Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM 12-MAY-14 4PJ9 TITLE STRUCTURE OF HUMAN MR1-5-OP-RU IN COMPLEX WITH HUMAN MAIT TRAJ20 TCR COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I-RELATED GENE COMPND 3 PROTEIN; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP RESIDUES 23-292; COMPND 6 SYNONYM: MHC CLASS I-RELATED GENE PROTEIN,CLASS I HISTOCOMPATIBILITY COMPND 7 ANTIGEN-LIKE PROTEIN; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 12 CHAIN: B; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: TCR-ALPHA; COMPND 16 CHAIN: C; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: TCR-BETA; COMPND 20 CHAIN: D; COMPND 21 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: MR1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MR1, TCR, IMMUNE COMPLEX, 5-OP-RU, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.W.BIRKINSHAW,J.ROSSJOHN REVDAT 3 01-OCT-14 4PJ9 1 JRNL REVDAT 2 06-AUG-14 4PJ9 1 JRNL REVDAT 1 02-JUL-14 4PJ9 0 JRNL AUTH S.B.ECKLE,R.W.BIRKINSHAW,L.KOSTENKO,A.J.CORBETT, JRNL AUTH 2 H.E.MCWILLIAM,R.REANTRAGOON,Z.CHEN,N.A.GHERARDIN,T.BEDDOE, JRNL AUTH 3 L.LIU,O.PATEL,B.MEEHAN,D.P.FAIRLIE,J.A.VILLADANGOS, JRNL AUTH 4 D.I.GODFREY,L.KJER-NIELSEN,J.MCCLUSKEY,J.ROSSJOHN JRNL TITL A MOLECULAR BASIS UNDERPINNING THE T CELL RECEPTOR JRNL TITL 2 HETEROGENEITY OF MUCOSAL-ASSOCIATED INVARIANT T CELLS. JRNL REF J.EXP.MED. V. 211 1585 2014 JRNL REFN ESSN 1540-9538 JRNL PMID 25049336 JRNL DOI 10.1084/JEM.20140484 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.73 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 88733 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.199 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 4453 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.04 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6439 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2015 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6124 REMARK 3 BIN R VALUE (WORKING SET) : 0.1997 REMARK 3 BIN FREE R VALUE : 0.2377 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.89 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 315 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6114 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 35 REMARK 3 SOLVENT ATOMS : 795 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.58 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.38550 REMARK 3 B22 (A**2) : 0.38550 REMARK 3 B33 (A**2) : -0.77110 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.225 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.125 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.116 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.117 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.112 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 6441 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 8781 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2871 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 149 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 962 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 6441 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 830 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 7593 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.00 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.83 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.58 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 25 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: {A|0 - 55} REMARK 3 ORIGIN FOR THE GROUP (A): 7.8886 2.9884 23.8794 REMARK 3 T TENSOR REMARK 3 T11: -0.0007 T22: -0.0715 REMARK 3 T33: -0.0003 T12: -0.0067 REMARK 3 T13: 0.0161 T23: -0.0267 REMARK 3 L TENSOR REMARK 3 L11: 2.0074 L22: 1.0568 REMARK 3 L33: 1.0893 L12: -0.1014 REMARK 3 L13: -0.2420 L23: 0.0005 REMARK 3 S TENSOR REMARK 3 S11: 0.0374 S12: -0.0062 S13: -0.3171 REMARK 3 S21: 0.0741 S22: -0.0085 S23: 0.0024 REMARK 3 S31: 0.2213 S32: 0.0100 S33: -0.0288 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: {A|56 - 133} REMARK 3 ORIGIN FOR THE GROUP (A): 3.2291 13.1867 15.8540 REMARK 3 T TENSOR REMARK 3 T11: -0.0618 T22: -0.0666 REMARK 3 T33: -0.0661 T12: 0.0276 REMARK 3 T13: 0.0325 T23: -0.0265 REMARK 3 L TENSOR REMARK 3 L11: 1.6143 L22: 1.3448 REMARK 3 L33: 1.6652 L12: 0.1333 REMARK 3 L13: 0.2960 L23: -0.1446 REMARK 3 S TENSOR REMARK 3 S11: 0.0740 S12: 0.2053 S13: 0.0077 REMARK 3 S21: -0.1172 S22: -0.0296 S23: 0.1003 REMARK 3 S31: -0.0367 S32: -0.0952 S33: -0.0444 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: {A|134 - 182} REMARK 3 ORIGIN FOR THE GROUP (A): 13.7287 15.2215 19.2540 REMARK 3 T TENSOR REMARK 3 T11: -0.1011 T22: -0.1095 REMARK 3 T33: -0.1021 T12: -0.0130 REMARK 3 T13: 0.0386 T23: -0.0030 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.6521 REMARK 3 L33: 1.2558 L12: 0.4946 REMARK 3 L13: -0.2648 L23: 0.8708 REMARK 3 S TENSOR REMARK 3 S11: -0.0405 S12: -0.0229 S13: 0.0950 REMARK 3 S21: -0.0859 S22: 0.0965 S23: -0.0691 REMARK 3 S31: -0.1437 S32: -0.0331 S33: -0.0560 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: {A|183 - 270} REMARK 3 ORIGIN FOR THE GROUP (A): 29.8060 -11.9913 3.7492 REMARK 3 T TENSOR REMARK 3 T11: 0.0983 T22: 0.0167 REMARK 3 T33: 0.0280 T12: 0.0965 REMARK 3 T13: -0.0225 T23: -0.0479 REMARK 3 L TENSOR REMARK 3 L11: 2.8512 L22: 1.7931 REMARK 3 L33: 2.4521 L12: -0.8539 REMARK 3 L13: -0.8836 L23: 0.7346 REMARK 3 S TENSOR REMARK 3 S11: 0.1670 S12: 0.4914 S13: -0.1458 REMARK 3 S21: -0.3041 S22: -0.2272 S23: 0.0627 REMARK 3 S31: 0.0678 S32: -0.2257 S33: 0.0602 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: {B|0 - 11} REMARK 3 ORIGIN FOR THE GROUP (A): 7.0034 -8.7927 5.7020 REMARK 3 T TENSOR REMARK 3 T11: -0.1173 T22: -0.0690 REMARK 3 T33: -0.0456 T12: 0.0263 REMARK 3 T13: -0.0347 T23: -0.1196 REMARK 3 L TENSOR REMARK 3 L11: 3.4977 L22: 1.8763 REMARK 3 L33: 3.0899 L12: -2.1853 REMARK 3 L13: 2.8221 L23: -3.1764 REMARK 3 S TENSOR REMARK 3 S11: 0.1338 S12: 0.2873 S13: -0.4735 REMARK 3 S21: 0.1736 S22: -0.0522 S23: 0.1433 REMARK 3 S31: 0.1308 S32: 0.0403 S33: -0.0816 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: {B|12 - 19} REMARK 3 ORIGIN FOR THE GROUP (A): 22.0326 -25.0955 16.4361 REMARK 3 T TENSOR REMARK 3 T11: 0.0906 T22: -0.0761 REMARK 3 T33: 0.1746 T12: 0.0891 REMARK 3 T13: -0.1584 T23: -0.0889 REMARK 3 L TENSOR REMARK 3 L11: 2.5624 L22: 2.5473 REMARK 3 L33: 1.8886 L12: -1.3479 REMARK 3 L13: -4.1380 L23: -1.4853 REMARK 3 S TENSOR REMARK 3 S11: 0.0869 S12: -0.2242 S13: -0.6052 REMARK 3 S21: 0.1478 S22: -0.0631 S23: -0.0645 REMARK 3 S31: 0.2149 S32: 0.3157 S33: -0.0238 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: {B|20 - 41} REMARK 3 ORIGIN FOR THE GROUP (A): 6.5689 -13.9830 13.0068 REMARK 3 T TENSOR REMARK 3 T11: -0.1515 T22: -0.2261 REMARK 3 T33: 0.0288 T12: -0.0271 REMARK 3 T13: -0.0249 T23: -0.0667 REMARK 3 L TENSOR REMARK 3 L11: 4.0040 L22: 2.7714 REMARK 3 L33: 2.8544 L12: -3.0139 REMARK 3 L13: 2.0641 L23: -1.4646 REMARK 3 S TENSOR REMARK 3 S11: 0.2260 S12: 0.0302 S13: -0.7877 REMARK 3 S21: 0.1923 S22: 0.0603 S23: 0.5890 REMARK 3 S31: 0.2662 S32: -0.1630 S33: -0.2863 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: {B|42 - 51} REMARK 3 ORIGIN FOR THE GROUP (A): 3.3914 -22.3311 18.1495 REMARK 3 T TENSOR REMARK 3 T11: 0.1062 T22: -0.1251 REMARK 3 T33: 0.4453 T12: -0.0434 REMARK 3 T13: 0.0512 T23: 0.0254 REMARK 3 L TENSOR REMARK 3 L11: 2.8149 L22: 2.3901 REMARK 3 L33: 0.3772 L12: 1.6244 REMARK 3 L13: 1.6714 L23: -0.7086 REMARK 3 S TENSOR REMARK 3 S11: 0.1178 S12: -0.5625 S13: -0.7497 REMARK 3 S21: 0.1468 S22: 0.1377 S23: 0.5683 REMARK 3 S31: 0.1917 S32: -0.2716 S33: -0.2555 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: {B|52 - 61} REMARK 3 ORIGIN FOR THE GROUP (A): 7.1474 0.2743 13.5841 REMARK 3 T TENSOR REMARK 3 T11: -0.1226 T22: -0.1361 REMARK 3 T33: -0.1241 T12: 0.0190 REMARK 3 T13: 0.0170 T23: -0.0578 REMARK 3 L TENSOR REMARK 3 L11: 2.3811 L22: 5.2852 REMARK 3 L33: 2.3131 L12: -0.2983 REMARK 3 L13: -0.2762 L23: 1.8376 REMARK 3 S TENSOR REMARK 3 S11: 0.0048 S12: 0.0060 S13: -0.0993 REMARK 3 S21: 0.1056 S22: 0.0267 S23: 0.1485 REMARK 3 S31: 0.1480 S32: -0.1518 S33: -0.0315 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: {B|62 - 71} REMARK 3 ORIGIN FOR THE GROUP (A): 9.9833 -14.7895 17.2063 REMARK 3 T TENSOR REMARK 3 T11: -0.0839 T22: -0.1539 REMARK 3 T33: 0.0411 T12: -0.0285 REMARK 3 T13: -0.0172 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 1.7941 L22: 0.4464 REMARK 3 L33: 1.5199 L12: -0.6637 REMARK 3 L13: -0.3109 L23: 1.4032 REMARK 3 S TENSOR REMARK 3 S11: 0.0872 S12: -0.1149 S13: -0.5907 REMARK 3 S21: 0.4099 S22: 0.0254 S23: 0.2688 REMARK 3 S31: 0.3987 S32: -0.0879 S33: -0.1125 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: {B|72 - 77} REMARK 3 ORIGIN FOR THE GROUP (A): 13.3591 -32.1145 11.6457 REMARK 3 T TENSOR REMARK 3 T11: 0.2564 T22: -0.1675 REMARK 3 T33: 0.6116 T12: 0.0798 REMARK 3 T13: -0.2581 T23: -0.2017 REMARK 3 L TENSOR REMARK 3 L11: 1.3670 L22: 2.0140 REMARK 3 L33: 0.0473 L12: -0.2709 REMARK 3 L13: 1.0348 L23: 0.1529 REMARK 3 S TENSOR REMARK 3 S11: 0.0308 S12: 0.1960 S13: -0.0108 REMARK 3 S21: 0.0053 S22: -0.0316 S23: 0.0430 REMARK 3 S31: -0.0033 S32: -0.0241 S33: 0.0008 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: {B|78 - 90} REMARK 3 ORIGIN FOR THE GROUP (A): -0.0250 -15.9007 6.4722 REMARK 3 T TENSOR REMARK 3 T11: -0.1383 T22: -0.1019 REMARK 3 T33: 0.2843 T12: -0.0410 REMARK 3 T13: -0.1183 T23: -0.1090 REMARK 3 L TENSOR REMARK 3 L11: 0.0001 L22: 9.5884 REMARK 3 L33: 1.3251 L12: -1.4406 REMARK 3 L13: 0.2697 L23: 0.3852 REMARK 3 S TENSOR REMARK 3 S11: 0.1247 S12: 0.1969 S13: -0.7621 REMARK 3 S21: -0.1251 S22: 0.2272 S23: 0.3551 REMARK 3 S31: 0.2492 S32: -0.1257 S33: -0.3518 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: {B|91 - 97} REMARK 3 ORIGIN FOR THE GROUP (A): 9.9223 -22.0386 5.5616 REMARK 3 T TENSOR REMARK 3 T11: -0.1406 T22: -0.2184 REMARK 3 T33: 0.1322 T12: 0.0524 REMARK 3 T13: -0.1521 T23: -0.2150 REMARK 3 L TENSOR REMARK 3 L11: 0.0101 L22: 3.2251 REMARK 3 L33: 6.3980 L12: -0.9201 REMARK 3 L13: -0.7874 L23: 0.1007 REMARK 3 S TENSOR REMARK 3 S11: -0.0313 S12: 0.2021 S13: -0.0562 REMARK 3 S21: -0.2665 S22: 0.0518 S23: 0.1903 REMARK 3 S31: 0.3415 S32: 0.0607 S33: -0.0205 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: {C|2 - 17} REMARK 3 ORIGIN FOR THE GROUP (A): 13.8172 43.3815 39.1288 REMARK 3 T TENSOR REMARK 3 T11: -0.0073 T22: -0.0400 REMARK 3 T33: 0.0512 T12: -0.0237 REMARK 3 T13: 0.0283 T23: 0.0094 REMARK 3 L TENSOR REMARK 3 L11: 0.8872 L22: 2.6639 REMARK 3 L33: 3.5756 L12: 0.9608 REMARK 3 L13: 0.3435 L23: -1.3306 REMARK 3 S TENSOR REMARK 3 S11: 0.0809 S12: -0.0619 S13: 0.2317 REMARK 3 S21: 0.0966 S22: -0.1305 S23: -0.0566 REMARK 3 S31: -0.0889 S32: -0.0534 S33: 0.0496 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: {C|18 - 52} REMARK 3 ORIGIN FOR THE GROUP (A): 9.3708 34.8258 31.9886 REMARK 3 T TENSOR REMARK 3 T11: -0.1490 T22: -0.1774 REMARK 3 T33: -0.1118 T12: -0.0270 REMARK 3 T13: 0.0349 T23: -0.0060 REMARK 3 L TENSOR REMARK 3 L11: 0.6613 L22: 2.2462 REMARK 3 L33: 1.3256 L12: 0.1497 REMARK 3 L13: 0.1832 L23: 0.1863 REMARK 3 S TENSOR REMARK 3 S11: 0.0172 S12: 0.0367 S13: 0.1042 REMARK 3 S21: 0.0440 S22: -0.0510 S23: -0.0135 REMARK 3 S31: -0.0582 S32: -0.0984 S33: 0.0338 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: {C|53 - 75} REMARK 3 ORIGIN FOR THE GROUP (A): 15.2877 39.2907 26.8588 REMARK 3 T TENSOR REMARK 3 T11: -0.1059 T22: -0.1258 REMARK 3 T33: -0.0452 T12: -0.0441 REMARK 3 T13: 0.0458 T23: 0.0181 REMARK 3 L TENSOR REMARK 3 L11: 2.4004 L22: 8.9532 REMARK 3 L33: 3.6693 L12: -3.0589 REMARK 3 L13: -0.6457 L23: 1.1112 REMARK 3 S TENSOR REMARK 3 S11: 0.1294 S12: 0.2463 S13: 0.1601 REMARK 3 S21: -0.4333 S22: -0.1307 S23: -0.2121 REMARK 3 S31: -0.2828 S32: 0.0339 S33: 0.0012 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: {C|76 - 91} REMARK 3 ORIGIN FOR THE GROUP (A): 7.0617 44.3096 33.4292 REMARK 3 T TENSOR REMARK 3 T11: -0.0598 T22: -0.0438 REMARK 3 T33: 0.0593 T12: -0.0005 REMARK 3 T13: 0.0268 T23: 0.0036 REMARK 3 L TENSOR REMARK 3 L11: 0.8638 L22: 8.7896 REMARK 3 L33: 2.6377 L12: 0.3048 REMARK 3 L13: 0.1953 L23: -0.3516 REMARK 3 S TENSOR REMARK 3 S11: 0.1037 S12: 0.1792 S13: 0.1314 REMARK 3 S21: -0.0805 S22: -0.3662 S23: -0.0749 REMARK 3 S31: -0.1606 S32: -0.1676 S33: 0.2625 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: {C|92 - 116} REMARK 3 ORIGIN FOR THE GROUP (A): 8.6523 44.7360 38.6896 REMARK 3 T TENSOR REMARK 3 T11: 0.0339 T22: -0.0442 REMARK 3 T33: 0.0892 T12: -0.0024 REMARK 3 T13: 0.0453 T23: -0.0286 REMARK 3 L TENSOR REMARK 3 L11: 0.6860 L22: 4.3588 REMARK 3 L33: 1.3111 L12: 0.4506 REMARK 3 L13: -0.2418 L23: 1.1782 REMARK 3 S TENSOR REMARK 3 S11: 0.1497 S12: -0.0205 S13: 0.3137 REMARK 3 S21: 0.1831 S22: -0.1441 S23: -0.0069 REMARK 3 S31: -0.1896 S32: -0.0429 S33: -0.0056 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: {C|117 - 135} REMARK 3 ORIGIN FOR THE GROUP (A): -4.4064 66.6246 57.1449 REMARK 3 T TENSOR REMARK 3 T11: 0.2044 T22: -0.1534 REMARK 3 T33: 0.0692 T12: -0.0043 REMARK 3 T13: 0.1857 T23: -0.2746 REMARK 3 L TENSOR REMARK 3 L11: 0.7826 L22: 5.2755 REMARK 3 L33: 1.7515 L12: -3.7662 REMARK 3 L13: -0.7747 L23: 1.4556 REMARK 3 S TENSOR REMARK 3 S11: -0.0253 S12: -0.1607 S13: 0.3080 REMARK 3 S21: 0.5217 S22: -0.0814 S23: 0.2036 REMARK 3 S31: -0.3452 S32: -0.0817 S33: 0.1067 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: {C|136 - 145} REMARK 3 ORIGIN FOR THE GROUP (A): 9.5394 61.0788 50.0654 REMARK 3 T TENSOR REMARK 3 T11: 0.0367 T22: -0.1578 REMARK 3 T33: 0.0247 T12: 0.0065 REMARK 3 T13: 0.0301 T23: -0.2407 REMARK 3 L TENSOR REMARK 3 L11: 4.1295 L22: 1.7094 REMARK 3 L33: 3.9969 L12: 4.6122 REMARK 3 L13: 1.2923 L23: -2.5166 REMARK 3 S TENSOR REMARK 3 S11: 0.0954 S12: -0.0098 S13: 0.1971 REMARK 3 S21: 0.1420 S22: 0.0666 S23: -0.2108 REMARK 3 S31: 0.0651 S32: 0.3661 S33: -0.1619 REMARK 3 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: {C|146 - 164} REMARK 3 ORIGIN FOR THE GROUP (A): 0.5358 58.6824 50.7047 REMARK 3 T TENSOR REMARK 3 T11: 0.0003 T22: -0.1354 REMARK 3 T33: 0.0517 T12: 0.0049 REMARK 3 T13: 0.0693 T23: -0.1350 REMARK 3 L TENSOR REMARK 3 L11: 4.2994 L22: 4.7226 REMARK 3 L33: 4.9689 L12: 1.9586 REMARK 3 L13: -3.3962 L23: 1.5689 REMARK 3 S TENSOR REMARK 3 S11: 0.1498 S12: -0.2010 S13: 0.3495 REMARK 3 S21: 0.2589 S22: -0.2684 S23: -0.3801 REMARK 3 S31: 0.0749 S32: -0.0234 S33: 0.1186 REMARK 3 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: {C|165 - 198} REMARK 3 ORIGIN FOR THE GROUP (A): 5.5471 65.7548 54.5478 REMARK 3 T TENSOR REMARK 3 T11: 0.1383 T22: -0.1435 REMARK 3 T33: 0.1280 T12: -0.0554 REMARK 3 T13: 0.0727 T23: -0.2333 REMARK 3 L TENSOR REMARK 3 L11: 4.6685 L22: 5.4519 REMARK 3 L33: 8.6780 L12: -0.5048 REMARK 3 L13: 1.2338 L23: 0.0787 REMARK 3 S TENSOR REMARK 3 S11: 0.2187 S12: -0.4237 S13: 0.9648 REMARK 3 S21: 0.5708 S22: -0.2773 S23: -0.2104 REMARK 3 S31: -0.3762 S32: 0.0374 S33: 0.0586 REMARK 3 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: {D|2 - 107} REMARK 3 ORIGIN FOR THE GROUP (A): -6.4068 25.5439 41.0312 REMARK 3 T TENSOR REMARK 3 T11: -0.1272 T22: -0.0594 REMARK 3 T33: -0.1194 T12: -0.0463 REMARK 3 T13: 0.0661 T23: -0.0431 REMARK 3 L TENSOR REMARK 3 L11: 1.5538 L22: 2.4606 REMARK 3 L33: 2.4567 L12: 0.2863 REMARK 3 L13: -0.1900 L23: 0.1138 REMARK 3 S TENSOR REMARK 3 S11: 0.0628 S12: 0.0228 S13: -0.0061 REMARK 3 S21: 0.2425 S22: -0.1230 S23: 0.1936 REMARK 3 S31: -0.0003 S32: -0.1820 S33: 0.0602 REMARK 3 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: {D|108 - 122} REMARK 3 ORIGIN FOR THE GROUP (A): -11.2442 36.4711 59.3694 REMARK 3 T TENSOR REMARK 3 T11: 0.1579 T22: 0.0477 REMARK 3 T33: -0.1209 T12: -0.0474 REMARK 3 T13: 0.1853 T23: -0.1579 REMARK 3 L TENSOR REMARK 3 L11: 2.5833 L22: 3.3981 REMARK 3 L33: 0.0000 L12: -0.4223 REMARK 3 L13: -2.5906 L23: 1.0445 REMARK 3 S TENSOR REMARK 3 S11: 0.0653 S12: -0.5863 S13: 0.2176 REMARK 3 S21: 0.9348 S22: -0.0970 S23: 0.2399 REMARK 3 S31: 0.2882 S32: -0.0146 S33: 0.0317 REMARK 3 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: {D|123 - 239} REMARK 3 ORIGIN FOR THE GROUP (A): -11.1808 56.4299 51.9643 REMARK 3 T TENSOR REMARK 3 T11: -0.0804 T22: -0.1705 REMARK 3 T33: 0.0072 T12: 0.1039 REMARK 3 T13: 0.1828 T23: -0.1575 REMARK 3 L TENSOR REMARK 3 L11: 3.2741 L22: 5.6377 REMARK 3 L33: 2.7784 L12: 1.7353 REMARK 3 L13: -1.6174 L23: -0.9820 REMARK 3 S TENSOR REMARK 3 S11: 0.3376 S12: 0.1058 S13: 0.6388 REMARK 3 S21: 0.6084 S22: -0.1469 S23: 0.7601 REMARK 3 S31: -0.3664 S32: -0.3549 S33: -0.1908 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4PJ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-14. REMARK 100 THE DEPOSITION ID IS D_1000201516. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-AUG-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89271 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, BIS-TRIS PROPANE, SODIUM REMARK 280 ACETATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.07500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.78000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.78000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.03750 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.78000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.78000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 153.11250 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.78000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.78000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 51.03750 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.78000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.78000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 153.11250 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 102.07500 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A 190 REMARK 465 THR A 191 REMARK 465 PHE A 192 REMARK 465 PRO A 193 REMARK 465 ASP A 247 REMARK 465 PRO A 248 REMARK 465 GLN A 249 REMARK 465 SER A 250 REMARK 465 SER A 251 REMARK 465 ASP B 98 REMARK 465 MET B 99 REMARK 465 GLY C 1 REMARK 465 SER C 127 REMARK 465 ASP C 128 REMARK 465 ASN C 176 REMARK 465 LYS C 177 REMARK 465 SER C 178 REMARK 465 ASP C 179 REMARK 465 PHE C 180 REMARK 465 SER C 199 REMARK 465 PRO C 200 REMARK 465 GLU C 201 REMARK 465 SER C 202 REMARK 465 SER C 203 REMARK 465 ILE D 1 REMARK 465 SER D 217 REMARK 465 GLU D 218 REMARK 465 ASN D 219 REMARK 465 ASP D 220 REMARK 465 GLU D 221 REMARK 465 TRP D 222 REMARK 465 THR D 223 REMARK 465 GLN D 224 REMARK 465 GLY D 240 REMARK 465 ARG D 241 REMARK 465 ALA D 242 REMARK 465 ASP D 243 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 189 CG CD CE NZ REMARK 470 VAL A 195 CG1 CG2 REMARK 470 THR A 196 OG1 CG2 REMARK 470 GLU A 219 CG CD OE1 OE2 REMARK 470 GLU A 220 CG CD OE1 OE2 REMARK 470 GLU A 224 CG CD OE1 OE2 REMARK 470 MET B 0 CG SD CE REMARK 470 GLU B 36 CG CD OE1 OE2 REMARK 470 GLU B 44 CG CD OE1 OE2 REMARK 470 LYS B 48 CG CD CE NZ REMARK 470 GLU B 50 CG CD OE1 OE2 REMARK 470 LYS B 58 CG CD CE NZ REMARK 470 GLU B 74 CG CD OE1 OE2 REMARK 470 LYS B 75 CG CD CE NZ REMARK 470 ARG B 97 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 56 CG CD OE1 OE2 REMARK 470 GLN C 112 CG CD OE1 NE2 REMARK 470 ARG C 122 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 125 CG CD CE NZ REMARK 470 LYS C 129 CG CD CE NZ REMARK 470 GLN C 140 CG CD OE1 NE2 REMARK 470 LYS C 147 CG CD CE NZ REMARK 470 ASP C 148 CG OD1 OD2 REMARK 470 ASP C 150 CG OD1 OD2 REMARK 470 LYS C 156 CG CD CE NZ REMARK 470 ASP C 165 CG OD1 OD2 REMARK 470 ASN C 184 CG OD1 ND2 REMARK 470 ASP C 194 CG OD1 OD2 REMARK 470 ARG D 28 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 117 CG CD CE NZ REMARK 470 GLU D 131 CG CD OE1 OE2 REMARK 470 LYS D 163 CG CD CE NZ REMARK 470 GLN D 174 CG CD OE1 NE2 REMARK 470 ARG D 192 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 204 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 225 CG OD1 OD2 REMARK 470 LYS D 228 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 29 -126.03 55.49 REMARK 500 PHE A 119 -54.25 -120.65 REMARK 500 ASN A 146 77.24 -106.04 REMARK 500 TRP B 60 -5.09 81.06 REMARK 500 ASN C 3 116.00 -162.39 REMARK 500 VAL C 50 -27.08 -141.69 REMARK 500 SER D 87 -178.63 -171.99 REMARK 500 THR D 99 124.05 -25.24 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 C 379 DISTANCE = 6.03 ANGSTROMS REMARK 525 HOH D 351 DISTANCE = 6.78 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 101 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN B 83 OD1 REMARK 620 2 HIS B 84 O 84.0 REMARK 620 3 LEU B 87 O 100.8 80.3 REMARK 620 4 HOH B 274 O 98.2 176.3 96.4 REMARK 620 5 HOH B 262 O 170.8 90.5 70.9 86.9 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 2LJ A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 101 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4L4T RELATED DB: PDB REMARK 900 RELATED ID: 4NQC RELATED DB: PDB REMARK 900 RELATED ID: 4PJ5 RELATED DB: PDB REMARK 900 RELATED ID: 4PJ7 RELATED DB: PDB REMARK 900 RELATED ID: 4PJ8 RELATED DB: PDB REMARK 900 RELATED ID: 4PJA RELATED DB: PDB REMARK 900 RELATED ID: 4PJB RELATED DB: PDB REMARK 900 RELATED ID: 4PJC RELATED DB: PDB REMARK 900 RELATED ID: 4PJD RELATED DB: PDB REMARK 900 RELATED ID: 4PJE RELATED DB: PDB REMARK 900 RELATED ID: 4PJF RELATED DB: PDB REMARK 900 RELATED ID: 4PJG RELATED DB: PDB REMARK 900 RELATED ID: 4PJH RELATED DB: PDB REMARK 900 RELATED ID: 4PJX RELATED DB: PDB REMARK 900 RELATED ID: 4PJI RELATED DB: PDB DBREF 4PJ9 A 1 270 UNP Q95460 HMR1_HUMAN 23 292 DBREF 4PJ9 B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 4PJ9 C 1 203 PDB 4PJ9 4PJ9 1 203 DBREF 4PJ9 D 1 243 PDB 4PJ9 4PJ9 1 243 SEQADV 4PJ9 MET A 0 UNP Q95460 INITIATING METHIONINE SEQADV 4PJ9 SER A 261 UNP Q95460 CYS 283 ENGINEERED MUTATION SEQADV 4PJ9 MET B 0 UNP P61769 INITIATING METHIONINE SEQRES 1 A 271 MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL SEQRES 2 A 271 SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL SEQRES 3 A 271 GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER SEQRES 4 A 271 VAL THR ARG GLN LYS GLU PRO ARG ALA PRO TRP MET ALA SEQRES 5 A 271 GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN SEQRES 6 A 271 LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU SEQRES 7 A 271 LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS SEQRES 8 A 271 THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP SEQRES 9 A 271 GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY SEQRES 10 A 271 GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP SEQRES 11 A 271 LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA SEQRES 12 A 271 TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN SEQRES 13 A 271 TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE SEQRES 14 A 271 LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO SEQRES 15 A 271 PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY SEQRES 16 A 271 VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO SEQRES 17 A 271 PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU SEQRES 18 A 271 ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER SEQRES 19 A 271 GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU SEQRES 20 A 271 ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU SEQRES 21 A 271 HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 C 203 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR SEQRES 2 C 203 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR SEQRES 3 C 203 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA SEQRES 4 C 203 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP SEQRES 5 C 203 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER SEQRES 6 C 203 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU SEQRES 7 C 203 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL ARG SEQRES 8 C 203 ASP GLY ASP TYR LYS LEU SER PHE GLY ALA GLY THR THR SEQRES 9 C 203 VAL THR VAL ARG ALA ASN ILE GLN ASN PRO ASP PRO ALA SEQRES 10 C 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER SEQRES 11 C 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL SEQRES 12 C 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS SEQRES 13 C 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN SEQRES 14 C 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS SEQRES 15 C 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR SEQRES 16 C 203 PHE PHE PRO SER PRO GLU SER SER SEQRES 1 D 243 ILE ALA GLY ILE THR GLN ALA PRO THR SER GLN ILE LEU SEQRES 2 D 243 ALA ALA GLY ARG ARG MET THR LEU ARG CYS THR GLN ASP SEQRES 3 D 243 MET ARG HIS ASN ALA MET TYR TRP TYR ARG GLN ASP LEU SEQRES 4 D 243 GLY LEU GLY LEU ARG LEU ILE HIS TYR SER ASN THR ALA SEQRES 5 D 243 GLY THR THR GLY LYS GLY GLU VAL PRO ASP GLY TYR SER SEQRES 6 D 243 VAL SER ARG ALA ASN THR ASP ASP PHE PRO LEU THR LEU SEQRES 7 D 243 ALA SER ALA VAL PRO SER GLN THR SER VAL TYR PHE CYS SEQRES 8 D 243 ALA SER SER ALA GLY ALA SER THR GLY GLU LEU PHE PHE SEQRES 9 D 243 GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP LEU LYS SEQRES 10 D 243 ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER SEQRES 11 D 243 GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL SEQRES 12 D 243 CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SEQRES 13 D 243 SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL SEQRES 14 D 243 CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU SEQRES 15 D 243 ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL SEQRES 16 D 243 SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG SEQRES 17 D 243 CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU SEQRES 18 D 243 TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SEQRES 19 D 243 SER ALA GLU ALA TRP GLY ARG ALA ASP HET 2LJ A 301 22 HET GOL A 302 6 HET GOL A 303 6 HET NA B 101 1 HETNAM 2LJ 1-DEOXY-1-({2,6-DIOXO-5-[(E)-(2-OXOPROPYLIDENE)AMINO]- HETNAM 2 2LJ 1,2,3,6-TETRAHYDROPYRIMIDIN-4-YL}AMINO)-D-RIBITOL HETNAM GOL GLYCEROL HETNAM NA SODIUM ION HETSYN 2LJ 5-(2-OXOPROPYLIDENEAMINO)-6-D-RIBITYLAMINOURACIL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 2LJ C12 H18 N4 O7 FORMUL 6 GOL 2(C3 H8 O3) FORMUL 8 NA NA 1+ FORMUL 9 HOH *795(H2 O) HELIX 1 AA1 ALA A 47 GLU A 52 1 6 HELIX 2 AA2 ALA A 55 ASN A 85 1 31 HELIX 3 AA3 ASP A 133 ALA A 145 1 13 HELIX 4 AA4 ASN A 146 GLU A 159 1 14 HELIX 5 AA5 GLU A 159 GLY A 172 1 14 HELIX 6 AA6 GLY A 172 GLN A 177 1 6 HELIX 7 AA7 GLN C 79 SER C 83 5 5 HELIX 8 AA8 ARG C 162 ASP C 165 5 4 HELIX 9 AA9 CYS C 182 PHE C 186 1 5 HELIX 10 AB1 VAL D 82 THR D 86 5 5 HELIX 11 AB2 ASP D 115 VAL D 119 5 5 HELIX 12 AB3 SER D 130 GLN D 138 1 9 HELIX 13 AB4 ALA D 197 ASN D 202 1 6 SHEET 1 AA1 8 GLU A 44 PRO A 45 0 SHEET 2 AA1 8 HIS A 31 ASP A 37 -1 N THR A 35 O GLU A 44 SHEET 3 AA1 8 PHE A 22 VAL A 28 -1 N GLY A 26 O ILE A 33 SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N LEU A 10 O ILE A 23 SHEET 5 AA1 8 THR A 91 LEU A 100 -1 O TYR A 92 N GLY A 11 SHEET 6 AA1 8 THR A 106 TYR A 114 -1 O ALA A 113 N GLN A 93 SHEET 7 AA1 8 GLN A 117 ASN A 123 -1 O PHE A 119 N TYR A 112 SHEET 8 AA1 8 SER A 128 ALA A 131 -1 O LEU A 130 N ILE A 121 SHEET 1 AA2 4 LEU A 183 LYS A 189 0 SHEET 2 AA2 4 THR A 196 PHE A 205 -1 O PHE A 199 N ASN A 187 SHEET 3 AA2 4 TYR A 238 LEU A 246 -1 O LEU A 246 N THR A 196 SHEET 4 AA2 4 ASP A 226 PRO A 232 -1 N GLY A 228 O TRP A 241 SHEET 1 AA3 4 GLU A 220 ILE A 221 0 SHEET 2 AA3 4 TYR A 211 LYS A 216 -1 N LYS A 216 O GLU A 220 SHEET 3 AA3 4 TYR A 254 HIS A 260 -1 O HIS A 257 N THR A 213 SHEET 4 AA3 4 VAL A 263 GLN A 268 -1 O LEU A 267 N CYS A 256 SHEET 1 AA4 4 LYS B 6 SER B 11 0 SHEET 2 AA4 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA4 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21 SHEET 4 AA4 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AA5 4 LYS B 6 SER B 11 0 SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21 SHEET 4 AA5 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AA6 4 GLU B 44 ARG B 45 0 SHEET 2 AA6 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AA6 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38 SHEET 4 AA6 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82 SHEET 1 AA7 5 ASN C 3 ASP C 5 0 SHEET 2 AA7 5 VAL C 18 GLN C 25 -1 O THR C 23 N ASP C 5 SHEET 3 AA7 5 TYR C 70 LEU C 75 -1 O LEU C 73 N ILE C 20 SHEET 4 AA7 5 PHE C 60 SER C 65 -1 N SER C 61 O LEU C 74 SHEET 5 AA7 5 GLY C 53 LYS C 57 -1 N LYS C 57 O PHE C 60 SHEET 1 AA8 5 GLU C 9 THR C 13 0 SHEET 2 AA8 5 THR C 103 ARG C 108 1 O ARG C 108 N ALA C 12 SHEET 3 AA8 5 ALA C 84 ARG C 91 -1 N ALA C 84 O VAL C 105 SHEET 4 AA8 5 LEU C 32 GLN C 37 -1 N GLN C 37 O SER C 85 SHEET 5 AA8 5 THR C 44 ASN C 49 -1 O ASN C 49 N LEU C 32 SHEET 1 AA9 4 GLU C 9 THR C 13 0 SHEET 2 AA9 4 THR C 103 ARG C 108 1 O ARG C 108 N ALA C 12 SHEET 3 AA9 4 ALA C 84 ARG C 91 -1 N ALA C 84 O VAL C 105 SHEET 4 AA9 4 LEU C 97 PHE C 99 -1 O SER C 98 N VAL C 90 SHEET 1 AB1 8 TYR C 152 ILE C 153 0 SHEET 2 AB1 8 PHE C 166 TRP C 174 -1 O TRP C 174 N TYR C 152 SHEET 3 AB1 8 SER C 130 THR C 135 -1 N CYS C 132 O ALA C 173 SHEET 4 AB1 8 ALA C 117 ASP C 123 -1 N TYR C 119 O LEU C 133 SHEET 5 AB1 8 GLU D 123 GLU D 128 -1 O GLU D 128 N ARG C 122 SHEET 6 AB1 8 LYS D 139 PHE D 149 -1 O VAL D 143 N PHE D 127 SHEET 7 AB1 8 TYR D 187 SER D 196 -1 O LEU D 189 N ALA D 146 SHEET 8 AB1 8 VAL D 169 THR D 171 -1 N CYS D 170 O ARG D 192 SHEET 1 AB2 8 CYS C 157 MET C 161 0 SHEET 2 AB2 8 PHE C 166 TRP C 174 -1 O PHE C 166 N MET C 161 SHEET 3 AB2 8 SER C 130 THR C 135 -1 N CYS C 132 O ALA C 173 SHEET 4 AB2 8 ALA C 117 ASP C 123 -1 N TYR C 119 O LEU C 133 SHEET 5 AB2 8 GLU D 123 GLU D 128 -1 O GLU D 128 N ARG C 122 SHEET 6 AB2 8 LYS D 139 PHE D 149 -1 O VAL D 143 N PHE D 127 SHEET 7 AB2 8 TYR D 187 SER D 196 -1 O LEU D 189 N ALA D 146 SHEET 8 AB2 8 LEU D 176 LYS D 177 -1 N LEU D 176 O ALA D 188 SHEET 1 AB3 4 ILE D 4 ALA D 7 0 SHEET 2 AB3 4 MET D 19 GLN D 25 -1 O THR D 24 N THR D 5 SHEET 3 AB3 4 LEU D 76 LEU D 78 -1 O LEU D 76 N LEU D 21 SHEET 4 AB3 4 SER D 65 VAL D 66 -1 N SER D 65 O THR D 77 SHEET 1 AB4 6 SER D 10 ALA D 14 0 SHEET 2 AB4 6 SER D 108 LEU D 113 1 O THR D 111 N LEU D 13 SHEET 3 AB4 6 SER D 87 SER D 94 -1 N TYR D 89 O SER D 108 SHEET 4 AB4 6 ALA D 31 ASP D 38 -1 N TYR D 35 O PHE D 90 SHEET 5 AB4 6 GLY D 42 SER D 49 -1 O ILE D 46 N TRP D 34 SHEET 6 AB4 6 GLY D 56 LYS D 57 -1 O GLY D 56 N TYR D 48 SHEET 1 AB5 4 SER D 10 ALA D 14 0 SHEET 2 AB5 4 SER D 108 LEU D 113 1 O THR D 111 N LEU D 13 SHEET 3 AB5 4 SER D 87 SER D 94 -1 N TYR D 89 O SER D 108 SHEET 4 AB5 4 PHE D 103 PHE D 104 -1 O PHE D 103 N SER D 93 SHEET 1 AB6 4 LYS D 163 VAL D 165 0 SHEET 2 AB6 4 VAL D 154 VAL D 160 -1 N TRP D 158 O VAL D 165 SHEET 3 AB6 4 PHE D 207 PHE D 213 -1 O GLN D 210 N SER D 157 SHEET 4 AB6 4 GLN D 232 ALA D 238 -1 O ALA D 238 N PHE D 207 SSBOND 1 CYS A 98 CYS A 161 1555 1555 2.07 SSBOND 2 CYS A 200 CYS A 256 1555 1555 2.01 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03 SSBOND 4 CYS C 22 CYS C 88 1555 1555 2.07 SSBOND 5 CYS C 132 CYS C 182 1555 1555 2.04 SSBOND 6 CYS D 23 CYS D 91 1555 1555 2.03 SSBOND 7 CYS D 144 CYS D 209 1555 1555 2.03 LINK NZ LYS A 43 C7 2LJ A 301 1555 1555 1.34 LINK OD1 ASN B 83 NA NA B 101 1555 1555 2.63 LINK O HIS B 84 NA NA B 101 1555 1555 2.60 LINK O LEU B 87 NA NA B 101 1555 1555 2.40 LINK NA NA B 101 O HOH B 274 1555 1555 2.53 LINK NA NA B 101 O HOH B 262 1555 1555 2.71 CISPEP 1 TYR A 206 PRO A 207 0 5.09 CISPEP 2 HIS B 31 PRO B 32 0 8.32 CISPEP 3 ALA D 7 PRO D 8 0 -4.88 CISPEP 4 TYR D 150 PRO D 151 0 -1.59 SITE 1 AC1 18 TYR A 7 ARG A 9 SER A 24 LYS A 43 SITE 2 AC1 18 HIS A 58 TYR A 62 LEU A 66 TRP A 69 SITE 3 AC1 18 ARG A 94 ILE A 96 TYR A 152 GLN A 153 SITE 4 AC1 18 TRP A 156 HOH A 441 HOH A 443 HOH A 445 SITE 5 AC1 18 HOH A 458 TYR C 95 SITE 1 AC2 6 THR A 2 SER A 4 ASP A 29 GLU A 99 SITE 2 AC2 6 GLU A 209 HOH A 638 SITE 1 AC3 7 LEU A 231 TRP A 241 HOH A 493 HOH A 507 SITE 2 AC3 7 HOH A 546 GLN B 8 VAL B 9 SITE 1 AC4 5 ASN B 83 HIS B 84 LEU B 87 HOH B 262 SITE 2 AC4 5 HOH B 274 CRYST1 111.560 111.560 204.150 90.00 90.00 90.00 P 41 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008964 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008964 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004898 0.00000 ATOM 1 N MET A 0 32.611 7.583 20.463 1.00 37.33 N ANISOU 1 N MET A 0 3509 5191 5486 545 185 -511 N ATOM 2 CA MET A 0 31.364 6.840 20.330 1.00 35.42 C ANISOU 2 CA MET A 0 3410 4859 5188 575 184 -509 C ATOM 3 C MET A 0 30.966 6.662 18.871 1.00 36.83 C ANISOU 3 C MET A 0 3626 5026 5341 597 291 -545 C ATOM 4 O MET A 0 31.203 7.552 18.048 1.00 37.38 O ANISOU 4 O MET A 0 3652 5150 5399 549 371 -552 O ATOM 5 CB MET A 0 30.206 7.566 21.061 1.00 36.95 C ANISOU 5 CB MET A 0 3711 5015 5315 482 146 -485 C ATOM 6 CG MET A 0 30.183 7.368 22.565 1.00 41.54 C ANISOU 6 CG MET A 0 4305 5593 5887 477 33 -452 C ATOM 7 SD MET A 0 28.563 7.619 23.372 1.00 44.96 S ANISOU 7 SD MET A 0 4892 5959 6231 411 -3 -427 S ATOM 8 CE MET A 0 28.350 9.424 23.152 1.00 41.01 C ANISOU 8 CE MET A 0 4380 5489 5713 284 50 -451 C ATOM 9 N ARG A 1 30.285 5.547 18.567 1.00 29.41 N ANISOU 9 N ARG A 1 2773 4016 4387 664 291 -566 N ATOM 10 CA ARG A 1 29.665 5.294 17.258 1.00 27.17 C ANISOU 10 CA ARG A 1 2546 3720 4057 681 376 -613 C ATOM 11 C ARG A 1 28.466 6.241 17.112 1.00 26.05 C ANISOU 11 C ARG A 1 2495 3568 3834 584 392 -590 C ATOM 12 O ARG A 1 28.103 6.896 18.090 1.00 22.63 O ANISOU 12 O ARG A 1 2087 3119 3392 518 337 -548 O ATOM 13 CB ARG A 1 29.165 3.838 17.190 1.00 25.01 C ANISOU 13 CB ARG A 1 2345 3356 3802 764 353 -649 C ATOM 14 CG ARG A 1 30.297 2.803 17.227 1.00 33.19 C ANISOU 14 CG ARG A 1 3296 4384 4931 878 346 -673 C ATOM 15 CD ARG A 1 29.727 1.409 17.070 1.00 37.94 C ANISOU 15 CD ARG A 1 3977 4875 5563 954 334 -715 C ATOM 16 NE ARG A 1 28.885 1.020 18.208 1.00 29.65 N ANISOU 16 NE ARG A 1 3016 3732 4516 931 247 -655 N ATOM 17 CZ ARG A 1 29.233 0.103 19.107 1.00 35.79 C ANISOU 17 CZ ARG A 1 3786 4443 5370 1001 179 -612 C ATOM 18 NH1 ARG A 1 30.379 -0.558 18.982 1.00 30.41 N ANISOU 18 NH1 ARG A 1 3010 3767 4778 1106 185 -628 N ATOM 19 NH2 ARG A 1 28.397 -0.229 20.080 1.00 25.78 N ANISOU 19 NH2 ARG A 1 2605 3098 4093 975 111 -549 N ATOM 20 N THR A 2 27.809 6.277 15.942 1.00 22.22 N ANISOU 20 N THR A 2 2060 3095 3288 581 463 -621 N ATOM 21 CA THR A 2 26.593 7.088 15.823 1.00 21.92 C ANISOU 21 CA THR A 2 2107 3043 3178 502 471 -592 C ATOM 22 C THR A 2 25.493 6.466 16.696 1.00 22.42 C ANISOU 22 C THR A 2 2270 3015 3232 495 394 -584 C ATOM 23 O THR A 2 25.397 5.245 16.779 1.00 19.85 O ANISOU 23 O THR A 2 1974 2634 2935 558 366 -618 O ATOM 24 CB THR A 2 26.161 7.197 14.354 1.00 29.26 C ANISOU 24 CB THR A 2 3061 4023 4035 509 555 -622 C ATOM 25 OG1 THR A 2 27.173 7.938 13.695 1.00 30.77 O ANISOU 25 OG1 THR A 2 3156 4303 4232 503 630 -606 O ATOM 26 CG2 THR A 2 24.814 7.913 14.187 1.00 26.57 C ANISOU 26 CG2 THR A 2 2806 3668 3621 443 556 -588 C ATOM 27 N HIS A 3 24.687 7.295 17.359 1.00 17.99 N ANISOU 27 N HIS A 3 1759 2434 2641 420 366 -540 N ATOM 28 CA HIS A 3 23.563 6.780 18.150 1.00 16.98 C ANISOU 28 CA HIS A 3 1723 2230 2498 406 306 -527 C ATOM 29 C HIS A 3 22.325 7.637 17.871 1.00 20.42 C ANISOU 29 C HIS A 3 2223 2664 2872 339 329 -508 C ATOM 30 O HIS A 3 22.445 8.779 17.404 1.00 18.61 O ANISOU 30 O HIS A 3 1965 2483 2623 297 377 -487 O ATOM 31 CB HIS A 3 23.893 6.755 19.666 1.00 17.18 C ANISOU 31 CB HIS A 3 1739 2233 2556 395 228 -488 C ATOM 32 CG HIS A 3 24.984 5.796 20.051 1.00 20.76 C ANISOU 32 CG HIS A 3 2133 2682 3073 472 190 -492 C ATOM 33 ND1 HIS A 3 24.774 4.432 20.056 1.00 22.95 N ANISOU 33 ND1 HIS A 3 2449 2889 3382 540 169 -505 N ATOM 34 CD2 HIS A 3 26.249 6.042 20.463 1.00 22.86 C ANISOU 34 CD2 HIS A 3 2300 3002 3383 489 169 -483 C ATOM 35 CE1 HIS A 3 25.922 3.886 20.424 1.00 23.19 C ANISOU 35 CE1 HIS A 3 2406 2932 3475 607 139 -497 C ATOM 36 NE2 HIS A 3 26.841 4.816 20.679 1.00 23.73 N ANISOU 36 NE2 HIS A 3 2386 3083 3550 579 135 -485 N ATOM 37 N SER A 4 21.145 7.102 18.168 1.00 15.89 N ANISOU 37 N SER A 4 1730 2032 2275 329 298 -508 N ATOM 38 CA SER A 4 19.936 7.869 17.961 1.00 16.24 C ANISOU 38 CA SER A 4 1826 2077 2267 274 315 -487 C ATOM 39 C SER A 4 18.916 7.605 19.056 1.00 18.49 C ANISOU 39 C SER A 4 2176 2300 2549 244 263 -463 C ATOM 40 O SER A 4 18.877 6.526 19.662 1.00 17.89 O ANISOU 40 O SER A 4 2124 2171 2500 272 221 -466 O ATOM 41 CB SER A 4 19.321 7.563 16.588 1.00 20.31 C ANISOU 41 CB SER A 4 2364 2618 2734 292 357 -525 C ATOM 42 OG SER A 4 18.849 6.229 16.532 1.00 23.02 O ANISOU 42 OG SER A 4 2750 2907 3091 325 328 -572 O ATOM 43 N LEU A 5 18.054 8.575 19.257 1.00 15.24 N ANISOU 43 N LEU A 5 1792 1893 2107 190 274 -434 N ATOM 44 CA LEU A 5 16.921 8.456 20.174 1.00 13.99 C ANISOU 44 CA LEU A 5 1692 1689 1934 157 242 -412 C ATOM 45 C LEU A 5 15.682 8.789 19.377 1.00 17.21 C ANISOU 45 C LEU A 5 2132 2103 2304 135 271 -413 C ATOM 46 O LEU A 5 15.670 9.819 18.692 1.00 16.99 O ANISOU 46 O LEU A 5 2081 2116 2256 121 312 -399 O ATOM 47 CB LEU A 5 17.064 9.411 21.363 1.00 13.52 C ANISOU 47 CB LEU A 5 1627 1634 1875 114 225 -383 C ATOM 48 CG LEU A 5 15.777 9.654 22.245 1.00 15.46 C ANISOU 48 CG LEU A 5 1930 1851 2095 73 213 -361 C ATOM 49 CD1 LEU A 5 15.284 8.323 22.953 1.00 13.42 C ANISOU 49 CD1 LEU A 5 1716 1548 1836 89 171 -347 C ATOM 50 CD2 LEU A 5 16.057 10.753 23.300 1.00 14.27 C ANISOU 50 CD2 LEU A 5 1766 1716 1939 32 206 -354 C ATOM 51 N AARG A 6 14.663 7.921 19.436 0.50 13.20 N ANISOU 51 N AARG A 6 1669 1557 1790 133 250 -423 N ATOM 52 N BARG A 6 14.634 7.966 19.448 0.50 13.19 N ANISOU 52 N BARG A 6 1668 1556 1788 131 251 -422 N ATOM 53 CA AARG A 6 13.412 8.126 18.701 0.50 12.72 C ANISOU 53 CA AARG A 6 1630 1511 1694 112 266 -428 C ATOM 54 CA BARG A 6 13.401 8.347 18.753 0.50 12.51 C ANISOU 54 CA BARG A 6 1600 1488 1665 108 270 -421 C ATOM 55 C AARG A 6 12.178 7.788 19.536 0.50 14.42 C ANISOU 55 C AARG A 6 1886 1679 1914 78 243 -410 C ATOM 56 C BARG A 6 12.169 7.791 19.460 0.50 14.40 C ANISOU 56 C BARG A 6 1882 1678 1909 78 244 -411 C ATOM 57 O AARG A 6 12.217 6.833 20.314 0.50 13.02 O ANISOU 57 O AARG A 6 1731 1448 1766 80 213 -407 O ATOM 58 O BARG A 6 12.216 6.727 20.088 0.50 13.04 O ANISOU 58 O BARG A 6 1732 1452 1769 85 214 -416 O ATOM 59 CB AARG A 6 13.395 7.227 17.442 0.50 12.41 C ANISOU 59 CB AARG A 6 1588 1488 1641 145 272 -487 C ATOM 60 CB BARG A 6 13.403 7.981 17.251 0.50 12.64 C ANISOU 60 CB BARG A 6 1603 1550 1650 137 291 -465 C ATOM 61 CG AARG A 6 14.326 7.641 16.306 0.50 19.53 C ANISOU 61 CG AARG A 6 2447 2461 2514 178 312 -505 C ATOM 62 CG BARG A 6 13.303 6.514 16.949 0.50 19.68 C ANISOU 62 CG BARG A 6 2515 2403 2562 161 266 -527 C ATOM 63 CD AARG A 6 14.463 6.502 15.287 0.50 25.23 C ANISOU 63 CD AARG A 6 3170 3194 3224 218 313 -585 C ATOM 64 CD BARG A 6 14.199 6.160 15.788 0.50 26.31 C ANISOU 64 CD BARG A 6 3324 3288 3384 208 292 -583 C ATOM 65 NE AARG A 6 15.571 6.733 14.358 0.50 27.99 N ANISOU 65 NE AARG A 6 3474 3613 3548 258 358 -606 N ATOM 66 NE BARG A 6 14.343 4.720 15.752 0.50 29.30 N ANISOU 66 NE BARG A 6 3720 3604 3808 238 269 -647 N ATOM 67 CZ AARG A 6 15.426 7.194 13.123 0.50 51.59 C ANISOU 67 CZ AARG A 6 6447 6692 6462 266 396 -615 C ATOM 68 CZ BARG A 6 15.261 4.024 16.413 0.50 36.28 C ANISOU 68 CZ BARG A 6 4598 4430 4758 273 255 -649 C ATOM 69 NH1AARG A 6 14.219 7.459 12.644 0.50 44.45 N ANISOU 69 NH1AARG A 6 5566 5820 5502 241 385 -608 N ATOM 70 NH1BARG A 6 16.208 4.652 17.128 0.50 10.55 N ANISOU 70 NH1BARG A 6 1307 1187 1515 281 256 -596 N ATOM 71 NH2AARG A 6 16.488 7.386 12.351 0.50 49.99 N ANISOU 71 NH2AARG A 6 6201 6557 6237 302 445 -628 N ATOM 72 NH2BARG A 6 15.256 2.702 16.359 0.50 22.12 N ANISOU 72 NH2BARG A 6 2824 2561 3018 301 237 -703 N ATOM 73 N TYR A 7 11.064 8.524 19.332 1.00 11.49 N ANISOU 73 N TYR A 7 1520 1330 1516 49 259 -390 N ATOM 74 CA TYR A 7 9.773 8.154 19.926 1.00 11.62 C ANISOU 74 CA TYR A 7 1564 1314 1538 16 245 -378 C ATOM 75 C TYR A 7 8.736 8.102 18.847 1.00 14.46 C ANISOU 75 C TYR A 7 1914 1707 1873 9 248 -398 C ATOM 76 O TYR A 7 8.659 9.021 18.022 1.00 13.88 O ANISOU 76 O TYR A 7 1816 1690 1765 20 271 -386 O ATOM 77 CB TYR A 7 9.323 9.128 21.013 1.00 12.26 C ANISOU 77 CB TYR A 7 1653 1392 1615 -13 259 -335 C ATOM 78 CG TYR A 7 10.233 9.182 22.214 1.00 13.44 C ANISOU 78 CG TYR A 7 1811 1523 1773 -14 246 -320 C ATOM 79 CD1 TYR A 7 10.067 8.294 23.280 1.00 14.75 C ANISOU 79 CD1 TYR A 7 2007 1653 1947 -24 220 -302 C ATOM 80 CD2 TYR A 7 11.205 10.177 22.330 1.00 14.07 C ANISOU 80 CD2 TYR A 7 1866 1626 1853 -10 259 -320 C ATOM 81 CE1 TYR A 7 10.865 8.384 24.425 1.00 16.31 C ANISOU 81 CE1 TYR A 7 2209 1853 2135 -22 200 -283 C ATOM 82 CE2 TYR A 7 11.974 10.304 23.485 1.00 15.09 C ANISOU 82 CE2 TYR A 7 1997 1754 1984 -16 238 -315 C ATOM 83 CZ TYR A 7 11.814 9.393 24.519 1.00 19.07 C ANISOU 83 CZ TYR A 7 2531 2237 2479 -18 205 -297 C ATOM 84 OH TYR A 7 12.601 9.513 25.635 1.00 15.71 O ANISOU 84 OH TYR A 7 2103 1828 2039 -20 177 -289 O ATOM 85 N PHE A 8 7.885 7.078 18.895 1.00 11.80 N ANISOU 85 N PHE A 8 1593 1336 1556 -12 225 -422 N ATOM 86 CA PHE A 8 6.766 6.939 17.962 1.00 12.16 C ANISOU 86 CA PHE A 8 1621 1419 1579 -27 216 -450 C ATOM 87 C PHE A 8 5.450 7.025 18.674 1.00 14.86 C ANISOU 87 C PHE A 8 1962 1745 1939 -70 215 -419 C ATOM 88 O PHE A 8 5.349 6.641 19.826 1.00 14.51 O ANISOU 88 O PHE A 8 1941 1643 1929 -93 216 -392 O ATOM 89 CB PHE A 8 6.809 5.580 17.225 1.00 14.67 C ANISOU 89 CB PHE A 8 1947 1714 1915 -25 189 -529 C ATOM 90 CG PHE A 8 7.951 5.438 16.251 1.00 17.94 C ANISOU 90 CG PHE A 8 2352 2163 2300 23 197 -578 C ATOM 91 CD1 PHE A 8 9.210 5.013 16.685 1.00 20.52 C ANISOU 91 CD1 PHE A 8 2690 2442 2663 56 202 -582 C ATOM 92 CD2 PHE A 8 7.743 5.602 14.886 1.00 18.98 C ANISOU 92 CD2 PHE A 8 2461 2382 2369 38 197 -623 C ATOM 93 CE1 PHE A 8 10.247 4.792 15.765 1.00 21.56 C ANISOU 93 CE1 PHE A 8 2807 2609 2776 103 216 -634 C ATOM 94 CE2 PHE A 8 8.766 5.319 13.966 1.00 21.49 C ANISOU 94 CE2 PHE A 8 2771 2738 2655 82 212 -679 C ATOM 95 CZ PHE A 8 10.022 4.982 14.417 1.00 19.69 C ANISOU 95 CZ PHE A 8 2551 2461 2471 115 226 -682 C ATOM 96 N ARG A 9 4.432 7.471 17.977 1.00 12.02 N ANISOU 96 N ARG A 9 1571 1442 1554 -80 212 -419 N ATOM 97 CA ARG A 9 3.062 7.427 18.472 1.00 12.97 C ANISOU 97 CA ARG A 9 1675 1557 1697 -120 210 -399 C ATOM 98 C ARG A 9 2.274 6.765 17.399 1.00 15.71 C ANISOU 98 C ARG A 9 1992 1943 2035 -137 175 -456 C ATOM 99 O ARG A 9 2.475 7.071 16.223 1.00 15.54 O ANISOU 99 O ARG A 9 1951 1994 1959 -108 163 -481 O ATOM 100 CB ARG A 9 2.492 8.830 18.811 1.00 13.16 C ANISOU 100 CB ARG A 9 1675 1619 1706 -111 242 -339 C ATOM 101 CG ARG A 9 3.215 9.523 19.927 1.00 13.71 C ANISOU 101 CG ARG A 9 1773 1651 1785 -102 275 -301 C ATOM 102 CD ARG A 9 2.639 10.892 20.268 1.00 12.52 C ANISOU 102 CD ARG A 9 1601 1522 1634 -92 312 -257 C ATOM 103 NE ARG A 9 3.627 11.553 21.138 1.00 13.04 N ANISOU 103 NE ARG A 9 1695 1555 1703 -84 338 -246 N ATOM 104 CZ ARG A 9 3.674 12.855 21.385 1.00 16.99 C ANISOU 104 CZ ARG A 9 2187 2056 2213 -69 374 -223 C ATOM 105 NH1 ARG A 9 2.722 13.656 20.931 1.00 10.62 N ANISOU 105 NH1 ARG A 9 1347 1274 1416 -53 394 -195 N ATOM 106 NH2 ARG A 9 4.687 13.369 22.063 1.00 12.41 N ANISOU 106 NH2 ARG A 9 1628 1449 1638 -69 388 -229 N ATOM 107 N LEU A 10 1.345 5.880 17.777 1.00 13.77 N ANISOU 107 N LEU A 10 1737 1656 1837 -189 160 -475 N ATOM 108 CA LEU A 10 0.447 5.241 16.831 1.00 13.21 C ANISOU 108 CA LEU A 10 1628 1624 1767 -220 120 -540 C ATOM 109 C LEU A 10 -0.986 5.379 17.383 1.00 18.10 C ANISOU 109 C LEU A 10 2203 2253 2423 -267 124 -505 C ATOM 110 O LEU A 10 -1.248 4.994 18.524 1.00 17.65 O ANISOU 110 O LEU A 10 2162 2123 2421 -303 149 -469 O ATOM 111 CB LEU A 10 0.831 3.752 16.618 1.00 13.65 C ANISOU 111 CB LEU A 10 1712 1603 1873 -245 95 -623 C ATOM 112 CG LEU A 10 -0.211 2.872 15.879 1.00 19.75 C ANISOU 112 CG LEU A 10 2444 2388 2672 -300 52 -707 C ATOM 113 CD1 LEU A 10 -0.303 3.224 14.385 1.00 20.79 C ANISOU 113 CD1 LEU A 10 2539 2645 2713 -272 16 -773 C ATOM 114 CD2 LEU A 10 0.106 1.369 16.004 1.00 21.32 C ANISOU 114 CD2 LEU A 10 2678 2467 2957 -334 40 -780 C ATOM 115 N GLY A 11 -1.882 5.896 16.564 1.00 15.24 N ANISOU 115 N GLY A 11 1780 1986 2025 -265 101 -511 N ATOM 116 CA GLY A 11 -3.294 6.062 16.894 1.00 15.52 C ANISOU 116 CA GLY A 11 1752 2049 2094 -304 100 -485 C ATOM 117 C GLY A 11 -4.113 5.312 15.866 1.00 20.77 C ANISOU 117 C GLY A 11 2362 2770 2760 -345 40 -566 C ATOM 118 O GLY A 11 -3.810 5.361 14.675 1.00 19.88 O ANISOU 118 O GLY A 11 2241 2734 2580 -315 0 -617 O ATOM 119 N VAL A 12 -5.096 4.547 16.320 1.00 18.75 N ANISOU 119 N VAL A 12 2068 2476 2579 -417 33 -585 N ATOM 120 CA VAL A 12 -5.969 3.743 15.455 1.00 21.34 C ANISOU 120 CA VAL A 12 2333 2849 2926 -475 -28 -675 C ATOM 121 C VAL A 12 -7.394 4.083 15.864 1.00 26.85 C ANISOU 121 C VAL A 12 2941 3593 3667 -513 -23 -630 C ATOM 122 O VAL A 12 -7.717 4.042 17.057 1.00 27.66 O ANISOU 122 O VAL A 12 3049 3627 3834 -543 32 -568 O ATOM 123 CB VAL A 12 -5.675 2.204 15.556 1.00 25.80 C ANISOU 123 CB VAL A 12 2937 3295 3571 -542 -41 -762 C ATOM 124 CG1 VAL A 12 -6.599 1.396 14.630 1.00 27.15 C ANISOU 124 CG1 VAL A 12 3038 3510 3768 -611 -108 -875 C ATOM 125 CG2 VAL A 12 -4.200 1.878 15.263 1.00 24.88 C ANISOU 125 CG2 VAL A 12 2906 3125 3424 -492 -36 -801 C ATOM 126 N SER A 13 -8.233 4.437 14.912 1.00 23.11 N ANISOU 126 N SER A 13 2383 3246 3153 -509 -77 -656 N ATOM 127 CA SER A 13 -9.615 4.752 15.253 1.00 23.90 C ANISOU 127 CA SER A 13 2382 3399 3301 -541 -75 -616 C ATOM 128 C SER A 13 -10.423 3.469 15.153 1.00 30.63 C ANISOU 128 C SER A 13 3179 4221 4238 -649 -113 -703 C ATOM 129 O SER A 13 -10.085 2.627 14.334 1.00 29.96 O ANISOU 129 O SER A 13 3113 4130 4142 -680 -168 -811 O ATOM 130 CB SER A 13 -10.151 5.841 14.327 1.00 25.85 C ANISOU 130 CB SER A 13 2552 3800 3468 -473 -117 -584 C ATOM 131 OG SER A 13 -10.134 5.401 12.976 1.00 26.57 O ANISOU 131 OG SER A 13 2619 3986 3491 -480 -203 -677 O ATOM 132 N ASP A 14 -11.460 3.287 15.988 1.00 31.81 N ANISOU 132 N ASP A 14 3262 4345 4478 -712 -79 -665 N ATOM 133 CA ASP A 14 -12.290 2.060 15.988 1.00 34.64 C ANISOU 133 CA ASP A 14 3560 4661 4940 -830 -106 -740 C ATOM 134 C ASP A 14 -11.405 0.781 15.971 1.00 38.64 C ANISOU 134 C ASP A 14 4160 5028 5495 -880 -111 -820 C ATOM 135 O ASP A 14 -11.537 -0.013 15.040 1.00 38.46 O ANISOU 135 O ASP A 14 4112 5017 5486 -930 -180 -943 O ATOM 136 CB ASP A 14 -13.250 2.042 14.767 1.00 38.98 C ANISOU 136 CB ASP A 14 3990 5357 5465 -856 -202 -823 C ATOM 137 CG ASP A 14 -14.350 3.087 14.739 1.00 58.85 C ANISOU 137 CG ASP A 14 6387 8010 7965 -819 -208 -751 C ATOM 138 OD1 ASP A 14 -14.314 4.018 15.579 1.00 60.26 O ANISOU 138 OD1 ASP A 14 6581 8177 8138 -756 -133 -637 O ATOM 139 OD2 ASP A 14 -15.241 2.983 13.864 1.00 69.62 O ANISOU 139 OD2 ASP A 14 7638 9494 9320 -850 -290 -812 O ATOM 140 N PRO A 15 -10.458 0.578 16.923 1.00 35.62 N ANISOU 140 N PRO A 15 3883 4516 5134 -860 -44 -759 N ATOM 141 CA PRO A 15 -9.600 -0.620 16.833 1.00 36.52 C ANISOU 141 CA PRO A 15 4079 4496 5300 -893 -52 -832 C ATOM 142 C PRO A 15 -10.360 -1.917 17.124 1.00 46.17 C ANISOU 142 C PRO A 15 5262 5612 6668 -1017 -52 -878 C ATOM 143 O PRO A 15 -11.396 -1.876 17.796 1.00 44.88 O ANISOU 143 O PRO A 15 5027 5457 6569 -1077 -17 -817 O ATOM 144 CB PRO A 15 -8.524 -0.361 17.889 1.00 36.80 C ANISOU 144 CB PRO A 15 4218 4443 5320 -833 18 -731 C ATOM 145 CG PRO A 15 -9.187 0.541 18.899 1.00 39.62 C ANISOU 145 CG PRO A 15 4538 4846 5669 -823 78 -611 C ATOM 146 CD PRO A 15 -10.124 1.401 18.113 1.00 35.44 C ANISOU 146 CD PRO A 15 3907 4469 5090 -805 38 -630 C ATOM 147 N ILE A 16 -9.841 -3.069 16.632 1.00 46.99 N ANISOU 147 N ILE A 16 5412 5610 6833 -1056 -83 -986 N ATOM 148 CA ILE A 16 -10.445 -4.386 16.908 1.00 50.61 C ANISOU 148 CA ILE A 16 5844 5933 7452 -1178 -77 -1034 C ATOM 149 C ILE A 16 -10.243 -4.712 18.404 1.00 57.63 C ANISOU 149 C ILE A 16 6791 6683 8423 -1195 16 -889 C ATOM 150 O ILE A 16 -9.389 -4.096 19.060 1.00 55.26 O ANISOU 150 O ILE A 16 6567 6381 8049 -1108 59 -790 O ATOM 151 CB ILE A 16 -9.910 -5.526 15.987 1.00 55.15 C ANISOU 151 CB ILE A 16 6458 6416 8082 -1210 -130 -1198 C ATOM 152 CG1 ILE A 16 -8.379 -5.721 16.126 1.00 55.18 C ANISOU 152 CG1 ILE A 16 6588 6322 8056 -1120 -103 -1186 C ATOM 153 CG2 ILE A 16 -10.330 -5.314 14.528 1.00 56.60 C ANISOU 153 CG2 ILE A 16 6569 6756 8181 -1214 -225 -1350 C ATOM 154 CD1 ILE A 16 -7.877 -7.154 15.952 1.00 61.98 C ANISOU 154 CD1 ILE A 16 7504 6997 9050 -1165 -107 -1287 C ATOM 155 N HIS A 17 -11.028 -5.662 18.940 1.00 58.37 N ANISOU 155 N HIS A 17 6845 6668 8666 -1310 45 -875 N ATOM 156 CA HIS A 17 -10.969 -6.052 20.351 1.00 59.77 C ANISOU 156 CA HIS A 17 7068 6723 8920 -1337 135 -727 C ATOM 157 C HIS A 17 -9.535 -6.442 20.771 1.00 61.75 C ANISOU 157 C HIS A 17 7451 6849 9162 -1263 159 -684 C ATOM 158 O HIS A 17 -8.833 -7.130 20.024 1.00 62.09 O ANISOU 158 O HIS A 17 7540 6811 9239 -1250 115 -794 O ATOM 159 CB HIS A 17 -11.957 -7.200 20.632 1.00 63.62 C ANISOU 159 CB HIS A 17 7493 7094 9587 -1482 158 -737 C ATOM 160 CG HIS A 17 -12.112 -7.503 22.089 1.00 68.32 C ANISOU 160 CG HIS A 17 8115 7594 10248 -1516 258 -565 C ATOM 161 ND1 HIS A 17 -11.452 -8.571 22.677 1.00 71.26 N ANISOU 161 ND1 HIS A 17 8576 7774 10726 -1536 297 -510 N ATOM 162 CD2 HIS A 17 -12.813 -6.842 23.041 1.00 70.44 C ANISOU 162 CD2 HIS A 17 8336 7947 10481 -1524 328 -436 C ATOM 163 CE1 HIS A 17 -11.789 -8.539 23.957 1.00 71.17 C ANISOU 163 CE1 HIS A 17 8569 7742 10731 -1560 386 -342 C ATOM 164 NE2 HIS A 17 -12.603 -7.513 24.225 1.00 70.97 N ANISOU 164 NE2 HIS A 17 8463 7882 10619 -1555 410 -299 N ATOM 165 N GLY A 18 -9.107 -5.933 21.925 1.00 56.10 N ANISOU 165 N GLY A 18 6790 6135 8391 -1207 224 -534 N ATOM 166 CA GLY A 18 -7.777 -6.178 22.476 1.00 54.87 C ANISOU 166 CA GLY A 18 6747 5884 8215 -1131 245 -471 C ATOM 167 C GLY A 18 -6.657 -5.314 21.913 1.00 56.42 C ANISOU 167 C GLY A 18 6994 6169 8275 -1011 206 -513 C ATOM 168 O GLY A 18 -5.521 -5.398 22.393 1.00 57.16 O ANISOU 168 O GLY A 18 7171 6204 8343 -940 221 -458 O ATOM 169 N VAL A 19 -6.949 -4.476 20.897 1.00 49.13 N ANISOU 169 N VAL A 19 6015 5387 7263 -985 157 -603 N ATOM 170 CA VAL A 19 -5.933 -3.623 20.268 1.00 45.95 C ANISOU 170 CA VAL A 19 5652 5072 6734 -878 126 -640 C ATOM 171 C VAL A 19 -6.049 -2.185 20.820 1.00 41.06 C ANISOU 171 C VAL A 19 5018 4581 6001 -820 158 -545 C ATOM 172 O VAL A 19 -7.130 -1.599 20.780 1.00 39.18 O ANISOU 172 O VAL A 19 4702 4437 5749 -851 162 -533 O ATOM 173 CB VAL A 19 -5.987 -3.676 18.719 1.00 50.89 C ANISOU 173 CB VAL A 19 6241 5767 7328 -874 53 -797 C ATOM 174 CG1 VAL A 19 -5.130 -2.584 18.083 1.00 49.45 C ANISOU 174 CG1 VAL A 19 6082 5705 7003 -768 33 -810 C ATOM 175 CG2 VAL A 19 -5.547 -5.046 18.220 1.00 52.36 C ANISOU 175 CG2 VAL A 19 6463 5812 7619 -909 29 -905 C ATOM 176 N PRO A 20 -4.952 -1.610 21.365 1.00 33.15 N ANISOU 176 N PRO A 20 4087 3583 4927 -738 181 -480 N ATOM 177 CA PRO A 20 -5.055 -0.244 21.902 1.00 29.49 C ANISOU 177 CA PRO A 20 3612 3227 4368 -688 214 -405 C ATOM 178 C PRO A 20 -5.312 0.806 20.816 1.00 28.00 C ANISOU 178 C PRO A 20 3369 3170 4099 -646 177 -462 C ATOM 179 O PRO A 20 -4.807 0.728 19.699 1.00 24.40 O ANISOU 179 O PRO A 20 2919 2739 3612 -617 127 -546 O ATOM 180 CB PRO A 20 -3.694 -0.004 22.577 1.00 30.07 C ANISOU 180 CB PRO A 20 3770 3265 4391 -616 233 -349 C ATOM 181 CG PRO A 20 -3.014 -1.332 22.617 1.00 36.11 C ANISOU 181 CG PRO A 20 4587 3895 5236 -631 219 -366 C ATOM 182 CD PRO A 20 -3.584 -2.151 21.513 1.00 33.15 C ANISOU 182 CD PRO A 20 4172 3489 4935 -685 177 -478 C ATOM 183 N GLU A 21 -6.105 1.795 21.179 1.00 22.84 N ANISOU 183 N GLU A 21 2665 2603 3412 -640 206 -409 N ATOM 184 CA GLU A 21 -6.380 2.983 20.384 1.00 21.70 C ANISOU 184 CA GLU A 21 2471 2581 3193 -587 183 -426 C ATOM 185 C GLU A 21 -5.097 3.813 20.226 1.00 22.09 C ANISOU 185 C GLU A 21 2584 2647 3160 -499 186 -413 C ATOM 186 O GLU A 21 -4.966 4.550 19.251 1.00 21.17 O ANISOU 186 O GLU A 21 2445 2614 2985 -451 156 -439 O ATOM 187 CB GLU A 21 -7.455 3.818 21.109 1.00 22.43 C ANISOU 187 CB GLU A 21 2501 2734 3289 -593 232 -357 C ATOM 188 CG GLU A 21 -7.979 5.008 20.339 1.00 36.05 C ANISOU 188 CG GLU A 21 4158 4577 4961 -540 212 -359 C ATOM 189 CD GLU A 21 -9.252 5.626 20.893 1.00 59.84 C ANISOU 189 CD GLU A 21 7086 7647 8002 -551 255 -309 C ATOM 190 OE1 GLU A 21 -9.478 5.542 22.125 1.00 44.90 O ANISOU 190 OE1 GLU A 21 5208 5713 6139 -577 322 -255 O ATOM 191 OE2 GLU A 21 -10.006 6.233 20.096 1.00 48.61 O ANISOU 191 OE2 GLU A 21 5582 6321 6568 -528 222 -320 O ATOM 192 N PHE A 22 -4.195 3.763 21.234 1.00 16.81 N ANISOU 192 N PHE A 22 1988 1912 2488 -480 223 -362 N ATOM 193 CA PHE A 22 -2.981 4.572 21.236 1.00 13.96 C ANISOU 193 CA PHE A 22 1678 1565 2061 -406 229 -347 C ATOM 194 C PHE A 22 -1.814 3.811 21.824 1.00 18.23 C ANISOU 194 C PHE A 22 2294 2017 2618 -398 232 -337 C ATOM 195 O PHE A 22 -1.950 3.183 22.862 1.00 15.99 O ANISOU 195 O PHE A 22 2033 1670 2372 -433 258 -289 O ATOM 196 CB PHE A 22 -3.185 5.870 22.034 1.00 15.37 C ANISOU 196 CB PHE A 22 1849 1789 2201 -374 279 -283 C ATOM 197 CG PHE A 22 -1.994 6.809 22.089 1.00 15.31 C ANISOU 197 CG PHE A 22 1885 1792 2138 -310 288 -271 C ATOM 198 CD1 PHE A 22 -1.759 7.727 21.063 1.00 16.20 C ANISOU 198 CD1 PHE A 22 1977 1966 2212 -262 273 -287 C ATOM 199 CD2 PHE A 22 -1.146 6.817 23.194 1.00 14.49 C ANISOU 199 CD2 PHE A 22 1839 1645 2021 -301 313 -237 C ATOM 200 CE1 PHE A 22 -0.699 8.643 21.151 1.00 14.74 C ANISOU 200 CE1 PHE A 22 1826 1785 1991 -212 289 -271 C ATOM 201 CE2 PHE A 22 -0.101 7.735 23.292 1.00 16.20 C ANISOU 201 CE2 PHE A 22 2084 1875 2195 -252 321 -233 C ATOM 202 CZ PHE A 22 0.140 8.624 22.251 1.00 14.85 C ANISOU 202 CZ PHE A 22 1891 1751 2002 -211 311 -251 C ATOM 203 N ILE A 23 -0.658 3.902 21.169 1.00 16.23 N ANISOU 203 N ILE A 23 2072 1765 2331 -347 208 -374 N ATOM 204 CA ILE A 23 0.603 3.286 21.635 1.00 17.30 C ANISOU 204 CA ILE A 23 2267 1826 2479 -322 205 -365 C ATOM 205 C ILE A 23 1.700 4.289 21.407 1.00 17.37 C ANISOU 205 C ILE A 23 2292 1884 2425 -258 208 -362 C ATOM 206 O ILE A 23 1.738 4.892 20.341 1.00 15.56 O ANISOU 206 O ILE A 23 2036 1720 2157 -232 196 -400 O ATOM 207 CB ILE A 23 0.968 1.936 20.905 1.00 21.61 C ANISOU 207 CB ILE A 23 2829 2298 3084 -333 171 -437 C ATOM 208 CG1 ILE A 23 -0.141 0.880 20.987 1.00 23.52 C ANISOU 208 CG1 ILE A 23 3050 2478 3410 -409 166 -453 C ATOM 209 CG2 ILE A 23 2.315 1.356 21.444 1.00 21.82 C ANISOU 209 CG2 ILE A 23 2911 2248 3132 -292 170 -415 C ATOM 210 CD1 ILE A 23 0.029 -0.329 19.982 1.00 30.62 C ANISOU 210 CD1 ILE A 23 3952 3311 4371 -425 128 -559 C ATOM 211 N SER A 24 2.647 4.395 22.343 1.00 14.70 N ANISOU 211 N SER A 24 1993 1516 2076 -233 221 -319 N ATOM 212 CA SER A 24 3.832 5.215 22.140 1.00 13.59 C ANISOU 212 CA SER A 24 1861 1411 1891 -180 221 -323 C ATOM 213 C SER A 24 5.047 4.472 22.668 1.00 17.31 C ANISOU 213 C SER A 24 2370 1825 2383 -154 205 -312 C ATOM 214 O SER A 24 5.044 4.027 23.821 1.00 16.04 O ANISOU 214 O SER A 24 2235 1623 2235 -169 210 -259 O ATOM 215 CB SER A 24 3.683 6.583 22.807 1.00 14.51 C ANISOU 215 CB SER A 24 1971 1578 1966 -174 253 -282 C ATOM 216 OG SER A 24 4.821 7.372 22.498 1.00 14.14 O ANISOU 216 OG SER A 24 1924 1557 1890 -133 253 -292 O ATOM 217 N VAL A 25 6.094 4.368 21.840 1.00 14.19 N ANISOU 217 N VAL A 25 1972 1435 1985 -111 190 -357 N ATOM 218 CA VAL A 25 7.323 3.626 22.196 1.00 14.38 C ANISOU 218 CA VAL A 25 2018 1408 2038 -74 172 -352 C ATOM 219 C VAL A 25 8.549 4.457 21.888 1.00 16.56 C ANISOU 219 C VAL A 25 2277 1737 2278 -28 175 -363 C ATOM 220 O VAL A 25 8.626 5.072 20.827 1.00 15.09 O ANISOU 220 O VAL A 25 2066 1606 2063 -16 187 -402 O ATOM 221 CB VAL A 25 7.391 2.236 21.475 1.00 17.58 C ANISOU 221 CB VAL A 25 2433 1740 2508 -67 154 -409 C ATOM 222 CG1 VAL A 25 8.703 1.486 21.789 1.00 18.02 C ANISOU 222 CG1 VAL A 25 2503 1737 2605 -14 138 -402 C ATOM 223 CG2 VAL A 25 6.197 1.361 21.860 1.00 17.46 C ANISOU 223 CG2 VAL A 25 2430 1657 2547 -124 153 -394 C ATOM 224 N GLY A 26 9.491 4.443 22.826 1.00 12.07 N ANISOU 224 N GLY A 26 1719 1157 1712 -6 164 -324 N ATOM 225 CA GLY A 26 10.794 5.064 22.676 1.00 11.48 C ANISOU 225 CA GLY A 26 1619 1123 1620 33 162 -334 C ATOM 226 C GLY A 26 11.847 4.028 22.352 1.00 15.46 C ANISOU 226 C GLY A 26 2117 1586 2171 84 142 -358 C ATOM 227 O GLY A 26 11.768 2.884 22.834 1.00 14.83 O ANISOU 227 O GLY A 26 2063 1433 2139 93 122 -337 O ATOM 228 N TYR A 27 12.884 4.447 21.578 1.00 12.05 N ANISOU 228 N TYR A 27 1647 1199 1731 121 152 -395 N ATOM 229 CA TYR A 27 14.035 3.614 21.198 1.00 12.67 C ANISOU 229 CA TYR A 27 1706 1253 1855 181 141 -425 C ATOM 230 C TYR A 27 15.329 4.376 21.321 1.00 17.33 C ANISOU 230 C TYR A 27 2248 1903 2435 208 143 -416 C ATOM 231 O TYR A 27 15.386 5.540 20.946 1.00 15.80 O ANISOU 231 O TYR A 27 2030 1773 2202 186 170 -420 O ATOM 232 CB TYR A 27 13.973 3.144 19.726 1.00 13.80 C ANISOU 232 CB TYR A 27 1839 1399 2005 203 164 -507 C ATOM 233 CG TYR A 27 12.779 2.290 19.377 1.00 17.06 C ANISOU 233 CG TYR A 27 2288 1755 2439 174 158 -543 C ATOM 234 CD1 TYR A 27 11.578 2.871 18.976 1.00 18.86 C ANISOU 234 CD1 TYR A 27 2522 2023 2620 123 168 -549 C ATOM 235 CD2 TYR A 27 12.860 0.898 19.402 1.00 18.58 C ANISOU 235 CD2 TYR A 27 2502 1850 2709 198 143 -573 C ATOM 236 CE1 TYR A 27 10.466 2.093 18.672 1.00 19.12 C ANISOU 236 CE1 TYR A 27 2577 2011 2678 88 157 -586 C ATOM 237 CE2 TYR A 27 11.751 0.104 19.084 1.00 19.02 C ANISOU 237 CE2 TYR A 27 2585 1843 2797 159 137 -613 C ATOM 238 CZ TYR A 27 10.561 0.711 18.721 1.00 19.49 C ANISOU 238 CZ TYR A 27 2645 1956 2804 101 142 -622 C ATOM 239 OH TYR A 27 9.460 -0.025 18.393 1.00 24.49 O ANISOU 239 OH TYR A 27 3292 2540 3471 55 133 -668 O ATOM 240 N VAL A 28 16.380 3.686 21.746 1.00 15.06 N ANISOU 240 N VAL A 28 1940 1591 2191 259 117 -406 N ATOM 241 CA VAL A 28 17.764 4.153 21.637 1.00 15.09 C ANISOU 241 CA VAL A 28 1879 1651 2203 295 119 -413 C ATOM 242 C VAL A 28 18.381 3.169 20.663 1.00 18.15 C ANISOU 242 C VAL A 28 2245 2010 2640 361 135 -470 C ATOM 243 O VAL A 28 18.390 1.965 20.948 1.00 14.97 O ANISOU 243 O VAL A 28 1866 1528 2295 399 111 -466 O ATOM 244 CB VAL A 28 18.538 4.303 22.961 1.00 18.03 C ANISOU 244 CB VAL A 28 2229 2041 2580 304 71 -357 C ATOM 245 CG1 VAL A 28 20.001 4.647 22.675 1.00 18.23 C ANISOU 245 CG1 VAL A 28 2172 2124 2630 342 73 -377 C ATOM 246 CG2 VAL A 28 17.892 5.389 23.814 1.00 16.71 C ANISOU 246 CG2 VAL A 28 2085 1911 2355 236 66 -325 C ATOM 247 N ASP A 29 18.789 3.657 19.466 1.00 15.92 N ANISOU 247 N ASP A 29 1924 1789 2336 372 182 -523 N ATOM 248 CA ASP A 29 19.266 2.790 18.374 1.00 16.45 C ANISOU 248 CA ASP A 29 1972 1844 2433 432 210 -597 C ATOM 249 C ASP A 29 18.160 1.746 18.076 1.00 20.23 C ANISOU 249 C ASP A 29 2516 2240 2930 425 202 -639 C ATOM 250 O ASP A 29 17.011 2.142 17.891 1.00 19.14 O ANISOU 250 O ASP A 29 2415 2113 2744 367 205 -638 O ATOM 251 CB ASP A 29 20.652 2.143 18.699 1.00 18.69 C ANISOU 251 CB ASP A 29 2199 2113 2788 509 196 -596 C ATOM 252 CG ASP A 29 21.704 3.189 19.048 1.00 29.29 C ANISOU 252 CG ASP A 29 3469 3542 4120 503 198 -559 C ATOM 253 OD1 ASP A 29 21.542 4.357 18.627 1.00 25.12 O ANISOU 253 OD1 ASP A 29 2926 3083 3537 451 232 -555 O ATOM 254 OD2 ASP A 29 22.686 2.840 19.750 1.00 29.94 O ANISOU 254 OD2 ASP A 29 3503 3619 4255 549 163 -531 O ATOM 255 N SER A 30 18.466 0.431 18.090 1.00 19.77 N ANISOU 255 N SER A 30 2467 2092 2951 481 189 -674 N ATOM 256 CA SER A 30 17.423 -0.567 17.813 1.00 21.10 C ANISOU 256 CA SER A 30 2694 2170 3154 463 183 -722 C ATOM 257 C SER A 30 16.731 -1.077 19.101 1.00 24.58 C ANISOU 257 C SER A 30 3183 2514 3642 431 140 -638 C ATOM 258 O SER A 30 15.887 -1.973 19.028 1.00 24.18 O ANISOU 258 O SER A 30 3176 2370 3640 410 134 -664 O ATOM 259 CB SER A 30 18.030 -1.749 17.052 1.00 27.76 C ANISOU 259 CB SER A 30 3526 2950 4071 537 201 -817 C ATOM 260 OG SER A 30 19.021 -2.389 17.848 1.00 40.81 O ANISOU 260 OG SER A 30 5157 4537 5813 606 180 -768 O ATOM 261 N HIS A 31 17.071 -0.501 20.265 1.00 20.11 N ANISOU 261 N HIS A 31 2607 1976 3057 423 112 -539 N ATOM 262 CA HIS A 31 16.554 -0.971 21.562 1.00 19.72 C ANISOU 262 CA HIS A 31 2601 1856 3037 401 75 -446 C ATOM 263 C HIS A 31 15.333 -0.226 22.034 1.00 18.49 C ANISOU 263 C HIS A 31 2479 1732 2813 316 77 -406 C ATOM 264 O HIS A 31 15.446 0.960 22.346 1.00 16.68 O ANISOU 264 O HIS A 31 2230 1594 2513 290 78 -380 O ATOM 265 CB HIS A 31 17.633 -0.840 22.663 1.00 21.09 C ANISOU 265 CB HIS A 31 2742 2055 3216 446 38 -362 C ATOM 266 CG HIS A 31 18.822 -1.684 22.390 1.00 26.81 C ANISOU 266 CG HIS A 31 3427 2738 4023 540 31 -383 C ATOM 267 ND1 HIS A 31 19.845 -1.233 21.582 1.00 30.01 N ANISOU 267 ND1 HIS A 31 3764 3217 4420 582 55 -446 N ATOM 268 CD2 HIS A 31 19.075 -2.960 22.754 1.00 30.08 C ANISOU 268 CD2 HIS A 31 3855 3037 4535 600 11 -350 C ATOM 269 CE1 HIS A 31 20.709 -2.232 21.513 1.00 30.34 C ANISOU 269 CE1 HIS A 31 3779 3195 4554 670 48 -455 C ATOM 270 NE2 HIS A 31 20.288 -3.294 22.195 1.00 31.40 N ANISOU 270 NE2 HIS A 31 3963 3210 4758 687 20 -398 N ATOM 271 N PRO A 32 14.210 -0.921 22.260 1.00 16.33 N ANISOU 271 N PRO A 32 2253 1379 2573 275 76 -392 N ATOM 272 CA PRO A 32 13.065 -0.240 22.906 1.00 16.70 C ANISOU 272 CA PRO A 32 2325 1459 2560 199 79 -341 C ATOM 273 C PRO A 32 13.476 0.157 24.329 1.00 18.97 C ANISOU 273 C PRO A 32 2616 1780 2811 203 54 -240 C ATOM 274 O PRO A 32 14.175 -0.607 24.992 1.00 17.91 O ANISOU 274 O PRO A 32 2486 1599 2721 251 27 -185 O ATOM 275 CB PRO A 32 11.941 -1.298 22.897 1.00 18.91 C ANISOU 275 CB PRO A 32 2645 1634 2904 159 84 -343 C ATOM 276 CG PRO A 32 12.453 -2.434 22.058 1.00 23.09 C ANISOU 276 CG PRO A 32 3173 2075 3525 209 84 -417 C ATOM 277 CD PRO A 32 13.938 -2.358 22.008 1.00 17.67 C ANISOU 277 CD PRO A 32 2453 1418 2845 291 74 -420 C ATOM 278 N ILE A 33 13.099 1.357 24.772 1.00 15.40 N ANISOU 278 N ILE A 33 2160 1414 2278 159 62 -220 N ATOM 279 CA ILE A 33 13.456 1.835 26.108 1.00 15.66 C ANISOU 279 CA ILE A 33 2195 1496 2259 156 38 -145 C ATOM 280 C ILE A 33 12.223 2.148 26.946 1.00 19.59 C ANISOU 280 C ILE A 33 2729 2006 2708 94 55 -97 C ATOM 281 O ILE A 33 12.297 2.089 28.180 1.00 18.53 O ANISOU 281 O ILE A 33 2613 1893 2535 92 36 -23 O ATOM 282 CB ILE A 33 14.403 3.087 26.046 1.00 17.76 C ANISOU 282 CB ILE A 33 2414 1861 2475 166 33 -176 C ATOM 283 CG1 ILE A 33 13.865 4.197 25.104 1.00 16.27 C ANISOU 283 CG1 ILE A 33 2209 1716 2255 127 75 -238 C ATOM 284 CG2 ILE A 33 15.829 2.672 25.639 1.00 16.79 C ANISOU 284 CG2 ILE A 33 2245 1738 2399 235 11 -196 C ATOM 285 CD1 ILE A 33 14.412 5.663 25.437 1.00 14.66 C ANISOU 285 CD1 ILE A 33 1972 1597 2001 107 79 -248 C ATOM 286 N THR A 34 11.121 2.547 26.287 1.00 15.55 N ANISOU 286 N THR A 34 2222 1497 2190 46 90 -139 N ATOM 287 CA THR A 34 9.897 2.972 26.976 1.00 14.70 C ANISOU 287 CA THR A 34 2134 1410 2039 -12 116 -104 C ATOM 288 C THR A 34 8.663 2.555 26.217 1.00 16.20 C ANISOU 288 C THR A 34 2329 1555 2271 -52 142 -134 C ATOM 289 O THR A 34 8.683 2.472 25.000 1.00 17.29 O ANISOU 289 O THR A 34 2448 1683 2438 -43 143 -203 O ATOM 290 CB THR A 34 9.856 4.549 27.175 1.00 19.26 C ANISOU 290 CB THR A 34 2693 2081 2544 -31 134 -129 C ATOM 291 OG1 THR A 34 9.674 5.227 25.922 1.00 18.96 O ANISOU 291 OG1 THR A 34 2627 2062 2515 -34 155 -195 O ATOM 292 CG2 THR A 34 11.090 5.118 27.875 1.00 18.90 C ANISOU 292 CG2 THR A 34 2632 2090 2457 -3 105 -120 C ATOM 293 N THR A 35 7.560 2.389 26.924 1.00 13.22 N ANISOU 293 N THR A 35 1969 1167 1886 -100 164 -85 N ATOM 294 CA THR A 35 6.307 2.072 26.286 1.00 13.88 C ANISOU 294 CA THR A 35 2044 1220 2010 -148 185 -113 C ATOM 295 C THR A 35 5.172 2.662 27.071 1.00 19.06 C ANISOU 295 C THR A 35 2697 1920 2623 -196 222 -72 C ATOM 296 O THR A 35 5.228 2.776 28.297 1.00 17.97 O ANISOU 296 O THR A 35 2581 1806 2441 -200 233 -4 O ATOM 297 CB THR A 35 6.111 0.525 26.101 1.00 19.99 C ANISOU 297 CB THR A 35 2837 1879 2881 -159 175 -103 C ATOM 298 OG1 THR A 35 4.959 0.304 25.254 1.00 20.15 O ANISOU 298 OG1 THR A 35 2834 1881 2941 -210 188 -159 O ATOM 299 CG2 THR A 35 5.925 -0.239 27.465 1.00 21.82 C ANISOU 299 CG2 THR A 35 3103 2060 3128 -175 184 10 C ATOM 300 N TYR A 36 4.114 2.980 26.350 1.00 15.56 N ANISOU 300 N TYR A 36 2223 1495 2193 -231 241 -114 N ATOM 301 CA TYR A 36 2.877 3.491 26.905 1.00 14.55 C ANISOU 301 CA TYR A 36 2079 1408 2042 -276 281 -85 C ATOM 302 C TYR A 36 1.748 3.066 25.982 1.00 17.74 C ANISOU 302 C TYR A 36 2445 1792 2504 -319 284 -125 C ATOM 303 O TYR A 36 1.925 3.097 24.757 1.00 15.15 O ANISOU 303 O TYR A 36 2097 1469 2191 -303 257 -196 O ATOM 304 CB TYR A 36 2.954 5.047 27.017 1.00 13.04 C ANISOU 304 CB TYR A 36 1870 1303 1781 -255 301 -105 C ATOM 305 CG TYR A 36 1.632 5.665 27.416 1.00 12.55 C ANISOU 305 CG TYR A 36 1781 1284 1704 -290 348 -91 C ATOM 306 CD1 TYR A 36 0.637 5.911 26.466 1.00 12.63 C ANISOU 306 CD1 TYR A 36 1742 1312 1746 -307 354 -126 C ATOM 307 CD2 TYR A 36 1.348 5.953 28.752 1.00 12.85 C ANISOU 307 CD2 TYR A 36 1836 1354 1694 -303 386 -41 C ATOM 308 CE1 TYR A 36 -0.633 6.352 26.848 1.00 12.30 C ANISOU 308 CE1 TYR A 36 1662 1307 1703 -336 398 -108 C ATOM 309 CE2 TYR A 36 0.124 6.502 29.125 1.00 14.37 C ANISOU 309 CE2 TYR A 36 1996 1588 1877 -330 439 -33 C ATOM 310 CZ TYR A 36 -0.875 6.667 28.177 1.00 18.51 C ANISOU 310 CZ TYR A 36 2466 2118 2448 -346 445 -63 C ATOM 311 OH TYR A 36 -2.103 7.118 28.569 1.00 15.96 O ANISOU 311 OH TYR A 36 2101 1836 2126 -369 497 -50 O ATOM 312 N ASP A 37 0.583 2.723 26.540 1.00 15.15 N ANISOU 312 N ASP A 37 2101 1454 2202 -374 316 -85 N ATOM 313 CA ASP A 37 -0.560 2.528 25.655 1.00 16.05 C ANISOU 313 CA ASP A 37 2162 1571 2365 -419 314 -131 C ATOM 314 C ASP A 37 -1.840 2.939 26.379 1.00 18.70 C ANISOU 314 C ASP A 37 2460 1952 2693 -463 366 -86 C ATOM 315 O ASP A 37 -1.853 3.120 27.610 1.00 17.48 O ANISOU 315 O ASP A 37 2330 1812 2501 -466 407 -17 O ATOM 316 CB ASP A 37 -0.615 1.119 25.038 1.00 19.02 C ANISOU 316 CB ASP A 37 2542 1851 2834 -453 285 -166 C ATOM 317 CG ASP A 37 -0.789 0.012 26.044 1.00 27.36 C ANISOU 317 CG ASP A 37 3629 2817 3952 -494 309 -87 C ATOM 318 OD1 ASP A 37 -1.829 -0.001 26.733 1.00 29.32 O ANISOU 318 OD1 ASP A 37 3852 3079 4211 -548 352 -32 O ATOM 319 OD2 ASP A 37 0.062 -0.897 26.071 1.00 31.06 O ANISOU 319 OD2 ASP A 37 4140 3195 4466 -474 287 -79 O ATOM 320 N SER A 38 -2.920 3.088 25.610 1.00 15.42 N ANISOU 320 N SER A 38 1979 1569 2309 -495 363 -127 N ATOM 321 CA SER A 38 -4.224 3.517 26.099 1.00 16.69 C ANISOU 321 CA SER A 38 2083 1782 2475 -532 411 -96 C ATOM 322 C SER A 38 -4.896 2.479 27.021 1.00 22.20 C ANISOU 322 C SER A 38 2780 2425 3229 -603 452 -30 C ATOM 323 O SER A 38 -5.891 2.806 27.662 1.00 22.68 O ANISOU 323 O SER A 38 2797 2533 3288 -633 507 10 O ATOM 324 CB SER A 38 -5.144 3.869 24.932 1.00 18.20 C ANISOU 324 CB SER A 38 2194 2029 2691 -543 385 -157 C ATOM 325 OG SER A 38 -5.216 2.790 24.015 1.00 20.48 O ANISOU 325 OG SER A 38 2471 2267 3044 -583 334 -214 O ATOM 326 N VAL A 39 -4.360 1.259 27.107 1.00 20.42 N ANISOU 326 N VAL A 39 2599 2099 3059 -626 432 -12 N ATOM 327 CA VAL A 39 -4.911 0.221 27.983 1.00 22.41 C ANISOU 327 CA VAL A 39 2857 2284 3375 -694 475 68 C ATOM 328 C VAL A 39 -4.218 0.314 29.364 1.00 24.40 C ANISOU 328 C VAL A 39 3176 2542 3552 -662 513 169 C ATOM 329 O VAL A 39 -4.898 0.398 30.379 1.00 24.70 O ANISOU 329 O VAL A 39 3203 2617 3565 -693 577 245 O ATOM 330 CB VAL A 39 -4.775 -1.199 27.348 1.00 27.47 C ANISOU 330 CB VAL A 39 3508 2795 4132 -739 437 38 C ATOM 331 CG1 VAL A 39 -5.221 -2.295 28.317 1.00 28.92 C ANISOU 331 CG1 VAL A 39 3706 2889 4394 -807 487 141 C ATOM 332 CG2 VAL A 39 -5.559 -1.287 26.029 1.00 27.93 C ANISOU 332 CG2 VAL A 39 3494 2869 4250 -779 396 -73 C ATOM 333 N THR A 40 -2.886 0.294 29.393 1.00 19.90 N ANISOU 333 N THR A 40 2670 1948 2944 -599 473 167 N ATOM 334 CA THR A 40 -2.133 0.395 30.663 1.00 20.33 C ANISOU 334 CA THR A 40 2784 2025 2917 -564 493 256 C ATOM 335 C THR A 40 -2.256 1.808 31.247 1.00 21.82 C ANISOU 335 C THR A 40 2962 2338 2991 -533 526 246 C ATOM 336 O THR A 40 -2.269 1.957 32.464 1.00 19.90 O ANISOU 336 O THR A 40 2745 2143 2674 -532 568 319 O ATOM 337 CB THR A 40 -0.632 0.053 30.476 1.00 26.27 C ANISOU 337 CB THR A 40 3592 2727 3664 -500 433 249 C ATOM 338 OG1 THR A 40 0.043 1.130 29.773 1.00 24.87 O ANISOU 338 OG1 THR A 40 3406 2613 3431 -444 398 160 O ATOM 339 CG2 THR A 40 -0.412 -1.287 29.783 1.00 27.31 C ANISOU 339 CG2 THR A 40 3734 2724 3918 -516 400 237 C ATOM 340 N ARG A 41 -2.270 2.845 30.369 1.00 18.04 N ANISOU 340 N ARG A 41 2449 1909 2496 -503 506 153 N ATOM 341 CA ARG A 41 -2.305 4.280 30.749 1.00 17.37 C ANISOU 341 CA ARG A 41 2354 1921 2325 -467 535 125 C ATOM 342 C ARG A 41 -1.102 4.640 31.660 1.00 19.27 C ANISOU 342 C ARG A 41 2655 2191 2474 -422 523 148 C ATOM 343 O ARG A 41 -1.177 5.583 32.455 1.00 18.45 O ANISOU 343 O ARG A 41 2556 2163 2291 -407 560 142 O ATOM 344 CB ARG A 41 -3.637 4.657 31.427 1.00 18.97 C ANISOU 344 CB ARG A 41 2511 2182 2514 -504 611 154 C ATOM 345 CG ARG A 41 -4.802 4.557 30.466 1.00 25.09 C ANISOU 345 CG ARG A 41 3209 2951 3374 -541 614 118 C ATOM 346 CD ARG A 41 -6.140 4.931 31.072 1.00 25.95 C ANISOU 346 CD ARG A 41 3257 3122 3482 -574 691 144 C ATOM 347 NE ARG A 41 -6.154 6.247 31.723 1.00 26.28 N ANISOU 347 NE ARG A 41 3299 3244 3441 -527 738 125 N ATOM 348 CZ ARG A 41 -6.200 7.425 31.113 1.00 37.92 C ANISOU 348 CZ ARG A 41 4744 4754 4911 -478 730 60 C ATOM 349 NH1 ARG A 41 -6.138 7.502 29.784 1.00 27.74 N ANISOU 349 NH1 ARG A 41 3423 3440 3674 -463 670 14 N ATOM 350 NH2 ARG A 41 -6.276 8.542 31.827 1.00 27.45 N ANISOU 350 NH2 ARG A 41 3420 3485 3525 -440 783 40 N ATOM 351 N GLN A 42 -0.024 3.865 31.555 1.00 14.64 N ANISOU 351 N GLN A 42 2111 1548 1903 -400 471 168 N ATOM 352 CA GLN A 42 1.214 4.054 32.326 1.00 14.87 C ANISOU 352 CA GLN A 42 2188 1607 1855 -356 443 191 C ATOM 353 C GLN A 42 2.420 4.019 31.424 1.00 18.94 C ANISOU 353 C GLN A 42 2710 2084 2401 -310 378 138 C ATOM 354 O GLN A 42 2.554 3.090 30.605 1.00 17.49 O ANISOU 354 O GLN A 42 2525 1820 2302 -312 349 132 O ATOM 355 CB GLN A 42 1.410 2.922 33.394 1.00 16.54 C ANISOU 355 CB GLN A 42 2442 1792 2051 -367 447 305 C ATOM 356 CG GLN A 42 0.370 2.853 34.524 1.00 30.17 C ANISOU 356 CG GLN A 42 4168 3569 3725 -410 519 382 C ATOM 357 CD GLN A 42 0.325 4.084 35.413 1.00 38.25 C ANISOU 357 CD GLN A 42 5194 4715 4624 -395 554 353 C ATOM 358 OE1 GLN A 42 1.322 4.773 35.672 1.00 33.57 O ANISOU 358 OE1 GLN A 42 4623 4172 3960 -352 517 311 O ATOM 359 NE2 GLN A 42 -0.841 4.378 35.911 1.00 26.23 N ANISOU 359 NE2 GLN A 42 3647 3243 3078 -431 629 368 N ATOM 360 N LYS A 43 3.343 4.973 31.610 1.00 15.84 N ANISOU 360 N LYS A 43 2324 1748 1945 -271 357 99 N ATOM 361 CA LYS A 43 4.611 4.897 30.899 1.00 15.08 C ANISOU 361 CA LYS A 43 2230 1625 1874 -228 301 61 C ATOM 362 C LYS A 43 5.486 3.888 31.651 1.00 19.52 C ANISOU 362 C LYS A 43 2827 2161 2427 -203 264 136 C ATOM 363 O LYS A 43 5.643 4.017 32.870 1.00 19.02 O ANISOU 363 O LYS A 43 2788 2157 2284 -202 269 189 O ATOM 364 CB LYS A 43 5.326 6.258 30.798 1.00 14.67 C ANISOU 364 CB LYS A 43 2164 1636 1774 -202 293 -5 C ATOM 365 CG LYS A 43 6.609 6.136 29.955 1.00 14.34 C ANISOU 365 CG LYS A 43 2113 1568 1767 -160 243 -41 C ATOM 366 CD LYS A 43 7.443 7.410 30.018 1.00 16.52 C ANISOU 366 CD LYS A 43 2373 1902 2004 -143 235 -94 C ATOM 367 CE LYS A 43 8.781 7.232 29.348 1.00 17.44 C ANISOU 367 CE LYS A 43 2472 2003 2151 -105 191 -118 C ATOM 368 NZ LYS A 43 9.590 8.478 29.368 1.00 15.68 N ANISOU 368 NZ LYS A 43 2225 1829 1905 -99 188 -169 N ATOM 369 N GLU A 44 6.025 2.876 30.952 1.00 15.44 N ANISOU 369 N GLU A 44 2314 1561 1990 -181 229 140 N ATOM 370 CA GLU A 44 6.830 1.839 31.612 1.00 15.98 C ANISOU 370 CA GLU A 44 2411 1589 2070 -147 195 222 C ATOM 371 C GLU A 44 8.170 1.624 30.916 1.00 19.23 C ANISOU 371 C GLU A 44 2811 1973 2524 -87 142 182 C ATOM 372 O GLU A 44 8.228 1.776 29.700 1.00 17.59 O ANISOU 372 O GLU A 44 2579 1738 2367 -82 142 98 O ATOM 373 CB GLU A 44 6.050 0.479 31.615 1.00 17.85 C ANISOU 373 CB GLU A 44 2668 1720 2396 -179 215 290 C ATOM 374 CG GLU A 44 4.742 0.523 32.393 1.00 27.92 C ANISOU 374 CG GLU A 44 3949 3021 3638 -241 274 349 C ATOM 375 CD GLU A 44 3.810 -0.667 32.224 1.00 60.51 C ANISOU 375 CD GLU A 44 8080 7041 7869 -291 304 400 C ATOM 376 OE1 GLU A 44 3.601 -1.127 31.076 1.00 49.82 O ANISOU 376 OE1 GLU A 44 6707 5606 6616 -304 293 329 O ATOM 377 OE2 GLU A 44 3.236 -1.102 33.247 1.00 71.37 O ANISOU 377 OE2 GLU A 44 9475 8420 9223 -323 342 506 O ATOM 378 N PRO A 45 9.228 1.180 31.639 1.00 18.28 N ANISOU 378 N PRO A 45 2701 1860 2383 -38 99 244 N ATOM 379 CA PRO A 45 10.501 0.884 30.958 1.00 18.17 C ANISOU 379 CA PRO A 45 2664 1816 2423 25 54 207 C ATOM 380 C PRO A 45 10.432 -0.384 30.095 1.00 22.88 C ANISOU 380 C PRO A 45 3268 2280 3144 43 56 202 C ATOM 381 O PRO A 45 9.654 -1.280 30.380 1.00 22.00 O ANISOU 381 O PRO A 45 3186 2090 3083 15 77 263 O ATOM 382 CB PRO A 45 11.494 0.677 32.122 1.00 20.23 C ANISOU 382 CB PRO A 45 2930 2127 2628 72 5 293 C ATOM 383 CG PRO A 45 10.632 0.240 33.276 1.00 25.38 C ANISOU 383 CG PRO A 45 3625 2785 3231 39 28 402 C ATOM 384 CD PRO A 45 9.329 0.964 33.109 1.00 20.44 C ANISOU 384 CD PRO A 45 3004 2186 2577 -32 89 353 C ATOM 385 N ARG A 46 11.256 -0.453 29.039 1.00 20.38 N ANISOU 385 N ARG A 46 2923 1940 2882 87 38 122 N ATOM 386 CA ARG A 46 11.365 -1.632 28.156 1.00 21.08 C ANISOU 386 CA ARG A 46 3015 1905 3089 114 38 91 C ATOM 387 C ARG A 46 12.788 -2.199 28.215 1.00 27.30 C ANISOU 387 C ARG A 46 3784 2667 3922 203 -2 111 C ATOM 388 O ARG A 46 13.098 -3.179 27.530 1.00 27.61 O ANISOU 388 O ARG A 46 3823 2602 4065 243 -2 79 O ATOM 389 CB ARG A 46 10.999 -1.270 26.688 1.00 18.91 C ANISOU 389 CB ARG A 46 2716 1632 2835 93 62 -38 C ATOM 390 CG ARG A 46 9.530 -0.957 26.465 1.00 25.42 C ANISOU 390 CG ARG A 46 3550 2465 3644 13 96 -59 C ATOM 391 CD ARG A 46 8.632 -2.169 26.256 1.00 30.38 C ANISOU 391 CD ARG A 46 4200 2974 4370 -25 110 -55 C ATOM 392 NE ARG A 46 9.204 -3.167 25.355 1.00 35.99 N ANISOU 392 NE ARG A 46 4909 3585 5179 16 98 -122 N ATOM 393 CZ ARG A 46 9.170 -3.163 24.020 1.00 46.21 C ANISOU 393 CZ ARG A 46 6183 4882 6494 18 101 -246 C ATOM 394 NH1 ARG A 46 9.729 -4.150 23.345 1.00 27.18 N ANISOU 394 NH1 ARG A 46 3775 2377 4175 61 94 -308 N ATOM 395 NH2 ARG A 46 8.590 -2.144 23.349 1.00 23.34 N ANISOU 395 NH2 ARG A 46 3260 2086 3521 -17 112 -307 N ATOM 396 N ALA A 47 13.661 -1.566 29.017 1.00 24.22 N ANISOU 396 N ALA A 47 3373 2374 3456 235 -37 155 N ATOM 397 CA ALA A 47 15.049 -2.005 29.223 1.00 25.29 C ANISOU 397 CA ALA A 47 3477 2509 3624 322 -84 187 C ATOM 398 C ALA A 47 15.360 -1.908 30.719 1.00 30.15 C ANISOU 398 C ALA A 47 4101 3196 4159 335 -126 307 C ATOM 399 O ALA A 47 14.919 -0.932 31.343 1.00 28.23 O ANISOU 399 O ALA A 47 3865 3054 3806 281 -121 309 O ATOM 400 CB ALA A 47 16.011 -1.141 28.410 1.00 25.34 C ANISOU 400 CB ALA A 47 3422 2593 3614 349 -90 87 C ATOM 401 N PRO A 48 16.065 -2.900 31.328 1.00 29.20 N ANISOU 401 N PRO A 48 3980 3027 4085 408 -167 408 N ATOM 402 CA PRO A 48 16.309 -2.842 32.782 1.00 29.17 C ANISOU 402 CA PRO A 48 3988 3111 3987 422 -212 533 C ATOM 403 C PRO A 48 17.220 -1.689 33.190 1.00 30.98 C ANISOU 403 C PRO A 48 4162 3501 4109 430 -260 492 C ATOM 404 O PRO A 48 17.088 -1.198 34.306 1.00 30.43 O ANISOU 404 O PRO A 48 4106 3539 3920 405 -285 548 O ATOM 405 CB PRO A 48 16.937 -4.205 33.108 1.00 33.24 C ANISOU 405 CB PRO A 48 4506 3526 4598 512 -246 648 C ATOM 406 CG PRO A 48 17.456 -4.720 31.829 1.00 37.70 C ANISOU 406 CG PRO A 48 5041 3985 5300 561 -231 553 C ATOM 407 CD PRO A 48 16.627 -4.136 30.729 1.00 32.37 C ANISOU 407 CD PRO A 48 4375 3295 4631 485 -172 415 C ATOM 408 N TRP A 49 18.087 -1.211 32.283 1.00 27.11 N ANISOU 408 N TRP A 49 3610 3032 3658 456 -268 388 N ATOM 409 CA TRP A 49 18.964 -0.083 32.584 1.00 26.41 C ANISOU 409 CA TRP A 49 3461 3086 3489 452 -309 338 C ATOM 410 C TRP A 49 18.174 1.243 32.582 1.00 26.67 C ANISOU 410 C TRP A 49 3510 3190 3433 357 -270 259 C ATOM 411 O TRP A 49 18.666 2.234 33.109 1.00 25.71 O ANISOU 411 O TRP A 49 3354 3184 3231 335 -301 224 O ATOM 412 CB TRP A 49 20.184 -0.035 31.648 1.00 24.84 C ANISOU 412 CB TRP A 49 3182 2887 3371 510 -323 264 C ATOM 413 CG TRP A 49 19.881 -0.255 30.199 1.00 24.71 C ANISOU 413 CG TRP A 49 3168 2772 3447 507 -259 174 C ATOM 414 CD1 TRP A 49 19.955 -1.434 29.518 1.00 28.43 C ANISOU 414 CD1 TRP A 49 3650 3120 4034 566 -241 178 C ATOM 415 CD2 TRP A 49 19.507 0.739 29.241 1.00 23.94 C ANISOU 415 CD2 TRP A 49 3063 2701 3333 447 -206 65 C ATOM 416 NE1 TRP A 49 19.635 -1.236 28.198 1.00 26.92 N ANISOU 416 NE1 TRP A 49 3457 2889 3884 543 -183 67 N ATOM 417 CE2 TRP A 49 19.386 0.092 27.992 1.00 27.58 C ANISOU 417 CE2 TRP A 49 3526 3067 3885 473 -162 6 C ATOM 418 CE3 TRP A 49 19.304 2.127 29.305 1.00 24.45 C ANISOU 418 CE3 TRP A 49 3114 2858 3317 377 -192 10 C ATOM 419 CZ2 TRP A 49 19.042 0.777 26.823 1.00 26.28 C ANISOU 419 CZ2 TRP A 49 3353 2914 3717 433 -108 -93 C ATOM 420 CZ3 TRP A 49 19.026 2.809 28.135 1.00 26.00 C ANISOU 420 CZ3 TRP A 49 3299 3049 3529 342 -136 -79 C ATOM 421 CH2 TRP A 49 18.902 2.135 26.912 1.00 26.56 C ANISOU 421 CH2 TRP A 49 3374 3043 3676 371 -96 -125 C ATOM 422 N MET A 50 16.931 1.250 32.051 1.00 21.75 N ANISOU 422 N MET A 50 2938 2498 2828 303 -204 231 N ATOM 423 CA MET A 50 16.062 2.437 32.112 1.00 20.03 C ANISOU 423 CA MET A 50 2738 2337 2535 223 -163 171 C ATOM 424 C MET A 50 15.379 2.443 33.474 1.00 25.09 C ANISOU 424 C MET A 50 3425 3032 3075 192 -168 251 C ATOM 425 O MET A 50 15.378 3.463 34.164 1.00 23.86 O ANISOU 425 O MET A 50 3263 2980 2822 156 -175 219 O ATOM 426 CB MET A 50 15.004 2.446 30.971 1.00 20.40 C ANISOU 426 CB MET A 50 2808 2303 2640 183 -95 112 C ATOM 427 CG MET A 50 15.597 2.702 29.611 1.00 22.48 C ANISOU 427 CG MET A 50 3027 2545 2970 204 -81 21 C ATOM 428 SD MET A 50 16.158 4.406 29.393 1.00 25.05 S ANISOU 428 SD MET A 50 3299 2975 3241 170 -75 -63 S ATOM 429 CE MET A 50 14.575 5.261 29.348 1.00 20.97 C ANISOU 429 CE MET A 50 2827 2461 2680 93 -15 -89 C ATOM 430 N ALA A 51 14.842 1.270 33.870 1.00 23.70 N ANISOU 430 N ALA A 51 3294 2784 2926 207 -161 356 N ATOM 431 CA ALA A 51 14.145 1.049 35.142 1.00 25.82 C ANISOU 431 CA ALA A 51 3611 3097 3104 183 -155 457 C ATOM 432 C ALA A 51 15.045 1.364 36.346 1.00 31.44 C ANISOU 432 C ALA A 51 4304 3943 3698 214 -224 504 C ATOM 433 O ALA A 51 14.592 1.988 37.299 1.00 32.63 O ANISOU 433 O ALA A 51 4476 4197 3724 174 -216 513 O ATOM 434 CB ALA A 51 13.666 -0.403 35.224 1.00 27.56 C ANISOU 434 CB ALA A 51 3871 3195 3403 204 -139 574 C ATOM 435 N GLU A 52 16.324 0.970 36.278 1.00 27.95 N ANISOU 435 N GLU A 52 3816 3510 3294 285 -292 525 N ATOM 436 CA GLU A 52 17.281 1.148 37.371 1.00 29.24 C ANISOU 436 CA GLU A 52 3948 3807 3353 322 -374 574 C ATOM 437 C GLU A 52 17.777 2.592 37.560 1.00 29.55 C ANISOU 437 C GLU A 52 3942 3980 3307 281 -400 450 C ATOM 438 O GLU A 52 18.289 2.905 38.633 1.00 28.62 O ANISOU 438 O GLU A 52 3808 3996 3071 287 -462 474 O ATOM 439 CB GLU A 52 18.516 0.246 37.131 1.00 31.46 C ANISOU 439 CB GLU A 52 4179 4049 3724 420 -439 632 C ATOM 440 CG GLU A 52 18.253 -1.234 37.368 1.00 48.65 C ANISOU 440 CG GLU A 52 6400 6113 5970 476 -436 785 C ATOM 441 CD GLU A 52 19.200 -2.211 36.689 1.00 79.48 C ANISOU 441 CD GLU A 52 10263 9914 10023 571 -466 813 C ATOM 442 OE1 GLU A 52 20.100 -1.768 35.937 1.00 79.14 O ANISOU 442 OE1 GLU A 52 10150 9890 10030 596 -487 710 O ATOM 443 OE2 GLU A 52 19.015 -3.434 36.889 1.00 75.79 O ANISOU 443 OE2 GLU A 52 9832 9336 9630 620 -462 940 O ATOM 444 N ASN A 53 17.717 3.428 36.517 1.00 23.62 N ANISOU 444 N ASN A 53 3165 3192 2619 241 -357 322 N ATOM 445 CA ASN A 53 18.334 4.757 36.564 1.00 22.76 C ANISOU 445 CA ASN A 53 3003 3182 2465 203 -380 204 C ATOM 446 C ASN A 53 17.372 5.948 36.565 1.00 25.86 C ANISOU 446 C ASN A 53 3426 3593 2808 121 -315 111 C ATOM 447 O ASN A 53 17.820 7.079 36.758 1.00 26.12 O ANISOU 447 O ASN A 53 3422 3701 2803 84 -330 15 O ATOM 448 CB ASN A 53 19.273 4.873 35.376 1.00 20.50 C ANISOU 448 CB ASN A 53 2647 2846 2295 231 -385 138 C ATOM 449 CG ASN A 53 20.537 4.085 35.589 1.00 33.14 C ANISOU 449 CG ASN A 53 4188 4474 3927 312 -465 201 C ATOM 450 OD1 ASN A 53 21.404 4.463 36.384 1.00 30.51 O ANISOU 450 OD1 ASN A 53 3804 4262 3526 321 -540 196 O ATOM 451 ND2 ASN A 53 20.670 2.975 34.894 1.00 21.89 N ANISOU 451 ND2 ASN A 53 2766 2942 2610 376 -453 255 N ATOM 452 N LEU A 54 16.085 5.710 36.323 1.00 21.94 N ANISOU 452 N LEU A 54 2989 3023 2325 94 -242 135 N ATOM 453 CA LEU A 54 15.081 6.771 36.313 1.00 21.13 C ANISOU 453 CA LEU A 54 2911 2931 2187 27 -175 56 C ATOM 454 C LEU A 54 14.134 6.570 37.492 1.00 25.85 C ANISOU 454 C LEU A 54 3567 3584 2672 6 -152 120 C ATOM 455 O LEU A 54 13.471 5.537 37.590 1.00 24.97 O ANISOU 455 O LEU A 54 3494 3418 2576 19 -128 222 O ATOM 456 CB LEU A 54 14.331 6.804 34.953 1.00 19.61 C ANISOU 456 CB LEU A 54 2725 2622 2104 11 -106 21 C ATOM 457 CG LEU A 54 15.212 7.271 33.770 1.00 23.12 C ANISOU 457 CG LEU A 54 3112 3034 2639 24 -113 -55 C ATOM 458 CD1 LEU A 54 14.575 6.906 32.440 1.00 21.68 C ANISOU 458 CD1 LEU A 54 2938 2748 2551 26 -60 -63 C ATOM 459 CD2 LEU A 54 15.475 8.809 33.831 1.00 22.09 C ANISOU 459 CD2 LEU A 54 2950 2960 2484 -23 -102 -159 C ATOM 460 N ALA A 55 14.111 7.553 38.401 1.00 24.17 N ANISOU 460 N ALA A 55 3355 3481 2347 -29 -157 56 N ATOM 461 CA ALA A 55 13.314 7.539 39.625 1.00 24.72 C ANISOU 461 CA ALA A 55 3473 3636 2283 -50 -132 98 C ATOM 462 C ALA A 55 11.793 7.512 39.308 1.00 26.45 C ANISOU 462 C ALA A 55 3733 3784 2534 -85 -31 110 C ATOM 463 O ALA A 55 11.414 7.851 38.170 1.00 23.11 O ANISOU 463 O ALA A 55 3293 3264 2221 -99 11 53 O ATOM 464 CB ALA A 55 13.669 8.762 40.477 1.00 26.15 C ANISOU 464 CB ALA A 55 3640 3945 2351 -83 -154 -15 C ATOM 465 N PRO A 56 10.926 7.082 40.267 1.00 21.46 N ANISOU 465 N PRO A 56 3341 2758 2054 -537 -59 256 N ATOM 466 CA PRO A 56 9.473 7.057 40.004 1.00 21.25 C ANISOU 466 CA PRO A 56 3311 2736 2025 -545 54 238 C ATOM 467 C PRO A 56 8.899 8.372 39.473 1.00 24.22 C ANISOU 467 C PRO A 56 3667 3128 2406 -517 152 119 C ATOM 468 O PRO A 56 7.961 8.306 38.685 1.00 22.70 O ANISOU 468 O PRO A 56 3434 2913 2278 -491 222 98 O ATOM 469 CB PRO A 56 8.875 6.757 41.391 1.00 24.43 C ANISOU 469 CB PRO A 56 3784 3218 2280 -621 76 303 C ATOM 470 CG PRO A 56 9.949 5.918 42.058 1.00 29.26 C ANISOU 470 CG PRO A 56 4429 3820 2868 -642 -53 405 C ATOM 471 CD PRO A 56 11.216 6.590 41.646 1.00 24.71 C ANISOU 471 CD PRO A 56 3821 3226 2342 -598 -125 344 C ATOM 472 N ASP A 57 9.450 9.546 39.888 1.00 21.91 N ANISOU 472 N ASP A 57 3406 2869 2051 -523 148 43 N ATOM 473 CA ASP A 57 8.950 10.854 39.441 1.00 21.67 C ANISOU 473 CA ASP A 57 3369 2836 2028 -493 233 -68 C ATOM 474 C ASP A 57 9.040 11.004 37.916 1.00 22.76 C ANISOU 474 C ASP A 57 3436 2902 2311 -430 242 -96 C ATOM 475 O ASP A 57 8.175 11.630 37.314 1.00 20.32 O ANISOU 475 O ASP A 57 3106 2581 2032 -395 323 -152 O ATOM 476 CB ASP A 57 9.706 12.006 40.114 1.00 24.61 C ANISOU 476 CB ASP A 57 3795 3232 2322 -519 205 -141 C ATOM 477 CG ASP A 57 9.065 13.354 39.821 1.00 37.32 C ANISOU 477 CG ASP A 57 5420 4827 3933 -488 296 -254 C ATOM 478 OD1 ASP A 57 7.860 13.531 40.154 1.00 41.26 O ANISOU 478 OD1 ASP A 57 5934 5363 4379 -477 394 -282 O ATOM 479 OD2 ASP A 57 9.733 14.204 39.201 1.00 38.13 O ANISOU 479 OD2 ASP A 57 5510 4877 4098 -471 272 -308 O ATOM 480 N HIS A 58 10.070 10.414 37.292 1.00 18.40 N ANISOU 480 N HIS A 58 2843 2307 1841 -410 160 -56 N ATOM 481 CA HIS A 58 10.186 10.457 35.841 1.00 16.79 C ANISOU 481 CA HIS A 58 2574 2048 1757 -352 171 -79 C ATOM 482 C HIS A 58 8.968 9.786 35.210 1.00 18.59 C ANISOU 482 C HIS A 58 2775 2259 2030 -329 228 -62 C ATOM 483 O HIS A 58 8.323 10.384 34.337 1.00 17.17 O ANISOU 483 O HIS A 58 2566 2065 1892 -292 288 -112 O ATOM 484 CB HIS A 58 11.476 9.756 35.353 1.00 16.42 C ANISOU 484 CB HIS A 58 2483 1972 1785 -329 80 -37 C ATOM 485 CG HIS A 58 11.570 9.723 33.850 1.00 18.30 C ANISOU 485 CG HIS A 58 2658 2166 2129 -268 101 -63 C ATOM 486 ND1 HIS A 58 11.105 8.630 33.110 1.00 19.91 N ANISOU 486 ND1 HIS A 58 2835 2331 2398 -232 103 -35 N ATOM 487 CD2 HIS A 58 12.036 10.666 32.997 1.00 17.16 C ANISOU 487 CD2 HIS A 58 2481 2013 2025 -245 121 -114 C ATOM 488 CE1 HIS A 58 11.313 8.948 31.835 1.00 17.17 C ANISOU 488 CE1 HIS A 58 2441 1964 2118 -183 125 -76 C ATOM 489 NE2 HIS A 58 11.892 10.148 31.720 1.00 17.84 N ANISOU 489 NE2 HIS A 58 2518 2069 2190 -190 138 -116 N ATOM 490 N TRP A 59 8.700 8.520 35.605 1.00 16.48 N ANISOU 490 N TRP A 59 2515 1986 1759 -354 198 14 N ATOM 491 CA TRP A 59 7.611 7.700 35.056 1.00 16.43 C ANISOU 491 CA TRP A 59 2482 1957 1803 -350 234 40 C ATOM 492 C TRP A 59 6.258 8.355 35.379 1.00 19.33 C ANISOU 492 C TRP A 59 2850 2380 2115 -369 334 6 C ATOM 493 O TRP A 59 5.391 8.355 34.520 1.00 17.50 O ANISOU 493 O TRP A 59 2571 2137 1941 -343 378 -17 O ATOM 494 CB TRP A 59 7.681 6.239 35.582 1.00 16.00 C ANISOU 494 CB TRP A 59 2451 1875 1754 -388 173 138 C ATOM 495 CG TRP A 59 9.043 5.635 35.338 1.00 17.67 C ANISOU 495 CG TRP A 59 2657 2033 2024 -353 73 168 C ATOM 496 CD1 TRP A 59 10.075 5.555 36.230 1.00 21.30 C ANISOU 496 CD1 TRP A 59 3146 2510 2436 -369 0 211 C ATOM 497 CD2 TRP A 59 9.566 5.191 34.080 1.00 15.77 C ANISOU 497 CD2 TRP A 59 2370 1726 1895 -287 41 143 C ATOM 498 NE1 TRP A 59 11.190 5.025 35.618 1.00 20.25 N ANISOU 498 NE1 TRP A 59 2978 2325 2391 -312 -76 221 N ATOM 499 CE2 TRP A 59 10.918 4.828 34.291 1.00 19.97 C ANISOU 499 CE2 TRP A 59 2898 2239 2451 -259 -45 174 C ATOM 500 CE3 TRP A 59 9.020 5.057 32.787 1.00 15.38 C ANISOU 500 CE3 TRP A 59 2281 1639 1923 -248 76 95 C ATOM 501 CZ2 TRP A 59 11.737 4.354 33.258 1.00 18.05 C ANISOU 501 CZ2 TRP A 59 2607 1943 2307 -186 -85 153 C ATOM 502 CZ3 TRP A 59 9.833 4.581 31.765 1.00 16.19 C ANISOU 502 CZ3 TRP A 59 2350 1688 2111 -181 33 72 C ATOM 503 CH2 TRP A 59 11.182 4.272 31.995 1.00 16.80 C ANISOU 503 CH2 TRP A 59 2419 1752 2212 -148 -38 97 C ATOM 504 N GLU A 60 6.096 8.945 36.586 1.00 17.45 N ANISOU 504 N GLU A 60 2659 2206 1764 -406 369 -3 N ATOM 505 CA GLU A 60 4.814 9.579 36.914 1.00 18.15 C ANISOU 505 CA GLU A 60 2739 2355 1802 -409 475 -44 C ATOM 506 C GLU A 60 4.612 10.834 36.080 1.00 19.22 C ANISOU 506 C GLU A 60 2847 2471 1983 -343 522 -137 C ATOM 507 O GLU A 60 3.519 11.018 35.554 1.00 17.26 O ANISOU 507 O GLU A 60 2550 2237 1773 -314 587 -158 O ATOM 508 CB GLU A 60 4.632 9.884 38.422 1.00 20.63 C ANISOU 508 CB GLU A 60 3116 2751 1970 -461 513 -42 C ATOM 509 CG GLU A 60 3.400 10.760 38.742 1.00 37.29 C ANISOU 509 CG GLU A 60 5213 4928 4027 -442 636 -109 C ATOM 510 CD GLU A 60 1.945 10.373 38.430 1.00 63.29 C ANISOU 510 CD GLU A 60 8431 8262 7356 -441 720 -89 C ATOM 511 OE1 GLU A 60 1.076 10.854 39.197 1.00 59.32 O ANISOU 511 OE1 GLU A 60 7927 7844 6768 -445 818 -121 O ATOM 512 OE2 GLU A 60 1.648 9.708 37.400 1.00 35.30 O ANISOU 512 OE2 GLU A 60 4823 4670 3921 -430 694 -54 O ATOM 513 N ARG A 61 5.647 11.668 35.914 1.00 14.87 N ANISOU 513 N ARG A 61 2325 1887 1438 -321 483 -184 N ATOM 514 CA ARG A 61 5.447 12.895 35.143 1.00 14.39 C ANISOU 514 CA ARG A 61 2249 1796 1422 -264 525 -261 C ATOM 515 C ARG A 61 5.161 12.612 33.685 1.00 16.83 C ANISOU 515 C ARG A 61 2492 2064 1840 -216 520 -250 C ATOM 516 O ARG A 61 4.245 13.223 33.129 1.00 16.35 O ANISOU 516 O ARG A 61 2399 2004 1808 -171 578 -285 O ATOM 517 CB ARG A 61 6.650 13.848 35.239 1.00 13.41 C ANISOU 517 CB ARG A 61 2170 1638 1289 -267 480 -306 C ATOM 518 CG ARG A 61 6.765 14.462 36.628 1.00 15.85 C ANISOU 518 CG ARG A 61 2555 1988 1481 -308 494 -348 C ATOM 519 CD ARG A 61 7.707 15.668 36.584 1.00 21.56 C ANISOU 519 CD ARG A 61 3319 2663 2209 -312 461 -412 C ATOM 520 NE ARG A 61 7.778 16.210 37.942 1.00 43.85 N ANISOU 520 NE ARG A 61 6225 5527 4910 -354 469 -465 N ATOM 521 CZ ARG A 61 6.865 17.031 38.457 1.00 60.25 C ANISOU 521 CZ ARG A 61 8344 7617 6930 -328 554 -543 C ATOM 522 NH1 ARG A 61 6.965 17.434 39.717 1.00 58.16 N ANISOU 522 NH1 ARG A 61 8161 7398 6540 -369 560 -597 N ATOM 523 NH2 ARG A 61 5.843 17.457 37.710 1.00 26.57 N ANISOU 523 NH2 ARG A 61 4038 3325 2731 -257 632 -571 N ATOM 524 N TYR A 62 5.916 11.691 33.077 1.00 12.92 N ANISOU 524 N TYR A 62 1975 1535 1397 -221 451 -204 N ATOM 525 CA TYR A 62 5.706 11.366 31.660 1.00 11.94 C ANISOU 525 CA TYR A 62 1797 1378 1362 -178 442 -202 C ATOM 526 C TYR A 62 4.421 10.576 31.436 1.00 14.96 C ANISOU 526 C TYR A 62 2139 1780 1766 -185 471 -178 C ATOM 527 O TYR A 62 3.814 10.733 30.375 1.00 12.55 O ANISOU 527 O TYR A 62 1789 1467 1514 -146 487 -197 O ATOM 528 CB TYR A 62 6.932 10.702 31.035 1.00 11.97 C ANISOU 528 CB TYR A 62 1790 1343 1415 -169 368 -178 C ATOM 529 CG TYR A 62 7.884 11.761 30.524 1.00 13.86 C ANISOU 529 CG TYR A 62 2030 1566 1669 -146 361 -214 C ATOM 530 CD1 TYR A 62 7.687 12.356 29.277 1.00 14.90 C ANISOU 530 CD1 TYR A 62 2132 1681 1847 -100 386 -240 C ATOM 531 CD2 TYR A 62 8.879 12.298 31.353 1.00 15.72 C ANISOU 531 CD2 TYR A 62 2299 1808 1865 -178 331 -220 C ATOM 532 CE1 TYR A 62 8.497 13.403 28.835 1.00 13.34 C ANISOU 532 CE1 TYR A 62 1940 1468 1662 -91 385 -261 C ATOM 533 CE2 TYR A 62 9.691 13.356 30.920 1.00 15.46 C ANISOU 533 CE2 TYR A 62 2266 1759 1850 -174 326 -250 C ATOM 534 CZ TYR A 62 9.501 13.891 29.655 1.00 16.75 C ANISOU 534 CZ TYR A 62 2401 1900 2065 -131 357 -266 C ATOM 535 OH TYR A 62 10.325 14.876 29.158 1.00 15.43 O ANISOU 535 OH TYR A 62 2232 1714 1919 -136 353 -280 O ATOM 536 N THR A 63 3.954 9.791 32.441 1.00 14.92 N ANISOU 536 N THR A 63 2147 1806 1716 -241 479 -131 N ATOM 537 CA THR A 63 2.638 9.129 32.324 1.00 15.07 C ANISOU 537 CA THR A 63 2118 1852 1755 -264 515 -104 C ATOM 538 C THR A 63 1.554 10.228 32.161 1.00 16.12 C ANISOU 538 C THR A 63 2209 2034 1881 -222 598 -157 C ATOM 539 O THR A 63 0.652 10.059 31.369 1.00 14.54 O ANISOU 539 O THR A 63 1946 1843 1735 -205 611 -159 O ATOM 540 CB THR A 63 2.350 8.254 33.569 1.00 17.58 C ANISOU 540 CB THR A 63 2462 2205 2012 -342 520 -36 C ATOM 541 OG1 THR A 63 3.192 7.109 33.550 1.00 15.91 O ANISOU 541 OG1 THR A 63 2281 1934 1831 -370 434 22 O ATOM 542 CG2 THR A 63 0.878 7.835 33.690 1.00 17.46 C ANISOU 542 CG2 THR A 63 2390 2244 2002 -381 581 -9 C ATOM 543 N GLN A 64 1.611 11.313 32.969 1.00 14.55 N ANISOU 543 N GLN A 64 2048 1866 1617 -206 649 -201 N ATOM 544 CA GLN A 64 0.624 12.416 32.894 1.00 13.72 C ANISOU 544 CA GLN A 64 1908 1794 1510 -149 729 -258 C ATOM 545 C GLN A 64 0.683 13.083 31.520 1.00 16.60 C ANISOU 545 C GLN A 64 2244 2108 1955 -78 708 -289 C ATOM 546 O GLN A 64 -0.360 13.382 30.926 1.00 15.56 O ANISOU 546 O GLN A 64 2048 2000 1865 -33 743 -301 O ATOM 547 CB GLN A 64 0.872 13.459 34.013 1.00 14.99 C ANISOU 547 CB GLN A 64 2136 1976 1583 -140 778 -314 C ATOM 548 CG GLN A 64 0.629 12.912 35.459 1.00 14.46 C ANISOU 548 CG GLN A 64 2100 1985 1410 -209 816 -285 C ATOM 549 CD GLN A 64 -0.782 12.382 35.658 1.00 22.26 C ANISOU 549 CD GLN A 64 3009 3054 2396 -225 890 -254 C ATOM 550 OE1 GLN A 64 -1.770 12.983 35.230 1.00 20.45 O ANISOU 550 OE1 GLN A 64 2712 2850 2206 -164 953 -294 O ATOM 551 NE2 GLN A 64 -0.910 11.211 36.273 1.00 22.86 N ANISOU 551 NE2 GLN A 64 3084 3168 2432 -310 880 -174 N ATOM 552 N LEU A 65 1.911 13.298 31.001 1.00 12.24 N ANISOU 552 N LEU A 65 1734 1494 1421 -70 648 -294 N ATOM 553 CA LEU A 65 2.084 13.907 29.669 1.00 11.66 C ANISOU 553 CA LEU A 65 1641 1378 1412 -12 627 -311 C ATOM 554 C LEU A 65 1.522 13.019 28.573 1.00 14.04 C ANISOU 554 C LEU A 65 1879 1687 1769 -6 597 -281 C ATOM 555 O LEU A 65 0.775 13.501 27.726 1.00 13.99 O ANISOU 555 O LEU A 65 1828 1688 1799 45 610 -292 O ATOM 556 CB LEU A 65 3.558 14.196 29.390 1.00 11.44 C ANISOU 556 CB LEU A 65 1661 1299 1387 -20 576 -313 C ATOM 557 CG LEU A 65 4.115 15.384 30.199 1.00 16.08 C ANISOU 557 CG LEU A 65 2313 1864 1934 -23 595 -356 C ATOM 558 CD1 LEU A 65 5.607 15.267 30.308 1.00 14.10 C ANISOU 558 CD1 LEU A 65 2096 1587 1676 -64 535 -343 C ATOM 559 CD2 LEU A 65 3.729 16.730 29.525 1.00 18.46 C ANISOU 559 CD2 LEU A 65 2619 2125 2271 40 628 -392 C ATOM 560 N LEU A 66 1.778 11.718 28.666 1.00 12.26 N ANISOU 560 N LEU A 66 1650 1460 1547 -57 555 -244 N ATOM 561 CA LEU A 66 1.296 10.742 27.667 1.00 11.34 C ANISOU 561 CA LEU A 66 1486 1341 1483 -63 516 -225 C ATOM 562 C LEU A 66 -0.211 10.585 27.688 1.00 14.39 C ANISOU 562 C LEU A 66 1802 1780 1884 -72 553 -217 C ATOM 563 O LEU A 66 -0.783 10.385 26.637 1.00 13.80 O ANISOU 563 O LEU A 66 1680 1711 1853 -53 527 -222 O ATOM 564 CB LEU A 66 1.977 9.383 27.863 1.00 10.38 C ANISOU 564 CB LEU A 66 1390 1184 1370 -114 459 -191 C ATOM 565 CG LEU A 66 3.340 9.284 27.140 1.00 13.83 C ANISOU 565 CG LEU A 66 1857 1572 1826 -84 408 -204 C ATOM 566 CD1 LEU A 66 4.292 8.331 27.908 1.00 12.78 C ANISOU 566 CD1 LEU A 66 1763 1406 1687 -121 362 -169 C ATOM 567 CD2 LEU A 66 3.149 8.857 25.650 1.00 12.09 C ANISOU 567 CD2 LEU A 66 1605 1337 1651 -52 375 -225 C ATOM 568 N ARG A 67 -0.863 10.741 28.847 1.00 13.63 N ANISOU 568 N ARG A 67 1697 1734 1749 -98 614 -209 N ATOM 569 CA ARG A 67 -2.342 10.688 28.901 1.00 14.09 C ANISOU 569 CA ARG A 67 1668 1861 1825 -103 661 -201 C ATOM 570 C ARG A 67 -2.933 11.886 28.128 1.00 16.67 C ANISOU 570 C ARG A 67 1948 2202 2182 -11 685 -241 C ATOM 571 O ARG A 67 -3.913 11.741 27.411 1.00 15.04 O ANISOU 571 O ARG A 67 1659 2033 2022 3 677 -234 O ATOM 572 CB ARG A 67 -2.812 10.668 30.353 1.00 12.66 C ANISOU 572 CB ARG A 67 1487 1742 1582 -147 735 -186 C ATOM 573 CG ARG A 67 -2.513 9.317 31.011 1.00 14.03 C ANISOU 573 CG ARG A 67 1691 1906 1734 -246 703 -122 C ATOM 574 CD ARG A 67 -2.847 9.350 32.475 1.00 17.00 C ANISOU 574 CD ARG A 67 2083 2353 2026 -293 777 -100 C ATOM 575 NE ARG A 67 -2.538 8.060 33.095 1.00 18.30 N ANISOU 575 NE ARG A 67 2284 2500 2169 -391 738 -22 N ATOM 576 CZ ARG A 67 -2.674 7.796 34.389 1.00 24.15 C ANISOU 576 CZ ARG A 67 3053 3298 2823 -454 785 23 C ATOM 577 NH1 ARG A 67 -3.112 8.736 35.229 1.00 18.20 N ANISOU 577 NH1 ARG A 67 2296 2629 1990 -427 881 -17 N ATOM 578 NH2 ARG A 67 -2.344 6.606 34.863 1.00 16.78 N ANISOU 578 NH2 ARG A 67 2162 2335 1879 -541 736 107 N ATOM 579 N GLY A 68 -2.253 13.034 28.177 1.00 14.45 N ANISOU 579 N GLY A 68 1726 1884 1883 48 701 -277 N ATOM 580 CA GLY A 68 -2.658 14.201 27.390 1.00 13.36 C ANISOU 580 CA GLY A 68 1563 1735 1779 138 712 -305 C ATOM 581 C GLY A 68 -2.336 14.022 25.913 1.00 16.81 C ANISOU 581 C GLY A 68 1992 2139 2255 158 639 -289 C ATOM 582 O GLY A 68 -3.180 14.323 25.059 1.00 16.25 O ANISOU 582 O GLY A 68 1857 2094 2222 207 627 -284 O ATOM 583 N TRP A 69 -1.129 13.517 25.591 1.00 12.10 N ANISOU 583 N TRP A 69 1455 1496 1648 123 589 -281 N ATOM 584 CA TRP A 69 -0.734 13.285 24.177 1.00 13.08 C ANISOU 584 CA TRP A 69 1577 1599 1793 141 527 -274 C ATOM 585 C TRP A 69 -1.666 12.257 23.522 1.00 16.80 C ANISOU 585 C TRP A 69 1981 2111 2292 116 488 -262 C ATOM 586 O TRP A 69 -1.988 12.361 22.341 1.00 15.87 O ANISOU 586 O TRP A 69 1835 2007 2189 149 449 -262 O ATOM 587 CB TRP A 69 0.740 12.845 24.058 1.00 11.14 C ANISOU 587 CB TRP A 69 1395 1308 1530 112 493 -273 C ATOM 588 CG TRP A 69 1.708 13.907 24.531 1.00 12.52 C ANISOU 588 CG TRP A 69 1629 1445 1684 127 517 -283 C ATOM 589 CD1 TRP A 69 1.484 15.255 24.612 1.00 15.75 C ANISOU 589 CD1 TRP A 69 2054 1836 2094 173 553 -296 C ATOM 590 CD2 TRP A 69 3.052 13.692 24.989 1.00 12.10 C ANISOU 590 CD2 TRP A 69 1625 1362 1612 91 500 -282 C ATOM 591 NE1 TRP A 69 2.617 15.895 25.078 1.00 15.92 N ANISOU 591 NE1 TRP A 69 2137 1814 2097 157 557 -306 N ATOM 592 CE2 TRP A 69 3.584 14.954 25.344 1.00 16.37 C ANISOU 592 CE2 TRP A 69 2209 1873 2140 105 525 -296 C ATOM 593 CE3 TRP A 69 3.852 12.544 25.159 1.00 12.77 C ANISOU 593 CE3 TRP A 69 1719 1439 1694 52 461 -271 C ATOM 594 CZ2 TRP A 69 4.890 15.105 25.850 1.00 14.49 C ANISOU 594 CZ2 TRP A 69 2013 1609 1884 69 509 -298 C ATOM 595 CZ3 TRP A 69 5.139 12.694 25.687 1.00 14.21 C ANISOU 595 CZ3 TRP A 69 1940 1599 1861 30 448 -269 C ATOM 596 CH2 TRP A 69 5.646 13.959 26.005 1.00 15.01 C ANISOU 596 CH2 TRP A 69 2073 1683 1947 34 470 -282 C ATOM 597 N GLN A 70 -2.094 11.270 24.304 1.00 14.72 N ANISOU 597 N GLN A 70 1694 1867 2031 50 495 -249 N ATOM 598 CA GLN A 70 -3.034 10.250 23.843 1.00 15.83 C ANISOU 598 CA GLN A 70 1770 2041 2206 4 456 -236 C ATOM 599 C GLN A 70 -4.368 10.914 23.414 1.00 17.31 C ANISOU 599 C GLN A 70 1862 2295 2420 49 471 -235 C ATOM 600 O GLN A 70 -4.861 10.620 22.327 1.00 14.27 O ANISOU 600 O GLN A 70 1433 1931 2058 53 413 -237 O ATOM 601 CB GLN A 70 -3.282 9.194 24.959 1.00 16.78 C ANISOU 601 CB GLN A 70 1885 2166 2325 -86 471 -207 C ATOM 602 CG GLN A 70 -4.520 8.319 24.684 1.00 17.56 C ANISOU 602 CG GLN A 70 1897 2307 2466 -147 446 -188 C ATOM 603 CD GLN A 70 -4.891 7.421 25.846 1.00 23.00 C ANISOU 603 CD GLN A 70 2575 3009 3153 -243 473 -143 C ATOM 604 OE1 GLN A 70 -4.054 7.025 26.649 1.00 19.08 O ANISOU 604 OE1 GLN A 70 2154 2468 2626 -276 479 -123 O ATOM 605 NE2 GLN A 70 -6.165 7.092 25.963 1.00 17.65 N ANISOU 605 NE2 GLN A 70 1800 2400 2506 -294 489 -118 N ATOM 606 N AGLN A 71 -4.942 11.779 24.266 0.50 16.02 N ANISOU 606 N AGLN A 71 1666 2170 2252 85 546 -236 N ATOM 607 N BGLN A 71 -4.931 11.803 24.264 0.50 16.53 N ANISOU 607 N BGLN A 71 1731 2234 2316 87 547 -236 N ATOM 608 CA AGLN A 71 -6.211 12.443 23.957 0.50 16.25 C ANISOU 608 CA AGLN A 71 1593 2266 2315 143 566 -234 C ATOM 609 CA BGLN A 71 -6.200 12.499 