HEADER IMMUNE SYSTEM 26-APR-07 2YXF TITLE THE HIGH RESOLUTION CRYSTAL STRUCTURE OF BETA2- TITLE 2 MICROGLOBULIN UNDER PHYSIOLOGICAL CONDITIONS COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 3 CHAIN: A; COMPND 4 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: B2M; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHIKARU1A KEYWDS IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR K.IWATA,T.MATSUURA,A.NAKAGAWA,Y.GOTO REVDAT 2 24-FEB-09 2YXF 1 VERSN REVDAT 1 30-OCT-07 2YXF 0 JRNL AUTH K.IWATA,T.MATSUURA,K.SAKURAI,A.NAKAGAWA,Y.GOTO JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF JRNL TITL 2 {BETA}2-MICROGLOBULIN FORMED AT PH 7.0 JRNL REF J.BIOCHEM.(TOKYO) V. 142 413 2007 JRNL REFN ISSN 0021-924X JRNL PMID 17646174 JRNL DOI 10.1093/JB/MVM148 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.13 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.13 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.49 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 36904 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) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.195 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1948 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.13 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.16 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2701 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.1880 REMARK 3 BIN FREE R VALUE SET COUNT : 152 REMARK 3 BIN FREE R VALUE : 0.2210 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 828 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 91 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 9.46 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.11 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.38000 REMARK 3 B22 (A**2) : 0.23000 REMARK 3 B33 (A**2) : 0.12000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.03000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.038 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.035 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.910 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 853 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 591 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1156 ; 1.227 ; 1.942 REMARK 3 BOND ANGLES OTHERS (DEGREES): 1431 ; 0.744 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 98 ; 6.909 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 45 ;33.353 ;24.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 148 ;11.286 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;21.752 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 120 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 939 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 180 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 132 ; 0.200 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 596 ; 0.195 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 399 ; 0.175 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 467 ; 0.084 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 67 ; 0.139 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 7 ; 0.207 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 30 ; 0.142 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.150 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 646 ; 1.187 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 195 ; 0.302 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 812 ; 1.369 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 431 ; 1.978 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 344 ; 2.541 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1836 ; 2.029 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 91 ; 2.980 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1420 ; 1.845 ; 3.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 2YXF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-07. REMARK 100 THE RCSB ID CODE IS RCSB027255. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-DEC-05 REMARK 200 TEMPERATURE (KELVIN) : 90.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL44XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.65 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38852 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.130 REMARK 200 RESOLUTION RANGE LOW (A) : 26.630 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.05100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.13 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.33200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 2D4F REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 25% GLYCEROL, 0.06M REMARK 280 AMMONIUMACETATE, 0.1M MOPS, PH 7.00, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 288K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.82200 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 14.45350 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.82200 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 14.45350 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 99 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 SER A 57 -91.98 -105.61 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2D4F RELATED DB: PDB REMARK 900 THE SAME PROTEIN AT 1.7A RESOLUTION DBREF 2YXF A 1 99 UNP P61769 B2MG_HUMAN 21 119 SEQADV 2YXF MET A 0 UNP P61769 EXPRESSION TAG SEQRES 1 A 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 A 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 A 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 A 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 A 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 A 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 A 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 A 100 LYS ILE VAL LYS TRP ASP ARG ASP MET FORMUL 2 HOH *91(H2 O) HELIX 1 1 PRO A 14 GLY A 18 5 5 SHEET 1 A 4 LYS A 6 ARG A 12 0 SHEET 2 A 4 PHE A 22 PHE A 30 -1 O ASN A 24 N TYR A 10 SHEET 3 A 4 PHE A 62 GLU A 69 -1 O LEU A 64 N VAL A 27 SHEET 4 A 4 HIS A 51 PHE A 56 -1 N ASP A 53 O LEU A 65 SHEET 1 B 4 GLU A 44 ARG A 45 0 SHEET 2 B 4 GLU A 36 LYS A 41 -1 N LYS A 41 O GLU A 44 SHEET 3 B 4 TYR A 78 ASN A 83 -1 O ALA A 79 N LEU A 40 SHEET 4 B 4 LYS A 91 LYS A 94 -1 O VAL A 93 N CYS A 80 SSBOND 1 CYS A 25 CYS A 80 1555 1555 2.02 CISPEP 1 HIS A 31 PRO A 32 0 -3.05 CRYST1 77.644 28.907 54.397 90.00 121.59 90.00 C 1 2 1 4 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 0.012879 0.000000 0.007920 0.00000 SCALE2 0.000000 0.034593 0.000000 0.00000 SCALE3 0.000000 0.000000 0.021581 0.00000 ATOM 1 N MET A 0 24.889 -22.648 9.921 1.00 10.99 N ANISOU 1 N MET A 0 1451 1219 1503 -12 -278 -32 N ATOM 2 CA MET A 0 24.226 -22.121 8.700 1.00 10.68 C ANISOU 2 CA MET A 0 1372 1173 1509 -5 -174 -41 C ATOM 3 C MET A 0 23.037 -22.993 8.332 1.00 9.77 C ANISOU 3 C MET A 0 1272 1041 1398 10 -115 -37 C ATOM 4 O MET A 0 22.963 -24.164 8.697 1.00 9.73 O ANISOU 4 O MET A 0 1237 1007 1453 16 -160 -16 O ATOM 5 CB MET A 0 25.217 -22.048 7.527 1.00 11.61 C ANISOU 5 CB MET A 0 1438 1317 1656 -33 -139 -51 C ATOM 6 CG MET A 0 25.759 -23.386 7.031 1.00 11.68 C ANISOU 6 CG MET A 0 1462 1366 1607 -27 -56 14 C ATOM 7 SD MET A 0 24.652 -24.337 5.959 1.00 12.08 S ANISOU 7 SD MET A 0 1476 1423 1689 3 -56 -77 S ATOM 8 CE MET A 0 24.824 -23.463 4.407 1.00 13.52 C ANISOU 8 CE MET A 0 1779 1714 1641 12 28 -160 C ATOM 9 N ILE A 1 22.098 -22.393 7.613 1.00 9.56 N ANISOU 9 N ILE A 1 1262 987 1382 28 -169 -80 N ATOM 10 CA ILE A 1 20.994 -23.130 7.033 1.00 9.72 C ANISOU 10 CA ILE A 1 1278 1064 1351 27 -95 -22 C ATOM 11 C ILE A 1 20.689 -22.543 5.665 1.00 8.83 C ANISOU 11 C ILE A 1 1157 908 1288 4 -72 -3 C ATOM 12 O ILE A 1 20.796 -21.325 5.449 1.00 9.30 O ANISOU 12 O ILE A 1 1307 818 1408 31 -153 23 O ATOM 13 CB ILE A 1 19.761 -23.117 7.958 1.00 10.57 C ANISOU 13 CB ILE A 1 1394 1244 1378 50 -82 -25 C ATOM 14 CG1 ILE A 1 18.703 -24.108 7.469 1.00 11.84 C ANISOU 14 CG1 ILE A 1 1519 1420 1556 15 -1 4 C ATOM 15 CG2 ILE A 1 19.197 -21.717 8.091 1.00 12.08 C ANISOU 15 CG2 ILE A 1 1602 1349 1637 97 -13 -5 C ATOM 16 CD1 ILE A 1 17.663 -24.440 8.519 1.00 12.63 C ANISOU 16 CD1 ILE A 1 1594 1555 1647 -11 21 24 C ATOM 17 N GLN A 2 20.331 -23.411 4.734 1.00 8.03 N ANISOU 17 N GLN A 2 1020 864 1164 8 -75 24 N ATOM 18 CA GLN A 2 19.861 -22.949 3.449 1.00 8.38 C ANISOU 18 CA GLN A 2 1066 926 1191 0 -41 30 C ATOM 19 C GLN A 2 18.662 -23.774 3.024 1.00 7.62 C ANISOU 19 C GLN A 2 958 855 1079 -10 -38 80 C ATOM 20 O GLN A 2 18.589 -24.990 3.259 1.00 7.67 O ANISOU 20 O GLN A 2 960 843 1110 -19 -98 80 O ATOM 21 CB GLN A 2 20.972 -22.932 2.401 1.00 8.49 C ANISOU 21 CB GLN A 2 1065 975 1183 -39 -50 40 C ATOM 22 CG GLN A 2 21.567 -24.287 2.126 1.00 9.06 C ANISOU 22 CG GLN A 2 1240 1016 1185 -84 5 18 C ATOM 23 CD GLN A 2 22.830 -24.216 1.285 1.00 9.43 C ANISOU 23 CD GLN A 2 1251 1023 1309 -96 113 -76 C ATOM 24 OE1 GLN A 2 23.557 -23.220 1.304 1.00 11.58 O ANISOU 24 OE1 GLN A 2 1595 1181 1624 -259 244 -103 O ATOM 25 NE2 GLN A 2 23.105 -25.283 0.557 1.00 9.37 N ANISOU 25 NE2 GLN A 2 1250 925 1383 -59 137 -100 N ATOM 26 N ARG A 3 17.701 -23.073 2.438 1.00 7.74 N ANISOU 26 N ARG A 3 945 835 1158 21 -74 44 N ATOM 27 CA ARG A 3 16.426 -23.655 2.043 1.00 9.17 C ANISOU 27 CA ARG A 3 1104 1109 1271 4 -67 11 C ATOM 28 C ARG A 3 16.047 -23.106 0.677 1.00 8.43 C ANISOU 28 C ARG A 3 1011 994 1196 21 -78 33 C ATOM 29 O ARG A 3 16.056 -21.891 0.463 1.00 8.43 O ANISOU 29 O ARG A 3 1119 920 1161 -1 -199 50 O ATOM 30 CB ARG A 3 15.339 -23.296 3.053 1.00 9.64 C ANISOU 30 CB ARG A 3 1084 1205 1371 31 -6 51 C ATOM 31 CG ARG A 3 15.622 -23.789 4.478 1.00 13.02 C ANISOU 31 CG ARG A 3 1602 1697 1646 -24 -15 35 C ATOM 32 CD ARG A 3 14.611 -23.305 5.478 1.00 15.73 C ANISOU 32 CD ARG A 3 1955 2140 1880 -30 73 -19 C ATOM 33 NE ARG A 3 14.250 -21.936 5.180 1.00 20.30 N ANISOU 33 NE ARG A 3 2545 2603 2564 -20 3 48 N ATOM 34 CZ ARG A 3 13.035 -21.425 5.302 1.00 21.57 C ANISOU 34 CZ ARG A 3 2755 2689 2750 47 32 15 C ATOM 35 NH1 ARG A 3 11.999 -22.137 5.740 1.00 22.89 N ANISOU 35 NH1 ARG A 3 2929 2859 2907 -16 54 11 N ATOM 36 NH2 ARG A 3 12.867 -20.172 4.948 1.00 21.99 N ANISOU 36 NH2 ARG A 3 2760 2702 2891 46 34 18 N ATOM 37 N THR A 4 15.713 -24.017 -0.229 1.00 8.77 N ANISOU 37 N THR A 4 1095 1084 1153 92 -90 5 N ATOM 38 CA THR A 4 15.298 -23.695 -1.584 1.00 9.67 C ANISOU 38 CA THR A 4 1190 1224 1258 93 -70 17 C ATOM 39 C THR A 4 13.930 -23.015 -1.542 1.00 9.39 C ANISOU 39 C THR A 4 1195 1142 1231 91 -104 0 C ATOM 40 O THR A 4 13.037 -23.474 -0.842 1.00 9.45 O ANISOU 40 O THR A 4 1098 1236 1254 135 -59 18 O ATOM 41 CB THR A 4 15.155 -25.019 -2.418 1.00 10.46 C ANISOU 41 CB THR A 4 1346 1344 1283 210 -4 -6 C ATOM 42 OG1 THR A 4 16.396 -25.739 -2.438 1.00 11.67 O ANISOU 42 OG1 THR A 4 1442 1480 1511 181 -32 -7 O ATOM 43 CG2 THR A 4 14.683 -24.769 -3.842 1.00 11.18 C ANISOU 43 CG2 THR A 4 1495 1360 1391 107 -83 7 C ATOM 44 N PRO A 5 13.745 -21.919 -2.298 1.00 9.98 N ANISOU 44 N PRO A 5 1306 1192 1292 59 -167 3 N ATOM 45 CA PRO A 5 12.439 -21.283 -2.366 1.00 10.61 C ANISOU 45 CA PRO A 5 1439 1208 1381 100 -186 -27 C ATOM 46 C PRO A 5 11.376 -22.167 -3.007 1.00 10.71 C ANISOU 46 C PRO A 5 1474 1248 1347 114 -205 -70 C ATOM 47 O PRO A 5 11.656 -22.833 -3.998 1.00 10.92 O ANISOU 47 O PRO A 5 1490 1278 1380 198 -254 -178 O ATOM 48 CB PRO A 5 12.697 -20.068 -3.274 1.00 11.24 C ANISOU 48 CB PRO A 5 1567 1227 1473 22 -301 4 C ATOM 49 CG PRO A 5 13.891 -20.408 -4.053 1.00 12.21 C ANISOU 49 CG PRO A 5 1751 1359 1527 -79 -142 49 C ATOM 50 CD PRO A 5 14.733 -21.204 -3.125 1.00 10.91 C ANISOU 50 CD PRO A 5 1485 1280 1377 -22 -120 -13 C ATOM 51 N LYS A 6 10.171 -22.165 -2.448 1.00 10.87 N ANISOU 51 N LYS A 6 1527 1225 1377 122 -163 -67 N ATOM 52 CA LYS A 6 8.986 -22.618 -3.172 1.00 10.88 C ANISOU 52 CA LYS A 6 1487 1218 1428 91 -145 -20 C ATOM 53 C LYS A 6 8.528 -21.442 -4.028 1.00 9.47 C ANISOU 53 C LYS A 6 1231 1079 1287 92 -153 -26 C ATOM 54 O LYS A 6 8.620 -20.290 -3.604 1.00 8.95 O ANISOU 54 O LYS A 6 1173 1012 1213 74 -187 -48 O ATOM 55 CB LYS A 6 7.885 -23.045 -2.201 1.00 11.98 C ANISOU 55 CB LYS A 6 1680 1330 1540 110 -82 11 C ATOM 56 CG LYS A 6 6.614 -23.570 -2.864 1.00 13.46 C ANISOU 56 CG LYS A 6 1776 1594 1742 70 -79 0 C ATOM 57 CD LYS A 6 5.532 -23.871 -1.831 1.00 14.91 C ANISOU 57 CD LYS A 6 1934 1834 1897 -8 5 10 C ATOM 58 CE LYS A 6 4.306 -24.487 -2.478 1.00 16.71 C ANISOU 58 CE LYS A 6 2051 2060 2235 -44 -12 0 C ATOM 59 NZ LYS A 6 3.277 -24.917 -1.488 1.00 18.43 N ANISOU 59 NZ LYS A 6 2230 2372 2399 -77 38 56 N ATOM 60 N ILE A 7 8.070 -21.733 -5.240 1.00 9.26 N ANISOU 60 N ILE A 7 1196 1011 1311 96 -168 -41 N ATOM 61 CA ILE A 7 7.716 -20.700 -6.203 1.00 9.53 C ANISOU 61 CA ILE A 7 1201 1103 1316 43 -156 -52 C ATOM 62 C ILE A 7 6.312 -20.972 -6.734 1.00 9.61 C ANISOU 62 C ILE A 7 1183 1133 1333 -1 -162 -55 C ATOM 63 O ILE A 7 6.042 -22.046 -7.265 1.00 10.65 O ANISOU 63 O ILE A 7 1327 1182 1535 34 -251 -165 O ATOM 64 CB ILE A 7 8.722 -20.682 -7.365 1.00 9.64 C