIN FOR THE GROUP (A): 15.9998 -29.1819 10.8388 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1312 T22: 0.1502 -REMARK 3 T33: 0.1780 T12: 0.0178 -REMARK 3 T13: -0.0068 T23: -0.0057 -REMARK 3 L TENSOR -REMARK 3 L11: 0.0500 L22: 0.0814 -REMARK 3 L33: 0.2482 L12: -0.0064 -REMARK 3 L13: -0.0006 L23: -0.1427 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0048 S12: 0.0020 S13: 0.2493 -REMARK 3 S21: 0.0802 S22: 0.0149 S23: -0.1391 -REMARK 3 S31: -0.0785 S32: -0.0440 S33: 0.0000 -REMARK 3 TLS GROUP : 7 -REMARK 3 SELECTION: (chain A and resid 140:224) -REMARK 3 ORIGIN FOR THE GROUP (A): 9.9353 -41.3947 15.1453 -REMARK 3 T TENSOR -REMARK 3 T11: 0.0934 T22: 0.0745 -REMARK 3 T33: 0.1054 T12: -0.0020 -REMARK 3 T13: -0.0027 T23: -0.0197 -REMARK 3 L TENSOR -REMARK 3 L11: 0.5752 L22: 0.4700 -REMARK 3 L33: 0.2096 L12: 0.0653 -REMARK 3 L13: -0.1833 L23: -0.2846 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0428 S12: 0.1121 S13: -0.0482 -REMARK 3 S21: 0.0253 S22: 0.0386 S23: -0.1052 -REMARK 3 S31: 0.0006 S32: -0.0174 S33: 0.0000 -REMARK 3 TLS GROUP : 8 -REMARK 3 SELECTION: (chain A and resid 225:247) -REMARK 3 ORIGIN FOR THE GROUP (A): 0.7560 -31.9870 26.3692 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1549 T22: 0.0805 -REMARK 3 T33: 0.1055 T12: 0.0151 -REMARK 3 T13: -0.0151 T23: 0.0012 -REMARK 3 L TENSOR -REMARK 3 L11: 0.1356 L22: 0.0378 -REMARK 3 L33: 0.0555 L12: -0.0798 -REMARK 3 L13: 0.0674 L23: -0.0466 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0772 S12: 0.0027 S13: 0.1597 -REMARK 3 S21: 0.1155 S22: 0.0023 S23: -0.1846 -REMARK 3 S31: -0.0997 S32: -0.0487 S33: -0.0003 -REMARK 3 TLS GROUP : 9 -REMARK 3 SELECTION: (chain A and resid 248:329) -REMARK 3 ORIGIN FOR THE GROUP (A): -5.9085 -37.9654 18.3039 -REMARK 3 T TENSOR -REMARK 3 T11: 0.0920 T22: 0.1009 -REMARK 3 T33: 0.0675 T12: -0.0082 -REMARK 3 T13: -0.0036 T23: 0.0107 -REMARK 3 L TENSOR -REMARK 3 L11: 0.4401 L22: 0.2274 -REMARK 3 L33: 0.3372 L12: -0.1399 -REMARK 3 L13: -0.2005 L23: -0.0276 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0103 S12: 0.1025 S13: -0.0126 -REMARK 3 S21: 0.0164 S22: 0.0378 S23: -0.0172 -REMARK 3 S31: 0.0227 S32: -0.1320 S33: 0.0000 -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 3R0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 -REMARK 100 -REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-11. -REMARK 100 THE RCSB ID CODE IS RCSB064346. -REMARK 200 -REMARK 200 EXPERIMENTAL DETAILS -REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION -REMARK 200 DATE OF DATA COLLECTION : 30-OCT-10 -REMARK 200 TEMPERATURE (KELVIN) : 100 -REMARK 200 PH : 8.5 -REMARK 200 NUMBER OF CRYSTALS USED : 1 -REMARK 200 -REMARK 200 SYNCHROTRON (Y/N) : Y -REMARK 200 RADIATION SOURCE : ELETTRA -REMARK 200 BEAMLINE : 5.2R -REMARK 200 X-RAY GENERATOR MODEL : NULL -REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M -REMARK 200 WAVELENGTH OR RANGE (A) : 1 -REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI111 -REMARK 200 OPTICS : MIRRORS -REMARK 200 -REMARK 200 DETECTOR TYPE : PIXEL -REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M -REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS -REMARK 200 DATA SCALING SOFTWARE : SCALA -REMARK 200 -REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28551 -REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 -REMARK 200 RESOLUTION RANGE LOW (A) : 46.180 -REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL -REMARK 200 -REMARK 200 OVERALL. -REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6 -REMARK 200 DATA REDUNDANCY : 2.800 -REMARK 200 R MERGE (I) : 0.08300 -REMARK 200 R SYM (I) : NULL -REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000 -REMARK 200 -REMARK 200 IN THE HIGHEST RESOLUTION SHELL. -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 -REMARK 200 COMPLETENESS FOR SHELL (%) : 57.4 -REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 -REMARK 200 R MERGE FOR SHELL (I) : 0.46200 -REMARK 200 R SYM FOR SHELL (I) : 0.46200 -REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700 -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: PDB ENTRY 2PVR -REMARK 200 -REMARK 200 REMARK: NULL -REMARK 280 -REMARK 280 CRYSTAL -REMARK 280 SOLVENT CONTENT, VS (%): 37.63 -REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97 -REMARK 280 -REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4000, 0.2M LI2SO4, 0.1M TRIS -REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY -REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 -REMARK 290 -REMARK 290 SYMOP SYMMETRY -REMARK 290 NNNMMM OPERATOR -REMARK 290 1555 X,Y,Z -REMARK 290 2555 -X,Y+1/2,-Z -REMARK 290 -REMARK 290 WHERE NNN -> OPERATOR NUMBER -REMARK 290 MMM -> TRANSLATION VECTOR -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS -REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM -REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY -REMARK 290 RELATED MOLECULES. -REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 -REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 -REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 23.09200 -REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 -REMARK 290 -REMARK 290 REMARK: NULL -REMARK 300 -REMARK 300 BIOMOLECULE: 1 -REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM -REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN -REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON -REMARK 300 BURIED SURFACE AREA. -REMARK 350 -REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN -REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE -REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS -REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND -REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. -REMARK 350 -REMARK 350 BIOMOLECULE: 1 -REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC -REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC -REMARK 350 SOFTWARE USED: PISA -REMARK 350 APPLY THE FOLLOWING TO CHAINS: A -REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 -REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 -REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 -REMARK 465 -REMARK 465 MISSING RESIDUES -REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE -REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN -REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) -REMARK 465 -REMARK 465 M RES C SSSEQI -REMARK 465 MET A 1 -REMARK 465 SER A 2 -REMARK 465 ASP A 330 -REMARK 465 GLN A 331 -REMARK 465 ALA A 332 -REMARK 465 ARG A 333 -REMARK 465 MET A 334 -REMARK 465 GLY A 335 -REMARK 465 SER A 336 -REMARK 465 SER A 337 -REMARK 480 -REMARK 480 ZERO OCCUPANCY ATOM -REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO -REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS -REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; -REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): -REMARK 480 M RES C SSEQI ATOMS -REMARK 480 VAL A 66 CA CB CG1 CG2 -REMARK 480 MET A 137 CA CB CG SD CE -REMARK 480 MET A 150 CA CB CG SD CE -REMARK 480 SER A 194 CA CB OG -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 PRO A 72 7.31 -63.10 -REMARK 500 LYS A 74 171.94 77.25 -REMARK 500 LYS A 75 -94.80 -122.48 -REMARK 500 ASP A 156 41.13 -151.35 -REMARK 500 ASP A 175 76.09 53.05 -REMARK 500 ALA A 193 155.33 68.87 -REMARK 500 MET A 208 54.56 -92.13 -REMARK 500 HIS A 234 73.11 -103.07 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 525 -REMARK 525 SOLVENT -REMARK 525 -REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT -REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST -REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT -REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE -REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; -REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE -REMARK 525 NUMBER; I=INSERTION CODE): -REMARK 525 -REMARK 525 M RES CSSEQI -REMARK 525 HOH A 630 DISTANCE = 5.37 ANGSTROMS -REMARK 525 HOH A 658 DISTANCE = 5.17 ANGSTROMS -REMARK 800 -REMARK 800 SITE -REMARK 800 SITE_IDENTIFIER: AC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU9 A 338 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 339 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC3 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 340 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC4 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 341 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC5 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 342 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC6 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 343 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC7 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 344 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC8 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 345 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC9 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 346 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 347 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 348 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC3 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 349 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC4 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 350 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC5 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 351 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC6 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 352 -REMARK 900 -REMARK 900 RELATED ENTRIES -REMARK 900 RELATED ID: 3PE1 RELATED DB: PDB -REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT -REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-4945 -REMARK 900 RELATED ID: 3PE2 RELATED DB: PDB -REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT -REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-5011 -DBREF 3R0T A 1 337 UNP P68400 CSK21_HUMAN 1 337 -SEQRES 1 A 337 MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR -SEQRES 2 A 337 ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR -SEQRES 3 A 337 GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR -SEQRES 4 A 337 GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU -SEQRES 5 A 337 VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL -SEQRES 6 A 337 VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE -SEQRES 7 A 337 LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY -SEQRES 8 A 337 PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO -SEQRES 9 A 337 VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN -SEQRES 10 A 337 ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP -SEQRES 11 A 337 TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA -SEQRES 12 A 337 LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP -SEQRES 13 A 337 VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG -SEQRES 14 A 337 LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR -SEQRES 15 A 337 HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG -SEQRES 16 A 337 TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET -SEQRES 17 A 337 TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET -SEQRES 18 A 337 LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS -SEQRES 19 A 337 GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS -SEQRES 20 A 337 VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS -SEQRES 21 A 337 TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU -SEQRES 22 A 337 GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS -SEQRES 23 A 337 SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP -SEQRES 24 A 337 PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG -SEQRES 25 A 337 LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR -SEQRES 26 A 337 THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER SER -HET FU9 A 338 32 -HET SO4 A 339 5 -HET SO4 A 340 5 -HET SO4 A 341 5 -HET SO4 A 342 5 -HET PEG A 343 7 -HET EDO A 344 4 -HET EDO A 345 4 -HET EDO A 346 4 -HET EDO A 347 4 -HET EDO A 348 4 -HET EDO A 349 4 -HET EDO A 350 4 -HET EDO A 351 4 -HET EDO A 352 4 -HETNAM FU9 3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL) -HETNAM 2 FU9 PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC -HETNAM 3 FU9 ACID -HETNAM SO4 SULFATE ION -HETNAM PEG DI(HYDROXYETHYL)ETHER -HETNAM EDO 1,2-ETHANEDIOL -HETSYN FU9 CX-5279 -HETSYN EDO ETHYLENE GLYCOL -FORMUL 2 FU9 C22 H16 F3 N5 O2 -FORMUL 3 SO4 4(O4 S 2-) -FORMUL 7 PEG C4 H10 O3 -FORMUL 8 EDO 9(C2 H6 O2) -FORMUL 17 HOH *334(H2 O) -HELIX 1 1 PRO A 20 ASP A 25 1 6 -HELIX 2 2 TYR A 26 HIS A 29 5 4 -HELIX 3 3 ASN A 35 ASP A 37 5 3 -HELIX 4 4 LYS A 76 ARG A 89 1 14 -HELIX 5 5 ASP A 120 TYR A 125 1 6 -HELIX 6 6 THR A 129 MET A 150 1 22 -HELIX 7 7 LYS A 158 HIS A 160 5 3 -HELIX 8 8 ASP A 175 ALA A 179 5 5 -HELIX 9 9 SER A 194 LYS A 198 5 5 -HELIX 10 10 GLY A 199 VAL A 204 1 6 -HELIX 11 11 TYR A 211 ARG A 228 1 18 -HELIX 12 12 ASP A 237 GLY A 250 1 14 -HELIX 13 13 GLY A 250 TYR A 261 1 12 -HELIX 14 14 ASP A 266 ILE A 272 5 7 -HELIX 15 15 ARG A 280 VAL A 285 5 6 -HELIX 16 16 ASN A 289 VAL A 293 5 5 -HELIX 17 17 SER A 294 LEU A 305 1 12 -HELIX 18 18 ASP A 308 ARG A 312 5 5 -HELIX 19 19 THR A 314 GLU A 320 1 7 -HELIX 20 20 HIS A 321 TYR A 325 5 5 -SHEET 1 A 5 TYR A 39 ARG A 47 0 -SHEET 2 A 5 SER A 51 ASN A 58 -1 O VAL A 53 N LEU A 45 -SHEET 3 A 5 LYS A 64 LEU A 70 -1 O VAL A 65 N ALA A 56 -SHEET 4 A 5 THR A 108 GLU A 114 -1 O LEU A 111 N LYS A 68 -SHEET 5 A 5 LEU A 97 ASP A 103 -1 N VAL A 101 O ALA A 110 -SHEET 1 B 2 ILE A 152 MET A 153 0 -SHEET 2 B 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153 -SHEET 1 C 2 VAL A 162 ASP A 165 0 -SHEET 2 C 2 LYS A 170 LEU A 173 -1 O LYS A 170 N ASP A 165 -CISPEP 1 GLU A 230 PRO A 231 0 1.13 -SITE 1 AC1 20 LEU A 45 GLY A 46 ARG A 47 VAL A 53 -SITE 2 AC1 20 VAL A 66 LYS A 68 PHE A 113 GLU A 114 -SITE 3 AC1 20 HIS A 115 VAL A 116 ASN A 118 MET A 163 -SITE 4 AC1 20 ILE A 174 ASP A 175 EDO A 345 EDO A 351 -SITE 5 AC1 20 HOH A 370 HOH A 381 HOH A 616 HOH A 636 -SITE 1 AC2 6 ARG A 80 ARG A 155 ASN A 189 VAL A 192 -SITE 2 AC2 6 HOH A 369 HOH A 677 -SITE 1 AC3 4 ARG A 191 LYS A 198 ASN A 238 PEG A 343 -SITE 1 AC4 8 ASP A 253 ARG A 278 ARG A 306 TYR A 307 -SITE 2 AC4 8 ASP A 308 HOH A 397 HOH A 442 HOH A 465 -SITE 1 AC5 5 LYS A 170 ARG A 172 HOH A 428 HOH A 463 -SITE 2 AC5 5 HOH A 649 -SITE 1 AC6 6 SER A 194 ARG A 195 TYR A 196 SO4 A 340 -SITE 2 AC6 6 HOH A 433 HOH A 619 -SITE 1 AC7 6 GLN A 36 TYR A 39 VAL A 101 ASP A 103 -SITE 2 AC7 6 PRO A 104 ARG A 280 -SITE 1 AC8 6 ASN A 118 ASP A 120 HIS A 160 FU9 A 338 -SITE 2 AC8 6 EDO A 348 EDO A 351 -SITE 1 AC9 4 ASP A 37 PRO A 295 HIS A 321 HOH A 620 -SITE 1 BC1 5 PHE A 232 HOH A 372 HOH A 573 HOH A 621 -SITE 2 BC1 5 HOH A 668 -SITE 1 BC2 9 ASN A 118 THR A 119 ASP A 120 PHE A 121 -SITE 2 BC2 9 PRO A 159 VAL A 162 MET A 163 ILE A 164 -SITE 3 BC2 9 EDO A 345 -SITE 1 BC3 6 LYS A 158 HIS A 160 SER A 194 EDO A 350 -SITE 2 BC3 6 HOH A 618 HOH A 619 -SITE 1 BC4 5 PRO A 159 PHE A 197 GLU A 230 EDO A 349 -SITE 2 BC4 5 HOH A 618 -SITE 1 BC5 5 ASN A 118 FU9 A 338 EDO A 345 HOH A 455 -SITE 2 BC5 5 HOH A 575 -SITE 1 BC6 7 PRO A 104 ARG A 278 LYS A 279 ASP A 302 -SITE 2 BC6 7 HOH A 531 HOH A 642 HOH A 679 -CRYST1 58.352 46.184 63.300 90.00 111.51 90.00 P 1 21 1 2 -ORIGX1 1.000000 0.000000 0.000000 0.00000 -ORIGX2 0.000000 1.000000 0.000000 0.00000 -ORIGX3 0.000000 0.000000 1.000000 0.00000 -SCALE1 0.017137 0.000000 0.006753 0.00000 -SCALE2 0.000000 0.021653 0.000000 0.00000 -SCALE3 0.000000 0.000000 0.016980 0.00000 -ATOM 1 N GLY A 3 -1.502 -62.453 29.985 1.00 40.82 N -ANISOU 1 N GLY A 3 5111 4857 5540 -349 80 -403 N -ATOM 2 CA GLY A 3 -0.651 -61.305 29.715 1.00 44.52 C -ANISOU 2 CA GLY A 3 5587 5318 6013 -345 98 -421 C -ATOM 3 C GLY A 3 -1.188 -60.418 28.604 1.00 39.81 C -ANISOU 3 C GLY A 3 4994 4745 5387 -353 122 -411 C -ATOM 4 O GLY A 3 -2.322 -60.588 28.164 1.00 36.32 O -ANISOU 4 O GLY A 3 4552 4328 4919 -359 125 -385 O -ATOM 5 N PRO A 4 -0.368 -59.467 28.133 1.00 38.43 N -ANISOU 5 N PRO A 4 4823 4562 5216 -353 140 -431 N -ATOM 6 CA PRO A 4 -0.839 -58.542 27.100 1.00 28.04 C -ANISOU 6 CA PRO A 4 3512 3269 3872 -360 164 -421 C -ATOM 7 C PRO A 4 -1.077 -59.249 25.772 1.00 26.24 C -ANISOU 7 C PRO A 4 3274 3054 3640 -386 172 -431 C -ATOM 8 O PRO A 4 -0.480 -60.287 25.482 1.00 29.56 O -ANISOU 8 O PRO A 4 3684 3461 4086 -400 164 -457 O -ATOM 9 CB PRO A 4 0.313 -57.540 26.978 1.00 34.55 C -ANISOU 9 CB PRO A 4 4342 4077 4709 -355 178 -446 C -ATOM 10 CG PRO A 4 1.524 -58.326 27.371 1.00 39.33 C -ANISOU 10 CG PRO A 4 4939 4652 5354 -358 165 -481 C -ATOM 11 CD PRO A 4 1.055 -59.258 28.461 1.00 39.89 C -ANISOU 11 CD PRO A 4 5007 4717 5431 -349 140 -465 C -ATOM 12 N VAL A 5 -1.971 -58.679 24.977 1.00 21.32 N -ANISOU 12 N VAL A 5 2656 2459 2987 -392 188 -409 N -ATOM 13 CA VAL A 5 -2.286 -59.191 23.656 1.00 25.36 C -ANISOU 13 CA VAL A 5 3158 2986 3490 -416 198 -415 C -ATOM 14 C VAL A 5 -1.179 -58.723 22.726 1.00 20.62 C -ANISOU 14 C VAL A 5 2556 2376 2904 -429 216 -450 C -ATOM 15 O VAL A 5 -0.725 -57.591 22.846 1.00 22.01 O -ANISOU 15 O VAL A 5 2740 2547 3076 -418 228 -453 O -ATOM 16 CB VAL A 5 -3.629 -58.612 23.180 1.00 14.07 C -ANISOU 16 CB VAL A 5 1735 1590 2021 -416 209 -378 C -ATOM 17 CG1 VAL A 5 -3.854 -58.886 21.709 1.00 17.54 C -ANISOU 17 CG1 VAL A 5 2167 2047 2450 -442 224 -386 C -ATOM 18 CG2 VAL A 5 -4.773 -59.147 24.037 1.00 23.46 C -ANISOU 18 CG2 VAL A 5 2926 2792 3196 -405 192 -344 C -ATOM 19 N PRO A 6 -0.720 -59.591 21.809 1.00 19.05 N -ANISOU 19 N PRO A 6 2345 2173 2721 -451 218 -477 N -ATOM 20 CA PRO A 6 0.332 -59.161 20.879 1.00 22.26 C -ANISOU 20 CA PRO A 6 2749 2571 3140 -464 235 -511 C -ATOM 21 C PRO A 6 -0.180 -58.203 19.796 1.00 19.43 C -ANISOU 21 C PRO A 6 2395 2237 2751 -473 259 -498 C -ATOM 22 O PRO A 6 -1.380 -58.098 19.579 1.00 23.70 O -ANISOU 22 O PRO A 6 2938 2804 3262 -474 262 -466 O -ATOM 23 CB PRO A 6 0.816 -60.479 20.258 1.00 22.71 C -ANISOU 23 CB PRO A 6 2791 2618 3221 -486 229 -541 C -ATOM 24 CG PRO A 6 -0.334 -61.414 20.398 1.00 24.95 C -ANISOU 24 CG PRO A 6 3071 2918 3492 -490 215 -515 C -ATOM 25 CD PRO A 6 -1.050 -61.022 21.661 1.00 24.62 C -ANISOU 25 CD PRO A 6 3039 2879 3436 -465 203 -481 C -ATOM 26 N SER A 7 0.745 -57.506 19.142 1.00 17.65 N -ANISOU 26 N SER A 7 2170 2004 2534 -480 276 -524 N -ATOM 27 CA SER A 7 0.417 -56.544 18.097 1.00 16.35 C -ANISOU 27 CA SER A 7 2008 1861 2343 -488 300 -515 C -ATOM 28 C SER A 7 1.444 -56.657 16.984 1.00 20.63 C -ANISOU 28 C SER A 7 2542 2394 2901 -510 313 -554 C -ATOM 29 O SER A 7 2.597 -57.000 17.244 1.00 20.28 O -ANISOU 29 O SER A 7 2493 2324 2888 -510 307 -587 O -ATOM 30 CB SER A 7 0.466 -55.121 18.661 1.00 17.57 C -ANISOU 30 CB SER A 7 2177 2015 2485 -467 308 -500 C -ATOM 31 OG SER A 7 0.286 -54.152 17.636 1.00 19.00 O -ANISOU 31 OG SER A 7 2361 2214 2643 -476 331 -495 O -ATOM 32 N ARG A 8 1.025 -56.363 15.754 1.00 20.45 N -ANISOU 32 N ARG A 8 2517 2395 2857 -527 331 -550 N -ATOM 33 CA ARG A 8 1.917 -56.328 14.585 1.00 21.97 C -ANISOU 33 CA ARG A 8 2703 2585 3062 -548 347 -584 C -ATOM 34 C ARG A 8 1.691 -55.027 13.836 1.00 21.54 C -ANISOU 34 C ARG A 8 2655 2548 2981 -550 370 -572 C -ATOM 35 O ARG A 8 0.571 -54.501 13.838 1.00 18.25 O -ANISOU 35 O ARG A 8 2246 2155 2534 -544 374 -536 O -ATOM 36 CB ARG A 8 1.572 -57.455 13.608 1.00 29.94 C -ANISOU 36 CB ARG A 8 3698 3606 4070 -574 346 -593 C -ATOM 37 CG ARG A 8 1.835 -58.846 14.104 1.00 37.53 C -ANISOU 37 CG ARG A 8 4651 4551 5059 -577 325 -610 C -ATOM 38 CD ARG A 8 3.325 -59.102 14.202 1.00 40.04 C -ANISOU 38 CD ARG A 8 4963 4838 5414 -580 323 -653 C -ATOM 39 NE ARG A 8 3.601 -60.471 14.624 1.00 40.22 N -ANISOU 39 NE ARG A 8 4975 4844 5464 -584 303 -669 N -ATOM 40 CZ ARG A 8 3.575 -60.878 15.889 1.00 42.42 C -ANISOU 40 CZ ARG A 8 5256 5106 5755 -566 282 -661 C -ATOM 41 NH1 ARG A 8 3.283 -60.018 16.864 1.00 33.21 N -ANISOU 41 NH1 ARG A 8 4102 3938 4577 -542 279 -636 N -ATOM 42 NH2 ARG A 8 3.841 -62.146 16.180 1.00 45.87 N -ANISOU 42 NH2 ARG A 8 5683 5528 6218 -572 264 -677 N -ATOM 43 N ALA A 9 2.731 -54.532 13.165 1.00 15.62 N -ANISOU 43 N ALA A 9 1904 1789 2243 -560 384 -602 N -ATOM 44 CA ALA A 9 2.572 -53.402 12.257 1.00 18.46 C -ANISOU 44 CA ALA A 9 2267 2166 2579 -566 407 -594 C -ATOM 45 C ALA A 9 1.606 -53.796 11.137 1.00 21.46 C -ANISOU 45 C ALA A 9 2642 2578 2936 -587 416 -580 C -ATOM 46 O ALA A 9 1.625 -54.930 10.662 1.00 21.38 O -ANISOU 46 O ALA A 9 2621 2568 2936 -605 409 -595 O -ATOM 47 CB ALA A 9 3.914 -52.996 11.673 1.00 14.16 C -ANISOU 47 CB ALA A 9 1720 1606 2055 -576 420 -633 C -ATOM 48 N ARG A 10 0.762 -52.862 10.709 1.00 13.86 N -ANISOU 48 N ARG A 10 1687 1639 1940 -586 429 -550 N -ATOM 49 CA ARG A 10 -0.195 -53.164 9.653 1.00 16.17 C -ANISOU 49 CA ARG A 10 1974 1962 2208 -605 438 -534 C -ATOM 50 C ARG A 10 0.395 -52.974 8.263 1.00 16.19 C -ANISOU 50 C ARG A 10 1970 1972 2210 -630 457 -560 C -ATOM 51 O ARG A 10 -0.245 -53.311 7.260 1.00 20.93 O -ANISOU 51 O ARG A 10 2563 2595 2793 -649 465 -553 O -ATOM 52 CB ARG A 10 -1.463 -52.325 9.813 1.00 20.15 C -ANISOU 52 CB ARG A 10 2489 2491 2677 -593 443 -489 C -ATOM 53 CG ARG A 10 -2.278 -52.639 11.048 1.00 33.68 C -ANISOU 53 CG ARG A 10 4208 4204 4385 -572 424 -460 C -ATOM 54 CD ARG A 10 -3.552 -51.806 11.037 1.00 41.52 C -ANISOU 54 CD ARG A 10 5211 5224 5342 -563 431 -416 C -ATOM 55 NE ARG A 10 -3.245 -50.409 10.738 1.00 55.14 N -ANISOU 55 NE ARG A 10 6944 6952 7056 -557 450 -413 N -ATOM 56 CZ ARG A 10 -4.138 -49.512 10.325 1.00 57.27 C -ANISOU 56 CZ ARG A 10 7221 7246 7295 -555 463 -382 C -ATOM 57 NH1 ARG A 10 -5.406 -49.859 10.157 1.00 51.33 N -ANISOU 57 NH1 ARG A 10 6468 6519 6518 -558 460 -351 N -ATOM 58 NH2 ARG A 10 -3.756 -48.265 10.082 1.00 58.40 N -ANISOU 58 NH2 ARG A 10 7370 7388 7430 -550 479 -382 N -ATOM 59 N VAL A 11 1.614 -52.434 8.208 1.00 17.69 N -ANISOU 59 N VAL A 11 2160 2142 2420 -629 465 -589 N -ATOM 60 CA VAL A 11 2.346 -52.276 6.954 1.00 18.09 C -ANISOU 60 CA VAL A 11 2203 2196 2474 -652 483 -618 C -ATOM 61 C VAL A 11 3.819 -52.578 7.179 1.00 22.01 C -ANISOU 61 C VAL A 11 2695 2661 3008 -653 479 -661 C -ATOM 62 O VAL A 11 4.294 -52.538 8.311 1.00 20.68 O -ANISOU 62 O VAL A 11 2531 2469 2858 -633 466 -665 O -ATOM 63 CB VAL A 11 2.206 -50.858 6.352 1.00 17.11 C -ANISOU 63 CB VAL A 11 2088 2088 2327 -652 504 -604 C -ATOM 64 CG1 VAL A 11 0.766 -50.601 5.959 1.00 21.02 C -ANISOU 64 CG1 VAL A 11 2586 2615 2785 -654 509 -563 C -ATOM 65 CG2 VAL A 11 2.716 -49.791 7.320 1.00 21.76 C -ANISOU 65 CG2 VAL A 11 2689 2658 2922 -626 504 -600 C -ATOM 66 N TYR A 12 4.526 -52.889 6.097 1.00 17.12 N -ANISOU 66 N TYR A 12 2064 2041 2398 -677 490 -693 N -ATOM 67 CA TYR A 12 5.951 -53.168 6.155 1.00 19.55 C -ANISOU 67 CA TYR A 12 2367 2322 2741 -681 488 -736 C -ATOM 68 C TYR A 12 6.273 -54.144 7.269 1.00 21.70 C -ANISOU 68 C TYR A 12 2636 2568 3041 -668 465 -747 C -ATOM 69 O TYR A 12 7.320 -54.030 7.919 1.00 22.08 O -ANISOU 69 O TYR A 12 2686 2589 3115 -658 459 -770 O -ATOM 70 CB TYR A 12 6.708 -51.872 6.405 1.00 15.19 C -ANISOU 70 CB TYR A 12 1824 1757 2191 -668 499 -742 C -ATOM 71 CG TYR A 12 6.436 -50.806 5.380 1.00 18.71 C -ANISOU 71 CG TYR A 12 2273 2225 2610 -678 522 -731 C -ATOM 72 CD1 TYR A 12 6.473 -51.100 4.028 1.00 19.73 C -ANISOU 72 CD1 TYR A 12 2393 2372 2733 -706 535 -746 C -ATOM 73 CD2 TYR A 12 6.138 -49.507 5.764 1.00 17.74 C -ANISOU 73 CD2 TYR A 12 2163 2107 2469 -660 529 -705 C -ATOM 74 CE1 TYR A 12 6.241 -50.128 3.081 1.00 18.96 C -ANISOU 74 CE1 TYR A 12 2298 2296 2611 -716 556 -735 C -ATOM 75 CE2 TYR A 12 5.887 -48.528 4.829 1.00 21.09 C -ANISOU 75 CE2 TYR A 12 2591 2553 2869 -670 550 -694 C -ATOM 76 CZ TYR A 12 5.938 -48.849 3.485 1.00 16.76 C -ANISOU 76 CZ TYR A 12 2033 2022 2315 -697 563 -709 C -ATOM 77 OH TYR A 12 5.705 -47.877 2.541 1.00 22.86 O -ANISOU 77 OH TYR A 12 2808 2815 3064 -707 583 -699 O -ATOM 78 N THR A 13 5.373 -55.095 7.495 1.00 19.83 N -ANISOU 78 N THR A 13 2396 2342 2799 -670 451 -729 N -ATOM 79 CA THR A 13 5.482 -55.969 8.655 1.00 22.60 C -ANISOU 79 CA THR A 13 2745 2671 3172 -656 428 -732 C -ATOM 80 C THR A 13 6.719 -56.847 8.586 1.00 25.56 C -ANISOU 80 C THR A 13 3108 3019 3583 -666 421 -776 C -ATOM 81 O THR A 13 7.417 -57.034 9.587 1.00 24.25 O -ANISOU 81 O THR A 13 2944 2827 3443 -651 408 -789 O -ATOM 82 CB THR A 13 4.245 -56.876 8.814 1.00 20.97 C -ANISOU 82 CB THR A 13 2535 2481 2950 -658 415 -704 C -ATOM 83 OG1 THR A 13 3.054 -56.090 8.692 1.00 26.40 O -ANISOU 83 OG1 THR A 13 3232 3196 3601 -652 423 -664 O -ATOM 84 CG2 THR A 13 4.268 -57.546 10.168 1.00 18.64 C -ANISOU 84 CG2 THR A 13 2241 2165 2674 -639 391 -700 C -ATOM 85 N ASP A 14 7.000 -57.363 7.393 1.00 25.50 N -ANISOU 85 N ASP A 14 3469 2039 4180 -271 566 -1070 N -ATOM 86 CA ASP A 14 8.052 -58.358 7.223 1.00 28.16 C -ANISOU 86 CA ASP A 14 3792 2362 4546 -223 643 -1099 C -ATOM 87 C ASP A 14 9.233 -57.872 6.392 1.00 23.39 C -ANISOU 87 C ASP A 14 3131 1840 3917 -248 629 -1101 C -ATOM 88 O ASP A 14 9.986 -58.690 5.854 1.00 20.94 O -ANISOU 88 O ASP A 14 2805 1531 3619 -234 699 -1140 O -ATOM 89 CB ASP A 14 7.484 -59.634 6.594 1.00 38.57 C -ANISOU 89 CB ASP A 14 5141 3635 5878 -246 740 -1168 C -ATOM 90 CG ASP A 14 6.515 -60.358 7.517 1.00 43.55 C -ANISOU 90 CG ASP A 14 5828 4175 6545 -204 770 -1167 C -ATOM 91 OD1 ASP A 14 6.987 -61.012 8.472 1.00 44.76 O -ANISOU 91 OD1 ASP A 14 5996 4269 6740 -114 800 -1150 O -ATOM 92 OD2 ASP A 14 5.290 -60.274 7.284 1.00 38.57 O -ANISOU 92 OD2 ASP A 14 5227 3530 5899 -259 763 -1184 O -ATOM 93 N VAL A 15 9.409 -56.558 6.296 1.00 22.43 N -ANISOU 93 N VAL A 15 2978 1785 3760 -282 540 -1060 N -ATOM 94 CA VAL A 15 10.496 -56.020 5.487 1.00 22.29 C -ANISOU 94 CA VAL A 15 2906 1849 3715 -310 522 -1060 C -ATOM 95 C VAL A 15 11.853 -56.585 5.890 1.00 24.88 C -ANISOU 95 C VAL A 15 3210 2167 4078 -228 560 -1052 C -ATOM 96 O VAL A 15 12.652 -56.938 5.027 1.00 26.13 O -ANISOU 96 O VAL A 15 3337 2362 4230 -245 605 -1086 O -ATOM 97 CB VAL A 15 10.549 -54.476 5.535 1.00 24.94 C -ANISOU 97 CB VAL A 15 3212 2252 4012 -347 413 -1007 C -ATOM 98 CG1 VAL A 15 9.453 -53.872 4.667 1.00 18.51 C -ANISOU 98 CG1 VAL A 15 2406 1475 3153 -449 382 -1029 C -ATOM 99 CG2 VAL A 15 10.416 -54.002 6.957 1.00 35.48 C -ANISOU 99 CG2 VAL A 15 4565 3547 5369 -277 353 -943 C -ATOM 100 N ASN A 16 12.122 -56.667 7.190 1.00 24.52 N -ANISOU 100 N ASN A 16 3178 2070 4069 -139 543 -1006 N -ATOM 101 CA ASN A 16 13.408 -57.186 7.659 1.00 27.34 C -ANISOU 101 CA ASN A 16 3513 2413 4461 -57 575 -994 C -ATOM 102 C ASN A 16 13.463 -58.705 7.613 1.00 29.82 C -ANISOU 102 C ASN A 16 3853 2662 4813 -17 682 -1045 C -ATOM 103 O ASN A 16 14.539 -59.292 7.465 1.00 31.81 O -ANISOU 103 O ASN A 16 4082 2919 5086 24 730 -1060 O -ATOM 104 CB ASN A 16 13.731 -56.692 9.072 1.00 23.17 C -ANISOU 104 CB ASN A 16 2990 1856 3958 25 514 -925 C -ATOM 105 CG ASN A 16 14.065 -55.224 9.109 1.00 22.63 C -ANISOU 105 CG ASN A 16 2885 1858 3854 -1 412 -872 C -ATOM 106 OD1 ASN A 16 14.844 -54.740 8.294 1.00 24.80 O -ANISOU 106 OD1 ASN A 16 3113 2207 4104 -39 397 -877 O -ATOM 107 ND2 ASN A 16 13.463 -54.498 10.043 1.00 17.96 N -ANISOU 107 ND2 ASN A 16 2315 1246 3262 17 340 -821 N -ATOM 108 N THR A 17 12.298 -59.332 7.744 1.00 34.34 N -ANISOU 108 N THR A 17 4476 3175 5396 -30 718 -1072 N -ATOM 109 CA THR A 17 12.194 -60.784 7.694 1.00 33.88 C -ANISOU 109 CA THR A 17 4448 3050 5373 2 819 -1123 C -ATOM 110 C THR A 17 12.802 -61.307 6.399 1.00 34.28 C -ANISOU 110 C THR A 17 4470 3144 5409 -42 883 -1180 C -ATOM 111 O THR A 17 13.375 -62.394 6.363 1.00 41.50 O -ANISOU 111 O THR A 17 5388 4024 6355 4 961 -1212 O -ATOM 112 CB THR A 17 10.718 -61.231 7.783 1.00 30.25 C -ANISOU 112 CB THR A 17 4043 2534 4916 -29 843 -1148 C -ATOM 113 OG1 THR A 17 10.090 -60.625 8.924 1.00 39.37 O -ANISOU 113 OG1 THR A 17 5224 3655 6079 3 777 -1093 O -ATOM 114 CG2 THR A 17 10.617 -62.750 7.882 1.00 31.13 C -ANISOU 114 CG2 THR A 17 4189 2569 5068 14 945 -1195 C -ATOM 115 N HIS A 18 12.694 -60.512 5.342 1.00 32.28 N -ANISOU 115 N HIS A 18 4187 2968 5108 -129 847 -1193 N -ATOM 116 CA HIS A 18 13.097 -60.948 4.008 1.00 36.98 C -ANISOU 116 CA HIS A 18 4759 3608 5684 -184 905 -1250 C -ATOM 117 C HIS A 18 14.301 -60.203 3.431 1.00 35.82 C -ANISOU 117 C HIS A 18 4552 3547 5513 -200 871 -1235 C -ATOM 118 O HIS A 18 14.665 -60.401 2.272 1.00 33.08 O -ANISOU 118 O HIS A 18 4179 3246 5143 -251 909 -1279 O -ATOM 119 CB HIS A 18 11.904 -60.867 3.061 1.00 37.24 C -ANISOU 119 CB HIS A 18 4813 3656 5682 -282 911 -1292 C -ATOM 120 CG HIS A 18 10.808 -61.825 3.409 1.00 38.02 C -ANISOU 120 CG HIS A 18 4968 3670 5806 -271 964 -1322 C -ATOM 121 ND1 HIS A 18 9.590 -61.419 3.913 1.00 34.86 N -ANISOU 121 ND1 HIS A 18 4605 3241 5401 -292 921 -1302 N -ATOM 122 CD2 HIS A 18 10.758 -63.177 3.347 1.00 35.48 C -ANISOU 122 CD2 HIS A 18 4674 3288 5517 -240 1058 -1369 C -ATOM 123 CE1 HIS A 18 8.830 -62.480 4.128 1.00 35.92 C -ANISOU 123 CE1 HIS A 18 4785 3301 5563 -276 986 -1336 C -ATOM 124 NE2 HIS A 18 9.516 -63.558 3.791 1.00 35.59 N -ANISOU 124 NE2 HIS A 18 4740 3239 5545 -245 1069 -1377 N -ATOM 125 N ARG A 19 14.903 -59.344 4.247 1.00 36.48 N -ANISOU 125 N ARG A 19 4611 3649 5600 -155 799 -1171 N -ATOM 126 CA ARG A 19 16.174 -58.707 3.911 1.00 32.17 C -ANISOU 126 CA ARG A 19 4007 3175 5040 -152 768 -1150 C -ATOM 127 C ARG A 19 17.295 -59.661 4.277 1.00 34.10 C -ANISOU 127 C ARG A 19 4240 3388 5327 -67 832 -1158 C -ATOM 128 O ARG A 19 17.129 -60.485 5.172 1.00 32.12 O -ANISOU 128 O ARG A 19 4025 3059 5119 4 870 -1155 O -ATOM 129 CB ARG A 19 16.353 -57.415 4.714 1.00 27.42 C -ANISOU 129 CB ARG A 19 3388 2603 4428 -134 663 -1076 C -ATOM 130 CG ARG A 19 15.479 -56.258 4.275 1.00 33.58 C -ANISOU 130 CG ARG A 19 4167 3432 5159 -220 586 -1062 C -ATOM 131 CD ARG A 19 16.222 -55.352 3.330 1.00 38.85 C -ANISOU 131 CD ARG A 19 4780 4196 5786 -278 546 -1057 C -ATOM 132 NE ARG A 19 15.389 -54.281 2.794 1.00 42.19 N -ANISOU 132 NE ARG A 19 5201 4668 6159 -366 477 -1049 N -ATOM 133 CZ ARG A 19 15.812 -53.412 1.882 1.00 44.31 C -ANISOU 133 CZ ARG A 19 5427 5023 6385 -431 437 -1047 C -ATOM 134 NH1 ARG A 19 17.053 -53.494 1.411 1.00 41.81 N -ANISOU 134 NH1 ARG A 19 5065 4751 6069 -419 459 -1053 N -ATOM 135 NH2 ARG A 19 15.001 -52.469 1.432 1.00 40.28 N -ANISOU 135 NH2 ARG A 19 4919 4553 5832 -510 375 -1040 N -ATOM 136 N PRO A 20 18.455 -59.541 3.603 1.00 34.02 N -ANISOU 136 N PRO A 20 4181 3439 5308 -73 844 -1166 N -ATOM 137 CA PRO A 20 19.609 -60.329 4.042 1.00 34.71 C -ANISOU 137 CA PRO A 20 4252 3500 5436 12 896 -1166 C -ATOM 138 C PRO A 20 19.906 -60.020 5.504 1.00 37.28 C -ANISOU 138 C PRO A 20 4585 3786 5795 100 845 -1101 C -ATOM 139 O PRO A 20 19.670 -58.899 5.955 1.00 30.21 O -ANISOU 139 O PRO A 20 3682 2916 4880 88 756 -1050 O -ATOM 140 CB PRO A 20 20.755 -59.812 3.162 1.00 33.68 C -ANISOU 140 CB PRO A 20 4059 3457 5281 -17 885 -1168 C -ATOM 141 CG PRO A 20 20.107 -59.121 2.020 1.00 36.39 C -ANISOU 141 CG PRO A 20 4394 3863 5571 -126 857 -1191 C -ATOM 142 CD PRO A 20 18.797 -58.598 2.524 1.00 31.96 C -ANISOU 142 CD PRO A 20 3873 3273 4998 -153 803 -1169 C -ATOM 143 N ARG A 21 20.419 -61.005 6.230 1.00 37.42 N -ANISOU 143 N ARG A 21 4617 3741 5861 188 900 -1104 N -ATOM 144 CA ARG A 21 20.750 -60.838 7.641 1.00 36.04 C -ANISOU 144 CA ARG A 21 4451 3521 5720 278 859 -1046 C -ATOM 145 C ARG A 21 21.672 -59.640 7.898 1.00 32.18 C -ANISOU 145 C ARG A 21 3912 3097 5217 289 775 -987 C -ATOM 146 O ARG A 21 21.509 -58.937 8.888 1.00 30.57 O -ANISOU 146 O ARG A 21 3718 2879 5019 323 703 -930 O -ATOM 147 CB ARG A 21 21.373 -62.126 8.183 1.00 40.30 C -ANISOU 147 CB ARG A 21 5005 3995 6313 367 939 -1064 C -ATOM 148 CG ARG A 21 21.677 -62.128 9.669 1.00 42.05 C -ANISOU 148 CG ARG A 21 5242 4160 6574 466 909 -1009 C -ATOM 149 CD ARG A 21 21.910 -63.551 10.157 1.00 50.92 C -ANISOU 149 CD ARG A 21 6395 5203 7747 543 997 -1038 C -ATOM 150 NE ARG A 21 22.545 -63.597 11.472 1.00 59.73 N -ANISOU 150 NE ARG A 21 7516 6276 8904 643 974 -987 N -ATOM 151 CZ ARG A 21 21.925 -63.936 12.599 1.00 65.53 C -ANISOU 151 CZ ARG A 21 8299 6932 9668 700 971 -965 C -ATOM 152 NH1 ARG A 21 20.638 -64.264 12.586 1.00 68.26 N -ANISOU 152 NH1 ARG A 21 8693 7234 10008 666 990 -988 N -ATOM 153 NH2 ARG A 21 22.597 -63.951 13.743 1.00 65.89 N -ANISOU 153 NH2 ARG A 21 8344 6943 9748 791 948 -919 N -ATOM 154 N GLU A 22 22.639 -59.413 7.011 1.00 26.59 N -ANISOU 154 N GLU A 22 3152 2459 4491 261 782 -1001 N -ATOM 155 CA GLU A 22 23.559 -58.283 7.140 1.00 27.88 C -ANISOU 155 CA GLU A 22 3264 2689 4639 266 705 -949 C -ATOM 156 C GLU A 22 22.824 -56.942 7.224 1.00 26.97 C -ANISOU 156 C GLU A 22 3149 2613 4484 209 606 -908 C -ATOM 157 O GLU A 22 23.340 -55.981 7.798 1.00 29.49 O -ANISOU 157 O GLU A 22 3443 2962 4799 232 528 -850 O -ATOM 158 CB GLU A 22 24.540 -58.252 5.963 1.00 29.37 C -ANISOU 158 CB GLU A 22 3399 2953 4807 226 733 -979 C -ATOM 159 CG GLU A 22 23.853 -58.257 4.602 1.00 47.78 C -ANISOU 159 CG GLU A 22 5732 5326 7096 123 761 -1034 C -ATOM 160 CD GLU A 22 24.822 -58.191 3.430 1.00 62.08 C -ANISOU 160 CD GLU A 22 7489 7212 8885 82 788 -1062 C -ATOM 161 OE1 GLU A 22 26.051 -58.129 3.664 1.00 61.20 O -ANISOU 161 OE1 GLU A 22 7337 7123 8791 134 785 -1039 O -ATOM 162 OE2 GLU A 22 24.347 -58.200 2.270 1.00 65.47 O -ANISOU 162 OE2 GLU A 22 7917 7678 9278 -2 812 -1108 O -ATOM 163 N TYR A 23 21.627 -56.875 6.644 1.00 24.08 N -ANISOU 163 N TYR A 23 2814 2247 4090 134 609 -938 N -ATOM 164 CA TYR A 23 20.863 -55.632 6.635 1.00 18.77 C -ANISOU 164 CA TYR A 23 2143 1612 3378 74 518 -904 C -ATOM 165 C TYR A 23 20.475 -55.171 8.042 1.00 22.62 C -ANISOU 165 C TYR A 23 2658 2051 3884 134 454 -843 C -ATOM 166 O TYR A 23 20.655 -54.005 8.389 1.00 21.90 O -ANISOU 166 O TYR A 23 2546 2000 3774 127 365 -790 O -ATOM 167 CB TYR A 23 19.615 -55.749 5.751 1.00 19.50 C -ANISOU 167 CB TYR A 23 2264 1707 3438 -15 540 -951 C -ATOM 168 CG TYR A 23 18.807 -54.468 5.689 1.00 20.47 C -ANISOU 168 CG TYR A 23 2389 1870 3518 -80 448 -919 C -ATOM 169 CD1 TYR A 23 19.171 -53.446 4.831 1.00 24.15 C -ANISOU 169 CD1 TYR A 23 2811 2426 3940 -149 396 -911 C -ATOM 170 CD2 TYR A 23 17.690 -54.278 6.500 1.00 19.19 C -ANISOU 170 CD2 TYR A 23 2273 1656 3361 -71 412 -895 C -ATOM 171 CE1 TYR A 23 18.454 -52.260 4.772 1.00 18.81 C -ANISOU 171 CE1 TYR A 23 2136 1786 3224 -208 310 -880 C -ATOM 172 CE2 TYR A 23 16.961 -53.090 6.454 1.00 17.09 C -ANISOU 172 CE2 TYR A 23 2008 1427 3057 -129 326 -865 C -ATOM 173 CZ TYR A 23 17.351 -52.083 5.582 1.00 17.84 C -ANISOU 173 CZ TYR A 23 2059 1612 3108 -198 275 -857 C -ATOM 174 OH TYR A 23 16.655 -50.893 5.497 1.00 17.48 O -ANISOU 174 OH TYR A 23 2013 1606 3022 -257 189 -828 O -ATOM 175 N TRP A 24 19.940 -56.087 8.844 1.00 21.93 N -ANISOU 175 N TRP A 24 2620 1877 3835 191 499 -852 N -ATOM 176 CA TRP A 24 19.401 -55.725 10.162 1.00 21.58 C -ANISOU 176 CA TRP A 24 2610 1780 3809 243 444 -799 C -ATOM 177 C TRP A 24 20.253 -56.195 11.353 1.00 22.11 C -ANISOU 177 C TRP A 24 2679 1795 3925 355 454 -765 C -ATOM 178 O TRP A 24 20.078 -55.721 12.479 1.00 19.22 O -ANISOU 178 O TRP A 24 2332 1398 3573 404 396 -711 O -ATOM 179 CB TRP A 24 17.965 -56.241 10.304 1.00 20.96 C -ANISOU 179 CB TRP A 24 2590 1640 3734 221 472 -825 C -ATOM 180 CG TRP A 24 17.844 -57.693 10.030 1.00 20.25 C -ANISOU 180 CG TRP A 24 2526 1494 3673 240 579 -885 C -ATOM 181 CD1 TRP A 24 17.385 -58.281 8.882 1.00 27.80 C -ANISOU 181 CD1 TRP A 24 3489 2463 4612 173 642 -949 C -ATOM 182 CD2 TRP A 24 18.205 -58.760 10.910 1.00 21.59 C -ANISOU 182 CD2 TRP A 24 2721 1587 3894 334 637 -886 C -ATOM 183 NE1 TRP A 24 17.437 -59.651 9.000 1.00 28.10 N -ANISOU 183 NE1 TRP A 24 3553 2435 4688 219 736 -990 N -ATOM 184 CE2 TRP A 24 17.932 -59.969 10.238 1.00 25.70 C -ANISOU 184 CE2 TRP A 24 3262 2077 4427 318 734 -952 C -ATOM 185 CE3 TRP A 24 18.724 -58.812 12.205 1.00 21.98 C -ANISOU 185 CE3 TRP A 24 2779 1592 3982 430 615 -837 C -ATOM 186 CZ2 TRP A 24 18.166 -61.215 10.819 1.00 32.78 C -ANISOU 186 CZ2 TRP A 24 4186 2898 5372 395 809 -971 C -ATOM 187 CZ3 TRP A 24 18.957 -60.051 12.780 1.00 23.29 C -ANISOU 187 CZ3 TRP A 24 2972 1683 4195 506 690 -856 C -ATOM 188 CH2 TRP A 24 18.673 -61.234 12.088 1.00 32.48 C -ANISOU 188 CH2 TRP A 24 4155 2817 5370 488 786 -922 C -ATOM 189 N ASP A 25 21.167 -57.130 11.108 1.00 25.51 N -ANISOU 189 N ASP A 25 3094 2216 4384 395 528 -795 N -ATOM 190 CA ASP A 25 22.022 -57.664 12.168 1.00 23.59 C -ANISOU 190 CA ASP A 25 2852 1924 4189 501 544 -768 C -ATOM 191 C ASP A 25 23.178 -56.701 12.412 1.00 21.98 C -ANISOU 191 C ASP A 25 2595 1778 3979 525 474 -716 C -ATOM 192 O ASP A 25 24.328 -56.996 12.075 1.00 25.57 O -ANISOU 192 O ASP A 25 3010 2260 4445 549 506 -726 O -ATOM 193 CB ASP A 25 22.538 -59.051 11.778 1.00 26.72 C -ANISOU 193 CB ASP A 25 3250 2287 4617 533 651 -823 C -ATOM 194 CG ASP A 25 23.374 -59.709 12.871 1.00 29.58 C -ANISOU 194 CG ASP A 25 3618 2591 5031 644 675 -799 C -ATOM 195 OD1 ASP A 25 23.339 -59.260 14.035 1.00 34.11 O -ANISOU 195 OD1 ASP A 25 4207 3134 5621 700 618 -744 O -ATOM 196 OD2 ASP A 25 24.069 -60.696 12.560 1.00 39.64 O -ANISOU 196 OD2 ASP A 25 4882 3851 6330 676 753 -837 O -ATOM 197 N TYR A 26 22.863 -55.547 12.991 1.00 19.11 N -ANISOU 197 N TYR A 26 2232 1433 3597 518 379 -660 N -ATOM 198 CA TYR A 26 23.839 -54.474 13.156 1.00 24.13 C -ANISOU 198 CA TYR A 26 2819 2131 4220 528 302 -608 C -ATOM 199 C TYR A 26 24.998 -54.829 14.081 1.00 26.18 C -ANISOU 199 C TYR A 26 3063 2361 4524 630 309 -576 C -ATOM 200 O TYR A 26 26.073 -54.239 13.984 1.00 25.78 O -ANISOU 200 O TYR A 26 2962 2365 4468 640 271 -548 O -ATOM 201 CB TYR A 26 23.165 -53.187 13.635 1.00 25.24 C -ANISOU 201 CB TYR A 26 2968 2291 4331 499 199 -555 C -ATOM 202 CG TYR A 26 22.463 -53.309 14.971 1.00 29.33 C -ANISOU 202 CG TYR A 26 3537 2730 4875 562 176 -520 C -ATOM 203 CD1 TYR A 26 23.164 -53.170 16.161 1.00 25.55 C -ANISOU 203 CD1 TYR A 26 3057 2221 4429 653 141 -467 C -ATOM 204 CD2 TYR A 26 21.096 -53.553 15.039 1.00 28.83 C -ANISOU 204 CD2 TYR A 26 3526 2622 4806 531 189 -539 C -ATOM 205 CE1 TYR A 26 22.523 -53.272 17.385 1.00 30.86 C -ANISOU 205 CE1 TYR A 26 3779 2821 5126 711 120 -434 C -ATOM 206 CE2 TYR A 26 20.447 -53.655 16.261 1.00 31.11 C -ANISOU 206 CE2 TYR A 26 3862 2839 5119 589 169 -507 C -ATOM 207 CZ TYR A 26 21.169 -53.517 17.427 1.00 32.80 C -ANISOU 207 CZ TYR A 26 4074 3024 5363 678 135 -454 C -ATOM 208 OH TYR A 26 20.534 -53.616 18.640 1.00 46.14 O -ANISOU 208 OH TYR A 26 5813 4643 7077 736 115 -422 O -ATOM 209 N GLU A 27 24.781 -55.787 14.975 1.00 30.09 N -ANISOU 209 N GLU A 27 3601 2769 5062 704 355 -580 N -ATOM 210 CA GLU A 27 25.817 -56.172 15.926 1.00 33.50 C -ANISOU 210 CA GLU A 27 4024 3166 5539 805 362 -549 C -ATOM 211 C GLU A 27 27.064 -56.717 15.227 1.00 34.74 C -ANISOU 211 C GLU A 27 4134 3359 5708 818 419 -579 C -ATOM 212 O GLU A 27 28.171 -56.640 15.770 1.00 31.43 O -ANISOU 212 O GLU A 27 3686 2944 5314 883 403 -547 O -ATOM 213 CB GLU A 27 25.273 -57.172 16.952 1.00 39.01 C -ANISOU 213 CB GLU A 27 4781 3763 6280 879 409 -553 C -ATOM 214 CG GLU A 27 24.503 -56.523 18.096 1.00 41.96 C -ANISOU 214 CG GLU A 27 5192 4096 6653 906 336 -499 C -ATOM 215 CD GLU A 27 23.580 -57.496 18.817 1.00 51.75 C -ANISOU 215 CD GLU A 27 6497 5241 7924 948 387 -515 C -ATOM 216 OE1 GLU A 27 22.369 -57.520 18.497 1.00 59.76 O -ANISOU 216 OE1 GLU A 27 7545 6242 8918 891 395 -539 O -ATOM 217 OE2 GLU A 27 24.059 -58.232 19.705 1.00 53.70 O -ANISOU 217 OE2 GLU A 27 6761 5427 8216 1037 419 -504 O -ATOM 218 N SER A 28 26.886 -57.236 14.014 1.00 30.96 N -ANISOU 218 N SER A 28 3646 2906 5211 754 484 -641 N -ATOM 219 CA SER A 28 27.990 -57.828 13.269 1.00 36.58 C -ANISOU 219 CA SER A 28 4316 3650 5933 761 546 -676 C -ATOM 220 C SER A 28 28.534 -56.868 12.216 1.00 30.71 C -ANISOU 220 C SER A 28 3514 3008 5146 687 505 -674 C -ATOM 221 O SER A 28 29.439 -57.215 11.458 1.00 32.55 O -ANISOU 221 O SER A 28 3707 3280 5380 680 550 -703 O -ATOM 222 CB SER A 28 27.553 -59.137 12.608 1.00 44.54 C -ANISOU 222 CB SER A 28 5352 4619 6952 746 652 -748 C -ATOM 223 OG SER A 28 26.789 -58.886 11.439 1.00 53.21 O -ANISOU 223 OG SER A 28 6449 5761 8006 644 660 -788 O -ATOM 224 N HIS A 29 27.977 -55.663 12.173 1.00 25.16 N -ANISOU 224 N HIS A 29 2807 2347 4404 631 419 -640 N -ATOM 225 CA HIS A 29 28.439 -54.637 11.241 1.00 21.69 C -ANISOU 225 CA HIS A 29 2315 2004 3922 559 370 -632 C -ATOM 226 C HIS A 29 29.912 -54.280 11.461 1.00 26.62 C -ANISOU 226 C HIS A 29 2884 2669 4561 608 344 -597 C -ATOM 227 O HIS A 29 30.346 -54.020 12.583 1.00 27.29 O -ANISOU 227 O HIS A 29 2971 2726 4674 681 299 -545 O -ATOM 228 CB HIS A 29 27.585 -53.373 11.353 1.00 23.44 C -ANISOU 228 CB HIS A 29 2546 2256 4104 502 276 -594 C -ATOM 229 CG HIS A 29 27.979 -52.301 10.384 1.00 27.70 C -ANISOU 229 CG HIS A 29 3034 2894 4598 424 224 -587 C -ATOM 230 ND1 HIS A 29 27.807 -52.433 9.024 1.00 25.50 N -ANISOU 230 ND1 HIS A 29 2739 2665 4285 341 265 -640 N -ATOM 231 CD2 HIS A 29 28.567 -51.096 10.575 1.00 29.49 C -ANISOU 231 CD2 HIS A 29 3222 3178 4805 418 135 -532 C -ATOM 232 CE1 HIS A 29 28.260 -51.350 8.417 1.00 32.65 C -ANISOU 232 CE1 HIS A 29 3598 3655 5154 286 204 -618 C -ATOM 233 NE2 HIS A 29 28.725 -50.521 9.336 1.00 30.23 N -ANISOU 233 NE2 HIS A 29 3277 3354 4855 331 125 -553 N -ATOM 234 N VAL A 30 30.679 -54.267 10.380 1.00 25.27 N -ANISOU 234 N VAL A 30 2664 2564 4373 566 372 -626 N -ATOM 235 CA VAL A 30 32.069 -53.837 10.449 1.00 27.58 C -ANISOU 235 CA VAL A 30 2899 2905 4675 600 344 -594 C -ATOM 236 C VAL A 30 32.195 -52.409 9.928 1.00 31.06 C -ANISOU 236 C VAL A 30 3299 3434 5068 529 256 -560 C -ATOM 237 O VAL A 30 31.979 -52.142 8.742 1.00 31.42 O -ANISOU 237 O VAL A 30 3326 3538 5074 443 266 -594 O -ATOM 238 CB VAL A 30 32.991 -54.763 9.647 1.00 32.05 C -ANISOU 238 CB VAL A 30 3433 3488 5256 609 433 -643 C -ATOM 239 CG1 VAL A 30 34.410 -54.192 9.598 1.00 37.88 C -ANISOU 239 CG1 VAL A 30 4107 4288 5999 632 399 -610 C -ATOM 240 CG2 VAL A 30 32.992 -56.153 10.259 1.00 36.74 C -ANISOU 240 CG2 VAL A 30 4064 3994 5900 688 516 -671 C -ATOM 241 N VAL A 31 32.548 -51.492 10.821 1.00 26.69 N -ANISOU 241 N VAL A 31 2733 2889 4519 566 169 -494 N -ATOM 242 CA VAL A 31 32.630 -50.086 10.462 1.00 29.93 C -ANISOU 242 CA VAL A 31 3109 3377 4885 504 78 -457 C -ATOM 243 C VAL A 31 33.782 -49.805 9.501 1.00 29.17 C -ANISOU 243 C VAL A 31 2946 3363 4773 472 86 -467 C -ATOM 244 O VAL A 31 34.892 -50.299 9.690 1.00 32.69 O -ANISOU 244 O VAL A 31 3363 3807 5253 532 120 -465 O -ATOM 245 CB VAL A 31 32.763 -49.203 11.714 1.00 29.72 C -ANISOU 245 CB VAL A 31 3086 3336 4869 557 -17 -382 C -ATOM 246 CG1 VAL A 31 33.047 -47.759 11.324 1.00 31.63 C -ANISOU 246 CG1 VAL A 31 3285 3664 5068 498 -110 -342 C -ATOM 247 CG2 VAL A 31 31.494 -49.294 12.554 1.00 31.17 C -ANISOU 247 CG2 VAL A 31 3336 3449 5059 573 -35 -370 C -ATOM 248 N GLU A 32 33.506 -49.022 8.463 1.00 30.99 N -ANISOU 248 N GLU A 32 3154 3667 4954 377 56 -478 N -ATOM 249 CA GLU A 32 34.537 -48.569 7.534 1.00 35.78 C -ANISOU 249 CA GLU A 32 3697 4359 5539 337 51 -482 C -ATOM 250 C GLU A 32 34.983 -47.149 7.904 1.00 36.55 C -ANISOU 250 C GLU A 32 3760 4511 5616 329 -59 -415 C -ATOM 251 O GLU A 32 34.229 -46.180 7.732 1.00 28.88 O -ANISOU 251 O GLU A 32 2798 3569 4605 266 -128 -395 O -ATOM 252 CB GLU A 32 34.016 -48.616 6.095 1.00 44.73 C -ANISOU 252 CB GLU A 32 4826 5541 6630 236 90 -539 C -ATOM 253 CG GLU A 32 35.001 -48.118 5.044 1.00 58.64 C -ANISOU 253 CG GLU A 32 6522 7393 8364 187 86 -546 C -ATOM 254 CD GLU A 32 34.422 -48.158 3.636 1.00 68.68 C -ANISOU 254 CD GLU A 32 7793 8710 9591 86 123 -602 C -ATOM 255 OE1 GLU A 32 33.430 -48.891 3.422 1.00 69.49 O -ANISOU 255 OE1 GLU A 32 7943 8767 9693 66 176 -646 O -ATOM 256 OE2 GLU A 32 34.954 -47.454 2.748 1.00 71.27 O -ANISOU 256 OE2 GLU A 32 8074 9121 9885 26 98 -601 O -ATOM 257 N TRP A 33 36.207 -47.033 8.415 1.00 28.21 N -ANISOU 257 N TRP A 33 2892 3925 3902 74 582 -704 N -ATOM 258 CA TRP A 33 36.697 -45.766 8.962 1.00 29.78 C -ANISOU 258 CA TRP A 33 3106 4157 4053 41 544 -647 C -ATOM 259 C TRP A 33 37.291 -44.837 7.913 1.00 27.70 C -ANISOU 259 C TRP A 33 2878 3930 3717 50 466 -611 C -ATOM 260 O TRP A 33 38.052 -45.266 7.039 1.00 25.31 O -ANISOU 260 O TRP A 33 2593 3660 3365 77 469 -570 O -ATOM 261 CB TRP A 33 37.739 -46.023 10.055 1.00 27.02 C -ANISOU 261 CB TRP A 33 2751 3849 3664 18 613 -554 C -ATOM 262 CG TRP A 33 37.227 -46.906 11.145 1.00 27.32 C -ANISOU 262 CG TRP A 33 2756 3855 3768 5 690 -582 C -ATOM 263 CD1 TRP A 33 37.440 -48.251 11.282 1.00 28.91 C -ANISOU 263 CD1 TRP A 33 2944 4052 3990 22 767 -575 C -ATOM 264 CD2 TRP A 33 36.401 -46.516 12.243 1.00 28.69 C -ANISOU 264 CD2 TRP A 33 2908 3995 3998 -26 698 -624 C -ATOM 265 NE1 TRP A 33 36.798 -48.717 12.404 1.00 28.81 N -ANISOU 