HEADER ISOMERASE 19-JUL-00 1E58 TITLE E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHOSPHOGLYCERATE MUTASE; COMPND 3 CHAIN: A; COMPND 4 EC: 5.4.2.1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 STRAIN: K12; SOURCE 4 GENE: PGM1; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET3A KEYWDS PHOSPHOHISTIDINE, GLYCOLYSIS AND GLUCONEOGENESIS, KEYWDS 2 PHOSPHOGLYCERATE MUTASE, ISOMERASE EXPDTA X-RAY DIFFRACTION AUTHOR C.S.BOND,W.N.HUNTER REVDAT 1 20-MAR-01 1E58 0 JRNL AUTH C.S.BOND,M.F.WHITE,W.N.HUNTER JRNL TITL HIGH-RESOLUTION STRUCTURE OF THE PHOSPHOHISTIDINE- JRNL TITL 2 ACTIVATED FORM OF ESCHERICHIA COLI COFACTOR- JRNL TITL 3 DEPENDENT PHOSPHOGLYCERATE MUTASE JRNL REF J.BIOL.CHEM. V. 276 3247 2001 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 1.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 83.0 REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1209 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.121 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.168 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.0 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 65026 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.1195 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 62531 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2065 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 15 REMARK 3 SOLVENT ATOMS : 425 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2434.16 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1977.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 17 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 22606 REMARK 3 NUMBER OF RESTRAINTS : 27457 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.014 REMARK 3 ANGLE DISTANCES (A) : 0.030 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.0314 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.079 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.085 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.076 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.042 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.080 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2 REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY REMARK 3 THE METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28 REMARK 3 (1995)53-56 REMARK 3 PHOSPHOHISTIDINE MODELLED AT 0.28 OCCUPANCY COUPLED TO A REMARK 3 0.72 OCCUPANCY HISTIDINE WITH THREE WATER MOLECULES REMARK 4 REMARK 4 1E58 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 20-JUL-2000. REMARK 100 THE EBI ID CODE IS EBI-5176. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-SEP-1999 REMARK 200 TEMPERATURE (KELVIN) : 105 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS BEAMLINE PX9.6 REMARK 200 BEAMLINE : PX9.6 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.89 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67122 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.25 REMARK 200 RESOLUTION RANGE LOW (A) : 30.0 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.4 REMARK 200 DATA REDUNDANCY : 2 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.047 REMARK 200 FOR THE DATA SET : 211 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26 REMARK 200 COMPLETENESS FOR SHELL (%) : 63 REMARK 200 DATA REDUNDANCY IN SHELL : 2 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.071 REMARK 200 FOR SHELL : 11 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: SHELX REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL (PH 8.0), REMARK 280 200 MM LI2SO4, 20% PEG 4000 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 1/2-X,1/2+Y,-Z REMARK 290 4555 1/2+X,1/2-Y,-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 30.78500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.50000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.78500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.50000 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 300 REMARK 300 BIOLOGICAL UNIT: HOMODIMER REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 61.57000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 400 REMARK 400 COMPOUND REMARK 400 CATALYTIC ACTIVITY: 2-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE = REMARK 400 3-PHOSPHOGLYCERATE + 2,3-DIPHOSPHOGLYCERATE. REMARK 400 PATHWAY: GLYCOLYSIS. REMARK 400 SIMILARITY: BELONGS TO THE PHOSPHOGLYCERATE MUTASE FAMILY. 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 ALA A 248 REMARK 465 LYS A 249 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 116 CB - CG - CD ANGL. DEV. = -13.2 DEGREES REMARK 500 ARG A 138 C - N - CA ANGL. DEV. = -14.7 DEGREES REMARK 500 GLU A 200 CB - CG - CD ANGL. DEV. = 15.