ANISOU 64 CB ILE A 7 1230 1108 1324 45 -117 -80 C ATOM 65 CG1 ILE A 7 10.148 -20.445 -6.859 1.00 10.02 C ANISOU 65 CG1 ILE A 7 1242 1189 1374 33 -75 -84 C ATOM 66 CG2 ILE A 7 8.357 -19.598 -8.375 1.00 10.33 C ANISOU 66 CG2 ILE A 7 1389 1168 1365 96 -100 -25 C ATOM 67 CD1 ILE A 7 11.206 -20.808 -7.874 1.00 10.65 C ANISOU 67 CD1 ILE A 7 1295 1270 1480 -3 -27 -82 C ATOM 68 N GLN A 8 5.418 -20.000 -6.584 1.00 9.24 N ANISOU 68 N GLN A 8 1029 1159 1320 -13 -161 -25 N ATOM 69 CA GLN A 8 4.043 -20.098 -7.065 1.00 9.90 C ANISOU 69 CA GLN A 8 1137 1242 1381 -2 -136 2 C ATOM 70 C GLN A 8 3.753 -18.894 -7.935 1.00 9.39 C ANISOU 70 C GLN A 8 1056 1187 1324 45 -137 -25 C ATOM 71 O GLN A 8 4.093 -17.770 -7.567 1.00 9.74 O ANISOU 71 O GLN A 8 1154 1198 1345 10 -234 29 O ATOM 72 CB GLN A 8 3.074 -20.148 -5.888 1.00 10.30 C ANISOU 72 CB GLN A 8 1143 1321 1446 -50 -131 15 C ATOM 73 CG GLN A 8 3.223 -21.407 -5.056 1.00 11.73 C ANISOU 73 CG GLN A 8 1414 1441 1601 -74 -48 20 C ATOM 74 CD GLN A 8 2.474 -21.333 -3.752 1.00 12.36 C ANISOU 74 CD GLN A 8 1463 1605 1625 -81 -26 74 C ATOM 75 OE1 GLN A 8 2.894 -20.652 -2.823 1.00 14.52 O ANISOU 75 OE1 GLN A 8 1775 1936 1804 -211 49 -17 O ATOM 76 NE2 GLN A 8 1.367 -22.054 -3.665 1.00 16.43 N ANISOU 76 NE2 GLN A 8 1789 2162 2289 -258 125 47 N ATOM 77 N VAL A 9 3.123 -19.139 -9.081 1.00 9.02 N ANISOU 77 N VAL A 9 1005 1120 1301 16 -143 6 N ATOM 78 CA VAL A 9 2.826 -18.093 -10.047 1.00 9.40 C ANISOU 78 CA VAL A 9 1017 1222 1332 19 -129 -3 C ATOM 79 C VAL A 9 1.328 -18.120 -10.323 1.00 9.30 C ANISOU 79 C VAL A 9 995 1177 1361 5 -123 -2 C ATOM 80 O VAL A 9 0.763 -19.160 -10.657 1.00 10.15 O ANISOU 80 O VAL A 9 1061 1285 1509 -25 -168 -108 O ATOM 81 CB VAL A 9 3.614 -18.315 -11.348 1.00 9.59 C ANISOU 81 CB VAL A 9 1077 1253 1312 28 -134 -21 C ATOM 82 CG1 VAL A 9 3.370 -17.169 -12.330 1.00 11.03 C ANISOU 82 CG1 VAL A 9 1359 1392 1437 70 -88 59 C ATOM 83 CG2 VAL A 9 5.104 -18.469 -11.046 1.00 10.04 C ANISOU 83 CG2 VAL A 9 1085 1392 1338 58 -126 -45 C ATOM 84 N TYR A 10 0.679 -16.975 -10.167 1.00 9.19 N ANISOU 84 N TYR A 10 934 1178 1378 34 -122 -8 N ATOM 85 CA TYR A 10 -0.780 -16.915 -10.242 1.00 9.52 C ANISOU 85 CA TYR A 10 987 1266 1362 56 -71 44 C ATOM 86 C TYR A 10 -1.238 -15.504 -10.536 1.00 9.31 C ANISOU 86 C TYR A 10 934 1275 1327 67 -59 93 C ATOM 87 O TYR A 10 -0.466 -14.552 -10.428 1.00 9.71 O ANISOU 87 O TYR A 10 978 1335 1376 46 -92 200 O ATOM 88 CB TYR A 10 -1.403 -17.412 -8.931 1.00 10.09 C ANISOU 88 CB TYR A 10 1069 1328 1433 63 -26 62 C ATOM 89 CG TYR A 10 -0.939 -16.664 -7.705 1.00 9.98 C ANISOU 89 CG TYR A 10 1067 1368 1355 0 -1 127 C ATOM 90 CD1 TYR A 10 0.208 -17.057 -7.029 1.00 11.04 C ANISOU 90 CD1 TYR A 10 1153 1466 1575 32 -44 124 C ATOM 91 CD2 TYR A 10 -1.635 -15.561 -7.224 1.00 10.03 C ANISOU 91 CD2 TYR A 10 1056 1413 1342 16 10 109 C ATOM 92 CE1 TYR A 10 0.643 -16.384 -5.908 1.00 12.17 C ANISOU 92 CE1 TYR A 10 1420 1612 1590 -16 -83 86 C ATOM 93 CE2 TYR A 10 -1.201 -14.871 -6.098 1.00 10.76 C ANISOU 93 CE2 TYR A 10 1254 1452 1381 -8 -3 105 C ATOM 94 CZ TYR A 10 -0.055 -15.292 -5.443 1.00 11.45 C ANISOU 94 CZ TYR A 10 1282 1606 1461 -91 -51 55 C ATOM 95 OH TYR A 10 0.391 -14.636 -4.321 1.00 13.07 O ANISOU 95 OH TYR A 10 1629 1869 1466 -115 -121 38 O ATOM 96 N SER A 11 -2.503 -15.370 -10.918 1.00 9.48 N ANISOU 96 N SER A 11 939 1291 1371 73 -40 100 N ATOM 97 CA SER A 11 -3.066 -14.068 -11.236 1.00 9.67 C ANISOU 97 CA SER A 11 1018 1305 1349 87 -12 96 C ATOM 98 C SER A 11 -4.195 -13.732 -10.277 1.00 9.51 C ANISOU 98 C SER A 11 966 1348 1297 56 10 128 C ATOM 99 O SER A 11 -4.872 -14.622 -9.755 1.00 10.30 O ANISOU 99 O SER A 11 1036 1363 1512 50 62 151 O ATOM 100 CB SER A 11 -3.552 -14.034 -12.681 1.00 10.25 C ANISOU 100 CB SER A 11 1116 1401 1377 171 -8 90 C ATOM 101 OG SER A 11 -4.594 -14.959 -12.892 1.00 12.07 O ANISOU 101 OG SER A 11 1387 1573 1623 122 -192 119 O ATOM 102 N ARG A 12 -4.374 -12.441 -10.024 1.00 9.23 N ANISOU 102 N ARG A 12 905 1326 1276 53 67 124 N ATOM 103 CA ARG A 12 -5.449 -11.953 -9.159 1.00 9.55 C ANISOU 103 CA ARG A 12 1007 1329 1291 59 77 105 C ATOM 104 C ARG A 12 -6.008 -10.657 -9.703 1.00 9.60 C ANISOU 104 C ARG A 12 1001 1333 1310 48 90 129 C ATOM 105 O ARG A 12 -5.264 -9.798 -10.188 1.00 10.41 O ANISOU 105 O ARG A 12 995 1442 1518 7 96 173 O ATOM 106 CB ARG A 12 -4.939 -11.662 -7.752 1.00 9.94 C ANISOU 106 CB ARG A 12 1049 1399 1328 85 79 43 C ATOM 107 CG ARG A 12 -4.429 -12.859 -6.991 1.00 10.54 C ANISOU 107 CG ARG A 12 1190 1465 1349 93 47 91 C ATOM 108 CD ARG A 12 -5.543 -13.769 -6.554 1.00 11.29 C ANISOU 108 CD ARG A 12 1210 1574 1504 68 33 101 C ATOM 109 NE ARG A 12 -5.046 -14.839 -5.697 1.00 12.44 N ANISOU 109 NE ARG A 12 1352 1709 1665 49 72 204 N ATOM 110 CZ ARG A 12 -4.788 -16.075 -6.105 1.00 12.55 C ANISOU 110 CZ ARG A 12 1348 1627 1792 -63 91 255 C ATOM 111 NH1 ARG A 12 -4.962 -16.446 -7.365 1.00 13.11 N ANISOU 111 NH1 ARG A 12 1354 1606 2019 40 60 152 N ATOM 112 NH2 ARG A 12 -4.346 -16.964 -5.227 1.00 13.83 N ANISOU 112 NH2 ARG A 12 1627 1734 1893 76 -9 320 N ATOM 113 N HIS A 13 -7.326 -10.516 -9.587 1.00 9.15 N ANISOU 113 N HIS A 13 948 1280 1248 46 74 115 N ATOM 114 CA HIS A 13 -8.026 -9.263 -9.842 1.00 9.59 C ANISOU 114 CA HIS A 13 1069 1314 1261 70 87 133 C ATOM 115 C HIS A 13 -8.386 -8.646 -8.496 1.00 9.55 C ANISOU 115 C HIS A 13 1089 1282 1255 72 109 135 C ATOM 116 O HIS A 13 -9.086 -9.279 -7.703 1.00 9.79 O ANISOU 116 O HIS A 13 1189 1295 1235 41 175 120 O ATOM 117 CB HIS A 13 -9.336 -9.515 -10.594 1.00 9.82 C ANISOU 117 CB HIS A 13 1037 1396 1298 86 73 132 C ATOM 118 CG HIS A 13 -9.171 -10.243 -11.886 1.00 10.80 C ANISOU 118 CG HIS A 13 1202 1570 1330 98 136 129 C ATOM 119 ND1 HIS A 13 -8.913 -9.597 -13.076 1.00 12.52 N ANISOU 119 ND1 HIS A 13 1552 1751 1453 5 28 161 N ATOM 120 CD2 HIS A 13 -9.246 -11.562 -12.181 1.00 12.69 C ANISOU 120 CD2 HIS A 13 1540 1734 1544 -44 125 95 C ATOM 121 CE1 HIS A 13 -8.835 -10.490 -14.045 1.00 13.25 C ANISOU 121 CE1 HIS A 13 1629 1849 1556 72 35 -13 C ATOM 122 NE2 HIS A 13 -9.023 -11.689 -13.529 1.00 14.10 N ANISOU 122 NE2 HIS A 13 1772 1893 1691 2 133 -98 N ATOM 123 N PRO A 14 -7.940 -7.412 -8.222 1.00 10.20 N ANISOU 123 N PRO A 14 1214 1313 1347 34 170 112 N ATOM 124 CA PRO A 14 -8.366 -6.797 -6.962 1.00 10.83 C ANISOU 124 CA PRO A 14 1338 1371 1406 58 135 106 C ATOM 125 C PRO A 14 -9.871 -6.564 -7.002 1.00 11.09 C ANISOU 125 C PRO A 14 1357 1431 1424 94 158 83 C ATOM 126 O PRO A 14 -10.399 -6.101 -8.010 1.00 11.67 O ANISOU 126 O PRO A 14 1432 1522 1479 219 240 209 O ATOM 127 CB PRO A 14 -7.592 -5.476 -6.929 1.00 11.43 C ANISOU 127 CB PRO A 14 1415 1420 1505 6 143 71 C ATOM 128 CG PRO A 14 -7.287 -5.185 -8.337 1.00 12.15 C ANISOU 128 CG PRO A 14 1537 1486 1594 -16 139 91 C ATOM 129 CD PRO A 14 -7.098 -6.501 -9.013 1.00 10.97 C ANISOU 129 CD PRO A 14 1332 1388 1445 -15 134 117 C ATOM 130 N ALA A 15 -10.568 -6.919 -5.934 1.00 11.40 N ANISOU 130 N ALA A 15 1423 1469 1439 109 146 154 N ATOM 131 CA ALA A 15 -12.030 -6.863 -5.946 1.00 12.36 C ANISOU 131 CA ALA A 15 1506 1632 1557 89 128 111 C ATOM 132 C ALA A 15 -12.578 -5.447 -6.132 1.00 13.17 C ANISOU 132 C ALA A 15 1644 1727 1630 116 133 115 C ATOM 133 O ALA A 15 -13.669 -5.284 -6.667 1.00 13.65 O ANISOU 133 O ALA A 15 1620 1836 1729 168 156 114 O ATOM 134 CB ALA A 15 -12.593 -7.486 -4.680 1.00 12.35 C ANISOU 134 CB ALA A 15 1511 1657 1523 97 109 144 C ATOM 135 N GLU A 16 -11.824 -4.441 -5.695 1.00 14.55 N ANISOU 135 N GLU A 16 1821 1860 1847 112 125 71 N ATOM 136 CA GLU A 16 -12.228 -3.041 -5.852 1.00 15.90 C ANISOU 136 CA GLU A 16 2038 1953 2050 99 76 56 C ATOM 137 C GLU A 16 -12.034 -2.520 -7.281 1.00 16.53 C ANISOU 137 C GLU A 16 2135 2019 2125 113 88 68 C ATOM 138 O GLU A 16 -12.558 -1.460 -7.631 1.00 17.61 O ANISOU 138 O GLU A 16 2322 2069 2299 141 77 91 O ATOM 139 CB GLU A 16 -11.488 -2.141 -4.846 1.00 17.21 C ANISOU 139 CB GLU A 16 2256 2099 2183 67 62 25 C ATOM 140 CG GLU A 16 -9.979 -1.985 -5.059 1.00 19.66 C ANISOU 140 CG GLU A 16 2500 2466 2502 0 53 6 C ATOM 141 CD GLU A 16 -9.133 -3.104 -4.455 1.00 21.94 C ANISOU 141 CD GLU A 16 2776 2772 2787 42 12 26 C ATOM 142 OE1 GLU A 16 -7.904 -2.905 -4.338 1.00 24.07 O ANISOU 142 OE1 GLU A 16 2963 3064 3116 -3 -42 16 O ATOM 143 OE2 GLU A 16 -9.675 -4.178 -4.111 1.00 23.00 O ANISOU 143 OE2 GLU A 16 2946 2903 2890 -49 34 14 O ATOM 144 N ASN A 17 -11.285 -3.258 -8.099 1.00 16.64 N ANISOU 144 N ASN A 17 2151 2038 2132 119 74 68 N ATOM 145 CA ASN A 17 -11.036 -2.875 -9.485 1.00 16.53 C ANISOU 145 CA ASN A 17 2136 2040 2103 95 69 66 C ATOM 146 C ASN A 17 -10.864 -4.134 -10.327 1.00 15.92 C ANISOU 146 C ASN A 17 2036 1976 2034 118 70 93 C ATOM 147 O ASN A 17 -9.762 -4.459 -10.773 1.00 15.40 O ANISOU 147 O ASN A 17 1965 1927 1958 130 118 126 O ATOM 148 CB ASN A 17 -9.798 -1.975 -9.565 1.00 17.40 C ANISOU 148 CB ASN A 17 2223 2151 2235 77 66 40 C ATOM 149 CG ASN A 17 -9.605 -1.353 -10.942 1.00 18.48 C ANISOU 149 CG ASN A 17 2394 2284 2342 68 61 66 C ATOM 150 OD1 ASN A 17 -10.483 -1.420 -11.801 1.00 22.00 O ANISOU 150 OD1 ASN A 17 2762 2854 2742 76 -49 46 O ATOM 151 ND2 ASN A 17 -8.441 -0.752 -11.157 1.00 21.59 N ANISOU 151 ND2 ASN A 17 2654 2723 2823 -41 34 21 N ATOM 152 N GLY A 18 -11.972 -4.834 -10.543 1.00 15.23 N ANISOU 152 N GLY A 18 1954 1894 1938 112 81 106 N ATOM 153 CA GLY A 18 -11.951 -6.189 -11.077 1.00 15.56 C ANISOU 153 CA GLY A 18 1942 1970 2000 100 57 81 C ATOM 154 C GLY A 18 -11.457 -6.331 -12.497 1.00 15.48 C ANISOU 154 C GLY A 18 1924 1978 1976 81 37 110 C ATOM 155 O GLY A 18 -11.091 -7.430 -12.906 1.00 15.69 O ANISOU 155 O GLY A 18 1893 2049 2019 115 58 96 O ATOM 156 N LYS A 19 -11.464 -5.235 -13.256 1.00 15.30 N ANISOU 156 N LYS A 19 1826 2003 1984 138 44 128 N ATOM 157 CA LYS A 19 -10.934 -5.242 -14.617 1.00 15.61 C ANISOU 157 CA LYS A 19 1895 2027 2006 122 24 100 C ATOM 158 C LYS A 19 -9.410 -5.319 -14.630 1.00 15.47 C ANISOU 158 C LYS A 19 1862 2006 2009 152 60 94 C ATOM 159 O LYS A 19 -8.818 -5.780 -15.607 1.00 16.83 O ANISOU 159 O LYS A 19 2029 2274 2091 145 107 52 O ATOM 160 CB LYS A 19 -11.412 -4.007 -15.388 1.00 16.43 C ANISOU 160 CB LYS A 19 2051 2117 2072 133 36 112 C ATOM 161 CG LYS A 19 -12.913 -3.986 -15.637 1.00 18.54 C ANISOU 161 CG LYS A 19 2257 2402 2383 93 -17 115 C ATOM 162 CD LYS A 19 -13.284 -4.944 -16.752 1.00 20.35 C ANISOU 162 CD LYS A 19 2531 2601 2597 19 1 29 C ATOM 163 CE LYS A 19 -14.776 -5.170 -16.844 1.00 20.81 C ANISOU 163 CE LYS A 19 2540 2684 2683 -17 -40 26 C ATOM 164 NZ LYS A 19 -15.061 -6.419 -17.596 1.00 21.97 N ANISOU 164 NZ LYS A 19 2765 2802 2778 -38 -43 -30 N ATOM 165 N SER A 20 -8.777 -4.853 -13.559 1.00 14.24 N ANISOU 165 N SER A 20 1665 1808 1935 171 83 130 N ATOM 166 CA SER A 20 -7.330 -4.966 -13.424 1.00 14.17 C ANISOU 166 CA SER A 20 1668 1774 1940 129 35 149 C ATOM 167 C SER A 20 -6.944 -6.403 -13.100 1.00 12.99 C ANISOU 167 C SER A 20 1489 1646 1801 100 56 176 C ATOM 168 O SER A 20 -7.696 -7.129 -12.445 1.00 12.82 O ANISOU 168 O SER A 20 1442 1595 1832 114 108 253 O ATOM 169 CB SER A 20 -6.815 -4.040 -12.329 1.00 15.04 C ANISOU 169 CB SER A 20 1756 1856 2101 141 6 92 C ATOM 170 OG SER A 20 -6.887 -2.686 -12.734 1.00 18.74 O ANISOU 170 OG SER A 20 2382 2142 2595 74 -33 126 O ATOM 171 N ASN A 21 -5.763 -6.800 -13.558 1.00 12.20 N ANISOU 171 N ASN A 21 1357 1577 1699 68 33 208 N ATOM 172 CA ASN A 21 -5.254 -8.152 -13.369 1.00 11.76 C ANISOU 172 CA ASN A 21 1279 1554 1632 72 4 163 C ATOM 173 C ASN A 21 -3.781 -8.060 -13.019 1.00 11.06 C ANISOU 173 C ASN A 21 1179 1475 1547 59 22 178 C ATOM 174 O ASN A 21 -3.047 -7.280 -13.624 1.00 11.07 O ANISOU 174 O ASN A 21 1140 1496 1567 38 -6 254 O ATOM 175 CB ASN A 21 -5.451 -8.955 -14.658 1.00 12.11 C ANISOU 175 CB ASN A 21 1283 1643 1674 67 -27 130 C ATOM 176 CG ASN A 21 -5.462 -10.459 -14.436 1.00 12.74 C ANISOU 176 CG ASN A 21 1427 1695 1717 75 -22 101 C ATOM 177 OD1 ASN A 21 -5.267 -10.948 -13.322 1.00 14.30 O ANISOU 177 OD1 ASN A 21 1702 1920 1809 91 -212 130 O ATOM 178 ND2 ASN A 21 -5.702 -11.203 -15.511 1.00 14.29 N ANISOU 178 ND2 ASN A 21 1562 1988 1876 71 -99 18 N ATOM 179 N PHE A 22 -3.356 -8.843 -12.035 1.00 10.35 N ANISOU 179 N PHE A 22 1061 1377 1493 49 -6 179 N ATOM 180 CA PHE A 22 -1.986 -8.809 -11.556 1.00 10.10 C ANISOU 180 CA PHE A 22 1092 1322 1423 50 20 110 C ATOM 181 C PHE A 22 -1.357 -10.174 -11.658 1.00 9.36 C ANISOU 181 C PHE A 22 1018 1232 1306 39 15 143 C ATOM 182 O PHE A 22 -1.961 -11.173 -11.280 1.00 9.47 O ANISOU 182 O PHE A 22 968 1181 1448 90 56 168 O ATOM 183 CB PHE A 22 -1.957 -8.320 -10.118 1.00 11.27 C ANISOU 183 CB PHE A 22 1249 1486 1546 17 28 58 C ATOM 184 CG PHE A 22 -2.274 -6.864 -9.994 1.00 11.83 C ANISOU 184 CG PHE A 22 1395 1466 1631 55 62 46 C ATOM 185 CD1 PHE A 22 -1.265 -5.938 -9.790 1.00 12.73 C ANISOU 185 CD1 PHE A 22 1568 1516 1750 -7 61 0 C ATOM 186 CD2 PHE A 22 -3.577 -6.404 -10.149 1.00 13.20 C ANISOU 186 CD2 PHE A 22 1605 1597 1813 154 26 16 C ATOM 187 CE1 PHE A 22 -1.553 -4.585 -9.696 1.00 14.06 C ANISOU 187 CE1 PHE A 