23.994 0.50 17.07 C ANISOU 609 CA BGLN A 71 1699 2369 2419 146 570 -235 C ATOM 610 C AGLN A 71 -6.031 13.393 22.747 0.50 17.98 C ANISOU 610 C AGLN A 71 1827 2460 2545 233 524 -240 C ATOM 611 C BGLN A 71 -6.093 13.343 22.715 0.50 19.58 C ANISOU 611 C BGLN A 71 2024 2667 2750 231 521 -239 C ATOM 612 O AGLN A 71 -6.925 13.458 21.899 0.50 16.95 O ANISOU 612 O AGLN A 71 1616 2378 2447 263 482 -228 O ATOM 613 O BGLN A 71 -7.007 13.303 21.887 0.50 18.52 O ANISOU 613 O BGLN A 71 1806 2584 2648 253 478 -226 O ATOM 614 CB AGLN A 71 -6.775 13.172 25.191 0.50 18.06 C ANISOU 614 CB AGLN A 71 1791 2537 2534 175 666 -246 C ATOM 615 CB BGLN A 71 -6.621 13.386 25.184 0.50 18.79 C ANISOU 615 CB BGLN A 71 1900 2618 2623 190 669 -251 C ATOM 616 CG AGLN A 71 -8.064 13.994 24.933 0.50 25.24 C ANISOU 616 CG AGLN A 71 2587 3515 3488 262 696 -249 C ATOM 617 CG BGLN A 71 -8.037 13.997 25.044 0.50 26.63 C ANISOU 617 CG BGLN A 71 2767 3691 3661 259 703 -251 C ATOM 618 CD AGLN A 71 -9.264 13.222 24.401 0.50 37.65 C ANISOU 618 CD AGLN A 71 4025 5173 5109 222 658 -220 C ATOM 619 CD BGLN A 71 -8.174 15.318 24.298 0.50 36.44 C ANISOU 619 CD BGLN A 71 4008 4905 4932 384 692 -263 C ATOM 620 OE1AGLN A 71 -9.380 11.991 24.518 0.50 31.82 O ANISOU 620 OE1AGLN A 71 3265 4452 4371 112 630 -197 O ATOM 621 OE1BGLN A 71 -7.201 16.010 23.954 0.50 25.42 O ANISOU 621 OE1BGLN A 71 2714 3425 3519 423 673 -274 O ATOM 622 NE2AGLN A 71 -10.217 13.949 23.835 0.50 31.09 N ANISOU 622 NE2AGLN A 71 3095 4393 4324 309 652 -217 N ATOM 623 NE2BGLN A 71 -9.418 15.715 24.052 0.50 30.85 N ANISOU 623 NE2BGLN A 71 3178 4269 4275 450 704 -256 N ATOM 624 N AMET A 72 -4.865 14.072 22.651 0.50 14.72 N ANISOU 624 N AMET A 72 1515 1976 2104 267 527 -251 N ATOM 625 N BMET A 72 -5.003 14.124 22.576 0.50 16.87 N ANISOU 625 N BMET A 72 1776 2254 2380 273 526 -250 N ATOM 626 CA AMET A 72 -4.510 14.967 21.529 0.50 15.83 C ANISOU 626 CA AMET A 72 1686 2083 2244 337 490 -243 C ATOM 627 CA BMET A 72 -4.805 14.977 21.398 0.50 18.03 C ANISOU 627 CA BMET A 72 1943 2377 2532 346 485 -239 C ATOM 628 C AMET A 72 -4.493 14.199 20.198 0.50 19.17 C ANISOU 628 C AMET A 72 2095 2527 2660 314 406 -231 C ATOM 629 C BMET A 72 -4.623 14.147 20.130 0.50 19.70 C ANISOU 629 C BMET A 72 2153 2603 2730 314 401 -230 C ATOM 630 O AMET A 72 -4.981 14.703 19.184 0.50 18.44 O ANISOU 630 O AMET A 72 1972 2460 2574 368 364 -212 O ATOM 631 O BMET A 72 -5.115 14.563 19.078 0.50 18.32 O ANISOU 631 O BMET A 72 1946 2455 2561 363 355 -211 O ATOM 632 CB AMET A 72 -3.136 15.650 21.770 0.50 17.76 C ANISOU 632 CB AMET A 72 2041 2250 2459 345 511 -252 C ATOM 633 CB BMET A 72 -3.642 15.967 21.578 0.50 20.79 C ANISOU 633 CB BMET A 72 2394 2648 2858 378 511 -246 C ATOM 634 CG AMET A 72 -3.212 16.786 22.794 0.50 22.06 C ANISOU 634 CG AMET A 72 2611 2761 3009 391 581 -273 C ATOM 635 CG BMET A 72 -4.060 17.277 22.273 0.50 25.91 C ANISOU 635 CG BMET A 72 3047 3272 3528 453 573 -260 C ATOM 636 SD AMET A 72 -1.654 17.371 23.578 0.50 25.55 S ANISOU 636 SD AMET A 72 3175 3119 3415 362 608 -295 S ATOM 637 SD BMET A 72 -5.465 18.205 21.550 0.50 33.03 S ANISOU 637 SD BMET A 72 3858 4207 4486 567 562 -237 S ATOM 638 CE AMET A 72 -2.392 18.134 25.049 0.50 22.75 C ANISOU 638 CE AMET A 72 2817 2769 3059 398 694 -342 C ATOM 639 CE BMET A 72 -4.968 18.315 19.814 0.50 28.57 C ANISOU 639 CE BMET A 72 3326 3624 3904 581 469 -187 C ATOM 640 N PHE A 73 -3.968 12.959 20.222 1.00 15.91 N ANISOU 640 N PHE A 73 1709 2105 2233 236 377 -244 N ATOM 641 CA PHE A 73 -3.850 12.079 19.052 1.00 16.42 C ANISOU 641 CA PHE A 73 1775 2179 2283 208 300 -254 C ATOM 642 C PHE A 73 -5.227 11.621 18.573 1.00 21.75 C ANISOU 642 C PHE A 73 2352 2924 2988 191 252 -248 C ATOM 643 O PHE A 73 -5.499 11.647 17.375 1.00 21.47 O ANISOU 643 O PHE A 73 2302 2920 2936 213 187 -248 O ATOM 644 CB PHE A 73 -2.961 10.859 19.358 1.00 16.71 C ANISOU 644 CB PHE A 73 1868 2171 2310 137 286 -276 C ATOM 645 CG PHE A 73 -1.860 10.650 18.350 1.00 17.68 C ANISOU 645 CG PHE A 73 2057 2267 2395 153 250 -297 C ATOM 646 CD1 PHE A 73 -0.907 11.636 18.124 1.00 18.44 C ANISOU 646 CD1 PHE A 73 2204 2342 2461 202 280 -286 C ATOM 647 CD2 PHE A 73 -1.740 9.443 17.666 1.00 17.33 C ANISOU 647 CD2 PHE A 73 2025 2214 2345 115 191 -332 C ATOM 648 CE1 PHE A 73 0.126 11.433 17.206 1.00 17.35 C ANISOU 648 CE1 PHE A 73 2115 2196 2283 213 260 -303 C ATOM 649 CE2 PHE A 73 -0.699 9.240 16.749 1.00 18.78 C ANISOU 649 CE2 PHE A 73 2267 2382 2486 138 171 -361 C ATOM 650 CZ PHE A 73 0.198 10.248 16.497 1.00 16.16 C ANISOU 650 CZ PHE A 73 1971 2050 2119 188 209 -343 C ATOM 651 N LYS A 74 -6.111 11.268 19.517 1.00 19.83 N ANISOU 651 N LYS A 74 2036 2714 2783 150 285 -240 N ATOM 652 CA LYS A 74 -7.481 10.852 19.205 1.00 19.68 C ANISOU 652 CA LYS A 74 1901 2771 2804 122 244 -229 C ATOM 653 C LYS A 74 -8.244 12.005 18.515 1.00 24.60 C ANISOU 653 C LYS A 74 2457 3449 3439 220 229 -208 C ATOM 654 O LYS A 74 -8.926 11.775 17.508 1.00 23.67 O ANISOU 654 O LYS A 74 2281 3384 3328 219 148 -203 O ATOM 655 CB LYS A 74 -8.205 10.405 20.493 1.00 20.98 C ANISOU 655 CB LYS A 74 1997 2971 3004 60 306 -214 C ATOM 656 CG LYS A 74 -9.659 9.987 20.267 1.00 24.15 C ANISOU 656 CG LYS A 74 2256 3464 3456 20 273 -196 C ATOM 657 CD LYS A 74 -10.292 9.535 21.579 1.00 36.28 C ANISOU 657 CD LYS A 74 3725 5042 5018 -51 348 -173 C ATOM 658 CE LYS A 74 -11.764 9.235 21.446 1.00 45.74 C ANISOU 658 CE LYS A 74 4760 6347 6273 -91 329 -149 C ATOM 659 NZ LYS A 74 -11.986 7.974 20.682 1.00 46.39 N ANISOU 659 NZ LYS A 74 4831 6417 6377 -203 222 -152 N ATOM 660 N VAL A 75 -8.121 13.234 19.063 1.00 20.79 N ANISOU 660 N VAL A 75 1990 2948 2962 306 300 -198 N ATOM 661 CA VAL A 75 -8.785 14.439 18.536 1.00 21.94 C ANISOU 661 CA VAL A 75 2084 3122 3130 415 291 -173 C ATOM 662 C VAL A 75 -8.236 14.765 17.129 1.00 23.17 C ANISOU 662 C VAL A 75 2304 3258 3243 452 212 -155 C ATOM 663 O VAL A 75 -9.020 15.036 16.234 1.00 21.64 O ANISOU 663 O VAL A 75 2044 3120 3058 495 146 -128 O ATOM 664 CB VAL A 75 -8.661 15.649 19.517 1.00 26.53 C ANISOU 664 CB VAL A 75 2690 3662 3728 497 387 -177 C ATOM 665 CG1 VAL A 75 -9.034 16.975 18.841 1.00 27.75 C ANISOU 665 CG1 VAL A 75 2832 3805 3908 621 367 -148 C ATOM 666 CG2 VAL A 75 -9.557 15.428 20.740 1.00 26.99 C ANISOU 666 CG2 VAL A 75 2655 3780 3822 479 464 -192 C ATOM 667 N GLU A 76 -6.921 14.714 16.944 1.00 19.27 N ANISOU 667 N GLU A 76 1929 2696 2699 431 219 -167 N ATOM 668 CA GLU A 76 -6.287 15.017 15.655 1.00 19.21 C ANISOU 668 CA GLU A 76 1987 2678 2636 458 162 -148 C ATOM 669 C GLU A 76 -6.700 14.011 14.570 1.00 22.52 C ANISOU 669 C GLU A 76 2374 3161 3022 410 67 -162 C ATOM 670 O GLU A 76 -7.039 14.433 13.464 1.00 22.22 O ANISOU 670 O GLU A 76 2324 3165 2952 454 2 -131 O ATOM 671 CB GLU A 76 -4.758 15.074 15.780 1.00 18.91 C ANISOU 671 CB GLU A 76 2066 2566 2554 435 200 -162 C ATOM 672 CG GLU A 76 -4.271 16.375 16.393 1.00 30.12 C ANISOU 672 CG GLU A 76 3535 3919 3991 491 266 -139 C ATOM 673 CD GLU A 76 -2.826 16.443 16.863 1.00 42.68 C ANISOU 673 CD GLU A 76 5220 5442 5555 455 312 -155 C ATOM 674 OE1 GLU A 76 -2.026 15.516 16.584 1.00 29.53 O ANISOU 674 OE1 GLU A 76 3587 3781 3854 400 295 -178 O ATOM 675 OE2 GLU A 76 -2.482 17.478 17.475 1.00 32.87 O ANISOU 675 OE2 GLU A 76 4018 4140 4332 488 360 -145 O ATOM 676 N LEU A 77 -6.703 12.702 14.891 1.00 18.87 N ANISOU 676 N LEU A 77 1901 2702 2568 320 54 -206 N ATOM 677 CA LEU A 77 -7.095 11.661 13.938 1.00 18.48 C ANISOU 677 CA LEU A 77 1831 2699 2493 263 -40 -236 C ATOM 678 C LEU A 77 -8.597 11.816 13.563 1.00 23.19 C ANISOU 678 C LEU A 77 2299 3385 3126 276 -104 -209 C ATOM 679 O LEU A 77 -8.939 11.739 12.382 1.00 23.57 O ANISOU 679 O LEU A 77 2336 3488 3130 284 -195 -208 O ATOM 680 CB LEU A 77 -6.783 10.254 14.492 1.00 17.37 C ANISOU 680 CB LEU A 77 1713 2516 2369 163 -39 -286 C ATOM 681 CG LEU A 77 -7.295 9.026 13.704 1.00 21.10 C ANISOU 681 CG LEU A 77 2166 3017 2835 87 -138 -331 C ATOM 682 CD1 LEU A 77 -6.825 9.036 12.218 1.00 19.68 C ANISOU 682 CD1 LEU A 77 2051 2860 2564 117 -207 -360 C ATOM 683 CD2 LEU A 77 -6.815 7.732 14.380 1.00 21.08 C ANISOU 683 CD2 LEU A 77 2210 2940 2862 -2 -127 -373 C ATOM 684 N LYS A 78 -9.464 12.110 14.540 1.00 19.22 N ANISOU 684 N LYS A 78 1698 2908 2698 287 -54 -186 N ATOM 685 CA LYS A 78 -10.882 12.345 14.248 1.00 20.15 C ANISOU 685 CA LYS A 78 1673 3121 2861 311 -107 -156 C ATOM 686 C LYS A 78 -11.052 13.558 13.286 1.00 26.20 C ANISOU 686 C LYS A 78 2439 3914 3601 427 -153 -107 C ATOM 687 O LYS A 78 -11.846 13.495 12.335 1.00 25.84 O ANISOU 687 O LYS A 78 2323 3949 3546 435 -254 -88 O ATOM 688 CB LYS A 78 -11.671 12.549 15.543 1.00 22.20 C ANISOU 688 CB LYS A 78 1827 3408 3201 316 -22 -142 C ATOM 689 CG LYS A 78 -13.177 12.563 15.316 1.00 31.32 C ANISOU 689 CG LYS A 78 2807 4676 4416 324 -74 -115 C ATOM 690 CD LYS A 78 -13.939 12.793 16.606 1.00 42.50 C ANISOU 690 CD LYS A 78 4111 6134 5904 336 29 -104 C ATOM 691 CE LYS A 78 -15.432 12.832 16.353 1.00 53.58 C ANISOU 691 CE LYS A 78 5320 7665 7375 350 -20 -74 C ATOM 692 NZ LYS A 78 -16.210 12.957 17.616 1.00 64.72 N ANISOU 692 NZ LYS A 78 6606 9134 8850 355 92 -67 N ATOM 693 N ARG A 79 -10.289 14.636 13.526 1.00 23.85 N ANISOU 693 N ARG A 79 2225 3547 3291 509 -86 -83 N ATOM 694 CA ARG A 79 -10.325 15.828 12.688 1.00 25.95 C ANISOU 694 CA ARG A 79 2512 3813 3535 615 -123 -24 C ATOM 695 C ARG A 79 -9.807 15.523 11.264 1.00 27.71 C ANISOU 695 C ARG A 79 2811 4062 3657 591 -215 -17 C ATOM 696 O ARG A 79 -10.393 16.031 10.310 1.00 28.56 O ANISOU 696 O ARG A 79 2884 4226 3741 647 -298 34 O ATOM 697 CB ARG A 79 -9.533 16.985 13.322 1.00 29.63 C ANISOU 697 CB ARG A 79 3065 4179 4013 687 -30 -4 C ATOM 698 CG ARG A 79 -9.852 18.347 12.699 1.00 45.95 C ANISOU 698 CG ARG A 79 5133 6232 6093 808 -61 69 C ATOM 699 CD ARG A 79 -9.236 19.510 13.463 1.00 65.90 C ANISOU 699 CD ARG A 79 7737 8646 8654 874 29 80 C ATOM 700 NE ARG A 79 -7.770 19.510 13.395 1.00 72.60 N ANISOU 700 NE ARG A 79 8726 9420 9439 820 65 71 N ATOM 701 CZ ARG A 79 -6.967 19.304 14.436 1.00 78.92 C ANISOU 701 CZ ARG A 79 9581 10158 10246 770 149 20 C ATOM 702 NH1 ARG A 79 -7.477 19.103 15.652 1.00 57.35 N ANISOU 702 NH1 ARG A 79 6790 7430 7571 765 212 -25 N ATOM 703 NH2 ARG A 79 -5.649 19.309 14.276 1.00 58.18 N ANISOU 703 NH2 ARG A 79 7064 7477 7566 722 171 18 N ATOM 704 N LEU A 80 -8.740 14.698 11.117 1.00 22.91 N ANISOU 704 N LEU A 80 2303 3417 2986 514 -201 -69 N ATOM 705 CA LEU A 80 -8.210 14.300 9.797 1.00 22.58 C ANISOU 705 CA LEU A 80 2335 3409 2836 490 -274 -80 C ATOM 706 C LEU A 80 -9.251 13.505 9.026 1.00 26.58 C ANISOU 706 C LEU A 80 2762 4011 3326 446 -391 -102 C ATOM 707 O LEU A 80 -9.489 13.782 7.848 1.00 25.91 O ANISOU 707 O LEU A 80 2687 3992 3166 475 -479 -71 O ATOM 708 CB LEU A 80 -6.896 13.486 9.902 1.00 21.47 C ANISOU 708 CB LEU A 80 2301 3210 2645 426 -226 -145 C ATOM 709 CG LEU A 80 -5.652 14.256 10.331 1.00 24.86 C ANISOU 709 CG LEU A 80 2821 3561 3063 459 -131 -121 C ATOM 710 CD1 LEU A 80 -4.395 13.420 10.116 1.00 23.56 C ANISOU 710 CD1 LEU A 80 2745 3369 2839 407 -105 -181 C ATOM 711 CD2 LEU A 80 -5.539 15.624 9.602 1.00 27.77 C ANISOU 711 CD2 LEU A 80 3223 3935 3392 540 -140 -35 C ATOM 712 N GLN A 81 -9.897 12.541 9.700 1.00 23.32 N ANISOU 712 N GLN A 81 2270 3610 2982 370 -398 -149 N ATOM 713 CA GLN A 81 -10.969 11.742 9.092 1.00 23.85 C ANISOU 713 CA GLN A 81 2247 3765 3052 309 -514 -173 C ATOM 714 C GLN A 81 -12.114 12.633 8.627 1.00 29.24 C ANISOU 714 C GLN A 81 2814 4538 3759 386 -583 -99 C ATOM 715 O GLN A 81 -12.697 12.345 7.593 1.00 30.77 O ANISOU 715 O GLN A 81 2973 4816 3901 365 -705 -100 O ATOM 716 CB GLN A 81 -11.498 10.686 10.059 1.00 24.22 C ANISOU 716 CB GLN A 81 2217 3799 3186 208 -495 -217 C ATOM 717 CG GLN A 81 -10.600 9.478 10.098 1.00 24.92 C ANISOU 717 CG GLN A 81 2412 3814 3241 117 -487 -297 C ATOM 718 CD GLN A 81 -11.158 8.361 10.916 1.00 34.72 C ANISOU 718 CD GLN A 81 3590 5037 4565 5 -488 -329 C ATOM 719 OE1 GLN A 81 -12.288 7.891 10.728 1.00 40.35 O ANISOU 719 OE1 GLN A 81 4192 5819 5320 -59 -568 -329 O ATOM 720 NE2 GLN A 81 -10.317 7.820 11.735 1.00 23.09 N ANISOU 720 NE2 GLN A 81 2193 3470 3110 -33 -412 -357 N ATOM 721 N ARG A 82 -12.427 13.719 9.367 1.00 26.83 N ANISOU 721 N ARG A 82 2452 4214 3528 479 -512 -38 N ATOM 722 CA ARG A 82 -13.490 14.632 8.935 1.00 28.26 C ANISOU 722 CA ARG A 82 2522 4471 3744 575 -577 36 C ATOM 723 C ARG A 82 -13.029 15.390 7.675 1.00 31.85 C ANISOU 723 C ARG A 82 3071 4935 4094 644 -646 93 C ATOM 724 O ARG A 82 -13.804 15.478 6.727 1.00 31.99 O ANISOU 724 O ARG A 82 3027 5048 4081 664 -769 132 O ATOM 725 CB ARG A 82 -13.915 15.599 10.049 1.00 28.57 C ANISOU 725 CB ARG A 82 2485 4477 3892 670 -478 75 C ATOM 726 CG ARG A 82 -15.091 16.500 9.621 1.00 40.61 C ANISOU 726 CG ARG A 82 3879 6081 5471 784 -550 150 C ATOM 727 CD ARG A 82 -15.977 16.956 10.773 1.00 50.04 C ANISOU 727 CD ARG A 82 4930 7290 6793 849 -467 157 C ATOM 728 NE ARG A 82 -15.256 17.749 11.768 1.00 55.71 N ANISOU 728 NE ARG A 82 5736 7892 7541 914 -329 148 N ATOM 729 CZ ARG A 82 -15.112 19.070 11.716 1.00 78.70 C ANISOU 729 CZ ARG A 82 8692 10735 10475 1051 -305 200 C ATOM 730 NH1 ARG A 82 -15.628 19.762 10.707 1.00 69.01 N ANISOU 730 NH1 ARG A 82 7431 9545 9244 1143 -410 277 N ATOM 731 NH2 ARG A 82 -14.446 19.709 12.670 1.00 67.86 N ANISOU 731 NH2 ARG A 82 7404 9253 9128 1092 -184 177 N ATOM 732 N HIS A 83 -11.758 15.875 7.647 1.00 27.81 N ANISOU 732 N HIS A 83 2709 4334 3524 667 -571 102 N ATOM 733 CA HIS A 83 -11.203 16.587 6.483 1.00 29.32 C ANISOU 733 CA HIS A 83 3002 4533 3606 719 -620 166 C ATOM 734 C HIS A 83 -11.243 15.717 5.210 1.00 33.26 C ANISOU 734 C HIS A 83 3531 5128 3980 650 -737 131 C ATOM 735 O HIS A 83 -11.635 16.209 4.153 1.00 33.95 O ANISOU 735 O HIS A 83 3616 5289 3996 696 -837 198 O ATOM 736 CB HIS A 83 -9.772 17.057 6.746 1.00 29.76 C ANISOU 736 CB HIS A 83 3200 4483 3624 725 -511 170 C ATOM 737 CG HIS A 83 -9.669 18.351 7.499 1.00 34.05 C ANISOU 737 CG HIS A 83 3752 4934 4251 818 -432 233 C ATOM 738 ND1 HIS A 83 -9.056 18.417 8.740 1.00 35.17 N ANISOU 738 ND1 HIS A 83 3924 4981 4460 803 -312 190 N ATOM 739 CD2 HIS A 83 -10.073 19.592 7.149 1.00 37.69 C ANISOU 739 CD2 HIS A 83 4207 5379 4736 925 -463 333 C ATOM 740 CE1 HIS A 83 -9.122 19.688 9.110 1.00 35.19 C ANISOU 740 CE1 HIS A 83 3937 4910 4522 897 -273 253 C ATOM 741 NE2 HIS A 83 -9.727 20.432 8.190 1.00 37.00 N ANISOU 741 NE2 HIS A 83 4147 5176 4735 976 -360 341 N ATOM 742 N TYR A 84 -10.880 14.424 5.330 1.00 28.38 N ANISOU 742 N TYR A 84 2940 4506 3336 543 -729 26 N ATOM 743 CA TYR A 84 -10.868 13.474 4.215 1.00 28.52 C ANISOU 743 CA TYR A 84 2999 4600 3237 471 -833 -36 C ATOM 744 C TYR A 84 -12.218 12.836 3.941 1.00 33.65 C ANISOU 744 C TYR A 84 3518 5346 3921 422 -961 -58 C ATOM 745 O TYR A 84 -12.340 12.107 2.953 1.00 33.67 O ANISOU 745 O TYR A 84 3551 5418 3822 362 -1067 -111 O ATOM 746 CB TYR A 84 -9.876 12.346 4.494 1.00 27.45 C ANISOU 746 CB TYR A 84 2955 4400 3073 386 -771 -147 C ATOM 747 CG TYR A 84 -8.435 12.713 4.267 1.00 27.32 C ANISOU 747 CG TYR A 84 3078 4331 2973 415 -680 -144 C ATOM 748 CD1 TYR A 84 -7.938 12.921 2.977 1.00 29.80 C ANISOU 748 CD1 TYR A 84 3481 4710 3131 433 -723 -129 C ATOM 749 CD2 TYR A 84 -7.545 12.793 5.331 1.00 25.47 C ANISOU 749 CD2 TYR A 84 2881 3991 2804 416 -552 -157 C ATOM 750 CE1 TYR A 84 -6.591 13.230 2.765 1.00 29.42 C ANISOU 750 CE1 TYR A 84 3546 4626 3006 451 -631 -124 C ATOM 751 CE2 TYR A 84 -6.202 13.101 5.129 1.00 25.35 C ANISOU 751 CE2 TYR A 84 2978 3937 2719 434 -472 -153 C ATOM 752 CZ TYR A 84 -5.733 13.325 3.846 1.00 29.05 C ANISOU 752 CZ TYR A 84 3523 4474 3042 451 -507 -135 C ATOM 753 OH TYR A 84 -4.403 13.630 3.670 1.00 29.06 O ANISOU 753 OH TYR A 84 3617 4446 2977 463 -417 -126 O ATOM 754 N ASN A 85 -13.215 13.071 4.829 1.00 30.62 N ANISOU 754 N ASN A 85 2987 4970 3677 440 -950 -24 N ATOM 755 CA ASN A 85 -14.551 12.467 4.780 1.00 31.90 C ANISOU 755 CA ASN A 85 2993 5226 3903 383 -1057 -39 C ATOM 756 C ASN A 85 -14.383 10.928 4.772 1.00 35.31 C ANISOU 756 C ASN A 85 3459 5641 4315 236 -1087 -157 C ATOM 757 O ASN A 85 -14.854 10.238 3.874 1.00 35.76 O ANISOU 757 O ASN A 85 3504 5774 4310 167 -1220 -202 O ATOM 758 CB ASN A 85 -15.392 13.002 3.582 1.00 38.58 C ANISOU 758 CB ASN A 85 3778 6197 4686 436 -1211 30 C ATOM 759 CG ASN A 85 -16.852 12.643 3.681 1.00 70.15 C ANISOU 759 CG ASN A 85 7578 10298 8777 398 -1314 38 C ATOM 760 OD1 ASN A 85 -17.544 12.994 4.643 1.00 65.92 O ANISOU 760 OD1 ASN A 85 6903 9763 8379 436 -1255 74 O ATOM 761 ND2 ASN A 85 -17.341 11.890 2.711 1.00 68.25 N ANISOU 761 ND2 ASN A 85 7318 10152 8460 314 -1466 -5 N ATOM 762 N HIS A 86 -13.609 10.424 5.754 1.00 32.35 N ANISOU 762 N HIS A 86 3146 5156 3988 193 -966 -209 N ATOM 763 CA HIS A 86 -13.282 9.005 5.947 1.00 31.49 C ANISOU 763 CA HIS A 86 3090 4992 3882 66 -972 -314 C ATOM 764 C HIS A 86 -14.003 8.437 7.150 1.00 37.18 C ANISOU 764 C HIS A 86 3691 5692 4743 -10 -932 -317 C ATOM 765 O HIS A 86 -14.002 9.051 8.215 1.00 37.04 O ANISOU 765 O HIS A 86 3627 5642 4806 41 -820 -266 O ATOM 766 CB HIS A 86 -11.765 8.828 6.157 1.00 29.98 C ANISOU 766 CB HIS A 86 3063 4690 3636 79 -866 -361 C ATOM 767 CG HIS A 86 -10.945 8.890 4.905 1.00 32.59 C ANISOU 767 CG HIS A 86 3526 5044 3814 109 -905 -393 C ATOM 768 ND1 HIS A 86 -9.562 8.975 4.959 1.00 32.42 N ANISOU 768 ND1 HIS A 86 3635 4948 3735 143 -806 -417 N ATOM 769 CD2 HIS A 86 -11.337 8.886 3.605 1.00 34.19 C ANISOU 769 CD2 HIS A 86 3740 5346 3904 109 -1030 -402 C ATOM 770 CE1 HIS A 86 -9.162 9.011 3.697 1.00 32.29 C ANISOU 770 CE1 HIS A 86 3703 4990 3574 162 -862 -441 C ATOM 771 NE2 HIS A 86 -10.201 8.973 2.850 1.00 33.59 N ANISOU 771 NE2 HIS A 86 3807 5261 3695 143 -998 -432 N ATOM 772 N SER A 87 -14.591 7.265 6.990 1.00 35.64 N ANISOU 772 N SER A 87 3454 5514 4575 -138 -1021 -378 N ATOM 773 CA SER A 87 -15.270 6.551 8.065 1.00 35.70 C ANISOU 773 CA SER A 87 3354 5502 4709 -240 -990 -379 C ATOM 774 C SER A 87 -14.529 5.232 8.301 1.00 37.61 C ANISOU 774 C SER A 87 3717 5625 4949 -351 -979 -469 C ATOM 775 O SER A 87 -13.719 4.826 7.472 1.00 37.31 O ANISOU 775 O SER A 87 3820 5543 4814 -350 -1020 -542 O ATOM 776 CB SER A 87 -16.737 6.323 7.712 1.00 39.67 C ANISOU 776 CB SER A 87 3679 6129 5266 -307 -1114 -358 C ATOM 777 OG SER A 87 -16.849 5.400 6.643 1.00 50.67 O ANISOU 777 OG SER A 87 5124 7537 6591 -403 -1260 -439 O ATOM 778 N GLY A 88 -14.789 4.585 9.419 1.00 33.40 N ANISOU 778 N GLY A 88 3132 5039 4519 -440 -921 -461 N ATOM 779 CA GLY A 88 -14.116 3.337 9.734 1.00 32.32 C ANISOU 779 CA GLY A 88 3110 4774 4397 -541 -913 -532 C ATOM 780 C GLY A 88 -12.770 3.586 10.377 1.00 34.19 C ANISOU 780 C GLY A 88 3477 4904 4608 -465 -785 -532 C ATOM 781 O GLY A 88 -12.495 4.688 10.851 1.00 33.78 O ANISOU 781 O GLY A 88 3409 4875 4551 -359 -689 -470 O ATOM 782 N SER A 89 -11.936 2.558 10.392 1.00 30.54 N ANISOU 782 N SER A 89 3144 4322 4137 -519 -789 -605 N ATOM 783 CA SER A 89 -10.637 2.534 11.043 1.00 30.22 C ANISOU 783 CA SER A 89 3223 4173 4087 -468 -683 -612 C ATOM 784 C SER A 89 -9.526 3.113 10.171 1.00 32.57 C ANISOU 784 C SER A 89 3634 4470 4271 -353 -665 -650 C ATOM 785 O SER A 89 -9.282 2.648 9.056 1.00 33.84 O ANISOU 785 O SER A 89 3868 4633 4357 -357 -745 -731 O ATOM 786 CB SER A 89 -10.292 1.104 11.447 1.00 32.36 C ANISOU 786 CB SER A 89 3572 4312 4412 -574 -704 -667 C ATOM 787 OG SER A 89 -9.157 1.117 12.291 1.00 38.74 O ANISOU 787 OG SER A 89 4466 5027 5228 -525 -600 -652 O ATOM 788 N HIS A 90 -8.862 4.142 10.692 1.00 25.95 N ANISOU 788 N HIS A 90 2809 3633 3417 -255 -558 -592 N ATOM 789 CA HIS A 90 -7.754 4.815 10.020 1.00 22.90 C ANISOU 789 CA HIS A 90 2519 3249 2933 -152 -521 -607 C ATOM 790 C HIS A 90 -6.616 4.925 11.009 1.00 26.50 C ANISOU 790 C HIS A 90 3038 3616 3414 -118 -408 -591 C ATOM 791 O HIS A 90 -6.841 4.738 12.211 1.00 26.97 O ANISOU 791 O HIS A 90 3057 3634 3557 -160 -359 -552 O ATOM 792 CB HIS A 90 -8.199 6.157 9.437 1.00 23.19 C ANISOU 792 CB HIS A 90 2499 3392 2919 -68 -528 -541 C ATOM 793 CG HIS A 90 -9.078 5.946 8.239 1.00 28.13 C ANISOU 793 CG HIS A 90 3088 4109 3492 -95 -658 -569 C ATOM 794 ND1 HIS A 90 -10.440 5.732 8.375 1.00 31.84 N ANISOU 794 ND1 HIS A 90 3428 4639 4029 -160 -731 -546 N ATOM 795 CD2 HIS A 90 -8.743 5.795 6.941 1.00 30.58 C ANISOU 795 CD2 HIS A 90 3476 4459 3686 -78 -727 -625 C ATOM 796 CE1 HIS A 90 -10.899 5.508 7.149 1.00 32.55 C ANISOU 796 CE1 HIS A 90 3520 4803 4045 -179 -852 -585 C ATOM 797 NE2 HIS A 90 -9.912 5.523 6.252 1.00 32.73 N ANISOU 797 NE2 HIS A 90 3672 4816 3949 -132 -854 -637 N ATOM 798 N ATHR A 91 -5.392 5.153 10.518 0.50 21.56 N ANISOU 798 N ATHR A 91 2509 2967 2715 -51 -370 -621 N ATOM 799 N BTHR A 91 -5.387 5.143 10.509 0.50 21.76 N ANISOU 799 N BTHR A 91 2536 2993 2740 -51 -371 -622 N ATOM 800 CA ATHR A 91 -4.240 5.264 11.409 0.50 20.16 C ANISOU 800 CA ATHR A 91 2386 2714 2561 -19 -273 -606 C ATOM 801 CA BTHR A 91 -4.166 5.180 11.320 0.50 20.49 C ANISOU 801 CA BTHR A 91 2436 2753 2598 -19 -277 -614 C ATOM 802 C ATHR A 91 -3.599 6.626 11.316 0.50 22.74 C ANISOU 802 C ATHR A 91 2723 3079 2837 70 -203 -550 C ATOM 803 C BTHR A 91 -3.479 6.552 11.257 0.50 22.69 C ANISOU 803 C BTHR A 91 2727 3068 2826 71 -203 -557 C ATOM 804 O ATHR A 91 -3.678 7.311 10.290 0.50 22.18 O ANISOU 804 O ATHR A 91 2657 3079 2689 117 -228 -538 O ATOM 805 O BTHR A 91 -3.414 7.172 10.193 0.50 21.93 O ANISOU 805 O BTHR A 91 2647 3040 2647 119 -225 -553 O ATOM 806 CB ATHR A 91 -3.195 4.163 11.167 0.50 25.96 C ANISOU 806 CB ATHR A 91 3218 3366 3281 -27 -280 -691 C ATOM 807 CB BTHR A 91 -3.235 4.042 10.845 0.50 27.65 C ANISOU 807 CB BTHR A 91 3440 3588 3479 -27 -299 -710 C ATOM 808 OG1ATHR A 91 -2.637 4.298 9.862 0.50 24.01 O ANISOU 808 OG1ATHR A 91 3028 3167 2928 27 -300 -746 O ATOM 809 OG1BTHR A 91 -3.899 2.790 11.029 0.50 27.96 O ANISOU 809 OG1BTHR A 91 3475 3568 3581 -120 -371 -756 O ATOM 810 CG2ATHR A 91 -3.748 2.768 11.382 0.50 24.95 C ANISOU 810 CG2ATHR A 91 3095 3166 3220 -121 -350 -744 C ATOM 811 CG2BTHR A 91 -1.913 4.004 11.571 0.50 24.42 C ANISOU 811 CG2BTHR A 91 3085 3105 3087 12 -216 -706 C ATOM 812 N TYR A 92 -2.952 7.011 12.413 1.00 17.77 N ANISOU 812 N TYR A 92 2102 2398 2250 86 -119 -511 N ATOM 813 CA TYR A 92 -2.234 8.256 12.546 1.00 15.13 C ANISOU 813 CA TYR A 92 1787 2076 1887 154 -48 -459 C ATOM 814 C TYR A 92 -0.923 7.916 13.235 1.00 17.39 C ANISOU 814 C TYR A 92 2130 2289 2188 156 12 -476 C ATOM 815 O TYR A 92 -0.917 7.134 14.196 1.00 14.38 O ANISOU 815 O TYR A 92 1748 1849 1868 109 18 -486 O ATOM 816 CB TYR A 92 -3.082 9.224 13.357 1.00 15.21 C ANISOU 816 CB TYR A 92 1726 2106 1948 168 -15 -390 C ATOM 817 CG TYR A 92 -2.561 10.638 13.496 1.00 16.59 C ANISOU 817 CG TYR A 92 1919 2280 2104 235 47 -334 C ATOM 818 CD1 TYR A 92 -2.105 11.350 12.387 1.00 18.93 C ANISOU 818 CD1 TYR A 92 2254 2612 2328 285 37 -315 C ATOM 819 CD2 TYR A 92 -2.687 11.326 14.701 1.00 18.16 C ANISOU 819 CD2 TYR A 92 2094 2449 2357 246 110 -298 C ATOM 820 CE1 TYR A 92 -1.689 12.683 12.502 1.00 20.60 C ANISOU 820 CE1 TYR A 92 2486 2810 2533 336 87 -255 C ATOM 821 CE2 TYR A 92 -2.282 12.654 14.826 1.00 19.06 C ANISOU 821 CE2 TYR A 92 2232 2548 2463 303 159 -253 C ATOM 822 CZ TYR A 92 -1.813 13.340 13.720 1.00 24.62 C ANISOU 822 CZ TYR A 92 2975 3272 3107 346 144 -227 C ATOM 823 OH TYR A 92 -1.466 14.666 13.872 1.00 23.50 O ANISOU 823 OH TYR A 92 2860 3101 2968 393 187 -176 O ATOM 824 N GLN A 93 0.182 8.448 12.720 1.00 13.78 N ANISOU 824 N GLN A 93 1720 1842 1673 205 50 -475 N ATOM 825 CA GLN A 93 1.479 8.142 13.292 1.00 13.31 C ANISOU 825 CA GLN A 93 1701 1728 1629 212 100 -491 C ATOM 826 C GLN A 93 2.342 9.357 13.402 1.00 15.57 C ANISOU 826 C GLN A 93 1999 2028 1891 250 165 -439 C ATOM 827 O GLN A 93 2.224 10.307 12.626 1.00 14.30 O ANISOU 827 O GLN A 93 1839 1918 1678 281 170 -403 O ATOM 828 CB GLN A 93 2.217 7.049 12.497 1.00 15.00 C ANISOU 828 CB GLN A 93 1962 1929 1809 222 77 -572 C ATOM 829 CG GLN A 93 1.590 5.646 12.619 1.00 17.19 C ANISOU 829 CG GLN A 93 2246 2152 2132 172 11 -632 C ATOM 830 CD GLN A 93 2.119 4.717 11.550 1.00 24.70 C ANISOU 830 CD GLN A 93 3252 3099 3036 195 -21 -728 C ATOM 831 OE1 GLN A 93 1.592 4.624 10.431 1.00 19.97 O ANISOU 831 OE1 GLN A 93 2664 2556 2370 197 -70 -771 O ATOM 832 NE2 GLN A 93 3.190 4.028 11.865 1.00 18.62 N ANISOU 832 NE2 GLN A 93 2516 2265 2294 220 4 -767 N ATOM 833 N ARG A 94 3.239 9.309 14.373 1.00 11.39 N ANISOU 833 N ARG A 94 1481 1448 1400 242 208 -431 N ATOM 834 CA ARG A 94 4.201 10.374 14.613 1.00 11.70 C ANISOU 834 CA ARG A 94 1530 1490 1427 262 266 -387 C ATOM 835 C ARG A 94 5.528 9.758 14.942 1.00 14.90 C ANISOU 835 C ARG A 94 1950 1867 1844 264 288 -414 C ATOM 836 O ARG A 94 5.595 8.725 15.620 1.00 14.64 O ANISOU 836 O ARG A 94 1921 1786 1858 245 267 -443 O ATOM 837 CB ARG A 94 3.757 11.268 15.806 1.00 12.27 C ANISOU 837 CB ARG A 94 1586 1530 1544 246 293 -337 C ATOM 838 CG ARG A 94 4.641 12.517 16.094 1.00 15.85 C ANISOU 838 CG ARG A 94 2058 1973 1992 256 343 -292 C ATOM 839 CD ARG A 94 4.228 13.025 17.456 1.00 14.50 C ANISOU 839 CD ARG A 94 1884 1760 1867 236 364 -274 C ATOM 840 NE ARG A 94 4.624 14.398 17.775 1.00 14.08 N ANISOU 840 NE ARG A 94 1852 1682 1816 243 400 -236 N ATOM 841 CZ ARG A 94 5.542 14.697 18.689 1.00 19.89 C ANISOU 841 CZ ARG A 94 2607 2383 2566 215 425 -234 C ATOM 842 NH1 ARG A 94 6.269 13.742 19.242 1.00 13.21 N ANISOU 842 NH1 ARG A 94 1757 1532 1729 188 416 -257 N ATOM 843 NH2 ARG A 94 5.751 15.956 19.038 1.00 13.30 N ANISOU 843 NH2 ARG A 94 1800 1514 1741 213 450 -208 N ATOM 844 N AMET A 95 6.609 10.373 14.461 0.50 10.91 N ANISOU 844 N AMET A 95 1450 1394 1303 285 330 -398 N ATOM 845 N BMET A 95 6.574 10.409 14.486 0.50 12.44 N ANISOU 845 N BMET A 95 1644 1587 1497 285 330 -396 N ATOM 846 CA AMET A 95 7.977 9.955 14.799 0.50 10.60 C ANISOU 846 CA AMET A 95 1405 1342 1281 293 356 -415 C ATOM 847 CA BMET A 95 7.928 10.044 14.839 0.50 13.01 C ANISOU 847 CA BMET A 95 1710 1646 1587 291 357 -410 C ATOM 848 C AMET A 95 8.813 11.202 15.020 0.50 15.50 C ANISOU 848 C AMET A 95 2015 1979 1895 281 405 -356 C ATOM 849 C BMET A 95 8.679 11.317 15.121 0.50 16.04 C ANISOU 849 C BMET A 95 2085 2042 1967 277 403 -350 C ATOM 850 O AMET A 95 8.874 12.060 14.135 0.50 14.70 O ANISOU 850 O AMET A 95 1919 1924 1741 289 429 -323 O ATOM 851 O BMET A 95 8.541 12.302 14.394 0.50 14.82 O ANISOU 851 O BMET A 95 1938 1924 1768 281 424 -310 O ATOM 852 CB AMET A 95 8.598 9.050 13.721 0.50 12.74 C ANISOU 852 CB AMET A 95 1681 1649 1512 335 357 -480 C ATOM 853 CB BMET A 95 8.606 9.210 13.752 0.50 16.07 C ANISOU 853 CB BMET A 95 2101 2073 1932 332 361 -471 C ATOM 854 CG AMET A 95 10.012 8.587 14.071 0.50 16.73 C ANISOU 854 CG AMET A 95 2163 2146 2046 358 385 -498 C ATOM 855 CG BMET A 95 9.857 8.543 14.246 0.50 21.19 C ANISOU 855 CG BMET A 95 2730 2700 2621 352 377 -496 C ATOM 856 SD AMET A 95 10.938 7.886 12.678 0.50 21.73 S ANISOU 856 SD AMET A 95 2790 2848 2617 425 417 -574 S ATOM 857 SD BMET A 95 11.354 9.483 13.932 0.50 27.05 S ANISOU 857 SD BMET A 95 3432 3511 3335 361 449 -456 S ATOM 858 CE AMET A 95 11.484 9.421 11.851 0.50 18.45 C ANISOU 858 CE AMET A 95 2354 2536 2119 412 488 -502 C ATOM 859 CE BMET A 95 12.235 8.266 12.923 0.50 25.06 C ANISOU 859 CE BMET A 95 3166 3303 3054 435 468 -547 C ATOM 860 N ILE A 96 9.446 11.298 16.200 1.00 12.07 N ANISOU 860 N ILE A 96 1571 1505 1511 256 412 -339 N ATOM 861 CA ILE A 96 10.326 12.388 16.592 1.00 11.44 C ANISOU 861 CA ILE A 96 1481 1429 1438 229 447 -291 C ATOM 862 C ILE A 96 11.651 11.758 16.976 1.00 15.93 C ANISOU 862 C ILE A 96 2014 2005 2033 233 452 -308 C ATOM 863 O ILE A 96 11.679 10.654 17.516 1.00 14.55 O ANISOU 863 O ILE A 96 1837 1800 1893 247 419 -342 O ATOM 864 CB ILE A 96 9.736 13.272 17.731 1.00 13.15 C ANISOU 864 CB ILE A 96 1720 1593 1684 192 443 -258 C ATOM 865 CG1 ILE A 96 10.459 14.641 17.776 1.00 12.42 C ANISOU 865 CG1 ILE A 96 1634 1498 1589 160 474 -210 C ATOM 866 CG2 ILE A 96 9.740 12.555 19.133 1.00 11.21 C ANISOU 866 CG2 ILE A 96 1476 1304 1480 169 416 -275 C ATOM 867 CD1 ILE A 96 9.850 15.703 18.693 1.00 16.02 C ANISOU 867 CD1 ILE A 96 2125 1894 2067 134 475 -189 C ATOM 868 N GLY A 97 12.742 12.445 16.734 1.00 15.04 N ANISOU 868 N GLY A 97 1871 1932 1912 218 488 -277 N ATOM 869 CA GLY A 97 14.007 11.882 17.176 1.00 15.29 C ANISOU 869 CA GLY A 97 1851 1979 1979 224 487 -289 C ATOM 870 C GLY A 97 15.218 12.693 16.811 1.00 18.96 C ANISOU 870 C GLY A 97 2264 2503 2436 198 532 -250 C ATOM 871 O GLY A 97 15.099 13.738 16.173 1.00 17.06 O ANISOU 871 O GLY A 97 2038 2286 2159 168 566 -208 O ATOM 872 N CYS A 98 16.396 12.203 17.222 1.00 16.39 N ANISOU 872 N CYS A 98 1873 2203 2149 206 529 -258 N ATOM 873 CA CYS A 98 17.656 12.876 16.945 1.00 17.75 C ANISOU 873 CA CYS A 98 1973 2445 2325 173 570 -219 C ATOM 874 C CYS A 98 18.749 11.871 16.780 1.00 21.52 C ANISOU 874 C CYS A 98 2366 2980 2832 234 580 -254 C ATOM 875 O CYS A 98 18.643 10.756 17.284 1.00 20.92 O ANISOU 875 O CYS A 98 2295 2862 2793 287 535 -297 O ATOM 876 CB CYS A 98 17.997 13.874 18.050 1.00 18.46 C ANISOU 876 CB CYS A 98 2065 2498 2452 87 543 -171 C ATOM 877 SG CYS A 98 18.018 13.161 19.730 1.00 22.25 S ANISOU 877 SG CYS A 98 2554 2914 2987 81 460 -190 S ATOM 878 N GLU A 99 19.817 12.276 16.108 1.00 18.82 N ANISOU 878 N GLU A 99 1943 2732 2478 224 639 -231 N ATOM 879 CA GLU A 99 21.019 11.470 15.984 1.00 18.89 C ANISOU 879 CA GLU A 99 1845 2810 2522 285 657 -259 C ATOM 880 C GLU A 99 22.188 12.254 16.480 1.00 23.12 C ANISOU 880 C GLU A 99 2286 3399 3099 211 663 -198 C ATOM 881 O GLU A 99 22.312 13.440 16.155 1.00 20.95 O ANISOU 881 O GLU A 99 2010 3152 2796 125 700 -139 O ATOM 882 CB GLU A 99 21.300 11.023 14.527 1.00 20.63 C ANISOU 882 CB GLU A 99 2030 3125 2681 359 739 -303 C ATOM 883 CG GLU A 99 20.227 10.122 13.954 1.00 35.92 C ANISOU 883 CG GLU A 99 4057 5016 4576 433 725 -378 C ATOM 884 CD GLU A 99 20.558 9.474 12.620 1.00 70.22 C ANISOU 884 CD GLU A 99 8375 9450 8857 519 797 -446 C ATOM 885 OE1 GLU A 99 21.759 9.282 12.313 1.00 44.16 O ANISOU 885 OE1 GLU A 99 4966 6242 5569 559 854 -457 O ATOM 886 OE2 GLU A 99 19.598 9.079 11.918 1.00 77.90 O ANISOU 886 OE2 GLU A 99 9430 10401 9767 552 791 -498 O ATOM 887 N LEU A 100 23.076 11.586 17.208 1.00 19.86 N ANISOU 887 N LEU A 100 1789 3000 2756 244 622 -209 N ATOM 888 CA LEU A 100 24.346 12.149 17.614 1.00 20.61 C ANISOU 888 CA LEU A 100 1764 3167 2898 183 622 -159 C ATOM 889 C LEU A 100 25.411 11.358 16.847 1.00 25.45 C ANISOU 889 C LEU A 100 2245 3894 3530 279 682 -191 C ATOM 890 O LEU A 100 25.603 10.153 17.090 1.00 23.03 O ANISOU 890 O LEU A 100 1912 3569 3268 388 648 -244 O ATOM 891 CB LEU A 100 24.523 12.081 19.132 1.00 20.34 C ANISOU 891 CB LEU A 100 1732 3070 2925 143 517 -140 C ATOM 892 CG LEU A 100 25.906 12.472 19.688 1.00 25.83 C ANISOU 892 CG LEU A 100 2291 3844 3680 85 491 -94 C ATOM 893 CD1 LEU A 100 26.196 13.980 19.515 1.00 26.02 C ANISOU 893 CD1 LEU A 100 2303 3899 3686 -57 523 -32 C ATOM 894 CD2 LEU A 100 26.007 12.091 21.169 1.00 27.75 C ANISOU 894 CD2 LEU A 100 2547 4028 3969 72 373 -87 C ATOM 895 N LEU A 101 26.003 11.989 15.839 1.00 25.23 N ANISOU 895 N LEU A 101 2144 3980 3462 249 778 -163 N ATOM 896 CA LEU A 101 26.993 11.325 14.986 1.00 28.37 C ANISOU 896 CA LEU A 101 2410 4506 3863 343 859 -200 C ATOM 897 C LEU A 101 28.347 11.186 15.657 1.00 33.45 C ANISOU 897 C LEU A 101 2886 5224 4600 343 833 -173 C ATOM 898 O LEU A 101 28.673 11.935 16.587 1.00 31.19 O ANISOU 898 O LEU A 101 2574 4917 4359 231 768 -108 O ATOM 899 CB LEU A 101 27.160 12.055 13.637 1.00 29.49 C ANISOU 899 CB LEU A 101 2528 4764 3914 305 981 -171 C ATOM 900 CG LEU A 101 26.067 11.733 12.612 1.00 35.51 C ANISOU 900 CG LEU A 101 3418 5502 4573 365 1023 -225 C ATOM 901 CD1 LEU A 101 24.768 12.515 12.894 1.00 34.02 C ANISOU 901 CD1 LEU A 101 3385 5192 4348 280 968 -185 C ATOM 902 CD2 LEU A 101 26.560 12.026 11.195 1.00 42.41 C ANISOU 902 CD2 LEU A 101 4232 6530 5351 373 1155 -216 C ATOM 903 N GLU A 102 29.131 10.210 15.166 1.00 34.30 N ANISOU 903 N GLU A 102 2879 5419 4737 473 881 -229 N ATOM 904 CA GLU A 102 30.501 9.920 15.596 1.00 37.12 C ANISOU 904 CA GLU A 102 3046 5872 5187 507 870 -212 C ATOM 905 C GLU A 102 31.342 11.203 15.691 1.00 40.75 C ANISOU 905 C GLU A 102 3390 6435 5658 351 896 -114 C ATOM 906 O GLU A 102 31.980 11.422 16.714 1.00 40.66 O ANISOU 906 O GLU A 102 3297 6425 5726 292 809 -68 O ATOM 907 CB GLU A 102 31.191 8.967 14.585 1.00 40.95 C ANISOU 907 CB GLU A 102 3418 6471 5672 668 971 -290 C ATOM 908 CG GLU A 102 30.962 7.487 14.787 1.00 56.68 C ANISOU 908 CG GLU A 102 5450 8372 7714 843 920 -385 C ATOM 909 CD GLU A 102 32.096 6.625 14.263 1.00 82.31 C ANISOU 909 CD GLU A 102 8526 11736 11014 1000 989 -446 C ATOM 910 OE1 GLU A 102 33.204 6.676 14.846 1.00 69.40 O ANISOU 910 OE1 GLU A 102 6717 10180 9472 1003 960 -399 O ATOM 911 OE2 GLU A 102 31.875 5.889 13.274 1.00 82.94 O ANISOU 911 OE2 GLU A 102 8642 11830 11043 1125 1069 -547 O ATOM 912 N ASP A 103 31.300 12.069 14.641 1.00 38.09 N ANISOU 912 N ASP A 103 3056 6179 5238 274 1008 -78 N ATOM 913 CA ASP A 103 32.084 13.325 14.587 1.00 39.38 C ANISOU 913 CA ASP A 103 3115 6436 5410 111 1044 23 C ATOM 914 C ASP A 103 31.523 14.477 15.483 1.00 41.68 C ANISOU 914 C ASP A 103 3523 6602 5710 -58 949 92 C ATOM 915 O ASP A 103 32.039 15.597 15.418 1.00 42.95 O ANISOU 915 O ASP A 103 3629 6811 5878 -208 972 176 O ATOM 916 CB ASP A 103 32.207 13.819 13.130 1.00 42.24 C ANISOU 916 CB ASP A 103 3452 6924 5672 87 1197 49 C ATOM 917 CG ASP A 103 30.895 14.178 12.440 1.00 54.21 C ANISOU 917 CG ASP A 103 5168 8354 7075 72 1224 44 C ATOM 918 OD1 ASP A 103 29.842 14.188 13.121 1.00 51.46 O ANISOU 918 OD1 ASP A 103 4977 7843 6731 63 1126 26 O ATOM 919 OD2 ASP A 103 30.921 14.449 11.216 1.00 60.82 O ANISOU 919 OD2 ASP A 103 5999 9294 7814 69 1343 61 O ATOM 920 N GLY A 104 30.495 14.193 16.287 1.00 33.58 N ANISOU 920 N GLY A 104 2654 5419 4686 -34 850 55 N ATOM 921 CA GLY A 104 29.884 15.160 17.197 1.00 31.30 C ANISOU 921 CA GLY A 104 2486 5005 4402 -167 762 97 C ATOM 922 C GLY A 104 28.753 15.992 16.616 1.00 32.84 C ANISOU 922 C GLY A 104 2844 5117 4515 -225 801 117 C ATOM 923 O GLY A 104 28.082 16.708 17.359 1.00 32.47 O ANISOU 923 O GLY A 104 2915 4950 4471 -309 732 135 O ATOM 924 N SER A 105 28.530 15.933 15.289 1.00 28.50 N ANISOU 924 N SER A 105 2305 4635 3890 -178 910 115 N ATOM 925 CA SER A 105 27.423 16.652 14.648 1.00 25.80 C ANISOU 925 CA SER A 105 2115 4221 3466 -217 940 140 C ATOM 926 C SER A 105 26.074 15.986 15.026 1.00 26.97 C ANISOU 926 C SER A 105 2413 4240 3592 -127 877 68 C ATOM 927 O SER A 105 26.048 14.851 15.531 1.00 24.29 O ANISOU 927 O SER A 105 2058 3882 3288 -27 831 -1 O ATOM 928 CB SER A 105 27.610 16.696 13.136 1.00 28.12 C ANISOU 928 CB SER A 105 2372 4640 3671 -189 1067 160 C ATOM 929 OG SER A 105 27.570 15.391 12.593 1.00 39.28 O ANISOU 929 OG SER A 105 3759 6113 5054 -32 1106 68 O ATOM 930 N THR A 106 24.966 16.714 14.839 1.00 21.72 N ANISOU 930 N THR A 106 1890 3483 2879 -169 869 92 N ATOM 931 CA THR A 106 23.649 16.209 15.213 1.00 19.90 C ANISOU 931 CA THR A 106 1789 3139 2632 -102 811 35 C ATOM 932 C THR A 106 22.648 16.401 14.081 1.00 23.89 C ANISOU 932 C THR A 106 2390 3640 3047 -71 860 39 C ATOM 933 O THR A 106 22.848 17.247 13.204 1.00 23.00 O ANISOU 933 O THR A 106 2274 3581 2885 -128 922 106 O ATOM 934 CB THR A 106 23.134 16.924 16.488 1.00 26.25 C ANISOU 934 CB THR A 106 2677 3815 3482 -182 724 51 C ATOM 935 OG1 THR A 106 22.917 18.303 16.169 1.00 25.65 O ANISOU 935 OG1 THR A 106 2657 3701 3386 -283 746 123 O ATOM 936 CG2 THR A 106 24.093 16.803 17.697 1.00 24.35 C ANISOU 936 CG2 THR A 106 2354 3579 3320 -226 659 51 C ATOM 937 N THR A 107 21.558 15.616 14.115 1.00 18.66 N ANISOU 937 N THR A 107 1812 2916 2362 13 824 -27 N ATOM 938 CA THR A 107 20.428 15.730 13.208 1.00 18.10 C ANISOU 938 CA THR A 107 1837 2828 2211 45 842 -31 C ATOM 939 C THR A 107 19.200 15.600 14.093 1.00 20.70 C ANISOU 939 C THR A 107 2265 3031 2570 57 762 -61 C ATOM 940 O THR A 107 19.286 15.013 15.168 1.00 19.55 O ANISOU 940 O THR A 107 2106 2835 2486 70 708 -99 O ATOM 941 CB THR A 107 20.420 14.685 12.066 1.00 26.04 C ANISOU 941 CB THR A 107 2824 3924 3145 146 892 -96 C ATOM 942 OG1 THR A 107 20.174 13.407 12.644 1.00 28.30 O ANISOU 942 OG1 THR A 107 3114 4162 3476 229 841 -186 O ATOM 943 CG2 THR A 107 21.701 14.694 11.180 1.00 26.08 C ANISOU 943 CG2 THR A 107 2717 4079 3113 149 989 -78 C ATOM 944 N GLY A 108 18.080 16.127 13.650 1.00 17.13 N ANISOU 944 N GLY A 108 1902 2535 2072 54 755 -40 N ATOM 945 CA GLY A 108 16.831 16.031 14.410 1.00 16.47 C ANISOU 945 CA GLY A 108 1899 2346 2013 70 691 -68 C ATOM 946 C GLY A 108 15.704 15.989 13.403 1.00 21.50 C ANISOU 946 C GLY A 108 2598 2991 2579 114 695 -72 C ATOM 947 O GLY A 108 15.843 16.562 12.320 1.00 22.25 O ANISOU 947 O GLY A 108 2698 3147 2610 103 740 -23 O ATOM 948 N PHE A 109 14.610 15.310 13.731 1.00 17.28 N ANISOU 948 N PHE A 109 2107 2405 2053 159 647 -125 N ATOM 949 CA PHE A 109 13.507 15.120 12.785 1.00 17.73 C ANISOU 949 CA PHE A 109 2212 2479 2047 201 636 -138 C ATOM 950 C PHE A 109 12.187 14.953 13.514 1.00 17.66 C ANISOU 950 C PHE A 109 2247 2389 2074 213 578 -161 C ATOM 951 O PHE A 109 12.141 14.464 14.637 1.00 14.19 O ANISOU 951 O PHE A 109 1801 1895 1695 207 550 -192 O ATOM 952 CB PHE A 109 13.762 13.887 11.880 1.00 20.59 C ANISOU 952 CB PHE A 109 2550 2917 2355 264 652 -210 C ATOM 953 CG PHE A 109 14.531 12.787 12.583 1.00 23.20 C ANISOU 953 CG PHE A 109 2832 3236 2746 292 645 -274 C ATOM 954 CD1 PHE A 109 13.871 11.801 13.284 1.00 25.67 C ANISOU 954 CD1 PHE A 109 3168 3480 3107 318 587 -331 C ATOM 955 CD2 PHE A 109 15.925 12.769 12.567 1.00 28.62 C ANISOU 955 CD2 PHE A 109 3445 3982 3447 289 692 -266 C ATOM 956 CE1 PHE A 109 14.580 10.808 13.957 1.00 27.72 C ANISOU 956 CE1 PHE A 109 3390 3716 3426 347 572 -376 C ATOM 957 CE2 PHE A 109 16.636 11.788 13.258 1.00 31.98 C ANISOU 957 CE2 PHE A 109 3821 4393 3937 325 675 -316 C ATOM 958 CZ PHE A 109 15.957 10.808 13.942 1.00 28.96 C ANISOU 958 CZ PHE A 109 3474 3929 3600 356 613 -369 C ATOM 959 N LEU A 110 11.108 15.363 12.849 1.00 14.06 N ANISOU 959 N LEU A 110 1832 1934 1577 230 561 -138 N ATOM 960 CA LEU A 110 9.767 15.244 13.368 1.00 14.01 C ANISOU 960 CA LEU A 110 1852 1872 1601 245 513 -156 C ATOM 961 C LEU A 110 8.836 15.134 12.180 1.00 17.06 C ANISOU 961 C LEU A 110 2257 2306 1918 280 489 -155 C ATOM 962 O LEU A 110 8.871 15.987 11.287 1.00 17.19 O ANISOU 962 O LEU A 110 2293 2360 1880 280 505 -93 O ATOM 963 CB LEU A 110 9.401 16.454 14.282 1.00 12.93 C ANISOU 963 CB LEU A 110 1739 1656 1516 215 510 -106 C ATOM 964 CG LEU A 110 7.917 16.612 14.679 1.00 15.75 C ANISOU 964 CG LEU A 110 2115 1970 1898 241 474 -111 C ATOM 965 CD1 LEU A 110 7.420 15.417 15.553 1.00 14.84 C ANISOU 965 CD1 LEU A 110 1979 1840 1819 244 448 -177 C ATOM 966 CD2 LEU A 110 7.715 17.917 15.462 1.00 18.22 C ANISOU 966 CD2 LEU A 110 2458 2207 2258 224 485 -70 C ATOM 967 N GLN A 111 7.993 14.104 12.182 1.00 13.04 N ANISOU 967 N GLN A 111 1745 1797 1413 304 445 -216 N ATOM 968 CA GLN A 111 7.053 13.917 11.090 1.00 15.28 C ANISOU 968 CA GLN A 111 2043 2132 1632 331 406 -224 C ATOM 969 C GLN A 111 5.848 13.129 11.513 1.00 18.33 C ANISOU 969 C GLN A 111 2419 2489 2058 335 348 -271 C ATOM 970 O GLN A 111 5.864 12.437 12.548 1.00 16.57 O ANISOU 970 O GLN A 111 2182 2213 1902 318 343 -309 O ATOM 971 CB GLN A 111 7.735 13.240 9.877 1.00 17.12 C ANISOU 971 CB GLN A 111 2282 2449 1774 352 424 -267 C ATOM 972 CG GLN A 111 8.597 12.030 10.222 1.00 23.05 C ANISOU 972 CG GLN A 111 3015 3191 2553 362 440 -350 C ATOM 973 CD GLN A 111 9.363 11.536 9.002 1.00 39.84 C ANISOU 973 CD GLN A 111 5146 5408 4584 394 475 -396 C ATOM 974 OE1 GLN A 111 9.842 12.309 8.170 1.00 27.77 O ANISOU 974 OE1 GLN A 111 3620 3953 2977 392 520 -343 O ATOM 975 NE2 GLN A 111 9.539 10.234 8.903 1.00 26.89 N ANISOU 975 NE2 GLN A 111 3507 3760 2950 425 460 -496 N ATOM 976 N TYR A 112 4.798 13.250 10.688 1.00 15.56 N ANISOU 976 N TYR A 112 2071 2179 1663 352 301 -261 N ATOM 977 CA TYR A 112 3.505 12.604 10.856 1.00 16.18 C ANISOU 977 CA TYR A 112 2126 2249 1770 348 238 -295 C ATOM 978 C TYR A 112 3.099 11.862 9.614 1.00 19.87 C ANISOU 978 C TYR A 112 2606 2786 2159 358 184 -344 C ATOM 979 O TYR A 112 3.424 12.264 8.492 1.00 19.40 O ANISOU 979 O TYR A 112 2573 2794 2003 378 189 -323 O ATOM 980 CB TYR A 112 2.410 13.628 11.181 1.00 17.36 C ANISOU 980 CB TYR A 112 2253 2386 1958 362 219 -229 C ATOM 981 CG TYR A 112 2.512 14.218 12.572 1.00 17.26 C ANISOU 981 CG TYR A 112 2230 2299 2029 352 263 -205 C ATOM 982 CD1 TYR A 112 3.353 15.300 12.833 1.00 17.71 C ANISOU 982 CD1 TYR A 112 2317 2322 2092 354 313 -154 C ATOM 983 CD2 TYR A 112 1.715 13.740 13.616 1.00 18.27 C ANISOU 983 CD2 TYR A 112 2321 2395 2225 335 252 -231 C ATOM 984 CE1 TYR A 112 3.407 15.889 14.106 1.00 15.24 C ANISOU 984 CE1 TYR A 112 2004 1940 1847 343 347 -143 C ATOM 985 CE2 TYR A 112 1.734 14.345 14.879 1.00 18.90 C ANISOU 985 CE2 TYR A 112 2398 2419 2363 329 295 -213 C ATOM 986 CZ TYR A 112 2.606 15.397 15.124 1.00 20.93 C ANISOU 986 CZ TYR A 112 2693 2639 2621 335 339 -176 C ATOM 987 OH TYR A 112 2.655 15.985 16.362 1.00 24.78 O ANISOU 987 OH TYR A 112 3188 3069 3157 326 376 -173 O ATOM 988 N ALA A 113 2.365 10.789 9.820 1.00 15.77 N ANISOU 988 N ALA A 113 2069 2249 1673 336 131 -408 N ATOM 989 CA ALA A 113 1.782 10.003 8.737 1.00 16.73 C ANISOU 989 CA ALA A 113 2203 2426 1728 333 61 -468 C ATOM 990 C ALA A 113 0.302 9.788 8.990 1.00 19.05 C ANISOU 990 C ALA A 113 2447 2718 2072 305 -13 -464 C ATOM 991 O ALA A 113 -0.112 9.679 10.143 1.00 19.01 O ANISOU 991 O ALA A 113 2403 2656 2163 279 -2 -450 O ATOM 992 CB ALA A 113 2.471 8.654 8.615 1.00 17.31 C ANISOU 992 CB ALA A 113 2310 2472 1797 324 60 -572 C ATOM 993 N TYR A 114 -0.484 9.705 7.909 1.00 15.69 N ANISOU 993 N TYR A 114 2018 2366 1577 306 -88 -476 N ATOM 994 CA TYR A 114 -1.901 9.351 7.969 1.00 16.28 C ANISOU 994 CA TYR A 114 2033 2458 1695 272 -172 -482 C ATOM 995 C TYR A 114 -2.081 8.153 7.063 1.00 21.04 C ANISOU 995 C TYR A 114 2669 3088 2238 237 -249 -582 C ATOM 996 O TYR A 114 -1.624 8.186 5.919 1.00 20.97 O ANISOU 996 O TYR A 114 2715 3142 2112 264 -262 -611 O ATOM 997 CB TYR A 114 -2.816 10.524 7.561 1.00 16.71 C ANISOU 997 CB TYR A 114 2040 2579 1731 308 -209 -392 C ATOM 998 CG TYR A 114 -4.287 10.154 7.526 1.00 18.68 C ANISOU 998 CG TYR A 114 2208 2867 2024 275 -302 -397 C ATOM 999 CD1 TYR A 114 -5.011 9.982 8.703 1.00 20.93 C ANISOU 999 CD1 TYR A 114 2416 3111 2427 244 -288 -384 C ATOM 1000 CD2 TYR A 114 -4.958 9.987 6.315 1.00 20.60 C ANISOU 1000 CD2 TYR A 114 2445 3199 2184 271 -404 -411 C ATOM 1001 CE1 TYR A 114 -6.361 9.648 8.680 1.00 22.58 C ANISOU 1001 CE1 TYR A 114 2531 3367 2681 207 -367 -383 C ATOM 1002 CE2 TYR A 114 -6.313 9.654 6.279 1.00 22.36 C ANISOU 1002 CE2 TYR A 114 2578 3466 2451 233 -497 -413 C ATOM 1003 CZ TYR A 114 -7.016 9.508 7.469 1.00 25.79 C ANISOU 1003 CZ TYR A 114 2923 3861 3016 202 -475 -396 C ATOM 1004 OH TYR A 114 -8.350 9.193 7.479 1.00 24.82 O ANISOU 1004 OH TYR A 114 2693 3791 2946 159 -559 -392 O ATOM 1005 N ASP A 115 -2.691 7.071 7.573 1.00 20.13 N ANISOU 1005 N ASP A 115 2528 2922 2199 174 -297 -639 N ATOM 1006 CA ASP A 115 -2.885 5.809 6.827 1.00 20.58 C ANISOU 1006 CA ASP A 115 2626 2976 2219 129 -378 -750 C ATOM 1007 C ASP A 115 -1.599 5.289 6.142 1.00 26.17 C ANISOU 1007 C ASP A 115 3431 3671 2841 168 -341 -836 C ATOM 1008 O ASP A 115 -1.646 4.851 4.996 1.00 28.75 O ANISOU 1008 O ASP A 115 3807 4051 3066 169 -398 -913 O ATOM 1009 CB ASP A 115 -4.022 5.947 5.798 1.00 23.61 C ANISOU 1009 CB ASP A 115 2976 3460 2535 110 -488 -750 C ATOM 1010 CG ASP A 115 -5.389 5.853 6.424 1.00 29.14 C ANISOU 1010 CG ASP A 115 3571 4163 3337 49 -549 -710 C ATOM 1011 OD1 ASP A 115 -5.486 5.351 7.577 1.00 28.04 O ANISOU 1011 OD1 ASP A 115 3401 3941 3312 3 -515 -707 O ATOM 1012 OD2 ASP A 115 -6.352 6.306 5.792 1.00 32.11 O ANISOU 1012 OD2 ASP A 115 3889 4631 3679 49 -628 -675 O ATOM 1013 N GLY A 116 -0.486 5.332 6.870 1.00 23.21 N ANISOU 1013 N GLY A 116 3079 3232 2508 199 -247 -826 N ATOM 1014 CA GLY A 116 0.805 4.803 6.444 1.00 23.60 C ANISOU 1014 CA GLY A 116 3199 3264 2505 244 -196 -904 C ATOM 1015 C GLY A 116 1.620 5.596 5.450 1.00 27.14 C ANISOU 1015 C GLY A 116 3679 3812 2823 306 -141 -888 C ATOM 1016 O GLY A 116 2.654 5.106 5.000 1.00 25.93 O ANISOU 1016 O GLY A 116 3574 3661 2617 346 -95 -963 O ATOM 1017 N GLN A 117 1.195 6.839 5.135 1.00 22.94 N ANISOU 1017 N GLN A 117 3116 3359 2240 317 -139 -785 N ATOM 1018 CA GLN A 117 1.879 7.719 4.188 1.00 22.80 C ANISOU 1018 CA GLN A 117 3128 3439 2094 362 -89 -742 C ATOM 1019 C GLN A 117 2.278 8.998 4.843 1.00 22.63 C ANISOU 1019 C GLN A 117 3075 3407 2118 379 -15 -617 C ATOM 1020 O GLN A 117 1.487 9.535 5.609 1.00 18.94 O ANISOU 1020 O GLN A 117 2559 2900 1737 362 -38 -547 O ATOM 1021 CB GLN A 117 0.904 8.080 3.034 1.00 25.42 C ANISOU 1021 CB GLN A 117 3469 3877 2312 356 -177 -722 C ATOM 1022 CG GLN A 117 0.678 7.015 2.014 1.00 54.52 C ANISOU 1022 CG GLN A 117 7208 7608 5899 343 -248 -850 C ATOM 1023 CD GLN A 117 -0.163 7.577 0.896 1.00 82.58 C ANISOU 1023 CD GLN A 117 10768 11282 9325 340 -333 -807 C ATOM 1024 OE1 GLN A 117 -1.361 7.277 0.781 1.00 82.04 O ANISOU 1024 OE1 GLN A 117 10668 11225 9279 299 -445 -821 O ATOM 1025 NE2 GLN A 117 0.433 8.444 0.080 1.00 71.36 N ANISOU 1025 NE2 GLN A 117 9382 9958 7772 380 -283 -741 N ATOM 1026 N ASP A 118 3.437 9.552 4.463 1.00 20.76 N ANISOU 1026 N ASP A 118 2862 3212 1814 409 70 -586 N ATOM 1027 CA ASP A 118 3.918 10.861 4.903 1.00 20.41 C ANISOU 1027 CA ASP A 118 2799 3160 1797 416 136 -465 C ATOM 1028 C ASP A 118 2.803 11.882 4.797 1.00 22.21 C ANISOU 1028 C ASP A 118 3008 3403 2028 415 81 -364 C ATOM 1029 O ASP A 118 2.113 11.930 3.773 1.00 21.95 O ANISOU 1029 O ASP A 118 2992 3449 1899 422 14 -359 O ATOM 1030 CB ASP A 118 5.091 11.316 4.024 1.00 23.41 C ANISOU 1030 CB ASP A 118 3210 3624 2061 437 215 -441 C ATOM 1031 CG ASP A 118 6.419 10.655 4.307 1.00 30.54 C ANISOU 1031 CG ASP A 118 4109 4512 2983 451 296 -510 C ATOM 1032 OD1 ASP A 118 6.527 9.944 5.336 1.00 30.51 O ANISOU 1032 OD1 ASP A 118 4082 4415 3095 446 293 -562 O ATOM 1033 OD2 ASP A 118 7.363 10.866 3.514 1.00 36.90 O ANISOU 1033 OD2 ASP A 118 4928 5404 3688 469 366 -505 O ATOM 1034 N PHE A 119 2.589 12.648 5.852 1.00 16.73 N ANISOU 1034 N PHE A 119 2280 2635 1443 411 101 -293 N ATOM 1035 CA PHE A 119 1.496 13.626 5.880 1.00 17.78 C ANISOU 1035 CA PHE A 119 2387 2767 1602 426 52 -202 C ATOM 1036 C PHE A 119 2.082 15.026 6.099 1.00 20.34 C ANISOU 1036 C PHE A 119 2729 3059 1941 441 114 -92 C ATOM 1037 O PHE A 119 1.833 15.918 5.312 1.00 19.20 O ANISOU 1037 O PHE A 119 2605 2956 1733 462 91 -5 O ATOM 1038 CB PHE A 119 0.492 13.232 7.001 1.00 18.62 C ANISOU 1038 CB PHE A 119 2434 2808 1835 412 16 -230 C ATOM 1039 CG PHE A 119 -0.697 14.146 7.147 1.00 19.09 C ANISOU 1039 CG PHE A 119 2448 2868 1939 440 -30 -151 C ATOM 1040 CD1 PHE A 119 -1.736 14.125 6.211 1.00 22.79 C ANISOU 1040 CD1 PHE A 119 2893 3413 2352 454 -124 -135 C ATOM 1041 CD2 PHE A 119 -0.791 15.021 8.223 1.00 20.06 C ANISOU 1041 CD2 PHE A 119 2548 2915 2161 457 16 -97 C ATOM 1042 CE1 PHE A 119 -2.840 14.979 6.345 1.00 23.44 C ANISOU 1042 CE1 PHE A 119 2921 3500 2487 494 -170 -59 C ATOM 1043 CE2 PHE A 119 -1.907 15.872 8.364 1.00 22.95 C ANISOU 1043 CE2 PHE A 119 2866 3277 2576 501 -22 -32 C ATOM 1044 CZ PHE A 119 -2.920 15.840 7.422 1.00 21.69 C ANISOU 1044 CZ PHE A 119 2674 3196 2370 522 -114 -10 C ATOM 1045 N LEU A 120 2.874 15.197 7.159 1.00 16.77 N ANISOU 1045 N LEU A 120 2271 2529 1571 424 184 -94 N ATOM 1046 CA LEU A 120 3.517 16.468 7.500 1.00 16.80 C ANISOU 1046 CA LEU A 120 2295 2484 1603 423 241 -2 C ATOM 1047 C LEU A 120 4.932 16.213 7.975 1.00 19.95 C ANISOU 1047 C LEU A 120 2699 2863 2017 391 319 -33 C ATOM 1048 O LEU A 120 5.151 15.349 8.829 1.00 18.64 O ANISOU 1048 O LEU A 120 2509 2660 1913 377 329 -109 O ATOM 1049 CB LEU A 120 2.713 17.211 8.590 1.00 16.63 C ANISOU 1049 CB LEU A 120 2249 2372 1696 438 230 34 C ATOM 1050 CG LEU A 120 1.419 17.914 8.133 1.00 21.55 C ANISOU 1050 CG LEU A 120 2859 3008 2321 485 162 98 C ATOM 1051 CD1 LEU A 120 0.586 18.274 9.323 1.00 20.83 C ANISOU 1051 CD1 LEU A 120 2727 2840 2348 508 160 94 C ATOM 1052 CD2 LEU A 120 1.717 19.159 7.314 1.00 24.02 C ANISOU 1052 CD2 LEU A 120 3222 3324 2581 503 166 213 C ATOM 1053 N ILE A 121 5.891 16.937 7.415 1.00 17.28 N ANISOU 1053 N ILE A 121 2387 2554 1623 375 371 32 N ATOM 1054 CA ILE A 121 7.311 16.775 7.758 1.00 17.12 C ANISOU 1054 CA ILE A 121 2356 2534 1614 343 446 14 C ATOM 1055 C ILE A 121 7.860 18.123 8.224 1.00 20.04 C ANISOU 1055 C ILE A 121 2740 2840 2034 308 486 111 C ATOM 1056 O ILE A 121 7.749 19.135 7.507 1.00 19.58 O ANISOU 1056 O ILE A 121 2717 2793 1929 304 485 210 O ATOM 1057 CB ILE A 121 8.118 16.196 6.556 1.00 21.24 C ANISOU 1057 CB ILE A 121 2883 3174 2014 348 485 -15 C ATOM 1058 CG1 ILE A 121 7.506 14.863 6.065 1.00 22.23 C ANISOU 1058 CG1 ILE A 121 3009 3347 2090 381 435 -125 C ATOM 1059 CG2 ILE A 121 9.639 16.045 6.920 1.00 22.55 C ANISOU 1059 CG2 ILE A 121 3015 3351 2201 320 568 -30 C ATOM 1060 CD1 ILE A 121 7.970 14.418 4.646 1.00 35.34 C ANISOU 1060 CD1 ILE A 121 4694 5135 3599 399 459 -157 C ATOM 1061 N PHE A 122 8.416 18.146 9.432 1.00 16.20 N ANISOU 1061 N PHE A 122 2233 2281 1641 280 511 86 N ATOM 1062 CA PHE A 122 8.957 19.395 10.004 1.00 16.50 C ANISOU 1062 CA PHE A 122 2290 2244 1736 236 540 162 C ATOM 1063 C PHE A 122 10.338 19.717 9.453 1.00 21.81 C ANISOU 1063 C PHE A 122 2950 2972 2363 185 604 210 C ATOM 1064 O PHE A 122 11.186 18.829 9.322 1.00 21.22 O ANISOU 1064 O PHE A 122 2832 2970 2262 181 639 154 O ATOM 1065 CB PHE A 122 9.030 19.304 11.562 1.00 16.71 C ANISOU 1065 CB PHE A 122 2301 2179 1869 218 537 111 C ATOM 1066 CG PHE A 122 9.422 20.581 12.298 1.00 16.73 C ANISOU 1066 CG PHE A 122 2334 2086 1937 172 552 167 C ATOM 1067 CD1 PHE A 122 8.726 21.771 12.088 1.00 19.96 C ANISOU 1067 CD1 PHE A 122 2794 2427 2362 186 533 240 C ATOM 1068 CD2 PHE A 122 10.453 20.578 13.235 1.00 17.19 C ANISOU 1068 CD2 PHE A 122 2372 2115 2046 117 577 143 C ATOM 1069 CE1 PHE A 122 9.071 22.946 12.789 1.00 20.78 C ANISOU 1069 CE1 PHE A 122 2939 2423 2534 144 543 280 C ATOM 1070 CE2 PHE A 122 10.773 21.744 13.968 1.00 19.13 C ANISOU 1070 CE2 PHE A 122 2654 2264 2352 66 580 181 C ATOM 1071 CZ PHE A 122 10.087 22.921 13.734 1.00 17.62 C ANISOU 1071 CZ PHE A 122 2523 1994 2178 79 566 245 C ATOM 1072 N ASN A 123 10.568 20.986 9.144 1.00 18.62 N ANISOU 1072 N ASN A 123 2583 2535 1957 145 619 317 N ATOM 1073 CA ASN A 123 11.892 21.453 8.753 1.00 20.51 C ANISOU 1073 CA ASN A 123 2804 2820 2168 76 684 379 C ATOM 1074 C ASN A 123 12.325 22.423 9.864 1.00 23.25 C ANISOU 1074 C ASN A 123 3165 3045 2625 13 684 412 C ATOM 1075 O ASN A 123 11.738 23.494 9.980 1.00 22.04 O ANISOU 1075 O ASN A 123 3073 2792 2509 7 655 478 O ATOM 1076 CB ASN A 123 11.895 22.103 7.354 1.00 23.48 C ANISOU 1076 CB ASN A 123 3218 3266 2438 65 703 489 C ATOM 1077 CG ASN A 123 13.268 22.534 6.884 1.00 35.19 C ANISOU 1077 CG ASN A 123 4671 4816 3883 -16 781 561 C ATOM 1078 OD1 ASN A 123 14.148 22.912 7.668 1.00 25.57 O ANISOU 1078 OD1 ASN A 123 3421 3549 2746 -83 808 570 O ATOM 1079 ND2 ASN A 123 13.475 22.519 5.584 1.00 27.62 N ANISOU 1079 ND2 ASN A 123 3720 3979 2795 -17 819 618 N ATOM 1080 N LYS A 124 13.261 22.012 10.730 1.00 20.72 N ANISOU 1080 N LYS A 124 2790 2723 2358 -27 706 358 N ATOM 1081 CA LYS A 124 13.657 22.832 11.889 1.00 21.57 C ANISOU 1081 CA LYS A 124 2912 2718 2564 -92 694 369 C ATOM 1082 C LYS A 124 14.621 23.972 11.517 1.00 29.36 C ANISOU 1082 C LYS A 124 3907 3691 3557 -191 729 476 C ATOM 1083 O LYS A 124 14.928 24.787 12.386 1.00 29.11 O ANISOU 1083 O LYS A 124 3902 3554 3606 -255 712 489 O ATOM 1084 CB LYS A 124 14.264 21.968 13.024 1.00 22.44 C ANISOU 1084 CB LYS A 124 2964 2836 2728 -101 688 275 C ATOM 1085 CG LYS A 124 15.564 21.240 12.674 1.00 21.17 C ANISOU 1085 CG LYS A 124 2711 2793 2539 -126 736 262 C ATOM 1086 CD LYS A 124 16.025 20.359 13.866 1.00 19.30 C ANISOU 1086 CD LYS A 124 2421 2549 2361 -120 712 176 C ATOM 1087 CE LYS A 124 17.330 19.642 13.578 1.00 21.18 C ANISOU 1087 CE LYS A 124 2557 2901 2588 -129 755 162 C ATOM 1088 NZ LYS A 124 18.483 20.569 13.517 1.00 23.43 N ANISOU 1088 NZ LYS A 124 2798 3209 2897 -230 789 237 N ATOM 1089 N ASP A 125 15.094 24.030 10.259 1.00 27.59 N ANISOU 1089 N ASP A 125 3664 3572 3247 -210 778 550 N ATOM 1090 CA ASP A 125 15.996 25.090 9.840 1.00 29.63 C ANISOU 1090 CA ASP A 125 3926 3826 3507 -316 818 666 C ATOM 1091 C ASP A 125 15.213 26.250 9.249 1.00 33.78 C ANISOU 1091 C ASP A 125 4553 4261 4021 -319 791 777 C ATOM 1092 O ASP A 125 15.544 27.398 9.545 1.00 33.99 O ANISOU 1092 O ASP A 125 4625 4177 4113 -403 783 855 O ATOM 1093 CB ASP A 125 17.069 24.563 8.871 1.00 32.64 C ANISOU 1093 CB ASP A 125 4221 4382 3800 -345 898 694 C ATOM 1094 CG ASP A 125 17.978 23.524 9.525 1.00 44.91 C ANISOU 1094 CG ASP A 125 5666 6011 5388 -340 922 593 C ATOM 1095 OD1 ASP A 125 18.124 23.553 10.783 1.00 43.56 O ANISOU 1095 OD1 ASP A 125 5485 5749 5316 -363 878 539 O ATOM 1096 OD2 ASP A 125 18.533 22.678 8.793 1.00 54.15 O ANISOU 1096 OD2 ASP A 125 6763 7329 6483 -307 981 565 O ATOM 1097 N THR A 126 14.145 25.969 8.472 1.00 29.37 N ANISOU 1097 N THR A 126 4035 3737 3388 -228 766 784 N ATOM 1098 CA THR A 126 13.293 27.034 7.905 1.00 29.35 C ANISOU 1098 CA THR A 126 4127 3647 3377 -211 727 895 C ATOM 1099 C THR A 126 12.084 27.253 8.832 1.00 31.90 C ANISOU 1099 C THR A 126 4500 3828 3792 -134 655 833 C ATOM 1100 O THR A 126 11.350 28.211 8.633 1.00 32.45 O ANISOU 1100 O THR A 126 4646 3792 3890 -108 614 911 O ATOM 1101 CB THR A 126 12.866 26.718 6.446 1.00 36.61 C ANISOU 1101 CB THR A 126 5059 4698 4153 -163 734 955 C ATOM 1102 OG1 THR A 126 11.991 25.587 6.437 1.00 29.57 O ANISOU 1102 OG1 THR A 126 4142 3868 3224 -60 700 842 O ATOM 1103 CG2 THR A 126 14.066 26.485 5.506 1.00 33.81 C ANISOU 1103 CG2 THR A 126 4652 4502 3691 -235 821 1010 C ATOM 1104 N LEU A 127 11.895 26.383 9.858 1.00 27.15 N ANISOU 1104 N LEU A 127 3853 3224 3239 -95 643 697 N ATOM 1105 CA LEU A 127 10.811 26.477 10.874 1.00 26.90 C ANISOU 1105 CA LEU A 127 3852 3078 3289 -26 592 624 C ATOM 1106 C LEU A 127 9.458 26.428 10.177 1.00 30.87 C ANISOU 1106 C LEU A 127 4381 3596 3753 75 547 648 C ATOM 1107 O LEU A 127 8.661 27.360 10.271 1.00 29.60 O ANISOU 1107 O LEU A 127 4280 3323 3645 116 508 695 O ATOM 1108 CB LEU A 127 10.946 27.748 11.758 1.00 27.68 C ANISOU 1108 CB LEU A 127 4019 3004 3495 -74 577 650 C ATOM 1109 CG LEU A 127 12.130 27.745 12.711 1.00 32.75 C ANISOU 1109 CG LEU A 127 4631 3624 4187 -173 601 603 C ATOM 1110 CD1 LEU A 127 12.461 29.144 13.168 1.00 35.98 C ANISOU 1110 CD1 LEU A 127 5119 3872 4680 -248 586 657 C ATOM 1111 CD2 LEU A 127 11.898 26.803 13.878 1.00 26.81 C ANISOU 1111 CD2 LEU A 127 3836 2886 3463 -135 589 468 C ATOM 1112 N SER A 128 9.251 25.363 9.394 1.00 27.26 N ANISOU 1112 N SER A 128 3877 3278 3201 114 548 617 N ATOM 1113 CA SER A 128 8.036 25.211 8.614 1.00 27.31 C ANISOU 1113 CA SER A 128 3897 3325 3156 198 496 639 C ATOM 1114 C SER A 128 7.655 23.767 8.512 1.00 28.64 C ANISOU 1114 C SER A 128 4006 3604 3273 241 486 532 C ATOM 1115 O SER A 128 8.470 22.880 8.764 1.00 26.44 O ANISOU 1115 O SER A 128 3682 3386 2979 208 526 459 O ATOM 1116 CB SER A 128 8.222 25.807 7.213 1.00 31.49 C ANISOU 1116 CB SER A 128 4467 3912 3585 180 498 772 C ATOM 1117 OG SER A 128 9.338 25.228 6.562 1.00 37.42 O ANISOU 1117 OG SER A 128 5184 4791 4242 121 560 773 O ATOM 1118 N TRP A 129 6.411 23.531 8.113 1.00 24.43 N ANISOU 1118 N TRP A 129 3470 3095 2718 314 426 525 N ATOM 1119 CA TRP A 129 5.905 22.189 7.919 1.00 22.50 C ANISOU 1119 CA TRP A 129 3177 2947 2427 349 401 429 C ATOM 1120 C TRP A 129 5.745 21.920 6.443 1.00 27.54 C ANISOU 1120 C TRP A 129 3827 3707 2929 364 377 471 C ATOM 1121 O TRP A 129 5.203 22.766 5.715 1.00 28.40 O ANISOU 1121 O TRP A 129 3976 3813 3004 389 337 575 O ATOM 1122 CB TRP A 129 4.577 22.047 8.647 1.00 20.49 C ANISOU 1122 CB TRP A 129 2895 2639 2250 410 347 380 C ATOM 1123 CG TRP A 129 4.771 21.870 10.119 1.00 20.91 C ANISOU 1123 CG TRP A 129 2928 2611 2405 391 378 304 C ATOM 1124 CD1 TRP A 129 4.714 22.833 11.089 1.00 23.37 C ANISOU 1124 CD1 TRP A 129 3266 2803 2809 392 391 320 C ATOM 1125 CD2 TRP A 129 5.090 20.643 10.783 1.00 19.51 C ANISOU 1125 CD2 TRP A 129 2707 2465 2239 369 395 200 C ATOM 1126 NE1 TRP A 129 4.905 22.264 12.325 1.00 21.19 N ANISOU 1126 NE1 TRP A 129 2963 2498 2590 371 415 230 N ATOM 1127 CE2 TRP A 129 5.172 20.924 12.163 1.00 22.51 C ANISOU 1127 CE2 TRP A 129 3088 2755 2711 354 417 165 C ATOM 1128 CE3 TRP A 129 5.239 19.312 10.346 1.00 20.24 C ANISOU 1128 CE3 TRP A 129 2768 2650 2274 364 389 131 C ATOM 1129 CZ2 TRP A 129 5.444 19.931 13.108 1.00 21.20 C ANISOU 1129 CZ2 TRP A 129 2889 2593 2574 330 431 79 C ATOM 1130 CZ3 TRP A 129 5.526 18.331 11.278 1.00 20.79 C ANISOU 1130 CZ3 TRP A 129 2806 2706 2386 344 403 44 C ATOM 1131 CH2 TRP A 129 5.588 18.635 12.644 1.00 21.05 C ANISOU 1131 CH2 TRP A 129 2837 2655 2507 327 421 25 C ATOM 1132 N LEU A 130 6.210 20.760 5.985 1.00 24.08 N ANISOU 1132 N LEU A 130 3363 3376 2412 352 398 392 N ATOM 1133 CA LEU A 130 6.019 20.401 4.576 1.00 25.84 C ANISOU 1133 CA LEU A 130 3604 3727 2487 368 374 410 C ATOM 1134 C LEU A 130 4.772 19.527 4.479 1.00 27.56 C ANISOU 1134 C LEU A 130 3796 3975 2699 417 291 331 C ATOM 1135 O LEU A 130 4.718 18.482 5.123 1.00 24.74 O ANISOU 1135 O LEU A 130 3401 3609 2391 417 291 216 O ATOM 1136 CB LEU A 130 7.259 19.697 3.993 1.00 27.10 C ANISOU 1136 CB LEU A 130 3755 3992 2551 334 449 365 C ATOM 1137 CG LEU A 130 7.137 19.152 2.565 1.00 34.43 C ANISOU 1137 CG LEU A 130 4706 5067 3308 351 434 353 C ATOM 1138 CD1 LEU A 130 7.100 20.306 1.530 1.00 36.53 C ANISOU 1138 CD1 LEU A 130 5028 5379 3473 338 428 510 C ATOM 1139 CD2 LEU A 130 8.302 18.230 2.254 1.00 38.35 C ANISOU 1139 CD2 LEU A 130 5179 5655 3735 337 515 264 C ATOM 1140 N ALA A 131 3.745 20.006 3.742 1.00 25.43 N ANISOU 1140 N ALA A 131 3545 3735 2383 455 213 401 N ATOM 1141 CA ALA A 131 2.444 19.349 3.550 1.00 25.76 C ANISOU 1141 CA ALA A 131 3552 3815 2419 496 118 347 C ATOM 1142 C ALA A 131 2.429 18.574 2.225 1.00 32.65 C ANISOU 1142 C ALA A 131 4448 4831 3127 492 83 310 C ATOM 1143 O ALA A 131 2.837 19.118 1.195 1.00 32.42 O ANISOU 1143 O ALA A 131 4469 4874 2974 485 93 396 O ATOM 1144 CB ALA A 131 1.328 20.399 3.547 1.00 26.86 C ANISOU 1144 CB ALA A 131 3688 3905 2612 548 47 450 C ATOM 1145 N VAL A 132 1.886 17.354 2.238 1.00 29.78 N ANISOU 1145 N VAL A 132 4052 4505 2757 494 34 188 N ATOM 1146 CA VAL A 132 1.857 16.472 1.067 1.00 31.91 C ANISOU 1146 CA VAL A 132 4350 4902 2874 488 -5 120 C ATOM 1147 C VAL A 132 0.621 16.696 0.168 1.00 35.66 C ANISOU 1147 C VAL A 132 4826 5451 3271 513 -127 170 C ATOM 1148 O VAL A 132 0.674 16.396 -1.023 1.00 37.28 O ANISOU 1148 O VAL A 132 5076 5776 3313 509 -161 158 O ATOM 1149 CB VAL A 132 1.954 14.985 1.511 1.00 36.07 C ANISOU 1149 CB VAL A 132 4852 5416 3437 470 -2 -45 C ATOM 1150 CG1 VAL A 132 3.249 14.734 2.299 1.00 35.35 C ANISOU 1150 CG1 VAL A 132 4758 5265 3410 453 111 -89 C ATOM 1151 CG2 VAL A 132 0.720 14.556 2.324 1.00 35.19 C ANISOU 1151 CG2 VAL A 132 4678 5240 3451 470 -82 -87 C ATOM 1152 N ASP A 133 -0.496 17.151 0.740 1.00 29.34 N ANISOU 1152 N ASP A 133 3971 4591 2584 542 -196 217 N ATOM 1153 CA ASP A 133 -1.740 17.344 -0.014 1.00 28.39 C ANISOU 1153 CA ASP A 133 3830 4543 2413 572 -325 267 C ATOM 1154 C ASP A 133 -2.526 18.524 0.601 1.00 29.73 C ANISOU 1154 C ASP A 133 3956 4628 2712 626 -354 384 C ATOM 1155 O ASP A 133 -2.013 19.203 1.489 1.00 26.49 O ANISOU 1155 O ASP A 133 3550 4107 2406 634 -272 422 O ATOM 1156 CB ASP A 133 -2.566 16.031 -0.016 1.00 29.05 C ANISOU 1156 CB ASP A 133 3864 4671 2504 547 -408 132 C ATOM 1157 CG ASP A 133 -3.144 15.586 1.336 1.00 33.31 C ANISOU 1157 CG ASP A 133 4319 5112 3226 539 -401 70 C ATOM 1158 OD1 ASP A 133 -2.901 16.269 2.346 1.00 33.70 O ANISOU 1158 OD1 ASP A 133 4349 5060 3394 558 -329 117 O ATOM 1159 OD2 ASP A 133 -3.819 14.542 1.377 1.00 34.96 O ANISOU 1159 OD2 ASP A 133 4484 5347 3453 506 -468 -28 O ATOM 1160 N ASN A 134 -3.751 18.745 0.136 1.00 22.56 N ANISOU 1160 N ASN A 134 3394 3186 1991 497 -555 480 N ATOM 1161 CA ASN A 134 -4.623 19.838 0.568 1.00 23.80 C ANISOU 1161 CA ASN A 134 3548 3344 2149 687 -670 441 C ATOM 1162 C ASN A 134 -5.029 19.748 2.034 1.00 26.89 C ANISOU 1162 C ASN A 134 3786 3824 2605 753 -643 358 C ATOM 1163 O ASN A 134 -5.078 20.786 2.681 1.00 28.39 O ANISOU 1163 O ASN A 134 4016 3944 2826 865 -692 338 O ATOM 1164 CB ASN A 134 -5.875 19.899 -0.311 1.00 23.73 C ANISOU 1164 CB ASN A 134 3510 3434 2072 786 -785 429 C ATOM 1165 CG ASN A 134 -5.639 20.612 -1.621 1.00 47.13 C ANISOU 1165 CG ASN A 134 6675 6265 4967 794 -864 508 C ATOM 1166 OD1 ASN A 134 -4.704 21.417 -1.770 1.00 39.76 O ANISOU 1166 OD1 ASN A 134 5922 5151 4035 769 -858 558 O ATOM 1167 ND2 ASN A 134 -6.508 20.352 -2.595 1.00 36.28 N ANISOU 1167 ND2 ASN A 134 5281 4980 3523 826 -941 513 N ATOM 1168 N VAL A 135 -5.314 18.542 2.560 1.00 23.72 N ANISOU 1168 N VAL A 135 3224 3570 2220 678 -563 308 N ATOM 1169 CA VAL A 135 -5.697 18.354 3.975 1.00 22.68 C ANISOU 1169 CA VAL A 135 2954 3524 2142 717 -528 222 C ATOM 1170 C VAL A 135 -4.498 18.686 4.867 1.00 25.52 C ANISOU 1170 C VAL A 135 3376 3755 2565 669 -458 244 C ATOM 1171 O VAL A 135 -4.645 19.450 5.840 1.00 24.32 O ANISOU 1171 O VAL A 135 3206 3575 2457 760 -483 202 O ATOM 1172 CB VAL A 135 -6.290 16.949 4.262 1.00 25.51 C ANISOU 1172 CB VAL A 135 3148 4061 2482 634 -453 161 C ATOM 1173 CG1 VAL A 135 -6.444 16.712 5.774 1.00 24.60 C ANISOU 1173 CG1 VAL A 135 2923 4005 2420 641 -398 78 C ATOM 1174 CG2 VAL A 135 -7.638 16.788 3.542 1.00 26.17 C ANISOU 1174 CG2 VAL A 135 3148 4293 2502 706 -531 114 C ATOM 1175 N ALA A 136 -3.300 18.174 4.515 1.00 20.11 N ANISOU 1175 N ALA A 136 2766 2989 1885 528 -374 305 N ATOM 1176 CA ALA A 136 -2.090 18.494 5.277 1.00 20.46 C ANISOU 1176 CA ALA A 136 2871 2917 1986 478 -311 320 C ATOM 1177 C ALA A 136 -1.821 20.016 5.214 1.00 24.39 C ANISOU 1177 C ALA A 136 3508 3271 2489 573 -379 345 C ATOM 1178 O ALA A 136 -1.436 20.594 6.223 1.00 22.13 O ANISOU 1178 O ALA A 136 3225 2932 2251 606 -361 321 O ATOM 1179 CB ALA A 136 -0.901 17.705 4.745 1.00 20.46 C ANISOU 1179 CB ALA A 136 2925 2863 1987 318 -219 371 C ATOM 1180 N HIS A 137 -2.100 20.663 4.048 1.00 23.24 N ANISOU 1180 N HIS A 137 3480 3064 2286 621 -461 389 N ATOM 1181 CA HIS A 137 -1.929 22.116 3.897 1.00 24.99 C ANISOU 1181 CA HIS A 137 3859 3141 2494 716 -530 412 C ATOM 1182 C HIS A 137 -2.782 22.893 4.924 1.00 26.03 C ANISOU 1182 C HIS A 137 3921 3307 2660 877 -592 351 C ATOM 1183 O HIS A 137 -2.275 23.850 5.495 1.00 24.78 O ANISOU 1183 O HIS A 137 3849 3039 2528 915 -587 353 O ATOM 1184 CB HIS A 137 -2.251 22.579 2.471 1.00 28.46 C ANISOU 1184 CB HIS A 137 4438 3520 2854 748 -618 465 C ATOM 1185 CG HIS A 137 -1.971 24.031 2.262 1.00 34.72 C ANISOU 1185 CG HIS A 137 5426 4145 3620 831 -680 493 C ATOM 1186 ND1 HIS A 137 -0.680 24.497 2.100 1.00 37.34 N ANISOU 1186 ND1 HIS A 137 5919 4321 3948 727 -614 530 N ATOM 1187 CD2 HIS A 137 -2.829 25.077 2.211 1.00 39.49 C ANISOU 1187 CD2 HIS A 137 6088 4718 4197 1005 -798 483 C ATOM 1188 CE1 HIS A 137 -0.787 25.810 1.969 1.00 38.63 C ANISOU 1188 CE1 HIS A 137 6245 4359 4075 833 -686 543 C ATOM 1189 NE2 HIS A 137 -2.063 26.205 2.012 1.00 40.27 N ANISOU 1189 NE2 HIS A 137 6401 4630 4268 1008 -802 520 N ATOM 1190 N THR A 138 -4.050 22.478 5.166 1.00 22.84 N ANISOU 1190 N THR A 138 3362 3060 2256 962 -642 290 N ATOM 1191 CA THR A 138 -4.941 23.099 6.174 1.00 23.28 C ANISOU 1191 CA THR A 138 3325 3168 2351 1107 -695 214 C ATOM 1192 C THR A 138 -4.310 22.992 7.575 1.00 25.72 C ANISOU 1192 C THR A 138 3574 3467 2732 1051 -601 179 C ATOM 1193 O THR A 138 -4.279 23.987 8.313 1.00 24.03 O ANISOU 1193 O THR A 138 3395 3182 2554 1134 -621 159 O ATOM 1194 CB THR A 138 -6.335 22.436 6.125 1.00 34.87 C ANISOU 1194 CB THR A 138 4620 4828 3802 1170 -745 138 C ATOM 1195 OG1 THR A 138 -6.883 22.653 4.819 1.00 38.31 O ANISOU 1195 OG1 THR A 138 5123 5267 4168 1232 -843 172 O ATOM 1196 CG2 THR A 138 -7.301 23.001 7.162 1.00 32.54 C ANISOU 1196 CG2 THR A 138 4211 4602 3550 1309 -794 40 C ATOM 1197 N ILE A 139 -3.776 21.791 7.933 1.00 21.73 N ANISOU 1197 N ILE A 139 2987 3023 2245 909 -498 175 N ATOM 1198 CA ILE A 139 -3.133 21.569 9.236 1.00 20.26 C ANISOU 1198 CA ILE A 139 2749 2830 2120 847 -412 146 C ATOM 1199 C ILE A 139 -1.843 22.406 9.341 1.00 24.52 C ANISOU 1199 C ILE A 139 3436 3201 2680 812 -378 199 C ATOM 1200 O ILE A 139 -1.628 23.050 10.366 1.00 25.46 O ANISOU 1200 O ILE A 139 3552 3277 2843 847 -361 171 O ATOM 1201 CB ILE A 139 -2.861 20.053 9.496 1.00 21.77 C ANISOU 1201 CB ILE A 139 2838 3119 2314 711 -318 132 C ATOM 1202 CG1 ILE A 139 -4.133 19.164 9.282 1.00 21.73 C ANISOU 1202 CG1 ILE A 139 2698 3286 2272 726 -338 73 C ATOM 1203 CG2 ILE A 139 -2.239 19.841 10.876 1.00 20.50 C ANISOU 1203 CG2 ILE A 139 2632 2947 2210 659 -242 100 C ATOM 1204 CD1 ILE A 139 -5.468 19.565 10.076 1.00 31.37 C ANISOU 1204 CD1 ILE A 139 3798 4613 3509 848 -395 -30 C ATOM 1205 N LYS A 140 -0.981 22.368 8.303 1.00 22.17 N ANISOU 1205 N LYS A 140 3263 2813 2346 730 -359 267 N ATOM 1206 CA LYS A 140 0.269 23.159 8.223 1.00 22.60 C ANISOU 1206 CA LYS A 140 3471 2711 2406 679 -321 308 C ATOM 1207 C LYS A 140 -0.046 24.646 8.490 1.00 27.98 C ANISOU 1207 C LYS A 140 4248 3299 3083 810 -385 302 C ATOM 1208 O LYS A 140 0.676 25.277 9.277 1.00 27.07 O ANISOU 1208 O LYS A 140 4178 3107 3000 795 -339 292 O ATOM 1209 CB LYS A 140 0.951 22.970 6.840 1.00 23.51 C ANISOU 1209 CB LYS A 140 3713 2751 2468 583 -309 370 C ATOM 1210 CG LYS A 140 1.844 24.120 6.350 1.00 26.82 C ANISOU 1210 CG LYS A 140 4336 2998 2858 564 -307 406 C ATOM 1211 CD LYS A 140 2.066 24.063 4.828 1.00 28.26 C ANISOU 1211 CD LYS A 140 4653 3115 2971 499 -328 460 C ATOM 1212 CE LYS A 140 2.774 25.291 4.288 1.00 30.49 C ANISOU 1212 CE LYS A 140 5160 3221 3205 486 -334 487 C ATOM 1213 NZ LYS A 140 4.242 25.233 4.550 1.00 35.27 N ANISOU 1213 NZ LYS A 140 5813 3754 3835 340 -222 474 N ATOM 1214 N AGLN A 141 -1.136 25.182 7.872 0.50 25.47 N ANISOU 1214 N AGLN A 141 3958 2994 2726 939 -492 302 N ATOM 1215 N BGLN A 141 -1.127 25.195 7.886 0.50 26.09 N ANISOU 1215 N BGLN A 141 4038 3072 2806 940 -492 302 N ATOM 1216 CA AGLN A 141 -1.573 26.575 8.068 0.50 26.86 C ANISOU 1216 CA AGLN A 141 4228 3083 2895 1084 -566 294 C ATOM 1217 CA BGLN A 141 -1.495 26.602 8.111 0.50 27.68 C ANISOU 1217 CA BGLN A 141 4337 3180 3000 1079 -560 294 C ATOM 1218 C AGLN A 141 -1.820 26.860 9.557 0.50 32.08 C ANISOU 1218 C AGLN A 141 4777 3785 3626 1137 -539 229 C ATOM 1219 C BGLN A 141 -1.802 26.867 9.589 0.50 32.39 C ANISOU 1219 C BGLN A 141 4816 3824 3667 1136 -537 229 C ATOM 1220 O AGLN A 141 -1.341 27.873 10.061 0.50 33.59 O ANISOU 1220 O AGLN A 141 5065 3867 3830 1164 -522 232 O ATOM 1221 O BGLN A 141 -1.344 27.877 10.120 0.50 33.83 O ANISOU 1221 O BGLN A 141 5091 3899 3863 1165 -520 230 O ATOM 1222 CB AGLN A 141 -2.838 26.903 7.245 0.50 29.02 C ANISOU 1222 CB AGLN A 141 4511 3395 3119 1230 -696 291 C ATOM 1223 CB BGLN A 141 -2.670 27.043 7.225 0.50 30.28 C ANISOU 1223 CB BGLN A 141 4701 3527 3276 1223 -690 298 C ATOM 1224 CG AGLN A 141 -2.623 26.930 5.728 0.50 35.90 C ANISOU 1224 CG AGLN A 141 5537 4193 3909 1195 -740 360 C ATOM 1225 CG BGLN A 141 -2.319 27.120 5.736 0.50 48.87 C ANISOU 1225 CG BGLN A 141 7225 5793 5550 1178 -725 371 C ATOM 1226 CD AGLN A 141 -3.832 27.461 4.979 0.50 42.60 C ANISOU 1226 CD AGLN A 141 6419 5061 4705 1361 -883 358 C ATOM 1227 CD BGLN A 141 -1.307 28.194 5.415 0.50 70.26 C ANISOU 1227 CD BGLN A 141 10168 8306 8221 1145 -703 418 C ATOM 1228 OE1AGLN A 141 -4.713 26.712 4.512 0.50 30.01 O ANISOU 1228 OE1AGLN A 141 4707 3604 3093 1387 -932 337 O ATOM 1229 OE1BGLN A 141 -1.621 29.391 5.380 0.50 66.81 O ANISOU 1229 OE1BGLN A 141 9861 7768 7755 1270 -773 423 O ATOM 1230 NE2AGLN A 141 -3.894 28.770 4.842 0.50 36.72 N ANISOU 1230 NE2AGLN A 141 5841 4181 3929 1477 -952 375 N ATOM 1231 NE2BGLN A 141 -0.070 27.783 5.168 0.50 59.36 N ANISOU 1231 NE2BGLN A 141 8851 6867 6837 974 -602 448 N ATOM 1232 N ALA A 142 -2.521 25.952 10.265 1.00 27.82 N ANISOU 1232 N ALA A 142 4043 3400 3126 1135 -525 168 N ATOM 1233 CA ALA A 142 -2.825 26.118 11.698 1.00 28.79 C ANISOU 1233 CA ALA A 142 4052 3571 3314 1169 -497 99 C ATOM 1234 C ALA A 142 -1.560 25.989 12.557 1.00 31.21 C ANISOU 1234 C ALA A 142 4377 3820 3660 1047 -389 111 C ATOM 1235 O ALA A 142 -1.349 26.788 13.468 1.00 30.43 O ANISOU 1235 O ALA A 142 4298 3665 3598 1078 -368 89 O ATOM 1236 CB ALA A 142 -3.871 25.107 12.161 1.00 29.33 C ANISOU 1236 CB ALA A 142 3924 3819 3403 1176 -502 23 C ATOM 1237 N TRP A 143 -0.702 25.020 12.234 1.00 26.48 N ANISOU 1237 N TRP A 143 3777 3232 3052 911 -322 145 N ATOM 1238 CA TRP A 143 0.496 24.768 13.036 1.00 25.53 C ANISOU 1238 CA TRP A 143 3658 3074 2969 799 -226 148 C ATOM 1239 C TRP A 143 1.548 25.856 12.843 1.00 30.36 C ANISOU 1239 C TRP A 143 4435 3533 3568 779 -201 186 C ATOM 1240 O TRP A 143 2.193 26.239 13.808 1.00 29.25 O ANISOU 1240 O TRP A 143 4296 3355 3463 749 -146 167 O ATOM 1241 CB TRP A 143 1.063 23.382 12.709 1.00 22.45 C ANISOU 1241 CB TRP A 143 3215 2743 2571 672 -169 165 C ATOM 1242 CG TRP A 143 0.229 22.240 13.228 1.00 22.37 C ANISOU 1242 CG TRP A 143 3046 2880 2573 662 -162 116 C ATOM 1243 CD1 TRP A 143 -0.978 22.311 13.869 1.00 25.10 C ANISOU 1243 CD1 TRP A 143 3287 3316 2933 747 -201 51 C ATOM 1244 CD2 TRP A 143 0.567 20.846 13.160 1.00 21.03 C ANISOU 1244 CD2 TRP A 143 2811 2781 2397 554 -104 119 C ATOM 1245 NE1 TRP A 143 -1.415 21.049 14.195 1.00 23.69 N ANISOU 1245 NE1 TRP A 143 2991 3262 2750 688 -168 11 N ATOM 1246 CE2 TRP A 143 -0.457 20.134 13.827 1.00 24.40 C ANISOU 1246 CE2 TRP A 143 3107 3336 2827 572 -106 56 C ATOM 1247 CE3 TRP A 143 1.663 20.134 12.638 1.00 21.75 C ANISOU 1247 CE3 TRP A 143 2947 2839 2480 441 -47 163 C ATOM 1248 CZ2 TRP A 143 -0.444 18.736 13.945 1.00 23.29 C ANISOU 1248 CZ2 TRP A 143 2894 3284 2671 481 -53 41 C ATOM 1249 CZ3 TRP A 143 1.679 18.750 12.759 1.00 22.67 C ANISOU 1249 CZ3 TRP A 143 2982 3042 2590 362 0 151 C ATOM 1250 CH2 TRP A 143 0.635 18.065 13.400 1.00 23.49 C ANISOU 1250 CH2 TRP A 143 2971 3266 2688 382 -2 94 C ATOM 1251 N GLU A 144 1.673 26.403 11.623 1.00 28.95 N ANISOU 1251 N GLU A 144 4403 3266 3332 795 -241 234 N ATOM 1252 CA GLU A 144 2.642 27.461 11.330 1.00 28.98 C ANISOU 1252 CA GLU A 144 4588 3117 3306 765 -211 263 C ATOM 1253 C GLU A 144 2.196 28.816 11.882 1.00 34.28 C ANISOU 1253 C GLU A 144 5330 3716 3980 885 -248 246 C ATOM 1254 O GLU A 144 3.026 29.715 11.990 1.00 35.70 O ANISOU 1254 O GLU A 144 5644 3778 4141 853 -203 255 O ATOM 1255 CB GLU A 144 2.917 27.567 9.839 1.00 30.30 C ANISOU 1255 CB GLU A 144 4906 3206 3402 728 -238 315 C ATOM 1256 CG GLU A 144 3.800 26.447 9.313 1.00 32.98 C ANISOU 1256 CG GLU A 144 5217 3574 3741 575 -171 331 C ATOM 1257 CD GLU A 144 4.091 26.567 7.833 1.00 42.38 C ANISOU 1257 CD GLU A 144 6562 4681 4860 522 -190 378 C ATOM 1258 OE1 GLU A 144 3.485 27.444 7.173 1.00 42.85 O ANISOU 1258 OE1 GLU A 144 6749 4668 4863 615 -269 403 O ATOM 1259 OE2 GLU A 144 4.889 25.752 7.320 1.00 31.38 O ANISOU 1259 OE2 GLU A 144 5163 3295 3465 390 -130 387 O ATOM 1260 N ALA A 145 0.916 28.959 12.268 1.00 30.85 N ANISOU 1260 N ALA A 145 4800 3354 3567 1018 -322 213 N ATOM 1261 CA ALA A 145 0.420 30.191 12.893 1.00 31.80 C ANISOU 1261 CA ALA A 145 4966 3415 3700 1140 -356 188 C ATOM 1262 C ALA A 145 0.903 30.270 14.360 1.00 35.85 C ANISOU 1262 C ALA A 145 5396 3946 4278 1089 -272 146 C ATOM 1263 O ALA A 145 0.795 31.317 15.000 1.00 35.54 O ANISOU 1263 O ALA A 145 5408 3843 4254 1156 -269 127 O ATOM 1264 CB ALA A 145 -1.098 30.237 12.846 1.00 32.81 C ANISOU 1264 CB ALA A 145 4999 3630 3838 1295 -461 150 C ATOM 1265 N ASN A 146 1.421 29.147 14.890 1.00 30.35 N ANISOU 1265 N ASN A 146 4577 3335 3618 973 -205 131 N ATOM 1266 CA ASN A 146 1.899 29.074 16.272 1.00 27.60 C ANISOU 1266 CA ASN A 146 4147 3013 3328 915 -130 92 C ATOM 1267 C ASN A 146 3.443 29.053 16.276 1.00 28.02 C ANISOU 1267 C ASN A 146 4281 2995 3370 782 -41 118 C ATOM 1268 O ASN A 146 4.061 27.995 16.444 1.00 23.20 O ANISOU 1268 O ASN A 146 3594 2445 2777 680 5 115 O ATOM 1269 CB ASN A 146 1.306 27.833 16.933 1.00 27.42 C ANISOU 1269 CB ASN A 146 3935 3136 3346 890 -127 49 C ATOM 1270 CG ASN A 146 1.525 27.795 18.436 1.00 43.20 C ANISOU 1270 CG ASN A 146 5845 5166 5401 850 -68 1 C ATOM 1271 OD1 ASN A 146 2.309 28.565 19.015 1.00 32.91 O ANISOU 1271 OD1 ASN A 146 4609 3784 4110 820 -17 5 O ATOM 1272 ND2 ASN A 146 0.875 26.861 19.094 1.00 33.77 N ANISOU 1272 ND2 ASN A 146 4507 4089 4236 835 -68 -47 N ATOM 1273 N GLN A 147 4.056 30.227 16.069 1.00 26.27 N ANISOU 1273 N GLN A 147 4220 2646 3114 783 -17 135 N ATOM 1274 CA GLN A 147 5.519 30.370 15.960 1.00 25.30 C ANISOU 1274 CA GLN A 147 4190 2453 2971 656 70 144 C ATOM 1275 C GLN A 147 6.264 29.908 17.215 1.00 24.47 C ANISOU 1275 C GLN A 147 3972 2406 2921 571 146 107 C ATOM 1276 O GLN A 147 7.315 29.299 17.079 1.00 23.10 O ANISOU 1276 O GLN A 147 3790 2242 2745 460 201 105 O ATOM 1277 CB GLN A 147 5.915 31.819 15.632 1.00 27.63 C ANISOU 1277 CB GLN A 147 4686 2603 3211 675 89 156 C ATOM 1278 CG GLN A 147 5.623 32.223 14.168 1.00 49.24 C ANISOU 1278 CG GLN A 147 7587 5252 5870 717 27 201 C ATOM 1279 CD GLN A 147 6.354 31.395 13.129 1.00 71.45 C ANISOU 1279 CD GLN A 147 10429 8067 8650 601 49 223 C ATOM 1280 OE1 GLN A 147 5.744 30.864 12.192 1.00 72.92 O ANISOU 1280 OE1 GLN A 147 10612 8281 8814 633 -19 253 O ATOM 1281 NE2 GLN A 147 7.673 31.262 13.262 1.00 56.88 N ANISOU 1281 NE2 GLN A 147 8610 6198 6802 462 144 202 N ATOM 1282 N HIS A 148 5.724 30.168 18.414 1.00 22.31 N ANISOU 1282 N HIS A 148 3611 2172 2695 621 147 73 N ATOM 1283 CA HIS A 148 6.361 29.737 19.681 1.00 21.04 C ANISOU 1283 CA HIS A 148 3346 2065 2582 544 211 38 C ATOM 1284 C HIS A 148 6.532 28.220 19.719 1.00 21.60 C ANISOU 1284 C HIS A 148 3295 2238 2675 480 211 34 C ATOM 1285 O HIS A 148 7.561 27.731 20.177 1.00 20.45 O ANISOU 1285 O HIS A 148 3117 2109 2543 388 266 21 O ATOM 1286 CB HIS A 148 5.559 30.217 20.906 1.00 21.64 C ANISOU 1286 CB HIS A 148 3349 2169 2704 609 205 1 C ATOM 1287 CG HIS A 148 5.636 31.699 21.134 1.00 26.18 C ANISOU 1287 CG HIS A 148 4041 2641 3264 652 229 -1 C ATOM 1288 ND1 HIS A 148 4.681 32.363 21.895 1.00 28.93 N ANISOU 1288 ND1 HIS A 148 4353 2991 3646 742 206 -30 N ATOM 1289 CD2 HIS A 148 6.550 32.599 20.695 1.00 29.30 C ANISOU 1289 CD2 HIS A 148 4593 2930 3610 611 279 16 C ATOM 1290 CE1 HIS A 148 5.033 33.640 21.887 1.00 29.60 C ANISOU 1290 CE1 HIS A 148 4577 2968 3703 759 241 -22 C ATOM 1291 NE2 HIS A 148 6.154 33.832 21.175 1.00 30.18 N ANISOU 1291 NE2 HIS A 148 4775 2972 3720 679 288 4 N ATOM 1292 N GLU A 149 5.530 27.490 19.212 1.00 17.33 N ANISOU 1292 N GLU A 149 2689 1763 2131 531 150 43 N ATOM 1293 CA GLU A 149 5.536 26.026 19.147 1.00 16.85 C ANISOU 1293 CA GLU A 149 2527 1797 2080 477 149 41 C ATOM 1294 C GLU A 149 6.618 25.530 18.186 1.00 19.88 C ANISOU 1294 C GLU A 149 2969 2148 2435 390 180 72 C ATOM 1295 O GLU A 149 7.293 24.556 18.482 1.00 19.18 O ANISOU 1295 O GLU A 149 2818 2105 2363 314 214 62 O ATOM 1296 CB GLU A 149 4.137 25.524 18.721 1.00 19.14 C ANISOU 1296 CB GLU A 149 2748 2162 2361 553 81 36 C ATOM 1297 CG GLU A 149 4.051 24.021 18.455 1.00 30.58 C ANISOU 1297 CG GLU A 149 4112 3704 3803 495 85 37 C ATOM 1298 CD GLU A 149 4.282 23.093 19.631 1.00 54.92 C ANISOU 1298 CD GLU A 149 7097 6855 6916 434 125 1 C ATOM 1299 OE1 GLU A 149 4.158 23.546 20.790 1.00 58.52 O ANISOU 1299 OE1 GLU A 149 7520 7312 7404 446 139 -35 O ATOM 1300 OE2 GLU A 149 4.566 21.898 19.391 1.00 48.39 O ANISOU 1300 OE2 GLU A 149 6231 6077 6077 371 143 9 O ATOM 1301 N LEU A 150 6.799 26.200 17.051 1.00 18.81 N ANISOU 1301 N LEU A 150 2960 1932 2257 398 167 104 N ATOM 1302 CA LEU A 150 7.851 25.800 16.097 1.00 18.72 C ANISOU 1302 CA LEU A 150 3013 1883 2218 302 203 122 C ATOM 1303 C LEU A 150 9.238 25.973 16.732 1.00 17.70 C ANISOU 1303 C LEU A 150 2895 1725 2106 211 280 90 C ATOM 1304 O LEU A 150 10.081 25.103 16.567 1.00 15.61 O ANISOU 1304 O LEU A 150 2590 1489 1851 128 314 80 O ATOM 1305 CB LEU A 150 7.757 26.629 14.813 1.00 19.43 C ANISOU 1305 CB LEU A 150 3259 1876 2248 321 176 157 C ATOM 1306 CG LEU A 150 6.397 26.653 14.099 1.00 26.36 C ANISOU 1306 CG LEU A 150 4142 2775 3101 425 88 186 C ATOM 1307 CD1 LEU A 150 6.383 27.731 13.044 1.00 28.83 C ANISOU 1307 CD1 LEU A 150 4638 2968 3349 455 59 218 C ATOM 1308 CD2 LEU A 150 6.093 25.333 13.458 1.00 28.82 C ANISOU 1308 CD2 LEU A 150 4369 3171 3409 390 70 203 C ATOM 1309 N LEU A 151 9.463 27.092 17.454 1.00 15.64 N ANISOU 1309 N LEU A 151 2685 1410 1847 229 308 70 N ATOM 1310 CA LEU A 151 10.741 27.385 18.141 1.00 15.62 C ANISOU 1310 CA LEU A 151 2691 1388 1856 145 383 30 C ATOM 1311 C LEU A 151 10.997 26.353 19.233 1.00 17.75 C ANISOU 1311 C LEU A 151 2812 1754 2178 119 394 3 C ATOM 1312 O LEU A 151 12.108 25.821 19.361 1.00 15.49 O ANISOU 1312 O LEU A 151 2495 1488 1903 38 436 -25 O ATOM 1313 CB LEU A 151 10.733 28.806 18.715 1.00 16.20 C ANISOU 1313 CB LEU A 151 2849 1389 1915 176 411 15 C ATOM 1314 CG LEU A 151 10.618 29.934 17.652 1.00 22.89 C ANISOU 1314 CG LEU A 151 3880 2120 2696 198 406 39 C ATOM 1315 CD1 LEU A 151 10.518 31.281 18.294 1.00 23.17 C ANISOU 1315 CD1 LEU A 151 4001 2086 2718 236 435 26 C ATOM 1316 CD2 LEU A 151 11.806 29.928 16.697 1.00 25.68 C ANISOU 1316 CD2 LEU A 151 4333 2419 3004 83 461 25 C ATOM 1317 N TYR A 152 9.942 26.040 19.992 1.00 15.00 N ANISOU 1317 N TYR A 152 2376 1465 1859 187 353 6 N ATOM 1318 CA TYR A 152 9.994 25.036 21.052 1.00 14.80 C ANISOU 1318 CA TYR A 152 2227 1524 1871 166 355 -18 C ATOM 1319 C TYR A 152 10.411 23.676 20.425 1.00 16.64 C ANISOU 1319 C TYR A 152 2417 1804 2101 117 351 -8 C ATOM 1320 O TYR A 152 11.284 23.002 20.958 1.00 14.75 O ANISOU 1320 O TYR A 152 2128 1596 1881 63 376 -32 O ATOM 1321 CB TYR A 152 8.616 24.959 21.799 1.00 14.62 C ANISOU 1321 CB TYR A 152 2134 1552 1870 241 313 -24 C ATOM 1322 CG TYR A 152 8.333 23.559 22.299 1.00 14.15 C ANISOU 1322 CG TYR A 152 1970 1581 1824 220 298 -36 C ATOM 1323 CD1 TYR A 152 8.909 23.092 23.479 1.00 14.94 C ANISOU 1323 CD1 TYR A 152 2016 1714 1948 174 324 -65 C ATOM 1324 CD2 TYR A 152 7.605 22.657 21.526 1.00 14.46 C ANISOU 1324 CD2 TYR A 152 1980 1670 1845 236 264 -19 C ATOM 1325 CE1 TYR A 152 8.762 21.766 23.880 1.00 14.26 C ANISOU 1325 CE1 TYR A 152 1862 1695 1862 149 313 -75 C ATOM 1326 CE2 TYR A 152 7.437 21.330 21.924 1.00 15.24 C ANISOU 1326 CE2 TYR A 152 2005 1843 1944 205 262 -31 C ATOM 1327 CZ TYR A 152 8.030 20.888 23.097 1.00 19.74 C ANISOU 1327 CZ TYR A 152 2535 2431 2532 163 286 -58 C ATOM 1328 OH TYR A 152 7.903 19.577 23.477 1.00 16.42 O ANISOU 1328 OH TYR A 152 2066 2071 2102 132 284 -70 O ATOM 1329 N GLN A 153 9.829 23.298 19.276 1.00 15.65 N ANISOU 1329 N GLN A 153 2315 1681 1951 135 319 26 N ATOM 1330 CA GLN A 153 10.212 22.010 18.658 1.00 15.95 C ANISOU 1330 CA GLN A 153 2314 1760 1985 82 322 35 C ATOM 1331 C GLN A 153 11.656 22.008 18.141 1.00 17.19 C ANISOU 1331 C GLN A 153 2516 1875 2140 -2 371 19 C ATOM 1332 O GLN A 153 12.324 20.993 18.263 1.00 15.67 O ANISOU 1332 O GLN A 153 2267 1723 1965 -48 386 4 O ATOM 1333 CB GLN A 153 9.276 21.598 17.501 1.00 17.47 C ANISOU 1333 CB GLN A 153 2521 1969 2147 110 283 74 C ATOM 1334 CG GLN A 153 7.891 21.218 17.980 1.00 25.37 C ANISOU 1334 CG GLN A 153 3448 3043 3149 178 240 71 C ATOM 1335 CD GLN A 153 7.770 19.847 18.632 1.00 30.08 C ANISOU 1335 CD GLN A 153 3950 3724 3755 148 249 54 C ATOM 1336 OE1 GLN A 153 8.743 19.200 19.073 1.00 26.30 O ANISOU 1336 OE1 GLN A 153 3451 3250 3293 92 281 41 O ATOM 1337 NE2 GLN A 153 6.542 19.415 18.783 1.00 29.85 N ANISOU 1337 NE2 GLN A 153 3866 3762 3713 188 220 44 N ATOM 1338 N LYS A 154 12.148 23.143 17.657 1.00 14.98 N ANISOU 1338 N LYS A 154 2338 1516 1838 -22 396 14 N ATOM 1339 CA LYS A 154 13.539 23.249 17.211 1.00 16.49 C ANISOU 1339 CA LYS A 154 2573 1670 2024 -114 452 -22 C ATOM 1340 C LYS A 154 14.490 23.072 18.420 1.00 19.55 C ANISOU 1340 C LYS A 154 2885 2097 2447 -144 486 -76 C ATOM 1341 O LYS A 154 15.448 22.309 18.344 1.00 17.06 O ANISOU 1341 O LYS A 154 2523 1810 2148 -201 508 -109 O ATOM 1342 CB LYS A 154 13.770 24.607 16.516 1.00 17.58 C ANISOU 1342 CB LYS A 154 2856 1708 2116 -135 479 -24 C ATOM 1343 CG LYS A 154 15.207 24.807 16.038 1.00 24.54 C ANISOU 1343 CG LYS A 154 3789 2551 2982 -246 548 -79 C ATOM 1344 CD LYS A 154 15.375 26.198 15.394 1.00 23.11 C ANISOU 1344 CD LYS A 154 3777 2262 2741 -275 581 -85 C ATOM 1345 CE LYS A 154 16.820 26.459 14.991 1.00 27.71 C ANISOU 1345 CE LYS A 154 4415 2812 3302 -401 662 -160 C ATOM 1346 NZ LYS A 154 17.287 25.494 13.957 1.00 23.53 N ANISOU 1346 NZ LYS A 154 3868 2296 2778 -475 669 -170 N ATOM 1347 N ASN A 155 14.201 23.760 19.539 1.00 16.57 N ANISOU 1347 N ASN A 155 2493 1721 2081 -103 486 -85 N ATOM 1348 CA ASN A 155 14.994 23.585 20.754 1.00 16.50 C ANISOU 1348 CA ASN A 155 2412 1755 2102 -127 509 -132 C ATOM 1349 C ASN A 155 14.946 22.134 21.249 1.00 17.34 C ANISOU 1349 C ASN A 155 2414 1938 2237 -116 476 -131 C ATOM 1350 O ASN A 155 15.973 21.604 21.675 1.00 14.43 O ANISOU 1350 O ASN A 155 1996 1600 1886 -154 491 -173 O ATOM 1351 CB ASN A 155 14.520 24.506 21.866 1.00 14.37 C ANISOU 1351 CB ASN A 155 2145 1477 1840 -87 513 -136 C ATOM 1352 CG ASN A 155 15.330 24.332 23.140 1.00 21.69 C ANISOU 1352 CG ASN A 155 3001 2449 2793 -116 534 -183 C ATOM 1353 OD1 ASN A 155 16.500 24.685 23.192 1.00 18.50 O ANISOU 1353 OD1 ASN A 155 2608 2038 2383 -176 582 -232 O ATOM 1354 ND2 ASN A 155 14.756 23.695 24.149 1.00 15.21 N ANISOU 1354 ND2 ASN A 155 2103 1679 1995 -80 499 -175 N ATOM 1355 N TRP A 156 13.761 21.510 21.217 1.00 15.72 N ANISOU 1355 N TRP A 156 2181 1763 2030 -64 431 -89 N ATOM 1356 CA TRP A 156 13.627 20.132 21.714 1.00 14.57 C ANISOU 1356 CA TRP A 156 1957 1681 1897 -58 405 -88 C ATOM 1357 C TRP A 156 14.507 19.191 20.883 1.00 17.65 C ANISOU 1357 C TRP A 156 2337 2080 2288 -106 417 -96 C ATOM 1358 O TRP A 156 15.268 18.425 21.445 1.00 16.90 O ANISOU 1358 O TRP A 156 2193 2017 2211 -121 417 -126 O ATOM 1359 CB TRP A 156 12.147 19.624 21.743 1.00 12.01 C ANISOU 1359 CB TRP A 156 1610 1393 1559 -8 366 -54 C ATOM 1360 CG TRP A 156 12.070 18.420 22.641 1.00 11.88 C ANISOU 1360 CG TRP A 156 1533 1433 1548 -10 351 -67 C ATOM 1361 CD1 TRP A 156 11.985 18.423 24.006 1.00 14.34 C ANISOU 1361 CD1 TRP A 156 1814 1765 1870 -1 344 -92 C ATOM 1362 CD2 TRP A 156 12.349 17.057 22.255 1.00 11.16 C ANISOU 1362 CD2 TRP A 156 1420 1374 1446 -33 347 -60 C ATOM 1363 NE1 TRP A 156 12.181 17.142 24.493 1.00 13.23 N ANISOU 1363 NE1 TRP A 156 1644 1662 1721 -15 331 -100 N ATOM 1364 CE2 TRP A 156 12.436 16.293 23.437 1.00 14.19 C ANISOU 1364 CE2 TRP A 156 1771 1790 1830 -31 334 -81 C ATOM 1365 CE3 TRP A 156 12.544 16.412 21.008 1.00 13.04 C ANISOU 1365 CE3 TRP A 156 1672 1610 1673 -58 355 -39 C ATOM 1366 CZ2 TRP A 156 12.730 14.917 23.423 1.00 13.91 C ANISOU 1366 CZ2 TRP A 156 1724 1781 1780 -45 327 -81 C ATOM 1367 CZ3 TRP A 156 12.807 15.039 20.990 1.00 13.75 C ANISOU 1367 CZ3 TRP A 156 1738 1733 1754 -76 354 -39 C ATOM 1368 CH2 TRP A 156 12.856 14.298 22.188 1.00 13.93 C ANISOU 1368 CH2 TRP A 156 1735 1784 1773 -64 339 -59 C ATOM 1369 N LEU A 157 14.402 19.262 19.554 1.00 14.81 N ANISOU 1369 N LEU A 157 2026 1690 1910 -128 425 -73 N ATOM 1370 CA LEU A 157 15.191 18.415 18.658 1.00 15.55 C ANISOU 1370 CA LEU A 157 2113 1787 2007 -182 443 -83 C ATOM 1371 C LEU A 157 16.697 18.630 18.799 1.00 18.34 C ANISOU 1371 C LEU A 157 2457 2129 2381 -237 482 -149 C ATOM 1372 O LEU A 157 17.450 17.661 18.858 1.00 19.19 O ANISOU 1372 O LEU A 157 2512 2270 2511 -257 484 -179 O ATOM 1373 CB LEU A 157 14.777 18.681 17.180 1.00 15.78 C ANISOU 1373 CB LEU A 157 2214 1774 2007 -206 449 -47 C ATOM 1374 CG LEU A 157 13.387 18.130 16.822 1.00 21.01 C ANISOU 1374 CG LEU A 157 2866 2468 2647 -160 410 9 C ATOM 1375 CD1 LEU A 157 12.938 18.571 15.431 1.00 20.49 C ANISOU 1375 CD1 LEU A 157 2878 2358 2547 -176 406 46 C ATOM 1376 CD2 LEU A 157 13.341 16.619 16.993 1.00 18.27 C ANISOU 1376 CD2 LEU A 157 2450 2183 2307 -167 405 13 C ATOM 1377 N GLU A 158 17.131 19.887 18.866 1.00 15.64 N ANISOU 1377 N GLU A 158 2167 1744 2031 -261 514 -179 N ATOM 1378 CA GLU A 158 18.560 20.212 18.826 1.00 17.10 C ANISOU 1378 CA GLU A 158 2349 1922 2225 -329 562 -256 C ATOM 1379 C GLU A 158 19.249 20.110 20.157 1.00 21.43 C ANISOU 1379 C GLU A 158 2823 2519 2800 -314 559 -307 C ATOM 1380 O GLU A 158 20.450 19.838 20.188 1.00 21.43 O ANISOU 1380 O GLU A 158 2779 2545 2818 -357 581 -379 O ATOM 1381 CB GLU A 158 18.760 21.631 18.254 1.00 18.38 C ANISOU 1381 CB GLU A 158 2618 2013 2351 -376 610 -274 C ATOM 1382 CG GLU A 158 18.284 21.688 16.797 1.00 22.39 C ANISOU 1382 CG GLU A 158 3215 2466 2828 -405 612 -232 C ATOM 1383 CD GLU A 158 18.437 23.035 16.122 1.00 27.46 C ANISOU 1383 CD GLU A 158 3992 3021 3420 -453 655 -246 C ATOM 1384 OE1 GLU A 158 18.739 24.023 16.830 1.00 28.64 O ANISOU 1384 OE1 GLU A 158 4172 3152 3557 -456 686 -279 O ATOM 1385 OE2 GLU A 158 18.244 23.111 14.884 1.00 27.24 O ANISOU 1385 OE2 GLU A 158 4051 2941 3360 -492 660 -222 O ATOM 1386 N GLU A 159 18.529 20.406 21.244 1.00 17.09 N ANISOU 1386 N GLU A 159 2259 1983 2252 -257 532 -279 N ATOM 1387 CA GLU A 159 19.154 20.438 22.573 1.00 15.82 C ANISOU 1387 CA GLU A 159 2038 1864 2110 -248 529 -324 C ATOM 1388 C GLU A 159 18.640 19.359 23.512 1.00 17.24 C ANISOU 1388 C GLU A 159 2158 2089 2303 -192 472 -297 C ATOM 1389 O GLU A 159 19.454 18.609 24.059 1.00 17.38 O ANISOU 1389 O GLU A 159 2118 2147 2337 -189 454 -337 O ATOM 1390 CB GLU A 159 18.953 21.817 23.235 1.00 17.74 C ANISOU 1390 CB GLU A 159 2322 2078 2338 -250 559 -331 C ATOM 1391 CG GLU A 159 19.345 23.013 22.359 1.00 23.60 C ANISOU 1391 CG GLU A 159 3156 2761 3051 -307 621 -355 C ATOM 1392 CD GLU A 159 20.768 23.072 21.832 1.00 46.92 C ANISOU 1392 CD GLU A 159 6105 5722 6000 -389 672 -441 C ATOM 1393 OE1 GLU A 159 21.687 22.592 22.534 1.00 37.50 O ANISOU 1393 OE1 GLU A 159 4828 4591 4832 -400 670 -502 O ATOM 1394 OE2 GLU A 159 20.966 23.620 20.722 1.00 47.05 O ANISOU 1394 OE2 GLU A 159 6207 5684 5986 -446 715 -453 O ATOM 1395 N GLU A 160 17.324 19.316 23.769 1.00 12.56 N ANISOU 1395 N GLU A 160 1582 1492 1700 -148 445 -239 N ATOM 1396 CA GLU A 160 16.766 18.359 24.743 1.00 12.71 C ANISOU 1396 CA GLU A 160 1561 1550 1720 -109 400 -222 C ATOM 1397 C GLU A 160 16.962 16.908 24.328 1.00 16.05 C ANISOU 1397 C GLU A 160 1961 1998 2140 -103 375 -215 C ATOM 1398 O GLU A 160 17.406 16.089 25.139 1.00 15.36 O ANISOU 1398 O GLU A 160 1842 1938 2055 -88 346 -235 O ATOM 1399 CB GLU A 160 15.263 18.617 24.946 1.00 13.52 C ANISOU 1399 CB GLU A 160 1684 1646 1808 -74 384 -177 C ATOM 1400 CG GLU A 160 14.998 19.811 25.860 1.00 22.36 C ANISOU 1400 CG GLU A 160 2813 2749 2934 -68 399 -188 C ATOM 1401 CD GLU A 160 15.372 19.494 27.303 1.00 40.85 C ANISOU 1401 CD GLU A 160 5117 5121 5284 -72 384 -218 C ATOM 1402 OE1 GLU A 160 14.783 18.553 27.890 1.00 23.80 O ANISOU 1402 OE1 GLU A 160 2942 2988 3114 -56 350 -207 O ATOM 1403 OE2 GLU A 160 16.370 20.077 27.779 1.00 22.24 O ANISOU 1403 OE2 GLU A 160 2750 2764 2938 -97 407 -256 O ATOM 1404 N CYS A 161 16.602 16.597 23.075 1.00 13.36 N ANISOU 1404 N CYS A 161 1642 1643 1790 -115 385 -184 N ATOM 1405 CA CYS A 161 16.686 15.231 22.530 1.00 13.12 C ANISOU 1405 CA CYS A 161 1599 1633 1755 -117 372 -172 C ATOM 1406 C CYS A 161 18.117 14.692 22.662 1.00 15.26 C ANISOU 1406 C CYS A 161 1831 1917 2050 -129 371 -228 C ATOM 1407 O CYS A 161 18.318 13.570 23.103 1.00 14.56 O ANISOU 1407 O CYS A 161 1723 1851 1959 -104 341 -233 O ATOM 1408 CB CYS A 161 16.229 15.213 21.074 1.00 13.84 C ANISOU 1408 CB CYS A 161 1721 1703 1833 -142 392 -137 C ATOM 1409 SG CYS A 161 16.091 13.544 20.383 1.00 17.66 S ANISOU 1409 SG CYS A 161 2194 2213 2304 -150 387 -113 S ATOM 1410 N ILE A 162 19.095 15.516 22.290 1.00 14.45 N ANISOU 1410 N ILE A 162 1723 1800 1967 -168 404 -278 N ATOM 1411 CA ILE A 162 20.520 15.152 22.359 1.00 15.70 C ANISOU 1411 CA ILE A 162 1832 1981 2153 -183 407 -353 C ATOM 1412 C ILE A 162 20.933 14.923 23.842 1.00 17.96 C ANISOU 1412 C ILE A 162 2077 2302 2445 -138 365 -383 C ATOM 1413 O ILE A 162 21.657 13.959 24.125 1.00 16.75 O ANISOU 1413 O ILE A 162 1885 2175 2304 -110 331 -418 O ATOM 1414 CB ILE A 162 21.405 16.208 21.632 1.00 18.65 C ANISOU 1414 CB ILE A 162 2214 2335 2536 -251 463 -413 C ATOM 1415 CG1 ILE A 162 21.105 16.265 20.112 1.00 17.52 C ANISOU 1415 CG1 ILE A 162 2122 2151 2383 -303 499 -386 C ATOM 1416 CG2 ILE A 162 22.912 15.989 21.906 1.00 20.42 C ANISOU 1416 CG2 ILE A 162 2370 2600 2790 -267 468 -515 C ATOM 1417 CD1 ILE A 162 21.391 14.848 19.246 1.00 20.08 C ANISOU 1417 CD1 ILE A 162 2418 2488 2724 -314 493 -386 C ATOM 1418 N ALA A 163 20.478 15.798 24.764 1.00 15.73 N ANISOU 1418 N ALA A 163 1808 2017 2151 -129 364 -372 N ATOM 1419 CA ALA A 163 20.800 15.664 26.202 1.00 16.32 C ANISOU 1419 CA ALA A 163 1854 2121 2226 -96 325 -397 C ATOM 1420 C ALA A 163 20.187 14.367 26.751 1.00 18.31 C ANISOU 1420 C ALA A 163 2120 2379 2457 -48 270 -356 C ATOM 1421 O ALA A 163 20.858 13.648 27.510 1.00 15.71 O ANISOU 1421 O ALA A 163 1770 2072 2128 -14 225 -388 O ATOM 1422 CB ALA A 163 20.322 16.876 27.003 1.00 17.02 C ANISOU 1422 CB ALA A 163 1961 2199 2306 -108 345 -388 C ATOM 1423 N TRP A 164 18.932 14.058 26.365 1.00 15.36 N ANISOU 1423 N TRP A 164 1789 1987 2060 -46 274 -293 N ATOM 1424 CA TRP A 164 18.290 12.796 26.771 1.00 14.75 C ANISOU 1424 CA TRP A 164 1740 1914 1950 -16 237 -261 C ATOM 1425 C TRP A 164 19.075 11.602 26.224 1.00 15.85 C ANISOU 1425 C TRP A 164 1869 2059 2094 1 219 -278 C ATOM 1426 O TRP A 164 19.303 10.631 26.942 1.00 15.77 O ANISOU 1426 O TRP A 164 1876 2053 2064 38 175 -285 O ATOM 1427 CB TRP A 164 16.828 12.717 26.270 1.00 12.81 C ANISOU 1427 CB TRP A 164 1531 1661 1677 -27 256 -206 C ATOM 1428 CG TRP A 164 15.852 13.511 27.091 1.00 14.91 C ANISOU 1428 CG TRP A 164 1809 1924 1931 -30 258 -194 C ATOM 1429 CD1 TRP A 164 15.117 14.587 26.678 1.00 17.64 C ANISOU 1429 CD1 TRP A 164 2157 2260 2285 -40 286 -177 C ATOM 1430 CD2 TRP A 164 15.435 13.228 28.431 1.00 15.34 C ANISOU 1430 CD2 TRP A 164 1883 1985 1961 -23 231 -201 C ATOM 1431 NE1 TRP A 164 14.236 14.963 27.667 1.00 17.18 N ANISOU 1431 NE1 TRP A 164 2107 2205 2215 -36 279 -177 N ATOM 1432 CE2 TRP A 164 14.443 14.180 28.772 1.00 18.72 C ANISOU 1432 CE2 TRP A 164 2312 2410 2390 -34 250 -194 C ATOM 1433 CE3 TRP A 164 15.805 12.254 29.389 1.00 17.06 C ANISOU 1433 CE3 TRP A 164 2125 2205 2150 -8 190 -217 C ATOM 1434 CZ2 TRP A 164 13.785 14.169 30.018 1.00 18.15 C ANISOU 1434 CZ2 TRP A 164 2258 2342 2296 -44 237 -205 C ATOM 1435 CZ3 TRP A 164 15.159 12.251 30.631 1.00 18.41 C ANISOU 1435 CZ3 TRP A 164 2329 2373 2292 -20 175 -223 C ATOM 1436 CH2 TRP A 164 14.184 13.216 30.945 1.00 18.76 C ANISOU 1436 CH2 TRP A 164 2365 2419 2343 -43 201 -220 C ATOM 1437 N LEU A 165 19.456 11.663 24.948 1.00 14.19 N ANISOU 1437 N LEU A 165 1641 1844 1907 -26 254 -284 N ATOM 1438 CA LEU A 165 20.212 10.577 24.300 1.00 13.87 C ANISOU 1438 CA LEU A 165 1584 1807 1878 -17 247 -306 C ATOM 1439 C LEU A 165 21.553 10.323 25.050 1.00 17.50 C ANISOU 1439 C LEU A 165 1998 2288 2362 23 205 -378 C ATOM 1440 O LEU A 165 21.861 9.176 25.380 1.00 15.49 O ANISOU 1440 O LEU A 165 1754 2035 2096 71 162 -385 O ATOM 1441 CB LEU A 165 20.470 10.911 22.820 1.00 12.85 C ANISOU 1441 CB LEU A 165 1441 1666 1774 -71 299 -313 C ATOM 1442 CG LEU A 165 21.351 9.948 21.970 1.00 17.00 C ANISOU 1442 CG LEU A 165 1939 2194 2324 -78 306 -348 C ATOM 1443 CD1 LEU A 165 20.865 8.468 22.069 1.00 14.81 C ANISOU 1443 CD1 LEU A 165 1698 1914 2015 -40 281 -306 C ATOM 1444 CD2 LEU A 165 21.354 10.410 20.501 1.00 17.47 C ANISOU 1444 CD2 LEU A 165 2004 2235 2400 -151 366 -345 C ATOM 1445 N LYS A 166 22.295 11.381 25.355 1.00 15.42 N ANISOU 1445 N LYS A 166 1690 2042 2125 6 216 -434 N ATOM 1446 CA LYS A 166 23.585 11.212 26.075 1.00 17.51 C ANISOU 1446 CA LYS A 166 1898 2342 2412 44 174 -514 C ATOM 1447 C LYS A 166 23.370 10.563 27.455 1.00 22.02 C ANISOU 1447 C LYS A 166 2501 2915 2950 108 103 -496 C ATOM 1448 O LYS A 166 24.143 9.696 27.873 1.00 21.73 O ANISOU 1448 O LYS A 166 2449 2893 2915 167 45 -534 O ATOM 1449 CB LYS A 166 24.324 12.556 26.224 1.00 19.19 C ANISOU 1449 CB LYS A 166 2062 2581 2648 1 210 -581 C ATOM 1450 CG LYS A 166 24.923 13.060 24.902 1.00 22.13 C ANISOU 1450 CG LYS A 166 2407 2952 3049 -66 275 -631 C ATOM 1451 CD LYS A 166 25.637 14.420 25.106 1.00 24.97 C ANISOU 1451 CD LYS A 166 2735 3336 3417 -120 321 -705 C ATOM 1452 CE LYS A 166 26.053 15.055 23.796 1.00 27.78 C ANISOU 1452 CE LYS A 166 3095 3676 3784 -206 398 -750 C ATOM 1453 NZ LYS A 166 26.273 16.526 23.934 1.00 33.54 N ANISOU 1453 NZ LYS A 166 3842 4404 4499 -270 458 -789 N ATOM 1454 N ARG A 167 22.299 10.963 28.137 1.00 18.57 N ANISOU 1454 N ARG A 167 2116 2461 2481 96 105 -439 N ATOM 1455 CA ARG A 167 21.951 10.445 29.443 1.00 18.84 C ANISOU 1455 CA ARG A 167 2198 2488 2474 135 48 -421 C ATOM 1456 C ARG A 167 21.620 8.918 29.351 1.00 20.12 C ANISOU 1456 C ARG A 167 2425 2624 2597 176 11 -388 C ATOM 1457 O ARG A 167 22.109 8.124 30.160 1.00 19.78 O ANISOU 1457 O ARG A 167 2409 2576 2529 232 -54 -407 O ATOM 1458 CB ARG A 167 20.763 11.271 29.946 1.00 21.82 C ANISOU 1458 CB ARG A 167 2611 2850 2830 94 78 -375 C ATOM 1459 CG ARG A 167 20.118 10.825 31.230 1.00 30.55 C ANISOU 1459 CG ARG A 167 3781 3941 3887 107 35 -352 C ATOM 1460 CD ARG A 167 19.321 12.002 31.799 1.00 25.64 C ANISOU 1460 CD ARG A 167 3159 3315 3266 61 70 -337 C ATOM 1461 NE ARG A 167 18.691 11.585 33.043 1.00 30.26 N ANISOU 1461 NE ARG A 167 3809 3885 3804 58 36 -324 N ATOM 1462 CZ ARG A 167 17.874 12.329 33.762 1.00 34.68 C ANISOU 1462 CZ ARG A 167 4383 4437 4355 18 58 -315 C ATOM 1463 NH1 ARG A 167 17.554 13.553 33.364 1.00 22.95 N ANISOU 1463 NH1 ARG A 167 2855 2958 2906 -12 111 -312 N ATOM 1464 NH2 ARG A 167 17.347 11.849 34.872 1.00 31.36 N ANISOU 1464 NH2 ARG A 167 4029 3999 3887 4 28 -312 N ATOM 1465 N PHE A 168 20.780 8.529 28.383 1.00 16.58 N ANISOU 1465 N PHE A 168 2007 2158 2135 147 55 -340 N ATOM 1466 CA PHE A 168 20.377 7.129 28.170 1.00 16.21 C ANISOU 1466 CA PHE A 168 2029 2086 2043 171 40 -307 C ATOM 1467 C PHE A 168 21.554 6.283 27.700 1.00 21.02 C ANISOU 1467 C PHE A 168 2610 2699 2679 220 11 -349 C ATOM 1468 O PHE A 168 21.654 5.120 28.095 1.00 21.31 O ANISOU 1468 O PHE A 168 2710 2711 2675 270 -33 -344 O ATOM 1469 CB PHE A 168 19.222 7.036 27.153 1.00 16.36 C ANISOU 1469 CB PHE A 168 2073 2099 2044 119 102 -253 C ATOM 1470 CG PHE A 168 17.903 7.693 27.550 1.00 16.96 C ANISOU 1470 CG PHE A 168 2178 2176 2090 79 128 -218 C ATOM 1471 CD1 PHE A 168 17.604 7.959 28.888 1.00 19.75 C ANISOU 1471 CD1 PHE A 168 2563 2525 2417 84 97 -225 C ATOM 1472 CD2 PHE A 168 16.960 8.038 26.584 1.00 17.94 C ANISOU 1472 CD2 PHE A 168 2296 2308 2213 36 180 -183 C ATOM 1473 CE1 PHE A 168 16.403 8.596 29.246 1.00 19.95 C ANISOU 1473 CE1 PHE A 168 2604 2555 2422 45 123 -205 C ATOM 1474 CE2 PHE A 168 15.734 8.635 26.950 1.00 18.82 C ANISOU 1474 CE2 PHE A 168 2423 2426 2300 9 198 -162 C ATOM 1475 CZ PHE A 168 15.459 8.888 28.277 1.00 17.17 C ANISOU 1475 CZ PHE A 168 2239 2214 2070 12 172 -176 C ATOM 1476 N LEU A 169 22.455 6.863 26.869 1.00 17.84 N ANISOU 1476 N LEU A 169 2118 2320 2340 204 37 -399 N ATOM 1477 CA LEU A 169 23.639 6.146 26.387 1.00 19.20 C ANISOU 1477 CA LEU A 169 2245 2503 2549 246 14 -458 C ATOM 1478 C LEU A 169 24.538 5.746 27.553 1.00 23.84 C ANISOU 1478 C LEU A 169 2825 3102 3130 332 -74 -510 C ATOM 1479 O LEU A 169 25.158 4.678 27.504 1.00 22.66 O ANISOU 1479 O LEU A 169 2686 2943 2980 398 -119 -537 O ATOM 1480 CB LEU A 169 24.452 6.974 25.366 1.00 19.04 C ANISOU 1480 CB LEU A 169 2129 2511 2594 196 65 -519 C ATOM 1481 CG LEU A 169 23.941 6.926 23.929 1.00 25.11 C ANISOU 1481 CG LEU A 169 2906 3261 3374 127 138 -483 C ATOM 1482 CD1 LEU A 169 24.545 8.084 23.092 1.00 24.36 C ANISOU 1482 CD1 LEU A 169 2744 3185 3328 54 195 -539 C ATOM 1483 CD2 LEU A 169 24.180 5.515 23.299 1.00 26.82 C ANISOU 1483 CD2 LEU A 169 3140 3461 3590 156 131 -481 C ATOM 1484 N GLU A 170 24.581 6.589 28.601 1.00 20.48 N ANISOU 1484 N GLU A 170 2388 2695 2697 332 -99 -524 N ATOM 1485 CA GLU A 170 25.393 6.317 29.791 1.00 21.19 C ANISOU 1485 CA GLU A 170 2475 2800 2775 409 -187 -572 C ATOM 1486 C GLU A 170 24.690 5.241 30.627 1.00 24.61 C ANISOU 1486 C GLU A 170 3038 3181 3132 455 -242 -514 C ATOM 1487 O GLU A 170 25.328 4.256 30.984 1.00 23.44 O ANISOU 1487 O GLU A 170 2923 3019 2966 540 -316 -539 O ATOM 1488 CB GLU A 170 25.662 7.614 30.594 1.00 22.28 C ANISOU 1488 CB GLU A 170 2559 2978 2928 380 -185 -606 C ATOM 1489 CG GLU A 170 26.514 7.424 31.843 1.00 31.85 C ANISOU 1489 CG GLU A 170 3760 4215 4126 454 -278 -659 C ATOM 1490 CD GLU A 170 27.922 6.869 31.685 1.00 52.97 C ANISOU 1490 CD GLU A 170 6357 6931 6838 535 -339 -754 C ATOM 1491 OE1 GLU A 170 28.524 7.000 30.592 1.00 43.12 O ANISOU 1491 OE1 GLU A 170 5026 5714 5646 514 -293 -809 O ATOM 1492 OE2 GLU A 170 28.432 6.307 32.680 1.00 49.78 O ANISOU 1492 OE2 GLU A 170 5979 6531 6406 620 -436 -779 O ATOM 1493 N TYR A 171 23.362 5.377 30.852 1.00 19.98 N ANISOU 1493 N TYR A 171 2532 2563 2496 397 -203 -441 N ATOM 1494 CA TYR A 171 22.596 4.352 31.580 1.00 19.35 C ANISOU 1494 CA TYR A 171 2591 2431 2332 417 -238 -394 C ATOM 1495 C TYR A 171 22.742 2.975 30.930 1.00 21.87 C ANISOU 1495 C TYR A 171 2968 2715 2625 463 -249 -383 C ATOM 1496 O TYR A 171 22.907 1.978 31.635 1.00 20.97 O ANISOU 1496 O TYR A 171 2955 2560 2451 527 -315 -381 O ATOM 1497 CB TYR A 171 21.096 4.697 31.611 1.00 19.31 C ANISOU 1497 CB TYR A 171 2643 2409 2286 333 -174 -334 C ATOM 1498 CG TYR A 171 20.702 5.953 32.351 1.00 19.88 C ANISOU 1498 CG TYR A 171 2682 2500 2369 283 -159 -335 C ATOM 1499 CD1 TYR A 171 21.566 6.550 33.278 1.00 22.08 C ANISOU 1499 CD1 TYR A 171 2918 2800 2669 312 -210 -379 C ATOM 1500 CD2 TYR A 171 19.436 6.503 32.189 1.00 19.83 C ANISOU 1500 CD2 TYR A 171 2692 2493 2349 211 -95 -297 C ATOM 1501 CE1 TYR A 171 21.186 7.696 33.986 1.00 23.20 C ANISOU 1501 CE1 TYR A 171 3037 2958 2821 260 -189 -380 C ATOM 1502 CE2 TYR A 171 19.039 7.631 32.901 1.00 21.54 C ANISOU 1502 CE2 TYR A 171 2884 2723 2578 168 -80 -301 C ATOM 1503 CZ TYR A 171 19.917 8.227 33.793 1.00 27.25 C ANISOU 1503 CZ TYR A 171 3569 3462 3324 189 -123 -339 C ATOM 1504 OH TYR A 171 19.508 9.353 34.446 1.00 26.54 O ANISOU 1504 OH TYR A 171 3456 3383 3246 141 -97 -342 O ATOM 1505 N GLY A 172 22.647 2.932 29.595 1.00 18.56 N ANISOU 1505 N GLY A 172 2497 2308 2245 428 -182 -374 N ATOM 1506 CA GLY A 172 22.738 1.671 28.866 1.00 18.58 C ANISOU 1506 CA GLY A 172 2551 2281 2229 458 -175 -362 C ATOM 1507 C GLY A 172 24.087 1.316 28.277 1.00 22.33 C ANISOU 1507 C GLY A 172 2942 2773 2769 523 -206 -428 C ATOM 1508 O GLY A 172 24.151 0.443 27.410 1.00 21.40 O ANISOU 1508 O GLY A 172 2843 2636 2653 530 -179 -420 O ATOM 1509 N LYS A 173 25.172 1.966 28.743 1.00 18.87 N ANISOU 1509 N LYS A 173 2408 2376 2384 567 -259 -501 N ATOM 1510 CA LYS A 173 26.544 1.807 28.219 1.00 19.41 C ANISOU 1510 CA LYS A 173 2370 2480 2525 624 -287 -590 C ATOM 1511 C LYS A 173 26.947 0.334 27.966 1.00 22.17 C ANISOU 1511 C LYS A 173 2780 2789 2857 709 -329 -598 C ATOM 1512 O LYS A 173 27.490 0.027 26.903 1.00 20.00 O ANISOU 1512 O LYS A 173 2437 2525 2637 704 -294 -638 O ATOM 1513 CB LYS A 173 27.533 2.452 29.214 1.00 25.14 C ANISOU 1513 CB LYS A 173 3023 3254 3276 680 -362 -668 C ATOM 1514 CG LYS A 173 28.910 2.730 28.646 1.00 52.00 C ANISOU 1514 CG LYS A 173 6277 6719 6763 707 -371 -784 C ATOM 1515 CD LYS A 173 29.782 3.502 29.639 1.00 61.93 C ANISOU 1515 CD LYS A 173 7455 8038 8037 745 -433 -864 C ATOM 1516 CE LYS A 173 31.140 3.843 29.067 1.00 75.77 C ANISOU 1516 CE LYS A 173 9052 9867 9870 758 -431 -998 C ATOM 1517 NZ LYS A 173 31.980 2.630 28.861 1.00 89.58 N ANISOU 1517 NZ LYS A 173 10784 11612 11640 872 -503 -1059 N ATOM 1518 N ASP A 174 26.704 -0.560 28.950 1.00 21.45 N ANISOU 1518 N ASP A 174 2821 2643 2684 784 -402 -565 N ATOM 1519 CA ASP A 174 27.076 -1.979 28.886 1.00 23.41 C ANISOU 1519 CA ASP A 174 3156 2840 2900 879 -452 -570 C ATOM 1520 C ASP A 174 26.410 -2.702 27.721 1.00 26.58 C ANISOU 1520 C ASP A 174 3605 3207 3288 819 -360 -518 C ATOM 1521 O ASP A 174 26.996 -3.632 27.173 1.00 25.19 O ANISOU 1521 O ASP A 174 3433 3009 3128 879 -372 -546 O ATOM 1522 CB ASP A 174 26.772 -2.686 30.216 1.00 26.22 C ANISOU 1522 CB ASP A 174 3678 3133 3151 951 -540 -535 C ATOM 1523 CG ASP A 174 27.680 -2.226 31.342 1.00 42.05 C ANISOU 1523 CG ASP A 174 5637 5169 5169 1037 -651 -598 C ATOM 1524 OD1 ASP A 174 28.778 -1.671 31.044 1.00 42.27 O ANISOU 1524 OD1 ASP A 174 5503 5269 5288 1071 -673 -687 O ATOM 1525 OD2 ASP A 174 27.309 -2.425 32.519 1.00 53.65 O ANISOU 1525 OD2 ASP A 174 7234 6596 6555 1063 -713 -566 O ATOM 1526 N THR A 175 25.223 -2.246 27.319 1.00 20.91 N ANISOU 1526 N THR A 175 2912 2489 2542 703 -269 -449 N ATOM 1527 CA THR A 175 24.516 -2.790 26.162 1.00 20.21 C ANISOU 1527 CA THR A 175 2856 2383 2441 630 -173 -400 C ATOM 1528 C THR A 175 24.845 -2.006 24.878 1.00 22.14 C ANISOU 1528 C THR A 175 2951 2678 2781 555 -101 -430 C ATOM 1529 O THR A 175 25.231 -2.581 23.872 1.00 19.64 O ANISOU 1529 O THR A 175 2603 2356 2501 547 -62 -448 O ATOM 1530 CB THR A 175 22.979 -2.713 26.418 1.00 25.51 C ANISOU 1530 CB THR A 175 3634 3035 3023 542 -116 -317 C ATOM 1531 OG1 THR A 175 22.676 -3.482 27.567 1.00 27.82 O ANISOU 1531 OG1 THR A 175 4080 3273 3216 595 -174 -297 O ATOM 1532 CG2 THR A 175 22.132 -3.186 25.205 1.00 25.50 C ANISOU 1532 CG2 THR A 175 3658 3030 3001 454 -11 -266 C ATOM 1533 N LEU A 176 24.612 -0.692 24.908 1.00 20.26 N ANISOU 1533 N LEU A 176 2637 2484 2578 490 -75 -432 N ATOM 1534 CA LEU A 176 24.666 0.166 23.730 1.00 19.86 C ANISOU 1534 CA LEU A 176 2482 2469 2596 400 3 -446 C ATOM 1535 C LEU A 176 26.052 0.435 23.204 1.00 23.03 C ANISOU 1535 C LEU A 176 2757 2905 3088 420 -9 -547 C ATOM 1536 O LEU A 176 26.206 0.678 22.012 1.00 23.50 O ANISOU 1536 O LEU A 176 2756 2977 3196 345 61 -565 O ATOM 1537 CB LEU A 176 23.996 1.523 24.069 1.00 19.53 C ANISOU 1537 CB LEU A 176 2416 2453 2551 336 26 -420 C ATOM 1538 CG LEU A 176 22.516 1.447 24.510 1.00 24.27 C ANISOU 1538 CG LEU A 176 3122 3032 3069 298 48 -334 C ATOM 1539 CD1 LEU A 176 22.039 2.804 25.008 1.00 22.13 C ANISOU 1539 CD1 LEU A 176 2817 2786 2805 257 56 -325 C ATOM 1540 CD2 LEU A 176 21.612 0.898 23.383 1.00 24.97 C ANISOU 1540 CD2 LEU A 176 3250 3108 3129 228 128 -276 C ATOM 1541 N GLN A 177 27.047 0.471 24.069 1.00 19.37 N ANISOU 1541 N GLN A 177 2250 2462 2646 510 -92 -621 N ATOM 1542 CA GLN A 177 28.367 0.858 23.580 1.00 20.05 C ANISOU 1542 CA GLN A 177 2200 2598 2820 517 -96 -738 C ATOM 1543 C GLN A 177 29.297 -0.327 23.488 1.00 24.05 C ANISOU 1543 C GLN A 177 2693 3094 3351 618 -151 -801 C ATOM 1544 O GLN A 177 30.498 -0.158 23.260 1.00 24.29 O ANISOU 1544 O GLN A 177 2604 3171 3453 646 -172 -918 O ATOM 1545 CB GLN A 177 28.959 1.973 24.473 1.00 21.50 C ANISOU 1545 CB GLN A 177 2309 2835 3025 534 -140 -802 C ATOM 1546 CG GLN A 177 28.019 3.214 24.546 1.00 20.38 C ANISOU 1546 CG GLN A 177 2184 2698 2861 435 -81 -740 C ATOM 1547 CD GLN A 177 28.554 4.335 25.415 1.00 35.05 C ANISOU 1547 CD GLN A 177 3978 4607 4734 439 -110 -799 C ATOM 1548 OE1 GLN A 177 27.844 4.926 26.258 1.00 30.73 O ANISOU 1548 OE1 GLN A 177 3480 4052 4145 426 -120 -743 O ATOM 1549 NE2 GLN A 177 29.777 4.729 25.164 1.00 25.41 N ANISOU 1549 NE2 GLN A 177 2641 3441 3574 441 -113 -918 N ATOM 1550 N ARG A 178 28.751 -1.529 23.654 1.00 20.56 N ANISOU 1550 N ARG A 178 2373 2591 2847 670 -171 -732 N ATOM 1551 CA ARG A 178 29.575 -2.730 23.553 1.00 21.43 C ANISOU 1551 CA ARG A 178 2490 2679 2974 775 -223 -786 C ATOM 1552 C ARG A 178 29.840 -3.096 22.071 1.00 23.68 C ANISOU 1552 C ARG A 178 2714 2963 3321 706 -136 -815 C ATOM 1553 O ARG A 178 29.164 -2.601 21.154 1.00 21.86 O ANISOU 1553 O ARG A 178 2473 2734 3096 577 -36 -767 O ATOM 1554 CB ARG A 178 28.884 -3.907 24.283 1.00 22.72 C ANISOU 1554 CB ARG A 178 2833 2766 3034 850 -269 -701 C ATOM 1555 CG ARG A 178 27.864 -4.693 23.435 1.00 22.35 C ANISOU 1555 CG ARG A 178 2889 2666 2936 775 -176 -610 C ATOM 1556 CD ARG A 178 27.113 -5.680 24.320 1.00 24.68 C ANISOU 1556 CD ARG A 178 3376 2889 3111 831 -215 -534 C ATOM 1557 NE ARG A 178 26.386 -6.707 23.559 1.00 22.16 N ANISOU 1557 NE ARG A 178 3163 2520 2738 783 -134 -470 N ATOM 1558 CZ ARG A 178 25.161 -6.550 23.069 1.00 27.14 C ANISOU 1558 CZ ARG A 178 3842 3151 3319 661 -37 -391 C ATOM 1559 NH1 ARG A 178 24.540 -5.381 23.173 1.00 19.77 N ANISOU 1559 NH1 ARG A 178 2855 2262 2395 580 -9 -367 N ATOM 1560 NH2 ARG A 178 24.558 -7.549 22.453 1.00 22.45 N ANISOU 1560 NH2 ARG A 178 3347 2516 2667 622 34 -341 N ATOM 1561 N THR A 179 30.794 -4.005 21.855 1.00 20.50 N ANISOU 1561 N THR A 179 2277 2552 2958 796 -177 -892 N ATOM 1562 CA THR A 179 31.079 -4.549 20.528 1.00 20.25 C ANISOU 1562 CA THR A 179 2201 2512 2983 740 -99 -923 C ATOM 1563 C THR A 179 31.172 -6.059 20.655 1.00 24.96 C ANISOU 1563 C THR A 179 2898 3043 3542 849 -140 -904 C ATOM 1564 O THR A 179 31.961 -6.561 21.457 1.00 24.85 O ANISOU 1564 O THR A 179 2886 3025 3530 997 -249 -966 O ATOM 1565 CB THR A 179 32.372 -3.946 19.886 1.00 27.41 C ANISOU 1565 CB THR A 179 2923 3488 4005 714 -87 -1076 C ATOM 1566 OG1 THR A 179 32.264 -2.525 19.854 1.00 32.67 O ANISOU 1566 OG1 THR A 179 3519 4205 4688 613 -48 -1092 O ATOM 1567 CG2 THR A 179 32.615 -4.455 18.447 1.00 27.14 C ANISOU 1567 CG2 THR A 179 2844 3440 4030 631 6 -1110 C ATOM 1568 N GLU A 180 30.365 -6.778 19.874 1.00 21.11 N ANISOU 1568 N GLU A 180 2502 2505 3015 778 -53 -819 N ATOM 1569 CA GLU A 180 30.471 -8.230 19.766 1.00 20.73 C ANISOU 1569 CA GLU A 180 2553 2390 2933 861 -66 -805 C ATOM 1570 C GLU A 180 30.877 -8.484 18.328 1.00 21.92 C ANISOU 1570 C GLU A 180 2613 2549 3166 775 30 -853 C ATOM 1571 O GLU A 180 30.076 -8.256 17.425 1.00 19.12 O ANISOU 1571 O GLU A 180 2271 2193 2800 630 140 -786 O ATOM 1572 CB GLU A 180 29.178 -8.977 20.169 1.00 21.66 C ANISOU 1572 CB GLU A 180 2874 2437 2917 849 -40 -670 C ATOM 1573 CG GLU A 180 28.745 -8.735 21.612 1.00 31.18 C ANISOU 1573 CG GLU A 180 4181 3629 4037 919 -129 -628 C ATOM 1574 CD GLU A 180 27.753 -9.739 22.172 1.00 49.83 C ANISOU 1574 CD GLU A 180 6762 5911 6261 937 -123 -530 C ATOM 1575 OE1 GLU A 180 27.990 -10.962 22.032 1.00 44.10 O ANISOU 1575 OE1 GLU A 180 6133 5121 5501 1008 -130 -530 O ATOM 1576 OE2 GLU A 180 26.763 -9.302 22.803 1.00 37.93 O ANISOU 1576 OE2 GLU A 180 5334 4402 4675 883 -114 -461 O ATOM 1577 N PRO A 181 32.152 -8.809 18.073 1.00 19.09 N ANISOU 1577 N PRO A 181 2144 2210 2899 852 -11 -981 N ATOM 1578 CA PRO A 181 32.593 -9.017 16.678 1.00 18.78 C ANISOU 1578 CA PRO A 181 2010 2181 2946 755 86 -1041 C ATOM 1579 C PRO A 181 31.866 -10.185 15.983 1.00 22.34 C ANISOU 1579 C PRO A 181 2588 2558 3342 712 170 -948 C ATOM 1580 O PRO A 181 31.472 -11.156 16.640 1.00 21.72 O ANISOU 1580 O PRO A 181 2660 2416 3175 812 128 -881 O ATOM 1581 CB PRO A 181 34.109 -9.314 16.821 1.00 20.75 C ANISOU 1581 CB PRO A 181 2131 2461 3291 883 2 -1207 C ATOM 1582 CG PRO A 181 34.473 -8.752 18.169 1.00 26.96 C ANISOU 1582 CG PRO A 181 2901 3287 4058 1005 -126 -1243 C ATOM 1583 CD PRO A 181 33.267 -9.029 19.025 1.00 21.87 C ANISOU 1583 CD PRO A 181 2449 2580 3282 1030 -149 -1087 C ATOM 1584 N PRO A 182 31.686 -10.132 14.649 1.00 18.61 N ANISOU 1584 N PRO A 182 2066 2090 2913 559 293 -943 N ATOM 1585 CA PRO A 182 31.021 -11.252 13.966 1.00 17.87 C ANISOU 1585 CA PRO A 182 2088 1934 2766 511 381 -859 C ATOM 1586 C PRO A 182 31.845 -12.536 13.915 1.00 21.40 C ANISOU 1586 C PRO A 182 2555 2333 3243 632 350 -924 C ATOM 1587 O PRO A 182 33.085 -12.513 13.810 1.00 21.48 O ANISOU 1587 O PRO A 182 2431 2372 3358 702 300 -1064 O ATOM 1588 CB PRO A 182 30.858 -10.730 12.525 1.00 18.05 C ANISOU 1588 CB PRO A 182 2024 1985 2849 315 510 -864 C ATOM 1589 CG PRO A 182 32.008 -9.814 12.328 1.00 21.25 C ANISOU 1589 CG PRO A 182 2253 2452 3371 304 480 -1010 C ATOM 1590 CD PRO A 182 32.104 -9.092 13.679 1.00 18.76 C ANISOU 1590 CD PRO A 182 1934 2169 3027 417 362 -1019 C ATOM 1591 N LEU A 183 31.131 -13.651 13.896 1.00 18.76 N ANISOU 1591 N LEU A 183 2891 1590 2646 577 -102 -184 N ATOM 1592 CA LEU A 183 31.689 -14.981 13.619 1.00 21.23 C ANISOU 1592 CA LEU A 183 3261 1823 2983 607 -86 -175 C ATOM 1593 C LEU A 183 31.375 -15.217 12.150 1.00 21.55 C ANISOU 1593 C LEU A 183 3300 1852 3035 602 -95 -254 C ATOM 1594 O LEU A 183 30.200 -15.214 11.792 1.00 18.89 O ANISOU 1594 O LEU A 183 2942 1526 2709 544 -101 -311 O ATOM 1595 CB LEU A 183 31.076 -16.052 14.528 1.00 23.87 C ANISOU 1595 CB LEU A 183 3649 2074 3345 568 -44 -135 C ATOM 1596 CG LEU A 183 31.856 -16.320 15.820 1.00 32.95 C ANISOU 1596 CG LEU A 183 4835 3227 4457 630 -34 -37 C ATOM 1597 CD1 LEU A 183 31.641 -15.235 16.820 1.00 34.60 C ANISOU 1597 CD1 LEU A 183 4997 3542 4608 616 -51 -18 C ATOM 1598 CD2 LEU A 183 31.500 -17.669 16.402 1.00 39.25 C ANISOU 1598 CD2 LEU A 183 5723 3902 5290 621 32 28 C ATOM 1599 N VAL A 184 32.406 -15.264 11.285 1.00 17.49 N ANISOU 1599 N VAL A 184 2791 1349 2506 670 -99 -267 N ATOM 1600 CA VAL A 184 32.211 -15.324 9.839 1.00 17.28 C ANISOU 1600 CA VAL A 184 2763 1348 2455 687 -108 -343 C ATOM 1601 C VAL A 184 32.707 -16.651 9.276 1.00 22.08 C ANISOU 1601 C VAL A 184 3422 1877 3090 721 -90 -393 C ATOM 1602 O VAL A 184 33.776 -17.119 9.653 1.00 20.44 O ANISOU 1602 O VAL A 184 3238 1627 2902 781 -70 -348 O ATOM 1603 CB VAL A 184 32.881 -14.126 9.113 1.00 20.55 C ANISOU 1603 CB VAL A 184 3142 1850 2815 740 -106 -319 C ATOM 1604 CG1 VAL A 184 32.517 -14.097 7.628 1.00 20.48 C ANISOU 1604 CG1 VAL A 184 3140 1898 2745 775 -115 -383 C ATOM 1605 CG2 VAL A 184 32.521 -12.784 9.773 1.00 19.09 C ANISOU 1605 CG2 VAL A 184 2917 1709 2627 712 -110 -270 C ATOM 1606 N ARG A 185 31.914 -17.245 8.368 1.00 21.41 N ANISOU 1606 N ARG A 185 3348 1779 3008 691 -101 -501 N ATOM 1607 CA ARG A 185 32.240 -18.501 7.694 1.00 21.82 C ANISOU 1607 CA ARG A 185 3451 1747 3093 716 -81 -588 C ATOM 1608 C ARG A 185 31.801 -18.421 6.224 1.00 25.96 C ANISOU 1608 C ARG A 185 3955 2364 3547 731 -115 -717 C ATOM 1609 O ARG A 185 30.918 -17.630 5.856 1.00 22.44 O ANISOU 1609 O ARG A 185 3457 2027 3042 707 -159 -742 O ATOM 1610 CB ARG A 185 31.587 -19.707 8.415 1.00 20.58 C ANISOU 1610 CB ARG A 185 3343 1432 3045 636 -46 -612 C ATOM 1611 CG ARG A 185 30.055 -19.786 8.266 1.00 25.89 C ANISOU 1611 CG ARG A 185 3970 2116 3749 515 -63 -712 C ATOM 1612 CD ARG A 185 29.395 -20.797 9.190 1.00 35.63 C ANISOU 1612 CD ARG A 185 5244 3188 5106 413 2 -705 C ATOM 1613 NE ARG A 185 27.946 -20.925 8.972 1.00 35.68 N ANISOU 1613 NE ARG A 185 5181 3215 5161 283 -7 -828 N ATOM 1614 CZ ARG A 185 27.025 -20.074 9.419 1.00 42.64 C ANISOU 1614 CZ ARG A 185 5980 4205 6018 228 -30 -806 C ATOM 1615 NH1 ARG A 185 27.385 -18.984 10.095 1.00 29.21 N ANISOU 1615 NH1 ARG A 185 4267 2589 4243 288 -46 -672 N ATOM 1616 NH2 ARG A 185 25.739 -20.287 9.168 1.00 32.50 N ANISOU 1616 NH2 ARG A 185 4612 2950 4787 114 -38 -937 N ATOM 1617 N VAL A 186 32.434 -19.244 5.391 1.00 23.88 N ANISOU 1617 N VAL A 186 3731 2066 3277 789 -97 -800 N ATOM 1618 CA VAL A 186 32.117 -19.364 3.983 1.00 25.09 C ANISOU 1618 CA VAL A 186 3873 2315 3345 819 -128 -942 C ATOM 1619 C VAL A 186 31.636 -20.787 3.734 1.00 32.00 C ANISOU 1619 C VAL A 186 4785 3065 4309 761 -120 -1107 C ATOM 1620 O VAL A 186 32.306 -21.728 4.135 1.00 31.74 O ANISOU 1620 O VAL A 186 4816 2875 4370 779 -65 -1097 O ATOM 1621 CB VAL A 186 33.290 -18.984 3.040 1.00 27.75 C ANISOU 1621 CB VAL A 186 4221 2747 3576 944 -101 -920 C ATOM 1622 CG1 VAL A 186 32.943 -19.293 1.577 1.00 28.35 C ANISOU 1622 CG1 VAL A 186 4300 2931 3542 990 -130 -1084 C ATOM 1623 CG2 VAL A 186 33.677 -17.524 3.203 1.00 25.83 C ANISOU 1623 CG2 VAL A 186 3939 2609 3264 979 -91 -770 C ATOM 1624 N ASN A 187 30.475 -20.934 3.106 1.00 31.08 N ANISOU 1624 N ASN A 187 4622 3014 4172 694 -174 -1263 N ATOM 1625 CA ASN A 187 29.925 -22.230 2.719 1.00 34.20 C ANISOU 1625 CA ASN A 187 5033 3300 4660 617 -168 -1466 C ATOM 1626 C ASN A 187 29.704 -22.248 1.219 1.00 39.13 C ANISOU 1626 C ASN A 187 5626 4093 5151 674 -233 -1657 C ATOM 1627 O ASN A 187 29.410 -21.214 0.620 1.00 35.90 O ANISOU 1627 O ASN A 187 5161 3896 4585 736 -297 -1634 O ATOM 1628 CB ASN A 187 28.601 -22.531 3.438 1.00 38.83 C ANISOU 1628 CB ASN A 187 5568 3816 5369 455 -172 -1518 C ATOM 1629 CG ASN A 187 28.629 -22.549 4.949 1.00 61.64 C ANISOU 1629 CG ASN A 187 8491 6558 8372 395 -103 -1336 C ATOM 1630 OD1 ASN A 187 29.628 -22.899 5.595 1.00 60.81 O ANISOU 1630 OD1 ASN A 187 8472 6322 8312 454 -39 -1206 O ATOM 1631 ND2 ASN A 187 27.481 -22.249 5.541 1.00 47.67 N ANISOU 1631 ND2 ASN A 187 6648 4816 6648 281 -113 -1336 N ATOM 1632 N ARG A 188 29.840 -23.432 0.619 1.00 40.29 N ANISOU 1632 N ARG A 188 5813 4142 5353 662 -212 -1848 N ATOM 1633 CA ARG A 188 29.614 -23.678 -0.800 1.00 42.40 C ANISOU 1633 CA ARG A 188 6053 4563 5493 712 -273 -2077 C ATOM 1634 C ARG A 188 28.281 -24.440 -0.915 1.00 50.22 C ANISOU 1634 C ARG A 188 6974 5517 6589 552 -320 -2321 C ATOM 1635 O ARG A 188 28.129 -25.486 -0.280 1.00 52.00 O ANISOU 1635 O ARG A 188 7241 5494 7024 433 -247 -2380 O ATOM 1636 CB ARG A 188 30.802 -24.481 -1.348 1.00 44.54 C ANISOU 1636 CB ARG A 188 6416 4743 5764 813 -207 -2139 C ATOM 1637 CG ARG A 188 30.938 -24.550 -2.863 1.00 59.17 C ANISOU 1637 CG ARG A 188 8259 6792 7429 918 -254 -2334 C ATOM 1638 CD ARG A 188 32.161 -25.380 -3.255 1.00 66.69 C ANISOU 1638 CD ARG A 188 9302 7633 8405 1021 -168 -2387 C ATOM 1639 NE ARG A 188 33.406 -24.740 -2.821 1.00 72.54 N ANISOU 1639 NE ARG A 188 10075 8373 9112 1134 -98 -2131 N ATOM 1640 CZ ARG A 188 34.233 -24.075 -3.622 1.00 84.94 C ANISOU 1640 CZ ARG A 188 11644 10129 10500 1277 -76 -2070 C ATOM 1641 NH1 ARG A 188 35.323 -23.501 -3.130 1.00 66.61 N ANISOU 1641 NH1 ARG A 188 9330 7797 8183 1350 -6 -1851 N ATOM 1642 NH2 ARG A 188 33.985 -23.991 -4.925 1.00 74.64 N ANISOU 1642 NH2 ARG A 188 10326 9032 9002 1348 -119 -2233 N ATOM 1643 N LYS A 189 27.305 -23.902 -1.669 1.00 47.29 N ANISOU 1643 N LYS A 189 6493 5390 6084 550 -433 -2454 N ATOM 1644 CA LYS A 189 25.998 -24.542 -1.852 1.00 63.30 C ANISOU 1644 CA LYS A 189 8415 7431 8206 394 -491 -2716 C ATOM 1645 C LYS A 189 25.746 -24.843 -3.327 1.00 91.48 C ANISOU 1645 C LYS A 189 11934 11209 11615 458 -590 -3007 C ATOM 1646 O LYS A 189 26.022 -24.005 -4.183 1.00 55.76 O ANISOU 1646 O LYS A 189 7404 6940 6842 628 -658 -2961 O ATOM 1647 CB LYS A 189 24.863 -23.677 -1.280 1.00 64.46 C ANISOU 1647 CB LYS A 189 8436 7703 8351 324 -552 -2643 C ATOM 1648 N GLY A 194 23.730 -27.300 -12.617 1.00 80.35 N ANISOU 1648 N GLY A 194 10125 11541 8864 966 -1368 -5281 N ATOM 1649 CA GLY A 194 25.019 -27.336 -11.932 1.00 78.00 C ANISOU 1649 CA GLY A 194 10014 10924 8697 994 -1175 -4969 C ATOM 1650 C GLY A 194 25.482 -25.911 -11.572 1.00 79.20 C ANISOU 1650 C GLY A 194 10223 11180 8691 1155 -1142 -4508 C ATOM 1651 O GLY A 194 26.505 -25.427 -12.076 1.00 79.00 O ANISOU 1651 O GLY A 194 10311 11245 8460 1351 -1077 -4326 O ATOM 1652 N VAL A 195 24.710 -25.246 -10.691 1.00 72.55 N ANISOU 1652 N VAL A 195 9294 10316 7955 1064 -1177 -4333 N ATOM 1653 CA VAL A 195 24.990 -23.885 -10.230 1.00 69.24 C ANISOU 1653 CA VAL A 195 8914 9964 7431 1185 -1147 -3922 C ATOM 1654 C VAL A 195 25.566 -23.904 -8.808 1.00 67.98 C ANISOU 1654 C VAL A 195 8837 9433 7560 1059 -995 -3647 C ATOM 1655 O VAL A 195 24.872 -24.287 -7.857 1.00 67.85 O ANISOU 1655 O VAL A 195 8754 9228 7798 862 -985 -3683 O ATOM 1656 CB VAL A 195 23.734 -22.987 -10.313 1.00 73.63 C ANISOU 1656 CB VAL A 195 9316 10799 7861 1218 -1300 -3912 C ATOM 1657 N THR A 196 26.841 -23.490 -8.671 1.00 59.66 N ANISOU 1657 N THR A 196 7919 8289 6459 1176 -873 -3378 N ATOM 1658 CA THR A 196 27.542 -23.418 -7.382 1.00 55.14 C ANISOU 1658 CA THR A 196 7425 7412 6115 1097 -739 -3108 C ATOM 1659 C THR A 196 27.577 -21.972 -6.862 1.00 51.21 C ANISOU 1659 C THR A 196 6923 6998 5538 1170 -732 -2770 C ATOM 1660 O THR A 196 27.923 -21.053 -7.603 1.00 49.02 O ANISOU 1660 O THR A 196 6673 6937 5018 1346 -743 -2643 O ATOM 1661 CB THR A 196 28.959 -23.991 -7.506 1.00 64.22 C ANISOU 1661 CB THR A 196 8704 8401 7297 1168 -610 -3064 C ATOM 1662 N ALA A 197 27.213 -21.776 -5.590 1.00 44.12 N ANISOU 1662 N ALA A 197 5998 5921 4845 1037 -703 -2626 N ATOM 1663 CA ALA A 197 27.241 -20.460 -4.955 1.00 41.32 C ANISOU 1663 CA ALA A 197 5641 5604 4454 1087 -687 -2327 C ATOM 1664 C ALA A 197 28.087 -20.477 -3.687 1.00 40.57 C ANISOU 1664 C ALA A 197 5620 5239 4557 1016 -564 -2110 C ATOM 1665 O ALA A 197 28.155 -21.506 -3.013 1.00 41.44 O ANISOU 1665 O ALA A 197 5751 5122 4871 890 -514 -2186 O ATOM 1666 CB ALA A 197 25.825 -20.006 -4.619 1.00 42.16 C ANISOU 1666 CB ALA A 197 5619 5818 4582 1016 -790 -2370 C ATOM 1667 N LEU A 198 28.738 -19.350 -3.375 1.00 32.55 N ANISOU 1667 N LEU A 198 4643 4246 3478 1102 -512 -1844 N ATOM 1668 CA LEU A 198 29.487 -19.167 -2.127 1.00 29.69 C ANISOU 1668 CA LEU A 198 4326 3676 3277 1047 -416 -1638 C ATOM 1669 C LEU A 198 28.683 -18.261 -1.235 1.00 31.68 C ANISOU 1669 C LEU A 198 4521 3937 3580 988 -447 -1508 C ATOM 1670 O LEU A 198 28.245 -17.199 -1.683 1.00 30.68 O ANISOU 1670 O LEU A 198 4361 3983 3312 1074 -493 -1438 O ATOM 1671 CB LEU A 198 30.898 -18.576 -2.311 1.00 28.41 C ANISOU 1671 CB LEU A 198 4234 3519 3043 1163 -323 -1456 C ATOM 1672 CG LEU A 198 31.919 -19.319 -3.188 1.00 34.98 C ANISOU 1672 CG LEU A 198 5123 4357 3811 1250 -268 -1550 C ATOM 1673 CD1 LEU A 198 33.172 -18.463 -3.361 1.00 33.79 C ANISOU 1673 CD1 LEU A 198 5007 4250 3582 1356 -170 -1351 C ATOM 1674 CD2 LEU A 198 32.314 -20.682 -2.578 1.00 37.11 C ANISOU 1674 CD2 LEU A 198 5429 4396 4277 1171 -225 -1652 C ATOM 1675 N PHE A 199 28.515 -18.655 0.022 1.00 27.14 N ANISOU 1675 N PHE A 199 3941 3176 3196 860 -411 -1466 N ATOM 1676 CA PHE A 199 27.796 -17.863 1.004 1.00 27.39 C ANISOU 1676 CA PHE A 199 3920 3202 3286 799 -424 -1349 C ATOM 1677 C PHE A 199 28.736 -17.436 2.105 1.00 29.54 C ANISOU 1677 C PHE A 199 4246 3339 3639 795 -342 -1142 C ATOM 1678 O PHE A 199 29.366 -18.277 2.746 1.00 29.12 O ANISOU 1678 O PHE A 199 4243 3119 3701 747 -283 -1130 O ATOM 1679 CB PHE A 199 26.612 -18.645 1.608 1.00 30.64 C ANISOU 1679 CB PHE A 199 4261 3540 3841 643 -450 -1486 C ATOM 1680 CG PHE A 199 25.404 -18.807 0.716 1.00 34.88 C ANISOU 1680 CG PHE A 199 4692 4251 4310 627 -554 -1700 C ATOM 1681 CD1 PHE A 199 25.411 -19.718 -0.335 1.00 38.60 C ANISOU 1681 CD1 PHE A 199 5162 4767 4738 635 -591 -1922 C ATOM 1682 CD2 PHE A 199 24.241 -18.082 0.956 1.00 38.93 C ANISOU 1682 CD2 PHE A 199 5093 4893 4805 608 -618 -1701 C ATOM 1683 CE1 PHE A 199 24.292 -19.868 -1.155 1.00 42.49 C ANISOU 1683 CE1 PHE A 199 5537 5449 5158 622 -702 -2147 C ATOM 1684 CE2 PHE A 199 23.115 -18.243 0.140 1.00 43.54 C ANISOU 1684 CE2 PHE A 199 5552 5667 5323 603 -728 -1915 C ATOM 1685 CZ PHE A 199 23.152 -19.127 -0.913 1.00 42.71 C ANISOU 1685 CZ PHE A 199 5441 5621 5164 608 -775 -2140 C ATOM 1686 N CYS A 200 28.863 -16.135 2.292 1.00 25.49 N ANISOU 1686 N CYS A 200 3724 2899 3062 854 -337 -988 N ATOM 1687 CA CYS A 200 29.610 -15.582 3.397 1.00 26.33 C ANISOU 1687 CA CYS A 200 3857 2905 3244 838 -274 -819 C ATOM 1688 C CYS A 200 28.587 -15.272 4.482 1.00 26.46 C ANISOU 1688 C CYS A 200 3821 2892 3340 747 -294 -794 C ATOM 1689 O CYS A 200 27.783 -14.380 4.280 1.00 23.91 O ANISOU 1689 O CYS A 200 3448 2678 2958 776 -336 -781 O ATOM 1690 CB CYS A 200 30.373 -14.338 2.970 1.00 29.73 C ANISOU 1690 CB CYS A 200 4306 3410 3579 939 -238 -684 C ATOM 1691 SG CYS A 200 31.492 -13.718 4.246 1.00 35.16 S ANISOU 1691 SG CYS A 200 5007 3985 4366 910 -163 -523 S ATOM 1692 N LYS A 201 28.598 -16.002 5.600 1.00 21.43 N ANISOU 1692 N LYS A 201 3197 2117 2827 653 -258 -783 N ATOM 1693 CA LYS A 201 27.600 -15.855 6.669 1.00 20.58 C ANISOU 1693 CA LYS A 201 3042 1985 2795 561 -259 -766 C ATOM 1694 C LYS A 201 28.230 -15.363 7.949 1.00 23.30 C ANISOU 1694 C LYS A 201 3414 2260 3179 554 -210 -620 C ATOM 1695 O LYS A 201 29.281 -15.866 8.361 1.00 22.39 O ANISOU 1695 O LYS A 201 3357 2055 3095 572 -170 -565 O ATOM 1696 CB LYS A 201 26.890 -17.201 6.929 1.00 22.82 C ANISOU 1696 CB LYS A 201 3316 2168 3186 443 -242 -883 C ATOM 1697 CG LYS A 201 26.428 -17.908 5.642 1.00 27.88 C ANISOU 1697 CG LYS A 201 3928 2865 3801 438 -291 -1073 C ATOM 1698 CD LYS A 201 25.323 -18.952 5.879 1.00 40.79 C ANISOU 1698 CD LYS A 201 5510 4429 5561 289 -279 -1222 C ATOM 1699 CE LYS A 201 23.971 -18.300 6.141 1.00 53.96 C ANISOU 1699 CE LYS A 201 7052 6223 7230 232 -321 -1260 C ATOM 1700 NZ LYS A 201 22.902 -19.291 6.454 1.00 63.46 N ANISOU 1700 NZ LYS A 201 8183 7354 8576 64 -289 -1405 N ATOM 1701 N ALA A 202 27.604 -14.352 8.553 1.00 17.72 N ANISOU 1701 N ALA A 202 2660 1609 2463 544 -220 -569 N ATOM 1702 CA ALA A 202 28.071 -13.746 9.800 1.00 16.07 C ANISOU 1702 CA ALA A 202 2465 1362 2279 537 -184 -458 C ATOM 1703 C ALA A 202 26.985 -13.834 10.841 1.00 20.68 C ANISOU 1703 C ALA A 202 3008 1938 2912 454 -168 -465 C ATOM 1704 O ALA A 202 25.818 -13.621 10.520 1.00 20.57 O ANISOU 1704 O ALA A 202 2924 1993 2896 428 -195 -534 O ATOM 1705 CB ALA A 202 28.457 -12.276 9.567 1.00 15.48 C ANISOU 1705 CB ALA A 202 2378 1353 2150 610 -190 -394 C ATOM 1706 N HIS A 203 27.352 -14.116 12.090 1.00 16.85 N ANISOU 1706 N HIS A 203 2557 1385 2458 423 -122 -393 N ATOM 1707 CA HIS A 203 26.392 -14.106 13.187 1.00 17.37 C ANISOU 1707 CA HIS A 203 2592 1456 2554 352 -87 -380 C ATOM 1708 C HIS A 203 27.095 -13.708 14.493 1.00 20.89 C ANISOU 1708 C HIS A 203 3073 1894 2972 376 -58 -282 C ATOM 1709 O HIS A 203 28.331 -13.577 14.522 1.00 18.34 O ANISOU 1709 O HIS A 203 2789 1557 2622 439 -72 -237 O ATOM 1710 CB HIS A 203 25.668 -15.467 13.320 1.00 19.53 C ANISOU 1710 CB HIS A 203 2872 1645 2904 253 -37 -427 C ATOM 1711 CG HIS A 203 26.501 -16.570 13.872 1.00 23.74 C ANISOU 1711 CG HIS A 203 3504 2047 3470 253 18 -356 C ATOM 1712 ND1 HIS A 203 27.524 -17.157 13.118 1.00 26.70 N ANISOU 1712 ND1 HIS A 203 3939 2359 3847 313 1 -366 N ATOM 1713 CD2 HIS A 203 26.439 -17.183 15.079 1.00 25.96 C ANISOU 1713 CD2 HIS A 203 3838 2252 3774 218 96 -267 C ATOM 1714 CE1 HIS A 203 28.022 -18.123 13.878 1.00 26.05 C ANISOU 1714 CE1 HIS A 203 3941 2157 3801 318 62 -287 C ATOM 1715 NE2 HIS A 203 27.406 -18.183 15.065 1.00 26.90 N ANISOU 1715 NE2 HIS A 203 4053 2250 3915 264 123 -216 N ATOM 1716 N GLY A 204 26.296 -13.528 15.547 1.00 18.76 N ANISOU 1716 N GLY A 204 2777 1650 2703 329 -19 -264 N ATOM 1717 CA GLY A 204 26.775 -13.198 16.885 1.00 18.44 C ANISOU 1717 CA GLY A 204 2765 1629 2613 353 6 -190 C ATOM 1718 C GLY A 204 27.297 -11.775 17.000 1.00 19.78 C ANISOU 1718 C GLY A 204 2904 1871 2742 411 -36 -200 C ATOM 1719 O GLY A 204 27.995 -11.463 17.951 1.00 19.67 O ANISOU 1719 O GLY A 204 2907 1885 2682 441 -37 -166 O ATOM 1720 N PHE A 205 26.969 -10.894 16.065 1.00 15.36 N ANISOU 1720 N PHE A 205 2300 1341 2198 431 -69 -250 N ATOM 1721 CA PHE A 205 27.550 -9.557 16.135 1.00 14.91 C ANISOU 1721 CA PHE A 205 2229 1311 2127 479 -86 -254 C ATOM 1722 C PHE A 205 26.605 -8.482 16.701 1.00 20.02 C ANISOU 1722 C PHE A 205 2828 2006 2774 480 -72 -289 C ATOM 1723 O PHE A 205 25.371 -8.584 16.636 1.00 17.85 O ANISOU 1723 O PHE A 205 2508 1764 2510 459 -61 -318 O ATOM 1724 CB PHE A 205 28.128 -9.104 14.771 1.00 15.59 C ANISOU 1724 CB PHE A 205 2321 1378 2225 526 -110 -257 C ATOM 1725 CG PHE A 205 27.143 -9.092 13.621 1.00 16.49 C ANISOU 1725 CG PHE A 205 2410 1518 2339 544 -130 -288 C ATOM 1726 CD1 PHE A 205 26.397 -7.942 13.328 1.00 16.23 C ANISOU 1726 CD1 PHE A 205 2341 1521 2303 590 -135 -300 C ATOM 1727 CD2 PHE A 205 26.972 -10.222 12.813 1.00 16.93 C ANISOU 1727 CD2 PHE A 205 2474 1566 2392 528 -148 -316 C ATOM 1728 CE1 PHE A 205 25.486 -7.929 12.258 1.00 18.10 C ANISOU 1728 CE1 PHE A 205 2544 1814 2518 633 -170 -330 C ATOM 1729 CE2 PHE A 205 26.071 -10.203 11.736 1.00 18.71 C ANISOU 1729 CE2 PHE A 205 2661 1848 2599 553 -183 -370 C ATOM 1730 CZ PHE A 205 25.309 -9.073 11.485 1.00 17.03 C ANISOU 1730 CZ PHE A 205 2404 1699 2368 610 -200 -373 C ATOM 1731 N TYR A 206 27.237 -7.452 17.279 1.00 16.95 N ANISOU 1731 N TYR A 206 2438 1621 2380 503 -70 -301 N ATOM 1732 CA TYR A 206 26.603 -6.255 17.834 1.00 16.21 C ANISOU 1732 CA TYR A 206 2312 1552 2296 519 -51 -348 C ATOM 1733 C TYR A 206 27.636 -5.128 17.761 1.00 19.85 C ANISOU 1733 C TYR A 206 2783 1967 2791 541 -50 -370 C ATOM 1734 O TYR A 206 28.776 -5.361 18.170 1.00 19.10 O ANISOU 1734 O TYR A 206 2699 1876 2684 523 -63 -371 O ATOM 1735 CB TYR A 206 26.076 -6.446 19.283 1.00 17.04 C ANISOU 1735 CB TYR A 206 2401 1721 2351 491 -21 -368 C ATOM 1736 CG TYR A 206 25.305 -5.225 19.732 1.00 17.63 C ANISOU 1736 CG TYR A 206 2437 1821 2442 519 3 -434 C ATOM 1737 CD1 TYR A 206 25.965 -4.112 20.259 1.00 18.63 C ANISOU 1737 CD1 TYR A 206 2569 1929 2581 537 6 -493 C ATOM 1738 CD2 TYR A 206 23.936 -5.112 19.480 1.00 17.48 C ANISOU 1738 CD2 TYR A 206 2365 1834 2441 532 23 -452 C ATOM 1739 CE1 TYR A 206 25.276 -2.934 20.554 1.00 18.56 C ANISOU 1739 CE1 TYR A 206 2535 1914 2605 573 36 -562 C ATOM 1740 CE2 TYR A 206 23.233 -3.956 19.815 1.00 17.76 C ANISOU 1740 CE2 TYR A 206 2363 1887 2499 581 48 -512 C ATOM 1741 CZ TYR A 206 23.907 -2.876 20.358 1.00 22.87 C ANISOU 1741 CZ TYR A 206 3037 2494 3160 604 58 -564 C ATOM 1742 OH TYR A 206 23.227 -1.729 20.653 1.00 24.62 O ANISOU 1742 OH TYR A 206 3231 2706 3416 660 90 -632 O ATOM 1743 N PRO A 207 27.307 -3.918 17.247 1.00 17.74 N ANISOU 1743 N PRO A 207 2510 1653 2576 581 -29 -387 N ATOM 1744 CA PRO A 207 25.979 -3.442 16.795 1.00 17.61 C ANISOU 1744 CA PRO A 207 2471 1649 2572 634 -20 -390 C ATOM 1745 C PRO A 207 25.514 -4.101 15.498 1.00 19.75 C ANISOU 1745 C PRO A 207 2739 1941 2823 667 -51 -343 C ATOM 1746 O PRO A 207 26.325 -4.752 14.832 1.00 18.38 O ANISOU 1746 O PRO A 207 2598 1749 2638 652 -67 -307 O ATOM 1747 CB PRO A 207 26.178 -1.918 16.655 1.00 19.94 C ANISOU 1747 CB PRO A 207 2785 1857 2934 683 20 -407 C ATOM 1748 CG PRO A 207 27.651 -1.757 16.387 1.00 23.77 C ANISOU 1748 CG PRO A 207 3304 2273 3455 645 34 -392 C ATOM 1749 CD PRO A 207 28.302 -2.825 17.226 1.00 19.45 C ANISOU 1749 CD PRO A 207 2739 1796 2854 579 -2 -414 C ATOM 1750 N PRO A 208 24.204 -3.980 15.144 1.00 18.52 N ANISOU 1750 N PRO A 208 2534 1843 2661 715 -65 -360 N ATOM 1751 CA PRO A 208 23.714 -4.620 13.902 1.00 19.13 C ANISOU 1751 CA PRO A 208 2591 1971 2706 749 -111 -346 C ATOM 1752 C PRO A 208 24.370 -4.095 12.614 1.00 23.58 C ANISOU 1752 C PRO A 208 3213 2494 3253 831 -117 -282 C ATOM 1753 O PRO A 208 24.437 -4.851 11.654 1.00 25.84 O ANISOU 1753 O PRO A 208 3503 2822 3494 841 -154 -276 O ATOM 1754 CB PRO A 208 22.200 -4.308 13.913 1.00 20.64 C ANISOU 1754 CB PRO A 208 2694 2252 2896 801 -127 -393 C ATOM 1755 CG PRO A 208 22.067 -3.092 14.772 1.00 24.62 C ANISOU 1755 CG PRO A 208 3203 2714 3438 841 -80 -403 C ATOM 1756 CD PRO A 208 23.108 -3.263 15.843 1.00 19.37 C ANISOU 1756 CD PRO A 208 2587 1989 2784 750 -44 -408 C ATOM 1757 N GLU A 209 24.853 -2.839 12.573 1.00 20.25 N ANISOU 1757 N GLU A 209 2839 1988 2868 886 -68 -239 N ATOM 1758 CA GLU A 209 25.498 -2.283 11.367 1.00 19.99 C ANISOU 1758 CA GLU A 209 2871 1903 2820 963 -43 -155 C ATOM 1759 C GLU A 209 26.726 -3.129 10.956 1.00 23.44 C ANISOU 1759 C GLU A 209 3342 2325 3238 900 -39 -135 C ATOM 1760 O GLU A 209 27.650 -3.291 11.741 1.00 21.17 O ANISOU 1760 O GLU A 209 3058 1989 2996 813 -15 -157 O ATOM 1761 CB GLU A 209 25.908 -0.814 11.586 1.00 21.68 C ANISOU 1761 CB GLU A 209 3137 1987 3112 1001 40 -115 C ATOM 1762 CG GLU A 209 24.739 0.163 11.788 1.00 33.79 C ANISOU 1762 CG GLU A 209 4655 3515 4669 1105 48 -121 C ATOM 1763 CD GLU A 209 23.893 0.026 13.047 1.00 47.17 C ANISOU 1763 CD GLU A 209 6273 5265 6384 1061 26 -223 C ATOM 1764 OE1 GLU A 209 24.430 -0.390 14.100 1.00 24.85 O ANISOU 1764 OE1 GLU A 209 3431 2431 3578 943 33 -286 O ATOM 1765 OE2 GLU A 209 22.676 0.310 12.970 1.00 44.17 O ANISOU 1765 OE2 GLU A 209 5842 4953 5988 1155 1 -239 O ATOM 1766 N ILE A 210 26.722 -3.668 9.728 1.00 20.32 N ANISOU 1766 N ILE A 210 2964 1989 2766 955 -68 -105 N ATOM 1767 CA ILE A 210 27.794 -4.505 9.183 1.00 18.81 C ANISOU 1767 CA ILE A 210 2802 1796 2548 918 -62 -93 C ATOM 1768 C ILE A 210 27.817 -4.323 7.663 1.00 24.67 C ANISOU 1768 C ILE A 210 3588 2587 3200 1030 -57 -30 C ATOM 1769 O ILE A 210 26.772 -4.088 7.061 1.00 25.47 O ANISOU 1769 O ILE A 210 3674 2769 3233 1128 -102 -27 O ATOM 1770 CB ILE A 210 27.586 -6.009 9.587 1.00 19.52 C ANISOU 1770 CB ILE A 210 2853 1937 2627 838 -121 -174 C ATOM 1771 CG1 ILE A 210 28.875 -6.854 9.375 1.00 17.84 C ANISOU 1771 CG1 ILE A 210 2671 1695 2414 798 -104 -169 C ATOM 1772 CG2 ILE A 210 26.340 -6.647 8.880 1.00 19.75 C ANISOU 1772 CG2 ILE A 210 2838 2074 2593 875 -192 -233 C ATOM 1773 CD1 ILE A 210 28.908 -8.213 10.169 1.00 16.61 C ANISOU 1773 CD1 ILE A 210 2498 1532 2281 716 -133 -225 C ATOM 1774 N TYR A 211 28.993 -4.432 7.063 1.00 21.15 N ANISOU 1774 N TYR A 211 3187 2108 2741 1026 -2 17 N ATOM 1775 CA TYR A 211 29.178 -4.363 5.616 1.00 22.37 C ANISOU 1775 CA TYR A 211 3393 2321 2787 1134 19 82 C ATOM 1776 C TYR A 211 29.847 -5.676 5.184 1.00 23.17 C ANISOU 1776 C TYR A 211 3487 2473 2843 1095 -6 21 C ATOM 1777 O TYR A 211 30.883 -6.045 5.734 1.00 21.15 O ANISOU 1777 O TYR A 211 3223 2154 2659 1011 31 7 O ATOM 1778 CB TYR A 211 30.007 -3.120 5.237 1.00 27.91 C ANISOU 1778 CB TYR A 211 4160 2921 3521 1172 147 209 C ATOM 1779 CG TYR A 211 30.467 -3.081 3.794 1.00 36.71 C ANISOU 1779 CG TYR A 211 5340 4092 4517 1276 202 299 C ATOM 1780 CD1 TYR A 211 29.585 -2.751 2.766 1.00 40.60 C ANISOU 1780 CD1 TYR A 211 5874 4685 4868 1437 172 361 C ATOM 1781 CD2 TYR A 211 31.789 -3.360 3.457 1.00 39.99 C ANISOU 1781 CD2 TYR A 211 5770 4480 4947 1227 286 321 C ATOM 1782 CE1 TYR A 211 30.006 -2.713 1.434 1.00 43.87 C ANISOU 1782 CE1 TYR A 211 6357 5172 5141 1549 227 450 C ATOM 1783 CE2 TYR A 211 32.222 -3.318 2.130 1.00 43.38 C ANISOU 1783 CE2 TYR A 211 6260 4971 5251 1326 354 407 C ATOM 1784 CZ TYR A 211 31.327 -2.991 1.123 1.00 52.66 C ANISOU 1784 CZ TYR A 211 7492 6248 6271 1489 326 476 C ATOM 1785 OH TYR A 211 31.758 -2.959 -0.184 1.00 58.23 O ANISOU 1785 OH TYR A 211 8265 7034 6824 1602 397 566 O ATOM 1786 N MET A 212 29.187 -6.422 4.301 1.00 19.08 N ANISOU 1786 N MET A 212 2962 2074 2213 1157 -79 -36 N ATOM 1787 CA MET A 212 29.680 -7.700 3.789 1.00 20.81 C ANISOU 1787 CA MET A 212 3181 2337 2388 1134 -104 -117 C ATOM 1788 C MET A 212 29.691 -7.614 2.294 1.00 26.68 C ANISOU 1788 C MET A 212 3967 3195 2974 1263 -100 -91 C ATOM 1789 O MET A 212 28.729 -7.117 1.711 1.00 27.55 O ANISOU 1789 O MET A 212 4076 3405 2988 1366 -148 -75 O ATOM 1790 CB MET A 212 28.812 -8.891 4.248 1.00 22.80 C ANISOU 1790 CB MET A 212 3375 2619 2669 1060 -197 -257 C ATOM 1791 CG MET A 212 28.579 -8.957 5.739 1.00 25.67 C ANISOU 1791 CG MET A 212 3701 2892 3159 950 -198 -269 C ATOM 1792 SD MET A 212 27.550 -10.371 6.173 1.00 30.11 S ANISOU 1792 SD MET A 212 4206 3473 3763 855 -270 -413 S ATOM 1793 CE MET A 212 28.756 -11.743 5.945 1.00 25.78 C ANISOU 1793 CE MET A 212 3709 2851 3236 819 -242 -455 C ATOM 1794 N THR A 213 30.766 -8.057 1.663 1.00 24.19 N ANISOU 1794 N THR A 213 3688 2884 2619 1276 -41 -83 N ATOM 1795 CA THR A 213 30.847 -8.014 0.199 1.00 25.36 C ANISOU 1795 CA THR A 213 3885 3160 2589 1410 -26 -58 C ATOM 1796 C THR A 213 31.788 -9.082 -0.310 1.00 28.33 C ANISOU 1796 C THR A 213 4272 3558 2935 1396 0 -135 C ATOM 1797 O THR A 213 32.623 -9.595 0.444 1.00 28.57 O ANISOU 1797 O THR A 213 4281 3482 3091 1299 35 -160 O ATOM 1798 CB THR A 213 31.271 -6.614 -0.313 1.00 32.04 C ANISOU 1798 CB THR A 213 4801 3986 3389 1503 93 131 C ATOM 1799 OG1 THR A 213 31.012 -6.567 -1.723 1.00 35.99 O ANISOU 1799 OG1 THR A 213 5352 4646 3675 1664 87 161 O ATOM 1800 CG2 THR A 213 32.757 -6.294 -0.055 1.00 33.27 C ANISOU 1800 CG2 THR A 213 4975 4021 3647 1432 239 213 C ATOM 1801 N TRP A 214 31.668 -9.387 -1.601 1.00 23.59 N ANISOU 1801 N TRP A 214 3703 3104 2155 1511 -17 -173 N ATOM 1802 CA TRP A 214 32.516 -10.344 -2.276 1.00 24.40 C ANISOU 1802 CA TRP A 214 3824 3247 2201 1528 16 -255 C ATOM 1803 C TRP A 214 33.456 -9.602 -3.202 1.00 30.88 C ANISOU 1803 C TRP A 214 4708 4117 2909 1629 154 -111 C ATOM 1804 O TRP A 214 33.060 -8.648 -3.871 1.00 31.83 O ANISOU 1804 O TRP A 214 4877 4318 2900 1743 182 10 O ATOM 1805 CB TRP A 214 31.672 -11.368 -3.038 1.00 23.56 C ANISOU 1805 CB TRP A 214 3699 3279 1973 1573 -105 -446 C ATOM 1806 CG TRP A 214 31.167 -12.464 -2.147 1.00 23.13 C ANISOU 1806 CG TRP A 214 3587 3131 2071 1438 -191 -607 C ATOM 1807 CD1 TRP A 214 29.947 -12.537 -1.538 1.00 25.05 C ANISOU 1807 CD1 TRP A 214 3769 3372 2378 1373 -289 -677 C ATOM 1808 CD2 TRP A 214 31.928 -13.588 -1.668 1.00 21.96 C ANISOU 1808 CD2 TRP A 214 3439 2859 2047 1353 -162 -694 C ATOM 1809 NE1 TRP A 214 29.879 -13.666 -0.752 1.00 24.01 N ANISOU 1809 NE1 TRP A 214 3608 3117 2397 1242 -312 -798 N ATOM 1810 CE2 TRP A 214 31.078 -14.340 -0.829 1.00 25.23 C ANISOU 1810 CE2 TRP A 214 3807 3190 2588 1238 -240 -807 C ATOM 1811 CE3 TRP A 214 33.242 -14.039 -1.886 1.00 22.61 C ANISOU 1811 CE3 TRP A 214 3554 2894 2145 1374 -71 -683 C ATOM 1812 CZ2 TRP A 214 31.482 -15.548 -0.247 1.00 23.63 C ANISOU 1812 CZ2 TRP A 214 3612 2847 2521 1153 -226 -898 C ATOM 1813 CZ3 TRP A 214 33.645 -15.226 -1.301 1.00 23.67 C ANISOU 1813 CZ3 TRP A 214 3682 2901 2410 1302 -73 -784 C ATOM 1814 CH2 TRP A 214 32.786 -15.943 -0.452 1.00 24.09 C ANISOU 1814 CH2 TRP A 214 3711 2855 2589 1195 -146 -875 C ATOM 1815 N MET A 215 34.702 -10.015 -3.213 1.00 29.55 N ANISOU 1815 N MET A 215 4536 3897 2793 1595 249 -113 N ATOM 1816 CA MET A 215 35.704 -9.430 -4.081 1.00 33.01 C ANISOU 1816 CA MET A 215 5021 4383 3140 1672 406 13 C ATOM 1817 C MET A 215 36.371 -10.549 -4.895 1.00 35.97 C ANISOU 1817 C MET A 215 5398 4850 3418 1725 425 -112 C ATOM 1818 O MET A 215 36.356 -11.708 -4.495 1.00 32.75 O ANISOU 1818 O MET A 215 4952 4404 3086 1670 343 -276 O ATOM 1819 CB MET A 215 36.701 -8.572 -3.297 1.00 36.43 C ANISOU 1819 CB MET A 215 5426 4666 3748 1575 540 146 C ATOM 1820 CG MET A 215 36.060 -7.274 -2.796 1.00 43.38 C ANISOU 1820 CG MET A 215 6330 5466 4689 1558 553 280 C ATOM 1821 SD MET A 215 37.266 -6.145 -2.094 1.00 51.26 S ANISOU 1821 SD MET A 215 7296 6296 5884 1443 732 416 S ATOM 1822 CE MET A 215 37.309 -4.918 -3.362 1.00 50.27 C ANISOU 1822 CE MET A 215 7283 6205 5611 1573 903 630 C ATOM 1823 N LYS A 216 36.864 -10.199 -6.070 1.00 35.79 N ANISOU 1823 N LYS A 216 5431 4950 3219 1844 537 -34 N ATOM 1824 CA LYS A 216 37.455 -11.146 -7.008 1.00 39.88 C ANISOU 1824 CA LYS A 216 5960 5586 3606 1922 568 -152 C ATOM 1825 C LYS A 216 38.862 -10.688 -7.321 1.00 48.86 C ANISOU 1825 C LYS A 216 7095 6711 4761 1930 775 -24 C ATOM 1826 O LYS A 216 39.083 -9.502 -7.601 1.00 48.47 O ANISOU 1826 O LYS A 216 7085 6657 4674 1957 906 175 O ATOM 1827 CB LYS A 216 36.564 -11.167 -8.264 1.00 44.44 C ANISOU 1827 CB LYS A 216 6604 6380 3902 2083 501 -195 C ATOM 1828 CG LYS A 216 36.948 -12.088 -9.407 1.00 69.24 C ANISOU 1828 CG LYS A 216 9770 9687 6852 2193 516 -343 C ATOM 1829 CD LYS A 216 35.853 -12.030 -10.492 1.00 79.73 C ANISOU 1829 CD LYS A 216 11147 11250 7895 2350 408 -404 C ATOM 1830 CE LYS A 216 35.781 -10.728 -11.267 1.00 89.31 C ANISOU 1830 CE LYS A 216 12446 12585 8904 2499 512 -155 C ATOM 1831 NZ LYS A 216 34.478 -10.577 -11.965 1.00 96.54 N ANISOU 1831 NZ LYS A 216 13386 13712 9582 2646 356 -206 N ATOM 1832 N ASN A 217 39.814 -11.627 -7.245 1.00 50.63 N ANISOU 1832 N ASN A 217 7266 6916 5056 1906 812 -139 N ATOM 1833 CA ASN A 217 41.245 -11.427 -7.516 1.00 53.80 C ANISOU 1833 CA ASN A 217 7628 7322 5491 1908 1005 -63 C ATOM 1834 C ASN A 217 41.789 -10.185 -6.766 1.00 62.18 C ANISOU 1834 C ASN A 217 8645 8256 6726 1797 1124 122 C ATOM 1835 O ASN A 217 42.499 -9.363 -7.349 1.00 64.35 O ANISOU 1835 O ASN A 217 8929 8561 6958 1817 1314 270 O ATOM 1836 CB ASN A 217 41.512 -11.329 -9.037 1.00 58.16 C ANISOU 1836 CB ASN A 217 8252 8069 5776 2065 1127 -25 C ATOM 1837 CG ASN A 217 40.738 -12.311 -9.895 1.00 80.17 C ANISOU 1837 CG ASN A 217 11096 11012 8352 2186 995 -213 C ATOM 1838 OD1 ASN A 217 40.016 -11.919 -10.819 1.00 80.54 O ANISOU 1838 OD1 ASN A 217 11225 11216 8160 2308 975 -171 O ATOM 1839 ND2 ASN A 217 40.872 -13.604 -9.621 1.00 65.07 N ANISOU 1839 ND2 ASN A 217 9141 9061 6521 2162 905 -431 N ATOM 1840 N GLY A 218 41.380 -10.045 -5.503 1.00 59.27 N ANISOU 1840 N GLY A 218 8231 7745 6545 1679 1016 107 N ATOM 1841 CA GLY A 218 41.809 -8.979 -4.610 1.00 59.28 C ANISOU 1841 CA GLY A 218 8177 7613 6734 1556 1095 228 C ATOM 1842 C GLY A 218 40.982 -7.713 -4.506 1.00 64.66 C ANISOU 1842 C GLY A 218 8926 8232 7409 1543 1109 377 C ATOM 1843 O GLY A 218 40.303 -7.509 -3.492 1.00 63.72 O ANISOU 1843 O GLY A 218 8791 8015 7407 1466 995 354 O ATOM 1844 N GLU A 219 41.093 -6.813 -5.517 1.00 63.00 N ANISOU 1844 N GLU A 219 8796 8070 7071 1622 1268 542 N ATOM 1845 CA GLU A 219 40.501 -5.465 -5.480 1.00 62.95 C ANISOU 1845 CA GLU A 219 8866 7975 7077 1625 1330 718 C ATOM 1846 C GLU A 219 39.219 -5.213 -6.325 1.00 64.62 C ANISOU 1846 C GLU A 219 9204 8295 7053 1796 1252 788 C ATOM 1847 O GLU A 219 38.707 -4.088 -6.280 1.00 65.96 O ANISOU 1847 O GLU A 219 9443 8382 7236 1822 1304 944 O ATOM 1848 CB GLU A 219 41.566 -4.438 -5.903 1.00 66.30 C ANISOU 1848 CB GLU A 219 9297 8334 7558 1587 1596 893 C ATOM 1849 N GLU A 220 38.676 -6.210 -7.041 1.00 57.69 N ANISOU 1849 N GLU A 220 8350 7596 5972 1914 1125 664 N ATOM 1850 CA GLU A 220 37.457 -5.959 -7.826 1.00 56.99 C ANISOU 1850 CA GLU A 220 8356 7645 5653 2083 1033 709 C ATOM 1851 C GLU A 220 36.192 -6.470 -7.108 1.00 54.77 C ANISOU 1851 C GLU A 220 8030 7366 5415 2055 793 553 C ATOM 1852 O GLU A 220 36.111 -7.659 -6.816 1.00 50.25 O ANISOU 1852 O GLU A 220 7390 6824 4878 1998 669 348 O ATOM 1853 CB GLU A 220 37.570 -6.600 -9.222 1.00 60.18 C ANISOU 1853 CB GLU A 220 8815 8283 5769 2250 1049 664 C ATOM 1854 N ILE A 221 35.194 -5.584 -6.837 1.00 51.95 N ANISOU 1854 N ILE A 221 7706 6970 5060 2098 740 651 N ATOM 1855 CA ILE A 221 33.934 -6.042 -6.226 1.00 49.91 C ANISOU 1855 CA ILE A 221 7392 6740 4833 2078 525 502 C ATOM 1856 C ILE A 221 33.166 -6.794 -7.324 1.00 51.40 C ANISOU 1856 C ILE A 221 7593 7179 4758 2232 393 378 C ATOM 1857 O ILE A 221 33.162 -6.377 -8.473 1.00 54.28 O ANISOU 1857 O ILE A 221 8041 7695 4889 2408 453 486 O ATOM 1858 CB ILE A 221 33.065 -4.948 -5.514 1.00 53.74 C ANISOU 1858 CB ILE A 221 7887 7117 5414 2078 497 612 C ATOM 1859 CG1 ILE A 221 33.872 -4.175 -4.432 1.00 53.73 C ANISOU 1859 CG1 ILE A 221 7869 6870 5674 1919 630 706 C ATOM 1860 CG2 ILE A 221 31.803 -5.585 -4.884 1.00 53.97 C ANISOU 1860 CG2 ILE A 221 7831 7197 5478 2044 283 432 C ATOM 1861 CD1 ILE A 221 33.207 -2.854 -3.867 1.00 60.56 C ANISOU 1861 CD1 ILE A 221 8772 7601 6636 1938 659 843 C ATOM 1862 N VAL A 222 32.608 -7.941 -6.964 1.00 43.91 N ANISOU 1862 N VAL A 222 6562 6271 3851 2158 228 143 N ATOM 1863 CA VAL A 222 31.860 -8.872 -7.797 1.00 43.43 C ANISOU 1863 CA VAL A 222 6477 6427 3597 2250 79 -55 C ATOM 1864 C VAL A 222 30.444 -8.344 -8.032 1.00 46.85 C ANISOU 1864 C VAL A 222 6893 7001 3906 2370 -59 -49 C ATOM 1865 O VAL A 222 29.829 -7.786 -7.116 1.00 43.65 O ANISOU 1865 O VAL A 222 6449 6484 3651 2308 -97 3 O ATOM 1866 CB VAL A 222 31.829 -10.255 -7.082 1.00 46.06 C ANISOU 1866 CB VAL A 222 6722 6680 4098 2083 -20 -303 C ATOM 1867 CG1 VAL A 222 31.049 -11.295 -7.882 1.00 47.90 C ANISOU 1867 CG1 VAL A 222 6917 7110 4172 2143 -170 -551 C ATOM 1868 CG2 VAL A 222 33.243 -10.756 -6.776 1.00 44.57 C ANISOU 1868 CG2 VAL A 222 6542 6354 4039 1989 110 -300 C ATOM 1869 N GLN A 223 29.925 -8.561 -9.250 1.00 46.17 N ANISOU 1869 N GLN A 223 6824 7178 3539 2549 -140 -120 N ATOM 1870 CA GLN A 223 28.560 -8.219 -9.654 1.00 47.23 C ANISOU 1870 CA GLN A 223 6919 7515 3512 2697 -300 -155 C ATOM 1871 C GLN A 223 27.591 -9.362 -9.285 1.00 50.97 C ANISOU 1871 C GLN A 223 7249 8056 4063 2582 -499 -469 C ATOM 1872 O GLN A 223 28.014 -10.521 -9.159 1.00 49.26 O ANISOU 1872 O GLN A 223 6997 7785 3934 2446 -511 -667 O ATOM 1873 CB GLN A 223 28.492 -7.951 -11.170 1.00 51.31 C ANISOU 1873 CB GLN A 223 7514 8317 3663 2960 -301 -95 C ATOM 1874 CG GLN A 223 29.332 -6.763 -11.680 1.00 61.31 C ANISOU 1874 CG GLN A 223 8936 9533 4824 3098 -84 240 C ATOM 1875 CD GLN A 223 28.994 -5.407 -11.079 1.00 72.50 C ANISOU 1875 CD GLN A 223 10401 10791 6353 3137 -15 497 C ATOM 1876 OE1 GLN A 223 28.076 -5.241 -10.263 1.00 71.56 O ANISOU 1876 OE1 GLN A 223 10198 10616 6377 3082 -135 439 O ATOM 1877 NE2 GLN A 223 29.765 -4.405 -11.448 1.00 54.25 N ANISOU 1877 NE2 GLN A 223 8227 8389 3996 3224 198 783 N ATOM 1878 N GLU A 224 26.291 -9.033 -9.142 1.00 47.63 N ANISOU 1878 N GLU A 224 6740 7749 3610 2641 -646 -516 N ATOM 1879 CA GLU A 224 25.197 -9.979 -8.876 1.00 46.91 C ANISOU 1879 CA GLU A 224 6491 7752 3582 2541 -832 -813 C ATOM 1880 C GLU A 224 25.342 -10.664 -7.494 1.00 46.80 C ANISOU 1880 C GLU A 224 6415 7464 3904 2264 -804 -905 C ATOM 1881 O GLU A 224 25.084 -11.860 -7.367 1.00 46.76 O ANISOU 1881 O GLU A 224 6328 7455 3982 2127 -879 -1160 O ATOM 1882 CB GLU A 224 25.085 -11.035 -10.015 1.00 49.92 C ANISOU 1882 CB GLU A 224 6837 8376 3756 2602 -937 -1077 C ATOM 1883 N ILE A 225 25.733 -9.896 -6.460 1.00 39.88 N ANISOU 1883 N ILE A 225 5581 6358 3213 2188 -693 -700 N ATOM 1884 CA ILE A 225 25.795 -10.416 -5.101 1.00 36.90 C ANISOU 1884 CA ILE A 225 5151 5750 3121 1957 -671 -761 C ATOM 1885 C ILE A 225 24.365 -10.391 -4.541 1.00 40.92 C ANISOU 1885 C ILE A 225 5524 6323 3701 1915 -799 -871 C ATOM 1886 O ILE A 225 23.662 -9.400 -4.728 1.00 43.38 O ANISOU 1886 O ILE A 225 5817 6746 3919 2059 -841 -767 O ATOM 1887 CB ILE A 225 26.768 -9.609 -4.171 1.00 38.27 C ANISOU 1887 CB ILE A 225 5406 5677 3456 1890 -512 -529 C ATOM 1888 CG1 ILE A 225 28.207 -9.496 -4.747 1.00 39.07 C ANISOU 1888 CG1 ILE A 225 5621 5729 3495 1934 -368 -408 C ATOM 1889 CG2 ILE A 225 26.797 -10.168 -2.701 1.00 35.42 C ANISOU 1889 CG2 ILE A 225 4989 5104 3363 1670 -500 -592 C ATOM 1890 CD1 ILE A 225 29.153 -8.494 -3.846 1.00 39.52 C ANISOU 1890 CD1 ILE A 225 5738 5559 3720 1868 -208 -182 C ATOM 1891 N ASP A 226 23.942 -11.449 -3.861 1.00 33.71 N ANISOU 1891 N ASP A 226 4516 5336 2956 1726 -849 -1069 N ATOM 1892 CA ASP A 226 22.674 -11.455 -3.145 1.00 31.90 C ANISOU 1892 CA ASP A 226 4148 5136 2837 1649 -936 -1166 C ATOM 1893 C ASP A 226 23.002 -11.206 -1.695 1.00 32.01 C ANISOU 1893 C ASP A 226 4187 4898 3078 1502 -833 -1040 C ATOM 1894 O ASP A 226 24.064 -11.620 -1.231 1.00 28.49 O ANISOU 1894 O ASP A 226 3825 4267 2735 1404 -733 -989 O ATOM 1895 CB ASP A 226 21.920 -12.776 -3.322 1.00 34.29 C ANISOU 1895 CB ASP A 226 4323 5518 3188 1521 -1039 -1471 C ATOM 1896 CG ASP A 226 21.258 -12.903 -4.667 1.00 45.52 C ANISOU 1896 CG ASP A 226 5672 7248 4376 1674 -1181 -1639 C ATOM 1897 OD1 ASP A 226 20.494 -11.983 -5.039 1.00 48.54 O ANISOU 1897 OD1 ASP A 226 5998 7827 4617 1845 -1263 -1576 O ATOM 1898 OD2 ASP A 226 21.455 -13.941 -5.323 1.00 49.95 O ANISOU 1898 OD2 ASP A 226 6225 7858 4895 1628 -1217 -1847 O ATOM 1899 N TYR A 227 22.136 -10.505 -0.989 1.00 28.58 N ANISOU 1899 N TYR A 227 3677 4470 2710 1503 -856 -992 N ATOM 1900 CA TYR A 227 22.388 -10.198 0.420 1.00 27.84 C ANISOU 1900 CA TYR A 227 3605 4163 2811 1377 -763 -882 C ATOM 1901 C TYR A 227 21.298 -10.722 1.289 1.00 32.89 C ANISOU 1901 C TYR A 227 4107 4800 3589 1236 -806 -1020 C ATOM 1902 O TYR A 227 20.126 -10.748 0.907 1.00 34.81 O ANISOU 1902 O TYR A 227 4217 5226 3782 1277 -911 -1149 O ATOM 1903 CB TYR A 227 22.526 -8.688 0.642 1.00 29.34 C ANISOU 1903 CB TYR A 227 3858 4318 2973 1506 -705 -664 C ATOM 1904 CG TYR A 227 23.681 -8.058 -0.106 1.00 30.49 C ANISOU 1904 CG TYR A 227 4146 4430 3010 1625 -621 -496 C ATOM 1905 CD1 TYR A 227 24.979 -8.119 0.397 1.00 31.11 C ANISOU 1905 CD1 TYR A 227 4316 4318 3186 1531 -502 -406 C ATOM 1906 CD2 TYR A 227 23.475 -7.376 -1.300 1.00 31.74 C ANISOU 1906 CD2 TYR A 227 4342 4754 2965 1838 -653 -421 C ATOM 1907 CE1 TYR A 227 26.045 -7.528 -0.277 1.00 30.65 C ANISOU 1907 CE1 TYR A 227 4370 4229 3045 1623 -406 -258 C ATOM 1908 CE2 TYR A 227 24.533 -6.772 -1.979 1.00 32.27 C ANISOU 1908 CE2 TYR A 227 4544 4780 2935 1942 -546 -249 C ATOM 1909 CZ TYR A 227 25.819 -6.860 -1.467 1.00 36.40 C ANISOU 1909 CZ TYR A 227 5144 5107 3579 1821 -417 -174 C ATOM 1910 OH TYR A 227 26.887 -6.311 -2.136 1.00 38.52 O ANISOU 1910 OH TYR A 227 5528 5338 3770 1902 -296 -17 O ATOM 1911 N GLY A 228 21.695 -11.171 2.451 1.00 28.93 N ANISOU 1911 N GLY A 228 3631 4103 3258 1071 -723 -996 N ATOM 1912 CA GLY A 228 20.753 -11.605 3.459 1.00 29.27 C ANISOU 1912 CA GLY A 228 3562 4113 3445 926 -723 -1088 C ATOM 1913 C GLY A 228 20.613 -10.436 4.396 1.00 31.48 C ANISOU 1913 C GLY A 228 3851 4341 3768 965 -673 -935 C ATOM 1914 O GLY A 228 21.623 -9.869 4.818 1.00 31.46 O ANISOU 1914 O GLY A 228 3965 4208 3782 986 -593 -781 O ATOM 1915 N ASP A 229 19.372 -10.060 4.718 1.00 26.26 N ANISOU 1915 N ASP A 229 3057 3788 3131 977 -717 -992 N ATOM 1916 CA ASP A 229 19.081 -8.958 5.628 1.00 24.23 C ANISOU 1916 CA ASP A 229 2795 3492 2920 1020 -670 -876 C ATOM 1917 C ASP A 229 19.795 -9.113 6.953 1.00 25.22 C ANISOU 1917 C ASP A 229 2997 3417 3168 885 -559 -797 C ATOM 1918 O ASP A 229 20.010 -10.239 7.413 1.00 22.99 O ANISOU 1918 O ASP A 229 2720 3050 2967 732 -523 -858 O ATOM 1919 CB ASP A 229 17.573 -8.913 5.906 1.00 27.24 C ANISOU 1919 CB ASP A 229 2991 4021 3339 1010 -726 -997 C ATOM 1920 CG ASP A 229 16.716 -8.412 4.766 1.00 37.48 C ANISOU 1920 CG ASP A 229 4187 5553 4500 1195 -849 -1058 C ATOM 1921 OD1 ASP A 229 17.287 -7.930 3.757 1.00 37.60 O ANISOU 1921 OD1 ASP A 229 4300 5613 4373 1356 -883 -973 O ATOM 1922 OD2 ASP A 229 15.470 -8.494 4.883 1.00 42.24 O ANISOU 1922 OD2 ASP A 229 4609 6309 5132 1186 -909 -1187 O ATOM 1923 N ILE A 230 20.065 -7.982 7.622 1.00 22.36 N ANISOU 1923 N ILE A 230 2688 2985 2823 946 -504 -670 N ATOM 1924 CA ILE A 230 20.612 -8.007 8.969 1.00 21.28 C ANISOU 1924 CA ILE A 230 2604 2700 2782 835 -413 -612 C ATOM 1925 C ILE A 230 19.419 -8.329 9.868 1.00 24.07 C ANISOU 1925 C ILE A 230 2831 3105 3209 745 -402 -699 C ATOM 1926 O ILE A 230 18.465 -7.555 9.914 1.00 23.06 O ANISOU 1926 O ILE A 230 2614 3076 3072 826 -426 -719 O ATOM 1927 CB ILE A 230 21.323 -6.685 9.315 1.00 24.15 C ANISOU 1927 CB ILE A 230 3058 2977 3143 923 -360 -482 C ATOM 1928 CG1 ILE A 230 22.518 -6.430 8.327 1.00 23.45 C ANISOU 1928 CG1 ILE A 230 3081 2839 2989 997 -350 -396 C ATOM 1929 CG2 ILE A 230 21.778 -6.676 10.794 1.00 23.32 C ANISOU 1929 CG2 ILE A 230 2982 2758 3119 815 -283 -454 C ATOM 1930 CD1 ILE A 230 22.961 -4.889 8.258 1.00 25.51 C ANISOU 1930 CD1 ILE A 230 3418 3030 3246 1115 -295 -271 C ATOM 1931 N LEU A 231 19.437 -9.509 10.512 1.00 20.86 N ANISOU 1931 N LEU A 231 2415 2635 2876 584 -357 -749 N ATOM 1932 CA LEU A 231 18.281 -9.953 11.296 1.00 21.00 C ANISOU 1932 CA LEU A 231 2308 2701 2969 478 -323 -832 C ATOM 1933 C LEU A 231 18.615 -10.158 12.763 1.00 22.47 C ANISOU 1933 C LEU A 231 2551 2774 3212 379 -215 -760 C ATOM 1934 O LEU A 231 19.720 -10.628 13.075 1.00 20.43 O ANISOU 1934 O LEU A 231 2415 2393 2954 342 -178 -688 O ATOM 1935 CB LEU A 231 17.736 -11.282 10.702 1.00 22.38 C ANISOU 1935 CB LEU A 231 2402 2910 3192 361 -349 -975 C ATOM 1936 CG LEU A 231 17.152 -11.198 9.288 1.00 27.40 C ANISOU 1936 CG LEU A 231 2941 3712 3757 452 -471 -1092 C ATOM 1937 CD1 LEU A 231 16.906 -12.580 8.710 1.00 28.95 C ANISOU 1937 CD1 LEU A 231 3084 3909 4008 320 -492 -1252 C ATOM 1938 CD2 LEU A 231 15.850 -10.381 9.286 1.00 29.27 C ANISOU 1938 CD2 LEU A 231 3011 4129 3980 533 -520 -1152 C ATOM 1939 N PRO A 232 17.644 -9.876 13.672 1.00 21.19 N ANISOU 1939 N PRO A 232 2293 2670 3088 344 -164 -786 N ATOM 1940 CA PRO A 232 17.886 -10.141 15.099 1.00 20.35 C ANISOU 1940 CA PRO A 232 2241 2483 3009 257 -55 -719 C ATOM 1941 C PRO A 232 17.884 -11.648 15.384 1.00 22.90 C ANISOU 1941 C PRO A 232 2581 2720 3398 99 14 -733 C ATOM 1942 O PRO A 232 16.942 -12.343 15.008 1.00 23.46 O ANISOU 1942 O PRO A 232 2538 2838 3539 7 20 -840 O ATOM 1943 CB PRO A 232 16.708 -9.436 15.788 1.00 22.47 C ANISOU 1943 CB PRO A 232 2383 2861 3292 274 -17 -762 C ATOM 1944 CG PRO A 232 15.585 -9.522 14.771 1.00 26.97 C ANISOU 1944 CG PRO A 232 2790 3567 3889 290 -90 -887 C ATOM 1945 CD PRO A 232 16.263 -9.368 13.438 1.00 22.41 C ANISOU 1945 CD PRO A 232 2276 2985 3253 389 -200 -882 C ATOM 1946 N SER A 233 18.921 -12.147 16.050 1.00 19.07 N ANISOU 1946 N SER A 233 2234 2111 2900 70 69 -631 N ATOM 1947 CA SER A 233 18.997 -13.577 16.400 1.00 20.03 C ANISOU 1947 CA SER A 233 2402 2118 3089 -59 154 -613 C ATOM 1948 C SER A 233 18.135 -13.899 17.634 1.00 23.47 C ANISOU 1948 C SER A 233 2792 2564 3563 -159 285 -588 C ATOM 1949 O SER A 233 17.827 -15.071 17.873 1.00 23.97 O ANISOU 1949 O SER A 233 2864 2535 3710 -288 381 -588 O ATOM 1950 CB SER A 233 20.442 -13.994 16.623 1.00 22.72 C ANISOU 1950 CB SER A 233 2907 2335 3391 -20 160 -502 C ATOM 1951 OG SER A 233 21.183 -13.735 15.439 1.00 23.53 O ANISOU 1951 OG SER A 233 3040 2437 3464 63 58 -532 O ATOM 1952 N GLY A 234 17.699 -12.855 18.345 1.00 20.00 N ANISOU 1952 N GLY A 234 2299 2231 3070 -102 299 -576 N ATOM 1953 CA GLY A 234 16.835 -12.959 19.522 1.00 20.88 C ANISOU 1953 CA GLY A 234 2353 2387 3193 -175 429 -557 C ATOM 1954 C GLY A 234 17.548 -12.900 20.859 1.00 26.99 C ANISOU 1954 C GLY A 234 3255 3126 3873 -142 508 -423 C ATOM 1955 O GLY A 234 16.888 -12.781 21.894 1.00 28.52 O ANISOU 1955 O GLY A 234 3411 3385 4041 -173 615 -400 O ATOM 1956 N ASP A 235 18.892 -12.992 20.865 1.00 24.81 N ANISOU 1956 N ASP A 235 3123 2769 3535 -72 456 -338 N ATOM 1957 CA ASP A 235 19.704 -12.940 22.094 1.00 25.09 C ANISOU 1957 CA ASP A 235 3275 2798 3459 -18 503 -222 C ATOM 1958 C ASP A 235 20.448 -11.577 22.264 1.00 28.20 C ANISOU 1958 C ASP A 235 3686 3267 3763 109 407 -244 C ATOM 1959 O ASP A 235 21.388 -11.472 23.064 1.00 27.19 O ANISOU 1959 O ASP A 235 3648 3145 3538 169 402 -177 O ATOM 1960 CB ASP A 235 20.734 -14.091 22.072 1.00 26.46 C ANISOU 1960 CB ASP A 235 3586 2834 3632 -23 517 -117 C ATOM 1961 CG ASP A 235 21.716 -14.028 20.911 1.00 30.55 C ANISOU 1961 CG ASP A 235 4139 3294 4174 35 392 -149 C ATOM 1962 OD1 ASP A 235 21.559 -13.140 20.041 1.00 26.49 O ANISOU 1962 OD1 ASP A 235 3550 2839 3677 71 301 -243 O ATOM 1963 OD2 ASP A 235 22.607 -14.892 20.846 1.00 34.06 O ANISOU 1963 OD2 ASP A 235 4687 3634 4620 52 396 -75 O ATOM 1964 N GLY A 236 20.067 -10.584 21.468 1.00 23.89 N ANISOU 1964 N GLY A 236 3054 2769 3253 152 330 -339 N ATOM 1965 CA GLY A 236 20.709 -9.275 21.486 1.00 22.45 C ANISOU 1965 CA GLY A 236 2888 2618 3023 256 257 -369 C ATOM 1966 C GLY A 236 21.759 -9.116 20.399 1.00 24.15 C ANISOU 1966 C GLY A 236 3155 2761 3261 303 161 -363 C ATOM 1967 O GLY A 236 22.294 -8.020 20.223 1.00 22.88 O ANISOU 1967 O GLY A 236 3003 2601 3088 375 112 -389 O ATOM 1968 N THR A 237 22.074 -10.214 19.668 1.00 19.92 N ANISOU 1968 N THR A 237 2653 2152 2762 259 148 -332 N ATOM 1969 CA THR A 237 23.032 -10.185 18.556 1.00 18.68 C ANISOU 1969 CA THR A 237 2539 1937 2620 303 71 -329 C ATOM 1970 C THR A 237 22.298 -10.355 17.200 1.00 20.74 C ANISOU 1970 C THR A 237 2735 2209 2937 293 28 -395 C ATOM 1971 O THR A 237 21.092 -10.641 17.146 1.00 19.77 O ANISOU 1971 O THR A 237 2524 2135 2853 238 53 -452 O ATOM 1972 CB THR A 237 24.172 -11.202 18.740 1.00 24.31 C ANISOU 1972 CB THR A 237 3350 2572 3317 295 77 -255 C ATOM 1973 OG1 THR A 237 23.670 -12.524 18.596 1.00 23.43 O ANISOU 1973 OG1 THR A 237 3250 2398 3256 216 128 -242 O ATOM 1974 CG2 THR A 237 24.916 -11.031 20.075 1.00 24.23 C ANISOU 1974 CG2 THR A 237 3393 2589 3226 329 99 -196 C ATOM 1975 N TYR A 238 23.036 -10.147 16.113 1.00 16.36 N ANISOU 1975 N TYR A 238 2213 1627 2377 349 -36 -395 N ATOM 1976 CA TYR A 238 22.492 -10.118 14.763 1.00 16.68 C ANISOU 1976 CA TYR A 238 2199 1707 2430 377 -93 -458 C ATOM 1977 C TYR A 238 23.224 -11.064 13.828 1.00 19.32 C ANISOU 1977 C TYR A 238 2589 1984 2767 367 -120 -463 C ATOM 1978 O TYR A 238 24.327 -11.506 14.129 1.00 17.93 O ANISOU 1978 O TYR A 238 2496 1731 2586 365 -101 -404 O ATOM 1979 CB TYR A 238 22.556 -8.661 14.225 1.00 16.53 C ANISOU 1979 CB TYR A 238 2171 1731 2380 492 -134 -449 C ATOM 1980 CG TYR A 238 21.597 -7.759 14.960 1.00 21.23 C ANISOU 1980 CG TYR A 238 2697 2387 2984 516 -110 -473 C ATOM 1981 CD1 TYR A 238 21.943 -7.186 16.183 1.00 23.62 C ANISOU 1981 CD1 TYR A 238 3030 2663 3280 511 -61 -447 C ATOM 1982 CD2 TYR A 238 20.312 -7.529 14.472 1.00 23.41 C ANISOU 1982 CD2 TYR A 238 2864 2762 3268 550 -138 -539 C ATOM 1983 CE1 TYR A 238 21.033 -6.405 16.897 1.00 27.06 C ANISOU 1983 CE1 TYR A 238 3402 3157 3723 537 -30 -484 C ATOM 1984 CE2 TYR A 238 19.408 -6.725 15.164 1.00 25.06 C ANISOU 1984 CE2 TYR A 238 3000 3032 3490 585 -110 -567 C ATOM 1985 CZ TYR A 238 19.768 -6.176 16.379 1.00 32.32 C ANISOU 1985 CZ TYR A 238 3962 3910 4407 576 -50 -539 C ATOM 1986 OH TYR A 238 18.867 -5.393 17.053 1.00 33.82 O ANISOU 1986 OH TYR A 238 4080 4161 4607 618 -15 -581 O ATOM 1987 N GLN A 239 22.594 -11.362 12.681 1.00 16.03 N ANISOU 1987 N GLN A 239 2116 1621 2353 372 -170 -545 N ATOM 1988 CA GLN A 239 23.149 -12.235 11.670 1.00 16.14 C ANISOU 1988 CA GLN A 239 2173 1598 2362 370 -200 -582 C ATOM 1989 C GLN A 239 22.817 -11.691 10.292 1.00 19.49 C ANISOU 1989 C GLN A 239 2553 2132 2720 464 -279 -640 C ATOM 1990 O GLN A 239 21.807 -11.018 10.119 1.00 18.96 O ANISOU 1990 O GLN A 239 2397 2173 2635 504 -315 -679 O ATOM 1991 CB GLN A 239 22.641 -13.686 11.847 1.00 17.48 C ANISOU 1991 CB GLN A 239 2325 1704 2613 244 -161 -656 C ATOM 1992 CG GLN A 239 21.098 -13.790 11.817 1.00 19.83 C ANISOU 1992 CG GLN A 239 2484 2093 2956 170 -167 -768 C ATOM 1993 CD GLN A 239 20.639 -15.205 12.019 1.00 25.93 C ANISOU 1993 CD GLN A 239 3241 2775 3837 21 -104 -844 C ATOM 1994 OE1 GLN A 239 20.446 -15.682 13.149 1.00 27.14 O ANISOU 1994 OE1 GLN A 239 3415 2843 4052 -69 -3 -785 O ATOM 1995 NE2 GLN A 239 20.368 -15.864 10.936 1.00 16.71 N ANISOU 1995 NE2 GLN A 239 2030 1627 2691 -9 -155 -982 N ATOM 1996 N ALA A 240 23.683 -11.970 9.316 1.00 16.81 N ANISOU 1996 N ALA A 240 2276 1777 2333 516 -303 -639 N ATOM 1997 CA ALA A 240 23.536 -11.500 7.937 1.00 18.36 C ANISOU 1997 CA ALA A 240 2455 2087 2433 627 -371 -674 C ATOM 1998 C ALA A 240 24.405 -12.367 7.021 1.00 22.19 C ANISOU 1998 C ALA A 240 3005 2543 2885 638 -379 -713 C ATOM 1999 O ALA A 240 25.260 -13.126 7.515 1.00 19.56 O ANISOU 1999 O ALA A 240 2737 2085 2609 579 -327 -687 O ATOM 2000 CB ALA A 240 23.965 -10.019 7.841 1.00 18.80 C ANISOU 2000 CB ALA A 240 2550 2161 2432 747 -360 -552 C ATOM 2001 N TRP A 241 24.194 -12.270 5.698 1.00 19.82 N ANISOU 2001 N TRP A 241 2688 2366 2479 729 -442 -777 N ATOM 2002 CA TRP A 241 25.015 -13.043 4.753 1.00 20.92 C ANISOU 2002 CA TRP A 241 2887 2494 2567 755 -445 -828 C ATOM 2003 C TRP A 241 25.090 -12.343 3.404 1.00 24.84 C ANISOU 2003 C TRP A 241 3397 3141 2900 911 -491 -814 C ATOM 2004 O TRP A 241 24.285 -11.457 3.123 1.00 24.37 O ANISOU 2004 O TRP A 241 3286 3202 2771 996 -539 -793 O ATOM 2005 CB TRP A 241 24.521 -14.506 4.588 1.00 20.52 C ANISOU 2005 CB TRP A 241 2798 2415 2585 644 -467 -1007 C ATOM 2006 CG TRP A 241 23.098 -14.645 4.135 1.00 23.10 C ANISOU 2006 CG TRP A 241 2996 2887 2895 619 -551 -1167 C ATOM 2007 CD1 TRP A 241 22.010 -14.857 4.928 1.00 26.64 C ANISOU 2007 CD1 TRP A 241 3343 3329 3450 504 -549 -1229 C ATOM 2008 CD2 TRP A 241 22.608 -14.615 2.779 1.00 24.68 C ANISOU 2008 CD2 TRP A 241 3139 3279 2958 714 -651 -1297 C ATOM 2009 NE1 TRP A 241 20.874 -14.958 4.160 1.00 27.62 N ANISOU 2009 NE1 TRP A 241 3335 3631 3530 512 -644 -1401 N ATOM 2010 CE2 TRP A 241 21.209 -14.811 2.836 1.00 29.69 C ANISOU 2010 CE2 TRP A 241 3621 4025 3633 647 -718 -1449 C ATOM 2011 CE3 TRP A 241 23.212 -14.415 1.526 1.00 26.32 C ANISOU 2011 CE3 TRP A 241 3405 3596 3001 857 -687 -1300 C ATOM 2012 CZ2 TRP A 241 20.394 -14.758 1.695 1.00 30.68 C ANISOU 2012 CZ2 TRP A 241 3641 4383 3633 731 -840 -1609 C ATOM 2013 CZ3 TRP A 241 22.409 -14.381 0.392 1.00 29.94 C ANISOU 2013 CZ3 TRP A 241 3778 4280 3318 946 -801 -1445 C ATOM 2014 CH2 TRP A 241 21.018 -14.557 0.480 1.00 31.90 C ANISOU 2014 CH2 TRP A 241 3866 4650 3605 886 -886 -1605 C ATOM 2015 N ALA A 242 26.076 -12.726 2.586 1.00 21.17 N ANISOU 2015 N ALA A 242 3004 2672 2367 963 -468 -816 N ATOM 2016 CA ALA A 242 26.246 -12.242 1.212 1.00 22.92 C ANISOU 2016 CA ALA A 242 3254 3045 2408 1116 -496 -804 C ATOM 2017 C ALA A 242 26.641 -13.432 0.343 1.00 26.77 C ANISOU 2017 C ALA A 242 3763 3561 2847 1112 -513 -954 C ATOM 2018 O ALA A 242 27.485 -14.230 0.752 1.00 26.03 O ANISOU 2018 O ALA A 242 3715 3325 2850 1038 -453 -966 O ATOM 2019 CB ALA A 242 27.291 -11.133 1.132 1.00 22.54 C ANISOU 2019 CB ALA A 242 3291 2954 2319 1204 -404 -604 C ATOM 2020 N SER A 243 26.008 -13.587 -0.811 1.00 23.66 N ANISOU 2020 N SER A 243 3331 3356 2303 1199 -600 -1080 N ATOM 2021 CA SER A 243 26.323 -14.718 -1.682 1.00 25.41 C ANISOU 2021 CA SER A 243 3568 3616 2469 1199 -621 -1257 C ATOM 2022 C SER A 243 26.636 -14.291 -3.093 1.00 29.64 C ANISOU 2022 C SER A 243 4148 4349 2765 1381 -640 -1245 C ATOM 2023 O SER A 243 26.195 -13.231 -3.538 1.00 28.51 O ANISOU 2023 O SER A 243 3998 4353 2481 1514 -673 -1140 O ATOM 2024 CB SER A 243 25.175 -15.730 -1.711 1.00 31.59 C ANISOU 2024 CB SER A 243 4245 4442 3318 1089 -715 -1509 C ATOM 2025 OG SER A 243 24.025 -15.193 -2.346 1.00 39.35 O ANISOU 2025 OG SER A 243 5127 5659 4167 1175 -833 -1585 O ATOM 2026 N ILE A 244 27.363 -15.151 -3.807 1.00 27.25 N ANISOU 2026 N ILE A 244 3895 4051 2409 1400 -615 -1355 N ATOM 2027 CA ILE A 244 27.735 -15.004 -5.213 1.00 30.27 C ANISOU 2027 CA ILE A 244 4325 4631 2547 1570 -623 -1379 C ATOM 2028 C ILE A 244 27.643 -16.341 -5.888 1.00 37.75 C ANISOU 2028 C ILE A 244 5250 5625 3468 1537 -678 -1660 C ATOM 2029 O ILE A 244 27.940 -17.362 -5.267 1.00 37.58 O ANISOU 2029 O ILE A 244 5232 5406 3639 1396 -641 -1762 O ATOM 2030 CB ILE A 244 29.159 -14.406 -5.409 1.00 34.06 C ANISOU 2030 CB ILE A 244 4913 5051 2977 1653 -476 -1165 C ATOM 2031 CG1 ILE A 244 30.214 -15.080 -4.468 1.00 32.03 C ANISOU 2031 CG1 ILE A 244 4686 4545 2937 1523 -376 -1142 C ATOM 2032 CG2 ILE A 244 29.118 -12.904 -5.207 1.00 37.50 C ANISOU 2032 CG2 ILE A 244 5376 5504 3368 1733 -428 -910 C ATOM 2033 CD1 ILE A 244 31.484 -15.226 -5.023 1.00 36.64 C ANISOU 2033 CD1 ILE A 244 5337 5124 3461 1593 -270 -1096 C ATOM 2034 N GLU A 245 27.287 -16.336 -7.169 1.00 37.43 N ANISOU 2034 N GLU A 245 5197 5841 3184 1678 -758 -1783 N ATOM 2035 CA GLU A 245 27.249 -17.537 -7.994 1.00 40.20 C ANISOU 2035 CA GLU A 245 5531 6270 3474 1669 -812 -2079 C ATOM 2036 C GLU A 245 28.617 -17.694 -8.667 1.00 46.46 C ANISOU 2036 C GLU A 245 6440 7055 4158 1774 -693 -2019 C ATOM 2037 O GLU A 245 29.191 -16.700 -9.123 1.00 46.33 O ANISOU 2037 O GLU A 245 6491 7139 3974 1922 -621 -1797 O ATOM 2038 CB GLU A 245 26.118 -17.443 -9.029 1.00 43.77 C ANISOU 2038 CB GLU A 245 5891 7043 3696 1779 -976 -2269 C ATOM 2039 CG GLU A 245 25.876 -18.744 -9.784 1.00 59.00 C ANISOU 2039 CG GLU A 245 7773 9052 5591 1735 -1054 -2638 C ATOM 2040 CD GLU A 245 25.242 -18.587 -11.153 1.00 83.72 C ANISOU 2040 CD GLU A 245 10850 12565 8395 1917 -1196 -2811 C ATOM 2041 OE1 GLU A 245 24.139 -17.998 -11.231 1.00 82.21 O ANISOU 2041 OE1 GLU A 245 10549 12571 8118 1970 -1326 -2826 O ATOM 2042 OE2 GLU A 245 25.837 -19.072 -12.145 1.00 73.95 O ANISOU 2042 OE2 GLU A 245 9674 11444 6981 2018 -1181 -2943 O ATOM 2043 N LEU A 246 29.158 -18.930 -8.685 1.00 44.30 N ANISOU 2043 N LEU A 246 6189 6645 3996 1694 -654 -2207 N ATOM 2044 CA LEU A 246 30.447 -19.245 -9.320 1.00 60.67 C ANISOU 2044 CA LEU A 246 8356 8712 5983 1791 -539 -2192 C ATOM 2045 C LEU A 246 30.234 -19.699 -10.754 1.00 79.52 C ANISOU 2045 C LEU A 246 10743 11362 8109 1922 -609 -2434 C ATOM 2046 O LEU A 246 29.450 -20.617 -10.985 1.00 56.31 O ANISOU 2046 O LEU A 246 7739 8452 5205 1846 -718 -2738 O ATOM 2047 CB LEU A 246 31.208 -20.337 -8.548 1.00 59.59 C ANISOU 2047 CB LEU A 246 8252 8280 6108 1665 -452 -2257 C ATOM 2048 CG LEU A 246 31.571 -20.079 -7.094 1.00 60.57 C ANISOU 2048 CG LEU A 246 8383 8149 6484 1547 -380 -2041 C ATOM 2049 CD1 LEU A 246 32.180 -21.324 -6.478 1.00 59.87 C ANISOU 2049 CD1 LEU A 246 8328 7798 6620 1456 -316 -2140 C ATOM 2050 CD2 LEU A 246 32.543 -18.926 -6.972 1.00 61.73 C ANISOU 2050 CD2 LEU A 246 8571 8318 6565 1637 -273 -1745 C ATOM 2051 N ASN A 252 39.422 -17.631 -11.333 1.00 62.11 N ANISOU 2051 N ASN A 252 8832 8897 5871 2338 550 -1287 N ATOM 2052 CA ASN A 252 38.855 -16.584 -10.482 1.00 59.92 C ANISOU 2052 CA ASN A 252 8537 8536 5694 2244 511 -1085 C ATOM 2053 C ASN A 252 38.944 -16.961 -8.988 1.00 57.56 C ANISOU 2053 C ASN A 252 8182 7980 5710 2084 464 -1083 C ATOM 2054 O ASN A 252 38.403 -17.997 -8.580 1.00 56.70 O ANISOU 2054 O ASN A 252 8065 7769 5709 2023 352 -1271 O ATOM 2055 CB ASN A 252 37.399 -16.292 -10.881 1.00 65.22 C ANISOU 2055 CB ASN A 252 9233 9340 6209 2275 357 -1138 C ATOM 2056 CG ASN A 252 37.179 -15.061 -11.743 1.00 94.22 C ANISOU 2056 CG ASN A 252 12961 13211 9628 2407 414 -944 C ATOM 2057 OD1 ASN A 252 38.052 -14.192 -11.913 1.00 90.74 O ANISOU 2057 OD1 ASN A 252 12546 12773 9157 2446 588 -720 O ATOM 2058 ND2 ASN A 252 35.964 -14.928 -12.259 1.00 85.02 N ANISOU 2058 ND2 ASN A 252 11808 12209 8286 2478 271 -1018 N ATOM 2059 N LEU A 253 39.658 -16.124 -8.196 1.00 49.38 N ANISOU 2059 N LEU A 253 7106 6842 4814 2020 559 -874 N ATOM 2060 CA LEU A 253 39.875 -16.284 -6.754 1.00 45.79 C ANISOU 2060 CA LEU A 253 6595 6179 4625 1890 527 -837 C ATOM 2061 C LEU A 253 39.006 -15.276 -5.972 1.00 41.02 C ANISOU 2061 C LEU A 253 5984 5519 4083 1799 462 -700 C ATOM 2062 O LEU A 253 39.136 -14.062 -6.127 1.00 38.76 O ANISOU 2062 O LEU A 253 5704 5278 3745 1810 542 -521 O ATOM 2063 CB LEU A 253 41.363 -16.139 -6.380 1.00 46.08 C ANISOU 2063 CB LEU A 253 6567 6162 4778 1885 669 -743 C ATOM 2064 CG LEU A 253 42.273 -17.387 -6.505 1.00 53.49 C ANISOU 2064 CG LEU A 253 7482 7069 5773 1947 706 -892 C ATOM 2065 CD1 LEU A 253 41.638 -18.671 -5.907 1.00 57.47 C ANISOU 2065 CD1 LEU A 253 8014 7426 6397 1910 572 -1068 C ATOM 2066 CD2 LEU A 253 42.812 -17.571 -7.919 1.00 55.57 C ANISOU 2066 CD2 LEU A 253 7773 7508 5832 2083 814 -956 C ATOM 2067 N TYR A 254 38.113 -15.799 -5.147 1.00 33.01 N ANISOU 2067 N TYR A 254 4960 4397 3184 1711 331 -787 N ATOM 2068 CA TYR A 254 37.139 -14.981 -4.438 1.00 30.29 C ANISOU 2068 CA TYR A 254 4606 4015 2890 1635 258 -694 C ATOM 2069 C TYR A 254 37.469 -14.811 -2.983 1.00 29.30 C ANISOU 2069 C TYR A 254 4433 3720 2981 1521 261 -612 C ATOM 2070 O TYR A 254 38.024 -15.706 -2.350 1.00 26.33 O ANISOU 2070 O TYR A 254 4036 3236 2733 1487 259 -676 O ATOM 2071 CB TYR A 254 35.744 -15.591 -4.577 1.00 31.69 C ANISOU 2071 CB TYR A 254 4791 4224 3025 1615 111 -855 C ATOM 2072 CG TYR A 254 35.223 -15.550 -5.996 1.00 35.59 C ANISOU 2072 CG TYR A 254 5319 4931 3272 1739 78 -938 C ATOM 2073 CD1 TYR A 254 34.557 -14.428 -6.483 1.00 37.51 C ANISOU 2073 CD1 TYR A 254 5578 5311 3362 1812 60 -820 C ATOM 2074 CD2 TYR A 254 35.423 -16.620 -6.865 1.00 39.14 C ANISOU 2074 CD2 TYR A 254 5789 5452 3630 1801 68 -1137 C ATOM 2075 CE1 TYR A 254 34.087 -14.377 -7.793 1.00 39.45 C ANISOU 2075 CE1 TYR A 254 5857 5783 3350 1954 22 -887 C ATOM 2076 CE2 TYR A 254 34.953 -16.581 -8.179 1.00 42.38 C ANISOU 2076 CE2 TYR A 254 6227 6090 3785 1928 29 -1230 C ATOM 2077 CZ TYR A 254 34.282 -15.458 -8.637 1.00 49.08 C ANISOU 2077 CZ TYR A 254 7088 7095 4464 2009 1 -1099 C ATOM 2078 OH TYR A 254 33.821 -15.410 -9.932 1.00 55.16 O ANISOU 2078 OH TYR A 254 7887 8118 4955 2160 -46 -1182 O ATOM 2079 N SER A 255 37.128 -13.644 -2.450 1.00 26.36 N ANISOU 2079 N SER A 255 4048 3327 2642 1474 266 -470 N ATOM 2080 CA SER A 255 37.308 -13.386 -1.026 1.00 24.76 C ANISOU 2080 CA SER A 255 3798 2987 2623 1367 255 -407 C ATOM 2081 C SER A 255 36.126 -12.621 -0.480 1.00 28.05 C ANISOU 2081 C SER A 255 4217 3385 3056 1315 183 -356 C ATOM 2082 O SER A 255 35.609 -11.709 -1.147 1.00 27.37 O ANISOU 2082 O SER A 255 4159 3382 2857 1372 197 -282 O ATOM 2083 CB SER A 255 38.625 -12.657 -0.748 1.00 26.82 C ANISOU 2083 CB SER A 255 4012 3222 2955 1352 378 -289 C ATOM 2084 OG SER A 255 38.645 -11.385 -1.372 1.00 37.46 O ANISOU 2084 OG SER A 255 5382 4626 4223 1381 467 -159 O ATOM 2085 N CYS A 256 35.677 -13.005 0.731 1.00 25.91 N ANISOU 2085 N CYS A 256 3918 3011 2917 1223 113 -390 N ATOM 2086 CA CYS A 256 34.617 -12.293 1.430 1.00 27.37 C ANISOU 2086 CA CYS A 256 4090 3172 3136 1168 55 -348 C ATOM 2087 C CYS A 256 35.241 -11.238 2.314 1.00 26.69 C ANISOU 2087 C CYS A 256 3975 3019 3148 1118 118 -226 C ATOM 2088 O CYS A 256 36.123 -11.565 3.114 1.00 23.82 O ANISOU 2088 O CYS A 256 3576 2589 2885 1073 140 -226 O ATOM 2089 CB CYS A 256 33.724 -13.214 2.254 1.00 30.53 C ANISOU 2089 CB CYS A 256 4476 3507 3618 1090 -36 -448 C ATOM 2090 SG CYS A 256 32.467 -12.297 3.206 1.00 35.58 S ANISOU 2090 SG CYS A 256 5082 4131 4305 1025 -90 -397 S ATOM 2091 N HIS A 257 34.739 -9.995 2.224 1.00 23.14 N ANISOU 2091 N HIS A 257 3536 2584 2672 1131 139 -134 N ATOM 2092 CA HIS A 257 35.188 -8.848 3.022 1.00 21.84 C ANISOU 2092 CA HIS A 257 3347 2342 2609 1075 203 -39 C ATOM 2093 C HIS A 257 34.072 -8.425 3.981 1.00 24.86 C ANISOU 2093 C HIS A 257 3717 2684 3046 1027 131 -45 C ATOM 2094 O HIS A 257 32.940 -8.224 3.555 1.00 24.83 O ANISOU 2094 O HIS A 257 3734 2734 2968 1077 79 -50 O ATOM 2095 CB HIS A 257 35.605 -7.673 2.113 1.00 23.02 C ANISOU 2095 CB HIS A 257 3534 2508 2704 1134 321 84 C ATOM 2096 CG HIS A 257 36.900 -7.878 1.395 1.00 27.21 C ANISOU 2096 CG HIS A 257 4058 3068 3211 1158 429 106 C ATOM 2097 ND1 HIS A 257 37.091 -8.942 0.522 1.00 30.09 N ANISOU 2097 ND1 HIS A 257 4441 3524 3469 1229 412 34 N ATOM 2098 CD2 HIS A 257 38.021 -7.126 1.409 1.00 29.62 C ANISOU 2098 CD2 HIS A 257 4332 3328 3593 1118 564 181 C ATOM 2099 CE1 HIS A 257 38.322 -8.814 0.061 1.00 29.54 C ANISOU 2099 CE1 HIS A 257 4350 3468 3405 1239 535 75 C ATOM 2100 NE2 HIS A 257 38.928 -7.748 0.576 1.00 30.34 N ANISOU 2100 NE2 HIS A 257 4414 3491 3622 1167 631 163 N ATOM 2101 N VAL A 258 34.392 -8.302 5.276 1.00 19.78 N ANISOU 2101 N VAL A 258 3030 1966 2521 940 125 -54 N ATOM 2102 CA VAL A 258 33.437 -7.939 6.316 1.00 17.73 C ANISOU 2102 CA VAL A 258 2752 1672 2311 891 70 -68 C ATOM 2103 C VAL A 258 33.997 -6.773 7.116 1.00 22.11 C ANISOU 2103 C VAL A 258 3281 2158 2962 839 131 -23 C ATOM 2104 O VAL A 258 35.100 -6.868 7.668 1.00 22.54 O ANISOU 2104 O VAL A 258 3293 2189 3083 790 160 -39 O ATOM 2105 CB VAL A 258 33.069 -9.131 7.255 1.00 20.16 C ANISOU 2105 CB VAL A 258 3039 1968 2653 836 -6 -147 C ATOM 2106 CG1 VAL A 258 32.089 -8.677 8.369 1.00 18.59 C ANISOU 2106 CG1 VAL A 258 2817 1749 2498 786 -43 -155 C ATOM 2107 CG2 VAL A 258 32.502 -10.325 6.473 1.00 20.36 C ANISOU 2107 CG2 VAL A 258 3085 2036 2614 865 -56 -219 C ATOM 2108 N GLU A 259 33.207 -5.703 7.233 1.00 18.55 N ANISOU 2108 N GLU A 259 2848 1677 2523 853 143 15 N ATOM 2109 CA GLU A 259 33.579 -4.512 8.007 1.00 18.47 C ANISOU 2109 CA GLU A 259 2819 1581 2618 798 204 34 C ATOM 2110 C GLU A 259 32.574 -4.374 9.135 1.00 21.10 C ANISOU 2110 C GLU A 259 3131 1906 2979 768 138 -19 C ATOM 2111 O GLU A 259 31.373 -4.267 8.878 1.00 18.97 O ANISOU 2111 O GLU A 259 2881 1667 2660 825 99 -11 O ATOM 2112 CB GLU A 259 33.584 -3.267 7.083 1.00 21.51 C ANISOU 2112 CB GLU A 259 3262 1908 3004 857 308 137 C ATOM 2113 CG GLU A 259 33.782 -1.937 7.794 1.00 40.95 C ANISOU 2113 CG GLU A 259 5719 4247 5595 801 385 147 C ATOM 2114 CD GLU A 259 35.202 -1.590 8.198 1.00 75.21 C ANISOU 2114 CD GLU A 259 10001 8524 10050 694 469 116 C ATOM 2115 OE1 GLU A 259 36.143 -1.872 7.418 1.00 80.29 O ANISOU 2115 OE1 GLU A 259 10637 9191 10679 695 535 154 O ATOM 2116 OE2 GLU A 259 35.366 -0.979 9.279 1.00 72.82 O ANISOU 2116 OE2 GLU A 259 9653 8160 9856 611 473 42 O ATOM 2117 N HIS A 260 33.064 -4.380 10.386 1.00 17.61 N ANISOU 2117 N HIS A 260 2641 1445 2607 689 124 -80 N ATOM 2118 CA HIS A 260 32.194 -4.249 11.539 1.00 16.00 C ANISOU 2118 CA HIS A 260 2417 1247 2416 662 75 -132 C ATOM 2119 C HIS A 260 32.888 -3.438 12.607 1.00 21.29 C ANISOU 2119 C HIS A 260 3045 1873 3170 594 104 -187 C ATOM 2120 O HIS A 260 34.007 -3.765 13.018 1.00 16.94 O ANISOU 2120 O HIS A 260 2448 1344 2644 548 101 -223 O ATOM 2121 CB HIS A 260 31.785 -5.653 12.084 1.00 15.49 C ANISOU 2121 CB HIS A 260 2338 1250 2297 647 -2 -169 C ATOM 2122 CG HIS A 260 30.834 -5.569 13.245 1.00 17.37 C ANISOU 2122 CG HIS A 260 2557 1508 2536 620 -33 -210 C ATOM 2123 ND1 HIS A 260 31.286 -5.677 14.549 1.00 18.04 N ANISOU 2123 ND1 HIS A 260 2614 1610 2630 574 -47 -253 N ATOM 2124 CD2 HIS A 260 29.510 -5.272 13.257 1.00 18.05 C ANISOU 2124 CD2 HIS A 260 2641 1611 2608 644 -46 -218 C ATOM 2125 CE1 HIS A 260 30.210 -5.521 15.318 1.00 17.79 C ANISOU 2125 CE1 HIS A 260 2573 1602 2583 567 -58 -279 C ATOM 2126 NE2 HIS A 260 29.116 -5.257 14.582 1.00 17.80 N ANISOU 2126 NE2 HIS A 260 2582 1601 2580 604 -55 -263 N ATOM 2127 N SER A 261 32.242 -2.329 13.001 1.00 20.49 N ANISOU 2127 N SER A 261 2954 1714 3118 595 134 -205 N ATOM 2128 CA SER A 261 32.662 -1.474 14.110 1.00 22.07 C ANISOU 2128 CA SER A 261 3114 1872 3398 528 155 -293 C ATOM 2129 C SER A 261 34.207 -1.171 14.084 1.00 24.17 C ANISOU 2129 C SER A 261 3330 2107 3746 455 205 -329 C ATOM 2130 O SER A 261 34.903 -1.348 15.078 1.00 22.67 O ANISOU 2130 O SER A 261 3069 1975 3568 399 165 -424 O ATOM 2131 CB SER A 261 32.220 -2.141 15.424 1.00 25.69 C ANISOU 2131 CB SER A 261 3538 2426 3797 509 75 -365 C ATOM 2132 OG SER A 261 32.360 -1.317 16.564 1.00 42.66 O ANISOU 2132 OG SER A 261 5652 4565 5994 463 82 -471 O ATOM 2133 N GLY A 262 34.691 -0.689 12.938 1.00 21.77 N ANISOU 2133 N GLY A 262 3056 1725 3490 464 297 -252 N ATOM 2134 CA GLY A 262 36.076 -0.268 12.722 1.00 22.28 C ANISOU 2134 CA GLY A 262 3066 1746 3654 387 378 -277 C ATOM 2135 C GLY A 262 37.089 -1.360 12.437 1.00 24.33 C ANISOU 2135 C GLY A 262 3267 2110 3868 383 346 -275 C ATOM 2136 O GLY A 262 38.291 -1.101 12.413 1.00 24.73 O ANISOU 2136 O GLY A 262 3238 2157 4003 314 402 -320 O ATOM 2137 N VAL A 263 36.632 -2.590 12.237 1.00 19.44 N ANISOU 2137 N VAL A 263 2677 1580 3129 455 262 -235 N ATOM 2138 CA VAL A 263 37.535 -3.712 11.991 1.00 18.42 C ANISOU 2138 CA VAL A 263 2503 1537 2957 473 232 -236 C ATOM 2139 C VAL A 263 37.181 -4.309 10.658 1.00 22.76 C ANISOU 2139 C VAL A 263 3128 2092 3428 552 254 -142 C ATOM 2140 O VAL A 263 36.009 -4.617 10.422 1.00 22.63 O ANISOU 2140 O VAL A 263 3179 2080 3339 604 209 -110 O ATOM 2141 CB VAL A 263 37.481 -4.767 13.132 1.00 20.22 C ANISOU 2141 CB VAL A 263 2698 1860 3123 489 114 -293 C ATOM 2142 CG1 VAL A 263 38.351 -5.988 12.799 1.00 19.54 C ANISOU 2142 CG1 VAL A 263 2584 1845 2997 537 87 -280 C ATOM 2143 CG2 VAL A 263 37.917 -4.156 14.453 1.00 20.70 C ANISOU 2143 CG2 VAL A 263 2677 1953 3234 425 83 -401 C ATOM 2144 N HIS A 264 38.185 -4.472 9.797 1.00 20.40 N ANISOU 2144 N HIS A 264 2805 1808 3140 560 324 -114 N ATOM 2145 CA HIS A 264 38.002 -5.067 8.478 1.00 21.96 C ANISOU 2145 CA HIS A 264 3068 2032 3244 642 350 -42 C ATOM 2146 C HIS A 264 38.564 -6.483 8.498 1.00 24.88 C ANISOU 2146 C HIS A 264 3407 2480 3567 680 289 -84 C ATOM 2147 O HIS A 264 39.670 -6.707 9.004 1.00 25.02 O ANISOU 2147 O HIS A 264 3334 2533 3640 652 291 -132 O ATOM 2148 CB HIS A 264 38.685 -4.220 7.392 1.00 26.36 C ANISOU 2148 CB HIS A 264 3636 2547 3831 641 497 33 C ATOM 2149 CG HIS A 264 38.318 -4.675 6.018 1.00 32.78 C ANISOU 2149 CG HIS A 264 4532 3406 4515 745 522 109 C ATOM 2150 ND1 HIS A 264 37.146 -4.248 5.401 1.00 36.26 N ANISOU 2150 ND1 HIS A 264 5068 3835 4875 819 516 179 N ATOM 2151 CD2 HIS A 264 38.941 -5.565 5.208 1.00 36.39 C ANISOU 2151 CD2 HIS A 264 4983 3940 4902 798 541 106 C ATOM 2152 CE1 HIS A 264 37.114 -4.872 4.234 1.00 36.73 C ANISOU 2152 CE1 HIS A 264 5174 3975 4807 909 525 211 C ATOM 2153 NE2 HIS A 264 38.185 -5.659 4.066 1.00 36.78 N ANISOU 2153 NE2 HIS A 264 5127 4029 4819 896 548 168 N ATOM 2154 N AMET A 265 37.792 -7.432 7.973 0.50 18.54 N ANISOU 2154 N AMET A 265 2671 1704 2670 747 233 -76 N ATOM 2155 N BMET A 265 37.797 -7.448 7.990 0.50 19.77 N ANISOU 2155 N BMET A 265 2825 1860 2825 747 231 -77 N ATOM 2156 CA AMET A 265 38.154 -8.837 7.953 0.50 18.43 C ANISOU 2156 CA AMET A 265 2652 1730 2619 791 182 -116 C ATOM 2157 CA BMET A 265 38.279 -8.817 7.955 0.50 20.26 C ANISOU 2157 CA BMET A 265 2878 1964 2857 790 187 -117 C ATOM 2158 C AMET A 265 38.058 -9.376 6.528 0.50 21.43 C ANISOU 2158 C AMET A 265 3088 2141 2912 865 214 -104 C ATOM 2159 C BMET A 265 38.069 -9.394 6.559 0.50 22.21 C ANISOU 2159 C BMET A 265 3186 2239 3012 865 213 -105 C ATOM 2160 O AMET A 265 37.133 -9.013 5.796 0.50 20.89 O ANISOU 2160 O AMET A 265 3081 2080 2776 893 216 -75 O ATOM 2161 O BMET A 265 37.112 -9.038 5.864 0.50 21.61 O ANISOU 2161 O BMET A 265 3170 2169 2870 891 212 -78 O ATOM 2162 CB AMET A 265 37.208 -9.596 8.899 0.50 20.10 C ANISOU 2162 CB AMET A 265 2892 1926 2818 781 83 -148 C ATOM 2163 CB BMET A 265 37.667 -9.690 9.070 0.50 22.63 C ANISOU 2163 CB BMET A 265 3190 2254 3155 782 87 -154 C ATOM 2164 CG AMET A 265 37.510 -11.064 9.037 0.50 24.37 C ANISOU 2164 CG AMET A 265 3448 2469 3344 826 42 -179 C ATOM 2165 CG BMET A 265 36.177 -9.918 8.979 0.50 27.03 C ANISOU 2165 CG BMET A 265 3814 2791 3666 780 40 -156 C ATOM 2166 SD AMET A 265 36.025 -12.015 9.424 0.50 29.13 S ANISOU 2166 SD AMET A 265 4121 3026 3919 812 -26 -202 S ATOM 2167 SD BMET A 265 35.440 -10.428 10.561 0.50 32.23 S ANISOU 2167 SD BMET A 265 4474 3428 4345 737 -34 -176 S ATOM 2168 CE AMET A 265 35.826 -11.620 11.089 0.50 26.00 C ANISOU 2168 CE AMET A 265 3695 2627 3557 761 -62 -184 C ATOM 2169 CE BMET A 265 36.277 -12.041 10.804 0.50 28.97 C ANISOU 2169 CE BMET A 265 4073 3002 3933 789 -55 -188 C ATOM 2170 N VAL A 266 39.001 -10.247 6.145 1.00 18.09 N ANISOU 2170 N VAL A 266 2641 1750 2480 911 234 -133 N ATOM 2171 CA VAL A 266 39.003 -10.880 4.815 1.00 17.90 C ANISOU 2171 CA VAL A 266 2669 1769 2364 990 265 -148 C ATOM 2172 C VAL A 266 39.070 -12.398 4.973 1.00 20.59 C ANISOU 2172 C VAL A 266 3027 2095 2702 1033 204 -225 C ATOM 2173 O VAL A 266 39.945 -12.900 5.682 1.00 19.45 O ANISOU 2173 O VAL A 266 2830 1938 2621 1043 196 -240 O ATOM 2174 CB VAL A 266 40.186 -10.372 3.916 1.00 21.60 C ANISOU 2174 CB VAL A 266 3098 2287 2822 1018 392 -109 C ATOM 2175 CG1 VAL A 266 40.139 -11.029 2.530 1.00 22.32 C ANISOU 2175 CG1 VAL A 266 3249 2444 2787 1114 424 -132 C ATOM 2176 CG2 VAL A 266 40.185 -8.843 3.783 1.00 22.54 C ANISOU 2176 CG2 VAL A 266 3212 2383 2970 966 482 -19 C ATOM 2177 N LEU A 267 38.194 -13.116 4.269 1.00 19.20 N ANISOU 2177 N LEU A 267 2921 1921 2453 1067 165 -280 N ATOM 2178 CA LEU A 267 38.232 -14.580 4.171 1.00 22.65 C ANISOU 2178 CA LEU A 267 3391 2318 2896 1108 131 -368 C ATOM 2179 C LEU A 267 38.486 -14.941 2.723 1.00 26.38 C ANISOU 2179 C LEU A 267 3895 2859 3270 1188 176 -426 C ATOM 2180 O LEU A 267 37.588 -14.771 1.891 1.00 24.70 O ANISOU 2180 O LEU A 267 3723 2701 2960 1200 154 -459 O ATOM 2181 CB LEU A 267 36.913 -15.215 4.656 1.00 24.42 C ANISOU 2181 CB LEU A 267 3663 2476 3141 1055 51 -419 C ATOM 2182 CG LEU A 267 36.711 -15.371 6.159 1.00 30.36 C ANISOU 2182 CG LEU A 267 4404 3149 3983 997 13 -378 C ATOM 2183 CD1 LEU A 267 36.350 -14.084 6.753 1.00 29.85 C ANISOU 2183 CD1 LEU A 267 4301 3118 3922 940 6 -310 C ATOM 2184 CD2 LEU A 267 35.561 -16.349 6.440 1.00 34.85 C ANISOU 2184 CD2 LEU A 267 5024 3636 4582 949 -31 -441 C ATOM 2185 N GLN A 268 39.711 -15.381 2.405 1.00 24.12 N ANISOU 2185 N GLN A 268 3579 2592 2995 1255 239 -441 N ATOM 2186 CA GLN A 268 40.089 -15.792 1.054 1.00 26.11 C ANISOU 2186 CA GLN A 268 3857 2919 3145 1344 296 -506 C ATOM 2187 C GLN A 268 39.580 -17.230 0.817 1.00 31.23 C ANISOU 2187 C GLN A 268 4569 3502 3795 1376 240 -648 C ATOM 2188 O GLN A 268 39.799 -18.097 1.659 1.00 29.41 O ANISOU 2188 O GLN A 268 4343 3158 3673 1373 213 -671 O ATOM 2189 CB GLN A 268 41.622 -15.691 0.891 1.00 28.73 C ANISOU 2189 CB GLN A 268 4113 3298 3504 1400 398 -475 C ATOM 2190 CG GLN A 268 42.200 -16.281 -0.404 1.00 44.80 C ANISOU 2190 CG GLN A 268 6168 5414 5441 1507 472 -553 C ATOM 2191 CD GLN A 268 41.880 -15.459 -1.627 1.00 67.37 C ANISOU 2191 CD GLN A 268 9065 8393 8140 1534 537 -514 C ATOM 2192 OE1 GLN A 268 42.269 -14.291 -1.734 1.00 63.66 O ANISOU 2192 OE1 GLN A 268 8558 7970 7661 1505 624 -393 O ATOM 2193 NE2 GLN A 268 41.197 -16.070 -2.598 1.00 57.04 N ANISOU 2193 NE2 GLN A 268 7833 7139 6701 1596 502 -621 N ATOM 2194 N VAL A 269 38.879 -17.473 -0.305 1.00 28.68 N ANISOU 2194 N VAL A 269 4298 3247 3353 1408 222 -745 N ATOM 2195 CA VAL A 269 38.345 -18.804 -0.579 1.00 29.49 C ANISOU 2195 CA VAL A 269 4454 3279 3473 1417 174 -912 C ATOM 2196 C VAL A 269 39.353 -19.531 -1.474 1.00 37.06 C ANISOU 2196 C VAL A 269 5425 4272 4384 1532 246 -1002 C ATOM 2197 O VAL A 269 39.647 -19.033 -2.560 1.00 40.05 O ANISOU 2197 O VAL A 269 5800 4801 4615 1601 299 -1005 O ATOM 2198 CB VAL A 269 36.913 -18.789 -1.184 1.00 33.75 C ANISOU 2198 CB VAL A 269 5021 3879 3922 1376 92 -1014 C ATOM 2199 CG1 VAL A 269 36.414 -20.216 -1.457 1.00 34.92 C ANISOU 2199 CG1 VAL A 269 5213 3937 4119 1362 52 -1219 C ATOM 2200 CG2 VAL A 269 35.939 -18.040 -0.281 1.00 31.91 C ANISOU 2200 CG2 VAL A 269 4764 3621 3741 1275 30 -925 C ATOM 2201 N PRO A 270 39.903 -20.686 -1.031 1.00 34.04 N ANISOU 2201 N PRO A 270 5061 3753 4120 1566 259 -1067 N ATOM 2202 CA PRO A 270 40.895 -21.411 -1.871 1.00 40.98 C ANISOU 2202 CA PRO A 270 5948 4662 4963 1692 334 -1166 C ATOM 2203 C PRO A 270 40.309 -21.979 -3.175 1.00 87.76 C ANISOU 2203 C PRO A 270 11930 10654 10760 1732 321 -1361 C ATOM 2204 O PRO A 270 39.202 -22.519 -3.213 1.00 54.33 O ANISOU 2204 O PRO A 270 7742 6355 6547 1662 245 -1486 O ATOM 2205 CB PRO A 270 41.399 -22.542 -0.962 1.00 41.62 C ANISOU 2205 CB PRO A 270 6049 4551 5215 1726 337 -1184 C ATOM 2206 CG PRO A 270 40.371 -22.702 0.090 1.00 43.45 C ANISOU 2206 CG PRO A 270 6318 4642 5550 1608 261 -1146 C ATOM 2207 CD PRO A 270 39.663 -21.377 0.255 1.00 36.58 C ANISOU 2207 CD PRO A 270 5404 3886 4607 1510 218 -1042 C TER 2208 PRO A 270 ATOM 2209 N MET B 0 -4.865 5.845 1.463 1.00 40.11 N ANISOU 2209 N MET B 0 4722 6122 4395 761 422 -556 N ATOM 2210 CA MET B 0 -4.734 4.596 2.197 1.00 39.83 C ANISOU 2210 CA MET B 0 4699 6063 4370 774 481 -546 C ATOM 2211 C MET B 0 -3.762 3.668 1.499 1.00 41.44 C ANISOU 2211 C MET B 0 4738 6267 4739 558 396 -638 C ATOM 2212 O MET B 0 -4.012 3.241 0.375 1.00 39.69 O ANISOU 2212 O MET B 0 4286 6172 4624 418 435 -649 O ATOM 2213 CB MET B 0 -6.103 3.911 2.344 1.00 43.02 C ANISOU 2213 CB MET B 0 4973 6615 4757 833 700 -377 C ATOM 2214 N ILE B 1 -2.644 3.377 2.160 1.00 36.42 N ANISOU 2214 N ILE B 1 4234 5498 4108 560 269 -706 N ATOM 2215 CA ILE B 1 -1.692 2.429 1.630 1.00 34.67 C ANISOU 2215 CA ILE B 1 3875 5288 4011 411 200 -781 C ATOM 2216 C ILE B 1 -1.737 1.194 2.494 1.00 35.14 C ANISOU 2216 C ILE B 1 3978 5280 4092 441 254 -772 C ATOM 2217 O ILE B 1 -1.977 1.282 3.694 1.00 35.72 O ANISOU 2217 O ILE B 1 4231 5276 4064 582 288 -713 O ATOM 2218 CB ILE B 1 -0.240 2.968 1.485 1.00 38.30 C ANISOU 2218 CB ILE B 1 4372 5684 4496 350 0 -817 C ATOM 2219 CG1 ILE B 1 0.404 3.375 2.827 1.00 39.61 C ANISOU 2219 CG1 ILE B 1 4824 5641 4584 447 -133 -812 C ATOM 2220 CG2 ILE B 1 -0.141 4.060 0.435 1.00 40.78 C ANISOU 2220 CG2 ILE B 1 4557 6100 4839 284 -75 -775 C ATOM 2221 CD1 ILE B 1 1.369 2.370 3.376 1.00 48.22 C ANISOU 2221 CD1 ILE B 1 5943 6661 5718 409 -179 -844 C ATOM 2222 N GLN B 2 -1.470 0.054 1.887 1.00 28.47 N ANISOU 2222 N GLN B 2 2978 4468 3371 331 240 -829 N ATOM 2223 CA GLN B 2 -1.343 -1.222 2.576 1.00 27.42 C ANISOU 2223 CA GLN B 2 2860 4249 3309 325 240 -823 C ATOM 2224 C GLN B 2 -0.038 -1.814 2.151 1.00 26.54 C ANISOU 2224 C GLN B 2 2714 4109 3261 260 119 -949 C ATOM 2225 O GLN B 2 0.304 -1.758 0.960 1.00 26.29 O ANISOU 2225 O GLN B 2 2547 4188 3253 214 73 -1028 O ATOM 2226 CB GLN B 2 -2.493 -2.169 2.243 1.00 29.38 C ANISOU 2226 CB GLN B 2 2954 4537 3671 269 300 -744 C ATOM 2227 CG GLN B 2 -3.870 -1.634 2.551 1.00 49.82 C ANISOU 2227 CG GLN B 2 5519 7211 6198 340 440 -555 C ATOM 2228 CD GLN B 2 -4.893 -2.648 2.139 1.00 59.29 C ANISOU 2228 CD GLN B 2 6533 8437 7559 238 442 -429 C ATOM 2229 OE1 GLN B 2 -4.913 -3.135 0.992 1.00 52.73 O ANISOU 2229 OE1 GLN B 2 5581 7608 6845 114 343 -536 O ATOM 2230 NE2 GLN B 2 -5.681 -3.070 3.108 1.00 44.52 N ANISOU 2230 NE2 GLN B 2 4634 6579 5701 300 520 -186 N ATOM 2231 N ARG B 3 0.696 -2.382 3.097 1.00 20.03 N ANISOU 2231 N ARG B 3 1998 3167 2446 282 75 -952 N ATOM 2232 CA ARG B 3 1.987 -3.000 2.794 1.00 19.06 C ANISOU 2232 CA ARG B 3 1844 3028 2372 246 -28 -1044 C ATOM 2233 C ARG B 3 1.987 -4.431 3.245 1.00 22.59 C ANISOU 2233 C ARG B 3 2283 3374 2927 232 -43 -1067 C ATOM 2234 O ARG B 3 1.637 -4.732 4.390 1.00 21.10 O ANISOU 2234 O ARG B 3 2179 3090 2747 257 0 -972 O ATOM 2235 CB ARG B 3 3.141 -2.268 3.461 1.00 21.34 C ANISOU 2235 CB ARG B 3 2266 3252 2589 263 -115 -1008 C ATOM 2236 CG ARG B 3 3.407 -0.865 2.984 1.00 31.20 C ANISOU 2236 CG ARG B 3 3515 4563 3776 251 -184 -960 C ATOM 2237 CD ARG B 3 4.409 -0.254 3.939 1.00 38.11 C ANISOU 2237 CD ARG B 3 4571 5297 4611 257 -330 -896 C ATOM 2238 NE ARG B 3 4.779 1.095 3.528 1.00 43.10 N ANISOU 2238 NE ARG B 3 5206 5942 5229 220 -474 -813 N ATOM 2239 CZ ARG B 3 5.848 1.378 2.800 1.00 58.76 C ANISOU 2239 CZ ARG B 3 7033 8025 7270 140 -600 -716 C ATOM 2240 NH1 ARG B 3 6.100 2.630 2.443 1.00 47.65 N ANISOU 2240 NH1 ARG B 3 5601 6619 5883 87 -762 -592 N ATOM 2241 NH2 ARG B 3 6.674 0.409 2.417 1.00 43.59 N ANISOU 2241 NH2 ARG B 3 4964 6215 5385 127 -576 -714 N ATOM 2242 N THR B 4 2.388 -5.311 2.338 1.00 19.85 N ANISOU 2242 N THR B 4 1834 3054 2654 218 -120 -1186 N ATOM 2243 CA THR B 4 2.460 -6.747 2.575 1.00 21.29 C ANISOU 2243 CA THR B 4 2011 3110 2967 207 -195 -1235 C ATOM 2244 C THR B 4 3.656 -7.056 3.482 1.00 24.58 C ANISOU 2244 C THR B 4 2523 3444 3371 229 -222 -1225 C ATOM 2245 O THR B 4 4.720 -6.469 3.307 1.00 23.80 O ANISOU 2245 O THR B 4 2441 3424 3180 260 -239 -1238 O ATOM 2246 CB THR B 4 2.585 -7.482 1.205 1.00 31.53 C ANISOU 2246 CB THR B 4 3215 4460 4304 245 -309 -1410 C ATOM 2247 OG1 THR B 4 1.460 -7.136 0.398 1.00 34.71 O ANISOU 2247 OG1 THR B 4 3535 4936 4718 211 -293 -1407 O ATOM 2248 CG2 THR B 4 2.624 -8.988 1.341 1.00 34.87 C ANISOU 2248 CG2 THR B 4 3662 4706 4882 247 -454 -1487 C ATOM 2249 N PRO B 5 3.522 -7.985 4.429 1.00 22.38 N ANISOU 2249 N PRO B 5 2284 3020 3199 205 -240 -1168 N ATOM 2250 CA PRO B 5 4.683 -8.312 5.272 1.00 21.90 C ANISOU 2250 CA PRO B 5 2308 2886 3129 221 -265 -1157 C ATOM 2251 C PRO B 5 5.745 -9.108 4.527 1.00 25.47 C ANISOU 2251 C PRO B 5 2720 3349 3609 269 -365 -1298 C ATOM 2252 O PRO B 5 5.447 -9.918 3.648 1.00 25.50 O ANISOU 2252 O PRO B 5 2663 3336 3687 303 -455 -1422 O ATOM 2253 CB PRO B 5 4.080 -9.171 6.391 1.00 23.47 C ANISOU 2253 CB PRO B 5 2517 2952 3450 187 -254 -1035 C ATOM 2254 CG PRO B 5 2.856 -9.805 5.772 1.00 29.42 C ANISOU 2254 CG PRO B 5 3151 3678 4350 136 -305 -1015 C ATOM 2255 CD PRO B 5 2.319 -8.765 4.815 1.00 24.77 C ANISOU 2255 CD PRO B 5 2529 3231 3651 151 -248 -1060 C ATOM 2256 N LYS B 6 6.983 -8.893 4.917 1.00 21.55 N ANISOU 2256 N LYS B 6 2269 2876 3042 293 -370 -1267 N ATOM 2257 CA LYS B 6 8.119 -9.702 4.506 1.00 21.48 C ANISOU 2257 CA LYS B 6 2230 2893 3038 375 -442 -1346 C ATOM 2258 C LYS B 6 8.236 -10.735 5.642 1.00 24.81 C ANISOU 2258 C LYS B 6 2718 3118 3589 331 -468 -1311 C ATOM 2259 O LYS B 6 8.079 -10.366 6.801 1.00 22.52 O ANISOU 2259 O LYS B 6 2501 2758 3300 261 -411 -1182 O ATOM 2260 CB LYS B 6 9.370 -8.831 4.321 1.00 22.82 C ANISOU 2260 CB LYS B 6 2370 3224 3076 408 -435 -1250 C ATOM 2261 CG LYS B 6 10.595 -9.633 3.891 1.00 29.99 C ANISOU 2261 CG LYS B 6 3220 4221 3955 536 -482 -1280 C ATOM 2262 CD LYS B 6 11.801 -8.741 3.651 1.00 30.85 C ANISOU 2262 CD LYS B 6 3241 4533 3949 559 -487 -1096 C ATOM 2263 CE LYS B 6 12.836 -9.501 2.840 1.00 38.02 C ANISOU 2263 CE LYS B 6 4037 5635 4775 766 -504 -1115 C ATOM 2264 NZ LYS B 6 14.068 -8.696 2.640 1.00 44.17 N ANISOU 2264 NZ LYS B 6 4674 6648 5459 786 -515 -844 N ATOM 2265 N ILE B 7 8.430 -12.010 5.328 1.00 22.26 N ANISOU 2265 N ILE B 7 2380 2706 3373 390 -570 -1425 N ATOM 2266 CA ILE B 7 8.427 -13.085 6.335 1.00 22.76 C ANISOU 2266 CA ILE B 7 2477 2568 3602 333 -622 -1376 C ATOM 2267 C ILE B 7 9.707 -13.865 6.214 1.00 27.12 C ANISOU 2267 C ILE B 7 3048 3110 4146 439 -686 -1451 C ATOM 2268 O ILE B 7 9.966 -14.432 5.161 1.00 25.73 O ANISOU 2268 O ILE B 7 2861 2969 3944 589 -785 -1619 O ATOM 2269 CB ILE B 7 7.185 -14.028 6.151 1.00 26.49 C ANISOU 2269 CB ILE B 7 2910 2873 4283 279 -749 -1406 C ATOM 2270 CG1 ILE B 7 5.831 -13.254 6.234 1.00 25.67 C ANISOU 2270 CG1 ILE B 7 2757 2818 4180 189 -668 -1282 C ATOM 2271 CG2 ILE B 7 7.220 -15.232 7.144 1.00 26.68 C ANISOU 2271 CG2 ILE B 7 2930 2685 4520 211 -842 -1316 C ATOM 2272 CD1 ILE B 7 4.689 -13.918 5.317 1.00 30.68 C ANISOU 2272 CD1 ILE B 7 3325 3355 4977 156 -838 -1346 C ATOM 2273 N GLN B 8 10.504 -13.910 7.280 1.00 23.30 N ANISOU 2273 N GLN B 8 2600 2588 3665 390 -635 -1326 N ATOM 2274 CA GLN B 8 11.779 -14.616 7.206 1.00 24.37 C ANISOU 2274 CA GLN B 8 2740 2736 3783 496 -678 -1361 C ATOM 2275 C GLN B 8 11.901 -15.546 8.395 1.00 28.08 C ANISOU 2275 C GLN B 8 3241 3009 4421 411 -708 -1284 C ATOM 2276 O GLN B 8 11.646 -15.152 9.529 1.00 26.30 O ANISOU 2276 O GLN B 8 3037 2740 4218 284 -632 -1127 O ATOM 2277 CB GLN B 8 12.939 -13.616 7.111 1.00 24.56 C ANISOU 2277 CB GLN B 8 2740 2970 3621 530 -598 -1240 C ATOM 2278 CG GLN B 8 12.803 -12.680 5.898 1.00 29.38 C ANISOU 2278 CG GLN B 8 3277 3803 4083 611 -577 -1272 C ATOM 2279 CD GLN B 8 13.836 -11.598 5.906 1.00 35.07 C ANISOU 2279 CD GLN B 8 3940 4712 4671 594 -540 -1071 C ATOM 2280 OE1 GLN B 8 13.625 -10.483 6.399 1.00 30.79 O ANISOU 2280 OE1 GLN B 8 3436 4155 4107 457 -528 -947 O ATOM 2281 NE2 GLN B 8 14.998 -11.932 5.431 1.00 29.73 N ANISOU 2281 NE2 GLN B 8 3178 4204 3913 741 -549 -1009 N ATOM 2282 N VAL B 9 12.228 -16.806 8.111 1.00 26.59 N ANISOU 2282 N VAL B 9 3057 2700 4345 505 -836 -1399 N ATOM 2283 CA VAL B 9 12.317 -17.897 9.090 1.00 26.79 C ANISOU 2283 CA VAL B 9 3088 2516 4575 431 -907 -1334 C ATOM 2284 C VAL B 9 13.756 -18.370 9.143 1.00 29.90 C ANISOU 2284 C VAL B 9 3503 2953 4903 552 -902 -1345 C ATOM 2285 O VAL B 9 14.330 -18.686 8.099 1.00 30.17 O ANISOU 2285 O VAL B 9 3555 3074 4833 769 -963 -1500 O ATOM 2286 CB VAL B 9 11.346 -19.056 8.720 1.00 32.16 C ANISOU 2286 CB VAL B 9 3762 2958 5500 423 -1132 -1441 C ATOM 2287 CG1 VAL B 9 11.253 -20.078 9.853 1.00 32.58 C ANISOU 2287 CG1 VAL B 9 3774 2795 5809 297 -1216 -1297 C ATOM 2288 CG2 VAL B 9 9.955 -18.524 8.354 1.00 31.74 C ANISOU 2288 CG2 VAL B 9 3666 2911 5483 332 -1145 -1420 C ATOM 2289 N TYR B 10 14.336 -18.435 10.348 1.00 23.58 N ANISOU 2289 N TYR B 10 2698 2116 4146 442 -827 -1170 N ATOM 2290 CA TYR B 10 15.743 -18.786 10.524 1.00 23.16 C ANISOU 2290 CA TYR B 10 2648 2124 4029 531 -800 -1122 C ATOM 2291 C TYR B 10 16.020 -19.176 11.951 1.00 27.54 C ANISOU 2291 C TYR B 10 3195 2557 4710 377 -765 -949 C ATOM 2292 O TYR B 10 15.234 -18.850 12.840 1.00 27.43 O ANISOU 2292 O TYR B 10 3177 2485 4762 223 -722 -835 O ATOM 2293 CB TYR B 10 16.637 -17.580 10.143 1.00 22.36 C ANISOU 2293 CB TYR B 10 2524 2291 3683 579 -687 -1018 C ATOM 2294 CG TYR B 10 16.286 -16.306 10.899 1.00 22.61 C ANISOU 2294 CG TYR B 10 2581 2355 3653 393 -607 -862 C ATOM 2295 CD1 TYR B 10 17.097 -15.835 11.926 1.00 23.77 C ANISOU 2295 CD1 TYR B 10 2758 2513 3760 283 -568 -663 C ATOM 2296 CD2 TYR B 10 15.158 -15.556 10.562 1.00 23.26 C ANISOU 2296 CD2 TYR B 10 2679 2453 3707 349 -594 -920 C ATOM 2297 CE1 TYR B 10 16.792 -14.648 12.604 1.00 24.69 C ANISOU 2297 CE1 TYR B 10 2952 2631 3799 159 -548 -554 C ATOM 2298 CE2 TYR B 10 14.822 -14.397 11.257 1.00 23.35 C ANISOU 2298 CE2 TYR B 10 2750 2482 3641 230 -542 -801 C ATOM 2299 CZ TYR B 10 15.650 -13.934 12.264 1.00 26.05 C ANISOU 2299 CZ TYR B 10 3153 2813 3931 149 -535 -633 C ATOM 2300 OH TYR B 10 15.305 -12.783 12.938 1.00 24.10 O ANISOU 2300 OH TYR B 10 3016 2553 3589 76 -535 -551 O ATOM 2301 N SER B 11 17.159 -19.816 12.192 1.00 24.91 N ANISOU 2301 N SER B 11 2857 2222 4385 443 -768 -906 N ATOM 2302 CA SER B 11 17.507 -20.195 13.562 1.00 24.29 C ANISOU 2302 CA SER B 11 2763 2045 4422 297 -731 -729 C ATOM 2303 C SER B 11 18.409 -19.130 14.211 1.00 26.70 C ANISOU 2303 C SER B 11 3090 2503 4553 216 -615 -533 C ATOM 2304 O SER B 11 19.132 -18.420 13.512 1.00 25.56 O ANISOU 2304 O SER B 11 2939 2537 4236 296 -589 -505 O ATOM 2305 CB SER B 11 18.182 -21.558 13.584 1.00 25.32 C ANISOU 2305 CB SER B 11 2877 2049 4694 391 -822 -774 C ATOM 2306 OG SER B 11 19.324 -21.540 12.749 1.00 30.10 O ANISOU 2306 OG SER B 11 3491 2822 5123 602 -799 -818 O ATOM 2307 N ARG B 12 18.387 -19.039 15.547 1.00 25.80 N ANISOU 2307 N ARG B 12 3808 2167 3827 627 -803 -877 N ATOM 2308 CA ARG B 12 19.232 -18.095 16.282 1.00 25.71 C ANISOU 2308 CA ARG B 12 3866 2196 3707 529 -667 -909 C ATOM 2309 C ARG B 12 20.720 -18.373 15.983 1.00 30.70 C ANISOU 2309 C ARG B 12 4405 2879 4383 570 -797 -1068 C ATOM 2310 O ARG B 12 21.465 -17.450 15.670 1.00 28.77 O ANISOU 2310 O ARG B 12 4139 2693 4100 568 -635 -1173 O ATOM 2311 CB ARG B 12 18.968 -18.210 17.794 1.00 24.92 C ANISOU 2311 CB ARG B 12 3889 2030 3551 391 -700 -783 C ATOM 2312 CG ARG B 12 19.958 -17.397 18.638 1.00 25.11 C ANISOU 2312 CG ARG B 12 3973 2130 3437 250 -621 -864 C ATOM 2313 CD ARG B 12 19.587 -17.412 20.095 1.00 25.86 C ANISOU 2313 CD ARG B 12 4222 2176 3427 129 -630 -738 C ATOM 2314 NE ARG B 12 18.255 -16.850 20.325 1.00 24.25 N ANISOU 2314 NE ARG B 12 4175 1846 3193 97 -390 -559 N ATOM 2315 CZ ARG B 12 17.703 -16.713 21.521 1.00 33.38 C ANISOU 2315 CZ ARG B 12 5518 2903 4262 11 -321 -409 C ATOM 2316 NH1 ARG B 12 18.349 -17.116 22.607 1.00 26.14 N ANISOU 2316 NH1 ARG B 12 4647 2033 3252 -41 -494 -434 N ATOM 2317 NH2 ARG B 12 16.502 -16.170 21.642 1.00 25.52 N ANISOU 2317 NH2 ARG B 12 4665 1770 3261 -5 -67 -210 N ATOM 2318 N HIS B 13 21.121 -19.646 16.097 1.00 29.03 N ANISOU 2318 N HIS B 13 4134 2625 4271 616 -1049 -1065 N ATOM 2319 CA HIS B 13 22.487 -20.117 15.877 1.00 30.68 C ANISOU 2319 CA HIS B 13 4247 2867 4542 673 -1177 -1144 C ATOM 2320 C HIS B 13 22.504 -21.041 14.662 1.00 33.32 C ANISOU 2320 C HIS B 13 4528 3122 5010 828 -1263 -1195 C ATOM 2321 O HIS B 13 21.459 -21.638 14.381 1.00 32.39 O ANISOU 2321 O HIS B 13 4434 2936 4938 846 -1299 -1168 O ATOM 2322 CB HIS B 13 23.015 -20.875 17.140 1.00 33.23 C ANISOU 2322 CB HIS B 13 4552 3223 4850 614 -1347 -1047 C ATOM 2323 CG HIS B 13 22.856 -20.140 18.442 1.00 37.77 C ANISOU 2323 CG HIS B 13 5212 3877 5260 456 -1294 -998 C ATOM 2324 ND1 HIS B 13 23.592 -18.992 18.726 1.00 40.38 N ANISOU 2324 ND1 HIS B 13 5541 4329 5473 328 -1190 -1108 N ATOM 2325 CD2 HIS B 13 22.064 -20.419 19.503 1.00 39.94 C ANISOU 2325 CD2 HIS B 13 5589 4107 5478 411 -1313 -862 C ATOM 2326 CE1 HIS B 13 23.223 -18.612 19.941 1.00 40.01 C ANISOU 2326 CE1 HIS B 13 5610 4321 5273 187 -1159 -1049 C ATOM 2327 NE2 HIS B 13 22.310 -19.435 20.453 1.00 40.37 N ANISOU 2327 NE2 HIS B 13 5729 4264 5345 250 -1232 -886 N ATOM 2328 N PRO B 14 23.653 -21.234 13.946 1.00 31.92 N ANISOU 2328 N PRO B 14 4286 2937 4907 933 -1292 -1267 N ATOM 2329 CA PRO B 14 23.673 -22.235 12.849 1.00 32.74 C ANISOU 2329 CA PRO B 14 4384 2931 5126 1070 -1361 -1311 C ATOM 2330 C PRO B 14 23.115 -23.577 13.357 1.00 38.16 C ANISOU 2330 C PRO B 14 5083 3520 5896 1032 -1481 -1231 C ATOM 2331 O PRO B 14 23.464 -24.003 14.465 1.00 37.12 O ANISOU 2331 O PRO B 14 4928 3403 5774 983 -1538 -1112 O ATOM 2332 CB PRO B 14 25.165 -22.332 12.482 1.00 35.17 C ANISOU 2332 CB PRO B 14 4634 3215 5513 1168 -1368 -1322 C ATOM 2333 CG PRO B 14 25.737 -20.987 12.889 1.00 38.68 C ANISOU 2333 CG PRO B 14 5036 3775 5884 1104 -1254 -1361 C ATOM 2334 CD PRO B 14 24.986 -20.614 14.140 1.00 34.18 C ANISOU 2334 CD PRO B 14 4504 3295 5188 921 -1259 -1306 C ATOM 2335 N ALA B 15 22.161 -24.174 12.618 1.00 35.65 N ANISOU 2335 N ALA B 15 4793 3124 5630 1051 -1498 -1299 N ATOM 2336 CA ALA B 15 21.473 -25.387 13.052 1.00 36.18 C ANISOU 2336 CA ALA B 15 4866 3067 5814 1000 -1555 -1255 C ATOM 2337 C ALA B 15 22.368 -26.626 13.043 1.00 42.83 C ANISOU 2337 C ALA B 15 5700 3778 6797 1066 -1564 -1214 C ATOM 2338 O ALA B 15 23.190 -26.816 12.144 1.00 42.19 O ANISOU 2338 O ALA B 15 5633 3651 6746 1158 -1544 -1273 O ATOM 2339 CB ALA B 15 20.243 -25.636 12.193 1.00 37.11 C ANISOU 2339 CB ALA B 15 4987 3159 5953 970 -1569 -1375 C ATOM 2340 N GLU B 16 22.219 -27.439 14.098 1.00 40.60 N ANISOU 2340 N GLU B 16 5400 3425 6601 1046 -1555 -1078 N ATOM 2341 CA GLU B 16 22.894 -28.722 14.310 1.00 41.94 C ANISOU 2341 CA GLU B 16 5552 3465 6918 1126 -1489 -975 C ATOM 2342 C GLU B 16 21.848 -29.667 14.863 1.00 45.71 C ANISOU 2342 C GLU B 16 6037 3789 7543 1090 -1422 -945 C ATOM 2343 O GLU B 16 21.195 -29.331 15.853 1.00 43.73 O ANISOU 2343 O GLU B 16 5781 3580 7256 1056 -1441 -853 O ATOM 2344 CB GLU B 16 24.102 -28.601 15.268 1.00 43.81 C ANISOU 2344 CB GLU B 16 5715 3839 7091 1199 -1502 -772 C ATOM 2345 CG GLU B 16 25.144 -27.562 14.886 1.00 55.83 C ANISOU 2345 CG GLU B 16 7200 5515 8498 1212 -1561 -804 C ATOM 2346 CD GLU B 16 26.161 -27.290 15.978 1.00 82.31 C ANISOU 2346 CD GLU B 16 10445 9071 11758 1227 -1615 -632 C ATOM 2347 OE1 GLU B 16 27.184 -28.013 16.026 1.00 77.39 O ANISOU 2347 OE1 GLU B 16 9743 8455 11206 1337 -1581 -474 O ATOM 2348 OE2 GLU B 16 25.924 -26.374 16.801 1.00 72.49 O ANISOU 2348 OE2 GLU B 16 9194 7989 10361 1126 -1679 -644 O ATOM 2349 N ASN B 17 21.636 -30.814 14.209 1.00 45.37 N ANISOU 2349 N ASN B 17 6019 3541 7678 1092 -1316 -1034 N ATOM 2350 CA ASN B 17 20.627 -31.770 14.678 1.00 46.80 C ANISOU 2350 CA ASN B 17 6192 3535 8054 1051 -1205 -1034 C ATOM 2351 C ASN B 17 20.957 -32.255 16.086 1.00 50.07 C ANISOU 2351 C ASN B 17 6564 3932 8528 1177 -1092 -766 C ATOM 2352 O ASN B 17 22.119 -32.529 16.384 1.00 50.26 O ANISOU 2352 O ASN B 17 6557 4020 8520 1304 -1031 -598 O ATOM 2353 CB ASN B 17 20.474 -32.947 13.714 1.00 49.36 C ANISOU 2353 CB ASN B 17 6556 3630 8567 1008 -1063 -1207 C ATOM 2354 CG ASN B 17 19.850 -32.566 12.391 1.00 66.12 C ANISOU 2354 CG ASN B 17 8713 5795 10616 879 -1189 -1495 C ATOM 2355 OD1 ASN B 17 20.190 -33.125 11.343 1.00 65.83 O ANISOU 2355 OD1 ASN B 17 8746 5656 10611 861 -1129 -1654 O ATOM 2356 ND2 ASN B 17 18.922 -31.607 12.402 1.00 47.04 N ANISOU 2356 ND2 ASN B 17 6252 3538 8082 801 -1346 -1549 N ATOM 2357 N GLY B 18 19.952 -32.239 16.954 1.00 45.65 N ANISOU 2357 N GLY B 18 5997 3318 8029 1160 -1074 -703 N ATOM 2358 CA GLY B 18 20.089 -32.667 18.337 1.00 46.11 C ANISOU 2358 CA GLY B 18 6030 3361 8130 1314 -957 -446 C ATOM 2359 C GLY B 18 20.599 -31.611 19.295 1.00 50.10 C ANISOU 2359 C GLY B 18 6535 4132 8368 1354 -1103 -288 C ATOM 2360 O GLY B 18 20.721 -31.889 20.491 1.00 51.06 O ANISOU 2360 O GLY B 18 6640 4289 8470 1497 -1031 -71 O ATOM 2361 N LYS B 19 20.877 -30.383 18.803 1.00 45.20 N ANISOU 2361 N LYS B 19 5936 3700 7536 1235 -1285 -402 N ATOM 2362 CA LYS B 19 21.356 -29.305 19.669 1.00 44.63 C ANISOU 2362 CA LYS B 19 5874 3873 7211 1221 -1400 -306 C ATOM 2363 C LYS B 19 20.293 -28.220 19.787 1.00 46.63 C ANISOU 2363 C LYS B 19 6220 4127 7370 1083 -1450 -374 C ATOM 2364 O LYS B 19 19.792 -27.725 18.778 1.00 43.96 O ANISOU 2364 O LYS B 19 5898 3763 7040 980 -1476 -536 O ATOM 2365 CB LYS B 19 22.701 -28.730 19.186 1.00 47.47 C ANISOU 2365 CB LYS B 19 6171 4443 7422 1207 -1498 -348 C ATOM 2366 CG LYS B 19 23.865 -29.706 19.362 1.00 54.35 C ANISOU 2366 CG LYS B 19 6937 5360 8352 1367 -1433 -182 C ATOM 2367 CD LYS B 19 25.207 -29.063 19.038 1.00 65.16 C ANISOU 2367 CD LYS B 19 8222 6947 9588 1353 -1538 -186 C ATOM 2368 CE LYS B 19 26.351 -30.047 19.117 1.00 79.37 C ANISOU 2368 CE LYS B 19 9903 8792 11461 1523 -1450 28 C ATOM 2369 NZ LYS B 19 27.643 -29.425 18.718 1.00 88.00 N ANISOU 2369 NZ LYS B 19 10897 10071 12468 1508 -1550 33 N ATOM 2370 N SER B 20 19.932 -27.883 21.036 1.00 39.55 N ANISOU 2370 N SER B 20 6138 2478 6410 749 -1382 -440 N ATOM 2371 CA SER B 20 18.923 -26.887 21.378 1.00 39.07 C ANISOU 2371 CA SER B 20 5990 2497 6356 583 -1174 -285 C ATOM 2372 C SER B 20 19.243 -25.552 20.708 1.00 40.73 C ANISOU 2372 C SER B 20 6128 3010 6340 590 -1111 -450 C ATOM 2373 O SER B 20 20.406 -25.139 20.613 1.00 38.13 O ANISOU 2373 O SER B 20 5817 2889 5780 705 -1132 -565 O ATOM 2374 CB SER B 20 18.814 -26.715 22.887 1.00 44.20 C ANISOU 2374 CB SER B 20 6706 3174 6915 572 -973 -4 C ATOM 2375 OG SER B 20 17.566 -26.123 23.208 1.00 55.98 O ANISOU 2375 OG SER B 20 8110 4673 8489 437 -796 187 O ATOM 2376 N ASN B 21 18.201 -24.930 20.167 1.00 37.01 N ANISOU 2376 N ASN B 21 5551 2548 5964 465 -1051 -449 N ATOM 2377 CA ASN B 21 18.309 -23.696 19.412 1.00 33.89 C ANISOU 2377 CA ASN B 21 5072 2399 5407 455 -1001 -581 C ATOM 2378 C ASN B 21 17.017 -22.900 19.569 1.00 35.02 C ANISOU 2378 C ASN B 21 5140 2540 5625 303 -848 -458 C ATOM 2379 O ASN B 21 16.163 -23.253 20.385 1.00 35.41 O ANISOU 2379 O ASN B 21 5196 2447 5813 225 -755 -246 O ATOM 2380 CB ASN B 21 18.561 -24.085 17.930 1.00 32.70 C ANISOU 2380 CB ASN B 21 4863 2269 5294 557 -1192 -824 C ATOM 2381 CG ASN B 21 19.348 -23.085 17.119 1.00 39.05 C ANISOU 2381 CG ASN B 21 5586 3384 5866 642 -1171 -951 C ATOM 2382 OD1 ASN B 21 19.267 -21.864 17.316 1.00 29.87 O ANISOU 2382 OD1 ASN B 21 4372 2382 4596 554 -1031 -882 O ATOM 2383 ND2 ASN B 21 20.113 -23.591 16.174 1.00 28.72 N ANISOU 2383 ND2 ASN B 21 4261 2167 4484 835 -1320 -1124 N ATOM 2384 N PHE B 22 16.882 -21.819 18.804 1.00 28.55 N ANISOU 2384 N PHE B 22 4240 1899 4710 277 -813 -563 N ATOM 2385 CA PHE B 22 15.673 -21.017 18.761 1.00 27.23 C ANISOU 2385 CA PHE B 22 3997 1749 4600 159 -688 -484 C ATOM 2386 C PHE B 22 15.274 -20.834 17.321 1.00 31.78 C ANISOU 2386 C PHE B 22 4463 2362 5249 150 -785 -657 C ATOM 2387 O PHE B 22 16.120 -20.546 16.474 1.00 29.94 O ANISOU 2387 O PHE B 22 4208 2289 4880 251 -862 -816 O ATOM 2388 CB PHE B 22 15.851 -19.647 19.461 1.00 26.83 C ANISOU 2388 CB PHE B 22 3985 1882 4325 155 -541 -421 C ATOM 2389 CG PHE B 22 15.762 -19.710 20.967 1.00 28.85 C ANISOU 2389 CG PHE B 22 4351 2105 4504 190 -422 -228 C ATOM 2390 CD1 PHE B 22 14.581 -19.384 21.623 1.00 33.11 C ANISOU 2390 CD1 PHE B 22 4875 2632 5073 156 -261 -47 C ATOM 2391 CD2 PHE B 22 16.853 -20.118 21.729 1.00 31.45 C ANISOU 2391 CD2 PHE B 22 4793 2441 4713 291 -467 -218 C ATOM 2392 CE1 PHE B 22 14.497 -19.443 23.022 1.00 35.97 C ANISOU 2392 CE1 PHE B 22 5341 3012 5316 252 -136 148 C ATOM 2393 CE2 PHE B 22 16.771 -20.184 23.126 1.00 36.17 C ANISOU 2393 CE2 PHE B 22 5505 3033 5206 370 -361 -41 C ATOM 2394 CZ PHE B 22 15.593 -19.842 23.763 1.00 35.76 C ANISOU 2394 CZ PHE B 22 5442 2988 5156 364 -191 144 C ATOM 2395 N LEU B 23 13.991 -21.018 17.043 1.00 29.51 N ANISOU 2395 N LEU B 23 4094 1944 5175 49 -783 -609 N ATOM 2396 CA LEU B 23 13.442 -20.816 15.719 1.00 29.84 C ANISOU 2396 CA LEU B 23 4035 2015 5289 52 -883 -775 C ATOM 2397 C LEU B 23 12.799 -19.449 15.696 1.00 30.83 C ANISOU 2397 C LEU B 23 4098 2305 5311 -19 -713 -718 C ATOM 2398 O LEU B 23 11.950 -19.166 16.539 1.00 30.98 O ANISOU 2398 O LEU B 23 4101 2282 5388 -113 -567 -531 O ATOM 2399 CB LEU B 23 12.436 -21.915 15.362 1.00 33.02 C ANISOU 2399 CB LEU B 23 4374 2139 6032 -15 -1046 -778 C ATOM 2400 CG LEU B 23 11.720 -21.747 14.020 1.00 39.43 C ANISOU 2400 CG LEU B 23 5085 2960 6936 3 -1184 -965 C ATOM 2401 CD1 LEU B 23 12.673 -21.995 12.841 1.00 39.66 C ANISOU 2401 CD1 LEU B 23 5161 3102 6807 228 -1376 -1249 C ATOM 2402 CD2 LEU B 23 10.504 -22.630 13.964 1.00 45.84 C ANISOU 2402 CD2 LEU B 23 5804 3471 8141 -126 -1330 -897 C ATOM 2403 N ASN B 24 13.238 -18.595 14.767 1.00 24.32 N ANISOU 2403 N ASN B 24 3237 1684 4321 50 -725 -856 N ATOM 2404 CA ASN B 24 12.750 -17.226 14.620 1.00 22.84 C ANISOU 2404 CA ASN B 24 3001 1648 4030 -1 -593 -819 C ATOM 2405 C ASN B 24 11.919 -17.039 13.379 1.00 28.34 C ANISOU 2405 C ASN B 24 3587 2377 4804 8 -656 -935 C ATOM 2406 O ASN B 24 12.220 -17.624 12.342 1.00 29.02 O ANISOU 2406 O ASN B 24 3644 2479 4904 123 -815 -1101 O ATOM 2407 CB ASN B 24 13.940 -16.253 14.510 1.00 19.44 C ANISOU 2407 CB ASN B 24 2591 1424 3371 59 -565 -841 C ATOM 2408 CG ASN B 24 14.864 -16.206 15.693 1.00 35.10 C ANISOU 2408 CG ASN B 24 4680 3402 5253 64 -532 -752 C ATOM 2409 OD1 ASN B 24 16.089 -16.099 15.554 1.00 34.72 O ANISOU 2409 OD1 ASN B 24 4632 3466 5095 131 -589 -783 O ATOM 2410 ND2 ASN B 24 14.310 -16.219 16.873 1.00 27.14 N ANISOU 2410 ND2 ASN B 24 3752 2292 4267 14 -439 -626 N ATOM 2411 N CYS B 25 10.902 -16.198 13.478 1.00 25.40 N ANISOU 2411 N CYS B 25 3164 2033 4454 -76 -540 -858 N ATOM 2412 CA CYS B 25 10.118 -15.721 12.358 1.00 25.19 C ANISOU 2412 CA CYS B 25 3035 2079 4457 -61 -573 -955 C ATOM 2413 C CYS B 25 10.020 -14.206 12.491 1.00 26.70 C ANISOU 2413 C CYS B 25 3231 2433 4482 -84 -421 -884 C ATOM 2414 O CYS B 25 9.351 -13.699 13.395 1.00 25.97 O ANISOU 2414 O CYS B 25 3164 2308 4394 -154 -291 -752 O ATOM 2415 CB CYS B 25 8.749 -16.373 12.238 1.00 27.78 C ANISOU 2415 CB CYS B 25 3269 2234 5053 -145 -630 -935 C ATOM 2416 SG CYS B 25 7.814 -15.778 10.808 1.00 32.28 S ANISOU 2416 SG CYS B 25 3716 2905 5644 -99 -701 -1084 S ATOM 2417 N TYR B 26 10.756 -13.499 11.638 1.00 21.22 N ANISOU 2417 N TYR B 26 2513 1915 3634 -2 -443 -954 N ATOM 2418 CA TYR B 26 10.819 -12.046 11.628 1.00 19.72 C ANISOU 2418 CA TYR B 26 2324 1852 3317 -23 -347 -884 C ATOM 2419 C TYR B 26 9.869 -11.549 10.572 1.00 23.78 C ANISOU 2419 C TYR B 26 2743 2443 3850 6 -343 -943 C ATOM 2420 O TYR B 26 10.024 -11.877 9.388 1.00 24.24 O ANISOU 2420 O TYR B 26 2726 2599 3885 119 -434 -1055 O ATOM 2421 CB TYR B 26 12.266 -11.584 11.366 1.00 19.42 C ANISOU 2421 CB TYR B 26 2280 1955 3142 33 -377 -860 C ATOM 2422 CG TYR B 26 12.474 -10.086 11.456 1.00 19.69 C ANISOU 2422 CG TYR B 26 2315 2064 3101 -16 -324 -759 C ATOM 2423 CD1 TYR B 26 12.548 -9.444 12.692 1.00 20.32 C ANISOU 2423 CD1 TYR B 26 2514 2042 3165 -90 -298 -683 C ATOM 2424 CD2 TYR B 26 12.660 -9.319 10.308 1.00 20.45 C ANISOU 2424 CD2 TYR B 26 2300 2329 3143 37 -323 -733 C ATOM 2425 CE1 TYR B 26 12.847 -8.084 12.783 1.00 20.75 C ANISOU 2425 CE1 TYR B 26 2584 2116 3183 -128 -315 -608 C ATOM 2426 CE2 TYR B 26 12.944 -7.957 10.386 1.00 20.45 C ANISOU 2426 CE2 TYR B 26 2291 2360 3120 -23 -307 -612 C ATOM 2427 CZ TYR B 26 13.033 -7.343 11.626 1.00 26.59 C ANISOU 2427 CZ TYR B 26 3198 2989 3916 -115 -323 -563 C ATOM 2428 OH TYR B 26 13.287 -5.996 11.701 1.00 25.53 O ANISOU 2428 OH TYR B 26 3072 2834 3794 -171 -365 -464 O ATOM 2429 N VAL B 27 8.827 -10.849 11.013 1.00 19.73 N ANISOU 2429 N VAL B 27 2236 1893 3367 -63 -248 -876 N ATOM 2430 CA VAL B 27 7.763 -10.352 10.138 1.00 19.47 C ANISOU 2430 CA VAL B 27 2112 1923 3362 -41 -237 -922 C ATOM 2431 C VAL B 27 7.893 -8.831 10.111 1.00 21.05 C ANISOU 2431 C VAL B 27 2346 2225 3428 -38 -158 -850 C ATOM 2432 O VAL B 27 7.820 -8.205 11.156 1.00 19.68 O ANISOU 2432 O VAL B 27 2269 1993 3216 -83 -89 -762 O ATOM 2433 CB VAL B 27 6.380 -10.859 10.623 1.00 25.00 C ANISOU 2433 CB VAL B 27 2762 2499 4237 -113 -203 -883 C ATOM 2434 CG1 VAL B 27 5.297 -10.474 9.639 1.00 25.86 C ANISOU 2434 CG1 VAL B 27 2758 2673 4394 -83 -224 -950 C ATOM 2435 CG2 VAL B 27 6.396 -12.390 10.801 1.00 26.02 C ANISOU 2435 CG2 VAL B 27 2863 2469 4553 -146 -313 -913 C ATOM 2436 N SER B 28 8.137 -8.243 8.932 1.00 17.79 N ANISOU 2436 N SER B 28 1860 1960 2938 39 -186 -880 N ATOM 2437 CA SER B 28 8.416 -6.807 8.869 1.00 17.33 C ANISOU 2437 CA SER B 28 1825 1968 2791 28 -141 -779 C ATOM 2438 C SER B 28 7.857 -6.135 7.629 1.00 21.62 C ANISOU 2438 C SER B 28 2274 2652 3291 111 -130 -793 C ATOM 2439 O SER B 28 7.481 -6.799 6.673 1.00 20.75 O ANISOU 2439 O SER B 28 2076 2625 3183 210 -176 -902 O ATOM 2440 CB SER B 28 9.940 -6.598 8.862 1.00 20.17 C ANISOU 2440 CB SER B 28 2180 2388 3095 27 -183 -693 C ATOM 2441 OG SER B 28 10.507 -7.318 7.771 1.00 26.70 O ANISOU 2441 OG SER B 28 2897 3374 3876 149 -225 -740 O ATOM 2442 N GLY B 29 7.903 -4.809 7.649 1.00 19.60 N ANISOU 2442 N GLY B 29 2044 2410 2992 87 -96 -686 N ATOM 2443 CA GLY B 29 7.520 -3.939 6.546 1.00 19.23 C ANISOU 2443 CA GLY B 29 1918 2496 2893 166 -76 -648 C ATOM 2444 C GLY B 29 6.056 -3.930 6.212 1.00 21.86 C ANISOU 2444 C GLY B 29 2228 2835 3243 212 -46 -747 C ATOM 2445 O GLY B 29 5.693 -3.496 5.123 1.00 21.71 O ANISOU 2445 O GLY B 29 2128 2953 3167 315 -42 -752 O ATOM 2446 N PHE B 30 5.196 -4.325 7.164 1.00 17.37 N ANISOU 2446 N PHE B 30 1716 2135 2749 147 -17 -796 N ATOM 2447 CA PHE B 30 3.766 -4.399 6.886 1.00 17.50 C ANISOU 2447 CA PHE B 30 1669 2166 2815 181 9 -864 C ATOM 2448 C PHE B 30 3.020 -3.162 7.394 1.00 19.57 C ANISOU 2448 C PHE B 30 2004 2402 3030 187 85 -794 C ATOM 2449 O PHE B 30 3.510 -2.440 8.255 1.00 18.18 O ANISOU 2449 O PHE B 30 1959 2143 2804 158 98 -719 O ATOM 2450 CB PHE B 30 3.146 -5.689 7.473 1.00 19.22 C ANISOU 2450 CB PHE B 30 1842 2281 3179 121 -6 -917 C ATOM 2451 CG PHE B 30 3.320 -5.912 8.961 1.00 20.02 C ANISOU 2451 CG PHE B 30 2043 2258 3304 39 62 -824 C ATOM 2452 CD1 PHE B 30 2.338 -5.503 9.863 1.00 21.46 C ANISOU 2452 CD1 PHE B 30 2250 2414 3488 41 168 -741 C ATOM 2453 CD2 PHE B 30 4.443 -6.577 9.459 1.00 20.02 C ANISOU 2453 CD2 PHE B 30 2107 2194 3306 -2 23 -814 C ATOM 2454 CE1 PHE B 30 2.485 -5.739 11.244 1.00 22.40 C ANISOU 2454 CE1 PHE B 30 2465 2458 3588 23 239 -645 C ATOM 2455 CE2 PHE B 30 4.607 -6.778 10.836 1.00 21.89 C ANISOU 2455 CE2 PHE B 30 2445 2333 3539 -45 82 -728 C ATOM 2456 CZ PHE B 30 3.616 -6.378 11.718 1.00 21.39 C ANISOU 2456 CZ PHE B 30 2410 2257 3459 -22 192 -643 C ATOM 2457 N HIS B 31 1.827 -2.939 6.854 1.00 17.85 N ANISOU 2457 N HIS B 31 1706 2250 2828 247 109 -835 N ATOM 2458 CA HIS B 31 0.948 -1.830 7.241 1.00 18.33 C ANISOU 2458 CA HIS B 31 1825 2308 2832 295 179 -787 C ATOM 2459 C HIS B 31 -0.462 -2.160 6.748 1.00 22.78 C ANISOU 2459 C HIS B 31 2241 2947 3466 341 200 -843 C ATOM 2460 O HIS B 31 -0.583 -2.560 5.593 1.00 23.65 O ANISOU 2460 O HIS B 31 2237 3140 3608 382 124 -932 O ATOM 2461 CB HIS B 31 1.441 -0.482 6.662 1.00 18.86 C ANISOU 2461 CB HIS B 31 1962 2405 2800 347 153 -729 C ATOM 2462 CG HIS B 31 0.987 0.695 7.475 1.00 22.45 C ANISOU 2462 CG HIS B 31 2562 2776 3191 393 178 -681 C ATOM 2463 ND1 HIS B 31 -0.335 1.079 7.501 1.00 24.57 N ANISOU 2463 ND1 HIS B 31 2808 3099 3429 488 241 -705 N ATOM 2464 CD2 HIS B 31 1.703 1.525 8.272 1.00 23.18 C ANISOU 2464 CD2 HIS B 31 2828 2732 3248 379 118 -626 C ATOM 2465 CE1 HIS B 31 -0.396 2.119 8.319 1.00 23.77 C ANISOU 2465 CE1 HIS B 31 2881 2904 3245 556 230 -673 C ATOM 2466 NE2 HIS B 31 0.812 2.420 8.807 1.00 24.35 N ANISOU 2466 NE2 HIS B 31 3086 2843 3322 492 137 -637 N ATOM 2467 N PRO B 32 -1.527 -2.138 7.571 1.00 20.75 N ANISOU 2467 N PRO B 32 1960 2679 3244 351 288 -791 N ATOM 2468 CA PRO B 32 -1.626 -1.662 8.977 1.00 20.15 C ANISOU 2468 CA PRO B 32 2020 2550 3085 383 386 -693 C ATOM 2469 C PRO B 32 -1.054 -2.702 9.962 1.00 24.41 C ANISOU 2469 C PRO B 32 2583 3003 3689 298 405 -640 C ATOM 2470 O PRO B 32 -0.509 -3.728 9.536 1.00 21.76 O ANISOU 2470 O PRO B 32 2172 2625 3470 201 331 -686 O ATOM 2471 CB PRO B 32 -3.136 -1.375 9.135 1.00 21.96 C ANISOU 2471 CB PRO B 32 2144 2878 3321 476 483 -644 C ATOM 2472 CG PRO B 32 -3.775 -2.418 8.243 1.00 26.80 C ANISOU 2472 CG PRO B 32 2518 3529 4137 398 425 -690 C ATOM 2473 CD PRO B 32 -2.861 -2.458 7.024 1.00 21.69 C ANISOU 2473 CD PRO B 32 1894 2877 3471 380 289 -821 C ATOM 2474 N SER B 33 -1.128 -2.415 11.273 1.00 23.04 N ANISOU 2474 N SER B 33 2533 2807 3415 367 493 -552 N ATOM 2475 CA SER B 33 -0.433 -3.198 12.302 1.00 23.38 C ANISOU 2475 CA SER B 33 2642 2773 3466 323 512 -492 C ATOM 2476 C SER B 33 -1.065 -4.529 12.698 1.00 28.59 C ANISOU 2476 C SER B 33 3123 3439 4299 252 588 -377 C ATOM 2477 O SER B 33 -0.341 -5.351 13.249 1.00 27.52 O ANISOU 2477 O SER B 33 3024 3223 4209 187 572 -342 O ATOM 2478 CB SER B 33 -0.241 -2.354 13.561 1.00 26.11 C ANISOU 2478 CB SER B 33 3208 3105 3608 477 552 -452 C ATOM 2479 OG SER B 33 -1.493 -1.969 14.088 1.00 30.90 O ANISOU 2479 OG SER B 33 3779 3832 4129 639 686 -364 O ATOM 2480 N ASP B 34 -2.377 -4.756 12.462 1.00 27.50 N ANISOU 2480 N ASP B 34 2782 3385 4281 259 658 -297 N ATOM 2481 CA ASP B 34 -2.964 -6.045 12.861 1.00 29.87 C ANISOU 2481 CA ASP B 34 2878 3658 4813 161 706 -137 C ATOM 2482 C ASP B 34 -2.400 -7.152 11.985 1.00 33.65 C ANISOU 2482 C ASP B 34 3274 3996 5516 -6 524 -254 C ATOM 2483 O ASP B 34 -2.348 -7.014 10.760 1.00 31.93 O ANISOU 2483 O ASP B 34 3019 3778 5334 -23 389 -428 O ATOM 2484 CB ASP B 34 -4.503 -6.052 12.831 1.00 33.98 C ANISOU 2484 CB ASP B 34 3156 4297 5458 192 806 15 C ATOM 2485 CG ASP B 34 -5.124 -7.280 13.500 1.00 62.35 C ANISOU 2485 CG ASP B 34 6517 7862 9311 93 879 274 C ATOM 2486 OD1 ASP B 34 -4.626 -7.691 14.586 1.00 65.85 O ANISOU 2486 OD1 ASP B 34 7044 8285 9690 119 975 418 O ATOM 2487 OD2 ASP B 34 -6.124 -7.818 12.954 1.00 74.26 O ANISOU 2487 OD2 ASP B 34 7748 9366 11101 -8 830 351 O ATOM 2488 N ILE B 35 -1.926 -8.223 12.631 1.00 31.08 N ANISOU 2488 N ILE B 35 2940 3560 5310 -92 515 -163 N ATOM 2489 CA ILE B 35 -1.303 -9.356 11.960 1.00 30.12 C ANISOU 2489 CA ILE B 35 2774 3283 5386 -215 324 -279 C ATOM 2490 C ILE B 35 -1.429 -10.610 12.838 1.00 34.26 C ANISOU 2490 C ILE B 35 3201 3682 6135 -316 346 -78 C ATOM 2491 O ILE B 35 -1.425 -10.526 14.068 1.00 34.53 O ANISOU 2491 O ILE B 35 3288 3765 6065 -263 524 126 O ATOM 2492 CB ILE B 35 0.183 -9.035 11.600 1.00 30.75 C ANISOU 2492 CB ILE B 35 3065 3349 5270 -177 238 -462 C ATOM 2493 CG1 ILE B 35 0.726 -9.952 10.484 1.00 30.52 C ANISOU 2493 CG1 ILE B 35 2989 3230 5377 -221 20 -646 C ATOM 2494 CG2 ILE B 35 1.103 -9.003 12.836 1.00 29.79 C ANISOU 2494 CG2 ILE B 35 3120 3201 4998 -150 328 -369 C ATOM 2495 CD1 ILE B 35 1.790 -9.322 9.653 1.00 33.44 C ANISOU 2495 CD1 ILE B 35 3477 3686 5543 -136 -46 -809 C ATOM 2496 N GLU B 36 -1.534 -11.759 12.195 1.00 30.25 N ANISOU 2496 N GLU B 36 2559 3007 5928 -438 149 -135 N ATOM 2497 CA GLU B 36 -1.587 -13.031 12.894 1.00 32.60 C ANISOU 2497 CA GLU B 36 2758 3133 6495 -556 120 57 C ATOM 2498 C GLU B 36 -0.379 -13.851 12.484 1.00 36.30 C ANISOU 2498 C GLU B 36 3361 3438 6992 -581 -84 -140 C ATOM 2499 O GLU B 36 -0.128 -14.011 11.290 1.00 36.20 O ANISOU 2499 O GLU B 36 3359 3380 7016 -558 -302 -403 O ATOM 2500 CB GLU B 36 -2.895 -13.777 12.599 1.00 36.40 C ANISOU 2500 CB GLU B 36 2933 3507 7391 -692 22 204 C ATOM 2501 N VAL B 37 0.404 -14.322 13.464 1.00 32.51 N ANISOU 2501 N VAL B 37 2996 2900 6456 -585 -10 -22 N ATOM 2502 CA VAL B 37 1.593 -15.123 13.179 1.00 31.67 C ANISOU 2502 CA VAL B 37 3020 2654 6361 -586 -191 -192 C ATOM 2503 C VAL B 37 1.577 -16.395 14.023 1.00 39.32 C ANISOU 2503 C VAL B 37 3929 3418 7593 -688 -218 26 C ATOM 2504 O VAL B 37 1.408 -16.336 15.244 1.00 40.30 O ANISOU 2504 O VAL B 37 4050 3599 7663 -683 1 306 O ATOM 2505 CB VAL B 37 2.924 -14.339 13.377 1.00 32.73 C ANISOU 2505 CB VAL B 37 3392 2924 6120 -466 -114 -316 C ATOM 2506 CG1 VAL B 37 4.148 -15.215 13.079 1.00 31.78 C ANISOU 2506 CG1 VAL B 37 3377 2689 6007 -446 -291 -469 C ATOM 2507 CG2 VAL B 37 2.961 -13.056 12.545 1.00 30.75 C ANISOU 2507 CG2 VAL B 37 3184 2854 5644 -378 -93 -480 C ATOM 2508 N ASP B 38 1.799 -17.540 13.361 1.00 36.22 N ANISOU 2508 N ASP B 38 3504 2791 7469 -750 -500 -109 N ATOM 2509 CA ASP B 38 1.923 -18.830 14.014 1.00 38.85 C ANISOU 2509 CA ASP B 38 3799 2878 8085 -850 -587 68 C ATOM 2510 C ASP B 38 3.204 -19.535 13.567 1.00 41.75 C ANISOU 2510 C ASP B 38 4352 3120 8391 -772 -808 -192 C ATOM 2511 O ASP B 38 3.602 -19.430 12.407 1.00 39.70 O ANISOU 2511 O ASP B 38 4156 2887 8043 -671 -1002 -514 O ATOM 2512 CB ASP B 38 0.701 -19.715 13.727 1.00 43.84 C ANISOU 2512 CB ASP B 38 4165 3269 9224 -1022 -774 211 C ATOM 2513 CG ASP B 38 -0.592 -19.186 14.325 1.00 56.11 C ANISOU 2513 CG ASP B 38 5485 4957 10877 -1098 -532 554 C ATOM 2514 OD1 ASP B 38 -0.615 -18.905 15.547 1.00 55.26 O ANISOU 2514 OD1 ASP B 38 5384 4995 10616 -1063 -228 864 O ATOM 2515 OD2 ASP B 38 -1.582 -19.055 13.573 1.00 68.13 O ANISOU 2515 OD2 ASP B 38 6816 6456 12612 -1164 -652 511 O ATOM 2516 N LEU B 39 3.858 -20.228 14.495 1.00 39.01 N ANISOU 2516 N LEU B 39 4091 2669 8061 -784 -765 -41 N ATOM 2517 CA LEU B 39 5.008 -21.063 14.178 1.00 38.73 C ANISOU 2517 CA LEU B 39 4214 2495 8009 -706 -982 -250 C ATOM 2518 C LEU B 39 4.464 -22.490 14.102 1.00 45.66 C ANISOU 2518 C LEU B 39 4974 2998 9377 -835 -1256 -166 C ATOM 2519 O LEU B 39 3.631 -22.876 14.934 1.00 46.72 O ANISOU 2519 O LEU B 39 4945 3015 9792 -991 -1156 193 O ATOM 2520 CB LEU B 39 6.162 -20.907 15.193 1.00 37.73 C ANISOU 2520 CB LEU B 39 4269 2481 7584 -621 -797 -167 C ATOM 2521 CG LEU B 39 6.886 -19.536 15.206 1.00 40.68 C ANISOU 2521 CG LEU B 39 4771 3171 7516 -498 -610 -281 C ATOM 2522 CD1 LEU B 39 7.850 -19.440 16.376 1.00 39.91 C ANISOU 2522 CD1 LEU B 39 4826 3146 7190 -434 -457 -162 C ATOM 2523 CD2 LEU B 39 7.682 -19.320 13.932 1.00 43.86 C ANISOU 2523 CD2 LEU B 39 5241 3661 7762 -374 -784 -616 C ATOM 2524 N LEU B 40 4.849 -23.231 13.052 1.00 43.11 N ANISOU 2524 N LEU B 40 4716 2491 9173 -755 -1618 -486 N ATOM 2525 CA LEU B 40 4.373 -24.590 12.821 1.00 46.02 C ANISOU 2525 CA LEU B 40 4998 2446 10040 -861 -1976 -475 C ATOM 2526 C LEU B 40 5.490 -25.624 12.877 1.00 49.30 C ANISOU 2526 C LEU B 40 5606 2666 10460 -748 -2190 -616 C ATOM 2527 O LEU B 40 6.608 -25.369 12.428 1.00 45.70 O ANISOU 2527 O LEU B 40 5340 2393 9630 -527 -2201 -892 O ATOM 2528 CB LEU B 40 3.640 -24.731 11.460 1.00 47.41 C ANISOU 2528 CB LEU B 40 5082 2497 10433 -835 -2329 -767 C ATOM 2529 CG LEU B 40 2.633 -23.653 11.019 1.00 50.69 C ANISOU 2529 CG LEU B 40 5334 3133 10791 -880 -2186 -751 C ATOM 2530 CD1 LEU B 40 2.122 -23.954 9.613 1.00 52.37 C ANISOU 2530 CD1 LEU B 40 5502 3204 11191 -797 -2601 -1101 C ATOM 2531 CD2 LEU B 40 1.456 -23.541 11.992 1.00 54.06 C ANISOU 2531 CD2 LEU B 40 5506 3525 11510 -1128 -1962 -289 C ATOM 2532 N LYS B 41 5.153 -26.801 13.419 1.00 48.50 N ANISOU 2532 N LYS B 41 5434 2189 10804 -900 -2366 -399 N ATOM 2533 CA LYS B 41 5.991 -27.994 13.496 1.00 50.41 C ANISOU 2533 CA LYS B 41 5837 2145 11174 -820 -2637 -500 C ATOM 2534 C LYS B 41 5.188 -29.120 12.846 1.00 59.28 C ANISOU 2534 C LYS B 41 6851 2789 12884 -928 -3131 -577 C ATOM 2535 O LYS B 41 4.153 -29.523 13.386 1.00 62.21 O ANISOU 2535 O LYS B 41 6989 2922 13727 -1194 -3143 -208 O ATOM 2536 CB LYS B 41 6.403 -28.332 14.945 1.00 52.41 C ANISOU 2536 CB LYS B 41 6119 2374 11419 -902 -2374 -109 C ATOM 2537 CG LYS B 41 7.126 -29.687 15.064 1.00 55.84 C ANISOU 2537 CG LYS B 41 6700 2451 12067 -844 -2685 -170 C ATOM 2538 CD LYS B 41 7.572 -29.993 16.480 1.00 57.94 C ANISOU 2538 CD LYS B 41 7005 2722 12288 -895 -2416 216 C ATOM 2539 CE LYS B 41 8.407 -31.253 16.521 1.00 67.11 C ANISOU 2539 CE LYS B 41 8342 3556 13602 -799 -2725 111 C ATOM 2540 NZ LYS B 41 8.800 -31.606 17.907 1.00 71.43 N ANISOU 2540 NZ LYS B 41 8923 4097 14121 -839 -2473 507 N ATOM 2541 N ASN B 42 5.632 -29.572 11.652 1.00 52.39 N ANISOU 2541 N ASN B 42 6382 2375 11148 -644 -554 -587 N ATOM 2542 CA ASN B 42 5.005 -30.609 10.816 1.00 54.10 C ANISOU 2542 CA ASN B 42 6574 2342 11639 -714 -729 -646 C ATOM 2543 C ASN B 42 3.531 -30.265 10.502 1.00 59.13 C ANISOU 2543 C ASN B 42 7197 2982 12287 -809 -777 -509 C ATOM 2544 O ASN B 42 2.676 -31.149 10.475 1.00 60.41 O ANISOU 2544 O ASN B 42 7274 2965 12715 -869 -920 -356 O ATOM 2545 CB ASN B 42 5.142 -32.008 11.457 1.00 54.83 C ANISOU 2545 CB ASN B 42 6528 2224 12079 -705 -861 -485 C ATOM 2546 CG ASN B 42 6.577 -32.393 11.748 1.00 64.67 C ANISOU 2546 CG ASN B 42 7766 3427 13379 -621 -839 -609 C ATOM 2547 OD1 ASN B 42 6.923 -32.795 12.864 1.00 60.67 O ANISOU 2547 OD1 ASN B 42 7155 2916 12981 -604 -852 -381 O ATOM 2548 ND2 ASN B 42 7.453 -32.236 10.765 1.00 45.66 N ANISOU 2548 ND2 ASN B 42 5463 997 10890 -580 -802 -964 N ATOM 2549 N GLY B 43 3.275 -28.975 10.258 1.00 54.65 N ANISOU 2549 N GLY B 43 6703 2605 11455 -825 -674 -560 N ATOM 2550 CA GLY B 43 1.959 -28.438 9.937 1.00 54.90 C ANISOU 2550 CA GLY B 43 6714 2647 11497 -914 -710 -446 C ATOM 2551 C GLY B 43 1.123 -28.045 11.136 1.00 60.17 C ANISOU 2551 C GLY B 43 7244 3443 12177 -894 -609 -135 C ATOM 2552 O GLY B 43 0.124 -27.338 10.987 1.00 61.35 O ANISOU 2552 O GLY B 43 7359 3638 12313 -946 -596 -53 O ATOM 2553 N GLU B 44 1.521 -28.493 12.331 1.00 56.47 N ANISOU 2553 N GLU B 44 6686 3032 11738 -831 -538 38 N ATOM 2554 CA GLU B 44 0.797 -28.235 13.573 1.00 56.28 C ANISOU 2554 CA GLU B 44 6525 3156 11702 -826 -423 332 C ATOM 2555 C GLU B 44 1.305 -26.977 14.259 1.00 56.64 C ANISOU 2555 C GLU B 44 6619 3467 11435 -749 -223 288 C ATOM 2556 O GLU B 44 2.509 -26.740 14.301 1.00 54.17 O ANISOU 2556 O GLU B 44 6408 3215 10960 -685 -182 136 O ATOM 2557 CB GLU B 44 0.915 -29.442 14.518 1.00 59.40 C ANISOU 2557 CB GLU B 44 6799 3481 12290 -840 -481 572 C ATOM 2558 N ARG B 45 0.384 -26.194 14.829 1.00 53.13 N ANISOU 2558 N ARG B 45 6090 3172 10925 -754 -102 423 N ATOM 2559 CA ARG B 45 0.708 -24.954 15.526 1.00 51.65 C ANISOU 2559 CA ARG B 45 5936 3229 10458 -680 83 379 C ATOM 2560 C ARG B 45 1.476 -25.228 16.833 1.00 54.98 C ANISOU 2560 C ARG B 45 6348 3787 10755 -641 188 513 C ATOM 2561 O ARG B 45 1.047 -26.057 17.638 1.00 55.40 O ANISOU 2561 O ARG B 45 6280 3836 10934 -695 190 759 O ATOM 2562 CB ARG B 45 -0.571 -24.149 15.816 1.00 51.13 C ANISOU 2562 CB ARG B 45 5752 3263 10411 -695 185 479 C ATOM 2563 CG ARG B 45 -0.296 -22.749 16.321 1.00 58.18 C ANISOU 2563 CG ARG B 45 6687 4378 11041 -613 349 372 C ATOM 2564 CD ARG B 45 -1.554 -22.050 16.778 1.00 65.06 C ANISOU 2564 CD ARG B 45 7405 5344 11972 -615 473 468 C ATOM 2565 NE ARG B 45 -1.214 -20.813 17.475 1.00 71.73 N ANISOU 2565 NE ARG B 45 8282 6405 12567 -525 638 367 N ATOM 2566 CZ ARG B 45 -1.175 -20.684 18.796 1.00 87.21 C ANISOU 2566 CZ ARG B 45 10195 8566 14376 -488 830 473 C ATOM 2567 NH1 ARG B 45 -1.499 -21.705 19.580 1.00 71.17 N ANISOU 2567 NH1 ARG B 45 8063 6560 12417 -550 880 709 N ATOM 2568 NH2 ARG B 45 -0.831 -19.526 19.345 1.00 76.77 N ANISOU 2568 NH2 ARG B 45 8923 7421 12823 -404 961 349 N ATOM 2569 N ILE B 46 2.610 -24.516 17.031 1.00 49.50 N ANISOU 2569 N ILE B 46 5782 3212 9813 -565 257 369 N ATOM 2570 CA ILE B 46 3.412 -24.603 18.258 1.00 48.97 C ANISOU 2570 CA ILE B 46 5734 3278 9597 -542 347 491 C ATOM 2571 C ILE B 46 2.732 -23.680 19.279 1.00 54.07 C ANISOU 2571 C ILE B 46 6325 4163 10057 -530 540 594 C ATOM 2572 O ILE B 46 2.406 -22.536 18.941 1.00 52.00 O ANISOU 2572 O ILE B 46 6092 3984 9679 -477 607 446 O ATOM 2573 CB ILE B 46 4.923 -24.267 18.029 1.00 49.39 C ANISOU 2573 CB ILE B 46 5943 3337 9486 -470 325 310 C ATOM 2574 CG1 ILE B 46 5.556 -25.177 16.946 1.00 48.33 C ANISOU 2574 CG1 ILE B 46 5844 2970 9551 -478 160 163 C ATOM 2575 CG2 ILE B 46 5.718 -24.364 19.347 1.00 50.73 C ANISOU 2575 CG2 ILE B 46 6135 3625 9515 -469 396 472 C ATOM 2576 CD1 ILE B 46 6.853 -24.651 16.327 1.00 44.97 C ANISOU 2576 CD1 ILE B 46 5559 2556 8972 -407 148 -77 C ATOM 2577 N GLU B 47 2.472 -24.192 20.499 1.00 53.30 N ANISOU 2577 N GLU B 47 6136 4172 9945 -592 620 844 N ATOM 2578 CA GLU B 47 1.788 -23.438 21.555 1.00 54.76 C ANISOU 2578 CA GLU B 47 6256 4604 9948 -595 830 938 C ATOM 2579 C GLU B 47 2.741 -22.510 22.324 1.00 57.54 C ANISOU 2579 C GLU B 47 6749 5145 9968 -534 947 856 C ATOM 2580 O GLU B 47 2.360 -21.377 22.628 1.00 57.68 O ANISOU 2580 O GLU B 47 6774 5327 9813 -474 1097 754 O ATOM 2581 CB GLU B 47 1.067 -24.385 22.541 1.00 58.97 C ANISOU 2581 CB GLU B 47 6627 5204 10576 -719 872 1252 C ATOM 2582 CG GLU B 47 -0.161 -25.092 21.977 1.00 73.56 C ANISOU 2582 CG GLU B 47 8307 6910 12734 -779 790 1370 C ATOM 2583 CD GLU B 47 -1.332 -24.217 21.565 1.00103.64 C ANISOU 2583 CD GLU B 47 12027 10760 16591 -736 897 1279 C ATOM 2584 OE1 GLU B 47 -1.601 -23.205 22.253 1.00105.59 O ANISOU 2584 OE1 GLU B 47 12257 11228 16635 -691 1108 1224 O ATOM 2585 OE2 GLU B 47 -1.983 -24.546 20.546 1.00 99.10 O ANISOU 2585 OE2 GLU B 47 11397 9982 16272 -752 760 1258 O ATOM 2586 N LYS B 48 3.957 -22.984 22.655 1.00 52.71 N ANISOU 2586 N LYS B 48 6241 4498 9290 -551 868 905 N ATOM 2587 CA LYS B 48 4.936 -22.196 23.408 1.00 51.61 C ANISOU 2587 CA LYS B 48 6249 4514 8848 -509 947 863 C ATOM 2588 C LYS B 48 5.704 -21.250 22.459 1.00 53.03 C ANISOU 2588 C LYS B 48 6569 4642 8937 -383 890 586 C ATOM 2589 O LYS B 48 6.865 -21.500 22.108 1.00 52.97 O ANISOU 2589 O LYS B 48 6663 4529 8935 -359 777 532 O ATOM 2590 CB LYS B 48 5.888 -23.115 24.186 1.00 55.13 C ANISOU 2590 CB LYS B 48 6730 4924 9293 -602 864 1068 C ATOM 2591 N VAL B 49 5.033 -20.168 22.027 1.00 45.86 N ANISOU 2591 N VAL B 49 5651 3805 7969 -313 959 419 N ATOM 2592 CA VAL B 49 5.618 -19.198 21.104 1.00 42.29 C ANISOU 2592 CA VAL B 49 5311 3323 7434 -219 885 179 C ATOM 2593 C VAL B 49 5.564 -17.807 21.740 1.00 45.54 C ANISOU 2593 C VAL B 49 5777 3931 7596 -144 1006 90 C ATOM 2594 O VAL B 49 4.491 -17.324 22.105 1.00 46.98 O ANISOU 2594 O VAL B 49 5854 4209 7789 -139 1129 86 O ATOM 2595 CB VAL B 49 4.942 -19.232 19.701 1.00 44.61 C ANISOU 2595 CB VAL B 49 5542 3464 7945 -228 775 46 C ATOM 2596 CG1 VAL B 49 5.428 -18.087 18.807 1.00 42.30 C ANISOU 2596 CG1 VAL B 49 5350 3182 7539 -163 695 -181 C ATOM 2597 CG2 VAL B 49 5.167 -20.573 19.011 1.00 44.58 C ANISOU 2597 CG2 VAL B 49 5515 3255 8169 -291 641 89 C ATOM 2598 N GLU B 50 6.734 -17.176 21.871 1.00 39.12 N ANISOU 2598 N GLU B 50 5120 3166 6577 -83 963 14 N ATOM 2599 CA GLU B 50 6.859 -15.828 22.410 1.00 37.92 C ANISOU 2599 CA GLU B 50 5045 3175 6189 -2 1035 -89 C ATOM 2600 C GLU B 50 7.048 -14.839 21.265 1.00 36.01 C ANISOU 2600 C GLU B 50 4842 2882 5960 69 903 -301 C ATOM 2601 O GLU B 50 7.383 -15.233 20.140 1.00 32.51 O ANISOU 2601 O GLU B 50 4407 2303 5641 45 764 -360 O ATOM 2602 CB GLU B 50 8.030 -15.754 23.399 1.00 39.35 C ANISOU 2602 CB GLU B 50 5381 3444 6127 3 1050 3 C ATOM 2603 N HIS B 51 6.794 -13.562 21.532 1.00 32.38 N ANISOU 2603 N HIS B 51 4394 2531 5377 142 939 -419 N ATOM 2604 CA HIS B 51 7.021 -12.552 20.524 1.00 29.90 C ANISOU 2604 CA HIS B 51 4112 2178 5069 190 780 -592 C ATOM 2605 C HIS B 51 7.384 -11.241 21.152 1.00 32.89 C ANISOU 2605 C HIS B 51 4574 2683 5240 284 786 -683 C ATOM 2606 O HIS B 51 6.968 -10.937 22.278 1.00 33.07 O ANISOU 2606 O HIS B 51 4582 2825 5158 316 949 -665 O ATOM 2607 CB HIS B 51 5.827 -12.400 19.565 1.00 31.94 C ANISOU 2607 CB HIS B 51 4216 2342 5577 149 727 -671 C ATOM 2608 CG HIS B 51 4.558 -11.919 20.200 1.00 38.16 C ANISOU 2608 CG HIS B 51 4855 3191 6453 174 874 -687 C ATOM 2609 ND1 HIS B 51 4.247 -10.566 20.256 1.00 40.58 N ANISOU 2609 ND1 HIS B 51 5128 3549 6743 248 849 -835 N ATOM 2610 CD2 HIS B 51 3.535 -12.628 20.736 1.00 42.50 C ANISOU 2610 CD2 HIS B 51 5265 3751 7133 132 1036 -577 C ATOM 2611 CE1 HIS B 51 3.056 -10.497 20.836 1.00 42.14 C ANISOU 2611 CE1 HIS B 51 5162 3782 7066 258 1018 -831 C ATOM 2612 NE2 HIS B 51 2.589 -11.710 21.145 1.00 43.57 N ANISOU 2612 NE2 HIS B 51 5275 3953 7327 185 1141 -669 N ATOM 2613 N SER B 52 8.141 -10.432 20.390 1.00 28.11 N ANISOU 2613 N SER B 52 5247 2226 3207 174 255 45 N ATOM 2614 CA SER B 52 8.505 -9.086 20.801 1.00 26.17 C ANISOU 2614 CA SER B 52 4933 2157 2853 253 179 5 C ATOM 2615 C SER B 52 7.270 -8.203 20.717 1.00 27.89 C ANISOU 2615 C SER B 52 4999 2510 3088 105 395 -26 C ATOM 2616 O SER B 52 6.322 -8.551 19.998 1.00 28.11 O ANISOU 2616 O SER B 52 4881 2533 3267 -37 539 -62 O ATOM 2617 CB SER B 52 9.603 -8.552 19.884 1.00 26.32 C ANISOU 2617 CB SER B 52 4711 2290 2999 366 -22 -129 C ATOM 2618 OG SER B 52 9.112 -8.385 18.560 1.00 30.19 O ANISOU 2618 OG SER B 52 4939 2873 3658 264 58 -224 O ATOM 2619 N ASP B 53 7.283 -7.042 21.403 1.00 23.67 N ANISOU 2619 N ASP B 53 4475 2094 2426 146 398 -37 N ATOM 2620 CA ASP B 53 6.206 -6.059 21.272 1.00 21.38 C ANISOU 2620 CA ASP B 53 4004 1935 2183 39 575 -92 C ATOM 2621 C ASP B 53 6.234 -5.522 19.856 1.00 24.34 C ANISOU 2621 C ASP B 53 4060 2434 2753 34 496 -206 C ATOM 2622 O ASP B 53 7.317 -5.465 19.260 1.00 23.65 O ANISOU 2622 O ASP B 53 3911 2370 2703 133 314 -251 O ATOM 2623 CB ASP B 53 6.408 -4.890 22.261 1.00 22.23 C ANISOU 2623 CB ASP B 53 4195 2132 2119 111 564 -101 C ATOM 2624 CG ASP B 53 6.062 -5.192 23.716 1.00 36.60 C ANISOU 2624 CG ASP B 53 6357 3853 3695 92 704 3 C ATOM 2625 OD1 ASP B 53 5.828 -6.375 24.040 1.00 36.83 O ANISOU 2625 OD1 ASP B 53 6602 3718 3672 39 795 109 O ATOM 2626 OD2 ASP B 53 5.985 -4.233 24.522 1.00 41.56 O ANISOU 2626 OD2 ASP B 53 7055 4557 4178 125 742 -24 O ATOM 2627 N LEU B 54 5.073 -5.101 19.318 1.00 20.33 N ANISOU 2627 N LEU B 54 3357 2001 2368 -73 629 -262 N ATOM 2628 CA LEU B 54 5.000 -4.450 18.011 1.00 20.02 C ANISOU 2628 CA LEU B 54 3064 2078 2465 -63 542 -358 C ATOM 2629 C LEU B 54 6.057 -3.319 17.955 1.00 22.77 C ANISOU 2629 C LEU B 54 3385 2516 2750 60 405 -387 C ATOM 2630 O LEU B 54 6.192 -2.527 18.915 1.00 20.99 O ANISOU 2630 O LEU B 54 3234 2321 2421 103 425 -373 O ATOM 2631 CB LEU B 54 3.584 -3.894 17.797 1.00 20.54 C ANISOU 2631 CB LEU B 54 2949 2211 2645 -154 674 -416 C ATOM 2632 CG LEU B 54 3.301 -3.212 16.427 1.00 23.35 C ANISOU 2632 CG LEU B 54 3078 2673 3122 -131 563 -505 C ATOM 2633 CD1 LEU B 54 3.153 -4.257 15.301 1.00 22.33 C ANISOU 2633 CD1 LEU B 54 2885 2504 3097 -183 496 -554 C ATOM 2634 CD2 LEU B 54 2.030 -2.351 16.528 1.00 26.00 C ANISOU 2634 CD2 LEU B 54 3242 3076 3561 -165 655 -566 C ATOM 2635 N SER B 55 6.859 -3.310 16.885 1.00 18.95 N ANISOU 2635 N SER B 55 2813 2059 2329 108 281 -436 N ATOM 2636 CA SER B 55 7.917 -2.319 16.741 1.00 18.94 C ANISOU 2636 CA SER B 55 2769 2117 2309 197 184 -478 C ATOM 2637 C SER B 55 7.650 -1.432 15.532 1.00 23.36 C ANISOU 2637 C SER B 55 3176 2762 2939 183 185 -528 C ATOM 2638 O SER B 55 6.934 -1.808 14.607 1.00 21.32 O ANISOU 2638 O SER B 55 2850 2515 2735 132 199 -545 O ATOM 2639 CB SER B 55 9.285 -2.987 16.661 1.00 22.90 C ANISOU 2639 CB SER B 55 3321 2556 2824 274 63 -503 C ATOM 2640 OG SER B 55 9.565 -3.836 17.760 1.00 34.32 O ANISOU 2640 OG SER B 55 4948 3902 4190 316 19 -443 O ATOM 2641 N PHE B 56 8.251 -0.251 15.539 1.00 21.99 N ANISOU 2641 N PHE B 56 2965 2633 2757 233 160 -557 N ATOM 2642 CA PHE B 56 7.966 0.782 14.550 1.00 20.55 C ANISOU 2642 CA PHE B 56 2693 2505 2611 230 173 -577 C ATOM 2643 C PHE B 56 9.175 1.136 13.700 1.00 22.69 C ANISOU 2643 C PHE B 56 2945 2768 2906 255 148 -621 C ATOM 2644 O PHE B 56 10.233 1.380 14.255 1.00 21.81 O ANISOU 2644 O PHE B 56 2837 2635 2817 289 124 -660 O ATOM 2645 CB PHE B 56 7.499 2.041 15.332 1.00 22.05 C ANISOU 2645 CB PHE B 56 2867 2724 2789 252 213 -573 C ATOM 2646 CG PHE B 56 6.279 1.776 16.176 1.00 24.30 C ANISOU 2646 CG PHE B 56 3156 3013 3062 217 290 -552 C ATOM 2647 CD1 PHE B 56 5.005 1.850 15.628 1.00 29.43 C ANISOU 2647 CD1 PHE B 56 3704 3691 3789 185 323 -561 C ATOM 2648 CD2 PHE B 56 6.401 1.437 17.522 1.00 28.04 C ANISOU 2648 CD2 PHE B 56 3744 3459 3452 217 333 -534 C ATOM 2649 CE1 PHE B 56 3.869 1.546 16.403 1.00 31.44 C ANISOU 2649 CE1 PHE B 56 3927 3940 4078 132 435 -569 C ATOM 2650 CE2 PHE B 56 5.270 1.143 18.295 1.00 32.05 C ANISOU 2650 CE2 PHE B 56 4277 3957 3943 161 462 -516 C ATOM 2651 CZ PHE B 56 4.014 1.174 17.723 1.00 31.21 C ANISOU 2651 CZ PHE B 56 4027 3875 3956 109 531 -541 C ATOM 2652 N SER B 57 9.012 1.212 12.368 1.00 18.76 N ANISOU 2652 N SER B 57 2435 2286 2407 236 158 -627 N ATOM 2653 CA SER B 57 10.103 1.624 11.477 1.00 17.60 C ANISOU 2653 CA SER B 57 2294 2121 2271 238 196 -669 C ATOM 2654 C SER B 57 9.915 3.091 11.016 1.00 20.51 C ANISOU 2654 C SER B 57 2682 2492 2618 244 242 -638 C ATOM 2655 O SER B 57 8.788 3.589 10.991 1.00 17.63 O ANISOU 2655 O SER B 57 2323 2151 2226 262 210 -589 O ATOM 2656 CB SER B 57 10.193 0.702 10.263 1.00 19.28 C ANISOU 2656 CB SER B 57 2541 2329 2456 213 202 -699 C ATOM 2657 OG SER B 57 10.530 -0.599 10.712 1.00 26.83 O ANISOU 2657 OG SER B 57 3485 3251 3459 215 166 -734 O ATOM 2658 N LYS B 58 11.008 3.732 10.560 1.00 19.33 N ANISOU 2658 N LYS B 58 2542 2302 2500 228 325 -674 N ATOM 2659 CA LYS B 58 11.016 5.125 10.057 1.00 21.27 C ANISOU 2659 CA LYS B 58 2844 2507 2729 222 398 -636 C ATOM 2660 C LYS B 58 10.096 5.311 8.833 1.00 24.02 C ANISOU 2660 C LYS B 58 3316 2861 2950 239 376 -560 C ATOM 2661 O LYS B 58 9.534 6.381 8.663 1.00 23.24 O ANISOU 2661 O LYS B 58 3277 2730 2823 274 367 -496 O ATOM 2662 CB LYS B 58 12.458 5.535 9.680 1.00 26.67 C ANISOU 2662 CB LYS B 58 3514 3125 3492 170 536 -707 C ATOM 2663 N ASP B 59 9.896 4.252 8.025 1.00 20.92 N ANISOU 2663 N ASP B 59 2966 2502 2480 229 341 -575 N ATOM 2664 CA ASP B 59 9.032 4.332 6.849 1.00 20.23 C ANISOU 2664 CA ASP B 59 3009 2426 2252 260 272 -526 C ATOM 2665 C ASP B 59 7.553 4.133 7.224 1.00 19.77 C ANISOU 2665 C ASP B 59 2872 2422 2219 310 107 -510 C ATOM 2666 O ASP B 59 6.728 4.012 6.327 1.00 18.78 O ANISOU 2666 O ASP B 59 2815 2316 2004 349 -8 -501 O ATOM 2667 CB ASP B 59 9.480 3.336 5.755 1.00 22.32 C ANISOU 2667 CB ASP B 59 3365 2700 2417 225 307 -580 C ATOM 2668 CG ASP B 59 9.215 1.858 6.059 1.00 24.82 C ANISOU 2668 CG ASP B 59 3579 3061 2791 208 229 -654 C ATOM 2669 OD1 ASP B 59 8.750 1.543 7.185 1.00 20.95 O ANISOU 2669 OD1 ASP B 59 2958 2589 2413 213 168 -652 O ATOM 2670 OD2 ASP B 59 9.459 1.029 5.181 1.00 29.70 O ANISOU 2670 OD2 ASP B 59 4268 3682 3337 186 243 -714 O ATOM 2671 N TRP B 60 7.219 4.115 8.546 1.00 16.01 N ANISOU 2671 N TRP B 60 2255 1965 1865 310 100 -521 N ATOM 2672 CA TRP B 60 5.858 3.987 9.099 1.00 16.19 C ANISOU 2672 CA TRP B 60 2167 2027 1958 336 8 -528 C ATOM 2673 C TRP B 60 5.344 2.538 9.143 1.00 20.91 C ANISOU 2673 C TRP B 60 2694 2658 2591 287 -36 -583 C ATOM 2674 O TRP B 60 4.281 2.292 9.723 1.00 21.61 O ANISOU 2674 O TRP B 60 2669 2769 2775 278 -65 -608 O ATOM 2675 CB TRP B 60 4.828 4.873 8.349 1.00 15.76 C ANISOU 2675 CB TRP B 60 2142 1968 1879 420 -109 -498 C ATOM 2676 CG TRP B 60 5.241 6.314 8.264 1.00 16.57 C ANISOU 2676 CG TRP B 60 2341 2002 1953 471 -62 -431 C ATOM 2677 CD1 TRP B 60 5.493 7.030 7.125 1.00 20.40 C ANISOU 2677 CD1 TRP B 60 3015 2426 2311 515 -81 -365 C ATOM 2678 CD2 TRP B 60 5.459 7.217 9.368 1.00 15.72 C ANISOU 2678 CD2 TRP B 60 2174 1859 1941 478 23 -427 C ATOM 2679 NE1 TRP B 60 5.812 8.337 7.450 1.00 20.02 N ANISOU 2679 NE1 TRP B 60 3018 2291 2299 543 -6 -312 N ATOM 2680 CE2 TRP B 60 5.800 8.476 8.820 1.00 19.95 C ANISOU 2680 CE2 TRP B 60 2844 2301 2434 522 50 -361 C ATOM 2681 CE3 TRP B 60 5.360 7.088 10.771 1.00 16.27 C ANISOU 2681 CE3 TRP B 60 2116 1957 2110 451 81 -475 C ATOM 2682 CZ2 TRP B 60 5.982 9.617 9.618 1.00 19.11 C ANISOU 2682 CZ2 TRP B 60 2715 2127 2418 541 120 -359 C ATOM 2683 CZ3 TRP B 60 5.572 8.207 11.567 1.00 17.69 C ANISOU 2683 CZ3 TRP B 60 2286 2087 2348 475 143 -479 C ATOM 2684 CH2 TRP B 60 5.884 9.457 10.992 1.00 19.13 C ANISOU 2684 CH2 TRP B 60 2571 2175 2521 517 159 -430 C ATOM 2685 N SER B 61 6.100 1.592 8.603 1.00 16.56 N ANISOU 2685 N SER B 61 2203 2097 1991 246 -16 -614 N ATOM 2686 CA SER B 61 5.681 0.180 8.629 1.00 17.24 C ANISOU 2686 CA SER B 61 2239 2185 2125 192 -49 -671 C ATOM 2687 C SER B 61 6.017 -0.452 9.999 1.00 22.93 C ANISOU 2687 C SER B 61 2916 2871 2924 154 31 -660 C ATOM 2688 O SER B 61 6.641 0.196 10.844 1.00 23.37 O ANISOU 2688 O SER B 61 2983 2917 2980 179 86 -625 O ATOM 2689 CB SER B 61 6.328 -0.598 7.489 1.00 20.58 C ANISOU 2689 CB SER B 61 2756 2596 2467 175 -59 -724 C ATOM 2690 OG SER B 61 7.717 -0.740 7.727 1.00 23.35 O ANISOU 2690 OG SER B 61 3145 2908 2818 167 47 -728 O ATOM 2691 N PHE B 62 5.579 -1.691 10.233 1.00 17.08 N ANISOU 2691 N PHE B 62 1623 2371 2496 267 332 -545 N ATOM 2692 CA PHE B 62 5.777 -2.348 11.524 1.00 16.41 C ANISOU 2692 CA PHE B 62 1544 2228 2462 151 330 -501 C ATOM 2693 C PHE B 62 6.559 -3.638 11.390 1.00 20.76 C ANISOU 2693 C PHE B 62 2070 2727 3092 102 248 -519 C ATOM 2694 O PHE B 62 6.643 -4.225 10.306 1.00 20.43 O ANISOU 2694 O PHE B 62 1969 2703 3090 146 183 -584 O ATOM 2695 CB PHE B 62 4.411 -2.657 12.183 1.00 18.48 C ANISOU 2695 CB PHE B 62 1743 2518 2759 109 350 -498 C ATOM 2696 CG PHE B 62 3.449 -1.495 12.185 1.00 19.27 C ANISOU 2696 CG PHE B 62 1847 2688 2787 175 410 -507 C ATOM 2697 CD1 PHE B 62 3.596 -0.449 13.094 1.00 21.64 C ANISOU 2697 CD1 PHE B 62 2216 2982 3023 161 479 -455 C ATOM 2698 CD2 PHE B 62 2.446 -1.404 11.229 1.00 21.09 C ANISOU 2698 CD2 PHE B 62 2007 2997 3009 268 393 -583 C ATOM 2699 CE1 PHE B 62 2.738 0.662 13.054 1.00 22.39 C ANISOU 2699 CE1 PHE B 62 2319 3135 3054 235 527 -471 C ATOM 2700 CE2 PHE B 62 1.617 -0.282 11.164 1.00 23.39 C ANISOU 2700 CE2 PHE B 62 2312 3355 3221 355 438 -599 C ATOM 2701 CZ PHE B 62 1.748 0.731 12.099 1.00 21.31 C ANISOU 2701 CZ PHE B 62 2125 3071 2902 334 504 -539 C ATOM 2702 N TYR B 63 7.128 -4.088 12.508 1.00 16.83 N ANISOU 2702 N TYR B 63 1615 2169 2612 22 246 -467 N ATOM 2703 CA TYR B 63 7.839 -5.357 12.539 1.00 17.84 C ANISOU 2703 CA TYR B 63 1732 2232 2812 -17 165 -478 C ATOM 2704 C TYR B 63 7.688 -6.004 13.905 1.00 23.04 C ANISOU 2704 C TYR B 63 2422 2833 3499 -99 179 -400 C ATOM 2705 O TYR B 63 7.443 -5.323 14.913 1.00 21.19 O ANISOU 2705 O TYR B 63 2227 2620 3203 -125 251 -342 O ATOM 2706 CB TYR B 63 9.320 -5.222 12.129 1.00 17.76 C ANISOU 2706 CB TYR B 63 1767 2216 2766 12 124 -515 C ATOM 2707 CG TYR B 63 10.191 -4.409 13.060 1.00 19.21 C ANISOU 2707 CG TYR B 63 2032 2399 2868 -5 180 -485 C ATOM 2708 CD1 TYR B 63 11.049 -5.033 13.966 1.00 21.86 C ANISOU 2708 CD1 TYR B 63 2407 2696 3205 -38 143 -469 C ATOM 2709 CD2 TYR B 63 10.259 -3.018 12.947 1.00 19.37 C ANISOU 2709 CD2 TYR B 63 2090 2460 2810 24 267 -487 C ATOM 2710 CE1 TYR B 63 11.908 -4.288 14.783 1.00 24.16 C ANISOU 2710 CE1 TYR B 63 2753 3008 3419 -42 192 -472 C ATOM 2711 CE2 TYR B 63 11.108 -2.264 13.759 1.00 20.23 C ANISOU 2711 CE2 TYR B 63 2256 2571 2859 5 324 -487 C ATOM 2712 CZ TYR B 63 11.941 -2.905 14.666 1.00 27.55 C ANISOU 2712 CZ TYR B 63 3202 3480 3786 -27 284 -489 C ATOM 2713 OH TYR B 63 12.761 -2.161 15.475 1.00 29.69 O ANISOU 2713 OH TYR B 63 3511 3775 3997 -36 340 -514 O ATOM 2714 N LEU B 64 7.856 -7.329 13.920 1.00 22.54 N ANISOU 2714 N LEU B 64 2342 2695 3527 -135 111 -400 N ATOM 2715 CA LEU B 64 7.738 -8.212 15.079 1.00 24.77 C ANISOU 2715 CA LEU B 64 2665 2899 3847 -207 118 -317 C ATOM 2716 C LEU B 64 8.655 -9.381 14.925 1.00 26.33 C ANISOU 2716 C LEU B 64 2885 3008 4109 -202 23 -330 C ATOM 2717 O LEU B 64 8.851 -9.848 13.801 1.00 23.66 O ANISOU 2717 O LEU B 64 2486 2663 3839 -170 -50 -418 O ATOM 2718 CB LEU B 64 6.282 -8.805 15.148 1.00 27.10 C ANISOU 2718 CB LEU B 64 2892 3174 4231 -274 159 -307 C ATOM 2719 CG LEU B 64 5.130 -7.939 15.576 1.00 33.89 C ANISOU 2719 CG LEU B 64 3722 4114 5040 -297 252 -291 C ATOM 2720 CD1 LEU B 64 3.883 -8.352 14.841 1.00 34.46 C ANISOU 2720 CD1 LEU B 64 3683 4209 5201 -316 261 -373 C ATOM 2721 CD2 LEU B 64 4.843 -8.114 17.060 1.00 39.34 C ANISOU 2721 CD2 LEU B 64 4469 4779 5701 -376 318 -181 C ATOM 2722 N LEU B 65 9.101 -9.945 16.046 1.00 22.93 N ANISOU 2722 N LEU B 65 2537 2512 3665 -228 20 -245 N ATOM 2723 CA LEU B 65 9.871 -11.182 16.047 1.00 22.32 C ANISOU 2723 CA LEU B 65 2496 2331 3653 -216 -73 -245 C ATOM 2724 C LEU B 65 9.129 -12.235 16.874 1.00 27.92 C ANISOU 2724 C LEU B 65 3244 2926 4441 -290 -39 -141 C ATOM 2725 O LEU B 65 8.893 -12.022 18.068 1.00 26.85 O ANISOU 2725 O LEU B 65 3174 2795 4233 -319 34 -32 O ATOM 2726 CB LEU B 65 11.297 -10.967 16.586 1.00 20.95 C ANISOU 2726 CB LEU B 65 2404 2179 3378 -152 -120 -248 C ATOM 2727 CG LEU B 65 12.144 -12.250 16.756 1.00 24.94 C ANISOU 2727 CG LEU B 65 2966 2580 3931 -119 -226 -245 C ATOM 2728 CD1 LEU B 65 12.561 -12.847 15.378 1.00 22.85 C ANISOU 2728 CD1 LEU B 65 2626 2293 3764 -90 -336 -372 C ATOM 2729 CD2 LEU B 65 13.399 -11.966 17.598 1.00 24.94 C ANISOU 2729 CD2 LEU B 65 3048 2625 3803 -48 -254 -245 C ATOM 2730 N TYR B 66 8.784 -13.366 16.240 1.00 26.24 N ANISOU 2730 N TYR B 66 2985 2611 4375 -320 -86 -177 N ATOM 2731 CA TYR B 66 8.163 -14.527 16.880 1.00 27.80 C ANISOU 2731 CA TYR B 66 3223 2664 4675 -399 -50 -88 C ATOM 2732 C TYR B 66 9.237 -15.579 17.035 1.00 30.28 C ANISOU 2732 C TYR B 66 3624 2855 5026 -350 -151 -66 C ATOM 2733 O TYR B 66 10.013 -15.808 16.103 1.00 28.31 O ANISOU 2733 O TYR B 66 3332 2612 4814 -286 -262 -179 O ATOM 2734 CB TYR B 66 6.972 -15.049 16.055 1.00 30.77 C ANISOU 2734 CB TYR B 66 3476 3007 5207 -473 -21 -168 C ATOM 2735 CG TYR B 66 5.693 -14.275 16.292 1.00 34.12 C ANISOU 2735 CG TYR B 66 3839 3526 5599 -537 97 -162 C ATOM 2736 CD1 TYR B 66 4.676 -14.798 17.083 1.00 37.64 C ANISOU 2736 CD1 TYR B 66 4297 3902 6102 -651 201 -85 C ATOM 2737 CD2 TYR B 66 5.502 -13.011 15.731 1.00 34.02 C ANISOU 2737 CD2 TYR B 66 3759 3672 5493 -482 107 -236 C ATOM 2738 CE1 TYR B 66 3.499 -14.087 17.309 1.00 39.76 C ANISOU 2738 CE1 TYR B 66 4498 4276 6335 -709 303 -101 C ATOM 2739 CE2 TYR B 66 4.325 -12.294 15.947 1.00 34.41 C ANISOU 2739 CE2 TYR B 66 3752 3815 5509 -525 203 -243 C ATOM 2740 CZ TYR B 66 3.326 -12.840 16.731 1.00 45.47 C ANISOU 2740 CZ TYR B 66 5150 5161 6965 -639 296 -185 C ATOM 2741 OH TYR B 66 2.162 -12.141 16.950 1.00 51.72 O ANISOU 2741 OH TYR B 66 5875 6058 7718 -681 385 -212 O ATOM 2742 N TYR B 67 9.334 -16.193 18.216 1.00 27.49 N ANISOU 2742 N TYR B 67 3396 2400 4650 -367 -117 76 N ATOM 2743 CA TYR B 67 10.399 -17.158 18.436 1.00 27.97 C ANISOU 2743 CA TYR B 67 3557 2344 4725 -293 -220 101 C ATOM 2744 C TYR B 67 9.997 -18.277 19.375 1.00 31.70 C ANISOU 2744 C TYR B 67 4148 2637 5259 -344 -166 256 C ATOM 2745 O TYR B 67 9.154 -18.097 20.252 1.00 31.24 O ANISOU 2745 O TYR B 67 4128 2578 5164 -422 -39 376 O ATOM 2746 CB TYR B 67 11.665 -16.449 18.964 1.00 28.56 C ANISOU 2746 CB TYR B 67 3702 2531 4620 -178 -275 96 C ATOM 2747 CG TYR B 67 11.470 -15.653 20.241 1.00 31.95 C ANISOU 2747 CG TYR B 67 4196 3048 4894 -182 -171 213 C ATOM 2748 CD1 TYR B 67 11.863 -16.168 21.475 1.00 36.26 C ANISOU 2748 CD1 TYR B 67 4881 3539 5358 -133 -162 347 C ATOM 2749 CD2 TYR B 67 10.917 -14.376 20.214 1.00 31.26 C ANISOU 2749 CD2 TYR B 67 4033 3108 4738 -219 -87 184 C ATOM 2750 CE1 TYR B 67 11.693 -15.439 22.651 1.00 37.89 C ANISOU 2750 CE1 TYR B 67 5132 3849 5416 -127 -71 444 C ATOM 2751 CE2 TYR B 67 10.714 -13.649 21.386 1.00 32.68 C ANISOU 2751 CE2 TYR B 67 4255 3375 4785 -222 3 276 C ATOM 2752 CZ TYR B 67 11.113 -14.181 22.602 1.00 45.33 C ANISOU 2752 CZ TYR B 67 5980 4937 6305 -177 10 402 C ATOM 2753 OH TYR B 67 10.929 -13.471 23.766 1.00 51.68 O ANISOU 2753 OH TYR B 67 6814 5851 6972 -170 95 484 O ATOM 2754 N THR B 68 10.614 -19.444 19.190 1.00 30.44 N ANISOU 2754 N THR B 68 4052 2321 5194 -299 -261 253 N ATOM 2755 CA THR B 68 10.361 -20.597 20.052 1.00 30.86 C ANISOU 2755 CA THR B 68 4245 2170 5309 -332 -213 412 C ATOM 2756 C THR B 68 11.635 -21.390 20.230 1.00 35.38 C ANISOU 2756 C THR B 68 4939 2645 5857 -195 -350 423 C ATOM 2757 O THR B 68 12.412 -21.535 19.285 1.00 32.74 O ANISOU 2757 O THR B 68 4537 2333 5568 -123 -488 269 O ATOM 2758 CB THR B 68 9.181 -21.469 19.548 1.00 37.77 C ANISOU 2758 CB THR B 68 5052 2887 6409 -476 -138 397 C ATOM 2759 OG1 THR B 68 8.791 -22.340 20.615 1.00 38.93 O ANISOU 2759 OG1 THR B 68 5354 2851 6585 -532 -40 587 O ATOM 2760 CG2 THR B 68 9.507 -22.305 18.293 1.00 33.20 C ANISOU 2760 CG2 THR B 68 4384 2214 6018 -454 -263 237 C ATOM 2761 N GLU B 69 11.841 -21.913 21.452 1.00 35.80 N ANISOU 2761 N GLU B 69 5174 2599 5830 -151 -312 604 N ATOM 2762 CA GLU B 69 12.971 -22.785 21.785 1.00 36.81 C ANISOU 2762 CA GLU B 69 5446 2614 5924 -3 -435 639 C ATOM 2763 C GLU B 69 12.714 -24.148 21.139 1.00 41.95 C ANISOU 2763 C GLU B 69 6110 3017 6813 -51 -475 620 C ATOM 2764 O GLU B 69 11.590 -24.650 21.220 1.00 43.66 O ANISOU 2764 O GLU B 69 6326 3092 7172 -197 -346 701 O ATOM 2765 CB GLU B 69 13.119 -22.904 23.311 1.00 39.83 C ANISOU 2765 CB GLU B 69 6021 2973 6139 64 -365 852 C ATOM 2766 CG GLU B 69 14.432 -23.541 23.748 1.00 58.63 C ANISOU 2766 CG GLU B 69 8553 5302 8422 265 -506 870 C ATOM 2767 CD GLU B 69 14.858 -23.307 25.185 1.00 87.67 C ANISOU 2767 CD GLU B 69 12386 9057 11866 389 -467 1028 C ATOM 2768 OE1 GLU B 69 13.976 -23.112 26.054 1.00 88.02 O ANISOU 2768 OE1 GLU B 69 12482 9102 11859 302 -308 1199 O ATOM 2769 OE2 GLU B 69 16.084 -23.343 25.446 1.00 82.05 O ANISOU 2769 OE2 GLU B 69 11739 8418 11017 580 -599 969 O ATOM 2770 N PHE B 70 13.709 -24.721 20.452 1.00 37.71 N ANISOU 2770 N PHE B 70 5566 2433 6329 61 -648 493 N ATOM 2771 CA PHE B 70 13.519 -26.017 19.782 1.00 39.01 C ANISOU 2771 CA PHE B 70 5726 2361 6734 24 -699 451 C ATOM 2772 C PHE B 70 14.833 -26.768 19.581 1.00 42.51 C ANISOU 2772 C PHE B 70 6248 2733 7172 199 -895 376 C ATOM 2773 O PHE B 70 15.910 -26.178 19.627 1.00 39.44 O ANISOU 2773 O PHE B 70 5858 2519 6609 338 -1008 292 O ATOM 2774 CB PHE B 70 12.790 -25.841 18.416 1.00 39.71 C ANISOU 2774 CB PHE B 70 5581 2501 7006 -99 -695 262 C ATOM 2775 CG PHE B 70 13.611 -25.480 17.194 1.00 39.65 C ANISOU 2775 CG PHE B 70 5415 2649 7001 -17 -862 27 C ATOM 2776 CD1 PHE B 70 13.532 -26.241 16.036 1.00 42.12 C ANISOU 2776 CD1 PHE B 70 5599 2880 7526 -41 -951 -135 C ATOM 2777 CD2 PHE B 70 14.446 -24.361 17.195 1.00 39.79 C ANISOU 2777 CD2 PHE B 70 5404 2905 6811 76 -921 -41 C ATOM 2778 CE1 PHE B 70 14.280 -25.904 14.904 1.00 41.67 C ANISOU 2778 CE1 PHE B 70 5391 2984 7459 33 -1100 -350 C ATOM 2779 CE2 PHE B 70 15.205 -24.035 16.067 1.00 40.92 C ANISOU 2779 CE2 PHE B 70 5406 3191 6951 139 -1059 -253 C ATOM 2780 CZ PHE B 70 15.094 -24.790 14.920 1.00 39.67 C ANISOU 2780 CZ PHE B 70 5121 2960 6990 117 -1147 -401 C ATOM 2781 N THR B 71 14.725 -28.073 19.325 1.00 42.23 N ANISOU 2781 N THR B 71 6269 2440 7337 188 -933 389 N ATOM 2782 CA THR B 71 15.862 -28.919 19.037 1.00 43.69 C ANISOU 2782 CA THR B 71 6517 2529 7552 349 -1127 302 C ATOM 2783 C THR B 71 15.663 -29.461 17.609 1.00 48.55 C ANISOU 2783 C THR B 71 6939 3089 8418 282 -1214 89 C ATOM 2784 O THR B 71 14.851 -30.365 17.428 1.00 51.20 O ANISOU 2784 O THR B 71 7276 3195 8981 171 -1141 127 O ATOM 2785 CB THR B 71 16.021 -30.007 20.120 1.00 54.58 C ANISOU 2785 CB THR B 71 8162 3644 8930 430 -1105 519 C ATOM 2786 OG1 THR B 71 16.229 -29.385 21.387 1.00 54.67 O ANISOU 2786 OG1 THR B 71 8323 3763 8685 507 -1031 695 O ATOM 2787 CG2 THR B 71 17.172 -30.938 19.838 1.00 52.62 C ANISOU 2787 CG2 THR B 71 7991 3284 8718 611 -1314 426 C ATOM 2788 N PRO B 72 16.370 -28.924 16.585 1.00 50.97 N ANISOU 2788 N PRO B 72 6883 2141 10343 832 -2662 -1933 N ATOM 2789 CA PRO B 72 16.169 -29.441 15.213 1.00 50.59 C ANISOU 2789 CA PRO B 72 6769 2174 10280 813 -2631 -1931 C ATOM 2790 C PRO B 72 16.563 -30.908 15.058 1.00 55.55 C ANISOU 2790 C PRO B 72 7400 2806 10900 792 -2625 -1970 C ATOM 2791 O PRO B 72 17.540 -31.363 15.655 1.00 53.96 O ANISOU 2791 O PRO B 72 7231 2542 10729 786 -2656 -1985 O ATOM 2792 CB PRO B 72 17.057 -28.549 14.335 1.00 52.40 C ANISOU 2792 CB PRO B 72 6948 2417 10544 821 -2648 -1882 C ATOM 2793 CG PRO B 72 17.951 -27.794 15.272 1.00 56.77 C ANISOU 2793 CG PRO B 72 7531 2878 11159 840 -2700 -1863 C ATOM 2794 CD PRO B 72 17.327 -27.792 16.624 1.00 52.27 C ANISOU 2794 CD PRO B 72 7037 2256 10568 855 -2714 -1897 C ATOM 2795 N THR B 73 15.748 -31.642 14.280 1.00 54.27 N ANISOU 2795 N THR B 73 7203 2707 10709 783 -2601 -1992 N ATOM 2796 CA THR B 73 15.870 -33.058 13.897 1.00 55.22 C ANISOU 2796 CA THR B 73 7308 2844 10829 769 -2608 -2037 C ATOM 2797 C THR B 73 15.988 -33.083 12.372 1.00 59.14 C ANISOU 2797 C THR B 73 7746 3423 11301 784 -2598 -2044 C ATOM 2798 O THR B 73 15.491 -32.165 11.719 1.00 58.75 O ANISOU 2798 O THR B 73 7678 3416 11227 796 -2583 -2009 O ATOM 2799 CB THR B 73 14.638 -33.838 14.438 1.00 68.37 C ANISOU 2799 CB THR B 73 8987 4500 12490 753 -2598 -2054 C ATOM 2800 OG1 THR B 73 14.758 -33.955 15.852 1.00 70.26 O ANISOU 2800 OG1 THR B 73 9293 4670 12732 737 -2602 -2046 O ATOM 2801 CG2 THR B 73 14.479 -35.230 13.846 1.00 74.40 C ANISOU 2801 CG2 THR B 73 9716 5284 13268 745 -2623 -2098 C ATOM 2802 N GLU B 74 16.634 -34.116 11.805 1.00 55.99 N ANISOU 2802 N GLU B 74 7322 3044 10906 787 -2612 -2091 N ATOM 2803 CA GLU B 74 16.786 -34.278 10.355 1.00 57.03 C ANISOU 2803 CA GLU B 74 7410 3264 10996 811 -2598 -2111 C ATOM 2804 C GLU B 74 15.431 -34.338 9.610 1.00 63.48 C ANISOU 2804 C GLU B 74 8218 4130 11772 826 -2605 -2117 C ATOM 2805 O GLU B 74 15.348 -33.846 8.485 1.00 65.27 O ANISOU 2805 O GLU B 74 8431 4425 11943 848 -2592 -2101 O ATOM 2806 CB GLU B 74 17.588 -35.556 10.034 1.00 58.52 C ANISOU 2806 CB GLU B 74 7572 3459 11204 818 -2622 -2186 C ATOM 2807 N LYS B 75 14.382 -34.916 10.241 1.00 59.53 N ANISOU 2807 N LYS B 75 7726 3589 11305 815 -2627 -2134 N ATOM 2808 CA LYS B 75 13.065 -35.130 9.631 1.00 59.65 C ANISOU 2808 CA LYS B 75 7722 3624 11317 831 -2648 -2149 C ATOM 2809 C LYS B 75 11.992 -34.073 9.970 1.00 63.87 C ANISOU 2809 C LYS B 75 8263 4139 11866 823 -2630 -2103 C ATOM 2810 O LYS B 75 11.064 -33.909 9.169 1.00 64.47 O ANISOU 2810 O LYS B 75 8321 4234 11940 840 -2653 -2109 O ATOM 2811 CB LYS B 75 12.522 -36.512 10.019 1.00 62.27 C ANISOU 2811 CB LYS B 75 8038 3916 11707 823 -2689 -2195 C ATOM 2812 N ASP B 76 12.077 -33.400 11.141 1.00 58.76 N ANISOU 2812 N ASP B 76 7641 3447 11239 802 -2599 -2068 N ATOM 2813 CA ASP B 76 11.067 -32.412 11.544 1.00 57.94 C ANISOU 2813 CA ASP B 76 7535 3322 11158 800 -2582 -2041 C ATOM 2814 C ASP B 76 11.103 -31.171 10.648 1.00 59.98 C ANISOU 2814 C ASP B 76 7783 3616 11391 814 -2598 -2006 C ATOM 2815 O ASP B 76 12.174 -30.638 10.355 1.00 59.33 O ANISOU 2815 O ASP B 76 7710 3555 11278 816 -2597 -1975 O ATOM 2816 CB ASP B 76 11.215 -32.017 13.025 1.00 59.82 C ANISOU 2816 CB ASP B 76 7811 3509 11410 786 -2550 -2024 C ATOM 2817 CG ASP B 76 10.805 -33.092 14.026 1.00 70.68 C ANISOU 2817 CG ASP B 76 9203 4845 12806 764 -2528 -2041 C ATOM 2818 OD1 ASP B 76 9.860 -33.860 13.725 1.00 71.27 O ANISOU 2818 OD1 ASP B 76 9240 4922 12918 758 -2530 -2058 O ATOM 2819 OD2 ASP B 76 11.394 -33.130 15.134 1.00 75.28 O ANISOU 2819 OD2 ASP B 76 9839 5389 13373 753 -2515 -2032 O ATOM 2820 N GLU B 77 9.911 -30.739 10.205 1.00 55.57 N ANISOU 2820 N GLU B 77 7201 3055 10859 820 -2618 -2009 N ATOM 2821 CA GLU B 77 9.685 -29.597 9.327 1.00 54.93 C ANISOU 2821 CA GLU B 77 7110 2994 10765 828 -2653 -1974 C ATOM 2822 C GLU B 77 9.138 -28.432 10.124 1.00 56.23 C ANISOU 2822 C GLU B 77 7266 3116 10985 822 -2654 -1957 C ATOM 2823 O GLU B 77 8.209 -28.605 10.922 1.00 55.04 O ANISOU 2823 O GLU B 77 7099 2926 10890 821 -2631 -1989 O ATOM 2824 CB GLU B 77 8.699 -29.964 8.199 1.00 57.27 C ANISOU 2824 CB GLU B 77 7391 3302 11065 843 -2703 -2001 C ATOM 2825 CG GLU B 77 9.173 -31.059 7.253 1.00 72.57 C ANISOU 2825 CG GLU B 77 9342 5290 12943 864 -2719 -2031 C ATOM 2826 CD GLU B 77 10.118 -30.592 6.163 1.00106.54 C ANISOU 2826 CD GLU B 77 13670 9664 17147 874 -2723 -1994 C ATOM 2827 OE1 GLU B 77 9.720 -29.711 5.365 1.00109.39 O ANISOU 2827 OE1 GLU B 77 14041 10037 17483 876 -2762 -1957 O ATOM 2828 OE2 GLU B 77 11.249 -31.125 6.092 1.00106.12 O ANISOU 2828 OE2 GLU B 77 13622 9651 17046 878 -2687 -2001 O ATOM 2829 N TYR B 78 9.709 -27.240 9.911 1.00 47.13 N ANISOU 2829 N TYR B 78 4543 2779 10586 330 -2742 -2355 N ATOM 2830 CA TYR B 78 9.250 -26.041 10.603 1.00 44.94 C ANISOU 2830 CA TYR B 78 4361 2605 10109 309 -2698 -2173 C ATOM 2831 C TYR B 78 8.841 -24.967 9.614 1.00 47.06 C ANISOU 2831 C TYR B 78 4466 3158 10257 209 -2399 -2160 C ATOM 2832 O TYR B 78 9.397 -24.890 8.517 1.00 47.26 O ANISOU 2832 O TYR B 78 4297 3249 10412 206 -2246 -2337 O ATOM 2833 CB TYR B 78 10.319 -25.518 11.574 1.00 46.39 C ANISOU 2833 CB TYR B 78 4564 2606 10456 457 -2960 -2226 C ATOM 2834 CG TYR B 78 10.494 -26.422 12.772 1.00 49.47 C ANISOU 2834 CG TYR B 78 5270 2675 10850 573 -3304 -2188 C ATOM 2835 CD1 TYR B 78 9.709 -26.262 13.912 1.00 51.31 C ANISOU 2835 CD1 TYR B 78 5921 2803 10772 590 -3355 -1952 C ATOM 2836 CD2 TYR B 78 11.411 -27.473 12.752 1.00 51.93 C ANISOU 2836 CD2 TYR B 78 5512 2757 11462 677 -3551 -2385 C ATOM 2837 CE1 TYR B 78 9.850 -27.109 15.011 1.00 54.62 C ANISOU 2837 CE1 TYR B 78 6740 2875 11137 713 -3647 -1913 C ATOM 2838 CE2 TYR B 78 11.542 -28.340 13.834 1.00 54.16 C ANISOU 2838 CE2 TYR B 78 6149 2717 11713 795 -3890 -2356 C ATOM 2839 CZ TYR B 78 10.763 -28.153 14.963 1.00 61.16 C ANISOU 2839 CZ TYR B 78 7508 3484 12245 814 -3938 -2119 C ATOM 2840 OH TYR B 78 10.929 -28.981 16.048 1.00 63.49 O ANISOU 2840 OH TYR B 78 8251 3406 12464 951 -4261 -2092 O ATOM 2841 N ALA B 79 7.844 -24.150 9.995 1.00 41.99 N ANISOU 2841 N ALA B 79 3942 2654 9357 139 -2293 -1948 N ATOM 2842 CA ALA B 79 7.348 -23.070 9.153 1.00 40.17 C ANISOU 2842 CA ALA B 79 3605 2679 8979 53 -2050 -1919 C ATOM 2843 C ALA B 79 6.730 -21.941 9.974 1.00 43.57 C ANISOU 2843 C ALA B 79 4155 3200 9198 42 -1997 -1705 C ATOM 2844 O ALA B 79 6.459 -22.079 11.172 1.00 42.91 O ANISOU 2844 O ALA B 79 4295 2972 9038 91 -2105 -1548 O ATOM 2845 CB ALA B 79 6.324 -23.604 8.147 1.00 40.48 C ANISOU 2845 CB ALA B 79 3642 2809 8930 -62 -1942 -1908 C ATOM 2846 N CYS B 80 6.516 -20.818 9.308 1.00 40.00 N ANISOU 2846 N CYS B 80 3607 2962 8628 -8 -1812 -1701 N ATOM 2847 CA CYS B 80 5.867 -19.651 9.875 1.00 38.74 C ANISOU 2847 CA CYS B 80 3544 2920 8255 -23 -1723 -1509 C ATOM 2848 C CYS B 80 4.625 -19.369 9.042 1.00 41.24 C ANISOU 2848 C CYS B 80 3820 3419 8431 -138 -1550 -1428 C ATOM 2849 O CYS B 80 4.722 -19.310 7.818 1.00 41.57 O ANISOU 2849 O CYS B 80 3762 3557 8474 -178 -1475 -1576 O ATOM 2850 CB CYS B 80 6.833 -18.474 9.878 1.00 39.47 C ANISOU 2850 CB CYS B 80 3553 3072 8371 35 -1706 -1591 C ATOM 2851 SG CYS B 80 6.186 -16.988 10.662 1.00 42.86 S ANISOU 2851 SG CYS B 80 4145 3622 8518 42 -1627 -1363 S ATOM 2852 N ARG B 81 3.456 -19.253 9.688 1.00 36.73 N ANISOU 2852 N ARG B 81 3348 2845 7762 -178 -1489 -1202 N ATOM 2853 CA ARG B 81 2.175 -18.985 9.026 1.00 35.57 C ANISOU 2853 CA ARG B 81 3121 2819 7573 -281 -1379 -1115 C ATOM 2854 C ARG B 81 1.721 -17.580 9.389 1.00 36.71 C ANISOU 2854 C ARG B 81 3305 3106 7535 -268 -1237 -965 C ATOM 2855 O ARG B 81 1.614 -17.250 10.575 1.00 36.59 O ANISOU 2855 O ARG B 81 3451 3010 7441 -209 -1182 -791 O ATOM 2856 CB ARG B 81 1.125 -20.035 9.403 1.00 34.94 C ANISOU 2856 CB ARG B 81 3048 2580 7648 -348 -1385 -979 C ATOM 2857 CG ARG B 81 -0.233 -19.817 8.731 1.00 43.13 C ANISOU 2857 CG ARG B 81 3938 3683 8766 -454 -1333 -900 C ATOM 2858 CD ARG B 81 -1.200 -20.938 9.055 1.00 46.35 C ANISOU 2858 CD ARG B 81 4288 3883 9438 -535 -1336 -784 C ATOM 2859 NE ARG B 81 -1.585 -20.931 10.469 1.00 51.82 N ANISOU 2859 NE ARG B 81 5124 4422 10142 -503 -1129 -543 N ATOM 2860 CZ ARG B 81 -1.987 -22.003 11.144 1.00 64.72 C ANISOU 2860 CZ ARG B 81 6828 5806 11956 -533 -1068 -435 C ATOM 2861 NH1 ARG B 81 -2.056 -23.187 10.546 1.00 49.96 N ANISOU 2861 NH1 ARG B 81 4854 3833 10296 -607 -1236 -550 N ATOM 2862 NH2 ARG B 81 -2.320 -21.901 12.424 1.00 53.02 N ANISOU 2862 NH2 ARG B 81 5573 4146 10428 -481 -821 -208 N ATOM 2863 N VAL B 82 1.508 -16.736 8.373 1.00 31.49 N ANISOU 2863 N VAL B 82 2561 2629 6774 -305 -1182 -1037 N ATOM 2864 CA VAL B 82 1.165 -15.327 8.596 1.00 29.46 C ANISOU 2864 CA VAL B 82 2342 2522 6328 -287 -1057 -920 C ATOM 2865 C VAL B 82 -0.111 -14.943 7.842 1.00 33.63 C ANISOU 2865 C VAL B 82 2783 3144 6852 -359 -1024 -866 C ATOM 2866 O VAL B 82 -0.282 -15.291 6.672 1.00 33.34 O ANISOU 2866 O VAL B 82 2698 3119 6853 -404 -1125 -1017 O ATOM 2867 CB VAL B 82 2.355 -14.391 8.215 1.00 31.82 C ANISOU 2867 CB VAL B 82 2658 2930 6500 -237 -1028 -1069 C ATOM 2868 CG1 VAL B 82 1.992 -12.907 8.332 1.00 30.19 C ANISOU 2868 CG1 VAL B 82 2509 2884 6078 -224 -909 -960 C ATOM 2869 CG2 VAL B 82 3.600 -14.697 9.053 1.00 32.25 C ANISOU 2869 CG2 VAL B 82 2754 2843 6657 -155 -1127 -1125 C ATOM 2870 N ASN B 83 -0.992 -14.196 8.519 1.00 31.14 N ANISOU 2870 N ASN B 83 2477 2862 6494 -353 -898 -655 N ATOM 2871 CA ASN B 83 -2.180 -13.633 7.897 1.00 31.69 C ANISOU 2871 CA ASN B 83 2434 3005 6603 -401 -888 -601 C ATOM 2872 C ASN B 83 -2.210 -12.145 8.175 1.00 33.68 C ANISOU 2872 C ASN B 83 2772 3414 6611 -346 -754 -510 C ATOM 2873 O ASN B 83 -1.794 -11.692 9.245 1.00 31.88 O ANISOU 2873 O ASN B 83 2684 3174 6254 -278 -631 -386 O ATOM 2874 CB ASN B 83 -3.473 -14.316 8.305 1.00 35.88 C ANISOU 2874 CB ASN B 83 2807 3371 7454 -461 -850 -434 C ATOM 2875 CG ASN B 83 -4.495 -14.315 7.190 1.00 60.79 C ANISOU 2875 CG ASN B 83 5775 6519 10802 -529 -1026 -504 C ATOM 2876 OD1 ASN B 83 -4.342 -13.649 6.145 1.00 45.92 O ANISOU 2876 OD1 ASN B 83 3955 4760 8732 -514 -1164 -656 O ATOM 2877 ND2 ASN B 83 -5.556 -15.082 7.376 1.00 61.76 N ANISOU 2877 ND2 ASN B 83 5690 6452 11323 -600 -1043 -400 N ATOM 2878 N HIS B 84 -2.667 -11.384 7.176 1.00 30.17 N ANISOU 2878 N HIS B 84 2294 3091 6079 -363 -812 -584 N ATOM 2879 CA HIS B 84 -2.697 -9.919 7.165 1.00 27.53 C ANISOU 2879 CA HIS B 84 2052 2919 5488 -315 -713 -536 C ATOM 2880 C HIS B 84 -3.721 -9.499 6.130 1.00 31.70 C ANISOU 2880 C HIS B 84 2512 3482 6052 -341 -842 -583 C ATOM 2881 O HIS B 84 -4.012 -10.285 5.227 1.00 31.12 O ANISOU 2881 O HIS B 84 2387 3312 6126 -386 -1047 -719 O ATOM 2882 CB HIS B 84 -1.276 -9.392 6.826 1.00 25.83 C ANISOU 2882 CB HIS B 84 1988 2802 5024 -281 -689 -700 C ATOM 2883 CG HIS B 84 -1.132 -7.901 6.840 1.00 27.21 C ANISOU 2883 CG HIS B 84 2280 3129 4929 -238 -583 -661 C ATOM 2884 ND1 HIS B 84 -0.962 -7.195 8.026 1.00 28.57 N ANISOU 2884 ND1 HIS B 84 2537 3322 4998 -180 -472 -491 N ATOM 2885 CD2 HIS B 84 -1.103 -7.031 5.809 1.00 26.88 C ANISOU 2885 CD2 HIS B 84 2336 3195 4684 -238 -581 -777 C ATOM 2886 CE1 HIS B 84 -0.849 -5.920 7.675 1.00 25.92 C ANISOU 2886 CE1 HIS B 84 2299 3126 4424 -158 -412 -507 C ATOM 2887 NE2 HIS B 84 -0.924 -5.774 6.350 1.00 26.38 N ANISOU 2887 NE2 HIS B 84 2369 3242 4414 -194 -461 -676 N ATOM 2888 N VAL B 85 -4.252 -8.268 6.224 1.00 27.38 N ANISOU 2888 N VAL B 85 1994 3043 5364 -301 -764 -486 N ATOM 2889 CA VAL B 85 -5.278 -7.796 5.278 1.00 28.78 C ANISOU 2889 CA VAL B 85 2119 3220 5595 -305 -943 -535 C ATOM 2890 C VAL B 85 -4.764 -7.872 3.804 1.00 31.91 C ANISOU 2890 C VAL B 85 2724 3612 5787 -306 -1157 -803 C ATOM 2891 O VAL B 85 -5.545 -8.224 2.933 1.00 32.47 O ANISOU 2891 O VAL B 85 2773 3559 6005 -319 -1434 -896 O ATOM 2892 CB VAL B 85 -5.805 -6.374 5.661 1.00 31.27 C ANISOU 2892 CB VAL B 85 2467 3657 5757 -243 -810 -392 C ATOM 2893 CG1 VAL B 85 -4.713 -5.312 5.582 1.00 28.23 C ANISOU 2893 CG1 VAL B 85 2349 3446 4930 -197 -691 -456 C ATOM 2894 CG2 VAL B 85 -7.036 -5.979 4.843 1.00 32.86 C ANISOU 2894 CG2 VAL B 85 2561 3803 6120 -234 -1037 -422 C ATOM 2895 N THR B 86 -3.457 -7.598 3.551 1.00 27.00 N ANISOU 2895 N THR B 86 2318 3075 4865 -286 -1025 -928 N ATOM 2896 CA THR B 86 -2.854 -7.622 2.204 1.00 28.54 C ANISOU 2896 CA THR B 86 2788 3224 4832 -269 -1102 -1169 C ATOM 2897 C THR B 86 -2.715 -9.039 1.607 1.00 35.81 C ANISOU 2897 C THR B 86 3716 3965 5924 -298 -1269 -1311 C ATOM 2898 O THR B 86 -2.346 -9.170 0.438 1.00 36.77 O ANISOU 2898 O THR B 86 4129 3988 5852 -266 -1334 -1508 O ATOM 2899 CB THR B 86 -1.463 -6.986 2.217 1.00 31.01 C ANISOU 2899 CB THR B 86 3261 3629 4892 -246 -830 -1244 C ATOM 2900 OG1 THR B 86 -0.643 -7.760 3.088 1.00 29.29 O ANISOU 2900 OG1 THR B 86 2872 3387 4869 -269 -730 -1212 O ATOM 2901 CG2 THR B 86 -1.481 -5.509 2.612 1.00 25.21 C ANISOU 2901 CG2 THR B 86 2592 3054 3933 -215 -685 -1139 C ATOM 2902 N LEU B 87 -2.957 -10.084 2.406 1.00 33.43 N ANISOU 2902 N LEU B 87 3154 3595 5951 -347 -1308 -1211 N ATOM 2903 CA LEU B 87 -2.838 -11.460 1.936 1.00 35.48 C ANISOU 2903 CA LEU B 87 3412 3683 6387 -377 -1472 -1332 C ATOM 2904 C LEU B 87 -4.239 -12.070 1.765 1.00 42.81 C ANISOU 2904 C LEU B 87 4163 4453 7648 -423 -1780 -1280 C ATOM 2905 O LEU B 87 -5.047 -12.008 2.698 1.00 42.84 O ANISOU 2905 O LEU B 87 3887 4464 7927 -459 -1728 -1080 O ATOM 2906 CB LEU B 87 -1.982 -12.283 2.919 1.00 34.69 C ANISOU 2906 CB LEU B 87 3171 3576 6434 -398 -1311 -1281 C ATOM 2907 CG LEU B 87 -0.554 -11.790 3.196 1.00 37.54 C ANISOU 2907 CG LEU B 87 3622 4033 6610 -355 -1064 -1341 C ATOM 2908 CD1 LEU B 87 0.017 -12.461 4.431 1.00 36.06 C ANISOU 2908 CD1 LEU B 87 3281 3808 6612 -358 -999 -1247 C ATOM 2909 CD2 LEU B 87 0.366 -12.036 1.996 1.00 43.48 C ANISOU 2909 CD2 LEU B 87 4595 4708 7217 -323 -1014 -1583 C ATOM 2910 N SER B 88 -4.539 -12.620 0.567 1.00 41.82 N ANISOU 2910 N SER B 88 4222 4148 7519 -412 -2095 -1460 N ATOM 2911 CA SER B 88 -5.853 -13.222 0.257 1.00 44.59 C ANISOU 2911 CA SER B 88 4399 4289 8255 -455 -2482 -1447 C ATOM 2912 C SER B 88 -6.057 -14.521 1.033 1.00 50.61 C ANISOU 2912 C SER B 88 4851 4940 9440 -544 -2474 -1350 C ATOM 2913 O SER B 88 -7.186 -14.888 1.345 1.00 52.32 O ANISOU 2913 O SER B 88 4755 5012 10113 -608 -2632 -1241 O ATOM 2914 CB SER B 88 -5.999 -13.481 -1.242 1.00 50.26 C ANISOU 2914 CB SER B 88 5500 4792 8806 -397 -2876 -1685 C ATOM 2915 OG SER B 88 -4.930 -14.265 -1.748 1.00 57.71 O ANISOU 2915 OG SER B 88 6729 5671 9527 -370 -2794 -1843 O ATOM 2916 N GLN B 89 -4.950 -15.204 1.348 1.00 46.86 N ANISOU 2916 N GLN B 89 4456 4504 8845 -545 -2276 -1392 N ATOM 2917 CA GLN B 89 -4.916 -16.444 2.115 1.00 46.75 C ANISOU 2917 CA GLN B 89 4234 4385 9145 -614 -2235 -1313 C ATOM 2918 C GLN B 89 -3.677 -16.445 3.031 1.00 47.61 C ANISOU 2918 C GLN B 89 4382 4635 9072 -583 -1895 -1267 C ATOM 2919 O GLN B 89 -2.702 -15.753 2.710 1.00 43.97 O ANISOU 2919 O GLN B 89 4121 4307 8279 -516 -1755 -1368 O ATOM 2920 CB GLN B 89 -4.940 -17.682 1.182 1.00 50.32 C ANISOU 2920 CB GLN B 89 4806 4610 9703 -632 -2560 -1494 C ATOM 2921 CG GLN B 89 -3.788 -17.774 0.174 1.00 68.90 C ANISOU 2921 CG GLN B 89 7567 6964 11650 -545 -2550 -1727 C ATOM 2922 CD GLN B 89 -3.725 -19.088 -0.586 1.00 94.16 C ANISOU 2922 CD GLN B 89 10925 9920 14932 -547 -2823 -1886 C ATOM 2923 OE1 GLN B 89 -2.906 -19.255 -1.497 1.00 92.93 O ANISOU 2923 OE1 GLN B 89 11143 9699 14468 -463 -2805 -2077 O ATOM 2924 NE2 GLN B 89 -4.555 -20.063 -0.226 1.00 85.02 N ANISOU 2924 NE2 GLN B 89 9509 8595 14199 -639 -3044 -1808 N ATOM 2925 N PRO B 90 -3.687 -17.209 4.158 1.00 45.90 N ANISOU 2925 N PRO B 90 4000 4352 9090 -623 -1772 -1122 N ATOM 2926 CA PRO B 90 -2.500 -17.245 5.033 1.00 44.57 C ANISOU 2926 CA PRO B 90 3910 4258 8766 -572 -1548 -1098 C ATOM 2927 C PRO B 90 -1.248 -17.682 4.270 1.00 49.54 C ANISOU 2927 C PRO B 90 4711 4885 9228 -523 -1591 -1332 C ATOM 2928 O PRO B 90 -1.313 -18.625 3.484 1.00 51.04 O ANISOU 2928 O PRO B 90 4952 4939 9502 -543 -1773 -1467 O ATOM 2929 CB PRO B 90 -2.886 -18.275 6.108 1.00 47.03 C ANISOU 2929 CB PRO B 90 4102 4400 9365 -618 -1497 -940 C ATOM 2930 CG PRO B 90 -4.359 -18.281 6.123 1.00 52.94 C ANISOU 2930 CG PRO B 90 4641 5046 10430 -696 -1538 -801 C ATOM 2931 CD PRO B 90 -4.764 -18.071 4.693 1.00 49.44 C ANISOU 2931 CD PRO B 90 4205 4606 9972 -711 -1833 -977 C ATOM 2932 N LYS B 91 -0.140 -16.948 4.438 1.00 43.59 N ANISOU 2932 N LYS B 91 3825 4923 7812 873 -2085 -1794 N ATOM 2933 CA LYS B 91 1.122 -17.257 3.767 1.00 41.86 C ANISOU 2933 CA LYS B 91 3857 4525 7522 778 -2088 -1855 C ATOM 2934 C LYS B 91 1.990 -18.126 4.691 1.00 44.09 C ANISOU 2934 C LYS B 91 4199 4652 7900 615 -1957 -1885 C ATOM 2935 O LYS B 91 2.233 -17.754 5.843 1.00 42.53 O ANISOU 2935 O LYS B 91 4023 4383 7754 663 -1826 -1832 O ATOM 2936 CB LYS B 91 1.841 -15.954 3.351 1.00 43.56 C ANISOU 2936 CB LYS B 91 4329 4637 7584 956 -2046 -1807 C ATOM 2937 CG LYS B 91 3.202 -16.130 2.666 1.00 51.51 C ANISOU 2937 CG LYS B 91 5569 5489 8512 864 -2013 -1858 C ATOM 2938 CD LYS B 91 3.094 -16.601 1.210 1.00 68.67 C ANISOU 2938 CD LYS B 91 7798 7701 10591 839 -2160 -1923 C ATOM 2939 CE LYS B 91 4.446 -16.756 0.546 1.00 83.22 C ANISOU 2939 CE LYS B 91 9870 9403 12347 776 -2090 -1960 C ATOM 2940 NZ LYS B 91 5.118 -15.446 0.315 1.00 92.83 N ANISOU 2940 NZ LYS B 91 11307 10528 13435 877 -1987 -1909 N ATOM 2941 N ILE B 92 2.431 -19.290 4.188 1.00 40.22 N ANISOU 2941 N ILE B 92 3769 4104 7409 448 -1999 -1969 N ATOM 2942 CA ILE B 92 3.278 -20.222 4.939 1.00 38.78 C ANISOU 2942 CA ILE B 92 3683 3778 7273 340 -1888 -2004 C ATOM 2943 C ILE B 92 4.684 -20.199 4.324 1.00 41.89 C ANISOU 2943 C ILE B 92 4284 4070 7562 374 -1861 -2035 C ATOM 2944 O ILE B 92 4.851 -20.463 3.125 1.00 41.68 O ANISOU 2944 O ILE B 92 4348 4047 7442 355 -1948 -2078 O ATOM 2945 CB ILE B 92 2.673 -21.666 5.005 1.00 42.72 C ANISOU 2945 CB ILE B 92 4135 4273 7825 135 -1917 -2072 C ATOM 2946 CG1 ILE B 92 1.314 -21.674 5.723 1.00 44.78 C ANISOU 2946 CG1 ILE B 92 4144 4666 8204 70 -1904 -2038 C ATOM 2947 CG2 ILE B 92 3.622 -22.660 5.687 1.00 42.09 C ANISOU 2947 CG2 ILE B 92 4237 4017 7738 81 -1799 -2111 C ATOM 2948 CD1 ILE B 92 0.198 -22.161 4.871 1.00 57.42 C ANISOU 2948 CD1 ILE B 92 5577 6433 9805 -84 -2062 -2089 C ATOM 2949 N VAL B 93 5.684 -19.849 5.155 1.00 37.24 N ANISOU 2949 N VAL B 93 3761 3409 6981 427 -1742 -2011 N ATOM 2950 CA VAL B 93 7.095 -19.792 4.780 1.00 35.78 C ANISOU 2950 CA VAL B 93 3706 3180 6711 451 -1689 -2036 C ATOM 2951 C VAL B 93 7.821 -20.867 5.587 1.00 38.80 C ANISOU 2951 C VAL B 93 4126 3503 7116 435 -1617 -2077 C ATOM 2952 O VAL B 93 7.848 -20.810 6.826 1.00 36.58 O ANISOU 2952 O VAL B 93 3809 3189 6899 456 -1554 -2056 O ATOM 2953 CB VAL B 93 7.721 -18.373 4.972 1.00 38.70 C ANISOU 2953 CB VAL B 93 4116 3550 7038 510 -1627 -1985 C ATOM 2954 CG1 VAL B 93 9.222 -18.385 4.673 1.00 37.79 C ANISOU 2954 CG1 VAL B 93 4072 3438 6849 491 -1556 -2017 C ATOM 2955 CG2 VAL B 93 7.015 -17.344 4.097 1.00 39.50 C ANISOU 2955 CG2 VAL B 93 4261 3679 7067 570 -1688 -1944 C ATOM 2956 N LYS B 94 8.410 -21.836 4.877 1.00 36.41 N ANISOU 2956 N LYS B 94 3930 3173 6731 430 -1624 -2133 N ATOM 2957 CA LYS B 94 9.124 -22.949 5.487 1.00 36.88 C ANISOU 2957 CA LYS B 94 4081 3173 6759 471 -1558 -2175 C ATOM 2958 C LYS B 94 10.529 -22.552 5.893 1.00 40.44 C ANISOU 2958 C LYS B 94 4507 3690 7170 578 -1482 -2172 C ATOM 2959 O LYS B 94 11.185 -21.776 5.188 1.00 40.27 O ANISOU 2959 O LYS B 94 4450 3748 7101 585 -1470 -2160 O ATOM 2960 CB LYS B 94 9.192 -24.155 4.514 1.00 39.95 C ANISOU 2960 CB LYS B 94 4648 3496 7034 456 -1588 -2232 C ATOM 2961 CG LYS B 94 7.839 -24.756 4.169 1.00 51.06 C ANISOU 2961 CG LYS B 94 6086 4847 8466 296 -1679 -2256 C ATOM 2962 CD LYS B 94 7.991 -25.893 3.161 1.00 60.58 C ANISOU 2962 CD LYS B 94 7536 5958 9524 266 -1717 -2317 C ATOM 2963 CE LYS B 94 6.731 -26.709 2.998 1.00 77.37 C ANISOU 2963 CE LYS B 94 9720 8016 11659 48 -1803 -2362 C ATOM 2964 NZ LYS B 94 5.734 -26.036 2.126 1.00 91.97 N ANISOU 2964 NZ LYS B 94 11412 9984 13548 -55 -1959 -2358 N ATOM 2965 N TRP B 95 11.001 -23.101 7.028 1.00 37.34 N ANISOU 2965 N TRP B 95 4134 3272 6783 654 -1429 -2189 N ATOM 2966 CA TRP B 95 12.374 -22.916 7.488 1.00 36.09 C ANISOU 2966 CA TRP B 95 3920 3220 6572 766 -1382 -2203 C ATOM 2967 C TRP B 95 13.308 -23.646 6.520 1.00 44.07 C ANISOU 2967 C TRP B 95 4996 4299 7451 870 -1352 -2240 C ATOM 2968 O TRP B 95 13.218 -24.872 6.369 1.00 43.55 O ANISOU 2968 O TRP B 95 5107 4140 7300 953 -1339 -2272 O ATOM 2969 CB TRP B 95 12.561 -23.425 8.925 1.00 34.15 C ANISOU 2969 CB TRP B 95 3712 2927 6336 862 -1355 -2217 C ATOM 2970 CG TRP B 95 13.972 -23.319 9.436 1.00 35.22 C ANISOU 2970 CG TRP B 95 3762 3217 6403 995 -1340 -2245 C ATOM 2971 CD1 TRP B 95 14.808 -22.243 9.335 1.00 38.13 C ANISOU 2971 CD1 TRP B 95 3955 3754 6777 939 -1347 -2238 C ATOM 2972 CD2 TRP B 95 14.693 -24.319 10.171 1.00 35.84 C ANISOU 2972 CD2 TRP B 95 3924 3312 6383 1203 -1319 -2288 C ATOM 2973 NE1 TRP B 95 16.028 -22.534 9.905 1.00 38.49 N ANISOU 2973 NE1 TRP B 95 3912 3965 6747 1082 -1347 -2280 N ATOM 2974 CE2 TRP B 95 15.978 -23.794 10.443 1.00 39.99 C ANISOU 2974 CE2 TRP B 95 4260 4069 6867 1278 -1336 -2309 C ATOM 2975 CE3 TRP B 95 14.388 -25.624 10.602 1.00 38.01 C ANISOU 2975 CE3 TRP B 95 4438 3427 6577 1335 -1284 -2314 C ATOM 2976 CZ2 TRP B 95 16.939 -24.508 11.167 1.00 40.31 C ANISOU 2976 CZ2 TRP B 95 4304 4220 6793 1521 -1342 -2354 C ATOM 2977 CZ3 TRP B 95 15.347 -26.335 11.310 1.00 40.52 C ANISOU 2977 CZ3 TRP B 95 4827 3806 6762 1592 -1270 -2353 C ATOM 2978 CH2 TRP B 95 16.606 -25.782 11.580 1.00 41.72 C ANISOU 2978 CH2 TRP B 95 4750 4225 6877 1705 -1309 -2373 C ATOM 2979 N ASP B 96 14.132 -22.883 5.799 1.00 44.72 N ANISOU 2979 N ASP B 96 4972 4523 7498 858 -1325 -2230 N ATOM 2980 CA ASP B 96 15.080 -23.445 4.837 1.00 47.31 C ANISOU 2980 CA ASP B 96 5339 4944 7695 975 -1266 -2252 C ATOM 2981 C ASP B 96 16.373 -23.738 5.585 1.00 53.70 C ANISOU 2981 C ASP B 96 6023 5935 8447 1141 -1215 -2278 C ATOM 2982 O ASP B 96 17.126 -22.817 5.908 1.00 52.28 O ANISOU 2982 O ASP B 96 5631 5931 8301 1078 -1197 -2274 O ATOM 2983 CB ASP B 96 15.283 -22.488 3.632 1.00 50.10 C ANISOU 2983 CB ASP B 96 5650 5359 8027 873 -1236 -2227 C ATOM 2984 CG ASP B 96 16.294 -22.931 2.580 1.00 68.35 C ANISOU 2984 CG ASP B 96 7994 7777 10198 994 -1143 -2237 C ATOM 2985 OD1 ASP B 96 16.363 -24.152 2.294 1.00 70.51 O ANISOU 2985 OD1 ASP B 96 8435 7989 10365 1155 -1132 -2259 O ATOM 2986 OD2 ASP B 96 16.970 -22.049 1.998 1.00 75.55 O ANISOU 2986 OD2 ASP B 96 8800 8814 11091 922 -1065 -2219 O ATOM 2987 N ARG B 97 16.583 -25.027 5.923 1.00 53.51 N ANISOU 2987 N ARG B 97 6148 5864 8319 1350 -1199 -2309 N ATOM 2988 CA ARG B 97 17.751 -25.515 6.657 1.00 85.75 C ANISOU 2988 CA ARG B 97 10144 10128 12308 1589 -1167 -2338 C ATOM 2989 C ARG B 97 18.969 -25.586 5.741 1.00118.23 C ANISOU 2989 C ARG B 97 14134 14486 16303 1731 -1082 -2340 C ATOM 2990 O ARG B 97 19.519 -24.552 5.370 1.00 82.21 O ANISOU 2990 O ARG B 97 9327 10112 11796 1589 -1052 -2327 O ATOM 2991 CB ARG B 97 17.462 -26.894 7.272 1.00 85.83 C ANISOU 2991 CB ARG B 97 10443 9961 12206 1796 -1163 -2365 C TER 2992 ARG B 97 ATOM 2993 N GLN C 2 14.451 23.805 39.368 1.00 47.38 N ANISOU 2993 N GLN C 2 8426 4560 5015 -309 -202 318 N ATOM 2994 CA GLN C 2 14.736 23.610 40.788 1.00 47.21 C ANISOU 2994 CA GLN C 2 8324 4573 5041 -348 -301 347 C ATOM 2995 C GLN C 2 15.275 24.905 41.451 1.00 46.30 C ANISOU 2995 C GLN C 2 7829 4637 5127 -299 -266 352 C ATOM 2996 O GLN C 2 15.366 24.946 42.675 1.00 47.21 O ANISOU 2996 O GLN C 2 7861 4809 5269 -380 -355 371 O ATOM 2997 CB GLN C 2 15.671 22.411 41.045 1.00 51.01 C ANISOU 2997 CB GLN C 2 9035 4848 5497 -176 -331 394 C ATOM 2998 CG GLN C 2 17.037 22.475 40.353 1.00 77.08 C ANISOU 2998 CG GLN C 2 12279 8070 8939 159 -189 424 C ATOM 2999 CD GLN C 2 17.220 21.470 39.234 1.00101.34 C ANISOU 2999 CD GLN C 2 15709 10912 11883 310 -105 410 C ATOM 3000 OE1 GLN C 2 16.364 20.616 38.964 1.00 98.63 O ANISOU 3000 OE1 GLN C 2 15707 10437 11330 154 -175 381 O ATOM 3001 NE2 GLN C 2 18.363 21.544 38.562 1.00 92.98 N ANISOU 3001 NE2 GLN C 2 14591 9799 10937 613 53 435 N ATOM 3002 N ASN C 3 15.571 25.964 40.663 1.00 36.43 N ANISOU 3002 N ASN C 3 6379 3469 3996 -196 -150 336 N ATOM 3003 CA ASN C 3 15.993 27.261 41.201 1.00 33.06 C ANISOU 3003 CA ASN C 3 5629 3196 3736 -181 -126 339 C ATOM 3004 C ASN C 3 15.844 28.376 40.159 1.00 29.00 C ANISOU 3004 C ASN C 3 4966 2762 3293 -143 -18 311 C ATOM 3005 O ASN C 3 16.502 28.358 39.123 1.00 26.94 O ANISOU 3005 O ASN C 3 4731 2440 3066 21 84 328 O ATOM 3006 CB ASN C 3 17.426 27.235 41.748 1.00 38.89 C ANISOU 3006 CB ASN C 3 6250 3914 4613 -8 -129 410 C ATOM 3007 CG ASN C 3 17.740 28.445 42.587 1.00 67.83 C ANISOU 3007 CG ASN C 3 9642 7727 8406 -71 -156 419 C ATOM 3008 OD1 ASN C 3 17.092 28.715 43.616 1.00 60.46 O ANISOU 3008 OD1 ASN C 3 8683 6863 7427 -254 -239 388 O ATOM 3009 ND2 ASN C 3 18.712 29.225 42.130 1.00 56.85 N ANISOU 3009 ND2 ASN C 3 8056 6384 7161 69 -79 462 N ATOM 3010 N ILE C 4 14.965 29.340 40.446 1.00 21.21 N ANISOU 3010 N ILE C 4 3831 1907 2321 -289 -33 272 N ATOM 3011 CA ILE C 4 14.721 30.479 39.582 1.00 21.11 C ANISOU 3011 CA ILE C 4 3675 1967 2377 -270 46 252 C ATOM 3012 C ILE C 4 14.948 31.723 40.427 1.00 25.35 C ANISOU 3012 C ILE C 4 3974 2616 3040 -294 43 240 C ATOM 3013 O ILE C 4 14.250 31.917 41.424 1.00 25.85 O ANISOU 3013 O ILE C 4 4002 2748 3072 -428 -12 208 O ATOM 3014 CB ILE C 4 13.324 30.437 38.922 1.00 24.87 C ANISOU 3014 CB ILE C 4 4233 2476 2741 -410 29 228 C ATOM 3015 CG1 ILE C 4 13.123 29.108 38.134 1.00 28.35 C ANISOU 3015 CG1 ILE C 4 4973 2779 3021 -421 9 243 C ATOM 3016 CG2 ILE C 4 13.144 31.667 38.004 1.00 25.00 C ANISOU 3016 CG2 ILE C 4 4100 2558 2843 -373 98 222 C ATOM 3017 CD1 ILE C 4 11.887 28.974 37.491 1.00 38.72 C ANISOU 3017 CD1 ILE C 4 6376 4120 4215 -580 -33 245 C ATOM 3018 N ASP C 5 15.954 32.522 40.069 1.00 19.44 N ANISOU 3018 N ASP C 5 3083 1881 2420 -175 103 268 N ATOM 3019 CA ASP C 5 16.292 33.712 40.841 1.00 19.17 C ANISOU 3019 CA ASP C 5 2864 1928 2493 -211 88 264 C ATOM 3020 C ASP C 5 16.072 34.954 40.062 1.00 19.47 C ANISOU 3020 C ASP C 5 2791 2009 2597 -197 152 247 C ATOM 3021 O ASP C 5 16.613 35.108 38.963 1.00 17.49 O ANISOU 3021 O ASP C 5 2525 1734 2385 -96 222 281 O ATOM 3022 CB ASP C 5 17.770 33.682 41.313 1.00 23.11 C ANISOU 3022 CB ASP C 5 3271 2419 3091 -123 67 341 C ATOM 3023 CG ASP C 5 18.037 32.674 42.417 1.00 43.37 C ANISOU 3023 CG ASP C 5 5919 4949 5611 -156 -32 370 C ATOM 3024 OD1 ASP C 5 17.408 32.795 43.511 1.00 44.98 O ANISOU 3024 OD1 ASP C 5 6146 5187 5757 -308 -105 328 O ATOM 3025 OD2 ASP C 5 18.866 31.764 42.199 1.00 49.64 O ANISOU 3025 OD2 ASP C 5 6762 5678 6422 -26 -29 438 O ATOM 3026 N GLN C 6 15.361 35.887 40.677 1.00 15.38 N ANISOU 3026 N GLN C 6 2200 1549 2092 -291 136 197 N ATOM 3027 CA GLN C 6 15.131 37.235 40.136 1.00 15.65 C ANISOU 3027 CA GLN C 6 2135 1612 2200 -279 182 180 C ATOM 3028 C GLN C 6 15.133 38.217 41.312 1.00 17.20 C ANISOU 3028 C GLN C 6 2265 1836 2434 -350 154 142 C ATOM 3029 O GLN C 6 14.858 37.795 42.431 1.00 17.57 O ANISOU 3029 O GLN C 6 2356 1898 2420 -429 111 112 O ATOM 3030 CB GLN C 6 13.834 37.336 39.273 1.00 16.26 C ANISOU 3030 CB GLN C 6 2241 1709 2229 -299 208 156 C ATOM 3031 CG GLN C 6 12.561 36.841 39.962 1.00 17.77 C ANISOU 3031 CG GLN C 6 2469 1953 2329 -402 175 118 C ATOM 3032 CD GLN C 6 11.354 36.965 39.046 1.00 25.54 C ANISOU 3032 CD GLN C 6 3445 2978 3280 -428 183 130 C ATOM 3033 OE1 GLN C 6 11.112 37.989 38.359 1.00 20.07 O ANISOU 3033 OE1 GLN C 6 2673 2295 2659 -382 213 138 O ATOM 3034 NE2 GLN C 6 10.575 35.940 39.010 1.00 11.90 N ANISOU 3034 NE2 GLN C 6 1805 1275 1443 -515 142 144 N ATOM 3035 N PRO C 7 15.498 39.502 41.115 1.00 16.79 N ANISOU 3035 N PRO C 7 2138 1777 2465 -335 175 144 N ATOM 3036 CA PRO C 7 15.518 40.429 42.264 1.00 16.90 C ANISOU 3036 CA PRO C 7 2145 1787 2488 -412 148 100 C ATOM 3037 C PRO C 7 14.135 40.616 42.855 1.00 19.26 C ANISOU 3037 C PRO C 7 2481 2113 2724 -452 182 14 C ATOM 3038 O PRO C 7 13.115 40.483 42.168 1.00 17.82 O ANISOU 3038 O PRO C 7 2282 1962 2527 -415 223 2 O ATOM 3039 CB PRO C 7 16.062 41.754 41.680 1.00 19.01 C ANISOU 3039 CB PRO C 7 2358 2022 2842 -388 164 124 C ATOM 3040 CG PRO C 7 15.946 41.634 40.211 1.00 23.03 C ANISOU 3040 CG PRO C 7 2837 2532 3381 -301 215 163 C ATOM 3041 CD PRO C 7 15.904 40.174 39.853 1.00 17.70 C ANISOU 3041 CD PRO C 7 2201 1875 2649 -263 220 187 C ATOM 3042 N THR C 8 14.095 40.905 44.144 1.00 17.14 N ANISOU 3042 N THR C 8 2261 1841 2411 -534 164 -36 N ATOM 3043 CA THR C 8 12.828 41.126 44.849 1.00 16.82 C ANISOU 3043 CA THR C 8 2251 1838 2304 -564 225 -119 C ATOM 3044 C THR C 8 12.154 42.418 44.339 1.00 19.50 C ANISOU 3044 C THR C 8 2550 2153 2705 -480 302 -157 C ATOM 3045 O THR C 8 10.950 42.440 44.086 1.00 17.82 O ANISOU 3045 O THR C 8 2288 1998 2485 -433 367 -179 O ATOM 3046 CB THR C 8 13.111 41.230 46.365 1.00 19.33 C ANISOU 3046 CB THR C 8 2663 2138 2542 -679 197 -167 C ATOM 3047 OG1 THR C 8 13.960 40.147 46.741 1.00 18.90 O ANISOU 3047 OG1 THR C 8 2639 2088 2456 -745 98 -105 O ATOM 3048 CG2 THR C 8 11.830 41.246 47.205 1.00 21.96 C ANISOU 3048 CG2 THR C 8 3035 2528 2783 -714 283 -252 C ATOM 3049 N GLU C 9 12.935 43.492 44.209 1.00 16.51 N ANISOU 3049 N GLU C 9 2192 1691 2388 -466 287 -152 N ATOM 3050 CA GLU C 9 12.386 44.798 43.817 1.00 18.79 C ANISOU 3050 CA GLU C 9 2483 1924 2733 -383 349 -187 C ATOM 3051 C GLU C 9 13.325 45.569 42.952 1.00 21.85 C ANISOU 3051 C GLU C 9 2862 2238 3201 -365 305 -128 C ATOM 3052 O GLU C 9 14.537 45.426 43.077 1.00 20.52 O ANISOU 3052 O GLU C 9 2702 2055 3040 -440 233 -75 O ATOM 3053 CB GLU C 9 12.091 45.672 45.061 1.00 21.66 C ANISOU 3053 CB GLU C 9 2965 2224 3040 -412 399 -283 C ATOM 3054 CG GLU C 9 11.054 45.133 46.028 1.00 34.91 C ANISOU 3054 CG GLU C 9 4658 3980 4625 -429 477 -353 C ATOM 3055 CD GLU C 9 10.952 45.900 47.333 1.00 67.37 C ANISOU 3055 CD GLU C 9 8930 8017 8651 -473 538 -454 C ATOM 3056 OE1 GLU C 9 11.156 47.136 47.321 1.00 62.80 O ANISOU 3056 OE1 GLU C 9 8449 7313 8099 -430 560 -490 O ATOM 3057 OE2 GLU C 9 10.637 45.266 48.366 1.00 70.62 O ANISOU 3057 OE2 GLU C 9 9393 8486 8953 -558 565 -498 O ATOM 3058 N MET C 10 12.769 46.410 42.085 1.00 19.02 N ANISOU 3058 N MET C 10 2480 1842 2905 -271 343 -123 N ATOM 3059 CA MET C 10 13.537 47.332 41.255 1.00 19.71 C ANISOU 3059 CA MET C 10 2579 1849 3059 -264 306 -69 C ATOM 3060 C MET C 10 12.796 48.644 41.177 1.00 23.45 C ANISOU 3060 C MET C 10 3116 2225 3567 -182 350 -114 C ATOM 3061 O MET C 10 11.572 48.649 41.058 1.00 23.07 O ANISOU 3061 O MET C 10 3023 2211 3533 -78 414 -143 O ATOM 3062 CB MET C 10 13.816 46.764 39.852 1.00 21.74 C ANISOU 3062 CB MET C 10 2745 2157 3357 -231 290 22 C ATOM 3063 CG MET C 10 14.710 45.526 39.873 1.00 25.34 C ANISOU 3063 CG MET C 10 3160 2682 3785 -282 259 72 C ATOM 3064 SD MET C 10 15.223 45.062 38.240 1.00 29.98 S ANISOU 3064 SD MET C 10 3691 3298 4403 -235 270 167 S ATOM 3065 CE MET C 10 16.565 46.293 37.998 1.00 26.39 C ANISOU 3065 CE MET C 10 3227 2789 4012 -293 238 234 C ATOM 3066 N THR C 11 13.531 49.761 41.295 1.00 18.40 N ANISOU 3066 N THR C 11 2587 1463 2940 -230 311 -112 N ATOM 3067 CA THR C 11 12.972 51.105 41.224 1.00 19.69 C ANISOU 3067 CA THR C 11 2859 1490 3131 -147 344 -153 C ATOM 3068 C THR C 11 13.736 51.884 40.164 1.00 24.77 C ANISOU 3068 C THR C 11 3524 2058 3829 -181 274 -67 C ATOM 3069 O THR C 11 14.979 51.883 40.171 1.00 22.87 O ANISOU 3069 O THR C 11 3297 1819 3575 -321 200 -8 O ATOM 3070 CB THR C 11 13.047 51.790 42.616 1.00 28.12 C ANISOU 3070 CB THR C 11 4121 2444 4121 -199 367 -253 C ATOM 3071 OG1 THR C 11 12.435 50.932 43.565 1.00 33.49 O ANISOU 3071 OG1 THR C 11 4772 3218 4736 -193 434 -322 O ATOM 3072 CG2 THR C 11 12.348 53.162 42.655 1.00 26.96 C ANISOU 3072 CG2 THR C 11 4127 2127 3990 -76 427 -315 C ATOM 3073 N ALA C 12 12.996 52.569 39.277 1.00 21.22 N ANISOU 3073 N ALA C 12 3072 1551 3442 -60 293 -46 N ATOM 3074 CA ALA C 12 13.588 53.447 38.249 1.00 22.12 C ANISOU 3074 CA ALA C 12 3234 1575 3597 -94 226 36 C ATOM 3075 C ALA C 12 12.641 54.593 37.966 1.00 27.50 C ANISOU 3075 C ALA C 12 4011 2114 4325 49 248 14 C ATOM 3076 O ALA C 12 11.469 54.527 38.339 1.00 27.80 O ANISOU 3076 O ALA C 12 4014 2166 4383 199 326 -44 O ATOM 3077 CB ALA C 12 13.885 52.654 36.974 1.00 21.71 C ANISOU 3077 CB ALA C 12 3033 1644 3571 -113 204 138 C ATOM 3078 N THR C 13 13.137 55.654 37.327 1.00 25.12 N ANISOU 3078 N THR C 13 3825 1676 4042 8 181 70 N ATOM 3079 CA THR C 13 12.329 56.834 37.030 1.00 25.57 C ANISOU 3079 CA THR C 13 4003 1564 4147 152 186 60 C ATOM 3080 C THR C 13 11.599 56.668 35.710 1.00 27.28 C ANISOU 3080 C THR C 13 4080 1844 4440 256 167 153 C ATOM 3081 O THR C 13 12.130 56.039 34.790 1.00 24.16 O ANISOU 3081 O THR C 13 3581 1560 4039 158 122 239 O ATOM 3082 CB THR C 13 13.248 58.072 37.039 1.00 31.19 C ANISOU 3082 CB THR C 13 4949 2078 4824 27 102 81 C ATOM 3083 OG1 THR C 13 13.902 58.069 38.303 1.00 34.60 O ANISOU 3083 OG1 THR C 13 5503 2474 5169 -99 104 6 O ATOM 3084 CG2 THR C 13 12.486 59.389 36.888 1.00 29.13 C ANISOU 3084 CG2 THR C 13 4876 1591 4600 183 104 61 C ATOM 3085 N GLU C 14 10.395 57.285 35.592 1.00 26.11 N ANISOU 3085 N GLU C 14 3942 1619 4360 457 200 145 N ATOM 3086 CA GLU C 14 9.640 57.259 34.341 1.00 25.65 C ANISOU 3086 CA GLU C 14 3763 1607 4376 547 153 255 C ATOM 3087 C GLU C 14 10.475 57.869 33.228 1.00 29.95 C ANISOU 3087 C GLU C 14 4405 2062 4912 424 43 355 C ATOM 3088 O GLU C 14 11.213 58.844 33.453 1.00 27.83 O ANISOU 3088 O GLU C 14 4336 1623 4616 349 4 341 O ATOM 3089 CB GLU C 14 8.255 57.948 34.452 1.00 28.53 C ANISOU 3089 CB GLU C 14 4110 1897 4832 799 198 252 C ATOM 3090 CG GLU C 14 8.300 59.418 34.747 1.00 41.37 C ANISOU 3090 CG GLU C 14 5982 3259 6479 896 194 216 C ATOM 3091 CD GLU C 14 6.961 60.126 34.784 1.00 51.90 C ANISOU 3091 CD GLU C 14 7293 4511 7918 1184 250 228 C ATOM 3092 OE1 GLU C 14 6.026 59.753 34.036 1.00 40.60 O ANISOU 3092 OE1 GLU C 14 5643 3210 6572 1290 224 332 O ATOM 3093 OE2 GLU C 14 6.872 61.102 35.553 1.00 38.93 O ANISOU 3093 OE2 GLU C 14 5865 2659 6268 1304 315 140 O ATOM 3094 N GLY C 15 10.368 57.253 32.054 1.00 28.69 N ANISOU 3094 N GLY C 15 4121 2021 4759 380 -6 457 N ATOM 3095 CA GLY C 15 11.104 57.653 30.866 1.00 29.61 C ANISOU 3095 CA GLY C 15 4308 2091 4851 251 -95 563 C ATOM 3096 C GLY C 15 12.397 56.875 30.737 1.00 33.26 C ANISOU 3096 C GLY C 15 4735 2669 5233 56 -78 572 C ATOM 3097 O GLY C 15 12.989 56.835 29.656 1.00 34.26 O ANISOU 3097 O GLY C 15 4871 2824 5324 -56 -117 664 O ATOM 3098 N ALA C 16 12.843 56.238 31.824 1.00 27.29 N ANISOU 3098 N ALA C 16 3937 1986 4447 21 -13 486 N ATOM 3099 CA ALA C 16 14.108 55.521 31.792 1.00 26.83 C ANISOU 3099 CA ALA C 16 3827 2038 4329 -138 5 507 C ATOM 3100 C ALA C 16 13.919 54.034 31.430 1.00 30.62 C ANISOU 3100 C ALA C 16 4154 2698 4781 -123 59 514 C ATOM 3101 O ALA C 16 12.921 53.662 30.811 1.00 28.64 O ANISOU 3101 O ALA C 16 3854 2487 4542 -42 52 538 O ATOM 3102 CB ALA C 16 14.840 55.682 33.111 1.00 27.61 C ANISOU 3102 CB ALA C 16 3980 2106 4404 -212 16 436 C ATOM 3103 N ILE C 17 14.915 53.217 31.727 1.00 30.13 N ANISOU 3103 N ILE C 17 4032 2739 4679 -211 99 511 N ATOM 3104 CA ILE C 17 14.911 51.792 31.365 1.00 31.56 C ANISOU 3104 CA ILE C 17 4112 3061 4817 -200 154 518 C ATOM 3105 C ILE C 17 15.094 50.945 32.639 1.00 36.53 C ANISOU 3105 C ILE C 17 4684 3760 5436 -193 191 440 C ATOM 3106 O ILE C 17 15.653 51.415 33.632 1.00 37.08 O ANISOU 3106 O ILE C 17 4783 3789 5516 -242 176 406 O ATOM 3107 CB ILE C 17 16.036 51.550 30.296 1.00 35.61 C ANISOU 3107 CB ILE C 17 4613 3629 5287 -291 182 610 C ATOM 3108 CG1 ILE C 17 15.759 52.314 28.994 1.00 37.59 C ANISOU 3108 CG1 ILE C 17 4940 3814 5527 -315 140 689 C ATOM 3109 CG2 ILE C 17 16.231 50.101 29.955 1.00 39.87 C ANISOU 3109 CG2 ILE C 17 5093 4286 5770 -271 256 611 C ATOM 3110 CD1 ILE C 17 17.036 52.807 28.212 1.00 51.66 C ANISOU 3110 CD1 ILE C 17 6745 5606 7278 -441 156 784 C ATOM 3111 N VAL C 18 14.539 49.733 32.643 1.00 24.42 N ANISOU 3111 N VAL C 18 3515 1949 3813 -378 165 110 N ATOM 3112 CA VAL C 18 14.751 48.812 33.736 1.00 22.74 C ANISOU 3112 CA VAL C 18 3259 1787 3595 -391 143 58 C ATOM 3113 C VAL C 18 14.985 47.440 33.097 1.00 23.31 C ANISOU 3113 C VAL C 18 3237 1961 3658 -399 182 80 C ATOM 3114 O VAL C 18 14.237 47.018 32.217 1.00 21.02 O ANISOU 3114 O VAL C 18 2932 1725 3330 -350 220 101 O ATOM 3115 CB VAL C 18 13.669 48.823 34.873 1.00 29.80 C ANISOU 3115 CB VAL C 18 4203 2681 4440 -325 127 -12 C ATOM 3116 CG1 VAL C 18 12.300 48.365 34.390 1.00 29.71 C ANISOU 3116 CG1 VAL C 18 4168 2737 4384 -236 168 -18 C ATOM 3117 CG2 VAL C 18 14.104 47.948 36.048 1.00 29.84 C ANISOU 3117 CG2 VAL C 18 4190 2718 4430 -359 97 -56 C ATOM 3118 N GLN C 19 16.050 46.767 33.524 1.00 20.12 N ANISOU 3118 N GLN C 19 2773 1577 3294 -458 163 75 N ATOM 3119 CA GLN C 19 16.371 45.434 33.040 1.00 18.43 C ANISOU 3119 CA GLN C 19 2475 1448 3080 -461 196 87 C ATOM 3120 C GLN C 19 16.177 44.475 34.198 1.00 20.16 C ANISOU 3120 C GLN C 19 2685 1705 3270 -447 155 37 C ATOM 3121 O GLN C 19 16.822 44.628 35.244 1.00 20.39 O ANISOU 3121 O GLN C 19 2728 1692 3326 -484 92 10 O ATOM 3122 CB GLN C 19 17.797 45.399 32.470 1.00 19.86 C ANISOU 3122 CB GLN C 19 2585 1619 3342 -534 215 125 C ATOM 3123 CG GLN C 19 18.156 44.016 31.909 1.00 19.31 C ANISOU 3123 CG GLN C 19 2430 1631 3276 -527 258 133 C ATOM 3124 CD GLN C 19 19.593 43.937 31.464 1.00 27.73 C ANISOU 3124 CD GLN C 19 3409 2690 4439 -593 286 159 C ATOM 3125 OE1 GLN C 19 20.029 44.669 30.587 1.00 21.30 O ANISOU 3125 OE1 GLN C 19 2595 1844 3654 -633 343 202 O ATOM 3126 NE2 GLN C 19 20.361 43.020 32.039 1.00 17.45 N ANISOU 3126 NE2 GLN C 19 2026 1414 3190 -605 250 136 N ATOM 3127 N ILE C 20 15.278 43.499 34.037 1.00 15.80 N ANISOU 3127 N ILE C 20 2120 1224 2660 -397 186 24 N ATOM 3128 CA ILE C 20 15.001 42.540 35.089 1.00 14.83 C ANISOU 3128 CA ILE C 20 2004 1133 2498 -388 159 -17 C ATOM 3129 C ILE C 20 15.678 41.232 34.750 1.00 18.50 C ANISOU 3129 C ILE C 20 2398 1649 2981 -404 164 -3 C ATOM 3130 O ILE C 20 15.262 40.548 33.820 1.00 15.70 O ANISOU 3130 O ILE C 20 2011 1349 2605 -379 214 14 O ATOM 3131 CB ILE C 20 13.477 42.318 35.340 1.00 17.79 C ANISOU 3131 CB ILE C 20 2415 1544 2801 -330 191 -49 C ATOM 3132 CG1 ILE C 20 12.709 43.663 35.479 1.00 19.80 C ANISOU 3132 CG1 ILE C 20 2729 1746 3049 -295 197 -64 C ATOM 3133 CG2 ILE C 20 13.273 41.353 36.560 1.00 15.56 C ANISOU 3133 CG2 ILE C 20 2160 1283 2471 -338 171 -90 C ATOM 3134 CD1 ILE C 20 11.180 43.500 35.375 1.00 24.86 C ANISOU 3134 CD1 ILE C 20 3367 2431 3646 -228 240 -89 C ATOM 3135 N ASN C 21 16.652 40.839 35.569 1.00 16.92 N ANISOU 3135 N ASN C 21 2183 1428 2818 -439 103 -16 N ATOM 3136 CA ASN C 21 17.418 39.607 35.370 1.00 17.24 C ANISOU 3136 CA ASN C 21 2154 1504 2892 -446 95 -7 C ATOM 3137 C ASN C 21 16.744 38.409 35.996 1.00 21.18 C ANISOU 3137 C ASN C 21 2689 2040 3320 -420 84 -32 C ATOM 3138 O ASN C 21 16.161 38.506 37.092 1.00 20.31 O ANISOU 3138 O ASN C 21 2656 1910 3150 -419 52 -63 O ATOM 3139 CB ASN C 21 18.829 39.764 35.975 1.00 18.40 C ANISOU 3139 CB ASN C 21 2259 1605 3129 -492 16 -8 C ATOM 3140 CG ASN C 21 19.664 40.845 35.303 1.00 31.66 C ANISOU 3140 CG ASN C 21 3886 3247 4896 -535 35 21 C ATOM 3141 OD1 ASN C 21 19.593 41.075 34.085 1.00 23.55 O ANISOU 3141 OD1 ASN C 21 2827 2241 3879 -532 121 53 O ATOM 3142 ND2 ASN C 21 20.490 41.527 36.084 1.00 25.83 N ANISOU 3142 ND2 ASN C 21 3147 2447 4220 -584 -48 10 N ATOM 3143 N CYS C 22 16.815 37.280 35.293 1.00 16.81 N ANISOU 3143 N CYS C 22 2086 1533 2767 -403 119 -20 N ATOM 3144 CA CYS C 22 16.308 36.006 35.779 1.00 17.49 C ANISOU 3144 CA CYS C 22 2203 1646 2795 -387 109 -38 C ATOM 3145 C CYS C 22 17.370 34.931 35.500 1.00 21.56 C ANISOU 3145 C CYS C 22 2657 2166 3368 -384 87 -28 C ATOM 3146 O CYS C 22 17.805 34.773 34.353 1.00 21.94 O ANISOU 3146 O CYS C 22 2638 2237 3462 -374 142 -10 O ATOM 3147 CB CYS C 22 14.967 35.659 35.126 1.00 18.38 C ANISOU 3147 CB CYS C 22 2332 1810 2840 -362 179 -41 C ATOM 3148 SG CYS C 22 14.261 34.078 35.675 1.00 22.97 S ANISOU 3148 SG CYS C 22 2955 2420 3352 -359 177 -61 S ATOM 3149 N THR C 23 17.831 34.237 36.534 1.00 16.99 N ANISOU 3149 N THR C 23 2107 1559 2789 -389 7 -42 N ATOM 3150 CA THR C 23 18.774 33.126 36.325 1.00 17.57 C ANISOU 3150 CA THR C 23 2123 1630 2923 -371 -22 -36 C ATOM 3151 C THR C 23 18.085 31.873 36.791 1.00 20.98 C ANISOU 3151 C THR C 23 2630 2069 3274 -357 -34 -47 C ATOM 3152 O THR C 23 17.354 31.903 37.783 1.00 19.14 O ANISOU 3152 O THR C 23 2493 1822 2959 -375 -60 -60 O ATOM 3153 CB THR C 23 20.125 33.335 37.036 1.00 29.41 C ANISOU 3153 CB THR C 23 3577 3079 4518 -385 -127 -37 C ATOM 3154 OG1 THR C 23 19.882 33.458 38.438 1.00 32.02 O ANISOU 3154 OG1 THR C 23 4013 3367 4785 -404 -221 -52 O ATOM 3155 CG2 THR C 23 20.884 34.567 36.515 1.00 22.89 C ANISOU 3155 CG2 THR C 23 2666 2242 3788 -414 -109 -24 C ATOM 3156 N TYR C 24 18.280 30.780 36.071 1.00 18.25 N ANISOU 3156 N TYR C 24 2248 1741 2945 -329 -4 -43 N ATOM 3157 CA TYR C 24 17.618 29.530 36.408 1.00 16.86 C ANISOU 3157 CA TYR C 24 2148 1565 2695 -322 -10 -51 C ATOM 3158 C TYR C 24 18.567 28.362 36.318 1.00 19.20 C ANISOU 3158 C TYR C 24 2415 1831 3049 -287 -56 -50 C ATOM 3159 O TYR C 24 19.489 28.362 35.499 1.00 18.52 O ANISOU 3159 O TYR C 24 2229 1751 3058 -260 -33 -48 O ATOM 3160 CB TYR C 24 16.400 29.292 35.472 1.00 16.20 C ANISOU 3160 CB TYR C 24 2076 1534 2546 -323 87 -54 C ATOM 3161 CG TYR C 24 16.764 29.173 34.006 1.00 16.11 C ANISOU 3161 CG TYR C 24 1989 1552 2581 -297 154 -48 C ATOM 3162 CD1 TYR C 24 16.994 27.931 33.423 1.00 16.74 C ANISOU 3162 CD1 TYR C 24 2066 1630 2666 -271 171 -55 C ATOM 3163 CD2 TYR C 24 16.841 30.300 33.191 1.00 16.05 C ANISOU 3163 CD2 TYR C 24 1930 1568 2602 -300 207 -36 C ATOM 3164 CE1 TYR C 24 17.371 27.820 32.093 1.00 18.66 C ANISOU 3164 CE1 TYR C 24 2255 1895 2940 -246 242 -54 C ATOM 3165 CE2 TYR C 24 17.182 30.197 31.846 1.00 16.21 C ANISOU 3165 CE2 TYR C 24 1902 1610 2647 -281 278 -28 C ATOM 3166 CZ TYR C 24 17.444 28.959 31.300 1.00 21.19 C ANISOU 3166 CZ TYR C 24 2531 2241 3279 -254 299 -39 C ATOM 3167 OH TYR C 24 17.798 28.861 29.974 1.00 21.29 O ANISOU 3167 OH TYR C 24 2512 2273 3305 -236 379 -37 O ATOM 3168 N GLN C 25 18.308 27.357 37.141 1.00 17.02 N ANISOU 3168 N GLN C 25 2231 1521 2716 -288 -112 -53 N ATOM 3169 CA GLN C 25 18.995 26.077 37.162 1.00 17.97 C ANISOU 3169 CA GLN C 25 2354 1601 2874 -249 -164 -53 C ATOM 3170 C GLN C 25 17.911 25.033 37.188 1.00 22.23 C ANISOU 3170 C GLN C 25 2995 2141 3310 -265 -129 -56 C ATOM 3171 O GLN C 25 17.201 24.919 38.179 1.00 21.54 O ANISOU 3171 O GLN C 25 3017 2034 3132 -304 -156 -52 O ATOM 3172 CB GLN C 25 19.948 25.947 38.370 1.00 20.55 C ANISOU 3172 CB GLN C 25 2708 1860 3239 -239 -307 -47 C ATOM 3173 CG GLN C 25 21.191 26.829 38.263 1.00 41.32 C ANISOU 3173 CG GLN C 25 5213 4485 6003 -224 -354 -47 C ATOM 3174 CD GLN C 25 20.975 28.133 38.985 1.00 66.90 C ANISOU 3174 CD GLN C 25 8485 7725 9211 -275 -384 -47 C ATOM 3175 OE1 GLN C 25 20.524 28.163 40.141 1.00 67.00 O ANISOU 3175 OE1 GLN C 25 8624 7702 9130 -304 -451 -47 O ATOM 3176 NE2 GLN C 25 21.276 29.246 38.321 1.00 54.99 N ANISOU 3176 NE2 GLN C 25 6876 6248 7771 -289 -329 -46 N ATOM 3177 N THR C 26 17.693 24.358 36.069 1.00 19.36 N ANISOU 3177 N THR C 26 2602 1801 2952 -243 -57 -64 N ATOM 3178 CA THR C 26 16.622 23.360 35.937 1.00 19.67 C ANISOU 3178 CA THR C 26 2729 1842 2903 -268 -20 -70 C ATOM 3179 C THR C 26 17.173 22.112 35.293 1.00 22.32 C ANISOU 3179 C THR C 26 3064 2142 3276 -220 -25 -79 C ATOM 3180 O THR C 26 18.242 22.167 34.669 1.00 20.96 O ANISOU 3180 O THR C 26 2799 1964 3199 -165 -21 -86 O ATOM 3181 CB THR C 26 15.441 23.936 35.085 1.00 23.48 C ANISOU 3181 CB THR C 26 3189 2395 3336 -301 78 -77 C ATOM 3182 OG1 THR C 26 15.935 24.351 33.801 1.00 24.31 O ANISOU 3182 OG1 THR C 26 3201 2535 3500 -266 134 -82 O ATOM 3183 CG2 THR C 26 14.704 25.088 35.776 1.00 23.59 C ANISOU 3183 CG2 THR C 26 3216 2439 3309 -342 89 -74 C ATOM 3184 N SER C 27 16.480 20.982 35.443 1.00 19.61 N ANISOU 3184 N SER C 27 2820 1768 2863 -242 -27 -82 N ATOM 3185 CA SER C 27 16.944 19.781 34.747 1.00 20.74 C ANISOU 3185 CA SER C 27 2974 1869 3037 -193 -26 -97 C ATOM 3186 C SER C 27 16.243 19.805 33.402 1.00 21.42 C ANISOU 3186 C SER C 27 3031 2012 3096 -205 75 -117 C ATOM 3187 O SER C 27 15.046 19.574 33.314 1.00 21.25 O ANISOU 3187 O SER C 27 3067 2012 2994 -264 106 -120 O ATOM 3188 CB SER C 27 16.657 18.503 35.540 1.00 28.98 C ANISOU 3188 CB SER C 27 4153 2834 4024 -210 -88 -89 C ATOM 3189 OG SER C 27 15.284 18.459 35.874 1.00 46.43 O ANISOU 3189 OG SER C 27 6443 5069 6131 -296 -49 -83 O ATOM 3190 N GLY C 28 16.968 20.200 32.380 1.00 18.23 N ANISOU 3190 N GLY C 28 2534 1635 2758 -156 126 -130 N ATOM 3191 CA GLY C 28 16.392 20.330 31.047 1.00 17.29 C ANISOU 3191 CA GLY C 28 2401 1567 2603 -165 215 -147 C ATOM 3192 C GLY C 28 15.708 21.674 30.896 1.00 17.95 C ANISOU 3192 C GLY C 28 2441 1720 2658 -207 250 -132 C ATOM 3193 O GLY C 28 15.401 22.361 31.886 1.00 17.07 O ANISOU 3193 O GLY C 28 2330 1617 2537 -240 214 -114 O ATOM 3194 N PHE C 29 15.479 22.068 29.649 1.00 13.16 N ANISOU 3194 N PHE C 29 1808 1157 2034 -202 320 -140 N ATOM 3195 CA PHE C 29 14.922 23.363 29.337 1.00 12.05 C ANISOU 3195 CA PHE C 29 1629 1074 1874 -229 350 -124 C ATOM 3196 C PHE C 29 13.970 23.302 28.141 1.00 14.99 C ANISOU 3196 C PHE C 29 2035 1484 2177 -247 393 -135 C ATOM 3197 O PHE C 29 14.375 22.898 27.047 1.00 14.09 O ANISOU 3197 O PHE C 29 1935 1365 2053 -218 439 -150 O ATOM 3198 CB PHE C 29 16.066 24.358 29.070 1.00 13.85 C ANISOU 3198 CB PHE C 29 1773 1309 2180 -198 381 -110 C ATOM 3199 CG PHE C 29 15.577 25.748 28.728 1.00 13.62 C ANISOU 3199 CG PHE C 29 1717 1324 2132 -222 409 -89 C ATOM 3200 CD1 PHE C 29 15.027 26.569 29.709 1.00 14.56 C ANISOU 3200 CD1 PHE C 29 1833 1453 2245 -253 367 -76 C ATOM 3201 CD2 PHE C 29 15.617 26.216 27.413 1.00 14.55 C ANISOU 3201 CD2 PHE C 29 1828 1468 2230 -213 478 -84 C ATOM 3202 CE1 PHE C 29 14.592 27.868 29.402 1.00 16.53 C ANISOU 3202 CE1 PHE C 29 2063 1733 2485 -266 388 -58 C ATOM 3203 CE2 PHE C 29 15.158 27.514 27.092 1.00 16.61 C ANISOU 3203 CE2 PHE C 29 2079 1759 2473 -232 493 -60 C ATOM 3204 CZ PHE C 29 14.663 28.342 28.096 1.00 14.47 C ANISOU 3204 CZ PHE C 29 1795 1493 2211 -255 445 -47 C ATOM 3205 N ASN C 30 12.720 23.748 28.337 1.00 10.65 N ANISOU 3205 N ASN C 30 1496 971 1580 -291 376 -129 N ATOM 3206 CA ASN C 30 11.742 23.796 27.251 1.00 11.51 C ANISOU 3206 CA ASN C 30 1628 1116 1630 -309 391 -137 C ATOM 3207 C ASN C 30 11.116 25.179 27.112 1.00 16.28 C ANISOU 3207 C ASN C 30 2190 1765 2230 -317 393 -117 C ATOM 3208 O ASN C 30 10.044 25.316 26.527 1.00 15.79 O ANISOU 3208 O ASN C 30 2139 1735 2127 -336 378 -122 O ATOM 3209 CB ASN C 30 10.661 22.723 27.397 1.00 12.46 C ANISOU 3209 CB ASN C 30 1800 1231 1703 -355 360 -159 C ATOM 3210 CG ASN C 30 11.144 21.362 26.910 1.00 17.28 C ANISOU 3210 CG ASN C 30 2477 1793 2297 -341 364 -184 C ATOM 3211 OD1 ASN C 30 11.480 21.187 25.741 1.00 18.38 O ANISOU 3211 OD1 ASN C 30 2643 1930 2412 -313 395 -199 O ATOM 3212 ND2 ASN C 30 11.110 20.358 27.770 1.00 13.74 N ANISOU 3212 ND2 ASN C 30 2071 1299 1852 -362 334 -192 N ATOM 3213 N GLY C 31 11.807 26.193 27.604 1.00 13.67 N ANISOU 3213 N GLY C 31 1814 1431 1947 -299 402 -96 N ATOM 3214 CA GLY C 31 11.327 27.557 27.412 1.00 13.87 C ANISOU 3214 CA GLY C 31 1811 1486 1973 -299 404 -75 C ATOM 3215 C GLY C 31 11.179 28.371 28.669 1.00 15.83 C ANISOU 3215 C GLY C 31 2028 1731 2255 -309 382 -68 C ATOM 3216 O GLY C 31 11.028 27.837 29.771 1.00 13.72 O ANISOU 3216 O GLY C 31 1774 1450 1991 -329 360 -81 O ATOM 3217 N LEU C 32 11.229 29.684 28.485 1.00 14.01 N ANISOU 3217 N LEU C 32 1774 1506 2042 -296 390 -48 N ATOM 3218 CA LEU C 32 11.191 30.650 29.574 1.00 13.88 C ANISOU 3218 CA LEU C 32 1740 1478 2057 -300 373 -44 C ATOM 3219 C LEU C 32 10.142 31.694 29.258 1.00 15.53 C ANISOU 3219 C LEU C 32 1939 1709 2253 -289 370 -39 C ATOM 3220 O LEU C 32 10.121 32.286 28.161 1.00 15.11 O ANISOU 3220 O LEU C 32 1891 1661 2189 -271 379 -18 O ATOM 3221 CB LEU C 32 12.592 31.294 29.800 1.00 13.54 C ANISOU 3221 CB LEU C 32 1674 1398 2071 -293 378 -26 C ATOM 3222 CG LEU C 32 12.713 32.220 31.049 1.00 18.09 C ANISOU 3222 CG LEU C 32 2248 1949 2676 -303 346 -28 C ATOM 3223 CD1 LEU C 32 14.103 32.183 31.644 1.00 18.69 C ANISOU 3223 CD1 LEU C 32 2303 1985 2812 -309 321 -23 C ATOM 3224 CD2 LEU C 32 12.329 33.688 30.735 1.00 18.34 C ANISOU 3224 CD2 LEU C 32 2276 1978 2715 -293 355 -12 C ATOM 3225 N PHE C 33 9.307 31.948 30.251 1.00 12.14 N ANISOU 3225 N PHE C 33 1503 1287 1824 -297 358 -58 N ATOM 3226 CA PHE C 33 8.193 32.876 30.154 1.00 13.47 C ANISOU 3226 CA PHE C 33 1649 1473 1994 -277 354 -62 C ATOM 3227 C PHE C 33 8.340 34.038 31.101 1.00 17.27 C ANISOU 3227 C PHE C 33 2133 1924 2503 -265 355 -65 C ATOM 3228 O PHE C 33 8.850 33.877 32.218 1.00 16.26 O ANISOU 3228 O PHE C 33 2028 1772 2378 -286 355 -77 O ATOM 3229 CB PHE C 33 6.874 32.169 30.519 1.00 14.54 C ANISOU 3229 CB PHE C 33 1763 1647 2115 -296 355 -93 C ATOM 3230 CG PHE C 33 6.418 31.024 29.642 1.00 15.61 C ANISOU 3230 CG PHE C 33 1897 1811 2224 -316 343 -99 C ATOM 3231 CD1 PHE C 33 5.424 31.217 28.680 1.00 16.21 C ANISOU 3231 CD1 PHE C 33 1944 1919 2296 -301 314 -100 C ATOM 3232 CD2 