265 NE1 TRP A 33 2902 4005 4041 2 822 -609 N -ATOM 266 CE2 TRP A 33 36.150 -47.673 13.011 1.00 31.32 C -ANISOU 266 CE2 TRP A 33 3214 4305 4383 -28 783 -639 C -ATOM 267 CE3 TRP A 33 35.839 -45.301 12.650 1.00 27.14 C -ANISOU 267 CE3 TRP A 33 2712 3786 3814 -52 642 -651 C -ATOM 268 CZ2 TRP A 33 35.365 -47.649 14.163 1.00 37.21 C -ANISOU 268 CZ2 TRP A 33 3932 5017 5190 -55 813 -680 C -ATOM 269 CZ3 TRP A 33 35.060 -45.281 13.801 1.00 31.89 C -ANISOU 269 CZ3 TRP A 33 3286 4354 4477 -78 673 -692 C -ATOM 270 CH2 TRP A 33 34.834 -46.446 14.543 1.00 36.40 C -ANISOU 270 CH2 TRP A 33 3830 4904 5097 -80 758 -705 C -ATOM 271 N GLY A 34 36.958 -43.557 8.018 1.00 19.32 N -ANISOU 271 N GLY A 34 1826 2865 2648 29 397 -623 N -ATOM 272 CA GLY A 34 37.572 -42.551 7.175 1.00 20.89 C -ANISOU 272 CA GLY A 34 2061 3102 2776 31 323 -580 C -ATOM 273 C GLY A 34 38.796 -41.952 7.849 1.00 20.68 C -ANISOU 273 C GLY A 34 2047 3134 2675 2 334 -470 C -ATOM 274 O GLY A 34 39.281 -42.471 8.855 1.00 19.71 O -ANISOU 274 O GLY A 34 1909 3027 2552 -13 406 -423 O -ATOM 275 N ASN A 35 39.285 -40.850 7.297 1.00 21.08 N -ANISOU 275 N ASN A 35 2129 3217 2665 -5 263 -430 N -ATOM 276 CA ASN A 35 40.481 -40.203 7.827 1.00 21.01 C -ANISOU 276 CA ASN A 35 2135 3266 2581 -31 266 -325 C -ATOM 277 C ASN A 35 40.111 -39.067 8.755 1.00 19.67 C -ANISOU 277 C ASN A 35 1964 3086 2425 -69 230 -329 C -ATOM 278 O ASN A 35 39.546 -38.064 8.329 1.00 19.55 O -ANISOU 278 O ASN A 35 1963 3053 2414 -74 150 -369 O -ATOM 279 CB ASN A 35 41.362 -39.685 6.696 1.00 31.70 C -ANISOU 279 CB ASN A 35 3524 4667 3853 -18 212 -268 C -ATOM 280 CG ASN A 35 41.922 -40.801 5.852 1.00 45.33 C -ANISOU 280 CG ASN A 35 5254 6415 5556 18 253 -249 C -ATOM 281 OD1 ASN A 35 42.064 -41.930 6.320 1.00 43.96 O -ANISOU 281 OD1 ASN A 35 5058 6237 5406 27 332 -243 O -ATOM 282 ND2 ASN A 35 42.243 -40.498 4.598 1.00 56.99 N -ANISOU 282 ND2 ASN A 35 6758 7913 6985 39 198 -239 N -ATOM 283 N GLN A 36 40.437 -39.226 10.032 1.00 19.13 N -ANISOU 283 N GLN A 36 1878 3028 2362 -95 289 -287 N -ATOM 284 CA GLN A 36 40.078 -38.230 11.033 1.00 15.71 C -ANISOU 284 CA GLN A 36 1441 2584 1945 -132 263 -292 C -ATOM 285 C GLN A 36 40.659 -36.855 10.698 1.00 19.46 C -ANISOU 285 C GLN A 36 1948 3095 2353 -149 183 -239 C -ATOM 286 O GLN A 36 40.077 -35.830 11.049 1.00 17.88 O -ANISOU 286 O GLN A 36 1750 2873 2170 -170 128 -270 O -ATOM 287 CB GLN A 36 40.530 -38.708 12.416 1.00 21.17 C -ANISOU 287 CB GLN A 36 2112 3289 2642 -155 345 -242 C -ATOM 288 CG GLN A 36 40.075 -37.832 13.577 1.00 21.47 C -ANISOU 288 CG GLN A 36 2141 3311 2706 -192 330 -253 C -ATOM 289 CD GLN A 36 41.051 -36.700 13.877 1.00 21.25 C -ANISOU 289 CD GLN A 36 2137 3332 2603 -219 291 -164 C -ATOM 290 OE1 GLN A 36 42.212 -36.745 13.473 1.00 23.76 O -ANISOU 290 OE1 GLN A 36 2475 3702 2851 -215 296 -80 O -ATOM 291 NE2 GLN A 36 40.574 -35.676 14.584 1.00 19.55 N -ANISOU 291 NE2 GLN A 36 1921 3102 2405 -247 250 -183 N -ATOM 292 N ASP A 37 41.806 -36.835 10.021 1.00 18.94 N -ANISOU 292 N ASP A 37 1906 3082 2209 -140 176 -159 N -ATOM 293 CA ASP A 37 42.446 -35.578 9.656 1.00 17.14 C -ANISOU 293 CA ASP A 37 1709 2891 1912 -156 102 -102 C -ATOM 294 C ASP A 37 41.708 -34.792 8.571 1.00 23.36 C -ANISOU 294 C ASP A 37 2517 3652 2707 -144 8 -166 C -ATOM 295 O ASP A 37 42.053 -33.642 8.309 1.00 24.20 O -ANISOU 295 O ASP A 37 2649 3780 2765 -160 -62 -130 O -ATOM 296 CB ASP A 37 43.906 -35.808 9.250 1.00 25.11 C -ANISOU 296 CB ASP A 37 2738 3967 2836 -151 125 4 C -ATOM 297 CG ASP A 37 44.052 -36.918 8.238 1.00 40.71 C -ANISOU 297 CG ASP A 37 4713 5946 4809 -111 155 -10 C -ATOM 298 OD1 ASP A 37 43.788 -38.085 8.603 1.00 45.25 O -ANISOU 298 OD1 ASP A 37 5263 6501 5430 -97 229 -38 O -ATOM 299 OD2 ASP A 37 44.420 -36.624 7.078 1.00 50.04 O -ANISOU 299 OD2 ASP A 37 5919 7151 5942 -94 106 6 O -ATOM 300 N ASP A 38 40.684 -35.392 7.957 1.00 18.40 N -ANISOU 300 N ASP A 38 1876 2975 2140 -116 4 -260 N -ATOM 301 CA ASP A 38 39.933 -34.694 6.916 1.00 17.82 C -ANISOU 301 CA ASP A 38 1821 2874 2077 -102 -85 -325 C -ATOM 302 C ASP A 38 39.051 -33.588 7.483 1.00 19.39 C -ANISOU 302 C ASP A 38 2017 3036 2313 -127 -144 -376 C -ATOM 303 O ASP A 38 38.601 -32.706 6.745 1.00 20.59 O -ANISOU 303 O ASP A 38 2190 3174 2461 -124 -229 -413 O -ATOM 304 CB ASP A 38 39.047 -35.657 6.124 1.00 21.36 C -ANISOU 304 CB ASP A 38 2255 3277 2582 -65 -72 -414 C -ATOM 305 CG ASP A 38 39.822 -36.499 5.148 1.00 20.81 C -ANISOU 305 CG ASP A 38 2198 3241 2468 -33 -46 -375 C -ATOM 306 OD1 ASP A 38 41.054 -36.289 5.012 1.00 19.37 O -ANISOU 306 OD1 ASP A 38 2035 3118 2207 -40 -41 -279 O -ATOM 307 OD2 ASP A 38 39.193 -37.374 4.512 1.00 22.14 O -ANISOU 307 OD2 ASP A 38 2356 3376 2680 -2 -29 -442 O -ATOM 308 N TYR A 39 38.792 -33.639 8.788 1.00 17.12 N -ANISOU 308 N TYR A 39 1705 2735 2064 -152 -99 -380 N -ATOM 309 CA TYR A 39 37.806 -32.746 9.401 1.00 21.33 C -ANISOU 309 CA TYR A 39 2230 3228 2646 -173 -145 -442 C -ATOM 310 C TYR A 39 38.407 -31.895 10.505 1.00 25.65 C -ANISOU 310 C TYR A 39 2783 3805 3160 -211 -147 -373 C -ATOM 311 O TYR A 39 39.029 -32.407 11.441 1.00 26.89 O -ANISOU 311 O TYR A 39 2925 3985 3306 -226 -73 -317 O -ATOM 312 CB TYR A 39 36.600 -33.553 9.906 1.00 17.99 C -ANISOU 312 CB TYR A 39 1769 2747 2318 -164 -99 -538 C -ATOM 313 CG TYR A 39 36.103 -34.481 8.839 1.00 22.60 C -ANISOU 313 CG TYR A 39 2349 3305 2933 -125 -91 -599 C -ATOM 314 CD1 TYR A 39 35.264 -34.016 7.829 1.00 17.51 C -ANISOU 314 CD1 TYR A 39 1715 2625 2311 -107 -169 -675 C -ATOM 315 CD2 TYR A 39 36.515 -35.808 8.797 1.00 22.55 C -ANISOU 315 CD2 TYR A 39 2329 3310 2931 -106 -10 -578 C -ATOM 316 CE1 TYR A 39 34.838 -34.852 6.825 1.00 18.86 C -ANISOU 316 CE1 TYR A 39 1884 2773 2508 -71 -164 -729 C -ATOM 317 CE2 TYR A 39 36.089 -36.654 7.794 1.00 17.79 C -ANISOU 317 CE2 TYR A 39 1723 2684 2354 -70 -5 -633 C -ATOM 318 CZ TYR A 39 35.244 -36.168 6.815 1.00 19.20 C -ANISOU 318 CZ TYR A 39 1912 2828 2555 -53 -82 -708 C -ATOM 319 OH TYR A 39 34.814 -37.000 5.816 1.00 19.34 O -ANISOU 319 OH TYR A 39 1927 2821 2599 -16 -78 -763 O -ATOM 320 N GLN A 40 38.242 -30.585 10.364 1.00 20.44 N -ANISOU 320 N GLN A 40 2144 3143 2480 -228 -233 -377 N -ATOM 321 CA GLN A 40 38.687 -29.645 11.379 1.00 23.33 C -ANISOU 321 CA GLN A 40 2516 3531 2818 -265 -246 -321 C -ATOM 322 C GLN A 40 37.490 -29.054 12.116 1.00 25.44 C -ANISOU 322 C GLN A 40 2765 3747 3153 -280 -275 -403 C -ATOM 323 O GLN A 40 36.630 -28.428 11.501 1.00 18.67 O -ANISOU 323 O GLN A 40 1916 2855 2322 -271 -349 -474 O -ATOM 324 CB GLN A 40 39.509 -28.527 10.738 1.00 34.83 C -ANISOU 324 CB GLN A 40 4012 5028 4194 -275 -324 -253 C -ATOM 325 CG GLN A 40 40.746 -29.031 10.015 1.00 50.56 C -ANISOU 325 CG GLN A 40 6023 7075 6114 -262 -298 -167 C -ATOM 326 CD GLN A 40 41.760 -27.934 9.734 1.00 59.10 C -ANISOU 326 CD GLN A 40 7140 8206 7111 -282 -358 -79 C -ATOM 327 OE1 GLN A 40 42.964 -28.138 9.879 1.00 55.16 O -ANISOU 327 OE1 GLN A 40 6648 7760 6550 -290 -321 16 O -ATOM 328 NE2 GLN A 40 41.275 -26.766 9.325 1.00 65.49 N -ANISOU 328 NE2 GLN A 40 7970 8997 7917 -291 -452 -111 N -ATOM 329 N LEU A 41 37.441 -29.246 13.431 1.00 23.57 N -ANISOU 329 N LEU A 41 2504 3507 2943 -301 -217 -393 N -ATOM 330 CA LEU A 41 36.349 -28.700 14.241 1.00 20.98 C -ANISOU 330 CA LEU A 41 2158 3135 2679 -317 -238 -466 C -ATOM 331 C LEU A 41 36.390 -27.164 14.297 1.00 19.58 C -ANISOU 331 C LEU A 41 2006 2964 2469 -340 -330 -451 C -ATOM 332 O LEU A 41 37.447 -26.569 14.485 1.00 19.99 O -ANISOU 332 O LEU A 41 2081 3062 2451 -359 -344 -359 O -ATOM 333 CB LEU A 41 36.379 -29.295 15.648 1.00 22.01 C -ANISOU 333 CB LEU A 41 2258 3265 2840 -336 -150 -451 C -ATOM 334 CG LEU A 41 36.328 -30.822 15.735 1.00 16.83 C -ANISOU 334 CG LEU A 41 1575 2601 2219 -317 -55 -465 C -ATOM 335 CD1 LEU A 41 36.442 -31.290 17.182 1.00 21.71 C -ANISOU 335 CD1 LEU A 41 2167 3222 2860 -340 27 -441 C -ATOM 336 CD2 LEU A 41 35.065 -31.354 15.093 1.00 21.48 C -ANISOU 336 CD2 LEU A 41 2145 3134 2882 -290 -64 -577 C -ATOM 337 N VAL A 42 35.236 -26.533 14.102 1.00 19.54 N -ANISOU 337 N VAL A 42 1998 2912 2514 -336 -394 -542 N -ATOM 338 CA VAL A 42 35.135 -25.075 14.052 1.00 20.83 C -ANISOU 338 CA VAL A 42 2187 3075 2654 -354 -489 -541 C -ATOM 339 C VAL A 42 34.472 -24.500 15.310 1.00 21.04 C -ANISOU 339 C VAL A 42 2194 3076 2725 -379 -490 -577 C -ATOM 340 O VAL A 42 34.941 -23.519 15.876 1.00 23.99 O -ANISOU 340 O VAL A 42 2584 3472 3060 -405 -525 -526 O -ATOM 341 CB VAL A 42 34.335 -24.623 12.808 1.00 23.88 C -ANISOU 341 CB VAL A 42 2589 3427 3058 -331 -575 -617 C -ATOM 342 CG1 VAL A 42 34.177 -23.108 12.793 1.00 31.16 C -ANISOU 342 CG1 VAL A 42 3537 4345 3959 -350 -675 -619 C -ATOM 343 CG2 VAL A 42 35.024 -25.100 11.544 1.00 26.27 C -ANISOU 343 CG2 VAL A 42 2913 3757 3311 -307 -580 -578 C -ATOM 344 N ARG A 43 33.359 -25.094 15.729 1.00 22.92 N -ANISOU 344 N ARG A 43 2396 3267 3044 -370 -453 -667 N -ATOM 345 CA ARG A 43 32.715 -24.661 16.959 1.00 24.76 C -ANISOU 345 CA ARG A 43 2608 3477 3322 -392 -445 -704 C -ATOM 346 C ARG A 43 31.737 -25.689 17.493 1.00 21.65 C -ANISOU 346 C ARG A 43 2171 3044 3012 -383 -373 -783 C -ATOM 347 O ARG A 43 31.151 -26.448 16.732 1.00 22.81 O -ANISOU 347 O ARG A 43 2306 3163 3198 -356 -362 -844 O -ATOM 348 CB ARG A 43 32.010 -23.318 16.766 1.00 27.32 C -ANISOU 348 CB ARG A 43 2947 3775 3657 -399 -548 -756 C -ATOM 349 CG ARG A 43 30.981 -23.300 15.662 1.00 34.69 C -ANISOU 349 CG ARG A 43 3881 4665 4635 -371 -606 -852 C -ATOM 350 CD ARG A 43 30.017 -22.147 15.890 1.00 42.48 C -ANISOU 350 CD ARG A 43 4868 5614 5657 -380 -687 -924 C -ATOM 351 NE ARG A 43 29.701 -21.445 14.653 1.00 56.71 N -ANISOU 351 NE ARG A 43 6699 7401 7447 -363 -784 -959 N -ATOM 352 CZ ARG A 43 28.484 -21.368 14.124 1.00 63.47 C -ANISOU 352 CZ ARG A 43 7544 8207 8366 -344 -828 -1066 C -ATOM 353 NH1 ARG A 43 27.453 -21.950 14.728 1.00 58.93 N -ANISOU 353 NH1 ARG A 43 6929 7593 7871 -339 -783 -1148 N -ATOM 354 NH2 ARG A 43 28.296 -20.702 12.993 1.00 69.65 N -ANISOU 354 NH2 ARG A 43 8356 8979 9130 -330 -918 -1090 N -ATOM 355 N LYS A 44 31.572 -25.709 18.812 1.00 17.42 N -ANISOU 355 N LYS A 44 1612 2504 2502 -405 -325 -782 N -ATOM 356 CA LYS A 44 30.643 -26.631 19.444 1.00 21.28 C -ANISOU 356 CA LYS A 44 2059 2956 3071 -400 -255 -855 C -ATOM 357 C LYS A 44 29.227 -26.110 19.235 1.00 21.78 C -ANISOU 357 C LYS A 44 2108 2964 3202 -392 -315 -971 C -ATOM 358 O LYS A 44 28.940 -24.967 19.552 1.00 23.47 O -ANISOU 358 O LYS A 44 2332 3172 3414 -407 -380 -986 O -ATOM 359 CB LYS A 44 30.944 -26.746 20.947 1.00 21.45 C -ANISOU 359 CB LYS A 44 2062 2992 3095 -429 -187 -813 C -ATOM 360 CG LYS A 44 30.318 -27.960 21.615 1.00 21.19 C -ANISOU 360 CG LYS A 44 1988 2934 3130 -425 -94 -861 C -ATOM 361 CD LYS A 44 30.501 -27.949 23.131 1.00 35.38 C -ANISOU 361 CD LYS A 44 3768 4742 4933 -454 -35 -828 C -ATOM 362 CE LYS A 44 31.946 -28.202 23.520 1.00 45.21 C -ANISOU 362 CE LYS A 44 5030 6042 6105 -468 13 -708 C -ATOM 363 NZ LYS A 44 32.201 -28.024 24.985 1.00 48.12 N -ANISOU 363 NZ LYS A 44 5387 6425 6471 -498 59 -669 N -ATOM 364 N LEU A 45 28.342 -26.939 18.695 1.00 18.06 N -ANISOU 364 N LEU A 45 1614 2454 2792 -367 -295 -1053 N -ATOM 365 CA LEU A 45 26.960 -26.503 18.506 1.00 21.60 C -ANISOU 365 CA LEU A 45 2047 2850 3311 -358 -349 -1166 C -ATOM 366 C LEU A 45 26.112 -26.868 19.720 1.00 23.72 C -ANISOU 366 C LEU A 45 2273 3091 3650 -371 -290 -1223 C -ATOM 367 O LEU A 45 25.174 -26.149 20.086 1.00 26.91 O -ANISOU 367 O LEU A 45 2664 3463 4097 -378 -334 -1294 O -ATOM 368 CB LEU A 45 26.374 -27.107 17.242 1.00 18.66 C -ANISOU 368 CB LEU A 45 1672 2448 2970 -324 -369 -1232 C -ATOM 369 CG LEU A 45 27.060 -26.735 15.927 1.00 21.04 C -ANISOU 369 CG LEU A 45 2015 2773 3208 -308 -434 -1189 C -ATOM 370 CD1 LEU A 45 26.280 -27.303 14.759 1.00 25.65 C -ANISOU 370 CD1 LEU A 45 2593 3319 3834 -274 -455 -1270 C -ATOM 371 CD2 LEU A 45 27.182 -25.232 15.792 1.00 25.51 C -ANISOU 371 CD2 LEU A 45 2612 3347 3734 -322 -533 -1174 C -ATOM 372 N GLY A 46 26.450 -27.981 20.357 1.00 25.86 N -ANISOU 372 N GLY A 46 2522 3373 3930 -376 -191 -1192 N -ATOM 373 CA GLY A 46 25.697 -28.415 21.512 1.00 29.67 C -ANISOU 373 CA GLY A 46 2964 3831 4477 -390 -128 -1240 C -ATOM 374 C GLY A 46 26.109 -29.772 22.036 1.00 27.87 C -ANISOU 374 C GLY A 46 2716 3615 4259 -391 -17 -1204 C -ATOM 375 O GLY A 46 26.994 -30.427 21.499 1.00 24.72 O -ANISOU 375 O GLY A 46 2332 3243 3816 -380 13 -1141 O -ATOM 376 N ARG A 47 25.423 -30.196 23.088 1.00 29.31 N -ANISOU 376 N ARG A 47 2862 3775 4501 -404 42 -1248 N -ATOM 377 CA ARG A 47 25.749 -31.420 23.783 1.00 33.06 C -ANISOU 377 CA ARG A 47 3314 4259 4987 -410 148 -1215 C -ATOM 378 C ARG A 47 24.461 -32.132 24.150 1.00 36.27 C -ANISOU 378 C ARG A 47 3677 4617 5486 -406 191 -1316 C -ATOM 379 O ARG A 47 23.528 -31.508 24.652 1.00 37.40 O -ANISOU 379 O ARG A 47 3802 4732 5675 -416 163 -1384 O -ATOM 380 CB ARG A 47 26.542 -31.090 25.050 1.00 32.66 C -ANISOU 380 CB ARG A 47 3268 4244 4896 -442 187 -1134 C -ATOM 381 CG ARG A 47 26.839 -32.287 25.915 1.00 41.28 C -ANISOU 381 CG ARG A 47 4337 5345 6004 -451 297 -1102 C -ATOM 382 CD ARG A 47 28.247 -32.213 26.464 1.00 50.96 C -ANISOU 382 CD ARG A 47 5586 6625 7152 -469 329 -982 C -ATOM 383 NE ARG A 47 28.286 -31.582 27.774 1.00 57.17 N -ANISOU 383 NE ARG A 47 6366 7422 7935 -499 342 -960 N -ATOM 384 CZ ARG A 47 29.381 -31.070 28.330 1.00 55.87 C -ANISOU 384 CZ ARG A 47 6225 7301 7703 -519 344 -864 C -ATOM 385 NH1 ARG A 47 30.544 -31.094 27.688 1.00 47.52 N -ANISOU 385 NH1 ARG A 47 5199 6283 6575 -512 332 -779 N -ATOM 386 NH2 ARG A 47 29.307 -30.525 29.533 1.00 60.60 N -ANISOU 386 NH2 ARG A 47 6816 7904 8304 -545 355 -854 N -ATOM 387 N GLY A 48 24.407 -33.430 23.879 1.00 36.61 N -ANISOU 387 N GLY A 48 3704 4649 5558 -391 258 -1327 N -ATOM 388 CA GLY A 48 23.269 -34.246 24.253 1.00 43.19 C -ANISOU 388 CA GLY A 48 4495 5439 6478 -388 309 -1414 C -ATOM 389 C GLY A 48 23.695 -35.271 25.280 1.00 43.23 C -ANISOU 389 C GLY A 48 4480 5458 6487 -404 417 -1368 C -ATOM 390 O GLY A 48 24.866 -35.337 25.638 1.00 43.65 O -ANISOU 390 O GLY A 48 4553 5554 6477 -415 448 -1269 O -ATOM 391 N LYS A 49 22.750 -36.074 25.756 1.00 47.80 N -ANISOU 391 N LYS A 49 5020 6000 7142 -406 473 -1438 N -ATOM 392 CA LYS A 49 23.079 -37.111 26.722 1.00 45.40 C -ANISOU 392 CA LYS A 49 4697 5706 6848 -421 577 -1399 C -ATOM 393 C LYS A 49 24.058 -38.100 26.109 1.00 35.92 C -ANISOU 393 C LYS A 49 3512 4528 5606 -404 619 -1331 C -ATOM 394 O LYS A 49 24.841 -38.728 26.817 1.00 41.93 O -ANISOU 394 O LYS A 49 4275 5316 6341 -418 692 -1260 O -ATOM 395 CB LYS A 49 21.813 -37.830 27.215 1.00 51.88 C -ANISOU 395 CB LYS A 49 5472 6480 7761 -424 626 -1493 C -ATOM 396 CG LYS A 49 20.568 -37.561 26.373 1.00 54.96 C -ANISOU 396 CG LYS A 49 5847 6824 8212 -404 563 -1604 C -ATOM 397 CD LYS A 49 19.284 -38.049 27.060 1.00 63.39 C -ANISOU 397 CD LYS A 49 6868 7849 9370 -413 606 -1697 C -ATOM 398 CE LYS A 49 19.201 -39.569 27.129 1.00 66.56 C -ANISOU 398 CE LYS A 49 7247 8235 9810 -407 696 -1702 C -ATOM 399 NZ LYS A 49 17.842 -40.044 27.535 1.00 67.59 N -ANISOU 399 NZ LYS A 49 7330 8317 10032 -411 727 -1804 N -ATOM 400 N TYR A 50 24.038 -38.206 24.784 1.00 34.83 N -ANISOU 400 N TYR A 50 3390 4382 5461 -375 572 -1352 N -ATOM 401 CA TYR A 50 24.788 -39.255 24.100 1.00 35.43 C -ANISOU 401 CA TYR A 50 3478 4473 5510 -355 613 -1304 C -ATOM 402 C TYR A 50 25.979 -38.786 23.272 1.00 28.57 C -ANISOU 402 C TYR A 50 2652 3648 4554 -343 566 -1221 C -ATOM 403 O TYR A 50 26.767 -39.608 22.816 1.00 28.32 O -ANISOU 403 O TYR A 50 2633 3638 4490 -329 604 -1168 O -ATOM 404 CB TYR A 50 23.855 -40.049 23.191 1.00 43.16 C -ANISOU 404 CB TYR A 50 4438 5407 6552 -327 611 -1393 C -ATOM 405 CG TYR A 50 22.747 -40.756 23.925 1.00 54.97 C -ANISOU 405 CG TYR A 50 5890 6861 8134 -336 668 -1470 C -ATOM 406 CD1 TYR A 50 23.027 -41.750 24.852 1.00 56.71 C -ANISOU 406 CD1 TYR A 50 6093 7087 8367 -351 765 -1436 C -ATOM 407 CD2 TYR A 50 21.416 -40.437 23.682 1.00 61.84 C -ANISOU 407 CD2 TYR A 50 6737 7684 9074 -330 626 -1579 C -ATOM 408 CE1 TYR A 50 22.012 -42.403 25.522 1.00 64.71 C -ANISOU 408 CE1 TYR A 50 7066 8062 9459 -361 818 -1506 C -ATOM 409 CE2 TYR A 50 20.395 -41.085 24.347 1.00 66.52 C -ANISOU 409 CE2 TYR A 50 7289 8240 9747 -339 679 -1650 C -ATOM 410 CZ TYR A 50 20.698 -42.068 25.265 1.00 69.94 C -ANISOU 410 CZ TYR A 50 7704 8680 10190 -355 775 -1613 C -ATOM 411 OH TYR A 50 19.681 -42.716 25.929 1.00 76.85 O -ANISOU 411 OH TYR A 50 8539 9518 11144 -365 829 -1682 O -ATOM 412 N SER A 51 26.097 -37.481 23.062 1.00 26.64 N -ANISOU 412 N SER A 51 2430 3417 4273 -349 484 -1212 N -ATOM 413 CA SER A 51 27.116 -36.963 22.159 1.00 21.41 C -ANISOU 413 CA SER A 51 1809 2793 3533 -338 430 -1142 C -ATOM 414 C SER A 51 27.318 -35.465 22.302 1.00 20.30 C -ANISOU 414 C SER A 51 1692 2671 3351 -354 351 -1120 C -ATOM 415 O SER A 51 26.550 -34.772 22.982 1.00 24.16 O -ANISOU 415 O SER A 51 2165 3138 3875 -371 328 -1170 O -ATOM 416 CB SER A 51 26.716 -37.240 20.715 1.00 32.43 C -ANISOU 416 CB SER A 51 3213 4167 4944 -303 385 -1195 C -ATOM 417 OG SER A 51 25.740 -36.300 20.289 1.00 34.14 O -ANISOU 417 OG SER A 51 3429 4351 5193 -299 301 -1276 O -ATOM 418 N GLU A 52 28.372 -34.982 21.655 1.00 16.13 N -ANISOU 418 N GLU A 52 1581 2569 1979 -40 -314 -497 N -ATOM 419 CA GLU A 52 28.588 -33.560 21.444 1.00 23.57 C -ANISOU 419 CA GLU A 52 2481 3477 2996 -23 -320 -459 C -ATOM 420 C GLU A 52 28.637 -33.333 19.949 1.00 20.74 C -ANISOU 420 C GLU A 52 2140 3135 2604 -51 -336 -394 C -ATOM 421 O GLU A 52 29.212 -34.133 19.223 1.00 18.50 O -ANISOU 421 O GLU A 52 1906 2875 2249 -74 -325 -391 O -ATOM 422 CB GLU A 52 29.909 -33.105 22.062 1.00 28.68 C -ANISOU 422 CB GLU A 52 3125 4090 3683 3 -285 -494 C -ATOM 423 CG GLU A 52 29.905 -33.045 23.568 1.00 38.23 C -ANISOU 423 CG GLU A 52 4307 5276 4942 36 -270 -555 C -ATOM 424 CD GLU A 52 31.054 -32.226 24.100 1.00 38.03 C -ANISOU 424 CD GLU A 52 4263 5210 4976 65 -242 -576 C -ATOM 425 OE1 GLU A 52 32.138 -32.267 23.489 1.00 34.57 O -ANISOU 425 OE1 GLU A 52 3854 4769 4512 56 -223 -568 O -ATOM 426 OE2 GLU A 52 30.868 -31.529 25.113 1.00 41.69 O -ANISOU 426 OE2 GLU A 52 4683 5645 5513 95 -241 -600 O -ATOM 427 N VAL A 53 28.049 -32.235 19.495 1.00 13.76 N -ANISOU 427 N VAL A 53 1217 2239 1773 -47 -362 -341 N -ATOM 428 CA VAL A 53 27.943 -31.958 18.074 1.00 13.64 C -ANISOU 428 CA VAL A 53 1213 2240 1730 -73 -381 -274 C -ATOM 429 C VAL A 53 28.707 -30.679 17.736 1.00 16.95 C -ANISOU 429 C VAL A 53 1607 2624 2210 -58 -373 -241 C -ATOM 430 O VAL A 53 28.517 -29.641 18.380 1.00 22.10 O -ANISOU 430 O VAL A 53 2210 3243 2944 -31 -377 -241 O -ATOM 431 CB VAL A 53 26.460 -31.816 17.660 1.00 18.78 C -ANISOU 431 CB VAL A 53 1842 2912 2382 -87 -421 -232 C -ATOM 432 CG1 VAL A 53 26.342 -31.425 16.200 1.00 21.71 C -ANISOU 432 CG1 VAL A 53 2220 3297 2730 -111 -442 -161 C -ATOM 433 CG2 VAL A 53 25.710 -33.115 17.919 1.00 17.35 C -ANISOU 433 CG2 VAL A 53 1688 2768 2138 -104 -429 -263 C -ATOM 434 N PHE A 54 29.553 -30.761 16.711 1.00 15.01 N -ANISOU 434 N PHE A 54 1395 2387 1923 -75 -363 -212 N -ATOM 435 CA PHE A 54 30.391 -29.648 16.297 1.00 17.97 C -ANISOU 435 CA PHE A 54 1751 2729 2346 -64 -354 -180 C -ATOM 436 C PHE A 54 30.131 -29.255 14.846 1.00 24.44 C -ANISOU 436 C PHE A 54 2576 3566 3145 -88 -377 -106 C -ATOM 437 O PHE A 54 29.832 -30.102 14.000 1.00 25.40 O -ANISOU 437 O PHE A 54 2735 3726 3189 -118 -388 -87 O -ATOM 438 CB PHE A 54 31.869 -30.031 16.448 1.00 18.44 C -ANISOU 438 CB PHE A 54 1845 2779 2382 -59 -315 -217 C -ATOM 439 CG PHE A 54 32.284 -30.353 17.857 1.00 19.95 C -ANISOU 439 CG PHE A 54 2031 2951 2597 -34 -289 -290 C -ATOM 440 CD1 PHE A 54 32.931 -29.402 18.634 1.00 18.78 C -ANISOU 440 CD1 PHE A 54 1848 2760 2528 -2 -271 -310 C -ATOM 441 CD2 PHE A 54 32.055 -31.607 18.399 1.00 18.57 C -ANISOU 441 CD2 PHE A 54 1887 2802 2366 -41 -281 -339 C -ATOM 442 CE1 PHE A 54 33.339 -29.687 19.936 1.00 24.13 C -ANISOU 442 CE1 PHE A 54 2521 3420 3227 23 -246 -378 C -ATOM 443 CE2 PHE A 54 32.464 -31.908 19.707 1.00 17.56 C -ANISOU 443 CE2 PHE A 54 1756 2657 2260 -16 -256 -406 C -ATOM 444 CZ PHE A 54 33.104 -30.942 20.475 1.00 23.65 C -ANISOU 444 CZ PHE A 54 2491 3386 3110 16 -239 -426 C -ATOM 445 N GLU A 55 30.227 -27.968 14.548 1.00 22.30 N -ANISOU 445 N GLU A 55 2266 3266 2939 -76 -385 -63 N -ATOM 446 CA GLU A 55 30.323 -27.556 13.158 1.00 20.33 C -ANISOU 446 CA GLU A 55 2027 3028 2669 -96 -398 4 C -ATOM 447 C GLU A 55 31.766 -27.797 12.768 1.00 22.63 C -ANISOU 447 C GLU A 55 2355 3314 2927 -101 -366 -5 C -ATOM 448 O GLU A 55 32.651 -27.626 13.588 1.00 19.13 O -ANISOU 448 O GLU A 55 1907 2843 2518 -79 -338 -48 O -ATOM 449 CB GLU A 55 29.979 -26.083 13.007 1.00 20.72 C -ANISOU 449 CB GLU A 55 2023 3046 2803 -80 -416 52 C -ATOM 450 CG GLU A 55 30.209 -25.530 11.613 1.00 27.79 C -ANISOU 450 CG GLU A 55 2925 3949 3686 -98 -427 122 C -ATOM 451 CD GLU A 55 29.842 -24.061 11.504 1.00 33.49 C -ANISOU 451 CD GLU A 55 3592 4638 4493 -80 -444 169 C -ATOM 452 OE1 GLU A 55 28.641 -23.745 11.593 1.00 46.55 O -ANISOU 452 OE1 GLU A 55 5216 6299 6174 -79 -474 189 O -ATOM 453 OE2 GLU A 55 30.749 -23.229 11.322 1.00 43.53 O -ANISOU 453 OE2 GLU A 55 4853 5880 5807 -68 -428 185 O -ATOM 454 N ALA A 56 32.013 -28.205 11.531 1.00 21.27 N -ANISOU 454 N ALA A 56 2221 3171 2690 -129 -370 34 N -ATOM 455 CA ALA A 56 33.384 -28.450 11.106 1.00 19.79 C -ANISOU 455 CA ALA A 56 2070 2981 2469 -134 -340 27 C -ATOM 456 C ALA A 56 33.534 -28.207 9.623 1.00 17.35 C -ANISOU 456 C ALA A 56 1778 2690 2125 -158 -352 94 C -ATOM 457 O ALA A 56 32.558 -27.981 8.923 1.00 19.31 O -ANISOU 457 O ALA A 56 2014 2956 2367 -172 -384 143 O -ATOM 458 CB ALA A 56 33.823 -29.867 11.462 1.00 17.19 C -ANISOU 458 CB ALA A 56 1792 2677 2065 -145 -319 -30 C -ATOM 459 N ILE A 57 34.773 -28.241 9.154 1.00 14.84 N -ANISOU 459 N ILE A 57 1488 2366 1784 -162 -327 97 N -ATOM 460 CA ILE A 57 35.046 -28.091 7.739 1.00 18.59 C -ANISOU 460 CA ILE A 57 1984 2860 2220 -184 -335 157 C -ATOM 461 C ILE A 57 35.735 -29.359 7.265 1.00 21.03 C -ANISOU 461 C ILE A 57 2354 3201 2434 -207 -317 136 C -ATOM 462 O ILE A 57 36.643 -29.877 7.920 1.00 20.95 O -ANISOU 462 O ILE A 57 2367 3183 2411 -198 -286 82 O -ATOM 463 CB ILE A 57 35.917 -26.844 7.456 1.00 25.09 C -ANISOU 463 CB ILE A 57 2781 3645 3105 -169 -322 190 C -ATOM 464 CG1 ILE A 57 36.276 -26.768 5.974 1.00 30.10 C -ANISOU 464 CG1 ILE A 57 3441 4301 3693 -193 -328 251 C -ATOM 465 CG2 ILE A 57 37.184 -26.883 8.282 1.00 33.95 C -ANISOU 465 CG2 ILE A 57 3912 4740 4248 -149 -283 136 C -ATOM 466 CD1 ILE A 57 37.222 -25.638 5.630 1.00 39.51 C -ANISOU 466 CD1 ILE A 57 4614 5459 4939 -180 -313 283 C -ATOM 467 N ASN A 58 35.261 -29.891 6.152 1.00 18.95 N -ANISOU 467 N ASN A 58 2119 2978 2104 -237 -337 176 N -ATOM 468 CA ASN A 58 35.931 -30.997 5.501 1.00 19.65 C -ANISOU 468 CA ASN A 58 2266 3099 2102 -260 -322 165 C -ATOM 469 C ASN A 58 37.007 -30.377 4.627 1.00 20.12 C -ANISOU 469 C ASN A 58 2334 3147 2163 -262 -308 204 C -ATOM 470 O ASN A 58 36.698 -29.790 3.598 1.00 24.45 O -ANISOU 470 O ASN A 58 2873 3704 2714 -274 -328 268 O -ATOM 471 CB ASN A 58 34.920 -31.765 4.643 1.00 20.67 C -ANISOU 471 CB ASN A 58 2418 3274 2160 -291 -352 195 C -ATOM 472 CG ASN A 58 35.549 -32.901 3.851 1.00 26.18 C -ANISOU 472 CG ASN A 58 3177 4008 2761 -317 -340 190 C -ATOM 473 OD1 ASN A 58 36.765 -32.968 3.688 1.00 20.69 O -ANISOU 473 OD1 ASN A 58 2506 3304 2050 -315 -312 179 O -ATOM 474 ND2 ASN A 58 34.705 -33.791 3.333 1.00 25.62 N -ANISOU 474 ND2 ASN A 58 3131 3980 2624 -343 -362 199 N -ATOM 475 N ILE A 59 38.267 -30.492 5.030 1.00 23.02 N -ANISOU 475 N ILE A 59 2718 3495 2532 -251 -272 168 N -ATOM 476 CA ILE A 59 39.337 -29.794 4.321 1.00 18.90 C -ANISOU 476 CA ILE A 59 2199 2957 2023 -249 -256 202 C -ATOM 477 C ILE A 59 39.719 -30.421 2.976 1.00 25.46 C -ANISOU 477 C ILE A 59 3078 3825 2769 -279 -258 238 C -ATOM 478 O ILE A 59 40.600 -29.913 2.289 1.00 28.14 O -ANISOU 478 O ILE A 59 3423 4155 3112 -280 -245 270 O -ATOM 479 CB ILE A 59 40.601 -29.638 5.194 1.00 19.71 C -ANISOU 479 CB ILE A 59 2304 3026 2160 -226 -218 152 C -ATOM 480 CG1 ILE A 59 41.247 -30.989 5.474 1.00 23.83 C -ANISOU 480 CG1 ILE A 59 2877 3569 2606 -235 -193 96 C -ATOM 481 CG2 ILE A 59 40.274 -28.943 6.495 1.00 24.78 C -ANISOU 481 CG2 ILE A 59 2896 3629 2889 -195 -216 118 C -ATOM 482 CD1 ILE A 59 42.601 -30.869 6.181 1.00 27.74 C -ANISOU 482 CD1 ILE A 59 3379 4035 3127 -215 -154 50 C -ATOM 483 N THR A 60 39.070 -31.520 2.602 1.00 23.15 N -ANISOU 483 N THR A 60 2820 3576 2402 -303 -272 233 N -ATOM 484 CA THR A 60 39.301 -32.108 1.281 1.00 28.27 C -ANISOU 484 CA THR A 60 3511 4262 2968 -333 -278 270 C -ATOM 485 C THR A 60 38.400 -31.484 0.206 1.00 33.71 C -ANISOU 485 C THR A 60 4180 4966 3661 -347 -313 345 C -ATOM 486 O THR A 60 38.637 -31.673 -0.991 1.00 35.69 O -ANISOU 486 O THR A 60 4458 5244 3858 -368 -318 387 O -ATOM 487 CB THR A 60 39.124 -33.643 1.272 1.00 28.82 C -ANISOU 487 CB THR A 60 3632 4373 2947 -354 -276 231 C -ATOM 488 OG1 THR A 60 37.726 -33.972 1.282 1.00 33.21 O -ANISOU 488 OG1 THR A 60 4177 4951 3490 -365 -308 240 O -ATOM 489 CG2 THR A 60 39.824 -34.272 2.470 1.00 34.17 C -ANISOU 489 CG2 THR A 60 4324 5033 3624 -338 -244 155 C -ATOM 490 N ASN A 61 37.372 -30.750 0.632 1.00 32.24 N -ANISOU 490 N ASN A 61 3946 4765 3538 -335 -337 360 N -ATOM 491 CA ASN A 61 36.517 -30.011 -0.301 1.00 23.44 C -ANISOU 491 CA ASN A 61 2807 3660 2439 -344 -370 431 C -ATOM 492 C ASN A 61 36.170 -28.609 0.202 1.00 26.12 C -ANISOU 492 C ASN A 61 3085 3958 2881 -318 -379 452 C -ATOM 493 O ASN A 61 35.462 -27.857 -0.460 1.00 32.10 O -ANISOU 493 O ASN A 61 3815 4717 3664 -322 -406 510 O -ATOM 494 CB ASN A 61 35.249 -30.802 -0.648 1.00 24.84 C -ANISOU 494 CB ASN A 61 2997 3880 2563 -367 -402 440 C -ATOM 495 CG ASN A 61 34.439 -31.177 0.578 1.00 24.36 C -ANISOU 495 CG ASN A 61 2918 3812 2525 -355 -408 388 C -ATOM 496 OD1 ASN A 61 34.612 -30.603 1.655 1.00 21.81 O -ANISOU 496 OD1 ASN A 61 2562 3452 2273 -328 -395 356 O -ATOM 497 ND2 ASN A 61 33.533 -32.135 0.417 1.00 28.38 N -ANISOU 497 ND2 ASN A 61 3447 4359 2976 -376 -428 380 N -ATOM 498 N ASN A 62 36.702 -28.257 1.367 1.00 28.34 N -ANISOU 498 N ASN A 62 3345 4200 3222 -292 -356 405 N -ATOM 499 CA ASN A 62 36.363 -27.004 2.041 1.00 21.69 C -ANISOU 499 CA ASN A 62 2444 3316 2479 -265 -363 414 C -ATOM 500 C ASN A 62 34.861 -26.833 2.269 1.00 26.87 C -ANISOU 500 C ASN A 62 3068 3981 3160 -265 -398 428 C -ATOM 501 O ASN A 62 34.375 -25.710 2.369 1.00 36.30 O -ANISOU 501 O ASN A 62 4214 5150 4427 -250 -414 461 O -ATOM 502 CB ASN A 62 36.946 -25.785 1.305 1.00 24.88 C -ANISOU 502 CB ASN A 62 2826 3696 2930 -258 -361 471 C -ATOM 503 CG ASN A 62 38.452 -25.672 1.464 1.00 36.50 C -ANISOU 503 CG ASN A 62 4315 5144 4409 -248 -323 448 C -ATOM 504 OD1 ASN A 62 39.053 -26.363 2.291 1.00 36.83 O -ANISOU 504 OD1 ASN A 62 4377 5181 4434 -240 -297 385 O -ATOM 505 ND2 ASN A 62 39.071 -24.797 0.676 1.00 36.86 N -ANISOU 505 ND2 ASN A 62 4352 5176 4479 -247 -318 498 N -ATOM 506 N GLU A 63 34.137 -27.947 2.364 1.00 20.47 N -ANISOU 506 N GLU A 63 2283 3206 2288 -282 -411 404 N -ATOM 507 CA GLU A 63 32.700 -27.902 2.646 1.00 27.40 C -ANISOU 507 CA GLU A 63 3132 4094 3184 -282 -443 412 C -ATOM 508 C GLU A 63 32.417 -27.958 4.145 1.00 26.20 C -ANISOU 508 C GLU A 63 2955 3918 3081 -258 -435 350 C -ATOM 509 O GLU A 63 33.075 -28.670 4.900 1.00 25.93 O -ANISOU 509 O GLU A 63 2945 3880 3027 -252 -408 290 O -ATOM 510 CB GLU A 63 31.973 -29.062 1.966 1.00 28.11 C -ANISOU 510 CB GLU A 63 3261 4236 3184 -313 -463 419 C -ATOM 511 CG GLU A 63 32.280 -29.215 0.497 1.00 42.84 C -ANISOU 511 CG GLU A 63 5158 6131 4989 -339 -470 473 C -ATOM 512 CD GLU A 63 31.424 -28.342 -0.383 1.00 58.90 C -ANISOU 512 CD GLU A 63 7160 8171 7047 -345 -503 545 C -ATOM 513 OE1 GLU A 63 30.940 -27.294 0.099 1.00 64.41 O -ANISOU 513 OE1 GLU A 63 7808 8839 7827 -325 -514 559 O -ATOM 514 OE2 GLU A 63 31.233 -28.715 -1.561 1.00 60.51 O -ANISOU 514 OE2 GLU A 63 7391 8411 7189 -371 -518 587 O -ATOM 515 N LYS A 64 31.414 -27.208 4.570 1.00 26.31 N -ANISOU 515 N LYS A 64 2921 3917 3158 -245 -459 365 N -ATOM 516 CA LYS A 64 30.963 -27.268 5.942 1.00 26.31 C -ANISOU 516 CA LYS A 64 2895 3898 3202 -223 -456 311 C -ATOM 517 C LYS A 64 30.304 -28.625 6.204 1.00 22.12 C -ANISOU 517 C LYS A 64 2397 3405 2602 -241 -463 273 C -ATOM 518 O LYS A 64 29.598 -29.153 5.355 1.00 20.96 O -ANISOU 518 O LYS A 64 2270 3297 2399 -266 -486 304 O -ATOM 519 CB LYS A 64 29.981 -26.130 6.190 1.00 37.02 C -ANISOU 519 CB LYS A 64 4194 5233 4639 -207 -482 343 C -ATOM 520 CG LYS A 64 29.812 -25.747 7.630 1.00 47.84 C -ANISOU 520 CG LYS A 64 5527 6570 6082 -176 -474 293 C -ATOM 521 CD LYS A 64 29.031 -24.452 7.729 1.00 54.69 C -ANISOU 521 CD LYS A 64 6336 7411 7033 -159 -498 333 C -ATOM 522 CE LYS A 64 29.715 -23.340 6.953 1.00 52.07 C -ANISOU 522 CE LYS A 64 5988 7055 6739 -154 -494 386 C -ATOM 523 NZ LYS A 64 28.918 -22.082 7.015 1.00 50.83 N -ANISOU 523 NZ LYS A 64 5775 6874 6663 -138 -519 427 N -ATOM 524 N VAL A 65 30.565 -29.195 7.373 1.00 18.69 N -ANISOU 524 N VAL A 65 1969 2961 2173 -226 -442 205 N -ATOM 525 CA VAL A 65 29.913 -30.418 7.802 1.00 21.64 C -ANISOU 525 CA VAL A 65 2366 3364 2490 -239 -448 164 C -ATOM 526 C VAL A 65 29.625 -30.341 9.292 1.00 17.68 C -ANISOU 526 C VAL A 65 1836 2838 2045 -212 -440 107 C -ATOM 527 O VAL A 65 29.958 -29.361 9.950 1.00 18.67 O -ANISOU 527 O VAL A 65 1923 2923 2248 -184 -430 100 O -ATOM 528 CB VAL A 65 30.784 -31.672 7.542 1.00 13.04 C -ANISOU 528 CB VAL A 65 1339 2301 1316 -257 -423 131 C -ATOM 529 CG1 VAL A 65 31.057 -31.825 6.059 1.00 21.10 C -ANISOU 529 CG1 VAL A 65 2391 3349 2276 -285 -431 185 C -ATOM 530 CG2 VAL A 65 32.090 -31.603 8.344 1.00 15.99 C -ANISOU 530 CG2 VAL A 65 1719 2643 1714 -235 -384 81 C -ATOM 531 N VAL A 66 29.005 -31.385 9.820 1.00 16.59 N -ANISOU 531 N VAL A 66 1715 2724 1866 -220 -444 67 N -ATOM 532 CA AVAL A 66 28.745 -31.475 11.250 1.00 14.78 C -ANISOU 532 CA AVAL A 66 1462 2475 1679 -196 -435 9 C -ATOM 533 CA BVAL A 66 28.758 -31.463 11.250 0.00 18.02 C -ANISOU 533 CA BVAL A 66 1872 2884 2089 -195 -435 9 C -ATOM 534 C VAL A 66 29.320 -32.773 11.792 1.00 20.05 C -ANISOU 534 C VAL A 66 2175 3158 2286 -201 -409 -54 C -ATOM 535 O VAL A 66 29.225 -33.822 11.148 1.00 20.95 O -ANISOU 535 O VAL A 66 2333 3308 2317 -229 -413 -52 O -ATOM 536 CB AVAL A 66 27.225 -31.384 11.528 1.00 20.20 C -ANISOU 536 CB AVAL A 66 2116 3173 2386 -197 -470 21 C -ATOM 537 CB BVAL A 66 27.258 -31.332 11.580 0.00 20.85 C -ANISOU 537 CB BVAL A 66 2197 3253 2474 -195 -469 19 C -ATOM 538 CG1AVAL A 66 26.895 -31.928 12.903 1.00 25.84 C -ANISOU 538 CG1AVAL A 66 2823 3881 3116 -180 -460 -45 C -ATOM 539 CG1BVAL A 66 26.533 -32.634 11.299 0.00 20.48 C -ANISOU 539 CG1BVAL A 66 2186 3251 2344 -222 -482 8 C -ATOM 540 CG2AVAL A 66 26.771 -29.942 11.392 1.00 22.92 C -ANISOU 540 CG2AVAL A 66 2406 3490 2812 -180 -489 69 C -ATOM 541 CG2BVAL A 66 27.069 -30.918 13.024 0.00 23.51 C -ANISOU 541 CG2BVAL A 66 2493 3557 2882 -162 -460 -28 C -ATOM 542 N VAL A 67 29.937 -32.703 12.969 1.00 16.83 N -ANISOU 542 N VAL A 67 1757 2720 1917 -174 -382 -109 N -ATOM 543 CA VAL A 67 30.561 -33.870 13.556 1.00 14.61 C -ANISOU 543 CA VAL A 67 1517 2450 1584 -176 -355 -171 C -ATOM 544 C VAL A 67 29.936 -34.202 14.892 1.00 14.30 C -ANISOU 544 C VAL A 67 1457 2404 1571 -158 -354 -225 C -ATOM 545 O VAL A 67 29.940 -33.386 15.812 1.00 15.49 O -ANISOU 545 O VAL A 67 1566 2521 1800 -129 -348 -243 O -ATOM 546 CB VAL A 67 32.074 -33.641 13.773 1.00 15.21 C -ANISOU 546 CB VAL A 67 1606 2499 1673 -161 -317 -195 C -ATOM 547 CG1 VAL A 67 32.709 -34.844 14.458 1.00 21.55 C -ANISOU 547 CG1 VAL A 67 2451 3313 2426 -161 -288 -262 C -ATOM 548 CG2 VAL A 67 32.750 -33.332 12.450 1.00 16.51 C -ANISOU 548 CG2 VAL A 67 1792 2671 1810 -179 -317 -142 C -ATOM 549 N LYS A 68 29.420 -35.421 15.000 1.00 12.79 N -ANISOU 549 N LYS A 68 1297 2246 1315 -176 -358 -252 N -ATOM 550 CA LYS A 68 28.808 -35.906 16.223 1.00 12.64 C -ANISOU 550 CA LYS A 68 1266 2226 1311 -162 -357 -304 C -ATOM 551 C LYS A 68 29.741 -36.897 16.913 1.00 15.60 C -ANISOU 551 C LYS A 68 1679 2602 1646 -157 -321 -369 C -ATOM 552 O LYS A 68 29.842 -38.066 16.509 1.00 15.67 O -ANISOU 552 O LYS A 68 1737 2644 1575 -181 -316 -382 O -ATOM 553 CB LYS A 68 27.469 -36.574 15.880 1.00 12.17 C -ANISOU 553 CB LYS A 68 1212 2203 1208 -186 -389 -288 C -ATOM 554 CG LYS A 68 26.699 -37.135 17.048 1.00 11.49 C -ANISOU 554 CG LYS A 68 1114 2121 1131 -175 -391 -337 C -ATOM 555 CD LYS A 68 25.333 -37.603 16.526 1.00 15.60 C -ANISOU 555 CD LYS A 68 1635 2677 1615 -200 -426 -308 C -ATOM 556 CE LYS A 68 24.525 -38.341 17.552 1.00 20.22 C -ANISOU 556 CE LYS A 68 2216 3273 2196 -194 -430 -355 C -ATOM 557 NZ LYS A 68 23.236 -38.802 16.909 1.00 15.69 N -ANISOU 557 NZ LYS A 68 1645 2735 1582 -222 -465 -323 N -ATOM 558 N ILE A 69 30.439 -36.419 17.942 1.00 14.89 N -ANISOU 558 N ILE A 69 1567 2476 1612 -126 -296 -410 N -ATOM 559 CA ILE A 69 31.349 -37.253 18.713 1.00 15.90 C -ANISOU 559 CA ILE A 69 1727 2602 1712 -117 -261 -474 C -ATOM 560 C ILE A 69 30.558 -37.973 19.790 1.00 21.50 C -ANISOU 560 C ILE A 69 2432 3321 2418 -109 -264 -522 C -ATOM 561 O ILE A 69 30.034 -37.349 20.720 1.00 21.01 O -ANISOU 561 O ILE A 69 2324 3236 2423 -84 -270 -538 O -ATOM 562 CB ILE A 69 32.492 -36.413 19.323 1.00 16.71 C -ANISOU 562 CB ILE A 69 1810 2663 1877 -86 -232 -495 C -ATOM 563 CG1 ILE A 69 33.206 -35.654 18.198 1.00 19.76 C -ANISOU 563 CG1 ILE A 69 2200 3040 2268 -95 -232 -442 C -ATOM 564 CG2 ILE A 69 33.432 -37.300 20.123 1.00 20.64 C -ANISOU 564 CG2 ILE A 69 2341 3159 2343 -76 -196 -562 C -ATOM 565 CD1 ILE A 69 34.332 -34.779 18.649 1.00 24.56 C -ANISOU 565 CD1 ILE A 69 2788 3608 2936 -68 -206 -456 C -ATOM 566 N LEU A 70 30.444 -39.289 19.641 1.00 20.37 N -ANISOU 566 N LEU A 70 2333 3211 2195 -131 -260 -545 N -ATOM 567 CA LEU A 70 29.596 -40.076 20.519 1.00 23.96 C -ANISOU 567 CA LEU A 70 2787 3680 2637 -129 -265 -586 C -ATOM 568 C LEU A 70 30.206 -40.202 21.906 1.00 30.96 C -ANISOU 568 C LEU A 70 3665 4542 3555 -98 -234 -653 C -ATOM 569 O LEU A 70 31.381 -40.549 22.052 1.00 33.58 O -ANISOU 569 O LEU A 70 4027 4867 3866 -93 -203 -684 O -ATOM 570 CB LEU A 70 29.350 -41.464 19.925 1.00 25.15 C -ANISOU 570 CB LEU A 70 2991 3874 2692 -162 -269 -591 C -ATOM 571 CG LEU A 70 28.742 -41.467 18.522 1.00 22.89 C -ANISOU 571 CG LEU A 70 2716 3615 2364 -195 -299 -527 C -ATOM 572 CD1 LEU A 70 28.592 -42.887 17.996 1.00 31.22 C -ANISOU 572 CD1 LEU A 70 3826 4711 3323 -227 -300 -538 C -ATOM 573 CD2 LEU A 70 27.395 -40.752 18.544 1.00 29.44 C -ANISOU 573 CD2 LEU A 70 3499 4445 3243 -193 -335 -492 C -ATOM 574 N LYS A 71 29.411 -39.913 22.930 1.00 37.86 N -ANISOU 574 N LYS A 71 4499 5404 4482 -77 -244 -675 N -ATOM 575 CA LYS A 71 29.855 -40.160 24.294 1.00 38.35 C -ANISOU 575 CA LYS A 71 4555 5448 4569 -48 -216 -742 C -ATOM 576 C LYS A 71 29.957 -41.665 24.456 1.00 43.80 C -ANISOU 576 C LYS A 71 5296 6168 5178 -65 -202 -783 C -ATOM 577 O LYS A 71 29.251 -42.411 23.770 1.00 43.64 O -ANISOU 577 O LYS A 71 5301 6181 5099 -95 -221 -762 O -ATOM 578 CB LYS A 71 28.876 -39.583 25.320 1.00 35.82 C -ANISOU 578 CB LYS A 71 4181 5111 4318 -24 -232 -755 C -ATOM 579 CG LYS A 71 28.901 -38.067 25.439 1.00 37.30 C -ANISOU 579 CG LYS A 71 4315 5262 4596 0 -240 -727 C -ATOM 580 CD LYS A 71 28.454 -37.637 26.827 1.00 44.12 C -ANISOU 580 CD LYS A 71 5132 6102 5528 34 -238 -767 C -ATOM 581 CE LYS A 71 28.532 -36.129 27.001 1.00 47.17 C -ANISOU 581 CE LYS A 71 5466 6451 6007 60 -245 -742 C -ATOM 582 NZ LYS A 71 27.389 -35.452 26.344 1.00 49.58 N -ANISOU 582 NZ LYS A 71 5740 6763 6337 48 -283 -684 N -ATOM 583 N PRO A 72 30.854 -42.122 25.342 1.00 59.77 N -ANISOU 583 N PRO A 72 7350 8035 7326 133 -514 86 N -ATOM 584 CA PRO A 72 31.000 -43.556 25.608 1.00 66.40 C -ANISOU 584 CA PRO A 72 8186 8830 8212 140 -541 130 C -ATOM 585 C PRO A 72 29.719 -44.126 26.201 1.00 74.42 C -ANISOU 585 C PRO A 72 9234 9848 9195 119 -528 172 C -ATOM 586 O PRO A 72 29.688 -45.283 26.621 1.00 77.36 O -ANISOU 586 O PRO A 72 9611 10188 9593 120 -551 217 O -ATOM 587 CB PRO A 72 32.137 -43.608 26.634 1.00 63.60 C -ANISOU 587 CB PRO A 72 7829 8481 7855 151 -594 160 C -ATOM 588 CG PRO A 72 32.902 -42.343 26.418 1.00 62.79 C -ANISOU 588 CG PRO A 72 7713 8412 7734 157 -592 115 C -ATOM 589 CD PRO A 72 31.867 -41.322 26.051 1.00 60.90 C -ANISOU 589 CD PRO A 72 7490 8208 7443 139 -544 83 C -ATOM 590 N VAL A 73 28.672 -43.308 26.235 1.00 80.09 N -ANISOU 590 N VAL A 73 9972 10603 9857 99 -492 158 N -ATOM 591 CA VAL A 73 27.368 -43.753 26.698 1.00 85.73 C -ANISOU 591 CA VAL A 73 10714 11321 10538 77 -473 190 C -ATOM 592 C VAL A 73 26.847 -44.868 25.792 1.00 85.27 C -ANISOU 592 C VAL A 73 10646 11216 10537 80 -454 190 C -ATOM 593 O VAL A 73 26.482 -44.634 24.636 1.00 81.60 O -ANISOU 593 O VAL A 73 10167 10743 10094 82 -419 147 O -ATOM 594 CB VAL A 73 26.351 -42.588 26.752 1.00 87.64 C -ANISOU 594 CB VAL A 73 10974 11609 10716 58 -433 165 C -ATOM 595 CG1 VAL A 73 25.018 -43.066 27.310 1.00 88.21 C -ANISOU 595 CG1 VAL A 73 11074 11687 10754 33 -414 198 C -ATOM 596 CG2 VAL A 73 26.900 -41.440 27.590 1.00 86.39 C -ANISOU 596 CG2 VAL A 73 10823 11497 10503 55 -450 160 C -ATOM 597 N LYS A 74 26.846 -46.084 26.328 1.00 85.27 N -ANISOU 597 N LYS A 74 10654 11185 10561 80 -478 239 N -ATOM 598 CA LYS A 74 26.312 -47.260 25.640 1.00 80.27 C -ANISOU 598 CA LYS A 74 10015 10505 9979 81 -463 247 C -ATOM 599 C LYS A 74 27.237 -47.829 24.560 1.00 74.78 C -ANISOU 599 C LYS A 74 9283 9764 9365 105 -471 219 C -ATOM 600 O LYS A 74 28.262 -47.236 24.224 1.00 69.76 O -ANISOU 600 O LYS A 74 8625 9134 8746 121 -484 188 O -ATOM 601 CB LYS A 74 24.892 -47.010 25.124 1.00 78.26 C -ANISOU 601 CB LYS A 74 9773 10265 9698 61 -413 227 C -ATOM 602 CG LYS A 74 23.899 -46.635 26.227 1.00 75.70 C -ANISOU 602 CG LYS A 74 9484 9980 9299 35 -403 256 C -ATOM 603 CD LYS A 74 23.861 -47.672 27.352 1.00 78.20 C -ANISOU 603 CD LYS A 74 9822 10280 9609 25 -435 321 C -ATOM 604 CE LYS A 74 24.887 -47.391 28.456 1.00 81.00 C -ANISOU 604 CE LYS A 74 10184 10652 9939 31 -482 350 C -ATOM 605 NZ LYS A 74 24.695 -46.065 29.108 1.00 80.63 N -ANISOU 605 NZ LYS A 74 10153 10664 9820 16 -473 336 N -ATOM 606 N LYS A 75 26.861 -48.990 24.032 1.00 72.99 N -ANISOU 606 N LYS A 75 9051 9494 9188 106 -462 231 N -ATOM 607 CA LYS A 75 27.791 -49.848 23.306 1.00 70.54 C -ANISOU 607 CA LYS A 75 8708 9132 8960 128 -479 220 C -ATOM 608 C LYS A 75 27.358 -50.162 21.875 1.00 62.81 C -ANISOU 608 C LYS A 75 7711 8127 8028 129 -438 177 C -ATOM 609 O LYS A 75 27.637 -49.396 20.953 1.00 63.31 O -ANISOU 609 O LYS A 75 7755 8201 8099 133 -416 125 O -ATOM 610 CB LYS A 75 27.980 -51.147 24.090 1.00 78.55 C -ANISOU 610 CB LYS A 75 9732 10110 10004 132 -516 280 C -ATOM 611 CG LYS A 75 26.970 -51.333 25.220 1.00 82.31 C -ANISOU 611 CG LYS A 75 10248 10606 10418 108 -517 331 C -ATOM 612 CD LYS A 75 27.632 -51.236 26.591 1.00 84.14 C -ANISOU 612 CD LYS A 75 10497 10855 10617 109 -567 377 C -ATOM 613 CE LYS A 75 28.239 -49.860 26.835 1.00 85.27 C -ANISOU 613 CE LYS A 75 10636 11046 10717 113 -573 349 C -ATOM 614 NZ LYS A 75 27.428 -49.015 27.763 1.00 83.83 N -ANISOU 614 NZ LYS A 75 10488 10918 10447 87 -561 363 N -ATOM 615 N LYS A 76 26.689 -51.299 21.695 1.00 55.57 N -ANISOU 615 N LYS A 76 6799 7174 7141 122 -428 201 N -ATOM 616 CA LYS A 76 26.199 -51.711 20.378 1.00 48.97 C -ANISOU 616 CA LYS A 76 5946 6311 6348 120 -389 164 C -ATOM 617 C LYS A 76 25.136 -50.752 19.843 1.00 37.27 C -ANISOU 617 C LYS A 76 4477 4868 4818 101 -343 129 C -ATOM 618 O LYS A 76 24.669 -50.886 18.709 1.00 35.16 O -ANISOU 618 O LYS A 76 4198 4586 4577 96 -309 94 O -ATOM 619 CB LYS A 76 25.621 -53.126 20.432 1.00 50.58 C -ANISOU 619 CB LYS A 76 6158 6472 6589 114 -388 201 C -ATOM 620 CG LYS A 76 24.477 -53.287 21.420 1.00 52.97 C -ANISOU 620 CG LYS A 76 6498 6795 6834 92 -382 247 C -ATOM 621 CD LYS A 76 23.565 -54.439 21.020 1.00 58.69 C -ANISOU 621 CD LYS A 76 7227 7483 7589 80 -359 262 C -ATOM 622 CE LYS A 76 22.619 -54.808 22.149 1.00 62.81 C -ANISOU 622 CE LYS A 76 7786 8017 8060 59 -363 315 C -ATOM 623 NZ LYS A 76 23.363 -55.336 23.330 1.00 64.57 N -ANISOU 623 NZ LYS A 76 8021 8227 8284 66 -414 370 N -ATOM 624 N LYS A 77 24.733 -49.800 20.673 1.00 33.14 N -ANISOU 624 N LYS A 77 3977 4393 4223 90 -344 140 N -ATOM 625 CA LYS A 77 23.899 -48.711 20.196 1.00 35.10 C -ANISOU 625 CA LYS A 77 4232 4679 4425 76 -306 103 C -ATOM 626 C LYS A 77 24.641 -47.953 19.092 1.00 28.18 C -ANISOU 626 C LYS A 77 3330 3804 3573 88 -296 45 C -ATOM 627 O LYS A 77 24.024 -47.397 18.181 1.00 23.31 O -ANISOU 627 O LYS A 77 2710 3198 2947 79 -260 5 O -ATOM 628 CB LYS A 77 23.535 -47.763 21.341 1.00 43.08 C -ANISOU 628 CB LYS A 77 5269 5741 5359 64 -312 122 C -ATOM 629 CG LYS A 77 23.018 -46.413 20.860 1.00 52.46 C -ANISOU 629 CG LYS A 77 6460 6969 6503 56 -281 77 C -ATOM 630 CD LYS A 77 22.330 -45.622 21.958 1.00 51.14 C -ANISOU 630 CD LYS A 77 6320 6849 6260 39 -278 96 C -ATOM 631 CE LYS A 77 21.900 -44.270 21.421 1.00 55.61 C -ANISOU 631 CE LYS A 77 6886 7453 6791 34 -249 49 C -ATOM 632 NZ LYS A 77 21.019 -43.540 22.368 1.00 60.18 N -ANISOU 632 NZ LYS A 77 7490 8075 7300 15 -238 63 N -ATOM 633 N ILE A 78 25.971 -47.935 19.174 1.00 21.48 N -ANISOU 633 N ILE A 78 2462 2945 2755 107 -327 39 N -ATOM 634 CA ILE A 78 26.763 -47.212 18.190 1.00 18.93 C -ANISOU 634 CA ILE A 78 2115 2624 2455 117 -318 -16 C -ATOM 635 C ILE A 78 26.637 -47.851 16.817 1.00 20.90 C -ANISOU 635 C ILE A 78 2344 2835 2763 116 -291 -49 C -ATOM 636 O ILE A 78 26.399 -47.163 15.826 1.00 19.77 O -ANISOU 636 O ILE A 78 2195 2703 2614 109 -261 -96 O -ATOM 637 CB ILE A 78 28.245 -47.140 18.591 1.00 25.23 C -ANISOU 637 CB ILE A 78 2895 3416 3277 137 -358 -14 C -ATOM 638 CG1 ILE A 78 28.405 -46.317 19.867 1.00 31.47 C -ANISOU 638 CG1 ILE A 78 3705 4250 4004 135 -382 12 C -ATOM 639 CG2 ILE A 78 29.061 -46.532 17.467 1.00 31.51 C -ANISOU 639 CG2 ILE A 78 3663 4207 4103 145 -345 -74 C -ATOM 640 CD1 ILE A 78 29.842 -46.246 20.373 1.00 36.61 C -ANISOU 640 CD1 ILE A 78 4338 4896 4675 155 -425 17 C -ATOM 641 N LYS A 79 26.811 -49.168 16.753 1.00 21.64 N -ANISOU 641 N LYS A 79 2427 2883 2913 123 -302 -26 N -ATOM 642 CA LYS A 79 26.642 -49.882 15.495 1.00 22.44 C -ANISOU 642 CA LYS A 79 2509 2945 3071 121 -275 -56 C -ATOM 643 C LYS A 79 25.212 -49.773 14.965 1.00 16.37 C -ANISOU 643 C LYS A 79 1757 2189 2274 99 -234 -65 C -ATOM 644 O LYS A 79 25.000 -49.703 13.758 1.00 17.17 O -ANISOU 644 O LYS A 79 1847 2280 2398 92 -204 -108 O -ATOM 645 CB LYS A 79 27.017 -51.352 15.654 1.00 21.41 C -ANISOU 645 CB LYS A 79 2367 2764 3006 131 -296 -25 C -ATOM 646 CG LYS A 79 28.496 -51.580 15.905 1.00 27.16 C -ANISOU 646 CG LYS A 79 3070 3470 3779 154 -334 -24 C -ATOM 647 CD LYS A 79 28.923 -52.933 15.393 1.00 33.52 C -ANISOU 647 CD LYS A 79 3851 4216 4668 164 -340 -22 C -ATOM 648 CE LYS A 79 30.415 -53.148 15.565 1.00 38.03 C -ANISOU 648 CE LYS A 79 4394 4765 5291 188 -378 -26 C -ATOM 649 NZ LYS A 79 30.792 -54.506 15.089 1.00 37.33 N -ANISOU 649 NZ LYS A 79 4281 4616 5287 199 -383 -23 N -ATOM 650 N ARG A 80 24.229 -49.789 15.859 1.00 17.21 N -ANISOU 650 N ARG A 80 1891 2316 2331 87 -233 -26 N -ATOM 651 CA ARG A 80 22.837 -49.686 15.435 1.00 20.64 C -ANISOU 651 CA ARG A 80 2340 2763 2737 67 -196 -34 C -ATOM 652 C ARG A 80 22.621 -48.387 14.681 1.00 19.09 C -ANISOU 652 C ARG A 80 2143 2600 2509 61 -171 -84 C -ATOM 653 O ARG A 80 22.065 -48.391 13.586 1.00 13.78 O -ANISOU 653 O ARG A 80 1464 1920 1851 51 -140 -116 O -ATOM 654 CB ARG A 80 21.897 -49.749 16.638 1.00 17.29 C -ANISOU 654 CB ARG A 80 1947 2363 2261 55 -199 13 C -ATOM 655 CG ARG A 80 20.432 -49.773 16.279 1.00 18.45 C -ANISOU 655 CG ARG A 80 2108 2519 2384 34 -162 8 C -ATOM 656 CD ARG A 80 19.594 -49.895 17.542 1.00 18.00 C -ANISOU 656 CD ARG A 80 2080 2484 2277 21 -167 55 C -ATOM 657 NE ARG A 80 19.612 -48.661 18.322 1.00 20.32 N -ANISOU 657 NE ARG A 80 2387 2826 2507 18 -175 54 N -ATOM 658 CZ ARG A 80 19.137 -48.553 19.562 1.00 27.70 C -ANISOU 658 CZ ARG A 80 3347 3786 3392 7 -184 93 C -ATOM 659 NH1 ARG A 80 18.636 -49.614 20.177 1.00 28.92 N -ANISOU 659 NH1 ARG A 80 3516 3922 3552 -3 -188 136 N -ATOM 660 NH2 ARG A 80 19.174 -47.385 20.192 1.00 24.51 N -ANISOU 660 NH2 ARG A 80 2954 3427 2932 4 -188 87 N -ATOM 661 N GLU A 81 23.067 -47.271 15.258 1.00 17.61 N -ANISOU 661 N GLU A 81 1963 2451 2278 65 -185 -89 N -ATOM 662 CA GLU A 81 22.856 -45.980 14.616 1.00 14.79 C -ANISOU 662 CA GLU A 81 1607 2126 1887 59 -164 -133 C -ATOM 663 C GLU A 81 23.611 -45.938 13.288 1.00 15.07 C -ANISOU 663 C GLU A 81 1617 2138 1970 64 -153 -182 C -ATOM 664 O GLU A 81 23.076 -45.504 12.277 1.00 12.64 O -ANISOU 664 O GLU A 81 1309 1835 1659 53 -125 -219 O -ATOM 665 CB GLU A 81 23.263 -44.819 15.530 1.00 