22 1800 1593 1948 -4 53 19 C ATOM 188 CE2 PHE A 22 -3.865 -5.053 -10.063 1.00 13.65 C ANISOU 188 CE2 PHE A 22 1750 1605 1829 95 73 48 C ATOM 189 CZ PHE A 22 -2.852 -4.147 -9.835 1.00 14.57 C ANISOU 189 CZ PHE A 22 1865 1696 1973 46 100 -1 C ATOM 190 N LEU A 23 -0.149 -10.195 -12.203 1.00 8.67 N ANISOU 190 N LEU A 23 954 1165 1174 57 10 134 N ATOM 191 CA LEU A 23 0.669 -11.389 -12.264 1.00 8.87 C ANISOU 191 CA LEU A 23 1009 1188 1172 48 -15 86 C ATOM 192 C LEU A 23 1.534 -11.412 -11.018 1.00 8.51 C ANISOU 192 C LEU A 23 973 1147 1113 47 -12 49 C ATOM 193 O LEU A 23 2.249 -10.450 -10.737 1.00 8.73 O ANISOU 193 O LEU A 23 1057 1137 1120 56 -43 134 O ATOM 194 CB LEU A 23 1.543 -11.357 -13.514 1.00 9.15 C ANISOU 194 CB LEU A 23 1060 1257 1157 41 -25 42 C ATOM 195 CG LEU A 23 2.483 -12.546 -13.709 1.00 9.74 C ANISOU 195 CG LEU A 23 1169 1320 1210 84 18 39 C ATOM 196 CD1 LEU A 23 1.704 -13.845 -13.811 1.00 11.58 C ANISOU 196 CD1 LEU A 23 1450 1424 1523 127 -41 5 C ATOM 197 CD2 LEU A 23 3.354 -12.338 -14.928 1.00 10.47 C ANISOU 197 CD2 LEU A 23 1271 1482 1222 93 51 73 C ATOM 198 N ASN A 24 1.448 -12.515 -10.276 1.00 8.47 N ANISOU 198 N ASN A 24 975 1122 1118 29 -25 79 N ATOM 199 CA ASN A 24 2.136 -12.679 -8.997 1.00 8.25 C ANISOU 199 CA ASN A 24 952 1075 1107 83 -11 67 C ATOM 200 C ASN A 24 3.128 -13.819 -9.048 1.00 8.34 C ANISOU 200 C ASN A 24 971 1068 1130 78 -49 49 C ATOM 201 O ASN A 24 2.818 -14.884 -9.561 1.00 8.69 O ANISOU 201 O ASN A 24 965 1103 1232 95 -114 65 O ATOM 202 CB ASN A 24 1.144 -13.030 -7.887 1.00 8.53 C ANISOU 202 CB ASN A 24 1009 1142 1088 51 8 89 C ATOM 203 CG ASN A 24 0.166 -11.928 -7.604 1.00 9.76 C ANISOU 203 CG ASN A 24 1023 1324 1359 57 50 149 C ATOM 204 OD1 ASN A 24 -0.799 -11.710 -8.346 1.00 12.79 O ANISOU 204 OD1 ASN A 24 1290 1955 1613 164 69 298 O ATOM 205 ND2 ASN A 24 0.397 -11.233 -6.518 1.00 10.86 N ANISOU 205 ND2 ASN A 24 1191 1394 1539 100 177 -14 N ATOM 206 N CYS A 25 4.299 -13.595 -8.458 1.00 8.30 N ANISOU 206 N CYS A 25 959 1067 1126 115 -69 -11 N ATOM 207 CA CYS A 25 5.238 -14.655 -8.152 1.00 8.51 C ANISOU 207 CA CYS A 25 1010 1065 1157 99 -29 17 C ATOM 208 C CYS A 25 5.487 -14.608 -6.653 1.00 8.42 C ANISOU 208 C CYS A 25 973 1046 1178 70 -23 37 C ATOM 209 O CYS A 25 6.013 -13.622 -6.131 1.00 8.95 O ANISOU 209 O CYS A 25 1149 1042 1208 9 -56 138 O ATOM 210 CB CYS A 25 6.535 -14.460 -8.924 1.00 8.77 C ANISOU 210 CB CYS A 25 1059 1125 1147 142 -37 20 C ATOM 211 SG CYS A 25 7.685 -15.823 -8.696 1.00 10.06 S ANISOU 211 SG CYS A 25 1222 1397 1203 320 -116 -36 S ATOM 212 N TYR A 26 5.077 -15.672 -5.969 1.00 8.10 N ANISOU 212 N TYR A 26 876 1074 1125 42 -5 4 N ATOM 213 CA TYR A 26 5.256 -15.778 -4.534 1.00 8.25 C ANISOU 213 CA TYR A 26 943 1057 1135 28 -10 16 C ATOM 214 C TYR A 26 6.362 -16.788 -4.272 1.00 7.78 C ANISOU 214 C TYR A 26 913 1003 1037 -7 -14 34 C ATOM 215 O TYR A 26 6.239 -17.968 -4.607 1.00 7.99 O ANISOU 215 O TYR A 26 869 1006 1159 -22 -37 -2 O ATOM 216 CB TYR A 26 3.950 -16.199 -3.863 1.00 9.34 C ANISOU 216 CB TYR A 26 1001 1249 1296 6 -6 -2 C ATOM 217 CG TYR A 26 4.055 -16.375 -2.367 1.00 9.62 C ANISOU 217 CG TYR A 26 1044 1330 1282 54 35 -15 C ATOM 218 CD1 TYR A 26 4.573 -15.378 -1.554 1.00 10.87 C ANISOU 218 CD1 TYR A 26 1085 1593 1450 -89 68 -65 C ATOM 219 CD2 TYR A 26 3.611 -17.546 -1.760 1.00 10.92 C ANISOU 219 CD2 TYR A 26 1278 1505 1365 6 47 51 C ATOM 220 CE1 TYR A 26 4.651 -15.549 -0.174 1.00 11.42 C ANISOU 220 CE1 TYR A 26 1151 1727 1457 1 -57 -87 C ATOM 221 CE2 TYR A 26 3.683 -17.722 -0.392 1.00 11.79 C ANISOU 221 CE2 TYR A 26 1373 1693 1411 57 12 41 C ATOM 222 CZ TYR A 26 4.205 -16.728 0.390 1.00 11.78 C ANISOU 222 CZ TYR A 26 1312 1788 1376 77 -11 -20 C ATOM 223 OH TYR A 26 4.268 -16.914 1.750 1.00 13.66 O ANISOU 223 OH TYR A 26 1710 2048 1429 -29 -35 62 O ATOM 224 N VAL A 27 7.450 -16.304 -3.676 1.00 7.51 N ANISOU 224 N VAL A 27 864 893 1093 31 -25 1 N ATOM 225 CA VAL A 27 8.676 -17.061 -3.485 1.00 7.60 C ANISOU 225 CA VAL A 27 895 893 1098 28 -19 -12 C ATOM 226 C VAL A 27 8.857 -17.201 -1.976 1.00 7.71 C ANISOU 226 C VAL A 27 952 870 1107 -17 1 -50 C ATOM 227 O VAL A 27 9.011 -16.201 -1.279 1.00 8.08 O ANISOU 227 O VAL A 27 1060 862 1148 -29 -112 -93 O ATOM 228 CB VAL A 27 9.851 -16.313 -4.137 1.00 7.51 C ANISOU 228 CB VAL A 27 877 897 1077 32 -31 -9 C ATOM 229 CG1 VAL A 27 11.123 -17.120 -4.036 1.00 8.41 C ANISOU 229 CG1 VAL A 27 946 1090 1159 123 13 -44 C ATOM 230 CG2 VAL A 27 9.537 -16.006 -5.597 1.00 8.85 C ANISOU 230 CG2 VAL A 27 981 1165 1215 59 -14 104 C ATOM 231 N SER A 28 8.783 -18.430 -1.467 1.00 7.94 N ANISOU 231 N SER A 28 990 898 1129 -30 15 -9 N ATOM 232 CA SER A 28 8.555 -18.613 -0.045 1.00 8.16 C ANISOU 232 CA SER A 28 983 955 1163 -34 2 13 C ATOM 233 C SER A 28 9.516 -19.575 0.627 1.00 8.21 C ANISOU 233 C SER A 28 1002 941 1174 -10 6 28 C ATOM 234 O SER A 28 9.975 -20.560 0.040 1.00 8.54 O ANISOU 234 O SER A 28 1125 899 1218 12 -50 46 O ATOM 235 CB SER A 28 7.114 -19.061 0.207 1.00 8.69 C ANISOU 235 CB SER A 28 1007 1090 1203 -58 -15 52 C ATOM 236 OG SER A 28 6.837 -20.292 -0.419 1.00 9.88 O ANISOU 236 OG SER A 28 1116 1228 1410 -142 -4 24 O ATOM 237 N GLY A 29 9.789 -19.273 1.889 1.00 8.16 N ANISOU 237 N GLY A 29 1034 941 1122 17 7 87 N ATOM 238 CA GLY A 29 10.520 -20.161 2.773 1.00 8.87 C ANISOU 238 CA GLY A 29 1104 1031 1232 21 2 111 C ATOM 239 C GLY A 29 11.996 -20.291 2.472 1.00 9.09 C ANISOU 239 C GLY A 29 1128 1020 1303 76 -16 122 C ATOM 240 O GLY A 29 12.579 -21.320 2.778 1.00 11.08 O ANISOU 240 O GLY A 29 1323 1163 1722 149 14 317 O ATOM 241 N PHE A 30 12.622 -19.258 1.921 1.00 8.33 N ANISOU 241 N PHE A 30 960 987 1218 99 -14 104 N ATOM 242 CA PHE A 30 13.997 -19.387 1.450 1.00 8.11 C ANISOU 242 CA PHE A 30 985 942 1154 54 -20 10 C ATOM 243 C PHE A 30 15.017 -18.808 2.418 1.00 7.89 C ANISOU 243 C PHE A 30 987 911 1101 73 18 -5 C ATOM 244 O PHE A 30 14.726 -17.921 3.223 1.00 7.63 O ANISOU 244 O PHE A 30 924 902 1072 102 39 -46 O ATOM 245 CB PHE A 30 14.176 -18.822 0.032 1.00 8.31 C ANISOU 245 CB PHE A 30 952 1056 1149 80 -27 -38 C ATOM 246 CG PHE A 30 13.846 -17.352 -0.125 1.00 7.84 C ANISOU 246 CG PHE A 30 908 996 1074 43 -69 -25 C ATOM 247 CD1 PHE A 30 12.548 -16.929 -0.400 1.00 7.66 C ANISOU 247 CD1 PHE A 30 901 939 1069 0 -21 21 C ATOM 248 CD2 PHE A 30 14.848 -16.397 -0.077 1.00 8.11 C ANISOU 248 CD2 PHE A 30 881 1109 1089 19 16 -33 C ATOM 249 CE1 PHE A 30 12.257 -15.588 -0.576 1.00 8.01 C ANISOU 249 CE1 PHE A 30 877 1041 1125 94 -12 23 C ATOM 250 CE2 PHE A 30 14.561 -15.056 -0.262 1.00 8.25 C ANISOU 250 CE2 PHE A 30 1012 1121 1001 -32 -10 -68 C ATOM 251 CZ PHE A 30 13.265 -14.657 -0.514 1.00 8.07 C ANISOU 251 CZ PHE A 30 1021 995 1047 54 -17 20 C ATOM 252 N HIS A 31 16.218 -19.358 2.339 1.00 7.39 N ANISOU 252 N HIS A 31 930 788 1087 69 -8 4 N ATOM 253 CA HIS A 31 17.361 -18.859 3.072 1.00 7.61 C ANISOU 253 CA HIS A 31 998 832 1062 26 -34 6 C ATOM 254 C HIS A 31 18.612 -19.332 2.350 1.00 7.57 C ANISOU 254 C HIS A 31 985 825 1064 3 -50 38 C ATOM 255 O HIS A 31 18.654 -20.464 1.898 1.00 7.28 O ANISOU 255 O HIS A 31 975 698 1093 16 -65 69 O ATOM 256 CB HIS A 31 17.374 -19.360 4.514 1.00 8.14 C ANISOU 256 CB HIS A 31 1047 935 1110 59 -18 22 C ATOM 257 CG HIS A 31 18.222 -18.512 5.404 1.00 8.57 C ANISOU 257 CG HIS A 31 1104 1032 1120 52 1 -76 C ATOM 258 ND1 HIS A 31 19.460 -18.897 5.863 1.00 9.80 N ANISOU 258 ND1 HIS A 31 1243 1070 1410 -7 -185 -57 N ATOM 259 CD2 HIS A 31 18.033 -17.250 5.857 1.00 10.01 C ANISOU 259 CD2 HIS A 31 1326 1089 1385 105 -127 -91 C ATOM 260 CE1 HIS A 31 19.977 -17.924 6.597 1.00 10.82 C ANISOU 260 CE1 HIS A 31 1420 1173 1518 43 -204 -82 C ATOM 261 NE2 HIS A 31 19.137 -16.907 6.598 1.00 11.01 N ANISOU 261 NE2 HIS A 31 1483 1275 1423 -9 -196 -88 N ATOM 262 N PRO A 32 19.642 -18.476 2.231 1.00 8.15 N ANISOU 262 N PRO A 32 967 905 1224 -7 -32 0 N ATOM 263 CA PRO A 32 19.723 -17.082 2.658 1.00 8.29 C ANISOU 263 CA PRO A 32 1043 871 1236 -44 -46 4 C ATOM 264 C PRO A 32 18.765 -16.205 1.863 1.00 7.54 C ANISOU 264 C PRO A 32 943 761 1159 -56 -17 -5 C ATOM 265 O PRO A 32 18.147 -16.639 0.883 1.00 7.43 O ANISOU 265 O PRO A 32 934 732 1155 -52 -1 -21 O ATOM 266 CB PRO A 32 21.179 -16.705 2.358 1.00 9.26 C ANISOU 266 CB PRO A 32 1110 1008 1398 -30 -78 16 C ATOM 267 CG PRO A 32 21.578 -17.605 1.277 1.00 9.92 C ANISOU 267 CG PRO A 32 1099 1189 1479 -99 6 -29 C ATOM 268 CD PRO A 32 20.888 -18.906 1.568 1.00 8.82 C ANISOU 268 CD PRO A 32 1026 1047 1278 0 -28 -33 C ATOM 269 N SER A 33 18.656 -14.958 2.287 1.00 7.72 N ANISOU 269 N SER A 33 1056 781 1095 -45 -18 -56 N ATOM 270 CA SER A 33 17.743 -14.022 1.659 1.00 7.80 C ANISOU 270 CA SER A 33 1041 794 1126 -20 22 -16 C ATOM 271 C SER A 33 18.213 -13.535 0.288 1.00 7.49 C ANISOU 271 C SER A 33 1046 757 1042 6 6 -44 C ATOM 272 O SER A 33 17.398 -13.043 -0.494 1.00 8.04 O ANISOU 272 O SER A 33 1126 814 1112 53 20 52 O ATOM 273 CB SER A 33 17.528 -12.827 2.579 1.00 8.23 C ANISOU 273 CB SER A 33 1140 811 1175 -14 37 3 C ATOM 274 OG SER A 33 18.765 -12.193 2.836 1.00 8.77 O ANISOU 274 OG SER A 33 1220 806 1303 -163 118 -105 O ATOM 275 N ASP A 34 19.503 -13.657 -0.018 1.00 7.09 N ANISOU 275 N ASP A 34 963 747 982 -12 -65 -4 N ATOM 276 CA ASP A 34 20.003 -13.256 -1.336 1.00 7.08 C ANISOU 276 CA ASP A 34 913 757 1019 0 -49 -12 C ATOM 277 C ASP A 34 19.199 -13.973 -2.407 1.00 6.81 C ANISOU 277 C ASP A 34 850 740 997 -18 -32 21 C ATOM 278 O ASP A 34 19.052 -15.193 -2.349 1.00 7.18 O ANISOU 278 O ASP A 34 1016 657 1053 -6 -77 1 O ATOM 279 CB ASP A 34 21.461 -13.654 -1.513 1.00 7.81 C ANISOU 279 CB ASP A 34 998 840 1128 -29 -34 -36 C ATOM 280 CG ASP A 34 22.358 -13.068 -0.474 1.00 9.30 C ANISOU 280 CG ASP A 34 1001 1204 1326 53 -49 -76 C ATOM 281 OD1 ASP A 34 22.133 -13.353 0.726 1.00 11.43 O ANISOU 281 OD1 ASP A 34 1478 1310 1554 -75 -151 25 O ATOM 282 OD2 ASP A 34 23.291 -12.344 -0.867 1.00 12.32 O ANISOU 282 OD2 ASP A 34 1466 1239 1973 -145 -171 13 O ATOM 283 N ILE A 35 18.693 -13.246 -3.393 1.00 6.66 N ANISOU 283 N ILE A 35 838 679 1012 -25 -24 -24 N ATOM 284 CA ILE A 35 17.861 -13.863 -4.416 1.00 7.01 C ANISOU 284 CA ILE A 35 883 756 1025 -42 -28 -35 C ATOM 285 C ILE A 35 17.700 -12.908 -5.587 1.00 7.11 C ANISOU 285 C ILE A 35 886 796 1017 -60 -54 2 C ATOM 286 O ILE A 35 17.858 -11.691 -5.442 1.00 7.59 O ANISOU 286 O ILE A 35 1003 777 1100 -81 -79 -8 O ATOM 287 CB ILE A 35 16.474 -14.260 -3.823 1.00 7.18 C ANISOU 287 CB ILE A 35 886 802 1037 -51 12 -21 C ATOM 288 CG1 ILE A 35 15.800 -15.367 -4.643 1.00 7.23 C ANISOU 288 CG1 ILE A 35 851 817 1079 -74 25 -49 C ATOM 289 CG2 ILE A 35 15.552 -13.042 -3.669 1.00 8.24 C ANISOU 289 CG2 ILE A 35 936 876 1316 -36 -20 -129 C ATOM 290 CD1 ILE A 35 14.660 -16.041 -3.907 1.00 7.95 C ANISOU 290 CD1 ILE A 35 1017 908 1094 -163 52 -88 C ATOM 291 N GLU A 36 17.392 -13.479 -6.743 1.00 7.51 N ANISOU 291 N GLU A 36 981 797 1072 -7 -65 4 N ATOM 292 CA GLU A 36 17.042 -12.719 -7.932 1.00 7.97 C ANISOU 292 CA GLU A 36 987 933 1107 -18 -62 0 C ATOM 293 C GLU A 36 15.741 -13.296 -8.458 1.00 7.64 C ANISOU 293 C GLU A 36 947 909 1045 -12 -82 -5 C ATOM 294 O GLU A 36 15.622 -14.507 -8.615 1.00 8.28 O ANISOU 294 O GLU A 36 999 919 1226 30 -157 -35 O ATOM 295 CB GLU A 36 18.135 -12.854 -8.984 1.00 8.38 C ANISOU 295 CB GLU A 36 994 1030 1159 -19 -8 -1 C ATOM 296 CG GLU A 36 17.872 -12.048 -10.243 1.00 9.97 C ANISOU 296 CG GLU A 36 1245 1246 1297 -32 -34 24 C ATOM 297 CD GLU A 36 18.995 -12.137 -11.250 1.00 12.46 C ANISOU 297 CD GLU A 36 1523 1697 1512 19 40 85 C ATOM 298 OE1 GLU A 36 19.763 -13.123 -11.216 1.00 16.38 O ANISOU 298 OE1 GLU A 36 2120 2212 1891 239 285 51 O ATOM 299 OE2 GLU A 36 19.103 -11.219 -12.085 1.00 15.97 O ANISOU 299 OE2 GLU A 36 1923 2207 1936 -75 140 237 O ATOM 300 N VAL A 37 14.765 -12.432 -8.715 1.00 7.79 N ANISOU 300 N VAL A 37 965 876 1118 0 -74 7 N ATOM 301 CA VAL A 37 13.435 -12.859 -9.137 1.00 8.04 C ANISOU 301 CA VAL A 37 980 979 1094 -24 -89 6 C ATOM 302 C VAL A 37 12.962 -11.943 -10.251 1.00 8.16 C ANISOU 302 C VAL A 37 996 996 1109 -21 -126 29 C ATOM 303 O VAL A 37 12.981 -10.722 -10.095 1.00 8.81 O ANISOU 303 O VAL A 37 1119 1003 1224 33 -156 74 O ATOM 304 CB VAL A 37 12.417 -12.831 -7.965 1.00 8.23 C ANISOU 304 CB VAL A 37 978 1010 1140 -15 -92 5 C ATOM 305 CG1 VAL A 37 11.043 -13.289 -8.440 1.00 9.23 C ANISOU 305 CG1 VAL A 37 1023 1189 1295 -1 -89 91 C ATOM 306 CG2 VAL A 37 12.912 -13.690 -6.798 1.00 8.38 C ANISOU 306 CG2 VAL A 37 1057 951 1176 -48 -72 52 C ATOM 307 N ASP A 38 12.534 -12.533 -11.365 1.00 8.56 N ANISOU 307 N ASP A 38 1032 1085 1135 11 -136 39 N ATOM 308 CA ASP A 38 11.941 -11.775 -12.460 1.00 9.04 C ANISOU 308 CA ASP A 38 1067 1206 1158 1 -82 57 C ATOM 309 C ASP A 38 10.644 -12.397 -12.913 1.00 9.06 C ANISOU 309 C ASP A 38 1085 1248 1109 25 -87 24 C ATOM 310 O ASP A 38 10.462 -13.611 -12.836 1.00 9.58 O ANISOU 310 O ASP A 38 1137 1243 1260 35 -195 15 O ATOM 311 CB ASP A 38 12.886 -11.721 -13.655 1.00 9.98 C ANISOU 311 CB ASP A 38 1198 1375 1215 11 -65 67 C ATOM 312 CG ASP A 38 