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 REMARK 500 O HOH Z 275 O HOH Z 276 2.04 REMARK 500 O HOH Z 276 O HOH Z 277 2.02 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 REMARK 500 O HOH Z 276 O HOH Z 417 2456 2.08 REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY REMARK 525 ASSOCIATED WITH: REMARK 525 PROTEIN CHAIN SOLVENT CHAIN REMARK 525 A Z REMARK 600 REMARK 600 HETEROGEN REMARK 600 PHS: PART OF PHOSPHOHISTIDINE AT HIS 10 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: HIS REMARK 800 SITE_DESCRIPTION: PHOSPHOHISTIDINE REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1E59 RELATED DB: PDB REMARK 900 E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE REMARK 900 COMPLEXED WITH VANADATE REMARK 900 DBREF 1E58 A 1 249 SWS P31217 PMG1_ECOLI 1 249 SEQRES 1 A 249 ALA VAL THR LYS LEU VAL LEU VAL ARG HIS GLY GLU SER SEQRES 2 A 249 GLN TRP ASN LYS GLU ASN ARG PHE THR GLY TRP TYR ASP SEQRES 3 A 249 VAL ASP LEU SER GLU LYS GLY VAL SER GLU ALA LYS ALA SEQRES 4 A 249 ALA GLY LYS LEU LEU LYS GLU GLU GLY TYR SER PHE ASP SEQRES 5 A 249 PHE ALA TYR THR SER VAL LEU LYS ARG ALA ILE HIS THR SEQRES 6 A 249 LEU TRP ASN VAL LEU ASP GLU LEU ASP GLN ALA TRP LEU SEQRES 7 A 249 PRO VAL GLU LYS SER TRP LYS LEU ASN GLU ARG HIS TYR SEQRES 8 A 249 GLY ALA LEU GLN GLY LEU ASN LYS ALA GLU THR ALA GLU SEQRES 9 A 249 LYS TYR GLY ASP GLU GLN VAL LYS GLN TRP ARG ARG GLY SEQRES 10 A 249 PHE ALA VAL THR PRO PRO GLU LEU THR LYS ASP ASP GLU SEQRES 11 A 249 ARG TYR PRO GLY HIS ASP PRO ARG TYR ALA LYS LEU SER SEQRES 12 A 249 GLU LYS GLU LEU PRO LEU THR GLU SER LEU ALA LEU THR SEQRES 13 A 249 ILE ASP ARG VAL ILE PRO TYR TRP ASN GLU THR ILE LEU SEQRES 14 A 249 PRO ARG MET LYS SER GLY GLU ARG VAL ILE ILE ALA ALA SEQRES 15 A 249 HIS GLY ASN SER LEU ARG ALA LEU VAL LYS TYR LEU ASP SEQRES 16 A 249 ASN MET SER GLU GLU GLU ILE LEU GLU LEU ASN ILE PRO SEQRES 17 A 249 THR GLY VAL PRO LEU VAL TYR GLU PHE ASP GLU ASN PHE SEQRES 18 A 249 LYS PRO LEU LYS ARG TYR TYR LEU GLY ASN ALA ASP GLU SEQRES 19 A 249 ILE ALA ALA LYS ALA ALA ALA VAL ALA ASN GLN GLY LYS SEQRES 20 A 249 ALA LYS HET SO4 A1001 5 HET SO4 A1002 5 HET CL A2001 1 HET PHS A1010 4 PART OF PHOSPHOHISTIDINE AT HIS 10 HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION HETNAM PHS PHOSPHONO GROUP FORMUL 2 SO4 2(O4 S1 2-) FORMUL 3 CL CL1 1- FORMUL 4 PHS H2 O3 P1 FORMUL 5 HOH *425(H2 O1) HELIX 1 1 SER A 13 GLU A 18 1 6 HELIX 2 2 SER A 30 GLU A 47 1 18 HELIX 3 3 LEU A 59 ASP A 74 1 16 HELIX 4 4 TRP A 84 ASN A 87 5 4 HELIX 5 5 TYR A 91 GLN A 95 5 5 HELIX 6 6 ASN A 98 GLY A 107 1 10 HELIX 7 7 GLY A 107 GLY A 117 1 11 HELIX 8 8 TYR A 132 ASP A 136 5 5 HELIX 9 9 ASP A 136 ALA A 140 5 5 HELIX 10 10 SER A 152 THR A 167 1 16 HELIX 11 11 THR A 167 SER A 174 1 8 HELIX 12 12 HIS A 183 ASP A 195 1 13 HELIX 13 13 SER A 198 LEU A 205 1 8 HELIX 14 14 ASN A 231 ALA A 239 1 9 SHEET 1 A 6 VAL A 80 LYS A 82 0 SHEET 2 A 6 PHE A 53 THR A 56 1 N ALA A 54 O GLU A 81 SHEET 3 A 6 VAL A 178 ALA A 182 1 N ILE A 179 O PHE A 53 SHEET 4 A 6 THR A 3 ARG A 9 1 N VAL A 6 O VAL A 178 SHEET 5 A 6 LEU A 213 PHE A 217 -1 N PHE A 217 O THR A 3 SHEET 6 A 6 PRO A 223 TYR A 228 -1 N TYR A 227 O VAL A 214 LINK P PHS A1010 NE2AHIS A 10 LINK P PHS A1010 NE2BHIS A 10 SITE 1 HIS 1 HIS A 10 CRYST1 61.570 113.000 40.260 90.00 90.00 90.00 P 21 21 2 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 0.016242 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008849 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024838 0.00000 ATOM 1 N AALA A 1 58.525 3.470 39.324 0.25 36.45 N ANISOU 1 N AALA A 1 4687 3299 5865 1254 -1837 -1634 N ATOM 2 CA AALA A 1 57.487 3.868 40.289 0.25 31.86 C ANISOU 2 CA AALA A 1 3737 3240 5129 1219 -1910 249 C ATOM 3 CB AALA A 1 58.109 3.785 41.672 0.25 32.19 C ANISOU 3 CB AALA A 1 3928 3284 5019 67 -1819 1100 C ATOM 4 N BALA A 1 57.891 3.962 41.834 0.75 32.27 N ANISOU 4 N BALA A 1 3491 3534 5235 -935 -2323 1187 N ATOM 5 CA BALA A 1 57.648 3.995 40.398 0.75 31.29 C ANISOU 5 CA BALA A 1 3750 3061 5079 1151 -1928 29 C ATOM 6 CB BALA A 1 56.955 2.698 39.979 0.75 24.59 C ANISOU 6 CB BALA A 1 1979 3056 4310 1276 -944 170 C ATOM 7 C ALA A 1 56.837 5.202 39.948 1.00 30.11 C ANISOU 7 C ALA A 1 3506 3094 4840 1084 -1344 456 C ATOM 8 O ALA A 1 56.079 5.859 40.669 1.00 27.20 O ANISOU 8 O ALA A 1 2865 3241 4229 947 -1270 1011 O ATOM 9 N VAL A 2 57.015 5.625 38.696 1.00 24.07 N ANISOU 9 N