13.15 C -ANISOU 665 CB GLU A 81 1411 1962 1625 63 -182 -129 C -ATOM 666 CG GLU A 81 23.170 -43.451 14.858 1.00 16.14 C -ANISOU 666 CG GLU A 81 1790 2370 1972 58 -162 -176 C -ATOM 667 CD GLU A 81 23.466 -42.292 15.800 1.00 15.49 C -ANISOU 667 CD GLU A 81 1720 2331 1833 61 -178 -172 C -ATOM 668 OE1 GLU A 81 23.835 -42.538 16.966 1.00 17.69 O -ANISOU 668 OE1 GLU A 81 2006 2617 2098 66 -205 -133 O -ATOM 669 OE2 GLU A 81 23.326 -41.132 15.373 1.00 17.23 O -ANISOU 669 OE2 GLU A 81 1944 2579 2024 56 -163 -207 O -ATOM 670 N ILE A 82 24.860 -46.399 13.293 1.00 14.70 N -ANISOU 670 N ILE A 82 1550 2066 1969 80 -177 -184 N -ATOM 671 CA ILE A 82 25.650 -46.429 12.065 1.00 16.94 C -ANISOU 671 CA ILE A 82 1809 2327 2303 83 -167 -232 C -ATOM 672 C ILE A 82 25.022 -47.246 10.945 1.00 14.45 C -ANISOU 672 C ILE A 82 1484 1978 2027 72 -137 -249 C -ATOM 673 O ILE A 82 24.960 -46.791 9.808 1.00 17.47 O -ANISOU 673 O ILE A 82 1861 2362 2416 62 -113 -295 O -ATOM 674 CB ILE A 82 27.076 -46.943 12.315 1.00 17.93 C -ANISOU 674 CB ILE A 82 1910 2425 2477 103 -199 -228 C -ATOM 675 CG1 ILE A 82 27.860 -45.916 13.140 1.00 19.47 C -ANISOU 675 CG1 ILE A 82 2109 2656 2634 113 -224 -226 C -ATOM 676 CG2 ILE A 82 27.736 -47.211 10.986 1.00 18.58 C -ANISOU 676 CG2 ILE A 82 1965 2476 2617 103 -182 -277 C -ATOM 677 CD1 ILE A 82 29.275 -46.375 13.546 1.00 19.46 C -ANISOU 677 CD1 ILE A 82 2085 2632 2678 134 -261 -219 C -ATOM 678 N LYS A 83 24.574 -48.461 11.257 1.00 16.91 N -ANISOU 678 N LYS A 83 1798 2261 2367 72 -140 -214 N -ATOM 679 CA LYS A 83 23.957 -49.340 10.267 1.00 15.88 C -ANISOU 679 CA LYS A 83 1660 2098 2277 60 -112 -227 C -ATOM 680 C LYS A 83 22.671 -48.732 9.705 1.00 15.01 C -ANISOU 680 C LYS A 83 1566 2012 2123 40 -79 -245 C -ATOM 681 O LYS A 83 22.418 -48.753 8.494 1.00 14.41 O -ANISOU 681 O LYS A 83 1482 1926 2069 28 -53 -283 O -ATOM 682 CB LYS A 83 23.666 -50.715 10.880 1.00 15.92 C -ANISOU 682 CB LYS A 83 1667 2069 2312 63 -124 -180 C -ATOM 683 CG LYS A 83 23.158 -51.746 9.891 1.00 20.59 C -ANISOU 683 CG LYS A 83 2248 2623 2953 53 -97 -193 C -ATOM 684 CD LYS A 83 24.091 -51.880 8.710 1.00 28.36 C -ANISOU 684 CD LYS A 83 3203 3579 3993 56 -88 -242 C -ATOM 685 CE LYS A 83 23.485 -52.752 7.630 1.00 29.59 C -ANISOU 685 CE LYS A 83 3350 3703 4190 41 -56 -261 C -ATOM 686 NZ LYS A 83 24.445 -52.981 6.521 1.00 31.14 N -ANISOU 686 NZ LYS A 83 3517 3870 4445 42 -47 -309 N -ATOM 687 N ILE A 84 21.862 -48.174 10.593 1.00 13.52 N -ANISOU 687 N ILE A 84 1402 1859 1876 35 -82 -218 N -ATOM 688 CA ILE A 84 20.628 -47.524 10.169 1.00 14.53 C -ANISOU 688 CA ILE A 84 1545 2013 1963 17 -53 -233 C -ATOM 689 C ILE A 84 20.924 -46.357 9.222 1.00 14.65 C -ANISOU 689 C ILE A 84 1556 2048 1964 13 -41 -285 C -ATOM 690 O ILE A 84 20.294 -46.227 8.174 1.00 17.01 O -ANISOU 690 O ILE A 84 1854 2344 2267 -1 -15 -314 O -ATOM 691 CB ILE A 84 19.787 -47.068 11.388 1.00 15.22 C -ANISOU 691 CB ILE A 84 1657 2136 1990 13 -59 -197 C -ATOM 692 CG1 ILE A 84 19.137 -48.292 12.054 1.00 18.48 C -ANISOU 692 CG1 ILE A 84 2078 2528 2415 9 -61 -151 C -ATOM 693 CG2 ILE A 84 18.709 -46.077 10.968 1.00 16.82 C -ANISOU 693 CG2 ILE A 84 1872 2371 2146 -1 -34 -220 C -ATOM 694 CD1 ILE A 84 18.420 -47.998 13.358 1.00 20.30 C -ANISOU 694 CD1 ILE A 84 2333 2791 2590 4 -68 -112 C -ATOM 695 N LEU A 85 21.880 -45.505 9.590 1.00 13.95 N -ANISOU 695 N LEU A 85 1464 1978 1858 24 -60 -295 N -ATOM 696 CA LEU A 85 22.262 -44.380 8.732 1.00 12.39 C -ANISOU 696 CA LEU A 85 1263 1798 1646 20 -50 -343 C -ATOM 697 C LEU A 85 22.742 -44.859 7.367 1.00 13.72 C -ANISOU 697 C LEU A 85 1412 1933 1868 14 -34 -383 C -ATOM 698 O LEU A 85 22.444 -44.247 6.344 1.00 15.24 O -ANISOU 698 O LEU A 85 1607 2133 2051 0 -12 -421 O -ATOM 699 CB LEU A 85 23.346 -43.523 9.403 1.00 11.31 C -ANISOU 699 CB LEU A 85 1125 1684 1489 34 -74 -346 C -ATOM 700 CG LEU A 85 22.857 -42.634 10.560 1.00 13.05 C -ANISOU 700 CG LEU A 85 1368 1947 1645 35 -85 -321 C -ATOM 701 CD1 LEU A 85 24.032 -42.138 11.415 1.00 14.85 C -ANISOU 701 CD1 LEU A 85 1591 2190 1861 51 -114 -313 C -ATOM 702 CD2 LEU A 85 22.024 -41.465 10.033 1.00 13.00 C -ANISOU 702 CD2 LEU A 85 1374 1970 1593 22 -62 -349 C -ATOM 703 N GLU A 86 23.509 -45.945 7.351 1.00 18.52 N -ANISOU 703 N GLU A 86 2001 2504 2533 23 -44 -375 N -ATOM 704 CA GLU A 86 23.985 -46.489 6.081 1.00 20.17 C -ANISOU 704 CA GLU A 86 2189 2679 2797 16 -27 -413 C -ATOM 705 C GLU A 86 22.861 -47.113 5.255 1.00 19.39 C -ANISOU 705 C GLU A 86 2094 2564 2710 -3 2 -419 C -ATOM 706 O GLU A 86 22.788 -46.897 4.047 1.00 16.08 O -ANISOU 706 O GLU A 86 1670 2139 2302 -18 24 -461 O -ATOM 707 CB GLU A 86 25.144 -47.460 6.291 1.00 16.99 C -ANISOU 707 CB GLU A 86 1761 2239 2455 32 -47 -406 C -ATOM 708 CG GLU A 86 26.458 -46.722 6.514 1.00 19.51 C -ANISOU 708 CG GLU A 86 2068 2570 2773 46 -68 -426 C -ATOM 709 CD GLU A 86 27.627 -47.636 6.802 1.00 28.89 C -ANISOU 709 CD GLU A 86 3230 3723 4023 64 -91 -417 C -ATOM 710 OE1 GLU A 86 27.481 -48.876 6.684 1.00 29.59 O -ANISOU 710 OE1 GLU A 86 3309 3773 4161 66 -89 -401 O -ATOM 711 OE2 GLU A 86 28.694 -47.095 7.168 1.00 29.86 O -ANISOU 711 OE2 GLU A 86 3343 3856 4146 77 -112 -427 O -ATOM 712 N ASN A 87 21.985 -47.874 5.905 1.00 19.41 N -ANISOU 712 N ASN A 87 2106 2560 2709 -3 1 -377 N -ATOM 713 CA ASN A 87 20.816 -48.424 5.213 1.00 20.98 C -ANISOU 713 CA ASN A 87 2310 2748 2914 -21 29 -380 C -ATOM 714 C ASN A 87 19.945 -47.357 4.556 1.00 19.21 C -ANISOU 714 C ASN A 87 2100 2554 2643 -38 49 -408 C -ATOM 715 O ASN A 87 19.450 -47.546 3.449 1.00 17.41 O -ANISOU 715 O ASN A 87 1870 2315 2431 -55 73 -435 O -ATOM 716 CB ASN A 87 19.955 -49.263 6.160 1.00 19.87 C -ANISOU 716 CB ASN A 87 2181 2602 2768 -19 24 -330 C -ATOM 717 CG ASN A 87 20.600 -50.577 6.524 1.00 21.93 C -ANISOU 717 CG ASN A 87 2427 2821 3085 -7 10 -304 C -ATOM 718 OD1 ASN A 87 21.596 -50.980 5.920 1.00 21.18 O -ANISOU 718 OD1 ASN A 87 2310 2697 3040 -2 7 -328 O -ATOM 719 ND2 ASN A 87 20.030 -51.261 7.518 1.00 17.18 N -ANISOU 719 ND2 ASN A 87 1838 2216 2476 -4 0 -255 N -ATOM 720 N LEU A 88 19.778 -46.228 5.233 1.00 15.95 N -ANISOU 720 N LEU A 88 1703 2181 2176 -33 39 -401 N -ATOM 721 CA LEU A 88 18.824 -45.208 4.808 1.00 12.77 C -ANISOU 721 CA LEU A 88 1317 1809 1727 -47 54 -420 C -ATOM 722 C LEU A 88 19.453 -44.119 3.939 1.00 15.70 C -ANISOU 722 C LEU A 88 1686 2193 2087 -52 58 -466 C -ATOM 723 O LEU A 88 18.756 -43.245 3.430 1.00 15.46 O -ANISOU 723 O LEU A 88 1668 2184 2022 -64 70 -486 O -ATOM 724 CB LEU A 88 18.159 -44.556 6.029 1.00 17.62 C -ANISOU 724 CB LEU A 88 1949 2459 2286 -41 44 -387 C -ATOM 725 CG LEU A 88 17.305 -45.438 6.947 1.00 18.61 C -ANISOU 725 CG LEU A 88 2082 2580 2408 -41 43 -342 C -ATOM 726 CD1 LEU A 88 16.814 -44.645 8.155 1.00 19.32 C -ANISOU 726 CD1 LEU A 88 2191 2709 2441 -37 33 -316 C -ATOM 727 CD2 LEU A 88 16.123 -46.027 6.190 1.00 16.43 C -ANISOU 727 CD2 LEU A 88 1808 2292 2145 -58 69 -347 C -ATOM 728 N ARG A 89 20.764 -44.185 3.750 1.00 14.49 N -ANISOU 728 N ARG A 89 1518 2025 1964 -44 47 -484 N -ATOM 729 CA ARG A 89 21.484 -43.102 3.091 1.00 17.92 C -ANISOU 729 CA ARG A 89 1951 2473 2383 -48 48 -525 C -ATOM 730 C ARG A 89 21.001 -42.898 1.665 1.00 20.43 C -ANISOU 730 C ARG A 89 2273 2785 2706 -72 74 -565 C -ATOM 731 O ARG A 89 20.855 -43.854 0.903 1.00 15.60 O -ANISOU 731 O ARG A 89 1649 2142 2135 -83 89 -575 O -ATOM 732 CB ARG A 89 22.997 -43.363 3.132 1.00 20.16 C -ANISOU 732 CB ARG A 89 2215 2738 2707 -36 34 -539 C -ATOM 733 CG ARG A 89 23.854 -42.207 2.630 1.00 24.12 C -ANISOU 733 CG ARG A 89 2717 3257 3192 -39 33 -580 C -ATOM 734 CD ARG A 89 25.283 -42.291 3.187 1.00 21.61 C -ANISOU 734 CD ARG A 89 2381 2932 2898 -21 11 -581 C -ATOM 735 NE ARG A 89 25.871 -43.608 2.952 1.00 17.86 N -ANISOU 735 NE ARG A 89 1882 2415 2489 -16 10 -579 N -ATOM 736 CZ ARG A 89 26.865 -44.131 3.664 1.00 29.70 C -ANISOU 736 CZ ARG A 89 3364 3900 4022 4 -13 -564 C -ATOM 737 NH1 ARG A 89 27.404 -43.449 4.672 1.00 28.08 N -ANISOU 737 NH1 ARG A 89 3163 3721 3787 20 -38 -547 N -ATOM 738 NH2 ARG A 89 27.324 -45.343 3.365 1.00 27.34 N -ANISOU 738 NH2 ARG A 89 3041 3560 3786 7 -12 -565 N -ATOM 739 N GLY A 90 20.750 -41.643 1.313 1.00 18.08 N -ANISOU 739 N GLY A 90 1990 2515 2365 -80 77 -587 N -ATOM 740 CA GLY A 90 20.262 -41.307 -0.013 1.00 15.39 C -ANISOU 740 CA GLY A 90 1655 2172 2021 -104 97 -623 C -ATOM 741 C GLY A 90 18.742 -41.294 -0.103 1.00 20.97 C -ANISOU 741 C GLY A 90 2376 2890 2703 -114 108 -608 C -ATOM 742 O GLY A 90 18.181 -40.884 -1.117 1.00 23.78 O -ANISOU 742 O GLY A 90 2740 3248 3048 -133 122 -634 O -ATOM 743 N GLY A 91 18.073 -41.754 0.950 1.00 18.29 N -ANISOU 743 N GLY A 91 2039 2556 2355 -102 102 -567 N -ATOM 744 CA GLY A 91 16.612 -41.768 0.975 1.00 15.75 C -ANISOU 744 CA GLY A 91 1728 2245 2010 -111 113 -552 C -ATOM 745 C GLY A 91 16.058 -40.359 1.088 1.00 16.34 C -ANISOU 745 C GLY A 91 1821 2355 2032 -112 109 -561 C -ATOM 746 O GLY A 91 16.758 -39.454 1.522 1.00 15.24 O -ANISOU 746 O GLY A 91 1686 2235 1869 -102 95 -567 O -ATOM 747 N PRO A 92 14.797 -40.152 0.677 1.00 13.63 N -ANISOU 747 N PRO A 92 1487 2021 1671 -125 120 -563 N -ATOM 748 CA PRO A 92 14.239 -38.790 0.685 1.00 10.85 C -ANISOU 748 CA PRO A 92 1150 1701 1273 -126 116 -575 C -ATOM 749 C PRO A 92 14.276 -38.131 2.061 1.00 12.49 C -ANISOU 749 C PRO A 92 1364 1936 1445 -108 102 -550 C -ATOM 750 O PRO A 92 13.742 -38.676 3.018 1.00 14.51 O -ANISOU 750 O PRO A 92 1619 2196 1697 -101 101 -517 O -ATOM 751 CB PRO A 92 12.789 -38.992 0.213 1.00 15.75 C -ANISOU 751 CB PRO A 92 1774 2321 1889 -140 130 -573 C -ATOM 752 CG PRO A 92 12.524 -40.431 0.318 1.00 22.20 C -ANISOU 752 CG PRO A 92 2580 3113 2742 -142 140 -552 C -ATOM 753 CD PRO A 92 13.825 -41.155 0.223 1.00 18.05 C -ANISOU 753 CD PRO A 92 2041 2562 2254 -137 136 -556 C -ATOM 754 N ASN A 93 14.931 -36.974 2.156 1.00 15.60 N -ANISOU 754 N ASN A 93 1766 2349 1813 -102 91 -567 N -ATOM 755 CA ASN A 93 14.928 -36.189 3.391 1.00 16.13 C -ANISOU 755 CA ASN A 93 1841 2447 1842 -88 79 -548 C -ATOM 756 C ASN A 93 15.581 -36.863 4.605 1.00 17.10 C -ANISOU 756 C ASN A 93 1957 2568 1973 -72 67 -515 C -ATOM 757 O ASN A 93 15.361 -36.460 5.735 1.00 15.52 O -ANISOU 757 O ASN A 93 1763 2391 1742 -63 59 -493 O -ATOM 758 CB ASN A 93 13.493 -35.719 3.694 1.00 16.21 C -ANISOU 758 CB ASN A 93 1860 2477 1822 -91 85 -539 C -ATOM 759 CG ASN A 93 12.975 -34.770 2.630 1.00 19.04 C -ANISOU 759 CG ASN A 93 2228 2842 2166 -103 90 -571 C -ATOM 760 OD1 ASN A 93 13.764 -34.182 1.890 1.00 15.66 O -ANISOU 760 OD1 ASN A 93 1802 2409 1737 -108 86 -599 O -ATOM 761 ND2 ASN A 93 11.648 -34.609 2.550 1.00 15.29 N -ANISOU 761 ND2 ASN A 93 1756 2375 1678 -110 98 -568 N -ATOM 762 N ILE A 94 16.389 -37.889 4.370 1.00 14.72 N -ANISOU 762 N ILE A 94 1642 2238 1713 -70 65 -513 N -ATOM 763 CA ILE A 94 17.151 -38.512 5.458 1.00 11.60 C -ANISOU 763 CA ILE A 94 1239 1838 1329 -55 50 -482 C -ATOM 764 C ILE A 94 18.513 -37.817 5.534 1.00 11.64 C -ANISOU 764 C ILE A 94 1241 1851 1331 -46 35 -501 C -ATOM 765 O ILE A 94 19.142 -37.618 4.517 1.00 11.72 O -ANISOU 765 O ILE A 94 1246 1848 1360 -52 40 -535 O -ATOM 766 CB ILE A 94 17.398 -40.017 5.164 1.00 17.52 C -ANISOU 766 CB ILE A 94 1974 2550 2132 -56 54 -470 C -ATOM 767 CG1 ILE A 94 16.071 -40.746 4.877 1.00 15.03 C -ANISOU 767 CG1 ILE A 94 1661 2225 1824 -68 72 -458 C -ATOM 768 CG2 ILE A 94 18.211 -40.673 6.287 1.00 18.80 C -ANISOU 768 CG2 ILE A 94 2130 2706 2309 -39 34 -437 C -ATOM 769 CD1 ILE A 94 15.070 -40.683 6.012 1.00 15.09 C -ANISOU 769 CD1 ILE A 94 1681 2256 1798 -65 71 -424 C -ATOM 770 N ILE A 95 18.963 -37.449 6.729 1.00 11.55 N -ANISOU 770 N ILE A 95 1234 1860 1296 -32 17 -479 N -ATOM 771 CA ILE A 95 20.273 -36.826 6.849 1.00 11.13 C -ANISOU 771 CA ILE A 95 1176 1814 1240 -23 2 -496 C -ATOM 772 C ILE A 95 21.332 -37.781 6.289 1.00 12.75 C -ANISOU 772 C ILE A 95 1361 1984 1500 -20 -1 -506 C -ATOM 773 O ILE A 95 21.238 -39.009 6.461 1.00 12.96 O -ANISOU 773 O ILE A 95 1378 1985 1561 -17 -2 -482 O -ATOM 774 CB ILE A 95 20.597 -36.440 8.316 1.00 11.01 C -ANISOU 774 CB ILE A 95 1166 1824 1192 -8 -18 -466 C -ATOM 775 CG1 ILE A 95 21.732 -35.409 8.345 1.00 12.93 C -ANISOU 775 CG1 ILE A 95 1408 2083 1420 -2 -29 -491 C -ATOM 776 CG2 ILE A 95 20.946 -37.676 9.154 1.00 12.19 C -ANISOU 776 CG2 ILE A 95 1306 1955 1369 2 -32 -427 C -ATOM 777 CD1 ILE A 95 21.335 -34.035 7.849 1.00 14.05 C -ANISOU 777 CD1 ILE A 95 1564 2249 1524 -11 -19 -522 C -ATOM 778 N THR A 96 22.320 -37.220 5.597 1.00 15.31 N -ANISOU 778 N THR A 96 1679 2304 1832 -22 -2 -543 N -ATOM 779 CA THR A 96 23.376 -38.007 4.991 1.00 11.90 C -ANISOU 779 CA THR A 96 1227 1841 1454 -21 -3 -560 C -ATOM 780 C THR A 96 24.583 -38.136 5.907 1.00 14.24 C -ANISOU 780 C THR A 96 1511 2138 1761 -2 -27 -546 C -ATOM 781 O THR A 96 25.209 -37.147 6.294 1.00 18.06 O -ANISOU 781 O THR A 96 1999 2646 2216 4 -39 -557 O -ATOM 782 CB THR A 96 23.843 -37.402 3.650 1.00 16.26 C -ANISOU 782 CB THR A 96 1777 2387 2013 -36 12 -612 C -ATOM 783 OG1 THR A 96 22.788 -37.499 2.694 1.00 18.45 O -ANISOU 783 OG1 THR A 96 2064 2658 2290 -55 33 -624 O -ATOM 784 CG2 THR A 96 25.057 -38.150 3.111 1.00 21.88 C -ANISOU 784 CG2 THR A 96 2466 3068 2780 -35 11 -633 C -ATOM 785 N LEU A 97 24.894 -39.373 6.244 1.00 14.79 N -ANISOU 785 N LEU A 97 1565 2180 1873 7 -36 -522 N -ATOM 786 CA LEU A 97 26.129 -39.680 6.941 1.00 16.95 C -ANISOU 786 CA LEU A 97 1823 2446 2171 25 -61 -512 C -ATOM 787 C LEU A 97 27.234 -39.676 5.910 1.00 15.10 C -ANISOU 787 C LEU A 97 1569 2192 1977 21 -55 -558 C -ATOM 788 O LEU A 97 27.267 -40.522 5.022 1.00 16.78 O -ANISOU 788 O LEU A 97 1768 2372 2236 13 -41 -574 O -ATOM 789 CB LEU A 97 26.042 -41.055 7.595 1.00 19.71 C -ANISOU 789 CB LEU A 97 2164 2770 2557 36 -74 -470 C -ATOM 790 CG LEU A 97 27.300 -41.519 8.340 1.00 15.61 C -ANISOU 790 CG LEU A 97 1626 2238 2068 55 -103 -455 C -ATOM 791 CD1 LEU A 97 27.589 -40.640 9.545 1.00 14.71 C -ANISOU 791 CD1 LEU A 97 1523 2160 1904 66 -127 -434 C -ATOM 792 CD2 LEU A 97 27.125 -42.960 8.777 1.00 16.73 C -ANISOU 792 CD2 LEU A 97 1760 2347 2251 63 -113 -416 C -ATOM 793 N ALA A 98 28.141 -38.717 6.022 1.00 13.74 N -ANISOU 793 N ALA A 98 1395 2038 1786 25 -65 -581 N -ATOM 794 CA ALA A 98 29.205 -38.567 5.038 1.00 17.45 C -ANISOU 794 CA ALA A 98 1848 2493 2289 19 -57 -630 C -ATOM 795 C ALA A 98 30.426 -39.427 5.344 1.00 16.81 C -ANISOU 795 C ALA A 98 1739 2386 2264 35 -76 -627 C -ATOM 796 O ALA A 98 31.154 -39.845 4.436 1.00 17.32 O -ANISOU 796 O ALA A 98 1781 2422 2375 29 -65 -663 O -ATOM 797 CB ALA A 98 29.607 -37.117 4.930 1.00 19.68 C -ANISOU 797 CB ALA A 98 2142 2808 2528 13 -56 -659 C -ATOM 798 N ASP A 99 30.661 -39.699 6.621 1.00 14.01 N -ANISOU 798 N ASP A 99 1381 2038 1904 55 -104 -585 N -ATOM 799 CA ASP A 99 31.871 -40.404 7.001 1.00 16.23 C -ANISOU 799 CA ASP A 99 1635 2296 2235 72 -128 -581 C -ATOM 800 C ASP A 99 31.774 -40.806 8.464 1.00 18.17 C -ANISOU 800 C ASP A 99 1886 2550 2469 91 -159 -524 C -ATOM 801 O ASP A 99 30.901 -40.337 9.193 1.00 15.16 O -ANISOU 801 O ASP A 99 1529 2197 2033 89 -162 -494 O -ATOM 802 CB ASP A 99 33.071 -39.476 6.802 1.00 18.00 C -ANISOU 802 CB ASP A 99 1848 2534 2456 74 -133 -622 C -ATOM 803 CG ASP A 99 34.365 -40.223 6.489 1.00 17.41 C -ANISOU 803 CG ASP A 99 1738 2426 2450 83 -143 -644 C -ATOM 804 OD1 ASP A 99 34.409 -41.468 6.574 1.00 18.50 O -ANISOU 804 OD1 ASP A 99 1860 2530 2641 93 -151 -624 O -ATOM 805 OD2 ASP A 99 35.345 -39.540 6.140 1.00 19.56 O -ANISOU 805 OD2 ASP A 99 1999 2706 2726 81 -143 -685 O -ATOM 806 N ILE A 100 32.673 -41.688 8.887 1.00 17.05 N -ANISOU 806 N ILE A 100 1720 2381 2377 108 -184 -510 N -ATOM 807 CA ILE A 100 32.795 -42.056 10.288 1.00 13.66 C -ANISOU 807 CA ILE A 100 1294 1958 1938 126 -219 -457 C -ATOM 808 C ILE A 100 34.291 -42.111 10.553 1.00 14.50 C -ANISOU 808 C ILE A 100 1373 2054 2082 143 -247 -470 C -ATOM 809 O ILE A 100 35.022 -42.741 9.793 1.00 18.43 O -ANISOU 809 O ILE A 100 1843 2518 2642 146 -242 -499 O -ATOM 810 CB ILE A 100 32.230 -43.455 10.560 1.00 17.79 C -ANISOU 810 CB ILE A 100 1815 2447 2496 131 -225 -415 C -ATOM 811 CG1 ILE A 100 30.811 -43.592 10.009 1.00 21.92 C -ANISOU 811 CG1 ILE A 100 2358 2970 2998 112 -192 -412 C -ATOM 812 CG2 ILE A 100 32.272 -43.743 12.057 1.00 18.94 C -ANISOU 812 CG2 ILE A 100 1971 2603 2623 146 -261 -358 C -ATOM 813 CD1 ILE A 100 30.397 -45.041 9.730 1.00 22.93 C -ANISOU 813 CD1 ILE A 100 2477 3055 3180 112 -186 -392 C -ATOM 814 N VAL A 101 34.743 -41.435 11.601 1.00 12.67 N -ANISOU 814 N VAL A 101 1148 1853 1812 154 -274 -451 N -ATOM 815 CA VAL A 101 36.164 -41.418 11.940 1.00 12.95 C -ANISOU 815 CA VAL A 101 1158 1883 1880 170 -303 -462 C -ATOM 816 C VAL A 101 36.305 -41.701 13.429 1.00 19.18 C -ANISOU 816 C VAL A 101 1954 2682 2652 186 -345 -405 C -ATOM 817 O VAL A 101 35.346 -41.553 14.190 1.00 19.93 O -ANISOU 817 O VAL A 101 2078 2800 2695 181 -346 -366 O -ATOM 818 CB VAL A 101 36.833 -40.062 11.632 1.00 17.75 C -ANISOU 818 CB VAL A 101 1765 2523 2457 164 -295 -509 C -ATOM 819 CG1 VAL A 101 36.673 -39.683 10.143 1.00 17.91 C -ANISOU 819 CG1 VAL A 101 1783 2536 2487 145 -254 -566 C -ATOM 820 CG2 VAL A 101 36.281 -38.968 12.545 1.00 18.27 C -ANISOU 820 CG2 VAL A 101 1861 2638 2442 160 -301 -486 C -ATOM 821 N LYS A 102 37.501 -42.114 13.840 1.00 16.87 N -ANISOU 821 N LYS A 102 1635 2373 2402 205 -378 -402 N -ATOM 822 CA LYS A 102 37.788 -42.335 15.250 1.00 16.94 C -ANISOU 822 CA LYS A 102 1650 2392 2395 220 -422 -349 C -ATOM 823 C LYS A 102 38.310 -41.036 15.830 1.00 21.09 C -ANISOU 823 C LYS A 102 2183 2964 2867 220 -434 -361 C -ATOM 824 O LYS A 102 39.368 -40.550 15.421 1.00 22.12 O -ANISOU 824 O LYS A 102 2290 3096 3018 225 -437 -404 O -ATOM 825 CB LYS A 102 38.858 -43.425 15.418 1.00 19.34 C -ANISOU 825 CB LYS A 102 1919 2654 2775 241 -457 -339 C -ATOM 826 CG LYS A 102 38.492 -44.754 14.770 1.00 29.98 C -ANISOU 826 CG LYS A 102 3254 3950 4186 242 -445 -333 C -ATOM 827 CD LYS A 102 39.469 -45.859 15.165 1.00 44.03 C -ANISOU 827 CD LYS A 102 5003 5688 6038 265 -485 -312 C -ATOM 828 CE LYS A 102 39.078 -47.185 14.531 1.00 45.45 C -ANISOU 828 CE LYS A 102 5171 5816 6281 266 -472 -306 C -ATOM 829 NZ LYS A 102 39.629 -48.348 15.281 1.00 50.62 N -ANISOU 829 NZ LYS A 102 5809 6433 6990 288 -517 -262 N -ATOM 830 N ASP A 103 37.599 -40.469 16.791 1.00 15.74 N -ANISOU 830 N ASP A 103 1638 1947 2394 -55 -449 -203 N -ATOM 831 CA ASP A 103 38.127 -39.275 17.428 1.00 16.68 C -ANISOU 831 CA ASP A 103 1733 2018 2587 -73 -484 -223 C -ATOM 832 C ASP A 103 39.247 -39.661 18.407 1.00 19.33 C -ANISOU 832 C ASP A 103 2059 2352 2932 -86 -522 -247 C -ATOM 833 O ASP A 103 39.066 -40.527 19.260 1.00 19.43 O -ANISOU 833 O ASP A 103 2103 2390 2888 -81 -538 -286 O -ATOM 834 CB ASP A 103 37.035 -38.463 18.117 1.00 13.90 C -ANISOU 834 CB ASP A 103 1406 1643 2234 -74 -499 -269 C -ATOM 835 CG ASP A 103 37.561 -37.160 18.663 1.00 22.96 C -ANISOU 835 CG ASP A 103 2529 2735 3459 -93 -532 -286 C -ATOM 836 OD1 ASP A 103 37.670 -36.192 17.884 1.00 23.60 O -ANISOU 836 OD1 ASP A 103 2582 2786 3598 -99 -519 -252 O -ATOM 837 OD2 ASP A 103 37.881 -37.098 19.867 1.00 24.50 O -ANISOU 837 OD2 ASP A 103 2735 2917 3657 -104 -572 -333 O -ATOM 838 N PRO A 104 40.417 -39.021 18.279 1.00 21.38 N -ANISOU 838 N PRO A 104 2275 2584 3264 -102 -538 -224 N -ATOM 839 CA PRO A 104 41.566 -39.448 19.084 1.00 20.53 C -ANISOU 839 CA PRO A 104 2154 2479 3166 -114 -571 -238 C -ATOM 840 C PRO A 104 41.509 -38.921 20.523 1.00 20.26 C -ANISOU 840 C PRO A 104 2137 2418 3145 -130 -620 -300 C -ATOM 841 O PRO A 104 42.218 -39.426 21.399 1.00 23.15 O -ANISOU 841 O PRO A 104 2502 2793 3500 -138 -650 -324 O -ATOM 842 CB PRO A 104 42.746 -38.820 18.338 1.00 22.97 C -ANISOU 842 CB PRO A 104 2409 2766 3551 -127 -569 -185 C -ATOM 843 CG PRO A 104 42.186 -37.543 17.813 1.00 21.03 C -ANISOU 843 CG PRO A 104 2152 2481 3356 -134 -560 -174 C -ATOM 844 CD PRO A 104 40.742 -37.862 17.425 1.00 16.97 C -ANISOU 844 CD PRO A 104 1677 1988 2781 -112 -527 -183 C -ATOM 845 N VAL A 105 40.686 -37.905 20.756 1.00 14.93 N -ANISOU 845 N VAL A 105 1474 1710 2490 -134 -627 -326 N -ATOM 846 CA VAL A 105 40.521 -37.351 22.096 1.00 14.93 C -ANISOU 846 CA VAL A 105 1493 1681 2499 -148 -671 -386 C -ATOM 847 C VAL A 105 39.449 -38.097 22.887 1.00 19.26 C -ANISOU 847 C VAL A 105 2093 2258 2968 -132 -673 -436 C -ATOM 848 O VAL A 105 39.673 -38.473 24.034 1.00 21.24 O -ANISOU 848 O VAL A 105 2360 2513 3196 -138 -707 -481 O -ATOM 849 CB VAL A 105 40.196 -35.831 22.062 1.00 18.21 C -ANISOU 849 CB VAL A 105 1899 2042 2978 -160 -681 -392 C -ATOM 850 CG1 VAL A 105 39.957 -35.311 23.474 1.00 18.50 C -ANISOU 850 CG1 VAL A 105 1963 2050 3017 -171 -725 -458 C -ATOM 851 CG2 VAL A 105 41.335 -35.052 21.407 1.00 18.80 C -ANISOU 851 CG2 VAL A 105 1924 2086 3135 -179 -684 -346 C -ATOM 852 N SER A 106 38.283 -38.316 22.279 1.00 20.03 N -ANISOU 852 N SER A 106 2214 2376 3022 -112 -638 -428 N -ATOM 853 CA SER A 106 37.201 -38.978 22.995 1.00 20.51 C -ANISOU 853 CA SER A 106 2322 2464 3007 -98 -639 -473 C -ATOM 854 C SER A 106 37.412 -40.488 23.038 1.00 26.82 C -ANISOU 854 C SER A 106 3137 3315 3739 -87 -630 -470 C -ATOM 855 O SER A 106 36.862 -41.174 23.908 1.00 27.67 O -ANISOU 855 O SER A 106 3280 3445 3786 -80 -643 -513 O -ATOM 856 CB SER A 106 35.854 -38.684 22.337 1.00 15.10 C -ANISOU 856 CB SER A 106 1655 1784 2297 -81 -606 -463 C -ATOM 857 OG SER A 106 35.819 -39.254 21.046 1.00 15.77 O -ANISOU 857 OG SER A 106 1729 1898 2365 -70 -563 -408 O -ATOM 858 N ARG A 107 38.199 -40.999 22.089 1.00 20.61 N -ANISOU 858 N ARG A 107 2323 2545 2962 -85 -607 -417 N -ATOM 859 CA ARG A 107 38.417 -42.435 21.952 1.00 22.22 C -ANISOU 859 CA ARG A 107 2543 2797 3102 -73 -593 -406 C -ATOM 860 C ARG A 107 37.098 -43.122 21.613 1.00 27.32 C -ANISOU 860 C ARG A 107 3229 3478 3672 -55 -562 -410 C -ATOM 861 O ARG A 107 36.841 -44.248 22.036 1.00 31.57 O -ANISOU 861 O ARG A 107 3799 4053 4141 -46 -563 -430 O -ATOM 862 CB ARG A 107 39.023 -43.010 23.240 1.00 27.91 C -ANISOU 862 CB ARG A 107 3274 3526 3803 -81 -632 -450 C -ATOM 863 CG ARG A 107 40.292 -42.276 23.706 1.00 33.68 C -ANISOU 863 CG ARG A 107 3967 4222 4609 -103 -668 -451 C -ATOM 864 CD ARG A 107 40.730 -42.707 25.107 1.00 35.10 C -ANISOU 864 CD ARG A 107 4161 4406 4769 -112 -710 -502 C -ATOM 865 NE ARG A 107 41.056 -44.130 25.149 1.00 27.37 N -ANISOU 865 NE ARG A 107 3196 3474 3730 -99 -701 -495 N -ATOM 866 CZ ARG A 107 42.144 -44.646 24.603 1.00 29.03 C -ANISOU 866 CZ ARG A 107 3377 3699 3954 -98 -691 -452 C -ATOM 867 NH1 ARG A 107 43.000 -43.850 23.983 1.00 30.32 N -ANISOU 867 NH1 ARG A 107 3493 3835 4190 -110 -690 -412 N -ATOM 868 NH2 ARG A 107 42.375 -45.948 24.673 1.00 28.45 N -ANISOU 868 NH2 ARG A 107 3320 3666 3822 -84 -681 -448 N -ATOM 869 N THR A 108 36.265 -42.426 20.844 1.00 22.72 N -ANISOU 869 N THR A 108 2646 2885 3104 -50 -537 -390 N -ATOM 870 CA THR A 108 34.984 -42.957 20.399 1.00 19.54 C -ANISOU 870 CA THR A 108 2276 2514 2633 -34 -506 -387 C -ATOM 871 C THR A 108 34.765 -42.583 18.938 1.00 20.95 C -ANISOU 871 C THR A 108 2435 2691 2835 -28 -465 -329 C -ATOM 872 O THR A 108 35.482 -41.740 18.393 1.00 17.29 O -ANISOU 872 O THR A 108 1932 2196 2443 -37 -463 -298 O -ATOM 873 CB THR A 108 33.813 -42.387 21.226 1.00 21.06 C -ANISOU 873 CB THR A 108 2498 2696 2810 -32 -522 -436 C -ATOM 874 OG1 THR A 108 33.752 -40.969 21.050 1.00 19.03 O -ANISOU 874 OG1 THR A 108 2217 2393 2623 -39 -526 -431 O -ATOM 875 CG2 THR A 108 33.996 -42.696 22.701 1.00 26.62 C -ANISOU 875 CG2 THR A 108 3222 3400 3491 -37 -564 -495 C -ATOM 876 N PRO A 109 33.764 -43.197 18.300 1.00 21.75 N -ANISOU 876 N PRO A 109 2562 2826 2876 -15 -432 -313 N -ATOM 877 CA PRO A 109 33.491 -42.855 16.903 1.00 18.62 C -ANISOU 877 CA PRO A 109 2148 2429 2497 -10 -393 -258 C -ATOM 878 C PRO A 109 32.887 -41.470 16.793 1.00 16.15 C -ANISOU 878 C PRO A 109 1821 2080 2236 -13 -393 -261 C -ATOM 879 O PRO A 109 32.127 -41.038 17.676 1.00 20.30 O -ANISOU 879 O PRO A 109 2367 2596 2751 -13 -413 -305 O -ATOM 880 CB PRO A 109 32.468 -43.915 16.470 1.00 18.07 C -ANISOU 880 CB PRO A 109 2118 2408 2341 3 -364 -250 C -ATOM 881 CG PRO A 109 32.593 -45.009 17.486 1.00 23.41 C -ANISOU 881 CG PRO A 109 2826 3111 2957 4 -386 -290 C -ATOM 882 CD PRO A 109 32.919 -44.307 18.769 1.00 17.86 C -ANISOU 882 CD PRO A 109 2116 2376 2293 -6 -430 -341 C -ATOM 883 N ALA A 110 33.225 -40.789 15.705 1.00 14.15 N -ANISOU 883 N ALA A 110 1533 1807 2037 -15 -370 -212 N -ATOM 884 CA ALA A 110 32.703 -39.468 15.404 1.00 13.72 C -ANISOU 884 CA ALA A 110 1462 1717 2034 -17 -365 -205 C -ATOM 885 C ALA A 110 31.998 -39.555 14.059 1.00 18.00 C -ANISOU 885 C ALA A 110 2002 2279 2557 -6 -319 -155 C -ATOM 886 O ALA A 110 32.630 -39.800 13.039 1.00 14.93 O -ANISOU 886 O ALA A 110 1591 1897 2184 -6 -295 -106 O -ATOM 887 CB ALA A 110 33.820 -38.443 15.352 1.00 15.53 C -ANISOU 887 CB ALA A 110 1648 1899 2354 -31 -382 -191 C -ATOM 888 N LEU A 111 30.683 -39.369 14.063 1.00 16.18 N -ANISOU 888 N LEU A 111 1797 2061 2291 3 -307 -167 N -ATOM 889 CA LEU A 111 29.911 -39.402 12.827 1.00 17.34 C -ANISOU 889 CA LEU A 111 1943 2228 2418 12 -264 -121 C -ATOM 890 C LEU A 111 29.906 -38.036 12.157 1.00 18.10 C -ANISOU 890 C LEU A 111 2005 2284 2589 10 -253 -93 C -ATOM 891 O LEU A 111 29.638 -37.012 12.804 1.00 17.83 O -ANISOU 891 O LEU A 111 1968 2214 2594 7 -273 -122 O -ATOM 892 CB LEU A 111 28.462 -39.835 13.092 1.00 16.33 C -ANISOU 892 CB LEU A 111 1855 2134 2215 22 -255 -142 C -ATOM 893 CG LEU A 111 28.202 -41.069 13.959 1.00 17.60 C -ANISOU 893 CG LEU A 111 2057 2334 2297 24 -270 -180 C -ATOM 894 CD1 LEU A 111 26.707 -41.375 13.972 1.00 14.61 C -ANISOU 894 CD1 LEU A 111 1713 1989 1850 33 -255 -189 C -ATOM 895 CD2 LEU A 111 28.984 -42.265 13.487 1.00 19.53 C -ANISOU 895 CD2 LEU A 111 2304 2606 2509 23 -259 -155 C -ATOM 896 N VAL A 112 30.169 -38.024 10.853 1.00 13.13 N -ANISOU 896 N VAL A 112 1352 1660 1978 11 -220 -35 N -ATOM 897 CA VAL A 112 30.215 -36.786 10.081 1.00 15.18 C -ANISOU 897 CA VAL A 112 1577 1883 2309 9 -205 -1 C -ATOM 898 C VAL A 112 28.989 -36.714 9.183 1.00 15.06 C -ANISOU 898 C VAL A 112 1571 1890 2260 20 -168 28 C -ATOM 899 O VAL A 112 28.768 -37.600 8.355 1.00 16.67 O -ANISOU 899 O VAL A 112 1785 2132 2415 25 -139 61 O -ATOM 900 CB VAL A 112 31.479 -36.734 9.217 1.00 14.05 C -ANISOU 900 CB VAL A 112 1394 1727 2218 2 -195 46 C -ATOM 901 CG1 VAL A 112 31.563 -35.402 8.457 1.00 18.45 C -ANISOU 901 CG1 VAL A 112 1914 2244 2852 -1 -182 80 C -ATOM 902 CG2 VAL A 112 32.707 -36.953 10.085 1.00 12.94 C -ANISOU 902 CG2 VAL A 112 1244 1572 2103 -9 -231 21 C -ATOM 903 N PHE A 113 28.193 -35.667 9.358 1.00 12.23 N -ANISOU 903 N PHE A 113 1213 1508 1927 24 -169 16 N -ATOM 904 CA PHE A 113 26.921 -35.514 8.624 1.00 13.54 C -ANISOU 904 CA PHE A 113 1388 1695 2060 35 -137 40 C -ATOM 905 C PHE A 113 26.944 -34.299 7.712 1.00 19.03 C -ANISOU 905 C PHE A 113 2048 2356 2825 36 -117 80 C -ATOM 906 O PHE A 113 27.703 -33.339 7.932 1.00 13.98 O -ANISOU 906 O PHE A 113 1382 1669 2261 28 -135 75 O -ATOM 907 CB PHE A 113 25.746 -35.309 9.586 1.00 13.58 C -ANISOU 907 CB PHE A 113 1425 1707 2028 44 -150 -7 C -ATOM 908 CG PHE A 113 25.487 -36.461 10.493 1.00 14.71 C -ANISOU 908 CG PHE A 113 1606 1886 2096 45 -168 -47 C -ATOM 909 CD1 PHE A 113 24.661 -37.501 10.092 1.00 16.37 C -ANISOU 909 CD1 PHE A 113 1845 2150 2227 51 -145 -33 C -ATOM 910 CD2 PHE A 113 26.023 -36.485 11.769 1.00 16.63 C -ANISOU 910 CD2 PHE A 113 1860 2111 2349 39 -207 -99 C -ATOM 911 CE1 PHE A 113 24.390 -38.552 10.943 1.00 17.88 C -ANISOU 911 CE1 PHE A 113 2071 2374 2347 51 -162 -71 C -ATOM 912 CE2 PHE A 113 25.770 -37.542 12.622 1.00 12.89 C -ANISOU 912 CE2 PHE A 113 1421 1671 1806 41 -224 -137 C -ATOM 913 CZ PHE A 113 24.953 -38.577 12.209 1.00 16.56 C -ANISOU 913 CZ PHE A 113 1913 2189 2191 47 -201 -122 C -ATOM 914 N GLU A 114 26.082 -34.324 6.704 1.00 13.90 N -ANISOU 914 N GLU A 114 1400 1731 2151 44 -81 119 N -ATOM 915 CA GLU A 114 25.899 -33.160 5.865 1.00 16.51 C -ANISOU 915 CA GLU A 114 1700 2032 2540 47 -60 155 C -ATOM 916 C GLU A 114 25.475 -31.998 6.758 1.00 18.96 C -ANISOU 916 C GLU A 114 2013 2302 2890 50 -83 116 C -ATOM 917 O GLU A 114 24.819 -32.187 7.791 1.00 18.28 O -ANISOU 917 O GLU A 114 1958 2225 2763 56 -102 69 O -ATOM 918 CB GLU A 114 24.819 -33.440 4.803 1.00 24.79 C -ANISOU 918 CB GLU A 114 2756 3120 3543 56 -19 197 C -ATOM 919 CG GLU A 114 23.413 -33.146 5.268 1.00 20.07 C -ANISOU 919 CG GLU A 114 2183 2535 2907 68 -17 173 C -ATOM 920 CD GLU A 114 22.336 -33.527 4.250 1.00 25.31 C -ANISOU 920 CD GLU A 114 2855 3243 3518 75 21 214 C -ATOM 921 OE1 GLU A 114 21.939 -32.672 3.433 1.00 30.42 O -ANISOU 921 OE1 GLU A 114 3480 3877 4201 81 45 250 O -ATOM 922 OE2 GLU A 114 21.859 -34.678 4.296 1.00 18.47 O -ANISOU 922 OE2 GLU A 114 2019 2425 2574 75 27 210 O -ATOM 923 N HIS A 115 25.849 -30.790 6.370 1.00 18.34 N -ANISOU 923 N HIS A 115 1902 2177 2888 47 -81 136 N -ATOM 924 CA HIS A 115 25.497 -29.610 7.140 1.00 20.92 C -ANISOU 924 CA HIS A 115 2232 2459 3256 51 -101 102 C -ATOM 925 C HIS A 115 24.212 -29.019 6.579 1.00 16.44 C -ANISOU 925 C HIS A 115 1668 1900 2677 67 -71 123 C -ATOM 926 O HIS A 115 24.087 -28.840 5.365 1.00 20.12 O -ANISOU 926 O HIS A 115 2112 2374 3157 69 -38 175 O -ATOM 927 CB HIS A 115 26.632 -28.588 7.052 1.00 24.21 C -ANISOU 927 CB HIS A 115 2614 2819 3766 37 -117 112 C -ATOM 928 CG HIS A 115 26.359 -27.307 7.776 1.00 25.64 C -ANISOU 928 CG HIS A 115 2798 2949 3995 40 -137 80 C -ATOM 929 ND1 HIS A 115 25.636 -26.276 7.212 1.00 21.34 N -ANISOU 929 ND1 HIS A 115 2245 2383 3480 51 -115 102 N -ATOM 930 CD2 HIS A 115 26.727 -26.879 9.007 1.00 24.97 C -ANISOU 930 CD2 HIS A 115 2727 2828 3933 33 -177 28 C -ATOM 931 CE1 HIS A 115 25.561 -25.273 8.068 1.00 21.73 C -ANISOU 931 CE1 HIS A 115 2303 2385 3568 51 -140 65 C -ATOM 932 NE2 HIS A 115 26.204 -25.617 9.170 1.00 21.36 N -ANISOU 932 NE2 HIS A 115 2271 2329 3518 40 -178 19 N -ATOM 933 N VAL A 116 23.257 -28.731 7.461 1.00 16.11 N -ANISOU 933 N VAL A 116 1654 1858 2608 79 -82 82 N -ATOM 934 CA VAL A 116 22.003 -28.097 7.069 1.00 18.56 C -ANISOU 934 CA VAL A 116 1970 2175 2908 97 -56 98 C -ATOM 935 C VAL A 116 21.928 -26.671 7.612 1.00 22.46 C -ANISOU 935 C VAL A 116 2460 2611 3465 103 -71 75 C -ATOM 936 O VAL A 116 21.982 -26.449 8.819 1.00 26.60 O -ANISOU 936 O VAL A 116 3005 3112 3991 103 -104 22 O -ATOM 937 CB VAL A 116 20.777 -28.902 7.567 1.00 21.44 C -ANISOU 937 CB VAL A 116 2371 2591 3183 110 -51 75 C -ATOM 938 CG1 VAL A 116 19.478 -28.216 7.149 1.00 22.86 C -ANISOU 938 CG1 VAL A 116 2553 2780 3353 129 -24 95 C -ATOM 939 CG2 VAL A 116 20.815 -30.314 7.019 1.00 23.08 C -ANISOU 939 CG2 VAL A 116 2587 2856 3326 103 -36 97 C -ATOM 940 N ASN A 117 21.828 -25.699 6.718 1.00 22.55 N -ANISOU 940 N ASN A 117 2445 2596 3529 107 -48 115 N -ATOM 941 CA ASN A 117 21.680 -24.314 7.146 1.00 19.94 C -ANISOU 941 CA ASN A 117 2112 2208 3256 114 -59 98 C -ATOM 942 C ASN A 117 20.259 -24.063 7.631 1.00 24.70 C -ANISOU 942 C ASN A 117 2744 2828 3815 138 -50 76 C -ATOM 943 O ASN A 117 19.460 -23.442 6.932 1.00 26.34 O -ANISOU 943 O ASN A 117 2942 3036 4029 153 -21 109 O -ATOM 944 CB ASN A 117 22.031 -23.366 6.001 1.00 28.30 C -ANISOU 944 CB ASN A 117 3133 3234 4385 110 -37 150 C -ATOM 945 CG ASN A 117 21.966 -21.913 6.414 1.00 36.42 C -ANISOU 945 CG ASN A 117 4160 4200 5477 116 -49 133 C -ATOM 946 OD1 ASN A 117 22.095 -21.589 7.596 1.00 43.08 O -ANISOU 946 OD1 ASN A 117 5026 5013 6329 116 -82 80 O -ATOM 947 ND2 ASN A 117 21.762 -21.025 5.444 1.00 41.10 N -ANISOU 947 ND2 ASN A 117 4729 4772 6115 122 -21 177 N -ATOM 948 N ASN A 118 19.935 -24.553 8.825 1.00 20.82 N -ANISOU 948 N ASN A 118 2285 2349 3275 143 -75 23 N -ATOM 949 CA ASN A 118 18.545 -24.502 9.284 1.00 30.46 C -ANISOU 949 CA ASN A 118 3534 3596 4443 167 -65 5 C -ATOM 950 C ASN A 118 18.199 -23.254 10.089 1.00 31.03 C -ANISOU 950 C ASN A 118 3620 3617 4553 182 -80 -29 C -ATOM 951 O ASN A 118 19.075 -22.466 10.452 1.00 30.53 O -ANISOU 951 O ASN A 118 3549 3494 4556 171 -104 -47 O -ATOM 952 CB ASN A 118 18.182 -25.756 10.090 1.00 23.22 C -ANISOU 952 CB ASN A 118 2648 2730 3444 167 -80 -30 C -ATOM 953 CG ASN A 118 18.701 -25.700 11.503 1.00 25.83 C -ANISOU 953 CG ASN A 118 3001 3030 3782 163 -123 -94 C -ATOM 954 OD1 ASN A 118 19.862 -25.363 11.731 1.00 26.50 O -ANISOU 954 OD1 ASN A 118 3074 3072 3924 145 -147 -106 O -ATOM 955 ND2 ASN A 118 17.838 -26.003 12.468 1.00 26.57 N -ANISOU 955 ND2 ASN A 118 3128 3147 3819 178 -133 -134 N -ATOM 956 N THR A 119 16.904 -23.081 10.346 1.00 25.53 N -ANISOU 956 N THR A 119 2945 2943 3814 207 -65 -37 N -ATOM 957 CA THR A 119 16.417 -22.084 11.282 1.00 23.06 C -ANISOU 957 CA THR A 119 2654 2590 3520 226 -79 -76 C -ATOM 958 C THR A 119 15.829 -22.852 12.459 1.00 23.83 C -ANISOU 958 C THR A 119 2788 2722 3546 236 -98 -126 C -ATOM 959 O THR A 119 14.883 -23.628 12.279 1.00 30.50 O -ANISOU 959 O THR A 119 3642 3627 4321 247 -79 -114 O -ATOM 960 CB THR A 119 15.299 -21.213 10.648 1.00 37.02 C -ANISOU 960 CB THR A 119 4415 4357 5293 253 -43 -43 C -ATOM 961 OG1 THR A 119 15.808 -20.513 9.502 1.00 31.49 O -ANISOU 961 OG1 THR A 119 3680 3628 4658 244 -23 7 O -ATOM 962 CG2 THR A 119 14.760 -20.211 11.660 1.00 34.55 C -ANISOU 962 CG2 THR A 119 4129 4003 4994 276 -57 -85 C -ATOM 963 N ASP A 120 16.379 -22.658 13.655 1.00 23.65 N -ANISOU 963 N ASP A 120 2786 2662 3539 231 -137 -182 N -ATOM 964 CA ASP A 120 15.913 -23.410 14.820 1.00 26.93 C -ANISOU 964 CA ASP A 120 3236 3109 3889 238 -158 -231 C -ATOM 965 C ASP A 120 14.393 -23.348 14.945 1.00 26.22 C -ANISOU 965 C ASP A 120 3165 3056 3743 270 -134 -229 C -ATOM 966 O ASP A 120 13.772 -22.328 14.645 1.00 30.45 O -ANISOU 966 O ASP A 120 3696 3568 4304 290 -114 -212 O -ATOM 967 CB ASP A 120 16.557 -22.922 16.117 1.00 28.82 C -ANISOU 967 CB ASP A 120 3497 3295 4158 234 -201 -292 C -ATOM 968 CG ASP A 120 16.245 -23.838 17.296 1.00 33.04 C -ANISOU 968 CG ASP A 120 4064 3864 4624 237 -224 -343 C -ATOM 969 OD1 ASP A 120 16.764 -24.977 17.315 1.00 33.53 O -ANISOU 969 OD1 ASP A 120 4125 3962 4655 219 -235 -345 O -ATOM 970 OD2 ASP A 120 15.483 -23.424 18.198 1.00 34.32 O -ANISOU 970 OD2 ASP A 120 4256 4018 4766 260 -232 -379 O -ATOM 971 N PHE A 121 13.797 -24.444 15.399 1.00 24.15 N -ANISOU 971 N PHE A 121 2923 2852 3402 273 -136 -245 N -ATOM 972 CA PHE A 121 12.345 -24.525 15.436 1.00 21.75 C -ANISOU 972 CA PHE A 121 2633 2593 3038 301 -113 -237 C -ATOM 973 C PHE A 121 11.775 -23.470 16.378 1.00 23.66 C -ANISOU 973 C PHE A 121 2898 2797 3295 328 -122 -274 C -ATOM 974 O PHE A 121 10.662 -22.990 16.179 1.00 27.82 O -ANISOU 974 O PHE A 121 3428 3339 3804 355 -96 -256 O -ATOM 975 CB PHE A 121 11.876 -25.931 15.814 1.00 23.07 C -ANISOU 975 CB PHE A 121 2819 2829 3118 297 -117 -249 C -ATOM 976 CG PHE A 121 12.101 -26.289 17.254 1.00 25.13 C -ANISOU 976 CG PHE A 121 3111 3083 3355 296 -155 -314 C -ATOM 977 CD1 PHE A 121 11.094 -26.106 18.194 1.00 23.30 C -ANISOU 977 CD1 PHE A 121 2908 2864 3082 323 -160 -347 C -ATOM 978 CD2 PHE A 121 13.311 -26.830 17.670 1.00 28.69 C -ANISOU 978 CD2 PHE A 121 3563 3517 3822 270 -187 -341 C -ATOM 979 CE1 PHE A 121 11.296 -26.439 19.526 1.00 23.90 C -ANISOU 979 CE1 PHE A 121 3012 2934 3133 323 -195 -407 C -ATOM 980 CE2 PHE A 121 13.513 -27.167 19.002 1.00 26.79 C -ANISOU 980 CE2 PHE A 121 3351 3271 3558 270 -222 -400 C -ATOM 981 CZ PHE A 121 12.498 -26.967 19.927 1.00 25.78 C -ANISOU 981 CZ PHE A 121 3252 3155 3389 296 -226 -434 C -ATOM 982 N LYS A 122 12.555 -23.088 17.383 1.00 30.38 N -ANISOU 982 N LYS A 122 3766 3597 4181 321 -159 -325 N -ATOM 983 CA LYS A 122 12.132 -22.049 18.319 1.00 32.67 C -ANISOU 983 CA LYS A 122 4082 3843 4490 346 -170 -364 C -ATOM 984 C LYS A 122 11.921 -20.682 17.664 1.00 41.90 C -ANISOU 984 C LYS A 122 5236 4964 5719 362 -147 -334 C -ATOM 985 O LYS A 122 11.182 -19.851 18.194 1.00 45.71 O -ANISOU 985 O LYS A 122 5740 5424 6202 392 -143 -352 O -ATOM 986 CB LYS A 122 13.126 -21.926 19.467 1.00 37.99 C -ANISOU 986 CB LYS A 122 4775 4468 5191 331 -216 -423 C -ATOM 987 CG LYS A 122 13.076 -23.079 20.447 1.00 44.58 C -ANISOU 987 CG LYS A 122 5634 5345 5960 326 -241 -465 C -ATOM 988 CD LYS A 122 11.936 -22.923 21.438 1.00 55.39 C -ANISOU 988 CD LYS A 122 7038 6729 7279 359 -242 -500 C -ATOM 989 CE LYS A 122 12.174 -23.821 22.635 1.00 61.85 C -ANISOU 989 CE LYS A 122 7883 7568 8050 350 -276 -554 C -ATOM 990 NZ LYS A 122 13.628 -23.838 22.973 1.00 63.05 N -ANISOU 990 NZ LYS A 122 8030 7674 8252 319 -313 -580 N -ATOM 991 N GLN A 123 12.574 -20.442 16.528 1.00 40.19 N -ANISOU 991 N GLN A 123 4986 4732 5554 344 -133 -289 N -ATOM 992 CA GLN A 123 12.338 -19.217 15.756 1.00 42.13 C -ANISOU 992 CA GLN A 123 5215 4937 5855 358 -107 -253 C -ATOM 993 C GLN A 123 11.438 -19.467 14.549 1.00 34.13 C -ANISOU 993 C GLN A 123 4178 3978 4812 369 -62 -191 C -ATOM 994 O GLN A 123 10.647 -18.611 14.166 1.00 41.66 O -ANISOU 994 O GLN A 123 5129 4922 5778 395 -35 -167 O -ATOM 995 CB GLN A 123 13.657 -18.592 15.287 1.00 53.75 C -ANISOU 995 CB GLN A 123 6663 6348 7411 331 -120 -241 C -ATOM 996 CG GLN A 123 13.475 -17.520 14.203 1.00 64.11 C -ANISOU 996 CG GLN A 123 7950 7630 8778 340 -89 -191 C -ATOM 997 CD GLN A 123 14.786 -16.886 13.747 1.00 71.16 C -ANISOU 997 CD GLN A 123 8819 8462 9755 312 -103 -179 C -ATOM 998 OE1 GLN A 123 15.835 -17.076 14.370 1.00 74.87 O -ANISOU 998 OE1 GLN A 123 9294 8904 10248 288 -139 -212 O -ATOM 999 NE2 GLN A 123 14.729 -16.127 12.653 1.00 65.45 N -ANISOU 999 NE2 GLN A 123 8069 7720 9078 316 -74 -129 N -ATOM 1000 N LEU A 124 11.559 -20.650 13.953 1.00 26.63 N -ANISOU 1000 N LEU A 124 3213 3085 3821 350 -54 -165 N -ATOM 1001 CA LEU A 124 10.862 -20.961 12.710 1.00 22.62 C -ANISOU 1001 CA LEU A 124 2680 2626 3287 355 -13 -104 C -ATOM 1002 C LEU A 124 9.352 -21.164 12.855 1.00 24.56 C -ANISOU 1002 C LEU A 124 2942 2927 3464 384 10 -96 C -ATOM 1003 O LEU A 124 8.578 -20.676 12.037 1.00 25.63 O -ANISOU 1003 O LEU A 124 3062 3077 3601 401 45 -51 O -ATOM 1004 CB LEU A 124 11.475 -22.198 12.058 1.00 22.93 C -ANISOU 1004 CB LEU A 124 2704 2708 3301 325 -12 -80 C -ATOM 1005 CG LEU A 124 10.905 -22.567 10.690 1.00 25.19 C -ANISOU 1005 CG LEU A 124 2965 3044 3563 324 28 -15 C -ATOM 1006 CD1 LEU A 124 11.267 -21.499 9.679 1.00 25.67 C -ANISOU 1006 CD1 LEU A 124 2994 3060 3698 323 49 28 C -ATOM 1007 CD2 LEU A 124 11.437 -23.922 10.244 1.00 27.28 C -ANISOU 1007 CD2 LEU A 124 3222 3353 3789 296 25 0 C -ATOM 1008 N TYR A 125 8.931 -21.888 13.884 1.00 25.83 N -ANISOU 1008 N TYR A 125 3131 3120 3562 390 -8 -137 N -ATOM 1009 CA TYR A 125 7.527 -22.269 13.993 1.00 24.24 C -ANISOU 1009 CA TYR A 125 2942 2981 3288 415 13 -126 C -ATOM 1010 C TYR A 125 6.575 -21.076 14.050 1.00 28.43 C -ANISOU 1010 C TYR A 125 3477 3491 3835 452 34 -118 C -ATOM 1011 O TYR A 125 5.461 -21.146 13.539 1.00 26.99 O -ANISOU 1011 O TYR A 125 3286 3357 3611 470 65 -80 O -ATOM 1012 CB TYR A 125 7.299 -23.210 15.177 1.00 28.48 C -ANISOU 1012 CB TYR A 125 3511 3553 3759 414 -14 -176 C -ATOM 1013 CG TYR A 125 7.733 -24.638 14.914 1.00 24.19 C -ANISOU 1013 CG TYR A 125 2963 3057 3169 384 -22 -169 C -ATOM 1014 CD1 TYR A 125 8.639 -24.937 13.905 1.00 29.65 C -ANISOU 1014 CD1 TYR A 125 3629 3743 3894 356 -16 -135 C -ATOM 1015 CD2 TYR A 125 7.214 -25.685 15.664 1.00 22.39 C -ANISOU 1015 CD2 TYR A 125 2759 2883 2865 384 -35 -196 C -ATOM 1016 CE1 TYR A 125 9.033 -26.246 13.663 1.00 26.87 C -ANISOU 1016 CE1 TYR A 125 3276 3434 3498 330 -22 -128 C -ATOM 1017 CE2 TYR A 125 7.593 -26.992 15.431 1.00 22.20 C -ANISOU 1017 CE2 TYR A 125 2736 2903 2798 357 -42 -189 C -ATOM 1018 CZ TYR A 125 8.506 -27.268 14.431 1.00 21.99 C -ANISOU 1018 CZ TYR A 125 2684 2867 2804 331 -35 -156 C -ATOM 1019 OH TYR A 125 8.884 -28.571 14.196 1.00 26.49 O -ANISOU 1019 OH TYR A 125 3256 3478 3329 306 -41 -150 O -ATOM 1020 N GLN A 126 7.001 -19.974 14.651 1.00 26.10 N -ANISOU 1020 N GLN A 126 3194 3126 3599 463 18 -150 N -ATOM 1021 CA GLN A 126 6.097 -18.830 14.741 1.00 33.26 C -ANISOU 1021 CA GLN A 126 4108 4011 4520 502 39 -143 C -ATOM 1022 C GLN A 126 6.057 -17.980 13.469 1.00 29.17 C -ANISOU 1022 C GLN A 126 3557 3471 4054 505 73 -85 C -ATOM 1023 O GLN A 126 5.333 -16.989 13.401 1.00 29.39 O -ANISOU 1023 O GLN A 126 3588 3481 4098 537 94 -72 O -ATOM 1024 CB GLN A 126 6.431 -17.966 15.950 1.00 44.05 C -ANISOU 1024 CB GLN A 126 5505 5311 5921 516 11 -202 C -ATOM 1025 CG GLN A 126 7.863 -17.509 15.994 1.00 47.35 C -ANISOU 1025 CG GLN A 126 5919 5658 6415 488 -17 -221 C -ATOM 1026 CD GLN A 126 8.249 -17.032 17.371 1.00 53.71 C -ANISOU 1026 CD GLN A 126 6761 6410 7236 494 -54 -288 C -ATOM 1027 OE1 GLN A 126 7.478 -17.178 18.322 1.00 58.27 O -ANISOU 1027 OE1 GLN A 126 7368 7008 7764 519 -60 -322 O -ATOM 1028 NE2 GLN A 126 9.439 -16.455 17.492 1.00 49.81 N -ANISOU 1028 NE2 GLN A 126 6266 5849 6813 472 -80 -307 N -ATOM 1029 N THR A 127 6.831 -18.369 12.462 1.00 30.64 N -ANISOU 1029 N THR A 127 3714 3662 4267 474 78 -50 N -ATOM 1030 CA THR A 127 6.793 -17.687 11.174 1.00 34.89 C -ANISOU 1030 CA THR A 127 4219 4188 4850 475 111 9 C -ATOM 1031 C THR A 127 6.149 -18.541 10.069 1.00 33.67 C -ANISOU 1031 C THR A 127 4041 4108 4645 469 143 67 C -ATOM 1032 O THR A 127 5.854 -18.034 8.989 1.00 36.13 O -ANISOU 1032 O THR A 127 4326 4421 4981 474 175 119 O -ATOM 1033 CB THR A 127 8.199 -17.225 10.733 1.00 41.61 C -ANISOU 1033 CB THR A 127 5051 4975 5782 447 96 13 C -ATOM 1034 OG1 THR A 127 8.992 -18.360 10.359 1.00 44.49 O -ANISOU 1034 OG1 THR A 127 5402 5370 6131 412 85 20 O -ATOM 1035 CG2 THR A 127 8.889 -16.482 11.867 1.00 40.35 C -ANISOU 1035 CG2 THR A 127 4917 4744 5669 448 60 -46 C -ATOM 1036 N LEU A 128 5.910 -19.824 10.341 1.00 27.96 N -ANISOU 1036 N LEU A 128 3328 3446 3851 456 134 57 N -ATOM 1037 CA LEU A 128 5.367 -20.718 9.316 1.00 25.47 C -ANISOU 1037 CA LEU A 128 2993 3201 3484 445 161 109 C -ATOM 1038 C LEU A 128 3.936 -20.357 8.941 1.00 23.54 C -ANISOU 1038 C LEU A 128 2744 2998 3204 476 197 147 C -ATOM 1039 O LEU A 128 3.091 -20.105 9.799 1.00 18.72 O -ANISOU 1039 O LEU A 128 2154 2396 2561 504 195 121 O -ATOM 1040 CB LEU A 128 5.424 -22.184 9.746 1.00 25.58 C -ANISOU 1040 CB LEU A 128 3023 3270 3427 424 143 89 C -ATOM 1041 CG LEU A 128 6.786 -22.867 9.916 1.00 27.72 C -ANISOU 1041 CG LEU A 128 3295 3520 3718 390 113 63 C -ATOM 1042 CD1 LEU A 128 6.568 -24.314 10.316 1.00 31.40 C -ANISOU 1042 CD1 LEU A 128 3780 4048 4103 376 100 48 C -ATOM 1043 CD2 LEU A 128 7.636 -22.779 8.646 1.00 22.75 C -ANISOU 1043 CD2 LEU A 128 2632 2872 3139 367 128 109 C -ATOM 1044 N THR A 129 3.672 -20.329 7.642 1.00 20.65 N -ANISOU 1044 N THR A 129 2348 2656 2843 470 229 209 N -ATOM 1045 CA THR A 129 2.322 -20.082 7.171 1.00 19.47 C -ANISOU 1045 CA THR A 129 2190 2553 2656 496 264 251 C -ATOM 1046 C THR A 129 1.583 -21.408 7.075 1.00 14.21 C -ANISOU 1046 C THR A 129 1528 1971 1898 484 269 266 C -ATOM 1047 O THR A 129 2.178 -22.475 7.260 1.00 21.10 O -ANISOU 1047 O THR A 129 2411 2863 2742 456 247 247 O -ATOM 1048 CB THR A 129 2.327 -19.442 5.779 1.00 19.10 C -ANISOU 1048 CB THR A 129 2107 2496 2654 494 297 314 C -ATOM 1049 OG1 THR A 129 2.928 -20.354 4.863 1.00 18.37 O -ANISOU 1049 OG1 THR A 129 1997 2430 2551 459 301 344 O -ATOM 1050 CG2 THR A 129 3.098 -18.121 5.779 1.00 18.42 C -ANISOU 1050 CG2 THR A 129 2014 2324 2661 503 293 303 C -ATOM 1051 N ASP A 130 0.280 -21.333 6.805 1.00 15.32 N -ANISOU 1051 N ASP A 130 1665 2164 1993 506 296 301 N -ATOM 1052 CA ASP A 130 -0.526 -22.526 6.555 1.00 15.53 C -ANISOU 1052 CA ASP A 130 1693 2275 1933 494 305 326 C -ATOM 1053 C ASP A 130 0.128 -23.367 5.463 1.00 19.62 C -ANISOU 1053 C ASP A 130 2195 2814 2448 455 310 361 C -ATOM 1054 O ASP A 130 0.277 -24.588 5.598 1.00 17.26 O -ANISOU 1054 O ASP A 130 1909 2555 2094 431 295 351 O -ATOM 1055 CB ASP A 130 -1.955 -22.139 6.156 1.00 18.05 C -ANISOU 1055 CB ASP A 130 2000 2641 2216 522 339 371 C -ATOM 1056 CG ASP A 130 -2.829 -23.349 5.827 1.00 28.92 C -ANISOU 1056 CG ASP A 130 3379 4108 3503 507 348 402 C -ATOM 1057 OD1 ASP A 130 -2.609 -24.435 6.409 1.00 22.80 O -ANISOU 1057 OD1 ASP A 130 2624 3359 2678 486 323 371 O -ATOM 1058 OD2 ASP A 130 -3.757 -23.205 4.997 1.00 27.70 O -ANISOU 1058 OD2 ASP A 130 3204 3997 3325 515 380 458 O -ATOM 1059 N TYR A 131 0.535 -22.713 4.382 1.00 14.64 N -ANISOU 1059 N TYR A 131 1535 2153 1875 451 331 402 N -ATOM 1060 CA TYR A 131 1.156 -23.441 3.282 1.00 13.86 C -ANISOU 1060 CA TYR A 131 1419 2071 1775 417 339 439 C -ATOM 1061 C TYR A 131 2.455 -24.118 3.740 1.00 15.86 C -ANISOU 1061 C TYR A 131 1687 2297 2044 390 306 396 C -ATOM 1062 O TYR A 131 2.677 -25.311 3.472 1.00 14.57 O -ANISOU 1062 O TYR A 131 1531 2174 1833 363 300 403 O -ATOM 1063 CB TYR A 131 1.384 -22.536 2.071 1.00 15.37 C -ANISOU 1063 CB TYR A 131 1576 2233 2031 419 368 490 C -ATOM 1064 CG TYR A 131 1.843 -23.309 0.861 1.00 21.42 C -ANISOU 1064 CG TYR A 131 2325 3026 2787 387 380 534 C -ATOM 1065 CD1 TYR A 131 0.934 -23.957 0.044 1.00 19.87 C -ANISOU 1065 CD1 TYR A 131 2122 2900 2529 379 405 584 C -ATOM 1066 CD2 TYR A 131 3.200 -23.422 0.557 1.00 22.65 C -ANISOU 1066 CD2 TYR A 131 2474 3139 2995 363 367 526 C -ATOM 1067 CE1 TYR A 131 1.356 -24.680 -1.065 1.00 24.62 C -ANISOU 1067 CE1 TYR A 131 2710 3524 3119 350 417 624 C -ATOM 1068 CE2 TYR A 131 3.631 -24.146 -0.538 1.00 26.18 C -ANISOU 1068 CE2 TYR A 131 2906 3610 3430 336 380 566 C -ATOM 1069 CZ TYR A 131 2.704 -24.773 -1.345 1.00 28.95 C -ANISOU 1069 CZ TYR A 131 3253 4029 3719 329 405 615 C -ATOM 1070 OH TYR A 131 3.120 -25.493 -2.437 1.00 28.68 O -ANISOU 1070 OH TYR A 131 3208 4017 3672 303 418 654 O -ATOM 1071 N ASP A 132 3.310 -23.369 4.433 1.00 15.64 N -ANISOU 1071 N ASP A 132 1664 2199 2080 396 284 353 N -ATOM 1072 CA ASP A 132 4.568 -23.953 4.912 1.00 16.36 C -ANISOU 1072 CA ASP A 132 1766 2261 2188 371 251 313 C -ATOM 1073 C ASP A 132 4.327 -25.233 5.736 1.00 16.52 C -ANISOU 1073 C ASP A 132 1817 2331 2130 361 229 278 C -ATOM 1074 O ASP A 132 5.054 -26.225 5.588 1.00 17.77 O -ANISOU 1074 O ASP A 132 1980 2503 2270 333 216 274 O -ATOM 1075 CB ASP A 132 5.359 -22.964 5.774 1.00 16.16 C -ANISOU 1075 CB ASP A 132 1747 2158 2234 382 226 265 C -ATOM 1076 CG ASP A 132 5.853 -21.751 5.005 1.00 24.34 C -ANISOU 1076 CG ASP A 132 2756 3137 3356 387 242 294 C -ATOM 1077 OD1 ASP A 132 6.131 -21.847 3.786 1.00 19.87 O -ANISOU 1077 OD1 ASP A 132 2163 2580 2808 371 264 344 O -ATOM 1078 OD2 ASP A 132 5.980 -20.686 5.651 1.00 32.84 O -ANISOU 1078 OD2 ASP A 132 3839 4157 4482 406 232 265 O -ATOM 1079 N ILE A 133 3.324 -25.208 6.613 1.00 15.85 N -ANISOU 1079 N ILE A 133 1752 2272 1998 383 225 255 N -ATOM 1080 CA ILE A 133 3.093 -26.341 7.508 1.00 15.83 C -ANISOU 1080 CA ILE A 133 1778 2312 1923 375 202 218 C -ATOM 1081 C ILE A 133 2.749 -27.580 6.693 1.00 18.20 C -ANISOU 1081 C ILE A 133 2077 2682 2156 351 216 258 C -ATOM 1082 O ILE A 133 3.313 -28.648 6.906 1.00 16.34 O -ANISOU 1082 O ILE A 133 1858 2463 1889 327 197 239 O -ATOM 1083 CB ILE A 133 1.996 -26.064 8.554 1.00 18.98 C -ANISOU 1083 CB ILE A 133 2199 2731 2283 406 198 190 C -ATOM 1084 CG1 ILE A 133 2.408 -24.933 9.494 1.00 19.17 C -ANISOU 1084 CG1 ILE A 133 2232 2684 2368 428 180 143 C -ATOM 1085 CG2 ILE A 133 1.692 -27.329 9.374 1.00 19.15 C -ANISOU 1085 CG2 ILE A 133 2249 2805 2223 395 176 159 C -ATOM 1086 CD1 ILE A 133 1.238 -24.411 10.344 1.00 19.40 C -ANISOU 1086 CD1 ILE A 133 2278 2728 2367 466 184 126 C -ATOM 1087 N ARG A 134 1.842 -27.434 5.733 1.00 18.06 N -ANISOU 1087 N ARG A 134 2042 2703 2118 356 249 315 N -ATOM 1088 CA ARG A 134 1.459 -28.566 4.900 1.00 19.42 C -ANISOU 1088 CA ARG A 134 2213 2940 2225 332 263 356 C -ATOM 1089 C ARG A 134 2.666 -29.056 4.105 1.00 14.78 C -ANISOU 1089 C ARG A 134 1616 2332 1666 302 261 370 C -ATOM 1090 O ARG A 134 2.908 -30.260 3.988 1.00 13.62 O -ANISOU 1090 O ARG A 134 1486 2221 1470 277 252 369 O -ATOM 1091 CB ARG A 134 0.338 -28.158 3.955 1.00 18.51 C -ANISOU 1091 CB ARG A 134 2077 2864 2092 343 300 417 C -ATOM 1092 CG ARG A 134 -0.812 -27.440 4.653 1.00 11.47 C -ANISOU 1092 CG ARG A 134 1189 1985 1185 379 307 409 C -ATOM 1093 CD ARG A 134 -2.009 -27.410 3.747 1.00 17.63 C -ANISOU 1093 CD ARG A 134 1951 2823 1925 384 341 471 C -ATOM 1094 NE ARG A 134 -3.040 -26.491 4.228 1.00 14.71 N -ANISOU 1094 NE ARG A 134 1578 2457 1555 422 353 473 N -ATOM 1095 CZ ARG A 134 -4.331 -26.635 3.950 1.00 19.25 C -ANISOU 1095 CZ ARG A 134 2146 3096 2072 432 375 512 C -ATOM 1096 NH1 ARG A 134 -4.736 -27.673 3.227 1.00 18.04 N -ANISOU 1096 NH1 ARG A 134 1992 3006 1856 404 383 551 N -ATOM 1097 NH2 ARG A 134 -5.207 -25.754 4.404 1.00 16.76 N -ANISOU 1097 NH2 ARG A 134 1827 2781 1761 470 387 513 N -ATOM 1098 N PHE A 135 3.409 -28.112 3.540 1.00 17.70 N -ANISOU 1098 N PHE A 135 1962 2647 2118 305 270 384 N -ATOM 1099 CA PHE A 135 4.584 -28.444 2.737 1.00 14.43 C -ANISOU 1099 CA PHE A 135 1534 2210 1739 280 270 401 C -ATOM 1100 C PHE A 135 5.599 -29.274 3.531 1.00 13.48 C -ANISOU 1100 C PHE A 135 1436 2075 1612 262 236 352 C -ATOM 1101 O PHE A 135 6.045 -30.343 3.091 1.00 17.50 O -ANISOU 1101 O PHE A 135 1952 2610 2086 238 234 363 O -ATOM 1102 CB PHE A 135 5.235 -27.171 2.205 1.00 13.99 C -ANISOU 1102 CB PHE A 135 1449 2090 1778 289 281 417 C -ATOM 1103 CG PHE A 135 6.443 -27.427 1.347 1.00 23.47 C -ANISOU 1103 CG PHE A 135 2632 3267 3019 265 283 439 C -ATOM 1104 CD1 PHE A 135 6.326 -27.524 -0.034 1.00 21.84 C -ANISOU 1104 CD1 PHE A 135 2404 3083 2812 255 314 500 C -ATOM 1105 CD2 PHE A 135 7.700 -27.584 1.925 1.00 22.43 C -ANISOU 1105 CD2 PHE A 135 2507 3092 2924 253 254 398 C -ATOM 1106 CE1 PHE A 135 7.454 -27.765 -0.823 1.00 20.28 C -ANISOU 1106 CE1 PHE A 135 2191 2864 2652 235 317 520 C -ATOM 1107 CE2 PHE A 135 8.813 -27.823 1.146 1.00 23.94 C -ANISOU 1107 CE2 PHE A 135 2681 3264 3152 233 257 420 C -ATOM 1108 CZ PHE A 135 8.690 -27.914 -0.229 1.00 22.75 C -ANISOU 1108 CZ PHE A 135 2508 3134 3000 225 289 481 C -ATOM 1109 N TYR A 136 5.956 -28.785 4.710 1.00 13.25 N -ANISOU 1109 N TYR A 136 1419 2004 1612 275 209 297 N -ATOM 1110 CA TYR A 136 6.996 -29.432 5.496 1.00 14.94 C -ANISOU 1110 CA TYR A 136 1651 2197 1828 259 175 249 C -ATOM 1111 C TYR A 136 6.495 -30.735 6.113 1.00 15.14 C -ANISOU 1111 C TYR A 136 1708 2281 1764 250 161 227 C -ATOM 1112 O TYR A 136 7.247 -31.697 6.250 1.00 17.40 O -ANISOU 1112 O TYR A 136 2008 2575 2030 230 144 211 O -ATOM 1113 CB TYR A 136 7.576 -28.465 6.538 1.00 17.09 C -ANISOU 1113 CB TYR A 136 1926 2404 2163 274 149 198 C -ATOM 1114 CG TYR A 136 8.453 -27.364 5.957 1.00 16.63 C -ANISOU 1114 CG TYR A 136 1838 2281 2198 274 155 214 C -ATOM 1115 CD1 TYR A 136 9.543 -27.667 5.139 1.00 19.48 C -ANISOU 1115 CD1 TYR A 136 2180 2626 2593 251 158 238 C -ATOM 1116 CD2 TYR A 136 8.193 -26.026 6.226 1.00 18.56 C -ANISOU 1116 CD2 TYR A 136 2075 2481 2497 297 159 207 C -ATOM 1117 CE1 TYR A 136 10.350 -26.666 4.622 1.00 21.51 C -ANISOU 1117 CE1 TYR A 136 2411 2827 2936 250 162 255 C -ATOM 1118 CE2 TYR A 136 8.990 -25.014 5.703 1.00 16.97 C -ANISOU 1118 CE2 TYR A 136 1848 2220 2381 296 163 222 C -ATOM 1119 CZ TYR A 136 10.065 -25.337 4.903 1.00 14.72 C -ANISOU 1119 CZ TYR A 136 1543 1922 2128 272 165 247 C -ATOM 1120 OH TYR A 136 10.874 -24.355 4.378 1.00 22.04 O -ANISOU 1120 OH TYR A 136 2443 2791 3139 269 169 264 O -ATOM 1121 N MET A 137 5.215 -30.781 6.477 1.00 16.57 N -ANISOU 1121 N MET A 137 1901 2505 1890 266 168 228 N -ATOM 1122 CA AMET A 137 4.618 -32.029 6.940 1.00 15.26 C -ANISOU 1122 CA AMET A 137 1765 2401 1635 256 158 215 C -ATOM 1123 CA BMET A 137 4.612 -32.026 6.941 0.00 15.30 C -ANISOU 1123 CA BMET A 137 1769 2405 1639 256 158 215 C -ATOM 1124 C MET A 137 4.739 -33.107 5.868 1.00 15.98 C -ANISOU 1124 C MET A 137 1855 2533 1682 228 174 258 C -ATOM 1125 O MET A 137 5.108 -34.241 6.155 1.00 16.30 O -ANISOU 1125 O MET A 137 1919 2597 1678 209 157 239 O -ATOM 1126 CB AMET A 137 3.148 -31.814 7.328 1.00 13.48 C -ANISOU 1126 CB AMET A 137 1547 2218 1359 277 169 220 C -ATOM 1127 CB BMET A 137 3.143 -31.811 7.320 0.00 14.47 C -ANISOU 1127 CB BMET A 137 1671 2343 1484 277 169 221 C -ATOM 1128 CG AMET A 137 2.971 -31.251 8.723 1.00 14.23 C -ANISOU 1128 CG AMET A 137 1657 2286 1464 302 146 164 C -ATOM 1129 CG BMET A 137 2.937 -31.528 8.800 0.00 14.00 C -ANISOU 1129 CG BMET A 137 1633 2268 1420 298 143 161 C -ATOM 1130 SD AMET A 137 3.362 -32.472 10.003 1.00 20.34 S -ANISOU 1130 SD AMET A 137 2468 3077 2182 287 106 102 S -ATOM 1131 SD BMET A 137 3.329 -32.976 9.799 0.00 21.63 S -ANISOU 1131 SD BMET A 137 2635 3261 2321 277 107 111 S -ATOM 1132 CE AMET A 137 1.836 -33.425 10.069 1.00 46.14 C -ANISOU 1132 CE AMET A 137 5753 6435 5341 287 117 123 C -ATOM 1133 CE BMET A 137 3.564 -32.239 11.415 0.00 20.62 C -ANISOU 1133 CE BMET A 137 2524 3084 2225 302 75 39 C -ATOM 1134 N TYR A 138 4.445 -32.743 4.627 1.00 12.97 N -ANISOU 1134 N TYR A 138 1449 2162 1316 226 206 316 N -ATOM 1135 CA TYR A 138 4.554 -33.690 3.530 1.00 11.88 C -ANISOU 1135 CA TYR A 138 1311 2061 1140 201 222 360 C -ATOM 1136 C TYR A 138 6.006 -34.147 3.401 1.00 11.80 C -ANISOU 1136 C TYR A 138 1303 2016 1164 183 208 345 C -ATOM 1137 O TYR A 138 6.280 -35.316 3.161 1.00 15.91 O -ANISOU 1137 O TYR A 138 1842 2567 1635 162 204 350 O -ATOM 1138 CB TYR A 138 4.108 -33.040 2.234 1.00 15.92 C -ANISOU 1138 CB TYR A 138 1793 2579 1675 204 258 422 C -ATOM 1139 CG TYR A 138 3.774 -34.023 1.140 1.00 17.92 C -ANISOU 1139 CG TYR A 138 2052 2887 1870 181 278 472 C -ATOM 1140 CD1 TYR A 138 2.588 -34.748 1.169 1.00 16.94 C -ANISOU 1140 CD1 TYR A 138 1946 2830 1660 175 284 488 C -ATOM 1141 CD2 TYR A 138 4.631 -34.205 0.068 1.00 22.10 C -ANISOU 1141 CD2 TYR A 138 2567 3400 2429 164 292 505 C -ATOM 1142 CE1 TYR A 138 2.277 -35.645 0.158 1.00 21.08 C -ANISOU 1142 CE1 TYR A 138 2477 3403 2129 151 302 534 C -ATOM 1143 CE2 TYR A 138 4.334 -35.086 -0.939 1.00 27.38 C -ANISOU 1143 CE2 TYR A 138 3244 4116 3043 143 311 550 C -ATOM 1144 CZ TYR A 138 3.160 -35.807 -0.894 1.00 19.30 C -ANISOU 1144 CZ TYR A 138 2241 3158 1935 136 315 564 C -ATOM 1145 OH TYR A 138 2.881 -36.684 -1.920 1.00 22.96 O -ANISOU 1145 OH TYR A 138 2714 3667 2344 112 333 609 O -ATOM 1146 N GLU A 139 6.937 -33.223 3.573 1.00 14.75 N -ANISOU 1146 N GLU A 139 1658 2326 1621 191 199 327 N -ATOM 1147 CA GLU A 139 8.349 -33.573 3.478 1.00 16.15 C -ANISOU 1147 CA GLU A 139 1832 2469 1836 175 185 314 C -ATOM 1148 C GLU A 139 8.779 -34.534 4.591 1.00 13.10 C -ANISOU 1148 C GLU A 139 1478 2090 1409 167 152 261 C -ATOM 1149 O GLU A 139 9.571 -35.448 4.356 1.00 13.07 O -ANISOU 1149 O GLU A 139 1484 2093 1390 148 145 262 O -ATOM 1150 CB GLU A 139 9.216 -32.311 3.454 1.00 14.66 C -ANISOU 1150 CB GLU A 139 1615 2210 1747 185 182 308 C -ATOM 1151 CG GLU A 139 8.999 -31.461 2.196 1.00 13.28 C -ANISOU 1151 CG GLU A 139 1407 2024 1615 190 216 366 C -ATOM 1152 CD GLU A 139 9.424 -32.176 0.931 1.00 20.95 C -ANISOU 1152 CD GLU A 139 2369 3018 2573 170 237 415 C -ATOM 1153 OE1 GLU A 139 10.524 -32.754 0.908 1.00 22.45 O -ANISOU 1153 OE1 GLU A 139 2562 3192 2774 155 224 404 O -ATOM 1154 OE2 GLU A 139 8.672 -32.160 -0.053 1.00 20.40 O -ANISOU 1154 OE2 GLU A 139 2289 2981 2480 170 267 465 O -ATOM 1155 N ILE A 140 8.270 -34.331 5.806 1.00 12.25 N -ANISOU 1155 N ILE A 140 1393 1793 1470 -117 97 1 N -ATOM 1156 CA ILE A 140 8.551 -35.271 6.901 1.00 14.01 C -ANISOU 1156 CA ILE A 140 1643 1958 1720 -108 82 -41 C -ATOM 1157 C ILE A 140 7.971 -36.656 6.577 1.00 17.14 C -ANISOU 1157 C ILE A 140 2045 2381 2089 -128 89 -81 C -ATOM 1158 O ILE A 140 8.593 -37.693 6.817 1.00 12.90 O -ANISOU 1158 O ILE A 140 1515 1814 1571 -130 92 -126 O -ATOM 1159 CB ILE A 140 7.958 -34.780 8.242 1.00 13.59 C -ANISOU 1159 CB ILE A 140 1618 1858 1687 -85 62 -20 C -ATOM 1160 CG1 ILE A 140 8.579 -33.438 8.639 1.00 18.92 C -ANISOU 1160 CG1 ILE A 140 2293 2500 2394 -68 55 12 C -ATOM 1161 CG2 ILE A 140 8.198 -35.806 9.345 1.00 14.03 C -ANISOU 1161 CG2 ILE A 140 1702 1863 1767 -76 47 -59 C -ATOM 1162 CD1 ILE A 140 7.880 -32.761 9.816 1.00 13.79 C -ANISOU 1162 CD1 ILE A 140 1674 1811 1757 -47 41 36 C -ATOM 1163 N LEU A 141 6.765 -36.666 6.025 1.00 13.18 N -ANISOU 1163 N LEU A 141 1536 1930 1542 -143 91 -63 N -ATOM 1164 CA LEU A 141 6.122 -37.916 5.672 1.00 11.84 C -ANISOU 1164 CA LEU A 141 1370 1787 1343 -166 95 -101 C -ATOM 1165 C LEU A 141 6.939 -38.706 4.646 1.00 12.40 C -ANISOU 1165 C LEU A 141 1429 1882 1401 -189 118 -146 C -ATOM 1166 O LEU A 141 6.977 -39.930 4.705 1.00 14.53 O -ANISOU 1166 O LEU A 141 1708 2138 1674 -201 124 -195 O -ATOM 1167 CB LEU A 141 4.708 -37.647 5.158 1.00 12.23 C -ANISOU 1167 CB LEU A 141 1407 1893 1345 -182 92 -65 C -ATOM 1168 CG LEU A 141 3.670 -37.372 6.248 1.00 16.86 C -ANISOU 1168 CG LEU A 141 2010 2451 1944 -162 75 -33 C -ATOM 1169 CD1 LEU A 141 2.324 -36.944 5.621 1.00 13.42 C -ANISOU 1169 CD1 LEU A 141 1555 2078 1467 -178 73 14 C -ATOM 1170 CD2 LEU A 141 3.480 -38.596 7.132 1.00 16.36 C -ANISOU 1170 CD2 LEU A 141 1971 2345 1900 -159 67 -75 C -ATOM 1171 N LYS A 142 7.602 -38.016 3.718 1.00 17.86 N -ANISOU 1171 N LYS A 142 2098 2606 2080 -194 133 -131 N -ATOM 1172 CA LYS A 142 8.466 -38.709 2.757 1.00 13.81 C -ANISOU 1172 CA LYS A 142 1575 2114 1556 -213 160 -174 C -ATOM 1173 C LYS A 142 9.566 -39.452 3.502 1.00 20.53 C -ANISOU 1173 C LYS A 142 2440 2897 2466 -197 165 -213 C -ATOM 1174 O LYS A 142 9.814 -40.631 3.254 1.00 16.81 O -ANISOU 1174 O LYS A 142 1974 2418 1995 -210 182 -265 O -ATOM 1175 CB LYS A 142 9.093 -37.735 1.760 1.00 18.22 C -ANISOU 1175 CB LYS A 142 2108 2714 2099 -215 177 -142 C -ATOM 1176 CG LYS A 142 8.122 -37.187 0.729 1.00 24.39 C -ANISOU 1176 CG LYS A 142 2872 3578 2817 -237 178 -106 C -ATOM 1177 CD LYS A 142 8.860 -36.236 -0.209 1.00 26.64 C -ANISOU 1177 CD LYS A 142 3129 3899 3092 -236 198 -72 C -ATOM 1178 CE LYS A 142 7.892 -35.483 -1.100 1.00 28.97 C -ANISOU 1178 CE LYS A 142 3403 4275 3331 -253 195 -20 C -ATOM 1179 NZ LYS A 142 8.615 -34.486 -1.930 1.00 31.54 N -ANISOU 1179 NZ LYS A 142 3700 4633 3653 -247 215 21 N -ATOM 1180 N ALA A 143 10.214 -38.750 4.426 1.00 13.04 N -ANISOU 1180 N ALA A 143 1493 1895 1566 -169 149 -188 N -ATOM 1181 CA ALA A 143 11.256 -39.342 5.252 1.00 13.66 C -ANISOU 1181 CA ALA A 143 1580 1908 1703 -152 147 -215 C -ATOM 1182 C ALA A 143 10.717 -40.512 6.079 1.00 14.94 C -ANISOU 1182 C ALA A 143 1763 2037 1875 -152 137 -248 C -ATOM 1183 O ALA A 143 11.360 -41.556 6.172 1.00 10.45 O -ANISOU 1183 O ALA A 143 1196 1439 1335 -153 152 -287 O -ATOM 1184 CB ALA A 143 11.864 -38.281 6.165 1.00 11.33 C -ANISOU 1184 CB ALA A 143 1286 1568 1451 -127 124 -177 C -ATOM 1185 N LEU A 144 9.536 -40.350 6.681 1.00 12.32 N -ANISOU 1185 N LEU A 144 1448 1709 1525 -149 116 -228 N -ATOM 1186 CA LEU A 144 8.990 -41.416 7.518 1.00 11.38 C -ANISOU 1186 CA LEU A 144 1349 1558 1419 -146 107 -254 C -ATOM 1187 C LEU A 144 8.525 -42.629 6.704 1.00 16.13 C -ANISOU 1187 C LEU A 144 1946 2189 1993 -175 129 -298 C -ATOM 1188 O LEU A 144 8.819 -43.773 7.056 1.00 14.52 O -ANISOU 1188 O LEU A 144 1749 1949 1818 -175 138 -337 O -ATOM 1189 CB LEU A 144 7.879 -40.906 8.440 1.00 10.75 C -ANISOU 1189 CB LEU A 144 1286 1469 1329 -132 82 -218 C -ATOM 1190 CG LEU A 144 8.342 -39.991 9.582 1.00 11.83 C -ANISOU 1190 CG LEU A 144 1437 1559 1500 -103 60 -188 C -ATOM 1191 CD1 LEU A 144 7.128 -39.512 10.385 1.00 14.17 C -ANISOU 1191 CD1 LEU A 144 1754 1851 1781 -90 43 -155 C -ATOM 1192 CD2 LEU A 144 9.362 -40.705 10.486 1.00 13.43 C -ANISOU 1192 CD2 LEU A 144 1648 1702 1752 -88 52 -212 C -ATOM 1193 N ASP A 145 7.819 -42.406 5.606 1.00 13.85 N -ANISOU 1193 N ASP A 145 1647 1966 1650 -201 138 -294 N -ATOM 1194 CA ASP A 145 7.465 -43.553 4.785 1.00 18.17 C -ANISOU 1194 CA ASP A 145 2193 2541 2168 -233 158 -343 C -ATOM 1195 C ASP A 145 8.721 -44.283 4.316 1.00 19.38 C -ANISOU 1195 C ASP A 145 2343 2673 2349 -237 190 -390 C -ATOM 1196 O ASP A 145 8.752 -45.516 4.275 1.00 15.27 O -ANISOU 1196 O ASP A 145 1829 2132 1842 -249 208 -439 O -ATOM 1197 CB ASP A 145 6.656 -43.160 3.568 1.00 15.59 C -ANISOU 1197 CB ASP A 145 1854 2295 1774 -264 161 -331 C -ATOM 1198 CG ASP A 145 6.184 -44.376 2.800 1.00 27.73 C -ANISOU 1198 CG ASP A 145 3396 3861 3280 -303 177 -386 C -ATOM 1199 OD1 ASP A 145 5.660 -45.311 3.449 1.00 22.16 O -ANISOU 1199 OD1 ASP A 145 2703 3122 2595 -305 171 -410 O -ATOM 1200 OD2 ASP A 145 6.373 -44.413 1.570 1.00 27.69 O -ANISOU 1200 OD2 ASP A 145 3382 3909 3230 -330 198 -406 O -ATOM 1201 N TYR A 146 9.754 -43.528 3.944 1.00 16.75 N -ANISOU 1201 N TYR A 146 1996 2343 2027 -226 201 -373 N -ATOM 1202 CA TYR A 146 10.993 -44.173 3.526 1.00 15.93 C -ANISOU 1202 CA TYR A 146 1885 2215 1954 -225 236 -411 C -ATOM 1203 C TYR A 146 11.571 -45.081 4.617 1.00 15.23 C -ANISOU 1203 C TYR A 146 1804 2051 1933 -205 235 -433 C -ATOM 1204 O TYR A 146 11.769 -46.276 4.388 1.00 15.96 O -ANISOU 1204 O TYR A 146 1899 2125 2040 -217 263 -482 O -ATOM 1205 CB TYR A 146 12.038 -43.165 3.034 1.00 13.74 C -ANISOU 1205 CB TYR A 146 1587 1948 1685 -213 247 -382 C -ATOM 1206 CG TYR A 146 13.252 -43.866 2.464 1.00 13.07 C -ANISOU 1206 CG TYR A 146 1492 1844 1628 -215 289 -421 C -ATOM 1207 CD1 TYR A 146 13.171 -44.535 1.243 1.00 19.16 C -ANISOU 1207 CD1 TYR A 146 2265 2659 2356 -244 327 -465 C -ATOM 1208 CD2 TYR A 146 14.465 -43.884 3.144 1.00 14.64 C -ANISOU 1208 CD2 TYR A 146 1681 1983 1897 -188 291 -413 C -ATOM 1209 CE1 TYR A 146 14.263 -45.194 0.711 1.00 21.98 C -ANISOU 1209 CE1 TYR A 146 2615 2996 2740 -243 373 -501 C -ATOM 1210 CE2 TYR A 146 15.573 -44.544 2.610 1.00 18.44 C -ANISOU 1210 CE2 TYR A 146 2151 2445 2411 -187 334 -443 C -ATOM 1211 CZ TYR A 146 15.457 -45.195 1.390 1.00 22.28 C -ANISOU 1211 CZ TYR A 146 2641 2972 2854 -214 378 -488 C -ATOM 1212 OH TYR A 146 16.522 -45.857 0.828 1.00 22.86 O -ANISOU 1212 OH TYR A 146 2704 3025 2958 -212 428 -521 O -ATOM 1213 N CYS A 147 11.832 -44.546 5.808 1.00 16.57 N -ANISOU 1213 N CYS A 147 1977 2177 2144 -176 204 -397 N -ATOM 1214 CA CYS A 147 12.454 -45.388 6.826 1.00 15.40 C -ANISOU 1214 CA CYS A 147 1832 1961 2058 -157 202 -411 C -ATOM 1215 C CYS A 147 11.556 -46.558 7.244 1.00 15.69 C -ANISOU 1215 C CYS A 147 1884 1982 2095 -166 202 -441 C -ATOM 1216 O CYS A 147 12.034 -47.682 7.390 1.00 14.85 O -ANISOU 1216 O CYS A 147 1775 1838 2029 -165 225 -475 O -ATOM 1217 CB CYS A 147 13.008 -44.592 8.018 1.00 16.91 C -ANISOU 1217 CB CYS A 147 2025 2110 2290 -128 167 -368 C -ATOM 1218 SG CYS A 147 11.806 -43.821 9.129 1.00 14.85 S -ANISOU 1218 SG CYS A 147 1788 1848 2006 -115 122 -328 S -ATOM 1219 N HIS A 148 10.253 -46.313 7.380 1.00 11.14 N -ANISOU 1219 N HIS A 148 1321 1436 1477 -175 181 -427 N -ATOM 1220 CA HIS A 148 9.321 -47.409 7.652 1.00 12.23 C -ANISOU 1220 CA HIS A 148 1470 1565 1613 -187 182 -453 C -ATOM 1221 C HIS A 148 9.364 -48.475 6.543 1.00 12.35 C -ANISOU 1221 C HIS A 148 1480 1597 1615 -219 221 -512 C -ATOM 1222 O HIS A 148 9.404 -49.674 6.823 1.00 18.03 O -ANISOU 1222 O HIS A 148 2202 2278 2370 -222 238 -547 O -ATOM 1223 CB HIS A 148 7.896 -46.880 7.835 1.00 12.31 C -ANISOU 1223 CB HIS A 148 1490 1610 1579 -193 155 -423 C -ATOM 1224 CG HIS A 148 7.739 -45.949 8.997 1.00 12.14 C -ANISOU 1224 CG HIS A 148 1479 1565 1571 -162 122 -372 C -ATOM 1225 ND1 HIS A 148 6.604 -45.192 9.194 1.00 12.53 N -ANISOU 1225 ND1 HIS A 148 1535 1642 1584 -161 102 -334 N -ATOM 1226 CD2 HIS A 148 8.572 -45.655 10.026 1.00 13.72 C -ANISOU 1226 CD2 HIS A 148 1683 1715 1814 -133 108 -353 C -ATOM 1227 CE1 HIS A 148 6.743 -44.475 10.296 1.00 17.68 C -ANISOU 1227 CE1 HIS A 148 2200 2262 2258 -131 79 -298 C -ATOM 1228 NE2 HIS A 148 7.933 -44.726 10.810 1.00 16.70 N -ANISOU 1228 NE2 HIS A 148 2075 2092 2178 -115 80 -310 N -ATOM 1229 N SER A 149 9.385 -48.047 5.285 1.00 17.95 N -ANISOU 1229 N SER A 149 2182 2363 2274 -243 238 -522 N -ATOM 1230 CA SER A 149 9.414 -48.999 4.167 1.00 14.90 C -ANISOU 1230 CA SER A 149 1797 1999 1866 -277 277 -582 C -ATOM 1231 C SER A 149 10.722 -49.777 4.188 1.00 14.78 C -ANISOU 1231 C SER A 149 1775 1930 1910 -264 315 -616 C -ATOM 1232 O SER A 149 10.831 -50.864 3.608 1.00 14.99 O -ANISOU 1232 O SER A 149 1806 1947 1942 -285 353 -672 O -ATOM 1233 CB SER A 149 9.262 -48.279 2.821 1.00 19.65 C -ANISOU 1233 CB SER A 149 2392 2677 2396 -303 287 -580 C -ATOM 1234 OG SER A 149 10.431 -47.536 2.487 1.00 18.10 O -ANISOU 1234 OG SER A 149 2182 2482 2213 -286 302 -562 O -ATOM 1235 N MET A 150 11.709 -49.215 4.875 1.00 15.91 N -ANISOU 1235 N MET A 150 1908 2037 2101 -230 306 -581 N -ATOM 1236 CA AMET A 150 13.019 -49.846 4.968 1.00 16.51 C -ANISOU 1236 CA AMET A 150 1972 2060 2241 -214 340 -600 C -ATOM 1237 CA BMET A 150 13.028 -49.828 4.985 0.00 17.16 C -ANISOU 1237 CA BMET A 150 2054 2142 2324 -214 340 -599 C -ATOM 1238 C MET A 150 13.207 -50.571 6.303 1.00 20.08 C -ANISOU 1238 C MET A 150 2424 2442 2763 -189 327 -592 C -ATOM 1239 O MET A 150 14.330 -50.894 6.690 1.00 20.12 O -ANISOU 1239 O MET A 150 2415 2400 2831 -168 343 -588 O -ATOM 1240 CB AMET A 150 14.111 -48.788 4.739 1.00 15.94 C -ANISOU 1240 CB AMET A 150 1883 1995 2180 -197 341 -565 C -ATOM 1241 CB BMET A 150 14.120 -48.767 4.829 0.00 16.51 C -ANISOU 1241 CB BMET A 150 1955 2064 2255 -195 339 -562 C -ATOM 1242 CG AMET A 150 14.020 -48.152 3.335 1.00 17.08 C -ANISOU 1242 CG AMET A 150 2023 2208 2257 -220 362 -572 C -ATOM 1243 CG BMET A 150 14.348 -48.356 3.385 0.00 16.72 C -ANISOU 1243 CG BMET A 150 1974 2147 2230 -216 371 -578 C -ATOM 1244 SD AMET A 150 14.813 -49.218 2.078 1.00 22.26 S -ANISOU 1244 SD AMET A 150 2676 2865 2916 -240 435 -639 S -ATOM 1245 SD BMET A 150 14.886 -49.761 2.393 0.00 22.35 S -ANISOU 1245 SD BMET A 150 2690 2848 2954 -236 441 -652 S -ATOM 1246 CE AMET A 150 16.541 -48.929 2.507 1.00 20.02 C -ANISOU 1246 CE AMET A 150 2365 2525 2715 -202 451 -608 C -ATOM 1247 CE BMET A 150 14.897 -49.055 0.749 0.00 22.77 C -ANISOU 1247 CE BMET A 150 2742 2985 2926 -263 469 -662 C -ATOM 1248 N GLY A 151 12.099 -50.832 6.992 1.00 16.45 N -ANISOU 1248 N GLY A 151 1978 1980 2292 -192 299 -586 N -ATOM 1249 CA GLY A 151 12.109 -51.622 8.215 1.00 16.97 C -ANISOU 1249 CA GLY A 151 2045 1985 2416 -171 288 -579 C -ATOM 1250 C GLY A 151 12.600 -50.939 9.481 1.00 17.90 C -ANISOU 1250 C GLY A 151 2160 2071 2568 -136 249 -524 C -ATOM 1251 O GLY A 151 13.004 -51.595 10.436 1.00 15.22 O -ANISOU 1251 O GLY A 151 1817 1680 2287 -116 245 -516 O -ATOM 1252 N ILE A 152 12.548 -49.617 9.502 1.00 15.74 N -ANISOU 1252 N ILE A 152 1891 1830 2261 -130 220 -487 N -ATOM 1253 CA ILE A 152 13.138 -48.868 10.603 1.00 9.20 C -ANISOU 1253 CA ILE A 152 1062 972 1461 -102 183 -440 C -ATOM 1254 C ILE A 152 12.165 -47.861 11.186 1.00 15.13 C -ANISOU 1254 C ILE A 152 1833 1746 2170 -96 143 -404 C -ATOM 1255 O ILE A 152 11.490 -47.139 10.455 1.00 15.32 O -ANISOU 1255 O ILE A 152 1861 1819 2140 -111 142 -399 O -ATOM 1256 CB ILE A 152 14.417 -48.150 10.118 1.00 15.76 C -ANISOU 1256 CB ILE A 152 1873 1804 2310 -96 192 -428 C -ATOM 1257 CG1 ILE A 152 15.510 -49.191 9.804 1.00 15.32 C -ANISOU 1257 CG1 ILE A 152 1796 1713 2314 -94 233 -455 C -ATOM 1258 CG2 ILE A 152 14.858 -47.078 11.129 1.00 12.81 C -ANISOU 1258 CG2 ILE A 152 1502 1413 1951 -74 147 -378 C -ATOM 1259 CD1 ILE A 152 16.546 -48.713 8.811 1.00 21.51 C -ANISOU 1259 CD1 ILE A 152 2559 2511 3102 -98 261 -457 C -ATOM 1260 N MET A 153 12.094 -47.818 12.514 1.00 10.93 N -ANISOU 1260 N MET A 153 1313 1179 1661 -73 111 -376 N -ATOM 1261 CA MET A 153 11.347 -46.769 13.187 1.00 13.52 C -ANISOU 1261 CA MET A 153 1662 1520 1954 -63 76 -340 C -ATOM 1262 C MET A 153 12.308 -45.759 13.812 1.00 14.47 C -ANISOU 1262 C MET A 153 1782 1620 2094 -46 48 -308 C -ATOM 1263 O MET A 153 13.354 -46.128 14.353 1.00 13.67 O -ANISOU 1263 O MET A 153 1671 1482 2042 -34 43 -304 O -ATOM 1264 CB MET A 153 10.367 -47.338 14.220 1.00 22.03 C -ANISOU 1264 CB MET A 153 2760 2579 3032 -52 61 -331 C -ATOM 1265 CG MET A 153 10.887 -48.463 15.062 1.00 22.27 C -ANISOU 1265 CG MET A 153 2785 2560 3116 -38 63 -338 C -ATOM 1266 SD MET A 153 9.599 -49.211 16.102 1.00 19.07 S -ANISOU 1266 SD MET A 153 2399 2139 2707 -27 52 -328 S -ATOM 1267 CE MET A 153 10.502 -50.655 16.656 1.00 16.75 C -ANISOU 1267 CE MET A 153 2087 1791 2486 -16 67 -341 C -ATOM 1268 N HIS A 154 11.954 -44.482 13.720 1.00 11.92 N -ANISOU 1268 N HIS A 154 1470 1323 1736 -45 32 -282 N -ATOM 1269 CA HIS A 154 12.844 -43.426 14.182 1.00 12.51 C -ANISOU 1269 CA HIS A 154 1545 1381 1828 -34 7 -255 C -ATOM 1270 C HIS A 154 12.829 -43.338 15.711 1.00 17.35 C -ANISOU 1270 C HIS A 154 2182 1955 2455 -15 -30 -235 C -ATOM 1271 O HIS A 154 13.884 -43.313 16.342 1.00 14.50 O -ANISOU 1271 O HIS A 154 1815 1562 2132 -6 -49 -225 O -ATOM 1272 CB HIS A 154 12.468 -42.089 13.536 1.00 13.29 C -ANISOU 1272 CB HIS A 154 1645 1515 1888 -41 5 -235 C -ATOM 1273 CG HIS A 154 13.413 -40.975 13.865 1.00 13.72 C -ANISOU 1273 CG HIS A 154 1697 1553 1964 -33 -17 -210 C -ATOM 1274 ND1 HIS A 154 13.393 -40.326 15.079 1.00 12.40 N -ANISOU 1274 ND1 HIS A 154 1555 1355 1801 -19 -52 -189 N -ATOM 1275 CD2 HIS A 154 14.407 -40.398 13.146 1.00 14.06 C -ANISOU 1275 CD2 HIS A 154 1715 1601 2025 -39 -9 -204 C -ATOM 1276 CE1 HIS A 154 14.334 -39.397 15.096 1.00 10.88 C -ANISOU 1276 CE1 HIS A 154 1353 1150 1630 -19 -67 -172 C -ATOM 1277 NE2 HIS A 154 14.963 -39.417 13.936 1.00 9.44 N -ANISOU 1277 NE2 HIS A 154 1138 989 1459 -30 -41 -179 N -ATOM 1278 N ARG A 155 11.624 -43.304 16.285 1.00 14.40 N -ANISOU 1278 N ARG A 155 1835 1587 2050 -8 -38 -226 N -ATOM 1279 CA ARG A 155 11.394 -43.304 17.744 1.00 11.74 C -ANISOU 1279 CA ARG A 155 1526 1217 1715 11 -67 -208 C -ATOM 1280 C ARG A 155 11.813 -42.032 18.495 1.00 11.12 C -ANISOU 1280 C ARG A 155 1469 1124 1632 20 -100 -183 C -ATOM 1281 O ARG A 155 11.818 -42.007 19.724 1.00 14.32 O -ANISOU 1281 O ARG A 155 1899 1502 2038 34 -126 -171 O -ATOM 1282 CB ARG A 155 11.978 -44.553 18.438 1.00 9.72 C -ANISOU 1282 CB ARG A 155 1263 928 1503 20 -71 -216 C -ATOM 1283 CG ARG A 155 11.563 -45.892 17.800 1.00 12.71 C -ANISOU 1283 CG ARG A 155 1623 1312 1893 11 -37 -244 C -ATOM 1284 CD ARG A 155 11.858 -47.089 18.722 1.00 10.60 C -ANISOU 1284 CD ARG A 155 1353 1008 1669 24 -40 -243 C -ATOM 1285 NE ARG A 155 13.268 -47.150 19.119 1.00 12.13 N -ANISOU 1285 NE ARG A 155 1528 1172 1908 30 -56 -233 N -ATOM 1286 CZ ARG A 155 13.792 -48.056 19.948 1.00 16.69 C -ANISOU 1286 CZ ARG A 155 2096 1716 2529 42 -63 -223 C -ATOM 1287 NH1 ARG A 155 13.029 -48.995 20.501 1.00 12.23 N -ANISOU 1287 NH1 ARG A 155 1539 1140 1968 51 -56 -223 N -ATOM 1288 NH2 ARG A 155 15.096 -48.012 20.239 1.00 13.85 N -ANISOU 1288 NH2 ARG A 155 1716 1335 2212 46 -79 -208 N -ATOM 1289 N ASP A 156 12.134 -40.970 17.771 1.00 13.28 N -ANISOU 1289 N ASP A 156 1734 1415 1898 12 -97 -177 N -ATOM 1290 CA ASP A 156 12.465 -39.714 18.440 1.00 8.89 C -ANISOU 1290 CA ASP A 156 1198 841 1339 17 -125 -156 C -ATOM 1291 C ASP A 156 12.108 -38.554 17.536 1.00 11.31 C -ANISOU 1291 C ASP A 156 1499 1176 1623 10 -111 -144 C -ATOM 1292 O ASP A 156 12.850 -37.582 17.427 1.00 13.86 O -ANISOU 1292 O ASP A 156 1815 1490 1960 6 -122 -133 O -ATOM 1293 CB ASP A 156 13.953 -39.679 18.823 1.00 10.43 C -ANISOU 1293 CB ASP A 156 1378 1007 1578 15 -150 -154 C -ATOM 1294 CG ASP A 156 14.268 -38.609 19.858 1.00 16.50 C -ANISOU 1294 CG ASP A 156 2176 1749 2343 19 -188 -138 C -ATOM 1295 OD1 ASP A 156 13.337 -38.125 20.552 1.00 13.46 O -ANISOU 1295 OD1 ASP A 156 1830 1361 1923 29 -194 -131 O -ATOM 1296 OD2 ASP A 156 15.461 -38.269 19.990 1.00 17.62 O -ANISOU 1296 OD2 ASP A 156 2303 1873 2518 12 -211 -132 O -ATOM 1297 N VAL A 157 10.956 -38.668 16.877 1.00 12.85 N -ANISOU 1297 N VAL A 157 1693 1406 1785 7 -85 -143 N -ATOM 1298 CA VAL A 157 10.463 -37.579 16.050 1.00 11.54 C -ANISOU 1298 CA VAL A 157 1520 1271 1596 1 -71 -124 C -ATOM 1299 C VAL A 157 10.029 -36.429 16.970 1.00 16.56 C -ANISOU 1299 C VAL A 157 2189 1883 2220 15 -87 -101 C -ATOM 1300 O VAL A 157 9.233 -36.625 17.894 1.00 14.25 O -ANISOU 1300 O VAL A 157 1928 1575 1912 29 -92 -97 O -ATOM 1301 CB VAL A 157 9.280 -38.042 15.153 1.00 13.30 C -ANISOU 1301 CB VAL A 157 1731 1539 1784 -8 -43 -125 C -ATOM 1302 CG1 VAL A 157 8.639 -36.848 14.452 1.00 12.02 C -ANISOU 1302 CG1 VAL A 157 1562 1409 1597 -11 -31 -95 C -ATOM 1303 CG2 VAL A 157 9.743 -39.081 14.133 1.00 14.95 C -ANISOU 1303 CG2 VAL A 157 1908 1771 2000 -26 -24 -154 C -ATOM 1304 N LYS A 158 10.572 -35.242 16.722 1.00 10.05 N -ANISOU 1304 N LYS A 158 1359 1053 1406 12 -91 -85 N -ATOM 1305 CA LYS A 158 10.285 -34.036 17.497 1.00 11.22 C -ANISOU 1305 CA LYS A 158 1539 1175 1550 23 -102 -66 C -ATOM 1306 C LYS A 158 10.892 -32.866 16.729 1.00 15.25 C -ANISOU 1306 C LYS A 158 2026 1690 2077 14 -96 -49 C -ATOM 1307 O LYS A 158 11.758 -33.074 15.870 1.00 10.97 O -ANISOU 1307 O LYS A 158 1449 1164 1555 2 -92 -55 O -ATOM 1308 CB LYS A 158 10.896 -34.128 18.910 1.00 10.10 C -ANISOU 1308 CB LYS A 158 1432 986 1422 30 -136 -79 C -ATOM 1309 CG LYS A 158 12.418 -34.210 18.932 1.00 14.66 C -ANISOU 1309 CG LYS A 158 1989 1543 2038 19 -161 -89 C -ATOM 1310 CD LYS A 158 12.933 -34.388 20.350 1.00 13.63 C -ANISOU 1310 CD LYS A 158 1890 1372 1915 23 -199 -98 C -ATOM 1311 CE LYS A 158 14.451 -34.454 20.379 1.00 13.01 C -ANISOU 1311 CE LYS A 158 1788 1276 1880 10 -227 -103 C -ATOM 1312 NZ LYS A 158 14.956 -34.412 21.806 1.00 20.64 N -ANISOU 1312 NZ LYS A 158 2787 2205 2848 10 -270 -107 N -ATOM 1313 N PRO A 159 10.437 -31.633 17.014 1.00 14.30 N -ANISOU 1313 N PRO A 159 1926 1556 1953 22 -92 -27 N -ATOM 1314 CA PRO A 159 10.897 -30.457 16.271 1.00 14.87 C -ANISOU 1314 CA PRO A 159 1975 1632 2045 15 -83 -5 C -ATOM 1315 C PRO A 159 12.424 -30.373 16.146 1.00 15.21 C -ANISOU 1315 C PRO A 159 1996 1656 2127 2 -104 -16 C -ATOM 1316 O PRO A 159 12.932 -30.092 15.064 1.00 13.78 O -ANISOU 1316 O PRO A 159 1775 1500 1961 -7 -89 -4 O -ATOM 1317 CB PRO A 159 10.351 -29.296 17.099 1.00 17.02 C -ANISOU 1317 CB PRO A 159 2284 1869 2315 27 -83 10 C -ATOM 1318 CG PRO A 159 9.043 -29.840 17.639 1.00 14.16 C -ANISOU 1318 CG PRO A 159 1949 1513 1917 42 -71 11 C -ATOM 1319 CD PRO A 159 9.361 -31.287 17.972 1.00 15.38 C -ANISOU 1319 CD PRO A 159 2105 1672 2066 39 -89 -19 C -ATOM 1320 N HIS A 160 13.145 -30.617 17.232 1.00 15.98 N -ANISOU 1320 N HIS A 160 2117 1713 2242 2 -138 -36 N -ATOM 1321 CA HIS A 160 14.604 -30.509 17.168 1.00 15.65 C -ANISOU 1321 CA HIS A 160 2052 1652 2243 -11 -161 -41 C -ATOM 1322 C HIS A 160 15.214 -31.430 16.119 1.00 16.29 C -ANISOU 1322 C HIS A 160 2087 1765 2338 -19 -145 -46 C -ATOM 1323 O HIS A 160 16.220 -31.087 15.495 1.00 19.06 O -ANISOU 1323 O HIS A 160 2404 2116 2723 -28 -145 -37 O -ATOM 1324 CB HIS A 160 15.234 -30.779 18.525 1.00 12.87 C -ANISOU 1324 CB HIS A 160 1730 1256 1903 -13 -204 -59 C -ATOM 1325 CG HIS A 160 16.734 -30.748 18.499 1.00 21.38 C -ANISOU 1325 CG HIS A 160 2780 2315 3028 -27 -231 -59 C -ATOM 1326 ND1 HIS A 160 17.465 -29.655 18.913 1.00 27.93 N -ANISOU 1326 ND1 HIS A 160 3616 3111 3886 -38 -257 -52 N -ATOM 1327 CD2 HIS A 160 17.636 -31.672 18.094 1.00 23.52 C -ANISOU 1327 CD2 HIS A 160 3014 2595 3327 -33 -234 -64 C -ATOM 1328 CE1 HIS A 160 18.754 -29.911 18.774 1.00 28.54 C -ANISOU 1328 CE1 HIS A 160 3660 3179 4007 -51 -278 -50 C -ATOM 1329 NE2 HIS A 160 18.886 -31.129 18.282 1.00 25.70 N -ANISOU 1329 NE2 HIS A 160 3272 2843 3648 -46 -263 -56 N -ATOM 1330 N ASN A 161 14.605 -32.593 15.903 1.00 15.14 N -ANISOU 1330 N ASN A 161 1941 1646 2168 -15 -130 -61 N -ATOM 1331 CA ASN A 161 15.190 -33.579 14.979 1.00 13.20 C -ANISOU 1331 CA ASN A 161 1656 1425 1934 -22 -112 -73 C -ATOM 1332 C ASN A 161 14.753 -33.427 13.523 1.00 14.47 C -ANISOU 1332 C ASN A 161 1787 1637 2073 -29 -73 -63 C -ATOM 1333 O ASN A 161 15.113 -34.228 12.663 1.00 14.47 O -ANISOU 1333 O ASN A 161 1760 1663 2075 -36 -52 -77 O -ATOM 1334 CB ASN A 161 14.914 -34.997 15.473 1.00 9.02 C -ANISOU 1334 CB ASN A 161 1139 893 1397 -18 -114 -98 C -ATOM 1335 CG ASN A 161 15.740 -35.340 16.688 1.00 11.33 C -ANISOU 1335 CG ASN A 161 1446 1141 1720 -15 -151 -105 C -ATOM 1336 OD1 ASN A 161 16.776 -34.708 16.932 1.00 14.17 O -ANISOU 1336 OD1 ASN A 161 1796 1476 2113 -20 -175 -95 O -ATOM 1337 ND2 ASN A 161 15.303 -36.329 17.455 1.00 12.48 N -ANISOU 1337 ND2 ASN A 161 1611 1277 1854 -7 -159 -118 N -ATOM 1338 N VAL A 162 13.958 -32.406 13.244 1.00 12.18 N -ANISOU 1338 N VAL A 162 1503 1363 1761 -27 -62 -39 N -ATOM 1339 CA VAL A 162 13.563 -32.140 11.866 1.00 13.50 C -ANISOU 1339 CA VAL A 162 1640 1584 1906 -34 -29 -21 C -ATOM 1340 C VAL A 162 14.177 -30.822 11.454 1.00 20.08 C -ANISOU 1340 C VAL A 162 2453 2412 2765 -36 -26 10 C -ATOM 1341 O VAL A 162 13.610 -29.757 11.727 1.00 25.06 O -ANISOU 1341 O VAL A 162 3097 3032 3393 -29 -27 35 O -ATOM 1342 CB VAL A 162 12.022 -32.045 11.726 1.00 17.56 C -ANISOU 1342 CB VAL A 162 2168 2130 2373 -30 -14 -7 C -ATOM 1343 CG1 VAL A 162 11.635 -31.684 10.289 1.00 15.46 C -ANISOU 1343 CG1 VAL A 162 1868 1925 2082 -41 16 17 C -ATOM 1344 CG2 VAL A 162 11.378 -33.355 12.126 1.00 15.58 C -ANISOU 1344 CG2 VAL A 162 1935 1884 2100 -30 -16 -36 C -ATOM 1345 N MET A 163 15.332 -30.891 10.796 1.00 13.91 N -ANISOU 1345 N MET A 163 1637 1633 2013 -43 -20 9 N -ATOM 1346 CA MET A 163 16.071 -29.698 10.415 1.00 11.33 C -ANISOU 1346 CA MET A 163 1287 1298 1721 -45 -18 39 C -ATOM 1347 C MET A 163 15.541 -29.122 9.116 1.00 16.36 C -ANISOU 1347 C MET A 163 1894 1989 2331 -48 17 71 C -ATOM 1348 O MET A 163 15.379 -29.836 8.129 1.00 18.29 O -ANISOU 1348 O MET A 163 2120 2284 2546 -55 42 63 O -ATOM 1349 CB MET A 163 17.565 -29.991 10.292 1.00 15.54 C -ANISOU 1349 CB MET A 163 1793 1809 2302 -50 -26 31 C -ATOM 1350 CG MET A 163 18.112 -30.646 11.532 1.00 19.96 C -ANISOU 1350 CG MET A 163 2376 2320 2887 -49 -62 5 C -ATOM 1351 SD MET A 163 19.863 -30.348 11.670 1.00 25.32 S -ANISOU 1351 SD MET A 163 3024 2960 3638 -56 -83 15 S -ATOM 1352 CE MET A 163 19.861 -28.569 11.719 1.00 19.94 C -ANISOU 1352 CE MET A 163 2342 2259 2976 -58 -92 51 C -ATOM 1353 N ILE A 164 15.275 -27.821 9.125 1.00 17.72 N -ANISOU 1353 N ILE A 164 2065 2153 2515 -43 19 107 N -ATOM 1354 CA ILE A 164 14.683 -27.161 7.971 1.00 19.38 C -ANISOU 1354 CA ILE A 164 2246 2416 2701 -45 50 147 C -ATOM 1355 C ILE A 164 15.505 -25.963 7.518 1.00 23.77 C -ANISOU 1355 C ILE A 164 2770 2959 3301 -44 58 184 C -ATOM 1356 O ILE A 164 15.735 -25.021 8.284 1.00 23.42 O -ANISOU 1356 O ILE A 164 2739 2862 3296 -40 41 196 O -ATOM 1357 CB ILE A 164 13.259 -26.675 8.287 1.00 18.16 C -ANISOU 1357 CB ILE A 164 2113 2269 2516 -36 55 168 C -ATOM 1358 CG1 ILE A 164 12.343 -27.858 8.580 1.00 17.33 C -ANISOU 1358 CG1 ILE A 164 2034 2185 2367 -38 51 138 C -ATOM 1359 CG2 ILE A 164 12.705 -25.841 7.146 1.00 23.44 C -ANISOU 1359 CG2 ILE A 164 2747 2990 3168 -37 85 220 C -ATOM 1360 CD1 ILE A 164 10.974 -27.438 9.130 1.00 23.01 C -ANISOU 1360 CD1 ILE A 164 2778 2901 3064 -27 53 158 C -ATOM 1361 N ASP A 165 15.961 -26.022 6.273 1.00 17.35 N -ANISOU 1361 N ASP A 165 1917 2194 2483 -51 84 202 N -ATOM 1362 CA ASP A 165 16.530 -24.869 5.607 1.00 22.07 C -ANISOU 1362 CA ASP A 165 2477 2794 3114 -49 100 248 C -ATOM 1363 C ASP A 165 15.374 -24.153 4.926 1.00 25.66 C -ANISOU 1363 C ASP A 165 2920 3297 3535 -46 125 293 C -ATOM 1364 O ASP A 165 14.928 -24.542 3.851 1.00 25.26 O -ANISOU 1364 O ASP A 165 2847 3315 3435 -52 149 305 O -ATOM 1365 CB ASP A 165 17.592 -25.289 4.585 1.00 25.30 C -ANISOU 1365 CB ASP A 165 2847 3233 3532 -56 121 248 C -ATOM 1366 CG ASP A 165 18.216 -24.103 3.872 1.00 29.53 C -ANISOU 1366 CG ASP A 165 3340 3772 4106 -53 139 300 C -ATOM 1367 OD1 ASP A 165 17.567 -23.037 3.798 1.00 31.11 O -ANISOU 1367 OD1 ASP A 165 3535 3975 4309 -48 146 341 O -ATOM 1368 OD2 ASP A 165 19.356 -24.237 3.389 1.00 31.96 O -ANISOU 1368 OD2 ASP A 165 3619 4079 4445 -56 149 302 O -ATOM 1369 N HIS A 166 14.895 -23.104 5.574 1.00 23.93 N -ANISOU 1369 N HIS A 166 2714 3040 3340 -37 118 319 N -ATOM 1370 CA HIS A 166 13.725 -22.377 5.107 1.00 21.26 C -ANISOU 1370 CA HIS A 166 2364 2736 2977 -31 141 367 C -ATOM 1371 C HIS A 166 14.007 -21.559 3.843 1.00 26.37 C -ANISOU 1371 C HIS A 166 2958 3428 3633 -31 171 425 C -ATOM 1372 O HIS A 166 13.080 -21.183 3.127 1.00 29.81 O -ANISOU 1372 O HIS A 166 3374 3917 4037 -30 193 470 O -ATOM 1373 CB HIS A 166 13.202 -21.477 6.233 1.00 18.53 C -ANISOU 1373 CB HIS A 166 2051 2327 2663 -18 130 377 C -ATOM 1374 CG HIS A 166 11.777 -21.053 6.060 1.00 22.64 C -ANISOU 1374 CG HIS A 166 2571 2877 3153 -9 151 416 C -ATOM 1375 ND1 HIS A 166 10.802 -21.896 5.571 1.00 23.89 N -ANISOU 1375 ND1 HIS A 166 2729 3099 3251 -14 157 416 N -ATOM 1376 CD2 HIS A 166 11.157 -19.880 6.334 1.00 25.06 C -ANISOU 1376 CD2 HIS A 166 2878 3155 3487 4 166 460 C -ATOM 1377 CE1 HIS A 166 9.645 -21.260 5.548 1.00 24.81 C -ANISOU 1377 CE1 HIS A 166 2841 3227 3357 -4 174 461 C -ATOM 1378 NE2 HIS A 166 9.832 -20.034 6.001 1.00 26.08 N -ANISOU 1378 NE2 HIS A 166 3004 3333 3573 8 183 489 N -ATOM 1379 N GLU A 167 15.278 -21.282 3.567 1.00 25.68 N -ANISOU 1379 N GLU A 167 2846 3321 3590 -34 172 428 N -ATOM 1380 CA GLU A 167 15.637 -20.567 2.344 1.00 27.70 C -ANISOU 1380 CA GLU A 167 3049 3620 3854 -34 203 484 C -ATOM 1381 C GLU A 167 15.410 -21.417 1.098 1.00 31.17 C -ANISOU 1381 C GLU A 167 3466 4150 4226 -44 225 485 C -ATOM 1382 O GLU A 167 14.751 -20.984 0.152 1.00 31.17 O -ANISOU 1382 O GLU A 167 3437 4212 4193 -44 250 535 O -ATOM 1383 CB GLU A 167 17.088 -20.072 2.396 1.00 34.72 C -ANISOU 1383 CB GLU A 167 3915 4462 4813 -34 199 488 C -ATOM 1384 CG GLU A 167 17.542 -19.360 1.126 1.00 45.22 C -ANISOU 1384 CG GLU A 167 5189 5837 6156 -32 233 548 C -ATOM 1385 CD GLU A 167 18.980 -18.868 1.207 1.00 55.68 C -ANISOU 1385 CD GLU A 167 6489 7112 7556 -32 229 555 C -ATOM 1386 OE1 GLU A 167 19.626 -19.064 2.259 1.00 55.80 O -ANISOU 1386 OE1 GLU A 167 6530 7058 7613 -36 196 514 O -ATOM 1387 OE2 GLU A 167 19.465 -18.282 0.216 1.00 61.72 O -ANISOU 1387 OE2 GLU A 167 7206 7907 8339 -29 258 605 O -ATOM 1388 N HIS A 168 15.945 -22.633 1.099 1.00 32.98 N -ANISOU 1388 N HIS A 168 3709 4385 4435 -52 218 430 N -ATOM 1389 CA HIS A 168 15.806 -23.523 -0.051 1.00 31.81 C -ANISOU 1389 CA HIS A 168 3547 4318 4223 -64 241 419 C -ATOM 1390 C HIS A 168 14.678 -24.531 0.122 1.00 29.42 C -ANISOU 1390 C HIS A 168 3276 4047 3856 -74 231 383 C -ATOM 1391 O HIS A 168 14.554 -25.464 -0.668 1.00 28.61 O -ANISOU 1391 O HIS A 168 3171 4002 3698 -88 245 359 O -ATOM 1392 CB HIS A 168 17.111 -24.266 -0.307 1.00 31.94 C -ANISOU 1392 CB HIS A 168 3554 4323 4257 -68 248 383 C -ATOM 1393 CG HIS A 168 18.295 -23.362 -0.463 1.00 35.89 C -ANISOU 1393 CG HIS A 168 4020 4790 4826 -60 257 418 C -ATOM 1394 ND1 HIS A 168 18.507 -22.604 -1.594 1.00 36.99 N -ANISOU 1394 ND1 HIS A 168 4115 4977 4964 -58 289 475 N -ATOM 1395 CD2 HIS A 168 19.326 -23.092 0.372 1.00 38.98 C -ANISOU 1395 CD2 HIS A 168 4413 5106 5291 -55 236 408 C -ATOM 1396 CE1 HIS A 168 19.622 -21.908 -1.451 1.00 42.46 C -ANISOU 1396 CE1 HIS A 168 4783 5622 5729 -50 289 498 C -ATOM 1397 NE2 HIS A 168 20.139 -22.186 -0.267 1.00 42.60 N -ANISOU 1397 NE2 HIS A 168 4828 5565 5794 -50 256 457 N -ATOM 1398 N ARG A 169 13.870 -24.345 1.162 1.00 22.57 N -ANISOU 1398 N ARG A 169 2440 3140 2996 -67 208 379 N -ATOM 1399 CA ARG A 169 12.726 -25.212 1.413 1.00 24.39 C -ANISOU 1399 CA ARG A 169 2698 3395 3173 -74 198 351 C -ATOM 1400 C ARG A 169 13.147 -26.674 1.487 1.00 25.91 C -ANISOU 1400 C ARG A 169 2912 3589 3344 -86 192 283 C -ATOM 1401 O ARG A 169 12.495 -27.546 0.911 1.00 30.85 O -ANISOU 1401 O ARG A 169 3542 4270 3911 -101 199 263 O -ATOM 1402 CB ARG A 169 11.678 -25.043 0.307 1.00 28.73 C -ANISOU 1402 CB ARG A 169 3223 4032 3662 -85 217 395 C -ATOM 1403 CG ARG A 169 11.495 -23.610 -0.180 1.00 36.09 C -ANISOU 1403 CG ARG A 169 4118 4978 4615 -75 234 473 C -ATOM 1404 CD ARG A 169 10.464 -22.862 0.632 1.00 41.23 C -ANISOU 1404 CD ARG A 169 4782 5596 5285 -61 226 505 C -ATOM 1405 NE ARG A 169 9.157 -23.518 0.621 1.00 45.50 N -ANISOU 1405 NE ARG A 169 5338 6181 5770 -70 219 501 N -ATOM 1406 CZ ARG A 169 8.135 -23.140 1.385 1.00 42.51 C -ANISOU 1406 CZ ARG A 169 4976 5775 5401 -58 213 522 C -ATOM 1407 NH1 ARG A 169 8.278 -22.109 2.209 1.00 43.44 N -ANISOU 1407 NH1 ARG A 169 5104 5823 5580 -37 215 543 N -ATOM 1408 NH2 ARG A 169 6.980 -23.787 1.337 1.00 35.17 N -ANISOU 1408 NH2 ARG A 169 4055 4886 4422 -67 207 520 N -ATOM 1409 N LYS A 170 14.229 -26.933 2.213 1.00 22.91 N -ANISOU 1409 N LYS A 170 2544 3146 3014 -79 178 250 N -ATOM 1410 CA LYS A 170 14.824 -28.261 2.299 1.00 28.35 C -ANISOU 1410 CA LYS A 170 3247 3828 3698 -87 177 191 C -ATOM 1411 C LYS A 170 14.737 -28.810 3.729 1.00 24.85 C -ANISOU 1411 C LYS A 170 2844 3319 3279 -80 144 152 C -ATOM 1412 O LYS A 170 14.959 -28.085 4.699 1.00 22.26 O -ANISOU 1412 O LYS A 170 2529 2933 2995 -68 122 164 O -ATOM 1413 CB LYS A 170 16.286 -28.186 1.844 1.00 29.58 C -ANISOU 1413 CB LYS A 170 3375 3970 3896 -85 192 191 C -ATOM 1414 CG LYS A 170 17.041 -29.505 1.885 1.00 39.56 C -ANISOU 1414 CG LYS A 170 4647 5220 5165 -90 197 136 C -ATOM 1415 CD LYS A 170 18.475 -29.358 1.350 1.00 45.79 C -ANISOU 1415 CD LYS A 170 5403 5998 5998 -87 217 145 C -ATOM 1416 CE LYS A 170 19.434 -28.787 2.395 1.00 43.65 C -ANISOU 1416 CE LYS A 170 5129 5648 5805 -75 188 155 C -ATOM 1417 NZ LYS A 170 20.823 -28.675 1.862 1.00 45.77 N -ANISOU 1417 NZ LYS A 170 5362 5907 6122 -72 208 168 N -ATOM 1418 N LEU A 171 14.432 -30.095 3.857 1.00 16.14 N -ANISOU 1418 N LEU A 171 1760 2224 2146 -88 142 105 N -ATOM 1419 CA LEU A 171 14.193 -30.683 5.171 1.00 17.78 C -ANISOU 1419 CA LEU A 171 2006 2380 2370 -81 114 73 C -ATOM 1420 C LEU A 171 14.986 -31.973 5.361 1.00 19.01 C -ANISOU 1420 C LEU A 171 2168 2514 2542 -85 114 22 C -ATOM 1421 O LEU A 171 15.107 -32.769 4.428 1.00 17.55 O -ANISOU 1421 O LEU A 171 1969 2369 2329 -97 140 0 O -ATOM 1422 CB LEU A 171 12.689 -30.964 5.327 1.00 14.16 C -ANISOU 1422 CB LEU A 171 1568 1949 1862 -84 110 73 C -ATOM 1423 CG LEU A 171 12.188 -31.498 6.668 1.00 21.01 C -ANISOU 1423 CG LEU A 171 2476 2769 2738 -75 84 47 C -ATOM 1424 CD1 LEU A 171 10.774 -30.977 6.939 1.00 18.92 C -ANISOU 1424 CD1 LEU A 171 2225 2520 2445 -70 81 77 C -ATOM 1425 CD2 LEU A 171 12.236 -33.022 6.671 1.00 17.94 C -ANISOU 1425 CD2 LEU A 171 2097 2384 2334 -84 86 -4 C -ATOM 1426 N ARG A 172 15.530 -32.175 6.565 1.00 15.49 N -ANISOU 1426 N ARG A 172 1741 2005 2140 -75 86 5 N -ATOM 1427 CA ARG A 172 16.263 -33.398 6.882 1.00 8.69 C -ANISOU 1427 CA ARG A 172 884 1117 1301 -76 85 -36 C -ATOM 1428 C ARG A 172 15.857 -33.940 8.252 1.00 9.85 C -ANISOU 1428 C ARG A 172 1067 1219 1456 -68 53 -57 C -ATOM 1429 O ARG A 172 15.859 -33.202 9.249 1.00 14.38 O -ANISOU 1429 O ARG A 172 1659 1754 2052 -59 24 -40 O -ATOM 1430 CB ARG A 172 17.791 -33.164 6.859 1.00 12.87 C -ANISOU 1430 CB ARG A 172 1387 1613 1890 -72 85 -28 C -ATOM 1431 CG ARG A 172 18.349 -32.738 5.490 1.00 12.76 C -ANISOU 1431 CG ARG A 172 1335 1641 1872 -78 121 -8 C -ATOM 1432 CD ARG A 172 18.351 -33.886 4.507 1.00 16.06 C -ANISOU 1432 CD ARG A 172 1744 2100 2257 -88 159 -41 C -ATOM 1433 NE ARG A 172 18.917 -33.507 3.211 1.00 17.01 N -ANISOU 1433 NE ARG A 172 1831 2262 2370 -92 196 -22 N -ATOM 1434 CZ ARG A 172 18.201 -33.106 2.164 1.00 24.72 C -ANISOU 1434 CZ ARG A 172 2799 3304 3291 -102 218 -5 C -ATOM 1435 NH1 ARG A 172 16.877 -33.016 2.241 1.00 20.57 N -ANISOU 1435 NH1 ARG A 172 2293 2809 2715 -109 206 -2 N -ATOM 1436 NH2 ARG A 172 18.808 -32.791 1.031 1.00 28.67 N -ANISOU 1436 NH2 ARG A 172 3268 3841 3785 -105 253 13 N -ATOM 1437 N LEU A 173 15.525 -35.229 8.306 1.00 10.07 N -ANISOU 1437 N LEU A 173 1106 1253 1468 -72 61 -93 N -ATOM 1438 CA LEU A 173 15.258 -35.898 9.578 1.00 10.24 C -ANISOU 1438 CA LEU A 173 1157 1232 1501 -64 35 -112 C -ATOM 1439 C LEU A 173 16.592 -36.409 10.147 1.00 13.44 C -ANISOU 1439 C LEU A 173 1552 1590 1963 -58 22 -124 C -ATOM 1440 O LEU A 173 17.284 -37.206 9.507 1.00 15.81 O -ANISOU 1440 O LEU A 173 1831 1896 2280 -63 48 -143 O -ATOM 1441 CB LEU A 173 14.293 -37.065 9.377 1.00 10.25 C -ANISOU 1441 CB LEU A 173 1170 1258 1465 -71 49 -142 C -ATOM 1442 CG LEU A 173 13.771 -37.860 10.581 1.00 16.27 C -ANISOU 1442 CG LEU A 173 1963 1986 2232 -62 28 -159 C -ATOM 1443 CD1 LEU A 173 13.079 -36.961 11.620 1.00 16.89 C -ANISOU 1443 CD1 LEU A 173 2070 2045 2303 -49 -1 -132 C -ATOM 1444 CD2 LEU A 173 12.817 -38.962 10.116 1.00 16.63 C -ANISOU 1444 CD2 LEU A 173 2013 2063 2243 -74 48 -187 C -ATOM 1445 N ILE A 174 16.933 -35.962 11.350 1.00 13.88 N -ANISOU 1445 N ILE A 174 1625 1600 2048 -49 -15 -112 N -ATOM 1446 CA ILE A 174 18.231 -36.271 11.936 1.00 16.84 C -ANISOU 1446 CA ILE A 174 1987 1932 2479 -46 -34 -114 C -ATOM 1447 C ILE A 174 18.133 -37.093 13.221 1.00 16.21 C -ANISOU 1447 C ILE A 174 1933 1816 2410 -38 -62 -128 C -ATOM 1448 O ILE A 174 17.030 -37.453 13.662 1.00 15.92 O -ANISOU 1448 O ILE A 174 1925 1786 2338 -34 -65 -138 O -ATOM 1449 CB ILE A 174 18.991 -34.981 12.265 1.00 15.01 C -ANISOU 1449 CB ILE A 174 1748 1675 2279 -46 -60 -84 C -ATOM 1450 CG1 ILE A 174 18.254 -34.179 13.346 1.00 13.87 C -ANISOU 1450 CG1 ILE A 174 1644 1510 2116 -41 -94 -74 C -ATOM 1451 CG2 ILE A 174 19.207 -34.142 10.997 1.00 14.38 C -ANISOU 1451 CG2 ILE A 174 1638 1629 2196 -52 -31 -63 C -ATOM 1452 CD1 ILE A 174 19.139 -33.101 14.005 1.00 17.54 C -ANISOU 1452 CD1 ILE A 174 2109 1935 2620 -44 -129 -54 C -ATOM 1453 N ASP A 175 19.303 -37.373 13.799 1.00 13.87 N -ANISOU 1453 N ASP A 175 1621 1482 2165 -36 -83 -123 N -ATOM 1454 CA ASP A 175 19.466 -38.091 15.068 1.00 15.55 C -ANISOU 1454 CA ASP A 175 1851 1659 2397 -29 -115 -128 C -ATOM 1455 C ASP A 175 18.743 -39.432 15.112 1.00 11.90 C -ANISOU 1455 C ASP A 175 1399 1205 1918 -24 -94 -154 C -ATOM 1456 O ASP A 175 17.702 -39.577 15.760 1.00 14.24 O -ANISOU 1456 O ASP A 175 1728 1503 2179 -18 -104 -159 O -ATOM 1457 CB ASP A 175 19.065 -37.238 16.271 1.00 13.77 C -ANISOU 1457 CB ASP A 175 1665 1414 2155 -26 -159 -116 C -ATOM 1458 