14.017 -10.770 -13.438 1.00 11.80 C ANISOU 312 CG ASP A 38 1334 1645 1503 -52 47 101 C ATOM 313 OD1 ASP A 38 13.752 -9.559 -13.334 1.00 12.84 O ANISOU 313 OD1 ASP A 38 1360 1681 1834 -183 120 122 O ATOM 314 OD2 ASP A 38 15.168 -11.231 -13.374 1.00 14.69 O ANISOU 314 OD2 ASP A 38 1446 2103 2032 23 -68 154 O ATOM 315 N LEU A 39 9.745 -11.550 -13.389 1.00 9.02 N ANISOU 315 N LEU A 39 1098 1279 1050 50 -75 50 N ATOM 316 CA LEU A 39 8.619 -12.001 -14.179 1.00 9.58 C ANISOU 316 CA LEU A 39 1137 1422 1079 49 -26 24 C ATOM 317 C LEU A 39 9.042 -11.935 -15.631 1.00 10.21 C ANISOU 317 C LEU A 39 1234 1493 1150 38 -17 53 C ATOM 318 O LEU A 39 9.765 -11.022 -16.026 1.00 10.62 O ANISOU 318 O LEU A 39 1328 1588 1118 -30 9 87 O ATOM 319 CB LEU A 39 7.404 -11.106 -13.952 1.00 9.48 C ANISOU 319 CB LEU A 39 1122 1395 1085 69 -16 70 C ATOM 320 CG LEU A 39 6.885 -11.081 -12.517 1.00 10.65 C ANISOU 320 CG LEU A 39 1224 1615 1205 114 -24 20 C ATOM 321 CD1 LEU A 39 5.723 -10.113 -12.396 1.00 11.57 C ANISOU 321 CD1 LEU A 39 1224 1675 1497 103 8 -2 C ATOM 322 CD2 LEU A 39 6.475 -12.459 -12.066 1.00 12.67 C ANISOU 322 CD2 LEU A 39 1559 1688 1565 194 103 89 C ATOM 323 N LEU A 40 8.596 -12.917 -16.407 1.00 10.23 N ANISOU 323 N LEU A 40 1257 1543 1084 53 6 17 N ATOM 324 CA LEU A 40 8.906 -13.001 -17.829 1.00 11.28 C ANISOU 324 CA LEU A 40 1421 1670 1194 61 -6 2 C ATOM 325 C LEU A 40 7.634 -12.972 -18.646 1.00 11.85 C ANISOU 325 C LEU A 40 1511 1775 1216 61 -37 20 C ATOM 326 O LEU A 40 6.629 -13.571 -18.261 1.00 11.75 O ANISOU 326 O LEU A 40 1480 1821 1163 53 -166 6 O ATOM 327 CB LEU A 40 9.632 -14.307 -18.158 1.00 11.49 C ANISOU 327 CB LEU A 40 1443 1718 1203 82 -14 -14 C ATOM 328 CG LEU A 40 10.848 -14.692 -17.319 1.00 11.60 C ANISOU 328 CG LEU A 40 1443 1738 1225 158 -33 -83 C ATOM 329 CD1 LEU A 40 11.448 -15.978 -17.856 1.00 12.59 C ANISOU 329 CD1 LEU A 40 1646 1688 1447 203 -12 -97 C ATOM 330 CD2 LEU A 40 11.888 -13.588 -17.288 1.00 13.50 C ANISOU 330 CD2 LEU A 40 1610 1870 1650 98 -54 -49 C ATOM 331 N LYS A 41 7.696 -12.273 -19.779 1.00 13.27 N ANISOU 331 N LYS A 41 1696 1928 1415 44 -29 39 N ATOM 332 CA LYS A 41 6.660 -12.323 -20.804 1.00 14.14 C ANISOU 332 CA LYS A 41 1811 2021 1537 46 -47 27 C ATOM 333 C LYS A 41 7.333 -12.797 -22.076 1.00 14.84 C ANISOU 333 C LYS A 41 1898 2100 1639 54 -33 20 C ATOM 334 O LYS A 41 8.241 -12.134 -22.581 1.00 14.77 O ANISOU 334 O LYS A 41 1954 2181 1473 69 -35 4 O ATOM 335 CB LYS A 41 6.045 -10.947 -21.037 1.00 14.59 C ANISOU 335 CB LYS A 41 1866 2046 1628 41 -41 26 C ATOM 336 CG LYS A 41 4.994 -10.929 -22.150 1.00 14.94 C ANISOU 336 CG LYS A 41 1882 2107 1685 45 -59 25 C ATOM 337 CD LYS A 41 4.421 -9.543 -22.380 1.00 15.72 C ANISOU 337 CD LYS A 41 2012 2160 1799 76 -37 41 C ATOM 338 CE LYS A 41 3.427 -9.539 -23.536 1.00 16.92 C ANISOU 338 CE LYS A 41 2083 2291 2052 103 -114 51 C ATOM 339 NZ LYS A 41 2.972 -8.168 -23.908 1.00 18.65 N ANISOU 339 NZ LYS A 41 2365 2406 2313 158 -100 76 N ATOM 340 N ASN A 42 6.900 -13.953 -22.569 1.00 15.67 N ANISOU 340 N ASN A 42 2030 2202 1722 46 -28 -2 N ATOM 341 CA ASN A 42 7.497 -14.568 -23.754 1.00 16.51 C ANISOU 341 CA ASN A 42 2137 2269 1864 37 0 -24 C ATOM 342 C ASN A 42 9.021 -14.633 -23.641 1.00 17.16 C ANISOU 342 C ASN A 42 2196 2350 1971 38 22 -15 C ATOM 343 O ASN A 42 9.749 -14.334 -24.593 1.00 18.01 O ANISOU 343 O ASN A 42 2317 2517 2007 27 85 -64 O ATOM 344 CB ASN A 42 7.045 -13.837 -25.022 1.00 17.11 C ANISOU 344 CB ASN A 42 2242 2321 1936 21 -27 -8 C ATOM 345 CG ASN A 42 5.539 -13.859 -25.190 1.00 17.71 C ANISOU 345 CG ASN A 42 2333 2429 1966 25 -38 -27 C ATOM 346 OD1 ASN A 42 4.897 -14.882 -24.952 1.00 18.61 O ANISOU 346 OD1 ASN A 42 2525 2614 1932 -12 -139 -1 O ATOM 347 ND2 ASN A 42 4.966 -12.727 -25.586 1.00 19.16 N ANISOU 347 ND2 ASN A 42 2568 2569 2139 66 -67 -3 N ATOM 348 N GLY A 43 9.490 -15.020 -22.453 1.00 17.37 N ANISOU 348 N GLY A 43 2207 2381 2012 43 6 -38 N ATOM 349 CA GLY A 43 10.914 -15.210 -22.193 1.00 17.43 C ANISOU 349 CA GLY A 43 2191 2373 2056 43 26 -14 C ATOM 350 C GLY A 43 11.717 -13.954 -21.903 1.00 17.80 C ANISOU 350 C GLY A 43 2252 2425 2084 22 25 -21 C ATOM 351 O GLY A 43 12.905 -14.042 -21.595 1.00 18.79 O ANISOU 351 O GLY A 43 2305 2584 2250 53 41 -28 O ATOM 352 N GLU A 44 11.080 -12.792 -21.999 1.00 17.59 N ANISOU 352 N GLU A 44 2218 2413 2051 11 50 -13 N ATOM 353 CA GLU A 44 11.748 -11.514 -21.790 1.00 17.76 C ANISOU 353 CA GLU A 44 2231 2411 2106 4 74 6 C ATOM 354 C GLU A 44 11.419 -11.016 -20.398 1.00 17.24 C ANISOU 354 C GLU A 44 2136 2374 2038 0 92 21 C ATOM 355 O GLU A 44 10.263 -11.052 -19.975 1.00 16.54 O ANISOU 355 O GLU A 44 2009 2402 1873 -15 160 76 O ATOM 356 CB GLU A 44 11.271 -10.487 -22.818 1.00 18.38 C ANISOU 356 CB GLU A 44 2318 2455 2209 -5 70 2 C ATOM 357 CG GLU A 44 11.548 -10.861 -24.272 1.00 19.76 C ANISOU 357 CG GLU A 44 2558 2605 2342 -22 4 -3 C ATOM 358 CD GLU A 44 12.943 -10.500 -24.735 1.00 21.63 C ANISOU 358 CD GLU A 44 2721 2804 2694 -24 50 -62 C ATOM 359 OE1 GLU A 44 13.470 -9.448 -24.312 1.00 24.46 O ANISOU 359 OE1 GLU A 44 3073 3104 3116 -120 -3 -108 O ATOM 360 OE2 GLU A 44 13.511 -11.258 -25.551 1.00 21.74 O ANISOU 360 OE2 GLU A 44 2692 2859 2707 -77 139 -119 O ATOM 361 N ARG A 45 12.434 -10.544 -19.690 1.00 17.40 N ANISOU 361 N ARG A 45 2126 2376 2107 8 94 66 N ATOM 362 CA ARG A 45 12.248 -9.966 -18.370 1.00 17.54 C ANISOU 362 CA ARG A 45 2175 2337 2151 24 77 71 C ATOM 363 C ARG A 45 11.320 -8.759 -18.453 1.00 16.85 C ANISOU 363 C ARG A 45 2104 2254 2040 13 103 115 C ATOM 364 O ARG A 45 11.509 -7.882 -19.298 1.00 17.21 O ANISOU 364 O ARG A 45 2153 2287 2096 33 171 197 O ATOM 365 CB ARG A 45 13.607 -9.558 -17.802 1.00 18.17 C ANISOU 365 CB ARG A 45 2214 2407 2283 4 55 89 C ATOM 366 CG ARG A 45 13.568 -8.802 -16.504 1.00 18.79 C ANISOU 366 CG ARG A 45 2328 2472 2338 0 43 48 C ATOM 367 CD ARG A 45 14.978 -8.569 -15.997 1.00 20.05 C ANISOU 367 CD ARG A 45 2425 2637 2555 -2 0 73 C ATOM 368 NE ARG A 45 15.005 -7.634 -14.877 1.00 21.50 N ANISOU 368 NE ARG A 45 2664 2791 2711 -32 -11 3 N ATOM 369 CZ ARG A 45 14.952 -6.308 -14.994 1.00 23.12 C ANISOU 369 CZ ARG A 45 2945 2886 2951 4 -12 5 C ATOM 370 NH1 ARG A 45 14.884 -5.725 -16.187 1.00 24.10 N ANISOU 370 NH1 ARG A 45 3124 3040 2992 -4 -27 32 N ATOM 371 NH2 ARG A 45 14.979 -5.553 -13.903 1.00 23.69 N ANISOU 371 NH2 ARG A 45 3049 2954 2995 3 -9 -1 N ATOM 372 N ILE A 46 10.304 -8.741 -17.593 1.00 16.07 N ANISOU 372 N ILE A 46 2003 2137 1964 55 96 115 N ATOM 373 CA ILE A 46 9.429 -7.587 -17.451 1.00 16.28 C ANISOU 373 CA ILE A 46 2032 2155 1996 31 60 125 C ATOM 374 C ILE A 46 10.166 -6.579 -16.569 1.00 16.56 C ANISOU 374 C ILE A 46 2079 2165 2048 18 41 117 C ATOM 375 O ILE A 46 10.448 -6.853 -15.402 1.00 15.96 O ANISOU 375 O ILE A 46 2016 2100 1947 23 26 155 O ATOM 376 CB ILE A 46 8.066 -7.990 -16.836 1.00 15.45 C ANISOU 376 CB ILE A 46 1927 2050 1892 59 57 125 C ATOM 377 CG1 ILE A 46 7.336 -8.960 -17.772 1.00 15.22 C ANISOU 377 CG1 ILE A 46 1889 2022 1872 72 44 130 C ATOM 378 CG2 ILE A 46 7.210 -6.762 -16.577 1.00 15.79 C ANISOU 378 CG2 ILE A 46 1937 2091 1971 86 87 100 C ATOM 379 CD1 ILE A 46 6.061 -9.550 -17.193 1.00 15.55 C ANISOU 379 CD1 ILE A 46 1893 2120 1891 45 13 123 C ATOM 380 N GLU A 47 10.501 -5.423 -17.138 1.00 17.58 N ANISOU 380 N GLU A 47 2242 2248 2189 1 36 116 N ATOM 381 CA GLU A 47 11.361 -4.446 -16.464 1.00 18.56 C ANISOU 381 CA GLU A 47 2353 2365 2333 -18 12 78 C ATOM 382 C GLU A 47 10.634 -3.694 -15.359 1.00 18.78 C ANISOU 382 C GLU A 47 2384 2381 2370 -34 7 83 C ATOM 383 O GLU A 47 11.220 -3.393 -14.318 1.00 19.88 O ANISOU 383 O GLU A 47 2525 2548 2479 -35 -26 68 O ATOM 384 CB GLU A 47 11.926 -3.436 -17.469 1.00 19.00 C ANISOU 384 CB GLU A 47 2414 2416 2389 -36 19 86 C ATOM 385 CG GLU A 47 12.796 -4.045 -18.556 1.00 20.38 C ANISOU 385 CG GLU A 47 2583 2600 2560 -12 32 51 C ATOM 386 CD GLU A 47 13.308 -3.009 -19.543 1.00 21.00 C ANISOU 386 CD GLU A 47 2681 2681 2613 -36 49 78 C ATOM 387 OE1 GLU A 47 12.479 -2.266 -20.115 1.00 24.32 O ANISOU 387 OE1 GLU A 47 3036 3061 3142 66 2 135 O ATOM 388 OE2 GLU A 47 14.538 -2.946 -19.756 1.00 24.49 O ANISOU 388 OE2 GLU A 47 2937 3196 3171 -10 17 37 O ATOM 389 N LYS A 48 9.365 -3.379 -15.595 1.00 18.43 N ANISOU 389 N LYS A 48 2344 2327 2328 -38 20 91 N ATOM 390 CA LYS A 48 8.555 -2.661 -14.628 1.00 18.14 C ANISOU 390 CA LYS A 48 2297 2284 2308 -48 5 80 C ATOM 391 C LYS A 48 7.742 -3.671 -13.832 1.00 17.20 C ANISOU 391 C LYS A 48 2156 2193 2185 -42 -18 78 C ATOM 392 O LYS A 48 6.759 -4.223 -14.333 1.00 17.61 O ANISOU 392 O LYS A 48 2171 2276 2243 -62 -23 85 O ATOM 393 CB LYS A 48 7.629 -1.668 -15.338 1.00 18.78 C ANISOU 393 CB LYS A 48 2389 2360 2383 -34 -1 76 C ATOM 394 CG LYS A 48 6.662 -0.926 -14.417 1.00 19.39 C ANISOU 394 CG LYS A 48 2458 2440 2466 -21 25 45 C ATOM 395 CD LYS A 48 5.710 -0.048 -15.214 1.00 20.17 C ANISOU 395 CD LYS A 48 2551 2533 2580 16 8 54 C ATOM 396 CE LYS A 48 4.450 0.263 -14.427 1.00 21.60 C ANISOU 396 CE LYS A 48 2694 2735 2775 42 46 29 C ATOM 397 NZ LYS A 48 4.747 0.862 -13.101 1.00 23.72 N ANISOU 397 NZ LYS A 48 3046 2998 2968 12 -30 -11 N ATOM 398 N VAL A 49 8.172 -3.931 -12.602 1.00 16.03 N ANISOU 398 N VAL A 49 1990 2009 2090 -57 -25 111 N ATOM 399 CA VAL A 49 7.367 -4.706 -11.672 1.00 15.18 C ANISOU 399 CA VAL A 49 1888 1894 1984 -31 -43 93 C ATOM 400 C VAL A 49 7.072 -3.806 -10.479 1.00 15.11 C ANISOU 400 C VAL A 49 1932 1859 1950 -48 -63 75 C ATOM 401 O VAL A 49 7.978 -3.405 -9.744 1.00 15.52 O ANISOU 401 O VAL A 49 1928 1912 2055 -78 -107 72 O ATOM 402 CB VAL A 49 8.043 -6.031 -11.271 1.00 14.09 C ANISOU 402 CB VAL A 49 1728 1800 1826 -30 -36 136 C ATOM 403 CG1 VAL A 49 7.202 -6.771 -10.233 1.00 13.44 C ANISOU 403 CG1 VAL A 49 1591 1739 1775 -35 -44 152 C ATOM 404 CG2 VAL A 49 8.243 -6.900 -12.504 1.00 13.67 C ANISOU 404 CG2 VAL A 49 1595 1857 1739 -34 -30 150 C ATOM 405 N GLU A 50 5.790 -3.489 -10.324 1.00 14.86 N ANISOU 405 N GLU A 50 1968 1760 1916 -18 -49 64 N ATOM 406 CA GLU A 50 5.304 -2.460 -9.410 1.00 15.67 C ANISOU 406 CA GLU A 50 2097 1871 1984 -1 -23 47 C ATOM 407 C GLU A 50 5.522 -2.781 -7.935 1.00 15.22 C ANISOU 407 C GLU A 50 2086 1756 1938 3 -30 28 C ATOM 408 O GLU A 50 5.726 -1.875 -7.134 1.00 16.14 O ANISOU 408 O GLU A 50 2272 1797 2060 -8 -51 8 O ATOM 409 CB GLU A 50 3.802 -2.222 -9.671 1.00 16.29 C ANISOU 409 CB GLU A 50 2163 1957 2069 27 -38 24 C ATOM 410 CG GLU A 50 3.507 -1.611 -11.051 1.00 17.50 C ANISOU 410 CG GLU A 50 2304 2126 2219 37 -18 56 C ATOM 411 CD GLU A 50 2.076 -1.818 -11.572 1.00 18.13 C ANISOU 411 CD GLU A 50 2352 2214 2319 -4 -35 27 C ATOM 412 OE1 GLU A 50 1.293 -2.651 -11.043 1.00 18.64 O ANISOU 412 OE1 GLU A 50 2364 2233 2484 -1 39 -36 O ATOM 413 OE2 GLU A 50 1.740 -1.125 -12.558 1.00 21.81 O ANISOU 413 OE2 GLU A 50 2876 2663 2746 59 -82 158 O ATOM 414 N HIS A 51 5.477 -4.062 -7.577 1.00 14.29 N ANISOU 414 N HIS A 51 1987 1624 1818 7 -42 22 N ATOM 415 CA HIS A 51 5.491 -4.462 -6.169 1.00 14.07 C ANISOU 415 CA HIS A 51 1938 1628 1778 15 -53 -5 C ATOM 416 C HIS A 51 6.468 -5.587 -5.886 1.00 13.04 C ANISOU 416 C HIS A 51 1835 1479 1639 -11 -59 -2 C ATOM 417 O HIS A 51 6.472 -6.609 -6.567 1.00 11.83 O ANISOU 417 O HIS A 51 1734 1352 1407 2 -124 -13 O ATOM 418 CB HIS A 51 4.098 -4.893 -5.746 1.00 14.97 C ANISOU 418 CB HIS A 51 2013 1813 1862 -3 -48 -15 C ATOM 419 CG HIS A 51 3.083 -3.807 -5.872 1.00 16.76 C ANISOU 419 CG HIS A 51 2193 2015 2159 78 -14 -4 C ATOM 420 ND1 HIS A 51 2.916 -2.833 -4.911 1.00 18.85 N ANISOU 420 ND1 HIS A 51 2495 2237 2427 152 -32 -40 N ATOM 421 CD2 HIS A 51 2.192 -3.528 -6.852 1.00 17.36 C ANISOU 421 CD2 HIS A 51 2376 2137 2081 79 -102 -117 C ATOM 422 CE1 HIS A 51 1.963 -2.002 -5.293 1.00 20.18 C ANISOU 422 CE1 HIS A 51 2539 2484 2644 103 -17 80 C ATOM 423 NE2 HIS A 51 1.504 -2.404 -6.465 1.00 19.56 N ANISOU 423 NE2 HIS A 51 2516 2412 2502 101 -35 -25 N ATOM 424 N SER A 52 7.287 -5.381 -4.860 1.00 12.66 N ANISOU 424 N SER A 52 1834 1407 1567 -30 -71 12 N ATOM 425 CA SER A 52 8.262 -6.370 -4.416 1.00 12.90 C ANISOU 425 CA SER A 52 1811 1497 1590 -21 -75 -6 C ATOM 426 C SER A 52 8.332 -6.317 -2.892 1.00 12.68 C ANISOU 426 C SER A 52 1812 1448 1555 -31 -73 -31 C ATOM 427 O SER A 52 9.025 -5.479 -2.325 1.00 14.24 O ANISOU 427 O SER A 52 2018 1689 1703 -140 -112 -62 O ATOM 428 CB SER A 52 9.622 -6.077 -5.052 1.00 13.18 C ANISOU 428 CB SER A 52 1824 1529 1653 -61 -70 -28 C ATOM 429 OG SER A 52 10.547 -7.109 -4.786 1.00 14.02 O ANISOU 429 OG SER A 52 1824 1674 1826 -63 -56 32 O ATOM 430 N ASP A 53 7.585 -7.205 -2.242 1.00 11.78 N ANISOU 430 N ASP A 53 1674 1339 1462 41 -77 -16 N ATOM 431 CA ASP A 53 7.394 -7.175 -0.793 1.00 11.86 C ANISOU 431 CA ASP A 53 1651 1361 1493 87 -46 -23 C ATOM 432 C ASP A 53 8.117 -8.335 -0.123 1.00 10.69 C ANISOU 432 C ASP A 53 1465 1242 1355 91 -35 -32 C ATOM 433 O ASP A 53 7.729 -9.495 -0.297 1.00 10.41 O ANISOU 433 O ASP A 53 1443 1228 1281 162 -111 -44 O ATOM 434 CB ASP A 53 5.900 -7.249 -0.465 1.00 12.92 C ANISOU 434 CB ASP A 53 1777 1505 