PHE C 33 6.929 29.738 29.826 1.00 16.92 C ANISOU 3232 CD2 PHE C 33 2096 1965 2366 -350 349 -105 C ATOM 3233 CE1 PHE C 33 4.946 30.141 27.915 1.00 17.39 C ANISOU 3233 CE1 PHE C 33 2100 2091 2418 -327 291 -111 C ATOM 3234 CE2 PHE C 33 6.460 28.658 29.051 1.00 19.75 C ANISOU 3234 CE2 PHE C 33 2465 2340 2697 -373 334 -116 C ATOM 3235 CZ PHE C 33 5.468 28.869 28.102 1.00 17.51 C ANISOU 3235 CZ PHE C 33 2155 2091 2407 -365 305 -120 C ATOM 3236 N TRP C 34 7.853 35.195 30.661 1.00 12.15 N ANISOU 3236 N TRP C 34 1476 1272 1871 -230 348 -55 N ATOM 3237 CA TRP C 34 7.669 36.367 31.512 1.00 12.37 C ANISOU 3237 CA TRP C 34 1511 1268 1923 -210 350 -68 C ATOM 3238 C TRP C 34 6.184 36.684 31.561 1.00 15.66 C ANISOU 3238 C TRP C 34 1889 1714 2349 -176 354 -94 C ATOM 3239 O TRP C 34 5.497 36.613 30.528 1.00 14.65 O ANISOU 3239 O TRP C 34 1731 1614 2222 -154 331 -84 O ATOM 3240 CB TRP C 34 8.468 37.581 31.021 1.00 11.20 C ANISOU 3240 CB TRP C 34 1388 1071 1798 -193 337 -34 C ATOM 3241 CG TRP C 34 9.938 37.471 31.325 1.00 12.00 C ANISOU 3241 CG TRP C 34 1506 1138 1916 -230 337 -18 C ATOM 3242 CD1 TRP C 34 10.923 37.048 30.476 1.00 14.70 C ANISOU 3242 CD1 TRP C 34 1841 1479 2264 -248 348 11 C ATOM 3243 CD2 TRP C 34 10.588 37.867 32.531 1.00 12.30 C ANISOU 3243 CD2 TRP C 34 1567 1133 1973 -250 322 -34 C ATOM 3244 NE1 TRP C 34 12.147 37.141 31.092 1.00 14.40 N ANISOU 3244 NE1 TRP C 34 1800 1406 2265 -277 339 15 N ATOM 3245 CE2 TRP C 34 11.975 37.646 32.353 1.00 16.79 C ANISOU 3245 CE2 TRP C 34 2125 1679 2574 -281 313 -11 C ATOM 3246 CE3 TRP C 34 10.137 38.380 33.759 1.00 14.35 C ANISOU 3246 CE3 TRP C 34 1858 1368 2226 -246 316 -69 C ATOM 3247 CZ2 TRP C 34 12.921 37.967 33.340 1.00 16.16 C ANISOU 3247 CZ2 TRP C 34 2059 1553 2526 -309 279 -19 C ATOM 3248 CZ3 TRP C 34 11.073 38.681 34.745 1.00 16.34 C ANISOU 3248 CZ3 TRP C 34 2147 1571 2491 -275 286 -77 C ATOM 3249 CH2 TRP C 34 12.449 38.476 34.527 1.00 16.41 C ANISOU 3249 CH2 TRP C 34 2138 1559 2539 -307 258 -51 C ATOM 3250 N TYR C 35 5.699 37.004 32.762 1.00 12.38 N ANISOU 3250 N TYR C 35 1474 1288 1940 -173 382 -131 N ATOM 3251 CA TYR C 35 4.319 37.423 33.045 1.00 13.55 C ANISOU 3251 CA TYR C 35 1572 1460 2115 -136 404 -167 C ATOM 3252 C TYR C 35 4.347 38.738 33.791 1.00 17.14 C ANISOU 3252 C TYR C 35 2060 1862 2590 -96 417 -186 C ATOM 3253 O TYR C 35 5.289 39.016 34.540 1.00 15.59 O ANISOU 3253 O TYR C 35 1930 1619 2373 -121 418 -185 O ATOM 3254 CB TYR C 35 3.573 36.365 33.911 1.00 13.85 C ANISOU 3254 CB TYR C 35 1585 1540 2137 -178 455 -206 C ATOM 3255 CG TYR C 35 3.202 35.113 33.143 1.00 15.27 C ANISOU 3255 CG TYR C 35 1724 1770 2308 -213 440 -197 C ATOM 3256 CD1 TYR C 35 1.900 34.907 32.692 1.00 17.83 C ANISOU 3256 CD1 TYR C 35 1962 2143 2669 -202 440 -217 C ATOM 3257 CD2 TYR C 35 4.140 34.115 32.908 1.00 15.84 C ANISOU 3257 CD2 TYR C 35 1841 1835 2340 -258 423 -173 C ATOM 3258 CE1 TYR C 35 1.564 33.774 31.941 1.00 17.45 C ANISOU 3258 CE1 TYR C 35 1885 2134 2612 -241 413 -211 C ATOM 3259 CE2 TYR C 35 3.809 32.967 32.194 1.00 17.82 C ANISOU 3259 CE2 TYR C 35 2070 2121 2578 -290 408 -169 C ATOM 3260 CZ TYR C 35 2.526 32.809 31.697 1.00 22.03 C ANISOU 3260 CZ TYR C 35 2528 2700 3141 -286 400 -188 C ATOM 3261 OH TYR C 35 2.233 31.665 31.000 1.00 24.19 O ANISOU 3261 OH TYR C 35 2791 3002 3399 -326 375 -187 O ATOM 3262 N GLN C 36 3.302 39.528 33.619 1.00 15.34 N ANISOU 3262 N GLN C 36 1787 1637 2405 -34 420 -206 N ATOM 3263 CA GLN C 36 3.128 40.770 34.345 1.00 14.81 C ANISOU 3263 CA GLN C 36 1751 1515 2360 14 440 -235 C ATOM 3264 C GLN C 36 1.940 40.581 35.305 1.00 19.20 C ANISOU 3264 C GLN C 36 2258 2105 2933 29 516 -298 C ATOM 3265 O GLN C 36 0.887 40.093 34.885 1.00 19.35 O ANISOU 3265 O GLN C 36 2180 2182 2990 43 526 -312 O ATOM 3266 CB GLN C 36 2.871 41.925 33.384 1.00 15.40 C ANISOU 3266 CB GLN C 36 1818 1554 2480 87 387 -210 C ATOM 3267 CG GLN C 36 2.699 43.302 34.076 1.00 17.17 C ANISOU 3267 CG GLN C 36 2086 1706 2733 147 402 -241 C ATOM 3268 CD GLN C 36 2.185 44.320 33.078 1.00 26.66 C ANISOU 3268 CD GLN C 36 3273 2872 3984 229 343 -217 C ATOM 3269 OE1 GLN C 36 1.091 44.165 32.522 1.00 25.22 O ANISOU 3269 OE1 GLN C 36 3003 2733 3845 281 324 -226 O ATOM 3270 NE2 GLN C 36 2.939 45.389 32.834 1.00 21.37 N ANISOU 3270 NE2 GLN C 36 2689 2118 3313 243 306 -185 N ATOM 3271 N GLN C 37 2.091 41.000 36.548 1.00 15.45 N ANISOU 3271 N GLN C 37 1849 1590 2432 25 569 -338 N ATOM 3272 CA GLN C 37 0.972 40.918 37.502 1.00 15.19 C ANISOU 3272 CA GLN C 37 1779 1583 2409 40 665 -403 C ATOM 3273 C GLN C 37 0.810 42.250 38.225 1.00 19.44 C ANISOU 3273 C GLN C 37 2372 2054 2962 105 698 -447 C ATOM 3274 O GLN C 37 1.663 42.631 39.038 1.00 17.27 O ANISOU 3274 O GLN C 37 2216 1717 2630 79 697 -455 O ATOM 3275 CB GLN C 37 1.193 39.764 38.506 1.00 14.75 C ANISOU 3275 CB GLN C 37 1774 1550 2278 -48 725 -417 C ATOM 3276 CG GLN C 37 -0.027 39.560 39.437 1.00 18.46 C ANISOU 3276 CG GLN C 37 2205 2055 2755 -48 847 -482 C ATOM 3277 CD GLN C 37 0.181 38.456 40.435 1.00 22.04 C ANISOU 3277 CD GLN C 37 2734 2519 3120 -140 908 -490 C ATOM 3278 OE1 GLN C 37 1.315 38.060 40.715 1.00 17.88 O ANISOU 3278 OE1 GLN C 37 2313 1957 2523 -190 854 -457 O ATOM 3279 NE2 GLN C 37 -0.899 37.981 41.044 1.00 18.64 N ANISOU 3279 NE2 GLN C 37 2256 2132 2694 -163 1022 -534 N ATOM 3280 N HIS C 38 -0.275 42.971 37.911 1.00 19.63 N ANISOU 3280 N HIS C 38 2310 2082 3065 193 716 -478 N ATOM 3281 CA HIS C 38 -0.603 44.217 38.593 1.00 20.81 C ANISOU 3281 CA HIS C 38 2503 2164 3238 270 759 -531 C ATOM 3282 C HIS C 38 -1.131 43.866 39.988 1.00 26.19 C ANISOU 3282 C HIS C 38 3212 2863 3878 244 893 -602 C ATOM 3283 O HIS C 38 -1.649 42.753 40.158 1.00 24.44 O ANISOU 3283 O HIS C 38 2923 2716 3646 188 952 -610 O ATOM 3284 CB HIS C 38 -1.623 45.033 37.777 1.00 22.80 C ANISOU 3284 CB HIS C 38 2648 2416 3600 383 730 -542 C ATOM 3285 CG HIS C 38 -0.967 45.806 36.685 1.00 26.33 C ANISOU 3285 CG HIS C 38 3137 2804 4063 417 609 -478 C ATOM 3286 ND1 HIS C 38 -1.071 45.417 35.357 1.00 28.25 N ANISOU 3286 ND1 HIS C 38 3310 3088 4335 419 522 -419 N ATOM 3287 CD2 HIS C 38 -0.162 46.889 36.762 1.00 27.61 C ANISOU 3287 CD2 HIS C 38 3417 2867 4207 438 567 -463 C ATOM 3288 CE1 HIS C 38 -0.336 46.275 34.673 1.00 26.70 C ANISOU 3288 CE1 HIS C 38 3195 2817 4131 441 440 -368 C ATOM 3289 NE2 HIS C 38 0.215 47.191 35.470 1.00 27.57 N ANISOU 3289 NE2 HIS C 38 3413 2842 4221 452 463 -392 N ATOM 3290 N ALA C 39 -0.938 44.771 40.992 1.00 25.54 N ANISOU 3290 N ALA C 39 3244 2702 3757 273 940 -653 N ATOM 3291 CA ALA C 39 -1.380 44.560 42.381 1.00 27.57 C ANISOU 3291 CA ALA C 39 3563 2961 3952 249 1077 -724 C ATOM 3292 C ALA C 39 -2.871 44.186 42.416 1.00 32.87 C ANISOU 3292 C ALA C 39 4077 3710 4702 286 1195 -775 C ATOM 3293 O ALA C 39 -3.682 44.871 41.780 1.00 32.69 O ANISOU 3293 O ALA C 39 3935 3692 4794 387 1185 -793 O ATOM 3294 CB ALA C 39 -1.136 45.829 43.223 1.00 29.88 C ANISOU 3294 CB ALA C 39 3993 3150 4212 303 1102 -779 C ATOM 3295 N GLY C 40 -3.180 43.063 43.080 1.00 30.46 N ANISOU 3295 N GLY C 40 3769 3464 4341 200 1293 -789 N ATOM 3296 CA GLY C 40 -4.529 42.524 43.219 1.00 31.87 C ANISOU 3296 CA GLY C 40 3797 3722 4590 204 1420 -835 C ATOM 3297 C GLY C 40 -5.158 42.008 41.934 1.00 35.05 C ANISOU 3297 C GLY C 40 4004 4203 5110 217 1349 -798 C ATOM 3298 O GLY C 40 -6.368 41.805 41.890 1.00 35.47 O ANISOU 3298 O GLY C 40 3898 4317 5261 241 1434 -840 O ATOM 3299 N GLU C 41 -4.356 41.791 40.879 1.00 30.36 N ANISOU 3299 N GLU C 41 3420 3606 4511 199 1195 -721 N ATOM 3300 CA GLU C 41 -4.841 41.294 39.588 1.00 29.19 C ANISOU 3300 CA GLU C 41 3118 3521 4452 206 1107 -681 C ATOM 3301 C GLU C 41 -4.184 39.949 39.243 1.00 29.99 C ANISOU 3301 C GLU C 41 3252 3660 4481 91 1057 -622 C ATOM 3302 O GLU C 41 -3.217 39.548 39.888 1.00 27.15 O ANISOU 3302 O GLU C 41 3036 3268 4012 21 1064 -603 O ATOM 3303 CB GLU C 41 -4.552 42.315 38.459 1.00 29.86 C ANISOU 3303 CB GLU C 41 3191 3561 4595 301 967 -643 C ATOM 3304 CG GLU C 41 -5.238 43.672 38.619 1.00 45.27 C ANISOU 3304 CG GLU C 41 5104 5464 6633 431 992 -696 C ATOM 3305 CD GLU C 41 -6.759 43.688 38.625 1.00 70.74 C ANISOU 3305 CD GLU C 41 8138 8749 9992 496 1066 -757 C ATOM 3306 OE1 GLU C 41 -7.371 42.947 37.822 1.00 57.57 O ANISOU 3306 OE1 GLU C 41 6328 7155 8392 475 1016 -737 O ATOM 3307 OE2 GLU C 41 -7.339 44.464 39.420 1.00 71.15 O ANISOU 3307 OE2 GLU C 41 8178 8769 10085 572 1171 -830 O ATOM 3308 N ALA C 42 -4.727 39.257 38.239 1.00 26.06 N ANISOU 3308 N ALA C 42 2626 3226 4049 75 999 -597 N ATOM 3309 CA ALA C 42 -4.178 38.004 37.732 1.00 25.27 C ANISOU 3309 CA ALA C 42 2552 3156 3893 -21 941 -545 C ATOM 3310 C ALA C 42 -2.908 38.244 36.890 1.00 24.76 C ANISOU 3310 C ALA C 42 2583 3046 3778 -11 811 -479 C ATOM 3311 O ALA C 42 -2.871 39.228 36.129 1.00 23.03 O ANISOU 3311 O ALA C 42 2346 2798 3607 72 734 -463 O ATOM 3312 CB ALA C 42 -5.213 37.319 36.860 1.00 26.60 C ANISOU 3312 CB ALA C 42 2556 3399 4153 -34 909 -546 C ATOM 3313 N PRO C 43 -1.897 37.327 36.918 1.00 19.69 N ANISOU 3313 N PRO C 43 2036 2397 3050 -93 782 -438 N ATOM 3314 CA PRO C 43 -0.777 37.450 35.974 1.00 17.56 C ANISOU 3314 CA PRO C 43 1827 2095 2751 -86 672 -379 C ATOM 3315 C PRO C 43 -1.262 37.328 34.520 1.00 21.98 C ANISOU 3315 C PRO C 43 2294 2692 3367 -56 586 -351 C ATOM 3316 O PRO C 43 -2.234 36.609 34.240 1.00 19.79 O ANISOU 3316 O PRO C 43 1915 2471 3131 -80 594 -369 O ATOM 3317 CB PRO C 43 0.098 36.232 36.316 1.00 18.24 C ANISOU 3317 CB PRO C 43 1995 2181 2755 -178 674 -353 C ATOM 3318 CG PRO C 43 -0.288 35.864 37.720 1.00 22.26 C ANISOU 3318 CG PRO C 43 2542 2691 3225 -225 781 -396 C ATOM 3319 CD PRO C 43 -1.767 36.087 37.716 1.00 19.96 C ANISOU 3319 CD PRO C 43 2121 2449 3015 -194 848 -443 C ATOM 3320 N THR C 44 -0.612 38.066 33.610 1.00 17.07 N ANISOU 3320 N THR C 44 1711 2031 2742 -9 501 -309 N ATOM 3321 CA THR C 44 -0.904 38.005 32.171 1.00 17.44 C ANISOU 3321 CA THR C 44 1711 2100 2816 18 407 -275 C ATOM 3322 C THR C 44 0.401 37.787 31.415 1.00 19.27 C ANISOU 3322 C THR C 44 2040 2302 2980 -12 354 -218 C ATOM 3323 O THR C 44 1.423 38.380 31.748 1.00 17.19 O ANISOU 3323 O THR C 44 1859 1984 2686 -11 363 -199 O ATOM 3324 CB THR C 44 -1.626 39.255 31.633 1.00 22.89 C ANISOU 3324 CB THR C 44 2351 2768 3578 120 355 -279 C ATOM 3325 OG1 THR C 44 -0.762 40.383 31.756 1.00 26.60 O ANISOU 3325 OG1 THR C 44 2918 3162 4026 159 345 -256 O ATOM 3326 CG2 THR C 44 -2.981 39.516 32.301 1.00 23.51 C ANISOU 3326 CG2 THR C 44 2308 2877 3746 165 411 -342 C ATOM 3327 N PHE C 45 0.350 36.940 30.393 1.00 17.13 N ANISOU 3327 N PHE C 45 1756 2063 2689 -41 302 -194 N ATOM 3328 CA PHE C 45 1.495 36.589 29.569 1.00 16.42 C ANISOU 3328 CA PHE C 45 1749 1953 2536 -69 268 -147 C ATOM 3329 C PHE C 45 2.120 37.800 28.909 1.00 19.68 C ANISOU 3329 C PHE C 45 2223 2311 2943 -18 229 -105 C ATOM 3330 O PHE C 45 1.409 38.623 28.327 1.00 17.89 O ANISOU 3330 O PHE C 45 1973 2074 2750 45 176 -98 O ATOM 3331 CB PHE C 45 1.019 35.602 28.480 1.00 18.17 C ANISOU 3331 CB PHE C 45 1946 2217 2741 -94 213 -139 C ATOM 3332 CG PHE C 45 2.045 35.295 27.413 1.00 18.26 C ANISOU 3332 CG PHE C 45 2046 2208 2686 -111 182 -95 C ATOM 3333 CD1 PHE C 45 3.113 34.446 27.678 1.00 18.45 C ANISOU 3333 CD1 PHE C 45 2122 2223 2666 -163 225 -88 C ATOM 3334 CD2 PHE C 45 1.938 35.853 26.139 1.00 21.78 C ANISOU 3334 CD2 PHE C 45 2525 2639 3111 -70 111 -61 C ATOM 3335 CE1 PHE C 45 4.030 34.116 26.674 1.00 18.68 C ANISOU 3335 CE1 PHE C 45 2222 2235 2641 -174 214 -55 C ATOM 3336 CE2 PHE C 45 2.877 35.550 25.146 1.00 23.63 C ANISOU 3336 CE2 PHE C 45 2849 2854 3274 -90 103 -23 C ATOM 3337 CZ PHE C 45 3.910 34.672 25.422 1.00 19.81 C ANISOU 3337 CZ PHE C 45 2403 2369 2757 -141 162 -24 C ATOM 3338 N LEU C 46 3.453 37.874 28.942 1.00 16.28 N ANISOU 3338 N LEU C 46 1870 1842 2474 -47 249 -76 N ATOM 3339 CA LEU C 46 4.200 38.912 28.246 1.00 16.73 C ANISOU 3339 CA LEU C 46 1992 1843 2519 -21 225 -29 C ATOM 3340 C LEU C 46 5.050 38.339 27.117 1.00 20.47 C ANISOU 3340 C LEU C 46 2520 2319 2938 -55 216 12 C ATOM 3341 O LEU C 46 5.089 38.920 26.035 1.00 20.22 O ANISOU 3341 O LEU C 46 2536 2264 2883 -30 179 52 O ATOM 3342 CB LEU C 46 5.152 39.681 29.182 1.00 17.44 C ANISOU 3342 CB LEU C 46 2126 1878 2623 -32 262 -29 C ATOM 3343 CG LEU C 46 4.596 40.707 30.148 1.00 24.33 C ANISOU 3343 CG LEU C 46 2989 2716 3538 12 272 -62 C ATOM 3344 CD1 LEU C 46 5.768 41.292 30.987 1.00 22.65 C ANISOU 3344 CD1 LEU C 46 2839 2443 3325 -18 296 -59 C ATOM 3345 CD2 LEU C 46 3.871 41.871 29.389 1.00 27.34 C ANISOU 3345 CD2 LEU C 46 3375 3063 3950 89 221 -44 C ATOM 3346 N SER C 47 5.843 37.275 27.402 1.00 16.43 N ANISOU 3346 N SER C 47 2013 1824 2403 -109 255 5 N ATOM 3347 CA SER C 47 6.780 36.743 26.392 1.00 15.60 C ANISOU 3347 CA SER C 47 1959 1716 2253 -136 267 38 C ATOM 3348 C SER C 47 7.153 35.321 26.633 1.00 17.18 C ANISOU 3348 C SER C 47 2148 1946 2435 -178 294 15 C ATOM 3349 O SER C 47 6.997 34.810 27.735 1.00 14.60 O ANISOU 3349 O SER C 47 1788 1630 2129 -198 308 -16 O ATOM 3350 CB SER C 47 8.078 37.566 26.353 1.00 20.07 C ANISOU 3350 CB SER C 47 2567 2229 2829 -147 301 73 C ATOM 3351 OG SER C 47 8.842 37.448 27.553 1.00 20.63 O ANISOU 3351 OG SER C 47 2616 2285 2938 -175 330 53 O ATOM 3352 N TYR C 48 7.637 34.678 25.582 1.00 16.04 N ANISOU 3352 N TYR C 48 2043 1806 2245 -191 302 32 N ATOM 3353 CA TYR C 48 8.159 33.309 25.605 1.00 16.23 C ANISOU 3353 CA TYR C 48 2073 1845 2250 -224 329 13 C ATOM 3354 C TYR C 48 9.439 33.300 24.803 1.00 20.18 C ANISOU 3354 C TYR C 48 2617 2319 2731 -228 376 40 C ATOM 3355 O TYR C 48 9.448 33.821 23.679 1.00 19.51 O ANISOU 3355 O TYR C 48 2584 2226 2604 -216 378 69 O ATOM 3356 CB TYR C 48 7.154 32.296 25.033 1.00 17.28 C ANISOU 3356 CB TYR C 48 2210 2014 2343 -234 291 -10 C ATOM 3357 CG TYR C 48 7.710 30.890 24.883 1.00 18.48 C ANISOU 3357 CG TYR C 48 2389 2166 2467 -263 317 -29 C ATOM 3358 CD1 TYR C 48 7.843 30.047 25.990 1.00 19.01 C ANISOU 3358 CD1 TYR C 48 2431 2232 2561 -290 330 -55 C ATOM 3359 CD2 TYR C 48 8.094 30.397 23.633 1.00 18.94 C ANISOU 3359 CD2 TYR C 48 2512 2219 2467 -261 327 -23 C ATOM 3360 CE1 TYR C 48 8.336 28.744 25.855 1.00 17.42 C ANISOU 3360 CE1 TYR C 48 2261 2019 2337 -309 345 -72 C ATOM 3361 CE2 TYR C 48 8.547 29.081 23.480 1.00 18.95 C ANISOU 3361 CE2 TYR C 48 2543 2212 2444 -280 350 -47 C ATOM 3362 CZ TYR C 48 8.664 28.259 24.592 1.00 23.53 C ANISOU 3362 CZ TYR C 48 3091 2787 3061 -301 355 -71 C ATOM 3363 OH TYR C 48 9.159 26.979 24.457 1.00 22.04 O ANISOU 3363 OH TYR C 48 2941 2580 2856 -311 373 -94 O ATOM 3364 N ASN C 49 10.506 32.712 25.373 1.00 15.32 N ANISOU 3364 N ASN C 49 1983 1690 2147 -246 415 30 N ATOM 3365 CA ASN C 49 11.796 32.568 24.711 1.00 16.15 C ANISOU 3365 CA ASN C 49 2104 1775 2255 -249 476 46 C ATOM 3366 C ASN C 49 12.232 31.150 24.887 1.00 16.74 C ANISOU 3366 C ASN C 49 2174 1854 2333 -255 491 16 C ATOM 3367 O ASN C 49 12.138 30.615 26.000 1.00 13.85 O ANISOU 3367 O ASN C 49 1778 1487 1998 -264 462 -6 O ATOM 3368 CB ASN C 49 12.896 33.514 25.271 1.00 14.44 C ANISOU 3368 CB ASN C 49 1851 1525 2110 -259 504 68 C ATOM 3369 CG ASN C 49 12.748 34.986 24.964 1.00 30.34 C ANISOU 3369 CG ASN C 49 3887 3516 4125 -257 501 104 C ATOM 3370 OD1 ASN C 49 13.504 35.621 24.196 1.00 27.31 O ANISOU 3370 OD1 ASN C 49 3527 3108 3742 -268 552 138 O ATOM 3371 ND2 ASN C 49 11.802 35.567 25.605 1.00 17.96 N ANISOU 3371 ND2 ASN C 49 2313 1948 2561 -243 448 97 N ATOM 3372 N VAL C 50 12.781 30.563 23.829 1.00 13.55 N ANISOU 3372 N VAL C 50 1808 1447 1894 -249 542 14 N ATOM 3373 CA VAL C 50 13.307 29.193 23.937 1.00 13.99 C ANISOU 3373 CA VAL C 50 1863 1494 1957 -243 561 -18 C ATOM 3374 C VAL C 50 14.610 29.062 23.114 1.00 20.67 C ANISOU 3374 C VAL C 50 2712 2322 2821 -228 652 -14 C ATOM 3375 O VAL C 50 15.464 28.246 23.462 1.00 20.62 O ANISOU 3375 O VAL C 50 2671 2298 2867 -213 675 -37 O ATOM 3376 CB VAL C 50 12.251 28.129 23.601 1.00 17.09 C ANISOU 3376 CB VAL C 50 2308 1902 2282 -251 520 -47 C ATOM 3377 CG1 VAL C 50 11.805 28.221 22.138 1.00 16.36 C ANISOU 3377 CG1 VAL C 50 2295 1820 2101 -247 532 -41 C ATOM 3378 CG2 VAL C 50 12.742 26.718 23.993 1.00 15.91 C ANISOU 3378 CG2 VAL C 50 2164 1731 2151 -246 527 -81 C ATOM 3379 N LEU C 51 14.775 29.876 22.060 1.00 19.37 N ANISOU 3379 N LEU C 51 2587 2157 2614 -231 705 14 N ATOM 3380 CA LEU C 51 16.051 29.959 21.343 1.00 20.60 C ANISOU 3380 CA LEU C 51 2735 2297 2796 -226 815 21 C ATOM 3381 C LEU C 51 16.832 31.165 21.898 1.00 24.14 C ANISOU 3381 C LEU C 51 3107 2731 3335 -247 835 55 C ATOM 3382 O LEU C 51 16.235 32.042 22.535 1.00 22.35 O ANISOU 3382 O LEU C 51 2869 2503 3118 -261 767 76 O ATOM 3383 CB LEU C 51 15.858 30.079 19.809 1.00 21.96 C ANISOU 3383 CB LEU C 51 3020 2470 2855 -228 878 34 C ATOM 3384 CG LEU C 51 15.036 28.997 19.081 1.00 27.08 C ANISOU 3384 CG LEU C 51 3766 3126 3397 -216 849 0 C ATOM 3385 CD1 LEU C 51 15.126 29.204 17.569 1.00 29.83 C ANISOU 3385 CD1 LEU C 51 4238 3465 3631 -219 923 14 C ATOM 3386 CD2 LEU C 51 15.523 27.581 19.414 1.00 26.53 C ANISOU 3386 CD2 LEU C 51 3671 3046 3365 -192 868 -52 C ATOM 3387 N ASP C 52 18.138 31.250 21.619 1.00 22.16 N ANISOU 3387 N ASP C 52 2801 2465 3152 -250 930 58 N ATOM 3388 CA ASP C 52 18.961 32.363 22.116 1.00 21.89 C ANISOU 3388 CA ASP C 52 2688 2413 3217 -281 947 88 C ATOM 3389 C ASP C 52 18.703 33.667 21.380 1.00 26.15 C ANISOU 3389 C ASP C 52 3294 2940 3702 -315 981 139 C ATOM 3390 O ASP C 52 18.380 33.660 20.197 1.00 28.18 O ANISOU 3390 O ASP C 52 3652 3200 3856 -315 1037 153 O ATOM 3391 CB ASP C 52 20.459 32.013 21.997 1.00 24.75 C ANISOU 3391 CB ASP C 52 2952 2765 3688 -279 1044 74 C ATOM 3392 CG ASP C 52 20.846 30.794 22.802 1.00 32.82 C ANISOU 3392 CG ASP C 52 3904 3786 4782 -237 997 28 C ATOM 3393 OD1 ASP C 52 20.243 30.576 23.885 1.00 31.82 O ANISOU 3393 OD1 ASP C 52 3774 3657 4658 -231 879 19 O ATOM 3394 OD2 ASP C 52 21.653 29.984 22.297 1.00 44.38 O ANISOU 3394 OD2 ASP C 52 5333 5247 6284 -206 1080 0 O ATOM 3395 N GLY C 53 18.876 34.776 22.079 1.00 25.48 N ANISOU 3395 N GLY C 53 3443 2958 3279 -81 1057 194 N ATOM 3396 CA GLY C 53 18.761 36.083 21.470 1.00 26.41 C ANISOU 3396 CA GLY C 53 3718 3008 3310 -51 1180 303 C ATOM 3397 C GLY C 53 17.706 36.966 22.084 1.00 28.63 C ANISOU 3397 C GLY C 53 3967 3294 3617 -116 968 288 C ATOM 3398 O GLY C 53 17.085 36.620 23.089 1.00 23.14 O ANISOU 3398 O GLY C 53 3101 2655 3037 -200 762 201 O ATOM 3399 N LEU C 54 17.513 38.111 21.451 1.00 28.01 N ANISOU 3399 N LEU C 54 4090 3132 3420 -50 1062 387 N ATOM 3400 CA LEU C 54 16.616 39.150 21.885 1.00 27.64 C ANISOU 3400 CA LEU C 54 4053 3063 3386 -71 912 396 C ATOM 3401 C LEU C 54 15.367 39.219 21.022 1.00 33.13 C ANISOU 3401 C LEU C 54 5011 3760 3817 135 687 344 C ATOM 3402 O LEU C 54 15.458 39.308 19.800 1.00 35.65 O ANISOU 3402 O LEU C 54 5671 4012 3863 331 766 395 O ATOM 3403 CB LEU C 54 17.382 40.477 21.839 1.00 29.09 C ANISOU 3403 CB LEU C 54 4280 3109 3664 -141 1182 543 C ATOM 3404 CG LEU C 54 16.668 41.712 22.384 1.00 32.87 C ANISOU 3404 CG LEU C 54 4782 3526 4182 -171 1074 566 C ATOM 3405 CD1 LEU C 54 16.628 41.689 23.893 1.00 30.03 C ANISOU 3405 CD1 LEU C 54 4118 3221 4071 -340 919 475 C ATOM 3406 CD2 LEU C 54 17.356 42.973 21.891 1.00 37.82 C ANISOU 3406 CD2 LEU C 54 5578 3955 4837 -194 1384 726 C ATOM 3407 N GLU C 55 14.205 39.204 21.674 1.00 27.61 N ANISOU 3407 N GLU C 55 4160 3120 3210 116 409 238 N ATOM 3408 CA GLU C 55 12.903 39.346 21.035 1.00 28.60 C ANISOU 3408 CA GLU C 55 4423 3249 3196 306 118 146 C ATOM 3409 C GLU C 55 12.261 40.645 21.517 1.00 30.02 C ANISOU 3409 C GLU C 55 4581 3390 3436 323 73 199 C ATOM 3410 O GLU C 55 12.114 40.839 22.719 1.00 24.50 O ANISOU 3410 O GLU C 55 3625 2717 2967 166 95 191 O ATOM 3411 CB GLU C 55 12.004 38.138 21.359 1.00 29.81 C ANISOU 3411 CB GLU C 55 4345 3478 3504 266 -149 -49 C ATOM 3412 CG GLU C 55 12.480 36.824 20.757 1.00 44.06 C ANISOU 3412 CG GLU C 55 6231 5290 5219 287 -156 -129 C ATOM 3413 CD GLU C 55 12.118 36.572 19.301 1.00 76.71 C ANISOU 3413 CD GLU C 55 10717 9379 9050 551 -364 -222 C ATOM 3414 OE1 GLU C 55 11.370 37.387 18.709 1.00 67.27 O ANISOU 3414 OE1 GLU C 55 9703 8149 7705 746 -562 -240 O ATOM 3415 OE2 GLU C 55 12.578 35.542 18.755 1.00 76.80 O ANISOU 3415 OE2 GLU C 55 10858 9374 8949 596 -351 -287 O ATOM 3416 N GLU C 56 11.893 41.545 20.593 1.00 31.02 N ANISOU 3416 N GLU C 56 5028 3433 3324 549 19 256 N ATOM 3417 CA GLU C 56 11.291 42.826 20.970 1.00 31.66 C ANISOU 3417 CA GLU C 56 5134 3453 3440 604 -19 313 C ATOM 3418 C GLU C 56 9.786 42.801 20.741 1.00 36.31 C ANISOU 3418 C GLU C 56 5664 4094 4039 808 -412 156 C ATOM 3419 O GLU C 56 9.331 42.308 19.711 1.00 37.41 O ANISOU 3419 O GLU C 56 5980 4242 3993 1023 -664 50 O ATOM 3420 CB GLU C 56 11.942 43.978 20.168 1.00 35.48 C ANISOU 3420 CB GLU C 56 6039 3762 3680 730 229 507 C ATOM 3421 N LYS C 57 9.018 43.350 21.689 1.00 33.07 N ANISOU 3421 N LYS C 57 5007 3703 3857 763 -476 125 N ATOM 3422 CA LYS C 57 7.561 43.435 21.599 1.00 35.84 C ANISOU 3422 CA LYS C 57 5200 4092 4324 950 -819 -30 C ATOM 3423 C LYS C 57 7.111 44.777 22.175 1.00 38.57 C ANISOU 3423 C LYS C 57 5564 4370 4720 1028 -762 53 C ATOM 3424 O LYS C 57 6.900 44.907 23.386 1.00 36.95 O ANISOU 3424 O LYS C 57 5088 4184 4766 873 -632 53 O ATOM 3425 CB LYS C 57 6.884 42.229 22.307 1.00 39.73 C ANISOU 3425 CB LYS C 57 5231 4685 5179 788 -929 -208 C ATOM 3426 CG LYS C 57 5.363 42.208 22.120 1.00 61.82 C ANISOU 3426 CG LYS C 57 7771 7506 8209 966 -1287 -403 C ATOM 3427 CD LYS C 57 4.731 40.863 22.450 1.00 75.45 C ANISOU 3427 CD LYS C 57 9078 9277 10312 808 -1398 -598 C ATOM 3428 CE LYS C 57 3.218 40.949 22.514 1.00 92.88 C ANISOU 3428 CE LYS C 57 10897 11486 12908 933 -1683 -793 C ATOM 3429 NZ LYS C 57 2.597 41.280 21.197 1.00104.54 N ANISOU 3429 NZ LYS C 57 12544 12952 14226 1277 -2180 -950 N ATOM 3430 N GLY C 58 7.012 45.773 21.302 1.00 36.48 N ANISOU 3430 N GLY C 58 5683 4000 4178 1295 -835 133 N ATOM 3431 CA GLY C 58 6.650 47.133 21.691 1.00 36.29 C ANISOU 3431 CA GLY C 58 5768 3870 4150 1410 -777 225 C ATOM 3432 C GLY C 58 7.761 47.746 22.521 1.00 36.58 C ANISOU 3432 C GLY C 58 5872 3804 4224 1146 -385 390 C ATOM 3433 O GLY C 58 8.928 47.696 22.119 1.00 34.62 O ANISOU 3433 O GLY C 58 5832 3481 3842 1025 -153 508 O ATOM 3434 N ARG C 59 7.426 48.245 23.723 1.00 33.09 N ANISOU 3434 N ARG C 59 5225 3349 3997 1053 -312 378 N ATOM 3435 CA ARG C 59 8.423 48.838 24.625 1.00 31.63 C ANISOU 3435 CA ARG C 59 5093 3049 3876 815 -27 479 C ATOM 3436 C ARG C 59 9.188 47.780 25.433 1.00 32.06 C ANISOU 3436 C ARG C 59 4884 3203 4093 525 81 429 C ATOM 3437 O ARG C 59 10.112 48.128 26.176 1.00 29.72 O ANISOU 3437 O ARG C 59 4605 2818 3870 332 248 472 O ATOM 3438 CB ARG C 59 7.760 49.817 25.604 1.00 31.34 C ANISOU 3438 CB ARG C 59 5030 2932 3947 883 -14 468 C ATOM 3439 CG ARG C 59 7.233 51.099 24.970 1.00 40.90 C ANISOU 3439 CG ARG C 59 6563 3984 4992 1164 -72 545 C ATOM 3440 CD ARG C 59 6.686 52.045 26.026 1.00 37.99 C ANISOU 3440 CD ARG C 59 6182 3519 4733 1223 -24 531 C ATOM 3441 NE ARG C 59 5.541 51.472 26.743 1.00 36.21 N ANISOU 3441 NE ARG C 59 5581 3454 4722 1307 -130 396 N ATOM 3442 CZ ARG C 59 5.548 51.103 28.020 1.00 39.74 C ANISOU 3442 CZ ARG C 59 5822 3940 5338 1150 8 343 C ATOM 3443 NH1 ARG C 59 6.643 51.247 28.754 1.00 30.19 N ANISOU 3443 NH1 ARG C 59 4740 2637 4096 917 168 381 N ATOM 3444 NH2 ARG C 59 4.456 50.596 28.575 1.00 33.34 N ANISOU 3444 NH2 ARG C 59 4688 3239 4743 1244 -9 245 N ATOM 3445 N PHE C 60 8.757 46.509 25.365 1.00 27.50 N ANISOU 3445 N PHE C 60 4061 2790 3599 508 -42 319 N ATOM 3446 CA PHE C 60 9.375 45.440 26.147 1.00 24.27 C ANISOU 3446 CA PHE C 60 3438 2460 3322 280 52 276 C ATOM 3447 C PHE C 60 10.216 44.528 25.266 1.00 26.72 C ANISOU 3447 C PHE C 60 3796 2821 3536 215 72 285 C ATOM 3448 O PHE C 60 9.801 44.203 24.160 1.00 28.42 O ANISOU 3448 O PHE C 60 4105 3070 3624 368 -71 252 O ATOM 3449 CB PHE C 60 8.300 44.617 26.897 1.00 25.84 C ANISOU 3449 CB PHE C 60 3332 2756 3729 285 -18 157 C ATOM 3450 CG PHE C 60 7.507 45.340 27.979 1.00 28.73 C ANISOU 3450 CG PHE C 60 3630 3069 4215 351 50 150 C ATOM 3451 CD1 PHE C 60 7.655 46.719 28.186 1.00 31.52 C ANISOU 3451 CD1 PHE C 60 4208 3298 4470 428 99 225 C ATOM 3452 CD2 PHE C 60 6.624 44.645 28.798 1.00 30.84 C ANISOU 3452 CD2 PHE C 60 3635 3379 4704 343 111 76 C ATOM 3453 CE1 PHE C 60 6.912 47.382 29.173 1.00 33.57 C ANISOU 3453 CE1 PHE C 60 4445 3495 4814 524 173 211 C ATOM 3454 CE2 PHE C 60 5.878 45.311 29.781 1.00 33.61 C ANISOU 3454 CE2 PHE C 60 3953 3664 5153 440 238 81 C ATOM 3455 CZ PHE C 60 6.023 46.670 29.959 1.00 32.75 C ANISOU 3455 CZ PHE C 60 4085 3451 4908 543 253 143 C ATOM 3456 N SER C 61 11.376 44.096 25.771 1.00 19.38 N ANISOU 3456 N SER C 61 2809 1889 2666 19 224 312 N ATOM 3457 CA SER C 61 12.258 43.142 25.088 1.00 18.99 C ANISOU 3457 CA SER C 61 2767 1886 2561 -43 287 318 C ATOM 3458 C SER C 61 12.567 42.001 26.023 1.00 19.74 C ANISOU 3458 C SER C 61 2636 2063 2801 -184 292 243 C ATOM 3459 O SER C 61 12.785 42.232 27.211 1.00 19.29 O ANISOU 3459 O SER C 61 2500 1978 2852 -273 328 234 O ATOM 3460 CB SER C 61 13.573 43.803 24.655 1.00 22.23 C ANISOU 3460 CB SER C 61 3330 2177 2940 -119 514 440 C ATOM 3461 OG SER C 61 13.342 44.741 23.629 1.00 35.27 O ANISOU 3461 OG SER C 61 5279 3715 4407 41 567 539 O ATOM 3462 N SER C 62 12.670 40.788 25.486 1.00 15.10 N ANISOU 3462 N SER C 62 2003 1550 2184 -181 256 190 N ATOM 3463 CA SER C 62 13.013 39.622 26.287 1.00 14.75 C ANISOU 3463 CA SER C 62 1797 1555 2251 -289 278 132 C ATOM 3464 C SER C 62 14.222 38.967 25.684 1.00 17.65 C ANISOU 3464 C SER C 62 2202 1937 2568 -321 377 157 C ATOM 3465 O SER C 62 14.231 38.678 24.488 1.00 17.92 O ANISOU 3465 O SER C 62 2369 1979 2463 -227 373 158 O ATOM 3466 CB SER C 62 11.839 38.635 26.331 1.00 19.52 C ANISOU 3466 CB SER C 62 2279 2201 2938 -260 157 24 C ATOM 3467 OG SER C 62 10.819 39.190 27.136 1.00 37.17 O ANISOU 3467 OG SER C 62 4419 4412 5292 -241 143 10 O ATOM 3468 N PHE C 63 15.244 38.734 26.497 1.00 14.74 N ANISOU 3468 N PHE C 63 1735 1562 2304 -419 454 165 N ATOM 3469 CA PHE C 63 16.472 38.114 26.032 1.00 14.42 C ANISOU 3469 CA PHE C 63 1666 1533 2281 -438 567 181 C ATOM 3470 C PHE C 63 16.664 36.746 26.669 1.00 17.83 C ANISOU 3470 C PHE C 63 2005 2011 2757 -448 515 108 C ATOM 3471 O PHE C 63 16.402 36.594 27.845 1.00 15.69 O ANISOU 3471 O PHE C 63 1687 1731 2546 -473 444 74 O ATOM 3472 CB PHE C 63 17.668 39.002 26.383 1.00 16.87 C ANISOU 3472 CB PHE C 63 1890 1771 2750 -530 676 229 C ATOM 3473 CG PHE C 63 19.036 38.396 26.120 1.00 19.71 C ANISOU 3473 CG PHE C 63 2118 2134 3236 -555 808 230 C ATOM 3474 CD1 PHE C 63 19.602 38.437 24.848 1.00 24.01 C ANISOU 3474 CD1 PHE C 63 2741 2643 3737 -512 1049 313 C ATOM 3475 CD2 PHE C 63 19.736 37.742 27.137 1.00 20.91 C ANISOU 3475 CD2 PHE C 63 2095 2314 3536 -581 701 148 C ATOM 3476 CE1 PHE C 63 20.859 37.856 24.603 1.00 26.59 C ANISOU 3476 CE1 PHE C 63 2911 2968 4223 -517 1220 315 C ATOM 3477 CE2 PHE C 63 20.977 37.141 26.880 1.00 23.95 C ANISOU 3477 CE2 PHE C 63 2316 2708 4075 -573 804 133 C ATOM 3478 CZ PHE C 63 21.534 37.218 25.618 1.00 24.12 C ANISOU 3478 CZ PHE C 63 2357 2700 4108 -553 1082 218 C ATOM 3479 N LEU C 64 17.241 35.801 25.942 1.00 14.05 N ANISOU 3479 N LEU C 64 1545 1558 2236 -404 581 96 N ATOM 3480 CA LEU C 64 17.594 34.516 26.540 1.00 13.29 C ANISOU 3480 CA LEU C 64 1389 1478 2182 -394 551 37 C ATOM 3481 C LEU C 64 18.993 34.073 26.117 1.00 19.94 C ANISOU 3481 C LEU C 64 2166 2331 3078 -355 676 52 C ATOM 3482 O LEU C 64 19.365 34.193 24.933 1.00 19.88 O ANISOU 3482 O LEU C 64 2234 2318 3001 -304 827 96 O ATOM 3483 CB LEU C 64 16.572 33.438 26.126 1.00 12.82 C ANISOU 3483 CB LEU C 64 1416 1412 2044 -359 479 -34 C ATOM 3484 CG LEU C 64 16.857 31.986 26.596 1.00 16.75 C ANISOU 3484 CG LEU C 64 1916 1880 2570 -340 482 -85 C ATOM 3485 CD1 LEU C 64 16.717 31.835 28.163 1.00 15.89 C ANISOU 3485 CD1 LEU C 64 1777 1725 2536 -366 464 -75 C ATOM 3486 CD2 LEU C 64 15.938 30.992 25.876 1.00 14.32 C ANISOU 3486 CD2 LEU C 64 1691 1523 2226 -328 416 -177 C ATOM 3487 N SER C 65 19.738 33.511 27.081 1.00 17.77 N ANISOU 3487 N SER C 65 1778 2058 2916 -343 620 13 N ATOM 3488 CA SER C 65 20.997 32.783 26.864 1.00 18.40 C ANISOU 3488 CA SER C 65 1749 2151 3090 -269 701 -4 C ATOM 3489 C SER C 65 20.851 31.399 27.498 1.00 20.64 C ANISOU 3489 C SER C 65 2113 2422 3306 -182 602 -62 C ATOM 3490 O SER C 65 20.890 31.277 28.723 1.00 18.97 O ANISOU 3490 O SER C 65 1901 2184 3122 -156 462 -92 O ATOM 3491 CB SER C 65 22.217 33.518 27.412 1.00 21.91 C ANISOU 3491 CB SER C 65 1943 2583 3798 -305 688 -19 C ATOM 3492 OG SER C 65 23.319 32.626 27.324 1.00 25.02 O ANISOU 3492 OG SER C 65 2196 2994 4316 -200 732 -58 O ATOM 3493 N ARG C 66 20.671 30.356 26.678 1.00 18.79 N ANISOU 3493 N ARG C 66 2003 2176 2959 -114 677 -80 N ATOM 3494 CA ARG C 66 20.512 29.001 27.229 1.00 19.51 C ANISOU 3494 CA ARG C 66 2205 2208 2998 -39 618 -128 C ATOM 3495 C ARG C 66 21.787 28.500 27.926 1.00 23.30 C ANISOU 3495 C ARG C 66 2581 2691 3579 94 578 -148 C ATOM 3496 O ARG C 66 21.691 27.926 29.008 1.00 22.55 O ANISOU 3496 O ARG C 66 2585 2535 3449 164 468 -165 O ATOM 3497 CB ARG C 66 20.091 28.000 26.138 1.00 21.25 C ANISOU 3497 CB ARG C 66 2594 2384 3097 5 681 -172 C ATOM 3498 CG ARG C 66 18.616 28.132 25.742 1.00 19.76 C ANISOU 3498 CG ARG C 66 2507 2153 2848 -99 606 -211 C ATOM 3499 CD ARG C 66 18.350 27.338 24.484 1.00 22.18 C ANISOU 3499 CD ARG C 66 2986 2407 3032 -33 601 -295 C ATOM 3500 NE ARG C 66 19.073 27.907 23.345 1.00 25.08 N ANISOU 3500 NE ARG C 66 3414 2838 3278 72 718 -255 N ATOM 3501 CZ ARG C 66 19.016 27.454 22.104 1.00 33.76 C ANISOU 3501 CZ ARG C 66 4742 3895 4192 194 736 -315 C ATOM 3502 NH1 ARG C 66 18.247 26.415 21.805 1.00 26.38 N ANISOU 3502 NH1 ARG C 66 3962 2855 3206 204 579 -454 N ATOM 3503 NH2 ARG C 66 19.744 28.023 21.151 1.00 26.17 N ANISOU 3503 NH2 ARG C 66 3882 2963 3099 317 928 -243 N ATOM 3504 N SER C 67 22.964 28.755 27.345 1.00 20.79 N ANISOU 3504 N SER C 67 2071 2427 3400 149 675 -146 N ATOM 3505 CA SER C 67 24.237 28.278 27.917 1.00 23.16 C ANISOU 3505 CA SER C 67 2197 2735 3867 301 604 -196 C ATOM 3506 C SER C 67 24.541 28.921 29.282 1.00 26.81 C ANISOU 3506 C SER C 67 2545 3193 4448 306 345 -245 C ATOM 3507 O SER C 67 25.176 28.283 30.119 1.00 26.79 O ANISOU 3507 O SER C 67 2537 3165 4477 483 164 -310 O ATOM 3508 CB SER C 67 25.401 28.504 26.952 1.00 26.97 C ANISOU 3508 CB SER C 67 2429 3259 4559 344 821 -185 C ATOM 3509 OG SER C 67 25.544 29.886 26.665 1.00 35.96 O ANISOU 3509 OG SER C 67 3385 4414 5865 185 915 -143 O ATOM 3510 N LYS C 68 24.033 30.138 29.528 1.00 22.40 N ANISOU 3510 N LYS C 68 1955 2640 3916 148 300 -226 N ATOM 3511 CA LYS C 68 24.233 30.833 30.803 1.00 22.44 C ANISOU 3511 CA LYS C 68 1919 2615 3992 164 32 -293 C ATOM 3512 C LYS C 68 23.073 30.595 31.772 1.00 25.58 C ANISOU 3512 C LYS C 68 2662 2945 4111 198 -55 -267 C ATOM 3513 O LYS C 68 23.184 30.990 32.930 1.00 26.55 O ANISOU 3513 O LYS C 68 2870 3018 4201 280 -280 -324 O ATOM 3514 CB LYS C 68 24.414 32.352 30.570 1.00 23.23 C ANISOU 3514 CB LYS C 68 1805 2718 4301 -18 52 -295 C ATOM 3515 CG LYS C 68 25.807 32.679 30.004 1.00 31.08 C ANISOU 3515 CG LYS C 68 2400 3724 5686 -42 131 -343 C ATOM 3516 CD LYS C 68 25.875 34.093 29.446 1.00 40.10 C ANISOU 3516 CD LYS C 68 3379 4821 7036 -254 292 -299 C ATOM 3517 CE LYS C 68 27.173 34.315 28.703 1.00 53.92 C ANISOU 3517 CE LYS C 68 4733 6545 9211 -297 513 -309 C ATOM 3518 NZ LYS C 68 27.155 35.592 27.954 1.00 62.79 N ANISOU 3518 NZ LYS C 68 5779 7578 10498 -501 794 -217 N ATOM 3519 N GLY C 69 21.963 30.009 31.296 1.00 19.68 N ANISOU 3519 N GLY C 69 2111 2176 3192 140 126 -192 N ATOM 3520 CA GLY C 69 20.760 29.820 32.114 1.00 17.42 C ANISOU 3520 CA GLY C 69 2098 1799 2724 138 146 -150 C ATOM 3521 C GLY C 69 20.311 31.193 32.579 1.00 20.54 C ANISOU 3521 C GLY C 69 2472 2200 3133 47 84 -145 C ATOM 3522 O GLY C 69 20.157 31.450 33.785 1.00 19.35 O ANISOU 3522 O GLY C 69 2503 1973 2875 145 -28 -160 O ATOM 3523 N TYR C 70 20.216 32.128 31.613 1.00 16.47 N ANISOU 3523 N TYR C 70 1772 1757 2729 -106 154 -128 N ATOM 3524 CA TYR C 70 19.951 33.520 31.942 1.00 16.94 C ANISOU 3524 CA TYR C 70 1801 1808 2828 -188 94 -128 C ATOM 3525 C TYR C 70 18.987 34.201 30.969 1.00 19.70 C ANISOU 3525 C TYR C 70 2128 2188 3168 -320 239 -65 C ATOM 3526 O TYR C 70 19.103 34.060 29.745 1.00 19.42 O ANISOU 3526 O TYR C 70 2019 2202 3159 -362 349 -39 O ATOM 3527 CB TYR C 70 21.309 34.269 31.938 1.00 20.25 C ANISOU 3527 CB TYR C 70 1983 2239 3471 -207 -36 -200 C ATOM 3528 CG TYR C 70 21.226 35.780 31.961 1.00 22.61 C ANISOU 3528 CG TYR C 70 2214 2500 3877 -332 -66 -205 C ATOM 3529 CD1 TYR C 70 20.760 36.454 33.085 1.00 23.74 C ANISOU 3529 CD1 TYR C 70 2529 2567 3924 -292 -224 -248 C ATOM 3530 CD2 TYR C 70 21.678 36.540 30.882 1.00 24.46 C ANISOU 3530 CD2 TYR C 70 2254 2740 4301 -467 88 -164 C ATOM 3531 CE1 TYR C 70 20.712 37.847 33.127 1.00 24.44 C ANISOU 3531 CE1 TYR C 70 2581 2592 4115 -398 -262 -266 C ATOM 3532 CE2 TYR C 70 21.682 37.938 30.932 1.00 26.07 C ANISOU 3532 CE2 TYR C 70 2416 2863 4627 -583 76 -167 C ATOM 3533 CZ TYR C 70 21.175 38.584 32.048 1.00 30.38 C ANISOU 3533 CZ TYR C 70 3120 3339 5084 -555 -117 -225 C ATOM 3534 OH TYR C 70 21.107 39.948 32.093 1.00 31.84 O ANISOU 3534 OH TYR C 70 3304 3421 5374 -661 -130 -234 O ATOM 3535 N SER C 71 18.101 35.008 31.521 1.00 15.11 N ANISOU 3535 N SER C 71 1640 1567 2536 -346 226 -48 N ATOM 3536 CA SER C 71 17.191 35.830 30.727 1.00 14.41 C ANISOU 3536 CA SER C 71 1533 1496 2444 -426 306 -2 C ATOM 3537 C SER C 71 17.056 37.208 31.328 1.00 17.54 C ANISOU 3537 C SER C 71 1965 1840 2860 -447 247 -1 C ATOM 3538 O SER C 71 17.188 37.364 32.546 1.00 15.98 O ANISOU 3538 O SER C 71 1872 1578 2621 -381 150 -42 O ATOM 3539 CB SER C 71 15.798 35.183 30.670 1.00 17.09 C ANISOU 3539 CB SER C 71 1936 1823 2733 -419 382 10 C ATOM 3540 OG SER C 71 14.815 36.006 30.043 1.00 20.04 O ANISOU 3540 OG SER C 71 2282 2212 3122 -450 396 27 O ATOM 3541 N TYR C 72 16.670 38.189 30.505 1.00 13.19 N ANISOU 3541 N TYR C 72 1392 1292 2329 -503 300 43 N ATOM 3542 CA TYR C 72 16.260 39.470 31.054 1.00 13.25 C ANISOU 3542 CA TYR C 72 1475 1224 2335 -506 262 47 C ATOM 3543 C TYR C 72 15.016 39.935 30.347 1.00 16.62 C ANISOU 3543 C TYR C 72 1940 1667 2707 -482 328 98 C ATOM 3544 O TYR C 72 14.750 39.598 29.180 1.00 14.59 O ANISOU 3544 O TYR C 72 1655 1466 2422 -475 365 123 O ATOM 3545 CB TYR C 72 17.336 40.581 31.075 1.00 14.73 C ANISOU 3545 CB TYR C 72 1610 1327 2659 -587 212 27 C ATOM 3546 CG TYR C 72 17.871 41.060 29.735 1.00 16.11 C ANISOU 3546 CG TYR C 72 1706 1488 2927 -669 358 99 C ATOM 3547 CD1 TYR C 72 17.134 41.937 28.937 1.00 17.79 C ANISOU 3547 CD1 TYR C 72 2038 1662 3059 -655 454 182 C ATOM 3548 CD2 TYR C 72 19.162 40.733 29.322 1.00 17.69 C ANISOU 3548 CD2 TYR C 72 1734 1684 3302 -733 422 87 C ATOM 3549 CE1 TYR C 72 17.631 42.398 27.710 1.00 18.95 C ANISOU 3549 CE1 TYR C 72 2212 1754 3234 -687 638 274 C ATOM 3550 CE2 TYR C 72 19.688 41.227 28.122 1.00 19.27 C ANISOU 3550 CE2 TYR C 72 1904 1829 3589 -794 649 179 C ATOM 3551 CZ TYR C 72 18.911 42.044 27.313 1.00 24.17 C ANISOU 3551 CZ TYR C 72 2722 2396 4065 -763 769 282 C ATOM 3552 OH TYR C 72 19.411 42.484 26.113 1.00 28.40 O ANISOU 3552 OH TYR C 72 3323 2845 4623 -778 1039 397 O ATOM 3553 N LEU C 73 14.240 40.692 31.079 1.00 14.96 N ANISOU 3553 N LEU C 73 1814 1397 2471 -434 318 97 N ATOM 3554 CA LEU C 73 13.098 41.405 30.551 1.00 14.40 C ANISOU 3554 CA LEU C 73 1764 1324 2385 -377 344 130 C ATOM 3555 C LEU C 73 13.502 42.868 30.608 1.00 17.54 C ANISOU 3555 C LEU C 73 2268 1616 2782 -391 325 155 C ATOM 3556 O LEU C 73 13.865 43.368 31.685 1.00 17.86 O ANISOU 3556 O LEU C 73 2391 1565 2828 -394 280 114 O ATOM 3557 CB LEU C 73 11.804 41.112 31.354 1.00 13.69 C ANISOU 3557 CB LEU C 73 1661 1224 2316 -294 405 111 C ATOM 3558 CG LEU C 73 10.557 41.925 30.930 1.00 18.70 C ANISOU 3558 CG LEU C 73 2261 1850 2993 -201 405 122 C ATOM 3559 CD1 LEU C 73 10.050 41.518 29.515 1.00 20.19 C ANISOU 3559 CD1 LEU C 73 2333 2121 3217 -179 308 99 C ATOM 3560 CD2 LEU C 73 9.422 41.738 31.942 1.00 18.54 C ANISOU 3560 CD2 LEU C 73 2196 1787 3060 -121 541 108 C ATOM 3561 N LEU C 74 13.492 43.537 29.467 1.00 15.64 N ANISOU 3561 N LEU C 74 2068 1354 2520 -385 355 216 N ATOM 3562 CA LEU C 74 13.873 44.945 29.383 1.00 17.29 C ANISOU 3562 CA LEU C 74 2404 1415 2750 -411 384 259 C ATOM 3563 C LEU C 74 12.629 45.807 29.154 1.00 23.43 C ANISOU 3563 C LEU C 74 3303 2156 3444 -260 370 294 C ATOM 3564 O LEU C 74 11.911 45.615 28.163 1.00 24.10 O ANISOU 3564 O LEU C 74 3399 2306 3450 -148 345 323 O ATOM 3565 CB LEU C 74 14.912 45.143 28.252 1.00 18.14 C ANISOU 3565 CB LEU C 74 2526 1469 2898 -496 507 335 C ATOM 3566 CG LEU C 74 15.537 46.541 28.074 1.00 26.44 C ANISOU 3566 CG LEU C 74 3694 2306 4044 -574 613 394 C ATOM 3567 CD1 LEU C 74 16.474 46.875 29.241 1.00 27.98 C ANISOU 3567 CD1 LEU C 74 3778 2393 4459 -726 527 287 C ATOM 3568 CD2 LEU C 74 16.336 46.610 26.773 1.00 28.53 C ANISOU 3568 CD2 LEU C 74 4009 2503 4328 -617 844 509 C ATOM 3569 N LEU C 75 12.390 46.766 30.057 1.00 19.57 N ANISOU 3569 N LEU C 75 2920 1548 2968 -229 354 272 N ATOM 3570 CA LEU C 75 11.274 47.692 29.919 1.00 20.65 C ANISOU 3570 CA LEU C 75 3174 1628 3043 -60 349 303 C ATOM 3571 C LEU C 75 11.840 49.043 29.537 1.00 23.45 C ANISOU 3571 C LEU C 75 3740 1780 3391 -90 398 367 C ATOM 3572 O LEU C 75 12.576 49.651 30.313 1.00 24.43 O ANISOU 3572 O LEU C 75 3932 1754 3596 -202 395 324 O ATOM 3573 CB LEU C 75 10.386 47.787 31.188 1.00 21.23 C ANISOU 3573 CB LEU C 75 3252 1692 3124 50 354 242 C ATOM 3574 CG LEU C 75 10.058 46.506 31.995 1.00 26.78 C ANISOU 3574 CG LEU C 75 3803 2508 3864 45 396 189 C ATOM 3575 CD1 LEU C 75 9.169 46.847 33.183 1.00 28.66 C ANISOU 3575 CD1 LEU C 75 4128 2677 4086 193 496 164 C ATOM 3576 CD2 LEU C 75 9.344 45.465 31.157 1.00 28.28 C ANISOU 3576 CD2 LEU C 75 3768 2849 4128 64 388 187 C ATOM 3577 N LYS C 76 11.557 49.482 28.320 1.00 25.37 N ANISOU 3577 N LYS C 76 3211 2395 4034 237 804 891 N ATOM 3578 CA LYS C 76 12.056 50.751 27.795 1.00 27.37 C ANISOU 3578 CA LYS C 76 3593 2506 4302 226 894 1029 C ATOM 3579 C LYS C 76 11.013 51.855 27.931 1.00 30.36 C ANISOU 3579 C LYS C 76 4130 2879 4528 287 664 955 C ATOM 3580 O LYS C 76 9.819 51.564 28.036 1.00 28.11 O ANISOU 3580 O LYS C 76 3881 2696 4105 377 485 798 O ATOM 3581 CB LYS C 76 12.480 50.601 26.326 1.00 32.55 C ANISOU 3581 CB LYS C 76 4490 3066 4812 304 1192 1123 C ATOM 3582 CG LYS C 76 13.740 49.778 26.134 1.00 50.45 C ANISOU 3582 CG LYS C 76 6583 5274 7313 252 1516 1236 C ATOM 3583 CD LYS C 76 13.588 48.791 24.985 1.00 68.92 C ANISOU 3583 CD LYS C 76 9179 7603 9407 371 1743 1197 C ATOM 3584 CE LYS C 76 14.347 49.211 23.750 1.00 86.62 C ANISOU 3584 CE LYS C 76 11695 9645 11572 401 2153 1348 C ATOM 3585 NZ LYS C 76 14.199 48.221 22.648 1.00 95.71 N ANISOU 3585 NZ LYS C 76 13189 10746 12432 519 2383 1299 N ATOM 3586 N GLU C 77 11.475 53.122 27.949 1.00 30.12 N ANISOU 3586 N GLU C 77 4172 2708 4563 235 672 1070 N ATOM 3587 CA GLU C 77 10.648 54.332 28.057 1.00 30.55 C ANISOU 3587 CA GLU C 77 4396 2707 4505 301 479 1025 C ATOM 3588 C GLU C 77 9.565 54.115 29.135 1.00 31.59 C ANISOU 3588 C GLU C 77 4407 2955 4642 336 253 838 C ATOM 3589 O GLU C 77 8.368 54.167 28.836 1.00 31.69 O ANISOU 3589 O GLU C 77 4500 3017 4524 480 120 716 O ATOM 3590 CB GLU C 77 10.036 54.652 26.679 1.00 34.18 C ANISOU 3590 CB GLU C 77 5187 3111 4691 458 488 1033 C ATOM 3591 CG GLU C 77 11.034 55.167 25.650 1.00 52.98 C ANISOU 3591 CG GLU C 77 7792 5315 7023 419 757 1226 C ATOM 3592 CD GLU C 77 11.303 56.660 25.705 1.00 87.13 C ANISOU 3592 CD GLU C 77 12257 9465 11383 373 728 1335 C ATOM 3593 OE1 GLU C 77 10.335 57.446 25.575 1.00 89.67 O ANISOU 3593 OE1 GLU C 77 12780 9745 11546 495 496 1270 O ATOM 3594 OE2 GLU C 77 12.486 57.043 25.854 1.00 83.01 O ANISOU 3594 OE2 GLU C 77 11634 8828 11077 215 931 1491 O ATOM 3595 N LEU C 78 10.009 53.784 30.371 1.00 27.16 N ANISOU 3595 N LEU C 78 3657 2415 4250 200 218 819 N ATOM 3596 CA LEU C 78 9.166 53.434 31.523 1.00 25.97 C ANISOU 3596 CA LEU C 78 3428 2340 4100 195 91 654 C ATOM 3597 C LEU C 78 7.986 54.355 31.718 1.00 30.53 C ANISOU 3597 C LEU C 78 4117 2884 4601 317 -19 541 C ATOM 3598 O LEU C 78 8.137 55.584 31.766 1.00 30.59 O ANISOU 3598 O LEU C 78 4263 2749 4608 322 -66 600 O ATOM 3599 CB LEU C 78 9.960 53.412 32.836 1.00 25.52 C ANISOU 3599 CB LEU C 78 3300 2208 4188 15 28 689 C ATOM 3600 CG LEU C 78 10.606 52.144 33.279 1.00 30.73 C ANISOU 3600 CG LEU C 78 3798 2927 4952 -86 50 706 C ATOM 3601 CD1 LEU C 78 11.270 52.370 34.634 1.00 31.89 C ANISOU 3601 CD1 LEU C 78 3961 2941 5215 -260 -114 740 C ATOM 3602 CD2 LEU C 78 9.591 50.950 33.381 1.00 31.73 C ANISOU 3602 CD2 LEU C 78 3876 3215 4966 -13 79 539 C ATOM 3603 N GLN C 79 6.811 53.753 31.859 1.00 26.07 N ANISOU 3603 N GLN C 79 3471 2427 4005 414 -51 377 N ATOM 3604 CA GLN C 79 5.590 54.516 32.103 1.00 26.64 C ANISOU 3604 CA GLN C 79 3574 2458 4090 552 -129 255 C ATOM 3605 C GLN C 79 5.105 54.172 33.490 1.00 29.01 C ANISOU 3605 C GLN C 79 3801 2769 4453 489 -67 119 C ATOM 3606 O GLN C 79 5.427 53.092 33.981 1.00 25.47 O ANISOU 3606 O GLN C 79 3270 2399 4007 371 -7 99 O ATOM 3607 CB GLN C 79 4.531 54.198 31.038 1.00 28.96 C ANISOU 3607 CB GLN C 79 3817 2825 4361 726 -226 182 C ATOM 3608 CG GLN C 79 4.805 54.861 29.678 1.00 37.11 C ANISOU 3608 CG GLN C 79 5060 3772 5266 820 -311 307 C ATOM 3609 CD GLN C 79 3.798 54.450 28.626 1.00 48.85 C ANISOU 3609 CD GLN C 79 6560 5297 6705 976 -487 239 C ATOM 3610 OE1 GLN C 79 2.657 54.077 28.919 1.00 43.82 O ANISOU 3610 OE1 GLN C 79 5724 4718 6207 1053 -589 91 O ATOM 3611 NE2 GLN C 79 4.200 54.494 27.370 1.00 43.70 N ANISOU 3611 NE2 GLN C 79 6159 4582 5863 1015 -527 349 N ATOM 3612 N MET C 80 4.327 55.061 34.128 1.00 27.09 N ANISOU 3612 N MET C 80 3621 2420 4251 571 -57 25 N ATOM 3613 CA MET C 80 3.788 54.791 35.466 1.00 27.25 C ANISOU 3613 CA MET C 80 3646 2406 4302 518 75 -114 C ATOM 3614 C MET C 80 2.989 53.473 35.489 1.00 27.97 C ANISOU 3614 C MET C 80 3511 2651 4466 524 162 -234 C ATOM 3615 O MET C 80 3.073 52.720 36.452 1.00 26.34 O ANISOU 3615 O MET C 80 3333 2450 4226 394 280 -289 O ATOM 3616 CB MET C 80 2.897 55.954 35.951 1.00 31.82 C ANISOU 3616 CB MET C 80 4319 2830 4942 658 134 -212 C ATOM 3617 CG MET C 80 3.634 57.300 36.078 1.00 36.46 C ANISOU 3617 CG MET C 80 5180 3227 5447 635 48 -108 C ATOM 3618 SD MET C 80 5.152 57.280 37.084 1.00 39.26 S ANISOU 3618 SD MET C 80 5784 3464 5671 350 -9 6 S ATOM 3619 CE MET C 80 4.492 56.911 38.678 1.00 35.86 C ANISOU 3619 CE MET C 80 5525 2934 5167 294 177 -171 C ATOM 3620 N LYS C 81 2.259 53.176 34.409 1.00 25.41 N ANISOU 3620 N LYS C 81 2998 2426 4229 660 75 -264 N ATOM 3621 CA LYS C 81 1.451 51.961 34.292 1.00 25.71 C ANISOU 3621 CA LYS C 81 2806 2592 4369 659 113 -374 C ATOM 3622 C LYS C 81 2.320 50.673 34.269 1.00 27.26 C ANISOU 3622 C LYS C 81 3013 2897 4448 494 134 -317 C ATOM 3623 O LYS C 81 1.768 49.575 34.377 1.00 27.17 O ANISOU 3623 O LYS C 81 2854 2972 4497 451 188 -407 O ATOM 3624 CB LYS C 81 0.547 52.038 33.045 1.00 30.51 C ANISOU 3624 CB LYS C 81 3257 3239 5097 835 -84 -403 C ATOM 3625 CG LYS C 81 1.308 51.931 31.714 1.00 40.38 C ANISOU 3625 CG LYS C 81 4650 4523 6168 851 -266 -265 C ATOM 3626 CD LYS C 81 0.377 52.087 30.524 1.00 54.36 C ANISOU 3626 CD LYS C 81 6367 6277 8011 1024 -525 -294 C ATOM 3627 CE LYS C 81 0.840 51.252 29.356 1.00 66.80 C ANISOU 3627 CE LYS C 81 8079 7908 9394 994 -646 -223 C ATOM 3628 NZ LYS C 81 0.050 51.538 28.130 1.00 78.22 N ANISOU 3628 NZ LYS C 81 9597 9280 10841 1156 -969 -228 N ATOM 3629 N ASP C 82 3.668 50.801 34.149 1.00 23.17 N ANISOU 3629 N ASP C 82 2649 2353 3803 403 99 -166 N ATOM 3630 CA ASP C 82 4.561 49.638 34.144 1.00 21.56 C ANISOU 3630 CA ASP C 82 2433 2220 3541 273 125 -101 C ATOM 3631 C ASP C 82 4.819 49.122 35.582 1.00 23.67 C ANISOU 3631 C ASP C 82 2765 2438 3792 116 212 -142 C ATOM 3632 O ASP C 82 5.367 48.022 35.736 1.00 21.92 O ANISOU 3632 O ASP C 82 2520 2262 3547 17 222 -114 O ATOM 3633 CB ASP C 82 5.881 49.943 33.422 1.00 22.30 C ANISOU 3633 CB ASP C 82 2608 2278 3589 247 83 80 C ATOM 3634 CG ASP C 82 5.707 50.263 31.939 1.00 30.35 C ANISOU 3634 CG ASP C 82 3666 3316 4551 385 29 130 C ATOM 3635 OD1 ASP C 82 4.702 49.790 31.335 1.00 29.86 O ANISOU 3635 OD1 ASP C 82 3545 3324 4478 481 -37 29 O ATOM 3636 OD2 ASP C 82 6.564 50.989 31.384 1.00 29.02 O ANISOU 3636 OD2 ASP C 82 3610 3066 4351 386 40 272 O ATOM 3637 N SER C 83 4.453 49.912 36.623 1.00 20.49 N ANISOU 3637 N SER C 83 2495 1911 3379 97 271 -205 N ATOM 3638 CA SER C 83 4.570 49.464 38.025 1.00 20.73 C ANISOU 3638 CA SER C 83 2699 1847 3331 -51 357 -256 C ATOM 3639 C SER C 83 3.710 48.227 38.200 1.00 22.88 C ANISOU 3639 C SER C 83 2844 2213 3635 -75 500 -379 C ATOM 3640 O SER C 83 2.489 48.264 38.003 1.00 23.39 O ANISOU 3640 O SER C 83 2748 2320 3818 23 621 -503 O ATOM 3641 CB SER C 83 4.144 50.545 39.019 1.00 22.79 C ANISOU 3641 CB SER C 83 3192 1927 3541 -44 447 -326 C ATOM 3642 OG SER C 83 5.054 51.631 38.973 1.00 33.51 O ANISOU 3642 OG SER C 83 4705 3168 4861 -64 284 -204 O ATOM 3643 N ALA C 84 4.357 47.125 38.508 1.00 18.59 N ANISOU 3643 N ALA C 84 2347 1691 3027 -203 470 -337 N ATOM 3644 CA ALA C 84 3.716 45.800 38.625 1.00 18.47 C ANISOU 3644 CA ALA C 84 2236 1753 3028 -256 588 -432 C ATOM 3645 C ALA C 84 4.747 44.823 39.091 1.00 20.70 C ANISOU 3645 C ALA C 84 2651 1999 3215 -394 502 -347 C ATOM 3646 O ALA C 84 5.916 45.177 39.192 1.00 20.42 O ANISOU 3646 O ALA C 84 2710 1890 3158 -433 335 -214 O ATOM 3647 CB ALA C 84 3.197 45.357 37.240 1.00 18.59 C ANISOU 3647 CB ALA C 84 1969 1935 3159 -142 537 -454 C ATOM 3648 N SER C 85 4.337 43.579 39.295 1.00 17.48 N ANISOU 3648 N SER C 85 2220 1631 2792 -465 595 -415 N ATOM 3649 CA SER C 85 5.253 42.507 39.582 1.00 17.45 C ANISOU 3649 CA SER C 85 2315 1593 2724 -568 494 -336 C ATOM 3650 C SER C 85 5.514 41.743 38.259 1.00 20.26 C ANISOU 3650 C SER C 85 2432 2099 3168 -486 435 -295 C ATOM 3651 O SER C 85 4.600 41.542 37.448 1.00 21.05 O ANISOU 3651 O SER C 85 2359 2313 3327 -412 500 -383 O ATOM 3652 CB SER C 85 4.695 41.626 40.695 1.00 22.44 C ANISOU 3652 CB SER C 85 3155 2129 3243 -706 645 -430 C ATOM 3653 OG SER C 85 5.440 40.427 40.814 1.00 32.93 O ANISOU 3653 OG SER C 85 4554 3431 4528 -784 535 -362 O ATOM 3654 N TYR C 86 6.772 41.394 38.006 1.00 16.35 N ANISOU 3654 N TYR C 86 1936 1576 2701 -490 302 -158 N ATOM 3655 CA TYR C 86 7.170 40.668 36.787 1.00 14.95 C ANISOU 3655 CA TYR C 86 1604 1493 2583 -405 298 -111 C ATOM 3656 C TYR C 86 7.687 39.311 37.194 1.00 17.91 C ANISOU 3656 C TYR C 86 2043 1815 2949 -479 274 -88 C ATOM 3657 O TYR C 86 8.591 39.212 38.026 1.00 17.49 O ANISOU 3657 O TYR C 86 2090 1630 2924 -553 154 5 O ATOM 3658 CB TYR C 86 8.210 41.470 35.963 1.00 15.17 C ANISOU 3658 CB TYR C 86 1544 1512 2707 -315 244 36 C ATOM 3659 CG TYR C 86 7.582 42.727 35.396 1.00 15.67 C ANISOU 3659 CG TYR C 86 1578 1623 2753 -227 263 7 C ATOM 3660 CD1 TYR C 86 6.937 42.709 34.158 1.00 16.57 C ANISOU 3660 CD1 TYR C 86 1632 1834 2831 -111 301 -42 C ATOM 3661 CD2 TYR C 86 7.485 43.891 36.163 1.00 16.54 C ANISOU 3661 CD2 TYR C 86 1769 1655 2859 -261 218 10 C ATOM 3662 CE1 TYR C 86 6.302 43.849 33.653 1.00 17.22 C ANISOU 3662 CE1 TYR C 86 1708 1933 2903 -18 271 -66 C ATOM 3663 CE2 TYR C 86 6.858 45.039 35.667 1.00 17.30 C ANISOU 3663 CE2 TYR C 86 1848 1774 2950 -164 229 -20 C ATOM 3664 CZ TYR C 86 6.249 45.006 34.421 1.00 20.71 C ANISOU 3664 CZ TYR C 86 2193 2305 3372 -38 247 -57 C ATOM 3665 OH TYR C 86 5.620 46.124 33.919 1.00 19.20 O ANISOU 3665 OH TYR C 86 2001 2110 3184 70 212 -79 O ATOM 3666 N LEU C 87 7.060 38.268 36.660 1.00 15.35 N ANISOU 3666 N LEU C 87 1680 1565 2589 -468 354 -176 N ATOM 3667 CA LEU C 87 7.375 36.889 37.028 1.00 14.87 C ANISOU 3667 CA LEU C 87 1707 1442 2503 -537 346 -175 C ATOM 3668 C LEU C 87 8.107 36.147 35.910 1.00 18.90 C ANISOU 3668 C LEU C 87 2137 1973 3072 -429 358 -110 C ATOM 3669 O LEU C 87 7.607 36.125 34.794 1.00 16.85 O ANISOU 3669 O LEU C 87 1821 1804 2777 -345 419 -164 O ATOM 3670 CB LEU C 87 6.085 36.105 37.371 1.00 14.67 C ANISOU 3670 CB LEU C 87 1736 1443 2396 -635 455 -331 C ATOM 3671 CG LEU C 87 4.963 36.810 38.186 1.00 20.66 C ANISOU 3671 CG LEU C 87 2528 2193 3130 -714 568 -440 C ATOM 3672 CD1 LEU C 87 3.750 35.858 38.422 1.00 19.50 C ANISOU 3672 CD1 LEU C 87 2374 2052 2983 -824 722 -583 C ATOM 3673 CD2 LEU C 87 5.463 37.303 39.490 1.00 26.62 C ANISOU 3673 CD2 LEU C 87 3518 2798 3799 -801 539 -386 C ATOM 3674 N CYS C 88 9.271 35.535 36.195 1.00 17.36 N ANISOU 3674 N CYS C 88 1958 1666 2971 -423 295 3 N ATOM 3675 CA CYS C 88 9.831 34.684 35.149 1.00 21.37 C ANISOU 3675 CA CYS C 88 2415 2169 3535 -309 382 39 C ATOM 3676 C CYS C 88 9.501 33.250 35.523 1.00 18.36 C ANISOU 3676 C CYS C 88 2167 1735 3074 -375 379 -35 C ATOM 3677 O CYS C 88 9.380 32.920 36.710 1.00 17.05 O ANISOU 3677 O CYS C 88 2124 1486 2868 -501 286 -46 O ATOM 3678 CB CYS C 88 11.323 34.887 34.888 1.00 27.39 C ANISOU 3678 CB CYS C 88 3041 2833 4534 -214 381 213 C ATOM 3679 SG CYS C 88 12.360 34.577 36.322 1.00 35.33 S ANISOU 3679 SG CYS C 88 4047 3648 5729 -302 137 334 S ATOM 3680 N ALA C 89 9.285 32.418 34.516 1.00 11.93 N ANISOU 3680 N ALA C 89 1387 946 2201 -303 482 -92 N ATOM 3681 CA ALA C 89 8.899 31.016 34.738 1.00 12.46 C ANISOU 3681 CA ALA C 89 1599 952 2183 -371 486 -172 C ATOM 3682 C ALA C 89 9.602 30.161 33.719 1.00 16.44 C ANISOU 3682 C ALA C 89 2143 1387 2717 -229 588 -138 C ATOM 3683 O ALA C 89 9.781 30.596 32.591 1.00 17.48 O ANISOU 3683 O ALA C 89 2249 1557 2835 -106 697 -122 O ATOM 3684 CB ALA C 89 7.381 30.838 34.614 1.00 12.94 C ANISOU 3684 CB ALA C 89 1707 1105 2104 -482 502 -338 C ATOM 3685 N VAL C 90 10.044 28.983 34.119 1.00 13.63 N ANISOU 3685 N VAL C 90 1886 900 2394 -235 570 -120 N ATOM 3686 CA VAL C 90 10.767 28.081 33.221 1.00 15.01 C ANISOU 3686 CA VAL C 90 2121 968 2616 -81 704 -91 C ATOM 3687 C VAL C 90 10.049 26.752 33.172 1.00 18.20 C ANISOU 3687 C VAL C 90 2750 1313 2850 -157 698 -214 C ATOM 3688 O VAL C 90 9.663 26.234 34.226 1.00 18.24 O ANISOU 3688 O VAL C 90 2837 1273 2820 -306 582 -244 O ATOM 3689 CB VAL C 90 12.250 27.890 33.663 1.00 19.47 C ANISOU 3689 CB VAL C 90 2548 1372 3478 31 688 75 C ATOM 3690 CG1 VAL C 90 12.985 26.883 32.760 1.00 19.95 C ANISOU 3690 CG1 VAL C 90 2666 1291 3624 214 890 98 C ATOM 3691 CG2 VAL C 90 12.990 29.210 33.697 1.00 19.08 C ANISOU 3691 CG2 VAL C 90 2252 1358 3641 80 680 204 C ATOM 3692 N ARG C 91 9.833 26.225 31.947 1.00 15.96 N ANISOU 3692 N ARG C 91 2617 1008 2439 -69 822 -288 N ATOM 3693 CA ARG C 91 9.274 24.891 31.680 1.00 17.93 C ANISOU 3693 CA ARG C 91 3116 1163 2532 -125 817 -402 C ATOM 3694 C ARG C 91 10.507 23.996 31.544 1.00 23.74 C ANISOU 3694 C ARG C 91 3920 1702 3397 47 943 -314 C ATOM 3695 O ARG C 91 11.321 24.235 30.667 1.00 21.57 O ANISOU 3695 O ARG C 91 3624 1374 3197 240 1139 -250 O ATOM 3696 CB ARG C 91 8.350 24.922 30.432 1.00 16.44 C ANISOU 3696 CB ARG C 91 3095 1026 2128 -132 823 -530 C ATOM 3697 CG ARG C 91 7.697 23.572 29.962 1.00 22.85 C ANISOU 3697 CG ARG C 91 4204 1715 2761 -205 781 -663 C ATOM 3698 CD ARG C 91 6.423 23.228 30.715 1.00 34.64 C ANISOU 3698 CD ARG C 91 5660 3263 4238 -464 607 -772 C ATOM 3699 NE ARG C 91 5.280 24.117 30.488 1.00 24.79 N ANISOU 3699 NE ARG C 91 4264 2169 2988 -572 475 -851 N ATOM 3700 CZ ARG C 91 4.082 23.932 31.036 1.00 48.51 C ANISOU 3700 CZ ARG C 91 7171 5214 6048 -793 365 -950 C ATOM 3701 NH1 ARG C 91 3.091 24.775 30.775 1.00 38.72 N ANISOU 3701 NH1 ARG C 91 5746 4092 4875 -858 244 -1014 N ATOM 3702 NH2 ARG C 91 3.856 22.879 31.824 1.00 34.06 N ANISOU 3702 NH2 ARG C 91 5428 3283 4232 -950 385 -984 N ATOM 3703 N ASP C 92 10.720 23.048 32.484 1.00 14.83 N ANISOU 3703 N ASP C 92 2083 1714 1838 44 347 -100 N ATOM 3704 CA ASP C 92 11.949 22.230 32.483 1.00 13.57 C ANISOU 3704 CA ASP C 92 1908 1482 1766 84 315 -90 C ATOM 3705 C ASP C 92 11.817 20.993 31.532 1.00 15.13 C ANISOU 3705 C ASP C 92 2133 1685 1929 84 396 -99 C ATOM 3706 O ASP C 92 10.821 20.872 30.817 1.00 14.58 O ANISOU 3706 O ASP C 92 2093 1681 1767 51 464 -112 O ATOM 3707 CB ASP C 92 12.330 21.820 33.936 1.00 14.92 C ANISOU 3707 CB ASP C 92 2164 1575 1931 89 186 -93 C ATOM 3708 CG ASP C 92 11.431 20.773 34.625 1.00 21.26 C ANISOU 3708 CG ASP C 92 3132 2361 2585 44 187 -108 C ATOM 3709 OD1 ASP C 92 10.570 20.158 33.931 1.00 20.08 O ANISOU 3709 OD1 ASP C 92 3000 2262 2365 11 289 -126 O ATOM 3710 OD2 ASP C 92 11.603 20.553 35.845 1.00 26.76 O ANISOU 3710 OD2 ASP C 92 3954 2981 3233 36 87 -106 O ATOM 3711 N GLY C 93 12.817 20.111 31.540 1.00 13.52 N ANISOU 3711 N GLY C 93 1918 1406 1814 123 376 -101 N ATOM 3712 CA GLY C 93 12.846 18.925 30.677 1.00 12.98 C ANISOU 3712 CA GLY C 93 1878 1324 1730 126 461 -115 C ATOM 3713 C GLY C 93 11.764 17.885 30.926 1.00 17.49 C ANISOU 3713 C GLY C 93 2578 1914 2153 81 473 -131 C ATOM 3714 O GLY C 93 11.538 17.007 30.083 1.00 16.37 O ANISOU 3714 O GLY C 93 2469 1778 1973 67 556 -149 O ATOM 3715 N ASP C 94 11.136 17.922 32.124 1.00 16.19 N ANISOU 3715 N ASP C 94 2503 1742 1907 48 403 -134 N ATOM 3716 CA ASP C 94 10.007 17.051 32.457 1.00 16.67 C ANISOU 3716 CA ASP C 94 2688 1811 1835 -18 446 -164 C ATOM 3717 C ASP C 94 8.689 17.810 32.266 1.00 17.61 C ANISOU 3717 C ASP C 94 2776 2025 1890 -78 501 -198 C ATOM 3718 O ASP C 94 7.647 17.373 32.761 1.00 16.99 O ANISOU 3718 O ASP C 94 2775 1950 1729 -148 544 -242 O ATOM 3719 CB ASP C 94 10.095 16.511 33.893 1.00 18.85 C ANISOU 3719 CB ASP C 94 3121 1990 2051 -31 366 -157 C ATOM 3720 CG ASP C 94 11.328 15.703 34.264 1.00 30.86 C ANISOU 3720 CG ASP C 94 4691 3391 3642 43 261 -128 C ATOM 3721 OD1 ASP C 94 11.902 15.025 33.368 1.00 28.64 O ANISOU 3721 OD1 ASP C 94 4345 3093 3443 87 300 -130 O ATOM 3722 OD2 ASP C 94 11.724 15.749 35.452 1.00 36.52 O ANISOU 3722 OD2 ASP C 94 5520 4019 4336 60 133 -109 O ATOM 3723 N TYR C 95 8.753 18.976 31.592 1.00 15.25 N ANISOU 3723 N TYR C 95 2364 1787 1643 -52 500 -184 N ATOM 3724 CA TYR C 95 7.602 19.852 31.291 1.00 14.83 C ANISOU 3724 CA TYR C 95 2258 1812 1563 -84 520 -214 C ATOM 3725 C TYR C 95 6.962 20.384 32.584 1.00 18.90 C ANISOU 3725 C TYR C 95 2806 2317 2059 -125 506 -242 C ATOM 3726 O TYR C 95 5.760 20.683 32.627 1.00 19.60 O ANISOU 3726 O TYR C 95 2865 2448 2135 -170 544 -300 O ATOM 3727 CB TYR C 95 6.567 19.126 30.371 1.00 13.60 C ANISOU 3727 CB TYR C 95 2109 1705 1352 -123 572 -265 C ATOM 3728 CG TYR C 95 7.151 18.805 29.018 1.00 13.60 C ANISOU 3728 CG TYR C 95 2105 1710 1351 -89 596 -241 C ATOM 3729 CD1 TYR C 95 7.037 19.705 27.956 1.00 15.23 C ANISOU 3729 CD1 TYR C 95 2274 1957 1555 -63 584 -224 C ATOM 3730 CD2 TYR C 95 7.892 17.634 28.811 1.00 12.38 C ANISOU 3730 CD2 TYR C 95 2007 1502 1194 -82 637 -233 C ATOM 3731 CE1 TYR C 95 7.654 19.454 26.724 1.00 15.65 C ANISOU 3731 CE1 TYR C 95 2368 1993 1586 -44 632 -202 C ATOM 3732 CE2 TYR C 95 8.476 17.356 27.571 1.00 12.30 C ANISOU 3732 CE2 TYR C 95 2006 1482 1187 -59 691 -220 C ATOM 3733 CZ TYR C 95 8.372 18.277 26.541 1.00 14.71 C ANISOU 3733 CZ TYR C 95 2293 1823 1472 -47 697 -205 C ATOM 3734 OH TYR C 95 8.932 17.997 25.328 1.00 13.18 O ANISOU 3734 OH TYR C 95 2151 1601 1255 -40 775 -198 O ATOM 3735 N LYS C 96 7.762 20.486 33.657 1.00 13.76 N ANISOU 3735 N LYS C 96 2219 1596 1413 -113 449 -213 N ATOM 3736 CA LYS C 96 7.233 21.070 34.885 1.00 13.62 C ANISOU 3736 CA LYS C 96 2266 1552 1357 -160 446 -240 C ATOM 3737 C LYS C 96 7.495 22.586 34.814 1.00 18.36 C ANISOU 3737 C LYS C 96 2762 2185 2031 -123 406 -219 C ATOM 3738 O LYS C 96 8.631 23.006 34.543 1.00 18.04 O ANISOU 3738 O LYS C 96 2666 2128 2061 -65 341 -170 O ATOM 3739 CB LYS C 96 7.887 20.429 36.124 1.00 15.63 C ANISOU 3739 CB LYS C 96 2693 1698 1548 -171 383 -220 C ATOM 3740 CG LYS C 96 7.429 21.032 37.463 1.00 19.91 C ANISOU 3740 CG LYS C 96 3357 2189 2018 -232 389 -249 C ATOM 3741 CD LYS C 96 8.167 20.400 38.673 1.00 28.12 C ANISOU 3741 CD LYS C 96 4620 3097 2965 -237 288 -220 C ATOM 3742 CE LYS C 96 9.549 20.970 38.924 1.00 35.86 C ANISOU 3742 CE LYS C 96 5562 4035 4026 -154 109 -167 C ATOM 3743 NZ LYS C 96 10.334 20.077 39.823 1.00 49.86 N ANISOU 3743 NZ LYS C 96 7540 5673 5733 -131 -35 -138 N ATOM 3744 N LEU C 97 6.451 23.392 35.012 1.00 16.15 N ANISOU 3744 N LEU C 97 2442 1940 1753 -157 454 -266 N ATOM 3745 CA LEU C 97 6.574 24.853 35.012 1.00 16.67 C ANISOU 3745 CA LEU C 97 2425 2023 1884 -126 423 -252 C ATOM 3746 C LEU C 97 6.848 25.334 36.426 1.00 18.87 C ANISOU 3746 C LEU C 97 2803 2235 2134 -158 396 -260 C ATOM 3747 O LEU C 97 6.060 25.042 37.325 1.00 20.24 O ANISOU 3747 O LEU C 97 3079 2373 2239 -229 462 -316 O ATOM 3748 CB LEU C 97 5.288 25.513 34.452 1.00 16.88 C ANISOU 3748 CB LEU C 97 2353 2110 1952 -131 471 -305 C ATOM 3749 CG LEU C 97 5.342 27.055 34.244 1.00 20.03 C ANISOU 3749 CG LEU C 97 2668 2519 2423 -85 438 -286 C ATOM 3750 CD1 LEU C 97 6.386 27.441 33.146 1.00 17.95 C ANISOU 3750 CD1 LEU C 97 2365 2267 2190 -19 389 -206 C ATOM 3751 CD2 LEU C 97 3.968 27.576 33.873 1.00 20.66 C ANISOU 3751 CD2 LEU C 97 2656 2633 2558 -83 462 -354 C ATOM 3752 N SER C 98 7.973 26.041 36.634 1.00 15.62 N ANISOU 3752 N SER C 98 2373 1792 1771 -116 308 -212 N ATOM 3753 CA SER C 98 8.360 26.625 37.933 1.00 16.83 C ANISOU 3753 CA SER C 98 2626 1874 1896 -142 249 -219 C ATOM 3754 C SER C 98 8.406 28.150 37.817 1.00 18.61 C ANISOU 3754 C SER C 98 2751 2119 2201 -123 246 -218 C ATOM 3755 O SER C 98 8.984 28.635 36.862 1.00 17.51 O ANISOU 3755 O SER C 98 2490 2011 2153 -69 228 -179 O ATOM 3756 CB SER C 98 9.749 26.131 38.351 1.00 22.03 C ANISOU 3756 CB SER C 98 3341 2460 2569 -107 109 -177 C ATOM 3757 OG SER C 98 9.790 24.757 38.688 1.00 33.25 O ANISOU 3757 OG SER C 98 4896 3832 3907 -121 87 -175 O ATOM 3758 N PHE C 99 7.877 28.895 38.785 1.00 14.76 N ANISOU 3758 N PHE C 99 2334 1596 1678 -170 276 -261 N ATOM 3759 CA PHE C 99 7.944 30.372 38.773 1.00 14.34 C ANISOU 3759 CA PHE C 99 2201 1546 1702 -152 274 -263 C ATOM 3760 C PHE C 99 8.984 30.868 39.735 1.00 17.92 C ANISOU 3760 C PHE C 99 2734 1923 2150 -164 166 -252 C ATOM 3761 O PHE C 99 9.149 30.275 40.790 1.00 16.60 O ANISOU 3761 O PHE C 99 2738 1688 1880 -208 115 -268 O ATOM 3762 CB PHE C 99 6.589 30.988 39.194 1.00 15.51 C ANISOU 3762 CB PHE C 99 2356 1695 1842 -197 391 -337 C ATOM 3763 CG PHE C 99 5.547 30.957 38.110 1.00 15.87 C ANISOU 3763 CG PHE C 99 2266 1812 1954 -166 460 -360 C ATOM 3764 CD1 PHE C 99 5.306 32.081 37.325 1.00 16.56 C ANISOU 3764 CD1 PHE C 99 2227 1926 2138 -106 451 -348 C ATOM 3765 CD2 PHE C 99 4.801 29.802 37.871 1.00 18.23 C ANISOU 3765 CD2 PHE C 99 2573 2138 2216 -195 518 -398 C ATOM 3766 CE1 PHE C 99 4.370 32.043 36.285 1.00 17.98 C ANISOU 3766 CE1 PHE C 99 2299 2158 2376 -65 467 -368 C ATOM 3767 CE2 PHE C 99 3.863 29.760 36.830 1.00 20.52 C ANISOU 3767 CE2 PHE C 99 2731 2489 2578 -162 545 -427 C ATOM 3768 CZ PHE C 99 3.637 30.882 36.058 1.00 18.48 C ANISOU 3768 CZ PHE C 99 2355 2254 2412 -93 506 -413 C ATOM 3769 N GLY C 100 9.593 32.006 39.418 1.00 17.13 N ANISOU 3769 N GLY C 100 2533 1824 2153 -131 131 -231 N ATOM 3770 CA GLY C 100 10.447 32.720 40.358 1.00 17.98 C ANISOU 3770 CA GLY C 100 2698 1857 2275 -151 29 -240 C ATOM 3771 C GLY C 100 9.519 33.457 41.312 1.00 21.31 C ANISOU 3771 C GLY C 100 3231 2243 2621 -212 104 -299 C ATOM 3772 O GLY C 100 8.300 33.488 41.091 1.00 19.39 O ANISOU 3772 O GLY C 100 2970 2038 2361 -227 238 -334 O ATOM 3773 N ALA C 101 10.070 34.070 42.362 1.00 18.37 N ANISOU 3773 N ALA C 101 2968 1793 2220 -250 21 -322 N ATOM 3774 CA ALA C 101 9.294 34.760 43.380 1.00 19.52 C ANISOU 3774 CA ALA C 101 3253 1883 2281 -320 102 -386 C ATOM 3775 C ALA C 101 8.656 36.055 42.855 1.00 21.09 C ANISOU 3775 C ALA C 101 3311 2114 2589 -300 218 -407 C ATOM 3776 O ALA C 101 7.745 36.560 43.488 1.00 20.22 O ANISOU 3776 O ALA C 101 3275 1967 2441 -349 334 -474 O ATOM 3777 CB ALA C 101 10.166 35.052 44.596 1.00 22.08 C ANISOU 3777 CB ALA C 101 3754 2103 2533 -365 -46 -404 C ATOM 3778 N GLY C 102 9.123 36.565 41.710 1.00 16.71 N ANISOU 3778 N GLY C 102 2572 1611 2168 -230 195 -355 N ATOM 3779 CA GLY C 102 8.604 37.806 41.123 1.00 15.09 C ANISOU 3779 CA GLY C 102 2256 1417 2061 -197 279 -361 C ATOM 3780 C GLY C 102 9.428 39.015 41.508 1.00 18.95 C ANISOU 3780 C GLY C 102 2746 1843 2610 -211 227 -363 C ATOM 3781 O GLY C 102 10.040 39.035 42.578 1.00 18.66 O ANISOU 3781 O GLY C 102 2830 1743 2517 -265 143 -392 O ATOM 3782 N THR C 103 9.494 40.006 40.611 1.00 14.60 N ANISOU 3782 N THR C 103 2079 1299 2170 -162 264 -332 N ATOM 3783 CA THR C 103 10.196 41.263 40.851 1.00 14.50 C ANISOU 3783 CA THR C 103 2057 1220 2233 -179 242 -339 C ATOM 3784 C THR C 103 9.198 42.371 40.871 1.00 18.90 C ANISOU 3784 C THR C 103 2612 1746 2822 -165 345 -371 C ATOM 3785 O THR C 103 8.545 42.600 39.849 1.00 18.53 O ANISOU 3785 O THR C 103 2485 1730 2826 -97 399 -340 O ATOM 3786 CB THR C 103 11.246 41.564 39.744 1.00 18.57 C ANISOU 3786 CB THR C 103 2455 1739 2863 -144 220 -277 C ATOM 3787 OG1 THR C 103 12.200 40.509 39.693 1.00 16.29 O ANISOU 3787 OG1 THR C 103 2138 1469 2583 -150 130 -260 O ATOM 3788 CG2 THR C 103 11.962 42.963 39.960 1.00 14.46 C ANISOU 3788 CG2 THR C 103 1919 1136 2440 -174 220 -294 C ATOM 3789 N THR C 104 9.101 43.099 41.977 1.00 15.72 N ANISOU 3789 N THR C 104 2306 1272 2397 -222 362 -436 N ATOM 3790 CA THR C 104 8.214 44.261 41.969 1.00 18.22 C ANISOU 3790 CA THR C 104 2606 1543 2776 -201 468 -474 C ATOM 3791 C THR C 104 8.953 45.466 41.372 1.00 22.59 C ANISOU 3791 C THR C 104 3101 2048 3434 -175 453 -432 C ATOM 3792 O THR C 104 9.998 45.889 41.877 1.00 21.47 O ANISOU 3792 O THR C 104 2994 1857 3306 -231 392 -441 O ATOM 3793 CB THR C 104 7.653 44.563 43.366 1.00 23.97 C ANISOU 3793 CB THR C 104 3473 2200 3434 -279 536 -574 C ATOM 3794 OG1 THR C 104 6.914 43.424 43.769 1.00 29.38 O ANISOU 3794 OG1 THR C 104 4219 2918 4027 -308 584 -612 O ATOM 3795 CG2 THR C 104 6.713 45.784 43.381 1.00 24.01 C ANISOU 3795 CG2 THR C 104 3445 2143 3536 -251 659 -628 C ATOM 3796 N VAL C 105 8.370 46.042 40.327 1.00 18.68 N ANISOU 3796 N VAL C 105 2531 1553 3015 -94 504 -392 N ATOM 3797 CA VAL C 105 8.930 47.226 39.691 1.00 17.34 C ANISOU 3797 CA VAL C 105 2341 1316 2931 -71 517 -349 C ATOM 3798 C VAL C 105 8.138 48.429 40.156 1.00 22.87 C ANISOU 3798 C VAL C 105 3073 1933 3685 -57 588 -404 C ATOM 3799 O VAL C 105 6.921 48.447 40.002 1.00 21.93 O ANISOU 3799 O VAL C 105 2923 1817 3593 5 631 -432 O ATOM 3800 CB VAL C 105 8.980 47.122 38.142 1.00 20.11 C ANISOU 3800 CB VAL C 105 2640 1692 3308 8 515 -255 C ATOM 3801 CG1 VAL C 105 9.381 48.464 37.506 1.00 21.02 C ANISOU 3801 CG1 VAL C 105 2781 1708 3496 28 557 -213 C ATOM 3802 CG2 VAL C 105 9.934 46.010 37.701 1.00 19.28 C ANISOU 3802 CG2 VAL C 105 2502 1652 3170 -18 470 -212 C ATOM 3803 N THR C 106 8.831 49.441 40.695 1.00 19.83 N ANISOU 3803 N THR C 106 2737 1463 3337 -112 600 -428 N ATOM 3804 CA THR C 106 8.238 50.717 41.108 1.00 21.05 C ANISOU 3804 CA THR C 106 2930 1516 3554 -102 676 -480 C ATOM 3805 C THR C 106 8.788 51.800 40.205 1.00 25.53 C ANISOU 3805 C THR C 106 3491 2006 4203 -67 690 -414 C ATOM 3806 O THR C 106 10.007 51.989 40.144 1.00 25.03 O ANISOU 3806 O THR C 106 3433 1922 4156 -132 667 -392 O ATOM 3807 CB THR C 106 8.541 51.028 42.598 1.00 28.89 C ANISOU 3807 CB THR C 106 4023 2452 4500 -211 688 -577 C ATOM 3808 OG1 THR C 106 7.978 49.993 43.393 1.00 33.66 O ANISOU 3808 OG1 THR C 106 4677 3108 5003 -249 695 -634 O ATOM 3809 CG2 THR C 106 7.989 52.407 43.053 1.00 30.55 C ANISOU 3809 CG2 THR C 106 4282 2545 4782 -209 786 -640 C ATOM 3810 N VAL C 107 7.890 52.526 39.521 1.00 22.60 N ANISOU 3810 N VAL C 107 3114 1579 3895 33 728 -390 N ATOM 3811 CA VAL C 107 8.273 53.613 38.629 1.00 22.81 C ANISOU 3811 CA VAL C 107 3182 1504 3980 72 750 -320 C ATOM 3812 C VAL C 107 8.124 54.915 39.406 1.00 29.64 C ANISOU 3812 C VAL C 107 4101 2246 4915 47 817 -387 C ATOM 3813 O VAL C 107 7.052 55.182 39.964 1.00 29.83 O ANISOU 3813 O VAL C 107 4113 2241 4980 89 851 -459 O ATOM 3814 CB VAL C 107 7.455 53.588 37.305 1.00 25.70 C ANISOU 3814 CB VAL C 107 3547 1863 4355 208 713 -240 C ATOM 3815 CG1 VAL C 107 7.914 54.685 36.342 1.00 25.65 C ANISOU 3815 CG1 VAL C 107 3644 1729 4375 241 740 -156 C ATOM 3816 CG2 VAL C 107 7.529 52.209 36.632 1.00 23.90 C ANISOU 3816 CG2 VAL C 107 3274 1760 4047 222 653 -190 C ATOM 3817 N ARG C 108 9.214 55.704 39.477 1.00 26.95 N ANISOU 3817 N ARG C 108 3810 1827 4602 -31 848 -378 N ATOM 3818 CA ARG C 108 9.201 57.009 40.159 1.00 28.27 C ANISOU 3818 CA ARG C 108 4043 1864 4835 -66 915 -440 C ATOM 3819 C ARG C 108 8.724 58.064 39.189 1.00 31.73 C ANISOU 3819 C ARG C 108 4537 2180 5339 39 954 -374 C ATOM 3820 O ARG C 108 9.165 58.091 38.034 1.00 29.46 O ANISOU 3820 O ARG C 108 4285 1871 5037 70 947 -274 O ATOM 3821 CB ARG C 108 10.602 57.412 40.691 1.00 30.20 C ANISOU 3821 CB ARG C 108 4313 2066 5097 -205 922 -473 C ATOM 3822 CG ARG C 108 11.240 56.453 41.686 1.00 39.16 C ANISOU 3822 CG ARG C 108 5417 3293 6169 -307 839 -538 C ATOM 3823 CD ARG C 108 12.653 56.883 42.108 1.00 49.76 C ANISOU 3823 CD ARG C 108 6758 4581 7569 -432 808 -581 C ATOM 3824 NE ARG C 108 13.616 56.955 40.998 1.00 55.31 N ANISOU 3824 NE ARG C 108 7398 5264 8353 -444 837 -512 N ATOM 3825 CZ ARG C 108 14.697 56.184 40.855 1.00 63.58 C ANISOU 3825 CZ ARG C 108 8352 6367 9439 -503 772 -515 C ATOM 3826 NH1 ARG C 108 15.509 56.356 39.821 1.00 45.60 N ANISOU 3826 NH1 ARG C 108 6025 4048 7252 -524 848 -468 N ATOM 3827 NH2 ARG C 108 14.977 55.244 41.751 1.00 48.15 N ANISOU 3827 NH2 ARG C 108 6364 4492 7437 -544 639 -571 N ATOM 3828 N ALA C 109 7.861 58.963 39.662 1.00 30.71 N ANISOU 3828 N ALA C 109 4436 1951 5282 90 1000 -433 N ATOM 3829 CA ALA C 109 7.371 60.051 38.834 1.00 31.79 C ANISOU 3829 CA ALA C 109 4643 1944 5492 202 1016 -376 C ATOM 3830 C ALA C 109 8.464 61.093 38.664 1.00 38.06 C ANISOU 3830 C ALA C 109 5544 2613 6304 119 1087 -345 C ATOM 3831 O ALA C 109 9.272 61.301 39.574 1.00 36.66 O ANISOU 3831 O ALA C 109 5366 2432 6132 -17 1133 -417 O ATOM 3832 CB ALA C 109 6.135 60.677 39.468 1.00 33.28 C ANISOU 3832 CB ALA C 109 4806 2053 5786 282 1050 -468 C ATOM 3833 N ASN C 110 8.511 61.715 37.487 1.00 37.70 N ANISOU 3833 N ASN C 110 5605 2457 6263 193 1092 -240 N ATOM 3834 CA ASN C 110 9.415 62.816 37.190 1.00 40.75 C ANISOU 3834 CA ASN C 110 6118 2689 6675 121 1188 -207 C ATOM 3835 C ASN C 110 8.682 64.095 37.643 1.00 48.50 C ANISOU 3835 C ASN C 110 7167 3509 7751 185 1228 -255 C ATOM 3836 O ASN C 110 7.734 64.526 36.973 1.00 49.47 O ANISOU 3836 O ASN C 110 7354 3539 7904 342 1176 -201 O ATOM 3837 CB ASN C 110 9.773 62.827 35.700 1.00 45.96 C ANISOU 3837 CB ASN C 110 6908 3287 7270 162 1195 -71 C ATOM 3838 CG ASN C 110 11.200 63.225 35.422 1.00 81.32 C ANISOU 3838 CG ASN C 110 11453 7691 11753 10 1325 -55 C ATOM 3839 OD1 ASN C 110 11.647 64.331 35.764 1.00 74.03 O ANISOU 3839 OD1 ASN C 110 10601 6626 10899 -61 1423 -91 O ATOM 3840 ND2 ASN C 110 11.945 62.328 34.787 1.00 75.90 N ANISOU 3840 ND2 ASN C 110 10738 7090 11012 -49 1341 -11 N ATOM 3841 N ILE C 111 9.028 64.612 38.845 1.00 44.76 N ANISOU 3841 N ILE C 111 6672 3005 7328 73 1300 -369 N ATOM 3842 CA ILE C 111 8.349 65.769 39.445 1.00 45.44 C ANISOU 3842 CA ILE C 111 6813 2942 7511 117 1359 -439 C ATOM 3843 C ILE C 111 9.030 67.056 38.946 1.00 54.23 C ANISOU 3843 C ILE C 111 8086 3858 8661 80 1449 -389 C ATOM 3844 O ILE C 111 10.143 67.385 39.373 1.00 54.51 O ANISOU 3844 O ILE C 111 8143 3869 8702 -82 1525 -432 O ATOM 3845 CB ILE C 111 8.284 65.649 41.009 1.00 46.83 C ANISOU 3845 CB ILE C 111 6922 3172 7700 11 1401 -594 C ATOM 3846 CG1 ILE C 111 7.540 64.360 41.473 1.00 44.44 C ANISOU 3846 CG1 ILE C 111 6495 3041 7350 42 1338 -642 C ATOM 3847 CG2 ILE C 111 7.708 66.909 41.686 1.00 47.18 C ANISOU 3847 CG2 ILE C 111 7036 3043 7847 32 1496 -683 C ATOM 3848 CD1 ILE C 111 6.025 64.202 41.005 1.00 44.77 C ANISOU 3848 CD1 ILE C 111 6465 3073 7471 232 1300 -636 C ATOM 3849 N GLN C 112 8.343 67.760 38.024 1.00 53.72 N ANISOU 3849 N GLN C 112 8139 3645 8627 233 1428 -302 N ATOM 3850 CA GLN C 112 8.819 68.975 37.354 1.00 56.11 C ANISOU 3850 CA GLN C 112 8642 3731 8946 225 1512 -231 C ATOM 3851 C GLN C 112 8.910 70.190 38.294 1.00 61.26 C ANISOU 3851 C GLN C 112 9343 4234 9700 159 1623 -333 C ATOM 3852 O GLN C 112 9.922 70.898 38.273 1.00 61.43 O ANISOU 3852 O GLN C 112 9464 4148 9727 25 1737 -334 O ATOM 3853 CB GLN C 112 7.917 69.313 36.153 1.00 58.78 C ANISOU 3853 CB GLN C 112 9121 3941 9273 431 1415 -109 C ATOM 3854 N ASN C 113 7.860 70.439 39.099 1.00 57.80 N ANISOU 3854 N ASN C 113 8833 3777 9352 246 1606 -429 N ATOM 3855 CA ASN C 113 7.821 71.586 40.005 1.00 58.41 C ANISOU 3855 CA ASN C 113 8967 3702 9525 194 1719 -536 C ATOM 3856 C ASN C 113 7.610 71.131 41.466 1.00 60.89 C ANISOU 3856 C ASN C 113 9148 4136 9852 101 1751 -698 C ATOM 3857 O ASN C 113 6.495 71.265 41.988 1.00 60.99 O ANISOU 3857 O ASN C 113 9104 4116 9953 201 1764 -781 O ATOM 3858 CB ASN C 113 6.729 72.573 39.559 1.00 62.10 C ANISOU 3858 CB ASN C 113 9525 3963 10108 393 1702 -506 C ATOM 3859 CG ASN C 113 6.869 73.049 38.129 1.00 91.64 C ANISOU 3859 CG ASN C 113 13457 7556 13805 493 1652 -339 C ATOM 3860 OD1 ASN C 113 6.114 72.642 37.236 1.00 84.08 O ANISOU 3860 OD1 ASN C 113 12507 6606 12834 667 1507 -249 O ATOM 3861 ND2 ASN C 113 7.841 73.920 37.879 1.00 87.71 N ANISOU 3861 ND2 ASN C 113 13139 6909 13279 377 1772 -300 N ATOM 3862 N PRO C 114 8.657 70.598 42.157 1.00 56.24 N ANISOU 3862 N PRO C 114 8520 3668 9182 -91 1765 -756 N ATOM 3863 CA PRO C 114 8.451 70.140 43.544 1.00 55.30 C ANISOU 3863 CA PRO C 114 8334 3642 9035 -182 1781 -903 C ATOM 3864 C PRO C 114 8.170 71.295 44.509 1.00 61.90 C ANISOU 3864 C PRO C 114 9262 4310 9947 -227 1904 -1030 C ATOM 3865 O PRO C 114 8.804 72.354 44.443 1.00 62.90 O ANISOU 3865 O PRO C 114 9497 4284 10117 -293 1973 -1030 O ATOM 3866 CB PRO C 114 9.742 69.389 43.892 1.00 55.81 C ANISOU 3866 CB PRO C 114 8364 3843 9001 -361 1725 -917 C ATOM 3867 CG PRO C 114 10.730 69.793 42.896 1.00 60.77 C ANISOU 3867 CG PRO C 114 9034 4406 9650 -399 1738 -818 C ATOM 3868 CD PRO C 114 10.040 70.348 41.696 1.00 57.21 C ANISOU 3868 CD PRO C 114 8658 3836 9244 -228 1760 -697 C ATOM 3869 N ASP C 115 7.167 71.100 45.371 1.00 58.28 N ANISOU 3869 N ASP C 115 8765 3865 9515 -190 1952 -1143 N ATOM 3870 CA ASP C 115 6.728 72.102 46.351 1.00 59.27 C ANISOU 3870 CA ASP C 115 8977 3829 9715 -226 2093 -1283 C ATOM 3871 C ASP C 115 6.408 71.366 47.666 1.00 61.77 C ANISOU 3871 C ASP C 115 9287 4240 9941 -331 2139 -1428 C ATOM 3872 O ASP C 115 5.240 71.293 48.060 1.00 60.63 O ANISOU 3872 O ASP C 115 9098 4065 9875 -249 2231 -1516 O ATOM 3873 CB ASP C 115 5.508 72.860 45.781 1.00 62.17 C ANISOU 3873 CB ASP C 115 9320 4039 10263 -16 2142 -1269 C ATOM 3874 CG ASP C 115 5.165 74.167 46.469 1.00 74.18 C ANISOU 3874 CG ASP C 115 10944 5341 11901 -26 2297 -1385 C ATOM 3875 OD1 ASP C 115 5.919 74.577 47.385 1.00 74.68 O ANISOU 3875 OD1 ASP C 115 11119 5365 11889 -210 2373 -1477 O ATOM 3876 OD2 ASP C 115 4.148 74.785 46.087 1.00 80.84 O ANISOU 3876 OD2 ASP C 115 11756 6043 12918 153 2329 -1391 O ATOM 3877 N PRO C 116 7.436 70.759 48.324 1.00 58.72 N ANISOU 3877 N PRO C 116 8951 3964 9397 -510 2070 -1458 N ATOM 3878 CA PRO C 116 7.170 69.917 49.505 1.00 58.77 C ANISOU 3878 CA PRO C 116 8999 4058 9274 -610 2089 -1576 C ATOM 3879 C PRO C 116 6.541 70.657 50.675 1.00 68.58 C ANISOU 3879 C PRO C 116 10375 5150 10533 -673 2269 -1746 C ATOM 3880 O PRO C 116 6.964 71.758 51.029 1.00 69.14 O ANISOU 3880 O PRO C 116 10561 5071 10637 -745 2333 -1801 O ATOM 3881 CB PRO C 116 8.552 69.368 49.870 1.00 59.31 C ANISOU 3881 CB PRO C 116 9118 4227 9192 -778 1941 -1564 C ATOM 3882 CG PRO C 116 9.514 70.340 49.265 1.00 64.08 C ANISOU 3882 CG PRO C 116 9732 4733 9880 -811 1919 -1508 C ATOM 3883 CD PRO C 116 8.875 70.743 47.985 1.00 59.56 C ANISOU 3883 CD PRO C 116 9073 4110 9445 -625 1963 -1389 C ATOM 3884 N ALA C 117 5.499 70.045 51.254 1.00 49.51 N ANISOU 3884 N ALA C 117 7418 3420 7974 -527 2013 -1998 N ATOM 3885 CA ALA C 117 4.766 70.611 52.388 1.00 50.74 C ANISOU 3885 CA ALA C 117 7632 3592 8055 -577 1879 -2215 C ATOM 3886 C ALA C 117 4.050 69.530 53.194 1.00 54.53 C ANISOU 3886 C ALA C 117 8154 4346 8218 -546 1677 -2302 C ATOM 3887 O ALA C 117 3.749 68.451 52.676 1.00 52.55 O ANISOU 3887 O ALA C 117 7917 4269 7783 -458 1666 -2182 O ATOM 3888 CB ALA C 117 3.756 71.644 51.904 1.00 51.72 C ANISOU 3888 CB ALA C 117 7926 3581 8145 -443 2042 -2176 C ATOM 3889 N VAL C 118 3.803 69.831 54.473 1.00 52.11 N ANISOU 3889 N VAL C 118 7886 4052 7862 -602 1532 -2512 N ATOM 3890 CA VAL C 118 3.067 68.975 55.391 1.00 51.30 C ANISOU 3890 CA VAL C 118 7871 4146 7475 -550 1408 -2602 C ATOM 3891 C VAL C 118 1.809 69.750 55.768 1.00 56.86 C ANISOU 3891 C VAL C 118 8709 4800 8094 -469 1466 -2665 C ATOM 3892 O VAL C 118 1.904 70.883 56.250 1.00 57.54 O ANISOU 3892 O VAL C 118 8838 4724 8301 -504 1448 -2777 O ATOM 3893 CB VAL C 118 3.898 68.516 56.619 1.00 56.51 C ANISOU 3893 CB VAL C 118 8519 4859 8093 -609 1198 -2789 C ATOM 3894 CG1 VAL C 118 3.046 67.689 57.585 1.00 56.00 C ANISOU 3894 CG1 VAL C 118 8615 4949 7712 -508 1149 -2859 C ATOM 3895 CG2 VAL C 118 5.141 67.735 56.191 1.00 55.66 C ANISOU 3895 CG2 VAL C 118 8262 4814 8072 -677 1136 -2735 C ATOM 3896 N TYR C 119 0.639 69.171 55.478 1.00 53.46 N ANISOU 3896 N TYR C 119 8328 4495 7490 -359 1535 -2599 N ATOM 3897 CA TYR C 119 -0.657 69.796 55.752 1.00 54.02 C ANISOU 3897 CA TYR C 119 8498 4538 7491 -264 1604 -2657 C ATOM 3898 C TYR C 119 -1.465 69.010 56.773 1.00 56.96 C ANISOU 3898 C TYR C 119 8932 5030 7680 -221 1593 -2737 C ATOM 3899 O TYR C 119 -1.357 67.779 56.847 1.00 54.12 O ANISOU 3899 O TYR C 119 8535 4803 7227 -229 1579 -2701 O ATOM 3900 CB TYR C 119 -1.482 69.922 54.456 1.00 54.64 C ANISOU 3900 CB TYR C 119 8563 4617 7582 -129 1715 -2548 C ATOM 3901 CG TYR C 119 -0.830 70.761 53.379 1.00 56.90 C ANISOU 3901 CG TYR C 119 8862 4740 8017 -102 1803 -2443 C ATOM 3902 CD1 TYR C 119 -0.704 72.141 53.522 1.00 60.52 C ANISOU 3902 CD1 TYR C 119 9404 5003 8588 -123 1871 -2492 C ATOM 3903 CD2 TYR C 119 -0.382 70.184 52.195 1.00 56.65 C ANISOU 3903 CD2 TYR C 119 8790 4725 8009 -29 1848 -2283 C ATOM 3904 CE1 TYR C 119 -0.091 72.917 52.540 1.00 62.24 C ANISOU 3904 CE1 TYR C 119 9658 5027 8964 -90 2021 -2383 C ATOM 3905 CE2 TYR C 119 0.208 70.953 51.192 1.00 58.47 C ANISOU 3905 CE2 TYR C 119 9077 4767 8372 38 1995 -2161 C ATOM 3906 CZ TYR C 119 0.342 72.322 51.364 1.00 66.42 C ANISOU 3906 CZ TYR C 119 10164 5561 9512 4 2103 -2210 C ATOM 3907 OH TYR C 119 0.916 73.086 50.377 1.00 65.33 O ANISOU 3907 OH TYR C 119 10106 5194 9522 80 2314 -2078 O ATOM 3908 N GLN C 120 -2.304 69.727 57.533 1.00 53.95 N ANISOU 3908 N GLN C 120 8662 4586 7250 -162 1632 -2832 N ATOM 3909 CA GLN C 120 -3.208 69.133 58.509 1.00 54.06 C ANISOU 3909 CA GLN C 120 8761 4662 7117 -89 1701 -2891 C ATOM 3910 C GLN C 120 -4.608 69.102 57.893 1.00 58.57 C ANISOU 3910 C GLN C 120 9257 5268 7730 1 1838 -2864 C ATOM 3911 O GLN C 120 -5.105 70.139 57.442 1.00 59.33 O ANISOU 3911 O GLN C 120 9366 5291 7887 57 1859 -2880 O ATOM 3912 CB GLN C 120 -3.181 69.905 59.840 1.00 56.84 C ANISOU 3912 CB GLN C 120 9309 4906 7383 -41 1654 -3018 C ATOM 3913 CG GLN C 120 -3.771 69.111 61.003 1.00 76.85 C ANISOU 3913 CG GLN C 120 11993 7474 9732 67 1751 -3059 C ATOM 3914 CD GLN C 120 -3.563 69.794 62.330 1.00101.17 C ANISOU 3914 CD GLN C 120 15323 10435 12683 175 1668 -3185 C ATOM 3915 OE1 GLN C 120 -2.496 69.698 62.948 1.00 99.72 O ANISOU 3915 OE1 GLN C 120 15235 10220 12433 191 1484 -3282 O ATOM 3916 NE2 GLN C 120 -4.588 70.482 62.807 1.00 92.55 N ANISOU 3916 NE2 GLN C 120 14348 9268 11547 283 1783 -3204 N ATOM 3917 N LEU C 121 -5.219 67.910 57.839 1.00 54.11 N ANISOU 3917 N LEU C 121 8606 4803 7151 24 1924 -2843 N ATOM 3918 CA LEU C 121 -6.545 67.691 57.257 1.00 53.80 C ANISOU 3918 CA LEU C 121 8433 4791 7217 111 2026 -2865 C ATOM 3919 C LEU C 121 -7.534 67.289 58.346 1.00 58.86 C ANISOU 3919 C LEU C 121 9109 5409 7845 152 2212 -2929 C ATOM 3920 O LEU C 121 -7.288 66.308 59.048 1.00 58.77 O ANISOU 3920 O LEU C 121 9154 5420 7755 121 2293 -2909 O ATOM 3921 CB LEU C 121 -6.471 66.596 56.166 1.00 52.64 C ANISOU 3921 CB LEU C 121 8115 4743 7143 110 1978 -2803 C ATOM 3922 CG LEU C 121 -5.979 66.996 54.764 1.00 56.62 C ANISOU 3922 CG LEU C 121 8577 5244 7693 167 1854 -2731 C ATOM 3923 CD1 LEU C 121 -4.474 67.271 54.727 1.00 56.08 C ANISOU 3923 CD1 LEU C 121 8593 5148 7567 65 1778 -2635 C ATOM 3924 CD2 LEU C 121 -6.302 65.928 53.778 1.00 57.72 C ANISOU 3924 CD2 LEU C 121 8568 5465 7898 240 1803 -2706 C ATOM 3925 N ARG C 122 -8.637 68.052 58.500 1.00 55.62 N ANISOU 3925 N ARG C 122 8690 4940 7504 242 2305 -3002 N ATOM 3926 CA ARG C 122 -9.671 67.783 59.506 1.00 56.70 C ANISOU 3926 CA ARG C 122 8855 5021 7669 302 2538 -3051 C ATOM 3927 C ARG C 122 -10.772 66.865 58.954 1.00 61.01 C ANISOU 3927 C ARG C 122 9126 5593 8461 320 2668 -3104 C ATOM 3928 O ARG C 122 -11.145 66.996 57.786 1.00 60.20 O ANISOU 3928 O ARG C 122 8831 5538 8504 360 2540 -3159 O ATOM 3929 CB ARG C 122 -10.286 69.104 60.014 1.00 57.04 C ANISOU 3929 CB ARG C 122 9026 4978 7671 399 2576 -3105 C ATOM 3930 N ASP C 123 -11.309 65.962 59.807 1.00 58.60 N ANISOU 3930 N ASP C 123 8816 5232 8218 317 2932 -3104 N ATOM 3931 CA ASP C 123 -12.387 65.017 59.467 1.00 59.77 C ANISOU 3931 CA ASP C 123 8674 5357 8678 312 3106 -3179 C ATOM 3932 C ASP C 123 -13.667 65.777 59.061 1.00 65.10 C ANISOU 3932 C ASP C 123 9144 5996 9595 409 3128 -3321 C ATOM 3933 O ASP C 123 -14.005 66.770 59.693 1.00 63.12 O ANISOU 3933 O ASP C 123 9041 5689 9253 485 3200 -3328 O ATOM 3934 CB ASP C 123 -12.660 64.077 60.671 1.00 63.10 C ANISOU 3934 CB ASP C 123 9203 5665 9108 306 3471 -3132 C ATOM 3935 CG ASP C 123 -13.675 62.947 60.493 1.00 73.36 C ANISOU 3935 CG ASP C 123 10204 6888 10782 268 3727 -3203 C ATOM 3936 OD1 ASP C 123 -14.192 62.771 59.364 1.00 74.08 O ANISOU 3936 OD1 ASP C 123 9961 7032 11155 249 3565 -3323 O ATOM 3937 OD2 ASP C 123 -13.922 62.214 61.473 1.00 79.06 O ANISOU 3937 OD2 ASP C 123 11038 7477 11522 278 4091 -3150 O ATOM 3938 N SER C 124 -14.360 65.308 57.998 1.00 64.63 N ANISOU 3938 N SER C 124 8752 5969 9836 433 3035 -3452 N ATOM 3939 CA SER C 124 -15.600 65.911 57.486 1.00 66.73 C ANISOU 3939 CA SER C 124 8782 6210 10364 560 3005 -3642 C ATOM 3940 C SER C 124 -16.772 65.733 58.480 1.00 75.68 C ANISOU 3940 C SER C 124 9793 7206 11757 567 3380 -3711 C ATOM 3941 O SER C 124 -17.744 66.487 58.426 1.00 76.32 O ANISOU 3941 O SER C 124 9753 7255 11991 679 3405 -3846 O ATOM 3942 CB SER C 124 -15.962 65.319 56.127 1.00 69.24 C ANISOU 3942 CB SER C 124 8787 6581 10941 625 2769 -3800 C ATOM 3943 OG SER C 124 -16.320 63.951 56.228 1.00 77.58 O ANISOU 3943 OG SER C 124 9601 7581 12296 528 2925 -3849 O ATOM 3944 N LYS C 125 -16.661 64.732 59.377 1.00 75.17 N ANISOU 3944 N LYS C 125 9781 7047 11735 468 3695 -3612 N ATOM 3945 CA LYS C 125 -17.626 64.406 60.426 1.00 79.01 C ANISOU 3945 CA LYS C 125 10210 7353 12459 481 4150 -3624 C ATOM 3946 C LYS C 125 -16.844 64.170 61.736 1.00 85.28 C ANISOU 3946 C LYS C 125 11439 8068 12897 478 4405 -3409 C ATOM 3947 O LYS C 125 -16.783 63.041 62.243 1.00 86.87 O ANISOU 3947 O LYS C 125 11667 8165 13175 426 4698 -3343 O ATOM 3948 CB LYS C 125 -18.476 63.184 60.016 1.00 83.07 C ANISOU 3948 CB LYS C 125 10292 7770 13499 408 4324 -3771 C ATOM 3949 N SER C 126 -16.201 65.248 62.245 1.00 80.39 N ANISOU 3949 N SER C 126 11178 7489 11876 559 4267 -3317 N ATOM 3950 CA SER C 126 -15.355 65.261 63.444 1.00113.22 C ANISOU 3950 CA SER C 126 15794 11584 15640 625 4386 -3161 C ATOM 3951 C SER C 126 -16.150 64.932 64.705 1.00143.85 C ANISOU 3951 C SER C 126 19827 15241 19587 752 4902 -3100 C ATOM 3952 O SER C 126 -15.653 64.208 65.565 1.00104.34 O ANISOU 3952 O SER C 126 15120 10139 14385 814 5125 -2990 O ATOM 3953 CB SER C 126 -14.676 66.619 63.600 1.00115.86 C ANISOU 3953 CB SER C 126 16403 11985 15632 696 4087 -3137 C ATOM 3954 OG SER C 126 -13.706 66.614 64.635 1.00124.79 O ANISOU 3954 OG SER C 126 17957 13066 16392 778 4091 -3038 O ATOM 3955 N LYS C 129 -10.979 64.441 64.911 1.00 68.12 N ANISOU 3955 N LYS C 129 11127 6010 8746 675 3871 -2918 N ATOM 3956 CA LYS C 129 -9.980 63.611 64.232 1.00 66.11 C ANISOU 3956 CA LYS C 129 10787 5892 8441 542 3661 -2899 C ATOM 3957 C LYS C 129 -9.285 64.373 63.099 1.00 67.47 C ANISOU 3957 C LYS C 129 10775 6216 8646 411 3246 -2930 C ATOM 3958 O LYS C 129 -9.921 65.148 62.375 1.00 65.92 O ANISOU 3958 O LYS C 129 10369 6039 8637 377 3172 -2972 O ATOM 3959 CB LYS C 129 -10.622 62.341 63.687 1.00 66.72 C ANISOU 3959 CB LYS C 129 10594 5967 8790 441 3890 -2883 C ATOM 3960 N SER C 130 -7.972 64.144 62.954 1.00 63.27 N ANISOU 3960 N SER C 130 10336 5775 7931 361 2997 -2911 N ATOM 3961 CA SER C 130 -7.168 64.770 61.906 1.00 61.05 C ANISOU 3961 CA SER C 130 9903 5599 7692 245 2663 -2915 C ATOM 3962 C SER C 130 -6.075 63.815 61.383 1.00 61.26 C ANISOU 3962 C SER C 130 9882 5745 7649 154 2514 -2864 C ATOM 3963 O SER C 130 -5.743 62.819 62.033 1.00 59.94 O ANISOU 3963 O SER C 130 9869 5582 7325 197 2615 -2847 O ATOM 3964 CB SER C 130 -6.549 66.078 62.400 1.00 65.41 C ANISOU 3964 CB SER C 130 10640 6093 8121 294 2471 -2971 C ATOM 3965 OG SER C 130 -5.420 65.870 63.233 1.00 75.76 O ANISOU 3965 OG SER C 130 12190 7390 9207 352 2339 -3010 O ATOM 3966 N VAL C 131 -5.553 64.120 60.189 1.00 56.15 N ANISOU 3966 N VAL C 131 9046 5182 7106 54 2298 -2832 N ATOM 3967 CA VAL C 131 -4.450 63.402 59.544 1.00 54.58 C ANISOU 3967 CA VAL C 131 8788 5094 6856 -27 2136 -2767 C ATOM 3968 C VAL C 131 -3.435 64.437 59.042 1.00 58.31 C ANISOU 3968 C VAL C 131 9238 5559 7357 -81 1906 -2765 C ATOM 3969 O VAL C 131 -3.798 65.592 58.784 1.00 57.98 O ANISOU 3969 O VAL C 131 9169 5441 7419 -68 1886 -2793 O ATOM 3970 CB VAL C 131 -4.859 62.403 58.408 1.00 56.90 C ANISOU 3970 CB VAL C 131 8858 5477 7284 -70 2161 -2697 C ATOM 3971 CG1 VAL C 131 -5.694 61.241 58.939 1.00 57.26 C ANISOU 3971 CG1 VAL C 131 8906 5501 7351 -48 2409 -2708 C ATOM 3972 CG2 VAL C 131 -5.559 63.101 57.242 1.00 56.27 C ANISOU 3972 CG2 VAL C 131 8581 5385 7413 -46 2099 -2704 C ATOM 3973 N CYS C 132 -2.174 64.018 58.908 1.00 55.08 N ANISOU 3973 N CYS C 132 8838 5214 6876 -137 1756 -2737 N ATOM 3974 CA CYS C 132 -1.114 64.851 58.365 1.00 55.54 C ANISOU 3974 CA CYS C 132 8830 5239 7033 -208 1583 -2729 C ATOM 3975 C CYS C 132 -0.781 64.346 56.977 1.00 54.63 C ANISOU 3975 C CYS C 132 8546 5203 7006 -252 1554 -2587 C ATOM 3976 O CYS C 132 -0.668 63.136 56.769 1.00 53.33 O ANISOU 3976 O CYS C 132 8358 5154 6753 -253 1562 -2524 O ATOM 3977 CB CYS C 132 0.111 64.874 59.273 1.00 57.98 C ANISOU 3977 CB CYS C 132 9252 5531 7245 -216 1422 -2837 C ATOM 3978 SG CYS C 132 -0.215 65.537 60.925 1.00 64.76 S ANISOU 3978 SG CYS C 132 10378 6266 7962 -80 1409 -3021 S ATOM 3979 N LEU C 133 -0.680 65.268 56.015 1.00 48.64 N ANISOU 3979 N LEU C 133 7706 4368 6407 -257 1540 -2530 N ATOM 3980 CA LEU C 133 -0.372 64.923 54.642 1.00 46.37 C ANISOU 3980 CA LEU C 133 7315 4118 6187 -232 1529 -2382 C ATOM 3981 C LEU C 133 0.934 65.551 54.201 1.00 49.93 C ANISOU 3981 C LEU C 133 7730 4481 6761 -299 1484 -2323 C ATOM 3982 O LEU C 133 1.016 66.772 54.094 1.00 50.52 O ANISOU 3982 O LEU C 133 7820 4401 6973 -308 1526 -2350 O ATOM 3983 CB LEU C 133 -1.516 65.338 53.689 1.00 45.75 C ANISOU 3983 CB LEU C 133 7203 3998 6183 -100 1597 -2354 C ATOM 3984 CG LEU C 133 -1.292 65.088 52.178 1.00 48.76 C ANISOU 3984 CG LEU C 133 7541 4382 6603 18 1577 -2206 C ATOM 3985 CD1 LEU C 133 -1.605 63.650 51.796 1.00 46.83 C ANISOU 3985 CD1 LEU C 133 7231 4279 6283 67 1522 -2165 C ATOM 3986 CD2 LEU C 133 -2.111 66.038 51.339 1.00 50.66 C ANISOU 3986 CD2 LEU C 133 7822 4514 6914 194 1625 -2218 C ATOM 3987 N PHE C 134 1.943 64.706 53.917 1.00 44.90 N ANISOU 3987 N PHE C 134 7038 3928 6093 -343 1421 -2240 N ATOM 3988 CA PHE C 134 3.210 65.133 53.327 1.00 44.57 C ANISOU 3988 CA PHE C 134 6918 3795 6221 -401 1419 -2160 C ATOM 3989 C PHE C 134 3.021 65.006 51.828 1.00 47.55 C ANISOU 3989 C PHE C 134 7292 4150 6626 -269 1517 -1955 C ATOM 3990 O PHE C 134 2.748 63.903 51.369 1.00 44.84 O ANISOU 3990 O PHE C 134 6953 3948 6137 -190 1477 -1869 O ATOM 3991 CB PHE C 134 4.403 64.293 53.838 1.00 45.46 C ANISOU 3991 CB PHE C 134 6977 4012 6284 -487 1292 -2194 C ATOM 3992 CG PHE C 134 5.774 64.661 53.305 1.00 47.41 C ANISOU 3992 CG PHE C 134 7091 4156 6765 -562 1300 -2132 C ATOM 3993 CD1 PHE C 134 6.107 65.987 53.037 1.00 51.29 C ANISOU 3993 CD1 PHE C 134 7521 4414 7551 -614 1403 -2148 C ATOM 3994 CD2 PHE C 134 6.749 63.688 53.123 1.00 49.30 C ANISOU 3994 CD2 PHE C 134 7262 4516 6955 -584 1226 -2069 C ATOM 3995 CE1 PHE C 134 7.371 66.325 52.550 1.00 53.55 C ANISOU 3995 CE1 PHE C 134 7655 4563 8127 -694 1466 -2093 C ATOM 3996 CE2 PHE C 134 8.018 64.029 52.645 1.00 53.42 C ANISOU 3996 CE2 PHE C 134 7628 4926 7745 -656 1262 -2019 C ATOM 3997 CZ PHE C 134 8.319 65.345 52.360 1.00 53.36 C ANISOU 3997 CZ PHE C 134 7535 4661 8077 -716 1397 -2031 C ATOM 3998 N THR C 135 3.076 66.122 51.064 1.00 45.34 N ANISOU 3998 N THR C 135 7038 3677 6514 -206 1651 -1884 N ATOM 3999 CA THR C 135 2.817 66.031 49.625 1.00 44.88 C ANISOU 3999 CA THR C 135 7049 3571 6431 7 1749 -1697 C ATOM 4000 C THR C 135 3.733 66.934 48.778 1.00 52.04 C ANISOU 4000 C THR C 135 7984 4241 7547 47 1946 -1550 C ATOM 4001 O THR C 135 4.447 67.784 49.316 1.00 53.47 O ANISOU 4001 O THR C 135 8093 4275 7949 -121 2012 -1622 O ATOM 4002 CB THR C 135 1.323 66.339 49.338 1.00 51.52 C ANISOU 4002 CB THR C 135 7984 4410 7180 188 1750 -1764 C ATOM 4003 OG1 THR C 135 1.024 66.065 47.969 1.00 51.21 O ANISOU 4003 OG1 THR C 135 8039 4344 7075 460 1778 -1623 O ATOM 4004 CG2 THR C 135 0.922 67.774 49.687 1.00 50.71 C ANISOU 4004 CG2 THR C 135 7946 4138 7182 175 1847 -1867 C ATOM 4005 N ASP C 136 3.692 66.720 47.434 1.00 46.23 N ANISOU 4005 N ASP C 136 6138 3883 7544 -221 635 -1558 N ATOM 4006 CA ASP C 136 4.369 67.500 46.389 1.00 46.60 C ANISOU 4006 CA ASP C 136 6070 3916 7720 -410 515 -1447 C ATOM 4007 C ASP C 136 5.905 67.478 46.476 1.00 50.37 C ANISOU 4007 C ASP C 136 6610 4519 8010 -456 437 -1668 C ATOM 4008 O ASP C 136 6.566 68.320 45.860 1.00 51.60 O ANISOU 4008 O ASP C 136 6674 4676 8254 -613 321 -1615 O ATOM 4009 CB ASP C 136 3.844 68.955 46.371 1.00 50.10 C ANISOU 4009 CB ASP C 136 6381 4079 8576 -406 513 -1333 C ATOM 4010 CG ASP C 136 2.383 69.064 45.980 1.00 60.05 C ANISOU 4010 CG ASP C 136 7489 5240 10087 -397 564 -1006 C ATOM 4011 OD1 ASP C 136 1.868 68.122 45.339 1.00 59.79 O ANISOU 4011 OD1 ASP C 136 7443 5399 9877 -514 544 -784 O ATOM 4012 OD2 ASP C 136 1.761 70.102 46.290 1.00 64.23 O ANISOU 4012 OD2 ASP C 136 7912 5494 11001 -286 624 -954 O ATOM 4013 N PHE C 137 6.467 66.481 47.171 1.00 45.45 N ANISOU 4013 N PHE C 137 6114 4025 7130 -346 473 -1866 N ATOM 4014 CA PHE C 137 7.911 66.293 47.268 1.00 44.45 C ANISOU 4014 CA PHE C 137 6008 4050 6831 -372 408 -2021 C ATOM 4015 C PHE C 137 8.421 65.562 46.016 1.00 49.08 C ANISOU 4015 C PHE C 137 6518 4854 7276 -490 360 -1949 C ATOM 4016 O PHE C 137 7.635 64.892 45.325 1.00 45.97 O ANISOU 4016 O PHE C 137 6132 4489 6845 -544 392 -1821 O ATOM 4017 CB PHE C 137 8.288 65.528 48.551 1.00 45.08 C ANISOU 4017 CB PHE C 137 6215 4165 6749 -232 448 -2212 C ATOM 4018 CG PHE C 137 7.581 64.208 48.771 1.00 45.01 C ANISOU 4018 CG PHE C 137 6282 4201 6619 -135 476 -2198 C ATOM 4019 CD1 PHE C 137 8.137 63.015 48.315 1.00 46.73 C ANISOU 4019 CD1 PHE C 137 6519 4554 6684 -108 433 -2213 C ATOM 4020 CD2 PHE C 137 6.386 64.151 49.481 1.00 46.87 C ANISOU 4020 CD2 PHE C 137 6575 4346 6887 -72 541 -2180 C ATOM 4021 CE1 PHE C 137 7.497 61.793 48.539 1.00 46.77 C ANISOU 4021 CE1 PHE C 137 6633 4568 6571 -40 418 -2191 C ATOM 4022 CE2 PHE C 137 5.744 62.929 49.704 1.00 48.86 C ANISOU 4022 CE2 PHE C 137 6910 4673 6982 -24 516 -2136 C ATOM 4023 CZ PHE C 137 6.302 61.758 49.230 1.00 46.23 C ANISOU 4023 CZ PHE C 137 6629 4439 6496 -17 436 -2134 C ATOM 4024 N ASP C 138 9.734 65.700 45.718 1.00 48.55 N ANISOU 4024 N ASP C 138 6381 4961 7107 -556 295 -2029 N ATOM 4025 CA ASP C 138 10.352 65.025 44.576 1.00 49.96 C ANISOU 4025 CA ASP C 138 6468 5378 7136 -664 293 -2030 C ATOM 4026 C ASP C 138 10.479 63.524 44.893 1.00 54.75 C ANISOU 4026 C ASP C 138 7179 6016 7606 -471 385 -2164 C ATOM 4027 O ASP C 138 10.458 63.130 46.063 1.00 53.70 O ANISOU 4027 O ASP C 138 7146 5782 7476 -288 391 -2244 O ATOM 4028 CB ASP C 138 11.699 65.662 44.184 1.00 53.45 C ANISOU 4028 CB ASP C 138 6764 6041 7502 -789 199 -2064 C ATOM 4029 CG ASP C 138 12.777 65.629 45.242 1.00 72.48 C ANISOU 4029 CG ASP C 138 9199 8501 9838 -638 181 -2183 C ATOM 4030 OD1 ASP C 138 12.602 66.297 46.298 1.00 75.95 O ANISOU 4030 OD1 ASP C 138 9744 8763 10352 -598 152 -2189 O ATOM 4031 OD2 ASP C 138 13.833 65.017 44.986 1.00 80.32 O ANISOU 4031 OD2 ASP C 138 10093 9725 10701 -592 200 -2258 O ATOM 4032 N SER C 139 10.571 62.690 43.855 1.00 53.24 N ANISOU 4032 N SER C 139 6974 5955 7298 -548 446 -2187 N ATOM 4033 CA SER C 139 10.597 61.233 44.006 1.00 53.58 C ANISOU 4033 CA SER C 139 7146 5969 7243 -375 524 -2310 C ATOM 4034 C SER C 139 11.905 60.691 44.642 1.00 61.97 C ANISOU 4034 C SER C 139 8146 7097 8304 -152 528 -2482 C ATOM 4035 O SER C 139 11.934 59.523 45.045 1.00 61.95 O ANISOU 4035 O SER C 139 8244 7003 8292 31 548 -2565 O ATOM 4036 CB SER C 139 10.323 60.565 42.667 1.00 54.67 C ANISOU 4036 CB SER C 139 7320 6201 7250 -561 617 -2309 C ATOM 4037 OG SER C 139 9.022 60.912 42.222 1.00 50.92 O ANISOU 4037 OG SER C 139 6907 5659 6782 -782 592 -2074 O ATOM 4038 N GLN C 140 12.941 61.545 44.798 1.00 61.40 N ANISOU 4038 N GLN C 140 7907 7172 8250 -181 477 -2489 N ATOM 4039 CA GLN C 140 14.207 61.185 45.454 1.00 63.64 C ANISOU 4039 CA GLN C 140 8085 7551 8543 -8 461 -2562 C ATOM 4040 C GLN C 140 14.042 61.156 46.994 1.00 68.69 C ANISOU 4040 C GLN C 140 8825 8028 9246 95 372 -2516 C ATOM 4041 O GLN C 140 14.904 60.616 47.691 1.00 69.74 O ANISOU 4041 O GLN C 140 8887 8199 9411 220 335 -2521 O ATOM 4042 CB GLN C 140 15.332 62.154 45.053 1.00 66.09 C ANISOU 4042 CB GLN C 140 8187 8130 8793 -140 414 -2526 C ATOM 4043 N THR C 141 12.933 61.729 47.515 1.00 64.25 N ANISOU 4043 N THR C 141 8403 7301 8708 16 343 -2460 N ATOM 4044 CA THR C 141 12.610 61.738 48.943 1.00 63.43 C ANISOU 4044 CA THR C 141 8403 7075 8622 44 286 -2451 C ATOM 4045 C THR C 141 12.016 60.374 49.340 1.00 66.96 C ANISOU 4045 C THR C 141 8956 7424 9060 171 263 -2472 C ATOM 4046 O THR C 141 11.059 59.908 48.717 1.00 65.63 O ANISOU 4046 O THR C 141 8884 7186 8865 182 302 -2458 O ATOM 4047 CB THR C 141 11.657 62.898 49.271 1.00 68.21 C ANISOU 4047 CB THR C 141 9093 7552 9271 -72 306 -2424 C ATOM 4048 OG1 THR C 141 12.243 64.130 48.850 1.00 69.23 O ANISOU 4048 OG1 THR C 141 9144 7740 9422 -204 281 -2390 O ATOM 4049 CG2 THR C 141 11.296 62.968 50.752 1.00 65.87 C ANISOU 4049 CG2 THR C 141 8906 7165 8956 -91 290 -2467 C ATOM 4050 N ASN C 142 12.581 59.754 50.386 1.00 64.39 N ANISOU 4050 N ASN C 142 8613 7103 8748 221 168 -2463 N ATOM 4051 CA ASN C 142 12.125 58.478 50.925 1.00 64.37 C ANISOU 4051 CA ASN C 142 8701 7009 8748 302 71 -2451 C ATOM 4052 C ASN C 142 11.343 58.716 52.219 1.00 68.37 C ANISOU 4052 C ASN C 142 9302 7489 9185 162 -10 -2423 C ATOM 4053 O ASN C 142 11.789 59.492 53.072 1.00 68.43 O ANISOU 4053 O ASN C 142 9269 7555 9175 22 -21 -2418 O ATOM 4054 CB ASN C 142 13.313 57.532 51.158 1.00 68.63 C ANISOU 4054 CB ASN C 142 9109 7572 9397 428 -15 -2426 C ATOM 4055 CG ASN C 142 14.161 57.263 49.930 1.00 96.95 C ANISOU 4055 CG ASN C 142 12569 11215 13052 583 109 -2501 C ATOM 4056 OD1 ASN C 142 15.386 57.431 49.948 1.00 93.58 O ANISOU 4056 OD1 ASN C 142 11939 10917 12698 631 118 -2467 O ATOM 4057 ND2 ASN C 142 13.537 56.838 48.833 1.00 88.75 N ANISOU 4057 ND2 ASN C 142 11640 10113 11967 631 215 -2596 N ATOM 4058 N VAL C 143 10.157 58.088 52.347 1.00 64.25 N ANISOU 4058 N VAL C 143 8917 6906 8591 163 -57 -2404 N ATOM 4059 CA VAL C 143 9.315 58.241 53.537 1.00 63.72 C ANISOU 4059 CA VAL C 143 8919 6869 8425 16 -119 -2397 C ATOM 4060 C VAL C 143 9.539 57.017 54.427 1.00 70.13 C ANISOU 4060 C VAL C 143 9735 7707 9206 -35 -355 -2328 C ATOM 4061 O VAL C 143 9.301 55.883 54.006 1.00 70.20 O ANISOU 4061 O VAL C 143 9813 7646 9214 68 -470 -2275 O ATOM 4062 CB VAL C 143 7.812 58.498 53.224 1.00 66.18 C ANISOU 4062 CB VAL C 143 9331 7158 8657 9 -35 -2376 C ATOM 4063 CG1 VAL C 143 7.017 58.756 54.505 1.00 66.28 C ANISOU 4063 CG1 VAL C 143 9372 7251 8560 -141 -57 -2411 C ATOM 4064 CG2 VAL C 143 7.638 59.665 52.254 1.00 65.48 C ANISOU 4064 CG2 VAL C 143 9199 7013 8668 42 154 -2386 C ATOM 4065 N SER C 144 10.036 57.264 55.647 1.00 68.66 N ANISOU 4065 N SER C 144 9479 7614 8994 -234 -444 -2311 N ATOM 4066 CA SER C 144 10.364 56.249 56.645 1.00 70.12 C ANISOU 4066 CA SER C 144 9615 7851 9175 -377 -714 -2193 C ATOM 4067 C SER C 144 9.208 56.012 57.603 1.00 75.12 C ANISOU 4067 C SER C 144 10336 8599 9608 -603 -833 -2192 C ATOM 4068 O SER C 144 8.424 56.928 57.861 1.00 74.49 O ANISOU 4068 O SER C 144 10310 8587 9405 -693 -657 -2311 O ATOM 4069 CB SER C 144 11.599 56.672 57.436 1.00 75.57 C ANISOU 4069 CB SER C 144 10159 8631 9922 -564 -761 -2117 C ATOM 4070 OG SER C 144 12.690 56.979 56.581 1.00 85.60 O ANISOU 4070 OG SER C 144 11319 9861 11343 -372 -650 -2100 O ATOM 4071 N GLN C 145 9.111 54.782 58.138 1.00 73.31 N ANISOU 4071 N GLN C 145 10103 8395 9357 -700 -1141 -2054 N ATOM 4072 CA GLN C 145 8.091 54.390 59.115 1.00 73.73 C ANISOU 4072 CA GLN C 145 10209 8626 9180 -976 -1329 -2018 C ATOM 4073 C GLN C 145 8.418 55.031 60.481 1.00 79.76 C ANISOU 4073 C GLN C 145 10875 9597 9835 -1379 -1346 -2046 C ATOM 4074 O GLN C 145 9.594 55.288 60.771 1.00 80.69 O ANISOU 4074 O GLN C 145 10880 9699 10080 -1473 -1358 -1981 O ATOM 4075 CB GLN C 145 8.012 52.851 59.212 1.00 75.75 C ANISOU 4075 CB GLN C 145 10493 8829 9459 -990 -1714 -1829 C ATOM 4076 CG GLN C 145 6.706 52.300 59.808 1.00 90.30 C ANISOU 4076 CG GLN C 145 12434 10866 11010 -1217 -1933 -1767 C ATOM 4077 CD GLN C 145 5.464 52.598 58.992 1.00106.28 C ANISOU 4077 CD GLN C 145 14613 12905 12865 -1044 -1729 -1833 C ATOM 4078 OE1 GLN C 145 5.461 52.535 57.757 1.00101.67 O ANISOU 4078 OE1 GLN C 145 14129 12119 12382 -748 -1579 -1844 O ATOM 4079 NE2 GLN C 145 4.369 52.905 59.676 1.00 95.74 N ANISOU 4079 NE2 GLN C 145 13282 11836 11260 -1261 -1723 -1856 N ATOM 4080 N SER C 146 7.381 55.322 61.295 1.00 95.92 N ANISOU 4080 N SER C 146 12555 12394 11495 -254 -1586 -504 N ATOM 4081 CA SER C 146 7.544 55.961 62.606 1.00 99.04 C ANISOU 4081 CA SER C 146 12984 13124 11522 -562 -1836 -623 C ATOM 4082 C SER C 146 8.114 55.007 63.655 1.00107.38 C ANISOU 4082 C SER C 146 14161 14409 12230 -430 -2218 -277 C ATOM 4083 O SER C 146 7.842 53.804 63.613 1.00107.39 O ANISOU 4083 O SER C 146 14428 14206 12168 -170 -2177 28 O ATOM 4084 CB SER C 146 6.215 56.516 63.106 1.00101.21 C ANISOU 4084 CB SER C 146 13596 13305 11555 -907 -1582 -902 C ATOM 4085 OG SER C 146 6.414 57.383 64.212 1.00113.19 O ANISOU 4085 OG SER C 146 15102 15128 12776 -1277 -1742 -1114 O ATOM 4086 N LYS C 147 8.885 55.563 64.612 1.00107.58 N ANISOU 4086 N LYS C 147 14006 14865 12006 -625 -2577 -328 N ATOM 4087 CA LYS C 147 9.489 54.824 65.721 1.00112.70 C ANISOU 4087 CA LYS C 147 14739 15831 12251 -526 -3020 9 C ATOM 4088 C LYS C 147 8.410 54.402 66.725 1.00116.42 C ANISOU 4088 C LYS C 147 15806 16235 12193 -743 -2944 57 C ATOM 4089 O LYS C 147 8.409 53.252 67.168 1.00119.05 O ANISOU 4089 O LYS C 147 16435 16509 12290 -497 -3082 458 O ATOM 4090 CB LYS C 147 10.577 55.665 66.410 1.00119.62 C ANISOU 4090 CB LYS C 147 15211 17256 12984 -747 -3421 -131 C ATOM 4091 N ASP C 148 7.482 55.327 67.061 1.00109.65 N ANISOU 4091 N ASP C 148 15138 15348 11175 -1200 -2681 -354 N ATOM 4092 CA ASP C 148 6.372 55.078 67.983 1.00109.48 C ANISOU 4092 CA ASP C 148 15667 15244 10685 -1487 -2525 -412 C ATOM 4093 C ASP C 148 5.330 54.175 67.324 1.00108.09 C ANISOU 4093 C ASP C 148 15821 14589 10660 -1285 -2137 -312 C ATOM 4094 O ASP C 148 4.965 54.399 66.165 1.00103.12 O ANISOU 4094 O ASP C 148 15011 13689 10481 -1165 -1837 -466 O ATOM 4095 CB ASP C 148 5.732 56.400 68.440 1.00110.27 C ANISOU 4095 CB ASP C 148 15800 15427 10671 -2025 -2301 -928 C ATOM 4096 N SER C 149 4.867 53.146 68.058 1.00105.74 N ANISOU 4096 N SER C 149 16017 14199 9961 -1264 -2136 -57 N ATOM 4097 CA SER C 149 3.870 52.179 67.581 1.00102.33 C ANISOU 4097 CA SER C 149 15948 13330 9603 -1132 -1743 18 C ATOM 4098 C SER C 149 2.463 52.805 67.494 1.00 99.98 C ANISOU 4098 C SER C 149 15818 12849 9320 -1510 -1291 -453 C ATOM 4099 O SER C 149 1.620 52.306 66.743 1.00 96.42 O ANISOU 4099 O SER C 149 15478 12075 9081 -1422 -928 -523 O ATOM 4100 CB SER C 149 3.845 50.950 68.485 1.00110.76 C ANISOU 4100 CB SER C 149 17530 14342 10211 -1032 -1849 424 C ATOM 4101 OG SER C 149 3.094 49.898 67.902 1.00118.40 O ANISOU 4101 OG SER C 149 18806 14868 11311 -860 -1455 524 O ATOM 4102 N ASP C 150 2.226 53.897 68.255 1.00 95.21 N ANISOU 4102 N ASP C 150 15204 12465 8505 -1934 -1303 -792 N ATOM 4103 CA ASP C 150 0.962 54.640 68.301 1.00 91.30 C ANISOU 4103 CA ASP C 150 14814 11824 8052 -2296 -887 -1260 C ATOM 4104 C ASP C 150 0.853 55.663 67.144 1.00 87.58 C ANISOU 4104 C ASP C 150 13880 11259 8136 -2218 -710 -1535 C ATOM 4105 O ASP C 150 -0.200 56.286 66.978 1.00 85.07 O ANISOU 4105 O ASP C 150 13574 10791 7958 -2418 -359 -1890 O ATOM 4106 CB