VAL A 2 1653 2537 4956 519 -951 157 N ATOM 10 CA VAL A 2 56.167 6.627 38.091 1.00 23.95 C ANISOU 10 CA VAL A 2 1687 2269 5144 -63 -785 958 C ATOM 11 C VAL A 2 54.814 6.017 37.710 1.00 18.21 C ANISOU 11 C VAL A 2 1933 1924 3062 231 -957 300 C ATOM 12 O VAL A 2 54.864 4.873 37.210 1.00 24.12 O ANISOU 12 O VAL A 2 3314 2021 3831 942 -1659 -4 O ATOM 13 CB VAL A 2 56.809 7.178 36.802 1.00 27.26 C ANISOU 13 CB VAL A 2 1660 3602 5097 259 -268 726 C ATOM 14 CG1 VAL A 2 55.782 8.003 36.074 1.00 37.30 C ANISOU 14 CG1 VAL A 2 4541 4165 5468 847 -1105 1775 C ATOM 15 CG2 VAL A 2 58.067 7.948 37.162 1.00 34.77 C ANISOU 15 CG2 VAL A 2 2122 2038 9050 -283 422 540 C ATOM 16 N THR A 3 53.715 6.723 37.924 1.00 15.38 N ANISOU 16 N THR A 3 1773 1697 2374 68 -1120 373 N ATOM 17 CA THR A 3 52.365 6.316 37.566 1.00 13.74 C ANISOU 17 CA THR A 3 1825 1407 1988 -165 -884 123 C ATOM 18 C THR A 3 51.933 7.109 36.345 1.00 12.99 C ANISOU 18 C THR A 3 1266 1425 2246 12 -762 307 C ATOM 19 O THR A 3 52.105 8.340 36.290 1.00 15.43 O ANISOU 19 O THR A 3 2250 1413 2199 172 -1015 131 O ATOM 20 CB THR A 3 51.358 6.595 38.706 1.00 14.90 C ANISOU 20 CB THR A 3 2062 1488 2111 113 -752 111 C ATOM 21 OG1 THR A 3 51.679 5.764 39.841 1.00 19.22 O ANISOU 21 OG1 THR A 3 2514 2400 2389 -306 -620 673 O ATOM 22 CG2 THR A 3 49.917 6.263 38.299 1.00 16.20 C ANISOU 22 CG2 THR A 3 2035 1786 2334 -40 -438 -94 C ATOM 23 N LYS A 4 51.379 6.473 35.326 1.00 11.41 N ANISOU 23 N LYS A 4 1130 1257 1950 58 -508 470 N ATOM 24 CA LYS A 4 50.872 7.122 34.146 1.00 11.55 C ANISOU 24 CA LYS A 4 1060 1438 1889 0 -451 434 C ATOM 25 C LYS A 4 49.336 7.221 34.150 1.00 10.52 C ANISOU 25 C LYS A 4 1071 1122 1805 -150 -525 544 C ATOM 26 O LYS A 4 48.656 6.262 34.567 1.00 10.18 O ANISOU 26 O LYS A 4 1238 865 1766 -192 -502 468 O ATOM 27 CB LYS A 4 51.321 6.407 32.873 1.00 14.63 C ANISOU 27 CB LYS A 4 1625 1926 2009 279 -339 306 C ATOM 28 CG LYS A 4 52.843 6.461 32.765 1.00 23.75 C ANISOU 28 CG LYS A 4 1593 3523 3908 1575 149 677 C ATOM 29 CD LYS A 4 53.279 6.385 31.333 1.00 25.72 C ANISOU 29 CD LYS A 4 1918 3735 4119 222 591 1690 C ATOM 30 CE LYS A 4 54.768 6.448 31.108 1.00 20.55 C ANISOU 30 CE LYS A 4 1860 1763 4187 324 512 717 C ATOM 31 NZ LYS A 4 54.997 5.872 29.765 1.00 26.31 N ANISOU 31 NZ LYS A 4 1734 4876 3388 644 -339 618 N ATOM 32 N LEU A 5 48.870 8.378 33.670 1.00 8.27 N ANISOU 32 N LEU A 5 919 785 1439 -214 -297 287 N ATOM 33 CA LEU A 5 47.462 8.700 33.414 1.00 7.49 C ANISOU 33 CA LEU A 5 930 698 1218 -204 -285 147 C ATOM 34 C LEU A 5 47.323 9.057 31.948 1.00 7.40 C ANISOU 34 C LEU A 5 839 761 1211 -205 -198 153 C ATOM 35 O LEU A 5 48.150 9.831 31.459 1.00 9.04 O ANISOU 35 O LEU A 5 1096 1005 1332 -545 -334 231 O ATOM 36 CB LEU A 5 46.982 9.846 34.295 1.00 8.38 C ANISOU 36 CB LEU A 5 970 989 1224 -163 -259 34 C ATOM 37 CG LEU A 5 45.615 10.443 34.033 1.00 8.28 C ANISOU 37 CG LEU A 5 1056 761 1328 -116 -280 91 C ATOM 38 CD1 LEU A 5 44.507 9.447 34.374 1.00 9.44 C ANISOU 38 CD1 LEU A 5 958 985 1644 -147 -60 -151 C ATOM 39 CD2 LEU A 5 45.430 11.715 34.826 1.00 9.52 C ANISOU 39 CD2 LEU A 5 1315 867 1434 -46 -292 -64 C ATOM 40 N VAL A 6 46.303 8.559 31.256 1.00 6.14 N ANISOU 40 N VAL A 6 672 546 1113 -105 -139 174 N ATOM 41 CA VAL A 6 46.062 8.948 29.890 1.00 6.29 C ANISOU 41 CA VAL A 6 735 576 1078 46 -124 169 C ATOM 42 C VAL A 6 44.726 9.668 29.778 1.00 5.79 C ANISOU 42 C VAL A 6 632 619 950 -67 -112 90 C ATOM 43 O VAL A 6 43.708 9.128 30.243 1.00 7.62 O ANISOU 43 O VAL A 6 689 730 1476 -164 -21 92 O ATOM 44 CB VAL A 6 46.104 7.751 28.924 1.00 6.45 C ANISOU 44 CB VAL A 6 643 721 1088 -4 109 85 C ATOM 45 CG1 VAL A 6 45.749 8.149 27.500 1.00 7.91 C ANISOU 45 CG1 VAL A 6 967 914 1123 88 42 -33 C ATOM 46 CG2 VAL A 6 47.477 7.035 28.991 1.00 8.29 C ANISOU 46 CG2 VAL A 6 674 979 1498 137 139 4 C ATOM 47 N LEU A 7 44.736 10.851 29.168 1.00 6.26 N ANISOU 47 N LEU A 7 673 608 1098 61 -29 122 N ATOM 48 CA LEU A 7 43.581 11.656 28.855 1.00 6.08 C ANISOU 48 CA LEU A 7 552 693 1065 25 -45 74 C ATOM 49 C LEU A 7 43.329 11.656 27.347 1.00 5.92 C ANISOU 49 C LEU A 7 575 627 1049 -65 0 93 C ATOM 50 O LEU A 7 44.287 11.742 26.583 1.00 6.86 O ANISOU 50 O LEU A 7 572 920 1114 -98 -2 81 O ATOM 51 CB LEU A 7 43.764 13.108 29.304 1.00 6.63 C ANISOU 51 CB LEU A 7 747 602 1171 -41 113 23 C ATOM 52 CG LEU A 7 44.220 13.329 30.750 1.00 8.11 C ANISOU 52 CG LEU A 7 1008 835 1238 -36 -55 -106 C ATOM 53 CD1 LEU A 7 44.386 14.836 31.024 1.00 9.01 C ANISOU 53 CD1 LEU A 7 1336 892 1194 -220 -19 -124 C ATOM 54 CD2 LEU A 7 43.294 12.715 31.756 1.00 