1627 102 -26 -75 C ATOM 435 CG ASP A 53 5.105 -6.120 -1.100 1.00 15.17 C ANISOU 435 CG ASP A 53 1976 1852 1935 130 -44 -38 C ATOM 436 OD1 ASP A 53 5.670 -5.024 -1.283 1.00 17.52 O ANISOU 436 OD1 ASP A 53 2285 1993 2375 193 -124 61 O ATOM 437 OD2 ASP A 53 3.915 -6.338 -1.410 1.00 18.61 O ANISOU 437 OD2 ASP A 53 2207 2317 2546 130 -97 -77 O ATOM 438 N LEU A 54 9.144 -8.008 0.660 1.00 10.02 N ANISOU 438 N LEU A 54 1404 1101 1299 23 12 -53 N ATOM 439 CA LEU A 54 9.949 -9.001 1.354 1.00 9.49 C ANISOU 439 CA LEU A 54 1301 1103 1200 7 48 -75 C ATOM 440 C LEU A 54 9.604 -9.022 2.831 1.00 8.70 C ANISOU 440 C LEU A 54 1183 999 1124 3 42 -54 C ATOM 441 O LEU A 54 9.448 -7.971 3.459 1.00 9.30 O ANISOU 441 O LEU A 54 1308 988 1236 16 74 -80 O ATOM 442 CB LEU A 54 11.437 -8.675 1.186 1.00 9.54 C ANISOU 442 CB LEU A 54 1333 1108 1183 -72 74 -53 C ATOM 443 CG LEU A 54 12.420 -9.734 1.692 1.00 9.70 C ANISOU 443 CG LEU A 54 1314 1197 1172 -55 104 -94 C ATOM 444 CD1 LEU A 54 12.406 -10.952 0.781 1.00 10.50 C ANISOU 444 CD1 LEU A 54 1325 1265 1400 -14 114 -171 C ATOM 445 CD2 LEU A 54 13.828 -9.157 1.814 1.00 10.56 C ANISOU 445 CD2 LEU A 54 1271 1309 1431 -66 85 -124 C ATOM 446 N SER A 55 9.526 -10.223 3.388 1.00 8.54 N ANISOU 446 N SER A 55 1121 1015 1107 46 104 -52 N ATOM 447 CA SER A 55 9.289 -10.397 4.810 1.00 8.53 C ANISOU 447 CA SER A 55 1080 1047 1111 42 58 -57 C ATOM 448 C SER A 55 10.021 -11.642 5.296 1.00 7.94 C ANISOU 448 C SER A 55 975 1001 1039 36 58 -43 C ATOM 449 O SER A 55 10.552 -12.421 4.506 1.00 8.32 O ANISOU 449 O SER A 55 1092 1068 999 38 44 -118 O ATOM 450 CB SER A 55 7.786 -10.500 5.092 1.00 8.85 C ANISOU 450 CB SER A 55 1104 1108 1149 25 68 -15 C ATOM 451 OG SER A 55 7.223 -11.621 4.446 1.00 10.19 O ANISOU 451 OG SER A 55 1117 1299 1456 -12 72 -9 O ATOM 452 N PHE A 56 10.062 -11.817 6.610 1.00 8.23 N ANISOU 452 N PHE A 56 1084 1011 1031 25 45 -50 N ATOM 453 CA PHE A 56 10.591 -13.039 7.189 1.00 8.76 C ANISOU 453 CA PHE A 56 1078 1159 1090 37 52 -34 C ATOM 454 C PHE A 56 9.704 -13.463 8.348 1.00 8.90 C ANISOU 454 C PHE A 56 1094 1232 1057 24 22 -16 C ATOM 455 O PHE A 56 8.972 -12.657 8.922 1.00 9.69 O ANISOU 455 O PHE A 56 1158 1315 1209 83 139 -6 O ATOM 456 CB PHE A 56 12.070 -12.885 7.610 1.00 9.24 C ANISOU 456 CB PHE A 56 1107 1224 1180 32 18 -31 C ATOM 457 CG PHE A 56 12.321 -11.829 8.656 1.00 9.19 C ANISOU 457 CG PHE A 56 940 1303 1246 8 74 -78 C ATOM 458 CD1 PHE A 56 12.640 -10.531 8.289 1.00 9.31 C ANISOU 458 CD1 PHE A 56 1018 1296 1220 12 51 -85 C ATOM 459 CD2 PHE A 56 12.268 -12.140 10.010 1.00 9.71 C ANISOU 459 CD2 PHE A 56 1135 1316 1236 -45 10 -47 C ATOM 460 CE1 PHE A 56 12.886 -9.560 9.244 1.00 9.70 C ANISOU 460 CE1 PHE A 56 1024 1246 1415 -12 22 -108 C ATOM 461 CE2 PHE A 56 12.518 -11.175 10.972 1.00 10.22 C ANISOU 461 CE2 PHE A 56 1172 1436 1273 -39 -49 -74 C ATOM 462 CZ PHE A 56 12.816 -9.883 10.584 1.00 10.11 C ANISOU 462 CZ PHE A 56 1094 1388 1358 -45 -47 -122 C ATOM 463 N SER A 57 9.736 -14.743 8.674 1.00 9.97 N ANISOU 463 N SER A 57 1267 1339 1180 4 49 30 N ATOM 464 CA SER A 57 8.981 -15.225 9.822 1.00 10.99 C ANISOU 464 CA SER A 57 1397 1479 1298 -38 31 55 C ATOM 465 C SER A 57 9.994 -15.492 10.920 1.00 11.77 C ANISOU 465 C SER A 57 1469 1570 1432 -59 13 24 C ATOM 466 O SER A 57 10.363 -14.577 11.663 1.00 12.50 O ANISOU 466 O SER A 57 1595 1643 1511 -49 -10 -23 O ATOM 467 CB SER A 57 8.137 -16.442 9.445 1.00 11.59 C ANISOU 467 CB SER A 57 1463 1585 1355 -80 -5 113 C ATOM 468 OG SER A 57 8.939 -17.469 8.921 1.00 12.29 O ANISOU 468 OG SER A 57 1644 1552 1472 -123 -83 170 O ATOM 469 N LYS A 58 10.487 -16.721 10.992 1.00 12.41 N ANISOU 469 N LYS A 58 1517 1640 1557 -29 -23 41 N ATOM 470 CA LYS A 58 11.727 -16.994 11.708 1.00 12.83 C ANISOU 470 CA LYS A 58 1582 1692 1599 -26 -27 59 C ATOM 471 C LYS A 58 12.843 -16.213 11.021 1.00 12.61 C ANISOU 471 C LYS A 58 1595 1666 1530 -22 -37 57 C ATOM 472 O LYS A 58 12.732 -15.849 9.842 1.00 11.95 O ANISOU 472 O LYS A 58 1519 1562 1457 -15 -22 78 O ATOM 473 CB LYS A 58 12.056 -18.486 11.687 1.00 14.11 C ANISOU 473 CB LYS A 58 1734 1802 1822 -16 -53 50 C ATOM 474 CG LYS A 58 11.037 -19.371 12.372 1.00 15.65 C ANISOU 474 CG LYS A 58 1835 2028 2081 -25 11 76 C ATOM 475 CD LYS A 58 10.972 -19.094 13.862 1.00 17.74 C ANISOU 475 CD LYS A 58 2203 2266 2270 -21 26 29 C ATOM 476 CE LYS A 58 10.181 -20.165 14.588 1.00 18.65 C ANISOU 476 CE LYS A 58 2380 2372 2333 -22 81 117 C ATOM 477 NZ LYS A 58 8.920 -20.459 13.882 1.00 21.41 N ANISOU 477 NZ LYS A 58 2690 2686 2759 0 -36 46 N ATOM 478 N ASP A 59 13.926 -15.978 11.751 1.00 12.67 N ANISOU 478 N ASP A 59 1589 1674 1550 -19 -43 80 N ATOM 479 CA ASP A 59 15.041 -15.196 11.231 1.00 13.07 C ANISOU 479 CA ASP A 59 1618 1703 1643 -31 -25 55 C ATOM 480 C ASP A 59 15.671 -15.808 9.982 1.00 12.79 C ANISOU 480 C ASP A 59 1533 1681 1645 -32 -18 75 C ATOM 481 O ASP A 59 16.355 -15.106 9.228 1.00 13.20 O ANISOU 481 O ASP A 59 1588 1722 1704 -54 45 144 O ATOM 482 CB ASP A 59 16.109 -15.022 12.314 1.00 13.63 C ANISOU 482 CB ASP A 59 1717 1776 1685 -25 -30 70 C ATOM 483 CG ASP A 59 15.691 -14.044 13.399 1.00 15.22 C ANISOU 483 CG ASP A 59 2017 1977 1786 -81 -47 -11 C ATOM 484 OD1 ASP A 59 14.680 -13.332 13.222 1.00 17.11 O ANISOU 484 OD1 ASP A 59 2234 2236 2031 -51 46 -150 O ATOM 485 OD2 ASP A 59 16.388 -13.990 14.435 1.00 19.12 O ANISOU 485 OD2 ASP A 59 2529 2566 2168 -61 -235 -9 O ATOM 486 N TRP A 60 15.437 -17.100 9.767 1.00 12.34 N ANISOU 486 N TRP A 60 1483 1636 1569 40 -36 70 N ATOM 487 CA TRP A 60 16.021 -17.840 8.659 1.00 12.55 C ANISOU 487 CA TRP A 60 1527 1625 1616 58 -37 44 C ATOM 488 C TRP A 60 14.970 -18.291 7.630 1.00 11.72 C ANISOU 488 C TRP A 60 1436 1484 1531 100 -44 75 C ATOM 489 O TRP A 60 15.219 -19.221 6.862 1.00 12.63 O ANISOU 489 O TRP A 60 1551 1642 1605 148 -18 93 O ATOM 490 CB TRP A 60 16.785 -19.060 9.201 1.00 14.41 C ANISOU 490 CB TRP A 60 1746 1797 1933 75 -80 26 C ATOM 491 CG TRP A 60 15.933 -19.952 10.051 1.00 16.60 C ANISOU 491 CG TRP A 60 1985 2033 2289 80 -33 79 C ATOM 492 CD1 TRP A 60 15.156 -20.990 9.628 1.00 17.81 C ANISOU 492 CD1 TRP A 60 2200 2186 2380 92 26 157 C ATOM 493 CD2 TRP A 60 15.762 -19.873 11.471 1.00 17.38 C ANISOU 493 CD2 TRP A 60 2202 2233 2166 99 -1 87 C ATOM 494 NE1 TRP A 60 14.510 -21.559 10.699 1.00 18.25 N ANISOU 494 NE1 TRP A 60 2283 2250 2401 2 80 159 N ATOM 495 CE2 TRP A 60 14.864 -20.893 11.840 1.00 17.23 C ANISOU 495 CE2 TRP A 60 2236 2188 2120 16 -5 41 C ATOM 496 CE3 TRP A 60 16.277 -19.035 12.466 1.00 16.59 C ANISOU 496 CE3 TRP A 60 2188 2086 2030 -135 -109 -96 C ATOM 497 CZ2 TRP A 60 14.476 -21.106 13.164 1.00 18.28 C ANISOU 497 CZ2 TRP A 60 2357 2372 2215 48 27 44 C ATOM 498 CZ3 TRP A 60 15.892 -19.248 13.782 1.00 16.70 C ANISOU 498 CZ3 TRP A 60 2209 2149 1986 -68 -54 -95 C ATOM 499 CH2 TRP A 60 14.996 -20.272 14.117 1.00 16.57 C ANISOU 499 CH2 TRP A 60 2216 2161 1917 -17 -11 -53 C ATOM 500 N SER A 61 13.812 -17.627 7.590 1.00 10.42 N ANISOU 500 N SER A 61 1305 1311 1342 98 -36 56 N ATOM 501 CA SER A 61 12.793 -17.942 6.591 1.00 9.85 C ANISOU 501 CA SER A 61 1245 1192 1304 52 0 55 C ATOM 502 C SER A 61 12.233 -16.690 5.946 1.00 8.71 C ANISOU 502 C SER A 61 1093 1048 1167 54 -2 67 C ATOM 503 O SER A 61 11.535 -15.941 6.604 1.00 8.87 O ANISOU 503 O SER A 61 1069 1133 1166 83 69 94 O ATOM 504 CB SER A 61 11.670 -18.771 7.224 1.00 10.46 C ANISOU 504 CB SER A 61 1349 1249 1374 11 -9 67 C ATOM 505 OG SER A 61 10.801 -19.280 6.230 1.00 12.57 O ANISOU 505 OG SER A 61 1740 1442 1593 -46 -102 31 O ATOM 506 N PHE A 62 12.556 -16.481 4.667 1.00 7.93 N ANISOU 506 N PHE A 62 991 931 1091 38 28 1 N ATOM 507 CA PHE A 62 12.147 -15.291 3.926 1.00 7.79 C ANISOU 507 CA PHE A 62 941 936 1081 57 34 7 C ATOM 508 C PHE A 62 11.041 -15.588 2.919 1.00 7.67 C ANISOU 508 C PHE A 62 977 906 1030 15 70 3 C ATOM 509 O PHE A 62 10.899 -16.714 2.431 1.00 7.69 O ANISOU 509 O PHE A 62 953 892 1076 12 47 17 O ATOM 510 CB PHE A 62 13.352 -14.651 3.226 1.00 7.92 C ANISOU 510 CB PHE A 62 932 986 1089 41 57 -19 C ATOM 511 CG PHE A 62 14.240 -13.880 4.155 1.00 7.74 C ANISOU 511 CG PHE A 62 871 1030 1040 -11 57 5 C ATOM 512 CD1 PHE A 62 14.177 -12.495 4.197 1.00 8.36 C ANISOU 512 CD1 PHE A 62 1009 1090 1076 -15 50 -35 C ATOM 513 CD2 PHE A 62 15.125 -14.527 5.013 1.00 8.56 C ANISOU 513 CD2 PHE A 62 1082 973 1196 -105 -25 72 C ATOM 514 CE1 PHE A 62 14.990 -11.768 5.065 1.00 8.90 C ANISOU 514 CE1 PHE A 62 1138 1054 1188 -47 141 -152 C ATOM 515 CE2 PHE A 62 15.925 -13.799 5.895 1.00 9.39 C ANISOU 515 CE2 PHE A 62 1143 1249 1174 -95 -14 35 C ATOM 516 CZ PHE A 62 15.859 -12.420 5.909 1.00 9.49 C ANISOU 516 CZ PHE A 62 1200 1258 1147 -88 72 -116 C ATOM 517 N TYR A 63 10.278 -14.540 2.617 1.00 7.42 N ANISOU 517 N TYR A 63 929 856 1032 19 42 -6 N ATOM 518 CA TYR A 63 9.120 -14.589 1.730 1.00 8.10 C ANISOU 518 CA TYR A 63 1016 972 1088 40 -5 -20 C ATOM 519 C TYR A 63 9.126 -13.345 0.865 1.00 8.21 C ANISOU 519 C TYR A 63 1063 957 1097 53 -10 -42 C ATOM 520 O TYR A 63 9.310 -12.238 1.372 1.00 8.77 O ANISOU 520 O TYR A 63 1284 961 1085 27 -68 -5 O ATOM 521 CB TYR A 63 7.815 -14.625 2.536 1.00 8.93 C ANISOU 521 CB TYR A 63 1058 1118 1215 20 -12 2 C ATOM 522 CG TYR A 63 7.814 -15.761 3.509 1.00 9.02 C ANISOU 522 CG TYR A 63 1026 1217 1185 22 30 15 C ATOM 523 CD1 TYR A 63 7.301 -17.003 3.160 1.00 9.43 C ANISOU 523 CD1 TYR A 63 1096 1335 1150 -63 57 -2 C ATOM 524 CD2 TYR A 63 8.404 -15.625 4.755 1.00 10.04 C ANISOU 524 CD2 TYR A 63 1142 1454 1217 -25 57 78 C ATOM 525 CE1 TYR A 63 7.360 -18.076 4.038 1.00 10.66 C ANISOU 525 CE1 TYR A 63 1243 1344 1461 -18 83 113 C ATOM 526 CE2 TYR A 63 8.467 -16.683 5.626 1.00 10.80 C ANISOU 526 CE2 TYR A 63 1244 1574 1283 26 -68 128 C ATOM 527 CZ TYR A 63 7.942 -17.898 5.269 1.00 10.94 C ANISOU 527 CZ TYR A 63 1292 1453 1410 75 61 189 C ATOM 528 OH TYR A 63 8.019 -18.934 6.166 1.00 13.31 O ANISOU 528 OH TYR A 63 1737 1655 1662 -35 60 331 O ATOM 529 N LEU A 64 8.916 -13.534 -0.433 1.00 8.00 N ANISOU 529 N LEU A 64 1079 903 1057 56 -13 -26 N ATOM 530 CA LEU A 64 8.839 -12.420 -1.368 1.00 8.39 C ANISOU 530 CA LEU A 64 1090 1006 1089 52 9 -11 C ATOM 531 C LEU A 64 7.578 -12.547 -2.198 1.00 7.86 C ANISOU 531 C LEU A 64 1025 898 1060 51 15 8 C ATOM 532 O LEU A 64 7.336 -13.586 -2.819 1.00 8.39 O ANISOU 532 O LEU A 64 1084 963 1140 55 -76 -19 O ATOM 533 CB LEU A 64 10.044 -12.427 -2.309 1.00 8.47 C ANISOU 533 CB LEU A 64 1093 954 1168 31 34 -36 C ATOM 534 CG LEU A 64 10.049 -11.286 -3.336 1.00 9.60 C ANISOU 534 CG LEU A 64 1238 1210 1198 4 91 44 C ATOM 535 CD1 LEU A 64 10.448 -9.991 -2.666 1.00 11.28 C ANISOU 535 CD1 LEU A 64 1501 1366 1418 -45 140 108 C ATOM 536 CD2 LEU A 64 10.958 -11.577 -4.516 1.00 10.66 C ANISOU 536 CD2 LEU A 64 1302 1454 1292 8 120 19 C ATOM 537 N LEU A 65 6.777 -11.484 -2.222 1.00 8.33 N ANISOU 537 N LEU A 65 1077 1026 1059 102 -18 32 N ATOM 538 CA LEU A 65 5.674 -11.381 -3.167 1.00 8.86 C ANISOU 538 CA LEU A 65 1125 1118 1122 67 -6 51 C ATOM 539 C LEU A 65 6.051 -10.322 -4.194 1.00 8.51 C ANISOU 539 C LEU A 65 1133 1042 1059 70 -41 56 C ATOM 540 O LEU A 65 6.275 -9.157 -3.855 1.00 9.42 O ANISOU 540 O LEU A 65 1341 1065 1173 107 -28 17 O ATOM 541 CB LEU A 65 4.356 -11.041 -2.472 1.00 9.30 C ANISOU 541 CB LEU A 65 1191 1172 1168 125 3 71 C ATOM 542 CG LEU A 65 3.146 -11.059 -3.410 1.00 10.52 C ANISOU 542 CG LEU A 65 1182 1433 1382 109 9 102 C ATOM 543 CD1 LEU A 65 2.899 -12.447 -3.968 1.00 12.16 C ANISOU 543 CD1 LEU A 65 1239 1757 1621 31 -104 -22 C ATOM 544 CD2 LEU A 65 1.904 -10.535 -2.711 1.00 11.84 C ANISOU 544 CD2 LEU A 65 1293 1642 1563 110 77 46 C ATOM 545 N TYR A 66 6.136 -10.754 -5.451 1.00 8.46 N ANISOU 545 N TYR A 66 1121 1028 1062 34 -36 49 N ATOM 546 CA TYR A 66 6.641 -9.942 -6.545 1.00 8.79 C ANISOU 546 CA TYR A 66 1117 1106 1114 22 -46 57 C ATOM 547 C TYR A 66 5.538 -9.917 -7.583 1.00 8.96 C ANISOU 547 C TYR A 66 1087 1149 1168 37 -51 74 C ATOM 548 O TYR A 66 5.196 -10.956 -8.149 1.00 9.03 O ANISOU 548 O TYR A 66 1173 1140 1114 15 -110 94 O ATOM 549 CB TYR A 66 7.904 -10.601 -7.075 1.00 8.92 C ANISOU 549 CB TYR A 66 1119 1138 1132 24 -57 57 C ATOM 550 CG TYR A 66 8.708 -9.827 -8.080 1.00 8.85 C ANISOU 550 CG TYR A 66 1109 1150 1103 56 -28 17 C ATOM 551 CD1 TYR A 66 9.367 -8.660 -7.724 1.00 10.11 C ANISOU 551 CD1 TYR A 66 1232 1308 1301 -5 -65 -14 C ATOM 552 CD2 TYR A 66 8.877 -10.303 -9.373 1.00 9.09 C ANISOU 552 CD2 TYR A 66 1257 1120 1074 71 -13 14 C ATOM 553 CE1 TYR A 66 10.144 -7.976 -8.639 1.00 10.37 C ANISOU 553 CE1 TYR A 66 1211 1327 1401 -22 -70 74 C ATOM 554 CE2 TYR A 66 9.657 -9.624 -10.290 1.00 9.73 C ANISOU 554 CE2 TYR A 66 1251 1270 1175 104 41 56 C ATOM 555 CZ TYR A 66 10.282 -8.464 -9.917 1.00 9.83 C ANISOU 555 CZ TYR A 66 1079 1309 1344 27 25 147 C ATOM 556 OH TYR A 66 11.059 -7.783 -10.830 1.00 10.48 O ANISOU 556 OH TYR A 66 1215 1347 1418 -20 59 198 O ATOM 557 N TYR A 67 4.926 -8.758 -7.801 1.00 9.11 N ANISOU 557 N TYR A 67 1112 1160 1190 18 -90 34 N ATOM 558 CA TYR A 67 3.720 -8.718 -8.616 1.00 9.91 C ANISOU 