CG ASP A 175 19.668 -37.758 17.577 1.00 18.09 C -ANISOU 1458 CG ASP A 175 2222 1923 2729 -22 -200 -112 C -ATOM 1459 OD1 ASP A 175 19.685 -37.009 18.566 1.00 25.06 O -ANISOU 1459 OD1 ASP A 175 3132 2784 3604 -24 -240 -102 O -ATOM 1460 OD2 ASP A 175 20.138 -38.913 17.612 1.00 17.02 O -ANISOU 1460 OD2 ASP A 175 2066 1779 2624 -19 -191 -118 O -ATOM 1461 N TRP A 176 19.340 -40.404 14.436 1.00 10.44 N -ANISOU 1461 N TRP A 176 1183 1021 1762 -26 -62 -168 N -ATOM 1462 CA TRP A 176 18.835 -41.764 14.373 1.00 12.13 C -ANISOU 1462 CA TRP A 176 1400 1236 1972 -23 -36 -195 C -ATOM 1463 C TRP A 176 19.374 -42.616 15.510 1.00 14.74 C -ANISOU 1463 C TRP A 176 1729 1526 2347 -13 -59 -189 C -ATOM 1464 O TRP A 176 19.362 -43.848 15.441 1.00 16.33 O -ANISOU 1464 O TRP A 176 1920 1716 2568 -9 -34 -207 O -ATOM 1465 CB TRP A 176 19.167 -42.350 12.996 1.00 9.25 C -ANISOU 1465 CB TRP A 176 1006 893 1616 -31 17 -217 C -ATOM 1466 CG TRP A 176 18.482 -41.546 11.946 1.00 14.39 C -ANISOU 1466 CG TRP A 176 1661 1592 2215 -42 36 -220 C -ATOM 1467 CD1 TRP A 176 18.866 -40.318 11.460 1.00 17.23 C -ANISOU 1467 CD1 TRP A 176 2010 1968 2571 -46 31 -196 C -ATOM 1468 CD2 TRP A 176 17.227 -41.849 11.323 1.00 15.90 C -ANISOU 1468 CD2 TRP A 176 1868 1822 2350 -52 58 -242 C -ATOM 1469 NE1 TRP A 176 17.936 -39.867 10.542 1.00 14.24 N -ANISOU 1469 NE1 TRP A 176 1636 1637 2136 -56 52 -200 N -ATOM 1470 CE2 TRP A 176 16.926 -40.788 10.441 1.00 14.83 C -ANISOU 1470 CE2 TRP A 176 1728 1728 2178 -61 67 -228 C -ATOM 1471 CE3 TRP A 176 16.346 -42.931 11.400 1.00 14.06 C -ANISOU 1471 CE3 TRP A 176 1650 1594 2099 -56 72 -270 C -ATOM 1472 CZ2 TRP A 176 15.770 -40.775 9.649 1.00 13.45 C -ANISOU 1472 CZ2 TRP A 176 1562 1602 1944 -74 86 -239 C -ATOM 1473 CZ3 TRP A 176 15.193 -42.915 10.614 1.00 18.70 C -ANISOU 1473 CZ3 TRP A 176 2247 2227 2629 -70 89 -284 C -ATOM 1474 CH2 TRP A 176 14.921 -41.848 9.750 1.00 17.10 C -ANISOU 1474 CH2 TRP A 176 2039 2069 2388 -80 95 -268 C -ATOM 1475 N GLY A 177 19.826 -41.949 16.570 1.00 17.31 N -ANISOU 1475 N GLY A 177 2065 1827 2685 -9 -107 -163 N -ATOM 1476 CA GLY A 177 20.432 -42.618 17.708 1.00 16.98 C -ANISOU 1476 CA GLY A 177 2019 1750 2683 -1 -137 -148 C -ATOM 1477 C GLY A 177 19.475 -43.454 18.545 1.00 18.84 C -ANISOU 1477 C GLY A 177 2283 1980 2896 9 -143 -157 C -ATOM 1478 O GLY A 177 19.911 -44.324 19.301 1.00 18.10 O -ANISOU 1478 O GLY A 177 2179 1861 2837 18 -155 -147 O -ATOM 1479 N LEU A 178 18.176 -43.188 18.429 1.00 17.53 N -ANISOU 1479 N LEU A 178 2149 1837 2673 9 -134 -171 N -ATOM 1480 CA LEU A 178 17.176 -44.027 19.082 1.00 14.17 C -ANISOU 1480 CA LEU A 178 1747 1409 2228 19 -132 -178 C -ATOM 1481 C LEU A 178 16.451 -44.951 18.098 1.00 16.85 C -ANISOU 1481 C LEU A 178 2077 1767 2559 14 -83 -208 C -ATOM 1482 O LEU A 178 15.591 -45.722 18.500 1.00 16.89 O -ANISOU 1482 O LEU A 178 2096 1769 2551 20 -76 -216 O -ATOM 1483 CB LEU A 178 16.140 -43.183 19.843 1.00 12.31 C -ANISOU 1483 CB LEU A 178 1557 1181 1938 24 -158 -169 C -ATOM 1484 CG LEU A 178 16.645 -42.387 21.050 1.00 20.05 C -ANISOU 1484 CG LEU A 178 2560 2140 2918 28 -208 -146 C -ATOM 1485 CD1 LEU A 178 15.481 -41.717 21.790 1.00 20.05 C -ANISOU 1485 CD1 LEU A 178 2609 2146 2864 36 -222 -141 C -ATOM 1486 CD2 LEU A 178 17.422 -43.291 21.978 1.00 26.37 C -ANISOU 1486 CD2 LEU A 178 3347 2913 3759 35 -231 -132 C -ATOM 1487 N ALA A 179 16.798 -44.873 16.817 1.00 17.60 N -ANISOU 1487 N ALA A 179 2148 1882 2659 2 -49 -225 N -ATOM 1488 CA ALA A 179 16.089 -45.653 15.801 1.00 14.08 C -ANISOU 1488 CA ALA A 179 1696 1460 2196 -8 -4 -258 C -ATOM 1489 C ALA A 179 16.336 -47.147 15.967 1.00 18.29 C -ANISOU 1489 C ALA A 179 2213 1963 2773 -3 19 -275 C -ATOM 1490 O ALA A 179 17.405 -47.553 16.434 1.00 16.14 O -ANISOU 1490 O ALA A 179 1919 1658 2556 6 13 -261 O -ATOM 1491 CB ALA A 179 16.472 -45.189 14.394 1.00 12.10 C -ANISOU 1491 CB ALA A 179 1424 1238 1935 -23 26 -271 C -ATOM 1492 N GLU A 180 15.346 -47.962 15.602 1.00 12.77 N -ANISOU 1492 N GLU A 180 1522 1276 2054 -10 46 -303 N -ATOM 1493 CA GLU A 180 15.467 -49.428 15.702 1.00 16.10 C -ANISOU 1493 CA GLU A 180 1929 1668 2521 -7 74 -322 C -ATOM 1494 C GLU A 180 14.892 -50.126 14.483 1.00 16.88 C -ANISOU 1494 C GLU A 180 2023 1787 2602 -28 121 -368 C -ATOM 1495 O GLU A 180 14.079 -49.555 13.758 1.00 20.07 O -ANISOU 1495 O GLU A 180 2441 2235 2951 -44 124 -380 O -ATOM 1496 CB GLU A 180 14.714 -49.965 16.919 1.00 17.20 C -ANISOU 1496 CB GLU A 180 2087 1786 2661 7 51 -307 C -ATOM 1497 CG GLU A 180 15.579 -50.424 18.072 1.00 20.57 C -ANISOU 1497 CG GLU A 180 2502 2172 3143 26 30 -277 C -ATOM 1498 CD GLU A 180 16.343 -51.715 17.797 1.00 22.60 C -ANISOU 1498 CD GLU A 180 2724 2394 3468 29 68 -291 C -ATOM 1499 OE1 GLU A 180 16.844 -52.301 18.774 1.00 27.51 O -ANISOU 1499 OE1 GLU A 180 3334 2982 4137 45 54 -263 O -ATOM 1500 OE2 GLU A 180 16.467 -52.142 16.629 1.00 21.15 O -ANISOU 1500 OE2 GLU A 180 2526 2217 3293 14 114 -327 O -ATOM 1501 N PHE A 181 15.294 -51.378 14.284 1.00 15.58 N -ANISOU 1501 N PHE A 181 1840 1592 2487 -28 158 -392 N -ATOM 1502 CA PHE A 181 14.721 -52.217 13.242 1.00 14.19 C -ANISOU 1502 CA PHE A 181 1663 1429 2298 -50 203 -442 C -ATOM 1503 C PHE A 181 13.410 -52.827 13.748 1.00 14.12 C -ANISOU 1503 C PHE A 181 1673 1420 2271 -54 195 -449 C -ATOM 1504 O PHE A 181 13.343 -53.300 14.885 1.00 18.49 O -ANISOU 1504 O PHE A 181 2228 1939 2858 -34 177 -425 O -ATOM 1505 CB PHE A 181 15.702 -53.333 12.877 1.00 20.31 C -ANISOU 1505 CB PHE A 181 2412 2165 3141 -48 251 -467 C -ATOM 1506 CG PHE A 181 16.925 -52.851 12.149 1.00 15.72 C -ANISOU 1506 CG PHE A 181 1810 1587 2578 -48 271 -465 C -ATOM 1507 CD1 PHE A 181 16.944 -52.809 10.760 1.00 14.82 C -ANISOU 1507 CD1 PHE A 181 1694 1503 2432 -70 313 -505 C -ATOM 1508 CD2 PHE A 181 18.051 -52.441 12.851 1.00 16.40 C -ANISOU 1508 CD2 PHE A 181 1875 1645 2711 -27 248 -422 C -ATOM 1509 CE1 PHE A 181 18.073 -52.365 10.077 1.00 18.59 C -ANISOU 1509 CE1 PHE A 181 2151 1985 2928 -68 335 -501 C -ATOM 1510 CE2 PHE A 181 19.184 -51.995 12.181 1.00 19.46 C -ANISOU 1510 CE2 PHE A 181 2239 2034 3120 -26 267 -416 C -ATOM 1511 CZ PHE A 181 19.190 -51.964 10.783 1.00 17.85 C -ANISOU 1511 CZ PHE A 181 2034 1860 2886 -45 313 -455 C -ATOM 1512 N TYR A 182 12.377 -52.812 12.909 1.00 15.91 N -ANISOU 1512 N TYR A 182 1913 1686 2445 -79 207 -479 N -ATOM 1513 CA TYR A 182 11.121 -53.453 13.270 1.00 15.25 C -ANISOU 1513 CA TYR A 182 1844 1602 2349 -85 203 -486 C -ATOM 1514 C TYR A 182 11.122 -54.933 12.900 1.00 17.20 C -ANISOU 1514 C TYR A 182 2078 1817 2639 -98 247 -531 C -ATOM 1515 O TYR A 182 11.323 -55.307 11.737 1.00 16.00 O -ANISOU 1515 O TYR A 182 1921 1678 2480 -123 285 -577 O -ATOM 1516 CB TYR A 182 9.887 -52.753 12.672 1.00 18.00 C -ANISOU 1516 CB TYR A 182 2209 2007 2623 -107 189 -489 C -ATOM 1517 CG TYR A 182 8.618 -53.520 13.013 1.00 16.76 C -ANISOU 1517 CG TYR A 182 2061 1846 2461 -115 187 -496 C -ATOM 1518 CD1 TYR A 182 8.076 -53.478 14.293 1.00 18.70 C -ANISOU 1518 CD1 TYR A 182 2317 2071 2716 -90 158 -456 C -ATOM 1519 CD2 TYR A 182 8.008 -54.340 12.076 1.00 19.91 C -ANISOU 1519 CD2 TYR A 182 2457 2260 2847 -148 216 -543 C -ATOM 1520 CE1 TYR A 182 6.926 -54.212 14.616 1.00 18.94 C -ANISOU 1520 CE1 TYR A 182 2353 2096 2748 -96 159 -459 C -ATOM 1521 CE2 TYR A 182 6.873 -55.068 12.388 1.00 19.00 C -ANISOU 1521 CE2 TYR A 182 2347 2139 2734 -157 213 -549 C -ATOM 1522 CZ TYR A 182 6.342 -55.009 13.656 1.00 15.86 C -ANISOU 1522 CZ TYR A 182 1956 1719 2350 -130 186 -505 C -ATOM 1523 OH TYR A 182 5.210 -55.755 13.948 1.00 16.36 O -ANISOU 1523 OH TYR A 182 2022 1775 2420 -139 186 -507 O -ATOM 1524 N HIS A 183 10.895 -55.764 13.913 1.00 13.33 N -ANISOU 1524 N HIS A 183 1586 1284 2194 -81 242 -517 N -ATOM 1525 CA HIS A 183 10.777 -57.203 13.740 1.00 16.68 C -ANISOU 1525 CA HIS A 183 1999 1671 2668 -91 282 -554 C -ATOM 1526 C HIS A 183 9.438 -57.638 14.349 1.00 17.75 C -ANISOU 1526 C HIS A 183 2146 1805 2792 -93 266 -545 C -ATOM 1527 O HIS A 183 9.170 -57.366 15.526 1.00 19.91 O -ANISOU 1527 O HIS A 183 2427 2068 3070 -67 232 -497 O -ATOM 1528 CB HIS A 183 11.932 -57.925 14.429 1.00 19.80 C -ANISOU 1528 CB HIS A 183 2371 2007 3147 -64 299 -537 C -ATOM 1529 CG HIS A 183 13.278 -57.644 13.826 1.00 23.30 C -ANISOU 1529 CG HIS A 183 2796 2444 3612 -61 321 -544 C -ATOM 1530 ND1 HIS A 183 13.671 -58.154 12.606 1.00 26.13 N -ANISOU 1530 ND1 HIS A 183 3148 2802 3980 -83 374 -598 N -ATOM 1531 CD2 HIS A 183 14.328 -56.924 14.288 1.00 23.44 C -ANISOU 1531 CD2 HIS A 183 2802 2455 3648 -39 299 -503 C -ATOM 1532 CE1 HIS A 183 14.900 -57.750 12.338 1.00 26.26 C -ANISOU 1532 CE1 HIS A 183 3147 2811 4020 -72 386 -586 C -ATOM 1533 NE2 HIS A 183 15.323 -57.004 13.343 1.00 23.62 N -ANISOU 1533 NE2 HIS A 183 2807 2473 3693 -46 339 -529 N -ATOM 1534 N PRO A 184 8.596 -58.312 13.555 1.00 18.36 N -ANISOU 1534 N PRO A 184 2228 1894 2855 -126 290 -591 N -ATOM 1535 CA PRO A 184 7.261 -58.658 14.067 1.00 20.60 C -ANISOU 1535 CA PRO A 184 2519 2180 3127 -130 273 -579 C -ATOM 1536 C PRO A 184 7.382 -59.436 15.373 1.00 19.16 C -ANISOU 1536 C PRO A 184 2327 1942 3011 -98 270 -545 C -ATOM 1537 O PRO A 184 8.157 -60.394 15.429 1.00 17.53 O -ANISOU 1537 O PRO A 184 2102 1687 2872 -92 304 -562 O -ATOM 1538 CB PRO A 184 6.688 -59.564 12.972 1.00 21.55 C -ANISOU 1538 CB PRO A 184 2638 2306 3243 -173 308 -643 C -ATOM 1539 CG PRO A 184 7.460 -59.235 11.744 1.00 27.23 C -ANISOU 1539 CG PRO A 184 3358 3052 3937 -194 333 -683 C -ATOM 1540 CD PRO A 184 8.839 -58.861 12.209 1.00 20.53 C -ANISOU 1540 CD PRO A 184 2498 2176 3126 -160 335 -655 C -ATOM 1541 N GLY A 185 6.657 -59.016 16.406 1.00 20.23 N -ANISOU 1541 N GLY A 185 2474 2084 3130 -77 234 -496 N -ATOM 1542 CA GLY A 185 6.621 -59.738 17.664 1.00 22.19 C -ANISOU 1542 CA GLY A 185 2714 2285 3432 -47 230 -460 C -ATOM 1543 C GLY A 185 7.681 -59.319 18.661 1.00 23.51 C -ANISOU 1543 C GLY A 185 2877 2432 3622 -11 209 -414 C -ATOM 1544 O GLY A 185 7.686 -59.763 19.807 1.00 21.28 O -ANISOU 1544 O GLY A 185 2591 2120 3376 17 199 -374 O -ATOM 1545 N GLN A 186 8.587 -58.453 18.232 1.00 18.73 N -ANISOU 1545 N GLN A 186 2274 1846 2995 -11 201 -416 N -ATOM 1546 CA GLN A 186 9.681 -58.035 19.095 1.00 19.73 C -ANISOU 1546 CA GLN A 186 2395 1956 3145 18 178 -375 C -ATOM 1547 C GLN A 186 9.188 -57.026 20.131 1.00 21.94 C -ANISOU 1547 C GLN A 186 2701 2257 3376 38 130 -326 C -ATOM 1548 O GLN A 186 8.395 -56.136 19.816 1.00 21.24 O -ANISOU 1548 O GLN A 186 2635 2210 3226 28 114 -328 O -ATOM 1549 CB GLN A 186 10.816 -57.448 18.254 1.00 19.54 C -ANISOU 1549 CB GLN A 186 2361 1943 3119 8 186 -393 C -ATOM 1550 CG GLN A 186 12.121 -57.280 19.003 1.00 28.53 C -ANISOU 1550 CG GLN A 186 3484 3055 4300 33 170 -355 C -ATOM 1551 CD GLN A 186 13.309 -57.145 18.062 1.00 33.03 C -ANISOU 1551 CD GLN A 186 4033 3623 4894 24 196 -378 C -ATOM 1552 OE1 GLN A 186 13.556 -58.021 17.227 1.00 36.94 O -ANISOU 1552 OE1 GLN A 186 4511 4098 5426 10 244 -419 O -ATOM 1553 NE2 GLN A 186 14.039 -56.042 18.182 1.00 31.62 N -ANISOU 1553 NE2 GLN A 186 3858 3463 4695 30 165 -354 N -ATOM 1554 N GLU A 187 9.638 -57.182 21.371 1.00 18.90 N -ANISOU 1554 N GLU A 187 2313 1846 3020 67 108 -282 N -ATOM 1555 CA GLU A 187 9.313 -56.226 22.420 1.00 20.08 C -ANISOU 1555 CA GLU A 187 2492 2014 3124 86 64 -239 C -ATOM 1556 C GLU A 187 10.428 -55.194 22.529 1.00 21.68 C -ANISOU 1556 C GLU A 187 2698 2225 3313 91 36 -224 C -ATOM 1557 O GLU A 187 11.603 -55.555 22.590 1.00 23.77 O -ANISOU 1557 O GLU A 187 2937 2466 3627 95 39 -218 O -ATOM 1558 CB GLU A 187 9.109 -56.943 23.754 1.00 20.03 C -ANISOU 1558 CB GLU A 187 2484 1978 3147 113 54 -197 C -ATOM 1559 CG GLU A 187 7.947 -57.944 23.721 1.00 24.92 C -ANISOU 1559 CG GLU A 187 3099 2586 3784 110 81 -206 C -ATOM 1560 CD GLU A 187 7.559 -58.446 25.099 1.00 37.68 C -ANISOU 1560 CD GLU A 187 4719 4181 5415 139 68 -157 C -ATOM 1561 OE1 GLU A 187 8.460 -58.672 25.935 1.00 39.16 O -ANISOU 1561 OE1 GLU A 187 4895 4348 5634 159 54 -124 O -ATOM 1562 OE2 GLU A 187 6.348 -58.617 25.345 1.00 41.74 O -ANISOU 1562 OE2 GLU A 187 5246 4702 5910 142 73 -149 O -ATOM 1563 N TYR A 188 10.058 -53.914 22.539 1.00 15.11 N -ANISOU 1563 N TYR A 188 1895 1427 2419 88 9 -217 N -ATOM 1564 CA TYR A 188 11.038 -52.823 22.537 1.00 16.20 C -ANISOU 1564 CA TYR A 188 2038 1575 2543 88 -18 -207 C -ATOM 1565 C TYR A 188 11.037 -52.054 23.843 1.00 20.21 C -ANISOU 1565 C TYR A 188 2575 2083 3020 107 -62 -167 C -ATOM 1566 O TYR A 188 10.068 -52.094 24.586 1.00 20.21 O -ANISOU 1566 O TYR A 188 2599 2086 2993 120 -70 -149 O -ATOM 1567 CB TYR A 188 10.774 -51.860 21.379 1.00 20.55 C -ANISOU 1567 CB TYR A 188 2596 2163 3049 67 -11 -233 C -ATOM 1568 CG TYR A 188 10.938 -52.538 20.054 1.00 17.41 C -ANISOU 1568 CG TYR A 188 2172 1769 2675 45 31 -275 C -ATOM 1569 CD1 TYR A 188 12.189 -52.652 19.486 1.00 20.03 C -ANISOU 1569 CD1 TYR A 188 2478 2088 3045 39 45 -288 C -ATOM 1570 CD2 TYR A 188 9.851 -53.117 19.397 1.00 14.15 C -ANISOU 1570 CD2 TYR A 188 1760 1369 2247 29 58 -303 C -ATOM 1571 CE1 TYR A 188 12.374 -53.289 18.296 1.00 22.63 C -ANISOU 1571 CE1 TYR A 188 2786 2418 3393 20 88 -329 C -ATOM 1572 CE2 TYR A 188 10.026 -53.767 18.182 1.00 16.03 C -ANISOU 1572 CE2 TYR A 188 1978 1611 2503 5 97 -347 C -ATOM 1573 CZ TYR A 188 11.306 -53.845 17.646 1.00 16.47 C -ANISOU 1573 CZ TYR A 188 2011 1654 2593 2 114 -361 C -ATOM 1574 OH TYR A 188 11.541 -54.479 16.454 1.00 20.28 O -ANISOU 1574 OH TYR A 188 2477 2138 3091 -20 157 -407 O -ATOM 1575 N ASN A 189 12.133 -51.353 24.109 1.00 17.19 N -ANISOU 1575 N ASN A 189 2191 1699 2643 108 -91 -152 N -ATOM 1576 CA ASN A 189 12.237 -50.467 25.263 1.00 16.32 C -ANISOU 1576 CA ASN A 189 2113 1591 2498 121 -136 -121 C -ATOM 1577 C ASN A 189 11.219 -49.337 25.126 1.00 13.85 C -ANISOU 1577 C ASN A 189 1837 1305 2119 118 -141 -127 C -ATOM 1578 O ASN A 189 11.091 -48.747 24.054 1.00 19.45 O -ANISOU 1578 O ASN A 189 2543 2035 2813 102 -125 -150 O -ATOM 1579 CB ASN A 189 13.664 -49.901 25.305 1.00 21.42 C -ANISOU 1579 CB ASN A 189 2742 2229 3165 114 -163 -111 C -ATOM 1580 CG ASN A 189 13.932 -49.018 26.518 1.00 29.77 C -ANISOU 1580 CG ASN A 189 3833 3289 4191 122 -214 -82 C -ATOM 1581 OD1 ASN A 189 13.101 -48.873 27.414 1.00 21.50 O -ANISOU 1581 OD1 ASN A 189 2821 2244 3102 135 -227 -68 O -ATOM 1582 ND2 ASN A 189 15.126 -48.436 26.556 1.00 36.70 N -ANISOU 1582 ND2 ASN A 189 4697 4161 5085 112 -243 -73 N -ATOM 1583 N VAL A 190 10.485 -49.029 26.191 1.00 16.54 N -ANISOU 1583 N VAL A 190 2215 1647 2423 134 -159 -105 N -ATOM 1584 CA VAL A 190 9.501 -47.942 26.108 1.00 12.06 C -ANISOU 1584 CA VAL A 190 1684 1101 1799 135 -158 -106 C -ATOM 1585 C VAL A 190 10.115 -46.579 26.443 1.00 15.38 C -ANISOU 1585 C VAL A 190 2130 1524 2191 131 -191 -100 C -ATOM 1586 O VAL A 190 9.466 -45.544 26.304 1.00 20.86 O -ANISOU 1586 O VAL A 190 2851 2232 2844 131 -189 -102 O -ATOM 1587 CB VAL A 190 8.233 -48.208 26.976 1.00 15.67 C -ANISOU 1587 CB VAL A 190 2170 1557 2226 155 -152 -87 C -ATOM 1588 CG1 VAL A 190 7.517 -49.486 26.524 1.00 17.61 C -ANISOU 1588 CG1 VAL A 190 2390 1800 2502 154 -118 -95 C -ATOM 1589 CG2 VAL A 190 8.596 -48.271 28.458 1.00 16.86 C -ANISOU 1589 CG2 VAL A 190 2345 1691 2369 174 -183 -58 C -ATOM 1590 N ARG A 191 11.381 -46.586 26.864 1.00 16.73 N -ANISOU 1590 N ARG A 191 2288 1680 2389 128 -221 -92 N -ATOM 1591 CA ARG A 191 12.080 -45.351 27.209 1.00 22.31 C -ANISOU 1591 CA ARG A 191 3016 2386 3075 121 -256 -88 C -ATOM 1592 C ARG A 191 12.767 -44.729 25.995 1.00 21.88 C -ANISOU 1592 C ARG A 191 2934 2340 3039 101 -248 -106 C -ATOM 1593 O ARG A 191 14.004 -44.608 25.941 1.00 20.27 O -ANISOU 1593 O ARG A 191 2707 2126 2868 91 -269 -102 O -ATOM 1594 CB ARG A 191 13.085 -45.591 28.343 1.00 23.22 C -ANISOU 1594 CB ARG A 191 3132 2484 3206 124 -298 -65 C -ATOM 1595 CG ARG A 191 12.454 -46.138 29.620 1.00 29.76 C -ANISOU 1595 CG ARG A 191 3990 3307 4011 144 -308 -43 C -ATOM 1596 CD ARG A 191 13.455 -46.172 30.759 1.00 41.24 C -ANISOU 1596 CD ARG A 191 5450 4752 5470 144 -356 -18 C -ATOM 1597 NE ARG A 191 13.795 -44.826 31.209 1.00 51.04 N -ANISOU 1597 NE ARG A 191 6728 5994 6671 133 -392 -22 N -ATOM 1598 CZ ARG A 191 14.845 -44.533 31.970 1.00 59.55 C -ANISOU 1598 CZ ARG A 191 7809 7066 7751 122 -442 -7 C -ATOM 1599 NH1 ARG A 191 15.671 -45.493 32.365 1.00 59.53 N -ANISOU 1599 NH1 ARG A 191 7771 7058 7790 123 -460 19 N -ATOM 1600 NH2 ARG A 191 15.075 -43.278 32.330 1.00 62.27 N -ANISOU 1600 NH2 ARG A 191 8191 7410 8058 108 -472 -17 N -ATOM 1601 N VAL A 192 11.943 -44.335 25.029 1.00 17.93 N -ANISOU 1601 N VAL A 192 2435 1860 2518 95 -217 -121 N -ATOM 1602 CA VAL A 192 12.375 -43.648 23.830 1.00 17.11 C -ANISOU 1602 CA VAL A 192 2309 1770 2421 78 -205 -136 C -ATOM 1603 C VAL A 192 11.491 -42.413 23.645 1.00 19.79 C -ANISOU 1603 C VAL A 192 2679 2127 2714 78 -200 -134 C -ATOM 1604 O VAL A 192 10.457 -42.270 24.326 1.00 16.33 O -ANISOU 1604 O VAL A 192 2275 1688 2242 92 -198 -124 O -ATOM 1605 CB VAL A 192 12.229 -44.550 22.583 1.00 13.70 C -ANISOU 1605 CB VAL A 192 1839 1353 2012 69 -165 -156 C -ATOM 1606 CG1 VAL A 192 13.139 -45.794 22.691 1.00 12.50 C -ANISOU 1606 CG1 VAL A 192 1654 1179 1915 70 -162 -159 C -ATOM 1607 CG2 VAL A 192 10.759 -44.966 22.400 1.00 16.11 C -ANISOU 1607 CG2 VAL A 192 2158 1676 2289 73 -138 -162 C -ATOM 1608 N ALA A 193 11.899 -41.536 22.725 1.00 19.02 N -ANISOU 1608 N ALA A 193 2566 2041 2618 64 -195 -139 N -ATOM 1609 CA ALA A 193 11.188 -40.292 22.418 1.00 16.89 C -ANISOU 1609 CA ALA A 193 2317 1785 2313 63 -187 -133 C -ATOM 1610 C ALA A 193 11.255 -39.273 23.554 1.00 15.43 C -ANISOU 1610 C ALA A 193 2176 1578 2109 71 -217 -121 C -ATOM 1611 O ALA A 193 11.463 -39.619 24.724 1.00 19.31 O -ANISOU 1611 O ALA A 193 2691 2049 2597 80 -242 -117 O -ATOM 1612 CB ALA A 193 9.720 -40.582 22.037 1.00 18.06 C -ANISOU 1612 CB ALA A 193 2472 1957 2432 69 -155 -131 C -ATOM 1613 N SER A 194 11.107 -38.003 23.210 1.00 13.79 N -ANISOU 1613 N SER A 194 1979 1374 1886 66 -213 -117 N -ATOM 1614 CA ASER A 194 11.015 -36.968 24.220 1.00 15.19 C -ANISOU 1614 CA ASER A 194 2202 1528 2041 72 -234 -110 C -ATOM 1615 CA BSER A 194 11.012 -36.959 24.217 0.00 17.17 C -ANISOU 1615 CA BSER A 194 2453 1779 2293 72 -234 -110 C -ATOM 1616 C SER A 194 9.630 -37.015 24.851 1.00 17.31 C -ANISOU 1616 C SER A 194 2508 1797 2271 92 -215 -102 C -ATOM 1617 O SER A 194 8.655 -37.342 24.182 1.00 14.94 O -ANISOU 1617 O SER A 194 2194 1521 1962 97 -183 -96 O -ATOM 1618 CB ASER A 194 11.242 -35.596 23.593 1.00 19.69 C -ANISOU 1618 CB ASER A 194 2769 2098 2615 62 -229 -106 C -ATOM 1619 CB BSER A 194 11.247 -35.583 23.594 0.00 19.96 C -ANISOU 1619 CB BSER A 194 2803 2132 2649 62 -229 -106 C -ATOM 1620 OG ASER A 194 10.557 -34.596 24.333 1.00 27.84 O -ANISOU 1620 OG ASER A 194 3849 3112 3618 72 -228 -100 O -ATOM 1621 OG BSER A 194 12.605 -35.405 23.235 0.00 19.92 O -ANISOU 1621 OG BSER A 194 2768 2119 2681 45 -251 -111 O -ATOM 1622 N ARG A 195 9.553 -36.690 26.139 1.00 16.00 N -ANISOU 1622 N ARG A 195 2390 1608 2083 103 -235 -100 N -ATOM 1623 CA ARG A 195 8.296 -36.756 26.887 1.00 18.85 C -ANISOU 1623 CA ARG A 195 2790 1965 2407 125 -216 -90 C -ATOM 1624 C ARG A 195 7.057 -36.308 26.103 1.00 13.43 C -ANISOU 1624 C ARG A 195 2098 1297 1708 133 -174 -76 C -ATOM 1625 O ARG A 195 6.065 -37.027 26.056 1.00 13.56 O -ANISOU 1625 O ARG A 195 2110 1327 1714 145 -151 -66 O -ATOM 1626 CB ARG A 195 8.384 -35.945 28.184 1.00 19.55 C -ANISOU 1626 CB ARG A 195 2937 2025 2467 131 -237 -93 C -ATOM 1627 CG ARG A 195 7.106 -35.990 29.023 1.00 19.35 C -ANISOU 1627 CG ARG A 195 2955 1993 2403 157 -213 -81 C -ATOM 1628 CD ARG A 195 7.168 -34.972 30.155 1.00 23.67 C -ANISOU 1628 CD ARG A 195 3565 2512 2918 161 -226 -89 C -ATOM 1629 NE ARG A 195 8.430 -35.070 30.875 1.00 28.80 N -ANISOU 1629 NE ARG A 195 4224 3148 3569 145 -277 -103 N -ATOM 1630 CZ ARG A 195 9.040 -34.049 31.465 1.00 28.67 C -ANISOU 1630 CZ ARG A 195 4245 3108 3541 131 -302 -119 C -ATOM 1631 NH1 ARG A 195 8.502 -32.833 31.440 1.00 23.38 N -ANISOU 1631 NH1 ARG A 195 3608 2420 2856 135 -277 -124 N -ATOM 1632 NH2 ARG A 195 10.188 -34.251 32.091 1.00 34.26 N -ANISOU 1632 NH2 ARG A 195 4956 3809 4252 113 -353 -128 N -ATOM 1633 N TYR A 196 7.109 -35.119 25.508 1.00 16.27 N -ANISOU 1633 N TYR A 196 2455 1657 2071 125 -164 -73 N -ATOM 1634 CA TYR A 196 5.908 -34.519 24.903 1.00 15.08 C -ANISOU 1634 CA TYR A 196 2302 1522 1908 135 -125 -52 C -ATOM 1635 C TYR A 196 5.446 -35.275 23.656 1.00 14.31 C -ANISOU 1635 C TYR A 196 2154 1464 1819 126 -104 -44 C -ATOM 1636 O TYR A 196 4.301 -35.118 23.204 1.00 12.73 O -ANISOU 1636 O TYR A 196 1946 1284 1606 134 -74 -23 O -ATOM 1637 CB TYR A 196 6.151 -33.048 24.575 1.00 17.38 C -ANISOU 1637 CB TYR A 196 2599 1799 2204 129 -119 -46 C -ATOM 1638 CG TYR A 196 6.797 -32.313 25.717 1.00 21.19 C -ANISOU 1638 CG TYR A 196 3129 2240 2680 129 -144 -62 C -ATOM 1639 CD1 TYR A 196 6.242 -32.350 26.990 1.00 20.98 C -ANISOU 1639 CD1 TYR A 196 3157 2191 2623 147 -144 -64 C -ATOM 1640 CD2 TYR A 196 7.989 -31.624 25.537 1.00 28.95 C -ANISOU 1640 CD2 TYR A 196 4105 3209 3687 109 -170 -74 C -ATOM 1641 CE1 TYR A 196 6.841 -31.693 28.048 1.00 24.20 C -ANISOU 1641 CE1 TYR A 196 3613 2564 3019 143 -169 -82 C -ATOM 1642 CE2 TYR A 196 8.600 -30.965 26.592 1.00 30.64 C -ANISOU 1642 CE2 TYR A 196 4363 3385 3893 104 -198 -91 C -ATOM 1643 CZ TYR A 196 8.019 -31.003 27.843 1.00 30.86 C -ANISOU 1643 CZ TYR A 196 4447 3392 3885 120 -198 -97 C -ATOM 1644 OH TYR A 196 8.622 -30.349 28.895 1.00 32.91 O -ANISOU 1644 OH TYR A 196 4756 3618 4132 112 -227 -117 O -ATOM 1645 N PHE A 197 6.313 -36.145 23.150 1.00 9.74 N -ANISOU 1645 N PHE A 197 1541 897 1262 111 -119 -62 N -ATOM 1646 CA PHE A 197 6.071 -36.815 21.877 1.00 16.08 C -ANISOU 1646 CA PHE A 197 2298 1739 2073 97 -101 -64 C -ATOM 1647 C PHE A 197 5.928 -38.330 22.044 1.00 13.97 C -ANISOU 1647 C PHE A 197 2020 1477 1813 98 -101 -76 C -ATOM 1648 O PHE A 197 5.819 -39.057 21.064 1.00 11.77 O -ANISOU 1648 O PHE A 197 1705 1225 1543 84 -87 -85 O -ATOM 1649 CB PHE A 197 7.192 -36.445 20.897 1.00 15.93 C -ANISOU 1649 CB PHE A 197 2245 1731 2077 77 -107 -74 C -ATOM 1650 CG PHE A 197 7.339 -34.967 20.720 1.00 14.48 C -ANISOU 1650 CG PHE A 197 2069 1540 1893 76 -105 -59 C -ATOM 1651 CD1 PHE A 197 6.569 -34.297 19.791 1.00 10.51 C -ANISOU 1651 CD1 PHE A 197 1549 1066 1379 74 -78 -36 C -ATOM 1652 CD2 PHE A 197 8.198 -34.234 21.536 1.00 14.96 C -ANISOU 1652 CD2 PHE A 197 2156 1563 1964 77 -131 -65 C -ATOM 1653 CE1 PHE A 197 6.665 -32.923 19.640 1.00 16.33 C -ANISOU 1653 CE1 PHE A 197 2291 1793 2121 75 -72 -18 C -ATOM 1654 CE2 PHE A 197 8.307 -32.865 21.398 1.00 14.59 C -ANISOU 1654 CE2 PHE A 197 2117 1504 1922 75 -127 -53 C -ATOM 1655 CZ PHE A 197 7.528 -32.205 20.445 1.00 12.99 C -ANISOU 1655 CZ PHE A 197 1895 1328 1712 76 -95 -28 C -ATOM 1656 N LYS A 198 5.924 -38.797 23.296 1.00 13.64 N -ANISOU 1656 N LYS A 198 2008 1407 1768 114 -116 -77 N -ATOM 1657 CA LYS A 198 5.833 -40.229 23.578 1.00 13.40 C -ANISOU 1657 CA LYS A 198 1966 1375 1750 117 -117 -85 C -ATOM 1658 C LYS A 198 4.433 -40.683 23.244 1.00 16.42 C -ANISOU 1658 C LYS A 198 2343 1779 2118 122 -88 -72 C -ATOM 1659 O LYS A 198 3.488 -40.016 23.642 1.00 13.01 O -ANISOU 1659 O LYS A 198 1936 1346 1663 137 -76 -50 O -ATOM 1660 CB LYS A 198 6.083 -40.501 25.068 1.00 13.19 C -ANISOU 1660 CB LYS A 198 1976 1317 1718 134 -139 -81 C -ATOM 1661 CG LYS A 198 7.565 -40.506 25.478 1.00 10.01 C -ANISOU 1661 CG LYS A 198 1571 895 1339 126 -174 -93 C -ATOM 1662 CD LYS A 198 7.681 -40.482 26.992 1.00 8.55 C -ANISOU 1662 CD LYS A 198 1429 684 1135 142 -199 -84 C -ATOM 1663 CE LYS A 198 9.133 -40.252 27.434 1.00 10.62 C -ANISOU 1663 CE LYS A 198 1690 929 1415 129 -240 -92 C -ATOM 1664 NZ LYS A 198 9.975 -41.450 27.150 1.00 14.76 N -ANISOU 1664 NZ LYS A 198 2171 1454 1982 122 -248 -96 N -ATOM 1665 N GLY A 199 4.302 -41.803 22.530 1.00 12.98 N -ANISOU 1665 N GLY A 199 1873 1361 1699 109 -77 -86 N -ATOM 1666 CA GLY A 199 2.982 -42.349 22.208 1.00 11.79 C -ANISOU 1666 CA GLY A 199 1712 1230 1538 109 -54 -74 C -ATOM 1667 C GLY A 199 2.319 -42.946 23.440 1.00 14.45 C -ANISOU 1667 C GLY A 199 2075 1543 1872 133 -54 -58 C -ATOM 1668 O GLY A 199 2.987 -43.298 24.399 1.00 16.53 O -ANISOU 1668 O GLY A 199 2356 1780 2146 145 -71 -62 O -ATOM 1669 N PRO A 200 0.980 -43.048 23.433 1.00 10.74 N -ANISOU 1669 N PRO A 200 1606 1086 1388 141 -34 -35 N -ATOM 1670 CA PRO A 200 0.311 -43.720 24.549 1.00 12.28 C -ANISOU 1670 CA PRO A 200 1821 1260 1583 165 -29 -17 C -ATOM 1671 C PRO A 200 0.882 -45.125 24.802 1.00 13.89 C -ANISOU 1671 C PRO A 200 2009 1449 1821 161 -37 -36 C -ATOM 1672 O PRO A 200 0.897 -45.581 25.950 1.00 15.84 O -ANISOU 1672 O PRO A 200 2277 1672 2071 183 -43 -24 O -ATOM 1673 CB PRO A 200 -1.144 -43.797 24.074 1.00 8.24 C -ANISOU 1673 CB PRO A 200 1296 772 1064 164 -5 7 C -ATOM 1674 CG PRO A 200 -1.313 -42.571 23.242 1.00 14.32 C -ANISOU 1674 CG PRO A 200 2060 1567 1815 153 2 17 C -ATOM 1675 CD PRO A 200 0.028 -42.401 22.518 1.00 15.01 C -ANISOU 1675 CD PRO A 200 2132 1660 1912 131 -15 -17 C -ATOM 1676 N GLU A 201 1.371 -45.795 23.758 1.00 10.11 N -ANISOU 1676 N GLU A 201 1493 984 1366 135 -35 -65 N -ATOM 1677 CA GLU A 201 1.900 -47.140 23.944 1.00 12.28 C -ANISOU 1677 CA GLU A 201 1749 1239 1679 132 -36 -82 C -ATOM 1678 C GLU A 201 3.086 -47.133 24.921 1.00 14.93 C -ANISOU 1678 C GLU A 201 2101 1545 2026 146 -60 -82 C -ATOM 1679 O GLU A 201 3.215 -48.024 25.770 1.00 13.14 O -ANISOU 1679 O GLU A 201 1876 1296 1821 161 -64 -73 O -ATOM 1680 CB GLU A 201 2.281 -47.803 22.605 1.00 15.02 C -ANISOU 1680 CB GLU A 201 2056 1602 2048 100 -25 -118 C -ATOM 1681 CG GLU A 201 3.278 -47.031 21.735 1.00 12.17 C -ANISOU 1681 CG GLU A 201 1686 1257 1682 82 -31 -138 C -ATOM 1682 CD GLU A 201 2.589 -46.095 20.760 1.00 16.55 C -ANISOU 1682 CD GLU A 201 2235 1850 2202 67 -23 -132 C -ATOM 1683 OE1 GLU A 201 1.789 -45.257 21.212 1.00 13.16 O -ANISOU 1683 OE1 GLU A 201 1828 1427 1746 82 -23 -101 O -ATOM 1684 OE2 GLU A 201 2.846 -46.196 19.545 1.00 13.80 O -ANISOU 1684 OE2 GLU A 201 1861 1528 1854 41 -13 -156 O -ATOM 1685 N LEU A 202 3.943 -46.123 24.803 1.00 14.58 N -ANISOU 1685 N LEU A 202 2066 1503 1970 142 -77 -88 N -ATOM 1686 CA LEU A 202 5.064 -45.991 25.714 1.00 14.40 C -ANISOU 1686 CA LEU A 202 2059 1456 1955 151 -105 -86 C -ATOM 1687 C LEU A 202 4.571 -45.641 27.113 1.00 13.86 C -ANISOU 1687 C LEU A 202 2035 1373 1858 178 -116 -58 C -ATOM 1688 O LEU A 202 5.108 -46.120 28.111 1.00 14.22 O -ANISOU 1688 O LEU A 202 2091 1400 1912 190 -135 -49 O -ATOM 1689 CB LEU A 202 6.035 -44.909 25.226 1.00 14.75 C -ANISOU 1689 CB LEU A 202 2103 1506 1995 137 -122 -97 C -ATOM 1690 CG LEU A 202 6.452 -44.972 23.756 1.00 11.63 C -ANISOU 1690 CG LEU A 202 1670 1131 1619 112 -107 -122 C -ATOM 1691 CD1 LEU A 202 7.373 -43.803 23.446 1.00 13.79 C -ANISOU 1691 CD1 LEU A 202 1945 1407 1887 103 -124 -126 C -ATOM 1692 CD2 LEU A 202 7.136 -46.309 23.442 1.00 14.66 C -ANISOU 1692 CD2 LEU A 202 2018 1504 2048 103 -100 -140 C -ATOM 1693 N LEU A 203 3.552 -44.789 27.180 1.00 10.65 N -ANISOU 1693 N LEU A 203 1654 976 1415 187 -102 -44 N -ATOM 1694 CA LEU A 203 3.105 -44.252 28.458 1.00 11.46 C -ANISOU 1694 CA LEU A 203 1806 1065 1485 212 -107 -22 C -ATOM 1695 C LEU A 203 2.335 -45.294 29.267 1.00 14.34 C -ANISOU 1695 C LEU A 203 2175 1421 1853 233 -95 0 C -ATOM 1696 O LEU A 203 2.190 -45.172 30.482 1.00 13.07 O -ANISOU 1696 O LEU A 203 2052 1246 1668 256 -102 18 O -ATOM 1697 CB LEU A 203 2.260 -42.997 28.224 1.00 10.73 C -ANISOU 1697 CB LEU A 203 1737 982 1359 217 -90 -11 C -ATOM 1698 CG LEU A 203 3.019 -41.862 27.516 1.00 16.30 C -ANISOU 1698 CG LEU A 203 2439 1693 2061 199 -101 -27 C -ATOM 1699 CD1 LEU A 203 2.074 -40.750 27.109 1.00 15.99 C -ANISOU 1699 CD1 LEU A 203 2413 1665 2000 203 -76 -12 C -ATOM 1700 CD2 LEU A 203 4.158 -41.327 28.381 1.00 16.19 C -ANISOU 1700 CD2 LEU A 203 2455 1657 2040 199 -135 -37 C -ATOM 1701 N VAL A 204 1.835 -46.319 28.589 1.00 18.39 N -ANISOU 1701 N VAL A 204 2650 1942 2396 225 -76 -2 N -ATOM 1702 CA VAL A 204 1.150 -47.409 29.271 1.00 16.36 C -ANISOU 1702 CA VAL A 204 2389 1673 2152 243 -63 19 C -ATOM 1703 C VAL A 204 2.034 -48.646 29.348 1.00 18.17 C -ANISOU 1703 C VAL A 204 2588 1888 2427 237 -73 9 C -ATOM 1704 O VAL A 204 1.582 -49.712 29.772 1.00 17.81 O -ANISOU 1704 O VAL A 204 2530 1832 2405 249 -61 24 O -ATOM 1705 CB VAL A 204 -0.215 -47.756 28.610 1.00 10.98 C -ANISOU 1705 CB VAL A 204 1687 1007 1476 240 -32 29 C -ATOM 1706 CG1 VAL A 204 -1.130 -46.542 28.617 1.00 16.54 C -ANISOU 1706 CG1 VAL A 204 2420 1724 2142 250 -18 48 C -ATOM 1707 CG2 VAL A 204 -0.022 -48.272 27.191 1.00 12.50 C -ANISOU 1707 CG2 VAL A 204 1834 1216 1699 207 -25 -1 C -ATOM 1708 N ASP A 205 3.294 -48.494 28.938 1.00 14.79 N -ANISOU 1708 N ASP A 205 2145 1458 2015 220 -94 -14 N -ATOM 1709 CA ASP A 205 4.294 -49.546 29.095 1.00 15.82 C -ANISOU 1709 CA ASP A 205 2248 1572 2192 217 -104 -19 C -ATOM 1710 C ASP A 205 4.026 -50.758 28.190 1.00 22.82 C -ANISOU 1710 C ASP A 205 3089 2455 3125 202 -76 -37 C -ATOM 1711 O ASP A 205 4.309 -51.892 28.570 1.00 25.55 O -ANISOU 1711 O ASP A 205 3414 2781 3513 209 -72 -29 O -ATOM 1712 CB ASP A 205 4.357 -49.970 30.573 1.00 24.18 C -ANISOU 1712 CB ASP A 205 3328 2613 3245 243 -119 14 C -ATOM 1713 CG ASP A 205 5.636 -50.713 30.931 1.00 37.88 C -ANISOU 1713 CG ASP A 205 5039 4333 5022 242 -139 18 C -ATOM 1714 OD1 ASP A 205 6.628 -50.624 30.171 1.00 36.53 O -ANISOU 1714 OD1 ASP A 205 4842 4160 4876 221 -148 -5 O -ATOM 1715 OD2 ASP A 205 5.647 -51.383 31.992 1.00 36.60 O -ANISOU 1715 OD2 ASP A 205 4882 4159 4867 262 -147 48 O -ATOM 1716 N TYR A 206 3.491 -50.516 26.993 1.00 14.96 N -ANISOU 1716 N TYR A 206 2079 1480 2124 181 -58 -59 N -ATOM 1717 CA TYR A 206 3.277 -51.581 26.007 1.00 14.72 C -ANISOU 1717 CA TYR A 206 2011 1450 2134 161 -33 -85 C -ATOM 1718 C TYR A 206 4.460 -51.685 25.057 1.00 14.68 C -ANISOU 1718 C TYR A 206 1978 1444 2154 138 -32 -119 C -ATOM 1719 O TYR A 206 4.713 -50.761 24.293 1.00 15.31 O -ANISOU 1719 O TYR A 206 2061 1546 2209 123 -37 -135 O -ATOM 1720 CB TYR A 206 2.013 -51.320 25.182 1.00 15.52 C -ANISOU 1720 CB TYR A 206 2108 1577 2210 146 -14 -90 C -ATOM 1721 CG TYR A 206 1.659 -52.485 24.279 1.00 14.67 C -ANISOU 1721 CG TYR A 206 1965 1469 2139 122 10 -117 C -ATOM 1722 CD1 TYR A 206 1.137 -53.666 24.806 1.00 18.65 C -ANISOU 1722 CD1 TYR A 206 2457 1950 2680 132 24 -105 C -ATOM 1723 CD2 TYR A 206 1.854 -52.412 22.905 1.00 15.70 C -ANISOU 1723 CD2 TYR A 206 2075 1622 2267 89 20 -154 C -ATOM 1724 CE1 TYR A 206 0.810 -54.738 23.983 1.00 16.60 C -ANISOU 1724 CE1 TYR A 206 2166 1685 2456 107 47 -134 C -ATOM 1725 CE2 TYR A 206 1.542 -53.477 22.078 1.00 13.49 C -ANISOU 1725 CE2 TYR A 206 1767 1342 2018 64 42 -185 C -ATOM 1726 CZ TYR A 206 1.013 -54.634 22.621 1.00 15.11 C -ANISOU 1726 CZ TYR A 206 1962 1520 2261 72 55 -176 C -ATOM 1727 OH TYR A 206 0.697 -55.688 21.793 1.00 16.04 O -ANISOU 1727 OH TYR A 206 2052 1632 2410 44 78 -210 O -ATOM 1728 N GLN A 207 5.159 -52.820 25.077 1.00 15.08 N -ANISOU 1728 N GLN A 207 2001 1469 2259 136 -23 -129 N -ATOM 1729 CA GLN A 207 6.453 -52.926 24.396 1.00 18.49 C -ANISOU 1729 CA GLN A 207 2408 1894 2722 121 -22 -155 C -ATOM 1730 C GLN A 207 6.423 -53.393 22.943 1.00 18.69 C -ANISOU 1730 C GLN A 207 2407 1930 2764 91 9 -199 C -ATOM 1731 O GLN A 207 7.420 -53.232 22.225 1.00 16.10 O -ANISOU 1731 O GLN A 207 2063 1603 2451 78 13 -221 O -ATOM 1732 CB GLN A 207 7.391 -53.850 25.183 1.00 16.62 C -ANISOU 1732 CB GLN A 207 2154 1622 2540 136 -27 -139 C -ATOM 1733 CG GLN A 207 7.692 -53.387 26.591 1.00 18.90 C -ANISOU 1733 CG GLN A 207 2468 1904 2810 162 -62 -97 C -ATOM 1734 CD GLN A 207 8.671 -54.310 27.280 1.00 24.07 C -ANISOU 1734 CD GLN A 207 3097 2527 3520 174 -68 -76 C -ATOM 1735 OE1 GLN A 207 8.278 -55.136 28.097 1.00 26.32 O -ANISOU 1735 OE1 GLN A 207 3379 2795 3825 192 -63 -49 O -ATOM 1736 NE2 GLN A 207 9.955 -54.196 26.928 1.00 20.65 N -ANISOU 1736 NE2 GLN A 207 2642 2087 3116 165 -77 -84 N -ATOM 1737 N MET A 208 5.316 -53.989 22.503 1.00 15.20 N -ANISOU 1737 N MET A 208 1960 1496 2321 79 30 -212 N -ATOM 1738 CA MET A 208 5.269 -54.565 21.153 1.00 13.79 C -ANISOU 1738 CA MET A 208 1757 1326 2156 47 60 -258 C -ATOM 1739 C MET A 208 4.736 -53.552 20.140 1.00 14.19 C -ANISOU 1739 C MET A 208 1817 1425 2151 25 57 -272 C -ATOM 1740 O MET A 208 3.758 -53.813 19.417 1.00 15.06 O -ANISOU 1740 O MET A 208 1922 1557 2245 2 71 -289 O -ATOM 1741 CB MET A 208 4.452 -55.867 21.152 1.00 15.06 C -ANISOU 1741 CB MET A 208 1903 1467 2353 40 84 -269 C -ATOM 1742 CG MET A 208 4.778 -56.815 20.007 1.00 18.48 C -ANISOU 1742 CG MET A 208 2310 1891 2821 10 118 -321 C -ATOM 1743 SD MET A 208 3.933 -58.428 20.086 1.00 20.80 S -ANISOU 1743 SD MET A 208 2584 2150 3168 1 148 -337 S -ATOM 1744 CE MET A 208 4.650 -59.091 21.589 1.00 36.70 C -ANISOU 1744 CE MET A 208 4590 4111 5243 43 143 -292 C -ATOM 1745 N TYR A 209 5.378 -52.386 20.102 1.00 14.68 N -ANISOU 1745 N TYR A 209 1890 1502 2185 30 38 -262 N -ATOM 1746 CA TYR A 209 4.928 -51.287 19.249 1.00 15.47 C -ANISOU 1746 CA TYR A 209 1998 1647 2233 14 34 -265 C -ATOM 1747 C TYR A 209 5.668 -51.312 17.920 1.00 16.22 C -ANISOU 1747 C TYR A 209 2072 1760 2331 -14 52 -304 C -ATOM 1748 O TYR A 209 6.423 -52.245 17.657 1.00 13.40 O -ANISOU 1748 O TYR A 209 1696 1378 2017 -20 72 -331 O -ATOM 1749 CB TYR A 209 5.095 -49.934 19.959 1.00 11.07 C -ANISOU 1749 CB TYR A 209 1466 1095 1644 34 6 -230 C -ATOM 1750 CG TYR A 209 6.518 -49.567 20.373 1.00 13.55 C -ANISOU 1750 CG TYR A 209 1781 1388 1980 45 -10 -226 C -ATOM 1751 CD1 TYR A 209 7.403 -49.025 19.461 1.00 14.76 C -ANISOU 1751 CD1 TYR A 209 1920 1556 2132 30 -7 -244 C -ATOM 1752 CD2 TYR A 209 6.945 -49.725 21.692 1.00 10.71 C -ANISOU 1752 CD2 TYR A 209 1434 996 1638 71 -31 -201 C -ATOM 1753 CE1 TYR A 209 8.693 -48.669 19.829 1.00 18.96 C -ANISOU 1753 CE1 TYR A 209 2448 2067 2687 39 -24 -237 C -ATOM 1754 CE2 TYR A 209 8.238 -49.362 22.079 1.00 16.38 C -ANISOU 1754 CE2 TYR A 209 2150 1697 2375 77 -52 -195 C -ATOM 1755 CZ TYR A 209 9.109 -48.843 21.139 1.00 17.04 C -ANISOU 1755 CZ TYR A 209 2217 1793 2463 61 -48 -213 C -ATOM 1756 OH TYR A 209 10.390 -48.479 21.503 1.00 15.81 O -ANISOU 1756 OH TYR A 209 2056 1620 2331 66 -70 -203 O -ATOM 1757 N ASP A 210 5.446 -50.303 17.078 1.00 12.80 N -ANISOU 1757 N ASP A 210 1641 1368 1853 -29 49 -304 N -ATOM 1758 CA ASP A 210 5.954 -50.345 15.701 1.00 10.01 C -ANISOU 1758 CA ASP A 210 1270 1042 1493 -58 70 -341 C -ATOM 1759 C ASP A 210 6.120 -48.956 15.095 1.00 11.19 C -ANISOU 1759 C ASP A 210 1422 1229 1600 -63 60 -326 C -ATOM 1760 O ASP A 210 6.145 -47.958 15.816 1.00 12.61 O -ANISOU 1760 O ASP A 210 1619 1406 1768 -42 37 -291 O -ATOM 1761 CB ASP A 210 5.084 -51.258 14.813 1.00 10.75 C -ANISOU 1761 CB ASP A 210 1352 1155 1577 -89 93 -375 C -ATOM 1762 CG ASP A 210 3.615 -50.829 14.764 1.00 15.03 C -ANISOU 1762 CG ASP A 210 1902 1732 2075 -97 81 -351 C -ATOM 1763 OD1 ASP A 210 3.333 -49.779 14.153 1.00 17.79 O -ANISOU 1763 OD1 ASP A 210 2253 2126 2381 -106 73 -336 O -ATOM 1764 OD2 ASP A 210 2.731 -51.551 15.298 1.00 15.69 O -ANISOU 1764 OD2 ASP A 210 1988 1802 2173 -94 81 -344 O -ATOM 1765 N TYR A 211 6.242 -48.885 13.771 1.00 10.85 N -ANISOU 1765 N TYR A 211 1364 1223 1535 -91 78 -353 N -ATOM 1766 CA TYR A 211 6.354 -47.607 13.075 1.00 10.39 C -ANISOU 1766 CA TYR A 211 1304 1206 1437 -97 72 -337 C -ATOM 1767 C TYR A 211 5.315 -46.577 13.500 1.00 14.59 C -ANISOU 1767 C TYR A 211 1850 1758 1933 -86 51 -292 C -ATOM 1768 O TYR A 211 5.556 -45.372 13.441 1.00 10.36 O -ANISOU 1768 O TYR A 211 1319 1237 1381 -78 41 -266 O -ATOM 1769 CB TYR A 211 6.202 -47.816 11.562 1.00 11.86 C -ANISOU 1769 CB TYR A 211 1474 1440 1593 -133 96 -369 C -ATOM 1770 CG TYR A 211 6.921 -49.015 10.988 1.00 9.21 C -ANISOU 1770 CG TYR A 211 1126 1086 1287 -149 126 -421 C -ATOM 1771 CD1 TYR A 211 8.311 -49.018 10.846 1.00 13.55 C -ANISOU 1771 CD1 TYR A 211 1665 1612 1870 -140 140 -433 C -ATOM 1772 CD2 TYR A 211 6.211 -50.139 10.560 1.00 11.36 C -ANISOU 1772 CD2 TYR A 211 1396 1364 1557 -174 144 -457 C -ATOM 1773 CE1 TYR A 211 8.967 -50.106 10.313 1.00 15.78 C -ANISOU 1773 CE1 TYR A 211 1937 1875 2184 -152 175 -479 C -ATOM 1774 CE2 TYR A 211 6.865 -51.238 10.017 1.00 14.27 C -ANISOU 1774 CE2 TYR A 211 1755 1711 1955 -189 177 -508 C -ATOM 1775 CZ TYR A 211 8.247 -51.209 9.892 1.00 13.96 C -ANISOU 1775 CZ TYR A 211 1707 1648 1950 -177 195 -518 C -ATOM 1776 OH TYR A 211 8.917 -52.279 9.350 1.00 14.37 O -ANISOU 1776 OH TYR A 211 1749 1675 2035 -189 234 -567 O -ATOM 1777 N SER A 212 4.140 -47.054 13.888 1.00 11.20 N -ANISOU 1777 N SER A 212 1428 1331 1496 -87 49 -283 N -ATOM 1778 CA SER A 212 3.035 -46.160 14.224 1.00 12.21 C -ANISOU 1778 CA SER A 212 1567 1479 1592 -77 36 -240 C -ATOM 1779 C SER A 212 3.364 -45.212 15.393 1.00 8.63 C -ANISOU 1779 C SER A 212 1138 995 1147 -43 18 -205 C -ATOM 1780 O SER A 212 2.763 -44.149 15.512 1.00 11.13 O -ANISOU 1780 O SER A 212 1464 1327 1438 -33 11 -170 O -ATOM 1781 CB SER A 212 1.762 -46.964 14.481 1.00 12.26 C -ANISOU 1781 CB SER A 212 1574 1488 1597 -83 38 -235 C -ATOM 1782 OG SER A 212 1.961 -47.941 15.491 1.00 12.60 O -ANISOU 1782 OG SER A 212 1626 1482 1680 -65 38 -245 O -ATOM 1783 N LEU A 213 4.334 -45.573 16.233 1.00 11.37 N -ANISOU 1783 N LEU A 213 1494 1296 1529 -25 10 -215 N -ATOM 1784 CA LEU A 213 4.826 -44.625 17.252 1.00 10.76 C -ANISOU 1784 CA LEU A 213 1441 1192 1455 2 -11 -188 C -ATOM 1785 C LEU A 213 5.200 -43.272 16.632 1.00 14.81 C -ANISOU 1785 C LEU A 213 1951 1728 1948 -3 -14 -175 C -ATOM 1786 O LEU A 213 4.847 -42.213 17.162 1.00 11.80 O -ANISOU 1786 O LEU A 213 1590 1343 1551 12 -23 -144 O -ATOM 1787 CB LEU A 213 6.051 -45.190 17.975 1.00 11.77 C -ANISOU 1787 CB LEU A 213 1571 1278 1625 13 -22 -202 C -ATOM 1788 CG LEU A 213 6.723 -44.207 18.928 1.00 15.92 C -ANISOU 1788 CG LEU A 213 2119 1779 2152 33 -47 -180 C -ATOM 1789 CD1 LEU A 213 5.835 -43.946 20.149 1.00 17.71 C -ANISOU 1789 CD1 LEU A 213 2379 1988 2360 56 -58 -153 C -ATOM 1790 CD2 LEU A 213 8.092 -44.747 19.354 1.00 14.74 C -ANISOU 1790 CD2 LEU A 213 1960 1596 2044 37 -59 -193 C -ATOM 1791 N ASP A 214 5.927 -43.309 15.515 1.00 12.40 N -ANISOU 1791 N ASP A 214 1620 1445 1646 -24 -3 -196 N -ATOM 1792 CA ASP A 214 6.403 -42.087 14.861 1.00 13.58 C -ANISOU 1792 CA ASP A 214 1761 1616 1782 -29 -4 -182 C -ATOM 1793 C ASP A 214 5.228 -41.224 14.408 1.00 11.99 C -ANISOU 1793 C ASP A 214 1560 1453 1541 -33 2 -151 C -ATOM 1794 O ASP A 214 5.343 -40.003 14.304 1.00 11.26 O -ANISOU 1794 O ASP A 214 1470 1368 1441 -27 -2 -124 O -ATOM 1795 CB ASP A 214 7.278 -42.419 13.647 1.00 13.08 C -ANISOU 1795 CB ASP A 214 1670 1575 1726 -51 14 -211 C -ATOM 1796 CG ASP A 214 8.605 -43.068 14.031 1.00 15.36 C -ANISOU 1796 CG ASP A 214 1953 1823 2060 -45 11 -233 C -ATOM 1797 OD1 ASP A 214 9.071 -42.892 15.179 1.00 14.00 O -ANISOU 1797 OD1 ASP A 214 1797 1610 1912 -25 -11 -220 O -ATOM 1798 OD2 ASP A 214 9.184 -43.755 13.163 1.00 14.88 O -ANISOU 1798 OD2 ASP A 214 1871 1773 2012 -61 33 -263 O -ATOM 1799 N MET A 215 4.105 -41.866 14.120 1.00 11.39 N -ANISOU 1799 N MET A 215 1479 1402 1447 -44 11 -151 N -ATOM 1800 CA MET A 215 2.942 -41.139 13.630 1.00 10.59 C -ANISOU 1800 CA MET A 215 1371 1341 1311 -49 16 -116 C -ATOM 1801 C MET A 215 2.242 -40.373 14.764 1.00 11.69 C -ANISOU 1801 C MET A 215 1537 1454 1449 -20 9 -77 C -ATOM 1802 O MET A 215 1.737 -39.267 14.552 1.00 13.02 O -ANISOU 1802 O MET A 215 1704 1641 1602 -15 13 -40 O -ATOM 1803 CB MET A 215 1.988 -42.084 12.888 1.00 11.39 C -ANISOU 1803 CB MET A 215 1454 1481 1392 -76 26 -129 C -ATOM 1804 CG MET A 215 2.641 -42.790 11.694 1.00 16.78 C -ANISOU 1804 CG MET A 215 2114 2191 2068 -107 37 -172 C -ATOM 1805 SD MET A 215 3.507 -41.675 10.551 1.00 14.79 S -ANISOU 1805 SD MET A 215 1844 1978 1798 -118 45 -164 S -ATOM 1806 CE MET A 215 2.120 -40.845 9.765 1.00 15.01 C -ANISOU 1806 CE MET A 215 1854 2071 1778 -133 45 -115 C -ATOM 1807 N TRP A 216 2.221 -40.948 15.967 1.00 11.33 N -ANISOU 1807 N TRP A 216 1517 1366 1424 0 1 -83 N -ATOM 1808 CA TRP A 216 1.779 -40.193 17.130 1.00 11.21 C -ANISOU 1808 CA TRP A 216 1533 1319 1407 29 -4 -52 C -ATOM 1809 C TRP A 216 2.648 -38.945 17.312 1.00 12.59 C -ANISOU 1809 C TRP A 216 1720 1476 1586 39 -12 -43 C -ATOM 1810 O TRP A 216 2.144 -37.830 17.439 1.00 14.33 O -ANISOU 1810 O TRP A 216 1951 1699 1796 51 -5 -11 O -ATOM 1811 CB TRP A 216 1.812 -41.028 18.418 1.00 6.73 C -ANISOU 1811 CB TRP A 216 992 709 857 49 -13 -62 C -ATOM 1812 CG TRP A 216 1.405 -40.200 19.609 1.00 13.29 C -ANISOU 1812 CG TRP A 216 1860 1509 1679 79 -16 -33 C -ATOM 1813 CD1 TRP A 216 2.226 -39.447 20.407 1.00 9.88 C -ANISOU 1813 CD1 TRP A 216 1457 1044 1252 94 -30 -34 C -ATOM 1814 CD2 TRP A 216 0.062 -39.969 20.087 1.00 13.28 C -ANISOU 1814 CD2 TRP A 216 1873 1509 1663 96 -1 2 C -ATOM 1815 NE1 TRP A 216 1.479 -38.794 21.368 1.00 14.93 N -ANISOU 1815 NE1 TRP A 216 2131 1663 1877 119 -24 -7 N -ATOM 1816 CE2 TRP A 216 0.153 -39.096 21.189 1.00 13.99 C -ANISOU 1816 CE2 TRP A 216 2004 1564 1748 123 -4 17 C -ATOM 1817 CE3 TRP A 216 -1.197 -40.434 19.701 1.00 11.54 C -ANISOU 1817 CE3 TRP A 216 1634 1316 1434 91 14 23 C -ATOM 1818 CZ2 TRP A 216 -0.972 -38.680 21.914 1.00 14.73 C -ANISOU 1818 CZ2 TRP A 216 2122 1647 1829 147 14 52 C -ATOM 1819 CZ3 TRP A 216 -2.320 -40.005 20.415 1.00 12.21 C -ANISOU 1819 CZ3 TRP A 216 1739 1391 1510 115 29 62 C -ATOM 1820 CH2 TRP A 216 -2.195 -39.146 21.511 1.00 16.29 C -ANISOU 1820 CH2 TRP A 216 2298 1870 2022 145 31 76 C -ATOM 1821 N SER A 217 3.966 -39.147 17.330 1.00 10.21 N -ANISOU 1821 N SER A 217 1417 1157 1307 34 -25 -71 N -ATOM 1822 CA SER A 217 4.913 -38.038 17.478 1.00 8.02 C -ANISOU 1822 CA SER A 217 1147 861 1040 39 -36 -66 C -ATOM 1823 C SER A 217 4.679 -36.954 16.437 1.00 10.36 C -ANISOU 1823 C SER A 217 1423 1192 1322 29 -22 -42 C -ATOM 1824 O SER A 217 4.692 -35.769 16.758 1.00 10.59 O -ANISOU 1824 O SER A 217 1466 1205 1352 40 -22 -19 O -ATOM 1825 CB SER A 217 6.350 -38.561 17.383 1.00 7.89 C -ANISOU 1825 CB SER A 217 1118 829 1052 29 -49 -97 C -ATOM 1826 OG SER A 217 6.576 -39.521 18.396 1.00 12.32 O -ANISOU 1826 OG SER A 217 1695 1357 1628 40 -63 -112 O -ATOM 1827 N LEU A 218 4.455 -37.361 15.189 1.00 10.19 N -ANISOU 1827 N LEU A 218 1367 1218 1287 7 -8 -47 N -ATOM 1828 CA LEU A 218 4.193 -36.403 14.132 1.00 9.10 C -ANISOU 1828 CA LEU A 218 1204 1120 1132 -4 6 -19 C -ATOM 1829 C LEU A 218 2.903 -35.642 14.397 1.00 12.87 C -ANISOU 1829 C LEU A 218 1691 1606 1593 10 16 26 C -ATOM 1830 O LEU A 218 2.821 -34.441 14.126 1.00 12.97 O -ANISOU 1830 O LEU A 218 1698 1625 1607 15 24 59 O -ATOM 1831 CB LEU A 218 4.110 -37.091 12.767 1.00 11.20 C -ANISOU 1831 CB LEU A 218 1436 1442 1379 -32 17 -33 C -ATOM 1832 CG LEU A 218 3.924 -36.171 11.554 1.00 13.16 C -ANISOU 1832 CG LEU A 218 1654 1741 1606 -46 31 -3 C -ATOM 1833 CD1 LEU A 218 5.199 -35.411 11.225 1.00 13.89 C -ANISOU 1833 CD1 LEU A 218 1736 1823 1719 -46 30 -4 C -ATOM 1834 CD2 LEU A 218 3.467 -36.973 10.342 1.00 11.86 C -ANISOU 1834 CD2 LEU A 218 1462 1636 1409 -77 41 -16 C -ATOM 1835 N GLY A 219 1.898 -36.337 14.926 1.00 10.33 N -ANISOU 1835 N GLY A 219 1381 1282 1263 17 18 30 N -ATOM 1836 CA GLY A 219 0.635 -35.690 15.243 1.00 10.36 C -ANISOU 1836 CA GLY A 219 1392 1288 1254 32 31 75 C -ATOM 1837 C GLY A 219 0.850 -34.643 16.323 1.00 16.41 C -ANISOU 1837 C GLY A 219 2195 2004 2036 60 32 90 C -ATOM 1838 O GLY A 219 0.261 -33.563 16.273 1.00 15.04 O -ANISOU 1838 O GLY A 219 2021 1832 1861 72 48 130 O -ATOM 1839 N CYS A 220 1.695 -34.955 17.305 1.00 14.35 N -ANISOU 1839 N CYS A 220 1965 1698 1790 70 14 57 N -ATOM 1840 CA CYS A 220 2.011 -33.977 18.352 1.00 14.61 C -ANISOU 1840 CA CYS A 220 2037 1682 1832 92 11 63 C -ATOM 1841 C CYS A 220 2.660 -32.726 17.759 1.00 17.41 C -ANISOU 1841 C CYS A 220 2379 2038 2199 86 15 76 C -ATOM 1842 O CYS A 220 2.312 -31.603 18.148 1.00 12.24 O -ANISOU 1842 O CYS A 220 1742 1360 1548 101 28 102 O -ATOM 1843 CB CYS A 220 2.921 -34.577 19.430 1.00 12.75 C -ANISOU 1843 CB CYS A 220 1832 1405 1607 98 -14 27 C -ATOM 1844 SG CYS A 220 2.153 -35.883 20.408 1.00 14.03 S -ANISOU 1844 SG CYS A 220 2016 1555 1759 112 -16 20 S -ATOM 1845 N MET A 221 3.586 -32.925 16.816 1.00 11.13 N -ANISOU 1845 N MET A 221 1551 1267 1412 64 6 59 N -ATOM 1846 CA MET A 221 4.206 -31.805 16.102 1.00 12.81 C -ANISOU 1846 CA MET A 221 1743 1486 1638 57 11 75 C -ATOM 1847 C MET A 221 3.153 -30.992 15.338 1.00 15.26 C -ANISOU 1847 C MET A 221 2030 1830 1936 59 38 125 C -ATOM 1848 O MET A 221 3.132 -29.764 15.418 1.00 14.88 O -ANISOU 1848 O MET A 221 1986 1763 1903 69 50 152 O -ATOM 1849 CB MET A 221 5.305 -32.292 15.145 1.00 11.62 C -ANISOU 1849 CB MET A 221 1559 1360 1496 34 2 51 C -ATOM 1850 CG MET A 221 6.523 -32.873 15.863 1.00 12.35 C -ANISOU 1850 CG MET A 221 1668 1414 1611 33 -24 12 C -ATOM 1851 SD MET