ASP C 150 0.817 55.348 69.659 1.00 96.66 C ANISOU 4106 CB ASP C 150 15705 12752 8268 -2794 -939 -1502 C ATOM 4107 N VAL C 151 1.933 55.820 66.345 1.00 80.31 N ANISOU 4107 N VAL C 151 12561 10417 7536 -1917 -939 -1361 N ATOM 4108 CA VAL C 151 1.989 56.724 65.191 1.00 75.05 C ANISOU 4108 CA VAL C 151 11495 9650 7370 -1812 -791 -1551 C ATOM 4109 C VAL C 151 2.049 55.870 63.914 1.00 72.64 C ANISOU 4109 C VAL C 151 11085 9124 7392 -1403 -715 -1316 C ATOM 4110 O VAL C 151 2.954 55.045 63.771 1.00 73.72 O ANISOU 4110 O VAL C 151 11170 9302 7538 -1131 -946 -983 O ATOM 4111 CB VAL C 151 3.173 57.730 65.284 1.00 80.59 C ANISOU 4111 CB VAL C 151 11831 10614 8175 -1887 -1037 -1624 C ATOM 4112 CG1 VAL C 151 3.211 58.659 64.069 1.00 77.12 C ANISOU 4112 CG1 VAL C 151 11049 10015 8239 -1782 -831 -1800 C ATOM 4113 CG2 VAL C 151 3.114 58.544 66.576 1.00 83.57 C ANISOU 4113 CG2 VAL C 151 12332 11232 8189 -2355 -1081 -1895 C ATOM 4114 N TYR C 152 1.086 56.071 62.996 1.00 63.22 N ANISOU 4114 N TYR C 152 9847 7709 6465 -1367 -387 -1497 N ATOM 4115 CA TYR C 152 1.006 55.321 61.734 1.00 59.36 C ANISOU 4115 CA TYR C 152 9274 7031 6251 -1057 -265 -1342 C ATOM 4116 C TYR C 152 1.359 56.204 60.533 1.00 58.60 C ANISOU 4116 C TYR C 152 8799 6900 6567 -922 -218 -1422 C ATOM 4117 O TYR C 152 0.788 57.282 60.376 1.00 56.71 O ANISOU 4117 O TYR C 152 8458 6639 6451 -1060 -65 -1679 O ATOM 4118 CB TYR C 152 -0.398 54.709 61.537 1.00 58.65 C ANISOU 4118 CB TYR C 152 9431 6762 6091 -1129 64 -1474 C ATOM 4119 CG TYR C 152 -0.958 54.015 62.760 1.00 62.43 C ANISOU 4119 CG TYR C 152 10337 7234 6149 -1346 117 -1476 C ATOM 4120 CD1 TYR C 152 -0.487 52.765 63.154 1.00 66.51 C ANISOU 4120 CD1 TYR C 152 11130 7694 6445 -1212 16 -1150 C ATOM 4121 CD2 TYR C 152 -1.973 54.598 63.514 1.00 63.40 C ANISOU 4121 CD2 TYR C 152 10611 7376 6104 -1682 306 -1801 C ATOM 4122 CE1 TYR C 152 -0.997 52.122 64.281 1.00 69.22 C ANISOU 4122 CE1 TYR C 152 11930 8005 6366 -1419 87 -1125 C ATOM 4123 CE2 TYR C 152 -2.504 53.955 64.633 1.00 66.43 C ANISOU 4123 CE2 TYR C 152 11428 7737 6076 -1923 396 -1823 C ATOM 4124 CZ TYR C 152 -2.012 52.718 65.012 1.00 74.58 C ANISOU 4124 CZ TYR C 152 12770 8716 6850 -1795 282 -1474 C ATOM 4125 OH TYR C 152 -2.527 52.082 66.113 1.00 78.58 O ANISOU 4125 OH TYR C 152 13763 9175 6918 -2038 392 -1469 O ATOM 4126 N ILE C 153 2.306 55.747 59.694 1.00 52.79 N ANISOU 4126 N ILE C 153 7874 6134 6051 -650 -322 -1197 N ATOM 4127 CA ILE C 153 2.724 56.464 58.483 1.00 49.90 C ANISOU 4127 CA ILE C 153 7196 5714 6051 -527 -254 -1244 C ATOM 4128 C ILE C 153 2.620 55.502 57.304 1.00 51.28 C ANISOU 4128 C ILE C 153 7372 5723 6390 -295 -107 -1096 C ATOM 4129 O ILE C 153 3.158 54.392 57.357 1.00 51.64 O ANISOU 4129 O ILE C 153 7493 5725 6405 -135 -175 -867 O ATOM 4130 CB ILE C 153 4.148 57.117 58.566 1.00 54.40 C ANISOU 4130 CB ILE C 153 7470 6435 6765 -504 -484 -1204 C ATOM 4131 CG1 ILE C 153 4.326 57.989 59.839 1.00 56.90 C ANISOU 4131 CG1 ILE C 153 7795 6963 6860 -798 -632 -1379 C ATOM 4132 CG2 ILE C 153 4.455 57.936 57.288 1.00 52.50 C ANISOU 4132 CG2 ILE C 153 6973 6087 6886 -423 -334 -1286 C ATOM 4133 CD1 ILE C 153 5.735 58.536 60.069 1.00 64.19 C ANISOU 4133 CD1 ILE C 153 8411 8109 7871 -832 -876 -1378 C ATOM 4134 N THR C 154 1.929 55.935 56.243 1.00 45.21 N ANISOU 4134 N THR C 154 6526 4864 5789 -279 105 -1222 N ATOM 4135 CA THR C 154 1.777 55.146 55.022 1.00 44.22 C ANISOU 4135 CA THR C 154 6391 4620 5791 -125 271 -1136 C ATOM 4136 C THR C 154 3.049 55.243 54.178 1.00 49.96 C ANISOU 4136 C THR C 154 6881 5312 6788 39 214 -1004 C ATOM 4137 O THR C 154 3.952 56.026 54.489 1.00 50.98 O ANISOU 4137 O THR C 154 6828 5521 7020 24 57 -1010 O ATOM 4138 CB THR C 154 0.563 55.625 54.197 1.00 47.53 C ANISOU 4138 CB THR C 154 6790 5025 6244 -179 474 -1313 C ATOM 4139 OG1 THR C 154 0.866 56.897 53.608 1.00 46.82 O ANISOU 4139 OG1 THR C 154 6492 4940 6355 -149 461 -1363 O ATOM 4140 CG2 THR C 154 -0.716 55.684 55.002 1.00 43.53 C ANISOU 4140 CG2 THR C 154 6445 4562 5531 -353 559 -1502 C ATOM 4141 N ASP C 155 3.101 54.475 53.091 1.00 47.02 N ANISOU 4141 N ASP C 155 6506 4826 6532 154 379 -927 N ATOM 4142 CA ASP C 155 4.197 54.544 52.141 1.00 47.79 C ANISOU 4142 CA ASP C 155 6393 4862 6903 279 403 -844 C ATOM 4143 C ASP C 155 3.906 55.711 51.180 1.00 48.77 C ANISOU 4143 C ASP C 155 6406 4992 7133 219 505 -970 C ATOM 4144 O ASP C 155 2.802 56.266 51.203 1.00 45.60 O ANISOU 4144 O ASP C 155 6082 4635 6607 132 555 -1088 O ATOM 4145 CB ASP C 155 4.341 53.197 51.398 1.00 50.69 C ANISOU 4145 CB ASP C 155 6842 5079 7339 391 596 -731 C ATOM 4146 CG ASP C 155 5.610 53.035 50.570 1.00 71.68 C ANISOU 4146 CG ASP C 155 9287 7644 10304 525 649 -642 C ATOM 4147 OD1 ASP C 155 6.610 53.750 50.853 1.00 73.75 O ANISOU 4147 OD1 ASP C 155 9317 7980 10724 563 473 -628 O ATOM 4148 OD2 ASP C 155 5.610 52.189 49.647 1.00 83.02 O ANISOU 4148 OD2 ASP C 155 10779 8937 11828 561 895 -619 O ATOM 4149 N LYS C 156 4.898 56.099 50.367 1.00 47.13 N ANISOU 4149 N LYS C 156 6017 4729 7160 274 546 -939 N ATOM 4150 CA LYS C 156 4.768 57.140 49.356 1.00 46.54 C ANISOU 4150 CA LYS C 156 5886 4616 7180 236 671 -1008 C ATOM 4151 C LYS C 156 3.879 56.620 48.225 1.00 50.57 C ANISOU 4151 C LYS C 156 6518 5105 7590 240 856 -999 C ATOM 4152 O LYS C 156 4.052 55.488 47.779 1.00 49.76 O ANISOU 4152 O LYS C 156 6463 4951 7493 269 966 -949 O ATOM 4153 CB LYS C 156 6.150 57.558 48.830 1.00 50.42 C ANISOU 4153 CB LYS C 156 6180 5041 7938 257 704 -993 C ATOM 4154 N CYS C 157 2.901 57.429 47.805 1.00 48.87 N ANISOU 4154 N CYS C 157 6348 4941 7279 211 894 -1054 N ATOM 4155 CA CYS C 157 1.952 57.111 46.735 1.00 49.60 C ANISOU 4155 CA CYS C 157 6515 5102 7227 199 1017 -1059 C ATOM 4156 C CYS C 157 1.979 58.207 45.670 1.00 48.25 C ANISOU 4156 C CYS C 157 6319 4907 7105 233 1077 -1007 C ATOM 4157 O CYS C 157 2.202 59.368 46.011 1.00 47.37 O ANISOU 4157 O CYS C 157 6167 4723 7106 263 1036 -1005 O ATOM 4158 CB CYS C 157 0.551 56.937 47.310 1.00 52.15 C ANISOU 4158 CB CYS C 157 6902 5563 7352 160 975 -1159 C ATOM 4159 SG CYS C 157 0.121 55.226 47.702 1.00 57.74 S ANISOU 4159 SG CYS C 157 7746 6298 7896 72 1066 -1218 S ATOM 4160 N VAL C 158 1.743 57.848 44.391 1.00 41.37 N ANISOU 4160 N VAL C 158 5499 4091 6130 209 1196 -965 N ATOM 4161 CA VAL C 158 1.724 58.815 43.286 1.00 40.93 C ANISOU 4161 CA VAL C 158 5475 4020 6055 244 1254 -870 C ATOM 4162 C VAL C 158 0.331 58.934 42.719 1.00 43.50 C ANISOU 4162 C VAL C 158 5824 4569 6134 279 1198 -849 C ATOM 4163 O VAL C 158 -0.223 57.934 42.257 1.00 41.81 O ANISOU 4163 O VAL C 158 5628 4530 5729 183 1237 -913 O ATOM 4164 CB VAL C 158 2.704 58.491 42.127 1.00 46.00 C ANISOU 4164 CB VAL C 158 6166 4567 6745 164 1438 -825 C ATOM 4165 CG1 VAL C 158 3.007 59.739 41.300 1.00 46.84 C ANISOU 4165 CG1 VAL C 158 6345 4571 6881 196 1510 -712 C ATOM 4166 CG2 VAL C 158 3.978 57.839 42.621 1.00 46.14 C ANISOU 4166 CG2 VAL C 158 6098 4428 7004 131 1503 -877 C ATOM 4167 N LEU C 159 -0.210 60.159 42.670 1.00 40.61 N ANISOU 4167 N LEU C 159 5447 4200 5782 415 1128 -763 N ATOM 4168 CA LEU C 159 -1.507 60.358 42.036 1.00 41.73 C ANISOU 4168 CA LEU C 159 5558 4588 5708 500 1040 -707 C ATOM 4169 C LEU C 159 -1.291 61.104 40.726 1.00 46.62 C ANISOU 4169 C LEU C 159 6284 5187 6242 573 1083 -495 C ATOM 4170 O LEU C 159 -0.321 61.851 40.590 1.00 45.98 O ANISOU 4170 O LEU C 159 6301 4838 6329 593 1195 -406 O ATOM 4171 CB LEU C 159 -2.547 61.051 42.950 1.00 42.37 C ANISOU 4171 CB LEU C 159 5527 4715 5856 640 929 -755 C ATOM 4172 CG LEU C 159 -2.271 62.453 43.490 1.00 47.87 C ANISOU 4172 CG LEU C 159 6242 5149 6797 782 962 -683 C ATOM 4173 CD1 LEU C 159 -2.726 63.533 42.503 1.00 50.08 C ANISOU 4173 CD1 LEU C 159 6562 5416 7050 1002 956 -447 C ATOM 4174 CD2 LEU C 159 -3.012 62.654 44.798 1.00 49.24 C ANISOU 4174 CD2 LEU C 159 6314 5325 7071 798 921 -851 C ATOM 4175 N ASP C 160 -2.178 60.891 39.763 1.00 44.82 N ANISOU 4175 N ASP C 160 6045 5255 5729 589 1004 -423 N ATOM 4176 CA ASP C 160 -2.066 61.529 38.463 1.00 46.55 C ANISOU 4176 CA ASP C 160 6404 5503 5781 651 1020 -189 C ATOM 4177 C ASP C 160 -3.349 62.279 38.144 1.00 51.58 C ANISOU 4177 C ASP C 160 6948 6378 6271 900 817 -18 C ATOM 4178 O ASP C 160 -4.406 61.661 37.980 1.00 51.81 O ANISOU 4178 O ASP C 160 6812 6796 6079 875 667 -105 O ATOM 4179 CB ASP C 160 -1.734 60.471 37.387 1.00 48.93 C ANISOU 4179 CB ASP C 160 6798 5974 5817 393 1125 -244 C ATOM 4180 CG ASP C 160 -1.508 60.948 35.955 1.00 61.40 C ANISOU 4180 CG ASP C 160 8578 7605 7146 370 1174 -23 C ATOM 4181 OD1 ASP C 160 -1.422 62.182 35.737 1.00 64.30 O ANISOU 4181 OD1 ASP C 160 9058 7800 7572 579 1153 221 O ATOM 4182 OD2 ASP C 160 -1.399 60.086 35.055 1.00 64.97 O ANISOU 4182 OD2 ASP C 160 9105 8245 7334 123 1267 -97 O ATOM 4183 N MET C 161 -3.252 63.619 38.076 1.00 49.13 N ANISOU 4183 N MET C 161 6733 5828 6107 1146 831 218 N ATOM 4184 CA MET C 161 -4.365 64.497 37.703 1.00 52.32 C ANISOU 4184 CA MET C 161 7063 6391 6426 1467 654 458 C ATOM 4185 C MET C 161 -4.283 64.685 36.186 1.00 59.79 C ANISOU 4185 C MET C 161 8207 7489 7024 1486 614 746 C ATOM 4186 O MET C 161 -3.737 65.674 35.694 1.00 61.27 O ANISOU 4186 O MET C 161 8643 7377 7258 1617 734 1010 O ATOM 4187 CB MET C 161 -4.319 65.825 38.477 1.00 55.24 C ANISOU 4187 CB MET C 161 7464 6366 7161 1727 749 561 C ATOM 4188 CG MET C 161 -4.578 65.665 39.961 1.00 56.03 C ANISOU 4188 CG MET C 161 7370 6383 7537 1685 770 269 C ATOM 4189 SD MET C 161 -4.446 67.230 40.857 1.00 61.06 S ANISOU 4189 SD MET C 161 8070 6532 8597 1909 962 331 S ATOM 4190 CE MET C 161 -6.063 67.886 40.595 1.00 61.48 C ANISOU 4190 CE MET C 161 7915 6793 8650 2329 783 535 C ATOM 4191 N ARG C 162 -4.774 63.664 35.464 1.00 57.42 N ANISOU 4191 N ARG C 162 7821 7646 6350 1299 484 662 N ATOM 4192 CA ARG C 162 -4.753 63.451 34.012 1.00 60.59 C ANISOU 4192 CA ARG C 162 8390 8324 6306 1182 435 840 C ATOM 4193 C ARG C 162 -5.046 64.702 33.157 1.00 69.95 C ANISOU 4193 C ARG C 162 9749 9493 7336 1513 317 1298 C ATOM 4194 O ARG C 162 -4.196 65.061 32.339 1.00 70.40 O ANISOU 4194 O ARG C 162 10148 9334 7266 1425 487 1485 O ATOM 4195 CB ARG C 162 -5.713 62.313 33.637 1.00 61.54 C ANISOU 4195 CB ARG C 162 8276 9041 6065 984 251 637 C ATOM 4196 CG ARG C 162 -5.144 60.950 34.002 1.00 68.44 C ANISOU 4196 CG ARG C 162 9143 9881 6981 579 471 246 C ATOM 4197 CD ARG C 162 -6.207 59.892 34.182 1.00 79.65 C ANISOU 4197 CD ARG C 162 10283 11775 8206 405 354 -47 C ATOM 4198 NE ARG C 162 -5.629 58.655 34.709 1.00 87.85 N ANISOU 4198 NE ARG C 162 11355 12661 9361 73 617 -391 N ATOM 4199 CZ ARG C 162 -6.329 57.574 35.040 1.00104.86 C ANISOU 4199 CZ ARG C 162 13337 15093 11412 -147 642 -709 C ATOM 4200 NH1 ARG C 162 -7.650 57.561 34.901 1.00 93.71 N ANISOU 4200 NH1 ARG C 162 11655 14175 9774 -103 406 -775 N ATOM 4201 NH2 ARG C 162 -5.714 56.498 35.513 1.00 91.04 N ANISOU 4201 NH2 ARG C 162 11675 13122 9796 -406 918 -965 N ATOM 4202 N SER C 163 -6.216 65.356 33.341 1.00 70.51 N ANISOU 4202 N SER C 163 9596 9765 7430 1897 53 1484 N ATOM 4203 CA SER C 163 -6.622 66.549 32.583 1.00 76.31 C ANISOU 4203 CA SER C 163 10473 10484 8037 2298 -84 1974 C ATOM 4204 C SER C 163 -5.667 67.737 32.782 1.00 80.96 C ANISOU 4204 C SER C 163 11418 10387 8955 2457 223 2192 C ATOM 4205 O SER C 163 -5.489 68.535 31.859 1.00 84.54 O ANISOU 4205 O SER C 163 12189 10716 9215 2629 248 2597 O ATOM 4206 CB SER C 163 -8.038 66.968 32.962 1.00 83.72 C ANISOU 4206 CB SER C 163 11024 11722 9063 2710 -393 2079 C ATOM 4207 OG SER C 163 -8.978 66.010 32.507 1.00 96.23 O ANISOU 4207 OG SER C 163 12292 14010 10260 2569 -694 1928 O ATOM 4208 N MET C 164 -5.061 67.847 33.980 1.00 74.06 N ANISOU 4208 N MET C 164 10505 9085 8548 2374 468 1917 N ATOM 4209 CA MET C 164 -4.116 68.909 34.325 1.00 74.09 C ANISOU 4209 CA MET C 164 10799 8453 8897 2442 804 2013 C ATOM 4210 C MET C 164 -2.677 68.519 33.971 1.00 73.79 C ANISOU 4210 C MET C 164 11039 8173 8823 2036 1096 1862 C ATOM 4211 O MET C 164 -1.776 69.350 34.111 1.00 73.31 O ANISOU 4211 O MET C 164 11233 7614 9006 2018 1407 1908 O ATOM 4212 CB MET C 164 -4.224 69.256 35.819 1.00 74.42 C ANISOU 4212 CB MET C 164 10630 8216 9432 2523 910 1762 C ATOM 4213 CG MET C 164 -5.317 70.253 36.112 1.00 82.78 C ANISOU 4213 CG MET C 164 11558 9217 10679 2994 813 1996 C ATOM 4214 SD MET C 164 -5.680 70.390 37.875 1.00 85.44 S ANISOU 4214 SD MET C 164 11589 9361 11514 3006 915 1613 S ATOM 4215 CE MET C 164 -7.462 70.220 37.838 1.00 85.05 C ANISOU 4215 CE MET C 164 11106 9827 11381 3367 540 1697 C ATOM 4216 N ASP C 165 -2.465 67.257 33.506 1.00 65.20 N ANISOU 4216 N ASP C 165 10024 7281 7466 2705 -422 759 N ATOM 4217 CA ASP C 165 -1.163 66.661 33.148 1.00 63.19 C ANISOU 4217 CA ASP C 165 9997 7057 6955 2560 -153 831 C ATOM 4218 C ASP C 165 -0.151 66.870 34.304 1.00 62.45 C ANISOU 4218 C ASP C 165 9777 6746 7205 2306 182 771 C ATOM 4219 O ASP C 165 1.027 67.160 34.074 1.00 62.08 O ANISOU 4219 O ASP C 165 9855 6622 7108 2233 467 983 O ATOM 4220 CB ASP C 165 -0.640 67.232 31.809 1.00 68.81 C ANISOU 4220 CB ASP C 165 11057 7778 7311 2755 -75 1242 C ATOM 4221 N PHE C 166 -0.655 66.746 35.551 1.00 55.99 N ANISOU 4221 N PHE C 166 8686 5867 6722 2166 138 483 N ATOM 4222 CA PHE C 166 0.078 66.942 36.804 1.00 52.50 C ANISOU 4222 CA PHE C 166 8109 5236 6604 1933 371 365 C ATOM 4223 C PHE C 166 0.136 65.643 37.624 1.00 54.11 C ANISOU 4223 C PHE C 166 8194 5591 6775 1721 361 35 C ATOM 4224 O PHE C 166 -0.878 64.957 37.782 1.00 53.90 O ANISOU 4224 O PHE C 166 8061 5724 6694 1697 150 -174 O ATOM 4225 CB PHE C 166 -0.592 68.065 37.628 1.00 54.62 C ANISOU 4225 CB PHE C 166 8226 5265 7261 1992 336 319 C ATOM 4226 CG PHE C 166 0.077 68.388 38.943 1.00 54.02 C ANISOU 4226 CG PHE C 166 8048 4979 7497 1760 535 171 C ATOM 4227 CD1 PHE C 166 1.139 69.286 39.001 1.00 58.16 C ANISOU 4227 CD1 PHE C 166 8698 5222 8177 1652 732 377 C ATOM 4228 CD2 PHE C 166 -0.360 67.804 40.129 1.00 53.39 C ANISOU 4228 CD2 PHE C 166 7757 4993 7538 1618 515 -168 C ATOM 4229 CE1 PHE C 166 1.763 69.580 40.220 1.00 57.69 C ANISOU 4229 CE1 PHE C 166 8549 4982 8388 1415 863 213 C ATOM 4230 CE2 PHE C 166 0.266 68.098 41.345 1.00 54.78 C ANISOU 4230 CE2 PHE C 166 7875 4995 7944 1416 670 -313 C ATOM 4231 CZ PHE C 166 1.326 68.979 41.381 1.00 54.04 C ANISOU 4231 CZ PHE C 166 7903 4626 8003 1322 821 -139 C ATOM 4232 N LYS C 167 1.323 65.335 38.166 1.00 48.54 N ANISOU 4232 N LYS C 167 7501 4833 6111 1553 578 7 N ATOM 4233 CA LYS C 167 1.567 64.175 39.021 1.00 45.37 C ANISOU 4233 CA LYS C 167 7048 4507 5682 1373 578 -259 C ATOM 4234 C LYS C 167 2.143 64.641 40.347 1.00 47.56 C ANISOU 4234 C LYS C 167 7176 4625 6271 1187 726 -347 C ATOM 4235 O LYS C 167 2.894 65.618 40.362 1.00 48.24 O ANISOU 4235 O LYS C 167 7246 4562 6522 1165 881 -176 O ATOM 4236 CB LYS C 167 2.524 63.176 38.353 1.00 47.15 C ANISOU 4236 CB LYS C 167 7460 4864 5591 1429 651 -235 C ATOM 4237 CG LYS C 167 1.867 62.260 37.330 1.00 50.46 C ANISOU 4237 CG LYS C 167 8085 5442 5645 1558 441 -299 C ATOM 4238 CD LYS C 167 2.814 61.136 36.907 1.00 52.58 C ANISOU 4238 CD LYS C 167 8573 5799 5608 1645 515 -369 C ATOM 4239 CE LYS C 167 3.428 61.351 35.547 1.00 60.78 C ANISOU 4239 CE LYS C 167 9790 6980 6323 1891 645 -150 C ATOM 4240 NZ LYS C 167 4.488 62.395 35.571 1.00 66.88 N ANISOU 4240 NZ LYS C 167 10409 7743 7260 1885 962 124 N ATOM 4241 N SER C 168 1.797 63.960 41.462 1.00 40.89 N ANISOU 4241 N SER C 168 6245 3805 5487 1022 670 -605 N ATOM 4242 CA SER C 168 2.355 64.328 42.761 1.00 39.33 C ANISOU 4242 CA SER C 168 5942 3483 5519 851 781 -713 C ATOM 4243 C SER C 168 2.479 63.144 43.694 1.00 42.37 C ANISOU 4243 C SER C 168 6351 3943 5804 688 738 -919 C ATOM 4244 O SER C 168 1.653 62.226 43.669 1.00 41.64 O ANISOU 4244 O SER C 168 6310 3952 5559 640 610 -1032 O ATOM 4245 CB SER C 168 1.549 65.437 43.443 1.00 41.91 C ANISOU 4245 CB SER C 168 6139 3673 6111 852 782 -792 C ATOM 4246 OG SER C 168 0.181 65.118 43.647 1.00 47.85 O ANISOU 4246 OG SER C 168 6779 4565 6837 879 662 -948 O ATOM 4247 N ASN C 169 3.516 63.195 44.538 1.00 38.59 N ANISOU 4247 N ASN C 169 5844 3405 5413 581 825 -955 N ATOM 4248 CA ASN C 169 3.796 62.198 45.562 1.00 38.07 C ANISOU 4248 CA ASN C 169 5837 3375 5255 446 776 -1116 C ATOM 4249 C ASN C 169 3.125 62.602 46.860 1.00 42.39 C ANISOU 4249 C ASN C 169 6298 3879 5930 276 781 -1294 C ATOM 4250 O ASN C 169 2.961 63.797 47.104 1.00 42.96 O ANISOU 4250 O ASN C 169 6259 3852 6213 284 848 -1306 O ATOM 4251 CB ASN C 169 5.312 62.069 45.776 1.00 37.16 C ANISOU 4251 CB ASN C 169 5701 3273 5146 462 835 -1057 C ATOM 4252 CG ASN C 169 6.081 61.579 44.579 1.00 45.11 C ANISOU 4252 CG ASN C 169 6768 4386 5987 668 882 -907 C ATOM 4253 OD1 ASN C 169 7.116 62.128 44.202 1.00 41.20 O ANISOU 4253 OD1 ASN C 169 6137 3948 5568 715 1011 -762 O ATOM 4254 ND2 ASN C 169 5.579 60.561 43.933 1.00 29.23 N ANISOU 4254 ND2 ASN C 169 4959 2415 3731 782 788 -944 N ATOM 4255 N SER C 170 2.741 61.621 47.695 1.00 39.25 N ANISOU 4255 N SER C 170 5988 3541 5386 127 719 -1429 N ATOM 4256 CA SER C 170 2.163 61.896 49.010 1.00 39.77 C ANISOU 4256 CA SER C 170 5990 3623 5498 -40 763 -1600 C ATOM 4257 C SER C 170 2.298 60.715 49.950 1.00 44.11 C ANISOU 4257 C SER C 170 6717 4210 5832 -219 704 -1670 C ATOM 4258 O SER C 170 2.314 59.562 49.526 1.00 43.87 O ANISOU 4258 O SER C 170 6871 4176 5621 -236 604 -1614 O ATOM 4259 CB SER C 170 0.694 62.324 48.920 1.00 44.66 C ANISOU 4259 CB SER C 170 6444 4341 6182 -38 798 -1676 C ATOM 4260 OG SER C 170 -0.204 61.230 48.839 1.00 56.38 O ANISOU 4260 OG SER C 170 7959 5973 7491 -185 728 -1703 O ATOM 4261 N ALA C 171 2.373 61.026 51.237 1.00 41.66 N ANISOU 4261 N ALA C 171 6401 3910 5519 -346 754 -1797 N ATOM 4262 CA ALA C 171 2.388 60.080 52.351 1.00 41.66 C ANISOU 4262 CA ALA C 171 6595 3948 5285 -537 713 -1852 C ATOM 4263 C ALA C 171 1.496 60.670 53.424 1.00 46.57 C ANISOU 4263 C ALA C 171 7115 4685 5895 -677 854 -2020 C ATOM 4264 O ALA C 171 1.469 61.891 53.584 1.00 47.59 O ANISOU 4264 O ALA C 171 7086 4786 6210 -578 938 -2128 O ATOM 4265 CB ALA C 171 3.803 59.852 52.858 1.00 42.06 C ANISOU 4265 CB ALA C 171 6773 3929 5280 -484 606 -1823 C ATOM 4266 N VAL C 172 0.709 59.830 54.088 1.00 43.79 N ANISOU 4266 N VAL C 172 6861 4456 5323 -904 895 -2042 N ATOM 4267 CA VAL C 172 -0.245 60.242 55.121 1.00 45.31 C ANISOU 4267 CA VAL C 172 6936 4843 5438 -1043 1083 -2200 C ATOM 4268 C VAL C 172 0.233 59.707 56.464 1.00 50.09 C ANISOU 4268 C VAL C 172 7815 5465 5752 -1221 1075 -2226 C ATOM 4269 O VAL C 172 0.766 58.596 56.535 1.00 49.72 O ANISOU 4269 O VAL C 172 8055 5317 5520 -1320 926 -2079 O ATOM 4270 CB VAL C 172 -1.693 59.759 54.782 1.00 51.09 C ANISOU 4270 CB VAL C 172 7484 5793 6134 -1213 1178 -2181 C ATOM 4271 CG1 VAL C 172 -2.709 60.223 55.824 1.00 54.01 C ANISOU 4271 CG1 VAL C 172 7651 6450 6419 -1320 1430 -2351 C ATOM 4272 CG2 VAL C 172 -2.122 60.211 53.386 1.00 50.03 C ANISOU 4272 CG2 VAL C 172 7109 5653 6248 -1009 1116 -2137 C ATOM 4273 N ALA C 173 0.053 60.502 57.524 1.00 48.44 N ANISOU 4273 N ALA C 173 7559 5369 5478 -1228 1218 -2420 N ATOM 4274 CA ALA C 173 0.410 60.114 58.882 1.00 49.93 C ANISOU 4274 CA ALA C 173 8019 5619 5331 -1389 1217 -2463 C ATOM 4275 C ALA C 173 -0.707 60.485 59.842 1.00 55.62 C ANISOU 4275 C ALA C 173 8638 6626 5871 -1508 1505 -2640 C ATOM 4276 O ALA C 173 -1.391 61.490 59.622 1.00 56.39 O ANISOU 4276 O ALA C 173 8440 6815 6170 -1342 1670 -2818 O ATOM 4277 CB ALA C 173 1.716 60.773 59.297 1.00 50.56 C ANISOU 4277 CB ALA C 173 8202 5547 5461 -1244 1045 -2557 C ATOM 4278 N TRP C 174 -0.915 59.668 60.889 1.00 53.58 N ANISOU 4278 N TRP C 174 8629 6518 5213 -1772 1578 -2580 N ATOM 4279 CA TRP C 174 -1.942 59.925 61.901 1.00 57.18 C ANISOU 4279 CA TRP C 174 8997 7317 5413 -1906 1904 -2735 C ATOM 4280 C TRP C 174 -1.637 59.178 63.204 1.00 63.06 C ANISOU 4280 C TRP C 174 10158 8147 5654 -2151 1911 -2655 C ATOM 4281 O TRP C 174 -0.860 58.217 63.207 1.00 60.73 O ANISOU 4281 O TRP C 174 10210 7643 5222 -2253 1657 -2425 O ATOM 4282 CB TRP C 174 -3.356 59.574 61.378 1.00 58.06 C ANISOU 4282 CB TRP C 174 8762 7700 5599 -2076 2135 -2667 C ATOM 4283 CG TRP C 174 -3.669 58.110 61.277 1.00 60.11 C ANISOU 4283 CG TRP C 174 9214 7967 5659 -2482 2091 -2370 C ATOM 4284 CD1 TRP C 174 -4.389 57.366 62.165 1.00 67.37 C ANISOU 4284 CD1 TRP C 174 10239 9151 6207 -2878 2314 -2264 C ATOM 4285 CD2 TRP C 174 -3.292 57.218 60.218 1.00 57.99 C ANISOU 4285 CD2 TRP C 174 9092 7404 5539 -2548 1812 -2145 C ATOM 4286 NE1 TRP C 174 -4.479 56.063 61.730 1.00 67.28 N ANISOU 4286 NE1 TRP C 174 10460 8974 6129 -3222 2165 -1972 N ATOM 4287 CE2 TRP C 174 -3.815 55.945 60.535 1.00 64.80 C ANISOU 4287 CE2 TRP C 174 10187 8308 6127 -3000 1848 -1919 C ATOM 4288 CE3 TRP C 174 -2.575 57.373 59.018 1.00 55.50 C ANISOU 4288 CE3 TRP C 174 8754 6795 5539 -2271 1551 -2114 C ATOM 4289 CZ2 TRP C 174 -3.632 54.833 59.706 1.00 63.39 C ANISOU 4289 CZ2 TRP C 174 10261 7831 5994 -3159 1596 -1702 C ATOM 4290 CZ3 TRP C 174 -2.389 56.271 58.202 1.00 56.10 C ANISOU 4290 CZ3 TRP C 174 9049 6641 5627 -2393 1334 -1908 C ATOM 4291 CH2 TRP C 174 -2.912 55.019 58.546 1.00 59.63 C ANISOU 4291 CH2 TRP C 174 9764 7080 5811 -2820 1340 -1722 C ATOM 4292 N SER C 175 -2.250 59.647 64.316 1.00 63.81 N ANISOU 4292 N SER C 175 10240 8557 5450 -2202 2203 -2854 N ATOM 4293 CA SER C 175 -2.142 59.089 65.666 1.00 93.17 C ANISOU 4293 CA SER C 175 14353 12439 8609 -2432 2278 -2800 C ATOM 4294 C SER C 175 -3.375 59.464 66.483 1.00118.09 C ANISOU 4294 C SER C 175 17309 16070 11490 -2532 2751 -2978 C ATOM 4295 O SER C 175 -3.870 60.583 66.363 1.00 81.70 O ANISOU 4295 O SER C 175 12355 11597 7092 -2254 2940 -3291 O ATOM 4296 CB SER C 175 -0.876 59.581 66.361 1.00 96.42 C ANISOU 4296 CB SER C 175 15085 12672 8877 -2240 2000 -2950 C ATOM 4297 OG SER C 175 -0.741 59.000 67.648 1.00107.93 O ANISOU 4297 OG SER C 175 16971 14291 9746 -2442 2027 -2873 O ATOM 4298 N ALA C 181 1.137 66.167 66.574 1.00 82.82 N ANISOU 4298 N ALA C 181 13091 10109 8269 -1032 1609 -4648 N ATOM 4299 CA ALA C 181 1.168 67.305 65.656 1.00 81.42 C ANISOU 4299 CA ALA C 181 12718 9592 8626 -816 1570 -4776 C ATOM 4300 C ALA C 181 1.951 66.990 64.371 1.00 80.84 C ANISOU 4300 C ALA C 181 12464 9274 8979 -873 1321 -4428 C ATOM 4301 O ALA C 181 2.924 66.228 64.400 1.00 78.48 O ANISOU 4301 O ALA C 181 12254 8974 8590 -1044 1061 -4214 O ATOM 4302 CB ALA C 181 1.770 68.520 66.342 1.00 85.27 C ANISOU 4302 CB ALA C 181 13462 9820 9117 -743 1406 -5183 C ATOM 4303 N CYS C 182 1.534 67.633 63.259 1.00 76.12 N ANISOU 4303 N CYS C 182 11622 8479 8823 -688 1400 -4386 N ATOM 4304 CA CYS C 182 2.084 67.511 61.905 1.00 72.55 C ANISOU 4304 CA CYS C 182 10982 7814 8769 -688 1242 -4076 C ATOM 4305 C CYS C 182 3.546 67.963 61.804 1.00 75.06 C ANISOU 4305 C CYS C 182 11391 7852 9275 -810 919 -4059 C ATOM 4306 O CYS C 182 4.270 67.471 60.931 1.00 70.74 O ANISOU 4306 O CYS C 182 10711 7258 8908 -874 775 -3762 O ATOM 4307 CB CYS C 182 1.206 68.272 60.918 1.00 73.08 C ANISOU 4307 CB CYS C 182 10829 7746 9191 -432 1404 -4078 C ATOM 4308 SG CYS C 182 -0.444 67.554 60.693 1.00 77.37 S ANISOU 4308 SG CYS C 182 11095 8702 9599 -328 1729 -4002 S ATOM 4309 N ALA C 183 3.971 68.889 62.693 1.00 75.05 N ANISOU 4309 N ALA C 183 11603 7690 9221 -850 809 -4392 N ATOM 4310 CA ALA C 183 5.324 69.444 62.760 1.00 75.85 C ANISOU 4310 CA ALA C 183 11770 7551 9498 -1035 484 -4433 C ATOM 4311 C ALA C 183 6.406 68.368 62.991 1.00 78.71 C ANISOU 4311 C ALA C 183 12096 8137 9673 -1223 225 -4215 C ATOM 4312 O ALA C 183 7.497 68.490 62.431 1.00 77.75 O ANISOU 4312 O ALA C 183 11817 7909 9814 -1343 5 -4060 O ATOM 4313 CB ALA C 183 5.397 70.489 63.863 1.00 81.38 C ANISOU 4313 CB ALA C 183 12767 8079 10074 -1064 404 -4889 C ATOM 4314 N ASN C 184 6.103 67.321 63.798 1.00 75.43 N ANISOU 4314 N ASN C 184 11821 8037 8801 -1237 259 -4185 N ATOM 4315 CA ASN C 184 7.045 66.245 64.133 1.00 74.67 C ANISOU 4315 CA ASN C 184 11763 8135 8473 -1342 -6 -3983 C ATOM 4316 C ASN C 184 6.683 64.875 63.504 1.00 75.05 C ANISOU 4316 C ASN C 184 11744 8338 8432 -1275 101 -3618 C ATOM 4317 O ASN C 184 7.441 63.912 63.671 1.00 74.02 O ANISOU 4317 O ASN C 184 11673 8321 8129 -1295 -122 -3424 O ATOM 4318 CB ASN C 184 7.144 66.095 65.653 1.00 80.33 C ANISOU 4318 CB ASN C 184 12810 9036 8677 -1429 -131 -4215 C ATOM 4319 N ALA C 185 5.547 64.795 62.777 1.00 69.56 N ANISOU 4319 N ALA C 185 10938 7634 7859 -1185 407 -3536 N ATOM 4320 CA ALA C 185 5.026 63.569 62.156 1.00 66.74 C ANISOU 4320 CA ALA C 185 10549 7385 7423 -1169 513 -3237 C ATOM 4321 C ALA C 185 6.069 62.808 61.316 1.00 68.39 C ANISOU 4321 C ALA C 185 10673 7533 7778 -1118 284 -2952 C ATOM 4322 O ALA C 185 6.249 61.607 61.525 1.00 67.79 O ANISOU 4322 O ALA C 185 10771 7540 7444 -1133 183 -2767 O ATOM 4323 CB ALA C 185 3.817 63.897 61.292 1.00 66.19 C ANISOU 4323 CB ALA C 185 10277 7295 7577 -1077 801 -3226 C ATOM 4324 N PHE C 186 6.771 63.504 60.404 1.00 63.99 N ANISOU 4324 N PHE C 186 9873 6830 7610 -1049 209 -2916 N ATOM 4325 CA PHE C 186 7.738 62.883 59.493 1.00 62.56 C ANISOU 4325 CA PHE C 186 9548 6644 7577 -954 57 -2665 C ATOM 4326 C PHE C 186 9.204 63.209 59.870 1.00 69.44 C ANISOU 4326 C PHE C 186 10304 7556 8524 -995 -232 -2702 C ATOM 4327 O PHE C 186 10.052 63.350 58.981 1.00 68.96 O ANISOU 4327 O PHE C 186 9981 7491 8732 -936 -291 -2563 O ATOM 4328 CB PHE C 186 7.434 63.320 58.043 1.00 62.01 C ANISOU 4328 CB PHE C 186 9252 6453 7857 -855 223 -2539 C ATOM 4329 CG PHE C 186 6.013 63.065 57.590 1.00 62.19 C ANISOU 4329 CG PHE C 186 9314 6476 7840 -813 456 -2510 C ATOM 4330 CD1 PHE C 186 5.650 61.841 57.035 1.00 63.68 C ANISOU 4330 CD1 PHE C 186 9581 6724 7890 -767 470 -2320 C ATOM 4331 CD2 PHE C 186 5.039 64.051 57.712 1.00 65.02 C ANISOU 4331 CD2 PHE C 186 9624 6776 8306 -811 639 -2688 C ATOM 4332 CE1 PHE C 186 4.336 61.608 56.616 1.00 63.83 C ANISOU 4332 CE1 PHE C 186 9588 6780 7886 -785 648 -2302 C ATOM 4333 CE2 PHE C 186 3.722 63.810 57.312 1.00 67.12 C ANISOU 4333 CE2 PHE C 186 9842 7118 8545 -764 832 -2665 C ATOM 4334 CZ PHE C 186 3.383 62.595 56.754 1.00 63.88 C ANISOU 4334 CZ PHE C 186 9464 6800 8006 -783 828 -2467 C ATOM 4335 N ASN C 187 9.505 63.265 61.187 1.00 69.16 N ANISOU 4335 N ASN C 187 10451 7610 8218 -1100 -417 -2881 N ATOM 4336 CA ASN C 187 10.842 63.571 61.720 1.00 72.04 C ANISOU 4336 CA ASN C 187 10696 8064 8613 -1173 -752 -2955 C ATOM 4337 C ASN C 187 11.872 62.468 61.438 1.00 76.71 C ANISOU 4337 C ASN C 187 11168 8830 9150 -996 -982 -2713 C ATOM 4338 O ASN C 187 13.059 62.778 61.302 1.00 78.13 O ANISOU 4338 O ASN C 187 11040 9121 9524 -1014 -1202 -2700 O ATOM 4339 CB ASN C 187 10.783 63.842 63.228 1.00 75.70 C ANISOU 4339 CB ASN C 187 11443 8597 8723 -1307 -912 -3225 C ATOM 4340 CG ASN C 187 10.463 65.272 63.601 1.00102.01 C ANISOU 4340 CG ASN C 187 14811 11755 12193 -1474 -842 -3555 C ATOM 4341 OD1 ASN C 187 10.167 66.125 62.754 1.00 96.39 O ANISOU 4341 OD1 ASN C 187 13940 10828 11858 -1491 -658 -3572 O ATOM 4342 ND2 ASN C 187 10.501 65.564 64.893 1.00 97.20 N ANISOU 4342 ND2 ASN C 187 14467 11213 11253 -1579 -1000 -3831 N ATOM 4343 N ASN C 188 11.429 61.199 61.340 1.00 72.33 N ANISOU 4343 N ASN C 188 10845 8294 8342 -826 -936 -2526 N ATOM 4344 CA ASN C 188 12.325 60.073 61.071 1.00 73.28 C ANISOU 4344 CA ASN C 188 10933 8524 8387 -572 -1154 -2311 C ATOM 4345 C ASN C 188 12.742 60.022 59.584 1.00 75.76 C ANISOU 4345 C ASN C 188 10908 8830 9048 -395 -1025 -2148 C ATOM 4346 O ASN C 188 13.743 59.380 59.245 1.00 76.77 O ANISOU 4346 O ASN C 188 10870 9099 9200 -145 -1198 -2018 O ATOM 4347 CB ASN C 188 11.688 58.750 61.500 1.00 74.49 C ANISOU 4347 CB ASN C 188 11549 8614 8141 -475 -1164 -2170 C ATOM 4348 CG ASN C 188 12.702 57.652 61.719 1.00 97.64 C ANISOU 4348 CG ASN C 188 14577 11629 10894 -186 -1498 -2005 C ATOM 4349 OD1 ASN C 188 13.351 57.570 62.767 1.00 93.40 O ANISOU 4349 OD1 ASN C 188 14132 11232 10125 -169 -1809 -2051 O ATOM 4350 ND2 ASN C 188 12.881 56.799 60.722 1.00 87.96 N ANISOU 4350 ND2 ASN C 188 13341 10321 9758 86 -1464 -1824 N ATOM 4351 N SER C 189 11.984 60.706 58.708 1.00 69.63 N ANISOU 4351 N SER C 189 10031 7914 8513 -491 -724 -2158 N ATOM 4352 CA SER C 189 12.272 60.764 57.275 1.00 67.90 C ANISOU 4352 CA SER C 189 9535 7694 8570 -347 -567 -2001 C ATOM 4353 C SER C 189 13.140 61.975 56.942 1.00 73.68 C ANISOU 4353 C SER C 189 9851 8497 9647 -497 -571 -2033 C ATOM 4354 O SER C 189 12.972 63.040 57.550 1.00 74.15 O ANISOU 4354 O SER C 189 9909 8459 9805 -762 -588 -2210 O ATOM 4355 CB SER C 189 10.977 60.819 56.470 1.00 67.63 C ANISOU 4355 CB SER C 189 9636 7482 8578 -364 -279 -1963 C ATOM 4356 OG SER C 189 10.144 59.712 56.763 1.00 74.56 O ANISOU 4356 OG SER C 189 10876 8296 9159 -314 -273 -1925 O ATOM 4357 N ILE C 190 14.066 61.811 55.974 1.00 70.96 N ANISOU 4357 N ILE C 190 9171 8316 9474 -338 -543 -1865 N ATOM 4358 CA ILE C 190 14.931 62.898 55.506 1.00 72.73 C ANISOU 4358 CA ILE C 190 8964 8635 10035 -532 -505 -1830 C ATOM 4359 C ILE C 190 14.083 63.728 54.524 1.00 75.44 C ANISOU 4359 C ILE C 190 9355 8735 10574 -642 -195 -1762 C ATOM 4360 O ILE C 190 13.976 63.396 53.336 1.00 74.57 O ANISOU 4360 O ILE C 190 9188 8658 10489 -451 6 -1577 O ATOM 4361 CB ILE C 190 16.286 62.396 54.905 1.00 77.90 C ANISOU 4361 CB ILE C 190 9182 9647 10770 -318 -562 -1668 C ATOM 4362 CG1 ILE C 190 17.068 61.525 55.924 1.00 80.52 C ANISOU 4362 CG1 ILE C 190 9489 10215 10890 -129 -922 -1734 C ATOM 4363 CG2 ILE C 190 17.145 63.578 54.415 1.00 81.36 C ANISOU 4363 CG2 ILE C 190 9140 10208 11566 -622 -483 -1599 C ATOM 4364 CD1 ILE C 190 18.183 60.617 55.338 1.00 86.64 C ANISOU 4364 CD1 ILE C 190 9922 11347 11650 286 -978 -1586 C ATOM 4365 N ILE C 191 13.412 64.752 55.055 1.00 71.40 N ANISOU 4365 N ILE C 191 9003 7971 10157 -900 -174 -1927 N ATOM 4366 CA ILE C 191 12.549 65.629 54.267 1.00 69.98 C ANISOU 4366 CA ILE C 191 8908 7522 10159 -965 69 -1879 C ATOM 4367 C ILE C 191 13.365 66.875 53.848 1.00 77.45 C ANISOU 4367 C ILE C 191 9591 8386 11450 -1249 95 -1802 C ATOM 4368 O ILE C 191 14.262 67.276 54.600 1.00 80.34 O ANISOU 4368 O ILE C 191 9793 8829 11905 -1491 -113 -1914 O ATOM 4369 CB ILE C 191 11.221 65.977 55.014 1.00 71.79 C ANISOU 4369 CB ILE C 191 9481 7513 10282 -1000 107 -2104 C ATOM 4370 CG1 ILE C 191 11.451 66.823 56.292 1.00 74.57 C ANISOU 4370 CG1 ILE C 191 9920 7756 10657 -1252 -72 -2387 C ATOM 4371 CG2 ILE C 191 10.413 64.706 55.315 1.00 69.60 C ANISOU 4371 CG2 ILE C 191 9431 7341 9671 -799 119 -2119 C ATOM 4372 CD1 ILE C 191 10.371 67.802 56.575 1.00 80.17 C ANISOU 4372 CD1 ILE C 191 10867 8161 11434 -1296 47 -2586 C ATOM 4373 N PRO C 192 13.108 67.485 52.660 1.00 73.92 N ANISOU 4373 N PRO C 192 9110 7789 11186 -1254 326 -1596 N ATOM 4374 CA PRO C 192 13.926 68.646 52.243 1.00 77.38 C ANISOU 4374 CA PRO C 192 9331 8125 11943 -1585 364 -1469 C ATOM 4375 C PRO C 192 13.815 69.844 53.188 1.00 82.85 C ANISOU 4375 C PRO C 192 10200 8464 12816 -1920 209 -1715 C ATOM 4376 O PRO C 192 12.814 69.991 53.891 1.00 80.85 O ANISOU 4376 O PRO C 192 10278 7987 12454 -1827 169 -1960 O ATOM 4377 CB PRO C 192 13.395 68.989 50.845 1.00 78.24 C ANISOU 4377 CB PRO C 192 9511 8092 12126 -1472 640 -1193 C ATOM 4378 CG PRO C 192 12.089 68.323 50.744 1.00 78.87 C ANISOU 4378 CG PRO C 192 9880 8109 11979 -1135 695 -1269 C ATOM 4379 CD PRO C 192 12.114 67.128 51.626 1.00 72.65 C ANISOU 4379 CD PRO C 192 9111 7560 10931 -986 539 -1448 C ATOM 4380 N GLU C 193 14.865 70.689 53.210 1.00 83.28 N ANISOU 4380 N GLU C 193 10022 8483 13136 -2323 123 -1662 N ATOM 4381 CA GLU C 193 14.949 71.888 54.057 1.00 86.42 C ANISOU 4381 CA GLU C 193 10604 8503 13730 -2705 -66 -1908 C ATOM 4382 C GLU C 193 13.890 72.937 53.679 1.00 88.94 C ANISOU 4382 C GLU C 193 11341 8258 14193 -2681 79 -1921 C ATOM 4383 O GLU C 193 13.480 73.720 54.536 1.00 90.59 O ANISOU 4383 O GLU C 193 11870 8097 14453 -2796 -61 -2232 O ATOM 4384 CB GLU C 193 16.352 72.518 53.976 1.00 93.14 C ANISOU 4384 CB GLU C 193 11071 9456 14863 -3205 -185 -1793 C ATOM 4385 CG GLU C 193 17.475 71.646 54.525 1.00106.03 C ANISOU 4385 CG GLU C 193 12245 11655 16387 -3232 -404 -1834 C ATOM 4386 CD GLU C 193 17.616 71.571 56.035 1.00126.87 C ANISOU 4386 CD GLU C 193 15005 14324 18875 -3328 -789 -2228 C ATOM 4387 OE1 GLU C 193 17.590 72.635 56.697 1.00125.02 O ANISOU 4387 OE1 GLU C 193 15004 13713 18786 -3697 -970 -2472 O ATOM 4388 OE2 GLU C 193 17.818 70.448 56.550 1.00116.54 O ANISOU 4388 OE2 GLU C 193 13580 13411 17290 -3039 -929 -2289 O ATOM 4389 N ASP C 194 13.442 72.932 52.405 1.00 82.57 N ANISOU 4389 N ASP C 194 10550 7397 13425 -2486 345 -1598 N ATOM 4390 CA ASP C 194 12.451 73.859 51.852 1.00 82.25 C ANISOU 4390 CA ASP C 194 10877 6859 13513 -2381 474 -1536 C ATOM 4391 C ASP C 194 10.986 73.391 52.082 1.00 80.35 C ANISOU 4391 C ASP C 194 10894 6588 13047 -1910 532 -1727 C ATOM 4392 O ASP C 194 10.069 73.986 51.505 1.00 80.98 O ANISOU 4392 O ASP C 194 11216 6351 13203 -1708 640 -1652 O ATOM 4393 CB ASP C 194 12.714 74.060 50.347 1.00 84.83 C ANISOU 4393 CB ASP C 194 11093 7195 13943 -2400 708 -1066 C ATOM 4394 N THR C 195 10.762 72.368 52.942 1.00 71.50 N ANISOU 4394 N THR C 195 9719 5797 11653 -1750 451 -1959 N ATOM 4395 CA THR C 195 9.418 71.854 53.243 1.00 67.52 C ANISOU 4395 CA THR C 195 9395 5336 10924 -1388 522 -2132 C ATOM 4396 C THR C 195 8.604 72.939 53.974 1.00 72.29 C ANISOU 4396 C THR C 195 10323 5523 11619 -1348 491 -2447 C ATOM 4397 O THR C 195 9.072 73.529 54.956 1.00 74.52 O ANISOU 4397 O THR C 195 10729 5635 11952 -1583 329 -2718 O ATOM 4398 CB THR C 195 9.468 70.513 54.024 1.00 70.94 C ANISOU 4398 CB THR C 195 9733 6189 11030 -1300 446 -2262 C ATOM 4399 OG1 THR C 195 10.246 69.568 53.291 1.00 67.45 O ANISOU 4399 OG1 THR C 195 9031 6075 10522 -1269 467 -1989 O ATOM 4400 CG2 THR C 195 8.084 69.908 54.259 1.00 66.24 C ANISOU 4400 CG2 THR C 195 9282 5685 10202 -1006 553 -2387 C ATOM 4401 N PHE C 196 7.398 73.207 53.450 1.00 66.38 N ANISOU 4401 N PHE C 196 9709 4623 10888 -1023 632 -2421 N ATOM 4402 CA PHE C 196 6.479 74.205 53.969 1.00 68.47 C ANISOU 4402 CA PHE C 196 10264 4513 11239 -846 642 -2706 C ATOM 4403 C PHE C 196 5.623 73.635 55.111 1.00 70.95 C ANISOU 4403 C PHE C 196 10610 5089 11260 -658 679 -3068 C ATOM 4404 O PHE C 196 4.938 72.624 54.947 1.00 67.16 O ANISOU 4404 O PHE C 196 9968 4984 10567 -472 787 -2999 O ATOM 4405 CB PHE C 196 5.596 74.756 52.829 1.00 70.56 C ANISOU 4405 CB PHE C 196 10610 4542 11657 -532 758 -2485 C ATOM 4406 CG PHE C 196 4.553 75.781 53.215 1.00 75.42 C ANISOU 4406 CG PHE C 196 11505 4774 12377 -222 774 -2758 C ATOM 4407 CD1 PHE C 196 4.918 76.972 53.836 1.00 82.84 C ANISOU 4407 CD1 PHE C 196 12777 5190 13510 -367 660 -2994 C ATOM 4408 CD2 PHE C 196 3.214 75.584 52.902 1.00 76.70 C ANISOU 4408 CD2 PHE C 196 11597 5088 12457 228 887 -2783 C ATOM 4409 CE1 PHE C 196 3.954 77.927 54.177 1.00 87.49 C ANISOU 4409 CE1 PHE C 196 13664 5389 14187 -1 675 -3275 C ATOM 4410 CE2 PHE C 196 2.252 76.542 53.239 1.00 83.23 C ANISOU 4410 CE2 PHE C 196 12641 5597 13387 596 909 -3046 C ATOM 4411 CZ PHE C 196 2.628 77.707 53.874 1.00 85.67 C ANISOU 4411 CZ PHE C 196 13320 5358 13871 511 811 -3297 C ATOM 4412 N PHE C 197 5.694 74.292 56.275 1.00 70.81 N ANISOU 4412 N PHE C 197 10824 4869 11213 -742 587 -3452 N ATOM 4413 CA PHE C 197 4.923 73.967 57.471 1.00 71.21 C ANISOU 4413 CA PHE C 197 10962 5139 10954 -581 650 -3828 C ATOM 4414 C PHE C 197 4.018 75.161 57.806 1.00 78.95 C ANISOU 4414 C PHE C 197 12223 5732 12043 -286 723 -4150 C ATOM 4415 O PHE C 197 4.435 76.062 58.537 1.00 82.20 O ANISOU 4415 O PHE C 197 12935 5783 12516 -412 588 -4454 O ATOM 4416 CB PHE C 197 5.840 73.607 58.650 1.00 74.00 C ANISOU 4416 CB PHE C 197 11377 5659 11082 -893 466 -4039 C ATOM 4417 CG PHE C 197 6.527 72.276 58.505 1.00 72.04 C ANISOU 4417 CG PHE C 197 10867 5849 10655 -1050 404 -3774 C ATOM 4418 CD1 PHE C 197 5.916 71.109 58.947 1.00 72.57 C ANISOU 4418 CD1 PHE C 197 10874 6330 10369 -927 508 -3779 C ATOM 4419 CD2 PHE C 197 7.793 72.187 57.936 1.00 74.03 C ANISOU 4419 CD2 PHE C 197 10940 6098 11091 -1317 247 -3517 C ATOM 4420 CE1 PHE C 197 6.557 69.876 58.818 1.00 70.82 C ANISOU 4420 CE1 PHE C 197 10489 6434 9984 -1032 424 -3540 C ATOM 4421 CE2 PHE C 197 8.433 70.953 57.809 1.00 73.92 C ANISOU 4421 CE2 PHE C 197 10696 6482 10908 -1374 185 -3299 C ATOM 4422 CZ PHE C 197 7.810 69.806 58.247 1.00 69.69 C ANISOU 4422 CZ PHE C 197 10175 6277 10026 -1212 258 -3316 C ATOM 4423 N PRO C 198 2.789 75.204 57.241 1.00 74.77 N ANISOU 4423 N PRO C 198 11602 5260 11549 126 910 -4098 N ATOM 4424 CA PRO C 198 1.891 76.346 57.515 1.00 81.32 C ANISOU 4424 CA PRO C 198 12677 5731 12491 513 980 -4410 C ATOM 4425 C PRO C 198 1.425 76.431 58.973 1.00127.62 C ANISOU 4425 C PRO C 198 18695 11742 18053 631 1065 -4923 C ATOM 4426 O PRO C 198 1.434 75.438 59.696 1.00 94.90 O ANISOU 4426 O PRO C 198 14407 8088 13563 483 1132 -4988 O ATOM 4427 CB PRO C 198 0.706 76.092 56.586 1.00 81.22 C ANISOU 4427 CB PRO C 198 12401 5926 12531 926 1142 -4203 C ATOM 4428 CG PRO C 198 0.729 74.612 56.322 1.00 79.57 C ANISOU 4428 CG PRO C 198 11835 6303 12096 741 1202 -3946 C ATOM 4429 CD PRO C 198 2.167 74.228 56.321 1.00 72.33 C ANISOU 4429 CD PRO C 198 10961 5344 11177 276 1036 -3772 C TER 4430 PRO C 198 ATOM 4431 N ALA D 2 -14.826 33.901 25.343 1.00 42.74 N ANISOU 4431 N ALA D 2 4567 6622 5050 746 -598 68 N ATOM 4432 CA ALA D 2 -14.114 32.691 25.799 1.00 41.58 C ANISOU 4432 CA ALA D 2 4426 6486 4885 572 -489 -36 C ATOM 4433 C ALA D 2 -13.011 33.025 26.809 1.00 41.72 C ANISOU 4433 C ALA D 2 4557 6355 4939 524 -319 -29 C ATOM 4434 O ALA D 2 -12.119 33.823 26.497 1.00 41.67 O ANISOU 4434 O ALA D 2 4712 6259 4860 540 -289 62 O ATOM 4435 CB ALA D 2 -13.512 31.930 24.618 1.00 42.35 C ANISOU 4435 CB ALA D 2 4621 6661 4808 479 -548 -44 C ATOM 4436 N GLY D 3 -13.086 32.421 27.999 1.00 33.50 N ANISOU 4436 N GLY D 3 3434 5292 4001 456 -213 -120 N ATOM 4437 CA GLY D 3 -12.087 32.648 29.033 1.00 30.38 C ANISOU 4437 CA GLY D 3 3137 4772 3635 402 -71 -122 C ATOM 4438 C GLY D 3 -12.072 31.651 30.167 1.00 29.06 C ANISOU 4438 C GLY D 3 2901 4605 3536 300 26 -223 C ATOM 4439 O GLY D 3 -12.649 30.562 30.079 1.00 27.82 O ANISOU 4439 O GLY D 3 2638 4539 3394 238 0 -298 O ATOM 4440 N ILE D 4 -11.435 32.039 31.251 1.00 23.55 N ANISOU 4440 N ILE D 4 2274 3799 2875 276 135 -223 N ATOM 4441 CA ILE D 4 -11.318 31.185 32.434 1.00 22.04 C ANISOU 4441 CA ILE D 4 2051 3591 2731 181 231 -301 C ATOM 4442 C ILE D 4 -11.857 31.957 33.629 1.00 25.29 C ANISOU 4442 C ILE D 4 2446 3932 3232 237 312 -318 C ATOM 4443 O ILE D 4 -11.563 33.141 33.759 1.00 24.82 O ANISOU 4443 O ILE D 4 2475 3780 3175 307 327 -266 O ATOM 4444 CB ILE D 4 -9.847 30.686 32.638 1.00 22.82 C ANISOU 4444 CB ILE D 4 2267 3640 2766 79 280 -294 C ATOM 4445 CG1 ILE D 4 -9.716 29.789 33.895 1.00 21.85 C ANISOU 4445 CG1 ILE D 4 2130 3492 2681 -10 364 -359 C ATOM 4446 CG2 ILE D 4 -8.804 31.854 32.631 1.00 21.00 C ANISOU 4446 CG2 ILE D 4 2167 3312 2499 100 302 -216 C ATOM 4447 CD1 ILE D 4 -8.397 28.890 33.953 1.00 21.53 C ANISOU 4447 CD1 ILE D 4 2163 3430 2586 -102 385 -362 C ATOM 4448 N THR D 5 -12.681 31.323 34.460 1.00 22.74 N ANISOU 4448 N THR D 5 2015 3647 2977 204 371 -393 N ATOM 4449 CA THR D 5 -13.209 32.020 35.634 1.00 23.61 C ANISOU 4449 CA THR D 5 2115 3695 3161 256 472 -422 C ATOM 4450 C THR D 5 -13.152 31.141 36.852 1.00 26.46 C ANISOU 4450 C THR D 5 2479 4046 3528 142 581 -488 C ATOM 4451 O THR D 5 -13.358 29.936 36.767 1.00 26.34 O ANISOU 4451 O THR D 5 2398 4101 3511 49 575 -525 O ATOM 4452 CB THR D 5 -14.660 32.555 35.442 1.00 37.16 C ANISOU 4452 CB THR D 5 3670 5471 4979 386 453 -437 C ATOM 4453 OG1 THR D 5 -15.552 31.455 35.289 1.00 42.04 O ANISOU 4453 OG1 THR D 5 4116 6217 5640 325 435 -497 O ATOM 4454 CG2 THR D 5 -14.795 33.528 34.281 1.00 38.24 C ANISOU 4454 CG2 THR D 5 3818 5605 5107 523 333 -356 C ATOM 4455 N GLN D 6 -12.993 31.764 38.009 1.00 24.01 N ANISOU 4455 N GLN D 6 2251 3647 3225 150 683 -505 N ATOM 4456 CA GLN D 6 -12.957 30.993 39.246 1.00 23.85 C ANISOU 4456 CA GLN D 6 2258 3613 3189 43 789 -559 C ATOM 4457 C GLN D 6 -13.847 31.640 40.277 1.00 27.90 C ANISOU 4457 C GLN D 6 2742 4100 3758 99 913 -612 C ATOM 4458 O GLN D 6 -14.121 32.832 40.178 1.00 27.72 O ANISOU 4458 O GLN D 6 2732 4027 3775 223 918 -603 O ATOM 4459 CB GLN D 6 -11.503 30.795 39.752 1.00 24.13 C ANISOU 4459 CB GLN D 6 2465 3571 3133 -49 787 -531 C ATOM 4460 CG GLN D 6 -10.757 32.053 40.116 1.00 26.51 C ANISOU 4460 CG GLN D 6 2904 3766 3404 -10 796 -504 C ATOM 4461 CD GLN D 6 -9.339 31.734 40.530 1.00 27.19 C ANISOU 4461 CD GLN D 6 3117 3804 3409 -112 773 -477 C ATOM 4462 OE1 GLN D 6 -8.421 31.836 39.746 1.00 20.00 O ANISOU 4462 OE1 GLN D 6 2237 2889 2472 -122 697 -425 O ATOM 4463 NE2 GLN D 6 -9.118 31.425 41.792 1.00 21.80 N ANISOU 4463 NE2 GLN D 6 2513 3087 2684 -185 838 -510 N ATOM 4464 N ALA D 7 -14.353 30.842 41.230 1.00 25.77 N ANISOU 4464 N ALA D 7 2436 3861 3493 13 1020 -668 N ATOM 4465 CA ALA D 7 -15.277 31.320 42.251 1.00 27.92 C ANISOU 4465 CA ALA D 7 2670 4125 3812 56 1169 -731 C ATOM 4466 C ALA D 7 -15.184 30.480 43.511 1.00 35.53 C ANISOU 4466 C ALA D 7 3712 5078 4711 -82 1291 -768 C ATOM 4467 O ALA D 7 -14.950 29.270 43.396 1.00 35.05 O ANISOU 4467 O ALA D 7 3643 5054 4619 -199 1260 -753 O ATOM 4468 CB ALA D 7 -16.713 31.295 41.726 1.00 29.36 C ANISOU 4468 CB ALA D 7 2612 4420 4123 136 1179 -765 C ATOM 4469 N PRO D 8 -15.411 31.072 44.722 1.00 34.19 N ANISOU 4469 N PRO D 8 3627 4851 4512 -69 1436 -818 N ATOM 4470 CA PRO D 8 -15.656 32.508 45.013 1.00 33.82 C ANISOU 4470 CA PRO D 8 3624 4730 4496 69 1496 -851 C ATOM 4471 C PRO D 8 -14.360 33.319 44.935 1.00 33.29 C ANISOU 4471 C PRO D 8 3758 4543 4349 79 1405 -807 C ATOM 4472 O PRO D 8 -13.300 32.747 45.080 1.00 30.72 O ANISOU 4472 O PRO D 8 3546 4197 3929 -34 1340 -769 O ATOM 4473 CB PRO D 8 -16.214 32.479 46.441 1.00 36.75 C ANISOU 4473 CB PRO D 8 4046 5089 4827 26 1696 -929 C ATOM 4474 CG PRO D 8 -15.573 31.289 47.076 1.00 41.07 C ANISOU 4474 CG PRO D 8 4703 5644 5257 -153 1702 -906 C ATOM 4475 CD PRO D 8 -15.392 30.268 45.964 1.00 36.05 C ANISOU 4475 CD PRO D 8 3953 5080 4663 -205 1560 -847 C ATOM 4476 N THR D 9 -14.433 34.634 44.746 1.00 29.88 N ANISOU 4476 N THR D 9 3369 4026 3958 210 1406 -814 N ATOM 4477 CA THR D 9 -13.208 35.430 44.680 1.00 30.24 C ANISOU 4477 CA THR D 9 3605 3950 3933 195 1327 -775 C ATOM 4478 C THR D 9 -12.721 35.799 46.087 1.00 35.19 C ANISOU 4478 C THR D 9 4433 4483 4454 121 1426 -836 C ATOM 4479 O THR D 9 -11.557 36.162 46.263 1.00 33.43 O ANISOU 4479 O THR D 9 4373 4179 4150 49 1357 -812 O ATOM 4480 CB THR D 9 -13.384 36.653 43.775 1.00 41.66 C ANISOU 4480 CB THR D 9 5042 5327 5460 351 1268 -740 C ATOM 4481 OG1 THR D 9 -14.592 37.321 44.112 1.00 40.94 O ANISOU 4481 OG1 THR D 9 4875 5219 5462 495 1384 -804 O ATOM 4482 CG2 THR D 9 -13.374 36.277 42.282 1.00 43.84 C ANISOU 4482 CG2 THR D 9 5188 5687 5782 386 1120 -654 C ATOM 4483 N SER D 10 -13.591 35.642 47.091 1.00 33.95 N ANISOU 4483 N SER D 10 4262 4348 4290 122 1588 -918 N ATOM 4484 CA SER D 10 -13.252 35.937 48.471 1.00 35.37 C ANISOU 4484 CA SER D 10 4642 4449 4347 48 1694 -986 C ATOM 4485 C SER D 10 -14.036 35.038 49.409 1.00 38.93 C ANISOU 4485 C SER D 10 5049 4984 4757 -20 1847 -1039 C ATOM 4486 O SER D 10 -15.232 34.796 49.189 1.00 39.96 O ANISOU 4486 O SER D 10 4989 5198 4997 51 1941 -1068 O ATOM 4487 CB SER D 10 -13.536 37.402 48.779 1.00 43.24 C ANISOU 4487 CB SER D 10 5741 5315 5374 171 1776 -1055 C ATOM 4488 OG SER D 10 -13.015 37.740 50.050 1.00 61.64 O ANISOU 4488 OG SER D 10 8302 7559 7561 80 1852 -1125 O ATOM 4489 N GLN D 11 -13.365 34.545 50.457 1.00 32.93 N ANISOU 4489 N GLN D 11 4467 4206 3839 -163 1869 -1047 N ATOM 4490 CA GLN D 11 -13.993 33.688 51.472 1.00 33.15 C ANISOU 4490 CA GLN D 11 4504 4297 3792 -252 2023 -1086 C ATOM 4491 C GLN D 11 -13.219 33.735 52.794 1.00 34.88 C ANISOU 4491 C GLN D 11 4994 4451 3809 -370 2054 -1114 C ATOM 4492 O GLN D 11 -11.981 33.703 52.810 1.00 31.54 O ANISOU 4492 O GLN D 11 4703 3985 3298 -444 1897 -1061 O ATOM 4493 CB GLN D 11 -14.066 32.233 50.956 1.00 33.51 C ANISOU 4493 CB GLN D 11 4414 4449 3868 -339 1959 -1010 C ATOM 4494 CG GLN D 11 -14.749 31.224 51.885 1.00 51.17 C ANISOU 4494 CG GLN D 11 6654 6748 6040 -449 2118 -1031 C ATOM 4495 CD GLN D 11 -16.250 31.196 51.759 1.00 66.12 C ANISOU 4495 CD GLN D 11 8329 8726 8067 -386 2286 -1092 C ATOM 4496 OE1 GLN D 11 -16.806 30.947 50.688 1.00 62.20 O ANISOU 4496 OE1 GLN D 11 7606 8303 7724 -330 2225 -1071 O ATOM 4497 NE2 GLN D 11 -16.937 31.363 52.877 1.00 61.28 N ANISOU 4497 NE2 GLN D 11 7776 8117 7391 -408 2503 -1170 N ATOM 4498 N ILE D 12 -13.971 33.817 53.898 1.00 33.06 N ANISOU 4498 N ILE D 12 4838 4223 3502 -388 2260 -1199 N ATOM 4499 CA ILE D 12 -13.472 33.686 55.259 1.00 32.64 C ANISOU 4499 CA ILE D 12 5041 4131 3229 -513 2317 -1229 C ATOM 4500 C ILE D 12 -14.033 32.367 55.717 1.00 38.86 C ANISOU 4500 C ILE D 12 5781 5014 3968 -617 2419 -1194 C ATOM 4501 O ILE D 12 -15.233 32.130 55.573 1.00 39.31 O ANISOU 4501 O ILE D 12 5659 5142 4135 -574 2579 -1230 O ATOM 4502 CB ILE D 12 -13.788 34.851 56.229 1.00 36.21 C ANISOU 4502 CB ILE D 12 5668 4496 3595 -468 2481 -1360 C ATOM 4503 CG1 ILE D 12 -13.252 36.196 55.696 1.00 35.80 C ANISOU 4503 CG1 ILE D 12 5670 4323 3608 -367 2380 -1393 C ATOM 4504 CG2 ILE D 12 -13.227 34.541 57.639 1.00 36.57 C ANISOU 4504 CG2 ILE D 12 5996 4521 3379 -622 2520 -1382 C ATOM 4505 CD1 ILE D 12 -13.772 37.413 56.485 1.00 39.01 C ANISOU 4505 CD1 ILE D 12 6224 4624 3974 -286 2564 -1539 C ATOM 4506 N LEU D 13 -13.174 31.508 56.247 1.00 36.84 N ANISOU 4506 N LEU D 13 5680 4759 3558 -755 2322 -1119 N ATOM 4507 CA LEU D 13 -13.558 30.169 56.662 1.00 38.48 C ANISOU 4507 CA LEU D 13 5880 5032 3709 -869 2395 -1063 C ATOM 4508 C LEU D 13 -12.996 29.821 58.029 1.00 40.75 C ANISOU 4508 C LEU D 13 6456 5288 3740 -1000 2420 -1047 C ATOM 4509 O LEU D 13 -11.834 30.122 58.306 1.00 38.74 O ANISOU 4509 O LEU D 13 6372 4980 3369 -1030 2251 -1020 O ATOM 4510 CB LEU D 13 -12.968 29.231 55.596 1.00 38.17 C ANISOU 4510 CB LEU D 13 5713 5020 3769 -886 2195 -949 C ATOM 4511 CG LEU D 13 -13.542 27.840 55.452 1.00 46.62 C ANISOU 4511 CG LEU D 13 6684 6150 4879 -971 2248 -889 C ATOM 4512 CD1 LEU D 13 -14.858 27.856 54.674 1.00 48.70 C ANISOU 4512 CD1 LEU D 13 6671 6491 5342 -906 2368 -941 C ATOM 4513 CD2 LEU D 13 -12.592 27.001 54.681 1.00 49.31 C ANISOU 4513 CD2 LEU D 13 7002 6481 5254 -995 2033 -784 C ATOM 4514 N ALA D 14 -13.819 29.200 58.896 1.00 39.16 N ANISOU 4514 N ALA D 14 6310 5125 3444 -1085 2628 -1063 N ATOM 4515 CA ALA D 14 -13.360 28.697 60.187 1.00 39.32 C ANISOU 4515 CA ALA D 14 6616 5123 3201 -1221 2653 -1027 C ATOM 4516 C ALA D 14 -12.502 27.448 59.932 1.00 40.83 C ANISOU 4516 C ALA D 14 6841 5311 3363 -1300 2451 -875 C ATOM 4517 O ALA D 14 -12.805 26.689 59.002 1.00 37.11 O ANISOU 4517 O ALA D 14 6166 4872 3063 -1287 2417 -820 O ATOM 4518 CB ALA D 14 -14.553 28.356 61.076 1.00 42.63 C ANISOU 4518 CB ALA D 14 7070 5587 3539 -1291 2954 -1078 C ATOM 4519 N ALA D 15 -11.426 27.244 60.721 1.00 38.97 N ANISOU 4519 N ALA D 15 6857 5035 2917 -1375 2308 -812 N ATOM 4520 CA ALA D 15 -10.557 26.067 60.580 1.00 38.47 C ANISOU 4520 CA ALA D 15 6841 4957 2819 -1431 2114 -665 C ATOM 4521 C ALA D 15 -11.355 24.779 60.812 1.00 42.79 C ANISOU 4521 C ALA D 15 7384 5519 3356 -1523 2260 -596 C ATOM 4522 O ALA D 15 -12.232 24.768 61.672 1.00 42.74 O ANISOU 4522 O ALA D 15 7471 5529 3238 -1594 2493 -642 O ATOM 4523 CB ALA D 15 -9.398 26.149 61.560 1.00 40.06 C ANISOU 4523 CB ALA D 15 7318 5123 2779 -1492 1952 -617 C ATOM 4524 N GLY D 16 -11.110 23.748 59.992 1.00 39.16 N ANISOU 4524 N GLY D 16 6806 5048 3025 -1522 2143 -498 N ATOM 4525 CA GLY D 16 -11.805 22.465 60.100 1.00 39.03 C ANISOU 4525 CA GLY D 16 6786 5024 3019 -1622 2264 -427 C ATOM 4526 C GLY D 16 -12.937 22.286 59.109 1.00 41.67 C ANISOU 4526 C GLY D 16 6831 5410 3591 -1603 2393 -485 C ATOM 4527 O GLY D 16 -13.443 21.177 58.938 1.00 42.35 O ANISOU 4527 O GLY D 16 6875 5484 3730 -1690 2459 -429 O ATOM 4528 N ARG D 17 -13.326 23.361 58.416 1.00 36.36 N ANISOU 4528 N ARG D 17 5960 4790 3067 -1492 2416 -593 N ATOM 4529 CA ARG D 17 -14.418 23.289 57.458 1.00 35.61 C ANISOU 4529 CA ARG D 17 5575 4760 3197 -1461 2517 -651 C ATOM 4530 C ARG D 17 -13.950 22.858 56.066 1.00 36.62 C ANISOU 4530 C ARG D 17 5530 4884 3501 -1400 2313 -606 C ATOM 4531 O ARG D 17 -12.800 23.094 55.684 1.00 32.57 O ANISOU 4531 O ARG D 17 5069 4331 2973 -1332 2105 -565 O ATOM 4532 CB ARG D 17 -15.138 24.638 57.382 1.00 39.35 C ANISOU 4532 CB ARG D 17 5919 5288 3746 -1355 2643 -782 C ATOM 4533 CG ARG D 17 -16.108 24.817 58.558 1.00 48.28 C ANISOU 4533 CG ARG D 17 7132 6449 4764 -1426 2929 -850 C ATOM 4534 CD ARG D 17 -16.985 26.042 58.419 1.00 66.15 C ANISOU 4534 CD ARG D 17 9231 8765 7139 -1303 3081 -986 C ATOM 4535 NE ARG D 17 -18.014 25.891 57.387 1.00 79.54 N ANISOU 4535 NE ARG D 17 10592 10545 9085 -1254 3131 -1020 N ATOM 4536 CZ ARG D 17 -19.221 25.370 57.593 1.00 98.69 C ANISOU 4536 CZ ARG D 17 12868 13049 11580 -1333 3352 -1054 C ATOM 4537 NH1 ARG D 17 -19.565 24.926 58.798 1.00 87.68 N ANISOU 4537 NH1 ARG D 17 11643 11654 10017 -1469 3563 -1052 N ATOM 4538 NH2 ARG D 17 -20.090 25.279 56.595 1.00 86.42 N ANISOU 4538 NH2 ARG D 17 10994 11582 10259 -1285 3360 -1086 N ATOM 4539 N ARG D 18 -14.858 22.192 55.329 1.00 32.80 N ANISOU 4539 N ARG D 18 4841 4445 3177 -1437 2380 -619 N ATOM 4540 CA ARG D 18 -14.647 21.763 53.960 1.00 30.69 C ANISOU 4540 CA ARG D 18 4398 4185 3076 -1389 2219 -599 C ATOM 4541 C ARG D 18 -14.899 22.966 53.040 1.00 32.69 C ANISOU 4541 C ARG D 18 4446 4504 3469 -1241 2173 -680 C ATOM 4542 O ARG D 18 -15.840 23.727 53.261 1.00 31.64 O ANISOU 4542 O ARG D 18 4208 4432 3384 -1202 2325 -763 O ATOM 4543 CB ARG D 18 -15.570 20.582 53.619 1.00 33.14 C ANISOU 4543 CB ARG D 18 4591 4515 3485 -1510 2312 -591 C ATOM 4544 CG ARG D 18 -15.374 20.057 52.190 1.00 32.91 C ANISOU 4544 CG ARG D 18 4402 4491 3613 -1475 2146 -582 C ATOM 4545 CD ARG D 18 -16.345 18.939 51.880 1.00 31.51 C ANISOU 4545 CD ARG D 18 4111 4329 3531 -1614 2238 -591 C ATOM 4546 NE ARG D 18 -16.122 18.420 50.529 1.00 30.96 N ANISOU 4546 NE ARG D 18 3918 4258 3589 -1586 2075 -593 N ATOM 4547 CZ ARG D 18 -15.259 17.457 50.235 1.00 37.39 C ANISOU 4547 CZ ARG D 18 4863 4969 4374 -1612 1951 -524 C ATOM 4548 NH1 ARG D 18 -14.508 16.911 51.189 1.00 25.51 N ANISOU 4548 NH1 ARG D 18 3611 3356 2727 -1657 1950 -434 N ATOM 4549 NH2 ARG D 18 -15.128 17.038 48.985 1.00 28.59 N ANISOU 4549 NH2 ARG D 18 3636 3858 3370 -1586 1823 -545 N ATOM 4550 N AMET D 19 -14.059 23.137 52.016 0.50 26.99 N ANISOU 4550 N AMET D 19 3674 3767 2813 -1152 1971 -653 N ATOM 4551 N BMET D 19 -14.040 23.140 52.023 0.50 29.51 N ANISOU 4551 N BMET D 19 3996 4085 3130 -1152 1970 -652 N ATOM 4552 CA AMET D 19 -14.225 24.224 51.067 0.50 26.53 C ANISOU 4552 CA AMET D 19 3445 3757 2877 -1014 1911 -709 C ATOM 4553 CA BMET D 19 -14.102 24.247 51.076 0.50 30.12 C ANISOU 4553 CA BMET D 19 3915 4205 3322 -1011 1898 -704 C ATOM 4554 C AMET D 19 -13.776 23.782 49.678 0.50 27.93 C ANISOU 4554 C AMET D 19 3507 3945 3160 -974 1734 -674 C ATOM 4555 C BMET D 19 -13.747 23.769 49.662 0.50 29.60 C ANISOU 4555 C BMET D 19 3720 4155 3371 -974 1730 -673 C ATOM 4556 O AMET D 19 -12.729 23.150 49.545 0.50 26.70 O ANISOU 4556 O AMET D 19 3461 3732 2951 -998 1609 -607 O ATOM 4557 O BMET D 19 -12.728 23.104 49.495 0.50 28.40 O ANISOU 4557 O BMET D 19 3672 3948 3172 -999 1605 -606 O ATOM 4558 CB AMET D 19 -13.441 25.462 51.535 0.50 28.92 C ANISOU 4558 CB AMET D 19 3883 4014 3090 -931 1866 -723 C ATOM 4559 CB BMET D 19 -13.105 25.330 51.555 0.50 33.40 C ANISOU 4559 CB BMET D 19 4491 4566 3634 -941 1827 -702 C ATOM 4560 CG AMET D 19 -13.605 26.670 50.646 0.50 32.59 C ANISOU 4560 CG AMET D 19 4209 4504 3671 -789 1817 -771 C ATOM 4561 CG BMET D 19 -12.713 26.366 50.523 0.50 37.94 C ANISOU 4561 CG BMET D 19 4968 5147 4302 -809 1703 -719 C ATOM 4562 SD AMET D 19 -15.318 27.224 50.559 0.50 38.02 S ANISOU 4562 SD AMET D 19 4679 5275 4493 -724 2007 -868 S ATOM 4563 SD BMET D 19 -13.840 27.767 50.538 0.50 45.52 S ANISOU 4563 SD BMET D 19 5810 6139 5347 -692 1843 -821 S ATOM 4564 CE AMET D 19 -15.264 28.133 49.058 0.50 33.72 C ANISOU 4564 CE AMET D 19 3964 4752 4097 -562 1855 -870 C ATOM 4565 CE BMET D 19 -12.879 28.918 49.661 0.50 41.05 C ANISOU 4565 CE BMET D 19 5257 5524 4817 -573 1671 -804 C ATOM 4566 N THR D 20 -14.565 24.127 48.650 1.00 24.50 N ANISOU 4566 N THR D 20 2852 3586 2870 -907 1724 -722 N ATOM 4567 CA THR D 20 -14.246 23.829 47.254 1.00 23.99 C ANISOU 4567 CA THR D 20 2677 3544 2894 -864 1565 -703 C ATOM 4568 C THR D 20 -14.158 25.153 46.481 1.00 27.66 C ANISOU 4568 C THR D 20 3055 4037 3418 -713 1489 -724 C ATOM 4569 O THR D 20 -15.083 25.970 46.511 1.00 29.46 O ANISOU 4569 O THR D 20 3167 4314 3713 -643 1570 -777 O ATOM 4570 CB THR D 20 -15.241 22.821 46.604 1.00 32.57 C ANISOU 4570 CB THR D 20 3596 4695 4085 -945 1590 -731 C ATOM 4571 OG1 THR D 20 -15.155 21.587 47.319 1.00 34.41 O ANISOU 4571 OG1 THR D 20 3951 4869 4254 -1090 1653 -697 O ATOM 4572 CG2 THR D 20 -14.917 22.536 45.097 1.00 27.44 C ANISOU 4572 CG2 THR D 20 2849 4072 3506 -901 1420 -723 C ATOM 4573 N LEU D 21 -13.050 25.347 45.793 1.00 22.23 N ANISOU 4573 N LEU D 21 2424 3314 2707 -663 1339 -678 N ATOM 4574 CA LEU D 21 -12.875 26.450 44.863 1.00 21.97 C ANISOU 4574 CA LEU D 21 2324 3298 2727 -537 1251 -679 C ATOM 4575 C LEU D 21 -13.180 25.931 43.459 1.00 25.41 C ANISOU 4575 C LEU D 21 2610 3801 3244 -521 1153 -677 C ATOM 4576 O LEU D 21 -12.670 24.887 43.054 1.00 23.85 O ANISOU 4576 O LEU D 21 2441 3594 3027 -587 1089 -653 O ATOM 4577 CB LEU D 21 -11.472 27.065 44.921 1.00 21.06 C ANISOU 4577 CB LEU D 21 2357 3111 2535 -506 1159 -633 C ATOM 4578 CG LEU D 21 -11.089 27.796 46.208 1.00 26.69 C ANISOU 4578 CG LEU D 21 3229 3757 3157 -518 1226 -644 C ATOM 4579 CD1 LEU D 21 -9.733 28.443 46.055 1.00 25.13 C ANISOU 4579 CD1 LEU D 21 3138 3502 2907 -497 1112 -602 C ATOM 4580 CD2 LEU D 21 -12.089 28.882 46.537 1.00 31.71 C ANISOU 4580 CD2 LEU D 21 3817 4397 3836 -441 1339 -708 C ATOM 4581 N AARG D 22 -14.028 26.660 42.736 0.50 22.31 N ANISOU 4581 N AARG D 22 2066 3474 2939 -427 1138 -704 N ATOM 4582 N BARG D 22 -14.032 26.651 42.739 0.50 23.45 N ANISOU 4582 N BARG D 22 2210 3618 3083 -428 1139 -704 N ATOM 4583 CA AARG D 22 -14.458 26.318 41.386 0.50 22.18 C ANISOU 4583 CA AARG D 22 1903 3537 2988 -404 1033 -708 C ATOM 4584 CA BARG D 22 -14.449 26.295 41.393 0.50 23.88 C ANISOU 4584 CA BARG D 22 2119 3751 3202 -406 1034 -708 C ATOM 4585 C AARG D 22 -13.585 27.013 40.362 0.50 25.17 C ANISOU 4585 C AARG D 22 2328 3897 3340 -313 903 -658 C ATOM 4586 C BARG D 22 -13.594 27.010 40.364 0.50 26.02 C ANISOU 4586 C BARG D 22 2434 4004 3447 -313 904 -659 C ATOM 4587 O AARG D 22 -13.179 28.152 40.571 0.50 23.77 O ANISOU 4587 O AARG D 22 2222 3667 3144 -231 906 -635 O ATOM 4588 O BARG D 22 -13.207 28.154 40.573 0.50 24.74 O ANISOU 4588 O BARG D 22 2341 3790 3268 -230 907 -636 O ATOM 4589 CB AARG D 22 -15.939 26.712 41.168 0.50 22.84 C ANISOU 4589 CB AARG D 22 1778 3718 3184 -347 1076 -758 C ATOM 4590 CB BARG D 22 -15.932 26.656 41.198 0.50 27.66 C ANISOU 4590 CB BARG D 22 2392 4327 3792 -354 1079 -759 C ATOM 4591 CG AARG D 22 -16.908 26.149 42.211 0.50 27.30 C ANISOU 4591 CG AARG D 22 2273 4314 3786 -440 1237 -812 C ATOM 4592 CG BARG D 22 -16.803 25.470 40.819 0.50 43.92 C ANISOU 4592 CG BARG D 22 4303 6473 5911 -463 1077 -800 C ATOM 4593 CD AARG D 22 -18.377 26.460 41.919 0.50 36.39 C ANISOU 4593 CD AARG D 22 3174 5582 5069 -385 1275 -866 C ATOM 4594 CD BARG D 22 -17.757 25.042 41.926 0.50 56.67 C ANISOU 4594 CD BARG D 22 5849 8114 7569 -554 1249 -850 C ATOM 4595 NE AARG D 22 -18.741 27.870 42.120 0.50 40.38 N ANISOU 4595 NE AARG D 22 3639 6081 5622 -216 1317 -875 N ATOM 4596 NE BARG D 22 -17.365 23.778 42.559 0.50 64.18 N ANISOU 4596 NE BARG D 22 6924 9005 8456 -719 1307 -842 N ATOM 4597 CZ AARG D 22 -19.014 28.421 43.301 0.50 55.67 C ANISOU 4597 CZ AARG D 22 5622 7976 7552 -191 1485 -910 C ATOM 4598 CZ BARG D 22 -17.594 22.569 42.048 0.50 75.92 C ANISOU 4598 CZ BARG D 22 8366 10513 9967 -842 1266 -858 C ATOM 4599 NH1AARG D 22 -18.941 27.699 44.412 0.50 47.53 N ANISOU 4599 NH1AARG D 22 4689 6915 6455 -330 1624 -930 N ATOM 4600 NH1BARG D 22 -17.213 21.482 42.705 0.50 54.82 N ANISOU 4600 NH1BARG D 22 5833 7760 7237 -979 1327 -840 N ATOM 4601 NH2AARG D 22 -19.351 29.700 43.380 0.50 44.02 N ANISOU 4601 NH2AARG D 22 4116 6479 6129 -25 1517 -926 N ATOM 4602 NH2BARG D 22 -18.192 22.440 40.871 0.50 70.44 N ANISOU 4602 NH2BARG D 22 7502 9914 9349 -829 1157 -890 N ATOM 4603 N CYS D 23 -13.297 26.327 39.260 1.00 22.03 N ANISOU 4603 N CYS D 23 1901 3536 2932 -337 798 -646 N ATOM 4604 CA CYS D 23 -12.563 26.878 38.129 1.00 21.01 C ANISOU 4604 CA CYS D 23 1806 3408 2770 -263 685 -600 C ATOM 4605 C CYS D 23 -13.149 26.306 36.854 1.00 25.75 C ANISOU 4605 C CYS D 23 2291 4102 3392 -268 590 -621 C ATOM 4606 O CYS D 23 -13.266 25.081 36.714 1.00 25.74 O ANISOU 4606 O CYS D 23 2272 4120 3389 -368 586 -659 O ATOM 4607 CB CYS D 23 -11.068 26.623 38.215 1.00 19.95 C ANISOU 4607 CB CYS D 23 1821 3201 2558 -300 661 -558 C ATOM 4608 SG CYS D 23 -10.139 27.325 36.834 1.00 23.57 S ANISOU 4608 SG CYS D 23 2318 3666 2970 -226 553 -500 S ATOM 4609 N THR D 24 -13.505 27.185 35.918 1.00 22.20 N ANISOU 4609 N THR D 24 1778 3701 2954 -163 507 -596 N ATOM 4610 CA THR D 24 -14.063 26.717 34.654 1.00 23.50 C ANISOU 4610 CA THR D 24 1844 3966 3118 -165 395 -615 C ATOM 4611 C THR D 24 -13.481 27.529 33.520 1.00 26.02 C ANISOU 4611 C THR D 24 2227 4290 3370 -73 293 -550 C ATOM 4612 O THR D 24 -13.216 28.726 33.675 1.00 26.23 O ANISOU 4612 O THR D 24 2307 4262 3397 23 304 -493 O ATOM 4613 CB THR D 24 -15.630 26.720 34.675 1.00 36.78 C ANISOU 4613 CB THR D 24 3321 5751 4903 -148 388 -665 C ATOM 4614 OG1 THR D 24 -16.116 26.043 33.511 1.00 43.29 O ANISOU 4614 OG1 THR D 24 4057 6677 5715 -188 265 -696 O ATOM 4615 CG2 THR D 24 -16.234 28.110 34.729 1.00 38.44 C ANISOU 4615 CG2 THR D 24 3462 5972 5173 9 381 -630 C ATOM 4616 N GLN D 25 -13.278 26.874 32.390 1.00 22.03 N ANISOU 4616 N GLN D 25 1731 3841 2800 -109 203 -560 N ATOM 4617 CA GLN D 25 -12.770 27.518 31.179 1.00 21.24 C ANISOU 4617 CA GLN D 25 1700 3759 2612 -38 109 -497 C ATOM 4618 C GLN D 25 -13.460 26.910 29.965 1.00 27.28 C ANISOU 4618 C GLN D 25 2390 4641 3335 -59 -15 -535 C ATOM 4619 O GLN D 25 -13.677 25.693 29.917 1.00 27.61 O ANISOU 4619 O GLN D 25 2398 4714 3379 -168 -15 -614 O ATOM 4620 CB GLN D 25 -11.225 27.457 31.068 1.00 20.05 C ANISOU 4620 CB GLN D 25 1710 3531 2376 -68 151 -459 C ATOM 4621 CG GLN D 25 -10.583 26.051 31.189 1.00 21.64 C ANISOU 4621 CG GLN D 25 1955 3715 2552 -179 192 -518 C ATOM 4622 CD GLN D 25 -10.517 25.228 29.910 1.00 25.71 C ANISOU 4622 CD GLN D 25 2487 4296 2985 -216 119 -559 C ATOM 4623 OE1 GLN D 25 -10.360 24.001 29.928 1.00 24.38 O ANISOU 4623 OE1 GLN D 25 2336 4115 2813 -299 141 -627 O ATOM 4624 NE2 GLN D 25 -10.604 25.865 28.772 1.00 14.93 N ANISOU 4624 NE2 GLN D 25 1139 2992 1543 -156 34 -519 N ATOM 4625 N ASP D 26 -13.794 27.745 28.983 1.00 25.34 N ANISOU 4625 N ASP D 26 2132 4451 3043 40 -126 -478 N ATOM 4626 CA ASP D 26 -14.460 27.269 27.763 1.00 27.32 C ANISOU 4626 CA ASP D 26 2323 4826 3232 24 -270 -509 C ATOM 4627 C ASP D 26 -13.549 27.436 26.530 1.00 31.84 C ANISOU 4627 C ASP D 26 3054 5403 3639 38 -329 -457 C ATOM 4628 O ASP D 26 -14.035 27.483 25.404 1.00 34.38 O ANISOU 4628 O ASP D 26 3364 5824 3877 63 -467 -448 O ATOM 4629 CB ASP D 26 -15.803 28.009 27.573 1.00 30.54 C ANISOU 4629 CB ASP D 26 2564 5324 3716 131 -377 -486 C ATOM 4630 CG ASP D 26 -15.675 29.516 27.482 1.00 40.12 C ANISOU 4630 CG ASP D 26 3834 6481 4929 293 -395 -370 C ATOM 4631 OD1 ASP D 26 -14.555 30.036 27.709 1.00 37.72 O ANISOU 4631 OD1 ASP D 26 3694 6063 4575 304 -310 -312 O ATOM 4632 OD2 ASP D 26 -16.696 30.181 27.184 1.00 53.23 O ANISOU 4632 OD2 ASP D 26 5373 8209 6644 411 -498 -337 O ATOM 4633 N MET D 27 -12.226 27.496 26.748 1.00 25.52 N ANISOU 4633 N MET D 27 2399 4508 2790 15 -224 -425 N ATOM 4634 CA MET D 27 -11.243 27.651 25.673 1.00 24.51 C ANISOU 4634 CA MET D 27 2420 4381 2511 18 -239 -378 C ATOM 4635 C MET D 27 -10.814 26.299 25.071 1.00 27.28 C ANISOU 4635 C MET D 27 2820 4766 2778 -87 -231 -472 C ATOM 4636 O MET D 27 -9.952 26.271 24.195 1.00 27.30 O ANISOU 4636 O MET D 27 2945 4776 2651 -94 -217 -452 O ATOM 4637 CB MET D 27 -10.018 28.409 26.224 1.00 24.83 C ANISOU 4637 CB MET D 27 2568 4309 2557 38 -122 -302 C ATOM 4638 CG MET D 27 -10.377 29.821 26.650 1.00 27.78 C ANISOU 4638 CG MET D 27 2934 4628 2993 142 -132 -211 C ATOM 4639 SD MET D 27 -8.990 30.793 27.265 1.00 31.15 S ANISOU 4639 SD MET D 27 3491 4919 3425 141 -11 -129 S ATOM 4640 CE MET D 27 -8.814 30.133 28.964 1.00 26.07 C ANISOU 4640 CE MET D 27 2783 4210 2911 72 99 -211 C ATOM 4641 N ARG D 28 -11.378 25.180 25.572 1.00 22.79 N ANISOU 4641 N ARG D 28 2166 4209 2285 -171 -222 -577 N ATOM 4642 CA ARG D 28 -11.044 23.802 25.175 1.00 23.71 C ANISOU 4642 CA ARG D 28 2336 4326 2348 -274 -202 -682 C ATOM 4643 C ARG D 28 -9.584 23.486 25.523 1.00 24.96 C ANISOU 4643 C ARG D 28 2609 4384 2491 -285 -67 -673 C ATOM 4644 O ARG D 28 -8.953 22.657 24.868 1.00 25.45 O ANISOU 4644 O ARG D 28 2759 4440 2471 -326 -40 -733 O ATOM 4645 CB ARG D 28 -11.351 23.509 23.676 1.00 28.42 C ANISOU 4645 CB ARG D 28 2982 5025 2789 -293 -324 -722 C ATOM 4646 N HIS D 29 -9.051 24.138 26.571 1.00 19.80 N ANISOU 4646 N HIS D 29 1949 3653 1921 -247 17 -604 N ATOM 4647 CA HIS D 29 -7.679 23.898 27.014 1.00 18.01 C ANISOU 4647 CA HIS D 29 1801 3344 1699 -255 129 -589 C ATOM 4648 C HIS D 29 -7.597 22.553 27.697 1.00 22.04 C ANISOU 4648 C HIS D 29 2306 3793 2275 -325 181 -673 C ATOM 4649 O HIS D 29 -8.448 22.232 28.519 1.00 21.15 O ANISOU 4649 O HIS D 29 2122 3664 2249 -364 176 -702 O ATOM 4650 CB HIS D 29 -7.219 25.013 27.971 1.00 17.51 C ANISOU 4650 CB HIS D 29 1731 3219 1701 -208 180 -497 C ATOM 4651 CG HIS D 29 -6.859 26.283 27.260 1.00 20.82 C ANISOU 4651 CG HIS D 29 2203 3659 2049 -147 159 -404 C ATOM 4652 ND1 HIS D 29 -6.513 27.413 27.956 1.00 21.17 N ANISOU 4652 ND1 HIS D 29 2260 3642 2141 -112 194 -324 N ATOM 4653 CD2 HIS D 29 -6.729 26.527 25.929 1.00 23.37 C ANISOU 4653 CD2 HIS D 29 2589 4045 2245 -128 115 -379 C ATOM 4654 CE1 HIS D 29 -6.224 28.324 27.043 1.00 21.55 C ANISOU 4654 CE1 HIS D 29 2376 3709 2104 -74 171 -248 C ATOM 4655 NE2 HIS D 29 -6.320 27.830 25.810 1.00 22.82 N ANISOU 4655 NE2 HIS D 29 2571 3948 2151 -80 126 -272 N ATOM 4656 N ASN D 30 -6.584 21.767 27.368 1.00 18.99 N ANISOU 4656 N ASN D 30 1998 3369 1849 -336 240 -709 N ATOM 4657 CA ASN D 30 -6.433 20.452 28.005 1.00 18.91 C ANISOU 4657 CA ASN D 30 2006 3276 1903 -389 289 -780 C ATOM 4658 C ASN D 30 -5.751 20.551 29.366 1.00 20.77 C ANISOU 4658 C ASN D 30 2236 3426 2229 -374 358 -723 C ATOM 4659 O ASN D 30 -6.057 19.766 30.271 1.00 20.70 O ANISOU 4659 O ASN D 30 2225 3348 2291 -420 380 -751 O ATOM 4660 CB ASN D 30 -5.637 19.516 27.077 1.00 18.21 C ANISOU 4660 CB ASN D 30 2008 3171 1741 -389 327 -850 C ATOM 4661 CG ASN D 30 -6.469 19.103 25.883 1.00 40.86 C ANISOU 4661 CG ASN D 30 4901 6111 4513 -435 250 -936 C ATOM 4662 OD1 ASN D 30 -6.134 19.381 24.716 1.00 30.69 O ANISOU 4662 OD1 ASN D 30 3671 4889 3099 -409 237 -943 O ATOM 4663 ND2 ASN D 30 -7.621 18.500 26.155 1.00 31.11 N ANISOU 4663 ND2 ASN D 30 3618 4874 3328 -515 194 -999 N ATOM 4664 N ALA D 31 -4.821 21.490 29.512 1.00 14.91 N ANISOU 4664 N ALA D 31 1501 2686 1479 -319 387 -643 N ATOM 4665 CA ALA D 31 -4.061 21.567 30.760 1.00 15.59 C ANISOU 4665 CA ALA D 31 1587 2699 1637 -310 434 -594 C ATOM 4666 C ALA D 31 -4.619 22.632 31.707 1.00 17.02 C ANISOU 4666 C ALA D 31 1729 2877 1859 -311 420 -537 C ATOM 4667 O ALA D 31 -4.909 23.763 31.291 1.00 15.28 O ANISOU 4667 O ALA D 31 1492 2703 1611 -281 392 -495 O ATOM 4668 CB ALA D 31 -2.575 21.816 30.467 1.00 15.97 C ANISOU 4668 CB ALA D 31 1655 2747 1665 -266 480 -553 C ATOM 4669 N MET D 32 -4.851 22.230 32.976 1.00 13.07 N ANISOU 4669 N MET D 32 1230 2316 1421 -345 443 -538 N ATOM 4670 CA MET D 32 -5.343 23.133 34.027 1.00 12.11 C ANISOU 4670 CA MET D 32 1087 2179 1333 -348 451 -500 C ATOM 4671 C MET D 32 -4.477 22.983 35.272 1.00 17.61 C ANISOU 4671 C MET D 32 1832 2806 2053 -362 481 -464 C ATOM 4672 O MET D 32 -3.811 21.954 35.459 1.00 16.96 O ANISOU 4672 O MET D 32 1784 2679 1979 -370 491 -473 O ATOM 4673 CB MET D 32 -6.828 22.886 34.321 1.00 13.81 C ANISOU 4673 CB MET D 32 1249 2415 1584 -387 449 -545 C ATOM 4674 CG MET D 32 -7.697 23.261 33.120 1.00 16.67 C ANISOU 4674 CG MET D 32 1547 2865 1923 -362 390 -569 C ATOM 4675 SD MET D 32 -9.451 23.174 33.405 1.00 20.63 S ANISOU 4675 SD MET D 32 1933 3417 2486 -398 378 -619 S ATOM 4676 CE MET D 32 -9.673 24.709 34.337 1.00 17.78 C ANISOU 4676 CE MET D 32 1554 3039 2163 -327 414 -559 C ATOM 4677 N TYR D 33 -4.401 24.075 36.055 1.00 12.43 N ANISOU 4677 N TYR D 33 1186 2137 1402 -355 488 -421 N ATOM 4678 CA TYR D 33 -3.500 24.183 37.188 1.00 12.60 C ANISOU 4678 CA TYR D 33 1257 2105 1425 -372 495 -383 C ATOM 4679 C TYR D 33 -4.125 24.935 38.325 1.00 17.47 C ANISOU 4679 C TYR D 33 1901 2695 2042 -394 520 -378 C ATOM 4680 O TYR D 33 -4.887 25.870 38.074 1.00 16.46 O ANISOU 4680 O TYR D 33 1746 2588 1921 -369 529 -385 O ATOM 4681 CB TYR D 33 -2.253 25.001 36.764 1.00 13.26 C ANISOU 4681 CB TYR D 33 1338 2205 1496 -348 474 -336 C ATOM 4682 CG TYR D 33 -1.619 24.635 35.435 1.00 17.63 C ANISOU 4682 CG TYR D 33 1860 2804 2037 -317 473 -341 C ATOM 4683 CD1 TYR D 33 -0.482 23.829 35.377 1.00 22.58 C ANISOU 4683 CD1 TYR D 33 2478 3424 2678 -303 476 -336 C ATOM 4684 CD2 TYR D 33 -2.149 25.099 34.238 1.00 18.38 C ANISOU 4684 CD2 TYR D 33 1936 2948 2098 -295 469 -349 C ATOM 4685 CE1 TYR D 33 0.127 23.523 34.151 1.00 26.88 C ANISOU 4685 CE1 TYR D 33 2995 4011 3206 -270 497 -350 C ATOM 4686 CE2 TYR D 33 -1.590 24.746 33.013 1.00 20.40 C ANISOU 4686 CE2 TYR D 33 2184 3249 2318 -273 479 -359 C ATOM 4687 CZ TYR D 33 -0.411 24.022 32.974 1.00 29.38 C ANISOU 4687 CZ TYR D 33 3312 4380 3471 -262 505 -361 C ATOM 4688 OH TYR D 33 0.170 23.774 31.748 1.00 32.81 O ANISOU 4688 OH TYR D 33 3739 4862 3864 -237 537 -377 O ATOM 4689 N TRP D 34 -3.693 24.626 39.551 1.00 13.86 N ANISOU 4689 N TRP D 34 1507 2189 1571 -430 526 -361 N ATOM 4690 CA TRP D 34 -4.019 25.402 40.749 1.00 14.75 C ANISOU 4690 CA TRP D 34 1676 2270 1660 -456 555 -358 C ATOM 4691 C TRP D 34 -2.745 25.828 41.417 1.00 17.86 C ANISOU 4691 C TRP D 34 2127 2638 2022 -474 509 -317 C ATOM 4692 O TRP D 34 -1.915 24.975 41.739 1.00 16.36 O ANISOU 4692 O TRP D 34 1957 2434 1823 -484 469 -290 O ATOM 4693 CB TRP D 34 -4.892 24.627 41.764 1.00 12.95 C ANISOU 4693 CB TRP D 34 1490 2014 1419 -505 612 -381 C ATOM 4694 CG TRP D 34 -6.357 24.728 41.475 1.00 13.79 C ANISOU 4694 CG TRP D 34 1525 2153 1561 -503 673 -431 C ATOM 4695 CD1 TRP D 34 -7.155 23.766 40.919 1.00 16.29 C ANISOU 4695 CD1 TRP D 34 1779 2496 1915 -526 689 -464 C ATOM 4696 CD2 TRP D 34 -7.204 25.858 41.734 1.00 14.15 C ANISOU 4696 CD2 TRP D 34 1545 2211 1619 -474 723 -456 C ATOM 4697 NE1 TRP D 34 -8.439 24.241 40.783 1.00 16.60 N ANISOU 4697 NE1 TRP D 34 1733 2582 1994 -516 736 -506 N ATOM 4698 CE2 TRP D 34 -8.511 25.501 41.331 1.00 18.86 C ANISOU 4698 CE2 TRP D 34 2040 2856 2268 -475 764 -500 C ATOM 4699 CE3 TRP D 34 -6.971 27.167 42.216 1.00 15.77 C ANISOU 4699 CE3 TRP D 34 1802 2386 1803 -445 733 -451 C ATOM 4700 CZ2 TRP D 34 -9.601 26.379 41.458 1.00 19.21 C ANISOU 4700 CZ2 TRP D 34 2018 2929 2352 -431 821 -534 C ATOM 4701 CZ3 TRP D 34 -8.056 28.027 42.364 1.00 18.66 C ANISOU 4701 CZ3 TRP D 34 2130 2758 2201 -401 798 -489 C ATOM 4702 CH2 TRP D 34 -9.353 27.631 41.981 1.00 19.71 C ANISOU 4702 CH2 TRP D 34 2145 2950 2395 -384 841 -527 C ATOM 4703 N TYR D 35 -2.618 27.136 41.683 1.00 14.59 N ANISOU 4703 N TYR D 35 1742 2210 1593 -479 509 -314 N ATOM 4704 CA TYR D 35 -1.478 27.718 42.392 1.00 15.66 C ANISOU 4704 CA TYR D 35 1932 2321 1695 -519 458 -286 C ATOM 4705 C TYR D 35 -1.932 28.443 43.636 1.00 18.17 C ANISOU 4705 C TYR D 35 2353 2592 1961 -559 489 -314 C ATOM 4706 O TYR D 35 -3.062 28.930 43.687 1.00 16.77 O ANISOU 4706 O TYR D 35 2184 2398 1790 -535 562 -353 O ATOM 4707 CB TYR D 35 -0.757 28.762 41.495 1.00 16.74 C ANISOU 4707 CB TYR D 35 2030 2471 1859 -512 433 -264 C ATOM 4708 CG TYR D 35 -0.113 28.204 40.248 1.00 16.63 C ANISOU 4708 CG TYR D 35 1926 2511 1882 -480 414 -238 C ATOM 4709 CD1 TYR D 35 1.213 27.784 40.257 1.00 18.90 C ANISOU 4709 CD1 TYR D 35 2173 2825 2183 -496 364 -206 C ATOM 4710 CD2 TYR D 35 -0.794 28.193 39.034 1.00 18.03 C ANISOU 4710 CD2 TYR D 35 2057 2718 2076 -430 445 -248 C ATOM 4711 CE1 TYR D 35 1.828 27.297 39.101 1.00 17.64 C ANISOU 4711 CE1 TYR D 35 1929 2716 2055 -460 371 -193 C ATOM 4712 CE2 TYR D 35 -0.191 27.710 37.868 1.00 19.76 C ANISOU 4712 CE2 TYR D 35 2213 2988 2308 -404 440 -233 C ATOM 4713 CZ TYR D 35 1.115 27.247 37.914 1.00 22.08 C ANISOU 4713 CZ TYR D 35 2470 3302 2617 -417 415 -210 C ATOM 4714 OH TYR D 35 1.715 26.754 36.790 1.00 21.42 O ANISOU 4714 OH TYR D 35 2325 3269 2545 -385 432 -206 O ATOM 4715 N ARG D 36 -1.057 28.532 44.634 1.00 14.60 N ANISOU 4715 N ARG D 36 1975 2121 1452 -615 433 -298 N ATOM 4716 CA ARG D 36 -1.266 29.432 45.746 1.00 15.36 C ANISOU 4716 CA ARG D 36 2189 2167 1479 -664 454 -333 C ATOM 4717 C ARG D 36 -0.165 30.485 45.625 1.00 20.50 C ANISOU 4717 C ARG D 36 2849 2804 2135 -708 384 -321 C ATOM 4718 O ARG D 36 0.912 30.197 45.095 1.00 20.88 O ANISOU 4718 O ARG D 36 2819 2896 2220 -717 308 -276 O ATOM 4719 CB ARG D 36 -1.326 28.765 47.135 1.00 14.57 C ANISOU 4719 CB ARG D 36 2201 2052 1282 -714 450 -334 C ATOM 4720 CG ARG D 36 -0.113 27.938 47.508 1.00 17.13 C ANISOU 4720 CG ARG D 36 2528 2401 1578 -741 331 -274 C ATOM 4721 CD ARG D 36 -0.293 27.390 48.909 1.00 22.48 C ANISOU 4721 CD ARG D 36 3348 3056 2138 -790 326 -266 C ATOM 4722 NE ARG D 36 -0.232 28.477 49.892 1.00 26.75 N ANISOU 4722 NE ARG D 36 4016 3566 2580 -857 324 -312 N ATOM 4723 CZ ARG D 36 -0.448 28.324 51.185 1.00 31.47 C ANISOU 4723 CZ ARG D 36 4771 4142 3044 -913 334 -322 C ATOM 4724 NH1 ARG D 36 -0.801 27.138 51.669 1.00 22.65 N ANISOU 4724 NH1 ARG D 36 3705 3026 1877 -912 356 -279 N ATOM 4725 NH2 ARG D 36 -0.341 29.357 52.005 1.00 26.27 N ANISOU 4725 NH2 ARG D 36 4238 3453 2290 -977 330 -377 N ATOM 4726 N GLN D 37 -0.447 31.715 46.049 1.00 17.06 N ANISOU 4726 N GLN D 37 2505 2306 1672 -735 418 -365 N ATOM 4727 CA GLN D 37 0.550 32.764 45.939 1.00 16.18 C ANISOU 4727 CA GLN D 37 2415 2166 1568 -799 358 -359 C ATOM 4728 C GLN D 37 0.718 33.368 47.314 1.00 22.93 C ANISOU 4728 C GLN D 37 3424 2965 2324 -883 337 -409 C ATOM 4729 O GLN D 37 -0.266 33.773 47.920 1.00 21.77 O ANISOU 4729 O GLN D 37 3378 2760 2132 -863 426 -469 O ATOM 4730 CB GLN D 37 0.134 33.810 44.893 1.00 16.53 C ANISOU 4730 CB GLN D 37 2439 2162 1679 -753 415 -360 C ATOM 4731 CG GLN D 37 1.246 34.853 44.649 1.00 21.02 C ANISOU 4731 CG GLN D 37 3029 2693 2264 -839 360 -342 C ATOM 4732 CD GLN D 37 0.918 35.774 43.508 1.00 29.02 C ANISOU 4732 CD GLN D 37 4033 3655 3339 -793 412 -320 C ATOM 4733 OE1 GLN D 37 -0.196 36.271 43.406 1.00 22.45 O ANISOU 4733 OE1 GLN D 37 3252 2761 2517 -712 484 -347 O ATOM 4734 NE2 GLN D 37 1.903 36.083 42.669 1.00 21.69 N ANISOU 4734 NE2 GLN D 37 3044 2747 2450 -845 377 -266 N ATOM 4735 N ASP D 38 1.956 33.422 47.803 1.00 22.82 N ANISOU 4735 N ASP D 38 3421 2974 2275 -977 220 -391 N ATOM 4736 CA ASP D 38 2.263 33.931 49.152 1.00 25.26 C ANISOU 4736 CA ASP D 38 3887 3243 2469 -1077 170 -441 C ATOM 4737 C ASP D 38 3.490 34.844 49.110 1.00 31.48 C ANISOU 4737 C ASP D 38 4669 4019 3273 -1191 67 -442 C ATOM 4738 O ASP D 38 4.408 34.594 48.328 1.00 29.29 O ANISOU 4738 O ASP D 38 4242 3809 3079 -1202 1 -383 O ATOM 4739 CB ASP D 38 2.503 32.749 50.114 1.00 26.49 C ANISOU 4739 CB ASP D 38 4073 3459 2531 -1091 97 -412 C ATOM 4740 CG ASP D 38 1.398 31.704 50.108 1.00 32.52 C ANISOU 4740 CG ASP D 38 4830 4236 3289 -1001 196 -399 C ATOM 4741 OD1 ASP D 38 0.377 31.912 50.814 1.00 31.08 O ANISOU 4741 OD1 ASP D 38 4771 4007 3032 -998 302 -456 O ATOM 4742 OD2 ASP D 38 1.556 30.664 49.398 1.00 31.32 O ANISOU 4742 OD2 ASP D 38 4552 4140 3209 -940 176 -338 O ATOM 4743 N LEU D 39 3.536 35.861 49.991 1.00 33.97 N ANISOU 4743 N LEU D 39 5149 4253 3506 -1286 57 -516 N ATOM 4744 CA LEU D 39 4.635 36.856 50.069 1.00 36.00 C ANISOU 4744 CA LEU D 39 5427 4480 3771 -1428 -38 -535 C ATOM 4745 C LEU D 39 6.032 36.176 50.134 1.00 38.27 C ANISOU 4745 C LEU D 39 5569 4894 4077 -1500 -206 -471 C ATOM 4746 O LEU D 39 6.254 35.299 50.965 1.00 38.36 O ANISOU 4746 O LEU D 39 5595 4975 4007 -1499 -295 -453 O ATOM 4747 CB LEU D 39 4.398 37.763 51.298 1.00 38.69 C ANISOU 4747 CB LEU D 39 6000 4719 3982 -1522 -34 -640 C ATOM 4748 CG LEU D 39 5.400 38.890 51.577 1.00 47.31 C ANISOU 4748 CG LEU D 39 7160 5754 5061 -1696 -129 -686 C ATOM 4749 CD1 LEU D 39 5.032 40.164 50.837 1.00 48.80 C ANISOU 4749 CD1 LEU D 39 7412 5796 5334 -1696 -19 -720 C ATOM 4750 CD2 LEU D 39 5.466 39.188 53.061 1.00 53.17 C ANISOU 4750 CD2 LEU D 39 8111 6460 5629 -1804 -193 -779 C ATOM 4751 N GLY D 40 6.908 36.527 49.192 1.00 35.06 N ANISOU 4751 N GLY D 40 5016 4519 3784 -1546 -238 -429 N ATOM 4752 CA GLY D 40 8.275 36.008 49.101 1.00 34.88 C ANISOU 4752 CA GLY D 40 4816 4623 3813 -1607 -381 -372 C ATOM 4753 C GLY D 40 8.463 34.626 48.492 1.00 37.04 C ANISOU 4753 C GLY D 40 4909 5009 4155 -1477 -390 -290 C ATOM 4754 O GLY D 40 9.603 34.184 48.313 1.00 35.59 O ANISOU 4754 O GLY D 40 4555 4932 4036 -1503 -495 -242 O ATOM 4755 N LEU D 41 7.360 33.921 48.165 1.00 32.45 N ANISOU 4755 N LEU D 41 4356 4405 3567 -1337 -281 -280 N ATOM 4756 CA LEU D 41 7.444 32.570 47.607 1.00 31.89 C ANISOU 4756 CA LEU D 41 4145 4418 3555 -1215 -280 -215 C ATOM 4757 C LEU D 41 6.903 32.498 46.179 1.00 34.74 C ANISOU 4757 C LEU D 41 4421 4770 4008 -1122 -148 -197 C ATOM 4758 O LEU D 41 7.070 31.474 45.513 1.00 36.17 O ANISOU 4758 O LEU D 41 4480 5015 4248 -1031 -137 -154 O ATOM 4759 CB LEU D 41 6.664 31.563 48.487 1.00 31.71 C ANISOU 4759 CB LEU D 41 4229 4383 3437 -1144 -281 -214 C ATOM 4760 CG LEU D 41 7.150 31.386 49.944 1.00 38.01 C ANISOU 4760 CG LEU D 41 5131 5198 4112 -1217 -422 -216 C ATOM 4761 CD1 LEU D 41 6.104 30.685 50.780 1.00 37.25 C ANISOU 4761 CD1 LEU D 41 5193 5060 3900 -1167 -370 -223 C ATOM 4762 CD2 LEU D 41 8.480 30.626 50.013 1.00 40.90 C ANISOU 4762 CD2 LEU D 41 5342 5671 4527 -1210 -585 -146 C ATOM 4763 N GLY D 42 6.209 33.544 45.748 1.00 26.97 N ANISOU 4763 N GLY D 42 3518 3703 3027 -1138 -51 -231 N ATOM 4764 CA GLY D 42 5.612 33.570 44.423 1.00 25.21 C ANISOU 4764 CA GLY D 42 3239 3471 2870 -1052 59 -211 C ATOM 4765 C GLY D 42 4.517 32.533 44.287 1.00 24.89 C ANISOU 4765 C GLY D 42 3203 3440 2815 -928 119 -213 C ATOM 4766 O GLY D 42 3.942 32.100 45.288 1.00 24.24 O ANISOU 4766 O GLY D 42 3211 3336 2664 -918 112 -240 O ATOM 4767 N LEU D 43 4.269 32.097 43.050 1.00 21.01 N ANISOU 4767 N LEU D 43 2618 2984 2381 -848 179 -185 N ATOM 4768 CA LEU D 43 3.278 31.079 42.710 1.00 18.37 C ANISOU 4768 CA LEU D 43 2267 2664 2047 -745 232 -191 C ATOM 4769 C LEU D 43 3.858 29.682 42.938 1.00 21.47 C ANISOU 4769 C LEU D 43 2590 3117 2450 -713 177 -166 C ATOM 4770 O LEU D 43 4.947 29.362 42.432 1.00 22.24 O ANISOU 4770 O LEU D 43 2576 3274 2599 -711 138 -133 O ATOM 4771 CB LEU D 43 2.882 31.232 41.221 1.00 17.48 C ANISOU 4771 CB LEU D 43 2092 2568 1980 -684 301 -175 C ATOM 4772 CG LEU D 43 2.025 32.452 40.840 1.00 21.25 C ANISOU 4772 CG LEU D 43 2645 2977 2453 -673 359 -188 C ATOM 4773 CD1 LEU D 43 1.994 32.630 39.318 1.00 19.71 C ANISOU 4773 CD1 LEU D 43 2390 2812 2287 -629 397 -150 C ATOM 4774 CD2 LEU D 43 0.607 32.318 41.396 1.00 20.89 C ANISOU 4774 CD2 LEU D 43 2664 2891 2383 -616 405 -234 C ATOM 4775 N ARG D 44 3.139 28.855 43.683 1.00 16.55 N ANISOU 4775 N ARG D 44 2032 2474 1784 -683 183 -179 N ATOM 4776 CA ARG D 44 3.540 27.470 43.938 1.00 16.40 C ANISOU 4776 CA ARG D 44 1978 2482 1773 -640 136 -149 C ATOM 4777 C ARG D 44 2.411 26.564 43.489 1.00 18.18 C ANISOU 4777 C ARG D 44 2213 2687 2006 -577 214 -168 C ATOM 4778 O ARG D 44 1.265 26.746 43.911 1.00 15.60 O ANISOU 4778 O ARG D 44 1965 2323 1639 -589 275 -201 O ATOM 4779 CB ARG D 44 3.904 27.227 45.421 1.00 16.46 C ANISOU 4779 CB ARG D 44 2078 2473 1703 -688 48 -133 C ATOM 4780 CG ARG D 44 5.257 27.810 45.840 1.00 20.70 C ANISOU 4780 CG ARG D 44 2571 3050 2242 -752 -68 -109 C ATOM 4781 CD ARG D 44 5.510 27.529 47.324 1.00 27.46 C ANISOU 4781 CD ARG D 44 3538 3895 2998 -797 -171 -92 C ATOM 4782 NE ARG D 44 4.487 28.169 48.161 1.00 25.50 N ANISOU 4782 NE ARG D 44 3460 3585 2645 -853 -110 -143 N ATOM 4783 CZ ARG D 44 4.226 27.861 49.429 1.00 36.13 C ANISOU 4783 CZ ARG D 44 4953 4905 3871 -888 -145 -141 C ATOM 4784 NH1 ARG D 44 4.939 26.932 50.055 1.00 26.16 N ANISOU 4784 NH1 ARG D 44 3697 3669 2572 -873 -264 -77 N ATOM 4785 NH2 ARG D 44 3.270 28.502 50.089 1.00 22.63 N ANISOU 4785 NH2 ARG D 44 3388 3141 2071 -934 -60 -200 N ATOM 4786 N LEU D 45 2.731 25.598 42.623 1.00 14.12 N ANISOU 4786 N LEU D 45 1617 2201 1549 -514 219 -154 N ATOM 4787 CA LEU D 45 1.743 24.688 42.081 1.00 13.19 C ANISOU 4787 CA LEU D 45 1504 2065 1443 -470 284 -180 C ATOM 4788 C LEU D 45 1.236 23.733 43.162 1.00 15.33 C ANISOU 4788 C LEU D 45 1871 2282 1672 -482 280 -172 C ATOM 4789 O LEU D 45 2.028 23.108 43.872 1.00 15.00 O ANISOU 4789 O LEU D 45 1857 2225 1618 -474 209 -127 O ATOM 4790 CB LEU D 45 2.334 23.900 40.878 1.00 12.52 C ANISOU 4790 CB LEU D 45 1326 2013 1420 -404 291 -179 C ATOM 4791 CG LEU D 45 1.387 22.987 40.144 1.00 14.77 C ANISOU 4791 CG LEU D 45 1616 2279 1716 -371 350 -219 C ATOM 4792 CD1 LEU D 45 0.329 23.809 39.342 1.00 14.47 C ANISOU 4792 CD1 LEU D 45 1563 2268 1666 -384 403 -257 C ATOM 4793 CD2 LEU D 45 2.161 22.012 39.221 1.00 13.32 C ANISOU 4793 CD2 LEU D 45 1372 2107 1581 -302 354 -225 C ATOM 4794 N ILE D 46 -0.088 23.603 43.250 1.00 10.96 N ANISOU 4794 N ILE D 46 1361 1703 1100 -502 356 -209 N ATOM 4795 CA ILE D 46 -0.721 22.687 44.215 1.00 12.23 C ANISOU 4795 CA ILE D 46 1621 1810 1217 -533 382 -200 C ATOM 4796 C ILE D 46 -0.974 21.326 43.559 1.00 17.05 C ANISOU 4796 C ILE D 46 2213 2391 1876 -502 404 -206 C ATOM 4797 O ILE D 46 -0.521 20.283 44.044 1.00 16.92 O ANISOU 4797 O ILE D 46 2258 2320 1853 -489 369 -164 O ATOM 4798 CB ILE D 46 -2.043 23.302 44.751 1.00 14.67 C ANISOU 4798 CB ILE D 46 1975 2112 1485 -583 471 -244 C ATOM 4799 CG1 ILE D 46 -1.745 24.659 45.460 1.00 16.06 C ANISOU 4799 CG1 ILE D 46 2199 2295 1608 -612 453 -250 C ATOM 4800 CG2 ILE D 46 -2.698 22.307 45.709 1.00 13.29 C ANISOU 4800 CG2 ILE D 46 1902 1885 1262 -632 519 -232 C ATOM 4801 CD1 ILE D 46 -3.017 25.546 45.682 1.00 18.01 C ANISOU 4801 CD1 ILE D 46 2463 2539 1842 -627 556 -308 C ATOM 4802 N HIS D 47 -1.737 21.361 42.463 1.00 15.04 N ANISOU 4802 N HIS D 47 1884 2164 1665 -492 457 -259 N ATOM 4803 CA HIS D 47 -2.116 20.214 41.642 1.00 14.25 C ANISOU 4803 CA HIS D 47 1766 2040 1609 -479 483 -290 C ATOM 4804 C HIS D 47 -2.253 20.684 40.215 1.00 17.52 C ANISOU 4804 C HIS D 47 2081 2520 2056 -444 490 -335 C ATOM 4805 O HIS D 47 -2.507 21.869 39.983 1.00 15.30 O ANISOU 4805 O HIS D 47 1757 2292 1765 -443 495 -341 O ATOM 4806 CB HIS D 47 -3.460 19.624 42.115 1.00 14.67 C ANISOU 4806 CB HIS D 47 1866 2056 1653 -552 554 -319 C ATOM 4807 CG HIS D 47 -3.378 18.775 43.352 1.00 18.77 C ANISOU 4807 CG HIS D 47 2511 2491 2131 -593 561 -270 C ATOM 4808 ND1 HIS D 47 -3.959 19.185 44.556 1.00 21.91 N ANISOU 4808 ND1 HIS D 47 2982 2881 2463 -658 607 -254 N ATOM 4809 CD2 HIS D 47 -2.818 17.561 43.531 1.00 20.19 C ANISOU 4809 CD2 HIS D 47 2767 2585 2320 -574 532 -231 C ATOM 4810 CE1 HIS D 47 -3.702 18.217 45.430 1.00 21.12 C ANISOU 4810 CE1 HIS D 47 3007 2697 2321 -684 598 -197 C ATOM 4811 NE2 HIS D 47 -3.056 17.202 44.852 1.00 22.11 N ANISOU 4811 NE2 HIS D 47 3139 2767 2496 -633 551 -179 N ATOM 4812 N TYR D 48 -2.199 19.753 39.270 1.00 14.72 N ANISOU 4812 N TYR D 48 1709 2155 1731 -419 496 -368 N ATOM 4813 CA TYR D 48 -2.338 20.052 37.853 1.00 14.01 C ANISOU 4813 CA TYR D 48 1547 2129 1648 -391 500 -413 C ATOM 4814 C TYR D 48 -3.097 18.919 37.184 1.00 17.36 C ANISOU 4814 C TYR D 48 1985 2526 2087 -417 523 -479 C ATOM 4815 O TYR D 48 -3.238 17.843 37.768 1.00 16.99 O ANISOU 4815 O TYR D 48 2006 2393 2056 -447 538 -481 O ATOM 4816 CB TYR D 48 -0.959 20.278 37.187 1.00 13.32 C ANISOU 4816 CB TYR D 48 1420 2072 1567 -323 478 -390 C ATOM 4817 CG TYR D 48 -0.102 19.038 36.996 1.00 15.22 C ANISOU 4817 CG TYR D 48 1684 2260 1841 -270 478 -396 C ATOM 4818 CD1 TYR D 48 0.006 18.425 35.746 1.00 17.90 C ANISOU 4818 CD1 TYR D 48 2010 2609 2183 -234 508 -456 C ATOM 4819 CD2 TYR D 48 0.624 18.493 38.057 1.00 15.18 C ANISOU 4819 CD2 TYR D 48 1719 2190 1858 -247 446 -344 C ATOM 4820 CE1 TYR D 48 0.839 17.314 35.550 1.00 19.19 C ANISOU 4820 CE1 TYR D 48 2197 2711 2385 -167 520 -470 C ATOM 4821 CE2 TYR D 48 1.396 17.334 37.890 1.00 16.96 C ANISOU 4821 CE2 TYR D 48 1964 2352 2126 -175 443 -345 C ATOM 4822 CZ TYR D 48 1.515 16.759 36.629 1.00 20.39 C ANISOU 4822 CZ TYR D 48 2381 2789 2577 -130 488 -413 C ATOM 4823 OH TYR D 48 2.311 15.657 36.434 1.00 19.22 O ANISOU 4823 OH TYR D 48 2255 2570 2479 -42 498 -423 O ATOM 4824 N SER D 49 -3.548 19.157 35.953 1.00 13.98 N ANISOU 4824 N SER D 49 1505 2163 1645 -411 519 -529 N ATOM 4825 CA SER D 49 -4.243 18.154 35.136 1.00 14.97 C ANISOU 4825 CA SER D 49 1641 2274 1771 -447 526 -607 C ATOM 4826 C SER D 49 -3.900 18.390 33.695 1.00 19.01 C ANISOU 4826 C SER D 49 2125 2855 2242 -402 510 -644 C ATOM 4827 O SER D 49 -4.164 19.479 33.180 1.00 18.21 O ANISOU 4827 O SER D 49 1972 2840 2108 -387 488 -627 O ATOM 4828 CB SER D 49 -5.755 18.236 35.365 1.00 16.56 C ANISOU 4828 CB SER D 49 1802 2504 1985 -529 531 -642 C ATOM 4829 OG SER D 49 -6.442 17.359 34.491 1.00 17.41 O ANISOU 4829 OG SER D 49 1908 2613 2093 -581 521 -725 O ATOM 4830 N ASN D 50 -3.316 17.390 33.022 1.00 15.58 N ANISOU 4830 N ASN D 50 1740 2378 1803 -376 527 -693 N ATOM 4831 CA ASN D 50 -2.906 17.584 31.626 1.00 15.00 C ANISOU 4831 CA ASN D 50 1658 2373 1669 -334 530 -732 C ATOM 4832 C ASN D 50 -4.010 17.322 30.628 1.00 18.40 C ANISOU 4832 C ASN D 50 2092 2851 2047 -392 497 -815 C ATOM 4833 O ASN D 50 -3.827 17.617 29.455 1.00 17.64 O ANISOU 4833 O ASN D 50 2001 2826 1874 -367 490 -843 O ATOM 4834 CB ASN D 50 -1.685 16.710 31.286 1.00 15.65 C ANISOU 4834 CB ASN D 50 1787 2395 1764 -264 578 -757 C ATOM 4835 CG ASN D 50 -0.413 17.285 31.871 1.00 28.95 C ANISOU 4835 CG ASN D 50 3426 4088 3485 -194 593 -672 C ATOM 4836 OD1 ASN D 50 -0.398 18.348 32.503 1.00 24.13 O ANISOU 4836 OD1 ASN D 50 2768 3520 2879 -208 567 -599 O ATOM 4837 ND2 ASN D 50 0.692 16.630 31.643 1.00 22.98 N ANISOU 4837 ND2 ASN D 50 2678 3295 2758 -117 635 -685 N ATOM 4838 N THR D 51 -5.156 16.761 31.078 1.00 15.47 N ANISOU 4838 N THR D 51 1719 2448 1712 -478 477 -856 N ATOM 4839 CA THR D 51 -6.293 16.431 30.209 1.00 15.55 C ANISOU 4839 CA THR D 51 1714 2510 1685 -553 429 -943 C ATOM 4840 C THR D 51 -7.414 15.896 31.074 1.00 19.20 C ANISOU 4840 C THR D 51 2149 2930 2218 -658 428 -964 C ATOM 4841 O THR D 51 -7.164 15.454 32.203 1.00 18.58 O ANISOU 4841 O THR D 51 2110 2751 2198 -671 479 -925 O ATOM 4842 CB THR D 51 -5.844 15.412 29.071 1.00 21.37 C ANISOU 4842 CB THR D 51 2546 3212 2363 -551 441 -1042 C ATOM 4843 OG1 THR D 51 -6.818 15.376 28.046 1.00 24.67 O ANISOU 4843 OG1 THR D 51 2947 3715 2713 -618 371 -1121 O ATOM 4844 CG2 THR D 51 -5.601 13.981 29.575 1.00 18.13 C ANISOU 4844 CG2 THR D 51 2232 2644 2013 -583 493 -1093 C ATOM 4845 N ALA D 52 -8.648 15.889 30.551 1.00 19.43 N ANISOU 4845 N ALA D 52 2108 3035 2238 -738 370 -1025 N ATOM 4846 CA ALA D 52 -9.790 15.332 31.301 1.00 19.80 C ANISOU 4846 CA ALA D 52 2109 3055 2360 -859 382 -1056 C ATOM 4847 C ALA D 52 -9.488 13.880 31.687 1.00 23.95 C ANISOU 4847 C ALA D 52 2760 3421 2919 -928 440 -1101 C ATOM 4848 O ALA D 52 -8.877 13.147 30.904 1.00 22.39 O ANISOU 4848 O ALA D 52 2662 3165 2680 -911 439 -1162 O ATOM 4849 CB ALA D 52 -11.061 15.388 30.449 1.00 21.45 C ANISOU 4849 CB ALA D 52 2214 3381 2557 -938 296 -1132 C ATOM 4850 N GLY D 53 -9.828 13.512 32.912 1.00 21.02 N ANISOU 4850 N GLY D 53 2400 2971 2615 -994 500 -1063 N ATOM 4851 CA GLY D 53 -9.659 12.139 33.389 1.00 22.23 C ANISOU 4851 CA GLY D 53 2688 2955 2805 -1068 556 -1089 C ATOM 4852 C GLY D 53 -8.368 11.832 34.121 1.00 23.75 C ANISOU 4852 C GLY D 53 3003 3018 3002 -967 603 -1009 C ATOM 4853 O GLY D 53 -8.141 10.680 34.487 1.00 23.40 O ANISOU 4853 O GLY D 53 3088 2816 2988 -1005 642 -1019 O ATOM 4854 N THR D 54 -7.493 12.824 34.320 1.00 18.17 N ANISOU 4854 N THR D 54 2260 2372 2270 -839 592 -930 N ATOM 4855 CA THR D 54 -6.233 12.566 35.020 1.00 17.21 C ANISOU 4855 CA THR D 54 2230 2148 2159 -740 617 -853 C ATOM 4856 C THR D 54 -5.815 13.796 35.780 1.00 20.27 C ANISOU 4856 C THR D 54 2553 2614 2534 -674 607 -755 C ATOM 4857 O THR D 54 -6.184 14.902 35.394 1.00 20.29 O ANISOU 4857 O THR D 54 2453 2745 2513 -663 582 -756 O ATOM 4858 CB THR D 54 -5.095 12.088 34.034 1.00 25.43 C ANISOU 4858 CB THR D 54 3329 3150 3185 -632 612 -894 C ATOM 4859 OG1 THR D 54 -4.019 11.543 34.819 1.00 22.68 O ANISOU 4859 OG1 THR D 54 3065 2680 2872 -545 632 -824 O ATOM 4860 CG2 THR D 54 -4.529 13.233 33.128 1.00 18.81 C ANISOU 4860 CG2 THR D 54 2395 2457 2292 -541 584 -890 C ATOM 4861 N THR D 55 -5.047 13.616 36.870 1.00 14.98 N ANISOU 4861 N THR D 55 1954 1862 1875 -631 619 -671 N ATOM 4862 CA THR D 55 -4.508 14.747 37.631 1.00 14.32 C ANISOU 4862 CA THR D 55 1828 1842 1771 -576 601 -586 C ATOM 4863 C THR D 55 -3.173 14.315 38.225 1.00 18.85 C ANISOU 4863 C THR D 55 2475 2333 2355 -485 579 -515 C ATOM 4864 O THR D 55 -2.914 13.108 38.345 1.00 20.51 O ANISOU 4864 O THR D 55 2784 2417 2593 -475 590 -517 O ATOM 4865 CB THR D 55 -5.444 15.273 38.785 1.00 23.91 C ANISOU 4865 CB THR D 55 3035 3078 2973 -661 633 -549 C ATOM 4866 OG1 THR D 55 -5.315 14.400 39.895 1.00 21.14 O ANISOU 4866 OG1 THR D 55 2807 2605 2620 -698 659 -496 O ATOM 4867 CG2 THR D 55 -6.941 15.452 38.397 1.00 21.22 C ANISOU 4867 CG2 THR D 55 2608 2806 2648 -759 663 -619 C ATOM 4868 N GLY D 56 -2.358 15.291 38.596 1.00 14.89 N ANISOU 4868 N GLY D 56 1924 1897 1837 -422 544 -454 N ATOM 4869 CA GLY D 56 -1.062 15.053 39.213 1.00 15.52 C ANISOU 4869 CA GLY D 56 2038 1929 1930 -335 502 -380 C ATOM 4870 C GLY D 56 -0.800 16.052 40.319 1.00 20.50 C ANISOU 4870 C GLY D 56 2659 2608 2522 -349 464 -306 C ATOM 4871 O GLY D 56 -1.422 17.114 40.367 1.00 18.50 O ANISOU 4871 O GLY D 56 2357 2434 2238 -400 479 -320 O ATOM 4872 N LYS D 57 0.170 15.750 41.182 1.00 17.92 N ANISOU 4872 N LYS D 57 2380 2234 2195 -296 407 -230 N ATOM 4873 CA LYS D 57 0.520 16.634 42.286 1.00 17.35 C ANISOU 4873 CA LYS D 57 2318 2204 2072 -317 355 -164 C ATOM 4874 C LYS D 57 1.493 17.714 41.868 1.00 19.21 C ANISOU 4874 C LYS D 57 2434 2543 2323 -271 310 -158 C ATOM 4875 O LYS D 57 2.420 17.476 41.095 1.00 19.94 O ANISOU 4875 O LYS D 57 2448 2656 2471 -188 294 -164 O ATOM 4876 CB LYS D 57 1.156 15.816 43.432 1.00 20.18 C ANISOU 4876 CB LYS D 57 2786 2471 2409 -285 290 -76 C ATOM 4877 CG LYS D 57 0.157 14.898 44.144 1.00 28.60 C ANISOU 4877 CG LYS D 57 4004 3426 3436 -362 342 -60 C ATOM 4878 CD LYS D 57 0.881 14.000 45.117 1.00 35.48 C ANISOU 4878 CD LYS D 57 5000 4194 4286 -310 268 40 C ATOM 4879 CE LYS D 57 -0.091 13.207 45.967 1.00 42.57 C ANISOU 4879 CE LYS D 57 6071 4978 5124 -407 329 74 C ATOM 4880 NZ LYS D 57 0.627 12.474 47.045 1.00 48.75 N ANISOU 4880 NZ LYS D 57 7000 5663 5859 -357 241 193 N ATOM 4881 N GLY D 58 1.342 18.871 42.467 1.00 16.85 N ANISOU 4881 N GLY D 58 2129 2299 1973 -327 294 -144 N ATOM 4882 CA GLY D 58 2.301 19.959 42.279 1.00 16.40 C ANISOU 4882 CA GLY D 58 1979 2326 1926 -311 245 -129 C ATOM 4883 C GLY D 58 3.379 19.911 43.336 1.00 21.40 C ANISOU 4883 C GLY D 58 2632 2957 2544 -294 140 -58 C ATOM 4884 O GLY D 58 3.716 18.845 43.857 1.00 21.53 O ANISOU 4884 O GLY D 58 2705 2908 2565 -246 96 -13 O ATOM 4885 N GLU D 59 3.903 21.080 43.686 1.00 18.23 N ANISOU 4885 N GLU D 59 2191 2619 2119 -337 92 -47 N ATOM 4886 CA GLU D 59 4.936 21.263 44.697 1.00 18.37 C ANISOU 4886 CA GLU D 59 2213 2657 2111 -343 -29 12 C ATOM 4887 C GLU D 59 4.354 21.207 46.120 1.00 22.74 C ANISOU 4887 C GLU D 59 2933 3158 2551 -408 -60 40 C ATOM 4888 O GLU D 59 5.032 20.730 47.021 1.00 23.03 O ANISOU 4888 O GLU D 59 3017 3181 2550 -389 -168 104 O ATOM 4889 CB GLU D 59 5.555 22.662 44.467 1.00 19.48 C ANISOU 4889 CB GLU D 59 2262 2879 2262 -399 -55 -4 C ATOM 4890 CG GLU D 59 6.852 22.939 45.194 1.00 36.61 C ANISOU 4890 CG GLU D 59 4376 5100 4433 -413 -192 45 C ATOM 4891 CD GLU D 59 7.340 24.376 45.079 1.00 52.59 C ANISOU 4891 CD GLU D 59 6336 7186 6460 -504 -211 23 C ATOM 4892 OE1 GLU D 59 7.015 25.052 44.073 1.00 41.40 O ANISOU 4892 OE1 GLU D 59 4871 5782 5077 -521 -114 -17 O ATOM 4893 OE2 GLU D 59 8.045 24.830 46.009 1.00 48.14 O ANISOU 4893 OE2 GLU D 59 5782 6653 5858 -565 -329 46 O ATOM 4894 N VAL D 60 3.131 21.751 46.339 1.00 19.13 N ANISOU 4894 N VAL D 60 2558 2679 2032 -481 33 -7 N ATOM 4895 CA VAL D 60 2.550 21.828 47.700 1.00 20.65 C ANISOU 4895 CA VAL D 60 2913 2831 2101 -552 32 8 C ATOM 4896 C VAL D 60 1.133 21.161 47.699 1.00 21.86 C ANISOU 4896 C VAL D 60 3145 2924 2236 -576 162 -19 C ATOM 4897 O VAL D 60 0.127 21.818 47.974 1.00 20.00 O ANISOU 4897 O VAL D 60 2953 2690 1955 -636 254 -68 O ATOM 4898 CB VAL D 60 2.554 23.308 48.232 1.00 24.02 C ANISOU 4898 CB VAL D 60 3370 3296 2461 -631 22 -30 C ATOM 4899 CG1 VAL D 60 3.980 23.776 48.527 1.00 25.19 C ANISOU 4899 CG1 VAL D 60 3463 3497 2610 -640 -126 6 C ATOM 4900 CG2 VAL D 60 1.875 24.275 47.254 1.00 21.88 C ANISOU 4900 CG2 VAL D 60 3021 3045 2248 -638 124 -100 C ATOM 4901 N PRO D 61 1.024 19.849 47.391 1.00 20.68 N ANISOU 4901 N PRO D 61 3010 2716 2131 -532 177 8 N ATOM 4902 CA PRO D 61 -0.324 19.238 47.296 1.00 19.11 C ANISOU 4902 CA PRO D 61 2866 2466 1930 -578 301 -26 C ATOM 4903 C PRO D 61 -1.022 18.895 48.618 1.00 23.71 C ANISOU 4903 C PRO D 61 3618 2992 2397 -659 349 8 C ATOM 4904 O PRO D 61 -2.241 18.720 48.588 1.00 23.78 O ANISOU 4904 O PRO D 61 3646 2985 2406 -721 473 -35 O ATOM 4905 CB PRO D 61 -0.052 17.938 46.536 1.00 20.02 C ANISOU 4905 CB PRO D 61 2958 2520 2130 -512 292 -10 C ATOM 4906 CG PRO D 61 1.327 17.548 46.950 1.00 25.40 C ANISOU 4906 CG PRO D 61 3654 3186 2812 -434 161 69 C ATOM 4907 CD PRO D 61 2.075 18.867 47.032 1.00 22.03 C ANISOU 4907 CD PRO D 61 3140 2861 2370 -437 91 62 C ATOM 4908 N ASP D 62 -0.275 18.710 49.747 1.00 21.94 N ANISOU 4908 N ASP D 62 3519 2743 2076 -663 252 87 N ATOM 4909 CA ASP D 62 -0.859 18.259 51.021 1.00 23.24 C ANISOU 4909 CA ASP D 62 3876 2849 2107 -742 298 133 C ATOM 4910 C ASP D 62 -1.943 19.208 51.552 1.00 26.02 C ANISOU 4910 C ASP D 62 4268 3240 2380 -836 428 63 C ATOM 4911 O ASP D 62 -1.748 20.427 51.597 1.00 23.37 O ANISOU 4911 O ASP D 62 3887 2969 2025 -839 409 14 O ATOM 4912 CB ASP D 62 0.219 18.030 52.105 1.00 27.00 C ANISOU 4912 CB ASP D 62 4480 3307 2473 -722 144 234 C ATOM 4913 CG ASP D 62 1.286 16.998 51.724 1.00 43.50 C ANISOU 4913 CG ASP D 62 6536 5348 4645 -608 16 314 C ATOM 4914 OD1 ASP D 62 0.995 16.113 50.873 1.00 44.51 O ANISOU 4914 OD1 ASP D 62 6619 5413 4882 -565 76 303 O ATOM 4915 OD2 ASP D 62 2.418 17.088 52.258 1.00 50.06 O ANISOU 4915 OD2 ASP D 62 7379 6206 5436 -558 -147 381 O ATOM 4916 N GLY D 63 -3.080 18.611 51.919 1.00 24.47 N ANISOU 4916 N GLY D 63 4152 2996 2149 -911 567 58 N ATOM 4917 CA GLY D 63 -4.259 19.308 52.431 1.00 24.62 C ANISOU 4917 CA GLY D 63 4199 3049 2108 -994 724 -11 C ATOM 4918 C GLY D 63 -5.219 19.718 51.326 1.00 26.48 C ANISOU 4918 C GLY D 63 4247 3334 2480 -983 829 -107 C ATOM 4919 O GLY D 63 -6.255 20.339 51.594 1.00 23.89 O ANISOU 4919 O GLY D 63 3899 3042 2137 -1030 964 -174 O ATOM 4920 N TYR D 64 -4.858 19.402 50.064 1.00 20.85 N ANISOU 4920 N TYR D 64 3395 2627 1899 -914 763 -117 N ATOM 4921 CA TYR D 64 -5.680 19.725 48.895 1.00 20.04 C ANISOU 4921 CA TYR D 64 3118 2577 1918 -897 828 -199 C ATOM 4922 C TYR D 64 -5.960 18.502 48.032 1.00 22.78 C ANISOU 4922 C TYR D 64 3416 2883 2357 -903 836 -200 C ATOM 4923 O TYR D 64 -5.142 17.593 47.966 1.00 21.18 O ANISOU 4923 O TYR D 64 3277 2611 2158 -872 757 -141 O ATOM 4924 CB TYR D 64 -4.976 20.766 47.986 1.00 19.09 C ANISOU 4924 CB TYR D 64 2876 2519 1858 -809 740 -228 C ATOM 4925 CG TYR D 64 -4.524 22.046 48.666 1.00 19.99 C ANISOU 4925 CG TYR D 64 3037 2660 1898 -803 711 -235 C ATOM 4926 CD1 TYR D 64 -5.378 23.140 48.773 1.00 21.45 C ANISOU 4926 CD1 TYR D 64 3189 2880 2082 -811 804 -304 C ATOM 4927 CD2 TYR D 64 -3.215 22.189 49.131 1.00 19.72 C ANISOU 4927 CD2 TYR D 64 3069 2617 1807 -785 583 -180 C ATOM 4928 CE1 TYR D 64 -4.966 24.321 49.392 1.00 21.71 C ANISOU 4928 CE1 TYR D 64 3286 2917 2046 -811 783 -322 C ATOM 4929 CE2 TYR D 64 -2.774 23.389 49.702 1.00 20.48 C ANISOU 4929 CE2 TYR D 64 3210 2734 1837 -798 546 -199 C ATOM 4930 CZ TYR D 64 -3.655 24.446 49.832 1.00 24.63 C ANISOU 4930 CZ TYR D 64 3732 3275 2353 -814 651 -272 C ATOM 4931 OH TYR D 64 -3.232 25.614 50.398 1.00 21.23 O ANISOU 4931 OH TYR D 64 3367 2843 1855 -833 621 -300 O ATOM 4932 N SER D 65 -7.062 18.529 47.292 1.00 20.36 N ANISOU 4932 N SER D 65 2987 2619 2131 -933 919 -272 N ATOM 4933 CA SER D 65 -7.351 17.503 46.287 1.00 20.89 C ANISOU 4933 CA SER D 65 2992 2656 2287 -947 915 -297 C ATOM 4934 C SER D 65 -8.064 18.151 45.120 1.00 22.35 C ANISOU 4934 C SER D 65 2995 2937 2559 -921 926 -380 C ATOM 4935 O SER D 65 -8.686 19.197 45.279 1.00 20.15 O ANISOU 4935 O SER D 65 2644 2732 2280 -914 975 -416 O ATOM 4936 CB SER D 65 -8.184 16.348 46.857 1.00 24.64 C ANISOU 4936 CB SER D 65 3554 3055 2751 -1068 1014 -284 C ATOM 4937 OG SER D 65 -9.495 16.798 47.140 1.00 28.99 O ANISOU 4937 OG SER D 65 4028 3674 3315 -1149 1142 -341 O ATOM 4938 N VAL D 66 -7.990 17.512 43.951 1.00 18.62 N ANISOU 4938 N VAL D 66 2460 2460 2155 -903 878 -412 N ATOM 4939 CA VAL D 66 -8.649 17.968 42.735 1.00 17.47 C ANISOU 4939 CA VAL D 66 2156 2406 2078 -882 866 -485 C ATOM 4940 C VAL D 66 -9.325 16.813 42.053 1.00 22.81 C ANISOU 4940 C VAL D 66 2804 3054 2808 -961 882 -536 C ATOM 4941 O VAL D 66 -8.981 15.659 42.301 1.00 20.49 O ANISOU 4941 O VAL D 66 2626 2652 2508 -1004 887 -512 O ATOM 4942 CB VAL D 66 -7.636 18.623 41.740 1.00 17.39 C ANISOU 4942 CB VAL D 66 2098 2436 2072 -767 766 -480 C ATOM 4943 CG1 VAL D 66 -7.179 20.001 42.217 1.00 15.81 C ANISOU 4943 CG1 VAL D 66 1894 2277 1834 -707 751 -449 C ATOM 4944 CG2 VAL D 66 -6.452 17.695 41.433 1.00 16.14 C ANISOU 4944 CG2 VAL D 66 2020 2201 1912 -726 706 -449 C ATOM 4945 N SER D 67 -10.205 17.138 41.109 1.00 21.25 N ANISOU 4945 N SER D 67 2459 2950 2664 -971 874 -607 N ATOM 4946 CA SER D 67 -10.789 16.162 40.202 1.00 21.46 C ANISOU 4946 CA SER D 67 2443 2970 2739 -1045 858 -674 C ATOM 4947 C SER D 67 -10.864 16.823 38.838 1.00 22.62 C ANISOU 4947 C SER D 67 2468 3224 2902 -971 772 -722 C ATOM 4948 O SER D 67 -10.931 18.061 38.730 1.00 21.24 O ANISOU 4948 O SER D 67 2213 3136 2722 -890 752 -707 O ATOM 4949 CB SER D 67 -12.149 15.647 40.687 1.00 25.77 C ANISOU 4949 CB SER D 67 2933 3527 3331 -1192 952 -713 C ATOM 4950 OG SER D 67 -13.148 16.647 40.611 1.00 33.33 O ANISOU 4950 OG SER D 67 3718 4618 4327 -1182 976 -748 O ATOM 4951 N ARG D 68 -10.821 16.012 37.807 1.00 19.83 N ANISOU 4951 N ARG D 68 2122 2855 2559 -998 721 -778 N ATOM 4952 CA ARG D 68 -10.935 16.503 36.437 1.00 21.09 C ANISOU 4952 CA ARG D 68 2187 3116 2709 -942 634 -826 C ATOM 4953 C ARG D 68 -11.754 15.516 35.627 1.00 27.29 C ANISOU 4953 C ARG D 68 2939 3910 3521 -1054 607 -920 C ATOM 4954 O ARG D 68 -11.210 14.805 34.776 1.00 26.80 O ANISOU 4954 O ARG D 68 2954 3801 3429 -1049 565 -964 O ATOM 4955 CB ARG D 68 -9.556 16.759 35.809 1.00 19.85 C ANISOU 4955 CB ARG D 68 2104 2939 2498 -824 584 -795 C ATOM 4956 CG ARG D 68 -9.663 17.416 34.416 1.00 22.45 C ANISOU 4956 CG ARG D 68 2355 3380 2793 -766 504 -829 C ATOM 4957 CD ARG D 68 -9.521 18.924 34.496 1.00 22.29 C ANISOU 4957 CD ARG D 68 2275 3437 2758 -670 486 -766 C ATOM 4958 NE ARG D 68 -9.696 19.527 33.170 1.00 21.66 N ANISOU 4958 NE ARG D 68 2138 3456 2634 -619 407 -785 N ATOM 4959 CZ ARG D 68 -8.732 19.663 32.267 1.00 22.42 C ANISOU 4959 CZ ARG D 68 2293 3560 2665 -557 377 -774 C ATOM 4960 NH1 ARG D 68 -8.978 20.261 31.113 1.00 16.60 N ANISOU 4960 NH1 ARG D 68 1520 2915 1872 -518 307 -781 N ATOM 4961 NH2 ARG D 68 -7.509 19.201 32.512 1.00 16.12 N ANISOU 4961 NH2 ARG D 68 1587 2681 1855 -532 419 -753 N ATOM 4962 N ALA D 69 -13.065 15.467 35.895 1.00 25.00 N ANISOU 4962 N ALA D 69 2529 3682 3289 -1159 635 -959 N ATOM 4963 CA ALA D 69 -13.971 14.585 35.153 1.00 26.79 C ANISOU 4963 CA ALA D 69 2698 3932 3549 -1292 598 -1057 C ATOM 4964 C ALA D 69 -14.152 15.088 33.718 1.00 31.52 C ANISOU 4964 C ALA D 69 3207 4657 4111 -1235 470 -1108 C ATOM 4965 O ALA D 69 -14.375 14.288 32.827 1.00 32.23 O ANISOU 4965 O ALA D 69 3317 4743 4184 -1314 410 -1193 O ATOM 4966 CB ALA D 69 -15.338 14.502 35.854 1.00 28.60 C ANISOU 4966 CB ALA D 69 2788 4218 3862 -1424 666 -1081 C ATOM 4967 N ASN D 70 -14.084 16.414 33.504 1.00 26.70 N ANISOU 4967 N ASN D 70 2512 4151 3480 -1102 426 -1057 N ATOM 4968 CA ASN D 70 -14.331 17.029 32.198 1.00 26.86 C ANISOU 4968 CA ASN D 70 2453 4299 3455 -1039 300 -1084 C ATOM 4969 C ASN D 70 -13.288 18.067 31.873 1.00 26.81 C ANISOU 4969 C ASN D 70 2510 4299 3376 -879 276 -1006 C ATOM 4970 O ASN D 