558 CA TYR A 67 1209 1246 1307 13 -67 51 C ATOM 559 C TYR A 67 3.515 -7.379 -9.293 1.00 10.29 C ANISOU 559 C TYR A 67 1246 1275 1386 18 -61 88 C ATOM 560 O TYR A 67 4.020 -6.349 -8.848 1.00 10.43 O ANISOU 560 O TYR A 67 1314 1223 1423 16 -72 142 O ATOM 561 CB TYR A 67 2.486 -9.126 -7.788 1.00 11.56 C ANISOU 561 CB TYR A 67 1388 1487 1515 -1 -42 48 C ATOM 562 CG TYR A 67 1.979 -8.116 -6.778 1.00 13.11 C ANISOU 562 CG TYR A 67 1638 1601 1740 48 29 -8 C ATOM 563 CD1 TYR A 67 2.524 -8.034 -5.503 1.00 13.13 C ANISOU 563 CD1 TYR A 67 1693 1582 1712 169 -26 10 C ATOM 564 CD2 TYR A 67 0.918 -7.274 -7.094 1.00 14.87 C ANISOU 564 CD2 TYR A 67 1826 1833 1989 117 26 -61 C ATOM 565 CE1 TYR A 67 2.034 -7.116 -4.570 1.00 13.98 C ANISOU 565 CE1 TYR A 67 1879 1788 1643 81 -36 -68 C ATOM 566 CE2 TYR A 67 0.418 -6.358 -6.176 1.00 15.56 C ANISOU 566 CE2 TYR A 67 1902 1946 2064 113 73 -84 C ATOM 567 CZ TYR A 67 0.980 -6.284 -4.920 1.00 14.84 C ANISOU 567 CZ TYR A 67 1823 1920 1895 97 69 -101 C ATOM 568 OH TYR A 67 0.477 -5.371 -4.014 1.00 16.02 O ANISOU 568 OH TYR A 67 2044 1984 2058 231 129 -208 O ATOM 569 N THR A 68 2.777 -7.408 -10.392 1.00 10.24 N ANISOU 569 N THR A 68 1229 1251 1408 26 -105 131 N ATOM 570 CA THR A 68 2.542 -6.201 -11.165 1.00 10.82 C ANISOU 570 CA THR A 68 1280 1340 1490 13 -76 153 C ATOM 571 C THR A 68 1.347 -6.375 -12.083 1.00 10.53 C ANISOU 571 C THR A 68 1227 1340 1431 45 -58 182 C ATOM 572 O THR A 68 0.965 -7.492 -12.422 1.00 9.78 O ANISOU 572 O THR A 68 1063 1261 1389 99 -85 203 O ATOM 573 CB THR A 68 3.806 -5.831 -11.967 1.00 11.66 C ANISOU 573 CB THR A 68 1332 1514 1583 -13 -75 190 C ATOM 574 OG1 THR A 68 3.803 -4.431 -12.259 1.00 13.25 O ANISOU 574 OG1 THR A 68 1483 1664 1885 -97 -98 235 O ATOM 575 CG2 THR A 68 3.926 -6.643 -13.241 1.00 12.45 C ANISOU 575 CG2 THR A 68 1327 1644 1759 26 -10 149 C ATOM 576 N GLU A 69 0.745 -5.261 -12.478 1.00 11.06 N ANISOU 576 N GLU A 69 1304 1379 1518 58 -53 154 N ATOM 577 CA GLU A 69 -0.400 -5.316 -13.366 1.00 11.60 C ANISOU 577 CA GLU A 69 1382 1503 1520 30 -47 169 C ATOM 578 C GLU A 69 0.015 -5.850 -14.723 1.00 11.28 C ANISOU 578 C GLU A 69 1321 1512 1452 1 -16 188 C ATOM 579 O GLU A 69 1.100 -5.539 -15.216 1.00 11.53 O ANISOU 579 O GLU A 69 1300 1628 1450 -115 37 247 O ATOM 580 CB GLU A 69 -1.058 -3.945 -13.522 1.00 11.89 C ANISOU 580 CB GLU A 69 1449 1518 1550 95 -29 145 C ATOM 581 CG GLU A 69 -2.426 -4.060 -14.191 1.00 13.31 C ANISOU 581 CG GLU A 69 1589 1724 1742 78 -107 111 C ATOM 582 CD GLU A 69 -3.258 -2.798 -14.151 1.00 14.68 C ANISOU 582 CD GLU A 69 1782 1845 1950 121 -77 180 C ATOM 583 OE1 GLU A 69 -2.865 -1.827 -13.478 1.00 19.23 O ANISOU 583 OE1 GLU A 69 2407 2332 2564 157 -112 -73 O ATOM 584 OE2 GLU A 69 -4.323 -2.789 -14.801 1.00 18.45 O ANISOU 584 OE2 GLU A 69 2110 2323 2576 120 -164 163 O ATOM 585 N PHE A 70 -0.845 -6.660 -15.326 1.00 11.50 N ANISOU 585 N PHE A 70 1368 1577 1421 -12 -13 170 N ATOM 586 CA PHE A 70 -0.584 -7.179 -16.659 1.00 12.35 C ANISOU 586 CA PHE A 70 1507 1682 1503 14 -43 125 C ATOM 587 C PHE A 70 -1.885 -7.373 -17.406 1.00 13.04 C ANISOU 587 C PHE A 70 1630 1751 1570 12 -63 117 C ATOM 588 O PHE A 70 -2.964 -7.292 -16.819 1.00 12.83 O ANISOU 588 O PHE A 70 1600 1733 1542 69 -168 162 O ATOM 589 CB PHE A 70 0.314 -8.432 -16.640 1.00 11.88 C ANISOU 589 CB PHE A 70 1429 1658 1425 -27 -4 103 C ATOM 590 CG PHE A 70 -0.381 -9.740 -16.326 1.00 11.18 C ANISOU 590 CG PHE A 70 1294 1646 1305 48 -91 98 C ATOM 591 CD1 PHE A 70 0.000 -10.894 -16.998 1.00 11.93 C ANISOU 591 CD1 PHE A 70 1442 1693 1397 22 -161 86 C ATOM 592 CD2 PHE A 70 -1.356 -9.849 -15.337 1.00 10.41 C ANISOU 592 CD2 PHE A 70 1212 1555 1187 68 -67 92 C ATOM 593 CE1 PHE A 70 -0.583 -12.114 -16.717 1.00 11.51 C ANISOU 593 CE1 PHE A 70 1407 1633 1333 28 -176 -8 C ATOM 594 CE2 PHE A 70 -1.950 -11.076 -15.059 1.00 10.55 C ANISOU 594 CE2 PHE A 70 1212 1538 1257 74 -87 127 C ATOM 595 CZ PHE A 70 -1.558 -12.206 -15.748 1.00 11.34 C ANISOU 595 CZ PHE A 70 1340 1634 1332 -6 -158 79 C ATOM 596 N THR A 71 -1.760 -7.591 -18.710 1.00 14.45 N ANISOU 596 N THR A 71 1850 1930 1708 39 -94 93 N ATOM 597 CA THR A 71 -2.908 -7.764 -19.589 1.00 15.33 C ANISOU 597 CA THR A 71 1932 2050 1842 38 -119 92 C ATOM 598 C THR A 71 -2.653 -8.989 -20.453 1.00 15.86 C ANISOU 598 C THR A 71 1966 2133 1923 48 -108 57 C ATOM 599 O THR A 71 -2.195 -8.873 -21.594 1.00 16.42 O ANISOU 599 O THR A 71 2059 2254 1927 66 -96 77 O ATOM 600 CB THR A 71 -3.147 -6.518 -20.467 1.00 15.88 C ANISOU 600 CB THR A 71 2062 2079 1889 59 -105 115 C ATOM 601 OG1 THR A 71 -3.335 -5.377 -19.621 1.00 17.95 O ANISOU 601 OG1 THR A 71 2467 2241 2112 45 -114 98 O ATOM 602 CG2 THR A 71 -4.379 -6.701 -21.349 1.00 16.47 C ANISOU 602 CG2 THR A 71 2106 2198 1953 40 -114 98 C ATOM 603 N PRO A 72 -2.918 -10.180 -19.901 1.00 16.32 N ANISOU 603 N PRO A 72 2002 2168 2028 37 -110 24 N ATOM 604 CA PRO A 72 -2.634 -11.398 -20.641 1.00 17.22 C ANISOU 604 CA PRO A 72 2139 2252 2151 31 -97 8 C ATOM 605 C PRO A 72 -3.566 -11.608 -21.833 1.00 18.15 C ANISOU 605 C PRO A 72 2236 2394 2265 22 -116 -12 C ATOM 606 O PRO A 72 -4.756 -11.294 -21.760 1.00 18.14 O ANISOU 606 O PRO A 72 2208 2454 2229 56 -149 -24 O ATOM 607 CB PRO A 72 -2.848 -12.495 -19.598 1.00 16.94 C ANISOU 607 CB PRO A 72 2119 2207 2110 17 -123 -1 C ATOM 608 CG PRO A 72 -3.791 -11.924 -18.637 1.00 16.25 C ANISOU 608 CG PRO A 72 2015 2121 2036 0 -120 29 C ATOM 609 CD PRO A 72 -3.474 -10.465 -18.567 1.00 16.09 C ANISOU 609 CD PRO A 72 1976 2120 2015 38 -103 26 C ATOM 610 N THR A 73 -3.006 -12.112 -22.925 1.00 19.43 N ANISOU 610 N THR A 73 2418 2558 2404 26 -97 -24 N ATOM 611 CA THR A 73 -3.795 -12.606 -24.050 1.00 20.59 C ANISOU 611 CA THR A 73 2591 2695 2537 5 -88 -32 C ATOM 612 C THR A 73 -3.547 -14.096 -24.126 1.00 21.65 C ANISOU 612 C THR A 73 2746 2782 2697 11 -71 -31 C ATOM 613 O THR A 73 -2.584 -14.588 -23.552 1.00 21.96 O ANISOU 613 O THR A 73 2835 2796 2711 18 -100 -35 O ATOM 614 CB THR A 73 -3.378 -11.960 -25.382 1.00 20.95 C ANISOU 614 CB THR A 73 2648 2723 2587 6 -79 -17 C ATOM 615 OG1 THR A 73 -2.044 -12.360 -25.718 1.00 22.52 O ANISOU 615 OG1 THR A 73 2808 2983 2765 25 -15 -35 O ATOM 616 CG2 THR A 73 -3.443 -10.447 -25.292 1.00 21.37 C ANISOU 616 CG2 THR A 73 2736 2752 2631 12 -64 -29 C ATOM 617 N GLU A 74 -4.385 -14.812 -24.867 1.00 22.60 N ANISOU 617 N GLU A 74 2882 2871 2833 -8 -70 -45 N ATOM 618 CA GLU A 74 -4.268 -16.271 -24.955 1.00 23.22 C ANISOU 618 CA GLU A 74 2962 2931 2929 -4 -49 -33 C ATOM 619 C GLU A 74 -2.918 -16.733 -25.523 1.00 23.56 C ANISOU 619 C GLU A 74 2992 2985 2972 2 -50 -32 C ATOM 620 O GLU A 74 -2.461 -17.835 -25.211 1.00 24.44 O ANISOU 620 O GLU A 74 3127 3055 3102 14 -51 -33 O ATOM 621 CB GLU A 74 -5.400 -16.864 -25.807 1.00 23.83 C ANISOU 621 CB GLU A 74 3041 3011 3002 -21 -55 -36 C ATOM 622 CG GLU A 74 -6.820 -16.426 -25.433 1.00 25.55 C ANISOU 622 CG GLU A 74 3215 3213 3278 7 -29 -30 C ATOM 623 CD GLU A 74 -7.165 -16.658 -23.973 1.00 27.42 C ANISOU 623 CD GLU A 74 3490 3481 3444 -4 4 -1 C ATOM 624 OE1 GLU A 74 -6.649 -17.625 -23.369 1.00 29.00 O ANISOU 624 OE1 GLU A 74 3729 3620 3669 15 -23 28 O ATOM 625 OE2 GLU A 74 -7.966 -15.867 -23.429 1.00 29.30 O ANISOU 625 OE2 GLU A 74 3709 3711 3711 58 34 -33 O ATOM 626 N LYS A 75 -2.281 -15.892 -26.340 1.00 23.72 N ANISOU 626 N LYS A 75 3013 3018 2980 6 -49 -39 N ATOM 627 CA LYS A 75 -1.052 -16.271 -27.049 1.00 23.48 C ANISOU 627 CA LYS A 75 2970 3001 2949 2 -49 -35 C ATOM 628 C LYS A 75 0.240 -16.078 -26.239 1.00 23.20 C ANISOU 628 C LYS A 75 2941 2967 2905 16 -49 -37 C ATOM 629 O LYS A 75 1.199 -16.827 -26.424 1.00 23.66 O ANISOU 629 O LYS A 75 2970 3049 2971 25 -50 -36 O ATOM 630 CB LYS A 75 -0.946 -15.539 -28.400 1.00 24.10 C ANISOU 630 CB LYS A 75 3051 3088 3017 9 -22 -22 C ATOM 631 CG LYS A 75 -0.710 -14.021 -28.336 1.00 25.68 C ANISOU 631 CG LYS A 75 3263 3242 3250 -31 -2 -16 C ATOM 632 CD LYS A 75 -1.988 -13.198 -28.508 1.00 26.90 C ANISOU 632 CD LYS A 75 3382 3414 3424 19 -7 0 C ATOM 633 CE LYS A 75 -2.489 -13.173 -29.941 1.00 27.64 C ANISOU 633 CE LYS A 75 3492 3523 3485 14 -18 4 C ATOM 634 NZ LYS A 75 -3.587 -12.177 -30.097 1.00 27.57 N ANISOU 634 NZ LYS A 75 3441 3497 3535 43 -14 20 N ATOM 635 N ASP A 76 0.268 -15.086 -25.350 1.00 22.34 N ANISOU 635 N ASP A 76 2825 2882 2780 25 -67 -28 N ATOM 636 CA ASP A 76 1.489 -14.763 -24.601 1.00 21.67 C ANISOU 636 CA ASP A 76 2746 2802 2684 25 -58 -8 C ATOM 637 C ASP A 76 1.738 -15.772 -23.481 1.00 20.93 C ANISOU 637 C ASP A 76 2633 2734 2586 9 -52 -31 C ATOM 638 O ASP A 76 0.799 -16.315 -22.912 1.00 21.42 O ANISOU 638 O ASP A 76 2655 2825 2656 4 -71 1 O ATOM 639 CB ASP A 76 1.417 -13.337 -24.040 1.00 22.11 C ANISOU 639 CB ASP A 76 2791 2856 2753 15 -46 -18 C ATOM 640 CG ASP A 76 1.520 -12.271 -25.127 1.00 22.95 C ANISOU 640 CG ASP A 76 2928 2957 2831 27 -64 9 C ATOM 641 OD1 ASP A 76 2.364 -12.417 -26.035 1.00 25.09 O ANISOU 641 OD1 ASP A 76 3187 3262 3084 49 -12 29 O ATOM 642 OD2 ASP A 76 0.769 -11.277 -25.069 1.00 24.83 O ANISOU 642 OD2 ASP A 76 3211 3153 3070 79 -76 17 O ATOM 643 N GLU A 77 3.010 -16.040 -23.190 1.00 19.60 N ANISOU 643 N GLU A 77 2490 2589 2365 1 -84 -46 N ATOM 644 CA GLU A 77 3.378 -16.936 -22.093 1.00 18.73 C ANISOU 644 CA GLU A 77 2392 2488 2237 -22 -91 -65 C ATOM 645 C GLU A 77 4.085 -16.147 -21.001 1.00 16.93 C ANISOU 645 C GLU A 77 2161 2295 1974 -20 -107 -49 C ATOM 646 O GLU A 77 4.992 -15.366 -21.286 1.00 17.12 O ANISOU 646 O GLU A 77 2280 2383 1840 -64 -124 -75 O ATOM 647 CB GLU A 77 4.257 -18.102 -22.573 1.00 19.06 C ANISOU 647 CB GLU A 77 2437 2506 2296 9 -97 -46 C ATOM 648 CG GLU A 77 5.596 -17.729 -23.208 1.00 21.03 C ANISOU 648 CG GLU A 77 2683 2735 2569 -21 -37 -6 C ATOM 649 CD GLU A 77 6.480 -18.937 -23.503 1.00 21.48 C ANISOU 649 CD GLU A 77 2714 2788 2657 13 -20 -36 C ATOM 650 OE1 GLU A 77 6.597 -19.834 -22.635 1.00 24.48 O ANISOU 650 OE1 GLU A 77 3171 3041 3088 28 -26 51 O ATOM 651 OE2 GLU A 77 7.075 -18.977 -24.604 1.00 25.07 O ANISOU 651 OE2 GLU A 77 3219 3298 3007 39 111 -39 O ATOM 652 N TYR A 78 3.647 -16.345 -19.760 1.00 14.90 N ANISOU 652 N TYR A 78 1846 2059 1754 -8 -172 -87 N ATOM 653 CA TYR A 78 4.241 -15.671 -18.610 1.00 13.90 C ANISOU 653 CA TYR A 78 1709 1919 1654 15 -156 -44 C ATOM 654 C TYR A 78 4.894 -16.673 -17.680 1.00 12.90 C ANISOU 654 C TYR A 78 1578 1796 1527 -18 -164 -42 C ATOM 655 O TYR A 78 4.510 -17.838 -17.624 1.00 13.03 O ANISOU 655 O TYR A 78 1586 1813 1550 -1 -267 -38 O ATOM 656 CB TYR A 78 3.187 -14.855 -17.868 1.00 13.55 C ANISOU 656 CB TYR A 78 1680 1880 1586 28 -134 -32 C ATOM 657 CG TYR A 78 2.659 -13.701 -18.689 1.00 13.42 C ANISOU 657 CG TYR A 78 1606 1954 1538 79 -127 -17 C ATOM 658 CD1 TYR A 78 3.275 -12.456 -18.652 1.00 12.48 C ANISOU 658 CD1 TYR A 78 1581 1831 1328 127 -56 3 C ATOM 659 CD2 TYR A 78 1.556 -13.858 -19.523 1.00 14.02 C ANISOU 659 CD2 TYR A 78 1749 1976 1601 55 -175 -31 C ATOM 660 CE1 TYR A 78 2.799 -11.396 -19.410 1.00 13.59 C ANISOU 660 CE1 TYR A 78 1719 1853 1590 78 -75 6 C ATOM 661 CE2 TYR A 78 1.075 -12.801 -20.287 1.00 14.37 C ANISOU 661 CE2 TYR A 78 1773 2063 1621 145 -72 22 C ATOM 662 CZ TYR A 78 1.699 -11.578 -20.226 1.00 14.24 C ANISOU 662 CZ TYR A 78 1833 2039 1538 155 -74 21 C ATOM 663 OH TYR A 78 1.227 -10.527 -20.979 1.00 15.74 O ANISOU 663 OH TYR A 78 2042 2099 1838 258 -148 121 O ATOM 664 N ALA A 79 5.896 -16.204 -16.950 1.00 11.99 N ANISOU 664 N ALA A 79 1463 1666 1426 0 -140 -77 N ATOM 665 CA ALA A 79 6.631 -17.061 -16.042 1.00 11.38 C ANISOU 665 CA ALA A 79 1372 1575 1377 18 -116 -94 C ATOM 666 C ALA A 79 7.302 -16.238 -14.962 1.00 10.48 C ANISOU 666 C ALA A 79 1271 1469 1241 24 -82 -85 C ATOM 667 O ALA A 79 7.374 -15.013 -15.050 1.00 10.84 O ANISOU 667 O ALA A 79 1315 1515 1286 23 -142 -95 O ATOM 668 CB ALA A 79 7.670 -17.870 -16.811 1.00 11.79 C ANISOU 668 CB ALA A 79 1444 1661 1373 34 -95 -157 C ATOM 669 N CYS A 80 7.798 -16.937 -13.950 1.00 9.91 N ANISOU 669 N CYS A 80 1138 1383 1244 44 -121 -87 N ATOM 670 CA CYS A 80 8.659 -16.346 -12.941 1.00 9.76 C ANISOU 670 CA CYS A 80 1101 1342 1262 58 -70 -88 C ATOM 671 C CYS A 80 9.987 -17.091 -12.952 1.00 9.47 C ANISOU 671 C CYS A 80 1110 1299 1187 73 -36 -96 C ATOM 672 O CYS A 80 10.007 -18.320 -12.975 1.00 10.20 O ANISOU 672 O CYS A 80 1107 1334 1433 72 -27 -90 O ATOM 673 CB CYS A 80 8.012 -16.463 -11.569 1.00 9.85 C ANISOU 673 CB CYS A 80 1064 1352 1325 99 -90 -80 C ATOM 674 SG CYS A 80 8.935 -15.623 -10.275 1.00 10.36 S ANISOU 674 SG CYS A 80 1096 1579 1259 91 -91 -184 S ATOM 675 N ARG A 81 11.085 -16.346 -12.961 1.00 9.19 N ANISOU 675 N ARG A 81 1033 1271 1185 97 -41 -92 N ATOM 676 CA ARG A 81 12.417 -16.923 -12.971 1.00 9.33 C ANISOU 676 CA ARG A 81 1063 1317 1163 74 -45 -68 C ATOM 677 C ARG A 81 13.136 -16.543 -11.693 1.00 8.44 C ANISOU 677 C ARG A 81 958 1190 1059 50 -29 -78 C ATOM 678 O ARG A 81 13.234 -15.361 -11.363 1.00 8.53 O ANISOU 678 O ARG A 81 1011 1144 1087 50 -92 -9 O ATOM 679 CB ARG A 81 13.208 -16.408 -14.161 1.00 9.77 C ANISOU 679 CB ARG A 81 1123 1391 1198 