A 221 7.872 -33.232 14.701 1.00 18.58 S -ANISOU 1851 SD MET A 221 2414 2228 2419 11 -27 -9 S -ATOM 1852 CE MET A 221 8.013 -31.674 13.847 1.00 10.91 C -ANISOU 1852 CE MET A 221 1419 1273 1455 8 -11 30 C -ATOM 1853 N LEU A 222 2.299 -31.678 14.586 1.00 13.02 N -ANISOU 1853 N LEU A 222 1720 1598 1630 48 47 137 N -ATOM 1854 CA LEU A 222 1.253 -31.001 13.836 1.00 10.60 C -ANISOU 1854 CA LEU A 222 1386 1330 1310 47 70 190 C -ATOM 1855 C LEU A 222 0.375 -30.150 14.750 1.00 11.17 C -ANISOU 1855 C LEU A 222 1486 1366 1393 76 88 225 C -ATOM 1856 O LEU A 222 0.137 -28.973 14.469 1.00 14.19 O -ANISOU 1856 O LEU A 222 1857 1747 1788 84 107 267 O -ATOM 1857 CB LEU A 222 0.412 -31.998 13.039 1.00 13.21 C -ANISOU 1857 CB LEU A 222 1688 1719 1611 28 71 194 C -ATOM 1858 CG LEU A 222 -0.696 -31.382 12.184 1.00 10.03 C -ANISOU 1858 CG LEU A 222 1251 1368 1194 23 90 254 C -ATOM 1859 CD1 LEU A 222 -0.140 -30.508 11.056 1.00 12.56 C -ANISOU 1859 CD1 LEU A 222 1535 1723 1513 10 97 278 C -ATOM 1860 CD2 LEU A 222 -1.555 -32.497 11.622 1.00 12.24 C -ANISOU 1860 CD2 LEU A 222 1509 1698 1444 1 84 251 C -ATOM 1861 N ALA A 223 -0.100 -30.737 15.845 1.00 10.39 N -ANISOU 1861 N ALA A 223 1423 1235 1290 92 85 210 N -ATOM 1862 CA ALA A 223 -0.955 -30.004 16.772 1.00 11.50 C -ANISOU 1862 CA ALA A 223 1594 1337 1437 121 107 241 C -ATOM 1863 C ALA A 223 -0.255 -28.740 17.268 1.00 17.44 C -ANISOU 1863 C ALA A 223 2372 2040 2213 133 113 240 C -ATOM 1864 O ALA A 223 -0.869 -27.681 17.331 1.00 12.42 O -ANISOU 1864 O ALA A 223 1739 1391 1591 149 141 281 O -ATOM 1865 CB ALA A 223 -1.359 -30.880 17.938 1.00 11.81 C -ANISOU 1865 CB ALA A 223 1672 1347 1468 136 101 219 C -ATOM 1866 N SER A 224 1.032 -28.847 17.610 1.00 15.01 N -ANISOU 1866 N SER A 224 2082 1705 1915 124 87 195 N -ATOM 1867 CA SER A 224 1.777 -27.685 18.103 1.00 11.85 C -ANISOU 1867 CA SER A 224 1707 1256 1539 131 87 190 C -ATOM 1868 C SER A 224 1.906 -26.601 17.028 1.00 14.62 C -ANISOU 1868 C SER A 224 2017 1627 1909 124 105 227 C -ATOM 1869 O SER A 224 1.892 -25.410 17.334 1.00 19.99 O -ANISOU 1869 O SER A 224 2713 2271 2613 136 124 246 O -ATOM 1870 CB SER A 224 3.168 -28.090 18.637 1.00 14.67 C -ANISOU 1870 CB SER A 224 2085 1585 1904 119 50 137 C -ATOM 1871 OG SER A 224 4.081 -28.342 17.583 1.00 15.88 O -ANISOU 1871 OG SER A 224 2195 1771 2066 96 35 128 O -ATOM 1872 N MET A 225 2.008 -27.004 15.767 1.00 14.19 N -ANISOU 1872 N MET A 225 1905 1453 2035 42 41 352 N -ATOM 1873 CA MET A 225 2.169 -26.027 14.695 1.00 14.12 C -ANISOU 1873 CA MET A 225 1863 1430 2072 35 49 392 C -ATOM 1874 C MET A 225 0.835 -25.351 14.319 1.00 15.20 C -ANISOU 1874 C MET A 225 2014 1593 2167 58 70 385 C -ATOM 1875 O MET A 225 0.747 -24.119 14.290 1.00 17.67 O -ANISOU 1875 O MET A 225 2331 1871 2513 66 40 391 O -ATOM 1876 CB MET A 225 2.801 -26.675 13.457 1.00 14.89 C -ANISOU 1876 CB MET A 225 1910 1555 2193 10 95 437 C -ATOM 1877 CG MET A 225 4.240 -27.172 13.649 1.00 22.12 C -ANISOU 1877 CG MET A 225 2804 2439 3162 -15 74 454 C -ATOM 1878 SD MET A 225 4.731 -28.223 12.259 1.00 33.16 S -ANISOU 1878 SD MET A 225 4149 3886 4564 -39 138 498 S -ATOM 1879 CE MET A 225 6.376 -28.710 12.724 1.00 48.15 C -ANISOU 1879 CE MET A 225 6030 5742 6524 -65 103 510 C -ATOM 1880 N ILE A 226 -0.197 -26.141 14.042 1.00 15.33 N -ANISOU 1880 N ILE A 226 2040 1672 2113 67 120 372 N -ATOM 1881 CA ILE A 226 -1.472 -25.542 13.606 1.00 16.81 C -ANISOU 1881 CA ILE A 226 2238 1888 2259 88 144 367 C -ATOM 1882 C ILE A 226 -2.176 -24.755 14.713 1.00 16.32 C -ANISOU 1882 C ILE A 226 2224 1802 2175 116 100 326 C -ATOM 1883 O ILE A 226 -2.868 -23.782 14.427 1.00 20.69 O -ANISOU 1883 O ILE A 226 2784 2352 2725 131 98 328 O -ATOM 1884 CB ILE A 226 -2.440 -26.548 12.927 1.00 14.15 C -ANISOU 1884 CB ILE A 226 1897 1626 1853 92 211 366 C -ATOM 1885 CG1 ILE A 226 -2.939 -27.603 13.922 1.00 14.27 C -ANISOU 1885 CG1 ILE A 226 1948 1669 1806 102 214 324 C -ATOM 1886 CG2 ILE A 226 -1.771 -27.188 11.710 1.00 15.37 C -ANISOU 1886 CG2 ILE A 226 2002 1805 2033 67 255 409 C -ATOM 1887 CD1 ILE A 226 -4.035 -28.491 13.350 1.00 13.53 C -ANISOU 1887 CD1 ILE A 226 1854 1647 1641 109 276 319 C -ATOM 1888 N PHE A 227 -1.965 -25.153 15.966 1.00 13.74 N -ANISOU 1888 N PHE A 227 1930 1458 1834 123 65 290 N -ATOM 1889 CA PHE A 227 -2.565 -24.489 17.119 1.00 13.81 C -ANISOU 1889 CA PHE A 227 1985 1443 1820 150 20 248 C -ATOM 1890 C PHE A 227 -1.641 -23.462 17.771 1.00 19.51 C -ANISOU 1890 C PHE A 227 2713 2090 2611 149 -49 247 C -ATOM 1891 O PHE A 227 -2.064 -22.699 18.641 1.00 19.54 O -ANISOU 1891 O PHE A 227 2751 2067 2605 173 -91 216 O -ATOM 1892 CB PHE A 227 -2.999 -25.527 18.162 1.00 11.50 C -ANISOU 1892 CB PHE A 227 1726 1177 1464 162 22 207 C -ATOM 1893 CG PHE A 227 -4.121 -26.426 17.696 1.00 14.02 C -ANISOU 1893 CG PHE A 227 2048 1569 1709 170 83 202 C -ATOM 1894 CD1 PHE A 227 -5.170 -25.916 16.952 1.00 13.31 C -ANISOU 1894 CD1 PHE A 227 1958 1511 1590 183 116 209 C -ATOM 1895 CD2 PHE A 227 -4.119 -27.778 18.001 1.00 12.26 C -ANISOU 1895 CD2 PHE A 227 1830 1382 1446 163 108 189 C -ATOM 1896 CE1 PHE A 227 -6.208 -26.746 16.519 1.00 14.19 C -ANISOU 1896 CE1 PHE A 227 2071 1688 1634 189 172 204 C -ATOM 1897 CE2 PHE A 227 -5.149 -28.608 17.578 1.00 14.53 C -ANISOU 1897 CE2 PHE A 227 2120 1735 1668 169 163 184 C -ATOM 1898 CZ PHE A 227 -6.192 -28.086 16.837 1.00 16.01 C -ANISOU 1898 CZ PHE A 227 2305 1953 1826 182 195 192 C -ATOM 1899 N ARG A 228 -0.370 -23.464 17.385 1.00 20.12 N -ANISOU 1899 N ARG A 228 2755 2133 2755 122 -61 279 N -ATOM 1900 CA ARG A 228 0.575 -22.509 17.958 1.00 20.90 C -ANISOU 1900 CA ARG A 228 2857 2161 2925 119 -127 280 C -ATOM 1901 C ARG A 228 0.688 -22.704 19.461 1.00 17.92 C -ANISOU 1901 C ARG A 228 2522 1758 2530 134 -176 234 C -ATOM 1902 O ARG A 228 0.559 -21.758 20.242 1.00 21.09 O -ANISOU 1902 O ARG A 228 2951 2118 2944 153 -227 210 O -ATOM 1903 CB ARG A 228 0.147 -21.075 17.629 1.00 25.45 C -ANISOU 1903 CB ARG A 228 3434 2709 3526 132 -148 289 C -ATOM 1904 CG ARG A 228 0.269 -20.733 16.157 1.00 33.26 C -ANISOU 1904 CG ARG A 228 4377 3711 4548 115 -109 340 C -ATOM 1905 CD ARG A 228 1.722 -20.488 15.760 1.00 48.78 C -ANISOU 1905 CD ARG A 228 6304 5631 6601 86 -132 380 C -ATOM 1906 NE ARG A 228 1.849 -20.068 14.363 1.00 61.30 N -ANISOU 1906 NE ARG A 228 7845 7227 8220 72 -97 431 N -ATOM 1907 CZ ARG A 228 1.787 -18.804 13.947 1.00 62.73 C -ANISOU 1907 CZ ARG A 228 8015 7375 8443 76 -118 451 C -ATOM 1908 NH1 ARG A 228 1.598 -17.820 14.819 1.00 64.73 N -ANISOU 1908 NH1 ARG A 228 8301 7582 8710 95 -174 423 N -ATOM 1909 NH2 ARG A 228 1.912 -18.521 12.656 1.00 57.33 N -ANISOU 1909 NH2 ARG A 228 7289 6707 7788 62 -83 498 N -ATOM 1910 N LYS A 229 0.925 -23.947 19.862 1.00 17.11 N -ANISOU 1910 N LYS A 229 2423 1681 2397 125 -159 221 N -ATOM 1911 CA LYS A 229 1.167 -24.287 21.251 1.00 20.15 C -ANISOU 1911 CA LYS A 229 2843 2045 2768 136 -202 181 C -ATOM 1912 C LYS A 229 2.247 -25.366 21.267 1.00 22.32 C -ANISOU 1912 C LYS A 229 3096 2320 3065 109 -194 194 C -ATOM 1913 O LYS A 229 1.987 -26.513 20.920 1.00 18.46 O -ANISOU 1913 O LYS A 229 2598 1882 2534 101 -145 197 O -ATOM 1914 CB LYS A 229 -0.117 -24.779 21.925 1.00 20.49 C -ANISOU 1914 CB LYS A 229 2927 2135 2724 164 -184 139 C -ATOM 1915 CG LYS A 229 0.053 -25.099 23.410 1.00 21.54 C -ANISOU 1915 CG LYS A 229 3099 2249 2838 179 -229 95 C -ATOM 1916 CD LYS A 229 -1.237 -25.594 24.052 1.00 23.14 C -ANISOU 1916 CD LYS A 229 3340 2501 2953 208 -210 57 C -ATOM 1917 CE LYS A 229 -1.012 -25.933 25.523 1.00 27.67 C -ANISOU 1917 CE LYS A 229 3949 3055 3508 222 -254 16 C -ATOM 1918 NZ LYS A 229 0.195 -26.799 25.752 1.00 24.08 N -ANISOU 1918 NZ LYS A 229 3478 2584 3088 196 -262 25 N -ATOM 1919 N GLU A 230 3.467 -25.001 21.651 1.00 20.77 N -ANISOU 1919 N GLU A 230 2890 2066 2937 95 -242 202 N -ATOM 1920 CA GLU A 230 4.595 -25.935 21.553 1.00 23.03 C -ANISOU 1920 CA GLU A 230 3150 2347 3252 67 -236 221 C -ATOM 1921 C GLU A 230 5.279 -26.085 22.900 1.00 28.82 C -ANISOU 1921 C GLU A 230 3910 3040 4000 71 -291 189 C -ATOM 1922 O GLU A 230 5.840 -25.118 23.408 1.00 25.95 O -ANISOU 1922 O GLU A 230 3554 2617 3687 74 -348 185 O -ATOM 1923 CB GLU A 230 5.605 -25.452 20.496 1.00 30.20 C -ANISOU 1923 CB GLU A 230 4009 3227 4237 40 -234 272 C -ATOM 1924 CG GLU A 230 6.444 -26.562 19.819 1.00 30.77 C -ANISOU 1924 CG GLU A 230 4043 3322 4325 10 -196 303 C -ATOM 1925 CD GLU A 230 7.524 -27.142 20.731 1.00 30.89 C -ANISOU 1925 CD GLU A 230 4064 3306 4367 -2 -233 291 C -ATOM 1926 OE1 GLU A 230 8.225 -26.363 21.408 1.00 33.35 O -ANISOU 1926 OE1 GLU A 230 4385 3557 4730 -2 -292 284 O -ATOM 1927 OE2 GLU A 230 7.673 -28.380 20.780 1.00 25.65 O -ANISOU 1927 OE2 GLU A 230 3397 2677 3673 -12 -203 286 O -ATOM 1928 N PRO A 231 5.239 -27.302 23.481 1.00 27.48 N -ANISOU 1928 N PRO A 231 3754 2901 3785 70 -275 167 N -ATOM 1929 CA PRO A 231 4.599 -28.478 22.877 1.00 24.36 C -ANISOU 1929 CA PRO A 231 3350 2575 3332 65 -209 172 C -ATOM 1930 C PRO A 231 3.102 -28.487 23.165 1.00 20.10 C -ANISOU 1930 C PRO A 231 2844 2078 2714 95 -188 141 C -ATOM 1931 O PRO A 231 2.646 -27.744 24.036 1.00 20.97 O -ANISOU 1931 O PRO A 231 2990 2166 2812 120 -229 110 O -ATOM 1932 CB PRO A 231 5.279 -29.637 23.603 1.00 19.75 C -ANISOU 1932 CB PRO A 231 2770 1993 2739 54 -215 158 C -ATOM 1933 CG PRO A 231 5.509 -29.097 24.980 1.00 25.62 C -ANISOU 1933 CG PRO A 231 3551 2689 3492 72 -281 121 C -ATOM 1934 CD PRO A 231 5.831 -27.621 24.792 1.00 34.45 C -ANISOU 1934 CD PRO A 231 4663 3753 4672 74 -323 135 C -ATOM 1935 N PHE A 232 2.350 -29.324 22.453 1.00 14.29 N -ANISOU 1935 N PHE A 232 2099 1405 1927 93 -127 149 N -ATOM 1936 CA PHE A 232 0.908 -29.368 22.613 1.00 12.68 C -ANISOU 1936 CA PHE A 232 1924 1247 1649 120 -102 124 C -ATOM 1937 C PHE A 232 0.501 -30.085 23.912 1.00 16.65 C -ANISOU 1937 C PHE A 232 2466 1764 2096 138 -117 79 C -ATOM 1938 O PHE A 232 -0.226 -29.525 24.740 1.00 16.27 O -ANISOU 1938 O PHE A 232 2455 1710 2017 166 -144 47 O -ATOM 1939 CB PHE A 232 0.257 -30.016 21.377 1.00 14.34 C -ANISOU 1939 CB PHE A 232 2107 1517 1824 111 -31 149 C -ATOM 1940 CG PHE A 232 -1.254 -29.980 21.399 1.00 10.54 C -ANISOU 1940 CG PHE A 232 1651 1083 1270 137 -3 127 C -ATOM 1941 CD1 PHE A 232 -1.927 -28.788 21.245 1.00 15.80 C -ANISOU 1941 CD1 PHE A 232 2329 1737 1937 156 -15 125 C -ATOM 1942 CD2 PHE A 232 -1.986 -31.137 21.582 1.00 15.46 C -ANISOU 1942 CD2 PHE A 232 2287 1761 1826 143 36 110 C -ATOM 1943 CE1 PHE A 232 -3.306 -28.746 21.277 1.00 14.01 C -ANISOU 1943 CE1 PHE A 232 2126 1553 1644 181 10 105 C -ATOM 1944 CE2 PHE A 232 -3.377 -31.101 21.613 1.00 21.47 C -ANISOU 1944 CE2 PHE A 232 3072 2566 2521 167 61 91 C -ATOM 1945 CZ PHE A 232 -4.031 -29.904 21.464 1.00 20.03 C -ANISOU 1945 CZ PHE A 232 2900 2371 2338 186 48 88 C -ATOM 1946 N PHE A 233 0.969 -31.318 24.096 1.00 13.15 N -ANISOU 1946 N PHE A 233 2016 1340 1642 122 -100 79 N -ATOM 1947 CA PHE A 233 0.723 -32.031 25.340 1.00 10.24 C -ANISOU 1947 CA PHE A 233 1681 982 1226 137 -116 40 C -ATOM 1948 C PHE A 233 1.920 -31.792 26.249 1.00 17.59 C -ANISOU 1948 C PHE A 233 2619 1854 2210 131 -176 30 C -ATOM 1949 O PHE A 233 2.962 -32.425 26.099 1.00 15.32 O -ANISOU 1949 O PHE A 233 2308 1554 1959 105 -175 47 O -ATOM 1950 CB PHE A 233 0.546 -33.536 25.095 1.00 8.84 C -ANISOU 1950 CB PHE A 233 1494 859 1005 124 -66 43 C -ATOM 1951 CG PHE A 233 -0.637 -33.896 24.209 1.00 12.81 C -ANISOU 1951 CG PHE A 233 1990 1423 1454 130 -5 52 C -ATOM 1952 CD1 PHE A 233 -1.951 -33.676 24.628 1.00 15.01 C -ANISOU 1952 CD1 PHE A 233 2301 1732 1670 159 2 25 C -ATOM 1953 CD2 PHE A 233 -0.426 -34.494 22.980 1.00 8.64 C -ANISOU 1953 CD2 PHE A 233 1423 924 937 106 44 86 C -ATOM 1954 CE1 PHE A 233 -3.034 -34.033 23.820 1.00 15.28 C -ANISOU 1954 CE1 PHE A 233 2328 1823 1655 164 57 33 C -ATOM 1955 CE2 PHE A 233 -1.495 -34.851 22.162 1.00 11.04 C -ANISOU 1955 CE2 PHE A 233 1720 1285 1191 112 99 94 C -ATOM 1956 CZ PHE A 233 -2.807 -34.612 22.581 1.00 14.96 C -ANISOU 1956 CZ PHE A 233 2249 1810 1627 140 106 67 C -ATOM 1957 N HIS A 234 1.758 -30.871 27.191 1.00 19.36 N -ANISOU 1957 N HIS A 234 2876 2041 2438 154 -228 2 N -ATOM 1958 CA HIS A 234 2.869 -30.352 27.983 1.00 16.77 C -ANISOU 1958 CA HIS A 234 2554 1650 2168 150 -291 -6 C -ATOM 1959 C HIS A 234 2.868 -30.973 29.384 1.00 19.59 C -ANISOU 1959 C HIS A 234 2948 2008 2490 166 -320 -47 C -ATOM 1960 O HIS A 234 2.524 -30.311 30.368 1.00 20.42 O -ANISOU 1960 O HIS A 234 3088 2090 2581 194 -364 -80 O -ATOM 1961 CB HIS A 234 2.719 -28.831 28.068 1.00 25.39 C -ANISOU 1961 CB HIS A 234 3657 2697 3292 167 -334 -11 C -ATOM 1962 CG HIS A 234 3.993 -28.100 28.362 1.00 32.21 C -ANISOU 1962 CG HIS A 234 4512 3491 4237 155 -391 -2 C -ATOM 1963 ND1 HIS A 234 5.040 -28.668 29.055 1.00 40.96 N -ANISOU 1963 ND1 HIS A 234 5620 4572 5372 141 -420 -8 N -ATOM 1964 CD2 HIS A 234 4.387 -26.841 28.053 1.00 35.70 C -ANISOU 1964 CD2 HIS A 234 4943 3882 4738 153 -426 14 C -ATOM 1965 CE1 HIS A 234 6.021 -27.789 29.167 1.00 38.12 C -ANISOU 1965 CE1 HIS A 234 5250 4149 5084 132 -470 2 C -ATOM 1966 NE2 HIS A 234 5.649 -26.672 28.568 1.00 36.86 N -ANISOU 1966 NE2 HIS A 234 5084 3974 4947 139 -475 16 N -ATOM 1967 N GLY A 235 3.249 -32.246 29.476 1.00 16.45 N -ANISOU 1967 N GLY A 235 2540 1635 2076 150 -295 -44 N -ATOM 1968 CA GLY A 235 3.246 -32.942 30.750 1.00 14.75 C -ANISOU 1968 CA GLY A 235 2356 1425 1825 163 -317 -80 C -ATOM 1969 C GLY A 235 4.442 -32.601 31.621 1.00 16.45 C -ANISOU 1969 C GLY A 235 2577 1578 2095 158 -379 -90 C -ATOM 1970 O GLY A 235 5.509 -32.280 31.110 1.00 16.97 O -ANISOU 1970 O GLY A 235 2613 1604 2229 134 -394 -62 O -ATOM 1971 N HIS A 236 4.270 -32.701 32.934 1.00 15.67 N -ANISOU 1971 N HIS A 236 2516 1473 1966 181 -416 -130 N -ATOM 1972 CA HIS A 236 5.350 -32.390 33.873 1.00 22.36 C -ANISOU 1972 CA HIS A 236 3373 2263 2861 180 -478 -144 C -ATOM 1973 C HIS A 236 6.243 -33.596 34.155 1.00 22.53 C -ANISOU 1973 C HIS A 236 3381 2287 2890 157 -471 -139 C -ATOM 1974 O HIS A 236 7.393 -33.449 34.608 1.00 22.88 O -ANISOU 1974 O HIS A 236 3421 2283 2989 145 -514 -139 O -ATOM 1975 CB HIS A 236 4.771 -31.824 35.169 1.00 29.40 C -ANISOU 1975 CB HIS A 236 4311 3141 3718 218 -524 -189 C -ATOM 1976 CG HIS A 236 4.039 -30.531 34.974 1.00 51.58 C -ANISOU 1976 CG HIS A 236 7134 5937 6528 241 -541 -195 C -ATOM 1977 ND1 HIS A 236 4.618 -29.435 34.370 1.00 62.08 N -ANISOU 1977 ND1 HIS A 236 8444 7217 7925 230 -566 -173 N -ATOM 1978 CD2 HIS A 236 2.774 -30.162 35.291 1.00 55.16 C -ANISOU 1978 CD2 HIS A 236 7617 6419 6922 275 -535 -220 C -ATOM 1979 CE1 HIS A 236 3.744 -28.444 34.328 1.00 61.33 C -ANISOU 1979 CE1 HIS A 236 8368 7122 7814 255 -576 -185 C -ATOM 1980 NE2 HIS A 236 2.618 -28.859 34.881 1.00 58.45 N -ANISOU 1980 NE2 HIS A 236 8033 6804 7372 283 -557 -214 N -ATOM 1981 N ASP A 237 5.694 -34.782 33.894 1.00 17.22 N -ANISOU 1981 N ASP A 237 2705 1674 2165 152 -418 -137 N -ATOM 1982 CA ASP A 237 6.420 -36.047 33.944 1.00 20.94 C -ANISOU 1982 CA ASP A 237 3159 2158 2639 128 -399 -128 C -ATOM 1983 C ASP A 237 5.661 -37.052 33.071 1.00 16.97 C -ANISOU 1983 C ASP A 237 2640 1721 2088 119 -329 -111 C -ATOM 1984 O ASP A 237 4.667 -36.691 32.458 1.00 19.66 O -ANISOU 1984 O ASP A 237 2980 2090 2397 130 -299 -106 O -ATOM 1985 CB ASP A 237 6.572 -36.560 35.387 1.00 22.73 C -ANISOU 1985 CB ASP A 237 3418 2379 2839 144 -434 -165 C -ATOM 1986 CG ASP A 237 5.234 -36.767 36.090 1.00 28.60 C -ANISOU 1986 CG ASP A 237 4199 3167 3502 178 -423 -198 C -ATOM 1987 OD1 ASP A 237 4.278 -37.248 35.447 1.00 22.27 O -ANISOU 1987 OD1 ASP A 237 3391 2418 2652 180 -370 -189 O -ATOM 1988 OD2 ASP A 237 5.143 -36.458 37.298 1.00 28.84 O -ANISOU 1988 OD2 ASP A 237 4264 3179 3516 204 -468 -232 O -ATOM 1989 N ASN A 238 6.113 -38.303 33.021 1.00 13.50 N -ANISOU 1989 N ASN A 238 2185 1304 1640 99 -303 -103 N -ATOM 1990 CA ASN A 238 5.502 -39.277 32.106 1.00 16.39 C -ANISOU 1990 CA ASN A 238 2532 1730 1968 87 -237 -85 C -ATOM 1991 C ASN A 238 4.082 -39.683 32.496 1.00 14.78 C -ANISOU 1991 C ASN A 238 2356 1578 1681 113 -211 -110 C -ATOM 1992 O ASN A 238 3.308 -40.145 31.651 1.00 16.78 O -ANISOU 1992 O ASN A 238 2596 1880 1899 110 -158 -96 O -ATOM 1993 CB ASN A 238 6.392 -40.515 31.925 1.00 20.71 C -ANISOU 1993 CB ASN A 238 3055 2285 2530 59 -217 -69 C -ATOM 1994 CG ASN A 238 7.712 -40.188 31.236 1.00 18.83 C -ANISOU 1994 CG ASN A 238 2781 2004 2370 30 -230 -36 C -ATOM 1995 OD1 ASN A 238 7.833 -39.172 30.551 1.00 20.39 O -ANISOU 1995 OD1 ASN A 238 2963 2177 2606 27 -237 -17 O -ATOM 1996 ND2 ASN A 238 8.710 -41.050 31.420 1.00 21.74 N -ANISOU 1996 ND2 ASN A 238 3135 2363 2763 9 -234 -29 N -ATOM 1997 N TYR A 239 3.742 -39.518 33.770 1.00 17.18 N -ANISOU 1997 N TYR A 239 2698 1875 1955 140 -247 -146 N -ATOM 1998 CA TYR A 239 2.401 -39.842 34.241 1.00 16.32 C -ANISOU 1998 CA TYR A 239 2618 1815 1768 167 -227 -171 C -ATOM 1999 C TYR A 239 1.461 -38.710 33.863 1.00 15.05 C -ANISOU 1999 C TYR A 239 2468 1657 1593 189 -225 -173 C -ATOM 2000 O TYR A 239 0.414 -38.932 33.245 1.00 14.74 O -ANISOU 2000 O TYR A 239 2426 1666 1509 195 -180 -167 O -ATOM 2001 CB TYR A 239 2.409 -40.089 35.747 1.00 15.78 C -ANISOU 2001 CB TYR A 239 2585 1739 1672 189 -266 -207 C -ATOM 2002 CG TYR A 239 3.456 -41.106 36.118 1.00 27.93 C -ANISOU 2002 CG TYR A 239 4112 3267 3232 167 -273 -204 C -ATOM 2003 CD1 TYR A 239 3.340 -42.421 35.703 1.00 29.10 C -ANISOU 2003 CD1 TYR A 239 4244 3460 3354 149 -225 -191 C -ATOM 2004 CD2 TYR A 239 4.581 -40.744 36.839 1.00 31.18 C -ANISOU 2004 CD2 TYR A 239 4529 3624 3694 163 -326 -213 C -ATOM 2005 CE1 TYR A 239 4.306 -43.359 36.015 1.00 32.55 C -ANISOU 2005 CE1 TYR A 239 4669 3888 3811 128 -230 -187 C -ATOM 2006 CE2 TYR A 239 5.554 -41.674 37.155 1.00 36.96 C -ANISOU 2006 CE2 TYR A 239 5250 4348 4447 142 -331 -208 C -ATOM 2007 CZ TYR A 239 5.408 -42.983 36.740 1.00 36.84 C -ANISOU 2007 CZ TYR A 239 5218 4378 4403 125 -282 -196 C -ATOM 2008 OH TYR A 239 6.367 -43.924 37.048 1.00 35.98 O -ANISOU 2008 OH TYR A 239 5097 4259 4313 104 -287 -192 O -ATOM 2009 N ASP A 240 1.868 -37.489 34.192 1.00 14.82 N -ANISOU 2009 N ASP A 240 2448 1576 1606 199 -275 -180 N -ATOM 2010 CA ASP A 240 1.081 -36.325 33.845 1.00 12.58 C -ANISOU 2010 CA ASP A 240 2174 1289 1316 219 -279 -182 C -ATOM 2011 C ASP A 240 0.957 -36.226 32.324 1.00 12.39 C -ANISOU 2011 C ASP A 240 2114 1282 1312 197 -232 -144 C -ATOM 2012 O ASP A 240 -0.039 -35.736 31.814 1.00 16.24 O -ANISOU 2012 O ASP A 240 2606 1795 1770 211 -209 -142 O -ATOM 2013 CB ASP A 240 1.707 -35.058 34.429 1.00 16.75 C -ANISOU 2013 CB ASP A 240 2717 1753 1896 230 -345 -195 C -ATOM 2014 CG ASP A 240 0.847 -33.831 34.232 1.00 19.21 C -ANISOU 2014 CG ASP A 240 3043 2058 2197 255 -355 -201 C -ATOM 2015 OD1 ASP A 240 -0.329 -33.830 34.655 1.00 19.42 O -ANISOU 2015 OD1 ASP A 240 3097 2122 2160 284 -343 -225 O -ATOM 2016 OD2 ASP A 240 1.344 -32.856 33.644 1.00 20.11 O -ANISOU 2016 OD2 ASP A 240 3141 2132 2369 245 -373 -183 O -ATOM 2017 N GLN A 241 1.957 -36.710 31.602 1.00 8.86 N -ANISOU 2017 N GLN A 241 1631 824 912 164 -217 -114 N -ATOM 2018 CA GLN A 241 1.888 -36.689 30.144 1.00 11.71 C -ANISOU 2018 CA GLN A 241 1956 1204 1291 144 -171 -76 C -ATOM 2019 C GLN A 241 0.636 -37.455 29.689 1.00 15.44 C -ANISOU 2019 C GLN A 241 2430 1745 1692 151 -112 -77 C -ATOM 2020 O GLN A 241 -0.116 -36.980 28.842 1.00 16.94 O -ANISOU 2020 O GLN A 241 2611 1956 1869 156 -83 -64 O -ATOM 2021 CB GLN A 241 3.156 -37.281 29.527 1.00 11.55 C -ANISOU 2021 CB GLN A 241 1897 1166 1325 108 -161 -45 C -ATOM 2022 CG GLN A 241 3.224 -37.165 27.999 1.00 10.08 C -ANISOU 2022 CG GLN A 241 1670 995 1164 87 -118 -4 C -ATOM 2023 CD GLN A 241 3.294 -35.719 27.517 1.00 15.13 C -ANISOU 2023 CD GLN A 241 2302 1596 1848 91 -141 10 C -ATOM 2024 OE1 GLN A 241 3.742 -34.843 28.238 1.00 14.33 O -ANISOU 2024 OE1 GLN A 241 2218 1445 1781 101 -195 -4 O -ATOM 2025 NE2 GLN A 241 2.866 -35.477 26.283 1.00 15.43 N -ANISOU 2025 NE2 GLN A 241 2315 1659 1888 85 -100 38 N -ATOM 2026 N LEU A 242 0.400 -38.633 30.263 1.00 10.57 N -ANISOU 2026 N LEU A 242 1825 1162 1030 153 -96 -93 N -ATOM 2027 CA LEU A 242 -0.772 -39.412 29.856 1.00 11.92 C -ANISOU 2027 CA LEU A 242 1998 1398 1135 159 -42 -94 C -ATOM 2028 C LEU A 242 -2.058 -38.715 30.280 1.00 14.50 C -ANISOU 2028 C LEU A 242 2356 1743 1409 194 -46 -118 C -ATOM 2029 O LEU A 242 -3.060 -38.769 29.557 1.00 13.00 O -ANISOU 2029 O LEU A 242 2162 1596 1182 199 -3 -110 O -ATOM 2030 CB LEU A 242 -0.719 -40.847 30.377 1.00 13.43 C -ANISOU 2030 CB LEU A 242 2193 1621 1291 152 -24 -104 C -ATOM 2031 CG LEU A 242 -1.835 -41.758 29.846 1.00 9.80 C -ANISOU 2031 CG LEU A 242 1728 1227 768 154 35 -100 C -ATOM 2032 CD1 LEU A 242 -1.836 -41.826 28.313 1.00 11.99 C -ANISOU 2032 CD1 LEU A 242 1968 1524 1065 133 81 -65 C -ATOM 2033 CD2 LEU A 242 -1.733 -43.158 30.455 1.00 12.60 C -ANISOU 2033 CD2 LEU A 242 2088 1608 1091 147 47 -111 C -ATOM 2034 N VAL A 243 -2.046 -38.061 31.443 1.00 12.11 N -ANISOU 2034 N VAL A 243 2087 1410 1105 217 -98 -147 N -ATOM 2035 CA VAL A 243 -3.229 -37.316 31.884 1.00 11.31 C -ANISOU 2035 CA VAL A 243 2017 1323 957 252 -106 -171 C -ATOM 2036 C VAL A 243 -3.546 -36.177 30.914 1.00 14.80 C -ANISOU 2036 C VAL A 243 2447 1754 1423 254 -99 -153 C -ATOM 2037 O VAL A 243 -4.704 -35.967 30.553 1.00 15.92 O -ANISOU 2037 O VAL A 243 2597 1933 1520 270 -70 -155 O -ATOM 2038 CB VAL A 243 -3.102 -36.776 33.329 1.00 11.56 C -ANISOU 2038 CB VAL A 243 2086 1321 984 279 -167 -207 C -ATOM 2039 CG1 VAL A 243 -4.403 -36.048 33.741 1.00 12.86 C -ANISOU 2039 CG1 VAL A 243 2284 1507 1095 317 -172 -231 C -ATOM 2040 CG2 VAL A 243 -2.769 -37.915 34.315 1.00 16.59 C -ANISOU 2040 CG2 VAL A 243 2736 1970 1597 278 -174 -225 C -ATOM 2041 N ARG A 244 -2.517 -35.458 30.476 1.00 13.14 N -ANISOU 2041 N ARG A 244 2215 1493 1285 236 -124 -133 N -ATOM 2042 CA ARG A 244 -2.696 -34.367 29.511 1.00 15.63 C -ANISOU 2042 CA ARG A 244 2516 1794 1631 235 -119 -112 C -ATOM 2043 C ARG A 244 -3.362 -34.881 28.252 1.00 15.75 C -ANISOU 2043 C ARG A 244 2504 1860 1620 223 -53 -85 C -ATOM 2044 O ARG A 244 -4.261 -34.246 27.707 1.00 12.85 O -ANISOU 2044 O ARG A 244 2139 1512 1232 236 -34 -82 O -ATOM 2045 CB ARG A 244 -1.350 -33.747 29.119 1.00 14.77 C -ANISOU 2045 CB ARG A 244 2380 1626 1607 212 -150 -88 C -ATOM 2046 CG ARG A 244 -0.552 -33.194 30.276 1.00 22.38 C -ANISOU 2046 CG ARG A 244 3366 2533 2606 221 -217 -111 C -ATOM 2047 CD ARG A 244 -1.248 -32.014 30.900 1.00 25.82 C -ANISOU 2047 CD ARG A 244 3835 2950 3027 255 -255 -137 C -ATOM 2048 NE ARG A 244 -0.450 -31.397 31.960 1.00 28.99 N -ANISOU 2048 NE ARG A 244 4256 3292 3467 264 -323 -159 N -ATOM 2049 CZ ARG A 244 -0.382 -30.084 32.165 1.00 36.40 C -ANISOU 2049 CZ ARG A 244 5207 4186 4439 279 -368 -167 C -ATOM 2050 NH1 ARG A 244 -1.042 -29.255 31.362 1.00 37.52 N -ANISOU 2050 NH1 ARG A 244 5342 4334 4582 286 -351 -153 N -ATOM 2051 NH2 ARG A 244 0.350 -29.596 33.158 1.00 34.32 N -ANISOU 2051 NH2 ARG A 244 4961 3869 4208 288 -430 -188 N -ATOM 2052 N ILE A 245 -2.894 -36.026 27.778 1.00 11.77 N -ANISOU 2052 N ILE A 245 1975 1379 1119 197 -19 -67 N -ATOM 2053 CA ILE A 245 -3.462 -36.637 26.580 1.00 12.87 C -ANISOU 2053 CA ILE A 245 2088 1569 1234 184 44 -43 C -ATOM 2054 C ILE A 245 -4.917 -37.034 26.838 1.00 14.62 C -ANISOU 2054 C ILE A 245 2335 1846 1375 208 74 -64 C -ATOM 2055 O ILE A 245 -5.809 -36.724 26.046 1.00 13.51 O -ANISOU 2055 O ILE A 245 2188 1735 1210 215 108 -53 O -ATOM 2056 CB ILE A 245 -2.660 -37.873 26.148 1.00 11.09 C -ANISOU 2056 CB ILE A 245 1833 1356 1024 154 71 -23 C -ATOM 2057 CG1 ILE A 245 -1.258 -37.443 25.660 1.00 11.82 C -ANISOU 2057 CG1 ILE A 245 1895 1398 1198 128 48 4 C -ATOM 2058 CG2 ILE A 245 -3.423 -38.636 25.069 1.00 11.12 C -ANISOU 2058 CG2 ILE A 245 1816 1419 990 146 136 -5 C -ATOM 2059 CD1 ILE A 245 -0.274 -38.585 25.437 1.00 12.57 C -ANISOU 2059 CD1 ILE A 245 1964 1497 1316 100 63 20 C -ATOM 2060 N ALA A 246 -5.154 -37.697 27.963 1.00 12.06 N -ANISOU 2060 N ALA A 246 2038 1534 1010 222 60 -92 N -ATOM 2061 CA ALA A 246 -6.508 -38.149 28.310 1.00 15.56 C -ANISOU 2061 CA ALA A 246 2504 2031 1376 245 87 -112 C -ATOM 2062 C ALA A 246 -7.532 -37.007 28.470 1.00 15.93 C -ANISOU 2062 C ALA A 246 2577 2081 1396 276 75 -127 C -ATOM 2063 O ALA A 246 -8.740 -37.196 28.245 1.00 13.93 O -ANISOU 2063 O ALA A 246 2333 1876 1086 291 110 -132 O -ATOM 2064 CB ALA A 246 -6.471 -39.007 29.552 1.00 11.17 C -ANISOU 2064 CB ALA A 246 1973 1484 786 254 69 -139 C -ATOM 2065 N LYS A 247 -7.062 -35.827 28.849 1.00 11.66 N -ANISOU 2065 N LYS A 247 2046 1487 896 286 26 -135 N -ATOM 2066 CA LYS A 247 -7.934 -34.645 28.914 1.00 12.20 C -ANISOU 2066 CA LYS A 247 2136 1552 947 314 12 -147 C -ATOM 2067 C LYS A 247 -8.454 -34.169 27.543 1.00 16.76 C -ANISOU 2067 C LYS A 247 2689 2148 1531 307 53 -119 C -ATOM 2068 O LYS A 247 -9.404 -33.388 27.463 1.00 17.83 O -ANISOU 2068 O LYS A 247 2841 2296 1639 330 55 -127 O -ATOM 2069 CB LYS A 247 -7.256 -33.496 29.671 1.00 17.22 C -ANISOU 2069 CB LYS A 247 2790 2125 1630 327 -54 -163 C -ATOM 2070 CG LYS A 247 -7.139 -33.748 31.176 1.00 16.66 C -ANISOU 2070 CG LYS A 247 2754 2042 1535 347 -96 -199 C -ATOM 2071 CD LYS A 247 -6.543 -32.566 31.918 1.00 21.58 C -ANISOU 2071 CD LYS A 247 3396 2603 2202 362 -163 -216 C -ATOM 2072 CE LYS A 247 -6.719 -32.738 33.424 1.00 30.61 C -ANISOU 2072 CE LYS A 247 4579 3744 3309 390 -201 -256 C -ATOM 2073 NZ LYS A 247 -5.992 -31.700 34.203 1.00 36.89 N -ANISOU 2073 NZ LYS A 247 5391 4476 4150 403 -269 -274 N -ATOM 2074 N VAL A 248 -7.840 -34.656 26.475 1.00 12.09 N -ANISOU 2074 N VAL A 248 1686 1563 1344 75 -38 181 N -ATOM 2075 CA VAL A 248 -8.200 -34.271 25.123 1.00 12.93 C -ANISOU 2075 CA VAL A 248 1765 1704 1445 66 -29 193 C -ATOM 2076 C VAL A 248 -8.879 -35.426 24.401 1.00 14.51 C -ANISOU 2076 C VAL A 248 1945 1939 1630 32 -27 192 C -ATOM 2077 O VAL A 248 -9.956 -35.253 23.824 1.00 15.30 O -ANISOU 2077 O VAL A 248 2019 2086 1709 28 -18 211 O -ATOM 2078 CB VAL A 248 -6.965 -33.818 24.318 1.00 14.10 C -ANISOU 2078 CB VAL A 248 1914 1829 1616 65 -34 179 C -ATOM 2079 CG1 VAL A 248 -7.336 -33.536 22.865 1.00 11.84 C -ANISOU 2079 CG1 VAL A 248 1599 1583 1319 57 -23 192 C -ATOM 2080 CG2 VAL A 248 -6.328 -32.579 24.956 1.00 13.22 C -ANISOU 2080 CG2 VAL A 248 1819 1683 1523 96 -34 177 C -ATOM 2081 N LEU A 249 -8.252 -36.598 24.427 1.00 10.40 N -ANISOU 2081 N LEU A 249 1435 1397 1120 7 -35 169 N -ATOM 2082 CA LEU A 249 -8.800 -37.773 23.752 1.00 11.45 C -ANISOU 2082 CA LEU A 249 1551 1557 1243 -29 -33 162 C -ATOM 2083 C LEU A 249 -9.828 -38.490 24.616 1.00 13.95 C -ANISOU 2083 C LEU A 249 1869 1883 1547 -37 -26 171 C -ATOM 2084 O LEU A 249 -10.607 -39.311 24.124 1.00 11.89 O -ANISOU 2084 O LEU A 249 1589 1652 1277 -67 -21 169 O -ATOM 2085 CB LEU A 249 -7.681 -38.755 23.370 1.00 14.12 C -ANISOU 2085 CB LEU A 249 1901 1864 1600 -52 -40 133 C -ATOM 2086 CG LEU A 249 -6.827 -38.430 22.142 1.00 15.35 C -ANISOU 2086 CG LEU A 249 2047 2021 1764 -56 -43 121 C -ATOM 2087 CD1 LEU A 249 -6.036 -37.140 22.301 1.00 16.15 C -ANISOU 2087 CD1 LEU A 249 2156 2100 1879 -25 -45 128 C -ATOM 2088 CD2 LEU A 249 -5.871 -39.576 21.829 1.00 16.02 C -ANISOU 2088 CD2 LEU A 249 2143 2078 1866 -80 -47 93 C -ATOM 2089 N GLY A 250 -9.820 -38.185 25.903 1.00 11.25 N -ANISOU 2089 N GLY A 250 1549 1518 1208 -11 -27 180 N -ATOM 2090 CA GLY A 250 -10.807 -38.741 26.815 1.00 12.99 C -ANISOU 2090 CA GLY A 250 1771 1747 1417 -13 -18 194 C -ATOM 2091 C GLY A 250 -10.363 -40.033 27.466 1.00 15.00 C -ANISOU 2091 C GLY A 250 2047 1968 1684 -29 -18 180 C -ATOM 2092 O GLY A 250 -9.541 -40.782 26.919 1.00 14.67 O -ANISOU 2092 O GLY A 250 2011 1906 1658 -50 -23 158 O -ATOM 2093 N THR A 251 -10.913 -40.307 28.643 1.00 14.90 N -ANISOU 2093 N THR A 251 2048 1949 1664 -16 -11 194 N -ATOM 2094 CA THR A 251 -10.521 -41.503 29.371 1.00 13.15 C -ANISOU 2094 CA THR A 251 1848 1695 1454 -25 -8 187 C -ATOM 2095 C THR A 251 -11.213 -42.780 28.884 1.00 8.74 C -ANISOU 2095 C THR A 251 1274 1147 899 -67 6 184 C -ATOM 2096 O THR A 251 -10.643 -43.864 28.999 1.00 14.97 O -ANISOU 2096 O THR A 251 2078 1904 1704 -84 9 170 O -ATOM 2097 CB THR A 251 -10.739 -41.352 30.888 1.00 14.93 C -ANISOU 2097 CB THR A 251 2097 1907 1670 9 -4 204 C -ATOM 2098 OG1 THR A 251 -12.054 -40.846 31.128 1.00 12.69 O -ANISOU 2098 OG1 THR A 251 1796 1660 1367 17 9 229 O -ATOM 2099 CG2 THR A 251 -9.721 -40.383 31.483 1.00 16.79 C -ANISOU 2099 CG2 THR A 251 2355 2118 1908 47 -20 196 C -ATOM 2100 N GLU A 252 -12.441 -42.687 28.371 1.00 12.44 N -ANISOU 2100 N GLU A 252 1712 1661 1354 -86 16 196 N -ATOM 2101 CA GLU A 252 -13.116 -43.925 27.956 1.00 12.07 C -ANISOU 2101 CA GLU A 252 1649 1624 1313 -130 29 189 C -ATOM 2102 C GLU A 252 -12.375 -44.625 26.814 1.00 14.45 C -ANISOU 2102 C GLU A 252 1946 1914 1629 -163 23 157 C -ATOM 2103 O GLU A 252 -12.242 -45.855 26.799 1.00 15.38 O -ANISOU 2103 O GLU A 252 2072 2007 1764 -192 33 142 O -ATOM 2104 CB GLU A 252 -14.589 -43.683 27.611 1.00 16.76 C -ANISOU 2104 CB GLU A 252 2206 2273 1889 -144 39 206 C -ATOM 2105 CG GLU A 252 -15.444 -43.419 28.844 1.00 24.41 C -ANISOU 2105 CG GLU A 252 3179 3248 2847 -119 52 237 C -ATOM 2106 CD GLU A 252 -15.562 -44.640 29.737 1.00 37.97 C -ANISOU 2106 CD GLU A 252 4915 4934 4579 -132 69 241 C -ATOM 2107 OE1 GLU A 252 -16.125 -45.661 29.284 1.00 46.30 O -ANISOU 2107 OE1 GLU A 252 5951 5996 5644 -175 81 232 O -ATOM 2108 OE2 GLU A 252 -15.084 -44.585 30.890 1.00 37.25 O -ANISOU 2108 OE2 GLU A 252 4855 4809 4488 -99 70 252 O -ATOM 2109 N ASP A 253 -11.865 -43.848 25.867 1.00 12.71 N -ANISOU 2109 N ASP A 253 1716 1709 1404 -158 10 147 N -ATOM 2110 CA ASP A 253 -11.094 -44.438 24.779 1.00 14.01 C -ANISOU 2110 CA ASP A 253 1878 1863 1580 -185 4 117 C -ATOM 2111 C ASP A 253 -9.712 -44.927 25.211 1.00 13.90 C -ANISOU 2111 C ASP A 253 1898 1792 1589 -174 0 102 C -ATOM 2112 O ASP A 253 -9.160 -45.855 24.610 1.00 15.55 O -ANISOU 2112 O ASP A 253 2112 1982 1813 -201 2 77 O -ATOM 2113 CB ASP A 253 -11.026 -43.498 23.582 1.00 12.33 C -ANISOU 2113 CB ASP A 253 1642 1689 1355 -182 -6 114 C -ATOM 2114 CG ASP A 253 -12.383 -43.335 22.908 1.00 17.70 C -ANISOU 2114 CG ASP A 253 2283 2431 2011 -201 -1 123 C -ATOM 2115 OD1 ASP A 253 -13.127 -44.333 22.818 1.00 21.86 O -ANISOU 2115 OD1 ASP A 253 2796 2970 2538 -237 8 114 O -ATOM 2116 OD2 ASP A 253 -12.707 -42.208 22.503 1.00 18.37 O -ANISOU 2116 OD2 ASP A 253 2350 2553 2078 -180 -5 140 O -ATOM 2117 N LEU A 254 -9.172 -44.327 26.266 1.00 14.24 N -ANISOU 2117 N LEU A 254 1965 1810 1635 -135 -7 115 N -ATOM 2118 CA LEU A 254 -7.936 -44.831 26.858 1.00 17.65 C -ANISOU 2118 CA LEU A 254 2428 2193 2086 -122 -11 104 C -ATOM 2119 C LEU A 254 -8.210 -46.203 27.447 1.00 17.43 C -ANISOU 2119 C LEU A 254 2413 2140 2069 -140 5 105 C -ATOM 2120 O LEU A 254 -7.431 -47.139 27.248 1.00 17.70 O -ANISOU 2120 O LEU A 254 2462 2141 2122 -153 9 87 O -ATOM 2121 CB LEU A 254 -7.403 -43.889 27.936 1.00 13.92 C -ANISOU 2121 CB LEU A 254 1975 1704 1610 -77 -23 117 C -ATOM 2122 CG LEU A 254 -6.195 -44.374 28.745 1.00 16.16 C -ANISOU 2122 CG LEU A 254 2289 1943 1910 -57 -30 109 C -ATOM 2123 CD1 LEU A 254 -5.041 -44.737 27.821 1.00 17.48 C -ANISOU 2123 CD1 LEU A 254 2456 2090 2096 -71 -37 83 C -ATOM 2124 CD2 LEU A 254 -5.801 -43.286 29.707 1.00 15.23 C -ANISOU 2124 CD2 LEU A 254 2183 1818 1784 -15 -44 117 C -ATOM 2125 N TYR A 255 -9.322 -46.337 28.165 1.00 15.47 N -ANISOU 2125 N TYR A 255 2161 1907 1810 -140 18 126 N -ATOM 2126 CA TYR A 255 -9.672 -47.645 28.704 1.00 14.01 C -ANISOU 2126 CA TYR A 255 1988 1699 1639 -159 39 130 C -ATOM 2127 C TYR A 255 -9.949 -48.666 27.596 1.00 15.80 C -ANISOU 2127 C TYR A 255 2198 1928 1878 -210 51 106 C -ATOM 2128 O TYR A 255 -9.550 -49.825 27.714 1.00 17.25 O -ANISOU 2128 O TYR A 255 2398 2073 2083 -226 65 96 O -ATOM 2129 CB TYR A 255 -10.823 -47.563 29.713 1.00 11.64 C -ANISOU 2129 CB TYR A 255 1684 1414 1324 -148 53 160 C -ATOM 2130 CG TYR A 255 -10.342 -47.244 31.116 1.00 14.69 C -ANISOU 2130 CG TYR A 255 2101 1777 1705 -100 50 180 C -ATOM 2131 CD1 TYR A 255 -9.822 -48.239 31.925 1.00 19.00 C -ANISOU 2131 CD1 TYR A 255 2674 2282 2264 -92 62 185 C -ATOM 2132 CD2 TYR A 255 -10.398 -45.949 31.629 1.00 21.03 C -ANISOU 2132 CD2 TYR A 255 2905 2599 2488 -62 36 193 C -ATOM 2133 CE1 TYR A 255 -9.373 -47.966 33.202 1.00 21.87 C -ANISOU 2133 CE1 TYR A 255 3064 2630 2618 -46 57 202 C -ATOM 2134 CE2 TYR A 255 -9.951 -45.669 32.916 1.00 19.68 C -ANISOU 2134 CE2 TYR A 255 2761 2409 2308 -20 32 206 C -ATOM 2135 CZ TYR A 255 -9.441 -46.687 33.694 1.00 23.45 C -ANISOU 2135 CZ TYR A 255 3263 2851 2796 -11 41 210 C -ATOM 2136 OH TYR A 255 -8.991 -46.440 34.979 1.00 28.51 O -ANISOU 2136 OH TYR A 255 3930 3478 3423 33 35 223 O -ATOM 2137 N ASP A 256 -10.613 -48.245 26.519 1.00 14.06 N -ANISOU 2137 N ASP A 256 1944 1752 1645 -234 46 97 N -ATOM 2138 CA ASP A 256 -10.837 -49.147 25.387 1.00 12.60 C -ANISOU 2138 CA ASP A 256 1743 1576 1470 -283 54 68 C -ATOM 2139 C ASP A 256 -9.503 -49.667 24.829 1.00 15.19 C -ANISOU 2139 C ASP A 256 2090 1866 1816 -287 49 41 C -ATOM 2140 O ASP A 256 -9.389 -50.829 24.451 1.00 16.15 O -ANISOU 2140 O ASP A 256 2217 1964 1957 -320 63 19 O -ATOM 2141 CB ASP A 256 -11.585 -48.454 24.254 1.00 15.74 C -ANISOU 2141 CB ASP A 256 2101 2034 1845 -301 44 62 C -ATOM 2142 CG ASP A 256 -13.069 -48.238 24.549 1.00 19.83 C -ANISOU 2142 CG ASP A 256 2592 2596 2348 -310 52 83 C -ATOM 2143 OD1 ASP A 256 -13.626 -48.836 25.501 1.00 17.04 O -ANISOU 2143 OD1 ASP A 256 2247 2225 2004 -314 69 99 O -ATOM 2144 OD2 ASP A 256 -13.683 -47.461 23.788 1.00 24.75 O -ANISOU 2144 OD2 ASP A 256 3183 3273 2948 -313 42 86 O -ATOM 2145 N TYR A 257 -8.517 -48.774 24.752 1.00 15.49 N -ANISOU 2145 N TYR A 257 2138 1898 1850 -254 31 42 N -ATOM 2146 CA TYR A 257 -7.181 -49.080 24.248 1.00 16.94 C -ANISOU 2146 CA TYR A 257 2337 2049 2050 -251 25 19 C -ATOM 2147 C TYR A 257 -6.490 -50.118 25.116 1.00 16.68 C -ANISOU 2147 C TYR A 257 2336 1960 2040 -243 37 20 C -ATOM 2148 O TYR A 257 -6.088 -51.176 24.634 1.00 17.14 O -ANISOU 2148 O TYR A 257 2403 1992 2117 -268 49 -2 O -ATOM 2149 CB TYR A 257 -6.340 -47.803 24.199 1.00 15.96 C -ANISOU 2149 CB TYR A 257 2215 1931 1919 -214 4 25 C -ATOM 2150 CG TYR A 257 -4.899 -47.994 23.768 1.00 19.32 C -ANISOU 2150 CG TYR A 257 2654 2323 2361 -207 -3 6 C -ATOM 2151 CD1 TYR A 257 -4.584 -48.768 22.650 1.00 15.97 C -ANISOU 2151 CD1 TYR A 257 2225 1896 1945 -238 4 -22 C -ATOM 2152 CD2 TYR A 257 -3.855 -47.373 24.451 1.00 16.61 C -ANISOU 2152 CD2 TYR A 257 2329 1957 2026 -168 -16 13 C -ATOM 2153 CE1 TYR A 257 -3.263 -48.936 22.234 1.00 17.06 C -ANISOU 2153 CE1 TYR A 257 2376 2007 2100 -229 -1 -39 C -ATOM 2154 CE2 TYR A 257 -2.520 -47.542 24.039 1.00 19.24 C -ANISOU 2154 CE2 TYR A 257 2672 2263 2377 -161 -22 -4 C -ATOM 2155 CZ TYR A 257 -2.245 -48.326 22.923 1.00 20.90 C -ANISOU 2155 CZ TYR A 257 2877 2470 2595 -191 -13 -29 C -ATOM 2156 OH TYR A 257 -0.956 -48.510 22.463 1.00 17.11 O -ANISOU 2156 OH TYR A 257 2405 1965 2132 -184 -17 -45 O -ATOM 2157 N ILE A 258 -6.349 -49.829 26.403 1.00 14.21 N -ANISOU 2157 N ILE A 258 2042 1631 1726 -207 35 45 N -ATOM 2158 CA ILE A 258 -5.643 -50.769 27.263 1.00 10.14 C -ANISOU 2158 CA ILE A 258 1557 1066 1229 -193 46 49 C -ATOM 2159 C ILE A 258 -6.434 -52.077 27.368 1.00 18.57 C -ANISOU 2159 C ILE A 258 2627 2117 2311 -227 75 49 C -ATOM 2160 O ILE A 258 -5.855 -53.152 27.504 1.00 17.83 O -ANISOU 2160 O ILE A 258 2554 1980 2239 -232 91 43 O -ATOM 2161 CB ILE A 258 -5.315 -50.188 28.660 1.00 17.19 C -ANISOU 2161 CB ILE A 258 2469 1949 2113 -144 37 76 C -ATOM 2162 CG1 ILE A 258 -6.582 -49.899 29.460 1.00 18.49 C -ANISOU 2162 CG1 ILE A 258 2627 2137 2260 -139 45 103 C -ATOM 2163 CG2 ILE A 258 -4.441 -48.930 28.538 1.00 16.83 C -ANISOU 2163 CG2 ILE A 258 2421 1914 2060 -114 9 71 C -ATOM 2164 CD1 ILE A 258 -6.303 -49.615 30.911 1.00 21.81 C -ANISOU 2164 CD1 ILE A 258 3071 2544 2671 -93 41 127 C -ATOM 2165 N ASP A 259 -7.759 -51.985 27.293 1.00 14.49 N -ANISOU 2165 N ASP A 259 2089 1634 1784 -250 84 58 N -ATOM 2166 CA ASP A 259 -8.585 -53.190 27.362 1.00 10.77 C -ANISOU 2166 CA ASP A 259 1616 1148 1329 -287 113 56 C -ATOM 2167 C ASP A 259 -8.388 -54.069 26.135 1.00 15.75 C -ANISOU 2167 C ASP A 259 2240 1767 1977 -333 122 18 C -ATOM 2168 O ASP A 259 -8.349 -55.295 26.241 1.00 16.39 O -ANISOU 2168 O ASP A 259 2336 1809 2084 -355 148 10 O -ATOM 2169 CB ASP A 259 -10.071 -52.841 27.510 1.00 13.74 C -ANISOU 2169 CB ASP A 259 1965 1567 1688 -304 119 72 C -ATOM 2170 CG ASP A 259 -10.432 -52.398 28.912 1.00 17.44 C -ANISOU 2170 CG ASP A 259 2446 2036 2146 -264 123 111 C -ATOM 2171 OD1 ASP A 259 -9.578 -52.489 29.819 1.00 17.27 O -ANISOU 2171 OD1 ASP A 259 2455 1979 2128 -227 122 125 O -ATOM 2172 OD2 ASP A 259 -11.594 -51.989 29.114 1.00 20.10 O -ANISOU 2172 OD2 ASP A 259 2761 2409 2467 -271 127 128 O -ATOM 2173 N LYS A 260 -8.288 -53.441 24.970 1.00 16.45 N -ANISOU 2173 N LYS A 260 2307 1893 2052 -346 103 -5 N -ATOM 2174 CA LYS A 260 -8.050 -54.174 23.730 1.00 18.59 C -ANISOU 2174 CA LYS A 260 2571 2159 2334 -386 109 -45 C -ATOM 2175 C LYS A 260 -6.789 -55.020 23.795 1.00 18.35 C -ANISOU 2175 C LYS A 260 2573 2070 2330 -377 119 -58 C -ATOM 2176 O LYS A 260 -6.776 -56.145 23.307 1.00 20.25 O -ANISOU 2176 O LYS A 260 2818 2283 2591 -411 140 -83 O -ATOM 2177 CB LYS A 260 -7.973 -53.228 22.528 1.00 22.54 C -ANISOU 2177 CB LYS A 260 3044 2709 2810 -391 85 -62 C -ATOM 2178 CG LYS A 260 -7.436 -53.912 21.284 1.00 18.05 C -ANISOU 2178 CG LYS A 260 2475 2133 2251 -422 89 -103 C -ATOM 2179 CD LYS A 260 -7.580 -53.048 20.041 1.00 24.81 C -ANISOU 2179 CD LYS A 260 3301 3047 3080 -429 69 -119 C -ATOM 2180 CE LYS A 260 -6.770 -53.635 18.886 1.00 24.53 C -ANISOU 2180 CE LYS A 260 3269 2999 3051 -449 71 -158 C -ATOM 2181 NZ LYS A 260 -6.780 -52.754 17.696 1.00 25.15 N -ANISOU 2181 NZ LYS A 260 3321 3134 3101 -449 53 -169 N -ATOM 2182 N TYR A 261 -5.734 -54.476 24.401 1.00 15.81 N -ANISOU 2182 N TYR A 261 2271 1730 2008 -330 105 -41 N -ATOM 2183 CA TYR A 261 -4.447 -55.171 24.486 1.00 16.61 C -ANISOU 2183 CA TYR A 261 2400 1780 2132 -314 112 -50 C -ATOM 2184 C TYR A 261 -4.249 -55.887 25.819 1.00 18.36 C -ANISOU 2184 C TYR A 261 2650 1956 2370 -289 131 -22 C -ATOM 2185 O TYR A 261 -3.162 -56.416 26.104 1.00 18.74 O -ANISOU 2185 O TYR A 261 2723 1963 2436 -266 137 -22 O -ATOM 2186 CB TYR A 261 -3.311 -54.191 24.198 1.00 13.37 C -ANISOU 2186 CB TYR A 261 1989 1378 1712 -280 85 -52 C -ATOM 2187 CG TYR A 261 -3.402 -53.696 22.780 1.00 12.86 C -ANISOU 2187 CG TYR A 261 1899 1353 1635 -305 73 -79 C -ATOM 2188 CD1 TYR A 261 -2.903 -54.460 21.727 1.00 16.26 C -ANISOU 2188 CD1 TYR A 261 2332 1769 2078 -331 83 -112 C -ATOM 2189 CD2 TYR A 261 -4.033 -52.488 22.482 1.00 13.21 C -ANISOU 2189 CD2 TYR A 261 1917 1449 1652 -302 55 -70 C -ATOM 2190 CE1 TYR A 261 -3.015 -54.031 20.421 1.00 17.30 C -ANISOU 2190 CE1 TYR A 261 2440 1940 2193 -353 74 -137 C -ATOM 2191 CE2 TYR A 261 -4.139 -52.044 21.176 1.00 14.91 C -ANISOU 2191 CE2 TYR A 261 2109 1704 1853 -321 46 -91 C -ATOM 2192 CZ TYR A 261 -3.628 -52.818 20.150 1.00 18.46 C -ANISOU 2192 CZ TYR A 261 2561 2141 2313 -347 54 -125 C -ATOM 2193 OH TYR A 261 -3.734 -52.382 18.848 1.00 16.58 O -ANISOU 2193 OH TYR A 261 2298 1945 2056 -364 46 -145 O -ATOM 2194 N ASN A 262 -5.318 -55.924 26.614 1.00 20.95 N -ANISOU 2194 N ASN A 262 2974 2293 2691 -292 142 2 N -ATOM 2195 CA ASN A 262 -5.294 -56.560 27.925 1.00 20.67 C -ANISOU 2195 CA ASN A 262 2965 2221 2668 -267 162 33 C -ATOM 2196 C ASN A 262 -4.110 -56.040 28.749 1.00 22.84 C -ANISOU 2196 C ASN A 262 3260 2482 2936 -210 144 51 C -ATOM 2197 O ASN A 262 -3.388 -56.816 29.369 1.00 24.99 O -ANISOU 2197 O ASN A 262 3559 2713 3225 -187 158 63 O -ATOM 2198 CB ASN A 262 -5.244 -58.090 27.790 1.00 19.62 C -ANISOU 2198 CB ASN A 262 2849 2036 2568 -295 199 22 C -ATOM 2199 CG ASN A 262 -6.526 -58.687 27.205 1.00 24.72 C -ANISOU 2199 CG ASN A 262 3475 2693 3224 -353 221 5 C -ATOM 2200 OD1 ASN A 262 -7.435 -57.976 26.769 1.00 31.16 O -ANISOU 2200 OD1 ASN A 262 4261 3560 4020 -374 207 -1 O -ATOM 2201 ND2 ASN A 262 -6.593 -60.010 27.190 1.00 30.97 N -ANISOU 2201 ND2 ASN A 262 4283 3437 4049 -379 257 -4 N -ATOM 2202 N ILE A 263 -3.931 -54.717 28.717 1.00 24.17 N -ANISOU 2202 N ILE A 263 3415 2688 3080 -187 112 53 N -ATOM 2203 CA ILE A 263 -2.900 -53.986 29.450 1.00 21.22 C -ANISOU 2203 CA ILE A 263 3054 2311 2696 -136 88 66 C -ATOM 2204 C ILE A 263 -3.539 -53.438 30.719 1.00 25.67 C -ANISOU 2204 C ILE A 263 3623 2892 3240 -106 85 98 C -ATOM 2205 O ILE A 263 -4.717 -53.070 30.720 1.00 29.14 O -ANISOU 2205 O ILE A 263 4046 3361 3666 -123 89 107 O -ATOM 2206 CB ILE A 263 -2.423 -52.744 28.657 1.00 25.79 C -ANISOU 2206 CB ILE A 263 3614 2923 3263 -132 57 48 C -ATOM 2207 CG1 ILE A 263 -1.774 -53.120 27.324 1.00 28.90 C -ANISOU 2207 CG1 ILE A 263 4000 3307 3672 -159 58 16 C -ATOM 2208 CG2 ILE A 263 -1.459 -51.899 29.479 1.00 29.30 C -ANISOU 2208 CG2 ILE A 263 4068 3366 3698 -83 32 59 C -ATOM 2209 CD1 ILE A 263 -1.470 -51.903 26.465 1.00 27.83 C -ANISOU 2209 CD1 ILE A 263 3843 3206 3524 -158 33 2 C -ATOM 2210 N GLU A 264 -2.765 -53.361 31.793 1.00 17.83 N -ANISOU 2210 N GLU A 264 2650 1883 2241 -60 77 116 N -ATOM 2211 CA GLU A 264 -3.236 -52.734 33.013 1.00 24.93 C -ANISOU 2211 CA GLU A 264 3555 2801 3116 -26 70 144 C -ATOM 2212 C GLU A 264 -2.507 -51.410 33.238 1.00 24.75 C -ANISOU 2212 C GLU A 264 3528 2800 3076 8 34 137 C -ATOM 2213 O GLU A 264 -1.284 -51.359 33.152 1.00 25.73 O -ANISOU 2213 O GLU A 264 3658 2909 3208 26 19 124 O -ATOM 2214 CB GLU A 264 -2.981 -53.680 34.180 1.00 29.60 C -ANISOU 2214 CB GLU A 264 4174 3361 3712 4 90 171 C -ATOM 2215 CG GLU A 264 -3.625 -53.267 35.462 1.00 34.03 C -ANISOU 2215 CG GLU A 264 4742 3940 4246 37 91 202 C -ATOM 2216 CD GLU A 264 -3.897 -54.454 36.355 1.00 37.05 C -ANISOU 2216 CD GLU A 264 5147 4293 4637 50 126 233 C -ATOM 2217 OE1 GLU A 264 -3.001 -55.323 36.490 1.00 36.76 O -ANISOU 2217 OE1 GLU A 264 5129 4222 4617 64 136 236 O -ATOM 2218 OE2 GLU A 264 -5.017 -54.520 36.902 1.00 38.19 O -ANISOU 2218 OE2 GLU A 264 5290 4450 4771 46 145 256 O -ATOM 2219 N LEU A 265 -3.252 -50.339 33.509 1.00 21.44 N -ANISOU 2219 N LEU A 265 3097 2415 2634 15 23 145 N -ATOM 2220 CA LEU A 265 -2.634 -49.062 33.845 1.00 23.13 C -ANISOU 2220 CA LEU A 265 3309 2646 2832 48 -8 138 C -ATOM 2221 C LEU A 265 -1.882 -49.174 35.170 1.00 22.61 C -ANISOU 2221 C LEU A 265 3266 2567 2756 95 -17 151 C -ATOM 2222 O LEU A 265 -2.321 -49.869 36.080 1.00 28.20 O -ANISOU 2222 O LEU A 265 3991 3268 3457 110 1 176 O -ATOM 2223 CB LEU A 265 -3.680 -47.945 33.981 1.00 25.27 C -ANISOU 2223 CB LEU A 265 3566 2953 3081 49 -14 146 C -ATOM 2224 CG LEU A 265 -4.121 -47.107 32.785 1.00 21.23 C -ANISOU 2224 CG LEU A 265 3028 2468 2570 21 -21 132 C -ATOM 2225 CD1 LEU A 265 -4.877 -45.903 33.296 1.00 22.47 C -ANISOU 2225 CD1 LEU A 265 3179 2656 2704 41 -28 144 C -ATOM 2226 CD2 LEU A 265 -2.928 -46.678 31.935 1.00 24.36 C -ANISOU 2226 CD2 LEU A 265 3418 2855 2981 19 -40 106 C -ATOM 2227 N ASP A 266 -0.755 -48.481 35.268 1.00 20.39 N -ANISOU 2227 N ASP A 266 2986 2286 2475 119 -45 135 N -ATOM 2228 CA ASP A 266 -0.071 -48.294 36.542 1.00 23.03 C -ANISOU 2228 CA ASP A 266 3337 2620 2793 167 -61 143 C -ATOM 2229 C ASP A 266 -1.109 -47.812 37.556 1.00 24.91 C -ANISOU 2229 C ASP A 266 3581 2880 3001 187 -57 164 C -ATOM 2230 O ASP A 266 -1.856 -46.870 37.277 1.00 22.29 O -ANISOU 2230 O ASP A 266 3237 2572 2661 176 -61 160 O -ATOM 2231 CB ASP A 266 1.025 -47.243 36.367 1.00 22.24 C -ANISOU 2231 CB ASP A 266 3228 2527 2696 181 -95 116 C -ATOM 2232 CG ASP A 266 1.930 -47.117 37.573 1.00 23.26 C -ANISOU 2232 CG ASP A 266 3371 2658 2811 227 -116 117 C -ATOM 2233 OD1 ASP A 266 1.467 -47.301 38.716 1.00 23.74 O -ANISOU 2233 OD1 ASP A 266 3447 2726 2846 256 -110 139 O -ATOM 2234 OD2 ASP A 266 3.114 -46.797 37.376 1.00 27.48 O -ANISOU 2234 OD2 ASP A 266 3898 3187 3356 236 -138 96 O -ATOM 2235 N PRO A 267 -1.178 -48.462 38.733 1.00 22.66 N -ANISOU 2235 N PRO A 267 3317 2591 2702 219 -46 189 N -ATOM 2236 CA PRO A 267 -2.197 -48.064 39.712 1.00 21.53 C -ANISOU 2236 CA PRO A 267 3182 2470 2529 239 -38 211 C -ATOM 2237 C PRO A 267 -2.005 -46.636 40.219 1.00 24.28 C -ANISOU 2237 C PRO A 267 3527 2843 2854 267 -68 196 C -ATOM 2238 O PRO A 267 -2.919 -46.071 40.826 1.00 24.50 O -ANISOU 2238 O PRO A 267 3558 2893 2859 280 -63 209 O -ATOM 2239 CB PRO A 267 -2.010 -49.076 40.855 1.00 20.50 C -ANISOU 2239 CB PRO A 267 3075 2328 2387 274 -23 240 C -ATOM 2240 CG PRO A 267 -0.622 -49.587 40.685 1.00 23.66 C -ANISOU 2240 CG PRO A 267 3480 2707 2804 285 -36 226 C -ATOM 2241 CD PRO A 267 -0.386 -49.610 39.198 1.00 21.88 C -ANISOU 2241 CD PRO A 267 3236 2467 2611 239 -37 201 C -ATOM 2242 N ARG A 268 -0.839 -46.047 39.979 1.00 20.69 N -ANISOU 2242 N ARG A 268 3067 2386 2407 274 -97 168 N -ATOM 2243 CA ARG A 268 -0.633 -44.675 40.429 1.00 