8.14 C ANISOU 54 CD2 LEU A 7 1315 675 1103 25 -183 106 C ATOM 55 N VAL A 8 42.074 11.606 26.928 1.00 5.98 N ANISOU 55 N VAL A 8 613 720 939 -110 21 186 N ATOM 56 CA VAL A 8 41.779 11.747 25.503 1.00 6.40 C ANISOU 56 CA VAL A 8 652 824 957 31 38 133 C ATOM 57 C VAL A 8 40.457 12.486 25.351 1.00 5.36 C ANISOU 57 C VAL A 8 731 573 733 25 76 -33 C ATOM 58 O VAL A 8 39.424 12.094 25.897 1.00 6.19 O ANISOU 58 O VAL A 8 562 748 1042 56 116 161 O ATOM 59 CB AVAL A 8 41.845 10.423 24.749 0.65 6.83 C ANISOU 59 CB AVAL A 8 747 827 1019 274 -35 63 C ATOM 60 CG1AVAL A 8 40.744 9.476 25.190 0.65 7.04 C ANISOU 60 CG1AVAL A 8 805 876 994 137 10 -151 C ATOM 61 CG2AVAL A 8 41.763 10.615 23.224 0.65 10.55 C ANISOU 61 CG2AVAL A 8 1769 1268 973 317 317 -15 C ATOM 62 CB BVAL A 8 41.652 10.420 24.745 0.35 8.66 C ANISOU 62 CB BVAL A 8 1167 985 1138 427 50 -191 C ATOM 63 CG1BVAL A 8 41.778 10.679 23.232 0.35 13.01 C ANISOU 63 CG1BVAL A 8 2080 1792 1071 1432 -25 -245 C ATOM 64 CG2BVAL A 8 42.655 9.337 25.122 0.35 7.21 C ANISOU 64 CG2BVAL A 8 653 936 1151 58 -192 -190 C ATOM 65 N ARG A 9 40.513 13.572 24.601 1.00 5.57 N ANISOU 65 N ARG A 9 682 608 825 -91 -30 25 N ATOM 66 CA ARG A 9 39.288 14.240 24.153 1.00 5.90 C ANISOU 66 CA ARG A 9 726 528 989 -31 -99 23 C ATOM 67 C ARG A 9 38.575 13.366 23.114 1.00 5.72 C ANISOU 67 C ARG A 9 707 465 1001 66 -105 22 C ATOM 68 O ARG A 9 39.210 12.761 22.265 1.00 7.01 O ANISOU 68 O ARG A 9 841 718 1106 52 38 -52 O ATOM 69 CB ARG A 9 39.599 15.629 23.589 1.00 6.01 C ANISOU 69 CB ARG A 9 913 554 817 -99 -84 53 C ATOM 70 CG ARG A 9 38.379 16.438 23.162 1.00 6.71 C ANISOU 70 CG ARG A 9 831 617 1100 -76 -66 138 C ATOM 71 CD ARG A 9 38.809 17.824 22.651 1.00 6.86 C ANISOU 71 CD ARG A 9 736 701 1168 -27 -12 140 C ATOM 72 NE ARG A 9 37.673 18.522 22.071 1.00 6.90 N ANISOU 72 NE ARG A 9 842 542 1237 -57 -78 95 N ATOM 73 CZ ARG A 9 37.740 19.494 21.195 1.00 7.59 C ANISOU 73 CZ ARG A 9 832 852 1202 3 73 245 C ATOM 74 NH1 ARG A 9 38.924 19.946 20.770 1.00 9.39 N ANISOU 74 NH1 ARG A 9 839 961 1769 -106 -10 397 N ATOM 75 NH2 ARG A 9 36.613 20.046 20.711 1.00 9.02 N ANISOU 75 NH2 ARG A 9 860 962 1605 101 160 470 N ATOM 76 N HIS A 10 37.223 13.358 23.156 1.00 5.66 N ANISOU 76 N HIS A 10 690 565 895 59 -126 -73 N ATOM 77 CA HIS A 10 36.427 12.646 22.146 1.00 5.83 C ANISOU 77 CA HIS A 10 766 578 872 -64 -90 52 C ATOM 78 C HIS A 10 36.943 12.958 20.733 1.00 6.20 C ANISOU 78 C HIS A 10 1005 479 872 143 7 124 C ATOM 79 O HIS A 10 37.394 14.092 20.446 1.00 6.59 O ANISOU 79 O HIS A 10 878 671 956 33 46 94 O ATOM 80 CB HIS A 10 34.960 13.029 22.259 1.00 6.25 C ANISOU 80 CB HIS A 10 704 744 925 -35 -162 98 C ATOM 81 CG AHIS A 10 34.685 14.464 22.022 0.71 6.30 C ANISOU 81 CG AHIS A 10 684 640 1068 -72 -217 68 C ATOM 82 ND1AHIS A 10 34.623 15.037 20.775 0.71 6.78 N ANISOU 82 ND1AHIS A 10 941 667 970 281 -16 -36 N ATOM 83 CD2AHIS A 10 34.411 15.515 22.871 0.71 6.39 C ANISOU 83 CD2AHIS A 10 996 674 757 -76 -120 134 C ATOM 84 CE1AHIS A 10 34.372 16.337 20.840 0.71 5.48 C ANISOU 84 CE1AHIS A 10 815 527 740 -58 25 -16 C ATOM 85 NE2AHIS A 10 34.231 16.632 22.118 0.71 6.36 N ANISOU 85 NE2AHIS A 10 947 657 813 34 88 26 N ATOM 86 CG BHIS A 10 34.648 14.452 21.941 0.28 6.22 C ANISOU 86 CG BHIS A 10 721 754 887 -7 -69 101 C ATOM 87 ND1BHIS A 10 34.432 14.953 20.680 0.28 6.06 N ANISOU 87 ND1BHIS A 10 718 569 1014 -414 -790 -15 N ATOM 88 CD2BHIS A 10 34.491 15.522 22.770 0.28 6.64 C ANISOU 88 CD2BHIS A 10 920 761 842 -30 105 120 C ATOM 89 CE1BHIS A 10 34.175 16.248 20.727 0.28 7.29 C ANISOU 89 CE1BHIS A 10 1019 790 962 189 -326 35 C ATOM 90 NE2BHIS A 10 34.202 16.631 21.987 0.28 7.85 N ANISOU 90 NE2BHIS A 10 1175 793 1014 82 -428 8 N ATOM 91 N GLY A 11 36.845 11.962 19.853 1.00 6.23 N ANISOU 91 N GLY A 11 957 537 871 8 33 125 N ATOM 92 CA GLY A 11 37.040 12.211 18.427 1.00 6.48 C ANISOU 92 CA GLY A 11 920 649 892 59 96 35 C ATOM 93 C GLY A 11 36.068 13.264 17.892 1.00 6.17 C ANISOU 93 C GLY A 11 985 548 810 38 -42 -63 C ATOM 94 O GLY A 11 35.041 13.550 18.534 1.00 6.41 O ANISOU 94 O GLY A 11 816 687 932 28 7 39 O ATOM 95 N GLU A 12 36.386 13.895 16.772 1.00 6.44 N ANISOU 95 N GLU A 12 836 663 950 173 91 -1 N ATOM 96 CA GLU A 12 35.536 14.913 16.167 1.00 6.57 C ANISOU 96 CA GLU A 12 961 640 894 24 -60 75 C ATOM 97 C GLU A 12 34.070 14.484 16.170 1.00 6.28 C ANISOU 97 C GLU A 12 933 632 819 150 -42 83 C ATOM 98 O GLU A 12 33.713 13.399 15.730 1.00 6.51 O ANISOU 98 O GLU A 12 793 759 920 80 9 -24 O ATOM 99 CB GLU A 12 35.979 15.198 14.723 1.00 6.58 C ANISOU 99 CB GLU A 12 873 