47 -21 -81 C ATOM 680 CG ARG A 81 14.620 -16.978 -14.235 1.00 10.75 C ANISOU 680 CG ARG A 81 1219 1544 1319 92 -6 -60 C ATOM 681 CD ARG A 81 15.325 -16.494 -15.463 1.00 12.95 C ANISOU 681 CD ARG A 81 1477 1920 1522 63 75 -15 C ATOM 682 NE ARG A 81 15.491 -15.051 -15.384 1.00 15.34 N ANISOU 682 NE ARG A 81 1857 2102 1868 72 91 24 N ATOM 683 CZ ARG A 81 15.626 -14.237 -16.428 1.00 16.77 C ANISOU 683 CZ ARG A 81 2118 2181 2074 69 29 79 C ATOM 684 NH1 ARG A 81 15.652 -14.709 -17.667 1.00 17.64 N ANISOU 684 NH1 ARG A 81 2243 2288 2169 126 113 33 N ATOM 685 NH2 ARG A 81 15.750 -12.931 -16.226 1.00 16.82 N ANISOU 685 NH2 ARG A 81 2089 2225 2077 54 78 45 N ATOM 686 N VAL A 82 13.676 -17.538 -11.001 1.00 8.02 N ANISOU 686 N VAL A 82 930 1073 1041 41 -33 -108 N ATOM 687 CA VAL A 82 14.341 -17.327 -9.729 1.00 8.19 C ANISOU 687 CA VAL A 82 968 1056 1085 55 1 -61 C ATOM 688 C VAL A 82 15.760 -17.879 -9.768 1.00 8.00 C ANISOU 688 C VAL A 82 959 966 1112 78 6 -50 C ATOM 689 O VAL A 82 15.981 -19.011 -10.199 1.00 8.75 O ANISOU 689 O VAL A 82 1053 1041 1228 99 -24 -175 O ATOM 690 CB VAL A 82 13.549 -18.013 -8.600 1.00 8.25 C ANISOU 690 CB VAL A 82 1027 1010 1096 10 55 -59 C ATOM 691 CG1 VAL A 82 14.280 -17.897 -7.272 1.00 8.53 C ANISOU 691 CG1 VAL A 82 1186 996 1056 -4 -7 3 C ATOM 692 CG2 VAL A 82 12.144 -17.422 -8.514 1.00 9.15 C ANISOU 692 CG2 VAL A 82 1126 1103 1245 18 103 -53 C ATOM 693 N ASN A 83 16.707 -17.071 -9.301 1.00 7.99 N ANISOU 693 N ASN A 83 932 964 1137 101 -7 -39 N ATOM 694 CA ASN A 83 18.059 -17.539 -9.033 1.00 8.31 C ANISOU 694 CA ASN A 83 979 1009 1170 81 -2 3 C ATOM 695 C ASN A 83 18.334 -17.434 -7.544 1.00 7.60 C ANISOU 695 C ASN A 83 862 896 1127 59 16 13 C ATOM 696 O ASN A 83 17.988 -16.436 -6.915 1.00 7.94 O ANISOU 696 O ASN A 83 952 911 1152 84 -57 1 O ATOM 697 CB ASN A 83 19.091 -16.716 -9.801 1.00 9.45 C ANISOU 697 CB ASN A 83 1105 1215 1268 96 1 90 C ATOM 698 CG ASN A 83 19.160 -17.081 -11.255 1.00 12.95 C ANISOU 698 CG ASN A 83 1590 1723 1609 48 -7 20 C ATOM 699 OD1 ASN A 83 19.463 -18.218 -11.599 1.00 15.21 O ANISOU 699 OD1 ASN A 83 1998 1879 1902 14 54 -88 O ATOM 700 ND2 ASN A 83 18.896 -16.119 -12.121 1.00 16.74 N ANISOU 700 ND2 ASN A 83 2322 2077 1958 22 -15 126 N ATOM 701 N HIS A 84 18.964 -18.464 -6.996 1.00 7.48 N ANISOU 701 N HIS A 84 886 837 1117 57 -2 -20 N ATOM 702 CA HIS A 84 19.235 -18.568 -5.571 1.00 7.47 C ANISOU 702 CA HIS A 84 905 839 1093 33 -11 -20 C ATOM 703 C HIS A 84 20.399 -19.525 -5.420 1.00 7.60 C ANISOU 703 C HIS A 84 937 844 1106 28 -16 -3 C ATOM 704 O HIS A 84 20.589 -20.396 -6.258 1.00 7.68 O ANISOU 704 O HIS A 84 978 838 1102 72 -9 -17 O ATOM 705 CB HIS A 84 17.995 -19.114 -4.851 1.00 7.34 C ANISOU 705 CB HIS A 84 862 776 1148 30 -27 -14 C ATOM 706 CG HIS A 84 18.080 -19.044 -3.363 1.00 7.17 C ANISOU 706 CG HIS A 84 813 753 1155 85 -2 -27 C ATOM 707 ND1 HIS A 84 18.349 -20.145 -2.572 1.00 7.59 N ANISOU 707 ND1 HIS A 84 929 809 1144 73 -58 -2 N ATOM 708 CD2 HIS A 84 17.924 -17.995 -2.522 1.00 7.32 C ANISOU 708 CD2 HIS A 84 891 739 1148 -7 34 -33 C ATOM 709 CE1 HIS A 84 18.366 -19.763 -1.307 1.00 7.30 C ANISOU 709 CE1 HIS A 84 966 806 1001 62 -66 -22 C ATOM 710 NE2 HIS A 84 18.111 -18.466 -1.248 1.00 7.46 N ANISOU 710 NE2 HIS A 84 913 870 1050 25 32 -117 N ATOM 711 N VAL A 85 21.170 -19.399 -4.347 1.00 7.51 N ANISOU 711 N VAL A 85 864 914 1076 41 7 -22 N ATOM 712 CA VAL A 85 22.321 -20.293 -4.159 1.00 8.18 C ANISOU 712 CA VAL A 85 974 983 1148 69 27 16 C ATOM 713 C VAL A 85 21.956 -21.772 -4.129 1.00 8.24 C ANISOU 713 C VAL A 85 992 966 1170 93 19 55 C ATOM 714 O VAL A 85 22.786 -22.611 -4.474 1.00 9.36 O ANISOU 714 O VAL A 85 1047 1132 1376 242 78 66 O ATOM 715 CB VAL A 85 23.155 -19.977 -2.896 1.00 9.19 C ANISOU 715 CB VAL A 85 1046 1215 1230 53 9 11 C ATOM 716 CG1 VAL A 85 23.899 -18.662 -3.059 1.00 10.92 C ANISOU 716 CG1 VAL A 85 1367 1346 1434 -26 3 -55 C ATOM 717 CG2 VAL A 85 22.309 -20.020 -1.632 1.00 9.42 C ANISOU 717 CG2 VAL A 85 1103 1292 1182 22 -16 -21 C ATOM 718 N THR A 86 20.728 -22.099 -3.733 1.00 7.82 N ANISOU 718 N THR A 86 990 865 1116 118 33 36 N ATOM 719 CA THR A 86 20.286 -23.486 -3.690 1.00 8.27 C ANISOU 719 CA THR A 86 1067 915 1159 94 18 24 C ATOM 720 C THR A 86 19.941 -24.064 -5.065 1.00 8.41 C ANISOU 720 C THR A 86 1110 926 1159 93 51 15 C ATOM 721 O THR A 86 19.725 -25.268 -5.172 1.00 9.18 O ANISOU 721 O THR A 86 1390 847 1249 79 63 -7 O ATOM 722 CB THR A 86 19.045 -23.649 -2.807 1.00 8.12 C ANISOU 722 CB THR A 86 1042 885 1155 115 15 38 C ATOM 723 OG1 THR A 86 18.003 -22.795 -3.290 1.00 7.70 O ANISOU 723 OG1 THR A 86 889 896 1138 92 3 55 O ATOM 724 CG2 THR A 86 19.379 -23.364 -1.350 1.00 9.23 C ANISOU 724 CG2 THR A 86 1271 1072 1162 167 3 -7 C ATOM 725 N LEU A 87 19.879 -23.218 -6.092 1.00 9.03 N ANISOU 725 N LEU A 87 1261 1017 1150 62 27 -27 N ATOM 726 CA LEU A 87 19.444 -23.611 -7.434 1.00 9.98 C ANISOU 726 CA LEU A 87 1381 1161 1248 14 1 -31 C ATOM 727 C LEU A 87 20.611 -23.544 -8.389 1.00 10.32 C ANISOU 727 C LEU A 87 1416 1187 1315 24 20 -45 C ATOM 728 O LEU A 87 21.074 -22.454 -8.716 1.00 11.63 O ANISOU 728 O LEU A 87 1608 1349 1459 -57 117 -44 O ATOM 729 CB LEU A 87 18.361 -22.654 -7.924 1.00 10.26 C ANISOU 729 CB LEU A 87 1513 1161 1223 -29 -54 -23 C ATOM 730 CG LEU A 87 17.075 -22.628 -7.115 1.00 10.63 C ANISOU 730 CG LEU A 87 1506 1279 1251 47 -110 -13 C ATOM 731 CD1 LEU A 87 16.191 -21.477 -7.555 1.00 11.93 C ANISOU 731 CD1 LEU A 87 1620 1349 1562 87 -179 -6 C ATOM 732 CD2 LEU A 87 16.335 -23.943 -7.251 1.00 11.97 C ANISOU 732 CD2 LEU A 87 1701 1384 1463 6 -32 5 C ATOM 733 N SER A 88 21.096 -24.694 -8.841 1.00 10.45 N ANISOU 733 N SER A 88 1255 1285 1428 94 29 3 N ATOM 734 CA SER A 88 22.264 -24.717 -9.713 1.00 11.28 C ANISOU 734 CA SER A 88 1346 1456 1481 93 34 29 C ATOM 735 C SER A 88 21.977 -24.110 -11.086 1.00 11.86 C ANISOU 735 C SER A 88 1360 1609 1538 117 25 66 C ATOM 736 O SER A 88 22.888 -23.614 -11.741 1.00 13.67 O ANISOU 736 O SER A 88 1569 1898 1727 47 32 221 O ATOM 737 CB SER A 88 22.804 -26.136 -9.841 1.00 11.73 C ANISOU 737 CB SER A 88 1336 1518 1600 132 52 7 C ATOM 738 OG SER A 88 21.779 -27.033 -10.194 1.00 12.64 O ANISOU 738 OG SER A 88 1519 1486 1797 196 61 -93 O ATOM 739 N GLN A 89 20.718 -24.156 -11.514 1.00 12.12 N ANISOU 739 N GLN A 89 1395 1668 1541 125 35 26 N ATOM 740 CA GLN A 89 20.259 -23.464 -12.718 1.00 12.97 C ANISOU 740 CA GLN A 89 1546 1748 1633 167 12 -4 C ATOM 741 C GLN A 89 19.104 -22.550 -12.317 1.00 12.32 C ANISOU 741 C GLN A 89 1429 1714 1536 170 2 -35 C ATOM 742 O GLN A 89 18.402 -22.843 -11.353 1.00 11.58 O ANISOU 742 O GLN A 89 1303 1685 1409 315 -4 -7 O ATOM 743 CB GLN A 89 19.755 -24.471 -13.758 1.00 13.87 C ANISOU 743 CB GLN A 89 1715 1830 1722 146 10 -35 C ATOM 744 CG GLN A 89 20.802 -25.467 -14.248 1.00 15.74 C ANISOU 744 CG GLN A 89 1978 2038 1962 164 62 -41 C ATOM 745 CD GLN A 89 20.198 -26.639 -15.011 1.00 17.30 C ANISOU 745 CD GLN A 89 2166 2192 2213 90 -34 -40 C ATOM 746 OE1 GLN A 89 19.233 -27.261 -14.565 1.00 21.97 O ANISOU 746 OE1 GLN A 89 2688 2819 2837 -77 50 15 O ATOM 747 NE2 GLN A 89 20.786 -26.960 -16.156 1.00 21.30 N ANISOU 747 NE2 GLN A 89 2725 2786 2581 54 45 -71 N ATOM 748 N PRO A 90 18.885 -21.448 -13.060 1.00 12.58 N ANISOU 748 N PRO A 90 1493 1673 1611 171 -1 -80 N ATOM 749 CA PRO A 90 17.696 -20.642 -12.784 1.00 12.49 C ANISOU 749 CA PRO A 90 1496 1628 1622 150 -36 -87 C ATOM 750 C PRO A 90 16.443 -21.501 -12.871 1.00 12.16 C ANISOU 750 C PRO A 90 1484 1583 1552 142 -69 -142 C ATOM 751 O PRO A 90 16.335 -22.359 -13.757 1.00 12.49 O ANISOU 751 O PRO A 90 1543 1671 1529 173 -118 -210 O ATOM 752 CB PRO A 90 17.701 -19.591 -13.900 1.00 13.28 C ANISOU 752 CB PRO A 90 1585 1718 1742 111 -55 -44 C ATOM 753 CG PRO A 90 19.059 -19.595 -14.470 1.00 14.11 C ANISOU 753 CG PRO A 90 1749 1837 1774 87 24 -17 C ATOM 754 CD PRO A 90 19.689 -20.911 -14.172 1.00 13.70 C ANISOU 754 CD PRO A 90 1639 1828 1736 102 -10 -15 C ATOM 755 N LYS A 91 15.518 -21.298 -11.941 1.00 11.75 N ANISOU 755 N LYS A 91 1442 1489 1532 131 -84 -135 N ATOM 756 CA LYS A 91 14.268 -22.031 -11.954 1.00 12.31 C ANISOU 756 CA LYS A 91 1504 1536 1637 118 -100 -124 C ATOM 757 C LYS A 91 13.201 -21.160 -12.596 1.00 11.29 C ANISOU 757 C LYS A 91 1372 1381 1536 143 -114 -179 C ATOM 758 O LYS A 91 12.955 -20.033 -12.146 1.00 10.76 O ANISOU 758 O LYS A 91 1285 1256 1547 225 -197 -223 O ATOM 759 CB LYS A 91 13.858 -22.429 -10.541 1.00 13.00 C ANISOU 759 CB LYS A 91 1626 1618 1695 137 -84 -90 C ATOM 760 CG LYS A 91 12.596 -23.256 -10.521 1.00 13.93 C ANISOU 760 CG LYS A 91 1688 1783 1821 58 -49 -55 C ATOM 761 CD LYS A 91 12.506 -24.198 -9.342 1.00 15.21 C ANISOU 761 CD LYS A 91 1927 1893 1956 39 -12 -18 C ATOM 762 CE LYS A 91 11.244 -25.058 -9.415 1.00 17.23 C ANISOU 762 CE LYS A 91 2135 2124 2286 -36 -6 35 C ATOM 763 NZ LYS A 91 11.138 -25.855 -10.669 1.00 20.33 N ANISOU 763 NZ LYS A 91 2535 2677 2511 13 7 -32 N ATOM 764 N ILE A 92 12.581 -21.680 -13.655 1.00 11.92 N ANISOU 764 N ILE A 92 1437 1471 1618 137 -155 -206 N ATOM 765 CA ILE A 92 11.532 -20.966 -14.369 1.00 12.74 C ANISOU 765 CA ILE A 92 1548 1590 1702 97 -128 -136 C ATOM 766 C ILE A 92 10.229 -21.710 -14.157 1.00 12.58 C ANISOU 766 C ILE A 92 1525 1527 1726 76 -136 -183 C ATOM 767 O ILE A 92 10.113 -22.893 -14.496 1.00 13.15 O ANISOU 767 O ILE A 92 1577 1576 1842 78 -174 -313 O ATOM 768 CB ILE A 92 11.841 -20.836 -15.869 1.00 13.51 C ANISOU 768 CB ILE A 92 1626 1738 1767 93 -109 -121 C ATOM 769 CG1 ILE A 92 13.131 -20.037 -16.067 1.00 14.40 C ANISOU 769 CG1 ILE A 92 1762 1894 1814 77 -74 -101 C ATOM 770 CG2 ILE A 92 10.679 -20.166 -16.603 1.00 13.65 C ANISOU 770 CG2 ILE A 92 1674 1784 1726 103 -149 -131 C ATOM 771 CD1 ILE A 92 13.622 -20.021 -17.488 1.00 15.21 C ANISOU 771 CD1 ILE A 92 1887 1989 1900 54 -3 -85 C ATOM 772 N VAL A 93 9.262 -21.016 -13.566 1.00 12.30 N ANISOU 772 N VAL A 93 1496 1525 1650 79 -153 -132 N ATOM 773 CA VAL A 93 7.951 -21.583 -13.303 1.00 12.88 C ANISOU 773 CA VAL A 93 1590 1599 1705 49 -102 -105 C ATOM 774 C VAL A 93 6.947 -20.836 -14.164 1.00 12.50 C ANISOU 774 C VAL A 93 1559 1545 1645 13 -133 -106 C ATOM 775 O VAL A 93 6.764 -19.623 -14.017 1.00 11.84 O ANISOU 775 O VAL A 93 1349 1485 1664 38 -155 -116 O ATOM 776 CB VAL A 93 7.579 -21.470 -11.813 1.00 12.78 C ANISOU 776 CB VAL A 93 1589 1581 1683 60 -114 -80 C ATOM 777 CG1 VAL A 93 6.175 -21.995 -11.568 1.00 13.85 C ANISOU 777 CG1 VAL A 93 1765 1676 1820 41 15 -61 C ATOM 778 CG2 VAL A 93 8.594 -22.226 -10.960 1.00 13.68 C ANISOU 778 CG2 VAL A 93 1762 1732 1702 86 -134 -51 C ATOM 779 N LYS A 94 6.320 -21.559 -15.088 1.00 13.69 N ANISOU 779 N LYS A 94 1729 1694 1776 22 -161 -118 N ATOM 780 CA LYS A 94 5.373 -20.954 -16.016 1.00 15.02 C ANISOU 780 CA LYS A 94 1883 1895 1927 -3 -140 -59 C ATOM 781 C LYS A 94 4.050 -20.678 -15.329 1.00 15.17 C ANISOU 781 C LYS A 94 1885 1917 1960 -10 -135 -54 C ATOM 782 O LYS A 94 3.618 -21.439 -14.463 1.00 15.69 O ANISOU 782 O LYS A 94 1885 1978 2096 33 -144 40 O ATOM 783 CB LYS A 94 5.156 -21.869 -17.222 1.00 15.61 C ANISOU 783 CB LYS A 94 1981 1968 1980 -33 -168 -78 C ATOM 784 CG LYS A 94 6.413 -22.082 -18.040 1.00 17.63 C ANISOU 784 CG LYS A 94 2237 2244 2215 7 -73 -38 C ATOM 785 CD LYS A 94 6.118 -22.821 -19.328 1.00 17.72 C ANISOU 785 CD LYS A 94 2282 2262 2189 9 -61 -63 C ATOM 786 CE LYS A 94 7.349 -22.929 -20.206 1.00 19.40 C ANISOU 786 CE LYS A 94 2486 2495 2390 44 25 -48 C ATOM 787 NZ LYS A 94 7.065 -23.725 -21.428 1.00 20.89 N ANISOU 787 NZ LYS A 94 2752 2673 2511 47 2 -99 N ATOM 788 N TRP A 95 3.416 -19.574 -15.709 1.00 15.36 N ANISOU 788 N TRP A 95 1894 1947 1992 -16 -131 -72 N ATOM 789 CA TRP A 95 2.067 -19.268 -15.251 1.00 16.37 C ANISOU 789 CA TRP A 95 2027 2075 2118 6 -79 -64 C ATOM 790 C TRP A 95 1.065 -20.147 -15.986 1.00 17.50 C ANISOU 790 C TRP A 95 2150 2228 2269 -7 -82 -65 C ATOM 791 O TRP A 95 1.023 -20.156 -17.217 1.00 17.42 O ANISOU 791 O TRP A 95 2073 2257 2288 -33 -137 -115 O ATOM 792 CB TRP A 95 1.728 -17.798 -15.510 1.00 15.02 C ANISOU 792 CB TRP A 95 1810 1938 1956 50 -117 -21 C ATOM 793 CG TRP A 95 0.316 -17.423 -15.174 1.00 14.45 C ANISOU 793 CG TRP A 95 1795 1832 1862 36 -155 -24 C ATOM 794 CD1 TRP A 95 -0.336 -17.647 -14.002 1.00 14.47 C ANISOU 794 CD1 TRP A 95 1784 1838 1873 17 -110 3 C ATOM 795 CD2 TRP A 95 -0.607 -16.728 -16.021 1.00 14.60 C ANISOU 795 CD2 TRP A 95 1824 1842 1882 -2 -101 -55 C ATOM 796 NE1 TRP A 95 -1.614 -17.144 -14.065 1.00 14.26 N ANISOU 796 NE1 TRP A 95 1805 1803 1809 -4 -76 -40 N ATOM 797 CE2 TRP A 95 -1.805 -16.574 -15.294 1.00 14.89 C ANISOU 797 CE2 TRP A 95 1846 1818 1993 -26 -84 -101 C ATOM 798 CE3 TRP A 95 -0.539 -16.231 -17.327 1.00 15.11 C ANISOU 798 CE3 TRP A 95 1831 1920 1990 1 -86 -114 C ATOM 799 CZ2 TRP A 95 -2.926 -15.941 -15.828 1.00 15.20 C ANISOU 799 CZ2 TRP A 95 1914 1897 1962 -26 -23 -66 C ATOM 800 CZ3 TRP A 95 -1.655 -15.600 -17.856 1.00 15.68 C ANISOU 800 CZ3 TRP A 95 1931 1960 2067 -22 -54 -84 C ATOM 801 CH2 TRP A 95 -2.832 -15.462 -17.105 1.00 