25.72 C -ANISOU 2243 CA ARG A 268 3701 3042 3027 296 -124 149 C -ATOM 2244 C ARG A 268 -1.552 -43.691 39.690 1.00 26.54 C -ANISOU 2244 C ARG A 268 3789 3161 3134 271 -120 143 C -ATOM 2245 O ARG A 268 -1.749 -42.565 40.143 1.00 27.62 O -ANISOU 2245 O ARG A 268 3926 3313 3254 289 -132 135 O -ATOM 2246 CB ARG A 268 0.836 -44.256 40.327 1.00 34.61 C -ANISOU 2246 CB ARG A 268 4823 4162 4166 308 -156 118 C -ATOM 2247 CG ARG A 268 1.291 -43.847 38.947 1.00 40.62 C -ANISOU 2247 CG ARG A 268 5564 4913 4959 272 -162 95 C -ATOM 2248 CD ARG A 268 2.733 -43.367 38.992 1.00 44.75 C -ANISOU 2248 CD ARG A 268 6080 5430 5493 286 -193 66 C -ATOM 2249 NE ARG A 268 3.676 -44.479 39.065 1.00 46.97 N -ANISOU 2249 NE ARG A 268 6366 5695 5785 294 -194 69 N -ATOM 2250 CZ ARG A 268 4.838 -44.428 39.704 1.00 47.02 C -ANISOU 2250 CZ ARG A 268 6373 5704 5787 323 -219 56 C -ATOM 2251 NH1 ARG A 268 5.200 -43.322 40.345 1.00 46.62 N -ANISOU 2251 NH1 ARG A 268 6320 5670 5724 344 -246 34 N -ATOM 2252 NH2 ARG A 268 5.635 -45.487 39.710 1.00 45.27 N -ANISOU 2252 NH2 ARG A 268 6156 5469 5577 333 -216 63 N -ATOM 2253 N PHE A 269 -2.116 -44.126 38.564 1.00 23.57 N -ANISOU 2253 N PHE A 269 3398 2779 2777 230 -101 148 N -ATOM 2254 CA PHE A 269 -3.081 -43.310 37.827 1.00 16.00 C -ANISOU 2254 CA PHE A 269 2422 1838 1818 208 -93 148 C -ATOM 2255 C PHE A 269 -4.441 -43.243 38.515 1.00 24.46 C -ANISOU 2255 C PHE A 269 3498 2931 2866 217 -74 176 C -ATOM 2256 O PHE A 269 -5.276 -42.417 38.153 1.00 27.65 O -ANISOU 2256 O PHE A 269 3888 3354 3264 209 -69 179 O -ATOM 2257 CB PHE A 269 -3.252 -43.815 36.394 1.00 20.28 C -ANISOU 2257 CB PHE A 269 2946 2375 2386 162 -81 143 C -ATOM 2258 CG PHE A 269 -2.112 -43.453 35.480 1.00 21.32 C -ANISOU 2258 CG PHE A 269 3067 2494 2540 151 -99 116 C -ATOM 2259 CD1 PHE A 269 -2.002 -42.175 34.964 1.00 20.05 C -ANISOU 2259 CD1 PHE A 269 2892 2344 2382 149 -112 101 C -ATOM 2260 CD2 PHE A 269 -1.173 -44.403 35.110 1.00 20.43 C -ANISOU 2260 CD2 PHE A 269 2957 2358 2447 141 -100 107 C -ATOM 2261 CE1 PHE A 269 -0.964 -41.835 34.107 1.00 19.32 C -ANISOU 2261 CE1 PHE A 269 2789 2240 2312 138 -126 79 C -ATOM 2262 CE2 PHE A 269 -0.128 -44.074 34.254 1.00 22.16 C -ANISOU 2262 CE2 PHE A 269 3165 2566 2687 131 -115 83 C -ATOM 2263 CZ PHE A 269 -0.026 -42.781 33.753 1.00 18.43 C -ANISOU 2263 CZ PHE A 269 2679 2107 2218 129 -128 69 C -ATOM 2264 N ASN A 270 -4.663 -44.102 39.506 1.00 22.09 N -ANISOU 2264 N ASN A 270 3215 2626 2552 237 -60 198 N -ATOM 2265 CA ASN A 270 -5.940 -44.125 40.223 1.00 22.61 C -ANISOU 2265 CA ASN A 270 3286 2711 2595 248 -39 227 C -ATOM 2266 C ASN A 270 -6.310 -42.791 40.865 1.00 29.10 C -ANISOU 2266 C ASN A 270 4110 3556 3391 277 -50 224 C -ATOM 2267 O ASN A 270 -7.489 -42.437 40.933 1.00 28.26 O -ANISOU 2267 O ASN A 270 3995 3469 3272 275 -33 242 O -ATOM 2268 CB ASN A 270 -5.948 -45.221 41.296 1.00 31.94 C -ANISOU 2268 CB ASN A 270 4489 3883 3765 271 -22 252 C -ATOM 2269 CG ASN A 270 -6.036 -46.623 40.710 1.00 36.06 C -ANISOU 2269 CG ASN A 270 5008 4381 4313 238 2 263 C -ATOM 2270 OD1 ASN A 270 -6.577 -46.824 39.624 1.00 34.58 O -ANISOU 2270 OD1 ASN A 270 4801 4194 4145 195 14 259 O -ATOM 2271 ND2 ASN A 270 -5.509 -47.602 41.441 1.00 39.76 N -ANISOU 2271 ND2 ASN A 270 5496 4830 4780 260 11 278 N -ATOM 2272 N ASP A 271 -5.307 -42.057 41.344 1.00 23.41 N -ANISOU 2272 N ASP A 271 3399 2831 2663 305 -78 200 N -ATOM 2273 CA ASP A 271 -5.547 -40.795 42.042 1.00 31.26 C -ANISOU 2273 CA ASP A 271 4400 3843 3634 336 -89 192 C -ATOM 2274 C ASP A 271 -5.306 -39.549 41.195 1.00 30.11 C -ANISOU 2274 C ASP A 271 4239 3697 3504 322 -103 166 C -ATOM 2275 O ASP A 271 -5.473 -38.429 41.685 1.00 32.25 O -ANISOU 2275 O ASP A 271 4515 3978 3760 345 -111 156 O -ATOM 2276 CB ASP A 271 -4.685 -40.708 43.303 1.00 44.70 C -ANISOU 2276 CB ASP A 271 6125 5545 5314 379 -109 180 C -ATOM 2277 CG ASP A 271 -5.034 -41.774 44.321 1.00 57.48 C -ANISOU 2277 CG ASP A 271 7762 7169 6910 403 -92 211 C -ATOM 2278 OD1 ASP A 271 -6.134 -42.362 44.220 1.00 57.84 O -ANISOU 2278 OD1 ASP A 271 7804 7220 6955 389 -62 243 O -ATOM 2279 OD2 ASP A 271 -4.206 -42.019 45.224 1.00 65.78 O -ANISOU 2279 OD2 ASP A 271 8830 8220 7944 437 -108 206 O -ATOM 2280 N ILE A 272 -4.902 -39.729 39.939 1.00 25.96 N -ANISOU 2280 N ILE A 272 3695 3160 3009 286 -105 155 N -ATOM 2281 CA ILE A 272 -4.565 -38.577 39.100 1.00 17.07 C -ANISOU 2281 CA ILE A 272 2555 2031 1900 275 -117 132 C -ATOM 2282 C ILE A 272 -5.295 -38.494 37.754 1.00 20.17 C -ANISOU 2282 C ILE A 272 2923 2433 2308 239 -101 142 C -ATOM 2283 O ILE A 272 -5.351 -37.417 37.153 1.00 19.32 O -ANISOU 2283 O ILE A 272 2803 2329 2208 235 -104 134 O -ATOM 2284 CB ILE A 272 -3.029 -38.463 38.847 1.00 19.50 C -ANISOU 2284 CB ILE A 272 2862 2317 2229 274 -143 101 C -ATOM 2285 CG1 ILE A 272 -2.500 -39.706 38.128 1.00 16.43 C -ANISOU 2285 CG1 ILE A 272 2468 1915 1861 247 -140 103 C -ATOM 2286 CG2 ILE A 272 -2.294 -38.231 40.142 1.00 23.80 C -ANISOU 2286 CG2 ILE A 272 3427 2860 2756 311 -164 85 C -ATOM 2287 CD1 ILE A 272 -1.009 -39.619 37.744 1.00 20.48 C -ANISOU 2287 CD1 ILE A 272 2977 2408 2398 244 -163 74 C -ATOM 2288 N LEU A 273 -5.855 -39.609 37.284 1.00 16.40 N -ANISOU 2288 N LEU A 273 2438 1960 1835 213 -83 160 N -ATOM 2289 CA LEU A 273 -6.372 -39.661 35.915 1.00 16.26 C -ANISOU 2289 CA LEU A 273 2394 1952 1831 176 -72 164 C -ATOM 2290 C LEU A 273 -7.742 -39.003 35.733 1.00 24.10 C -ANISOU 2290 C LEU A 273 3371 2976 2809 175 -55 185 C -ATOM 2291 O LEU A 273 -7.988 -38.357 34.716 1.00 26.12 O -ANISOU 2291 O LEU A 273 3607 3245 3072 160 -54 183 O -ATOM 2292 CB LEU A 273 -6.406 -41.099 35.399 1.00 22.71 C -ANISOU 2292 CB LEU A 273 3207 2762 2661 144 -60 169 C -ATOM 2293 CG LEU A 273 -6.874 -41.316 33.961 1.00 23.94 C -ANISOU 2293 CG LEU A 273 3336 2931 2830 103 -50 167 C -ATOM 2294 CD1 LEU A 273 -6.095 -40.435 32.990 1.00 23.68 C -ANISOU 2294 CD1 LEU A 273 3290 2895 2811 98 -65 147 C -ATOM 2295 CD2 LEU A 273 -6.763 -42.787 33.566 1.00 26.06 C -ANISOU 2295 CD2 LEU A 273 3605 3185 3113 73 -39 166 C -ATOM 2296 N GLY A 274 -8.637 -39.192 36.695 1.00 19.27 N -ANISOU 2296 N GLY A 274 2769 2378 2176 193 -42 207 N -ATOM 2297 CA GLY A 274 -9.977 -38.625 36.611 1.00 19.77 C -ANISOU 2297 CA GLY A 274 2816 2471 2223 195 -24 230 C -ATOM 2298 C GLY A 274 -10.826 -39.215 35.499 1.00 18.33 C -ANISOU 2298 C GLY A 274 2605 2311 2049 155 -9 242 C -ATOM 2299 O GLY A 274 -10.466 -40.235 34.914 1.00 19.30 O -ANISOU 2299 O GLY A 274 2723 2423 2188 124 -8 233 O -ATOM 2300 N ARG A 275 -11.973 -38.583 35.234 1.00 16.23 N -ANISOU 2300 N ARG A 275 2319 2079 1770 156 5 261 N -ATOM 2301 CA ARG A 275 -12.822 -38.918 34.090 1.00 15.31 C -ANISOU 2301 CA ARG A 275 2168 1991 1656 120 16 270 C -ATOM 2302 C ARG A 275 -12.916 -37.718 33.164 1.00 15.98 C -ANISOU 2302 C ARG A 275 2234 2096 1742 124 11 269 C -ATOM 2303 O ARG A 275 -13.203 -36.606 33.607 1.00 21.43 O -ANISOU 2303 O ARG A 275 2928 2793 2420 156 14 278 O -ATOM 2304 CB ARG A 275 -14.229 -39.337 34.542 1.00 18.34 C -ANISOU 2304 CB ARG A 275 2538 2404 2025 116 39 299 C -ATOM 2305 CG ARG A 275 -14.277 -40.674 35.268 1.00 23.99 C -ANISOU 2305 CG ARG A 275 3268 3102 2745 105 50 305 C -ATOM 2306 CD ARG A 275 -15.717 -41.203 35.330 1.00 24.86 C -ANISOU 2306 CD ARG A 275 3355 3244 2847 87 75 332 C -ATOM 2307 NE ARG A 275 -16.572 -40.403 36.204 1.00 20.86 N -ANISOU 2307 NE ARG A 275 2849 2759 2317 123 86 358 N -ATOM 2308 CZ ARG A 275 -17.884 -40.590 36.326 1.00 24.59 C -ANISOU 2308 CZ ARG A 275 3299 3265 2781 115 108 384 C -ATOM 2309 NH1 ARG A 275 -18.472 -41.552 35.632 1.00 24.74 N -ANISOU 2309 NH1 ARG A 275 3290 3298 2812 70 119 386 N -ATOM 2310 NH2 ARG A 275 -18.605 -39.829 37.144 1.00 17.81 N -ANISOU 2310 NH2 ARG A 275 2442 2424 1899 152 119 408 N -ATOM 2311 N HIS A 276 -12.696 -37.953 31.873 1.00 11.87 N -ANISOU 2311 N HIS A 276 1692 1585 1233 92 7 257 N -ATOM 2312 CA HIS A 276 -12.668 -36.889 30.885 1.00 12.28 C -ANISOU 2312 CA HIS A 276 1725 1654 1285 96 4 257 C -ATOM 2313 C HIS A 276 -13.342 -37.310 29.598 1.00 15.62 C -ANISOU 2313 C HIS A 276 2113 2116 1706 61 9 262 C -ATOM 2314 O HIS A 276 -13.107 -38.402 29.073 1.00 11.30 O -ANISOU 2314 O HIS A 276 1560 1564 1168 26 7 247 O -ATOM 2315 CB HIS A 276 -11.224 -36.498 30.577 1.00 16.69 C -ANISOU 2315 CB HIS A 276 2300 2178 1864 101 -13 232 C -ATOM 2316 CG HIS A 276 -10.451 -36.093 31.785 1.00 18.23 C -ANISOU 2316 CG HIS A 276 2527 2337 2062 133 -23 221 C -ATOM 2317 ND1 HIS A 276 -10.579 -34.848 32.361 1.00 15.88 N -ANISOU 2317 ND1 HIS A 276 2240 2037 1758 168 -21 227 N -ATOM 2318 CD2 HIS A 276 -9.541 -36.764 32.529 1.00 19.78 C -ANISOU 2318 CD2 HIS A 276 2749 2501 2267 136 -35 204 C -ATOM 2319 CE1 HIS A 276 -9.777 -34.768 33.407 1.00 18.06 C -ANISOU 2319 CE1 HIS A 276 2543 2281 2036 189 -33 211 C -ATOM 2320 NE2 HIS A 276 -9.137 -35.918 33.530 1.00 23.89 N -ANISOU 2320 NE2 HIS A 276 3291 3003 2783 171 -42 198 N -ATOM 2321 N SER A 277 -14.192 -36.431 29.092 1.00 11.47 N -ANISOU 2321 N SER A 277 1563 1629 1165 72 18 282 N -ATOM 2322 CA SER A 277 -14.809 -36.653 27.795 1.00 12.21 C -ANISOU 2322 CA SER A 277 1620 1768 1253 43 21 286 C -ATOM 2323 C SER A 277 -13.795 -36.429 26.685 1.00 16.92 C -ANISOU 2323 C SER A 277 2213 2353 1861 33 9 266 C -ATOM 2324 O SER A 277 -12.798 -35.710 26.871 1.00 17.78 O -ANISOU 2324 O SER A 277 2344 2428 1983 55 2 258 O -ATOM 2325 CB SER A 277 -15.974 -35.677 27.622 1.00 16.67 C -ANISOU 2325 CB SER A 277 2159 2380 1797 65 33 317 C -ATOM 2326 OG SER A 277 -15.486 -34.357 27.784 1.00 21.24 O -ANISOU 2326 OG SER A 277 2753 2940 2379 104 33 323 O -ATOM 2327 N ARG A 278 -14.032 -37.035 25.523 1.00 12.32 N -ANISOU 2327 N ARG A 278 1604 1802 1274 -1 8 258 N -ATOM 2328 CA ARG A 278 -13.207 -36.729 24.361 1.00 12.55 C -ANISOU 2328 CA ARG A 278 1627 1832 1310 -7 0 244 C -ATOM 2329 C ARG A 278 -13.596 -35.337 23.892 1.00 16.68 C -ANISOU 2329 C ARG A 278 2134 2384 1821 24 7 270 C -ATOM 2330 O ARG A 278 -14.783 -35.001 23.876 1.00 15.61 O -ANISOU 2330 O ARG A 278 1973 2292 1664 33 17 295 O -ATOM 2331 CB ARG A 278 -13.429 -37.754 23.248 1.00 15.01 C -ANISOU 2331 CB ARG A 278 1913 2173 1616 -50 -3 228 C -ATOM 2332 CG ARG A 278 -12.469 -37.612 22.065 1.00 15.25 C -ANISOU 2332 CG ARG A 278 1940 2201 1653 -58 -10 210 C -ATOM 2333 CD ARG A 278 -12.190 -38.990 21.457 1.00 15.79 C -ANISOU 2333 CD ARG A 278 2005 2266 1727 -102 -15 179 C -ATOM 2334 NE ARG A 278 -10.979 -39.019 20.633 1.00 22.77 N -ANISOU 2334 NE ARG A 278 2897 3129 2624 -107 -22 158 N -ATOM 2335 CZ ARG A 278 -10.279 -40.124 20.394 1.00 19.51 C -ANISOU 2335 CZ ARG A 278 2496 2690 2226 -135 -25 129 C -ATOM 2336 NH1 ARG A 278 -10.669 -41.274 20.929 1.00 17.53 N -ANISOU 2336 NH1 ARG A 278 2252 2427 1981 -162 -22 117 N -ATOM 2337 NH2 ARG A 278 -9.193 -40.087 19.630 1.00 16.75 N -ANISOU 2337 NH2 ARG A 278 2153 2324 1887 -137 -30 112 N -ATOM 2338 N LYS A 279 -12.614 -34.520 23.527 1.00 15.90 N -ANISOU 2338 N LYS A 279 2046 2260 1736 42 4 265 N -ATOM 2339 CA LYS A 279 -12.898 -33.142 23.113 1.00 19.66 C -ANISOU 2339 CA LYS A 279 2509 2755 2204 75 15 292 C -ATOM 2340 C LYS A 279 -12.930 -33.009 21.592 1.00 25.53 C -ANISOU 2340 C LYS A 279 3224 3540 2937 65 17 296 C -ATOM 2341 O LYS A 279 -12.280 -33.774 20.887 1.00 25.94 O -ANISOU 2341 O LYS A 279 3273 3587 2994 36 7 273 O -ATOM 2342 CB LYS A 279 -11.838 -32.188 23.666 1.00 12.05 C -ANISOU 2342 CB LYS A 279 1576 1738 1266 104 15 286 C -ATOM 2343 CG LYS A 279 -11.649 -32.222 25.171 1.00 11.59 C -ANISOU 2343 CG LYS A 279 1549 1638 1216 119 11 277 C -ATOM 2344 CD LYS A 279 -12.963 -32.139 25.954 1.00 16.74 C -ANISOU 2344 CD LYS A 279 2195 2318 1846 133 22 301 C -ATOM 2345 CE LYS A 279 -12.727 -32.098 27.472 1.00 17.42 C -ANISOU 2345 CE LYS A 279 2315 2365 1939 153 19 293 C -ATOM 2346 NZ LYS A 279 -12.103 -33.344 28.060 1.00 11.69 N -ANISOU 2346 NZ LYS A 279 1609 1612 1222 130 5 268 N -ATOM 2347 N ARG A 280 -13.671 -32.030 21.082 1.00 18.34 N -ANISOU 2347 N ARG A 280 2290 2670 2009 90 29 328 N -ATOM 2348 CA ARG A 280 -13.604 -31.723 19.654 1.00 17.01 C -ANISOU 2348 CA ARG A 280 2095 2540 1828 89 33 337 C -ATOM 2349 C ARG A 280 -12.442 -30.759 19.408 1.00 19.11 C -ANISOU 2349 C ARG A 280 2380 2762 2118 112 39 338 C -ATOM 2350 O ARG A 280 -12.166 -29.882 20.228 1.00 17.85 O -ANISOU 2350 O ARG A 280 2243 2562 1977 141 47 346 O -ATOM 2351 CB ARG A 280 -14.918 -31.132 19.154 1.00 19.93 C -ANISOU 2351 CB ARG A 280 2429 2977 2166 108 45 374 C -ATOM 2352 CG ARG A 280 -16.122 -32.016 19.469 1.00 19.67 C -ANISOU 2352 CG ARG A 280 2374 2988 2111 85 40 374 C -ATOM 2353 CD ARG A 280 -17.388 -31.493 18.852 1.00 21.61 C -ANISOU 2353 CD ARG A 280 2578 3308 2324 101 50 409 C -ATOM 2354 NE ARG A 280 -18.544 -32.185 19.405 1.00 22.34 N -ANISOU 2354 NE ARG A 280 2651 3434 2401 84 48 412 N -ATOM 2355 CZ ARG A 280 -19.076 -33.297 18.904 1.00 21.65 C -ANISOU 2355 CZ ARG A 280 2537 3390 2300 41 37 394 C -ATOM 2356 NH1 ARG A 280 -20.130 -33.844 19.500 1.00 24.34 N -ANISOU 2356 NH1 ARG A 280 2861 3757 2632 26 39 399 N -ATOM 2357 NH2 ARG A 280 -18.557 -33.859 17.817 1.00 20.23 N -ANISOU 2357 NH2 ARG A 280 2346 3225 2114 13 26 369 N -ATOM 2358 N TRP A 281 -11.771 -30.915 18.275 1.00 14.12 N -ANISOU 2358 N TRP A 281 1739 2139 1488 100 36 328 N -ATOM 2359 CA TRP A 281 -10.521 -30.183 18.049 1.00 16.44 C -ANISOU 2359 CA TRP A 281 2050 2385 1810 115 42 324 C -ATOM 2360 C TRP A 281 -10.728 -28.682 17.919 1.00 18.79 C -ANISOU 2360 C TRP A 281 2345 2683 2111 158 64 361 C -ATOM 2361 O TRP A 281 -9.796 -27.897 18.115 1.00 17.10 O -ANISOU 2361 O TRP A 281 2150 2418 1928 175 72 359 O -ATOM 2362 CB TRP A 281 -9.802 -30.721 16.814 1.00 17.65 C -ANISOU 2362 CB TRP A 281 2193 2552 1962 93 37 308 C -ATOM 2363 CG TRP A 281 -9.271 -32.078 17.027 1.00 17.73 C -ANISOU 2363 CG TRP A 281 2215 2542 1980 55 19 269 C -ATOM 2364 CD1 TRP A 281 -9.752 -33.240 16.498 1.00 16.72 C -ANISOU 2364 CD1 TRP A 281 2070 2453 1830 22 9 252 C -ATOM 2365 CD2 TRP A 281 -8.169 -32.438 17.865 1.00 15.93 C -ANISOU 2365 CD2 TRP A 281 2018 2249 1784 47 9 242 C -ATOM 2366 NE1 TRP A 281 -9.002 -34.304 16.945 1.00 21.00 N -ANISOU 2366 NE1 TRP A 281 2634 2954 2392 -6 -3 217 N -ATOM 2367 CE2 TRP A 281 -8.022 -33.835 17.784 1.00 17.81 C -ANISOU 2367 CE2 TRP A 281 2259 2488 2020 11 -4 212 C -ATOM 2368 CE3 TRP A 281 -7.283 -31.710 18.673 1.00 20.27 C -ANISOU 2368 CE3 TRP A 281 2595 2742 2367 68 10 238 C -ATOM 2369 CZ2 TRP A 281 -7.029 -34.520 18.475 1.00 14.31 C -ANISOU 2369 CZ2 TRP A 281 1842 1992 1603 -2 -15 184 C -ATOM 2370 CZ3 TRP A 281 -6.299 -32.394 19.362 1.00 20.78 C -ANISOU 2370 CZ3 TRP A 281 2683 2757 2456 53 -4 207 C -ATOM 2371 CH2 TRP A 281 -6.183 -33.788 19.261 1.00 20.51 C -ANISOU 2371 CH2 TRP A 281 2650 2726 2416 21 -16 183 C -ATOM 2372 N GLU A 282 -11.950 -28.294 17.577 1.00 17.72 N -ANISOU 2372 N GLU A 282 2182 2605 1945 175 75 394 N -ATOM 2373 CA GLU A 282 -12.283 -26.891 17.372 1.00 22.08 C -ANISOU 2373 CA GLU A 282 2729 3163 2497 219 100 434 C -ATOM 2374 C GLU A 282 -12.059 -26.035 18.619 1.00 18.02 C -ANISOU 2374 C GLU A 282 2246 2590 2012 245 110 435 C -ATOM 2375 O GLU A 282 -11.806 -24.835 18.523 1.00 21.37 O -ANISOU 2375 O GLU A 282 2678 2989 2454 277 131 457 O -ATOM 2376 CB GLU A 282 -13.731 -26.749 16.868 1.00 23.89 C -ANISOU 2376 CB GLU A 282 2921 3470 2685 234 108 469 C -ATOM 2377 CG GLU A 282 -13.923 -27.113 15.393 1.00 24.12 C -ANISOU 2377 CG GLU A 282 2915 3564 2684 223 105 477 C -ATOM 2378 CD GLU A 282 -14.131 -28.611 15.143 1.00 32.25 C -ANISOU 2378 CD GLU A 282 3931 4627 3695 174 80 442 C -ATOM 2379 OE1 GLU A 282 -14.075 -29.414 16.104 1.00 26.65 O -ANISOU 2379 OE1 GLU A 282 3240 3886 2998 148 66 414 O -ATOM 2380 OE2 GLU A 282 -14.355 -28.988 13.967 1.00 35.47 O -ANISOU 2380 OE2 GLU A 282 4309 5092 4074 162 75 443 O -ATOM 2381 N ARG A 283 -12.135 -26.635 19.794 1.00 18.51 N -ANISOU 2381 N ARG A 283 2328 2627 2080 231 95 412 N -ATOM 2382 CA ARG A 283 -11.917 -25.849 21.007 1.00 23.86 C -ANISOU 2382 CA ARG A 283 3035 3250 2780 256 103 409 C -ATOM 2383 C ARG A 283 -10.508 -25.245 21.094 1.00 19.13 C -ANISOU 2383 C ARG A 283 2461 2585 2221 260 105 389 C -ATOM 2384 O ARG A 283 -10.306 -24.280 21.810 1.00 17.24 O -ANISOU 2384 O ARG A 283 2242 2305 2003 285 117 390 O -ATOM 2385 CB ARG A 283 -12.217 -26.658 22.273 1.00 24.15 C -ANISOU 2385 CB ARG A 283 3089 3274 2811 242 87 387 C -ATOM 2386 CG ARG A 283 -11.326 -27.869 22.474 1.00 23.06 C -ANISOU 2386 CG ARG A 283 2964 3112 2685 204 62 348 C -ATOM 2387 CD ARG A 283 -10.992 -28.066 23.958 1.00 33.52 C -ANISOU 2387 CD ARG A 283 4322 4390 4023 207 52 325 C -ATOM 2388 NE ARG A 283 -12.183 -28.252 24.784 1.00 44.40 N -ANISOU 2388 NE ARG A 283 5698 5794 5378 217 56 340 N -ATOM 2389 CZ ARG A 283 -12.171 -28.318 26.114 1.00 40.28 C -ANISOU 2389 CZ ARG A 283 5202 5243 4859 228 51 328 C -ATOM 2390 NH1 ARG A 283 -11.033 -28.203 26.788 1.00 40.36 N -ANISOU 2390 NH1 ARG A 283 5241 5200 4893 229 40 299 N -ATOM 2391 NH2 ARG A 283 -13.303 -28.493 26.770 1.00 38.76 N -ANISOU 2391 NH2 ARG A 283 5006 5079 4644 237 58 346 N -ATOM 2392 N PHE A 284 -9.545 -25.808 20.370 1.00 18.17 N -ANISOU 2392 N PHE A 284 2337 2454 2111 234 94 368 N -ATOM 2393 CA PHE A 284 -8.174 -25.305 20.427 1.00 14.05 C -ANISOU 2393 CA PHE A 284 1835 1874 1631 234 95 348 C -ATOM 2394 C PHE A 284 -7.924 -24.208 19.401 1.00 16.47 C -ANISOU 2394 C PHE A 284 2129 2179 1949 257 121 377 C -ATOM 2395 O PHE A 284 -6.839 -23.639 19.340 1.00 20.06 O -ANISOU 2395 O PHE A 284 2596 2585 2440 259 128 365 O -ATOM 2396 CB PHE A 284 -7.194 -26.453 20.236 1.00 12.75 C -ANISOU 2396 CB PHE A 284 1675 1695 1475 198 71 312 C -ATOM 2397 CG PHE A 284 -7.348 -27.514 21.273 1.00 15.57 C -ANISOU 2397 CG PHE A 284 2046 2045 1823 179 49 287 C -ATOM 2398 CD1 PHE A 284 -6.951 -27.273 22.581 1.00 19.39 C -ANISOU 2398 CD1 PHE A 284 2558 2484 2326 188 41 267 C -ATOM 2399 CD2 PHE A 284 -7.938 -28.723 20.966 1.00 14.48 C -ANISOU 2399 CD2 PHE A 284 1894 1949 1658 153 37 283 C -ATOM 2400 CE1 PHE A 284 -7.109 -28.233 23.553 1.00 17.92 C -ANISOU 2400 CE1 PHE A 284 2385 2294 2130 175 23 248 C -ATOM 2401 CE2 PHE A 284 -8.094 -29.693 21.936 1.00 20.28 C -ANISOU 2401 CE2 PHE A 284 2642 2675 2388 137 21 263 C -ATOM 2402 CZ PHE A 284 -7.686 -29.449 23.232 1.00 19.51 C -ANISOU 2402 CZ PHE A 284 2573 2533 2307 150 14 248 C -ATOM 2403 N VAL A 285 -8.939 -23.919 18.598 1.00 17.01 N -ANISOU 2403 N VAL A 285 2172 2304 1988 274 137 415 N -ATOM 2404 CA VAL A 285 -8.831 -22.883 17.575 1.00 15.13 C -ANISOU 2404 CA VAL A 285 1920 2073 1756 300 166 450 C -ATOM 2405 C VAL A 285 -9.205 -21.525 18.144 1.00 19.44 C -ANISOU 2405 C VAL A 285 2478 2590 2318 340 194 476 C -ATOM 2406 O VAL A 285 -10.203 -21.396 18.843 1.00 25.56 O -ANISOU 2406 O VAL A 285 3254 3382 3075 356 196 488 O -ATOM 2407 CB VAL A 285 -9.760 -23.184 16.392 1.00 17.36 C -ANISOU 2407 CB VAL A 285 2167 2436 1994 304 171 482 C -ATOM 2408 CG1 VAL A 285 -9.635 -22.095 15.331 1.00 15.97 C -ANISOU 2408 CG1 VAL A 285 1977 2269 1822 337 203 523 C -ATOM 2409 CG2 VAL A 285 -9.456 -24.549 15.821 1.00 15.22 C -ANISOU 2409 CG2 VAL A 285 1885 2194 1706 264 144 453 C -ATOM 2410 N HIS A 286 -8.400 -20.510 17.848 1.00 15.71 N -ANISOU 2410 N HIS A 286 2015 2072 1883 356 218 484 N -ATOM 2411 CA HIS A 286 -8.680 -19.159 18.321 1.00 16.81 C -ANISOU 2411 CA HIS A 286 2168 2177 2044 394 249 507 C -ATOM 2412 C HIS A 286 -8.181 -18.144 17.297 1.00 18.14 C -ANISOU 2412 C HIS A 286 2328 2328 2235 416 284 539 C -ATOM 2413 O HIS A 286 -7.607 -18.528 16.274 1.00 21.26 O -ANISOU 2413 O HIS A 286 2708 2741 2628 402 282 542 O -ATOM 2414 CB HIS A 286 -8.066 -18.927 19.704 1.00 19.10 C -ANISOU 2414 CB HIS A 286 2492 2398 2369 387 239 467 C -ATOM 2415 CG HIS A 286 -6.617 -19.291 19.790 1.00 19.90 C -ANISOU 2415 CG HIS A 286 2605 2450 2505 356 221 424 C -ATOM 2416 ND1 HIS A 286 -5.653 -18.681 19.021 1.00 15.99 N -ANISOU 2416 ND1 HIS A 286 2107 1923 2045 356 240 429 N -ATOM 2417 CD2 HIS A 286 -5.969 -20.191 20.568 1.00 15.79 C -ANISOU 2417 CD2 HIS A 286 2099 1909 1991 325 187 378 C -ATOM 2418 CE1 HIS A 286 -4.471 -19.201 19.306 1.00 15.81 C -ANISOU 2418 CE1 HIS A 286 2094 1863 2049 326 217 387 C -ATOM 2419 NE2 HIS A 286 -4.636 -20.116 20.244 1.00 19.04 N -ANISOU 2419 NE2 HIS A 286 2515 2280 2441 308 185 355 N -ATOM 2420 N SER A 287 -8.404 -16.857 17.552 1.00 16.89 N -ANISOU 2420 N SER A 287 2180 2136 2100 452 319 565 N -ATOM 2421 CA SER A 287 -8.170 -15.850 16.518 1.00 20.35 C -ANISOU 2421 CA SER A 287 2608 2567 2556 480 359 607 C -ATOM 2422 C SER A 287 -6.711 -15.770 16.066 1.00 21.62 C -ANISOU 2422 C SER A 287 2776 2678 2761 458 362 585 C -ATOM 2423 O SER A 287 -6.420 -15.305 14.962 1.00 21.89 O -ANISOU 2423 O SER A 287 2796 2721 2803 473 389 619 O -ATOM 2424 CB SER A 287 -8.684 -14.483 16.969 1.00 32.23 C -ANISOU 2424 CB SER A 287 4126 4037 4081 524 400 637 C -ATOM 2425 OG SER A 287 -8.160 -14.143 18.238 1.00 46.24 O -ANISOU 2425 OG SER A 287 5934 5740 5895 514 394 594 O -ATOM 2426 N GLU A 288 -5.804 -16.247 16.911 1.00 17.86 N -ANISOU 2426 N GLU A 288 2319 2155 2313 424 334 531 N -ATOM 2427 CA GLU A 288 -4.370 -16.171 16.624 1.00 20.78 C -ANISOU 2427 CA GLU A 288 2694 2473 2728 402 335 506 C -ATOM 2428 C GLU A 288 -3.795 -17.389 15.907 1.00 22.45 C -ANISOU 2428 C GLU A 288 2890 2720 2921 369 307 488 C -ATOM 2429 O GLU A 288 -2.641 -17.354 15.475 1.00 25.72 O -ANISOU 2429 O GLU A 288 3304 3101 3370 353 310 474 O -ATOM 2430 CB GLU A 288 -3.574 -15.896 17.896 1.00 19.55 C -ANISOU 2430 CB GLU A 288 2567 2245 2618 385 323 456 C -ATOM 2431 CG GLU A 288 -3.702 -14.474 18.401 1.00 25.22 C -ANISOU 2431 CG GLU A 288 3302 2909 3372 414 360 468 C -ATOM 2432 CD GLU A 288 -5.077 -14.186 18.980 1.00 28.04 C -ANISOU 2432 CD GLU A 288 3665 3294 3696 445 368 491 C -ATOM 2433 OE1 GLU A 288 -5.539 -14.977 19.839 1.00 28.20 O -ANISOU 2433 OE1 GLU A 288 3692 3335 3687 433 334 465 O -ATOM 2434 OE2 GLU A 288 -5.690 -13.170 18.577 1.00 32.21 O -ANISOU 2434 OE2 GLU A 288 4190 3821 4228 483 409 537 O -ATOM 2435 N ASN A 289 -4.574 -18.463 15.789 1.00 17.01 N -ANISOU 2435 N ASN A 289 2188 2093 2180 358 280 487 N -ATOM 2436 CA ASN A 289 -4.109 -19.631 15.040 1.00 14.65 C -ANISOU 2436 CA ASN A 289 1875 1829 1862 328 256 470 C -ATOM 2437 C ASN A 289 -5.053 -20.086 13.921 1.00 17.87 C -ANISOU 2437 C ASN A 289 2254 2320 2216 338 259 505 C -ATOM 2438 O ASN A 289 -4.719 -20.995 13.165 1.00 20.11 O -ANISOU 2438 O ASN A 289 2524 2636 2480 315 243 493 O -ATOM 2439 CB ASN A 289 -3.796 -20.808 15.983 1.00 13.48 C -ANISOU 2439 CB ASN A 289 1740 1670 1711 292 214 419 C -ATOM 2440 CG ASN A 289 -5.048 -21.359 16.686 1.00 13.63 C -ANISOU 2440 CG ASN A 289 1760 1730 1690 294 196 419 C -ATOM 2441 OD1 ASN A 289 -6.176 -21.196 16.210 1.00 14.95 O -ANISOU 2441 OD1 ASN A 289 1909 1951 1821 314 208 455 O -ATOM 2442 ND2 ASN A 289 -4.841 -22.036 17.816 1.00 14.30 N -ANISOU 2442 ND2 ASN A 289 1863 1790 1779 273 168 379 N -ATOM 2443 N GLN A 290 -6.217 -19.447 13.798 1.00 16.88 N -ANISOU 2443 N GLN A 290 2118 2232 2065 371 279 547 N -ATOM 2444 CA GLN A 290 -7.253 -19.927 12.870 1.00 17.56 C -ANISOU 2444 CA GLN A 290 2174 2405 2094 380 276 577 C -ATOM 2445 C GLN A 290 -6.783 -19.966 11.405 1.00 19.52 C -ANISOU 2445 C GLN A 290 2400 2685 2330 383 290 598 C -ATOM 2446 O GLN A 290 -7.243 -20.786 10.606 1.00 20.97 O -ANISOU 2446 O GLN A 290 2561 2939 2468 373 274 600 O -ATOM 2447 CB GLN A 290 -8.534 -19.091 13.006 1.00 18.94 C -ANISOU 2447 CB GLN A 290 2339 2612 2247 421 299 622 C -ATOM 2448 CG GLN A 290 -8.395 -17.681 12.463 1.00 28.56 C -ANISOU 2448 CG GLN A 290 3557 3806 3488 464 346 670 C -ATOM 2449 CD GLN A 290 -9.456 -16.725 12.985 1.00 44.27 C -ANISOU 2449 CD GLN A 290 5548 5799 5472 506 371 706 C -ATOM 2450 OE1 GLN A 290 -10.498 -17.144 13.491 1.00 48.16 O -ANISOU 2450 OE1 GLN A 290 6033 6333 5931 507 355 706 O -ATOM 2451 NE2 GLN A 290 -9.186 -15.424 12.871 1.00 46.74 N -ANISOU 2451 NE2 GLN A 290 5872 6066 5822 541 414 739 N -ATOM 2452 N HIS A 291 -5.878 -19.069 11.049 1.00 22.27 N -ANISOU 2452 N HIS A 291 2757 2986 2720 398 319 613 N -ATOM 2453 CA HIS A 291 -5.339 -19.049 9.692 1.00 21.04 C -ANISOU 2453 CA HIS A 291 2583 2855 2555 405 336 634 C -ATOM 2454 C HIS A 291 -4.492 -20.299 9.375 1.00 22.80 C -ANISOU 2454 C HIS A 291 2805 3084 2774 362 305 589 C -ATOM 2455 O HIS A 291 -4.117 -20.524 8.221 1.00 21.85 O -ANISOU 2455 O HIS A 291 2669 2996 2637 363 312 601 O -ATOM 2456 CB HIS A 291 -4.511 -17.780 9.473 1.00 22.46 C -ANISOU 2456 CB HIS A 291 2773 2972 2787 429 378 660 C -ATOM 2457 CG HIS A 291 -3.267 -17.723 10.303 1.00 18.36 C -ANISOU 2457 CG HIS A 291 2279 2367 2328 401 371 616 C -ATOM 2458 ND1 HIS A 291 -3.288 -17.477 11.659 1.00 20.87 N -ANISOU 2458 ND1 HIS A 291 2621 2633 2676 393 360 587 N -ATOM 2459 CD2 HIS A 291 -1.967 -17.912 9.976 1.00 23.04 C -ANISOU 2459 CD2 HIS A 291 2875 2922 2956 379 371 594 C -ATOM 2460 CE1 HIS A 291 -2.054 -17.500 12.128 1.00 25.00 C -ANISOU 2460 CE1 HIS A 291 3159 3090 3248 368 353 549 C -ATOM 2461 NE2 HIS A 291 -1.232 -17.765 11.126 1.00 24.33 N -ANISOU 2461 NE2 HIS A 291 3061 3013 3169 358 359 552 N -ATOM 2462 N LEU A 292 -4.186 -21.097 10.396 1.00 18.11 N -ANISOU 2462 N LEU A 292 2230 2458 2195 327 271 539 N -ATOM 2463 CA LEU A 292 -3.398 -22.322 10.213 1.00 20.91 C -ANISOU 2463 CA LEU A 292 2586 2812 2548 287 243 496 C -ATOM 2464 C LEU A 292 -4.297 -23.557 10.264 1.00 22.19 C -ANISOU 2464 C LEU A 292 2737 3034 2660 265 210 476 C -ATOM 2465 O LEU A 292 -3.842 -24.690 10.064 1.00 18.70 O -ANISOU 2465 O LEU A 292 2295 2600 2209 232 187 441 O -ATOM 2466 CB LEU A 292 -2.331 -22.431 11.299 1.00 18.13 C -ANISOU 2466 CB LEU A 292 2260 2382 2247 264 228 453 C -ATOM 2467 CG LEU A 292 -1.379 -21.236 11.400 1.00 20.31 C -ANISOU 2467 CG LEU A 292 2547 2592 2580 279 258 463 C -ATOM 2468 CD1 LEU A 292 -0.432 -21.394 12.571 1.00 16.41 C -ANISOU 2468 CD1 LEU A 292 2076 2029 2132 255 238 417 C -ATOM 2469 CD2 LEU A 292 -0.606 -21.064 10.098 1.00 21.98 C -ANISOU 2469 CD2 LEU A 292 2743 2811 2799 285 281 483 C -ATOM 2470 N VAL A 293 -5.577 -23.332 10.528 1.00 17.53 N -ANISOU 2470 N VAL A 293 2137 2484 2039 282 211 499 N -ATOM 2471 CA VAL A 293 -6.515 -24.428 10.739 1.00 15.85 C -ANISOU 2471 CA VAL A 293 1914 2324 1784 259 183 480 C -ATOM 2472 C VAL A 293 -7.551 -24.489 9.629 1.00 17.89 C -ANISOU 2472 C VAL A 293 2138 2671 1988 274 188 512 C -ATOM 2473 O VAL A 293 -8.038 -23.473 9.146 1.00 25.60 O -ANISOU 2473 O VAL A 293 3101 3672 2953 314 215 559 O -ATOM 2474 CB VAL A 293 -7.238 -24.317 12.112 1.00 18.48 C -ANISOU 2474 CB VAL A 293 2261 2636 2124 261 173 474 C -ATOM 2475 CG1 VAL A 293 -8.172 -25.501 12.336 1.00 25.32 C -ANISOU 2475 CG1 VAL A 293 3117 3554 2952 235 146 454 C -ATOM 2476 CG2 VAL A 293 -6.238 -24.232 13.244 1.00 19.51 C -ANISOU 2476 CG2 VAL A 293 2425 2684 2304 249 166 441 C -ATOM 2477 N SER A 294 -7.879 -25.702 9.231 1.00 20.35 N -ANISOU 2477 N SER A 294 2436 3032 2265 243 163 486 N -ATOM 2478 CA SER A 294 -8.859 -25.933 8.198 1.00 21.02 C -ANISOU 2478 CA SER A 294 2485 3208 2293 251 162 507 C -ATOM 2479 C SER A 294 -9.530 -27.226 8.589 1.00 20.12 C -ANISOU 2479 C SER A 294 2365 3125 2155 211 130 469 C -ATOM 2480 O SER A 294 -8.993 -27.968 9.403 1.00 17.73 O -ANISOU 2480 O SER A 294 2085 2772 1880 179 113 429 O -ATOM 2481 CB SER A 294 -8.160 -26.082 6.841 1.00 21.16 C -ANISOU 2481 CB SER A 294 2491 3253 2297 251 170 509 C -ATOM 2482 OG SER A 294 -7.153 -27.082 6.890 1.00 18.82 O -ANISOU 2482 OG SER A 294 2212 2920 2020 212 152 460 O -ATOM 2483 N PRO A 295 -10.704 -27.511 8.017 1.00 21.46 N -ANISOU 2483 N PRO A 295 2501 3379 2275 212 123 482 N -ATOM 2484 CA PRO A 295 -11.323 -28.808 8.297 1.00 18.83 C -ANISOU 2484 CA PRO A 295 2159 3076 1921 169 94 443 C -ATOM 2485 C PRO A 295 -10.376 -29.955 7.936 1.00 20.45 C -ANISOU 2485 C PRO A 295 2376 3259 2134 128 78 394 C -ATOM 2486 O PRO A 295 -10.314 -30.946 8.660 1.00 14.43 O -ANISOU 2486 O PRO A 295 1628 2469 1386 91 59 355 O -ATOM 2487 CB PRO A 295 -12.551 -28.812 7.380 1.00 22.58 C -ANISOU 2487 CB PRO A 295 2590 3652 2339 180 92 467 C -ATOM 2488 CG PRO A 295 -12.860 -27.352 7.173 1.00 26.98 C -ANISOU 2488 CG PRO A 295 3137 4221 2891 236 121 526 C -ATOM 2489 CD PRO A 295 -11.528 -26.673 7.123 1.00 23.95 C -ANISOU 2489 CD PRO A 295 2783 3765 2551 253 141 533 C -ATOM 2490 N GLU A 296 -9.656 -29.816 6.826 1.00 18.47 N -ANISOU 2490 N GLU A 296 2120 3023 1876 136 87 397 N -ATOM 2491 CA GLU A 296 -8.674 -30.821 6.409 1.00 15.13 C -ANISOU 2491 CA GLU A 296 1709 2577 1461 102 76 353 C -ATOM 2492 C GLU A 296 -7.577 -31.050 7.450 1.00 13.28 C -ANISOU 2492 C GLU A 296 1514 2250 1283 86 72 326 C -ATOM 2493 O GLU A 296 -7.228 -32.197 7.727 1.00 16.78 O -ANISOU 2493 O GLU A 296 1970 2672 1736 49 55 283 O -ATOM 2494 CB GLU A 296 -8.040 -30.457 5.067 1.00 19.47 C -ANISOU 2494 CB GLU A 296 2248 3155 1995 121 91 368 C -ATOM 2495 CG GLU A 296 -8.990 -30.591 3.886 1.00 19.29 C -ANISOU 2495 CG GLU A 296 2186 3235 1909 128 88 381 C -ATOM 2496 CD GLU A 296 -9.898 -29.395 3.724 1.00 31.25 C -ANISOU 2496 CD GLU A 296 3677 4794 3401 175 106 439 C -ATOM 2497 OE1 GLU A 296 -9.616 -28.335 4.327 1.00 25.80 O -ANISOU 2497 OE1 GLU A 296 3005 4052 2747 206 127 472 O -ATOM 2498 OE2 GLU A 296 -10.900 -29.522 2.985 1.00 30.89 O -ANISOU 2498 OE2 GLU A 296 3596 4837 3302 180 99 450 O -ATOM 2499 N ALA A 297 -7.042 -29.972 8.027 1.00 16.22 N -ANISOU 2499 N ALA A 297 1903 2566 1692 115 89 351 N -ATOM 2500 CA ALA A 297 -6.010 -30.101 9.067 1.00 15.01 C -ANISOU 2500 CA ALA A 297 1784 2328 1591 103 84 326 C -ATOM 2501 C ALA A 297 -6.546 -30.827 10.295 1.00 16.97 C -ANISOU 2501 C ALA A 297 2045 2558 1845 80 64 302 C -ATOM 2502 O ALA A 297 -5.874 -31.700 10.841 1.00 14.90 O -ANISOU 2502 O ALA A 297 1803 2253 1605 52 50 265 O -ATOM 2503 CB ALA A 297 -5.459 -28.741 9.470 1.00 10.57 C -ANISOU 2503 CB ALA A 297 1235 1715 1066 138 106 356 C -ATOM 2504 N LEU A 298 -7.753 -30.467 10.734 1.00 17.46 N -ANISOU 2504 N LEU A 298 2095 2652 1887 92 65 325 N -ATOM 2505 CA LEU A 298 -8.337 -31.094 11.918 1.00 15.81 C -ANISOU 2505 CA LEU A 298 1897 2428 1682 73 49 307 C -ATOM 2506 C LEU A 298 -8.621 -32.578 11.694 1.00 20.87 C -ANISOU 2506 C LEU A 298 2531 3096 2304 30 30 270 C -ATOM 2507 O LEU A 298 -8.366 -33.406 12.573 1.00 18.70 O -ANISOU 2507 O LEU A 298 2276 2780 2048 6 17 240 O -ATOM 2508 CB LEU A 298 -9.582 -30.348 12.392 1.00 15.69 C -ANISOU 2508 CB LEU A 298 1869 2444 1650 99 58 342 C -ATOM 2509 CG LEU A 298 -9.293 -28.912 12.841 1.00 17.81 C -ANISOU 2509 CG LEU A 298 2152 2673 1945 141 79 374 C -ATOM 2510 CD1 LEU A 298 -10.552 -28.260 13.397 1.00 17.28 C -ANISOU 2510 CD1 LEU A 298 2073 2633 1860 166 87 406 C -ATOM 2511 CD2 LEU A 298 -8.190 -28.912 13.876 1.00 21.82 C -ANISOU 2511 CD2 LEU A 298 2695 3098 2499 134 73 348 C -ATOM 2512 N ASP A 299 -9.107 -32.930 10.512 1.00 15.45 N -ANISOU 2512 N ASP A 299 1816 2476 1580 21 28 269 N -ATOM 2513 CA ASP A 299 -9.361 -34.332 10.236 1.00 17.28 C -ANISOU 2513 CA ASP A 299 2040 2732 1795 -23 12 230 C -ATOM 2514 C ASP A 299 -8.050 -35.116 10.185 1.00 20.94 C -ANISOU 2514 C ASP A 299 2530 3141 2287 -46 7 192 C -ATOM 2515 O ASP A 299 -7.965 -36.223 10.689 1.00 16.04 O -ANISOU 2515 O ASP A 299 1922 2495 1677 -78 -5 159 O -ATOM 2516 CB ASP A 299 -10.146 -34.524 8.940 1.00 20.75 C -ANISOU 2516 CB ASP A 299 2441 3258 2184 -29 10 233 C -ATOM 2517 CG ASP A 299 -10.443 -35.986 8.665 1.00 24.08 C -ANISOU 2517 CG ASP A 299 2856 3703 2592 -78 -7 187 C -ATOM 2518 OD1 ASP A 299 -11.171 -36.611 9.464 1.00 24.36 O -ANISOU 2518 OD1 ASP A 299 2890 3735 2631 -101 -15 175 O -ATOM 2519 OD2 ASP A 299 -9.942 -36.520 7.664 1.00 18.58 O -ANISOU 2519 OD2 ASP A 299 2153 3024 1881 -94 -9 163 O -ATOM 2520 N PHE A 300 -7.029 -34.531 9.572 1.00 13.76 N -ANISOU 2520 N PHE A 300 1626 2212 1390 -26 18 201 N -ATOM 2521 CA PHE A 300 -5.727 -35.197 9.463 1.00 12.88 C -ANISOU 2521 CA PHE A 300 1537 2051 1306 -43 15 168 C -ATOM 2522 C PHE A 300 -5.151 -35.408 10.852 1.00 13.21 C -ANISOU 2522 C PHE A 300 1610 2020 1390 -48 8 155 C -ATOM 2523 O PHE A 300 -4.756 -36.511 11.189 1.00 12.95 O -ANISOU 2523 O PHE A 300 1592 1958 1369 -76 -2 121 O -ATOM 2524 CB PHE A 300 -4.785 -34.367 8.607 1.00 13.01 C -ANISOU 2524 CB PHE A 300 1551 2061 1330 -18 31 186 C -ATOM 2525 CG PHE A 300 -3.400 -34.936 8.494 1.00 14.47 C -ANISOU 2525 CG PHE A 300 1757 2196 1546 -31 31 157 C -ATOM 2526 CD1 PHE A 300 -3.216 -36.289 8.269 1.00 13.16 C -ANISOU 2526 CD1 PHE A 300 1596 2030 1374 -66 19 116 C -ATOM 2527 CD2 PHE A 300 -2.289 -34.116 8.604 1.00 16.21 C -ANISOU 2527 CD2 PHE A 300 1990 2367 1802 -9 43 171 C -ATOM 2528 CE1 PHE A 300 -1.939 -36.818 8.150 1.00 18.29 C -ANISOU 2528 CE1 PHE A 300 2265 2635 2051 -75 20 91 C -ATOM 2529 CE2 PHE A 300 -1.004 -34.645 8.491 1.00 16.16 C -ANISOU 2529 CE2 PHE A 300 1999 2317 1824 -20 42 145 C -ATOM 2530 CZ PHE A 300 -0.837 -35.988 8.272 1.00 15.65 C -ANISOU 2530 CZ PHE A 300 1940 2256 1751 -51 31 107 C -ATOM 2531 N LEU A 301 -5.119 -34.352 11.659 1.00 13.73 N -ANISOU 2531 N LEU A 301 1686 2056 1477 -20 15 181 N -ATOM 2532 CA LEU A 301 -4.614 -34.454 13.029 1.00 12.83 C -ANISOU 2532 CA LEU A 301 1600 1878 1398 -21 7 169 C -ATOM 2533 C LEU A 301 -5.380 -35.517 13.809 1.00 14.49 C -ANISOU 2533 C LEU A 301 1816 2092 1599 -47 -6 150 C -ATOM 2534 O LEU A 301 -4.781 -36.352 14.497 1.00 13.42 O -ANISOU 2534 O LEU A 301 1701 1913 1485 -64 -15 124 O -ATOM 2535 CB LEU A 301 -4.721 -33.109 13.746 1.00 13.19 C -ANISOU 2535 CB LEU A 301 1651 1901 1459 14 16 199 C -ATOM 2536 CG LEU A 301 -4.337 -33.111 15.227 1.00 15.24 C -ANISOU 2536 CG LEU A 301 1938 2102 1749 16 7 187 C -ATOM 2537 CD1 LEU A 301 -2.839 -33.453 15.417 1.00 11.44 C -ANISOU 2537 CD1 LEU A 301 1477 1565 1304 8 1 160 C -ATOM 2538 CD2 LEU A 301 -4.686 -31.755 15.867 1.00 16.30 C -ANISOU 2538 CD2 LEU A 301 2077 2224 1893 50 18 216 C -ATOM 2539 N ASP A 302 -6.709 -35.476 13.696 1.00 11.08 N -ANISOU 2539 N ASP A 302 1361 1712 1135 -48 -6 166 N -ATOM 2540 CA ASP A 302 -7.570 -36.438 14.370 1.00 12.93 C -ANISOU 2540 CA ASP A 302 1596 1956 1360 -74 -15 152 C -ATOM 2541 C ASP A 302 -7.205 -37.876 14.023 1.00 14.36 C -ANISOU 2541 C ASP A 302 1783 2130 1543 -113 -22 112 C -ATOM 2542 O ASP A 302 -7.375 -38.778 14.838 1.00 14.26 O -ANISOU 2542 O ASP A 302 1784 2093 1541 -133 -28 95 O -ATOM 2543 CB ASP A 302 -9.031 -36.198 13.981 1.00 16.89 C -ANISOU 2543 CB ASP A 302 2065 2528 1824 -72 -12 173 C -ATOM 2544 CG ASP A 302 -9.992 -36.992 14.840 1.00 23.97 C -ANISOU 2544 CG ASP A 302 2961 3431 2715 -94 -18 166 C -ATOM 2545 OD1 ASP A 302 -9.848 -36.948 16.076 1.00 18.24 O -ANISOU 2545 OD1 ASP A 302 2259 2659 2011 -86 -19 168 O -ATOM 2546 OD2 ASP A 302 -10.873 -37.676 14.276 1.00 22.53 O -ANISOU 2546 OD2 ASP A 302 2753 3300 2507 -121 -22 156 O -ATOM 2547 N LYS A 303 -6.727 -38.090 12.798 1.00 13.25 N -ANISOU 2547 N LYS A 303 1631 2011 1392 -122 -20 99 N -ATOM 2548 CA LYS A 303 -6.422 -39.432 12.327 1.00 7.65 C -ANISOU 2548 CA LYS A 303 926 1298 682 -159 -25 60 C -ATOM 2549 C LYS A 303 -4.999 -39.873 12.681 1.00 10.87 C -ANISOU 2549 C LYS A 303 1364 1639 1127 -160 -26 39 C -ATOM 2550 O LYS A 303 -4.669 -41.047 12.555 1.00 12.84 O -ANISOU 2550 O LYS A 303 1624 1871 1383 -188 -28 7 O -ATOM 2551 CB LYS A 303 -6.667 -39.535 10.817 1.00 9.15 C -ANISOU 2551 CB LYS A 303 1089 1550 838 -169 -23 52 C -ATOM 2552 CG LYS A 303 -8.162 -39.570 10.453 1.00 15.23 C -ANISOU 2552 CG LYS A 303 1826 2394 1569 -180 -27 61 C -ATOM 2553 CD LYS A 303 -8.372 -39.403 8.956 1.00 24.26 C -ANISOU 2553 CD LYS A 303 2940 3605 2674 -180 -25 59 C -ATOM 2554 CE LYS A 303 -9.761 -39.859 8.543 1.00 23.95 C -ANISOU 2554 CE LYS A 303 2866 3638 2595 -204 -33 52 C -ATOM 2555 NZ LYS A 303 -10.780 -39.395 9.526 1.00 25.12 N -ANISOU 2555 NZ LYS A 303 3006 3794 2744 -193 -34 80 N -ATOM 2556 N LEU A 304 -4.166 -38.936 13.132 1.00 14.49 N -ANISOU 2556 N LEU A 304 1836 2059 1609 -130 -23 57 N -ATOM 2557 CA LEU A 304 -2.828 -39.277 13.625 1.00 14.62 C -ANISOU 2557 CA LEU A 304 1880 2014 1663 -128 -25 39 C -ATOM 2558 C LEU A 304 -2.880 -39.565 15.129 1.00 15.95 C -ANISOU 2558 C LEU A 304 2070 2139 1851 -126 -33 38 C -ATOM 2559 O LEU A 304 -2.313 -40.546 15.612 1.00 11.66 O -ANISOU 2559 O LEU A 304 1546 1558 1326 -140 -37 16 O -ATOM 2560 CB LEU A 304 -1.850 -38.131 13.367 1.00 11.76 C -ANISOU 2560 CB LEU A 304 1518 1631 1319 -99 -19 56 C -ATOM 2561 CG LEU A 304 -1.496 -37.772 11.918 1.00 12.22 C -ANISOU 2561 CG LEU A 304 1558 1723 1363 -94 -8 61 C -ATOM 2562 CD1 LEU A 304 -0.530 -36.593 11.885 1.00 14.93 C -ANISOU 2562 CD1 LEU A 304 1903 2035 1732 -64 1 81 C -ATOM 2563 CD2 LEU A 304 -0.901 -38.969 11.197 1.00 16.97 C -ANISOU 2563 CD2 LEU A 304 2164 2322 1963 -119 -9 27 C -ATOM 2564 N LEU A 305 -3.570 -38.698 15.863 1.00 9.26 N -ANISOU 2564 N LEU A 305 1220 1298 999 -106 -33 64 N -ATOM 2565 CA LEU A 305 -3.639 -38.809 17.314 1.00 8.11 C -ANISOU 2565 CA LEU A 305 1096 1117 869 -98 -40 65 C -ATOM 2566 C LEU A 305 -4.734 -39.772 17.778 1.00 13.02 C -ANISOU 2566 C LEU A 305 1717 1756 1475 -121 -41 61 C -ATOM 2567 O LEU A 305 -5.809 -39.345 18.230 1.00 14.69 O -ANISOU 2567 O LEU A 305 1918 1992 1670 -114 -39 81 O -ATOM 2568 CB LEU A 305 -3.798 -37.424 17.948 1.00 13.54 C -ANISOU 2568 CB LEU A 305 1785 1799 1561 -65 -38 92 C -ATOM 2569 CG LEU A 305 -2.624 -36.455 17.713 1.00 13.78 C -ANISOU 2569 CG LEU A 305 1820 1801 1616 -43 -36 95 C -ATOM 2570 CD1 LEU A 305 -2.843 -35.123 18.411 1.00 14.01 C -ANISOU 2570 CD1 LEU A 305 1852 1819 1651 -12 -32 118 C -ATOM 2571 CD2 LEU A 305 -1.271 -37.086 18.148 1.00 11.71 C -ANISOU 2571 CD2 LEU A 305 1578 1487 1383 -48 -45 69 C -ATOM 2572 N ARG A 306 -4.460 -41.066 17.633 1.00 11.77 N -ANISOU 2572 N ARG A 306 1567 1583 1324 -149 -41 34 N -ATOM 2573 CA ARG A 306 -5.316 -42.134 18.165 1.00 16.22 C -ANISOU 2573 CA ARG A 306 2132 2149 1880 -174 -39 26 C -ATOM 2574 C ARG A 306 -4.569 -42.875 19.267 1.00 15.18 C -ANISOU 2574 C ARG A 306 2032 1960 1776 -171 -41 16 C -ATOM 2575 O ARG A 306 -3.367 -43.138 19.130 1.00 12.13 O -ANISOU 2575 O ARG A 306 1660 1539 1409 -168 -43 1 O -ATOM 2576 CB ARG A 306 -5.685 -43.156 17.079 1.00 16.18 C -ANISOU 2576 CB ARG A 306 2113 2173 1863 -213 -34 1 C -ATOM 2577 CG ARG A 306 -5.997 -42.602 15.698 1.00 20.67 C -ANISOU 2577 CG ARG A 306 2652 2797 2405 -216 -34 3 C -ATOM 2578 CD ARG A 306 -7.187 -41.648 15.685 1.00 14.86 C -ANISOU 2578 CD ARG A 306 1891 2113 1643 -202 -34 33 C -ATOM 2579 NE ARG A 306 -8.367 -42.186 16.360 1.00 16.74 N -ANISOU 2579 NE ARG A 306 2121 2366 1873 -219 -32 36 N -ATOM 2580 CZ ARG A 306 -9.517 -41.524 16.470 1.00 23.86 C -ANISOU 2580 CZ ARG A 306 3001 3313 2753 -210 -31 62 C -ATOM 2581 NH1 ARG A 306 -9.652 -40.307 15.949 1.00 19.50 N -ANISOU 2581 NH1 ARG A 306 2431 2794 2183 -181 -31 87 N -ATOM 2582 NH2 ARG A 306 -10.539 -42.074 17.105 1.00 23.47 N -ANISOU 2582 NH2 ARG A 306 2945 3276 2699 -227 -28 65 N -ATOM 2583 N TYR A 307 -5.257 -43.228 20.356 1.00 15.70 N -ANISOU 2583 N TYR A 307 2107 2017 1841 -171 -38 26 N -ATOM 2584 CA TYR A 307 -4.615 -44.043 21.391 1.00 13.78 C -ANISOU 2584 CA TYR A 307 1893 1724 1619 -167 -38 19 C -ATOM 2585 C TYR A 307 -4.084 -45.320 20.743 1.00 16.10 C -ANISOU 2585 C TYR A 307 2193 1998 1926 -196 -31 -9 C -ATOM 2586 O TYR A 307 -2.914 -45.666 20.883 1.00 14.00 O -ANISOU 2586 O TYR A 307 1946 1694 1681 -188 -34 -21 O -ATOM 2587 CB TYR A 307 -5.608 -44.448 22.482 1.00 14.89 C -ANISOU 2587 CB TYR A 307 2040 1865 1754 -169 -32 34 C -ATOM 2588 CG TYR A 307 -5.969 -43.379 23.492 1.00 9.87 C -ANISOU 2588 CG TYR A 307 1407 1232 1109 -135 -37 60 C -ATOM 2589 CD1 TYR A 307 -4.993 -42.796 24.299 1.00 9.86 C -ANISOU 2589 CD1 TYR A 307 1427 1198 1121 -102 -47 63 C -ATOM 2590 CD2 TYR A 307 -7.291 -42.988 23.670 1.00 11.28 C -ANISOU 2590 CD2 TYR A 307 1570 1450 1268 -135 -31 80 C -ATOM 2591 CE1 TYR A 307 -5.319 -41.839 25.243 1.00 10.50 C -ANISOU 2591 CE1 TYR A 307 1514 1283 1194 -71 -52 82 C -ATOM 2592 CE2 TYR A 307 -7.634 -42.031 24.620 1.00 12.82 C -ANISOU 2592 CE2 TYR A 307 1770 1647 1454 -103 -34 103 C -ATOM 2593 CZ TYR A 307 -6.642 -41.463 25.399 1.00 11.41 C -ANISOU 2593 CZ TYR A 307 1614 1433 1287 -71 -44 102 C -ATOM 2594 OH TYR A 307 -6.962 -40.519 26.329 1.00 14.50 O -ANISOU 2594 OH TYR A 307 2013 1826 1670 -39 -46 121 O -ATOM 2595 N ASP A 308 -4.967 -46.017 20.031 1.00 11.03 N -ANISOU 2595 N ASP A 308 1534 1385 1271 -231 -22 -21 N -ATOM 2596 CA ASP A 308 -4.633 -47.309 19.425 1.00 9.46 C -ANISOU 2596 CA ASP A 308 1342 1168 1084 -263 -13 -51 C -ATOM 2597 C ASP A 308 -3.653 -47.133 18.271 1.00 10.89 C -ANISOU 2597 C ASP A 308 1519 1351 1267 -263 -16 -70 C -ATOM 2598 O ASP A 308 -4.006 -46.597 17.222 1.00 14.36 O -ANISOU 2598 O ASP A 308 1934 1836 1686 -270 -19 -73 O -ATOM 2599 CB ASP A 308 -5.909 -48.009 18.928 1.00 11.30 C -ANISOU 2599 CB ASP A 308 1554 1435 1303 -304 -3 -63 C -ATOM 2600 CG ASP A 308 -5.679 -49.471 18.592 1.00 19.77 C -ANISOU 2600 CG ASP A 308 2640 2479 2394 -339 11 -95 C -ATOM 2601 OD1 ASP A 308 -4.509 -49.861 18.416 1.00 16.78 O -ANISOU 2601 OD1 ASP A 308 2280 2063 2033 -331 13 -109 O -ATOM 2602 OD2 ASP A 308 -6.665 -50.237 18.523 1.00 17.40 O -ANISOU 2602 OD2 ASP A 308 2329 2193 2091 -373 22 -105 O -ATOM 2603 N HIS A 309 -2.412 -47.571 18.477 1.00 13.38 N -ANISOU 2603 N HIS A 309 1857 1620 1607 -252 -15 -81 N -ATOM 2604 CA HIS A 309 -1.360 -47.394 17.481 1.00 11.12 C -ANISOU 2604 CA HIS A 309 1568 1331 1326 -248 -17 -96 C -ATOM 2605 C HIS A 309 -1.730 -48.055 16.154 1.00 11.53 C -ANISOU 2605 C HIS A 309 1605 1412 1363 -283 -9 -124 C -ATOM 2606 O HIS A 309 -1.319 -47.593 15.094 1.00 16.33 O -ANISOU 2606 O HIS A 309 2200 2045 1961 -280 -10 -131 O -ATOM 2607 CB HIS A 309 -0.036 -47.950 17.998 1.00 10.39 C -ANISOU 2607 CB HIS A 309 1501 1184 1263 -232 -16 -104 C -ATOM 2608 CG HIS A 309 -0.130 -49.357 18.522 1.00 13.59 C -ANISOU 2608 CG HIS A 309 1927 1553 1683 -250 -2 -116 C -ATOM 2609 ND1 HIS A 309 -0.571 -49.655 19.796 1.00 12.91 N -ANISOU 2609 ND1 HIS A 309 1855 1447 1604 -242 0 -99 N -ATOM 2610 CD2 HIS A 309 0.165 -50.547 17.944 1.00 12.13 C -ANISOU 2610 CD2 HIS A 309 1751 1347 1510 -274 13 -143 C -ATOM 2611 CE1 HIS A 309 -0.528 -50.961 19.983 1.00 15.80 C -ANISOU 2611 CE1 HIS A 309 2238 1779 1985 -260 17 -113 C -ATOM 2612 NE2 HIS A 309 -0.077 -51.526 18.875 1.00 12.85 N -ANISOU 2612 NE2 HIS A 309 1863 1404 1617 -280 25 -141 N -ATOM 2613 N GLN A 310 -2.534 -49.116 16.221 1.00 12.00 N -ANISOU 2613 N GLN A 310 1666 1472 1422 -316 2 -140 N -ATOM 2614 CA GLN A 310 -2.998 -49.806 15.021 1.00 13.71 C -ANISOU 2614 CA GLN A 310 1868 1719 1624 -353 9 -171 C -ATOM 2615 C GLN A 310 -4.025 -48.983 14.230 1.00 17.52 C -ANISOU 2615 C GLN A 310 2316 2272 2070 -361 0 -164 C -ATOM 2616 O GLN A 310 -4.256 -49.246 13.056 1.00 21.80 O -ANISOU 2616 O GLN A 310 2840 2851 2592 -384 2 -189 O -ATOM 2617 CB GLN A 310 -3.604 -51.169 15.378 1.00 16.55 C -ANISOU 2617 CB GLN A 310 2238 2055 1997 -389 24 -192 C -ATOM 2618 CG GLN A 310 -2.585 -52.221 15.828 1.00 16.02 C -ANISOU 2618 CG GLN A 310 2204 1920 1964 -387 38 -205 C -ATOM 2619 CD GLN A 310 -3.238 -53.565 16.137 1.00 22.15 C -ANISOU 2619 CD GLN A 310 2990 2670 2755 -424 58 -224 C -ATOM 2620 OE1 GLN A 310 -4.403 -53.792 15.807 1.00 23.71 O -ANISOU 2620 OE1 GLN A 310 3168 2903 2939 -458 61 -235 O -ATOM 2621 NE2 GLN A 310 -2.486 -54.464 16.768 1.00 20.70 N -ANISOU 2621 NE2 GLN A 310 2837 2425 2603 -417 74 -227 N -ATOM 2622 N SER A 311 -4.638 -47.996 14.871 1.00 16.22 N -ANISOU 2622 N SER A 311 2141 2129 1895 -339 -8 -131 N -ATOM 2623 CA SER A 311 -5.673 -47.184 14.217 1.00 17.81 C -ANISOU 2623 CA SER A 311 2308 2398 2062 -341 -15 -118 C -ATOM 2624 C SER A 311 -5.134 -45.910 13.556 1.00 15.40 C -ANISOU 2624 C SER A 311 1991 2118 1743 -308 -22 -100 C -ATOM 2625 O SER A 311 -5.857 -45.220 12.819 1.00 16.17 O -ANISOU 2625 O SER A 311 2060 2275 1809 -306 -25 -88 O -ATOM 2626 CB SER A 311 -6.769 -46.814 15.222 1.00 19.97 C -ANISOU 2626 CB SER A 311 2574 2685 2330 -335 -17 -91 C -ATOM 2627 OG SER A 311 -7.411 -47.976 15.708 1.00 20.18 O -ANISOU 2627 OG SER A 311 2604 2695 2367 -369 -7 -106 O -ATOM 2628 N ARG A 312 -3.875 -45.584 13.820 1.00 11.53 N -ANISOU 2628 N ARG A 312 1521 1583 1275 -282 -22 -94 N -ATOM 2629 CA ARG A 312 -3.304 -44.364 13.260 1.00 17.36 C -ANISOU 2629 CA ARG A 312 2250 2338 2007 -252 -25 -75 C -ATOM 2630 C ARG A 312 -3.084 -44.494 11.766 1.00 12.80 C -ANISOU 2630 C ARG A 312 1657 1798 1410 -263 -21 -94 C -ATOM 2631 O ARG A 312 -2.858 -45.599 11.272 1.00 15.63 O -ANISOU 2631 O ARG A 312 2022 2148 1770 -290 -16 -128 O -ATOM 2632 CB ARG A 312 -1.983 -44.033 13.953 1.00 12.82 C -ANISOU 2632 CB ARG A 312 1700 1705 1466 -225 -27 -68 C -ATOM 2633 CG ARG A 312 -2.184 -43.790 15.439 1.00 12.41 C -ANISOU 2633 CG ARG A 312 1664 1622 1430 -209 -32 -49 C -ATOM 2634 CD ARG A 312 -0.857 -43.645 16.168 1.00 13.88 C -ANISOU 2634 CD ARG A 312 1873 1754 1649 -186 -36 -49 C -ATOM 2635 NE ARG A 312 -1.078 -43.857 17.599 1.00 12.13 N -ANISOU 2635 NE ARG A 312 1669 1501 1438 -177 -41 -40 N -ATOM 2636 CZ ARG A 312 -0.173 -44.318 18.446 1.00 11.88 C -ANISOU 2636 CZ ARG A 312 1660 1422 1431 -166 -44 -46 C -ATOM 2637 NH1 ARG A 312 1.061 -44.602 18.028 1.00 9.98 N -ANISOU 2637 NH1 ARG A 312 1427 1155 1210 -163 -43 -61 N -ATOM 2638 NH2 ARG A 312 -0.504 -44.481 19.718 1.00 11.43 N -ANISOU 2638 NH2 ARG A 312 1618 1346 1378 -156 -47 -35 N -ATOM 2639 N LEU A 313 -3.175 -43.369 11.050 1.00 14.10 N -ANISOU 2639 N LEU A 313 1800 2003 1553 -241 -22 -71 N -ATOM 2640 CA LEU A 313 -2.753 -43.316 9.651 1.00 13.97 C -ANISOU 2640 CA LEU A 313 1771 2020 1518 -242 -16 -83 C -ATOM 2641 C LEU A 313 -1.297 -43.773 9.547 1.00 14.85 C -ANISOU 2641 C LEU A 313 1905 2078 1659 -238 -11 -101 C -ATOM 2642 O LEU A 313 -0.465 -43.434 10.398 1.00 14.51 O -ANISOU 2642 O LEU A 313 1880 1984 1648 -218 -12 -89 O -ATOM 2643 CB LEU A 313 -2.831 -41.886 9.106 1.00 13.10 C -ANISOU 2643 CB LEU A 313 1641 1947 1390 -208 -14 -46 C -ATOM 2644 CG LEU A 313 -4.215 -41.294 8.842 1.00 17.71 C -ANISOU 2644 CG LEU A 313 2195 2597 1936 -205 -17 -24 C -ATOM 2645 CD1 LEU A 313 -4.074 -39.872 8.380 1.00 17.18 C -ANISOU 2645 CD1 LEU A 313 2115 2554 1860 -166 -10 15 C -ATOM 2646 CD2 LEU A 313 -4.961 -42.117 7.817 1.00 18.11 C -ANISOU 2646 CD2 LEU A 313 2224 2707 1950 -236 -20 -53 C -ATOM 2647 N THR A 314 -0.998 -44.537 8.503 1.00 12.49 N -ANISOU 2647 N THR A 314 1604 1794 1347 -257 -5 -132 N -ATOM 2648 CA THR A 314 0.385 -44.839 8.167 1.00 15.26 C -ANISOU 2648 CA THR A 314 1972 2106 1721 -249 3 -146 C -ATOM 2649 C THR A 314 0.949 -43.624 7.446 1.00 16.88 C -ANISOU 2649 C THR A 314 2163 2332 1919 -217 9 -119 C -ATOM 2650 O THR A 314 0.201 -42.717 7.059 1.00 11.64 O -ANISOU 2650 O THR A 314 1478 1718 1229 -204 8 -94 O -ATOM 2651 CB THR A 314 0.529 -46.097 7.268 1.00 16.89 C -ANISOU 2651 CB THR A 314 2182 2319 1915 -279 11 -191 C -ATOM 2652 OG1 THR A 314 -0.054 -45.862 5.979 1.00 15.50 O -ANISOU 2652 OG1 THR A 314 1980 2213 1695 -285 12 -197 O -ATOM 2653 CG2 THR A 314 -0.121 -47.312 7.914 1.00 12.26 C -ANISOU 2653 CG2 THR A 314 1608 1713 1338 -314 9 -218 C -ATOM 2654 N ALA A 315 2.263 -43.597 7.262 1.00 14.41 N -ANISOU 2654 N ALA A 315 1862 1982 1632 -203 17 -122 N -ATOM 2655 CA ALA A 315 2.883 -42.479 6.577 1.00 11.71 C -ANISOU 2655 CA ALA A 315 1507 1654 1288 -174 26 -96 C -ATOM 2656 C ALA A 315 2.349 -42.389 5.148 1.00 13.77 C -ANISOU 2656 C ALA A 315 1746 1985 1503 -176 33 -99 C -ATOM 2657 O ALA A 315 2.072 -41.307 4.662 1.00 14.51 O -ANISOU 2657 O ALA A 315 1820 2115 1578 -154 38 -67 O -ATOM 2658 CB ALA A 315 4.406 -42.618 6.578 1.00 10.32 C -ANISOU 2658 CB ALA A 315 1345 1428 1148 -162 34 -103 C -ATOM 2659 N ARG A 316 2.217 -43.531 4.478 1.00 14.39 N -ANISOU 2659 N ARG A 316 1826 2080 1561 -203 34 -138 N -ATOM 2660 CA ARG A 316 1.766 -43.531 3.102 1.00 18.76 C -ANISOU 2660 CA ARG A 316 2358 2702 2067 -207 39 -146 C -ATOM 2661 C ARG A 316 0.317 -43.045 3.017 1.00 17.86 C -ANISOU 2661 C ARG A 316 2220 2652 1915 -210 29 -129 C -ATOM 2662 O ARG A 316 0.001 -42.189 2.195 1.00 16.65 O -ANISOU 2662 O ARG A 316 2043 2553 1728 -188 33 -104 O -ATOM 2663 CB ARG A 316 1.921 -44.913 2.482 1.00 25.06 C -ANISOU 2663 CB ARG A 316 3167 3502 2854 -238 42 -197 C -ATOM 2664 CG ARG A 316 1.825 -44.912 0.976 1.00 32.68 C -ANISOU 2664 CG ARG A 316 4112 4532 3771 -236 49 -210 C -ATOM 2665 CD ARG A 316 3.045 -44.242 0.368 1.00 33.59 C -ANISOU 2665 CD ARG A 316 4229 4636 3897 -202 66 -188 C -ATOM 2666 NE ARG A 316 2.842 -43.924 -1.040 1.00 37.24 N -ANISOU 2666 NE ARG A 316 4671 5171 4309 -190 74 -186 N -ATOM 2667 CZ ARG A 316 3.233 -44.702 -2.043 1.00 39.95 C -ANISOU 2667 CZ ARG A 316 5017 5533 4629 -200 83 -222 C -ATOM 2668 NH1 ARG A 316 3.857 -45.844 -1.792 1.00 36.37 N -ANISOU 2668 NH1 ARG A 316 4588 5028 4202 -222 86 -263 N -ATOM 2669 NH2 ARG A 316 3.009 -44.330 -3.295 1.00 46.64 N -ANISOU 2669 NH2 ARG A 316 5843 6452 5426 -185 89 -217 N -ATOM 2670 N GLU A 317 -0.552 -43.563 3.883 1.00 20.72 N -ANISOU 2670 N GLU A 317 2586 3006 2282 -234 16 -140 N -ATOM 2671 CA GLU A 317 -1.939 -43.089 3.938 1.00 19.64 C -ANISOU 2671 CA GLU A 317 2423 2926 2113 -236 7 -122 C -ATOM 2672 C GLU A 317 -2.000 -41.611 4.239 1.00 15.69 C -ANISOU 2672 C GLU A 317 1914 2432 1617 -196 10 -69 C -ATOM 2673 O GLU A 317 -2.847 -40.895 3.708 1.00 19.26 O -ANISOU 2673 O GLU A 317 2339 2946 2032 -182 10 -44 O -ATOM 2674 CB GLU A 317 -2.733 -43.789 5.037 1.00 19.38 C -ANISOU 2674 CB GLU A 317 2398 2870 2094 -264 -4 -136 C -ATOM 2675 CG GLU A 317 -2.967 -45.256 4.850 1.00 18.62 C -ANISOU 2675 CG GLU A 317 2310 2770 1996 -308 -5 -187 C -ATOM 2676 CD GLU A 317 -3.789 -45.824 5.983 1.00 24.97 C -ANISOU 2676 CD GLU A 317 3119 3551 2817 -333 -12 -193 C -ATOM 2677 OE1 GLU A 317 -3.367 -45.717 7.160 1.00 16.99 O -ANISOU 2677 OE1 GLU A 317 2131 2480 1844 -321 -11 -176 O -ATOM 2678 OE2 GLU A 317 -4.874 -46.364 5.698 1.00 21.41 O -ANISOU 2678 OE2 GLU A 317 2649 3145 2341 -364 -18 -214 O -ATOM 2679 N ALA A 318 -1.136 -41.153 5.142 1.00 13.91 N -ANISOU 2679 N ALA A 318 1709 2140 1436 -178 14 -52 N -ATOM 2680 CA ALA A 318 -1.126 -39.745 5.506 1.00 12.13 C -ANISOU 2680 CA ALA A 318 1478 1911 1221 -141 19 -5 C -ATOM 2681 C ALA A 318 -0.857 -38.898 4.258 1.00 16.66 C -ANISOU 2681 C ALA A 318 2032 2528 1770 -114 34 20 C -ATOM 2682 O ALA A 318 -1.473 -37.841 4.053 1.00 18.18 O -ANISOU 2682 O ALA A 318 2206 2758 1944 -89 39 58 O -ATOM 2683 CB ALA A 318 -0.082 -39.474 6.606 1.00 13.18 C -ANISOU 2683 CB ALA A 318 1636 1965 1407 -129 20 2 C -ATOM 2684 N MET A 319 0.042 -39.376 3.402 1.00 13.28 N -ANISOU 2684 N MET A 319 1609 2097 1340 -118 42 -1 N -ATOM 2685 CA MET A 319 0.398 -38.630 2.205 1.00 15.25 C -ANISOU 2685 CA MET A 319 1842 2386 1568 -90 59 23 C -ATOM 2686 C MET A 319 -0.755 -38.553 1.207 1.00 16.72 C -ANISOU 2686 C MET A 319 1998 2662 1692 -89 57 28 C -ATOM 2687 O MET A 319 -0.764 -37.683 0.340 1.00 17.25 O -ANISOU 2687 O MET A 319 2048 2772 1735 -59 71 62 O -ATOM 2688 CB MET A 319 1.658 -39.205 1.554 1.00 16.77 C -ANISOU 2688 CB MET A 319 2046 2553 1773 -94 70 -1 C -ATOM 2689 CG MET A 319 2.863 -39.060 2.459 1.00 19.83 C -ANISOU 2689 CG MET A 319 2457 2859 2220 -87 74 1 C -ATOM 2690 SD MET A 319 4.299 -39.836 1.733 1.00 21.15 S -ANISOU 2690 SD MET A 319 2636 2997 2402 -92 87 -28 S -ATOM 2691 CE MET A 319 4.618 -38.655 0.434 1.00 20.13 C -ANISOU 2691 CE MET A 319 2485 2914 2251 -54 112 13 C -ATOM 2692 N GLU A 320 -1.739 -39.434 1.360 1.00 18.27 N -ANISOU 2692 N GLU A 320 2188 2888 1865 -122 39 -2 N -ATOM 2693 CA GLU A 320 -2.947 -39.395 0.526 1.00 21.93 C -ANISOU 2693 CA GLU A 320 2621 3443 2270 -124 32 0 C -ATOM 2694 C GLU A 320 -4.002 -38.417 1.050 1.00 20.65 C -ANISOU 2694 C GLU A 320 2439 3308 2097 -104 29 44 C -ATOM 2695 O GLU A 320 -5.022 -38.195 0.394 1.00 22.25 O -ANISOU 2695 O GLU A 320 2613 3591 2252 -98 24 55 O -ATOM 2696 CB GLU A 320 -3.581 -40.791 0.410 1.00 19.95 C -ANISOU 2696 CB GLU A 320 2367 3214 1999 -172 16 -55 C -ATOM 2697 CG GLU A 320 -2.645 -41.900 -0.076 1.00 21.28 C -ANISOU 2697 CG GLU A 320 2555 3354 2176 -196 20 -104 C -ATOM 2698 CD GLU A 320 -2.428 -41.879 -1.574 1.00 25.98 C -ANISOU 2698 CD GLU A 320 3135 4013 2725 -184 28 -112 C -ATOM 2699 OE1 GLU A 320 -3.383 -42.179 -2.317 1.00 26.11 O -ANISOU 2699 OE1 GLU A 320 3125 4106 2690 -198 17 -130 O -ATOM 2700 OE2 GLU A 320 -1.300 -41.574 -2.018 1.00 25.28 O -ANISOU 2700 OE2 GLU A 320 3057 3898 2650 -161 45 -101 O -ATOM 2701 N HIS A 321 -3.790 -37.843 2.231 1.00 16.18 N -ANISOU 2701 N HIS A 321 1891 2681 1576 -91 31 67 N -ATOM 2702 CA HIS A 321 -4.855 -37.050 2.866 1.00 16.84 C -ANISOU 2702 CA HIS A 321 1960 2786 1652 -75 28 103 C -ATOM 2703 C HIS A 321 -5.165 -35.716 2.170 1.00 15.40 C -ANISOU 2703 C HIS A 321 1755 2652 1444 -30 44 156 C -ATOM 2704 O HIS A 321 -4.260 -35.033 1.703 1.00 17.60 O -ANISOU 2704 O HIS A 321 2040 2912 1736 -2 63 179 O -ATOM 2705 CB HIS A 321 -4.550 -36.815 4.355 1.00 20.12 C -ANISOU 2705 CB HIS A 321 2402 3122 2120 -74 27 110 C -ATOM 2706 CG HIS A 321 -5.740 -36.367 5.147 1.00 22.62 C -ANISOU 2706 CG HIS A 321 2707 3457 2429 -68 20 134 C -ATOM 2707 ND1 HIS A 321 -6.159 -35.056 5.184 1.00 20.36 N -ANISOU 2707 ND1 HIS A 321 2408 3190 2136 -29 33 183 N -ATOM 2708 CD2 HIS A 321 -6.608 -37.059 5.924 1.00 15.63 C -ANISOU 2708 CD2 HIS A 321 1822 2575 1542 -95 6 116 C -ATOM 2709 CE1 HIS A 321 -7.231 -34.957 5.951 1.00 17.67 C -ANISOU 2709 CE1 HIS A 321 2060 2864 1789 -31 25 194 C -ATOM 2710 NE2 HIS A 321 -7.526 -36.159 6.410 1.00 16.05 N -ANISOU 2710 NE2 HIS A 321 1861 2651 1587 -72 8 154 N -ATOM 2711 N PRO A 322 -6.464 -35.339 2.099 1.00 15.12 N -ANISOU 2711 N PRO A 322 1692 2681 1372 -21 39 179 N -ATOM 2712 CA PRO A 322 -6.861 -34.059 1.493 1.00 17.97 C -ANISOU 2712 CA PRO A 322 2030 3091 1707 26 56 234 C -ATOM 2713 C PRO A 322 -6.088 -32.819 1.991 1.00 16.23 C -ANISOU 2713 C PRO A 322 1828 2806 1531 65 79 277 C -ATOM 2714 O PRO A 322 -5.974 -31.831 1.255 1.00 16.40 O -ANISOU 2714 O PRO A 322 1838 2855 1540 104 101 320 O -ATOM 2715 CB PRO A 322 -8.358 -33.961 1.843 1.00 17.98 C -ANISOU 2715 CB PRO A 322 2006 3148 1679 25 44 248 C -ATOM 2716 CG PRO A 322 -8.810 -35.382 1.890 1.00 19.75 C -ANISOU 2716 CG PRO A 322 2225 3391 1887 -27 20 192 C -ATOM 2717 CD PRO A 322 -7.634 -36.159 2.471 1.00 19.58 C -ANISOU 2717 CD PRO A 322 2242 3282 1915 -55 18 153 C -ATOM 2718 N TYR A 323 -5.571 -32.863 3.215 1.00 16.49 N -ANISOU 2718 N TYR A 323 1891 2758 1617 53 76 266 N -ATOM 2719 CA TYR A 323 -4.765 -31.771 3.760 1.00 19.60 C -ANISOU 2719 CA TYR A 323 2303 3086 2058 83 96 297 C -ATOM 2720 C TYR A 323 -3.636 -31.382 2.793 1.00 14.72 C -ANISOU 2720 C TYR A 323 1687 2458 1449 101 117 308 C -ATOM 2721 O TYR A 323 -3.253 -30.216 2.691 1.00 20.48 O -ANISOU 2721 O TYR A 323 2418 3167 2198 136 142 349 O -ATOM 2722 CB TYR A 323 -4.192 -32.201 5.125 1.00 20.93 C -ANISOU 2722 CB TYR A 323 2503 3172 2277 59 84 267 C -ATOM 2723 CG TYR A 323 -3.380 -31.170 5.892 1.00 15.71 C -ANISOU 2723 CG TYR A 323 1862 2438 1668 83 99 289 C -ATOM 2724 CD1 TYR A 323 -3.919 -29.938 6.247 1.00 17.09 C -ANISOU 2724 CD1 TYR A 323 2033 2613 1849 117 115 332 C -ATOM 2725 CD2 TYR A 323 -2.086 -31.461 6.319 1.00 13.12 C -ANISOU 2725 CD2 TYR A 323 1558 2042 1386 70 98 264 C -ATOM 2726 CE1 TYR A 323 -3.190 -29.012 6.976 1.00 11.61 C -ANISOU 2726 CE1 TYR A 323 1357 1849 1204 134 129 346 C -ATOM 2727 CE2 TYR A 323 -1.345 -30.546 7.037 1.00 14.16 C -ANISOU 2727 CE2 TYR A 323 1706 2110 1566 87 109 278 C -ATOM 2728 CZ TYR A 323 -1.894 -29.330 7.362 1.00 14.72 C -ANISOU 2728 CZ TYR A 323 1772 2179 1642 118 125 317 C -ATOM 2729 OH TYR A 323 -1.155 -28.436 8.087 1.00 20.27 O -ANISOU 2729 OH TYR A 323 2491 2815 2394 132 137 326 O -ATOM 2730 N PHE A 324 -3.130 -32.357 2.053 1.00 16.82 N -ANISOU 2730 N PHE A 324 1952 2739 1698 78 110 273 N -ATOM 2731 CA PHE A 324 -1.978 -32.112 1.191 1.00 15.81 C -ANISOU 2731 CA PHE A 324 1829 2599 1581 93 130 280 C -ATOM 2732 C PHE A 324 -2.346 -31.802 -0.260 1.00 18.98 C -ANISOU 2732 C PHE A 324 2203 3083 1927 118 144 305 C -ATOM 2733 O PHE A 324 -1.474 -31.587 -1.091 1.00 16.21 O -ANISOU 2733 O PHE A 324 1852 2730 1578 134 164 315 O -ATOM 2734 CB PHE A 324 -1.002 -33.283 1.274 1.00 16.75 C -ANISOU 2734 CB PHE A 324 1968 2676 1722 58 119 228 C -ATOM 2735 CG PHE A 324 -0.463 -33.499 2.651 1.00 20.78 C -ANISOU 2735 CG PHE A 324 2504 3104 2287 41 108 208 C -ATOM 2736 CD1 PHE A 324 0.399 -32.571 3.222 1.00 16.26 C -ANISOU 2736 CD1 PHE A 324 1945 2468 1765 61 123 231 C -ATOM 2737 CD2 PHE A 324 -0.835 -34.611 3.389 1.00 17.22 C -ANISOU 2737 CD2 PHE A 324 2065 2641 1838 5 84 168 C -ATOM 2738 CE1 PHE A 324 0.892 -32.759 4.513 1.00 16.20 C -ANISOU 2738 CE1 PHE A 324 1961 2390 1805 46 111 211 C -ATOM 2739 CE2 PHE A 324 -0.345 -34.809 4.679 1.00 18.85 C -ANISOU 2739 CE2 PHE A 324 2295 2775 2091 -8 74 152 C -ATOM 2740 CZ PHE A 324 0.518 -33.880 5.239 1.00 14.78 C -ANISOU 2740 CZ PHE A 324 1792 2201 1621 14 86 173 C -ATOM 2741 N TYR A 325 -3.640 -31.739 -0.563 1.00 17.95 N -ANISOU 2741 N TYR A 325 2046 3027 1746 125 136 319 N -ATOM 2742 CA TYR A 325 -4.043 -31.424 -1.931 1.00 15.72 C -ANISOU 2742 CA TYR A 325 1735 2831 1405 153 147 345 C -ATOM 2743 C TYR A 325 -3.513 -30.063 -2.388 1.00 12.87 C -ANISOU 2743 C TYR A 325 1373 2459 1059 203 184 405 C -ATOM 2744 O TYR A 325 -3.205 -29.881 -3.565 1.00 16.53 O -ANISOU 2744 O TYR A 325 1823 2967 1490 226 201 422 O -ATOM 2745 CB TYR A 325 -5.573 -31.458 -2.087 1.00 14.31 C -ANISOU 2745 CB TYR A 325 1526 2738 1173 155 131 354 C -ATOM 2746 CG TYR A 325 -6.212 -32.828 -2.011 1.00 20.03 C -ANISOU 2746 CG TYR A 325 2244 3497 1871 106 98 296 C -ATOM 2747 CD1 TYR A 325 -5.448 -33.994 -2.001 1.00 19.25 C -ANISOU 2747 CD1 TYR A 325 2165 3360 1788 65 86 239 C -ATOM 2748 CD2 TYR A 325 -7.596 -32.953 -1.962 1.00 22.59 C -ANISOU 2748 CD2 TYR A 325 2540 3890 2154 100 81 298 C -ATOM 2749 CE1 TYR A 325 -6.046 -35.240 -1.933 1.00 20.90 C -ANISOU 2749 CE1 TYR A 325 2369 3596 1976 19 60 186 C -ATOM 2750 CE2 TYR A 325 -8.199 -34.184 -1.891 1.00 27.87 C -ANISOU 2750 CE2 TYR A 325 3201 4588 2802 52 53 245 C -ATOM 2751 CZ TYR A 325 -7.429 -35.321 -1.881 1.00 26.19 C -ANISOU 2751 CZ TYR A 325 3010 4334 2608 12 44 188 C -ATOM 2752 OH TYR A 325 -8.061 -36.536 -1.807 1.00 27.33 O -ANISOU 2752 OH TYR A 325 3146 4503 2734 -37 19 135 O -ATOM 2753 N THR A 326 -3.391 -29.112 -1.460 1.00 15.82 N -ANISOU 2753 N THR A 326 1759 2771 1481 221 198 436 N -ATOM 2754 CA THR A 326 -2.988 -27.758 -1.836 1.00 16.96 C -ANISOU 2754 CA THR A 326 1901 2899 1642 269 237 495 C -ATOM 2755 C THR A 326 -1.467 -27.636 -2.033 1.00 18.62 C -ANISOU 2755 C THR A 326 2131 3045 1900 268 257 490 C -ATOM 2756 O THR A 326 -0.991 -26.698 -2.669 1.00 21.52 O -ANISOU 2756 O THR A 326 2492 3408 2275 305 292 536 O -ATOM 2757 CB THR A 326 -3.486 -26.697 -0.831 1.00 29.18 C -ANISOU 2757 CB THR A 326 3456 4409 3224 290 248 532 C -ATOM 2758 OG1 THR A 326 -3.153 -25.386 -1.308 1.00 35.24 O -ANISOU 2758 OG1 THR A 326 4219 5164 4006 338 289 591 O -ATOM 2759 CG2 THR A 326 -2.859 -26.906 0.515 1.00 29.96 C -ANISOU 2759 CG2 THR A 326 3584 4414 3386 261 236 498 C -ATOM 2760 N VAL A 327 -0.729 -28.608 -1.516 1.00 15.81 N -ANISOU 2760 N VAL A 327 1794 2639 1573 228 237 437 N -ATOM 2761 CA VAL A 327 0.736 -28.637 -1.653 1.00 15.17 C -ANISOU 2761 CA VAL A 327 1730 2498 1538 223 252 426 C -ATOM 2762 C VAL A 327 1.175 -28.987 -3.077 1.00 17.69 C -ANISOU 2762 C VAL A 327 2035 2869 1817 233 266 427 C -ATOM 2763 O VAL A 327 0.740 -29.990 -3.643 1.00 20.21 O -ANISOU 2763 O VAL A 327 2346 3246 2086 214 245 394 O -ATOM 2764 CB VAL A 327 1.344 -29.628 -0.666 1.00 17.41 C -ANISOU 2764 CB VAL A 327 2036 2718 1860 179 226 370 C -ATOM 2765 CG1 VAL A 327 2.856 -29.734 -0.874 1.00 19.37 C -ANISOU 2765 CG1 VAL A 327 2296 2912 2151 175 241 358 C -ATOM 2766 CG2 VAL A 327 1.035 -29.193 0.754 1.00 19.91 C -ANISOU 2766 CG2 VAL A 327 2366 2980 2217 174 216 372 C -ATOM 2767 N VAL A 328 2.033 -28.154 -3.662 1.00 15.51 N -ANISOU 2767 N VAL A 328 1758 2572 1563 263 302 465 N -ATOM 2768 CA VAL A 328 2.514 -28.395 -5.019 1.00 20.21 C -ANISOU 2768 CA VAL A 328 2342 3216 2122 278 319 471 C -ATOM 2769 C VAL A 328 3.404 -29.626 -5.074 1.00 24.03 C -ANISOU 2769 C VAL A 328 2840 3675 2617 242 303 413 C -ATOM 2770 O VAL A 328 4.365 -29.737 -4.311 1.00 19.02 O -ANISOU 2770 O VAL A 328 2223 2961 2042 223 302 393 O -ATOM 2771 CB VAL A 328 3.305 -27.190 -5.582 1.00 25.81 C -ANISOU 2771 CB VAL A 328 3047 3900 2860 319 367 528 C -ATOM 2772 CG1 VAL A 328 4.060 -27.595 -6.842 1.00 29.17 C -ANISOU 2772 CG1 VAL A 328 3465 4360 3257 329 384 526 C -ATOM 2773 CG2 VAL A 328 2.381 -26.013 -5.863 1.00 23.63 C -ANISOU 2773 CG2 VAL A 328 2754 3665 2560 364 390 591 C -ATOM 2774 N LYS A 329 3.092 -30.536 -5.991 1.00 24.47 N -ANISOU 2774 N LYS A 329 2886 3800 2612 233 290 385 N -ATOM 2775 CA LYS A 329 3.924 -31.719 -6.204 1.00 36.96 C -ANISOU 2775 CA LYS A 329 4481 5363 4199 202 279 332 C -ATOM 2776 C LYS A 329 4.956 -31.494 -7.318 1.00 37.65 C -ANISOU 2776 C LYS A 329 4564 5459 4282 228 313 351 C -ATOM 2777 O LYS A 329 6.148 -31.770 -7.146 1.00 41.50 O -ANISOU 2777 O LYS A 329 5066 5887 4816 217 322 333 O -ATOM 2778 CB LYS A 329 3.054 -32.936 -6.528 1.00 43.00 C -ANISOU 2778 CB LYS A 329 5240 6192 4905 173 248 282 C -ATOM 2779 CG LYS A 329 1.943 -33.186 -5.519 1.00 44.23 C -ANISOU 2779 CG LYS A 329 5397 6349 5060 148 217 265 C -ATOM 2780 CD LYS A 329 2.471 -33.174 -4.088 1.00 41.48 C -ANISOU 2780 CD LYS A 329 5072 5904 4783 128 208 253 C -ATOM 2781 CE LYS A 329 1.384 -33.590 -3.102 1.00 39.67 C -ANISOU 2781 CE LYS A 329 4845 5678 4551 101 178 232 C -ATOM 2782 NZ LYS A 329 0.137 -32.776 -3.236 1.00 36.68 N -ANISOU 2782 NZ LYS A 329 4443 5359 4134 126 179 273 N -TER 2783 LYS A 329 -HETATM 2784 N1 FU9 A 338 23.421 -29.478 10.420 1.00 19.97 N -HETATM 2785 C2 FU9 A 338 23.434 -28.488 11.339 1.00 19.82 C -HETATM 2786 N3 FU9 A 338 23.310 -28.750 12.649 1.00 16.65 N -HETATM 2787 C4 FU9 A 338 23.185 -30.006 13.072 1.00 14.99 C -HETATM 2788 C5 FU9 A 338 23.147 -31.045 12.151 1.00 13.79 C -HETATM 2789 C6 FU9 A 338 23.287 -30.744 10.797 1.00 17.01 C -HETATM 2790 OAA FU9 A 338 22.464 -36.547 15.342 1.00 13.61 O -HETATM 2791 OAB FU9 A 338 22.086 -37.214 13.268 1.00 16.32 O -HETATM 2792 FAC FU9 A 338 24.116 -31.123 20.289 1.00 37.04 F -HETATM 2793 FAD FU9 A 338 22.009 -30.950 20.696 1.00 39.25 F -HETATM 2794 FAE FU9 A 338 22.714 -32.258 19.128 1.00 40.80 F -HETATM 2795 CAF FU9 A 338 22.594 -27.556 18.409 1.00 18.66 C -HETATM 2796 CAG FU9 A 338 22.777 -27.761 17.049 1.00 19.72 C -HETATM 2797 CAH FU9 A 338 22.658 -28.643 19.269 1.00 16.31 C -HETATM 2798 CAI FU9 A 338 22.800 -34.725 12.202 1.00 10.51 C -HETATM 2799 CAJ FU9 A 338 22.968 -33.433 11.721 1.00 13.22 C -HETATM 2800 CAL FU9 A 338 22.973 -30.130 17.400 1.00 17.88 C -HETATM 2801 CAM FU9 A 338 22.708 -33.870 14.448 1.00 13.89 C -HETATM 2802 CAN FU9 A 338 23.500 -24.762 11.531 1.00 23.65 C -HETATM 2803 CAO FU9 A 338 24.834 -25.307 12.063 1.00 31.24 C -HETATM 2804 NAQ FU9 A 338 22.885 -31.520 14.849 1.00 14.98 N -HETATM 2805 NAS FU9 A 338 22.985 -29.154 15.196 1.00 14.12 N -HETATM 2806 NAT FU9 A 338 23.580 -27.216 10.980 1.00 21.94 N -HETATM 2807 CAU FU9 A 338 22.486 -36.365 14.101 1.00 15.99 C -HETATM 2808 CAV FU9 A 338 22.877 -29.044 16.527 1.00 14.02 C -HETATM 2809 CAW FU9 A 338 22.708 -34.950 13.574 1.00 15.52 C -HETATM 2810 CAX FU9 A 338 22.843 -29.925 18.771 1.00 18.91 C -HETATM 2811 CAZ FU9 A 338 23.093 -30.247 14.432 1.00 14.63 C -HETATM 2812 CBA FU9 A 338 22.874 -32.568 13.978 1.00 14.78 C -HETATM 2813 CBB FU9 A 338 22.996 -32.352 12.609 1.00 12.09 C -HETATM 2814 CBE FU9 A 338 23.598 -26.197 12.040 1.00 24.43 C -HETATM 2815 CBF FU9 A 338 22.914 -31.103 19.747 1.00 33.36 C -HETATM 2816 S SO4 A 339 16.994 -48.427 23.467 1.00 56.37 S -HETATM 2817 O1 SO4 A 339 18.081 -47.592 22.948 1.00 54.07 O -HETATM 2818 O2 SO4 A 339 16.573 -49.386 22.452 1.00 44.10 O -HETATM 2819 O3 SO4 A 339 17.449 -49.155 24.652 1.00 62.33 O -HETATM 2820 O4 SO4 A 339 15.862 -47.573 23.827 1.00 55.64 O -HETATM 2821 S SO4 A 340 12.335 -41.463 29.821 1.00 55.41 S -HETATM 2822 O1 SO4 A 340 12.524 -41.505 28.365 1.00 49.11 O -HETATM 2823 O2 SO4 A 340 11.605 -42.648 30.264 1.00 51.42 O -HETATM 2824 O3 SO4 A 340 13.642 -41.420 30.480 1.00 56.91 O -HETATM 2825 O4 SO4 A 340 11.578 -40.268 30.194 1.00 53.41 O -HETATM 2826 S SO4 A 341 -8.673 -44.194 19.555 1.00 20.92 S -HETATM 2827 O1 SO4 A 341 -8.890 -44.407 18.118 1.00 26.24 O -HETATM 2828 O2 SO4 A 341 -9.987 -44.244 20.203 1.00 24.61 O -HETATM 2829 O3 SO4 A 341 -7.781 -45.264 20.045 1.00 17.72 O -HETATM 2830 O4 SO4 A 341 -8.117 -42.851 19.768 1.00 12.17 O -HETATM 2831 S SO4 A 342 16.660 -32.532 -1.544 1.00 60.53 S -HETATM 2832 O1 SO4 A 342 18.092 -32.240 -1.608 1.00 60.37 O -HETATM 2833 O2 SO4 A 342 16.008 -31.860 -2.665 1.00 66.82 O -HETATM 2834 O3 SO4 A 342 16.445 -33.972 -1.635 1.00 60.76 O -HETATM 2835 O4 SO4 A 342 16.083 -32.057 -0.290 1.00 56.69 O -HETATM 2836 C1 PEG A 343 11.944 -32.966 28.991 1.00 56.31 C -HETATM 2837 O1 PEG A 343 11.298 -31.707 29.225 1.00 56.67 O -HETATM 2838 C2 PEG A 343 11.484 -33.531 27.650 1.00 53.96 C -HETATM 2839 O2 PEG A 343 12.178 -34.752 27.413 1.00 55.88 O -HETATM 2840 C3 PEG A 343 11.570 -35.803 28.154 1.00 52.84 C -HETATM 2841 C4 PEG A 343 12.333 -37.112 28.003 1.00 49.96 C -HETATM 2842 O4 PEG A 343 11.995 -37.950 29.120 1.00 53.07 O -HETATM 2843 C1 EDO A 344 36.720 -34.839 14.137 1.00 36.42 C -HETATM 2844 O1 EDO A 344 37.874 -34.042 13.843 1.00 41.78 O -HETATM 2845 C2 EDO A 344 37.172 -36.201 14.636 1.00 35.03 C -HETATM 2846 O2 EDO A 344 38.187 -36.015 15.626 1.00 42.78 O -HETATM 2847 C1 EDO A 345 19.415 -27.579 15.641 1.00 36.05 C -HETATM 2848 O1 EDO A 345 18.612 -26.416 15.884 1.00 36.30 O -HETATM 2849 C2 EDO A 345 18.554 -28.838 15.673 1.00 30.48 C -HETATM 2850 O2 EDO A 345 17.199 -28.530 15.316 1.00 26.54 O -HETATM 2851 C1 EDO A 346 46.096 -32.820 6.362 1.00 34.89 C -HETATM 2852 O1 EDO A 346 45.187 -33.876 6.713 1.00 41.33 O -HETATM 2853 C2 EDO A 346 46.688 -33.074 4.975 1.00 39.51 C -HETATM 2854 O2 EDO A 346 47.830 -33.946 5.050 1.00 29.68 O -HETATM 2855 C1 EDO A 347 -3.512 -28.782 24.927 1.00 31.45 C -HETATM 2856 O1 EDO A 347 -4.315 -28.235 25.980 1.00 34.75 O -HETATM 2857 C2 EDO A 347 -3.161 -30.226 25.258 1.00 23.02 C -HETATM 2858 O2 EDO A 347 -2.455 -30.258 26.501 1.00 28.27 O -HETATM 2859 C1 EDO A 348 13.925 -26.745 12.537 1.00 30.67 C -HETATM 2860 O1 EDO A 348 15.064 -26.455 11.710 1.00 27.06 O -HETATM 2861 C2 EDO A 348 14.326 -27.670 13.686 1.00 28.04 C -HETATM 2862 O2 EDO A 348 15.184 -26.970 14.593 1.00 34.93 O -HETATM 2863 C1 EDO A 349 13.940 -31.689 22.311 1.00 39.56 C -HETATM 2864 O1 EDO A 349 14.512 -30.521 21.707 1.00 45.99 O -HETATM 2865 C2 EDO A 349 13.327 -31.365 23.668 1.00 44.54 C -HETATM 2866 O2 EDO A 349 12.614 -32.504 24.166 1.00 44.84 O -HETATM 2867 C1 EDO A 350 10.835 -28.583 23.200 1.00 32.95 C -HETATM 2868 O1 EDO A 350 9.779 -27.664 23.502 1.00 33.08 O -HETATM 2869 C2 EDO A 350 10.240 -29.859 22.616 1.00 31.46 C -HETATM 2870 O2 EDO A 350 9.881 -29.645 21.243 1.00 32.80 O -HETATM 2871 C1 EDO A 351 20.986 -23.426 13.465 1.00 52.38 C -HETATM 2872 O1 EDO A 351 20.721 -22.062 13.812 1.00 57.95 O -HETATM 2873 C2 EDO A 351 20.228 -24.368 14.395 1.00 49.78 C -HETATM 2874 O2 EDO A 351 20.793 -24.356 15.712 1.00 46.66 O -HETATM 2875 C1 EDO A 352 -13.220 -35.583 18.281 1.00 37.90 C -HETATM 2876 O1 EDO A 352 -13.664 -35.017 17.031 1.00 39.89 O -HETATM 2877 C2 EDO A 352 -11.932 -36.382 18.091 1.00 40.36 C -HETATM 2878 O2 EDO A 352 -12.190 -37.673 17.506 1.00 34.29 O -HETATM 2879 O HOH A 353 8.987 -40.871 17.285 1.00 11.54 O -HETATM 2880 O HOH A 354 19.887 -46.447 16.454 1.00 14.49 O -HETATM 2881 O HOH A 355 2.911 -32.739 22.505 1.00 12.91 O -HETATM 2882 O HOH A 356 17.796 -55.912 14.153 1.00 18.39 O -HETATM 2883 O HOH A 357 3.501 -48.348 17.810 1.00 12.78 O -HETATM 2884 O HOH A 358 4.072 -45.639 8.010 1.00 15.13 O -HETATM 2885 O HOH A 359 5.129 -56.420 16.508 1.00 14.96 O -HETATM 2886 O HOH A 360 2.642 -49.571 11.395 1.00 16.54 O -HETATM 2887 O HOH A 361 6.648 -54.967 18.038 1.00 14.45 O -HETATM 2888 O HOH A 362 2.678 -37.208 23.829 1.00 13.76 O -HETATM 2889 O HOH A 363 -12.542 -41.011 25.190 1.00 13.06 O -HETATM 2890 O HOH A 364 3.806 -30.836 20.403 1.00 14.14 O -HETATM 2891 O HOH A 365 3.656 -45.923 5.361 1.00 14.29 O -HETATM 2892 O HOH A 366 22.685 -41.517 5.775 1.00 15.45 O -HETATM 2893 O HOH A 367 10.733 -37.427 20.575 1.00 19.09 O -HETATM 2894 O HOH A 368 2.780 -53.781 16.835 1.00 14.74 O -HETATM 2895 O HOH A 369 14.426 -50.921 22.150 1.00 20.60 O -HETATM 2896 O HOH A 370 21.855 -39.865 13.360 1.00 13.76 O -HETATM 2897 O HOH A 371 42.009 -38.747 25.405 1.00 17.57 O -HETATM 2898 O HOH A 372 -4.465 -31.544 28.119 1.00 19.13 O -HETATM 2899 O HOH A 373 4.265 -54.914 26.848 1.00 23.39 O -HETATM 2900 O HOH A 374 17.533 -39.711 18.780 1.00 16.97 O -HETATM 2901 O HOH A 375 0.699 -45.713 11.723 1.00 17.36 O -HETATM 2902 O HOH A 376 2.793 -46.915 10.393 1.00 16.79 O -HETATM 2903 O HOH A 377 -14.155 -40.349 27.563 1.00 15.62 O -HETATM 2904 O HOH A 378 20.975 -39.402 2.890 1.00 21.54 O -HETATM 2905 O HOH A 379 9.134 -41.397 0.598 1.00 19.48 O -HETATM 2906 O HOH A 380 -4.935 -25.756 7.552 1.00 18.32 O -HETATM 2907 O HOH A 381 21.984 -35.285 17.697 1.00 18.29 O -HETATM 2908 O HOH A 382 0.274 -51.267 14.343 1.00 18.60 O -HETATM 2909 O HOH A 383 -1.149 -47.631 12.399 1.00 21.52 O -HETATM 2910 O HOH A 384 0.018 -50.293 11.987 1.00 20.34 O -HETATM 2911 O HOH A 385 39.348 -42.611 11.751 1.00 16.81 O -HETATM 2912 O HOH A 386 -7.995 -37.924 17.848 1.00 14.71 O -HETATM 2913 O HOH A 387 37.834 -39.677 5.231 1.00 20.11 O -HETATM 2914 O HOH A 388 -6.813 -42.787 11.904 1.00 13.63 O -HETATM 2915 O HOH A 389 11.369 -28.600 13.194 1.00 21.39 O -HETATM 2916 O HOH A 390 -3.234 -56.930 17.914 1.00 24.53 O -HETATM 2917 O HOH A 391 -1.347 -35.492 36.694 1.00 18.42 O -HETATM 2918 O HOH A 392 1.543 -47.653 4.618 1.00 22.24 O -HETATM 2919 O HOH A 393 22.234 -57.364 15.694 1.00 32.79 O -HETATM 2920 O HOH A 394 16.303 -42.005 16.506 1.00 16.12 O -HETATM 2921 O HOH A 395 14.367 -37.035 22.773 1.00 24.20 O -HETATM 2922 O HOH A 396 5.423 -24.868 -3.326 1.00 20.38 O -HETATM 2923 O HOH A 397 -9.125 -46.712 21.995 1.00 19.61 O -HETATM 2924 O HOH A 398 -1.139 -18.620 6.435 1.00 21.33 O -HETATM 2925 O HOH A 399 -11.422 -52.354 23.775 1.00 22.96 O -HETATM 2926 O HOH A 400 -7.604 -26.782 3.277 1.00 21.94 O -HETATM 2927 O HOH A 401 -13.582 -42.892 31.940 1.00 19.54 O -HETATM 2928 O HOH A 402 21.093 -26.219 3.957 1.00 23.45 O -HETATM 2929 O HOH A 403 43.640 -41.818 21.066 1.00 21.26 O -HETATM 2930 O HOH A 404 6.222 -31.065 0.101 1.00 21.88 O -HETATM 2931 O HOH A 405 5.926 -29.808 19.127 1.00 25.17 O -HETATM 2932 O HOH A 406 10.860 -50.969 28.444 1.00 23.36 O -HETATM 2933 O HOH A 407 23.244 -54.092 4.147 1.00 23.70 O -HETATM 2934 O HOH A 408 26.114 -50.905 5.506 1.00 23.66 O -HETATM 2935 O HOH A 409 -2.706 -21.923 21.212 1.00 21.27 O -HETATM 2936 O HOH A 410 0.774 -42.278 -0.412 1.00 29.93 O -HETATM 2937 O HOH A 411 23.379 -41.136 19.237 1.00 27.98 O -HETATM 2938 O HOH A 412 -10.318 -16.170 19.802 1.00 21.17 O -HETATM 2939 O HOH A 413 -7.632 -14.724 21.421 1.00 24.65 O -HETATM 2940 O HOH A 414 -15.121 -30.129 22.991 1.00 31.12 O -HETATM 2941 O HOH A 415 5.720 -44.137 32.363 1.00 32.89 O -HETATM 2942 O HOH A 416 -1.666 -25.760 8.506 1.00 20.16 O -HETATM 2943 O HOH A 417 17.143 -26.886 19.125 1.00 29.81 O -HETATM 2944 O HOH A 418 -4.114 -29.928 30.383 1.00 26.31 O -HETATM 2945 O HOH A 419 4.413 -46.642 34.675 1.00 32.14 O -HETATM 2946 O HOH A 420 10.164 -56.549 9.469 1.00 21.53 O -HETATM 2947 O HOH A 421 41.959 -41.303 14.987 1.00 24.00 O -HETATM 2948 O HOH A 422 -5.506 -28.983 0.729 1.00 24.63 O -HETATM 2949 O HOH A 423 -4.991 -46.372 9.146 1.00 30.81 O -HETATM 2950 O HOH A 424 27.660 -30.729 4.215 1.00 29.30 O -HETATM 2951 O HOH A 425 -21.404 -41.199 36.611 1.00 27.34 O -HETATM 2952 O HOH A 426 -2.740 -35.777 -0.544 1.00 20.22 O -HETATM 2953 O HOH A 427 -8.719 -49.412 21.249 1.00 29.92 O -HETATM 2954 O HOH A 428 16.577 -35.947 0.068 1.00 21.27 O -HETATM 2955 O HOH A 429 3.162 -42.870 31.959 1.00 22.42 O -HETATM 2956 O HOH A 430 -8.147 -43.271 9.276 1.00 29.09 O -HETATM 2957 O HOH A 431 31.321 -36.279 22.820 1.00 34.85 O -HETATM 2958 O HOH A 432 23.663 -61.490 5.037 1.00 37.50 O -HETATM 2959 O HOH A 433 9.789 -37.458 31.225 1.00 36.24 O -HETATM 2960 O HOH A 434 2.995 -25.731 25.757 1.00 31.26 O -HETATM 2961 O HOH A 435 -7.586 -40.501 5.760 1.00 22.37 O -HETATM 2962 O HOH A 436 -13.460 -28.763 3.650 1.00 41.17 O -HETATM 2963 O HOH A 437 -14.286 -47.573 28.134 1.00 28.78 O -HETATM 2964 O HOH A 438 8.992 -23.871 21.291 1.00 31.83 O -HETATM 2965 O HOH A 439 -11.063 -51.070 21.222 1.00 32.01 O -HETATM 2966 O HOH A 440 40.192 -26.924 14.795 1.00 25.66 O -HETATM 2967 O HOH A 441 8.846 -52.049 29.945 1.00 35.68 O -HETATM 2968 O HOH A 442 -9.323 -46.912 17.430 1.00 22.12 O -HETATM 2969 O HOH A 443 24.442 -44.374 18.580 1.00 28.11 O -HETATM 2970 O HOH A 444 -4.785 -23.809 21.307 1.00 23.80 O -HETATM 2971 O HOH A 445 0.403 -42.968 -3.612 1.00 25.15 O -HETATM 2972 O HOH A 446 -7.421 -35.680 36.038 1.00 23.99 O -HETATM 2973 O HOH A 447 30.472 -48.622 8.290 1.00 27.71 O -HETATM 2974 O HOH A 448 24.588 -23.891 18.696 1.00 39.99 O -HETATM 2975 O HOH A 449 -4.227 -19.079 5.923 1.00 25.82 O -HETATM 2976 O HOH A 450 -16.376 -33.756 16.087 1.00 26.91 O -HETATM 2977 O HOH A 451 -5.542 -40.836 3.692 1.00 26.34 O -HETATM 2978 O HOH A 452 -13.062 -33.825 34.162 1.00 25.66 O -HETATM 2979 O HOH A 453 2.877 -40.653 -2.024 1.00 36.34 O -HETATM 2980 O HOH A 454 8.408 -43.660 28.127 1.00 26.95 O -HETATM 2981 O HOH A 455 23.336 -24.450 16.087 1.00 23.85 O -HETATM 2982 O HOH A 456 -6.877 -38.794 -1.320 1.00 29.85 O -HETATM 2983 O HOH A 457 6.574 -42.217 0.161 1.00 32.59 O -HETATM 2984 O HOH A 458 4.250 -56.808 24.850 1.00 29.79 O -HETATM 2985 O HOH A 459 18.670 -36.527 1.628 1.00 41.68 O -HETATM 2986 O HOH A 460 2.731 -37.384 38.612 1.00 40.20 O -HETATM 2987 O HOH A 461 -8.272 -42.805 6.840 1.00 21.73 O -HETATM 2988 O HOH A 462 29.512 -44.707 6.245 1.00 30.57 O -HETATM 2989 O HOH A 463 13.783 -31.554 1.480 1.00 26.91 O -HETATM 2990 O HOH A 464 19.473 -40.454 20.444 1.00 32.00 O -HETATM 2991 O HOH A 465 -12.156 -44.554 18.915 1.00 26.17 O -HETATM 2992 O HOH A 466 33.404 -34.346 22.535 1.00 40.28 O -HETATM 2993 O HOH A 467 24.614 -42.885 20.996 1.00 27.93 O -HETATM 2994 O HOH A 468 0.554 -47.234 33.162 1.00 31.37 O -HETATM 2995 O HOH A 469 -9.790 -34.492 20.818 1.00 32.61 O -HETATM 2996 O HOH A 470 2.873 -47.067 32.777 1.00 36.55 O -HETATM 2997 O HOH A 471 -5.167 -15.793 12.654 1.00 33.66 O -HETATM 2998 O HOH A 472 22.380 -51.519 3.454 1.00 30.05 O -HETATM 2999 O HOH A 473 -4.059 -51.031 37.829 1.00 36.69 O -HETATM 3000 O HOH A 474 -4.934 -46.758 37.318 1.00 29.20 O -HETATM 3001 O HOH A 475 -3.943 -35.056 37.565 1.00 26.44 O -HETATM 3002 O HOH A 476 42.444 -43.224 16.922 1.00 30.61 O -HETATM 3003 O HOH A 477 -1.280 -39.304 -3.392 1.00 28.50 O -HETATM 3004 O HOH A 478 -13.624 -53.509 28.381 1.00 31.89 O -HETATM 3005 O HOH A 479 36.688 -36.539 3.451 1.00 40.64 O -HETATM 3006 O HOH A 480 -11.940 -46.797 21.061 1.00 26.59 O -HETATM 3007 O HOH A 481 39.690 -30.436 14.892 1.00 22.81 O -HETATM 3008 O HOH A 482 -12.156 -35.922 36.712 1.00 31.35 O -HETATM 3009 O HOH A 483 11.129 -59.699 22.041 1.00 28.91 O -HETATM 3010 O HOH A 484 -12.156 -36.058 12.025 1.00 31.53 O -HETATM 3011 O HOH A 485 0.691 -35.685 38.432 1.00 29.26 O -HETATM 3012 O HOH A 486 -15.249 -28.824 25.276 1.00 33.35 O -HETATM 3013 O HOH A 487 -17.117 -32.681 26.885 1.00 29.66 O -HETATM 3014 O HOH A 488 16.588 -54.905 16.453 1.00 26.49 O -HETATM 3015 O HOH A 489 25.439 -56.069 9.491 1.00 29.14 O -HETATM 3016 O HOH A 490 45.408 -39.758 7.676 1.00 36.57 O -HETATM 3017 O HOH A 491 31.016 -52.455 6.147 1.00 49.61 O -HETATM 3018 O HOH A 492 -11.225 -39.951 12.195 1.00 30.54 O -HETATM 3019 O HOH A 493 -8.669 -30.348 26.891 1.00 32.98 O -HETATM 3020 O HOH A 494 -8.812 -56.960 28.616 1.00 38.66 O -HETATM 3021 O HOH A 495 5.944 -56.460 28.158 1.00 42.20 O -HETATM 3022 O HOH A 496 -6.596 -51.753 8.705 1.00 41.18 O -HETATM 3023 O HOH A 497 -11.037 -26.208 3.618 1.00 44.65 O -HETATM 3024 O HOH A 498 -3.234 -43.681 42.897 1.00 42.07 O -HETATM 3025 O HOH A 499 42.432 -41.227 10.656 1.00 32.84 O -HETATM 3026 O HOH A 500 31.718 -33.575 2.882 1.00 31.86 O -HETATM 3027 O HOH A 501 -9.625 -34.728 37.096 1.00 31.70 O -HETATM 3028 O HOH A 502 9.199 -52.110 1.314 1.00 40.53 O -HETATM 3029 O HOH A 503 20.046 -49.891 1.955 1.00 31.41 O -HETATM 3030 O HOH A 504 41.837 -42.981 12.600 1.00 27.78 O -HETATM 3031 O HOH A 505 -7.323 -50.590 14.907 1.00 28.55 O -HETATM 3032 O HOH A 506 -7.186 -53.302 30.877 1.00 26.87 O -HETATM 3033 O HOH A 507 9.388 -39.697 -1.489 1.00 30.55 O -HETATM 3034 O HOH A 508 -13.871 -42.218 18.577 1.00 29.56 O -HETATM 3035 O HOH A 509 -1.937 -55.736 13.465 1.00 31.56 O -HETATM 3036 O HOH A 510 -12.295 -43.120 34.267 1.00 42.79 O -HETATM 3037 O HOH A 511 15.669 -52.821 21.172 1.00 28.09 O -HETATM 3038 O HOH A 512 -3.645 -30.545 32.931 1.00 29.39 O -HETATM 3039 O HOH A 513 10.723 -61.471 14.569 1.00 35.50 O -HETATM 3040 O HOH A 514 43.133 -41.011 23.974 1.00 24.97 O -HETATM 3041 O HOH A 515 12.327 -58.376 -0.032 1.00 33.37 O -HETATM 3042 O HOH A 516 13.442 -35.011 -1.078 1.00 51.72 O -HETATM 3043 O HOH A 517 -11.705 -27.740 1.000 1.00 36.49 O -HETATM 3044 O HOH A 518 -5.860 -42.693 -1.803 1.00 34.88 O -HETATM 3045 O HOH A 519 17.950 -53.316 22.670 1.00 34.24 O -HETATM 3046 O HOH A 520 19.622 -57.566 15.677 1.00 37.57 O -HETATM 3047 O HOH A 521 -8.882 -41.271 44.550 1.00 47.56 O -HETATM 3048 O HOH A 522 -13.228 -50.239 28.060 1.00 33.31 O -HETATM 3049 O HOH A 523 0.028 -51.910 36.102 1.00 34.92 O -HETATM 3050 O HOH A 524 -1.579 -21.597 23.731 1.00 34.19 O -HETATM 3051 O HOH A 525 11.834 -60.657 -0.713 1.00 33.81 O -HETATM 3052 O HOH A 526 22.340 -29.992 3.535 1.00 33.35 O -HETATM 3053 O HOH A 527 -6.869 -48.041 6.855 1.00 44.06 O -HETATM 3054 O HOH A 528 25.428 -25.634 4.585 1.00 36.24 O -HETATM 3055 O HOH A 529 5.592 -46.281 30.843 1.00 37.42 O -HETATM 3056 O HOH A 530 34.118 -44.081 5.974 1.00 42.31 O -HETATM 3057 O HOH A 531 -9.727 -36.677 19.920 1.00 29.57 O -HETATM 3058 O HOH A 532 41.958 -44.391 20.994 1.00 32.80 O -HETATM 3059 O HOH A 533 29.946 -25.609 2.803 1.00 31.26 O -HETATM 3060 O HOH A 534 -16.297 -31.170 13.532 1.00 36.73 O -HETATM 3061 O HOH A 535 20.135 -21.628 3.369 1.00 36.24 O -HETATM 3062 O HOH A 536 -5.726 -12.160 15.693 1.00 35.86 O -HETATM 3063 O HOH A 537 15.438 -64.473 6.272 1.00 47.94 O -HETATM 3064 O HOH A 538 25.336 -60.721 15.449 1.00 44.65 O -HETATM 3065 O HOH A 539 36.246 -51.381 12.114 1.00 43.19 O -HETATM 3066 O HOH A 540 -10.406 -12.657 12.914 1.00 44.14 O -HETATM 3067 O HOH A 541 -4.024 -57.459 32.035 1.00 29.96 O -HETATM 3068 O HOH A 542 -9.628 -39.050 4.423 1.00 40.58 O -HETATM 3069 O HOH A 543 -11.825 -18.407 15.845 1.00 43.15 O -HETATM 3070 O HOH A 544 29.965 -49.690 5.661 1.00 36.88 O -HETATM 3071 O HOH A 545 1.589 -17.726 10.004 1.00 34.66 O -HETATM 3072 O HOH A 546 24.998 -45.095 0.252 1.00 45.15 O -HETATM 3073 O HOH A 547 40.331 -25.921 4.480 1.00 43.50 O -HETATM 3074 O HOH A 548 -9.017 -49.318 18.607 1.00 42.10 O -HETATM 3075 O HOH A 549 -17.098 -27.192 24.175 1.00 24.07 O -HETATM 3076 O HOH A 550 -11.582 -32.895 30.824 1.00 37.29 O -HETATM 3077 O HOH A 551 -13.016 -49.345 20.451 1.00 33.16 O -HETATM 3078 O HOH A 552 14.318 -55.182 21.070 1.00 30.29 O -HETATM 3079 O HOH A 553 -2.595 -32.555 34.139 1.00 32.88 O -HETATM 3080 O HOH A 554 11.397 -33.436 -1.627 1.00 36.25 O -HETATM 3081 O HOH A 555 18.931 -45.870 1.296 1.00 29.31 O -HETATM 3082 O HOH A 556 -8.316 -12.231 22.397 1.00 34.91 O -HETATM 3083 O HOH A 557 4.166 -56.597 4.985 1.00 33.50 O -HETATM 3084 O HOH A 558 0.796 -49.582 32.362 1.00 41.85 O -HETATM 3085 O HOH A 559 -11.599 -18.937 20.443 1.00 44.26 O -HETATM 3086 O HOH A 560 1.785 -52.390 30.681 1.00 27.95 O -HETATM 3087 O HOH A 561 4.156 -23.647 16.847 1.00 36.00 O -HETATM 3088 O HOH A 562 18.500 -51.548 0.573 1.00 33.29 O -HETATM 3089 O HOH A 563 -14.599 -49.080 30.299 1.00 37.03 O -HETATM 3090 O HOH A 564 33.863 -30.493 24.531 1.00 34.27 O -HETATM 3091 O HOH A 565 19.680 -40.421 -3.506 1.00 41.55 O -HETATM 3092 O HOH A 566 -7.157 -47.993 35.960 1.00 30.89 O -HETATM 3093 O HOH A 567 -5.034 -24.078 23.853 1.00 41.10 O -HETATM 3094 O HOH A 568 29.486 -55.523 7.750 1.00 38.26 O -HETATM 3095 O HOH A 569 -7.865 -50.118 38.360 1.00 46.08 O -HETATM 3096 O HOH A 570 25.449 -60.897 9.766 1.00 50.64 O -HETATM 3097 O HOH A 571 5.339 -41.809 -1.955 1.00 41.56 O -HETATM 3098 O HOH A 572 10.026 -51.195 32.720 1.00 36.14 O -HETATM 3099 O HOH A 573 -3.816 -27.684 28.935 1.00 48.98 O -HETATM 3100 O HOH A 574 -3.764 -62.391 26.213 1.00 54.21 O -HETATM 3101 O HOH A 575 18.609 -20.792 13.803 1.00 29.57 O -HETATM 3102 O HOH A 576 -5.911 -50.429 39.984 1.00 31.27 O -HETATM 3103 O HOH A 577 10.886 -54.346 1.006 1.00 27.43 O -HETATM 3104 O HOH A 578 7.886 -43.712 33.472 1.00 40.79 O -HETATM 3105 O HOH A 579 21.565 -56.109 3.123 1.00 31.07 O -HETATM 3106 O HOH A 580 26.921 -54.949 7.785 1.00 38.95 O -HETATM 3107 O HOH A 581 5.219 -37.752 -3.409 1.00 31.63 O -HETATM 3108 O HOH A 582 23.543 -26.288 2.871 1.00 38.05 O -HETATM 3109 O HOH A 583 -3.752 -37.691 -3.065 1.00 35.09 O -HETATM 3110 O HOH A 584 33.644 -52.199 13.564 1.00 32.43 O -HETATM 3111 O HOH A 585 12.975 -52.583 28.329 1.00 38.29 O -HETATM 3112 O HOH A 586 -7.329 -46.771 9.945 1.00 38.33 O -HETATM 3113 O HOH A 587 15.709 -24.026 20.958 1.00 37.85 O -HETATM 3114 O HOH A 588 -6.695 -29.987 28.212 1.00 41.24 O -HETATM 3115 O HOH A 589 2.114 -60.305 23.873 1.00 41.47 O -HETATM 3116 O HOH A 590 -12.107 -36.412 39.559 1.00 33.57 O -HETATM 3117 O HOH A 591 0.659 -37.607 -2.181 1.00 38.27 O -HETATM 3118 O HOH A 592 -7.474 -11.257 19.867 1.00 38.67 O -HETATM 3119 O HOH A 593 -0.958 -57.855 30.505 1.00 37.24 O -HETATM 3120 O HOH A 594 8.309 -39.434 34.616 1.00 28.39 O -HETATM 3121 O HOH A 595 7.165 -48.266 31.823 1.00 40.15 O -HETATM 3122 O HOH A 596 9.210 -44.839 30.298 1.00 42.43 O -HETATM 3123 O HOH A 597 38.333 -41.802 3.751 1.00 44.38 O -HETATM 3124 O HOH A 598 11.855 -49.430 30.513 1.00 44.09 O -HETATM 3125 O HOH A 599 -13.199 -49.022 17.846 1.00 43.38 O -HETATM 3126 O HOH A 600 -12.130 -33.036 13.150 1.00 41.24 O -HETATM 3127 O HOH A 601 2.030 -54.408 28.689 1.00 33.15 O -HETATM 3128 O HOH A 602 12.591 -52.701 2.190 1.00 31.39 O -HETATM 3129 O HOH A 603 -22.838 -42.228 38.659 1.00 41.52 O -HETATM 3130 O HOH A 604 43.553 -46.577 21.223 1.00 39.70 O -HETATM 3131 O HOH A 605 21.818 -33.439 0.661 1.00 34.62 O -HETATM 3132 O HOH A 606 6.823 -39.637 -2.417 1.00 38.12 O -HETATM 3133 O HOH A 607 -2.702 -45.750 44.276 1.00 48.77 O -HETATM 3134 O HOH A 608 -11.272 -31.729 1.446 1.00 39.82 O -HETATM 3135 O HOH A 609 32.326 -24.884 9.038 1.00 38.28 O -HETATM 3136 O HOH A 610 35.295 -25.089 -1.615 1.00 49.23 O -HETATM 3137 O HOH A 611 7.698 -50.635 34.147 1.00 44.01 O -HETATM 3138 O HOH A 612 9.908 -34.472 35.583 1.00 42.93 O -HETATM 3139 O HOH A 613 37.928 -49.254 7.995 1.00 33.32 O -HETATM 3140 O HOH A 614 23.152 -26.273 22.215 1.00 41.20 O -HETATM 3141 O HOH A 615 41.285 -28.672 16.660 1.00 35.58 O -HETATM 3142 O HOH A 616 20.942 -32.581 17.029 1.00 26.57 O -HETATM 3143 O HOH A 617 22.035 -38.838 19.645 1.00 32.26 O -HETATM 3144 O HOH A 618 12.202 -30.676 19.997 1.00 14.82 O -HETATM 3145 O HOH A 619 14.373 -33.985 25.464 1.00 38.59 O -HETATM 3146 O HOH A 620 43.061 -34.427 4.985 1.00 35.88 O -HETATM 3147 O HOH A 621 -0.776 -29.421 28.143 1.00 20.64 O -HETATM 3148 O HOH A 622 3.095 -22.818 13.914 1.00 27.75 O -HETATM 3149 O HOH A 623 9.209 -20.408 16.731 1.00 38.23 O -HETATM 3150 O HOH A 624 3.905 -62.107 18.929 1.00 27.78 O -HETATM 3151 O HOH A 625 -0.182 -59.831 16.492 1.00 25.49 O -HETATM 3152 O HOH A 626 19.234 -38.595 0.745 1.00 35.60 O -HETATM 3153 O HOH A 627 9.452 -30.821 34.123 1.00 45.46 O -HETATM 3154 O HOH A 628 -12.153 -25.558 0.203 1.00 36.58 O -HETATM 3155 O HOH A 629 12.513 -56.905 2.268 1.00 32.28 O -HETATM 3156 O HOH A 630 12.552 -43.701 -2.672 1.00 39.41 O -HETATM 3157 O HOH A 631 24.894 -50.854 2.690 1.00 47.58 O -HETATM 3158 O HOH A 632 16.843 -21.855 7.294 1.00 31.74 O -HETATM 3159 O HOH A 633 6.043 -30.978 -2.727 1.00 40.43 O -HETATM 3160 O HOH A 634 44.817 -28.772 11.400 1.00 34.20 O -HETATM 3161 O HOH A 635 23.360 -38.250 -0.120 1.00 35.95 O -HETATM 3162 O HOH A 636 23.070 -35.013 20.269 1.00 37.93 O -HETATM 3163 O HOH A 637 -1.905 -57.581 15.499 1.00 37.08 O -HETATM 3164 O HOH A 638 -7.143 -62.724 28.374 1.00 43.76 O -HETATM 3165 O HOH A 639 -6.909 -22.965 3.883 1.00 36.99 O -HETATM 3166 O HOH A 640 35.774 -34.414 23.348 1.00 45.32 O -HETATM 3167 O HOH A 641 -12.621 -31.610 10.278 1.00 33.08 O -HETATM 3168 O HOH A 642 -13.569 -36.962 14.949 1.00 39.45 O -HETATM 3169 O HOH A 643 40.843 -44.553 18.615 1.00 34.61 O -HETATM 3170 O HOH A 644 15.373 -14.592 15.843 1.00 43.78 O -HETATM 3171 O HOH A 645 -6.338 -22.228 6.340 1.00 37.51 O -HETATM 3172 O HOH A 646 -8.097 -20.886 7.364 1.00 46.49 O -HETATM 3173 O HOH A 647 -1.390 -14.623 14.431 1.00 40.72 O -HETATM 3174 O HOH A 648 12.668 -60.723 16.841 1.00 38.81 O -HETATM 3175 O HOH A 649 19.780 -34.799 -1.808 1.00 38.64 O -HETATM 3176 O HOH A 650 4.401 -40.543 40.978 1.00 43.07 O -HETATM 3177 O HOH A 651 9.323 -46.983 31.784 1.00 53.17 O -HETATM 3178 O HOH A 652 -17.525 -43.561 33.887 1.00 35.48 O -HETATM 3179 O HOH A 653 25.803 -54.363 3.372 1.00 35.60 O -HETATM 3180 O HOH A 654 42.827 -26.398 5.086 1.00 36.77 O -HETATM 3181 O HOH A 655 15.340 -43.345 -2.787 1.00 43.07 O -HETATM 3182 O HOH A 656 42.969 -31.562 10.198 1.00 36.97 O -HETATM 3183 O HOH A 657 33.204 -51.226 16.085 1.00 54.54 O -HETATM 3184 O HOH A 658 -5.037 -26.627 34.398 1.00 49.78 O -HETATM 3185 O HOH A 659 -1.910 -34.521 -2.811 1.00 41.69 O -HETATM 3186 O HOH A 660 32.752 -37.926 24.216 1.00 43.13 O -HETATM 3187 O HOH A 661 17.955 -18.788 10.146 1.00 40.71 O -HETATM 3188 O HOH A 662 41.125 -44.687 9.088 1.00 40.62 O -HETATM 3189 O HOH A 663 14.143 -18.449 8.697 1.00 44.61 O -HETATM 3190 O HOH A 664 32.632 -23.638 3.736 1.00 42.30 O -HETATM 3191 O HOH A 665 43.601 -34.187 12.677 1.00 38.07 O -HETATM 3192 O HOH A 666 44.029 -39.282 13.971 1.00 36.52 O -HETATM 3193 O HOH A 667 4.442 -61.705 9.312 1.00 43.23 O -HETATM 3194 O HOH A 668 -6.223 -27.476 27.565 1.00 57.32 O -HETATM 3195 O HOH A 669 25.591 -23.039 3.959 1.00 49.88 O -HETATM 3196 O HOH A 670 10.349 -47.112 -0.137 1.00 39.41 O -HETATM 3197 O HOH A 671 16.192 -62.081 7.266 1.00 49.49 O -HETATM 3198 O HOH A 672 11.988 -17.990 10.583 1.00 43.35 O -HETATM 3199 O HOH A 673 33.949 -53.866 15.617 1.00 53.72 O -HETATM 3200 O HOH A 674 -4.454 -28.624 36.023 1.00 55.78 O -HETATM 3201 O HOH A 675 -13.092 -20.997 17.495 1.00 45.73 O -HETATM 3202 O HOH A 676 38.424 -43.378 18.884 1.00 48.49 O -HETATM 3203 O HOH A 677 17.663 -51.580 24.458 1.00 49.03 O -HETATM 3204 O HOH A 678 -0.956 -26.433 28.785 1.00 40.13 O -HETATM 3205 O HOH A 679 -12.680 -40.260 17.294 1.00 35.21 O -HETATM 3206 O HOH A 680 11.973 -60.029 11.207 1.00 40.14 O -HETATM 3207 O HOH A 681 10.583 -20.475 2.116 1.00 36.94 O -HETATM 3208 O HOH A 682 -16.460 -32.838 24.455 1.00 31.74 O -HETATM 3209 O HOH A 683 11.946 -31.462 32.508 1.00 41.88 O -HETATM 3210 O HOH A 684 17.725 -33.871 21.326 1.00 31.82 O -HETATM 3211 O HOH A 685 17.274 -36.842 20.894 1.00 39.21 O -HETATM 3212 O HOH A 686 18.354 -35.010 19.012 1.00 27.88 O -CONECT 2784 2785 2789 -CONECT 2785 2784 2786 2806 -CONECT 2786 2785 2787 -CONECT 2787 2786 2788 2811 -CONECT 2788 2787 2789 2813 -CONECT 2789 2784 2788 -CONECT 2790 2807 -CONECT 2791 2807 -CONECT 2792 2815 -CONECT 2793 2815 -CONECT 2794 2815 -CONECT 2795 2796 2797 -CONECT 2796 2795 2808 -CONECT 2797 2795 2810 -CONECT 2798 2799 2809 -CONECT 2799 2798 2813 -CONECT 2800 2808 2810 -CONECT 2801 2809 2812 -CONECT 2802 2803 2814 -CONECT 2803 2802 2814 -CONECT 2804 2811 2812 -CONECT 2805 2808 2811 -CONECT 2806 2785 2814 -CONECT 2807 2790 2791 2809 -CONECT 2808 2796 2800 2805 -CONECT 2809 2798 2801 2807 -CONECT 2810 2797 2800 2815 -CONECT 2811 2787 2804 2805 -CONECT 2812 2801 2804 2813 -CONECT 2813 2788 2799 2812 -CONECT 2814 2802 2803 2806 -CONECT 2815 2792 2793 2794 2810 -CONECT 2816 2817 2818 2819 2820 -CONECT 2817 2816 -CONECT 2818 2816 -CONECT 2819 2816 -CONECT 2820 2816 -CONECT 2821 2822 2823 2824 2825 -CONECT 2822 2821 -CONECT 2823 2821 -CONECT 2824 2821 -CONECT 2825 2821 -CONECT 2826 2827 2828 2829 2830 -CONECT 2827 2826 -CONECT 2828 2826 -CONECT 2829 2826 -CONECT 2830 2826 -CONECT 2831 2832 2833 2834 2835 -CONECT 2832 2831 -CONECT 2833 2831 -CONECT 2834 2831 -CONECT 2835 2831 -CONECT 2836 2837 2838 -CONECT 2837 2836 -CONECT 2838 2836 2839 -CONECT 2839 2838 2840 -CONECT 2840 2839 2841 -CONECT 2841 2840 2842 -CONECT 2842 2841 -CONECT 2843 2844 2845 -CONECT 2844 2843 -CONECT 2845 2843 2846 -CONECT 2846 2845 -CONECT 2847 2848 2849 -CONECT 2848 2847 -CONECT 2849 2847 2850 -CONECT 2850 2849 -CONECT 2851 2852 2853 -CONECT 2852 2851 -CONECT 2853 2851 2854 -CONECT 2854 2853 -CONECT 2855 2856 2857 -CONECT 2856 2855 -CONECT 2857 2855 2858 -CONECT 2858 2857 -CONECT 2859 2860 2861 -CONECT 2860 2859 -CONECT 2861 2859 2862 -CONECT 2862 2861 -CONECT 2863 2864 2865 -CONECT 2864 2863 -CONECT 2865 2863 2866 -CONECT 2866 2865 -CONECT 2867 2868 2869 -CONECT 2868 2867 -CONECT 2869 2867 2870 -CONECT 2870 2869 -CONECT 2871 2872 2873 -CONECT 2872 2871 -CONECT 2873 2871 2874 -CONECT 2874 2873 -CONECT 2875 2876 2877 -CONECT 2876 2875 -CONECT 2877 2875 2878 -CONECT 2878 2877 -MASTER 473 0 15 20 9 0 32 6 3194 1 95 26 -END |