676 953 -44 -60 -48 C ATOM 100 CG GLU A 12 35.289 16.428 14.148 1.00 6.96 C ANISOU 100 CG GLU A 12 1083 723 838 38 28 48 C ATOM 101 CD GLU A 12 35.345 16.544 12.660 1.00 8.67 C ANISOU 101 CD GLU A 12 1670 727 896 -10 117 40 C ATOM 102 OE1 GLU A 12 34.870 15.622 11.954 1.00 8.59 O ANISOU 102 OE1 GLU A 12 1509 862 893 -107 -72 59 O ATOM 103 OE2 GLU A 12 35.869 17.566 12.137 1.00 11.85 O ANISOU 103 OE2 GLU A 12 2382 1265 856 -712 -93 147 O ATOM 104 N SER A 13 33.221 15.407 16.669 1.00 6.66 N ANISOU 104 N SER A 13 993 702 836 149 105 140 N ATOM 105 CA SER A 13 31.791 15.168 16.638 1.00 6.74 C ANISOU 105 CA SER A 13 949 687 925 177 112 40 C ATOM 106 C SER A 13 31.136 15.736 15.380 1.00 6.67 C ANISOU 106 C SER A 13 1107 563 865 60 34 29 C ATOM 107 O SER A 13 31.721 16.556 14.664 1.00 7.59 O ANISOU 107 O SER A 13 1290 718 877 -1 70 50 O ATOM 108 CB SER A 13 31.080 15.761 17.862 1.00 6.90 C ANISOU 108 CB SER A 13 1007 726 889 154 122 31 C ATOM 109 OG SER A 13 30.849 17.137 17.632 1.00 7.63 O ANISOU 109 OG SER A 13 1225 670 1006 169 112 -19 O ATOM 110 N GLN A 14 29.898 15.300 15.095 1.00 7.06 N ANISOU 110 N GLN A 14 1182 649 852 -4 -6 -14 N ATOM 111 CA GLN A 14 29.184 15.856 13.921 1.00 7.55 C ANISOU 111 CA GLN A 14 1184 712 971 6 -52 60 C ATOM 112 C GLN A 14 28.991 17.370 14.059 1.00 7.55 C ANISOU 112 C GLN A 14 1079 797 992 4 54 97 C ATOM 113 O GLN A 14 29.030 18.081 13.054 1.00 8.51 O ANISOU 113 O GLN A 14 1518 821 895 80 -44 176 O ATOM 114 CB GLN A 14 27.818 15.169 13.774 1.00 9.03 C ANISOU 114 CB GLN A 14 1263 785 1384 8 -195 -109 C ATOM 115 CG GLN A 14 27.110 15.367 12.449 1.00 10.58 C ANISOU 115 CG GLN A 14 1183 1235 1604 237 -317 47 C ATOM 116 CD GLN A 14 27.938 14.955 11.254 1.00 13.50 C ANISOU 116 CD GLN A 14 1532 2227 1369 164 -541 -405 C ATOM 117 OE1 GLN A 14 28.636 13.918 11.329 1.00 16.29 O ANISOU 117 OE1 GLN A 14 1654 2730 1808 601 -199 -790 O ATOM 118 NE2 GLN A 14 27.775 15.704 10.183 1.00 18.02 N ANISOU 118 NE2 GLN A 14 2037 3280 1529 -406 -335 227 N ATOM 119 N TRP A 15 28.756 17.895 15.271 1.00 7.21 N ANISOU 119 N TRP A 15 1117 644 979 142 150 83 N ATOM 120 CA TRP A 15 28.575 19.323 15.485 1.00 7.93 C ANISOU 120 CA TRP A 15 1139 744 1131 208 38 28 C ATOM 121 C TRP A 15 29.913 20.076 15.557 1.00 7.48 C ANISOU 121 C TRP A 15 1184 632 1025 181 -92 73 C ATOM 122 O TRP A 15 29.933 21.285 15.250 1.00 8.30 O ANISOU 122 O TRP A 15 1161 693 1300 201 192 244 O ATOM 123 CB TRP A 15 27.654 19.640 16.661 1.00 7.57 C ANISOU 123 CB TRP A 15 1187 776 912 304 -50 -6 C ATOM 124 CG TRP A 15 26.214 19.388 16.370 1.00 7.56 C ANISOU 124 CG TRP A 15 1189 615 1068 101 62 20 C ATOM 125 CD1 TRP A 15 25.676 18.775 15.251 1.00 8.96 C ANISOU 125 CD1 TRP A 15 1322 757 1327 49 -56 -97 C ATOM 126 CD2 TRP A 15 25.089 19.773 17.182 1.00 7.89 C ANISOU 126 CD2 TRP A 15 1103 841 1055 178 34 162 C ATOM 127 NE1 TRP A 15 24.298 18.749 15.346 1.00 9.92 N ANISOU 127 NE1 TRP A 15 1340 944 1484 84 -223 3 N ATOM 128 CE2 TRP A 15 23.918 19.370 16.529 1.00 8.93 C ANISOU 128 CE2 TRP A 15 1188 925 1280 169 -145 267 C ATOM 129 CE3 TRP A 15 24.983 20.438 18.399 1.00 8.18 C ANISOU 129 CE3 TRP A 15 1301 757 1052 373 80 187 C ATOM 130 CZ2 TRP A 15 22.656 19.582 17.060 1.00 10.66 C ANISOU 130 CZ2 TRP A 15 1147 1150 1751 41 -11 294 C ATOM 131 CZ3 TRP A 15 23.715 20.658 18.933 1.00 8.84 C ANISOU 131 CZ3 TRP A 15 1444 606 1308 359 350 205 C ATOM 132 CH2 TRP A 15 22.551 20.231 18.255 1.00 10.75 C ANISOU 132 CH2 TRP A 15 1320 1196 1570 463 130 530 C ATOM 133 N ASN A 16 31.036 19.426 15.888 1.00 6.96 N ANISOU 133 N ASN A 16 1144 529 971 91 -36 193 N ATOM 134 CA ASN A 16 32.334 20.013 15.627 1.00 7.23 C ANISOU 134 CA ASN A 16 1209 694 846 14 -10 171 C ATOM 135 C ASN A 16 32.504 20.283 14.100 1.00 7.13 C ANISOU 135 C ASN A 16 978 834 898 -69 -66 122 C ATOM 136 O ASN A 16 32.815 21.411 13.667 1.00 8.09 O ANISOU 136 O ASN A 16 1390 766 918 -44 42 163 O ATOM 137 CB ASN A 16 33.449 19.127 16.144 1.00 7.75 C ANISOU 137 CB ASN A 16 1155 831 958 38 18 170 C ATOM 138 CG ASN A 16 33.588 18.817 17.604 1.00 6.46 C ANISOU 138 CG ASN A 16 758 783 911 3 43 119 C ATOM 139 OD1 ASN A 16 34.143 17.745 17.970 1.00 7.93 O ANISOU 139 OD1 ASN A 16 1208 765 1040 150 -154 41 O ATOM 140 ND2 ASN A 16 33.160 19.713 18.485 1.00 7.51 N ANISOU 140 ND2 ASN A 16 1054 810 988 72 -18 41 N ATOM 141 N LYS A 17 32.231 19.292 13.277 1.00 7.74 N ANISOU 141 N LYS A 17 1383 667 889 98 16 124 N ATOM 142 CA LYS A 17 32.308 19.418 11.830 1.00 7.97 C ANISOU 142 CA LYS A 17 1273 827 928 189 59 33 C ATOM 143 C LYS A 17 31.386 20.525 11.339 1.00 