15.61 C ANISOU 801 CH2 TRP A 95 1922 1953 2053 -23 -33 -58 C ATOM 802 N ASP A 96 0.268 -20.887 -15.225 1.00 19.26 N ANISOU 802 N ASP A 96 2383 2434 2498 -32 -48 -59 N ATOM 803 CA ASP A 96 -0.896 -21.570 -15.777 1.00 20.54 C ANISOU 803 CA ASP A 96 2548 2588 2667 -60 -46 -63 C ATOM 804 C ASP A 96 -1.985 -20.517 -16.004 1.00 21.64 C ANISOU 804 C ASP A 96 2702 2718 2802 -22 -38 -44 C ATOM 805 O ASP A 96 -2.372 -19.814 -15.073 1.00 21.91 O ANISOU 805 O ASP A 96 2712 2782 2829 -28 -35 -48 O ATOM 806 CB ASP A 96 -1.375 -22.652 -14.809 1.00 20.90 C ANISOU 806 CB ASP A 96 2607 2634 2698 -47 -37 -34 C ATOM 807 CG ASP A 96 -2.469 -23.529 -15.396 1.00 20.97 C ANISOU 807 CG ASP A 96 2621 2639 2707 -80 -37 -46 C ATOM 808 OD1 ASP A 96 -3.358 -23.001 -16.096 1.00 23.20 O ANISOU 808 OD1 ASP A 96 2856 2904 3054 -45 -77 -8 O ATOM 809 OD2 ASP A 96 -2.440 -24.751 -15.142 1.00 24.19 O ANISOU 809 OD2 ASP A 96 3069 2936 3183 -41 -51 66 O ATOM 810 N ARG A 97 -2.469 -20.418 -17.241 1.00 23.10 N ANISOU 810 N ARG A 97 2898 2917 2959 -13 -46 -34 N ATOM 811 CA ARG A 97 -3.432 -19.382 -17.646 1.00 24.23 C ANISOU 811 CA ARG A 97 3043 3060 3100 6 -44 -16 C ATOM 812 C ARG A 97 -4.753 -19.431 -16.877 1.00 24.72 C ANISOU 812 C ARG A 97 3111 3127 3153 2 -29 -24 C ATOM 813 O ARG A 97 -5.457 -18.423 -16.777 1.00 24.89 O ANISOU 813 O ARG A 97 3121 3150 3184 6 -41 -42 O ATOM 814 CB ARG A 97 -3.716 -19.490 -19.148 1.00 24.72 C ANISOU 814 CB ARG A 97 3120 3133 3140 6 -39 -11 C ATOM 815 CG ARG A 97 -2.482 -19.281 -20.009 1.00 25.86 C ANISOU 815 CG ARG A 97 3258 3292 3273 -8 -13 2 C ATOM 816 CD ARG A 97 -2.801 -18.776 -21.409 1.00 26.97 C ANISOU 816 CD ARG A 97 3412 3497 3338 41 -24 5 C ATOM 817 NE ARG A 97 -2.029 -17.565 -21.673 1.00 28.43 N ANISOU 817 NE ARG A 97 3597 3582 3620 -46 18 24 N ATOM 818 CZ ARG A 97 -2.342 -16.358 -21.202 1.00 29.02 C ANISOU 818 CZ ARG A 97 3693 3648 3682 -20 0 -8 C ATOM 819 NH1 ARG A 97 -3.431 -16.177 -20.458 1.00 29.25 N ANISOU 819 NH1 ARG A 97 3707 3634 3772 -66 49 6 N ATOM 820 NH2 ARG A 97 -1.566 -15.317 -21.480 1.00 29.96 N ANISOU 820 NH2 ARG A 97 3851 3766 3765 -1 -38 7 N ATOM 821 N ASP A 98 -5.088 -20.604 -16.350 1.00 25.17 N ANISOU 821 N ASP A 98 3169 3184 3209 -12 -25 -27 N ATOM 822 CA ASP A 98 -6.280 -20.778 -15.536 1.00 25.46 C ANISOU 822 CA ASP A 98 3207 3221 3244 -14 -10 -19 C ATOM 823 C ASP A 98 -5.913 -20.710 -14.054 1.00 25.68 C ANISOU 823 C ASP A 98 3235 3247 3274 -30 -16 -21 C ATOM 824 O ASP A 98 -6.585 -21.286 -13.196 1.00 25.92 O ANISOU 824 O ASP A 98 3274 3274 3298 -47 -1 -18 O ATOM 825 CB ASP A 98 -6.951 -22.111 -15.881 1.00 25.77 C ANISOU 825 CB ASP A 98 3249 3253 3289 -14 -14 -30 C ATOM 826 CG ASP A 98 -7.465 -22.145 -17.307 1.00 26.57 C ANISOU 826 CG ASP A 98 3366 3374 3355 -6 -18 -32 C ATOM 827 OD1 ASP A 98 -8.313 -21.294 -17.651 1.00 27.42 O ANISOU 827 OD1 ASP A 98 3459 3489 3469 21 -39 -40 O ATOM 828 OD2 ASP A 98 -7.021 -23.018 -18.083 1.00 27.49 O ANISOU 828 OD2 ASP A 98 3490 3501 3455 4 -1 -117 O TER 829 ASP A 98 HETATM 830 O HOH A 100 5.645 -20.140 -2.806 1.00 10.07 O ANISOU 830 O HOH A 100 1204 1342 1279 -46 -78 93 O HETATM 831 O HOH A 101 21.080 -16.959 -2.931 1.00 11.12 O ANISOU 831 O HOH A 101 1133 1055 2034 -39 -89 -358 O HETATM 832 O HOH A 102 11.087 -8.795 -13.422 1.00 11.31 O ANISOU 832 O HOH A 102 1497 1391 1408 -39 74 194 O HETATM 833 O HOH A 103 6.470 -10.863 1.907 1.00 13.66 O ANISOU 833 O HOH A 103 1589 1974 1625 -121 -135 74 O HETATM 834 O HOH A 104 19.988 -14.524 4.811 1.00 14.00 O ANISOU 834 O HOH A 104 2149 1497 1674 -367 -325 4 O HETATM 835 O HOH A 105 23.997 -20.654 2.026 1.00 14.47 O ANISOU 835 O HOH A 105 1874 1456 2166 -86 -113 -106 O HETATM 836 O HOH A 106 2.764 -3.536 -14.523 1.00 14.41 O ANISOU 836 O HOH A 106 1763 1984 1726 -104 -154 398 O HETATM 837 O HOH A 107 22.017 -20.437 -8.357 1.00 12.11 O ANISOU 837 O HOH A 107 1526 1455 1618 72 108 -20 O HETATM 838 O HOH A 108 20.198 -19.702 -9.473 1.00 16.13 O ANISOU 838 O HOH A 108 1637 2358 2131 310 327 -134 O HETATM 839 O HOH A 109 7.726 -16.158 -20.423 1.00 17.44 O ANISOU 839 O HOH A 109 2212 2585 1827 81 -164 -73 O HETATM 840 O HOH A 110 15.595 -13.856 -12.536 1.00 14.50 O ANISOU 840 O HOH A 110 1610 2124 1775 -50 107 101 O HETATM 841 O HOH A 111 -3.859 -17.935 -11.362 1.00 18.54 O ANISOU 841 O HOH A 111 2128 2105 2810 16 -208 35 O HETATM 842 O HOH A 112 19.602 -26.873 -7.650 1.00 15.28 O ANISOU 842 O HOH A 112 2150 1589 2065 -129 178 -181 O HETATM 843 O HOH A 113 18.990 -14.933 8.488 1.00 16.05 O ANISOU 843 O HOH A 113 2514 1675 1908 76 61 -135 O HETATM 844 O HOH A 114 1.684 -18.430 -19.392 1.00 17.15 O ANISOU 844 O HOH A 114 2002 2439 2076 -155 -323 -213 O HETATM 845 O HOH A 115 16.449 -24.724 -11.072 1.00 18.55 O ANISOU 845 O HOH A 115 2305 2517 2223 118 -45 -49 O HETATM 846 O HOH A 116 -4.805 -5.375 -15.965 1.00 16.62 O ANISOU 846 O HOH A 116 1955 2179 2178 -29 13 308 O HETATM 847 O HOH A 117 13.303 -24.298 -14.581 1.00 18.41 O ANISOU 847 O HOH A 117 2486 2066 2443 186 -192 -335 O HETATM 848 O HOH A 118 17.281 -26.684 -4.847 1.00 14.40 O ANISOU 848 O HOH A 118 1771 1747 1950 232 -62 -114 O HETATM 849 O HOH A 119 2.432 -21.929 -9.515 1.00 16.93 O ANISOU 849 O HOH A 119 2261 1853 2319 -92 -517 55 O HETATM 850 O HOH A 120 -2.362 -9.470 -6.824 1.00 19.95 O ANISOU 850 O HOH A 120 2451 2658 2471 44 -24 74 O HETATM 851 O HOH A 121 -3.823 -14.273 -3.128 1.00 18.53 O ANISOU 851 O HOH A 121 2338 2582 2120 90 83 121 O HETATM 852 O HOH A 122 0.937 -7.992 -20.139 1.00 19.15 O ANISOU 852 O HOH A 122 2449 2607 2221 18 -41 164 O HETATM 853 O HOH A 123 22.812 -19.525 7.210 1.00 19.23 O ANISOU 853 O HOH A 123 2590 1965 2750 0 -230 60 O HETATM 854 O HOH A 124 4.833 -4.103 -16.175 1.00 19.24 O ANISOU 854 O HOH A 124 2266 2510 2534 -44 -7 91 O HETATM 855 O HOH A 125 17.098 -26.600 5.121 1.00 21.09 O ANISOU 855 O HOH A 125 2517 2686 2810 -161 156 -73 O HETATM 856 O HOH A 126 13.842 -16.730 14.511 1.00 21.51 O ANISOU 856 O HOH A 126 2907 2760 2504 -85 -64 86 O HETATM 857 O HOH A 127 24.280 -14.814 1.857 1.00 21.36 O ANISOU 857 O HOH A 127 2659 2616 2840 48 -109 153 O HETATM 858 O HOH A 128 8.606 -24.429 -6.226 1.00 18.39 O ANISOU 858 O HOH A 128 2568 2042 2377 236 -263 -70 O HETATM 859 O HOH A 129 17.211 -9.658 -12.958 1.00 21.24 O ANISOU 859 O HOH A 129 2531 2745 2791 -47 -56 149 O HETATM 860 O HOH A 130 -9.939 -5.255 -1.125 1.00 19.02 O ANISOU 860 O HOH A 130 2753 1711 2760 -1 -118 -10 O HETATM 861 O HOH A 131 12.019 -13.762 13.656 1.00 18.78 O ANISOU 861 O HOH A 131 2283 2474 2378 55 -54 -163 O HETATM 862 O HOH A 132 -15.133 -7.403 -7.211 1.00 18.44 O ANISOU 862 O HOH A 132 2253 2397 2356 206 132 -164 O HETATM 863 O HOH A 133 -4.777 -19.116 -8.599 1.00 21.12 O ANISOU 863 O HOH A 133 2459 2648 2914 -61 -73 12 O HETATM 864 O HOH A 134 0.798 -21.198 -12.313 1.00 23.32 O ANISOU 864 O HOH A 134 3253 2577 3028 -59 140 -141 O HETATM 865 O HOH A 135 6.473 -24.541 -15.033 1.00 20.37 O ANISOU 865 O HOH A 135 2769 2150 2819 39 -163 -133 O HETATM 866 O HOH A 136 16.713 -22.672 -16.429 1.00 26.32 O ANISOU 866 O HOH A 136 3460 3448 3090 15 76 -27 O HETATM 867 O HOH A 137 -14.536 -3.455 -10.022 1.00 22.80 O ANISOU 867 O HOH A 137 2708 2917 3038 126 120 13 O HETATM 868 O HOH A 138 18.834 -16.036 -14.975 1.00 24.88 O ANISOU 868 O HOH A 138 3250 3158 3044 30 -67 25 O HETATM 869 O HOH A 139 -12.313 -9.196 -14.484 1.00 22.01 O ANISOU 869 O HOH A 139 2593 3039 2731 1 49 6 O HETATM 870 O HOH A 140 22.763 -22.066 11.569 1.00 21.65 O ANISOU 870 O HOH A 140 2878 2703 2644 -4 143 -193 O HETATM 871 O HOH A 141 -6.702 -13.294 -12.236 1.00 19.63 O ANISOU 871 O HOH A 141 2326 2533 2597 -30 -52 -28 O HETATM 872 O HOH A 142 -0.372 -10.776 -22.916 1.00 26.56 O ANISOU 872 O HOH A 142 3251 3445 3394 -2 -79 -57 O HETATM 873 O HOH A 143 -16.002 -3.876 -7.587 1.00 20.06 O ANISOU 873 O HOH A 143 2477 2448 2695 -114 -51 148 O HETATM 874 O HOH A 144 20.686 -14.499 -6.458 1.00 24.56 O ANISOU 874 O HOH A 144 3029 3181 3123 37 56 -65 O HETATM 875 O HOH A 145 -6.798 -9.495 -17.762 1.00 23.21 O ANISOU 875 O HOH A 145 2776 3190 2853 115 -144 3 O HETATM 876 O HOH A 146 22.893 -19.633 4.433 1.00 25.52 O ANISOU 876 O HOH A 146 3276 3310 3108 16 33 0 O HETATM 877 O HOH A 147 21.533 -14.011 -9.462 1.00 21.77 O ANISOU 877 O HOH A 147 2607 2792 2870 92 39 -12 O HETATM 878 O HOH A 148 -1.349 -12.714 -3.511 1.00 21.85 O ANISOU 878 O HOH A 148 2683 2967 2650 -8 3 -161 O HETATM 879 O HOH A 149 15.206 -25.789 -13.245 1.00 29.84 O ANISOU 879 O HOH A 149 3782 3762 3791 32 -47 -64 O HETATM 880 O HOH A 150 8.126 -3.327 -18.290 1.00 28.09 O ANISOU 880 O HOH A 150 3574 3558 3539 -2 -26 85 O HETATM 881 O HOH A 151 6.712 -6.971 3.510 1.00 26.28 O ANISOU 881 O HOH A 151 3352 3205 3427 52 18 -20 O HETATM 882 O HOH A 152 7.361 -3.724 0.509 1.00 27.72 O ANISOU 882 O HOH A 152 3658 3309 3564 69 -50 -56 O HETATM 883 O HOH A 153 13.494 -23.297 -5.804 1.00 26.73 O ANISOU 883 O HOH A 153 3358 3333 3463 -18 -34 -90 O HETATM 884 O HOH A 154 9.725 -4.974 -19.962 1.00 27.78 O ANISOU 884 O HOH A 154 3552 3615 3385 23 0 40 O HETATM 885 O HOH A 155 13.158 -13.856 -25.635 1.00 33.56 O ANISOU 885 O HOH A 155 4241 4277 4233 -3 -27 -31 O HETATM 886 O HOH A 156 12.969 -25.689 0.703 1.00 23.25 O ANISOU 886 O HOH A 156 2841 2949 3043 -8 -12 187 O HETATM 887 O HOH A 157 23.459 -20.923 -10.392 1.00 26.89 O ANISOU 887 O HOH A 157 3251 3501 3464 -72 74 40 O HETATM 888 O HOH A 158 -8.741 -13.928 -15.030 1.00 28.67 O ANISOU 888 O HOH A 158 3534 3630 3729 -15 29 -66 O HETATM 889 O HOH A 159 8.269 -9.876 -24.180 1.00 28.99 O ANISOU 889 O HOH A 159 3811 3669 3532 -23 -80 51 O HETATM 890 O HOH A 160 7.463 -22.407 1.378 1.00 27.81 O ANISOU 890 O HOH A 160 3668 3438 3458 0 -82 62 O HETATM 891 O HOH A 161 25.900 -19.850 10.233 1.00 31.10 O ANISOU 891 O HOH A 161 4013 3827 3975 -18 -51 -95 O HETATM 892 O HOH A 162 15.462 -17.812 -18.908 1.00 34.44 O ANISOU 892 O HOH A 162 4378 4387 4318 0 24 28 O HETATM 893 O HOH A 163 -6.245 -2.188 -9.752 1.00 35.60 O ANISOU 893 O HOH A 163 4535 4467 4523 -11 21 13 O HETATM 894 O HOH A 164 5.267 -2.928 -2.925 1.00 31.71 O ANISOU 894 O HOH A 164 4103 3983 3959 16 -65 27 O HETATM 895 O HOH A 165 10.707 -23.324 0.826 1.00 26.80 O ANISOU 895 O HOH A 165 3457 3348 3375 75 0 -11 O HETATM 896 O HOH A 166 -1.308 -10.297 -4.628 1.00 30.96 O ANISOU 896 O HOH A 166 3910 4001 3852 84 49 24 O HETATM 897 O HOH A 167 6.350 -10.173 -25.994 1.00 34.65 O ANISOU 897 O HOH A 167 4394 4418 4351 24 -5 -8 O HETATM 898 O HOH A 168 -8.752 -1.385 -14.724 1.00 40.69 O ANISOU 898 O HOH A 168 5176 5145 5137 11 3 2 O HETATM 899 O HOH A 169 7.661 -2.562 -4.089 1.00 29.74 O ANISOU 899 O HOH A 169 3846 3636 3815 30 -57 -6 O HETATM 900 O HOH A 170 2.153 -4.413 -2.128 1.00 28.30 O ANISOU 900 O HOH A 170 3585 3577 3589 25 -65 -18 O HETATM 901 O HOH A 171 12.414 -6.036 -3.247 1.00 26.19 O ANISOU 901 O HOH A 171 3282 3267 3401 -77 -78 -18 O HETATM 902 O HOH A 172 7.183 -24.320 -8.547 1.00 28.06 O ANISOU 902 O HOH A 172 3651 3494 3514 39 1 16 O HETATM 903 O HOH A 173 -6.245 -9.617 -20.354 1.00 32.02 O ANISOU 903 O HOH A 173 4068 4120 3978 77 -23 18 O HETATM 904 O HOH A 174 3.341 -6.423 -16.734 1.00 22.14 O ANISOU 904 O HOH A 174 2699 2937 2774 -86 90 -11 O HETATM 905 O HOH A 175 24.186 -25.012 -13.861 1.00 25.61 O ANISOU 905 O HOH A 175 3220 3328 3181 -23 -13 51 O HETATM 906 O HOH A 176 -6.739 -6.543 -17.464 1.00 34.73 O ANISOU 906 O HOH A 176 4382 4378 4434 30 -44 5 O HETATM 907 O HOH A 177 -5.980 -14.074 -15.649 1.00 28.30 O ANISOU 907 O HOH A 177 3506 3552 3694 45 -5 -30 O HETATM 908 O HOH A 178 15.175 -7.538 -25.029 1.00 32.37 O ANISOU 908 O HOH A 178 4036 4164 4096 7 46 -47 O HETATM 909 O HOH A 179 -0.409 -23.172 -1.865 1.00 36.31 O ANISOU 909 O HOH A 179 4526 4634 4634 -8 14 12 O HETATM 910 O HOH A 180 -11.759 -11.697 -15.387 1.00 30.77 O ANISOU 910 O HOH A 180 3910 3920 3858 -23 -49 19 O HETATM 911 O HOH A 181 4.957 -19.558 -26.292 1.00 39.33 O ANISOU 911 O HOH A 181 5007 4972 4962 8 6 1 O HETATM 912 O HOH A 182 -17.881 -5.484 -17.262 1.00 44.87 O ANISOU 912 O HOH A 182 5699 5690 5658 5 11 5 O HETATM 913 O HOH A 183 7.919 -18.864 -20.471 1.00 38.70 O ANISOU 913 O HOH A 183 4930 4905 4869 9 0 -41 O HETATM 914 O HOH A 184 10.103 -2.873 -2.490 1.00 36.71 O ANISOU 914 O HOH A 184 4653 4622 4670 -39 -17 11 O HETATM 915 O HOH A 185 10.428 -25.352 -13.241 1.00 34.54 O ANISOU 915 O HOH A 185 4396 4351 4376 -6 11 4 O HETATM 916 O HOH A 186 11.284 -24.457 -6.213 1.00 30.80 O ANISOU 916 O HOH A 186 3901 3835 3964 38 -32 -94 O HETATM 917 O HOH A 187 -8.790 -8.223 -16.416 1.00 32.03 O ANISOU 917 O HOH A 187 4045 4092 4032 -21 24 25 O HETATM 918 O HOH A 188 -12.517 -2.549 -12.742 1.00 28.61 O ANISOU 918 O HOH A 188 3801 3561 3508 93 7 73 O HETATM 919 O HOH A 189 -4.598 0.762 -12.658 1.00 41.32 O ANISOU 919 O HOH A 189 5229 5256 5214 -15 -6 4 O HETATM 920 O HOH A 190 -7.522 -18.679 -12.141 1.00 38.20 O ANISOU 920 O HOH A 190 4816 4854 4842 5 -14 -26 O CONECT 211 674 CONECT 674 211 MASTER 260 0 0 1 8 0 0 6 919 1 2 8 END