70 -12.680 18.648 32.776 1.00 24.20 O ANISOU 4970 O ASN D 70 2223 3915 3057 -812 348 -931 O ATOM 4971 CB ASN D 70 -15.721 17.712 32.190 1.00 30.03 C ANISOU 4971 CB ASN D 70 2637 4844 3927 -1050 256 -1098 C ATOM 4972 CG ASN D 70 -16.829 16.869 32.760 1.00 59.36 C ANISOU 4972 CG ASN D 70 6250 8567 7738 -1217 309 -1162 C ATOM 4973 OD1 ASN D 70 -17.392 17.177 33.813 1.00 60.88 O ANISOU 4973 OD1 ASN D 70 6355 8769 8009 -1235 408 -1135 O ATOM 4974 ND2 ASN D 70 -17.101 15.744 32.124 1.00 51.32 N ANISOU 4974 ND2 ASN D 70 5258 7531 6712 -1356 262 -1252 N ATOM 4975 N THR D 71 -13.185 18.400 30.591 1.00 23.57 N ANISOU 4975 N THR D 71 2098 3969 2889 -827 172 -1023 N ATOM 4976 CA THR D 71 -12.224 19.398 30.108 1.00 22.95 C ANISOU 4976 CA THR D 71 2083 3904 2732 -692 151 -948 C ATOM 4977 C THR D 71 -12.448 20.771 30.735 1.00 24.50 C ANISOU 4977 C THR D 71 2202 4134 2971 -595 166 -862 C ATOM 4978 O THR D 71 -11.481 21.415 31.108 1.00 23.31 O ANISOU 4978 O THR D 71 2128 3928 2799 -521 213 -791 O ATOM 4979 CB THR D 71 -12.339 19.490 28.573 1.00 27.22 C ANISOU 4979 CB THR D 71 2633 4541 3170 -673 33 -984 C ATOM 4980 OG1 THR D 71 -11.976 18.216 28.080 1.00 27.76 O ANISOU 4980 OG1 THR D 71 2804 4552 3193 -757 42 -1073 O ATOM 4981 CG2 THR D 71 -11.407 20.556 27.962 1.00 23.23 C ANISOU 4981 CG2 THR D 71 2198 4055 2572 -548 18 -899 C ATOM 4982 N ASP D 72 -13.708 21.221 30.834 1.00 21.22 N ANISOU 4982 N ASP D 72 1633 3808 2622 -596 125 -873 N ATOM 4983 CA ASP D 72 -14.019 22.582 31.280 1.00 22.44 C ANISOU 4983 CA ASP D 72 1716 3992 2819 -483 133 -802 C ATOM 4984 C ASP D 72 -13.750 22.890 32.742 1.00 27.43 C ANISOU 4984 C ASP D 72 2376 4536 3510 -475 264 -766 C ATOM 4985 O ASP D 72 -13.429 24.040 33.051 1.00 28.68 O ANISOU 4985 O ASP D 72 2559 4671 3667 -373 283 -701 O ATOM 4986 CB ASP D 72 -15.496 22.914 31.000 1.00 26.23 C ANISOU 4986 CB ASP D 72 2000 4597 3370 -471 57 -831 C ATOM 4987 CG ASP D 72 -15.841 23.095 29.535 1.00 44.46 C ANISOU 4987 CG ASP D 72 4272 7016 5606 -434 -107 -838 C ATOM 4988 OD1 ASP D 72 -15.191 22.446 28.689 1.00 46.68 O ANISOU 4988 OD1 ASP D 72 4669 7286 5782 -481 -151 -866 O ATOM 4989 OD2 ASP D 72 -16.814 23.834 29.239 1.00 55.15 O ANISOU 4989 OD2 ASP D 72 5478 8470 7006 -358 -193 -819 O ATOM 4990 N ASP D 73 -13.863 21.900 33.633 1.00 22.98 N ANISOU 4990 N ASP D 73 1830 3915 2988 -586 352 -806 N ATOM 4991 CA ASP D 73 -13.839 22.168 35.075 1.00 22.01 C ANISOU 4991 CA ASP D 73 1729 3727 2908 -591 473 -779 C ATOM 4992 C ASP D 73 -12.687 21.547 35.833 1.00 22.49 C ANISOU 4992 C ASP D 73 1954 3666 2926 -633 540 -751 C ATOM 4993 O ASP D 73 -12.327 20.397 35.596 1.00 20.11 O ANISOU 4993 O ASP D 73 1720 3317 2605 -708 534 -781 O ATOM 4994 CB ASP D 73 -15.153 21.640 35.681 1.00 25.40 C ANISOU 4994 CB ASP D 73 2023 4201 3426 -689 536 -836 C ATOM 4995 CG ASP D 73 -16.417 22.140 34.994 1.00 44.91 C ANISOU 4995 CG ASP D 73 4289 6809 5964 -652 462 -870 C ATOM 4996 OD1 ASP D 73 -16.619 23.373 34.948 1.00 45.15 O ANISOU 4996 OD1 ASP D 73 4263 6878 6013 -518 442 -830 O ATOM 4997 OD2 ASP D 73 -17.227 21.291 34.537 1.00 59.07 O ANISOU 4997 OD2 ASP D 73 5978 8670 7797 -759 421 -938 O ATOM 4998 N PHE D 74 -12.171 22.290 36.832 1.00 18.74 N ANISOU 4998 N PHE D 74 1545 3137 2440 -585 604 -699 N ATOM 4999 CA PHE D 74 -11.066 21.803 37.657 1.00 16.90 C ANISOU 4999 CA PHE D 74 1458 2799 2163 -614 649 -662 C ATOM 5000 C PHE D 74 -11.263 22.271 39.109 1.00 20.55 C ANISOU 5000 C PHE D 74 1956 3222 2629 -627 747 -640 C ATOM 5001 O PHE D 74 -10.648 23.258 39.515 1.00 20.54 O ANISOU 5001 O PHE D 74 2010 3197 2597 -560 749 -600 O ATOM 5002 CB PHE D 74 -9.702 22.269 37.063 1.00 16.17 C ANISOU 5002 CB PHE D 74 1446 2683 2014 -535 588 -614 C ATOM 5003 CG PHE D 74 -8.462 21.586 37.615 1.00 16.65 C ANISOU 5003 CG PHE D 74 1630 2655 2042 -554 601 -580 C ATOM 5004 CD1 PHE D 74 -8.445 20.210 37.842 1.00 18.08 C ANISOU 5004 CD1 PHE D 74 1863 2776 2231 -626 623 -604 C ATOM 5005 CD2 PHE D 74 -7.283 22.307 37.824 1.00 17.25 C ANISOU 5005 CD2 PHE D 74 1765 2705 2083 -497 583 -524 C ATOM 5006 CE1 PHE D 74 -7.288 19.576 38.302 1.00 18.79 C ANISOU 5006 CE1 PHE D 74 2061 2781 2297 -618 621 -564 C ATOM 5007 CE2 PHE D 74 -6.122 21.671 38.281 1.00 18.36 C ANISOU 5007 CE2 PHE D 74 1991 2780 2204 -501 577 -491 C ATOM 5008 CZ PHE D 74 -6.128 20.304 38.500 1.00 16.97 C ANISOU 5008 CZ PHE D 74 1864 2545 2038 -550 593 -508 C ATOM 5009 N PRO D 75 -12.134 21.610 39.907 1.00 19.88 N ANISOU 5009 N PRO D 75 1847 3131 2574 -721 835 -671 N ATOM 5010 CA PRO D 75 -12.376 22.093 41.282 1.00 19.26 C ANISOU 5010 CA PRO D 75 1814 3024 2480 -734 945 -657 C ATOM 5011 C PRO D 75 -11.271 21.706 42.262 1.00 22.11 C ANISOU 5011 C PRO D 75 2358 3283 2759 -765 962 -602 C ATOM 5012 O PRO D 75 -10.775 20.579 42.245 1.00 21.68 O ANISOU 5012 O PRO D 75 2381 3169 2685 -822 940 -585 O ATOM 5013 CB PRO D 75 -13.704 21.406 41.674 1.00 21.82 C ANISOU 5013 CB PRO D 75 2042 3387 2863 -841 1042 -708 C ATOM 5014 CG PRO D 75 -13.692 20.108 40.908 1.00 25.40 C ANISOU 5014 CG PRO D 75 2493 3823 3334 -927 987 -730 C ATOM 5015 CD PRO D 75 -13.009 20.455 39.582 1.00 21.85 C ANISOU 5015 CD PRO D 75 2028 3403 2873 -831 850 -725 C ATOM 5016 N LEU D 76 -10.892 22.647 43.112 1.00 17.82 N ANISOU 5016 N LEU D 76 1886 2718 2167 -723 993 -578 N ATOM 5017 CA LEU D 76 -9.912 22.430 44.158 1.00 17.34 C ANISOU 5017 CA LEU D 76 1993 2577 2017 -751 996 -526 C ATOM 5018 C LEU D 76 -10.628 22.310 45.504 1.00 23.39 C ANISOU 5018 C LEU D 76 2824 3324 2737 -828 1129 -536 C ATOM 5019 O LEU D 76 -11.291 23.255 45.923 1.00 23.40 O ANISOU 5019 O LEU D 76 2786 3360 2744 -800 1208 -574 O ATOM 5020 CB LEU D 76 -8.922 23.596 44.206 1.00 16.49 C ANISOU 5020 CB LEU D 76 1937 2459 1870 -672 932 -499 C ATOM 5021 CG LEU D 76 -7.862 23.524 45.313 1.00 17.96 C ANISOU 5021 CG LEU D 76 2285 2580 1960 -701 908 -448 C ATOM 5022 CD1 LEU D 76 -6.848 22.436 45.011 1.00 15.51 C ANISOU 5022 CD1 LEU D 76 2020 2232 1643 -708 821 -397 C ATOM 5023 CD2 LEU D 76 -7.172 24.878 45.495 1.00 19.23 C ANISOU 5023 CD2 LEU D 76 2483 2736 2087 -649 867 -443 C ATOM 5024 N THR D 77 -10.420 21.201 46.219 1.00 20.50 N ANISOU 5024 N THR D 77 2577 2895 2318 -917 1157 -498 N ATOM 5025 CA THR D 77 -11.039 20.994 47.513 1.00 21.71 C ANISOU 5025 CA THR D 77 2818 3025 2403 -1005 1292 -497 C ATOM 5026 C THR D 77 -10.014 21.025 48.649 1.00 24.53 C ANISOU 5026 C THR D 77 3382 3313 2624 -1015 1262 -431 C ATOM 5027 O THR D 77 -8.921 20.462 48.541 1.00 23.63 O ANISOU 5027 O THR D 77 3353 3145 2481 -997 1146 -369 O ATOM 5028 CB THR D 77 -11.817 19.656 47.505 1.00 25.05 C ANISOU 5028 CB THR D 77 3227 3426 2864 -1124 1366 -499 C ATOM 5029 OG1 THR D 77 -12.818 19.750 46.496 1.00 27.10 O ANISOU 5029 OG1 THR D 77 3280 3771 3247 -1122 1381 -570 O ATOM 5030 CG2 THR D 77 -12.473 19.312 48.875 1.00 29.19 C ANISOU 5030 CG2 THR D 77 3860 3924 3307 -1240 1529 -486 C ATOM 5031 N LEU D 78 -10.411 21.691 49.739 1.00 20.91 N ANISOU 5031 N LEU D 78 3000 2863 2082 -1042 1369 -451 N ATOM 5032 CA LEU D 78 -9.772 21.731 51.058 1.00 21.14 C ANISOU 5032 CA LEU D 78 3242 2838 1950 -1082 1372 -403 C ATOM 5033 C LEU D 78 -10.683 20.922 51.959 1.00 25.39 C ANISOU 5033 C LEU D 78 3862 3358 2428 -1203 1534 -394 C ATOM 5034 O LEU D 78 -11.735 21.418 52.348 1.00 26.65 O ANISOU 5034 O LEU D 78 3967 3565 2592 -1231 1695 -460 O ATOM 5035 CB LEU D 78 -9.617 23.179 51.562 1.00 21.71 C ANISOU 5035 CB LEU D 78 3354 2933 1963 -1030 1389 -452 C ATOM 5036 CG LEU D 78 -8.481 23.985 50.902 1.00 25.60 C ANISOU 5036 CG LEU D 78 3818 3425 2484 -940 1224 -442 C ATOM 5037 CD1 LEU D 78 -8.861 24.431 49.481 1.00 25.01 C ANISOU 5037 CD1 LEU D 78 3539 3399 2566 -856 1198 -482 C ATOM 5038 CD2 LEU D 78 -8.144 25.198 51.752 1.00 28.16 C ANISOU 5038 CD2 LEU D 78 4259 3734 2705 -930 1233 -477 C ATOM 5039 N ALA D 79 -10.346 19.659 52.215 1.00 23.89 N ANISOU 5039 N ALA D 79 3787 3095 2195 -1272 1503 -314 N ATOM 5040 CA ALA D 79 -11.185 18.755 53.017 1.00 26.60 C ANISOU 5040 CA ALA D 79 4223 3402 2480 -1408 1661 -290 C ATOM 5041 C ALA D 79 -11.357 19.251 54.452 1.00 31.73 C ANISOU 5041 C ALA D 79 5050 4054 2952 -1462 1779 -285 C ATOM 5042 O ALA D 79 -12.459 19.167 54.986 1.00 31.15 O ANISOU 5042 O ALA D 79 4966 4009 2861 -1554 1978 -323 O ATOM 5043 CB ALA D 79 -10.607 17.352 53.015 1.00 28.20 C ANISOU 5043 CB ALA D 79 4554 3497 2663 -1455 1582 -191 C ATOM 5044 N SER D 80 -10.291 19.817 55.055 1.00 28.86 N ANISOU 5044 N SER D 80 4838 3670 2459 -1410 1661 -249 N ATOM 5045 CA SER D 80 -10.358 20.324 56.424 1.00 29.81 C ANISOU 5045 CA SER D 80 5154 3790 2382 -1463 1754 -252 C ATOM 5046 C SER D 80 -9.399 21.482 56.521 1.00 34.43 C ANISOU 5046 C SER D 80 5776 4393 2913 -1374 1615 -279 C ATOM 5047 O SER D 80 -8.210 21.278 56.765 1.00 34.52 O ANISOU 5047 O SER D 80 5906 4367 2843 -1353 1434 -202 O ATOM 5048 CB SER D 80 -10.033 19.218 57.425 1.00 33.84 C ANISOU 5048 CB SER D 80 5912 4219 2724 -1562 1751 -134 C ATOM 5049 OG SER D 80 -10.244 19.692 58.742 1.00 40.44 O ANISOU 5049 OG SER D 80 6947 5066 3352 -1628 1865 -145 O ATOM 5050 N ALA D 81 -9.902 22.696 56.255 1.00 32.19 N ANISOU 5050 N ALA D 81 5375 4165 2692 -1317 1691 -389 N ATOM 5051 CA ALA D 81 -9.074 23.907 56.165 1.00 32.10 C ANISOU 5051 CA ALA D 81 5376 4158 2662 -1238 1568 -430 C ATOM 5052 C ALA D 81 -8.285 24.197 57.444 1.00 34.90 C ANISOU 5052 C ALA D 81 5988 4483 2789 -1290 1508 -404 C ATOM 5053 O ALA D 81 -8.807 24.047 58.546 1.00 35.20 O ANISOU 5053 O ALA D 81 6193 4514 2668 -1372 1648 -412 O ATOM 5054 CB ALA D 81 -9.921 25.104 55.797 1.00 32.50 C ANISOU 5054 CB ALA D 81 5291 4249 2809 -1171 1692 -549 C ATOM 5055 N VAL D 82 -6.999 24.556 57.274 1.00 29.78 N ANISOU 5055 N VAL D 82 5368 3823 2124 -1249 1293 -370 N ATOM 5056 CA VAL D 82 -6.097 24.907 58.389 1.00 29.88 C ANISOU 5056 CA VAL D 82 5605 3819 1928 -1299 1184 -348 C ATOM 5057 C VAL D 82 -5.602 26.368 58.158 1.00 31.84 C ANISOU 5057 C VAL D 82 5819 4075 2205 -1256 1115 -439 C ATOM 5058 O VAL D 82 -5.585 26.799 56.995 1.00 28.02 O ANISOU 5058 O VAL D 82 5137 3602 1908 -1178 1086 -467 O ATOM 5059 CB VAL D 82 -4.917 23.904 58.584 1.00 33.05 C ANISOU 5059 CB VAL D 82 6088 4202 2268 -1309 970 -212 C ATOM 5060 CG1 VAL D 82 -5.413 22.534 59.055 1.00 34.30 C ANISOU 5060 CG1 VAL D 82 6351 4322 2358 -1366 1049 -118 C ATOM 5061 CG2 VAL D 82 -4.055 23.777 57.326 1.00 30.07 C ANISOU 5061 CG2 VAL D 82 5507 3836 2081 -1218 799 -176 C ATOM 5062 N PRO D 83 -5.199 27.121 59.225 1.00 29.59 N ANISOU 5062 N PRO D 83 5736 3776 1729 -1315 1087 -485 N ATOM 5063 CA PRO D 83 -4.763 28.520 59.031 1.00 28.86 C ANISOU 5063 CA PRO D 83 5632 3669 1665 -1292 1032 -579 C ATOM 5064 C PRO D 83 -3.628 28.724 58.009 1.00 31.20 C ANISOU 5064 C PRO D 83 5770 3977 2108 -1245 821 -534 C ATOM 5065 O PRO D 83 -3.607 29.764 57.363 1.00 30.05 O ANISOU 5065 O PRO D 83 5535 3812 2070 -1204 828 -603 O ATOM 5066 CB PRO D 83 -4.320 28.941 60.434 1.00 32.05 C ANISOU 5066 CB PRO D 83 6310 4057 1810 -1390 993 -613 C ATOM 5067 CG PRO D 83 -5.209 28.118 61.350 1.00 37.50 C ANISOU 5067 CG PRO D 83 7148 4753 2349 -1445 1166 -590 C ATOM 5068 CD PRO D 83 -5.223 26.773 60.668 1.00 31.81 C ANISOU 5068 CD PRO D 83 6288 4049 1751 -1414 1123 -463 C ATOM 5069 N SER D 84 -2.712 27.752 57.834 1.00 27.26 N ANISOU 5069 N SER D 84 5234 3504 1619 -1245 646 -417 N ATOM 5070 CA SER D 84 -1.619 27.866 56.861 1.00 26.02 C ANISOU 5070 CA SER D 84 4911 3371 1605 -1199 465 -374 C ATOM 5071 C SER D 84 -2.145 27.845 55.406 1.00 28.42 C ANISOU 5071 C SER D 84 4986 3681 2133 -1108 543 -386 C ATOM 5072 O SER D 84 -1.396 28.176 54.477 1.00 28.17 O ANISOU 5072 O SER D 84 4814 3667 2225 -1069 439 -371 O ATOM 5073 CB SER D 84 -0.603 26.748 57.060 1.00 30.54 C ANISOU 5073 CB SER D 84 5492 3969 2142 -1200 280 -250 C ATOM 5074 OG SER D 84 -1.181 25.498 56.726 1.00 37.57 O ANISOU 5074 OG SER D 84 6337 4847 3092 -1158 354 -182 O ATOM 5075 N GLN D 85 -3.438 27.496 55.209 1.00 23.62 N ANISOU 5075 N GLN D 85 4340 3066 1571 -1081 728 -414 N ATOM 5076 CA GLN D 85 -4.036 27.495 53.875 1.00 21.59 C ANISOU 5076 CA GLN D 85 3875 2823 1506 -1000 793 -431 C ATOM 5077 C GLN D 85 -4.589 28.891 53.521 1.00 24.49 C ANISOU 5077 C GLN D 85 4200 3171 1934 -960 882 -529 C ATOM 5078 O GLN D 85 -5.106 29.085 52.421 1.00 23.89 O ANISOU 5078 O GLN D 85 3962 3108 2006 -886 925 -545 O ATOM 5079 CB GLN D 85 -5.082 26.385 53.717 1.00 21.71 C ANISOU 5079 CB GLN D 85 3838 2847 1562 -997 918 -409 C ATOM 5080 CG GLN D 85 -4.387 25.031 53.703 1.00 25.35 C ANISOU 5080 CG GLN D 85 4317 3303 2010 -1010 805 -303 C ATOM 5081 CD GLN D 85 -5.350 23.893 53.642 1.00 36.46 C ANISOU 5081 CD GLN D 85 5707 4699 3447 -1033 924 -280 C ATOM 5082 OE1 GLN D 85 -6.258 23.788 54.452 1.00 29.78 O ANISOU 5082 OE1 GLN D 85 4954 3846 2516 -1095 1073 -306 O ATOM 5083 NE2 GLN D 85 -5.192 23.042 52.652 1.00 26.81 N ANISOU 5083 NE2 GLN D 85 4363 3476 2348 -993 872 -239 N ATOM 5084 N THR D 86 -4.403 29.873 54.416 1.00 23.01 N ANISOU 5084 N THR D 86 4169 2945 1630 -1005 893 -593 N ATOM 5085 CA THR D 86 -4.708 31.286 54.148 1.00 22.74 C ANISOU 5085 CA THR D 86 4130 2862 1647 -965 956 -684 C ATOM 5086 C THR D 86 -3.789 31.704 53.000 1.00 26.41 C ANISOU 5086 C THR D 86 4467 3329 2238 -933 814 -644 C ATOM 5087 O THR D 86 -2.559 31.621 53.136 1.00 25.94 O ANISOU 5087 O THR D 86 4436 3282 2137 -992 654 -597 O ATOM 5088 CB THR D 86 -4.486 32.137 55.413 1.00 28.49 C ANISOU 5088 CB THR D 86 5085 3537 2203 -1040 974 -762 C ATOM 5089 OG1 THR D 86 -5.464 31.800 56.405 1.00 29.12 O ANISOU 5089 OG1 THR D 86 5281 3619 2164 -1064 1143 -806 O ATOM 5090 CG2 THR D 86 -4.490 33.658 55.117 1.00 28.84 C ANISOU 5090 CG2 THR D 86 5154 3502 2304 -1008 1000 -850 C ATOM 5091 N SER D 87 -4.365 32.109 51.868 1.00 22.53 N ANISOU 5091 N SER D 87 3830 2833 1897 -842 869 -655 N ATOM 5092 CA SER D 87 -3.574 32.455 50.691 1.00 21.98 C ANISOU 5092 CA SER D 87 3643 2769 1939 -814 758 -609 C ATOM 5093 C SER D 87 -4.448 33.069 49.607 1.00 25.20 C ANISOU 5093 C SER D 87 3936 3160 2480 -708 839 -630 C ATOM 5094 O SER D 87 -5.666 33.242 49.785 1.00 24.22 O ANISOU 5094 O SER D 87 3802 3024 2375 -648 975 -684 O ATOM 5095 CB SER D 87 -2.931 31.175 50.116 1.00 21.75 C ANISOU 5095 CB SER D 87 3502 2814 1950 -816 656 -518 C ATOM 5096 OG SER D 87 -1.825 31.500 49.294 1.00 24.67 O ANISOU 5096 OG SER D 87 3794 3196 2384 -821 538 -475 O ATOM 5097 N VAL D 88 -3.807 33.390 48.480 1.00 19.60 N ANISOU 5097 N VAL D 88 3133 2455 1858 -683 754 -583 N ATOM 5098 CA VAL D 88 -4.478 33.802 47.258 1.00 18.54 C ANISOU 5098 CA VAL D 88 2882 2320 1842 -581 793 -573 C ATOM 5099 C VAL D 88 -4.324 32.626 46.317 1.00 21.56 C ANISOU 5099 C VAL D 88 3119 2793 2279 -562 739 -508 C ATOM 5100 O VAL D 88 -3.195 32.154 46.086 1.00 21.18 O ANISOU 5100 O VAL D 88 3050 2777 2220 -612 639 -457 O ATOM 5101 CB VAL D 88 -4.000 35.151 46.655 1.00 22.93 C ANISOU 5101 CB VAL D 88 3475 2796 2442 -567 760 -569 C ATOM 5102 CG1 VAL D 88 -4.754 35.450 45.357 1.00 22.06 C ANISOU 5102 CG1 VAL D 88 3249 2693 2439 -450 788 -541 C ATOM 5103 CG2 VAL D 88 -4.216 36.296 47.654 1.00 23.29 C ANISOU 5103 CG2 VAL D 88 3689 2729 2432 -587 825 -651 C ATOM 5104 N TYR D 89 -5.455 32.081 45.850 1.00 18.14 N ANISOU 5104 N TYR D 89 2585 2405 1902 -495 806 -519 N ATOM 5105 CA TYR D 89 -5.445 30.927 44.949 1.00 16.63 C ANISOU 5105 CA TYR D 89 2271 2291 1758 -482 763 -475 C ATOM 5106 C TYR D 89 -5.740 31.314 43.511 1.00 20.17 C ANISOU 5106 C TYR D 89 2610 2764 2289 -402 740 -453 C ATOM 5107 O TYR D 89 -6.726 32.000 43.240 1.00 21.61 O ANISOU 5107 O TYR D 89 2758 2935 2519 -327 793 -480 O ATOM 5108 CB TYR D 89 -6.460 29.883 45.418 1.00 16.50 C ANISOU 5108 CB TYR D 89 2219 2313 1738 -493 842 -501 C ATOM 5109 CG TYR D 89 -6.060 29.270 46.731 1.00 17.99 C ANISOU 5109 CG TYR D 89 2529 2481 1825 -579 852 -499 C ATOM 5110 CD1 TYR D 89 -5.338 28.079 46.775 1.00 17.93 C ANISOU 5110 CD1 TYR D 89 2529 2493 1792 -624 782 -446 C ATOM 5111 CD2 TYR D 89 -6.390 29.886 47.943 1.00 19.25 C ANISOU 5111 CD2 TYR D 89 2812 2596 1905 -609 932 -548 C ATOM 5112 CE1 TYR D 89 -4.953 27.516 47.991 1.00 18.72 C ANISOU 5112 CE1 TYR D 89 2755 2570 1788 -694 775 -428 C ATOM 5113 CE2 TYR D 89 -5.990 29.346 49.159 1.00 19.91 C ANISOU 5113 CE2 TYR D 89 3030 2664 1869 -692 930 -538 C ATOM 5114 CZ TYR D 89 -5.280 28.158 49.179 1.00 23.60 C ANISOU 5114 CZ TYR D 89 3502 3154 2312 -733 844 -471 C ATOM 5115 OH TYR D 89 -4.919 27.627 50.382 1.00 20.29 O ANISOU 5115 OH TYR D 89 3227 2716 1765 -806 831 -448 O ATOM 5116 N PHE D 90 -4.904 30.827 42.584 1.00 15.26 N ANISOU 5116 N PHE D 90 1935 2183 1682 -411 660 -403 N ATOM 5117 CA PHE D 90 -5.119 31.082 41.181 1.00 14.98 C ANISOU 5117 CA PHE D 90 1815 2180 1697 -346 633 -376 C ATOM 5118 C PHE D 90 -5.273 29.836 40.406 1.00 19.32 C ANISOU 5118 C PHE D 90 2272 2804 2263 -342 609 -370 C ATOM 5119 O PHE D 90 -4.397 28.962 40.453 1.00 17.22 O ANISOU 5119 O PHE D 90 2011 2554 1977 -386 574 -351 O ATOM 5120 CB PHE D 90 -3.943 31.860 40.528 1.00 15.67 C ANISOU 5120 CB PHE D 90 1933 2243 1778 -361 577 -325 C ATOM 5121 CG PHE D 90 -3.914 33.331 40.858 1.00 17.57 C ANISOU 5121 CG PHE D 90 2266 2392 2018 -355 597 -328 C ATOM 5122 CD1 PHE D 90 -4.682 34.238 40.133 1.00 19.62 C ANISOU 5122 CD1 PHE D 90 2521 2619 2316 -266 615 -316 C ATOM 5123 CD2 PHE D 90 -3.142 33.808 41.907 1.00 19.13 C ANISOU 5123 CD2 PHE D 90 2566 2529 2175 -435 590 -344 C ATOM 5124 CE1 PHE D 90 -4.680 35.601 40.462 1.00 20.62 C ANISOU 5124 CE1 PHE D 90 2753 2632 2448 -252 640 -321 C ATOM 5125 CE2 PHE D 90 -3.129 35.175 42.220 1.00 22.54 C ANISOU 5125 CE2 PHE D 90 3102 2856 2605 -438 612 -360 C ATOM 5126 CZ PHE D 90 -3.917 36.054 41.509 1.00 19.74 C ANISOU 5126 CZ PHE D 90 2753 2451 2297 -343 645 -349 C ATOM 5127 N ACYS D 91 -6.343 29.763 39.622 0.50 15.78 N ANISOU 5127 N ACYS D 91 1740 2401 1855 -283 618 -386 N ATOM 5128 N BCYS D 91 -6.349 29.749 39.624 0.50 17.20 N ANISOU 5128 N BCYS D 91 1919 2581 2035 -284 618 -386 N ATOM 5129 CA ACYS D 91 -6.491 28.670 38.675 0.50 15.47 C ANISOU 5129 CA ACYS D 91 1623 2430 1826 -286 584 -389 C ATOM 5130 CA BCYS D 91 -6.438 28.632 38.697 0.50 17.55 C ANISOU 5130 CA BCYS D 91 1888 2693 2087 -289 583 -388 C ATOM 5131 C ACYS D 91 -5.943 29.171 37.331 0.50 18.30 C ANISOU 5131 C ACYS D 91 1968 2813 2171 -245 527 -345 C ATOM 5132 C BCYS D 91 -5.976 29.149 37.324 0.50 19.38 C ANISOU 5132 C BCYS D 91 2103 2952 2309 -244 527 -346 C ATOM 5133 O ACYS D 91 -5.956 30.385 37.081 0.50 17.58 O ANISOU 5133 O ACYS D 91 1908 2691 2083 -200 521 -314 O ATOM 5134 O BCYS D 91 -6.070 30.355 37.056 0.50 19.02 O ANISOU 5134 O BCYS D 91 2083 2876 2267 -196 521 -317 O ATOM 5135 CB ACYS D 91 -7.947 28.229 38.580 0.50 16.22 C ANISOU 5135 CB ACYS D 91 1624 2574 1964 -267 613 -436 C ATOM 5136 CB BCYS D 91 -7.832 28.012 38.664 0.50 19.03 C ANISOU 5136 CB BCYS D 91 1987 2928 2315 -281 614 -437 C ATOM 5137 SG ACYS D 91 -8.250 26.871 37.417 0.50 20.06 S ANISOU 5137 SG ACYS D 91 2027 3137 2456 -291 563 -460 S ATOM 5138 SG BCYS D 91 -9.024 28.875 37.613 0.50 24.18 S ANISOU 5138 SG BCYS D 91 2537 3636 3015 -181 584 -441 S ATOM 5139 N ALA D 92 -5.401 28.265 36.497 1.00 13.58 N ANISOU 5139 N ALA D 92 1346 2261 1554 -262 495 -340 N ATOM 5140 CA ALA D 92 -4.886 28.633 35.181 1.00 12.68 C ANISOU 5140 CA ALA D 92 1230 2182 1408 -233 458 -302 C ATOM 5141 C ALA D 92 -5.116 27.507 34.201 1.00 17.93 C ANISOU 5141 C ALA D 92 1848 2912 2051 -234 433 -336 C ATOM 5142 O ALA D 92 -5.299 26.360 34.608 1.00 16.52 O ANISOU 5142 O ALA D 92 1653 2733 1891 -271 446 -382 O ATOM 5143 CB ALA D 92 -3.374 28.971 35.229 1.00 12.66 C ANISOU 5143 CB ALA D 92 1275 2151 1384 -268 463 -257 C ATOM 5144 N SER D 93 -5.088 27.836 32.909 1.00 15.02 N ANISOU 5144 N SER D 93 1480 2592 1637 -200 399 -312 N ATOM 5145 CA SER D 93 -5.190 26.825 31.878 1.00 16.06 C ANISOU 5145 CA SER D 93 1590 2785 1726 -207 375 -353 C ATOM 5146 C SER D 93 -4.279 27.178 30.729 1.00 19.03 C ANISOU 5146 C SER D 93 2011 3192 2028 -193 375 -311 C ATOM 5147 O SER D 93 -3.952 28.355 30.523 1.00 18.28 O ANISOU 5147 O SER D 93 1953 3079 1912 -173 377 -241 O ATOM 5148 CB SER D 93 -6.641 26.615 31.410 1.00 18.21 C ANISOU 5148 CB SER D 93 1800 3115 2003 -189 320 -394 C ATOM 5149 OG SER D 93 -7.209 27.724 30.736 1.00 21.18 O ANISOU 5149 OG SER D 93 2171 3523 2355 -123 268 -345 O ATOM 5150 N SER D 94 -3.884 26.149 29.962 1.00 15.13 N ANISOU 5150 N SER D 94 1524 2736 1488 -209 384 -356 N ATOM 5151 CA SER D 94 -3.075 26.311 28.747 1.00 15.47 C ANISOU 5151 CA SER D 94 1612 2824 1443 -200 404 -331 C ATOM 5152 C SER D 94 -3.507 25.257 27.735 1.00 19.45 C ANISOU 5152 C SER D 94 2128 3385 1878 -204 380 -408 C ATOM 5153 O SER D 94 -4.059 24.231 28.131 1.00 18.19 O ANISOU 5153 O SER D 94 1941 3210 1762 -229 366 -482 O ATOM 5154 CB SER D 94 -1.583 26.222 29.076 1.00 16.56 C ANISOU 5154 CB SER D 94 1753 2935 1606 -218 479 -309 C ATOM 5155 OG SER D 94 -1.233 24.927 29.515 1.00 21.13 O ANISOU 5155 OG SER D 94 2309 3492 2230 -226 504 -373 O ATOM 5156 N ALA D 95 -3.335 25.520 26.433 1.00 19.72 N ANISOU 5156 N ALA D 95 2215 3480 1796 -191 373 -393 N ATOM 5157 CA ALA D 95 -3.777 24.583 25.387 1.00 21.58 C ANISOU 5157 CA ALA D 95 2483 3775 1940 -204 341 -475 C ATOM 5158 C ALA D 95 -3.286 23.142 25.703 1.00 27.93 C ANISOU 5158 C ALA D 95 3285 4536 2790 -229 401 -572 C ATOM 5159 O ALA D 95 -4.103 22.212 25.712 1.00 28.80 O ANISOU 5159 O ALA D 95 3388 4642 2914 -261 357 -657 O ATOM 5160 CB ALA D 95 -3.324 25.050 24.007 1.00 23.06 C ANISOU 5160 CB ALA D 95 2757 4030 1976 -191 355 -441 C ATOM 5161 N GLY D 96 -2.018 23.018 26.083 1.00 22.78 N ANISOU 5161 N GLY D 96 2631 3844 2181 -215 493 -553 N ATOM 5162 CA GLY D 96 -1.396 21.772 26.524 1.00 22.86 C ANISOU 5162 CA GLY D 96 2636 3794 2255 -211 551 -622 C ATOM 5163 C GLY D 96 -0.252 22.047 27.487 1.00 27.94 C ANISOU 5163 C GLY D 96 3230 4393 2992 -190 606 -560 C ATOM 5164 O GLY D 96 0.089 23.213 27.721 1.00 24.19 O ANISOU 5164 O GLY D 96 2731 3936 2523 -195 608 -475 O ATOM 5165 N ALA D 97 0.332 20.979 28.101 1.00 30.02 N ANISOU 5165 N ALA D 97 3481 4591 3333 -169 642 -601 N ATOM 5166 CA ALA D 97 1.485 21.108 29.043 1.00 31.58 C ANISOU 5166 CA ALA D 97 3619 4756 3622 -142 674 -545 C ATOM 5167 C ALA D 97 2.779 21.464 28.301 1.00 37.35 C ANISOU 5167 C ALA D 97 4313 5547 4331 -111 758 -523 C ATOM 5168 O ALA D 97 3.739 21.947 28.903 1.00 37.33 O ANISOU 5168 O ALA D 97 4239 5551 4394 -107 775 -462 O ATOM 5169 CB ALA D 97 1.673 19.821 29.834 1.00 32.99 C ANISOU 5169 CB ALA D 97 3806 4845 3883 -114 674 -586 C ATOM 5170 N ASER D 98 2.825 21.138 27.014 0.50 32.66 N ANISOU 5170 N ASER D 98 3766 4999 3643 -96 815 -580 N ATOM 5171 N BSER D 98 2.796 21.261 26.972 0.50 35.81 N ANISOU 5171 N BSER D 98 4167 5405 4036 -100 813 -573 N ATOM 5172 CA ASER D 98 3.989 21.368 26.181 0.50 32.15 C ANISOU 5172 CA ASER D 98 3673 5000 3543 -71 923 -572 C ATOM 5173 CA BSER D 98 3.889 21.683 26.095 0.50 36.86 C ANISOU 5173 CA BSER D 98 4275 5610 4121 -85 916 -554 C ATOM 5174 C ASER D 98 3.738 22.506 25.197 0.50 32.93 C ANISOU 5174 C ASER D 98 3821 5177 3514 -118 935 -521 C ATOM 5175 C BSER D 98 3.578 23.130 25.728 0.50 42.68 C ANISOU 5175 C BSER D 98 5034 6399 4782 -142 892 -467 C ATOM 5176 O ASER D 98 4.653 22.889 24.468 0.50 32.45 O ANISOU 5176 O ASER D 98 3744 5177 3406 -119 1037 -499 O ATOM 5177 O BSER D 98 2.393 23.487 25.782 0.50 43.26 O ANISOU 5177 O BSER D 98 5158 6462 4817 -166 801 -456 O ATOM 5178 CB ASER D 98 4.324 20.088 25.415 0.50 36.91 C ANISOU 5178 CB ASER D 98 4316 5590 4118 -12 1003 -682 C ATOM 5179 CB BSER D 98 3.965 20.782 24.862 0.50 40.84 C ANISOU 5179 CB BSER D 98 4849 6138 4529 -51 993 -655 C ATOM 5180 OG ASER D 98 4.233 18.929 26.228 0.50 41.81 O ANISOU 5180 OG ASER D 98 4936 6110 4839 31 974 -732 O ATOM 5181 OG BSER D 98 3.844 19.405 25.185 0.50 40.45 O ANISOU 5181 OG BSER D 98 4821 6006 4541 -5 991 -747 O ATOM 5182 N ATHR D 99 2.481 23.008 25.125 0.50 27.14 N ANISOU 5182 N ATHR D 99 3147 4442 2722 -152 836 -503 N ATOM 5183 N BTHR D 99 4.593 23.970 25.381 0.50 39.90 N ANISOU 5183 N BTHR D 99 4642 6099 4417 -164 972 -401 N ATOM 5184 CA ATHR D 99 2.150 24.057 24.172 0.50 25.57 C ANISOU 5184 CA ATHR D 99 3014 4306 2396 -181 828 -444 C ATOM 5185 CA BTHR D 99 4.433 25.419 25.103 0.50 39.50 C ANISOU 5185 CA BTHR D 99 4628 6073 4305 -223 959 -302 C ATOM 5186 C ATHR D 99 1.230 25.145 24.763 0.50 24.28 C ANISOU 5186 C ATHR D 99 2853 4117 2256 -203 723 -363 C ATOM 5187 C BTHR D 99 3.015 25.821 24.633 0.50 42.16 C ANISOU 5187 C BTHR D 99 5070 6407 4541 -228 863 -292 C ATOM 5188 O ATHR D 99 0.178 24.852 25.322 0.50 22.98 O ANISOU 5188 O ATHR D 99 2679 3920 2133 -199 634 -394 O ATOM 5189 O BTHR D 99 2.472 25.317 23.642 0.50 45.39 O ANISOU 5189 O BTHR D 99 5555 6857 4836 -211 857 -346 O ATOM 5190 CB ATHR D 99 1.592 23.435 22.857 0.50 32.86 C ANISOU 5190 CB ATHR D 99 4038 5282 3166 -175 826 -524 C ATOM 5191 CB BTHR D 99 5.505 26.015 24.177 0.50 50.52 C ANISOU 5191 CB BTHR D 99 6020 7539 5637 -257 1087 -256 C ATOM 5192 OG1ATHR D 99 1.517 24.436 21.848 0.50 31.83 O ANISOU 5192 OG1ATHR D 99 3984 5219 2893 -196 832 -452 O ATOM 5193 OG1BTHR D 99 5.413 27.439 24.258 0.50 54.95 O ANISOU 5193 OG1BTHR D 99 6615 8085 6177 -323 1062 -147 O ATOM 5194 CG2ATHR D 99 0.251 22.697 23.022 0.50 30.33 C ANISOU 5194 CG2ATHR D 99 3740 4936 2847 -182 710 -600 C ATOM 5195 CG2BTHR D 99 5.356 25.602 22.761 0.50 47.47 C ANISOU 5195 CG2BTHR D 99 5729 7215 5092 -239 1155 -305 C ATOM 5196 N AGLY D 100 1.654 26.400 24.599 0.50 20.54 N ANISOU 5196 N AGLY D 100 2394 3653 1756 -228 748 -263 N ATOM 5197 N BGLY D 100 2.479 26.756 25.392 0.50 32.70 N ANISOU 5197 N BGLY D 100 3870 5162 3391 -249 786 -224 N ATOM 5198 CA AGLY D 100 0.912 27.590 25.001 0.50 20.03 C ANISOU 5198 CA AGLY D 100 2353 3552 1704 -236 668 -180 C ATOM 5199 CA BGLY D 100 1.162 27.363 25.310 0.50 30.26 C ANISOU 5199 CA BGLY D 100 3622 4838 3039 -239 683 -195 C ATOM 5200 C AGLY D 100 1.236 28.186 26.353 0.50 23.98 C ANISOU 5200 C AGLY D 100 2795 3980 2335 -259 660 -138 C ATOM 5201 C BGLY D 100 1.121 28.158 26.588 0.50 28.80 C ANISOU 5201 C BGLY D 100 3397 4579 2966 -257 648 -143 C ATOM 5202 O AGLY D 100 1.778 27.521 27.234 0.50 23.62 O ANISOU 5202 O AGLY D 100 2678 3911 2384 -263 679 -178 O ATOM 5203 O BGLY D 100 1.378 27.598 27.660 0.50 28.25 O ANISOU 5203 O BGLY D 100 3263 4473 2998 -260 644 -179 O ATOM 5204 N GLU D 101 0.902 29.470 26.503 1.00 22.45 N ANISOU 5204 N GLU D 101 2647 3745 2139 -270 627 -55 N ATOM 5205 CA GLU D 101 1.000 30.266 27.722 1.00 20.67 C ANISOU 5205 CA GLU D 101 2402 3438 2014 -296 608 -18 C ATOM 5206 C GLU D 101 -0.193 30.012 28.652 1.00 19.45 C ANISOU 5206 C GLU D 101 2226 3244 1921 -256 531 -63 C ATOM 5207 O GLU D 101 -1.236 29.523 28.214 1.00 18.71 O ANISOU 5207 O GLU D 101 2133 3185 1792 -212 479 -101 O ATOM 5208 CB GLU D 101 1.142 31.768 27.394 1.00 22.22 C ANISOU 5208 CB GLU D 101 2680 3586 2175 -324 619 85 C ATOM 5209 CG GLU D 101 -0.123 32.435 26.855 1.00 22.15 C ANISOU 5209 CG GLU D 101 2752 3557 2106 -258 544 128 C ATOM 5210 CD GLU D 101 -0.242 32.466 25.343 1.00 42.35 C ANISOU 5210 CD GLU D 101 5387 6184 4520 -239 545 169 C ATOM 5211 OE1 GLU D 101 0.387 31.619 24.666 1.00 38.72 O ANISOU 5211 OE1 GLU D 101 4911 5804 3998 -263 605 127 O ATOM 5212 OE2 GLU D 101 -0.961 33.355 24.833 1.00 35.00 O ANISOU 5212 OE2 GLU D 101 4542 5224 3532 -194 487 244 O ATOM 5213 N LEU D 102 -0.013 30.305 29.935 1.00 15.40 N ANISOU 5213 N LEU D 102 1690 2666 1496 -281 526 -63 N ATOM 5214 CA LEU D 102 -1.085 30.182 30.899 1.00 16.30 C ANISOU 5214 CA LEU D 102 1790 2740 1664 -253 479 -102 C ATOM 5215 C LEU D 102 -2.029 31.360 30.812 1.00 20.14 C ANISOU 5215 C LEU D 102 2327 3181 2144 -210 444 -58 C ATOM 5216 O LEU D 102 -1.607 32.513 30.624 1.00 20.31 O ANISOU 5216 O LEU D 102 2414 3152 2152 -224 460 11 O ATOM 5217 CB LEU D 102 -0.573 30.054 32.351 1.00 16.79 C ANISOU 5217 CB LEU D 102 1830 2750 1800 -296 489 -122 C ATOM 5218 CG LEU D 102 0.229 28.808 32.722 1.00 25.42 C ANISOU 5218 CG LEU D 102 2867 3869 2920 -316 504 -162 C ATOM 5219 CD1 LEU D 102 0.526 28.775 34.239 1.00 26.47 C ANISOU 5219 CD1 LEU D 102 2999 3950 3108 -352 487 -171 C ATOM 5220 CD2 LEU D 102 -0.519 27.618 32.444 1.00 29.08 C ANISOU 5220 CD2 LEU D 102 3312 4363 3376 -282 492 -223 C ATOM 5221 N PHE D 103 -3.314 31.055 30.989 1.00 16.38 N ANISOU 5221 N PHE D 103 1817 2719 1688 -156 401 -99 N ATOM 5222 CA PHE D 103 -4.400 32.016 31.098 1.00 17.14 C ANISOU 5222 CA PHE D 103 1930 2776 1807 -88 365 -74 C ATOM 5223 C PHE D 103 -4.871 31.893 32.520 1.00 19.13 C ANISOU 5223 C PHE D 103 2149 2980 2139 -94 388 -128 C ATOM 5224 O PHE D 103 -5.276 30.809 32.922 1.00 18.38 O ANISOU 5224 O PHE D 103 1989 2926 2066 -113 391 -192 O ATOM 5225 CB PHE D 103 -5.530 31.739 30.069 1.00 19.16 C ANISOU 5225 CB PHE D 103 2146 3111 2022 -20 293 -80 C ATOM 5226 CG PHE D 103 -5.147 32.101 28.651 1.00 21.41 C ANISOU 5226 CG PHE D 103 2500 3436 2201 -7 266 -13 C ATOM 5227 CD1 PHE D 103 -5.491 33.339 28.113 1.00 26.63 C ANISOU 5227 CD1 PHE D 103 3232 4055 2831 59 227 77 C ATOM 5228 CD2 PHE D 103 -4.414 31.216 27.860 1.00 22.19 C ANISOU 5228 CD2 PHE D 103 2606 3605 2222 -57 288 -36 C ATOM 5229 CE1 PHE D 103 -5.123 33.679 26.798 1.00 28.06 C ANISOU 5229 CE1 PHE D 103 3501 4270 2892 63 207 153 C ATOM 5230 CE2 PHE D 103 -4.043 31.555 26.554 1.00 25.91 C ANISOU 5230 CE2 PHE D 103 3155 4116 2572 -53 280 25 C ATOM 5231 CZ PHE D 103 -4.411 32.780 26.025 1.00 25.95 C ANISOU 5231 CZ PHE D 103 3240 4086 2535 2 237 124 C ATOM 5232 N PHE D 104 -4.762 32.963 33.313 1.00 15.01 N ANISOU 5232 N PHE D 104 1687 2364 1653 -91 415 -105 N ATOM 5233 CA PHE D 104 -5.139 32.863 34.724 1.00 14.36 C ANISOU 5233 CA PHE D 104 1596 2237 1624 -106 451 -163 C ATOM 5234 C PHE D 104 -6.542 33.355 35.010 1.00 19.36 C ANISOU 5234 C PHE D 104 2197 2852 2307 -16 454 -187 C ATOM 5235 O PHE D 104 -6.990 34.311 34.382 1.00 18.85 O ANISOU 5235 O PHE D 104 2157 2757 2247 66 427 -140 O ATOM 5236 CB PHE D 104 -4.163 33.688 35.590 1.00 16.19 C ANISOU 5236 CB PHE D 104 1919 2372 1859 -169 483 -146 C ATOM 5237 CG PHE D 104 -2.819 33.035 35.795 1.00 17.15 C ANISOU 5237 CG PHE D 104 2036 2521 1960 -264 484 -143 C ATOM 5238 CD1 PHE D 104 -2.541 32.327 36.964 1.00 18.35 C ANISOU 5238 CD1 PHE D 104 2179 2672 2122 -316 492 -188 C ATOM 5239 CD2 PHE D 104 -1.836 33.105 34.813 1.00 17.40 C ANISOU 5239 CD2 PHE D 104 2066 2585 1961 -296 478 -91 C ATOM 5240 CE1 PHE D 104 -1.289 31.724 37.159 1.00 17.95 C ANISOU 5240 CE1 PHE D 104 2108 2648 2062 -384 477 -178 C ATOM 5241 CE2 PHE D 104 -0.579 32.511 35.013 1.00 19.30 C ANISOU 5241 CE2 PHE D 104 2273 2859 2201 -370 482 -91 C ATOM 5242 CZ PHE D 104 -0.324 31.811 36.180 1.00 16.69 C ANISOU 5242 CZ PHE D 104 1923 2526 1892 -405 473 -134 C ATOM 5243 N GLY D 105 -7.164 32.746 36.025 1.00 17.50 N ANISOU 5243 N GLY D 105 1912 2628 2108 -30 495 -255 N ATOM 5244 CA GLY D 105 -8.435 33.156 36.626 1.00 18.25 C ANISOU 5244 CA GLY D 105 1963 2707 2264 43 533 -296 C ATOM 5245 C GLY D 105 -8.192 34.419 37.449 1.00 22.33 C ANISOU 5245 C GLY D 105 2593 3099 2792 63 584 -293 C ATOM 5246 O GLY D 105 -7.050 34.822 37.635 1.00 19.11 O ANISOU 5246 O GLY D 105 2288 2628 2345 -4 581 -264 O ATOM 5247 N GLU D 106 -9.236 35.026 38.001 1.00 21.20 N ANISOU 5247 N GLU D 106 2430 2919 2705 149 636 -331 N ATOM 5248 CA GLU D 106 -9.120 36.303 38.725 1.00 22.88 C ANISOU 5248 CA GLU D 106 2768 2995 2932 184 691 -340 C ATOM 5249 C GLU D 106 -8.399 36.222 40.090 1.00 26.76 C ANISOU 5249 C GLU D 106 3366 3426 3375 72 754 -393 C ATOM 5250 O GLU D 106 -7.994 37.257 40.630 1.00 26.87 O ANISOU 5250 O GLU D 106 3514 3318 3377 64 784 -403 O ATOM 5251 CB GLU D 106 -10.538 36.890 38.950 1.00 26.54 C ANISOU 5251 CB GLU D 106 3164 3442 3479 329 744 -380 C ATOM 5252 CG GLU D 106 -11.430 36.855 37.712 1.00 43.16 C ANISOU 5252 CG GLU D 106 5133 5630 5634 448 663 -334 C ATOM 5253 CD GLU D 106 -12.395 35.679 37.585 1.00 64.22 C ANISOU 5253 CD GLU D 106 7608 8451 8339 443 656 -380 C ATOM 5254 OE1 GLU D 106 -11.943 34.513 37.667 1.00 29.49 O ANISOU 5254 OE1 GLU D 106 3187 4124 3894 317 649 -399 O ATOM 5255 OE2 GLU D 106 -13.595 35.929 37.323 1.00 61.27 O ANISOU 5255 OE2 GLU D 106 7104 8126 8050 566 647 -393 O ATOM 5256 N GLY D 107 -8.290 35.017 40.646 1.00 22.52 N ANISOU 5256 N GLY D 107 2782 2967 2806 -13 769 -427 N ATOM 5257 CA GLY D 107 -7.742 34.800 41.978 1.00 22.15 C ANISOU 5257 CA GLY D 107 2834 2883 2701 -113 816 -472 C ATOM 5258 C GLY D 107 -8.859 34.726 43.011 1.00 28.35 C ANISOU 5258 C GLY D 107 3607 3666 3498 -82 929 -550 C ATOM 5259 O GLY D 107 -9.895 35.383 42.870 1.00 27.39 O ANISOU 5259 O GLY D 107 3436 3526 3444 32 983 -577 O ATOM 5260 N SER D 108 -8.665 33.890 44.030 1.00 20.17 N ANISOU 5260 N SER D 108 2887 2422 2354 -52 1164 -904 N ATOM 5261 CA SER D 108 -9.579 33.675 45.136 1.00 21.00 C ANISOU 5261 CA SER D 108 2935 2650 2393 -123 1210 -970 C ATOM 5262 C SER D 108 -8.821 33.893 46.406 1.00 25.89 C ANISOU 5262 C SER D 108 3660 3162 3014 -139 1214 -961 C ATOM 5263 O SER D 108 -7.875 33.154 46.690 1.00 24.82 O ANISOU 5263 O SER D 108 3629 2913 2890 -214 1192 -906 O ATOM 5264 CB SER D 108 -10.169 32.263 45.112 1.00 24.07 C ANISOU 5264 CB SER D 108 3286 3124 2735 -287 1262 -1003 C ATOM 5265 OG SER D 108 -10.909 32.001 43.934 1.00 30.99 O ANISOU 5265 OG SER D 108 4042 4132 3601 -285 1243 -1053 O ATOM 5266 N ARG D 109 -9.209 34.905 47.168 1.00 24.21 N ANISOU 5266 N ARG D 109 3414 2988 2796 -68 1242 -1016 N ATOM 5267 CA ARG D 109 -8.551 35.157 48.435 1.00 24.36 C ANISOU 5267 CA ARG D 109 3529 2941 2785 -85 1236 -1039 C ATOM 5268 C ARG D 109 -9.228 34.331 49.541 1.00 29.38 C ANISOU 5268 C ARG D 109 4213 3662 3287 -204 1300 -1061 C ATOM 5269 O ARG D 109 -10.400 34.551 49.858 1.00 29.30 O ANISOU 5269 O ARG D 109 4130 3752 3249 -220 1389 -1125 O ATOM 5270 CB ARG D 109 -8.561 36.653 48.764 1.00 26.41 C ANISOU 5270 CB ARG D 109 3734 3186 3114 32 1271 -1110 C ATOM 5271 CG ARG D 109 -7.682 37.003 49.951 1.00 41.05 C ANISOU 5271 CG ARG D 109 5677 4974 4947 21 1242 -1169 C ATOM 5272 CD ARG D 109 -7.296 38.462 49.925 1.00 56.51 C ANISOU 5272 CD ARG D 109 7563 6861 7048 142 1291 -1251 C ATOM 5273 NE ARG D 109 -6.173 38.720 50.822 1.00 72.70 N ANISOU 5273 NE ARG D 109 9681 8831 9111 137 1230 -1336 N ATOM 5274 CZ ARG D 109 -5.757 39.931 51.175 1.00 94.36 C ANISOU 5274 CZ ARG D 109 12359 11517 11976 210 1291 -1463 C ATOM 5275 NH1 ARG D 109 -6.382 41.014 50.726 1.00 81.11 N ANISOU 5275 NH1 ARG D 109 10555 9838 10424 300 1443 -1493 N ATOM 5276 NH2 ARG D 109 -4.715 40.070 51.981 1.00 87.29 N ANISOU 5276 NH2 ARG D 109 11509 10568 11091 200 1210 -1570 N ATOM 5277 N LEU D 110 -8.483 33.401 50.142 1.00 24.85 N ANISOU 5277 N LEU D 110 3766 3030 2647 -276 1272 -1000 N ATOM 5278 CA LEU D 110 -9.035 32.607 51.225 1.00 26.08 C ANISOU 5278 CA LEU D 110 4002 3242 2665 -362 1365 -997 C ATOM 5279 C LEU D 110 -8.319 32.926 52.556 1.00 30.39 C ANISOU 5279 C LEU D 110 4689 3768 3088 -337 1311 -1002 C ATOM 5280 O LEU D 110 -7.094 32.923 52.610 1.00 29.03 O ANISOU 5280 O LEU D 110 4576 3515 2940 -302 1184 -957 O ATOM 5281 CB LEU D 110 -8.956 31.106 50.888 1.00 26.46 C ANISOU 5281 CB LEU D 110 4079 3262 2714 -460 1423 -910 C ATOM 5282 CG LEU D 110 -9.336 30.132 52.027 1.00 33.00 C ANISOU 5282 CG LEU D 110 5021 4105 3411 -528 1560 -873 C ATOM 5283 CD1 LEU D 110 -10.825 30.217 52.389 1.00 34.97 C ANISOU 5283 CD1 LEU D 110 5211 4437 3638 -562 1730 -984 C ATOM 5284 CD2 LEU D 110 -8.973 28.724 51.672 1.00 31.61 C ANISOU 5284 CD2 LEU D 110 4865 3865 3278 -611 1636 -767 C ATOM 5285 N THR D 111 -9.102 33.234 53.611 1.00 25.84 N ANISOU 5285 N THR D 111 4163 3266 2391 -355 1407 -1072 N ATOM 5286 CA THR D 111 -8.585 33.453 54.953 1.00 27.69 C ANISOU 5286 CA THR D 111 4549 3518 2454 -340 1367 -1092 C ATOM 5287 C THR D 111 -9.150 32.367 55.846 1.00 31.76 C ANISOU 5287 C THR D 111 5213 4060 2795 -401 1503 -1029 C ATOM 5288 O THR D 111 -10.372 32.289 56.013 1.00 33.16 O ANISOU 5288 O THR D 111 5366 4262 2972 -451 1684 -1084 O ATOM 5289 CB THR D 111 -8.918 34.874 55.485 1.00 35.36 C ANISOU 5289 CB THR D 111 5474 4532 3428 -309 1395 -1241 C ATOM 5290 OG1 THR D 111 -8.368 35.839 54.597 1.00 39.53 O ANISOU 5290 OG1 THR D 111 5863 5009 4148 -234 1315 -1287 O ATOM 5291 CG2 THR D 111 -8.356 35.122 56.873 1.00 37.00 C ANISOU 5291 CG2 THR D 111 5840 4783 3435 -303 1341 -1294 C ATOM 5292 N VAL D 112 -8.271 31.535 56.418 1.00 27.15 N ANISOU 5292 N VAL D 112 4779 3456 2082 -385 1433 -911 N ATOM 5293 CA VAL D 112 -8.697 30.464 57.331 1.00 27.83 C ANISOU 5293 CA VAL D 112 5037 3551 1987 -411 1591 -819 C ATOM 5294 C VAL D 112 -8.351 30.888 58.756 1.00 35.75 C ANISOU 5294 C VAL D 112 6233 4622 2727 -357 1531 -843 C ATOM 5295 O VAL D 112 -7.176 31.093 59.071 1.00 35.52 O ANISOU 5295 O VAL D 112 6253 4616 2625 -291 1314 -817 O ATOM 5296 CB VAL D 112 -8.116 29.066 56.992 1.00 29.35 C ANISOU 5296 CB VAL D 112 5267 3673 2213 -423 1613 -638 C ATOM 5297 CG1 VAL D 112 -8.715 28.006 57.923 1.00 30.65 C ANISOU 5297 CG1 VAL D 112 5604 3829 2214 -433 1849 -544 C ATOM 5298 CG2 VAL D 112 -8.366 28.705 55.530 1.00 25.86 C ANISOU 5298 CG2 VAL D 112 4628 3176 2022 -491 1658 -644 C ATOM 5299 N LEU D 113 -9.365 30.967 59.623 1.00 36.24 N ANISOU 5299 N LEU D 113 6409 4711 2649 -388 1727 -903 N ATOM 5300 CA LEU D 113 -9.196 31.426 60.999 1.00 40.01 C ANISOU 5300 CA LEU D 113 7090 5266 2847 -351 1701 -950 C ATOM 5301 C LEU D 113 -9.626 30.380 62.026 1.00 47.46 C ANISOU 5301 C LEU D 113 8293 6194 3546 -333 1902 -829 C ATOM 5302 O LEU D 113 -10.669 29.739 61.860 1.00 45.66 O ANISOU 5302 O LEU D 113 8064 5879 3406 -388 2176 -812 O ATOM 5303 CB LEU D 113 -10.045 32.695 61.206 1.00 40.70 C ANISOU 5303 CB LEU D 113 7103 5374 2986 -409 1796 -1153 C ATOM 5304 CG LEU D 113 -9.457 34.107 60.993 1.00 45.97 C ANISOU 5304 CG LEU D 113 7622 6091 3753 -393 1621 -1309 C ATOM 5305 CD1 LEU D 113 -8.036 34.117 60.466 1.00 46.79 C ANISOU 5305 CD1 LEU D 113 7653 6200 3926 -316 1348 -1265 C ATOM 5306 CD2 LEU D 113 -10.388 34.968 60.187 1.00 45.49 C ANISOU 5306 CD2 LEU D 113 7341 5986 3958 -445 1746 -1421 C ATOM 5307 N GLU D 114 -8.854 30.253 63.115 1.00 48.59 N ANISOU 5307 N GLU D 114 8659 6422 3383 -245 1778 -760 N ATOM 5308 CA GLU D 114 -9.199 29.347 64.212 1.00 53.21 C ANISOU 5308 CA GLU D 114 9536 6997 3683 -192 1976 -628 C ATOM 5309 C GLU D 114 -10.495 29.808 64.895 1.00 59.31 C ANISOU 5309 C GLU D 114 10422 7729 4385 -267 2262 -768 C ATOM 5310 O GLU D 114 -11.282 28.968 65.327 1.00 61.34 O ANISOU 5310 O GLU D 114 10842 7885 4581 -266 2569 -689 O ATOM 5311 CB GLU D 114 -8.061 29.258 65.237 1.00 57.66 C ANISOU 5311 CB GLU D 114 10312 7695 3900 -61 1735 -534 C ATOM 5312 CG GLU D 114 -7.732 27.827 65.631 1.00 73.44 C ANISOU 5312 CG GLU D 114 12505 9659 5741 51 1826 -255 C ATOM 5313 CD GLU D 114 -6.734 27.123 64.730 1.00 91.45 C ANISOU 5313 CD GLU D 114 14622 11896 8231 87 1656 -93 C ATOM 5314 OE1 GLU D 114 -5.559 27.554 64.693 1.00 91.54 O ANISOU 5314 OE1 GLU D 114 14564 11994 8224 146 1310 -109 O ATOM 5315 OE2 GLU D 114 -7.114 26.110 64.099 1.00 78.49 O ANISOU 5315 OE2 GLU D 114 12920 10120 6782 51 1888 38 O ATOM 5316 N ASP D 115 -10.732 31.140 64.925 1.00 55.03 N ANISOU 5316 N ASP D 115 9773 7236 3900 -336 2195 -983 N ATOM 5317 CA ASP D 115 -11.899 31.782 65.533 1.00 56.94 C ANISOU 5317 CA ASP D 115 10087 7424 4123 -429 2452 -1141 C ATOM 5318 C ASP D 115 -12.352 32.994 64.707 1.00 58.41 C ANISOU 5318 C ASP D 115 9973 7595 4627 -525 2429 -1332 C ATOM 5319 O ASP D 115 -11.543 33.873 64.415 1.00 57.23 O ANISOU 5319 O ASP D 115 9682 7536 4524 -507 2186 -1413 O ATOM 5320 CB ASP D 115 -11.557 32.214 66.981 1.00 62.05 C ANISOU 5320 CB ASP D 115 11025 8183 4370 -393 2411 -1192 C ATOM 5321 CG ASP D 115 -12.677 32.855 67.786 1.00 83.65 C ANISOU 5321 CG ASP D 115 13889 10847 7047 -501 2701 -1353 C ATOM 5322 OD1 ASP D 115 -13.866 32.566 67.498 1.00 85.67 O ANISOU 5322 OD1 ASP D 115 14100 10928 7523 -578 3012 -1373 O ATOM 5323 OD2 ASP D 115 -12.366 33.586 68.753 1.00 94.03 O ANISOU 5323 OD2 ASP D 115 15358 12273 8097 -510 2631 -1468 O ATOM 5324 N LEU D 116 -13.654 33.066 64.387 1.00 53.78 N ANISOU 5324 N LEU D 116 9286 6882 4266 -617 2701 -1409 N ATOM 5325 CA LEU D 116 -14.244 34.156 63.597 1.00 51.67 C ANISOU 5325 CA LEU D 116 8731 6590 4312 -690 2714 -1560 C ATOM 5326 C LEU D 116 -14.553 35.423 64.436 1.00 59.16 C ANISOU 5326 C LEU D 116 9722 7553 5205 -765 2799 -1737 C ATOM 5327 O LEU D 116 -15.041 36.407 63.874 1.00 58.46 O ANISOU 5327 O LEU D 116 9394 7435 5382 -819 2839 -1852 O ATOM 5328 CB LEU D 116 -15.535 33.675 62.908 1.00 50.42 C ANISOU 5328 CB LEU D 116 8423 6297 4437 -751 2954 -1580 C ATOM 5329 CG LEU D 116 -15.433 32.448 61.998 1.00 53.07 C ANISOU 5329 CG LEU D 116 8673 6609 4882 -712 2931 -1453 C ATOM 5330 CD1 LEU D 116 -16.809 31.979 61.574 1.00 53.45 C ANISOU 5330 CD1 LEU D 116 8592 6529 5188 -782 3205 -1530 C ATOM 5331 CD2 LEU D 116 -14.573 32.730 60.764 1.00 50.33 C ANISOU 5331 CD2 LEU D 116 8095 6353 4675 -661 2637 -1411 C ATOM 5332 N LYS D 117 -14.268 35.409 65.752 1.00 58.31 N ANISOU 5332 N LYS D 117 9911 7492 4754 -765 2835 -1757 N ATOM 5333 CA LYS D 117 -14.543 36.541 66.651 1.00 60.80 C ANISOU 5333 CA LYS D 117 10293 7822 4985 -858 2943 -1943 C ATOM 5334 C LYS D 117 -13.612 37.737 66.406 1.00 66.36 C ANISOU 5334 C LYS D 117 10805 8657 5751 -849 2705 -2072 C ATOM 5335 O LYS D 117 -13.967 38.855 66.767 1.00 67.02 O ANISOU 5335 O LYS D 117 10818 8729 5917 -947 2831 -2250 O ATOM 5336 CB LYS D 117 -14.444 36.105 68.117 1.00 65.80 C ANISOU 5336 CB LYS D 117 11327 8489 5187 -849 3038 -1926 C ATOM 5337 N ASN D 118 -12.438 37.505 65.795 1.00 62.93 N ANISOU 5337 N ASN D 118 10278 8323 5311 -737 2398 -1993 N ATOM 5338 CA ASN D 118 -11.447 38.543 65.506 1.00 62.52 C ANISOU 5338 CA ASN D 118 10036 8365 5353 -708 2184 -2124 C ATOM 5339 C ASN D 118 -11.695 39.244 64.138 1.00 62.94 C ANISOU 5339 C ASN D 118 9744 8337 5836 -706 2204 -2146 C ATOM 5340 O ASN D 118 -10.900 40.106 63.759 1.00 62.59 O ANISOU 5340 O ASN D 118 9524 8329 5928 -668 2074 -2248 O ATOM 5341 CB ASN D 118 -10.015 37.953 65.572 1.00 65.16 C ANISOU 5341 CB ASN D 118 10448 8818 5494 -583 1853 -2040 C ATOM 5342 CG ASN D 118 -9.715 36.816 64.617 1.00 93.85 C ANISOU 5342 CG ASN D 118 14039 12396 9225 -498 1742 -1816 C ATOM 5343 OD1 ASN D 118 -10.587 36.309 63.907 1.00 89.20 O ANISOU 5343 OD1 ASN D 118 13380 11698 8815 -528 1904 -1719 O ATOM 5344 ND2 ASN D 118 -8.459 36.387 64.576 1.00 87.46 N ANISOU 5344 ND2 ASN D 118 13257 11657 8319 -397 1466 -1744 N ATOM 5345 N VAL D 119 -12.785 38.901 63.408 1.00 56.44 N ANISOU 5345 N VAL D 119 8818 7400 5226 -736 2374 -2063 N ATOM 5346 CA VAL D 119 -13.051 39.568 62.127 1.00 52.84 C ANISOU 5346 CA VAL D 119 8052 6892 5133 -708 2380 -2068 C ATOM 5347 C VAL D 119 -13.937 40.819 62.414 1.00 56.28 C ANISOU 5347 C VAL D 119 8359 7270 5754 -803 2625 -2225 C ATOM 5348 O VAL D 119 -14.880 40.772 63.217 1.00 54.91 O ANISOU 5348 O VAL D 119 8307 7035 5522 -911 2852 -2278 O ATOM 5349 CB VAL D 119 -13.517 38.669 60.917 1.00 54.75 C ANISOU 5349 CB VAL D 119 8180 7082 5541 -661 2355 -1913 C ATOM 5350 CG1 VAL D 119 -13.560 37.176 61.232 1.00 54.88 C ANISOU 5350 CG1 VAL D 119 8405 7091 5356 -661 2354 -1783 C ATOM 5351 CG2 VAL D 119 -14.772 39.160 60.205 1.00 53.43 C ANISOU 5351 CG2 VAL D 119 7791 6841 5669 -694 2533 -1944 C ATOM 5352 N PHE D 120 -13.527 41.962 61.834 1.00 52.69 N ANISOU 5352 N PHE D 120 7675 6820 5527 -761 2599 -2303 N ATOM 5353 CA PHE D 120 -14.177 43.260 62.038 1.00 53.29 C ANISOU 5353 CA PHE D 120 7591 6837 5820 -838 2841 -2444 C ATOM 5354 C PHE D 120 -14.330 44.031 60.722 1.00 53.35 C ANISOU 5354 C PHE D 120 7289 6793 6188 -740 2864 -2395 C ATOM 5355 O PHE D 120 -13.398 44.044 59.922 1.00 49.91 O ANISOU 5355 O PHE D 120 6774 6384 5804 -615 2679 -2341 O ATOM 5356 CB PHE D 120 -13.363 44.112 63.032 1.00 56.66 C ANISOU 5356 CB PHE D 120 8076 7330 6124 -893 2850 -2645 C ATOM 5357 CG PHE D 120 -13.404 43.669 64.478 1.00 61.24 C ANISOU 5357 CG PHE D 120 8961 7968 6339 -1001 2887 -2726 C ATOM 5358 CD1 PHE D 120 -12.526 42.700 64.952 1.00 65.51 C ANISOU 5358 CD1 PHE D 120 9736 8619 6535 -938 2642 -2664 C ATOM 5359 CD2 PHE D 120 -14.276 44.267 65.381 1.00 65.20 C ANISOU 5359 CD2 PHE D 120 9522 8409 6840 -1158 3178 -2861 C ATOM 5360 CE1 PHE D 120 -12.547 42.309 66.294 1.00 69.14 C ANISOU 5360 CE1 PHE D 120 10502 9147 6622 -1007 2676 -2721 C ATOM 5361 CE2 PHE D 120 -14.288 43.885 66.727 1.00 70.94 C ANISOU 5361 CE2 PHE D 120 10565 9189 7198 -1249 3224 -2937 C ATOM 5362 CZ PHE D 120 -13.424 42.908 67.173 1.00 70.04 C ANISOU 5362 CZ PHE D 120 10697 9205 6711 -1160 2967 -2861 C ATOM 5363 N PRO D 121 -15.471 44.717 60.489 1.00 50.27 N ANISOU 5363 N PRO D 121 6724 6318 6058 -783 3100 -2409 N ATOM 5364 CA PRO D 121 -15.587 45.531 59.265 1.00 48.50 C ANISOU 5364 CA PRO D 121 6213 6058 6157 -657 3129 -2343 C ATOM 5365 C PRO D 121 -14.819 46.857 59.443 1.00 52.65 C ANISOU 5365 C PRO D 121 6613 6566 6825 -636 3235 -2478 C ATOM 5366 O PRO D 121 -14.475 47.203 60.579 1.00 53.86 O ANISOU 5366 O PRO D 121 6874 6739 6851 -756 3316 -2653 O ATOM 5367 CB PRO D 121 -17.102 45.743 59.144 1.00 50.92 C ANISOU 5367 CB PRO D 121 6386 6281 6678 -718 3348 -2317 C ATOM 5368 CG PRO D 121 -17.585 45.763 60.563 1.00 56.25 C ANISOU 5368 CG PRO D 121 7237 6904 7231 -913 3550 -2458 C ATOM 5369 CD PRO D 121 -16.664 44.867 61.357 1.00 52.41 C ANISOU 5369 CD PRO D 121 7051 6505 6358 -942 3371 -2487 C ATOM 5370 N PRO D 122 -14.517 47.637 58.391 1.00 48.39 N ANISOU 5370 N PRO D 122 5851 5986 6547 -485 3260 -2422 N ATOM 5371 CA PRO D 122 -13.788 48.885 58.629 1.00 48.58 C ANISOU 5371 CA PRO D 122 5748 5968 6741 -470 3417 -2580 C ATOM 5372 C PRO D 122 -14.689 50.016 59.099 1.00 53.66 C ANISOU 5372 C PRO D 122 6228 6530 7631 -573 3777 -2674 C ATOM 5373 O PRO D 122 -15.909 49.963 58.935 1.00 51.49 O ANISOU 5373 O PRO D 122 5885 6211 7469 -609 3897 -2577 O ATOM 5374 CB PRO D 122 -13.232 49.214 57.247 1.00 49.21 C ANISOU 5374 CB PRO D 122 5669 6001 7026 -249 3355 -2453 C ATOM 5375 CG PRO D 122 -14.277 48.712 56.320 1.00 53.25 C ANISOU 5375 CG PRO D 122 6121 6522 7589 -173 3308 -2239 C ATOM 5376 CD PRO D 122 -14.813 47.458 56.954 1.00 48.79 C ANISOU 5376 CD PRO D 122 5760 6028 6751 -313 3171 -2225 C ATOM 5377 N GLU D 123 -14.055 51.046 59.661 1.00 46.33 N ANISOU 5377 N GLU D 123 7068 4722 5814 64 2915 -2266 N ATOM 5378 CA GLU D 123 -14.631 52.337 59.976 1.00 49.11 C ANISOU 5378 CA GLU D 123 7437 4911 6313 114 3221 -2370 C ATOM 5379 C GLU D 123 -14.068 53.234 58.901 1.00 52.62 C ANISOU 5379 C GLU D 123 7684 5393 6917 276 3009 -2291 C ATOM 5380 O GLU D 123 -12.902 53.043 58.519 1.00 50.43 O ANISOU 5380 O GLU D 123 7462 5215 6483 251 2683 -2213 O ATOM 5381 CB GLU D 123 -14.277 52.795 61.395 1.00 52.94 C ANISOU 5381 CB GLU D 123 8392 5236 6485 -95 3424 -2509 C ATOM 5382 CG GLU D 123 -15.101 52.098 62.463 1.00 68.63 C ANISOU 5382 CG GLU D 123 10580 7147 8348 -246 3745 -2597 C ATOM 5383 CD GLU D 123 -14.469 52.115 63.839 1.00 94.77 C ANISOU 5383 CD GLU D 123 14434 10373 11200 -519 3803 -2686 C ATOM 5384 OE1 GLU D 123 -15.051 52.750 64.747 1.00 83.39 O ANISOU 5384 OE1 GLU D 123 13250 8743 9692 -627 4220 -2856 O ATOM 5385 OE2 GLU D 123 -13.394 51.494 64.012 1.00 93.97 O ANISOU 5385 OE2 GLU D 123 14505 10389 10809 -631 3437 -2579 O ATOM 5386 N VAL D 124 -14.889 54.126 58.322 1.00 50.07 N ANISOU 5386 N VAL D 124 7093 4998 6932 452 3181 -2277 N ATOM 5387 CA VAL D 124 -14.407 54.974 57.223 1.00 48.51 C ANISOU 5387 CA VAL D 124 6709 4833 6890 613 2981 -2169 C ATOM 5388 C VAL D 124 -14.623 56.444 57.576 1.00 55.08 C ANISOU 5388 C VAL D 124 7619 5427 7882 677 3271 -2241 C ATOM 5389 O VAL D 124 -15.719 56.828 57.986 1.00 56.02 O ANISOU 5389 O VAL D 124 7657 5395 8233 738 3633 -2302 O ATOM 5390 CB VAL D 124 -15.063 54.597 55.859 1.00 50.46 C ANISOU 5390 CB VAL D 124 6523 5250 7399 784 2805 -2012 C ATOM 5391 CG1 VAL D 124 -14.574 55.498 54.729 1.00 49.25 C ANISOU 5391 CG1 VAL D 124 6218 5126 7369 938 2611 -1879 C ATOM 5392 CG2 VAL D 124 -14.812 53.133 55.508 1.00 48.06 C ANISOU 5392 CG2 VAL D 124 6186 5145 6930 695 2556 -1974 C ATOM 5393 N ALA D 125 -13.570 57.261 57.399 1.00 51.89 N ANISOU 5393 N ALA D 125 7362 4971 7383 661 3135 -2234 N ATOM 5394 CA ALA D 125 -13.611 58.708 57.626 1.00 53.65 C ANISOU 5394 CA ALA D 125 7682 4943 7758 712 3394 -2302 C ATOM 5395 C ALA D 125 -12.946 59.445 56.461 1.00 56.39 C ANISOU 5395 C ALA D 125 7866 5322 8238 853 3159 -2149 C ATOM 5396 O ALA D 125 -11.925 58.983 55.937 1.00 51.58 O ANISOU 5396 O ALA D 125 7265 4886 7446 800 2812 -2071 O ATOM 5397 CB ALA D 125 -12.920 59.059 58.936 1.00 55.75 C ANISOU 5397 CB ALA D 125 8427 5055 7701 451 3533 -2506 C ATOM 5398 N VAL D 126 -13.548 60.568 56.036 1.00 55.70 N ANISOU 5398 N VAL D 126 7618 5054 8492 1043 3369 -2088 N ATOM 5399 CA VAL D 126 -13.019 61.411 54.959 1.00 55.29 C ANISOU 5399 CA VAL D 126 7435 4989 8586 1185 3203 -1925 C ATOM 5400 C VAL D 126 -12.482 62.681 55.612 1.00 60.05 C ANISOU 5400 C VAL D 126 8337 5293 9188 1101 3445 -2064 C ATOM 5401 O VAL D 126 -13.204 63.340 56.368 1.00 61.56 O ANISOU 5401 O VAL D 126 8630 5219 9540 1116 3855 -2192 O ATOM 5402 CB VAL D 126 -14.064 61.697 53.836 1.00 60.82 C ANISOU 5402 CB VAL D 126 7707 5722 9679 1469 3195 -1691 C ATOM 5403 CG1 VAL D 126 -13.674 62.901 52.976 1.00 61.51 C ANISOU 5403 CG1 VAL D 126 7731 5687 9954 1620 3156 -1530 C ATOM 5404 CG2 VAL D 126 -14.264 60.472 52.960 1.00 58.83 C ANISOU 5404 CG2 VAL D 126 7203 5800 9350 1492 2852 -1554 C ATOM 5405 N PHE D 127 -11.205 62.998 55.346 1.00 54.57 N ANISOU 5405 N PHE D 127 7789 4627 8316 993 3217 -2052 N ATOM 5406 CA PHE D 127 -10.558 64.186 55.901 1.00 56.29 C ANISOU 5406 CA PHE D 127 8301 4575 8512 866 3400 -2190 C ATOM 5407 C PHE D 127 -10.522 65.278 54.834 1.00 60.18 C ANISOU 5407 C PHE D 127 8614 4933 9319 1079 3425 -2007 C ATOM 5408 O PHE D 127 -10.038 65.061 53.727 1.00 57.35 O ANISOU 5408 O PHE D 127 8061 4763 8968 1170 3120 -1807 O ATOM 5409 CB PHE D 127 -9.160 63.837 56.437 1.00 56.44 C ANISOU 5409 CB PHE D 127 8598 4702 8146 568 3135 -2297 C ATOM 5410 CG PHE D 127 -9.221 62.878 57.604 1.00 56.94 C ANISOU 5410 CG PHE D 127 8887 4856 7891 349 3132 -2455 C ATOM 5411 CD1 PHE D 127 -9.249 63.348 58.909 1.00 61.14 C ANISOU 5411 CD1 PHE D 127 9812 5181 8239 112 3401 -2699 C ATOM 5412 CD2 PHE D 127 -9.272 61.501 57.395 1.00 55.90 C ANISOU 5412 CD2 PHE D 127 8604 5003 7631 367 2879 -2358 C ATOM 5413 CE1 PHE D 127 -9.342 62.465 59.986 1.00 62.17 C ANISOU 5413 CE1 PHE D 127 10183 5396 8044 -100 3402 -2821 C ATOM 5414 CE2 PHE D 127 -9.367 60.618 58.473 1.00 58.62 C ANISOU 5414 CE2 PHE D 127 9168 5413 7692 174 2890 -2474 C ATOM 5415 CZ PHE D 127 -9.397 61.107 59.764 1.00 59.01 C ANISOU 5415 CZ PHE D 127 9611 5270 7539 -59 3141 -2694 C ATOM 5416 N GLU D 128 -11.106 66.424 55.160 1.00 60.37 N ANISOU 5416 N GLU D 128 8709 4616 9614 1165 3820 -2068 N ATOM 5417 CA GLU D 128 -11.247 67.577 54.273 1.00 61.59 C ANISOU 5417 CA GLU D 128 8708 4569 10122 1390 3922 -1880 C ATOM 5418 C GLU D 128 -9.914 68.268 53.941 1.00 64.12 C ANISOU 5418 C GLU D 128 9207 4827 10327 1254 3774 -1876 C ATOM 5419 O GLU D 128 -9.034 68.332 54.801 1.00 62.76 O ANISOU 5419 O GLU D 128 9361 4605 9880 956 3769 -2105 O ATOM 5420 CB GLU D 128 -12.204 68.593 54.899 1.00 66.93 C ANISOU 5420 CB GLU D 128 9448 4839 11142 1502 4454 -1977 C ATOM 5421 CG GLU D 128 -13.652 68.144 54.832 1.00 77.52 C ANISOU 5421 CG GLU D 128 10463 6216 12776 1737 4613 -1871 C ATOM 5422 CD GLU D 128 -14.688 69.219 55.092 1.00 91.70 C ANISOU 5422 CD GLU D 128 12178 7599 15063 1955 5134 -1860 C ATOM 5423 OE1 GLU D 128 -14.302 70.375 55.380 1.00 80.80 O ANISOU 5423 OE1 GLU D 128 11048 5862 13789 1917 5422 -1962 O ATOM 5424 OE2 GLU D 128 -15.894 68.902 54.990 1.00 86.53 O ANISOU 5424 OE2 GLU D 128 11192 6966 14718 2163 5266 -1742 O ATOM 5425 N PRO D 129 -9.780 68.848 52.718 1.00 61.28 N ANISOU 5425 N PRO D 129 8643 4455 10186 1455 3663 -1608 N ATOM 5426 CA PRO D 129 -8.525 69.523 52.351 1.00 60.92 C ANISOU 5426 CA PRO D 129 8748 4335 10063 1324 3554 -1592 C ATOM 5427 C PRO D 129 -8.178 70.727 53.216 1.00 66.82 C ANISOU 5427 C PRO D 129 9828 4680 10878 1156 3902 -1817 C ATOM 5428 O PRO D 129 -9.059 71.453 53.685 1.00 69.44 O ANISOU 5428 O PRO D 129 10219 4693 11471 1265 4307 -1888 O ATOM 5429 CB PRO D 129 -8.767 69.970 50.908 1.00 63.09 C ANISOU 5429 CB PRO D 129 8748 4630 10594 1608 3454 -1240 C ATOM 5430 CG PRO D 129 -9.847 69.095 50.408 1.00 66.86 C ANISOU 5430 CG PRO D 129 8912 5352 11140 1817 3319 -1070 C ATOM 5431 CD PRO D 129 -10.726 68.848 51.584 1.00 63.49 C ANISOU 5431 CD PRO D 129 8544 4816 10764 1786 3595 -1288 C ATOM 5432 N SER D 130 -6.870 70.927 53.402 1.00 62.15 N ANISOU 5432 N SER D 130 9447 4100 10069 879 3750 -1928 N ATOM 5433 CA SER D 130 -6.282 72.019 54.169 1.00 64.79 C ANISOU 5433 CA SER D 130 10127 4088 10401 631 4003 -2161 C ATOM 5434 C SER D 130 -6.452 73.351 53.422 1.00 70.45 C ANISOU 5434 C SER D 130 10801 4459 11509 831 4263 -1998 C ATOM 5435 O SER D 130 -6.193 73.414 52.217 1.00 69.21 O ANISOU 5435 O SER D 130 10413 4415 11468 1008 4067 -1707 O ATOM 5436 CB SER D 130 -4.800 71.733 54.414 1.00 66.67 C ANISOU 5436 CB SER D 130 10509 4500 10321 282 3678 -2265 C ATOM 5437 OG SER D 130 -4.194 72.715 55.239 1.00 79.77 O ANISOU 5437 OG SER D 130 12523 5855 11931 -27 3878 -2518 O ATOM 5438 N GLU D 131 -6.878 74.410 54.134 1.00 69.43 N ANISOU 5438 N GLU D 131 10917 3888 11575 794 4724 -2183 N ATOM 5439 CA GLU D 131 -7.033 75.749 53.556 1.00 71.88 C ANISOU 5439 CA GLU D 131 11227 3795 12287 973 5029 -2043 C ATOM 5440 C GLU D 131 -5.661 76.272 53.116 1.00 74.81 C ANISOU 5440 C GLU D 131 11712 4145 12567 752 4848 -2022 C ATOM 5441 O GLU D 131 -5.552 76.988 52.117 1.00 75.47 O ANISOU 5441 O GLU D 131 11671 4087 12917 942 4884 -1758 O ATOM 5442 CB GLU D 131 -7.698 76.714 54.561 1.00 77.45 C ANISOU 5442 CB GLU D 131 12224 3996 13206 933 5612 -2306 C ATOM 5443 N ALA D 132 -4.614 75.864 53.850 1.00 69.85 N ANISOU 5443 N ALA D 132 11301 3677 11564 347 4633 -2277 N ATOM 5444 CA ALA D 132 -3.219 76.189 53.575 1.00 69.45 C ANISOU 5444 CA ALA D 132 11324 3658 11405 77 4419 -2286 C ATOM 5445 C ALA D 132 -2.752 75.558 52.254 1.00 69.24 C ANISOU 5445 C ALA D 132 10948 3980 11380 261 4043 -1943 C ATOM 5446 O ALA D 132 -1.958 76.180 51.550 1.00 69.51 O ANISOU 5446 O ALA D 132 10961 3924 11527 217 4014 -1816 O ATOM 5447 CB ALA D 132 -2.351 75.704 54.714 1.00 70.19 C ANISOU 5447 CB ALA D 132 11665 3904 11102 -378 4217 -2599 C ATOM 5448 N GLU D 133 -3.255 74.343 51.910 1.00 61.45 N ANISOU 5448 N GLU D 133 9712 3369 10269 451 3790 -1803 N ATOM 5449 CA GLU D 133 -2.922 73.665 50.649 1.00 58.63 C ANISOU 5449 CA GLU D 133 9058 3337 9883 620 3470 -1502 C ATOM 5450 C GLU D 133 -3.564 74.401 49.468 1.00 64.35 C ANISOU 5450 C GLU D 133 9628 3901 10921 963 3616 -1177 C ATOM 5451 O GLU D 133 -2.902 74.626 48.452 1.00 62.62 O ANISOU 5451 O GLU D 133 9325 3732 10736 995 3503 -964 O ATOM 5452 CB GLU D 133 -3.361 72.188 50.671 1.00 56.62 C ANISOU 5452 CB GLU D 133 8619 3483 9410 703 3200 -1474 C ATOM 5453 CG GLU D 133 -2.909 71.404 49.445 1.00 62.84 C ANISOU 5453 CG GLU D 133 9157 4601 10119 817 2889 -1221 C ATOM 5454 CD GLU D 133 -3.656 70.128 49.092 1.00 77.05 C ANISOU 5454 CD GLU D 133 10746 6731 11798 992 2690 -1120 C ATOM 5455 OE1 GLU D 133 -4.572 69.725 49.847 1.00 61.97 O ANISOU 5455 OE1 GLU D 133 8850 4830 9867 1032 2771 -1240 O ATOM 5456 OE2 GLU D 133 -3.322 69.533 48.042 1.00 65.72 O ANISOU 5456 OE2 GLU D 133 9146 5536 10291 1072 2477 -929 O ATOM 5457 N ILE D 134 -4.846 74.788 49.624 1.00 63.79 N ANISOU 5457 N ILE D 134 9519 3628 11089 1212 3878 -1126 N ATOM 5458 CA ILE D 134 -5.641 75.493 48.619 1.00 65.86 C ANISOU 5458 CA ILE D 134 9611 3723 11690 1565 4010 -783 C ATOM 5459 C ILE D 134 -4.977 76.830 48.253 1.00 73.39 C ANISOU 5459 C ILE D 134 10727 4305 12854 1518 4225 -707 C ATOM 5460 O ILE D 134 -4.794 77.095 47.068 1.00 72.81 O ANISOU 5460 O ILE D 134 10531 4273 12862 1673 4117 -381 O ATOM 5461 CB ILE D 134 -7.106 75.665 49.113 1.00 70.85 C ANISOU 5461 CB ILE D 134 10158 4168 12592 1810 4289 -784 C ATOM 5462 CG1 ILE D 134 -7.833 74.300 49.126 1.00 68.17 C ANISOU 5462 CG1 ILE D 134 9584 4235 12082 1901 4033 -760 C ATOM 5463 CG2 ILE D 134 -7.880 76.697 48.275 1.00 74.03 C ANISOU 5463 CG2 ILE D 134 10413 4276 13439 2162 4495 -430 C ATOM 5464 CD1 ILE D 134 -8.885 74.126 50.228 1.00 75.64 C ANISOU 5464 CD1 ILE D 134 10551 5053 13136 1939 4313 -971 C ATOM 5465 N SER D 135 -4.591 77.648 49.249 1.00 73.79 N ANISOU 5465 N SER D 135 11077 3996 12965 1276 4527 -1010 N ATOM 5466 CA SER D 135 -3.966 78.946 48.974 1.00 77.27 C ANISOU 5466 CA SER D 135 11694 4041 13624 1199 4768 -968 C ATOM 5467 C SER D 135 -2.514 78.803 48.478 1.00 80.10 C ANISOU 5467 C SER D 135 12074 4588 13773 935 4501 -952 C ATOM 5468 O SER D 135 -2.035 79.687 47.770 1.00 81.96 O ANISOU 5468 O SER D 135 12352 4599 14191 952 4617 -776 O ATOM 5469 CB SER D 135 -4.020 79.855 50.200 1.00 84.67 C ANISOU 5469 CB SER D 135 12971 4518 14680 987 5194 -1328 C ATOM 5470 OG SER D 135 -3.374 79.283 51.325 1.00 94.45 O ANISOU 5470 OG SER D 135 14414 5914 15558 584 5070 -1719 O ATOM 5471 N HIS D 136 -1.831 77.696 48.811 1.00 73.42 N ANISOU 5471 N HIS D 136 11178 4137 12579 708 4163 -1108 N ATOM 5472 CA HIS D 136 -0.438 77.501 48.403 1.00 72.01 C ANISOU 5472 CA HIS D 136 10975 4136 12251 460 3929 -1095 C ATOM 5473 C HIS D 136 -0.277 76.827 47.038 1.00 72.32 C ANISOU 5473 C HIS D 136 10752 4502 12225 667 3673 -755 C ATOM 5474 O HIS D 136 0.654 77.179 46.317 1.00 72.42 O ANISOU 5474 O HIS D 136 10751 4493 12272 575 3651 -628 O ATOM 5475 CB HIS D 136 0.328 76.687 49.457 1.00 71.35 C ANISOU 5475 CB HIS D 136 10957 4287 11864 100 3693 -1408 C ATOM 5476 CG HIS D 136 1.817 76.751 49.325 1.00 74.96 C ANISOU 5476 CG HIS D 136 11404 4819 12258 -216 3522 -1448 C ATOM 5477 ND1 HIS D 136 2.567 75.615 49.089 1.00 74.20 N ANISOU 5477 ND1 HIS D 136 11100 5125 11966 -295 3168 -1398 N ATOM 5478 CD2 HIS D 136 2.649 77.815 49.408 1.00 79.75 C ANISOU 5478 CD2 HIS D 136 12162 5130 13009 -467 3679 -1528 C ATOM 5479 CE1 HIS D 136 3.825 76.021 49.043 1.00 74.98 C ANISOU 5479 CE1 HIS D 136 11202 5172 12116 -580 3116 -1438 C ATOM 5480 NE2 HIS D 136 3.923 77.337 49.220 1.00 78.66 N ANISOU 5480 NE2 HIS D 136 11881 5231 12774 -705 3406 -1519 N ATOM 5481 N THR D 137 -1.140 75.850 46.697 1.00 66.30 N ANISOU 5481 N THR D 137 9800 4037 11353 910 3496 -625 N ATOM 5482 CA THR D 137 -1.002 75.072 45.457 1.00 63.98 C ANISOU 5482 CA THR D 137 9300 4081 10928 1059 3244 -348 C ATOM 5483 C THR D 137 -2.159 75.241 44.454 1.00 69.52 C ANISOU 5483 C THR D 137 9874 4787 11755 1427 3261 -1 C ATOM 5484 O THR D 137 -2.013 74.818 43.303 1.00 68.78 O ANISOU 5484 O THR D 137 9672 4923 11540 1523 3085 249 O ATOM 5485 CB THR D 137 -0.873 73.569 45.790 1.00 63.20 C ANISOU 5485 CB THR D 137 9079 4393 10541 979 2947 -483 C ATOM 5486 OG1 THR D 137 -2.062 73.121 46.444 1.00 61.67 O ANISOU 5486 OG1 THR D 137 8851 4244 10336 1112 2961 -569 O ATOM 5487 CG2 THR D 137 0.357 73.242 46.635 1.00 59.42 C ANISOU 5487 CG2 THR D 137 8670 3979 9927 627 2841 -748 C ATOM 5488 N GLN D 138 -3.309 75.809 44.893 1.00 68.15 N ANISOU 5488 N GLN D 138 9706 4371 11818 1620 3467 17 N ATOM 5489 CA GLN D 138 -4.545 75.978 44.099 1.00 69.28 C ANISOU 5489 CA GLN D 138 9674 4510 12138 1979 3461 362 C ATOM 5490 C GLN D 138 -5.146 74.587 43.787 1.00 69.25 C ANISOU 5490 C GLN D 138 9453 4960 11897 2067 3136 415 C ATOM 5491 O GLN D 138 -5.920 74.419 42.840 1.00 69.89 O ANISOU 5491 O GLN D 138 9361 5187 12006 2300 2986 734 O ATOM 5492 CB GLN D 138 -4.320 76.827 42.826 1.00 72.86 C ANISOU 5492 CB GLN D 138 10138 4830 12713 2116 3491 747 C ATOM 5493 CG GLN D 138 -4.425 78.338 43.051 1.00 91.86 C ANISOU 5493 CG GLN D 138 12695 6705 15503 2187 3872 808 C ATOM 5494 CD GLN D 138 -3.396 78.902 44.006 1.00112.57 C ANISOU 5494 CD GLN D 138 15570 9057 18144 1857 4101 443 C ATOM 5495 OE1 GLN D 138 -2.182 78.685 43.867 1.00105.28 O ANISOU 5495 OE1 GLN D 138 14721 8260 17020 1591 3990 337 O ATOM 5496 NE2 GLN D 138 -3.867 79.646 45.000 1.00107.50 N ANISOU 5496 NE2 GLN D 138 15061 8028 17755 1854 4436 241 N ATOM 5497 N LYS D 139 -4.792 73.604 44.631 1.00 61.70 N ANISOU 5497 N LYS D 139 8521 4214 10709 1862 3024 101 N ATOM 5498 CA LYS D 139 -5.241 72.215 44.585 1.00 58.16 C ANISOU 5498 CA LYS D 139 7910 4157 10032 1884 2758 67 C ATOM 5499 C LYS D 139 -5.751 71.808 45.964 1.00 61.70 C ANISOU 5499 C LYS D 139 8393 4569 10480 1807 2861 -239 C ATOM 5500 O LYS D 139 -5.336 72.385 46.976 1.00 62.14 O ANISOU 5500 O LYS D 139 8650 4373 10587 1634 3072 -487 O ATOM 5501 CB LYS D 139 -4.110 71.280 44.124 1.00 56.64 C ANISOU 5501 CB LYS D 139 7726 4269 9526 1695 2515 20 C ATOM 5502 CG LYS D 139 -3.749 71.428 42.653 1.00 64.90 C ANISOU 5502 CG LYS D 139 8739 5414 10504 1773 2412 326 C ATOM 5503 CD LYS D 139 -2.432 70.739 42.323 1.00 68.35 C ANISOU 5503 CD LYS D 139 9215 6044 10708 1562 2293 239 C ATOM 5504 CE LYS D 139 -1.911 71.125 40.957 1.00 78.69 C ANISOU 5504 CE LYS D 139 10564 7370 11965 1596 2292 512 C ATOM 5505 NZ LYS D 139 -2.629 70.412 39.864 1.00 88.32 N ANISOU 5505 NZ LYS D 139 11698 8869 12990 1738 2092 737 N ATOM 5506 N ALA D 140 -6.642 70.815 46.004 1.00 56.69 N ANISOU 5506 N ALA D 140 7586 4182 9771 1907 2717 -228 N ATOM 5507 CA ALA D 140 -7.226 70.328 47.247 1.00 55.68 C ANISOU 5507 CA ALA D 140 7487 4041 9627 1842 2825 -491 C ATOM 5508 C ALA D 140 -7.151 68.802 47.317 1.00 56.25 C ANISOU 5508 C ALA D 140 7475 4497 9402 1744 2547 -582 C ATOM 5509 O ALA D 140 -7.591 68.118 46.389 1.00 54.50 O ANISOU 5509 O ALA D 140 7058 4530 9118 1866 2332 -389 O ATOM 5510 CB ALA D 140 -8.665 70.794 47.344 1.00 58.68 C ANISOU 5510 CB ALA D 140 7710 4249 10335 2102 3030 -373 C ATOM 5511 N THR D 141 -6.581 68.272 48.412 1.00 51.84 N ANISOU 5511 N THR D 141 7077 3970 8648 1507 2547 -867 N ATOM 5512 CA THR D 141 -6.461 66.833 48.604 1.00 49.60 C ANISOU 5512 CA THR D 141 6737 4003 8106 1410 2314 -955 C ATOM 5513 C THR D 141 -7.393 66.359 49.698 1.00 54.25 C ANISOU 5513 C THR D 141 7349 4575 8691 1394 2442 -1131 C ATOM 5514 O THR D 141 -7.345 66.850 50.824 1.00 55.67 O ANISOU 5514 O THR D 141 7739 4539 8874 1262 2658 -1342 O ATOM 5515 CB THR D 141 -5.010 66.402 48.903 1.00 55.39 C ANISOU 5515 CB THR D 141 7599 4832 8613 1157 2155 -1082 C ATOM 5516 OG1 THR D 141 -4.130 67.013 47.966 1.00 52.93 O ANISOU 5516 OG1 THR D 141 7279 4481 8353 1158 2114 -934 O ATOM 5517 CG2 THR D 141 -4.826 64.878 48.851 1.00 52.43 C ANISOU 5517 CG2 THR D 141 7135 4773 8014 1102 1911 -1107 C ATOM 5518 N LEU D 142 -8.237 65.396 49.349 1.00 50.35 N ANISOU 5518 N LEU D 142 6656 4304 8173 1506 2321 -1051 N ATOM 5519 CA LEU D 142 -9.143 64.707 50.258 1.00 50.55 C ANISOU 5519 CA LEU D 142 6665 4363 8181 1487 2421 -1196 C ATOM 5520 C LEU D 142 -8.462 63.413 50.666 1.00 52.03 C ANISOU 5520 C LEU D 142 6933 4783 8053 1293 2207 -1322 C ATOM 5521 O LEU D 142 -7.896 62.740 49.802 1.00 49.69 O ANISOU 5521 O LEU D 142 6543 4700 7635 1291 1958 -1214 O ATOM 5522 CB LEU D 142 -10.484 64.417 49.567 1.00 51.68 C ANISOU 5522 CB LEU D 142 6501 4612 8524 1714 2398 -1009 C ATOM 5523 CG LEU D 142 -11.403 65.591 49.303 1.00 59.76 C ANISOU 5523 CG LEU D 142 7384 5394 9929 1944 2624 -851 C ATOM 5524 CD1 LEU D 142 -11.221 66.128 47.890 1.00 60.51 C ANISOU 5524 CD1 LEU D 142 7339 5542 10112 2096 2439 -544 C ATOM 5525 CD2 LEU D 142 -12.837 65.184 49.511 1.00 64.00 C ANISOU 5525 CD2 LEU D 142 7670 5967 10681 2079 2723 -812 C ATOM 5526 N VAL D 143 -8.462 63.076 51.959 1.00 49.10 N ANISOU 5526 N VAL D 143 6754 4356 7545 1124 2315 -1539 N ATOM 5527 CA VAL D 143 -7.824 61.835 52.402 1.00 47.08 C ANISOU 5527 CA VAL D 143 6574 4304 7010 951 2105 -1621 C ATOM 5528 C VAL D 143 -8.876 60.932 53.052 1.00 53.48 C ANISOU 5528 C VAL D 143 7355 5183 7780 953 2194 -1702 C ATOM 5529 O VAL D 143 -9.602 61.362 53.947 1.00 54.57 O ANISOU 5529 O VAL D 143 7607 5145 7984 932 2473 -1829 O ATOM 5530 CB VAL D 143 -6.591 62.079 53.321 1.00 50.02 C ANISOU 5530 CB VAL D 143 7219 4600 7186 695 2055 -1765 C ATOM 5531 CG1 VAL D 143 -6.220 60.833 54.129 1.00 48.40 C ANISOU 5531 CG1 VAL D 143 7115 4556 6718 523 1890 -1845 C ATOM 5532 CG2 VAL D 143 -5.394 62.562 52.505 1.00 49.02 C ANISOU 5532 CG2 VAL D 143 7048 4486 7090 675 1894 -1658 C ATOM 5533 N CYS D 144 -8.952 59.688 52.588 1.00 50.28 N ANISOU 5533 N CYS D 144 6811 5013 7279 968 1992 -1635 N ATOM 5534 CA CYS D 144 -9.853 58.705 53.157 1.00 51.90 C ANISOU 5534 CA CYS D 144 6986 5293 7439 943 2058 -1704 C ATOM 5535 C CYS D 144 -9.075 57.738 54.017 1.00 53.25 C ANISOU 5535 C CYS D 144 7362 5541 7330 740 1937 -1800 C ATOM 5536 O CYS D 144 -7.999 57.274 53.631 1.00 51.13 O ANISOU 5536 O CYS D 144 7097 5383 6947 686 1701 -1739 O ATOM 5537 CB CYS D 144 -10.629 57.971 52.077 1.00 53.32 C ANISOU 5537 CB CYS D 144 6874 5661 7725 1081 1935 -1568 C ATOM 5538 SG CYS D 144 -11.679 56.650 52.719 1.00 58.58 S ANISOU 5538 SG CYS D 144 7485 6422 8349 1019 2009 -1654 S ATOM 5539 N LEU D 145 -9.643 57.392 55.159 1.00 49.36 N ANISOU 5539 N LEU D 145 7028 4986 6742 634 2109 -1930 N ATOM 5540 CA LEU D 145 -9.004 56.480 56.084 1.00 48.64 C ANISOU 5540 CA LEU D 145 7154 4955 6370 436 1995 -1991 C ATOM 5541 C LEU D 145 -9.973 55.387 56.510 1.00 50.58 C ANISOU 5541 C LEU D 145 7376 5262 6581 421 2096 -2023 C ATOM 5542 O LEU D 145 -11.016 55.682 57.099 1.00 52.38 O ANISOU 5542 O LEU D 145 7642 5374 6886 426 2391 -2119 O ATOM 5543 CB LEU D 145 -8.502 57.282 57.296 1.00 50.99 C ANISOU 5543 CB LEU D 145 7794 5087 6493 235 2105 -2134 C ATOM 5544 CG LEU D 145 -7.367 56.696 58.119 1.00 56.63 C ANISOU 5544 CG LEU D 145 8742 5871 6903 4 1867 -2139 C ATOM 5545 CD1 LEU D 145 -6.058 56.704 57.351 1.00 55.63 C ANISOU 5545 CD1 LEU D 145 8482 5844 6810 18 1554 -2007 C ATOM 5546 CD2 LEU D 145 -7.188 57.492 59.407 1.00 60.88 C ANISOU 5546 CD2 LEU D 145 9658 6244 7228 -237 2013 -2311 C ATOM 5547 N ALA D 146 -9.654 54.136 56.151 1.00 42.85 N ANISOU 5547 N ALA D 146 6316 4445 5522 410 1885 -1942 N ATOM 5548 CA ALA D 146 -10.419 52.957 56.539 1.00 42.44 C ANISOU 5548 CA ALA D 146 6256 4446 5421 368 1957 -1963 C ATOM 5549 C ALA D 146 -9.645 52.278 57.656 1.00 46.96 C ANISOU 5549 C ALA D 146 7123 5013 5708 175 1866 -1978 C ATOM 5550 O ALA D 146 -8.477 51.944 57.468 1.00 46.46 O ANISOU 5550 O ALA D 146 7081 5015 5556 142 1607 -1886 O ATOM 5551 CB ALA D 146 -10.633 52.026 55.347 1.00 41.26 C ANISOU 5551 CB ALA D 146 5839 4453 5385 473 1804 -1866 C ATOM 5552 N THR D 147 -10.237 52.166 58.845 1.00 45.31 N ANISOU 5552 N THR D 147 7147 4712 5355 41 2082 -2079 N ATOM 5553 CA THR D 147 -9.501 51.623 59.994 1.00 45.95 C ANISOU 5553 CA THR D 147 7555 4787 5116 -168 1974 -2067 C ATOM 5554 C THR D 147 -10.234 50.505 60.747 1.00 50.17 C ANISOU 5554 C THR D 147 8218 5316 5529 -260 2118 -2078 C ATOM 5555 O THR D 147 -11.456 50.387 60.655 1.00 50.02 O ANISOU 5555 O THR D 147 8081 5259 5666 -200 2391 -2150 O ATOM 5556 CB THR D 147 -9.201 52.760 60.995 1.00 50.13 C ANISOU 5556 CB THR D 147 8407 5186 5454 -339 2083 -2192 C ATOM 5557 OG1 THR D 147 -10.418 53.451 61.297 1.00 52.94 O ANISOU 5557 OG1 THR D 147 8796 5395 5924 -309 2491 -2349 O ATOM 5558 CG2 THR D 147 -8.136 53.731 60.496 1.00 44.40 C ANISOU 5558 CG2 THR D 147 7633 4460 4778 -324 1880 -2164 C ATOM 5559 N GLY D 148 -9.459 49.742 61.521 1.00 47.57 N ANISOU 5559 N GLY D 148 8124 5017 4933 -413 1930 -1987 N ATOM 5560 CA GLY D 148 -9.922 48.678 62.406 1.00 49.25 C ANISOU 5560 CA GLY D 148 8542 5207 4963 -539 2036 -1962 C ATOM 5561 C GLY D 148 -10.575 47.480 61.747 1.00 51.87 C ANISOU 5561 C GLY D 148 8636 5585 5489 -428 2082 -1903 C ATOM 5562 O GLY D 148 -11.477 46.878 62.330 1.00 53.34 O ANISOU 5562 O GLY D 148 8924 5715 5626 -505 2324 -1947 O ATOM 5563 N PHE D 149 -10.133 47.109 60.550 1.00 45.26 N ANISOU 5563 N PHE D 149 7504 4836 4859 -271 1876 -1815 N ATOM 5564 CA PHE D 149 -10.737 45.955 59.888 1.00 43.38 C ANISOU 5564 CA PHE D 149 7068 4629 4785 -203 1921 -1785 C ATOM 5565 C PHE D 149 -9.832 44.718 59.971 1.00 46.02 C ANISOU 5565 C PHE D 149 7474 4968 5044 -226 1709 -1619 C ATOM 5566 O PHE D 149 -8.619 44.833 60.151 1.00 45.10 O ANISOU 5566 O PHE D 149 7433 4867 4835 -234 1462 -1498 O ATOM 5567 CB PHE D 149 -11.128 46.261 58.428 1.00 43.10 C ANISOU 5567 CB PHE D 149 6671 4674 5032 -35 1900 -1824 C ATOM 5568 CG PHE D 149 -10.016 46.723 57.520 1.00 42.78 C ANISOU 5568 CG PHE D 149 6508 4698 5050 72 1648 -1751 C ATOM 5569 CD1 PHE D 149 -9.287 45.808 56.765 1.00 43.74 C ANISOU 5569 CD1 PHE D 149 6530 4861 5228 126 1474 -1654 C ATOM 5570 CD2 PHE D 149 -9.710 48.076 57.400 1.00 43.70 C ANISOU 5570 CD2 PHE D 149 6611 4807 5185 115 1626 -1784 C ATOM 5571 CE1 PHE D 149 -8.265 46.241 55.913 1.00 43.24 C ANISOU 5571 CE1 PHE D 149 6351 4843 5236 220 1292 -1592 C ATOM 5572 CE2 PHE D 149 -8.691 48.505 56.547 1.00 44.74 C ANISOU 5572 CE2 PHE D 149 6627 4988 5383 202 1421 -1713 C ATOM 5573 CZ PHE D 149 -7.964 47.584 55.823 1.00 41.52 C ANISOU 5573 CZ PHE D 149 6118 4633 5026 252 1259 -1616 C ATOM 5574 N TYR D 150 -10.451 43.536 59.875 1.00 42.98 N ANISOU 5574 N TYR D 150 7053 4553 4725 -241 1820 -1605 N ATOM 5575 CA TYR D 150 -9.795 42.229 59.885 1.00 43.28 C ANISOU 5575 CA TYR D 150 7139 4547 4757 -243 1691 -1448 C ATOM 5576 C TYR D 150 -10.729 41.203 59.237 1.00 46.71 C ANISOU 5576 C TYR D 150 7424 4955 5368 -234 1861 -1514 C ATOM 5577 O TYR D 150 -11.904 41.161 59.608 1.00 46.05 O ANISOU 5577 O TYR D 150 7358 4849 5291 -318 2104 -1622 O ATOM 5578 CB TYR D 150 -9.382 41.786 61.304 1.00 46.71 C ANISOU 5578 CB TYR D 150 7919 4908 4921 -388 1649 -1308 C ATOM 5579 CG TYR D 150 -8.463 40.582 61.313 1.00 49.68 C ANISOU 5579 CG TYR D 150 8321 5224 5331 -351 1465 -1085 C ATOM 5580 CD1 TYR D 150 -7.082 40.735 61.233 1.00 51.71 C ANISOU 5580 CD1 TYR D 150 8538 5509 5601 -286 1159 -911 C ATOM 5581 CD2 TYR D 150 -8.974 39.288 61.377 1.00 52.05 C ANISOU 5581 CD2 TYR D 150 8662 5420 5695 -376 1613 -1038 C ATOM 5582 CE1 TYR D 150 -6.231 39.631 61.218 1.00 53.76 C ANISOU 5582 CE1 TYR D 150 8777 5688 5963 -221 1011 -679 C ATOM 5583 CE2 TYR D 150 -8.132 38.176 61.377 1.00 54.29 C ANISOU 5583 CE2 TYR D 150 8965 5606 6055 -320 1476 -818 C ATOM 5584 CZ TYR D 150 -6.760 38.353 61.286 1.00 63.37 C ANISOU 5584 CZ TYR D 150 10051 6779 7246 -228 1178 -631 C ATOM 5585 OH TYR D 150 -5.919 37.267 61.278 1.00 67.40 O ANISOU 5585 OH TYR D 150 10542 7171 7897 -145 1063 -389 O ATOM 5586 N PRO D 151 -10.271 40.380 58.260 1.00 43.96 N ANISOU 5586 N PRO D 151 6926 4598 5179 -151 1767 -1468 N ATOM 5587 CA PRO D 151 -8.934 40.321 57.650 1.00 43.13 C ANISOU 5587 CA PRO D 151 6747 4498 5142 -35 1541 -1349 C ATOM 5588 C PRO D 151 -8.703 41.512 56.726 1.00 46.75 C ANISOU 5588 C PRO D 151 7015 5074 5672 61 1450 -1429 C ATOM 5589 O PRO D 151 -9.576 42.375 56.614 1.00 46.06 O ANISOU 5589 O PRO D 151 6858 5056 5585 49 1545 -1555 O ATOM 5590 CB PRO D 151 -8.955 38.981 56.910 1.00 45.15 C ANISOU 5590 CB PRO D 151 6930 4666 5558 -11 1609 -1341 C ATOM 5591 CG PRO D 151 -10.380 38.826 56.505 1.00 49.24 C ANISOU 5591 CG PRO D 151 7354 5222 6132 -94 1806 -1525 C ATOM 5592 CD PRO D 151 -11.182 39.403 57.635 1.00 45.48 C ANISOU 5592 CD PRO D 151 7003 4759 5519 -190 1928 -1559 C ATOM 5593 N ASP D 152 -7.534 41.577 56.074 1.00 44.46 N ANISOU 5593 N ASP D 152 6634 4793 5467 163 1285 -1341 N ATOM 5594 CA ASP D 152 -7.173 42.752 55.285 1.00 44.52 C ANISOU 5594 CA ASP D 152 6496 4896 5523 244 1198 -1387 C ATOM 5595 C ASP D 152 -7.726 42.802 53.835 1.00 48.82 C ANISOU 5595 C ASP D 152 6846 5514 6188 302 1262 -1506 C ATOM 5596 O ASP D 152 -7.096 43.464 52.997 1.00 49.77 O ANISOU 5596 O ASP D 152 6861 5687 6363 383 1179 -1494 O ATOM 5597 CB ASP D 152 -5.639 42.935 55.268 1.00 46.87 C ANISOU 5597 CB ASP D 152 6770 5173 5864 309 1004 -1233 C ATOM 5598 CG ASP D 152 -4.836 41.778 54.693 1.00 59.19 C ANISOU 5598 CG ASP D 152 8257 6644 7587 387 992 -1130 C ATOM 5599 OD1 ASP D 152 -5.426 40.693 54.464 1.00 61.24 O ANISOU 5599 OD1 ASP D 152 8541 6834 7892 369 1133 -1175 O ATOM 5600 OD2 ASP D 152 -3.621 41.950 54.486 1.00 64.60 O ANISOU 5600 OD2 ASP D 152 8856 7311 8379 461 864 -1006 O ATOM 5601 N AHIS D 153 -8.897 42.196 53.561 0.50 43.50 N ANISOU 5601 N AHIS D 153 6132 4853 5541 239 1397 -1612 N ATOM 5602 N BHIS D 153 -8.866 42.129 53.525 0.50 46.88 N ANISOU 5602 N BHIS D 153 6560 5279 5974 239 1397 -1610 N ATOM 5603 CA AHIS D 153 -9.460 42.242 52.216 0.50 41.89 C ANISOU 5603 CA AHIS D 153 5760 4744 5410 251 1408 -1711 C ATOM 5604 CA BHIS D 153 -9.381 42.251 52.162 0.50 46.80 C ANISOU 5604 CA BHIS D 153 6381 5367 6035 257 1401 -1707 C ATOM 5605 C AHIS D 153 -10.534 43.332 52.125 0.50 46.15 C ANISOU 5605 C AHIS D 153 6174 5393 5967 254 1430 -1775 C ATOM 5606 C BHIS D 153 -10.500 43.305 52.101 0.50 48.49 C ANISOU 5606 C BHIS D 153 6471 5688 6263 255 1428 -1774 C ATOM 5607 O AHIS D 153 -11.667 43.155 52.577 0.50 46.06 O ANISOU 5607 O AHIS D 153 6128 5386 5985 180 1547 -1836 O ATOM 5608 O BHIS D 153 -11.625 43.080 52.552 0.50 48.52 O ANISOU 5608 O BHIS D 153 6444 5695 6295 178 1545 -1835 O ATOM 5609 CB AHIS D 153 -10.000 40.873 51.771 0.50 42.61 C ANISOU 5609 CB AHIS D 153 5856 4789 5546 157 1509 -1786 C ATOM 5610 CB BHIS D 153 -9.791 40.942 51.439 0.50 49.20 C ANISOU 5610 CB BHIS D 153 6670 5637 6386 178 1484 -1786 C ATOM 5611 CG AHIS D 153 -10.247 40.746 50.290 0.50 44.84 C ANISOU 5611 CG AHIS D 153 6023 5162 5851 133 1481 -1880 C ATOM 5612 CG BHIS D 153 -10.032 39.703 52.254 0.50 54.32 C ANISOU 5612 CG BHIS D 153 7449 6148 7044 90 1606 -1776 C ATOM 5613 ND1AHIS D 153 -10.921 39.658 49.769 0.50 46.95 N ANISOU 5613 ND1AHIS D 153 6291 5410 6139 1 1566 -1990 N ATOM 5614 ND1BHIS D 153 -11.301 39.148 52.358 0.50 57.29 N ANISOU 5614 ND1BHIS D 153 7794 6532 7442 -42 1729 -1880 N ATOM 5615 CD2AHIS D 153 -9.899 41.569 49.271 0.50 44.99 C ANISOU 5615 CD2AHIS D 153 5956 5287 5850 200 1380 -1878 C ATOM 5616 CD2BHIS D 153 -9.142 38.851 52.817 0.50 56.75 C ANISOU 5616 CD2BHIS D 153 7894 6297 7371 115 1624 -1663 C ATOM 5617 CE1AHIS D 153 -10.964 39.854 48.462 0.50 46.33 C ANISOU 5617 CE1AHIS D 153 6141 5439 6023 -24 1496 -2057 C ATOM 5618 CE1BHIS D 153 -11.149 38.022 53.034 0.50 57.70 C ANISOU 5618 CE1BHIS D 153 7997 6422 7504 -98 1835 -1835 C ATOM 5619 NE2AHIS D 153 -10.361 40.987 48.116 0.50 45.57 N ANISOU 5619 NE2AHIS D 153 5995 5421 5898 101 1387 -1982 N ATOM 5620 NE2BHIS D 153 -9.867 37.795 53.323 0.50 57.84 N ANISOU 5620 NE2BHIS D 153 8122 6334 7521 2 1770 -1693 N ATOM 5621 N VAL D 154 -10.141 44.474 51.543 1.00 43.14 N ANISOU 5621 N VAL D 154 5712 5081 5598 348 1334 -1745 N ATOM 5622 CA VAL D 154 -10.980 45.654 51.315 1.00 42.70 C ANISOU 5622 CA VAL D 154 5517 5103 5603 395 1344 -1763 C ATOM 5623 C VAL D 154 -10.703 46.199 49.901 1.00 45.41 C ANISOU 5623 C VAL D 154 5737 5550 5967 467 1219 -1728 C ATOM 5624 O VAL D 154 -9.594 46.037 49.376 1.00 43.52 O ANISOU 5624 O VAL D 154 5560 5295 5682 496 1152 -1692 O ATOM 5625 CB VAL D 154 -10.791 46.781 52.380 1.00 46.60 C ANISOU 5625 CB VAL D 154 6105 5524 6076 431 1398 -1743 C ATOM 5626 CG1 VAL D 154 -11.351 46.381 53.745 1.00 46.90 C ANISOU 5626 CG1 VAL D 154 6286 5474 6061 334 1558 -1789 C ATOM 5627 CG2 VAL D 154 -9.329 47.235 52.481 1.00 45.86 C ANISOU 5627 CG2 VAL D 154 6122 5388 5913 470 1278 -1670 C ATOM 5628 N GLU D 155 -11.703 46.862 49.308 1.00 41.41 N ANISOU 5628 N GLU D 155 5054 5142 5540 495 1195 -1721 N ATOM 5629 CA GLU D 155 -11.594 47.541 48.020 1.00 40.05 C ANISOU 5629 CA GLU D 155 4779 5076 5364 557 1064 -1655 C ATOM 5630 C GLU D 155 -12.090 48.963 48.214 1.00 42.82 C ANISOU 5630 C GLU D 155 5016 5417 5837 672 1082 -1580 C ATOM 5631 O GLU D 155 -13.253 49.177 48.568 1.00 42.98 O ANISOU 5631 O GLU D 155 4887 5448 5994 679 1152 -1584 O ATOM 5632 CB GLU D 155 -12.368 46.814 46.917 1.00 42.53 C ANISOU 5632 CB GLU D 155 4982 5531 5646 457 973 -1685 C ATOM 5633 CG GLU D 155 -11.712 45.522 46.460 1.00 57.34 C ANISOU 5633 CG GLU D 155 7005 7385 7398 349 984 -1770 C ATOM 5634 CD GLU D 155 -12.429 44.792 45.339 1.00 86.29 C ANISOU 5634 CD GLU D 155 10617 11182 10987 198 898 -1834 C ATOM 5635 OE1 GLU D 155 -13.635 45.053 45.119 1.00 84.97 O ANISOU 5635 OE1 GLU D 155 10256 11139 10889 152 808 -1810 O ATOM 5636 OE2 GLU D 155 -11.782 43.941 44.687 1.00 81.83 O ANISOU 5636 OE2 GLU D 155 10200 10587 10303 115 926 -1909 O ATOM 5637 N LEU D 156 -11.182 49.923 48.061 1.00 38.42 N ANISOU 5637 N LEU D 156 4526 4810 5263 760 1053 -1513 N ATOM 5638 CA LEU D 156 -11.457 51.340 48.234 1.00 39.11 C ANISOU 5638 CA LEU D 156 4545 4838 5476 874 1099 -1442 C ATOM 5639 C LEU D 156 -11.683 52.026 46.875 1.00 43.82 C ANISOU 5639 C LEU D 156 5004 5540 6107 955 963 -1305 C ATOM 5640 O LEU D 156 -10.913 51.819 45.939 1.00 42.72 O ANISOU 5640 O LEU D 156 4931 5466 5834 932 858 -1270 O ATOM 5641 CB LEU D 156 -10.290 51.990 48.990 1.00 38.37 C ANISOU 5641 CB LEU D 156 4636 4605 5340 888 1153 -1456 C ATOM 5642 CG LEU D 156 -10.573 53.307 49.697 1.00 44.10 C ANISOU 5642 CG LEU D 156 5377 5193 6187 956 1289 -1452 C ATOM 5643 CD1 LEU D 156 -9.670 53.475 50.892 1.00 44.09 C ANISOU 5643 CD1 LEU D 156 5603 5063 6086 871 1354 -1533 C ATOM 5644 CD2 LEU D 156 -10.420 54.481 48.756 1.00 48.62 C ANISOU 5644 CD2 LEU D 156 5864 5756 6852 1075 1240 -1325 C ATOM 5645 N SER D 157 -12.741 52.853 46.783 1.00 42.45 N ANISOU 5645 N SER D 157 4640 5369 6121 1050 982 -1214 N ATOM 5646 CA SER D 157 -13.084 53.598 45.569 1.00 42.99 C ANISOU 5646 CA SER D 157 4562 5533 6239 1138 830 -1032 C ATOM 5647 C SER D 157 -13.620 54.980 45.928 1.00 47.86 C ANISOU 5647 C SER D 157 5057 6012 7115 1306 946 -919 C ATOM 5648 O SER D 157 -14.234 55.147 46.988 1.00 47.91 O ANISOU 5648 O SER D 157 5015 5895 7294 1334 1143 -995 O ATOM 5649 CB SER D 157 -14.104 52.827 44.737 1.00 47.49 C ANISOU 5649 CB SER D 157 4945 6308 6792 1057 654 -988 C ATOM 5650 OG SER D 157 -15.269 52.526 45.489 1.00 56.87 O ANISOU 5650 OG SER D 157 5945 7484 8180 1045 749 -1035 O ATOM 5651 N TRP D 158 -13.373 55.968 45.056 1.00 45.50 N ANISOU 5651 N TRP D 158 4732 5709 6847 1413 856 -739 N ATOM 5652 CA TRP D 158 -13.822 57.348 45.244 1.00 47.74 C ANISOU 5652 CA TRP D 158 4905 5828 7405 1592 975 -600 C ATOM 5653 C TRP D 158 -14.972 57.649 44.314 1.00 54.49 C ANISOU 5653 C TRP D 158 5460 6810 8432 1693 802 -358 C ATOM 5654 O TRP D 158 -14.924 57.302 43.133 1.00 54.24 O ANISOU 5654 O TRP D 158 5407 6983 8218 1633 539 -236 O ATOM 5655 CB TRP D 158 -12.688 58.338 45.002 1.00 46.39 C ANISOU 5655 CB TRP D 158 4922 5522 7181 1644 1016 -543 C ATOM 5656 CG TRP D 158 -11.708 58.465 46.125 1.00 45.76 C ANISOU 5656 CG TRP D 158 5082 5265 7040 1571 1205 -741 C ATOM 5657 CD1 TRP D 158 -10.473 57.894 46.201 1.00 47.02 C ANISOU 5657 CD1 TRP D 158 5438 5457 6971 1441 1156 -852 C ATOM 5658 CD2 TRP D 158 -11.834 59.305 47.279 1.00 46.69 C ANISOU 5658 CD2 TRP D 158 5270 5137 7332 1612 1463 -833 C ATOM 5659 NE1 TRP D 158 -9.831 58.305 47.345 1.00 45.96 N ANISOU 5659 NE1 TRP D 158 5475 5141 6848 1386 1316 -989 N ATOM 5660 CE2 TRP D 158 -10.647 59.163 48.032 1.00 48.84 C ANISOU 5660 CE2 TRP D 158 5798 5333 7427 1472 1513 -1000 C ATOM 5661 CE3 TRP D 158 -12.848 60.151 47.764 1.00 50.00 C ANISOU 5661 CE3 TRP D 158 5563 5383 8053 1746 1675 -793 C ATOM 5662 CZ2 TRP D 158 -10.425 59.869 49.217 1.00 48.77 C ANISOU 5662 CZ2 TRP D 158 5959 5097 7473 1427 1736 -1139 C ATOM 5663 CZ3 TRP D 158 -12.633 60.835 48.950 1.00 52.15 C ANISOU 5663 CZ3 TRP D 158 6020 5398 8397 1718 1958 -953 C ATOM 5664 CH2 TRP D 158 -11.438 60.683 49.668 1.00 51.05 C ANISOU 5664 CH2 TRP D 158 6173 5207 8018 1541 1973 -1132 C ATOM 5665 N TRP D 159 -16.012 58.286 44.854 1.00 53.42 N ANISOU 5665 N TRP D 159 5095 6550 8652 1835 953 -284 N ATOM 5666 CA TRP D 159 -17.221 58.620 44.118 1.00 56.75 C ANISOU 5666 CA TRP D 159 5157 7076 9330 1954 789 -17 C ATOM 5667 C TRP D 159 -17.483 60.117 44.222 1.00 61.83 C ANISOU 5667 C TRP D 159 5693 7473 10326 2199 958 181 C ATOM 5668 O TRP D 159 -17.683 60.645 45.322 1.00 60.88 O ANISOU 5668 O TRP D 159 5587 7092 10453 2285 1306 62 O ATOM 5669 CB TRP D 159 -18.409 57.782 44.644 1.00 57.07 C ANISOU 5669 CB TRP D 159 4932 7200 9552 1894 826 -96 C ATOM 5670 CG TRP D 159 -18.219 56.310 44.415 1.00 56.38 C ANISOU 5670 CG TRP D 159 4944 7340 9138 1648 652 -266 C ATOM 5671 CD1 TRP D 159 -17.364 55.479 45.079 1.00 56.35 C ANISOU 5671 CD1 TRP D 159 5240 7299 8872 1498 774 -532 C ATOM 5672 CD2 TRP D 159 -18.840 55.517 43.397 1.00 58.13 C ANISOU 5672 CD2 TRP D 159 4985 7847 9254 1514 318 -168 C ATOM 5673 NE1 TRP D 159 -17.397 54.221 44.522 1.00 55.48 N ANISOU 5673 NE1 TRP D 159 5151 7403 8524 1300 572 -610 N ATOM 5674 CE2 TRP D 159 -18.311 54.210 43.502 1.00 59.91 C ANISOU 5674 CE2 TRP D 159 5435 8167 9161 1287 298 -412 C ATOM 5675 CE3 TRP D 159 -19.814 55.777 42.418 1.00 63.19 C ANISOU 5675 CE3 TRP D 159 5293 8672 10045 1551 21 112 C ATOM 5676 CZ2 TRP D 159 -18.723 53.167 42.664 1.00 60.58 C ANISOU 5676 CZ2 TRP D 159 5454 8502 9063 1081 29 -423 C ATOM 5677 CZ3 TRP D 159 -20.218 54.744 41.585 1.00 65.94 C ANISOU 5677 CZ3 TRP D 159 5571 9304 10180 1325 -295 111 C ATOM 5678 CH2 TRP D 159 -19.681 53.456 41.716 1.00 64.17 C ANISOU 5678 CH2 TRP D 159 5603 9148 9630 1085 -270 -174 C ATOM 5679 N VAL D 160 -17.410 60.802 43.069 1.00 59.69 N ANISOU 5679 N VAL D 160 5360 7266 10052 2298 731 476 N ATOM 5680 CA VAL D 160 -17.637 62.238 42.938 1.00 62.05 C ANISOU 5680 CA VAL D 160 5555 7330 10691 2545 852 728 C ATOM 5681 C VAL D 160 -18.951 62.439 42.171 1.00 70.18 C ANISOU 5681 C VAL D 160 6144 8496 12024 2687 608 1087 C ATOM 5682 O VAL D 160 -19.052 62.050 41.002 1.00 70.71 O ANISOU 5682 O VAL D 160 6152 8851 11864 2602 208 1285 O ATOM 5683 CB VAL D 160 -16.443 62.976 42.271 1.00 65.05 C ANISOU 5683 CB VAL D 160 6228 7636 10852 2555 807 822 C ATOM 5684 CG1 VAL D 160 -16.729 64.467 42.134 1.00 68.30 C ANISOU 5684 CG1 VAL D 160 6534 7771 11645 2815 951 1100 C ATOM 5685 CG2 VAL D 160 -15.141 62.748 43.045 1.00 60.96 C ANISOU 5685 CG2 VAL D 160 6087 7000 10075 2401 1015 485 C ATOM 5686 N ASN D 161 -19.958 63.021 42.858 1.00 69.34 N ANISOU 5686 N ASN D 161 5733 8181 12434 2886 857 1166 N ATOM 5687 CA ASN D 161 -21.305 63.339 42.363 1.00 73.90 C ANISOU 5687 CA ASN D 161 5805 8823 13450 3067 691 1527 C ATOM 5688 C ASN D 161 -22.060 62.094 41.824 1.00 79.39 C ANISOU 5688 C ASN D 161 6242 9914 14008 2874 304 1557 C ATOM 5689 O ASN D 161 -22.824 62.196 40.856 1.00 82.69 O ANISOU 5689 O ASN D 161 6328 10537 14554 2924 -73 1918 O ATOM 5690 CB ASN D 161 -21.260 64.462 41.307 1.00 75.33 C ANISOU 5690 CB ASN D 161 5913 8957 13750 3267 488 1963 C ATOM 5691 CG ASN D 161 -20.788 65.794 41.839 1.00 87.35 C ANISOU 5691 CG ASN D 161 7602 10045 15543 3485 898 1980 C ATOM 5692 OD1 ASN D 161 -19.914 66.442 41.264 1.00 81.21 O ANISOU 5692 OD1 ASN D 161 7091 9194 14570 3505 843 2091 O ATOM 5693 ND2 ASN D 161 -21.370 66.250 42.933 1.00 77.85 N ANISOU 5693 ND2 ASN D 161 6254 8524 14802 3640 1343 1866 N ATOM 5694 N GLY D 162 -21.873 60.959 42.500 1.00 73.24 N ANISOU 5694 N GLY D 162 5614 9221 12993 2648 407 1189 N ATOM 5695 CA GLY D 162 -22.526 59.694 42.173 1.00 73.49 C ANISOU 5695 CA GLY D 162 5453 9577 12893 2426 121 1137 C ATOM 5696 C GLY D 162 -21.797 58.805 41.184 1.00 75.48 C ANISOU 5696 C GLY D 162 5984 10133 12561 2159 -254 1074 C ATOM 5697 O GLY D 162 -22.239 57.680 40.935 1.00 75.26 O ANISOU 5697 O GLY D 162 5864 10353 12377 1933 -464 979 O ATOM 5698 N LYS D 163 -20.682 59.295 40.610 1.00 70.48 N ANISOU 5698 N LYS D 163 5701 9466 11613 2170 -308 1116 N ATOM 5699 CA LYS D 163 -19.881 58.551 39.632 1.00 68.50 C ANISOU 5699 CA LYS D 163 5757 9459 10809 1929 -592 1051 C ATOM 5700 C LYS D 163 -18.489 58.240 40.172 1.00 67.37 C ANISOU 5700 C LYS D 163 6063 9176 10357 1840 -331 723 C ATOM 5701 O LYS D 163 -17.856 59.104 40.788 1.00 65.22 O ANISOU 5701 O LYS D 163 5935 8636 10209 1991 -50 685 O ATOM 5702 CB LYS D 163 -19.770 59.332 38.316 1.00 73.91 C ANISOU 5702 CB LYS D 163 6458 10256 11369 1993 -910 1424 C ATOM 5703 N GLU D 164 -18.007 57.006 39.928 1.00 62.22 N ANISOU 5703 N GLU D 164 5625 8696 9319 1585 -425 492 N ATOM 5704 CA GLU D 164 -16.684 56.572 40.379 1.00 58.38 C ANISOU 5704 CA GLU D 164 5519 8098 8563 1494 -213 209 C ATOM 5705 C GLU D 164 -15.582 57.312 39.606 1.00 63.46 C ANISOU 5705 C GLU D 164 6424 8695 8994 1536 -239 326 C ATOM 5706 O GLU D 164 -15.685 57.473 38.386 1.00 64.80 O ANISOU 5706 O GLU D 164 6605 9037 8978 1492 -505 541 O ATOM 5707 CB GLU D 164 -16.511 55.052 40.251 1.00 58.06 C ANISOU 5707 CB GLU D 164 5614 8225 8221 1231 -287 -36 C ATOM 5708 CG GLU D 164 -15.381 54.523 41.126 1.00 62.19 C ANISOU 5708 CG GLU D 164 6424 8587 8618 1179 -18 -322 C ATOM 5709 CD GLU D 164 -14.907 53.101 40.886 1.00 72.96 C ANISOU 5709 CD GLU D 164 7983 10058 9680 949 -50 -542 C ATOM 5710 OE1 GLU D 164 -15.717 52.262 40.429 1.00 64.36 O ANISOU 5710 OE1 GLU D 164 6782 9150 8523 789 -221 -566 O ATOM 5711 OE2 GLU D 164 -13.728 52.816 41.198 1.00 62.86 O ANISOU 5711 OE2 GLU D 164 6957 8665 8263 924 108 -691 O ATOM 5712 N VAL D 165 -14.547 57.781 40.331 1.00 58.77 N ANISOU 5712 N VAL D 165 6039 7868 8423 1605 34 193 N ATOM 5713 CA VAL D 165 -13.430 58.522 39.753 1.00 58.99 C ANISOU 5713 CA VAL D 165 6301 7811 8302 1640 69 281 C ATOM 5714 C VAL D 165 -12.123 57.709 39.931 1.00 60.84 C ANISOU 5714 C VAL D 165 6823 8030 8263 1482 185 20 C ATOM 5715 O VAL D 165 -12.014 56.893 40.853 1.00 58.33 O ANISOU 5715 O VAL D 165 6528 7678 7956 1409 301 -217 O ATOM 5716 CB VAL D 165 -13.350 59.971 40.330 1.00 64.26 C ANISOU 5716 CB VAL D 165 6928 8198 9291 1858 275 400 C ATOM 5717 CG1 VAL D 165 -12.704 60.019 41.710 1.00 61.67 C ANISOU 5717 CG1 VAL D 165 6729 7642 9060 1851 577 130 C ATOM 5718 CG2 VAL D 165 -12.648 60.922 39.371 1.00 65.67 C ANISOU 5718 CG2 VAL D 165 7253 8326 9373 1917 230 624 C ATOM 5719 N HIS D 166 -11.164 57.906 39.007 1.00 57.78 N ANISOU 5719 N HIS D 166 6643 7667 7642 1432 157 86 N ATOM 5720 CA HIS D 166 -9.858 57.243 39.020 1.00 55.20 C ANISOU 5720 CA HIS D 166 6553 7309 7110 1307 284 -113 C ATOM 5721 C HIS D 166 -8.738 58.273 38.894 1.00 56.65 C ANISOU 5721 C HIS D 166 6878 7318 7327 1375 429 -35 C ATOM 5722 O HIS D 166 -7.681 58.098 39.499 1.00 53.91 O ANISOU 5722 O HIS D 166 6634 6850 6997 1335 592 -197 O ATOM 5723 CB HIS D 166 -9.764 56.191 37.909 1.00 57.21 C ANISOU 5723 CB HIS D 166 6938 7774 7026 1124 152 -154 C ATOM 5724 CG HIS D 166 -10.716 55.050 38.106 1.00 61.29 C ANISOU 5724 CG HIS D 166 7342 8440 7507 1011 36 -280 C ATOM 5725 ND1 HIS D 166 -11.961 55.031 37.492 1.00 65.85 N ANISOU 5725 ND1 HIS D 166 7752 9206 8060 976 -219 -127 N ATOM 5726 CD2 HIS D 166 -10.591 53.946 38.879 1.00 61.21 C ANISOU 5726 CD2 HIS D 166 7348 8401 7506 924 139 -523 C ATOM 5727 CE1 HIS D 166 -12.538 53.909 37.891 1.00 64.85 C ANISOU 5727 CE1 HIS D 166 7550 9160 7928 852 -247 -306 C ATOM 5728 NE2 HIS D 166 -11.752 53.223 38.724 1.00 62.50 N ANISOU 5728 NE2 HIS D 166 7374 8729 7646 822 -24 -545 N ATOM 5729 N SER D 167 -8.980 59.355 38.130 1.00 54.32 N ANISOU 5729 N SER D 167 6572 7006 7064 1473 360 230 N ATOM 5730 CA SER D 167 -8.031 60.456 37.951 1.00 53.60 C ANISOU 5730 CA SER D 167 6606 6729 7032 1536 507 334 C ATOM 5731 C SER D 167 -7.841 61.196 39.276 1.00 53.93 C ANISOU 5731 C SER D 167 6590 6517 7383 1632 702 236 C ATOM 5732 O SER D 167 -8.813 61.429 39.997 1.00 53.73 O ANISOU 5732 O SER D 167 6402 6436 7575 1731 708 239 O ATOM 5733 CB SER D 167 -8.511 61.418 36.867 1.00 59.44 C ANISOU 5733 CB SER D 167 7341 7497 7745 1628 378 674 C ATOM 5734 OG SER D 167 -7.587 62.477 36.679 1.00 68.11 O ANISOU 5734 OG SER D 167 8575 8395 8907 1677 546 776 O ATOM 5735 N GLY D 168 -6.588 61.514 39.589 1.00 47.74 N ANISOU 5735 N GLY D 168 5943 5582 6614 1579 868 139 N ATOM 5736 CA GLY D 168 -6.197 62.206 40.809 1.00 46.32 C ANISOU 5736 CA GLY D 168 5770 5164 6664 1604 1044 18 C ATOM 5737 C GLY D 168 -6.304 61.358 42.058 1.00 47.59 C ANISOU 5737 C GLY D 168 5896 5336 6849 1533 1070 -233 C ATOM 5738 O GLY D 168 -6.231 61.889 43.165 1.00 46.74 O ANISOU 5738 O GLY D 168 5810 5048 6899 1533 1198 -342 O ATOM 5739 N VAL D 169 -6.449 60.033 41.893 1.00 43.74 N ANISOU 5739 N VAL D 169 5386 5046 6188 1452 961 -329 N ATOM 5740 CA VAL D 169 -6.592 59.082 42.999 1.00 42.33 C ANISOU 5740 CA VAL D 169 5186 4890 6007 1380 975 -539 C ATOM 5741 C VAL D 169 -5.354 58.195 43.126 1.00 46.92 C ANISOU 5741 C VAL D 169 5860 5500 6466 1254 986 -667 C ATOM 5742 O VAL D 169 -4.824 57.721 42.123 1.00 45.37 O ANISOU 5742 O VAL D 169 5707 5397 6132 1213 957 -626 O ATOM 5743 CB VAL D 169 -7.879 58.210 42.819 1.00 45.42 C ANISOU 5743 CB VAL D 169 5449 5455 6352 1390 859 -541 C ATOM 5744 CG1 VAL D 169 -7.901 56.987 43.745 1.00 43.07 C ANISOU 5744 CG1 VAL D 169 5164 5199 6002 1289 875 -747 C ATOM 5745 CG2 VAL D 169 -9.140 59.040 42.998 1.00 46.70 C ANISOU 5745 CG2 VAL D 169 5455 5562 6728 1528 871 -420 C ATOM 5746 N CYS D 170 -4.944 57.930 44.374 1.00 46.12 N ANISOU 5746 N CYS D 170 5790 5314 6418 1189 1033 -815 N ATOM 5747 CA CYS D 170 -3.906 56.965 44.708 1.00 46.74 C ANISOU 5747 CA CYS D 170 5908 5416 6434 1086 1018 -913 C ATOM 5748 C CYS D 170 -4.198 56.389 46.091 1.00 47.20 C ANISOU 5748 C CYS D 170 5986 5449 6500 1028 1010 -1046 C ATOM 5749 O CYS D 170 -4.398 57.123 47.058 1.00 46.65 O ANISOU 5749 O CYS D 170 5964 5262 6497 1012 1063 -1095 O ATOM 5750 CB CYS D 170 -2.491 57.530 44.593 1.00 49.40 C ANISOU 5750 CB CYS D 170 6280 5654 6834 1038 1063 -878 C ATOM 5751 SG CYS D 170 -2.036 58.698 45.897 1.00 55.32 S ANISOU 5751 SG CYS D 170 7089 6213 7719 971 1105 -935 S ATOM 5752 N THR D 171 -4.293 55.064 46.147 1.00 42.14 N ANISOU 5752 N THR D 171 5333 4903 5776 987 966 -1107 N ATOM 5753 CA THR D 171 -4.586 54.281 47.346 1.00 41.45 C ANISOU 5753 CA THR D 171 5281 4805 5662 924 957 -1210 C ATOM 5754 C THR D 171 -3.341 53.493 47.730 1.00 44.43 C ANISOU 5754 C THR D 171 5687 5163 6033 852 910 -1219 C ATOM 5755 O THR D 171 -2.612 53.080 46.835 1.00 42.94 O ANISOU 5755 O THR D 171 5456 5002 5857 868 915 -1173 O ATOM 5756 CB THR D 171 -5.781 53.362 47.035 1.00 44.99 C ANISOU 5756 CB THR D 171 5674 5365 6056 937 951 -1246 C ATOM 5757 OG1 THR D 171 -6.901 54.179 46.702 1.00 47.32 O ANISOU 5757 OG1 THR D 171 5889 5678 6411 1015 971 -1198 O ATOM 5758 CG2 THR D 171 -6.136 52.405 48.174 1.00 40.61 C ANISOU 5758 CG2 THR D 171 5168 4797 5466 865 968 -1342 C ATOM 5759 N ASP D 172 -3.092 53.295 49.046 1.00 42.40 N ANISOU 5759 N ASP D 172 5502 4850 5760 769 871 -1265 N ATOM 5760 CA ASP D 172 -1.965 52.486 49.527 1.00 42.82 C ANISOU 5760 CA ASP D 172 5551 4886 5832 707 784 -1228 C ATOM 5761 C ASP D 172 -2.079 51.062 48.942 1.00 46.31 C ANISOU 5761 C ASP D 172 5947 5382 6269 747 812 -1226 C ATOM 5762 O ASP D 172 -3.169 50.489 48.999 1.00 44.86 O ANISOU 5762 O ASP D 172 5793 5241 6011 750 853 -1290 O ATOM 5763 CB ASP D 172 -1.928 52.407 51.068 1.00 45.29 C ANISOU 5763 CB ASP D 172 5985 5155 6068 592 708 -1261 C ATOM 5764 CG ASP D 172 -1.998 53.703 51.853 1.00 57.94 C ANISOU 5764 CG ASP D 172 7704 6681 7631 506 717 -1316 C ATOM 5765 OD1 ASP D 172 -1.397 54.714 51.404 1.00 59.82 O ANISOU 5765 OD1 ASP D 172 7902 6872 7954 506 720 -1289 O ATOM 5766 OD2 ASP D 172 -2.567 53.685 52.965 1.00 61.02 O ANISOU 5766 OD2 ASP D 172 8247 7039 7899 416 738 -1392 O ATOM 5767 N PRO D 173 -1.007 50.479 48.357 1.00 44.79 N ANISOU 5767 N PRO D 173 5676 5168 6173 772 820 -1161 N ATOM 5768 CA PRO D 173 -1.137 49.126 47.777 1.00 44.63 C ANISOU 5768 CA PRO D 173 5645 5156 6156 801 898 -1184 C ATOM 5769 C PRO D 173 -1.498 48.053 48.810 1.00 49.00 C ANISOU 5769 C PRO D 173 6256 5682 6681 763 861 -1197 C ATOM 5770 O PRO D 173 -2.154 47.069 48.461 1.00 48.90 O ANISOU 5770 O PRO D 173 6275 5678 6628 761 942 -1261 O ATOM 5771 CB PRO D 173 0.243 48.859 47.172 1.00 47.08 C ANISOU 5771 CB PRO D 173 5857 5402 6631 840 954 -1103 C ATOM 5772 CG PRO D 173 1.166 49.785 47.869 1.00 52.45 C ANISOU 5772 CG PRO D 173 6471 6046 7411 807 836 -1014 C ATOM 5773 CD PRO D 173 0.358 51.013 48.170 1.00 47.65 C ANISOU 5773 CD PRO D 173 5949 5478 6676 769 792 -1071 C ATOM 5774 N GLN D 174 -1.098 48.254 50.080 1.00 45.16 N ANISOU 5774 N GLN D 174 5804 5160 6194 707 737 -1137 N ATOM 5775 CA GLN D 174 -1.365 47.289 51.137 1.00 45.03 C ANISOU 5775 CA GLN D 174 5874 5110 6125 658 692 -1115 C ATOM 5776 C GLN D 174 -1.764 47.976 52.438 1.00 47.90 C ANISOU 5776 C GLN D 174 6375 5483 6341 552 604 -1135 C ATOM 5777 O GLN D 174 -1.181 49.011 52.797 1.00 46.56 O ANISOU 5777 O GLN D 174 6215 5311 6165 499 510 -1111 O ATOM 5778 CB GLN D 174 -0.127 46.400 51.376 1.00 47.68 C ANISOU 5778 CB GLN D 174 6127 5367 6623 687 621 -961 C ATOM 5779 N PRO D 175 -2.712 47.370 53.196 1.00 44.28 N ANISOU 5779 N PRO D 175 6046 5018 5760 497 652 -1186 N ATOM 5780 CA PRO D 175 -3.085 47.947 54.493 1.00 44.44 C ANISOU 5780 CA PRO D 175 6247 5028 5611 374 616 -1219 C ATOM 5781 C PRO D 175 -1.943 47.818 55.497 1.00 47.24 C ANISOU 5781 C PRO D 175 6674 5357 5916 276 403 -1076 C ATOM 5782 O PRO D 175 -1.114 46.929 55.357 1.00 46.82 O ANISOU 5782 O PRO D 175 6522 5283 5986 325 307 -929 O ATOM 5783 CB PRO D 175 -4.304 47.107 54.917 1.00 46.32 C ANISOU 5783 CB PRO D 175 6585 5256 5760 343 755 -1290 C ATOM 5784 CG PRO D 175 -4.754 46.391 53.681 1.00 49.86 C ANISOU 5784 CG PRO D 175 6883 5730 6332 443 856 -1329 C ATOM 5785 CD PRO D 175 -3.490 46.145 52.924 1.00 45.38 C ANISOU 5785 CD PRO D 175 6194 5147 5903 520 769 -1227 C ATOM 5786 N LEU D 176 -1.876 48.717 56.485 1.00 44.94 N ANISOU 5786 N LEU D 176 6553 5064 5460 129 329 -1110 N ATOM 5787 CA LEU D 176 -0.843 48.630 57.518 1.00 46.06 C ANISOU 5787 CA LEU D 176 6785 5209 5507 -14 74 -965 C ATOM 5788 C LEU D 176 -1.448 48.037 58.798 1.00 50.27 C ANISOU 5788 C LEU D 176 7595 5726 5778 -153 73 -957 C ATOM 5789 O LEU D 176 -2.661 48.151 59.015 1.00 48.63 O ANISOU 5789 O LEU D 176 7530 5493 5453 -173 304 -1115 O ATOM 5790 CB LEU D 176 -0.137 49.980 57.788 1.00 46.81 C ANISOU 5790 CB LEU D 176 6913 5311 5562 -143 -52 -998 C ATOM 5791 CG LEU D 176 -0.961 51.232 58.135 1.00 51.35 C ANISOU 5791 CG LEU D 176 7687 5841 5982 -241 121 -1210 C ATOM 5792 CD1 LEU D 176 -1.329 51.271 59.611 1.00 53.48 C ANISOU 5792 CD1 LEU D 176 8304 6090 5928 -467 101 -1266 C ATOM 5793 CD2 LEU D 176 -0.170 52.503 57.804 1.00 52.17 C ANISOU 5793 CD2 LEU D 176 7722 5924 6178 -296 51 -1239 C ATOM 5794 N LYS D 177 -0.605 47.404 59.633 1.00 48.12 N ANISOU 5794 N LYS D 177 7388 5467 5429 -250 -182 -754 N ATOM 5795 CA LYS D 177 -1.036 46.800 60.895 1.00 49.93 C ANISOU 5795 CA LYS D 177 7916 5683 5374 -404 -214 -700 C ATOM 5796 C LYS D 177 -1.163 47.865 61.986 1.00 55.19 C ANISOU 5796 C LYS D 177 8900 6364 5707 -662 -256 -818 C ATOM 5797 O LYS D 177 -0.217 48.626 62.220 1.00 55.77 O ANISOU 5797 O LYS D 177 8966 6479 5747 -787 -494 -773 O ATOM 5798 CB LYS D 177 -0.059 45.698 61.339 1.00 54.47 C ANISOU 5798 CB LYS D 177 8434 6259 6001 -400 -497 -391 C ATOM 5799 CG LYS D 177 -0.285 44.351 60.680 1.00 66.38 C ANISOU 5799 CG LYS D 177 9783 7693 7745 -196 -362 -298 C ATOM 5800 CD LYS D 177 0.683 43.318 61.236 1.00 77.81 C ANISOU 5800 CD LYS D 177 11185 9109 9271 -184 -630 40 C ATOM 5801 CE LYS D 177 0.444 41.946 60.659 1.00 89.44 C ANISOU 5801 CE LYS D 177 12542 10459 10983 7 -453 123 C ATOM 5802 NZ LYS D 177 1.390 40.944 61.218 1.00101.16 N ANISOU 5802 NZ LYS D 177 13967 11878 12592 46 -699 487 N ATOM 5803 N GLU D 178 -2.331 47.916 62.655 1.00 51.94 N ANISOU 5803 N GLU D 178 8775 5905 5056 -760 -2 -979 N ATOM 5804 CA GLU D 178 -2.578 48.872 63.745 1.00 53.84 C ANISOU 5804 CA GLU D 178 9383 6122 4951 -1023 45 -1129 C ATOM 5805 C GLU D 178 -1.799 48.477 65.010 1.00 61.78 C ANISOU 5805 C GLU D 178 10669 7182 5624 -1280 -287 -936 C ATOM 5806 O GLU D 178 -1.465 49.341 65.817 1.00 63.08 O ANISOU 5806 O GLU D 178 11105 7359 5505 -1543 -397 -1012 O ATOM 5807 CB GLU D 178 -4.077 48.990 64.057 1.00 54.82 C ANISOU 5807 CB GLU D 178 9710 6156 4962 -1038 472 -1352 C ATOM 5808 CG GLU D 178 -4.887 49.606 62.928 1.00 60.65 C ANISOU 5808 CG GLU D 178 10188 6850 6005 -823 762 -1531 C ATOM 5809 CD GLU D 178 -6.375 49.758 63.177 1.00 75.93 C ANISOU 5809 CD GLU D 178 12240 8694 7917 -816 1184 -1727 C ATOM 5810 OE1 GLU D 178 -6.935 48.991 63.992 1.00 73.56 O ANISOU 5810 OE1 GLU D 178 12159 8366 7425 -920 1304 -1714 O ATOM 5811 OE2 GLU D 178 -6.987 50.643 62.539 1.00 73.12 O ANISOU 5811 OE2 GLU D 178 11738 8285 7761 -699 1404 -1876 O ATOM 5812 N GLN D 179 -1.524 47.173 65.182 1.00 60.17 N ANISOU 5812 N GLN D 179 10413 7001 5448 -1216 -447 -679 N ATOM 5813 CA GLN D 179 -0.771 46.627 66.313 1.00 64.02 C ANISOU 5813 CA GLN D 179 11126 7547 5652 -1426 -808 -416 C ATOM 5814 C GLN D 179 0.276 45.641 65.763 1.00 68.20 C ANISOU 5814 C GLN D 179 11284 8107 6522 -1229 -1112 -78 C ATOM 5815 O GLN D 179 0.053 44.431 65.820 1.00 67.54 O ANISOU 5815 O GLN D 179 11186 7970 6506 -1115 -1073 95 O ATOM 5816 CB GLN D 179 -1.722 45.969 67.331 1.00 67.35 C ANISOU 5816 CB GLN D 179 11956 7915 5719 -1567 -613 -427 C ATOM 5817 CG GLN D 179 -2.520 46.971 68.171 1.00 84.10 C ANISOU 5817 CG GLN D 179 14513 9996 7446 -1831 -349 -724 C ATOM 5818 CD GLN D 179 -3.598 46.327 69.018 1.00107.62 C ANISOU 5818 CD GLN D 179 17862 12897 10132 -1941 -46 -770 C ATOM 5819 OE1 GLN D 179 -4.203 45.306 68.659 1.00103.92 O ANISOU 5819 OE1 GLN D 179 17260 12373 9850 -1758 135 -699 O ATOM 5820 NE2 GLN D 179 -3.900 46.943 70.148 1.00101.14 N ANISOU 5820 NE2 GLN D 179 17533 12053 8844 -2261 57 -914 N ATOM 5821 N PRO D 180 1.417 46.141 65.211 1.00 66.45 N ANISOU 5821 N PRO D 180 10751 7947 6551 -1182 -1378 16 N ATOM 5822 CA PRO D 180 2.409 45.241 64.581 1.00 67.34 C ANISOU 5822 CA PRO D 180 10463 8055 7069 -962 -1592 323 C ATOM 5823 C PRO D 180 2.924 44.068 65.434 