8.59 C ANISOU 143 C LYS A 17 1549 917 798 347 112 77 C ATOM 144 O LYS A 17 31.830 21.338 10.518 1.00 9.85 O ANISOU 144 O LYS A 17 1803 1044 895 124 34 143 O ATOM 145 CB LYS A 17 31.963 18.099 11.118 1.00 8.74 C ANISOU 145 CB LYS A 17 1472 851 1000 108 -63 30 C ATOM 146 CG LYS A 17 31.889 18.244 9.611 1.00 9.54 C ANISOU 146 CG LYS A 17 1458 1161 1004 255 5 -46 C ATOM 147 CD LYS A 17 31.533 17.017 8.803 1.00 11.13 C ANISOU 147 CD LYS A 17 1607 1457 1167 237 -123 -295 C ATOM 148 CE LYS A 17 31.315 17.334 7.314 1.00 14.78 C ANISOU 148 CE LYS A 17 2504 1928 1184 737 -212 -467 C ATOM 149 NZ LYS A 17 31.113 16.156 6.446 1.00 15.58 N ANISOU 149 NZ LYS A 17 2251 2332 1335 635 -399 -737 N ATOM 150 N GLU A 18 30.142 20.568 11.848 1.00 8.57 N ANISOU 150 N GLU A 18 1462 944 849 362 29 66 N ATOM 151 CA GLU A 18 29.144 21.514 11.363 1.00 9.06 C ANISOU 151 CA GLU A 18 1490 1124 827 415 48 149 C ATOM 152 C GLU A 18 29.253 22.888 12.024 1.00 9.18 C ANISOU 152 C GLU A 18 1536 1083 870 509 175 79 C ATOM 153 O GLU A 18 28.452 23.797 11.723 1.00 12.26 O ANISOU 153 O GLU A 18 2104 1265 1287 647 -208 120 O ATOM 154 CB GLU A 18 27.729 20.946 11.526 1.00 12.36 C ANISOU 154 CB GLU A 18 1548 1514 1636 205 -308 527 C ATOM 155 CG GLU A 18 27.485 19.668 10.692 1.00 16.79 C ANISOU 155 CG GLU A 18 2586 1535 2259 -55 -1395 563 C ATOM 156 CD GLU A 18 26.080 19.119 10.942 1.00 23.67 C ANISOU 156 CD GLU A 18 2942 3064 2987 -965 -1859 878 C ATOM 157 OE1 GLU A 18 25.209 19.798 11.539 1.00 27.90 O ANISOU 157 OE1 GLU A 18 3019 4821 2760 -2117 -420 166 O ATOM 158 OE2 GLU A 18 25.767 18.006 10.516 1.00 30.34 O ANISOU 158 OE2 GLU A 18 3348 2020 6159 -723 -2759 1688 O ATOM 159 N ASN A 19 30.211 23.105 12.933 1.00 8.92 N ANISOU 159 N ASN A 19 1577 846 966 417 172 125 N ATOM 160 CA ASN A 19 30.443 24.411 13.566 1.00 8.92 C ANISOU 160 CA ASN A 19 1457 708 1223 394 118 216 C ATOM 161 C ASN A 19 29.232 24.852 14.356 1.00 8.29 C ANISOU 161 C ASN A 19 1517 633 999 299 80 79 C ATOM 162 O ASN A 19 28.771 25.992 14.240 1.00 9.67 O ANISOU 162 O ASN A 19 1711 679 1284 385 215 125 O ATOM 163 CB ASN A 19 30.880 25.439 12.515 1.00 10.14 C ANISOU 163 CB ASN A 19 1731 989 1132 128 171 158 C ATOM 164 CG ASN A 19 31.481 26.692 13.141 1.00 9.65 C ANISOU 164 CG ASN A 19 1737 887 1043 241 236 145 C ATOM 165 OD1 ASN A 19 32.096 26.596 14.206 1.00 10.41 O ANISOU 165 OD1 ASN A 19 1503 1063 1391 149 34 159 O ATOM 166 ND2 ASN A 19 31.278 27.853 12.494 1.00 11.29 N ANISOU 166 ND2 ASN A 19 2019 1019 1252 157 348 299 N ATOM 167 N ARG A 20 28.713 23.959 15.233 1.00 7.95 N ANISOU 167 N ARG A 20 1218 730 1074 275 -58 181 N ATOM 168 CA ARG A 20 27.597 24.253 16.135 1.00 8.40 C ANISOU 168 CA ARG A 20 1411 718 1064 167 49 128 C ATOM 169 C ARG A 20 28.021 24.069 17.579 1.00 7.87 C ANISOU 169 C ARG A 20 1250 617 1124 245 -43 77 C ATOM 170 O ARG A 20 28.709 23.105 17.950 1.00 8.83 O ANISOU 170 O ARG A 20 1419 778 1156 454 40 46 O ATOM 171 CB ARG A 20 26.367 23.364 15.840 1.00 9.72 C ANISOU 171 CB ARG A 20 1385 892 1416 80 -93 72 C ATOM 172 CG ARG A 20 25.724 23.540 14.484 1.00 10.60 C ANISOU 172 CG ARG A 20 1819 987 1222 -96 -56 -9 C ATOM 173 CD AARG A 20 24.622 22.565 14.126 0.50 13.19 C ANISOU 173 CD AARG A 20 2124 775 2114 71 -633 -219 C ATOM 174 NE AARG A 20 23.322 22.771 14.731 0.50 13.41 N ANISOU 174 NE AARG A 20 1636 1091 2367 -17 -889 198 N ATOM 175 CZ AARG A 20 22.152 22.192 14.575 0.50 16.50 C ANISOU 175 CZ AARG A 20 2155 1321 2795 -606 -1437 946 C ATOM 176 NH1AARG A 20 22.060 21.188 13.695 0.50 22.86 N ANISOU 176 NH1AARG A 20 3530 2501 2654 -1426 -1580 421 N ATOM 177 NH2AARG A 20 21.028 22.519 15.236 0.50 19.02 N ANISOU 177 NH2AARG A 20 1841 2766 2618 -1699 -1233 861 N ATOM 178 CD BARG A 20 24.620 22.492 14.352 0.50 15.44 C ANISOU 178 CD BARG A 20 2377 1133 2358 -378 -685 -251 C ATOM 179 NE BARG A 20 23.937 22.543 13.072 0.50 17.21 N ANISOU 179 NE BARG A 20 2624 2016 1900 -1061 -367 47 N ATOM 180 CZ BARG A 20 23.153 23.531 12.667 0.50 19.23 C ANISOU 180 CZ BARG A 20 2234 3322 1752 -446 -675 -137 C ATOM 181 NH1BARG A 20 22.926 24.592 13.435 0.50 16.37 N ANISOU 181 NH1BARG A 20 1616 3466 1138 167 -212 319 N ATOM 182 NH2BARG A 20 22.601 23.430 11.466 0.50 28.48 N ANISOU 182 NH2BARG A 20 4639 5006 1177 362 -666 -141 N ATOM 183 N PHE A 21 27.599 25.001 18.445 1.00 7.16 N ANISOU 183 N PHE A 21 1053 618 1050 228 53 207 N ATOM 184 CA PHE A 21 27.787 24.850 19.865 1.00 7.23 C ANISOU 184 CA PHE A 21 1069 557 1123 152 13 75 C ATOM 185 C PHE A 21 27.022 23.630 20.380 1.00 6.75 C ANISOU 185 C PHE A 21 1056 615 893 131 -13 104 C