1.00 77.05 C ANISOU 5823 C PRO D 180 11760 9287 8229 -999 -1891 706 C ATOM 5824 O PRO D 180 3.319 43.054 64.857 1.00 76.93 O ANISOU 5824 O PRO D 180 11454 9195 8582 -754 -1895 922 O ATOM 5825 CB PRO D 180 3.558 46.182 64.228 1.00 69.74 C ANISOU 5825 CB PRO D 180 10510 8436 7552 -1014 -1855 358 C ATOM 5826 CG PRO D 180 2.902 47.495 64.014 1.00 72.12 C ANISOU 5826 CG PRO D 180 10965 8732 7704 -1114 -1607 -7 C ATOM 5827 CD PRO D 180 1.813 47.556 65.044 1.00 68.32 C ANISOU 5827 CD PRO D 180 10964 8228 6766 -1313 -1434 -168 C ATOM 5828 N ALA D 181 2.913 44.190 66.775 1.00 78.15 N ANISOU 5828 N ALA D 181 12295 9497 7902 -1304 -2122 795 N ATOM 5829 CA ALA D 181 3.363 43.130 67.684 1.00 82.40 C ANISOU 5829 CA ALA D 181 12949 10046 8315 -1367 -2439 1195 C ATOM 5830 C ALA D 181 2.375 41.947 67.721 1.00 86.24 C ANISOU 5830 C ALA D 181 13585 10391 8791 -1223 -2111 1219 C ATOM 5831 O ALA D 181 2.806 40.797 67.838 1.00 87.81 O ANISOU 5831 O ALA D 181 13668 10522 9174 -1089 -2260 1570 O ATOM 5832 CB ALA D 181 3.554 43.691 69.086 1.00 87.39 C ANISOU 5832 CB ALA D 181 14026 10804 8374 -1781 -2765 1251 C ATOM 5833 N LEU D 182 1.061 42.237 67.628 1.00 80.48 N ANISOU 5833 N LEU D 182 13095 9604 7878 -1252 -1659 858 N ATOM 5834 CA LEU D 182 -0.016 41.246 67.662 1.00 79.48 C ANISOU 5834 CA LEU D 182 13119 9346 7731 -1161 -1302 821 C ATOM 5835 C LEU D 182 -0.134 40.506 66.328 1.00 80.29 C ANISOU 5835 C LEU D 182 12814 9333 8358 -818 -1067 796 C ATOM 5836 O LEU D 182 0.010 41.119 65.263 1.00 77.26 O ANISOU 5836 O LEU D 182 12130 8972 8254 -677 -973 610 O ATOM 5837 CB LEU D 182 -1.354 41.924 68.012 1.00 78.58 C ANISOU 5837 CB LEU D 182 13353 9218 7288 -1325 -900 439 C ATOM 5838 CG LEU D 182 -1.660 42.130 69.505 1.00 87.45 C ANISOU 5838 CG LEU D 182 15032 10375 7819 -1677 -954 459 C ATOM 5839 CD1 LEU D 182 -1.014 43.393 70.043 1.00 89.44 C ANISOU 5839 CD1 LEU D 182 15450 10754 7780 -1942 -1224 375 C ATOM 5840 CD2 LEU D 182 -3.151 42.220 69.742 1.00 89.37 C ANISOU 5840 CD2 LEU D 182 15555 10524 7877 -1746 -428 148 C ATOM 5841 N ASN D 183 -0.405 39.184 66.392 1.00 77.01 N ANISOU 5841 N ASN D 183 12422 8782 8057 -705 -957 982 N ATOM 5842 CA ASN D 183 -0.558 38.330 65.210 1.00 74.22 C ANISOU 5842 CA ASN D 183 11752 8288 8162 -422 -707 952 C ATOM 5843 C ASN D 183 -1.977 38.434 64.619 1.00 73.88 C ANISOU 5843 C ASN D 183 11763 8201 8106 -406 -243 568 C ATOM 5844 O ASN D 183 -2.161 38.185 63.422 1.00 71.25 O ANISOU 5844 O ASN D 183 11156 7810 8107 -217 -40 427 O ATOM 5845 CB ASN D 183 -0.204 36.872 65.534 1.00 78.08 C ANISOU 5845 CB ASN D 183 12244 8614 8808 -317 -775 1319 C ATOM 5846 CG ASN D 183 1.286 36.606 65.606 1.00106.28 C ANISOU 5846 CG ASN D 183 15555 12188 12639 -208 -1189 1721 C ATOM 5847 OD1 ASN D 183 2.064 36.978 64.713 1.00101.18 O ANISOU 5847 OD1 ASN D 183 14537 11564 12342 -53 -1257 1703 O ATOM 5848 ND2 ASN D 183 1.718 35.925 66.659 1.00100.72 N ANISOU 5848 ND2 ASN D 183 15025 11451 11792 -284 -1469 2117 N ATOM 5849 N ASP D 184 -2.966 38.816 65.449 1.00 69.36 N ANISOU 5849 N ASP D 184 11539 7660 7153 -616 -77 403 N ATOM 5850 CA ASP D 184 -4.360 38.990 65.030 1.00 65.94 C ANISOU 5850 CA ASP D 184 11138 7197 6719 -622 348 63 C ATOM 5851 C ASP D 184 -4.696 40.497 64.866 1.00 64.36 C ANISOU 5851 C ASP D 184 10934 7115 6404 -697 418 -230 C ATOM 5852 O ASP D 184 -5.871 40.873 64.856 1.00 62.56 O ANISOU 5852 O ASP D 184 10788 6873 6107 -751 743 -487 O ATOM 5853 CB ASP D 184 -5.300 38.314 66.049 1.00 70.30 C ANISOU 5853 CB ASP D 184 12056 7662 6994 -788 566 86 C ATOM 5854 CG ASP D 184 -5.361 39.007 67.400 1.00 85.71 C ANISOU 5854 CG ASP D 184 14428 9683 8455 -1063 485 96 C ATOM 5855 OD1 ASP D 184 -4.282 39.282 67.980 1.00 89.01 O ANISOU 5855 OD1 ASP D 184 14937 10181 8702 -1151 92 318 O ATOM 5856 OD2 ASP D 184 -6.483 39.288 67.870 1.00 92.54 O ANISOU 5856 OD2 ASP D 184 15529 10519 9112 -1204 822 -124 O ATOM 5857 N SER D 185 -3.651 41.343 64.725 1.00 58.63 N ANISOU 5857 N SER D 185 10091 6485 5699 -695 123 -177 N ATOM 5858 CA SER D 185 -3.723 42.804 64.568 1.00 56.33 C ANISOU 5858 CA SER D 185 9794 6279 5328 -763 148 -412 C ATOM 5859 C SER D 185 -4.722 43.245 63.502 1.00 55.96 C ANISOU 5859 C SER D 185 9541 6218 5503 -623 484 -699 C ATOM 5860 O SER D 185 -4.799 42.631 62.437 1.00 53.27 O ANISOU 5860 O SER D 185 8921 5851 5468 -432 557 -696 O ATOM 5861 CB SER D 185 -2.352 43.362 64.195 1.00 58.09 C ANISOU 5861 CB SER D 185 9796 6581 5693 -719 -205 -281 C ATOM 5862 OG SER D 185 -2.389 44.761 63.954 1.00 61.17 O ANISOU 5862 OG SER D 185 10171 7027 6045 -778 -163 -505 O ATOM 5863 N ARG D 186 -5.462 44.326 63.791 1.00 51.40 N ANISOU 5863 N ARG D 186 9107 5650 4772 -727 684 -937 N ATOM 5864 CA ARG D 186 -6.416 44.907 62.852 1.00 48.38 C ANISOU 5864 CA ARG D 186 8516 5261 4606 -599 968 -1174 C ATOM 5865 C ARG D 186 -5.655 45.840 61.901 1.00 49.69 C ANISOU 5865 C ARG D 186 8426 5487 4966 -483 811 -1201 C ATOM 5866 O ARG D 186 -4.506 46.197 62.179 1.00 49.52 O ANISOU 5866 O ARG D 186 8433 5505 4876 -548 527 -1081 O ATOM 5867 CB ARG D 186 -7.568 45.600 63.574 1.00 49.18 C ANISOU 5867 CB ARG D 186 8852 5307 4527 -732 1296 -1390 C ATOM 5868 CG ARG D 186 -8.472 44.618 64.313 1.00 62.32 C ANISOU 5868 CG ARG D 186 10719 6900 6060 -827 1527 -1380 C ATOM 5869 CD ARG D 186 -9.875 45.157 64.451 1.00 69.13 C ANISOU 5869 CD ARG D 186 11612 7697 6959 -854 1952 -1618 C ATOM 5870 NE ARG D 186 -10.200 45.552 65.818 1.00 75.98 N ANISOU 5870 NE ARG D 186 12913 8489 7467 -1092 2143 -1698 N ATOM 5871 CZ ARG D 186 -11.222 46.336 66.149 1.00 86.70 C ANISOU 5871 CZ ARG D 186 14359 9758 8825 -1143 2537 -1920 C ATOM 5872 NH1 ARG D 186 -11.451 46.635 67.420 1.00 86.15 N ANISOU 5872 NH1 ARG D 186 14737 9603 8393 -1384 2740 -2002 N ATOM 5873 NH2 ARG D 186 -12.017 46.836 65.209 1.00 57.76 N ANISOU 5873 NH2 ARG D 186 10338 6081 5525 -958 2737 -2051 N ATOM 5874 N TYR D 187 -6.270 46.180 60.756 1.00 44.14 N ANISOU 5874 N TYR D 187 7463 4796 4511 -321 978 -1335 N ATOM 5875 CA TYR D 187 -5.605 46.935 59.698 1.00 41.71 C ANISOU 5875 CA TYR D 187 6909 4538 4403 -195 860 -1341 C ATOM 5876 C TYR D 187 -6.191 48.308 59.451 1.00 42.70 C ANISOU 5876 C TYR D 187 7014 4648 4561 -182 1025 -1520 C ATOM 5877 O TYR D 187 -7.305 48.612 59.861 1.00 42.14 O ANISOU 5877 O TYR D 187 7044 4527 4441 -222 1283 -1658 O ATOM 5878 CB TYR D 187 -5.647 46.139 58.374 1.00 40.95 C ANISOU 5878 CB TYR D 187 6524 4467 4570 -11 876 -1305 C ATOM 5879 CG TYR D 187 -4.896 44.828 58.408 1.00 44.02 C ANISOU 5879 CG TYR D 187 6887 4827 5011 18 736 -1119 C ATOM 5880 CD1 TYR D 187 -3.568 44.751 57.996 1.00 46.16 C ANISOU 5880 CD1 TYR D 187 7013 5108 5416 88 520 -965 C ATOM 5881 CD2 TYR D 187 -5.521 43.653 58.819 1.00 45.88 C ANISOU 5881 CD2 TYR D 187 7223 5004 5206 -15 849 -1088 C ATOM 5882 CE1 TYR D 187 -2.868 43.544 58.030 1.00 48.06 C ANISOU 5882 CE1 TYR D 187 7205 5289 5768 142 421 -772 C ATOM 5883 CE2 TYR D 187 -4.834 42.439 58.851 1.00 47.38 C ANISOU 5883 CE2 TYR D 187 7393 5128 5481 29 747 -900 C ATOM 5884 CZ TYR D 187 -3.508 42.389 58.453 1.00 54.00 C ANISOU 5884 CZ TYR D 187 8077 5967 6475 119 536 -738 C ATOM 5885 OH TYR D 187 -2.826 41.200 58.487 1.00 56.97 O ANISOU 5885 OH TYR D 187 8408 6247 6992 188 464 -533 O ATOM 5886 N ALA D 188 -5.425 49.117 58.717 1.00 38.73 N ANISOU 5886 N ALA D 188 6357 4173 4184 -111 899 -1503 N ATOM 5887 CA ALA D 188 -5.770 50.472 58.300 1.00 38.28 C ANISOU 5887 CA ALA D 188 6249 4083 4212 -68 1027 -1629 C ATOM 5888 C ALA D 188 -5.320 50.685 56.872 1.00 41.12 C ANISOU 5888 C ALA D 188 6321 4496 4805 104 947 -1571 C ATOM 5889 O ALA D 188 -4.294 50.135 56.462 1.00 39.49 O ANISOU 5889 O ALA D 188 6009 4334 4660 135 756 -1444 O ATOM 5890 CB ALA D 188 -5.117 51.488 59.220 1.00 40.43 C ANISOU 5890 CB ALA D 188 6755 4300 4308 -248 956 -1674 C ATOM 5891 N LEU D 189 -6.101 51.452 56.106 1.00 38.26 N ANISOU 5891 N LEU D 189 5832 4122 4585 217 1106 -1649 N ATOM 5892 CA LEU D 189 -5.809 51.758 54.710 1.00 37.65 C ANISOU 5892 CA LEU D 189 5522 4096 4687 365 1052 -1593 C ATOM 5893 C LEU D 189 -6.190 53.191 54.419 1.00 42.70 C ANISOU 5893 C LEU D 189 6137 4667 5419 419 1172 -1649 C ATOM 5894 O LEU D 189 -7.250 53.647 54.850 1.00 44.01 O ANISOU 5894 O LEU D 189 6351 4765 5605 425 1370 -1738 O ATOM 5895 CB LEU D 189 -6.555 50.793 53.756 1.00 36.93 C ANISOU 5895 CB LEU D 189 5257 4089 4687 471 1093 -1577 C ATOM 5896 CG LEU D 189 -6.192 50.878 52.262 1.00 40.39 C ANISOU 5896 CG LEU D 189 5507 4598 5244 588 1026 -1514 C ATOM 5897 CD1 LEU D 189 -4.890 50.166 51.965 1.00 39.57 C ANISOU 5897 CD1 LEU D 189 5382 4505 5149 582 893 -1426 C ATOM 5898 CD2 LEU D 189 -7.286 50.275 51.399 1.00 44.19 C ANISOU 5898 CD2 LEU D 189 5853 5161 5776 647 1086 -1538 C ATOM 5899 N SER D 190 -5.317 53.903 53.696 1.00 38.36 N ANISOU 5899 N SER D 190 5509 4115 4953 462 1080 -1586 N ATOM 5900 CA SER D 190 -5.563 55.281 53.315 1.00 38.24 C ANISOU 5900 CA SER D 190 5469 4009 5049 524 1192 -1608 C ATOM 5901 C SER D 190 -5.573 55.445 51.796 1.00 40.02 C ANISOU 5901 C SER D 190 5485 4305 5414 682 1158 -1503 C ATOM 5902 O SER D 190 -4.998 54.642 51.051 1.00 37.42 O ANISOU 5902 O SER D 190 5063 4078 5077 708 1040 -1431 O ATOM 5903 CB SER D 190 -4.545 56.223 53.949 1.00 42.20 C ANISOU 5903 CB SER D 190 6123 4408 5503 387 1143 -1639 C ATOM 5904 OG SER D 190 -3.332 56.268 53.219 1.00 53.21 O ANISOU 5904 OG SER D 190 7406 5849 6964 395 980 -1533 O ATOM 5905 N SER D 191 -6.260 56.497 51.349 1.00 37.57 N ANISOU 5905 N SER D 191 5118 3925 5232 785 1281 -1488 N ATOM 5906 CA SER D 191 -6.350 56.867 49.947 1.00 37.18 C ANISOU 5906 CA SER D 191 4908 3931 5287 922 1245 -1362 C ATOM 5907 C SER D 191 -6.465 58.354 49.849 1.00 43.25 C ANISOU 5907 C SER D 191 5696 4544 6193 985 1365 -1330 C ATOM 5908 O SER D 191 -7.041 58.985 50.732 1.00 44.48 O ANISOU 5908 O SER D 191 5940 4554 6408 970 1532 -1419 O ATOM 5909 CB SER D 191 -7.545 56.198 49.279 1.00 39.45 C ANISOU 5909 CB SER D 191 5038 4345 5606 1014 1238 -1322 C ATOM 5910 OG SER D 191 -7.660 56.597 47.923 1.00 43.78 O ANISOU 5910 OG SER D 191 5462 4962 6209 1120 1172 -1183 O ATOM 5911 N ARG D 192 -5.923 58.920 48.779 1.00 39.87 N ANISOU 5911 N ARG D 192 5207 4121 5821 1051 1314 -1205 N ATOM 5912 CA ARG D 192 -6.004 60.353 48.544 1.00 40.64 C ANISOU 5912 CA ARG D 192 5321 4048 6072 1125 1434 -1141 C ATOM 5913 C ARG D 192 -6.719 60.616 47.223 1.00 44.10 C ANISOU 5913 C ARG D 192 5597 4559 6598 1298 1400 -950 C ATOM 5914 O ARG D 192 -6.636 59.809 46.293 1.00 41.43 O ANISOU 5914 O ARG D 192 5182 4407 6150 1309 1256 -874 O ATOM 5915 CB ARG D 192 -4.598 60.989 48.552 1.00 40.56 C ANISOU 5915 CB ARG D 192 5413 3943 6053 1017 1413 -1143 C ATOM 5916 N LEU D 193 -7.474 61.717 47.172 1.00 42.66 N ANISOU 5916 N LEU D 193 5373 4222 6614 1425 1536 -868 N ATOM 5917 CA LEU D 193 -8.169 62.185 45.975 1.00 43.18 C ANISOU 5917 CA LEU D 193 5282 4332 6791 1597 1483 -634 C ATOM 5918 C LEU D 193 -7.847 63.645 45.833 1.00 48.68 C ANISOU 5918 C LEU D 193 6047 4786 7662 1668 1628 -536 C ATOM 5919 O LEU D 193 -8.109 64.419 46.756 1.00 49.59 O ANISOU 5919 O LEU D 193 6234 4665 7943 1679 1843 -633 O ATOM 5920 CB LEU D 193 -9.691 61.930 46.018 1.00 44.16 C ANISOU 5920 CB LEU D 193 5205 4515 7058 1718 1492 -576 C ATOM 5921 CG LEU D 193 -10.569 62.796 45.084 1.00 51.21 C ANISOU 5921 CG LEU D 193 5913 5377 8169 1921 1466 -298 C ATOM 5922 CD1 LEU D 193 -10.402 62.411 43.615 1.00 51.00 C ANISOU 5922 CD1 LEU D 193 5832 5586 7960 1923 1199 -97 C ATOM 5923 CD2 LEU D 193 -12.014 62.732 45.483 1.00 54.57 C ANISOU 5923 CD2 LEU D 193 6111 5788 8835 2038 1540 -266 C ATOM 5924 N ARG D 194 -7.241 64.020 44.709 1.00 45.35 N ANISOU 5924 N ARG D 194 5637 4399 7194 1696 1541 -359 N ATOM 5925 CA ARG D 194 -6.873 65.409 44.503 1.00 46.71 C ANISOU 5925 CA ARG D 194 5888 4324 7537 1755 1688 -247 C ATOM 5926 C ARG D 194 -7.680 66.027 43.380 1.00 52.80 C ANISOU 5926 C ARG D 194 6529 5097 8434 1957 1636 66 C ATOM 5927 O ARG D 194 -7.812 65.449 42.297 1.00 52.63 O ANISOU 5927 O ARG D 194 6439 5313 8246 1975 1428 225 O ATOM 5928 CB ARG D 194 -5.372 65.558 44.247 1.00 45.13 C ANISOU 5928 CB ARG D 194 5832 4099 7218 1603 1678 -285 C ATOM 5929 CG ARG D 194 -4.837 66.897 44.722 1.00 53.18 C ANISOU 5929 CG ARG D 194 6985 4802 8419 1566 1888 -316 C ATOM 5930 CD ARG D 194 -3.341 66.970 44.598 1.00 54.73 C ANISOU 5930 CD ARG D 194 7283 4984 8529 1382 1872 -373 C ATOM 5931 NE ARG D 194 -2.773 68.033 45.428 1.00 56.28 N ANISOU 5931 NE ARG D 194 7624 4891 8867 1259 2052 -500 N ATOM 5932 CZ ARG D 194 -1.480 68.339 45.449 1.00 65.91 C ANISOU 5932 CZ ARG D 194 8917 6047 10080 1076 2060 -551 C ATOM 5933 NH1 ARG D 194 -0.623 67.681 44.680 1.00 46.15 N ANISOU 5933 NH1 ARG D 194 6342 3732 7463 1025 1934 -477 N ATOM 5934 NH2 ARG D 194 -1.035 69.308 46.237 1.00 52.44 N ANISOU 5934 NH2 ARG D 194 7354 4077 8494 930 2213 -684 N ATOM 5935 N VAL D 195 -8.252 67.203 43.672 1.00 51.16 N ANISOU 5935 N VAL D 195 6298 4614 8525 2102 1833 159 N ATOM 5936 CA VAL D 195 -9.065 67.991 42.757 1.00 54.03 C ANISOU 5936 CA VAL D 195 6521 4917 9093 2326 1805 500 C ATOM 5937 C VAL D 195 -8.549 69.442 42.784 1.00 60.11 C ANISOU 5937 C VAL D 195 7433 5326 10078 2378 2046 584 C ATOM 5938 O VAL D 195 -7.723 69.781 43.640 1.00 58.48 O ANISOU 5938 O VAL D 195 7416 4930 9874 2225 2235 338 O ATOM 5939 CB VAL D 195 -10.594 67.892 43.068 1.00 60.07 C ANISOU 5939 CB VAL D 195 7027 5685 10111 2506 1820 581 C ATOM 5940 CG1 VAL D 195 -11.125 66.477 42.826 1.00 58.13 C ANISOU 5940 CG1 VAL D 195 6631 5806 9651 2438 1555 539 C ATOM 5941 CG2 VAL D 195 -10.936 68.379 44.482 1.00 60.46 C ANISOU 5941 CG2 VAL D 195 7121 5433 10417 2521 2165 346 C ATOM 5942 N SER D 196 -9.012 70.285 41.842 1.00 59.39 N ANISOU 5942 N SER D 196 7261 5143 10162 2575 2024 942 N ATOM 5943 CA SER D 196 -8.629 71.699 41.811 1.00 62.08 C ANISOU 5943 CA SER D 196 7732 5105 10749 2647 2276 1056 C ATOM 5944 C SER D 196 -9.322 72.437 42.950 1.00 68.56 C ANISOU 5944 C SER D 196 8529 5572 11948 2753 2609 926 C ATOM 5945 O SER D 196 -10.410 72.021 43.370 1.00 68.58 O ANISOU 5945 O SER D 196 8330 5634 12093 2870 2611 909 O ATOM 5946 CB SER D 196 -8.987 72.331 40.471 1.00 67.98 C ANISOU 5946 CB SER D 196 8403 5857 11571 2838 2145 1515 C ATOM 5947 OG SER D 196 -10.388 72.353 40.247 1.00 79.92 O ANISOU 5947 OG SER D 196 9633 7414 13320 3080 2042 1771 O ATOM 5948 N ALA D 197 -8.699 73.513 43.462 1.00 67.77 N ANISOU 5948 N ALA D 197 8642 5092 12017 2695 2917 816 N ATOM 5949 CA ALA D 197 -9.280 74.318 44.542 1.00 70.53 C ANISOU 5949 CA ALA D 197 9036 5043 12719 2770 3306 661 C ATOM 5950 C ALA D 197 -10.714 74.730 44.208 1.00 79.20 C ANISOU 5950 C ALA D 197 9845 6027 14220 3118 3373 979 C ATOM 5951 O ALA D 197 -11.606 74.444 45.003 1.00 80.00 O ANISOU 5951 O ALA D 197 9818 6087 14491 3188 3519 842 O ATOM 5952 CB ALA D 197 -8.432 75.549 44.804 1.00 73.32 C ANISOU 5952 CB ALA D 197 9661 4986 13212 2670 3607 580 C ATOM 5953 N THR D 198 -10.947 75.304 43.000 1.00 78.90 N ANISOU 5953 N THR D 198 9684 5973 14321 3329 3238 1426 N ATOM 5954 CA THR D 198 -12.264 75.771 42.517 1.00 82.81 C ANISOU 5954 CA THR D 198 9859 6369 15235 3680 3237 1827 C ATOM 5955 C THR D 198 -13.313 74.640 42.536 1.00 86.15 C ANISOU 5955 C THR D 198 9955 7157 15621 3745 2980 1852 C ATOM 5956 O THR D 198 -14.485 74.908 42.811 1.00 88.49 O ANISOU 5956 O THR D 198 9970 7307 16346 3985 3120 1992 O ATOM 5957 CB THR D 198 -12.163 76.395 41.111 1.00 91.68 C ANISOU 5957 CB THR D 198 10944 7506 16384 3835 3028 2328 C ATOM 5958 OG1 THR D 198 -11.711 75.418 40.173 1.00 90.06 O ANISOU 5958 OG1 THR D 198 10752 7780 15687 3681 2587 2411 O ATOM 5959 CG2 THR D 198 -11.256 77.622 41.070 1.00 91.67 C ANISOU 5959 CG2 THR D 198 11240 7088 16503 3799 3328 2346 C ATOM 5960 N PHE D 199 -12.884 73.385 42.268 1.00 78.83 N ANISOU 5960 N PHE D 199 9057 6677 14215 3526 2636 1710 N ATOM 5961 CA PHE D 199 -13.761 72.212 42.288 1.00 77.89 C ANISOU 5961 CA PHE D 199 8668 6915 14012 3527 2387 1691 C ATOM 5962 C PHE D 199 -14.168 71.879 43.730 1.00 81.92 C ANISOU 5962 C PHE D 199 9174 7291 14659 3468 2696 1304 C ATOM 5963 O PHE D 199 -15.343 71.586 43.975 1.00 82.80 O ANISOU 5963 O PHE D 199 8980 7443 15038 3613 2717 1374 O ATOM 5964 CB PHE D 199 -13.093 71.005 41.611 1.00 75.99 C ANISOU 5964 CB PHE D 199 8517 7129 13226 3293 1994 1621 C ATOM 5965 CG PHE D 199 -14.034 69.866 41.298 1.00 77.37 C ANISOU 5965 CG PHE D 199 8409 7682 13307 3294 1679 1688 C ATOM 5966 CD1 PHE D 199 -14.869 69.917 40.187 1.00 83.40 C ANISOU 5966 CD1 PHE D 199 8908 8630 14149 3446 1360 2115 C ATOM 5967 CD2 PHE D 199 -14.069 68.731 42.100 1.00 76.66 C ANISOU 5967 CD2 PHE D 199 8326 7765 13036 3119 1681 1335 C ATOM 5968 CE1 PHE D 199 -15.738 68.861 39.897 1.00 84.50 C ANISOU 5968 CE1 PHE D 199 8783 9124 14199 3405 1051 2163 C ATOM 5969 CE2 PHE D 199 -14.933 67.673 41.806 1.00 79.43 C ANISOU 5969 CE2 PHE D 199 8422 8446 13310 3094 1406 1384 C ATOM 5970 CZ PHE D 199 -15.761 67.744 40.706 1.00 80.56 C ANISOU 5970 CZ PHE D 199 8295 8773 13540 3226 1091 1785 C ATOM 5971 N TRP D 200 -13.210 71.956 44.685 1.00 76.79 N ANISOU 5971 N TRP D 200 8864 6478 13835 3245 2940 912 N ATOM 5972 CA TRP D 200 -13.496 71.716 46.100 1.00 76.08 C ANISOU 5972 CA TRP D 200 8857 6240 13811 3148 3255 535 C ATOM 5973 C TRP D 200 -14.339 72.866 46.702 1.00 83.98 C ANISOU 5973 C TRP D 200 9788 6769 15353 3373 3724 575 C ATOM 5974 O TRP D 200 -15.240 72.585 47.496 1.00 84.55 O ANISOU 5974 O TRP D 200 9727 6774 15625 3428 3945 441 O ATOM 5975 CB TRP D 200 -12.209 71.507 46.922 1.00 71.79 C ANISOU 5975 CB TRP D 200 8705 5669 12903 2821 3334 139 C ATOM 5976 CG TRP D 200 -12.439 71.589 48.407 1.00 73.44 C ANISOU 5976 CG TRP D 200 9089 5637 13178 2706 3715 -229 C ATOM 5977 CD1 TRP D 200 -12.132 72.638 49.224 1.00 78.68 C ANISOU 5977 CD1 TRP D 200 10028 5877 13992 2637 4121 -427 C ATOM 5978 CD2 TRP D 200 -13.201 70.670 49.205 1.00 72.77 C ANISOU 5978 CD2 TRP D 200 8914 5684 13051 2664 3771 -414 C ATOM 5979 NE1 TRP D 200 -12.597 72.401 50.498 1.00 78.71 N ANISOU 5979 NE1 TRP D 200 10153 5754 13998 2532 4421 -744 N ATOM 5980 CE2 TRP D 200 -13.257 71.198 50.514 1.00 78.47 C ANISOU 5980 CE2 TRP D 200 9897 6060 13857 2554 4219 -731 C ATOM 5981 CE3 TRP D 200 -13.805 69.425 48.952 1.00 72.09 C ANISOU 5981 CE3 TRP D 200 8580 5969 12841 2676 3497 -358 C ATOM 5982 CZ2 TRP D 200 -13.884 70.521 51.568 1.00 77.73 C ANISOU 5982 CZ2 TRP D 200 9834 5989 13711 2464 4406 -979 C ATOM 5983 CZ3 TRP D 200 -14.431 68.759 49.994 1.00 73.29 C ANISOU 5983 CZ3 TRP D 200 8734 6134 12977 2596 3679 -598 C ATOM 5984 CH2 TRP D 200 -14.459 69.301 51.285 1.00 75.63 C ANISOU 5984 CH2 TRP D 200 9302 6091 13342 2494 4131 -897 C ATOM 5985 N GLN D 201 -14.048 74.143 46.328 1.00 82.88 N ANISOU 5985 N GLN D 201 9744 6280 15466 3501 3911 758 N ATOM 5986 CA GLN D 201 -14.752 75.334 46.835 1.00 86.97 C ANISOU 5986 CA GLN D 201 10226 6283 16537 3727 4405 808 C ATOM 5987 C GLN D 201 -16.263 75.281 46.558 1.00 95.10 C ANISOU 5987 C GLN D 201 10773 7320 18040 4065 4416 1126 C ATOM 5988 O GLN D 201 -17.030 75.884 47.311 1.00 99.13 O ANISOU 5988 O GLN D 201 11210 7447 19009 4225 4885 1058 O ATOM 5989 CB GLN D 201 -14.192 76.657 46.251 1.00 90.59 C ANISOU 5989 CB GLN D 201 10836 6386 17197 3828 4547 1029 C ATOM 5990 CG GLN D 201 -12.668 76.848 46.227 1.00 91.56 C ANISOU 5990 CG GLN D 201 11363 6504 16919 3519 4487 823 C ATOM 5991 CD GLN D 201 -11.980 77.219 47.521 1.00 95.13 C ANISOU 5991 CD GLN D 201 12214 6654 17276 3234 4870 334 C ATOM 5992 OE1 GLN D 201 -12.216 76.644 48.591 1.00 90.05 O ANISOU 5992 OE1 GLN D 201 11653 6048 16513 3085 5010 -13 O ATOM 5993 NE2 GLN D 201 -11.013 78.118 47.416 1.00 76.00 N ANISOU 5993 NE2 GLN D 201 10073 3964 14840 3104 5005 293 N ATOM 5994 N ASN D 202 -16.684 74.588 45.475 1.00 90.62 N ANISOU 5994 N ASN D 202 9879 7176 17377 4161 3913 1473 N ATOM 5995 CA ASN D 202 -18.088 74.462 45.071 1.00 93.63 C ANISOU 5995 CA ASN D 202 9748 7638 18190 4453 3810 1827 C ATOM 5996 C ASN D 202 -18.885 73.639 46.115 1.00 97.09 C ANISOU 5996 C ASN D 202 10033 8140 18716 4395 4007 1527 C ATOM 5997 O ASN D 202 -18.539 72.477 46.364 1.00 92.86 O ANISOU 5997 O ASN D 202 9607 7959 17717 4130 3785 1260 O ATOM 5998 CB ASN D 202 -18.188 73.835 43.666 1.00 92.52 C ANISOU 5998 CB ASN D 202 9375 7978 17800 4473 3171 2221 C ATOM 5999 CG ASN D 202 -19.567 73.795 43.025 1.00110.58 C ANISOU 5999 CG ASN D 202 11108 10389 20518 4757 2947 2679 C ATOM 6000 OD1 ASN D 202 -20.579 74.224 43.584 1.00103.36 O ANISOU 6000 OD1 ASN D 202 9891 9199 20182 4994 3274 2752 O ATOM 6001 ND2 ASN D 202 -19.636 73.259 41.818 1.00102.72 N ANISOU 6001 ND2 ASN D 202 9961 9819 19250 4725 2377 3003 N ATOM 6002 N PRO D 203 -19.946 74.228 46.737 1.00 97.30 N ANISOU 6002 N PRO D 203 9812 7805 19351 4641 4455 1572 N ATOM 6003 CA PRO D 203 -20.720 73.478 47.746 1.00 96.83 C ANISOU 6003 CA PRO D 203 9620 7782 19390 4578 4700 1287 C ATOM 6004 C PRO D 203 -21.610 72.378 47.149 1.00 99.90 C ANISOU 6004 C PRO D 203 9532 8639 19786 4614 4249 1512 C ATOM 6005 O PRO D 203 -22.057 71.499 47.889 1.00 98.15 O ANISOU 6005 O PRO D 203 9248 8547 19498 4482 4355 1249 O ATOM 6006 CB PRO D 203 -21.577 74.562 48.423 1.00104.06 C ANISOU 6006 CB PRO D 203 10391 8131 21017 4862 5346 1321 C ATOM 6007 CG PRO D 203 -21.055 75.878 47.922 1.00110.76 C ANISOU 6007 CG PRO D 203 11400 8614 22070 5024 5470 1543 C ATOM 6008 CD PRO D 203 -20.474 75.598 46.582 1.00104.05 C ANISOU 6008 CD PRO D 203 10507 8171 20856 4989 4807 1880 C ATOM 6009 N ARG D 204 -21.878 72.432 45.827 1.00 97.54 N ANISOU 6009 N ARG D 204 8915 8588 19557 4770 3752 1999 N ATOM 6010 CA ARG D 204 -22.704 71.453 45.112 1.00 97.72 C ANISOU 6010 CA ARG D 204 8489 9072 19567 4774 3257 2249 C ATOM 6011 C ARG D 204 -21.938 70.154 44.847 1.00 96.03 C ANISOU 6011 C ARG D 204 8527 9338 18622 4413 2830 2007 C ATOM 6012 O ARG D 204 -22.561 69.099 44.700 1.00 95.76 O ANISOU 6012 O ARG D 204 8227 9650 18506 4313 2557 2009 O ATOM 6013 CB ARG D 204 -23.210 72.042 43.788 1.00103.02 C ANISOU 6013 CB ARG D 204 8784 9829 20528 5037 2859 2868 C ATOM 6014 N ASN D 205 -20.594 70.229 44.786 1.00 87.62 N ANISOU 6014 N ASN D 205 7958 8274 17059 4215 2790 1802 N ATOM 6015 CA ASN D 205 -19.737 69.075 44.543 1.00 82.35 C ANISOU 6015 CA ASN D 205 7553 8002 15736 3894 2443 1575 C ATOM 6016 C ASN D 205 -19.717 68.154 45.768 1.00 82.92 C ANISOU 6016 C ASN D 205 7768 8104 15633 3679 2678 1113 C ATOM 6017 O ASN D 205 -19.429 68.597 46.884 1.00 81.74 O ANISOU 6017 O ASN D 205 7875 7626 15555 3642 3135 815 O ATOM 6018 CB ASN D 205 -18.327 69.515 44.133 1.00 79.30 C ANISOU 6018 CB ASN D 205 7599 7569 14963 3773 2375 1526 C ATOM 6019 CG ASN D 205 -18.208 69.861 42.663 1.00 96.99 C ANISOU 6019 CG ASN D 205 9750 9981 17123 3868 1967 1968 C ATOM 6020 OD1 ASN D 205 -18.856 69.266 41.793 1.00 92.43 O ANISOU 6020 OD1 ASN D 205 8888 9742 16489 3881 1553 2231 O ATOM 6021 ND2 ASN D 205 -17.348 70.810 42.344 1.00 86.74 N ANISOU 6021 ND2 ASN D 205 8717 8457 15782 3903 2066 2054 N ATOM 6022 N HIS D 206 -20.091 66.879 45.541 1.00 77.81 N ANISOU 6022 N HIS D 206 6959 7843 14763 3528 2364 1071 N ATOM 6023 CA HIS D 206 -20.203 65.809 46.531 1.00 75.40 C ANISOU 6023 CA HIS D 206 6740 7632 14279 3321 2505 701 C ATOM 6024 C HIS D 206 -19.083 64.787 46.352 1.00 74.78 C ANISOU 6024 C HIS D 206 7000 7837 13575 3027 2225 480 C ATOM 6025 O HIS D 206 -18.853 64.309 45.240 1.00 73.53 O ANISOU 6025 O HIS D 206 6791 7982 13165 2965 1798 654 O ATOM 6026 CB HIS D 206 -21.574 65.127 46.404 1.00 78.70 C ANISOU 6026 CB HIS D 206 6669 8240 14994 3379 2391 841 C ATOM 6027 CG HIS D 206 -21.787 63.985 47.348 1.00 80.19 C ANISOU 6027 CG HIS D 206 6922 8527 15020 3166 2534 498 C ATOM 6028 ND1 HIS D 206 -21.980 64.194 48.701 1.00 82.64 N ANISOU 6028 ND1 HIS D 206 7373 8530 15496 3159 3066 216 N ATOM 6029 CD2 HIS D 206 -21.867 62.659 47.095 1.00 79.78 C ANISOU 6029 CD2 HIS D 206 6825 8827 14661 2952 2227 412 C ATOM 6030 CE1 HIS D 206 -22.153 62.995 49.227 1.00 80.15 C ANISOU 6030 CE1 HIS D 206 7094 8400 14961 2947 3052 -11 C ATOM 6031 NE2 HIS D 206 -22.091 62.040 48.299 1.00 78.77 N ANISOU 6031 NE2 HIS D 206 6802 8611 14516 2823 2560 95 N ATOM 6032 N PHE D 207 -18.414 64.437 47.459 1.00 68.71 N ANISOU 6032 N PHE D 207 6577 6963 12566 2841 2475 105 N ATOM 6033 CA PHE D 207 -17.299 63.490 47.482 1.00 64.31 C ANISOU 6033 CA PHE D 207 6337 6619 11479 2580 2270 -113 C ATOM 6034 C PHE D 207 -17.587 62.355 48.458 1.00 67.46 C ANISOU 6034 C PHE D 207 6786 7103 11743 2403 2380 -390 C ATOM 6035 O PHE D 207 -18.012 62.614 49.586 1.00 69.05 O ANISOU 6035 O PHE D 207 7044 7070 12123 2411 2766 -563 O ATOM 6036 CB PHE D 207 -15.996 64.209 47.873 1.00 64.27 C ANISOU 6036 CB PHE D 207 6733 6402 11284 2501 2417 -263 C ATOM 6037 CG PHE D 207 -15.647 65.422 47.042 1.00 67.12 C ANISOU 6037 CG PHE D 207 7094 6616 11794 2662 2385 -11 C ATOM 6038 CD1 PHE D 207 -14.764 65.321 45.974 1.00 67.98 C ANISOU 6038 CD1 PHE D 207 7298 6909 11623 2603 2068 125 C ATOM 6039 CD2 PHE D 207 -16.179 66.673 47.345 1.00 72.54 C ANISOU 6039 CD2 PHE D 207 7706 6946 12909 2868 2714 88 C ATOM 6040 CE1 PHE D 207 -14.434 66.443 45.212 1.00 70.65 C ANISOU 6040 CE1 PHE D 207 7660 7099 12085 2740 2058 370 C ATOM 6041 CE2 PHE D 207 -15.862 67.792 46.572 1.00 76.96 C ANISOU 6041 CE2 PHE D 207 8276 7345 13621 3021 2695 344 C ATOM 6042 CZ PHE D 207 -14.985 67.672 45.516 1.00 73.49 C ANISOU 6042 CZ PHE D 207 7939 7108 12875 2950 2359 487 C ATOM 6043 N ARG D 208 -17.347 61.101 48.032 1.00 61.51 N ANISOU 6043 N ARG D 208 6041 6662 10667 2235 2072 -436 N ATOM 6044 CA ARG D 208 -17.592 59.933 48.869 1.00 59.86 C ANISOU 6044 CA ARG D 208 5888 6540 10318 2061 2151 -669 C ATOM 6045 C ARG D 208 -16.502 58.879 48.708 1.00 61.42 C ANISOU 6045 C ARG D 208 6346 6934 10058 1848 1916 -806 C ATOM 6046 O ARG D 208 -16.169 58.486 47.591 1.00 60.02 O ANISOU 6046 O ARG D 208 6121 6971 9712 1820 1596 -681 O ATOM 6047 CB ARG D 208 -18.971 59.317 48.551 1.00 60.33 C ANISOU 6047 CB ARG D 208 5533 6760 10628 2102 2068 -550 C ATOM 6048 CG ARG D 208 -19.326 58.060 49.351 1.00 63.17 C ANISOU 6048 CG ARG D 208 5929 7205 10868 1915 2161 -772 C ATOM 6049 CD ARG D 208 -20.741 57.579 49.074 1.00 78.77 C ANISOU 6049 CD ARG D 208 7459 9310 13159 1948 2113 -652 C ATOM 6050 NE ARG D 208 -20.918 57.117 47.694 1.00 87.03 N ANISOU 6050 NE ARG D 208 8284 10661 14121 1915 1651 -446 N ATOM 6051 CZ ARG D 208 -20.897 55.843 47.315 1.00 96.44 C ANISOU 6051 CZ ARG D 208 9492 12099 15052 1706 1412 -527 C ATOM 6052 NH1 ARG D 208 -20.719 54.878 48.209 1.00 81.05 N ANISOU 6052 NH1 ARG D 208 7741 10123 12931 1534 1583 -781 N ATOM 6053 NH2 ARG D 208 -21.068 55.523 46.040 1.00 81.44 N ANISOU 6053 NH2 ARG D 208 7430 10460 13052 1653 1008 -351 N ATOM 6054 N CYS D 209 -15.985 58.401 49.843 1.00 58.03 N ANISOU 6054 N CYS D 209 6194 6421 9434 1694 2089 -1054 N ATOM 6055 CA CYS D 209 -15.036 57.305 49.888 1.00 56.13 C ANISOU 6055 CA CYS D 209 6171 6332 8824 1506 1909 -1176 C ATOM 6056 C CYS D 209 -15.816 56.035 50.214 1.00 57.93 C ANISOU 6056 C CYS D 209 6294 6689 9027 1399 1911 -1260 C ATOM 6057 O CYS D 209 -16.466 55.960 51.258 1.00 58.52 O ANISOU 6057 O CYS D 209 6384 6640 9212 1371 2183 -1377 O ATOM 6058 CB CYS D 209 -13.924 57.560 50.897 1.00 56.55 C ANISOU 6058 CB CYS D 209 6585 6226 8675 1392 2041 -1349 C ATOM 6059 SG CYS D 209 -12.796 56.159 51.097 1.00 58.95 S ANISOU 6059 SG CYS D 209 7110 6689 8600 1186 1836 -1460 S ATOM 6060 N GLN D 210 -15.766 55.055 49.315 1.00 51.83 N ANISOU 6060 N GLN D 210 5434 6147 8114 1326 1638 -1210 N ATOM 6061 CA GLN D 210 -16.464 53.782 49.451 1.00 51.30 C ANISOU 6061 CA GLN D 210 5266 6207 8020 1201 1611 -1285 C ATOM 6062 C GLN D 210 -15.456 52.671 49.761 1.00 51.96 C ANISOU 6062 C GLN D 210 5629 6331 7783 1035 1546 -1423 C ATOM 6063 O GLN D 210 -14.444 52.550 49.074 1.00 49.54 O ANISOU 6063 O GLN D 210 5442 6091 7290 1017 1367 -1392 O ATOM 6064 CB GLN D 210 -17.235 53.500 48.149 1.00 54.05 C ANISOU 6064 CB GLN D 210 5305 6774 8457 1216 1346 -1124 C ATOM 6065 CG GLN D 210 -18.080 52.245 48.145 1.00 64.90 C ANISOU 6065 CG GLN D 210 6531 8286 9844 1065 1300 -1194 C ATOM 6066 CD GLN D 210 -18.841 52.117 46.851 1.00 79.11 C ANISOU 6066 CD GLN D 210 8029 10309 11719 1050 1002 -1026 C ATOM 6067 OE1 GLN D 210 -19.958 52.623 46.710 1.00 73.51 O ANISOU 6067 OE1 GLN D 210 6974 9623 11331 1143 997 -882 O ATOM 6068 NE2 GLN D 210 -18.237 51.459 45.867 1.00 68.26 N ANISOU 6068 NE2 GLN D 210 6782 9098 10054 926 748 -1032 N ATOM 6069 N VAL D 211 -15.707 51.889 50.820 1.00 48.36 N ANISOU 6069 N VAL D 211 5279 5815 7280 922 1716 -1561 N ATOM 6070 CA VAL D 211 -14.817 50.788 51.184 1.00 45.61 C ANISOU 6070 CA VAL D 211 5177 5483 6669 781 1660 -1655 C ATOM 6071 C VAL D 211 -15.633 49.500 51.224 1.00 47.86 C ANISOU 6071 C VAL D 211 5367 5848 6970 658 1678 -1713 C ATOM 6072 O VAL D 211 -16.459 49.307 52.113 1.00 48.54 O ANISOU 6072 O VAL D 211 5426 5858 7158 612 1896 -1778 O ATOM 6073 CB VAL D 211 -13.997 51.021 52.489 1.00 48.78 C ANISOU 6073 CB VAL D 211 5892 5721 6922 727 1807 -1743 C ATOM 6074 CG1 VAL D 211 -13.171 49.787 52.857 1.00 46.89 C ANISOU 6074 CG1 VAL D 211 5857 5503 6458 597 1722 -1785 C ATOM 6075 CG2 VAL D 211 -13.085 52.234 52.355 1.00 48.21 C ANISOU 6075 CG2 VAL D 211 5916 5574 6828 809 1762 -1698 C ATOM 6076 N GLN D 212 -15.400 48.634 50.237 1.00 43.35 N ANISOU 6076 N GLN D 212 4759 5415 6299 589 1475 -1699 N ATOM 6077 CA GLN D 212 -16.033 47.324 50.133 1.00 43.12 C ANISOU 6077 CA GLN D 212 4669 5452 6261 439 1472 -1768 C ATOM 6078 C GLN D 212 -15.254 46.353 51.004 1.00 44.86 C ANISOU 6078 C GLN D 212 5175 5562 6308 345 1565 -1851 C ATOM 6079 O GLN D 212 -14.066 46.139 50.781 1.00 43.04 O ANISOU 6079 O GLN D 212 5118 5311 5925 357 1467 -1836 O ATOM 6080 CB GLN D 212 -16.086 46.851 48.664 1.00 43.86 C ANISOU 6080 CB GLN D 212 4648 5722 6295 379 1228 -1736 C ATOM 6081 CG GLN D 212 -16.563 45.408 48.487 1.00 47.52 C ANISOU 6081 CG GLN D 212 5105 6233 6717 183 1224 -1838 C ATOM 6082 CD GLN D 212 -18.051 45.243 48.645 1.00 59.52 C ANISOU 6082 CD GLN D 212 6342 7815 8459 106 1277 -1846 C ATOM 6083 OE1 GLN D 212 -18.841 45.674 47.803 1.00 53.80 O ANISOU 6083 OE1 GLN D 212 5342 7243 7858 109 1110 -1759 O ATOM 6084 NE2 GLN D 212 -18.462 44.559 49.698 1.00 51.87 N ANISOU 6084 NE2 GLN D 212 5427 6733 7549 20 1500 -1934 N ATOM 6085 N PHE D 213 -15.913 45.800 52.013 1.00 41.76 N ANISOU 6085 N PHE D 213 4820 5087 5958 256 1764 -1917 N ATOM 6086 CA PHE D 213 -15.307 44.836 52.924 1.00 40.31 C ANISOU 6086 CA PHE D 213 4909 4791 5615 160 1852 -1959 C ATOM 6087 C PHE D 213 -15.763 43.450 52.545 1.00 46.14 C ANISOU 6087 C PHE D 213 5607 5558 6368 19 1852 -2013 C ATOM 6088 O PHE D 213 -16.949 43.253 52.293 1.00 47.61 O ANISOU 6088 O PHE D 213 5572 5808 6710 -53 1906 -2052 O ATOM 6089 CB PHE D 213 -15.697 45.155 54.389 1.00 42.09 C ANISOU 6089 CB PHE D 213 5277 4884 5831 129 2107 -1994 C ATOM 6090 CG PHE D 213 -15.266 44.131 55.427 1.00 41.90 C ANISOU 6090 CG PHE D 213 5542 4747 5630 9 2199 -2004 C ATOM 6091 CD1 PHE D 213 -13.919 43.922 55.708 1.00 40.70 C ANISOU 6091 CD1 PHE D 213 5627 4550 5288 20 2059 -1936 C ATOM 6092 CD2 PHE D 213 -16.211 43.402 56.145 1.00 43.68 C ANISOU 6092 CD2 PHE D 213 5790 4907 5898 -116 2428 -2058 C ATOM 6093 CE1 PHE D 213 -13.526 42.999 56.680 1.00 41.08 C ANISOU 6093 CE1 PHE D 213 5931 4493 5182 -81 2113 -1896 C ATOM 6094 CE2 PHE D 213 -15.814 42.455 57.092 1.00 45.23 C ANISOU 6094 CE2 PHE D 213 6275 4992 5919 -227 2509 -2035 C ATOM 6095 CZ PHE D 213 -14.475 42.265 57.358 1.00 41.48 C ANISOU 6095 CZ PHE D 213 6036 4477 5248 -203 2337 -1942 C ATOM 6096 N TYR D 214 -14.837 42.494 52.493 1.00 43.30 N ANISOU 6096 N TYR D 214 5442 5137 5875 -26 1800 -2011 N ATOM 6097 CA TYR D 214 -15.195 41.108 52.213 1.00 44.99 C ANISOU 6097 CA TYR D 214 5668 5325 6103 -174 1844 -2077 C ATOM 6098 C TYR D 214 -15.123 40.386 53.544 1.00 49.80 C ANISOU 6098 C TYR D 214 6498 5769 6655 -242 2028 -2062 C ATOM 6099 O TYR D 214 -14.045 40.258 54.131 1.00 49.03 O ANISOU 6099 O TYR D 214 6621 5574 6434 -189 1999 -1980 O ATOM 6100 CB TYR D 214 -14.297 40.501 51.117 1.00 46.66 C ANISOU 6100 CB TYR D 214 5940 5549 6241 -175 1705 -2087 C ATOM 6101 CG TYR D 214 -14.481 41.192 49.783 1.00 50.09 C ANISOU 6101 CG TYR D 214 6192 6158 6684 -146 1529 -2096 C ATOM 6102 CD1 TYR D 214 -15.560 40.884 48.959 1.00 53.77 C ANISOU 6102 CD1 TYR D 214 6470 6752 7208 -284 1468 -2168 C ATOM 6103 CD2 TYR D 214 -13.621 42.212 49.380 1.00 50.77 C ANISOU 6103 CD2 TYR D 214 6288 6286 6715 4 1411 -2017 C ATOM 6104 CE1 TYR D 214 -15.769 41.559 47.760 1.00 55.11 C ANISOU 6104 CE1 TYR D 214 6486 7099 7355 -270 1270 -2140 C ATOM 6105 CE2 TYR D 214 -13.806 42.877 48.168 1.00 52.34 C ANISOU 6105 CE2 TYR D 214 6346 6640 6900 27 1252 -1997 C ATOM 6106 CZ TYR D 214 -14.876 42.538 47.356 1.00 62.42 C ANISOU 6106 CZ TYR D 214 7457 8053 8207 -109 1171 -2050 C ATOM 6107 OH TYR D 214 -15.081 43.200 46.173 1.00 66.61 O ANISOU 6107 OH TYR D 214 7863 8752 8692 -101 979 -1997 O ATOM 6108 N GLY D 215 -16.296 40.053 54.069 1.00 48.13 N ANISOU 6108 N GLY D 215 6212 5534 6540 -357 2213 -2120 N ATOM 6109 CA GLY D 215 -16.436 39.430 55.375 1.00 48.80 C ANISOU 6109 CA GLY D 215 6516 5465 6560 -445 2428 -2103 C ATOM 6110 C GLY D 215 -17.079 38.069 55.343 1.00 54.36 C ANISOU 6110 C GLY D 215 7224 6094 7338 -619 2560 -2162 C ATOM 6111 O GLY D 215 -16.798 37.264 54.447 1.00 54.27 O ANISOU 6111 O GLY D 215 7192 6081 7346 -667 2462 -2198 O ATOM 6112 N LEU D 216 -17.928 37.804 56.350 1.00 52.06 N ANISOU 6112 N LEU D 216 6984 5715 7083 -729 2818 -2181 N ATOM 6113 CA LEU D 216 -18.642 36.541 56.528 1.00 58.26 C ANISOU 6113 CA LEU D 216 7787 6397 7952 -919 3001 -2233 C ATOM 6114 C LEU D 216 -19.932 36.496 55.698 1.00 97.33 C ANISOU 6114 C LEU D 216 12361 11471 13148 -1038 3018 -2353 C ATOM 6115 O LEU D 216 -20.324 37.488 55.083 1.00 65.41 O ANISOU 6115 O LEU D 216 8043 7594 9215 -955 2893 -2367 O ATOM 6116 CB LEU D 216 -18.965 36.318 58.020 1.00 59.41 C ANISOU 6116 CB LEU D 216 8173 6388 8011 -999 3293 -2186 C ATOM 6117 CG LEU D 216 -17.796 36.381 59.028 1.00 62.62 C ANISOU 6117 CG LEU D 216 8968 6686 8140 -926 3256 -2039 C ATOM 6118 CD1 LEU D 216 -18.314 36.330 60.461 1.00 64.60 C ANISOU 6118 CD1 LEU D 216 9464 6815 8267 -1041 3558 -2010 C ATOM 6119 CD2 LEU D 216 -16.792 35.251 58.811 1.00 63.97 C ANISOU 6119 CD2 LEU D 216 9322 6740 8243 -918 3126 -1935 C ATOM 6120 N ASP D 225 -22.736 38.914 69.772 1.00 90.96 N ANISOU 6120 N ASP D 225 14869 9289 10401 -2050 6593 -2370 N ATOM 6121 CA ASP D 225 -22.856 40.073 70.653 1.00 93.20 C ANISOU 6121 CA ASP D 225 15458 9490 10465 -2112 6916 -2509 C ATOM 6122 C ASP D 225 -22.981 41.352 69.812 1.00 93.72 C ANISOU 6122 C ASP D 225 15099 9635 10876 -1884 6840 -2642 C ATOM 6123 O ASP D 225 -24.017 42.022 69.851 1.00 95.38 O ANISOU 6123 O ASP D 225 15068 9755 11417 -1845 7285 -2799 O ATOM 6124 CB ASP D 225 -21.659 40.145 71.619 1.00 95.99 C ANISOU 6124 CB ASP D 225 16469 9838 10166 -2255 6687 -2395 C ATOM 6125 N ARG D 226 -21.932 41.679 69.048 1.00 85.05 N ANISOU 6125 N ARG D 226 13897 8689 9728 -1726 6295 -2563 N ATOM 6126 CA ARG D 226 -21.920 42.817 68.126 1.00 81.77 C ANISOU 6126 CA ARG D 226 13083 8358 9628 -1499 6150 -2644 C ATOM 6127 C ARG D 226 -22.476 42.332 66.781 1.00 80.86 C ANISOU 6127 C ARG D 226 12341 8367 10014 -1344 5965 -2605 C ATOM 6128 O ARG D 226 -22.592 41.120 66.585 1.00 79.68 O ANISOU 6128 O ARG D 226 12140 8241 9895 -1423 5881 -2521 O ATOM 6129 CB ARG D 226 -20.499 43.403 67.986 1.00 78.64 C ANISOU 6129 CB ARG D 226 12905 8059 8917 -1437 5675 -2576 C ATOM 6130 CG ARG D 226 -19.463 42.394 67.495 1.00 81.23 C ANISOU 6130 CG ARG D 226 13250 8512 9100 -1415 5153 -2376 C ATOM 6131 CD ARG D 226 -18.090 43.001 67.351 1.00 83.63 C ANISOU 6131 CD ARG D 226 13710 8908 9156 -1353 4709 -2301 C ATOM 6132 NE ARG D 226 -17.082 41.965 67.128 1.00 86.92 N ANISOU 6132 NE ARG D 226 14202 9401 9424 -1352 4285 -2089 N ATOM 6133 CZ ARG D 226 -16.724 41.503 65.934 1.00 89.19 C ANISOU 6133 CZ ARG D 226 14125 9791 9972 -1186 3971 -2011 C ATOM 6134 NH1 ARG D 226 -17.279 41.988 64.830 1.00 68.28 N ANISOU 6134 NH1 ARG D 226 11023 7214 7704 -1024 3980 -2114 N ATOM 6135 NH2 ARG D 226 -15.800 40.559 65.834 1.00 73.12 N ANISOU 6135 NH2 ARG D 226 12185 7779 7818 -1183 3653 -1820 N ATOM 6136 N ALA D 227 -22.816 43.258 65.861 1.00 75.32 N ANISOU 6136 N ALA D 227 11188 7738 9693 -1141 5898 -2658 N ATOM 6137 CA ALA D 227 -23.353 42.920 64.535 1.00 73.36 C ANISOU 6137 CA ALA D 227 10352 7633 9887 -1015 5679 -2615 C ATOM 6138 C ALA D 227 -22.429 41.967 63.784 1.00 73.80 C ANISOU 6138 C ALA D 227 10424 7827 9791 -1013 5180 -2495 C ATOM 6139 O ALA D 227 -21.205 42.059 63.930 1.00 71.49 O ANISOU 6139 O ALA D 227 10444 7559 9157 -992 4892 -2426 O ATOM 6140 CB ALA D 227 -23.560 44.183 63.716 1.00 73.41 C ANISOU 6140 CB ALA D 227 9972 7703 10218 -791 5595 -2639 C ATOM 6141 N LYS D 228 -23.017 41.033 63.010 1.00 69.57 N ANISOU 6141 N LYS D 228 9552 7363 9518 -1051 5099 -2474 N ATOM 6142 CA LYS D 228 -22.278 40.064 62.217 1.00 66.70 C ANISOU 6142 CA LYS D 228 9182 7095 9067 -1058 4700 -2390 C ATOM 6143 C LYS D 228 -21.365 40.816 61.240 1.00 67.09 C ANISOU 6143 C LYS D 228 9112 7288 9093 -866 4282 -2347 C ATOM 6144 O LYS D 228 -21.855 41.685 60.511 1.00 67.15 O ANISOU 6144 O LYS D 228 8757 7387 9369 -739 4236 -2378 O ATOM 6145 CB LYS D 228 -23.231 39.112 61.476 1.00 69.99 C ANISOU 6145 CB LYS D 228 9228 7559 9807 -1158 4723 -2420 C ATOM 6146 N PRO D 229 -20.031 40.575 61.276 1.00 60.08 N ANISOU 6146 N PRO D 229 8522 6407 7897 -837 3994 -2258 N ATOM 6147 CA PRO D 229 -19.128 41.314 60.371 1.00 56.27 C ANISOU 6147 CA PRO D 229 7932 6048 7401 -665 3635 -2219 C ATOM 6148 C PRO D 229 -19.165 40.728 58.952 1.00 57.21 C ANISOU 6148 C PRO D 229 7733 6295 7710 -626 3372 -2210 C ATOM 6149 O PRO D 229 -18.187 40.154 58.448 1.00 54.28 O ANISOU 6149 O PRO D 229 7460 5947 7218 -601 3117 -2147 O ATOM 6150 CB PRO D 229 -17.761 41.185 61.050 1.00 56.95 C ANISOU 6150 CB PRO D 229 8435 6079 7124 -677 3465 -2118 C ATOM 6151 CG PRO D 229 -17.854 39.936 61.865 1.00 63.19 C ANISOU 6151 CG PRO D 229 9489 6751 7770 -841 3611 -2062 C ATOM 6152 CD PRO D 229 -19.295 39.605 62.114 1.00 61.47 C ANISOU 6152 CD PRO D 229 9119 6475 7761 -955 3982 -2163 C ATOM 6153 N VAL D 230 -20.329 40.895 58.312 1.00 53.69 N ANISOU 6153 N VAL D 230 6898 5928 7573 -632 3448 -2273 N ATOM 6154 CA VAL D 230 -20.652 40.411 56.971 1.00 52.77 C ANISOU 6154 CA VAL D 230 6461 5954 7637 -651 3221 -2286 C ATOM 6155 C VAL D 230 -20.018 41.289 55.886 1.00 54.57 C ANISOU 6155 C VAL D 230 6548 6325 7861 -483 2901 -2241 C ATOM 6156 O VAL D 230 -19.573 42.401 56.171 1.00 53.84 O ANISOU 6156 O VAL D 230 6525 6218 7712 -343 2895 -2206 O ATOM 6157 CB VAL D 230 -22.194 40.323 56.774 1.00 59.00 C ANISOU 6157 CB VAL D 230 6858 6789 8769 -745 3398 -2343 C ATOM 6158 CG1 VAL D 230 -22.794 39.196 57.607 1.00 61.17 C ANISOU 6158 CG1 VAL D 230 7255 6926 9060 -950 3696 -2392 C ATOM 6159 CG2 VAL D 230 -22.886 41.654 57.080 1.00 59.61 C ANISOU 6159 CG2 VAL D 230 6718 6867 9065 -611 3574 -2333 C ATOM 6160 N THR D 231 -19.995 40.782 54.636 1.00 50.32 N ANISOU 6160 N THR D 231 5836 5915 7369 -522 2652 -2249 N ATOM 6161 CA THR D 231 -19.535 41.510 53.457 1.00 48.76 C ANISOU 6161 CA THR D 231 5496 5867 7165 -397 2357 -2202 C ATOM 6162 C THR D 231 -20.453 42.722 53.341 1.00 54.75 C ANISOU 6162 C THR D 231 5932 6701 8170 -289 2396 -2159 C ATOM 6163 O THR D 231 -21.682 42.577 53.334 1.00 57.12 O ANISOU 6163 O THR D 231 5941 7039 8723 -368 2504 -2177 O ATOM 6164 CB THR D 231 -19.529 40.578 52.238 1.00 55.92 C ANISOU 6164 CB THR D 231 6320 6879 8048 -525 2147 -2247 C ATOM 6165 OG1 THR D 231 -18.548 39.574 52.479 1.00 56.36 O ANISOU 6165 OG1 THR D 231 6698 6805 7912 -576 2171 -2270 O ATOM 6166 CG2 THR D 231 -19.209 41.298 50.931 1.00 53.17 C ANISOU 6166 CG2 THR D 231 5827 6702 7671 -434 1853 -2195 C ATOM 6167 N GLN D 232 -19.859 43.918 53.371 1.00 49.98 N ANISOU 6167 N GLN D 232 5380 6087 7523 -107 2345 -2095 N ATOM 6168 CA GLN D 232 -20.617 45.171 53.374 1.00 50.64 C ANISOU 6168 CA GLN D 232 5195 6183 7864 34 2430 -2037 C ATOM 6169 C GLN D 232 -19.798 46.337 52.832 1.00 53.52 C ANISOU 6169 C GLN D 232 5595 6576 8163 217 2251 -1951 C ATOM 6170 O GLN D 232 -18.566 46.289 52.815 1.00 51.27 O ANISOU 6170 O GLN D 232 5591 6266 7622 234 2135 -1953 O ATOM 6171 CB GLN D 232 -21.073 45.499 54.821 1.00 52.53 C ANISOU 6171 CB GLN D 232 5555 6232 8174 33 2835 -2097 C ATOM 6172 CG GLN D 232 -19.911 45.776 55.779 1.00 56.97 C ANISOU 6172 CG GLN D 232 6566 6654 8426 50 2916 -2131 C ATOM 6173 CD GLN D 232 -20.294 45.677 57.223 1.00 70.06 C ANISOU 6173 CD GLN D 232 8450 8134 10034 -43 3302 -2214 C ATOM 6174 OE1 GLN D 232 -20.342 44.590 57.811 1.00 62.24 O ANISOU 6174 OE1 GLN D 232 7639 7095 8913 -201 3404 -2251 O ATOM 6175 NE2 GLN D 232 -20.519 46.819 57.837 1.00 64.93 N ANISOU 6175 NE2 GLN D 232 7839 7366 9466 44 3542 -2244 N ATOM 6176 N ILE D 233 -20.497 47.403 52.447 1.00 52.34 N ANISOU 6176 N ILE D 233 5146 6459 8280 356 2253 -1859 N ATOM 6177 CA ILE D 233 -19.898 48.650 51.995 1.00 51.90 C ANISOU 6177 CA ILE D 233 5099 6396 8223 540 2139 -1761 C ATOM 6178 C ILE D 233 -20.021 49.663 53.154 1.00 58.42 C ANISOU 6178 C ILE D 233 6032 7004 9161 642 2485 -1801 C ATOM 6179 O ILE D 233 -21.106 49.852 53.706 1.00 60.70 O ANISOU 6179 O ILE D 233 6128 7208 9726 658 2760 -1819 O ATOM 6180 CB ILE D 233 -20.545 49.143 50.667 1.00 56.26 C ANISOU 6180 CB ILE D 233 5264 7123 8987 627 1877 -1597 C ATOM 6181 CG1 ILE D 233 -20.031 48.318 49.468 1.00 55.48 C ANISOU 6181 CG1 ILE D 233 5209 7222 8650 507 1525 -1583 C ATOM 6182 CG2 ILE D 233 -20.293 50.636 50.437 1.00 57.37 C ANISOU 6182 CG2 ILE D 233 5357 7193 9250 847 1874 -1468 C ATOM 6183 CD1 ILE D 233 -20.959 48.281 48.252 1.00 62.61 C ANISOU 6183 CD1 ILE D 233 5739 8342 9706 468 1247 -1453 C ATOM 6184 N VAL D 234 -18.886 50.245 53.555 1.00 54.05 N ANISOU 6184 N VAL D 234 5801 6348 8385 682 2491 -1831 N ATOM 6185 CA VAL D 234 -18.797 51.281 54.577 1.00 54.76 C ANISOU 6185 CA VAL D 234 6072 6224 8510 744 2792 -1894 C ATOM 6186 C VAL D 234 -18.294 52.527 53.838 1.00 57.36 C ANISOU 6186 C VAL D 234 6339 6538 8916 916 2654 -1784 C ATOM 6187 O VAL D 234 -17.308 52.447 53.096 1.00 53.00 O ANISOU 6187 O VAL D 234 5873 6092 8172 918 2362 -1727 O ATOM 6188 CB VAL D 234 -17.927 50.888 55.812 1.00 58.06 C ANISOU 6188 CB VAL D 234 6952 6527 8580 590 2916 -2027 C ATOM 6189 CG1 VAL D 234 -18.021 51.949 56.912 1.00 59.46 C ANISOU 6189 CG1 VAL D 234 7340 6475 8777 602 3268 -2126 C ATOM 6190 CG2 VAL D 234 -18.334 49.522 56.370 1.00 58.37 C ANISOU 6190 CG2 VAL D 234 7062 6594 8521 419 3002 -2092 C ATOM 6191 N SER D 235 -19.021 53.645 53.974 1.00 56.19 N ANISOU 6191 N SER D 235 6018 6248 9084 1066 2884 -1742 N ATOM 6192 CA SER D 235 -18.696 54.895 53.282 1.00 56.54 C ANISOU 6192 CA SER D 235 5981 6240 9260 1246 2796 -1613 C ATOM 6193 C SER D 235 -18.688 56.108 54.193 1.00 61.44 C ANISOU 6193 C SER D 235 6775 6570 10001 1317 3168 -1696 C ATOM 6194 O SER D 235 -19.359 56.124 55.226 1.00 63.27 O ANISOU 6194 O SER D 235 7066 6637 10336 1274 3546 -1825 O ATOM 6195 CB SER D 235 -19.695 55.155 52.155 1.00 62.17 C ANISOU 6195 CB SER D 235 6220 7075 10328 1402 2642 -1397 C ATOM 6196 OG SER D 235 -19.611 54.178 51.133 1.00 69.85 O ANISOU 6196 OG SER D 235 7070 8320 11150 1314 2263 -1322 O ATOM 6197 N ALA D 236 -17.949 57.139 53.769 1.00 57.50 N ANISOU 6197 N ALA D 236 6362 5991 9493 1417 3085 -1628 N ATOM 6198 CA ALA D 236 -17.872 58.456 54.402 1.00 59.79 C ANISOU 6198 CA ALA D 236 6810 5983 9924 1494 3416 -1693 C ATOM 6199 C ALA D 236 -17.969 59.508 53.297 1.00 64.29 C ANISOU 6199 C ALA D 236 7123 6521 10782 1725 3295 -1463 C ATOM 6200 O ALA D 236 -17.398 59.317 52.211 1.00 61.86 O ANISOU 6200 O ALA D 236 6739 6415 10349 1747 2912 -1313 O ATOM 6201 CB ALA D 236 -16.588 58.600 55.200 1.00 59.12 C ANISOU 6201 CB ALA D 236 7206 5809 9448 1307 3427 -1871 C ATOM 6202 N GLU D 237 -18.739 60.573 53.549 1.00 63.85 N ANISOU 6202 N GLU D 237 6930 6204 11125 1900 3641 -1421 N ATOM 6203 CA GLU D 237 -19.041 61.651 52.602 1.00 66.17 C ANISOU 6203 CA GLU D 237 6948 6414 11780 2155 3589 -1162 C ATOM 6204 C GLU D 237 -18.560 63.042 53.068 1.00 71.95 C ANISOU 6204 C GLU D 237 7935 6786 12617 2222 3907 -1232 C ATOM 6205 O GLU D 237 -18.386 63.287 54.265 1.00 72.15 O ANISOU 6205 O GLU D 237 8292 6579 12543 2092 4278 -1496 O ATOM 6206 CB GLU D 237 -20.567 61.723 52.364 1.00 71.57 C ANISOU 6206 CB GLU D 237 7133 7076 12984 2354 3728 -982 C ATOM 6207 CG GLU D 237 -21.185 60.488 51.723 1.00 84.17 C ANISOU 6207 CG GLU D 237 8406 9023 14552 2291 3388 -875 C ATOM 6208 CD GLU D 237 -22.685 60.548 51.483 1.00114.88 C ANISOU 6208 CD GLU D 237 11753 12913 18983 2463 3485 -679 C ATOM 6209 OE1 GLU D 237 -23.390 61.276 52.220 1.00113.88 O ANISOU 6209 OE1 GLU D 237 11527 12480 19262 2602 3958 -712 O ATOM 6210 OE2 GLU D 237 -23.156 59.856 50.551 1.00111.00 O ANISOU 6210 OE2 GLU D 237 10930 12723 18519 2446 3092 -493 O ATOM 6211 N ALA D 238 -18.413 63.963 52.093 1.00 69.73 N ANISOU 6211 N ALA D 238 7503 6451 12542 2416 3771 -985 N ATOM 6212 CA ALA D 238 -18.009 65.372 52.245 1.00 70.96 C ANISOU 6212 CA ALA D 238 7839 6255 12869 2515 4038 -984 C ATOM 6213 C ALA D 238 -18.563 66.195 51.079 1.00 75.39 C ANISOU 6213 C ALA D 238 8021 6772 13853 2820 3922 -600 C ATOM 6214 O ALA D 238 -18.660 65.675 49.964 1.00 73.59 O ANISOU 6214 O ALA D 238 7538 6859 13565 2869 3482 -352 O ATOM 6215 CB ALA D 238 -16.488 65.482 52.288 1.00 68.89 C ANISOU 6215 CB ALA D 238 7991 6019 12164 2308 3861 -1121 C ATOM 6216 N TRP D 239 -18.916 67.471 51.321 1.00 74.83 N ANISOU 6216 N TRP D 239 7932 6301 14197 3013 4315 -543 N ATOM 6217 CA TRP D 239 -19.462 68.343 50.279 1.00 89.73 C ANISOU 6217 CA TRP D 239 9462 8100 16533 3326 4231 -138 C ATOM 6218 C TRP D 239 -18.463 69.416 49.844 1.00105.79 C ANISOU 6218 C TRP D 239 11758 9933 18505 3354 4220 -62 C ATOM 6219 O TRP D 239 -17.627 69.848 50.630 1.00 67.93 O ANISOU 6219 O TRP D 239 7389 4911 13512 3180 4476 -355 O ATOM 6220 CB TRP D 239 -20.776 68.987 50.742 1.00 93.27 C ANISOU 6220 CB TRP D 239 9592 8220 17627 3586 4697 -49 C ATOM 6221 CG TRP D 239 -21.926 68.029 50.730 1.00 95.04 C ANISOU 6221 CG TRP D 239 9385 8684 18041 3626 4607 31 C ATOM 6222 CD1 TRP D 239 -22.317 67.205 51.744 1.00 97.39 C ANISOU 6222 CD1 TRP D 239 9751 9012 18241 3457 4851 -267 C ATOM 6223 CD2 TRP D 239 -22.787 67.739 49.621 1.00 96.55 C ANISOU 6223 CD2 TRP D 239 9025 9145 18513 3811 4208 442 C ATOM 6224 NE1 TRP D 239 -23.388 66.440 51.347 1.00 98.11 N ANISOU 6224 NE1 TRP D 239 9346 9353 18578 3532 4662 -79 N ATOM 6225 CE2 TRP D 239 -23.701 66.749 50.048 1.00100.99 C ANISOU 6225 CE2 TRP D 239 9316 9878 19177 3740 4249 355 C ATOM 6226 CE3 TRP D 239 -22.883 68.227 48.306 1.00 99.35 C ANISOU 6226 CE3 TRP D 239 9101 9618 19031 4009 3808 887 C ATOM 6227 CZ2 TRP D 239 -24.704 66.245 49.212 1.00102.39 C ANISOU 6227 CZ2 TRP D 239 8930 10342 19633 3849 3893 684 C ATOM 6228 CZ3 TRP D 239 -23.883 67.733 47.481 1.00103.06 C ANISOU 6228 CZ3 TRP D 239 9032 10381 19745 4119 3437 1227 C ATOM 6229 CH2 TRP D 239 -24.775 66.750 47.932 1.00104.18 C ANISOU 6229 CH2 TRP D 239 8890 10694 19999 4031 3471 1118 C TER 6230 TRP D 239 HETATM 6231 C4 2LJ A 301 7.032 9.222 24.759 1.00 13.41 C HETATM 6232 C6 2LJ A 301 8.682 9.372 27.247 1.00 15.90 C HETATM 6233 C7 2LJ A 301 9.592 9.439 28.438 1.00 17.20 C HETATM 6234 C8 2LJ A 301 10.677 10.490 28.454 1.00 16.28 C HETATM 6235 N1 2LJ A 301 7.566 11.411 23.098 1.00 12.19 N HETATM 6236 N3 2LJ A 301 6.440 9.426 23.525 1.00 14.24 N HETATM 6237 N5 2LJ A 301 8.729 10.267 26.299 1.00 17.70 N HETATM 6238 C4A 2LJ A 301 7.953 10.269 25.142 1.00 15.59 C HETATM 6239 O4 2LJ A 301 6.770 8.208 25.411 1.00 15.77 O HETATM 6240 C2 2LJ A 301 6.662 10.473 22.671 1.00 13.31 C HETATM 6241 O2 2LJ A 301 6.108 10.551 21.574 1.00 14.61 O HETATM 6242 C8A 2LJ A 301 8.204 11.378 24.302 1.00 14.11 C HETATM 6243 N8 2LJ A 301 9.179 12.282 24.644 1.00 13.61 N HETATM 6244 C1' 2LJ A 301 9.862 13.176 23.722 1.00 15.61 C HETATM 6245 C2' 2LJ A 301 9.261 14.617 23.649 1.00 14.32 C HETATM 6246 O2' 2LJ A 301 9.316 15.175 24.964 1.00 14.83 O HETATM 6247 C3' 2LJ A 301 7.848 14.657 23.063 1.00 12.33 C HETATM 6248 O3' 2LJ A 301 7.788 13.902 21.845 1.00 15.83 O HETATM 6249 C4' 2LJ A 301 7.337 16.071 22.786 1.00 12.43 C HETATM 6250 O4' 2LJ A 301 5.994 15.964 22.297 1.00 12.62 O HETATM 6251 C5' 2LJ A 301 8.240 16.812 21.738 1.00 14.66 C HETATM 6252 O5' 2LJ A 301 7.663 18.042 21.319 1.00 19.01 O HETATM 6253 C1 GOL A 302 21.598 5.236 13.395 1.00 56.33 C HETATM 6254 O1 GOL A 302 20.887 6.464 13.483 1.00 57.15 O HETATM 6255 C2 GOL A 302 22.026 4.755 14.762 1.00 54.70 C HETATM 6256 O2 GOL A 302 20.875 4.590 15.592 1.00 50.92 O HETATM 6257 C3 GOL A 302 22.742 3.430 14.627 1.00 56.37 C HETATM 6258 O3 GOL A 302 23.214 2.978 15.888 1.00 56.73 O HETATM 6259 C1 GOL A 303 16.163 -15.799 6.739 1.00 65.93 C HETATM 6260 O1 GOL A 303 15.543 -16.579 5.721 1.00 67.42 O HETATM 6261 C2 GOL A 303 17.649 -15.658 6.494 1.00 62.75 C HETATM 6262 O2 GOL A 303 18.242 -16.951 6.376 1.00 63.61 O HETATM 6263 C3 GOL A 303 17.891 -14.879 5.224 1.00 59.79 C HETATM 6264 O3 GOL A 303 18.090 -13.508 5.511 1.00 57.97 O HETATM 6265 NA NA B 101 -5.965 -11.979 4.919 1.00 60.82 NA1+ HETATM 6266 O HOH A 401 -3.222 27.583 15.182 1.00 57.56 O HETATM 6267 O HOH A 402 42.107 -11.782 -0.765 1.00 51.43 O HETATM 6268 O HOH A 403 35.188 -19.407 9.272 1.00 39.51 O HETATM 6269 O HOH A 404 39.834 -0.251 14.485 1.00 29.94 O HETATM 6270 O HOH A 405 24.909 -2.794 5.554 1.00 58.27 O HETATM 6271 O HOH A 406 -10.894 11.908 0.622 1.00 44.13 O HETATM 6272 O HOH A 407 36.364 -16.221 10.044 1.00 40.49 O HETATM 6273 O HOH A 408 -6.378 25.194 9.662 1.00 48.85 O HETATM 6274 O HOH A 409 16.458 -5.666 2.313 1.00 43.99 O HETATM 6275 O HOH A 410 19.901 -9.261 -2.163 1.00 36.46 O HETATM 6276 O HOH A 411 36.254 -2.740 17.118 1.00 33.83 O HETATM 6277 O HOH A 412 29.206 -4.382 -1.909 1.00 70.52 O HETATM 6278 O HOH A 413 31.820 -12.224 19.256 1.00 32.51 O HETATM 6279 O HOH A 414 35.485 -10.947 13.943 1.00 33.78 O HETATM 6280 O HOH A 415 41.901 -19.539 2.999 1.00 52.52 O HETATM 6281 O HOH A 416 19.668 -5.491 6.172 1.00 38.35 O HETATM 6282 O HOH A 417 22.304 -12.958 -8.000 1.00 54.58 O HETATM 6283 O HOH A 418 34.902 -20.521 6.515 1.00 30.95 O HETATM 6284 O HOH A 419 23.959 -8.002 4.349 1.00 45.08 O HETATM 6285 O HOH A 420 26.940 -7.071 -6.527 1.00 34.06 O HETATM 6286 O HOH A 421 -14.191 9.642 0.942 1.00 62.52 O HETATM 6287 O HOH A 422 -7.908 21.695 11.237 1.00 56.74 O HETATM 6288 O HOH A 423 32.829 -9.111 22.959 1.00 51.98 O HETATM 6289 O HOH A 424 17.432 -12.255 0.991 1.00 62.46 O HETATM 6290 O HOH A 425 -8.867 10.115 0.257 1.00 54.38 O HETATM 6291 O HOH A 426 -6.237 16.196 0.265 1.00 34.50 O HETATM 6292 O HOH A 427 -13.334 5.677 4.476 1.00 49.12 O HETATM 6293 O HOH A 428 19.403 -13.515 -7.668 1.00 43.70 O HETATM 6294 O HOH A 429 26.103 -5.888 3.853 1.00 36.66 O HETATM 6295 O HOH A 430 41.167 -9.466 -1.085 1.00 45.33 O HETATM 6296 O HOH A 431 -12.049 18.826 9.991 1.00 49.73 O HETATM 6297 O HOH A 432 17.927 -8.603 -0.356 1.00 55.59 O HETATM 6298 O HOH A 433 26.880 -4.322 1.767 1.00 64.92 O HETATM 6299 O HOH A 434 -14.743 17.616 3.777 1.00 73.31 O HETATM 6300 O HOH A 435 43.162 -19.364 0.576 1.00 59.95 O HETATM 6301 O HOH A 436 34.192 -17.893 13.352 1.00 37.97 O HETATM 6302 O HOH A 437 35.476 -6.038 20.050 1.00 56.42 O HETATM 6303 O HOH A 438 32.127 -19.368 12.423 1.00 36.91 O HETATM 6304 O HOH A 439 30.466 -20.861 16.800 1.00 70.40 O HETATM 6305 O HOH A 440 35.598 -8.019 13.728 1.00 27.28 O HETATM 6306 O HOH A 441 6.427 10.839 18.910 1.00 13.42 O HETATM 6307 O HOH A 442 29.528 3.535 21.090 1.00 14.77 O HETATM 6308 O HOH A 443 6.945 5.577 25.469 1.00 17.31 O HETATM 6309 O HOH A 444 11.870 16.378 10.184 1.00 17.84 O HETATM 6310 O HOH A 445 11.165 14.092 26.565 1.00 15.54 O HETATM 6311 O HOH A 446 13.111 12.146 26.097 1.00 16.21 O HETATM 6312 O HOH A 447 -2.052 15.615 34.813 1.00 16.36 O HETATM 6313 O HOH A 448 -0.449 6.308 9.602 1.00 20.09 O HETATM 6314 O HOH A 449 12.428 17.306 27.418 1.00 16.78 O HETATM 6315 O HOH A 450 33.954 -6.044 14.992 1.00 19.77 O HETATM 6316 O HOH A 451 15.882 16.945 30.241 1.00 27.92 O HETATM 6317 O HOH A 452 -0.177 13.793 20.660 1.00 20.44 O HETATM 6318 O HOH A 453 20.358 18.962 15.036 1.00 20.94 O HETATM 6319 O HOH A 454 2.700 0.715 29.376 1.00 19.00 O HETATM 6320 O HOH A 455 8.728 -2.044 20.165 1.00 19.22 O HETATM 6321 O HOH A 456 5.642 17.877 35.067 1.00 35.78 O HETATM 6322 O HOH A 457 23.624 -13.962 16.162 1.00 22.38 O HETATM 6323 O HOH A 458 4.691 18.243 22.859 1.00 20.97 O HETATM 6324 O HOH A 459 -5.945 10.210 28.296 1.00 21.94 O HETATM 6325 O HOH A 460 18.841 -10.104 18.770 1.00 24.65 O HETATM 6326 O HOH A 461 0.216 16.235 27.877 1.00 16.30 O HETATM 6327 O HOH A 462 27.206 9.315 19.157 1.00 25.48 O HETATM 6328 O HOH A 463 2.690 16.392 21.506 1.00 20.17 O HETATM 6329 O HOH A 464 -5.646 8.095 21.389 1.00 20.13 O HETATM 6330 O HOH A 465 -7.061 5.135 27.890 1.00 21.44 O HETATM 6331 O HOH A 466 2.630 -0.247 26.685 1.00 22.96 O HETATM 6332 O HOH A 467 24.781 -17.623 10.574 1.00 26.00 O HETATM 6333 O HOH A 468 22.811 14.792 28.980 1.00 18.50 O HETATM 6334 O HOH A 469 -9.795 9.259 16.643 1.00 24.61 O HETATM 6335 O HOH A 470 18.679 17.602 11.078 1.00 26.74 O HETATM 6336 O HOH A 471 17.846 18.023 28.902 1.00 23.21 O HETATM 6337 O HOH A 472 4.227 4.299 35.144 1.00 21.25 O HETATM 6338 O HOH A 473 24.006 -15.628 8.763 1.00 25.85 O HETATM 6339 O HOH A 474 35.063 -7.301 10.940 1.00 26.38 O HETATM 6340 O HOH A 475 -7.638 1.570 23.984 1.00 23.86 O HETATM 6341 O HOH A 476 29.735 -17.955 10.975 1.00 27.67 O HETATM 6342 O HOH A 477 28.996 4.904 13.671 1.00 29.50 O HETATM 6343 O HOH A 478 4.116 19.059 39.097 1.00 25.95 O HETATM 6344 O HOH A 479 14.956 19.955 9.441 1.00 38.22 O HETATM 6345 O HOH A 480 -8.312 7.107 17.855 1.00 27.61 O HETATM 6346 O HOH A 481 14.559 17.257 10.008 1.00 30.92 O HETATM 6347 O HOH A 482 18.997 24.974 19.341 1.00 27.81 O HETATM 6348 O HOH A 483 17.678 23.851 25.605 1.00 23.08 O HETATM 6349 O HOH A 484 28.258 7.309 27.851 1.00 28.55 O HETATM 6350 O HOH A 485 21.773 -5.948 22.494 1.00 25.29 O HETATM 6351 O HOH A 486 4.164 5.022 14.650 1.00 26.76 O HETATM 6352 O HOH A 487 19.409 17.293 16.905 1.00 25.43 O HETATM 6353 O HOH A 488 11.044 9.846 42.481 1.00 27.09 O HETATM 6354 O HOH A 489 9.610 -4.585 20.620 1.00 28.18 O HETATM 6355 O HOH A 490 -7.027 10.891 30.892 1.00 27.41 O HETATM 6356 O HOH A 491 0.327 15.013 17.850 1.00 23.38 O HETATM 6357 O HOH A 492 22.037 19.145 24.327 1.00 25.87 O HETATM 6358 O HOH A 493 20.149 -12.937 7.162 1.00 27.54 O HETATM 6359 O HOH A 494 23.972 16.956 27.827 1.00 27.20 O HETATM 6360 O HOH A 495 4.046 22.549 2.182 1.00 29.94 O HETATM 6361 O HOH A 496 32.475 -4.523 24.191 1.00 26.24 O HETATM 6362 O HOH A 497 20.588 -18.638 11.039 1.00 38.76 O HETATM 6363 O HOH A 498 3.134 31.699 18.924 1.00 39.03 O HETATM 6364 O HOH A 499 37.651 -18.828 -4.985 1.00 36.63 O HETATM 6365 O HOH A 500 24.537 -1.768 7.917 1.00 32.01 O HETATM 6366 O HOH A 501 30.309 -1.027 26.789 1.00 35.23 O HETATM 6367 O HOH A 502 -11.533 16.281 16.439 1.00 29.53 O HETATM 6368 O HOH A 503 24.001 17.651 25.338 1.00 26.52 O HETATM 6369 O HOH A 504 24.501 -0.275 31.188 1.00 30.74 O HETATM 6370 O HOH A 505 11.944 14.137 8.793 1.00 28.23 O HETATM 6371 O HOH A 506 1.695 13.198 40.815 1.00 32.04 O HETATM 6372 O HOH A 507 12.999 -17.258 5.310 1.00 38.35 O HETATM 6373 O HOH A 508 -4.242 2.744 7.883 1.00 31.23 O HETATM 6374 O HOH A 509 0.075 16.458 21.151 1.00 33.10 O HETATM 6375 O HOH A 510 22.232 19.873 18.188 1.00 28.75 O HETATM 6376 O HOH A 511 15.314 -2.973 25.116 1.00 34.75 O HETATM 6377 O HOH A 512 12.775 18.375 6.965 1.00 34.12 O HETATM 6378 O HOH A 513 3.518 19.884 36.428 1.00 29.83 O HETATM 6379 O HOH A 514 -7.592 7.572 23.313 1.00 33.02 O HETATM 6380 O HOH A 515 4.311 6.168 37.037 1.00 29.28 O HETATM 6381 O HOH A 516 23.536 9.500 32.400 1.00 31.04 O HETATM 6382 O HOH A 517 33.304 0.150 10.412 1.00 48.41 O HETATM 6383 O HOH A 518 23.232 -2.604 30.141 1.00 34.45 O HETATM 6384 O HOH A 519 -3.283 9.928 37.893 1.00 32.61 O HETATM 6385 O HOH A 520 2.473 10.903 1.224 1.00 32.78 O HETATM 6386 O HOH A 521 21.275 -15.028 8.446 1.00 26.04 O HETATM 6387 O HOH A 522 17.749 -5.918 12.044 1.00 43.33 O HETATM 6388 O HOH A 523 1.717 7.061 37.437 1.00 29.84 O HETATM 6389 O HOH A 524 39.796 -11.651 -3.932 1.00 36.37 O HETATM 6390 O HOH A 525 15.320 10.212 37.658 1.00 34.96 O HETATM 6391 O HOH A 526 -8.201 9.708 24.817 1.00 32.44 O HETATM 6392 O HOH A 527 26.029 1.522 18.146 1.00 35.57 O HETATM 6393 O HOH A 528 -1.790 0.053 34.316 1.00 41.89 O HETATM 6394 O HOH A 529 29.115 0.452 13.772 1.00 33.58 O HETATM 6395 O HOH A 530 17.700 9.777 36.904 1.00 38.02 O HETATM 6396 O HOH A 531 -5.412 16.940 12.809 1.00 32.82 O HETATM 6397 O HOH A 532 25.410 19.456 13.865 1.00 41.57 O HETATM 6398 O HOH A 533 -2.679 7.353 38.006 1.00 41.29 O HETATM 6399 O HOH A 534 5.229 7.994 2.774 1.00 35.96 O HETATM 6400 O HOH A 535 -11.158 9.002 14.301 1.00 31.67 O HETATM 6401 O HOH A 536 32.798 -1.123 22.061 1.00 42.78 O HETATM 6402 O HOH A 537 8.677 23.252 4.630 1.00 43.94 O HETATM 6403 O HOH A 538 26.714 1.224 14.623 1.00 36.12 O HETATM 6404 O HOH A 539 -5.938 5.820 34.446 1.00 45.59 O HETATM 6405 O HOH A 540 -2.524 2.085 18.638 1.00 34.64 O HETATM 6406 O HOH A 541 12.451 -3.404 31.759 1.00 49.38 O HETATM 6407 O HOH A 542 -2.803 16.568 12.288 1.00 29.82 O HETATM 6408 O HOH A 543 4.222 22.492 15.095 1.00 36.29 O HETATM 6409 O HOH A 544 24.010 -10.455 23.559 1.00 45.85 O HETATM 6410 O HOH A 545 6.110 5.982 38.976 1.00 35.40 O HETATM 6411 O HOH A 546 17.198 -11.696 3.923 1.00 38.06 O HETATM 6412 O HOH A 547 -6.534 8.392 34.502 1.00 48.72 O HETATM 6413 O HOH A 548 24.078 0.634 19.678 1.00 36.25 O HETATM 6414 O HOH A 549 -5.834 7.512 18.794 1.00 30.08 O HETATM 6415 O AHOH A 550 -1.039 10.917 4.459 0.50 21.50 O HETATM 6416 O BHOH A 550 -2.660 11.521 3.413 0.50 21.92 O HETATM 6417 O HOH A 551 24.730 13.192 30.081 1.00 39.43 O HETATM 6418 O HOH A 552 6.446 28.596 9.405 1.00 40.60 O HETATM 6419 O HOH A 553 0.070 24.518 17.229 1.00 56.83 O HETATM 6420 O HOH A 554 17.599 -8.012 19.303 1.00 44.51 O HETATM 6421 O HOH A 555 6.968 2.407 36.317 1.00 50.64 O HETATM 6422 O HOH A 556 20.968 -7.149 24.543 1.00 40.81 O HETATM 6423 O HOH A 557 11.615 4.114 39.177 1.00 38.31 O HETATM 6424 O HOH A 558 15.678 -5.622 16.253 1.00 43.45 O HETATM 6425 O HOH A 559 7.281 20.098 42.158 1.00 35.66 O HETATM 6426 O HOH A 560 3.729 12.869 42.433 1.00 39.04 O HETATM 6427 O HOH A 561 30.581 -0.872 9.630 1.00 48.85 O HETATM 6428 O HOH A 562 14.270 12.419 8.726 1.00 43.27 O HETATM 6429 O HOH A 563 29.336 11.075 19.097 1.00 37.25 O HETATM 6430 O HOH A 564 10.833 11.978 5.571 1.00 46.18 O HETATM 6431 O HOH A 565 3.449 31.212 24.050 1.00 40.70 O HETATM 6432 O HOH A 566 8.878 30.270 10.304 1.00 47.64 O HETATM 6433 O HOH A 567 3.560 17.856 19.124 1.00 46.64 O HETATM 6434 O HOH A 568 21.385 6.782 37.748 1.00 43.77 O HETATM 6435 O HOH A 569 18.763 2.166 14.892 1.00 42.60 O HETATM 6436 O HOH A 570 29.325 -4.816 27.801 1.00 36.07 O HETATM 6437 O HOH A 571 29.096 -0.491 7.410 1.00 55.03 O HETATM 6438 O HOH A 572 -2.798 -0.256 17.967 1.00 44.67 O HETATM 6439 O HOH A 573 10.134 19.596 5.793 1.00 39.66 O HETATM 6440 O HOH A 574 2.102 28.459 21.725 1.00 35.62 O HETATM 6441 O HOH A 575 19.233 -3.782 11.671 1.00 45.83 O HETATM 6442 O HOH A 576 4.676 5.155 3.026 1.00 49.73 O HETATM 6443 O HOH A 577 21.391 16.156 30.907 1.00 32.26 O HETATM 6444 O HOH A 578 31.849 4.245 23.507 1.00 42.38 O HETATM 6445 O HOH A 579 26.327 17.528 20.989 1.00 47.42 O HETATM 6446 O HOH A 580 19.025 20.837 10.684 1.00 47.94 O HETATM 6447 O HOH A 581 14.418 -3.431 17.409 1.00 37.00 O HETATM 6448 O HOH A 582 -5.231 16.339 25.758 1.00 38.73 O HETATM 6449 O HOH A 583 23.135 1.377 34.432 1.00 38.01 O HETATM 6450 O HOH A 584 -8.379 10.664 27.266 1.00 42.87 O HETATM 6451 O HOH A 585 12.036 -4.738 25.397 1.00 45.46 O HETATM 6452 O HOH A 586 31.139 2.242 13.782 1.00 56.64 O HETATM 6453 O HOH A 587 24.007 -15.919 -5.209 1.00 43.06 O HETATM 6454 O HOH A 588 18.112 -2.904 25.777 1.00 44.23 O HETATM 6455 O HOH A 589 -13.863 5.897 12.932 1.00 42.46 O HETATM 6456 O HOH A 590 8.703 7.981 5.316 1.00 54.58 O HETATM 6457 O HOH A 591 -13.617 -0.273 17.981 1.00 49.11 O HETATM 6458 O HOH A 592 3.976 36.898 21.954 1.00 47.88 O HETATM 6459 O HOH A 593 -17.301 8.541 4.226 1.00 58.55 O HETATM 6460 O HOH A 594 -9.841 8.904 29.288 1.00 67.73 O HETATM 6461 O HOH A 595 1.435 23.200 0.960 1.00 41.02 O HETATM 6462 O HOH A 596 34.976 -4.652 22.795 1.00 51.28 O HETATM 6463 O HOH A 597 30.481 10.913 12.107 1.00 51.13 O HETATM 6464 O HOH A 598 -3.160 -3.385 31.648 1.00 48.28 O HETATM 6465 O HOH A 599 21.028 19.144 11.506 1.00 48.41 O HETATM 6466 O HOH A 600 6.981 12.780 1.404 1.00 42.51 O HETATM 6467 O HOH A 601 20.501 0.038 14.750 1.00 46.11 O HETATM 6468 O HOH A 602 32.441 0.912 25.469 1.00 63.16 O HETATM 6469 O HOH A 603 -15.341 11.197 9.553 1.00 46.79 O HETATM 6470 O HOH A 604 19.536 26.964 12.755 1.00 52.86 O HETATM 6471 O HOH A 605 -0.729 15.551 -3.365 1.00 57.32 O HETATM 6472 O HOH A 606 24.204 13.383 8.908 1.00 52.99 O HETATM 6473 O HOH A 607 26.749 16.849 28.395 1.00 56.07 O HETATM 6474 O HOH A 608 2.962 -2.946 27.447 1.00 62.89 O HETATM 6475 O HOH A 609 -12.889 0.124 9.064 1.00 58.80 O HETATM 6476 O HOH A 610 -2.785 8.803 3.388 1.00 44.07 O HETATM 6477 O HOH A 611 34.558 -1.350 18.730 1.00 47.57 O HETATM 6478 O HOH A 612 21.616 21.998 15.366 1.00 64.03 O HETATM 6479 O HOH A 613 28.596 16.782 20.009 1.00 52.77 O HETATM 6480 O HOH A 614 -6.403 1.290 8.475 1.00 53.66 O HETATM 6481 O HOH A 615 21.401 20.825 26.364 1.00 51.68 O HETATM 6482 O HOH A 616 -12.959 15.659 19.169 1.00 50.74 O HETATM 6483 O HOH A 617 5.572 28.191 4.986 1.00 58.43 O HETATM 6484 O HOH A 618 -7.047 20.396 18.108 1.00 59.38 O HETATM 6485 O HOH A 619 4.558 21.043 -0.739 1.00 56.57 O HETATM 6486 O HOH A 620 15.948 23.584 4.585 1.00 49.84 O HETATM 6487 O HOH A 621 -12.240 13.051 19.899 1.00 43.89 O HETATM 6488 O HOH A 622 24.709 8.064 34.799 1.00 43.63 O HETATM 6489 O HOH A 623 -11.694 10.541 25.289 1.00 47.75 O HETATM 6490 O HOH A 624 0.820 -2.522 23.727 1.00 42.84 O HETATM 6491 O HOH A 625 -12.074 5.184 17.861 1.00 48.70 O HETATM 6492 O HOH A 626 21.422 -16.406 -2.484 1.00 38.39 O HETATM 6493 O HOH A 627 -7.323 -4.506 30.093 1.00 60.77 O HETATM 6494 O HOH A 628 25.672 19.608 10.778 1.00 63.65 O HETATM 6495 O HOH A 629 30.056 -20.213 13.921 1.00 46.96 O HETATM 6496 O HOH A 630 -10.770 1.557 6.947 1.00 56.82 O HETATM 6497 O HOH A 631 1.469 29.299 7.031 1.00 50.22 O HETATM 6498 O HOH A 632 24.291 5.083 35.127 1.00 47.01 O HETATM 6499 O HOH A 633 19.544 -4.996 27.378 1.00 66.95 O HETATM 6500 O HOH A 634 26.675 9.534 27.114 1.00 24.15 O HETATM 6501 O HOH A 635 -6.210 7.178 3.391 1.00 33.97 O HETATM 6502 O HOH A 636 -14.162 12.187 12.064 1.00 34.20 O HETATM 6503 O HOH A 637 -1.145 -3.125 26.918 1.00 37.44 O HETATM 6504 O HOH A 638 22.858 0.365 16.361 1.00 40.56 O HETATM 6505 O HOH A 639 -3.292 3.238 35.160 1.00 51.36 O HETATM 6506 O HOH A 640 15.454 14.840 34.562 1.00 42.01 O HETATM 6507 O HOH A 641 -3.565 20.002 16.015 1.00 51.95 O HETATM 6508 O HOH A 642 11.143 21.464 3.911 1.00 43.54 O HETATM 6509 O HOH A 643 -10.620 15.198 26.831 1.00 38.39 O HETATM 6510 O HOH A 644 32.446 -13.037 -10.653 1.00 47.13 O HETATM 6511 O HOH A 645 8.416 3.531 39.066 1.00 51.98 O HETATM 6512 O HOH A 646 13.680 9.658 9.214 1.00 53.57 O HETATM 6513 O HOH A 647 -12.440 9.401 18.103 1.00 50.14 O HETATM 6514 O HOH A 648 4.622 12.164 0.020 1.00 49.83 O HETATM 6515 O HOH A 649 3.791 20.667 21.682 1.00 47.58 O HETATM 6516 O HOH A 650 20.670 23.839 12.599 1.00 58.77 O HETATM 6517 O HOH A 651 11.328 24.871 3.812 1.00 51.07 O HETATM 6518 O HOH A 652 22.754 -20.130 9.697 1.00 54.75 O HETATM 6519 O HOH A 653 23.212 19.872 21.915 1.00 50.08 O HETATM 6520 O HOH A 654 16.588 -6.211 8.280 1.00 47.06 O HETATM 6521 O HOH A 655 16.390 -4.795 20.542 1.00 40.95 O HETATM 6522 O HOH A 656 16.369 28.028 12.019 1.00 50.25 O HETATM 6523 O HOH A 657 33.150 10.215 11.962 1.00 59.74 O HETATM 6524 O HOH A 658 13.125 12.507 37.840 1.00 52.27 O HETATM 6525 O HOH A 659 25.914 3.325 33.620 1.00 59.56 O HETATM 6526 O HOH A 660 33.431 1.952 15.334 1.00 57.57 O HETATM 6527 O HOH A 661 22.707 11.206 9.551 1.00 53.48 O HETATM 6528 O HOH A 662 14.247 -6.786 6.840 1.00 53.29 O HETATM 6529 O HOH A 663 13.963 -13.015 21.430 1.00 74.03 O HETATM 6530 O HOH A 664 32.760 -6.829 -11.536 1.00 65.62 O HETATM 6531 O HOH A 665 12.798 11.965 41.996 1.00 56.68 O HETATM 6532 O HOH A 666 -16.644 14.975 6.627 1.00 51.90 O HETATM 6533 O HOH A 667 31.495 -9.895 -11.408 1.00 50.88 O HETATM 6534 O HOH A 668 -11.210 12.731 27.321 1.00 57.84 O HETATM 6535 O HOH A 669 20.334 25.966 15.554 1.00 52.12 O HETATM 6536 O HOH A 670 -8.694 1.242 27.634 1.00 52.81 O HETATM 6537 O HOH A 671 -0.589 18.062 19.195 1.00 50.96 O HETATM 6538 O HOH A 672 -7.620 -2.645 14.844 1.00 51.01 O HETATM 6539 O HOH A 673 15.792 -5.089 27.325 1.00 53.20 O HETATM 6540 O HOH A 674 -14.420 6.879 21.244 1.00 63.95 O HETATM 6541 O HOH A 675 29.173 12.757 8.902 1.00 61.28 O HETATM 6542 O HOH A 676 33.495 7.332 23.429 1.00 67.50 O HETATM 6543 O HOH A 677 -9.013 3.913 24.227 1.00 57.78 O HETATM 6544 O HOH A 678 36.575 -4.144 1.092 1.00 56.35 O HETATM 6545 O HOH A 679 -9.642 6.629 31.120 1.00 77.78 O HETATM 6546 O HOH A 680 -11.075 18.953 16.687 1.00 48.23 O HETATM 6547 O HOH A 681 -5.284 21.935 12.854 1.00 71.50 O HETATM 6548 O HOH A 682 29.684 13.000 21.466 1.00 55.75 O HETATM 6549 O HOH A 683 30.586 8.846 26.951 1.00 67.39 O HETATM 6550 O HOH A 684 -12.364 17.408 21.393 1.00 58.03 O HETATM 6551 O HOH A 685 21.427 -1.886 10.585 1.00 61.00 O HETATM 6552 O HOH A 686 21.302 -1.147 17.940 1.00 33.80 O HETATM 6553 O HOH A 687 2.780 24.652 15.703 1.00 31.23 O HETATM 6554 O HOH A 688 24.320 17.271 10.953 1.00 43.21 O HETATM 6555 O HOH A 689 23.036 20.679 13.428 1.00 70.49 O HETATM 6556 O HOH A 690 31.742 1.970 20.885 1.00 59.86 O HETATM 6557 O HOH A 691 2.469 33.105 16.809 1.00 59.52 O HETATM 6558 O HOH A 692 -4.468 23.443 15.468 1.00 57.98 O HETATM 6559 O HOH A 693 8.297 28.018 4.353 1.00 63.48 O HETATM 6560 O HOH A 694 -2.242 -4.137 29.247 1.00 50.33 O HETATM 6561 O HOH A 695 26.135 0.076 33.794 1.00 72.40 O HETATM 6562 O HOH A 696 18.008 12.432 9.688 1.00 72.05 O HETATM 6563 O HOH A 697 -14.284 14.507 0.498 1.00 63.59 O HETATM 6564 O HOH A 698 31.621 -7.079 24.586 1.00 60.33 O HETATM 6565 O HOH A 699 1.982 4.561 39.443 1.00 67.69 O HETATM 6566 O HOH A 700 11.266 8.535 7.142 1.00 63.46 O HETATM 6567 O HOH A 701 30.091 -7.232 26.733 1.00 59.25 O HETATM 6568 O HOH A 702 -15.658 8.639 11.325 1.00 63.07 O HETATM 6569 O HOH A 703 25.370 -4.080 33.258 1.00 62.25 O HETATM 6570 O HOH A 704 29.623 -1.703 12.279 1.00 26.22 O HETATM 6571 O HOH A 705 7.177 -3.067 29.533 1.00 49.92 O HETATM 6572 O HOH A 706 19.003 -4.922 19.690 1.00 52.44 O HETATM 6573 O HOH A 707 -5.128 -0.785 12.192 1.00 48.24 O HETATM 6574 O HOH A 708 17.982 -3.075 13.902 1.00 56.33 O HETATM 6575 O HOH A 709 22.425 19.696 28.631 1.00 51.11 O HETATM 6576 O HOH A 710 10.009 29.484 6.434 1.00 61.96 O HETATM 6577 O HOH A 711 31.313 -25.471 2.423 1.00 52.17 O HETATM 6578 O HOH A 712 11.565 31.459 10.715 1.00 51.88 O HETATM 6579 O HOH A 713 26.833 19.955 17.148 1.00 61.65 O HETATM 6580 O HOH A 714 -0.851 3.983 38.889 1.00 71.59 O HETATM 6581 O HOH A 715 18.142 21.407 26.661 1.00 34.41 O HETATM 6582 O HOH A 716 26.428 -13.803 -8.112 1.00 46.73 O HETATM 6583 O HOH A 717 4.986 20.699 16.980 1.00 51.78 O HETATM 6584 O HOH A 718 3.049 19.205 16.115 1.00 55.06 O HETATM 6585 O HOH A 719 1.167 19.530 17.689 1.00 59.25 O HETATM 6586 O HOH A 720 -1.444 28.208 21.868 1.00 52.93 O HETATM 6587 O HOH A 721 9.391 1.715 36.705 1.00 52.07 O HETATM 6588 O HOH B 201 0.498 -4.792 -0.233 1.00 40.00 O HETATM 6589 O HOH B 202 9.690 -1.599 5.078 1.00 43.99 O HETATM 6590 O HOH B 203 10.503 1.777 2.855 1.00 41.22 O HETATM 6591 O HOH B 204 -0.219 -9.091 -1.161 1.00 55.48 O HETATM 6592 O HOH B 205 -7.913 -4.120 2.072 1.00 48.91 O HETATM 6593 O HOH B 206 7.286 -2.568 3.095 1.00 52.78 O HETATM 6594 O HOH B 207 8.693 3.951 2.205 1.00 50.88 O HETATM 6595 O HOH B 208 5.865 -4.325 1.659 1.00 53.49 O HETATM 6596 O HOH B 209 15.351 -9.256 -0.096 1.00 58.37 O HETATM 6597 O HOH B 210 7.082 -13.339 -1.312 1.00 64.61 O HETATM 6598 O HOH B 211 7.006 -8.676 0.683 1.00 64.87 O HETATM 6599 O HOH B 212 24.849 -22.462 20.369 1.00 61.45 O HETATM 6600 O HOH B 213 13.764 -13.107 1.825 1.00 64.24 O HETATM 6601 O HOH B 214 5.743 -1.706 23.574 1.00 20.39 O HETATM 6602 O HOH B 215 9.292 -2.522 9.166 1.00 23.75 O HETATM 6603 O HOH B 216 4.553 -1.896 21.058 1.00 21.12 O HETATM 6604 O HOH B 217 6.163 2.842 12.360 1.00 21.22 O HETATM 6605 O HOH B 218 11.122 -10.006 7.367 1.00 22.10 O HETATM 6606 O HOH B 219 21.007 -26.258 16.644 1.00 28.33 O HETATM 6607 O HOH B 220 12.160 2.236 7.566 1.00 30.63 O HETATM 6608 O HOH B 221 8.810 8.085 10.514 1.00 29.52 O HETATM 6609 O HOH B 222 10.757 -6.421 17.467 1.00 37.80 O HETATM 6610 O HOH B 223 2.250 -3.310 21.455 1.00 32.75 O HETATM 6611 O HOH B 224 18.391 -20.854 9.675 1.00 32.51 O HETATM 6612 O HOH B 225 23.993 -16.528 16.809 1.00 38.24 O HETATM 6613 O HOH B 226 -2.463 0.000 12.300 1.00 36.73 O HETATM 6614 O HOH B 227 -4.575 -3.218 11.449 1.00 37.92 O HETATM 6615 O HOH B 228 10.923 -3.015 6.937 1.00 34.64 O HETATM 6616 O HOH B 229 12.787 -30.943 15.835 1.00 48.99 O HETATM 6617 O HOH B 230 13.162 -0.624 11.242 1.00 41.32 O HETATM 6618 O HOH B 231 8.165 -12.717 2.387 1.00 35.01 O HETATM 6619 O HOH B 232 15.325 -5.530 13.436 1.00 34.13 O HETATM 6620 O HOH B 233 4.043 2.719 5.547 1.00 36.58 O HETATM 6621 O HOH B 234 14.828 -15.637 19.398 1.00 32.49 O HETATM 6622 O HOH B 235 1.843 -20.034 1.158 1.00 45.07 O HETATM 6623 O HOH B 236 5.512 -27.206 9.621 1.00 41.72 O HETATM 6624 O HOH B 237 -0.031 -6.133 15.908 1.00 39.88 O HETATM 6625 O HOH B 238 23.145 -17.911 12.877 1.00 36.07 O HETATM 6626 O HOH B 239 2.234 -20.344 17.261 1.00 35.61 O HETATM 6627 O HOH B 240 14.210 -20.142 5.794 1.00 40.73 O HETATM 6628 O HOH B 241 9.610 -7.426 23.497 1.00 39.86 O HETATM 6629 O HOH B 242 -0.401 -13.930 16.163 1.00 48.10 O HETATM 6630 O HOH B 243 2.647 -5.943 20.682 1.00 39.75 O HETATM 6631 O HOH B 244 12.193 -27.121 8.231 1.00 42.51 O HETATM 6632 O HOH B 245 14.265 -29.773 11.965 1.00 41.16 O HETATM 6633 O HOH B 246 5.323 -9.050 23.622 1.00 49.27 O HETATM 6634 O HOH B 247 -6.143 -5.052 9.451 1.00 34.78 O HETATM 6635 O HOH B 248 22.288 -23.586 19.015 1.00 51.87 O HETATM 6636 O HOH B 249 5.737 -4.149 27.316 1.00 53.86 O HETATM 6637 O HOH B 250 20.981 -18.836 22.789 1.00 38.85 O HETATM 6638 O HOH B 251 5.113 -13.003 24.066 1.00 54.46 O HETATM 6639 O HOH B 252 8.623 -21.531 1.822 1.00 45.32 O HETATM 6640 O HOH B 253 13.548 2.466 10.870 1.00 41.43 O HETATM 6641 O HOH B 254 13.049 -10.460 21.227 1.00 45.94 O HETATM 6642 O HOH B 255 13.144 3.923 5.894 1.00 48.21 O HETATM 6643 O HOH B 256 1.792 -15.883 19.818 1.00 50.89 O HETATM 6644 O HOH B 257 21.074 -22.797 10.128 1.00 50.08 O HETATM 6645 O HOH B 258 20.112 -21.515 22.169 1.00 51.11 O HETATM 6646 O HOH B 259 7.058 5.322 4.035 1.00 38.47 O HETATM 6647 O HOH B 260 -5.689 9.675 2.553 1.00 47.85 O HETATM 6648 O HOH B 261 15.492 -16.051 24.429 1.00 63.66 O HETATM 6649 O HOH B 262 -7.308 -10.191 3.382 1.00 47.19 O HETATM 6650 O HOH B 263 -6.275 -1.971 5.395 1.00 46.66 O HETATM 6651 O HOH B 264 10.068 -20.998 23.907 1.00 56.71 O HETATM 6652 O HOH B 265 2.018 -17.512 17.750 1.00 50.96 O HETATM 6653 O HOH B 266 5.136 -33.084 15.224 1.00 64.66 O HETATM 6654 O HOH B 267 3.684 -12.323 -0.243 1.00 45.85 O HETATM 6655 O HOH B 268 -2.282 -20.946 2.696 1.00 67.94 O HETATM 6656 O HOH B 269 23.404 -25.318 17.272 1.00 47.32 O HETATM 6657 O HOH B 270 11.873 -29.304 20.188 1.00 50.01 O HETATM 6658 O HOH B 271 -4.140 -6.930 8.881 1.00 30.65 O HETATM 6659 O HOH B 272 12.015 -4.104 19.027 1.00 43.51 O HETATM 6660 O HOH B 273 12.758 -4.207 9.754 1.00 48.43 O HETATM 6661 O HOH B 274 -7.864 -13.588 4.462 1.00 51.38 O HETATM 6662 O HOH B 275 -0.751 -15.733 0.869 1.00 48.28 O HETATM 6663 O HOH B 276 0.575 -9.528 16.642 1.00 57.18 O HETATM 6664 O HOH B 277 0.153 -18.223 -0.247 1.00 51.93 O HETATM 6665 O HOH B 278 -2.047 -3.591 16.204 1.00 54.42 O HETATM 6666 O HOH B 279 3.526 -27.047 20.741 1.00 58.51 O HETATM 6667 O HOH B 280 11.603 -21.036 2.390 1.00 55.91 O HETATM 6668 O HOH B 281 17.201 -19.897 7.257 1.00 51.68 O HETATM 6669 O HOH B 282 23.238 -31.270 11.952 1.00 57.20 O HETATM 6670 O HOH B 283 13.163 -7.610 16.850 1.00 45.68 O HETATM 6671 O HOH B 284 8.490 -26.862 6.755 1.00 52.79 O HETATM 6672 O HOH B 285 -5.407 -9.626 10.157 1.00 67.20 O HETATM 6673 O HOH B 286 5.171 -12.164 2.079 1.00 53.91 O HETATM 6674 O HOH B 287 22.076 -29.034 23.198 1.00 56.63 O HETATM 6675 O HOH B 288 -2.511 -26.484 14.246 1.00 51.50 O HETATM 6676 O HOH B 289 23.004 -25.804 21.698 1.00 59.24 O HETATM 6677 O HOH B 290 9.862 -5.202 3.453 1.00 41.63 O HETATM 6678 O HOH B 291 18.242 -35.894 13.348 1.00 62.59 O HETATM 6679 O HOH B 292 -1.496 -26.883 18.539 1.00 51.48 O HETATM 6680 O HOH B 293 13.179 -32.297 18.860 1.00 55.27 O HETATM 6681 O HOH B 294 6.046 -32.884 18.413 1.00 72.04 O HETATM 6682 O HOH B 295 10.879 -5.487 5.857 1.00 30.20 O HETATM 6683 O HOH B 296 -1.471 -17.404 11.398 1.00 43.37 O HETATM 6684 O HOH B 297 -4.968 -2.078 14.768 1.00 53.24 O HETATM 6685 O HOH B 298 3.080 -7.676 22.813 1.00 60.93 O HETATM 6686 O HOH B 299 -2.426 -11.914 -1.574 1.00 62.08 O HETATM 6687 O HOH B 300 11.718 -26.434 24.298 1.00 66.46 O HETATM 6688 O HOH B 301 -1.443 -16.213 17.128 1.00 75.09 O HETATM 6689 O HOH B 302 7.050 -19.222 0.930 1.00 57.54 O HETATM 6690 O HOH B 303 15.487 -2.216 13.292 1.00 65.87 O HETATM 6691 O HOH B 304 26.748 -22.063 17.639 1.00 61.75 O HETATM 6692 O HOH B 305 22.902 -34.975 11.607 1.00 65.26 O HETATM 6693 O HOH B 306 4.068 -6.690 26.652 1.00 78.71 O HETATM 6694 O HOH B 307 7.968 -7.747 25.819 1.00 63.88 O HETATM 6695 O HOH B 308 13.210 0.631 15.260 1.00 47.79 O HETATM 6696 O HOH B 309 12.601 2.893 14.195 1.00 33.46 O HETATM 6697 O HOH C 301 12.394 43.803 49.473 1.00 54.24 O HETATM 6698 O HOH C 302 17.078 53.516 33.952 1.00 31.54 O HETATM 6699 O HOH C 303 13.963 48.976 44.561 1.00 26.75 O HETATM 6700 O HOH C 304 12.573 37.758 46.292 1.00 23.24 O HETATM 6701 O HOH C 305 21.787 34.943 39.886 1.00 46.84 O HETATM 6702 O HOH C 306 22.090 43.938 28.812 1.00 37.17 O HETATM 6703 O HOH C 307 18.832 36.881 38.771 1.00 32.60 O HETATM 6704 O HOH C 308 17.813 42.941 37.369 1.00 24.41 O HETATM 6705 O HOH C 309 20.546 40.736 38.927 1.00 33.88 O HETATM 6706 O HOH C 310 16.261 38.293 44.985 1.00 40.03 O HETATM 6707 O HOH C 311 26.112 25.459 30.150 1.00 56.70 O HETATM 6708 O HOH C 312 23.038 26.133 31.177 1.00 51.22 O HETATM 6709 O HOH C 313 14.801 54.393 44.927 1.00 70.45 O HETATM 6710 O HOH C 314 18.185 37.595 41.747 1.00 45.42 O HETATM 6711 O HOH C 315 23.178 41.404 29.652 1.00 43.33 O HETATM 6712 O HOH C 316 23.531 32.926 40.320 1.00 63.52 O HETATM 6713 O HOH C 317 17.149 57.664 35.518 1.00 40.54 O HETATM 6714 O HOH C 318 20.347 46.686 26.616 1.00 65.65 O HETATM 6715 O HOH C 319 19.890 50.188 33.761 1.00 28.36 O HETATM 6716 O HOH C 320 26.253 24.726 27.340 1.00 63.74 O HETATM 6717 O HOH C 321 12.128 22.919 23.760 1.00 13.22 O HETATM 6718 O HOH C 322 -3.754 35.503 32.337 1.00 18.10 O HETATM 6719 O HOH C 323 -2.011 41.911 35.817 1.00 20.59 O HETATM 6720 O HOH C 324 13.106 12.880 34.494 1.00 23.55 O HETATM 6721 O HOH C 325 3.768 22.449 35.632 1.00 16.59 O HETATM 6722 O HOH C 326 5.599 33.830 41.031 1.00 19.91 O HETATM 6723 O HOH C 327 12.229 37.683 43.657 1.00 19.08 O HETATM 6724 O HOH C 328 15.180 34.322 22.373 1.00 25.34 O HETATM 6725 O HOH C 329 10.352 35.118 27.646 1.00 20.18 O HETATM 6726 O HOH C 330 12.738 31.993 21.285 1.00 20.45 O HETATM 6727 O HOH C 331 18.177 48.062 35.029 1.00 20.22 O HETATM 6728 O HOH C 332 19.222 26.601 29.465 1.00 21.31 O HETATM 6729 O HOH C 333 10.651 23.902 36.202 1.00 25.82 O HETATM 6730 O HOH C 334 14.315 16.349 32.671 1.00 21.51 O HETATM 6731 O HOH C 335 6.157 23.539 39.788 1.00 17.52 O HETATM 6732 O HOH C 336 7.149 36.136 22.990 1.00 29.56 O HETATM 6733 O HOH C 337 -0.956 42.541 33.328 1.00 24.60 O HETATM 6734 O HOH C 338 13.936 21.188 37.005 1.00 26.57 O HETATM 6735 O HOH C 339 0.314 47.177 39.916 1.00 25.94 O HETATM 6736 O HOH C 340 12.745 29.386 42.825 1.00 40.56 O HETATM 6737 O HOH C 341 21.970 30.161 35.629 1.00 28.34 O HETATM 6738 O HOH C 342 2.676 47.801 31.236 1.00 29.74 O HETATM 6739 O HOH C 343 -2.724 36.301 27.962 1.00 27.14 O HETATM 6740 O HOH C 344 21.965 34.507 23.746 1.00 27.98 O HETATM 6741 O HOH C 345 4.593 47.795 25.050 1.00 42.18 O HETATM 6742 O HOH C 346 3.860 29.472 31.216 1.00 24.27 O HETATM 6743 O HOH C 347 10.249 32.879 21.218 1.00 24.53 O HETATM 6744 O HOH C 348 5.043 25.496 28.235 1.00 37.11 O HETATM 6745 O HOH C 349 6.439 41.490 26.056 1.00 29.29 O HETATM 6746 O HOH C 350 1.582 42.566 41.945 1.00 36.83 O HETATM 6747 O HOH C 351 5.214 65.351 44.164 1.00 37.76 O HETATM 6748 O HOH C 352 11.016 18.186 36.911 1.00 30.97 O HETATM 6749 O HOH C 353 13.935 54.561 27.358 1.00 44.53 O HETATM 6750 O HOH C 354 19.904 20.118 32.433 1.00 32.29 O HETATM 6751 O HOH C 355 -7.163 40.384 36.921 1.00 37.10 O HETATM 6752 O HOH C 356 18.873 23.556 31.987 1.00 45.83 O HETATM 6753 O HOH C 357 19.373 24.691 27.572 1.00 27.74 O HETATM 6754 O HOH C 358 20.093 25.209 33.692 1.00 51.70 O HETATM 6755 O HOH C 359 0.577 50.254 37.635 1.00 39.16 O HETATM 6756 O HOH C 360 1.829 55.000 43.873 1.00 36.37 O HETATM 6757 O HOH C 361 3.036 27.335 29.846 1.00 30.09 O HETATM 6758 O HOH C 362 6.761 40.733 43.174 1.00 35.12 O HETATM 6759 O HOH C 363 8.985 41.106 25.394 1.00 37.04 O HETATM 6760 O HOH C 364 6.979 58.751 42.302 1.00 32.68 O HETATM 6761 O HOH C 365 4.148 57.612 32.669 1.00 40.31 O HETATM 6762 O HOH C 366 8.649 23.734 40.805 1.00 32.05 O HETATM 6763 O HOH C 367 -1.156 38.622 27.710 1.00 29.65 O HETATM 6764 O HOH C 368 9.557 39.526 23.600 1.00 41.32 O HETATM 6765 O HOH C 369 4.953 48.242 41.741 1.00 36.59 O HETATM 6766 O HOH C 370 3.732 38.684 41.879 1.00 30.97 O HETATM 6767 O HOH C 371 7.507 57.635 30.061 1.00 41.56 O HETATM 6768 O HOH C 372 10.620 27.940 41.866 1.00 50.85 O HETATM 6769 O HOH C 373 1.206 55.366 32.472 1.00 37.60 O HETATM 6770 O HOH C 374 8.880 40.965 45.000 1.00 43.58 O HETATM 6771 O HOH C 375 12.985 34.277 42.538 1.00 36.33 O HETATM 6772 O HOH C 376 11.238 46.711 22.416 1.00 48.27 O HETATM 6773 O HOH C 377 19.476 30.763 39.725 1.00 43.44 O HETATM 6774 O HOH C 378 19.378 22.322 29.161 1.00 38.74 O HETATM 6775 O HOH C 379 -5.319 37.302 28.363 1.00 40.46 O HETATM 6776 O HOH C 380 19.350 38.672 19.173 1.00 39.00 O HETATM 6777 O HOH C 381 19.478 30.426 18.857 1.00 37.93 O HETATM 6778 O HOH C 382 20.086 18.779 30.086 1.00 35.87 O HETATM 6779 O HOH C 383 6.546 36.510 45.930 1.00 38.01 O HETATM 6780 O HOH C 384 17.900 46.609 23.581 1.00 44.68 O HETATM 6781 O HOH C 385 -5.140 40.247 34.742 1.00 40.69 O HETATM 6782 O HOH C 386 0.460 41.041 29.474 1.00 43.92 O HETATM 6783 O HOH C 387 21.827 41.563 25.261 1.00 39.36 O HETATM 6784 O HOH C 388 0.357 48.037 32.253 1.00 41.20 O HETATM 6785 O HOH C 389 15.883 56.040 28.396 1.00 60.79 O HETATM 6786 O HOH C 390 23.953 32.893 24.436 1.00 47.35 O HETATM 6787 O HOH C 391 15.608 45.825 22.781 1.00 38.79 O HETATM 6788 O HOH C 392 7.342 25.240 26.735 1.00 35.32 O HETATM 6789 O HOH C 393 -1.240 42.387 45.464 1.00 63.03 O HETATM 6790 O HOH C 394 -4.056 43.830 35.265 1.00 55.49 O HETATM 6791 O HOH C 395 19.029 44.858 25.130 1.00 44.21 O HETATM 6792 O HOH C 396 5.104 43.636 25.276 1.00 43.13 O HETATM 6793 O HOH C 397 1.738 40.095 25.609 1.00 58.12 O HETATM 6794 O HOH C 398 9.615 55.838 50.759 1.00 51.94 O HETATM 6795 O HOH C 399 -4.276 43.920 46.336 1.00 55.43 O HETATM 6796 O HOH C 400 12.917 20.905 39.728 1.00 79.13 O HETATM 6797 O HOH C 401 28.086 30.580 27.612 1.00 52.94 O HETATM 6798 O HOH C 402 -3.595 47.188 40.262 1.00 44.77 O HETATM 6799 O HOH C 403 23.218 30.175 20.284 1.00 52.55 O HETATM 6800 O HOH C 404 11.195 31.146 45.027 1.00 43.00 O HETATM 6801 O HOH C 405 2.217 46.924 28.409 1.00 66.40 O HETATM 6802 O HOH C 406 -3.728 62.151 63.821 1.00 54.97 O HETATM 6803 O HOH C 407 21.887 24.572 26.428 1.00 55.52 O HETATM 6804 O HOH C 408 -4.244 47.574 36.900 1.00 68.90 O HETATM 6805 O HOH C 409 0.042 40.686 43.484 1.00 51.07 O HETATM 6806 O HOH C 410 21.861 32.397 18.058 1.00 60.03 O HETATM 6807 O HOH C 411 24.394 37.466 28.215 1.00 44.78 O HETATM 6808 O HOH C 412 2.856 46.790 41.979 1.00 45.73 O HETATM 6809 O HOH C 413 19.433 41.250 18.384 1.00 62.84 O HETATM 6810 O HOH C 414 11.207 63.547 40.739 1.00 57.68 O HETATM 6811 O HOH C 415 20.030 17.475 34.635 1.00 58.56 O HETATM 6812 O HOH C 416 9.784 36.815 23.305 1.00 48.25 O HETATM 6813 O HOH C 417 0.532 44.825 29.959 1.00 56.28 O HETATM 6814 O HOH C 418 0.047 63.318 33.867 1.00 53.60 O HETATM 6815 O HOH C 419 4.386 67.227 42.256 1.00 49.04 O HETATM 6816 O HOH C 420 -0.795 37.890 24.719 1.00 50.95 O HETATM 6817 O HOH C 421 4.405 53.920 40.142 1.00 47.83 O HETATM 6818 O HOH C 422 -6.504 39.042 32.701 1.00 45.25 O HETATM 6819 O HOH C 423 13.995 59.525 33.171 1.00 51.64 O HETATM 6820 O HOH C 424 13.143 41.299 17.704 1.00 56.37 O HETATM 6821 O HOH C 425 6.568 55.982 42.630 1.00 46.09 O HETATM 6822 O HOH C 426 -3.222 43.766 32.189 1.00 48.78 O HETATM 6823 O HOH C 427 19.450 27.932 17.809 1.00 50.64 O HETATM 6824 O HOH C 428 1.430 53.108 45.659 1.00 56.59 O HETATM 6825 O HOH C 429 21.481 40.987 22.539 1.00 55.49 O HETATM 6826 O HOH C 430 1.081 48.556 43.870 1.00 49.55 O HETATM 6827 O HOH C 431 -14.877 69.187 60.879 1.00 60.90 O HETATM 6828 O HOH C 432 2.458 50.865 26.407 1.00 67.61 O HETATM 6829 O HOH C 433 8.309 60.325 30.986 1.00 59.97 O HETATM 6830 O HOH C 434 0.755 57.545 38.085 1.00 49.73 O HETATM 6831 O HOH C 435 -1.669 57.215 39.932 1.00 54.97 O HETATM 6832 O HOH C 436 12.860 60.903 40.113 1.00 73.20 O HETATM 6833 O HOH C 437 22.070 27.782 18.475 1.00 74.29 O HETATM 6834 O HOH C 438 -1.929 49.980 36.138 1.00 63.76 O HETATM 6835 O HOH C 439 17.972 49.264 23.777 1.00 56.32 O HETATM 6836 O HOH C 440 10.907 40.028 17.965 1.00 51.71 O HETATM 6837 O HOH C 441 22.529 36.009 21.562 1.00 53.77 O HETATM 6838 O HOH C 442 2.646 42.662 25.679 1.00 52.41 O HETATM 6839 O HOH C 443 -4.185 46.548 33.346 1.00 69.02 O HETATM 6840 O HOH C 444 25.059 35.797 25.928 1.00 63.78 O HETATM 6841 O HOH C 445 14.315 64.648 50.823 1.00 57.25 O HETATM 6842 O HOH C 446 21.813 34.837 19.234 1.00 60.60 O HETATM 6843 O HOH C 447 5.543 54.988 44.945 1.00 58.57 O HETATM 6844 O HOH C 448 23.173 29.460 24.409 1.00 36.31 O HETATM 6845 O HOH C 449 -0.033 63.878 46.048 1.00 47.02 O HETATM 6846 O HOH C 450 -2.573 39.863 42.536 1.00 58.31 O HETATM 6847 O HOH C 451 15.891 58.829 31.114 1.00 67.90 O HETATM 6848 O HOH C 452 19.713 23.448 41.628 1.00 71.92 O HETATM 6849 O HOH C 453 22.763 26.612 23.759 1.00 64.34 O HETATM 6850 O HOH C 454 6.275 54.613 55.798 1.00 61.14 O HETATM 6851 O HOH C 455 14.855 61.309 51.744 1.00 58.36 O HETATM 6852 O HOH C 456 8.989 59.272 59.169 1.00 63.97 O HETATM 6853 O HOH C 457 -3.521 39.057 44.957 1.00 45.79 O HETATM 6854 O HOH C 458 16.288 58.950 53.004 1.00 60.69 O HETATM 6855 O HOH C 459 12.077 34.129 16.109 1.00 68.77 O HETATM 6856 O HOH C 460 8.172 39.038 20.164 1.00 60.06 O HETATM 6857 O HOH C 461 7.304 76.617 56.277 1.00 68.10 O HETATM 6858 O HOH C 462 -1.964 49.210 33.297 1.00 58.62 O HETATM 6859 O HOH C 463 1.540 55.158 39.250 1.00 52.00 O HETATM 6860 O HOH C 464 -15.757 61.353 57.643 1.00 56.18 O HETATM 6861 O HOH C 465 4.983 58.582 30.310 1.00 61.23 O HETATM 6862 O HOH C 466 -11.444 67.634 63.152 1.00 59.31 O HETATM 6863 O HOH C 467 8.199 42.729 47.229 1.00 53.54 O HETATM 6864 O HOH C 468 1.329 51.557 51.396 1.00 87.57 O HETATM 6865 O HOH C 469 20.900 25.851 41.677 1.00 61.08 O HETATM 6866 O HOH C 470 6.719 55.254 26.966 1.00 47.73 O HETATM 6867 O HOH C 471 9.760 48.150 43.780 1.00 38.24 O HETATM 6868 O HOH D 301 -14.306 17.262 54.185 1.00 34.27 O HETATM 6869 O HOH D 302 -13.538 15.495 47.248 1.00 54.59 O HETATM 6870 O HOH D 303 -12.492 15.115 50.289 1.00 38.73 O HETATM 6871 O HOH D 304 -17.566 16.720 46.299 1.00 51.94 O HETATM 6872 O HOH D 305 9.624 39.300 49.662 1.00 54.01 O HETATM 6873 O HOH D 306 9.061 38.006 52.303 1.00 61.96 O HETATM 6874 O HOH D 307 -18.857 18.910 47.233 1.00 58.68 O HETATM 6875 O HOH D 308 1.162 18.773 25.881 1.00 9.61 O HETATM 6876 O HOH D 309 5.456 25.270 41.825 1.00 16.29 O HETATM 6877 O HOH D 310 3.173 30.357 47.247 1.00 20.81 O HETATM 6878 O HOH D 311 -2.086 35.117 30.191 1.00 18.47 O HETATM 6879 O HOH D 312 -14.758 23.675 39.056 1.00 21.27 O HETATM 6880 O HOH D 313 -2.298 28.183 25.996 1.00 17.83 O HETATM 6881 O HOH D 314 -12.118 18.873 44.014 1.00 22.83 O HETATM 6882 O HOH D 315 5.284 21.122 40.556 1.00 20.59 O HETATM 6883 O HOH D 316 3.774 15.965 33.958 1.00 21.86 O HETATM 6884 O HOH D 317 -13.113 24.110 27.560 1.00 26.31 O HETATM 6885 O HOH D 318 3.324 24.769 37.264 1.00 21.42 O HETATM 6886 O HOH D 319 -8.513 18.139 50.420 1.00 26.32 O HETATM 6887 O HOH D 320 -6.085 15.202 44.022 1.00 22.94 O HETATM 6888 O HOH D 321 -3.780 15.228 42.010 1.00 24.91 O HETATM 6889 O HOH D 322 -14.341 17.125 38.127 1.00 30.64 O HETATM 6890 O HOH D 323 -9.367 17.450 28.058 1.00 24.69 O HETATM 6891 O HOH D 324 -0.875 24.793 54.068 1.00 30.70 O HETATM 6892 O HOH D 325 4.879 36.128 42.597 1.00 26.42 O HETATM 6893 O HOH D 326 -13.970 18.196 35.742 1.00 26.70 O HETATM 6894 O HOH D 327 -1.831 18.722 28.084 1.00 24.94 O HETATM 6895 O HOH D 328 -11.120 16.441 45.062 1.00 33.08 O HETATM 6896 O HOH D 329 3.322 14.231 38.351 1.00 28.08 O HETATM 6897 O HOH D 330 1.841 20.496 33.309 1.00 26.92 O HETATM 6898 O HOH D 331 2.645 19.439 50.185 1.00 32.53 O HETATM 6899 O HOH D 332 -2.201 25.738 59.961 1.00 31.15 O HETATM 6900 O HOH D 333 -10.136 16.086 49.682 1.00 30.00 O HETATM 6901 O HOH D 334 6.167 27.560 40.778 1.00 26.84 O HETATM 6902 O HOH D 335 -10.020 13.027 38.251 1.00 36.61 O HETATM 6903 O HOH D 336 -2.749 15.875 47.922 1.00 31.55 O HETATM 6904 O HOH D 337 -10.021 34.566 30.705 1.00 31.74 O HETATM 6905 O HOH D 338 -5.613 10.825 38.046 1.00 28.85 O HETATM 6906 O HOH D 339 -5.477 35.502 52.087 1.00 34.11 O HETATM 6907 O HOH D 340 0.231 22.079 50.858 1.00 29.86 O HETATM 6908 O HOH D 341 -14.745 16.452 28.764 1.00 29.52 O HETATM 6909 O HOH D 342 -7.324 34.803 31.671 1.00 36.15 O HETATM 6910 O HOH D 343 -8.724 13.234 28.215 1.00 27.17 O HETATM 6911 O HOH D 344 7.279 25.393 49.147 1.00 36.21 O HETATM 6912 O HOH D 345 -4.851 14.516 46.351 1.00 35.26 O HETATM 6913 O HOH D 346 -5.414 39.444 57.003 1.00 49.30 O HETATM 6914 O HOH D 347 2.142 25.081 27.879 1.00 30.91 O HETATM 6915 O HOH D 348 -8.684 36.446 34.713 1.00 33.87 O HETATM 6916 O HOH D 349 -15.551 30.716 31.656 1.00 42.12 O HETATM 6917 O HOH D 350 -7.218 38.133 43.998 1.00 45.76 O HETATM 6918 O HOH D 351 -24.949 32.683 56.320 1.00 62.65 O HETATM 6919 O HOH D 352 3.216 18.297 32.716 1.00 31.11 O HETATM 6920 O HOH D 353 -3.487 15.812 51.579 1.00 41.96 O HETATM 6921 O HOH D 354 -5.503 29.341 23.522 1.00 34.36 O HETATM 6922 O HOH D 355 -15.812 29.215 38.154 1.00 41.46 O HETATM 6923 O HOH D 356 -7.579 20.151 53.895 1.00 36.55 O HETATM 6924 O HOH D 357 -17.418 25.043 49.198 1.00 39.92 O HETATM 6925 O HOH D 358 -13.974 19.142 57.263 1.00 43.60 O HETATM 6926 O HOH D 359 1.279 36.182 51.607 1.00 44.31 O HETATM 6927 O HOH D 360 4.771 16.870 45.417 1.00 43.55 O HETATM 6928 O HOH D 361 -10.223 38.312 42.639 1.00 38.08 O HETATM 6929 O HOH D 362 -11.769 55.483 59.679 1.00 44.05 O HETATM 6930 O HOH D 363 -15.106 50.170 46.776 1.00 41.52 O HETATM 6931 O HOH D 364 -6.609 16.810 51.764 1.00 38.41 O HETATM 6932 O HOH D 365 -4.237 35.815 23.923 1.00 50.67 O HETATM 6933 O HOH D 366 -0.725 14.786 49.051 1.00 37.71 O HETATM 6934 O HOH D 367 -3.129 20.553 55.686 1.00 42.37 O HETATM 6935 O HOH D 368 -17.515 21.696 56.591 1.00 39.95 O HETATM 6936 O HOH D 369 -2.015 22.371 53.617 1.00 50.59 O HETATM 6937 O HOH D 370 -3.913 58.840 39.976 1.00 37.59 O HETATM 6938 O HOH D 371 -21.521 44.316 50.115 1.00 45.22 O HETATM 6939 O HOH D 372 1.983 37.863 47.490 1.00 52.96 O HETATM 6940 O HOH D 373 -5.770 20.893 55.594 1.00 43.38 O HETATM 6941 O HOH D 374 1.086 24.840 51.473 1.00 57.38 O HETATM 6942 O HOH D 375 -14.307 17.463 42.955 1.00 45.50 O HETATM 6943 O HOH D 376 -0.718 37.031 47.856 1.00 39.82 O HETATM 6944 O HOH D 377 -9.726 8.551 33.882 1.00 45.96 O HETATM 6945 O HOH D 378 -8.661 27.932 22.567 1.00 48.99 O HETATM 6946 O HOH D 379 3.937 36.695 45.916 1.00 43.57 O HETATM 6947 O HOH D 380 -12.360 26.468 64.155 1.00 54.47 O HETATM 6948 O HOH D 381 -0.646 31.631 55.000 1.00 43.27 O HETATM 6949 O HOH D 382 -15.028 37.348 52.206 1.00 41.88 O HETATM 6950 O HOH D 383 -6.159 23.744 62.588 1.00 47.51 O HETATM 6951 O HOH D 384 -2.664 12.905 42.672 1.00 43.55 O HETATM 6952 O HOH D 385 -13.853 39.310 45.796 1.00 61.31 O HETATM 6953 O HOH D 386 -8.417 21.303 60.189 1.00 49.14 O HETATM 6954 O HOH D 387 -6.352 23.210 23.322 1.00 51.33 O HETATM 6955 O HOH D 388 7.564 29.039 43.135 1.00 59.53 O HETATM 6956 O HOH D 389 -8.546 40.806 64.837 1.00 60.65 O HETATM 6957 O HOH D 390 -8.413 49.198 47.532 1.00 41.18 O HETATM 6958 O HOH D 391 -2.773 29.509 23.570 1.00 38.19 O HETATM 6959 O HOH D 392 -1.969 11.070 39.998 1.00 37.41 O HETATM 6960 O HOH D 393 -16.934 29.331 58.037 1.00 45.82 O HETATM 6961 O HOH D 394 1.813 28.113 54.725 1.00 51.56 O HETATM 6962 O HOH D 395 -13.861 48.266 63.257 1.00 47.61 O HETATM 6963 O HOH D 396 -16.992 35.814 46.648 1.00 49.92 O HETATM 6964 O HOH D 397 -19.129 32.730 54.511 1.00 57.31 O HETATM 6965 O HOH D 398 -1.480 51.437 54.378 1.00 48.42 O HETATM 6966 O HOH D 399 -14.703 23.888 62.075 1.00 54.36 O HETATM 6967 O HOH D 400 -12.333 39.384 40.937 1.00 53.91 O HETATM 6968 O HOH D 401 -18.295 49.667 60.350 1.00 56.82 O HETATM 6969 O HOH D 402 -2.996 35.828 51.751 1.00 47.34 O HETATM 6970 O HOH D 403 -7.972 13.153 44.058 1.00 53.88 O HETATM 6971 O HOH D 404 3.332 29.376 52.910 1.00 49.21 O HETATM 6972 O HOH D 405 -19.298 32.822 43.994 1.00 51.33 O HETATM 6973 O HOH D 406 -6.409 31.603 63.196 1.00 56.57 O HETATM 6974 O HOH D 407 -4.679 32.855 61.807 1.00 56.59 O HETATM 6975 O HOH D 408 5.743 27.968 53.180 1.00 66.00 O HETATM 6976 O HOH D 409 -9.738 19.930 24.536 1.00 42.40 O HETATM 6977 O HOH D 410 -5.755 36.973 31.183 1.00 44.55 O HETATM 6978 O HOH D 411 -21.906 52.965 55.531 1.00 53.07 O HETATM 6979 O HOH D 412 -17.567 54.434 59.484 1.00 48.54 O HETATM 6980 O HOH D 413 -12.714 10.501 34.549 1.00 57.33 O HETATM 6981 O HOH D 414 -7.069 17.409 54.428 1.00 45.31 O HETATM 6982 O HOH D 415 -1.504 37.394 45.368 1.00 32.72 O HETATM 6983 O HOH D 416 -16.191 19.998 29.381 1.00 38.75 O HETATM 6984 O HOH D 417 1.736 25.607 53.893 1.00 43.21 O HETATM 6985 O HOH D 418 -16.764 34.798 53.660 1.00 38.22 O HETATM 6986 O HOH D 419 -5.143 32.830 59.161 1.00 40.17 O HETATM 6987 O HOH D 420 -2.294 72.760 57.273 1.00 50.47 O HETATM 6988 O HOH D 421 -8.061 32.951 64.783 1.00 48.84 O HETATM 6989 O HOH D 422 -8.958 38.677 36.199 1.00 53.30 O HETATM 6990 O HOH D 423 -6.070 37.223 54.785 1.00 59.67 O HETATM 6991 O HOH D 424 8.620 28.856 45.891 1.00 50.89 O HETATM 6992 O HOH D 425 -20.782 44.522 61.003 1.00 55.63 O HETATM 6993 O HOH D 426 -18.853 24.427 33.846 1.00 57.94 O HETATM 6994 O HOH D 427 -15.490 50.141 42.366 1.00 61.12 O HETATM 6995 O HOH D 428 -16.839 38.956 46.263 1.00 68.46 O HETATM 6996 O HOH D 429 -8.774 15.998 55.824 1.00 49.32 O HETATM 6997 O HOH D 430 9.934 38.029 47.215 1.00 51.85 O HETATM 6998 O HOH D 431 -17.981 46.873 45.549 1.00 53.29 O HETATM 6999 O HOH D 432 -17.392 36.939 50.948 1.00 64.20 O HETATM 7000 O HOH D 433 -19.229 43.867 63.626 1.00 60.48 O HETATM 7001 O HOH D 434 -10.635 68.580 39.475 1.00 65.56 O HETATM 7002 O HOH D 435 -6.271 55.666 39.949 1.00 58.75 O HETATM 7003 O HOH D 436 -14.093 13.334 29.641 1.00 58.29 O HETATM 7004 O HOH D 437 2.049 46.494 45.236 1.00 56.74 O HETATM 7005 O HOH D 438 -11.691 59.379 36.551 1.00 65.20 O HETATM 7006 O HOH D 439 -7.382 12.562 40.228 1.00 64.48 O HETATM 7007 O HOH D 440 4.271 25.397 52.505 1.00 65.44 O HETATM 7008 O HOH D 441 -22.637 34.881 55.121 1.00 67.48 O HETATM 7009 O HOH D 442 -8.867 50.961 65.032 1.00 60.90 O HETATM 7010 O HOH D 443 -17.330 48.871 62.978 1.00 66.34 O HETATM 7011 O HOH D 444 -20.503 60.152 55.877 1.00 63.96 O HETATM 7012 O HOH D 445 -22.640 52.962 50.967 1.00 66.92 O HETATM 7013 O HOH D 446 -5.713 19.215 58.199 1.00 59.23 O HETATM 7014 O HOH D 447 -19.327 52.402 60.287 1.00 50.68 O HETATM 7015 O HOH D 448 -17.539 27.151 37.942 1.00 87.28 O HETATM 7016 O HOH D 449 4.735 33.820 52.995 1.00 54.82 O HETATM 7017 O HOH D 450 -9.373 12.545 46.347 1.00 59.64 O HETATM 7018 O HOH D 451 -11.143 49.994 43.860 1.00 52.11 O HETATM 7019 O HOH D 452 -14.707 28.492 64.654 1.00 70.72 O HETATM 7020 O HOH D 453 -17.298 72.943 40.285 1.00 57.72 O HETATM 7021 O HOH D 454 -13.345 64.686 40.568 1.00 54.89 O HETATM 7022 O HOH D 455 -1.966 35.577 25.423 1.00 37.76 O HETATM 7023 O HOH D 456 2.451 39.514 44.057 1.00 64.21 O HETATM 7024 O HOH D 457 -11.798 11.663 36.825 1.00 56.89 O HETATM 7025 O HOH D 458 -2.923 40.944 61.494 1.00 54.27 O HETATM 7026 O HOH D 459 4.823 14.390 44.370 1.00 55.34 O HETATM 7027 O HOH D 460 7.342 19.496 46.961 1.00 50.69 O HETATM 7028 O HOH D 461 -5.780 47.270 49.098 1.00 59.35 O HETATM 7029 O HOH D 462 -15.239 30.979 65.571 1.00 58.86 O HETATM 7030 O HOH D 463 -10.171 43.002 41.448 1.00 73.59 O HETATM 7031 O HOH D 464 -7.794 25.386 22.546 1.00 64.63 O HETATM 7032 O HOH D 465 -19.750 30.419 40.271 1.00 74.14 O HETATM 7033 O HOH D 466 9.677 34.241 52.827 1.00 69.85 O HETATM 7034 O HOH D 467 -6.113 27.414 21.689 1.00 59.51 O HETATM 7035 O HOH D 468 -19.439 58.533 58.369 1.00 47.21 O HETATM 7036 O HOH D 469 -8.499 52.911 45.019 1.00 41.01 O HETATM 7037 O HOH D 470 -9.539 24.586 65.287 1.00 65.03 O HETATM 7038 O HOH D 471 -6.664 47.802 66.643 1.00 65.90 O HETATM 7039 O HOH D 472 -7.730 78.169 42.717 1.00 73.48 O HETATM 7040 O HOH D 473 -18.554 28.945 48.679 1.00 62.28 O HETATM 7041 O HOH D 474 -12.635 50.840 67.258 1.00 68.39 O HETATM 7042 O HOH D 475 -23.404 47.170 52.568 1.00 61.91 O HETATM 7043 O HOH D 476 1.909 20.448 54.492 1.00 59.72 O HETATM 7044 O HOH D 477 -11.717 71.828 56.475 1.00 60.08 O HETATM 7045 O HOH D 478 -23.474 51.481 48.865 1.00 59.76 O HETATM 7046 O HOH D 479 -18.673 33.604 48.871 1.00 64.43 O HETATM 7047 O HOH D 480 2.010 50.201 61.577 1.00 55.55 O HETATM 7048 O HOH D 481 -1.833 20.719 58.425 1.00 54.92 O HETATM 7049 O HOH D 482 -18.626 23.821 38.423 1.00 62.70 O HETATM 7050 O HOH D 483 2.626 21.343 51.886 1.00 44.41 O HETATM 7051 O HOH D 484 -2.666 32.107 22.921 1.00 47.74 O HETATM 7052 O HOH D 485 -9.332 64.566 40.286 1.00 70.27 O HETATM 7053 O HOH D 486 7.575 31.978 54.267 1.00 55.66 O HETATM 7054 O HOH D 487 -11.365 73.582 53.840 1.00 66.98 O HETATM 7055 O HOH D 488 -6.645 13.168 47.844 1.00 59.41 O HETATM 7056 O HOH D 489 -13.694 27.956 22.577 1.00 55.88 O HETATM 7057 O HOH D 490 3.028 14.460 48.927 1.00 57.91 O HETATM 7058 O HOH D 491 -18.641 14.402 36.623 1.00 54.71 O HETATM 7059 O HOH D 492 -0.505 25.812 21.799 1.00 47.47 O HETATM 7060 O HOH D 493 -6.910 8.826 37.077 1.00 61.63 O HETATM 7061 O HOH D 494 11.487 32.626 47.312 1.00 48.56 O CONECT 368 6233 CONECT 877 1409 CONECT 1409 877 CONECT 1691 2090 CONECT 2090 1691 CONECT 2416 2851 CONECT 2851 2416 CONECT 2876 6265 CONECT 2881 6265 CONECT 2905 6265 CONECT 3148 3679 CONECT 3679 3148 CONECT 3978 4308 CONECT 4308 3978 CONECT 4608 5137 5138 CONECT 5137 4608 CONECT 5138 4608 CONECT 5538 6059 CONECT 6059 5538 CONECT 6231 6236 6238 6239 CONECT 6232 6233 6237 CONECT 6233 368 6232 6234 CONECT 6234 6233 CONECT 6235 6240 6242 CONECT 6236 6231 6240 CONECT 6237 6232 6238 CONECT 6238 6231 6237 6242 CONECT 6239 6231 CONECT 6240 6235 6236 6241 CONECT 6241 6240 CONECT 6242 6235 6238 6243 CONECT 6243 6242 6244 CONECT 6244 6243 6245 CONECT 6245 6244 6246 6247 CONECT 6246 6245 CONECT 6247 6245 6248 6249 CONECT 6248 6247 CONECT 6249 6247 6250 6251 CONECT 6250 6249 CONECT 6251 6249 6252 CONECT 6252 6251 CONECT 6253 6254 6255 CONECT 6254 6253 CONECT 6255 6253 6256 6257 CONECT 6256 6255 CONECT 6257 6255 6258 CONECT 6258 6257 CONECT 6259 6260 6261 CONECT 6260 6259 CONECT 6261 6259 6262 6263 CONECT 6262 6261 CONECT 6263 6261 6264 CONECT 6264 6263 CONECT 6265 2876 2881 2905 6649 CONECT 6265 6661 CONECT 6649 6265 CONECT 6661 6265 MASTER 801 0 4 13 76 0 11 6 6944 4 57 64 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
4pj7
RCSB PDB
PDBbind
MR1-5-OP-RU
4pj8
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MR1-5-OP-RU
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Entry Information
PDB ID
4pj9
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
MAIT TRAJ20 TCR
Ligand Name
MR1-5-OP-RU
EC.Number
E.C.-.-.-.-
Resolution
2(Å)
Affinity (Kd/Ki/IC50)
Kd=2.4uM
Release Year
2014
Protein/NA Sequence
Check fasta file
Primary Reference
(2014) J.Exp.Med. Vol. 211: pp. 1585-1600
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q95460
P61769
Entrez Gene ID
NCBI Entrez Gene ID:
3140
567
ASD
Information of known allosteric effects of PDB entries
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