ATOM 186 O PHE A 21 25.830 23.493 20.100 1.00 8.07 O ANISOU 186 O PHE A 21 1104 722 1240 53 -96 240 O ATOM 187 CB PHE A 21 27.272 26.077 20.608 1.00 7.82 C ANISOU 187 CB PHE A 21 1210 626 1135 154 279 161 C ATOM 188 CG PHE A 21 27.787 27.427 20.202 1.00 9.21 C ANISOU 188 CG PHE A 21 1682 568 1250 0 268 26 C ATOM 189 CD1 PHE A 21 29.065 27.857 20.463 1.00 13.46 C ANISOU 189 CD1 PHE A 21 1997 1461 1654 -667 298 -47 C ATOM 190 CD2 PHE A 21 26.909 28.292 19.522 1.00 12.08 C ANISOU 190 CD2 PHE A 21 2505 652 1433 514 387 217 C ATOM 191 CE1 PHE A 21 29.457 29.157 20.119 1.00 16.61 C ANISOU 191 CE1 PHE A 21 2893 1567 1852 -1114 653 -281 C ATOM 192 CE2 PHE A 21 27.286 29.552 19.133 1.00 16.91 C ANISOU 192 CE2 PHE A 21 3559 940 1924 408 660 587 C ATOM 193 CZ PHE A 21 28.557 29.972 19.467 1.00 18.18 C ANISOU 193 CZ PHE A 21 3877 1262 1769 -476 1272 -4 C ATOM 194 N THR A 22 27.698 22.774 21.159 1.00 6.62 N ANISOU 194 N THR A 22 929 549 1037 -28 -73 75 N ATOM 195 CA THR A 22 27.064 21.509 21.566 1.00 6.90 C ANISOU 195 CA THR A 22 1170 471 980 39 64 129 C ATOM 196 C THR A 22 26.738 21.435 23.056 1.00 5.96 C ANISOU 196 C THR A 22 864 446 956 42 0 -19 C ATOM 197 O THR A 22 25.586 21.206 23.437 1.00 6.51 O ANISOU 197 O THR A 22 836 636 1002 -28 -69 11 O ATOM 198 CB THR A 22 27.954 20.293 21.192 1.00 6.57 C ANISOU 198 CB THR A 22 877 625 993 5 18 32 C ATOM 199 OG1 THR A 22 28.341 20.357 19.807 1.00 8.47 O ANISOU 199 OG1 THR A 22 1404 782 1032 -12 188 28 O ATOM 200 CG2 THR A 22 27.193 18.995 21.363 1.00 7.21 C ANISOU 200 CG2 THR A 22 1094 422 1222 111 -177 168 C ATOM 201 N GLY A 23 27.734 21.606 23.925 1.00 6.14 N ANISOU 201 N GLY A 23 782 588 964 -72 138 -32 N ATOM 202 CA GLY A 23 27.503 21.499 25.371 1.00 5.80 C ANISOU 202 CA GLY A 23 691 598 913 -48 67 -60 C ATOM 203 C GLY A 23 27.027 20.098 25.740 1.00 5.67 C ANISOU 203 C GLY A 23 633 564 957 85 23 73 C ATOM 204 O GLY A 23 27.623 19.091 25.334 1.00 6.33 O ANISOU 204 O GLY A 23 857 619 929 179 -48 -26 O ATOM 205 N TRP A 24 25.905 20.000 26.478 1.00 5.55 N ANISOU 205 N TRP A 24 582 515 1014 22 -37 41 N ATOM 206 CA TRP A 24 25.351 18.724 26.874 1.00 5.41 C ANISOU 206 CA TRP A 24 719 504 831 -15 -20 42 C ATOM 207 C TRP A 24 24.483 18.104 25.778 1.00 5.30 C ANISOU 207 C TRP A 24 530 540 943 25 -73 34 C ATOM 208 O TRP A 24 24.044 16.979 25.953 1.00 6.13 O ANISOU 208 O TRP A 24 840 591 900 -62 -19 15 O ATOM 209 CB TRP A 24 24.555 18.860 28.193 1.00 5.36 C ANISOU 209 CB TRP A 24 646 421 968 -65 9 -20 C ATOM 210 CG TRP A 24 25.385 19.068 29.413 1.00 5.59 C ANISOU 210 CG TRP A 24 720 518 885 27 -23 -16 C ATOM 211 CD1 TRP A 24 26.636 19.632 29.554 1.00 5.72 C ANISOU 211 CD1 TRP A 24 612 690 870 129 12 83 C ATOM 212 CD2 TRP A 24 24.995 18.692 30.750 1.00 6.05 C ANISOU 212 CD2 TRP A 24 778 608 913 -6 46 -3 C ATOM 213 NE1 TRP A 24 27.014 19.621 30.872 1.00 5.87 N ANISOU 213 NE1 TRP A 24 779 582 871 -62 -76 -5 N ATOM 214 CE2 TRP A 24 26.027 19.035 31.639 1.00 5.93 C ANISOU 214 CE2 TRP A 24 795 565 894 41 45 -28 C ATOM 215 CE3 TRP A 24 23.866 18.067 31.320 1.00 6.02 C ANISOU 215 CE3 TRP A 24 690 528 1069 94 74 -10 C ATOM 216 CZ2 TRP A 24 25.958 18.798 33.003 1.00 6.35 C ANISOU 216 CZ2 TRP A 24 771 745 895 100 57 -94 C ATOM 217 CZ3 TRP A 24 23.779 17.814 32.675 1.00 6.63 C ANISOU 217 CZ3 TRP A 24 769 650 1101 14 114 79 C ATOM 218 CH2 TRP A 24 24.853 18.186 33.512 1.00 6.69 C ANISOU 218 CH2 TRP A 24 754 830 958 176 161 -32 C ATOM 219 N TYR A 25 24.251 18.739 24.633 1.00 5.82 N ANISOU 219 N TYR A 25 744 554 915 18 -39 -32 N ATOM 220 CA TYR A 25 23.527 18.040 23.590 1.00 5.84 C ANISOU 220 CA TYR A 25 657 641 922 52 -62 -14 C ATOM 221 C TYR A 25 24.279 16.775 23.191 1.00 5.93 C ANISOU 221 C TYR A 25 809 555 888 102 -60 -56 C ATOM 222 O TYR A 25 25.516 16.824 22.968 1.00 6.54 O ANISOU 222 O TYR A 25 821 700 963 165 27 33 O ATOM 223 CB TYR A 25 23.281 18.959 22.349 1.00 7.08 C ANISOU 223 CB TYR A 25 983 572 1135 -83 -262 157 C ATOM 224 CG TYR A 25 22.551 18.197 21.275 1.00 6.29 C ANISOU 224 CG TYR A 25 809 581 998 -11 -194 142 C ATOM 225 CD1 TYR A 25 21.190 17.987 21.332 1.00 9.52 C ANISOU 225 CD1 TYR A 25 906 1510 1203 -172 -237 31 C ATOM 226 CD2 TYR A 25 23.227 17.612 20.189 1.00 8.19 C ANISOU 226 CD2 TYR A 25 1129 893 1088 277 -286 -39 C ATOM 227 CE1 TYR A 25 20.501 17.258 20.342 1.00 10.48 C ANISOU 227 CE1 TYR A 25 865 1440 1675 -151 -230 -304 C ATOM 228 CE2 TYR A 25 22.582 16.880 19.215 1.00 8.80 C ANISOU 228 CE2 TYR A 25 1223 920 1201 207 -236 -118 C ATOM 229 CZ TYR A 25 21.212 16.707 19.298 1.00 10.38 C ANISOU 229 CZ TYR A 25 1238 1403 1304 38 -364 -142 C ATOM 230 OH TYR A 25 20.515 15.985 18.360 1.00 14.71 O ANISOU 230 OH TYR A 25 1710 2054 1825 -288 -450 -657 O ATOM 231 N ASP A 26 23.572 15.649 23.065 1.00 6.24 N ANISOU 231 N ASP A 26 698 742 933 96 -69 -143 N ATOM 232 CA ASP A 26 24.257 14.354 22.973 1.00 6.27 C ANISOU 232 CA ASP A 26 856 580 945 6 -16 -85 C ATOM 233 C ASP A 26 24.507 13.907 21.526 1.00 5.61 C ANISOU 233 C ASP A 26 667 524 941 43 1 -66 C ATOM 234 O ASP A 26 24.040 12.864 21.064 1.00 7.66 O ANISOU 234 O ASP A 26 1224 728 957 -128 6 -141 O ATOM 235 CB ASP A 26 23.454 13.289 23.736 1.00 6.01 C ANISOU 235 CB ASP A 26 711 686 887 12 81 -168 C ATOM 236 CG ASP A 26 24.265 12.067 24.056 1.00 6.22 C ANISOU 236 CG ASP A 26 790 629 944 -47 -10 -45 C ATOM 237 OD1 ASP A 26 25.523 12.142 23.983 1.00 6.77 O ANISOU 237 OD1 ASP A 26 808 586 1179 -13 -6 173 O ATOM 238 OD2 ASP A 26 23.657 11.018 24.374 1.00 9.02 O ANISOU 238 OD2 ASP A 26 1042 657 1726 -69 367 -8 O ATOM 239 N VAL A 27 25.297 14.707 20.790 1.00 6.56 N ANISOU 239 N VAL A 27 810 746 937 -15 -34 32 N ATOM 240 CA VAL A 27 25.614 14.431 19.394 1.00 6.58 C ANISOU 240 CA VAL A 27 859 715 924 42 -76 40 C ATOM 241 C VAL A 27 26.638 13.307 19.246 1.00 6.49 C ANISOU 241 C VAL A 27 1017 643 807 79 -89 104 C ATOM 242 O VAL A 27 27.537 13.149 20.086 1.00 6.74 O ANISOU 242 O VAL A 27 894 798 867 160 -70 -16 O ATOM 243 CB VAL A 27 26.107 15.713 18.693 1.00 6.89 C ANISOU 243 CB VAL A 27 888 743 986 175 84 104 C ATOM 244 CG1 VAL A 27 27.488 16.115 19.148 1.00 8.43 C ANISOU 244 CG1 VAL A 27 866 874 1465 -59 226 -49 C ATOM 245 CG2 VAL A 27 26.032 15.593 17.152 1.00 10.27 C ANISOU 245 CG2 VAL A 27 2100 833 968 175 30 71 C ATOM 246 N ASP A 28 26.589 12.549 18.169 1.00 6.68 N ANISOU 246 N ASP A 28 833 807 899 99 -166 57 N ATOM 247 CA ASP A 28 27.562 11.478 17.970 1.00 7.50 C ANISOU 247 CA ASP A 28 1032 685 1133 93 181 56 C ATOM 248 C ASP A 28 28.828 11.991 17.256 1.00 6.26 C ANISOU 248 C ASP A 28 1047 499 834 79 63 -56 C ATOM 249 O ASP A 28 28.939 13.098 16.736 1.00 6.98 O ANISOU 249 O ASP A 28 906 647 1097 -14 -48 82 O ATOM 250 CB ASP A 28 26.953 10.274 17.273 1.00 9.19 C ANISOU 250 CB ASP A 28 936 847 1708 -22 166 -139 C ATOM 251 CG ASP A 28 27.464 8.925 17.785 1.00 9.34 C ANISOU 251 CG ASP A 28 1221 890 1439 40 132 -140 C ATOM 252 OD1 ASP A 28 28.578 8.804 18.326 1.00 10.76 O ANISOU 252 OD1 ASP A 28 1044 1219 1823 -79 193 605 O ATOM 253 OD2 ASP A 28 26.767 7.912 17.569 1.00 14.03 O ANISOU 253 OD2 ASP A 28 2042 919 2371 -222 -364 -42 O ATOM 254 N LEU A 29 29.814 11.077 17.253 1.00 6.42 N ANISOU 254 N LEU A 29 797 688 956 11 8 113 N ATOM 255 CA LEU A 29 31.005 11.180 16.436 1.00 5.98 C ANISOU 255 CA LEU A 29 928 487 856 -59 74 7 C ATOM 256 C LEU A 29 30.660 11.405 14.976 1.00 6.38 C ANISOU 256 C LEU A 29 754 758 913 -9 -30 36 C ATOM 257 O LEU A 29 29.708 10.800 14.469 1.00 7.22 O ANISOU 257 O LEU A 29 810 875 1057 -17 -91 83 O ATOM 258 CB LEU A 29 31.883 9.926 16.589 1.00 6.05 C ANISOU 258 CB LEU A 29 850 547 902 -43 40 -87 C ATOM 259 CG LEU A 29 32.500 9.703 17.963 1.00 6.14 C ANISOU 259 CG LEU A 29 1024 555 754 29 197 -29 C ATOM 260 CD1 LEU A 29 33.244 8.385 18.012 1.00 7.37 C ANISOU 260 CD1 LEU A 29 1025 750 1025 131 20 -4 C ATOM 261 CD2 LEU A 29 33.411 10.855 18.350 1.00 6.73 C ANISOU 261 CD2 LEU A 29 1010 787 760 -29 -65 75 C ATOM 262 N SER A 30 31.422 12.221 14.259 1.00 6.46 N ANISOU 262 N SER A 30 940 746 768 20 -92 19 N ATOM 263 CA SER A 30 31.375 12.214 12.793 1.00 6.92 C ANISOU 263 CA SER A 30 968 937 725 64 -129 87 C ATOM 264 C SER A 30 32.140 10.952 12.286 1.00 6.79 C ANISOU 264 C SER A 30 918 828 834 -144 -49 -10 C ATOM 265 O SER A 30 32.823 10.283 13.075 1.00 7.05 O ANISOU 265 O SER A 30 936 805 937 47 -44 22 O ATOM 266 CB SER A 30 32.051 13.454 12.242 1.00 7.46 C ANISOU 266 CB SER A 30 994 895 944 237 87 152 C ATOM 267 OG SER A 30 33.443 13.393 12.608 1.00 7.33 O ANISOU 267 OG SER A 30 1033 812 940 144 -47 104 O ATOM 268 N GLU A 31 32.061 10.693 11.001 1.00 8.07 N ANISOU 268 N GLU A 31 1200 1068 800 60 -59 -53 N ATOM 269 CA GLU A 31 32.876 9.649 10.383 1.00 8.53 C ANISOU 269 CA GLU A 31 1365 892 984 -29 -54 -154 C ATOM 270 C GLU A 31 34.360 9.847 10.680 1.00 7.72 C ANISOU 270 C GLU A 31 1314 846 774 94 176 -59 C ATOM 271 O GLU A 31 35.087 8.898 11.064 1.00 8.27 O ANISOU 271 O GLU A 31 1474 843 824 117 35 -61 O ATOM 272 CB GLU A 31 32.619 9.555 8.884 1.00 11.91 C ANISOU 272 CB GLU A 31 1873 1611 1042 232 -129 -344 C ATOM 273 CG GLU A 31 33.306 8.403 8.177 1.00 12.69 C ANISOU 273 CG GLU A 31 1771 1804 1248 252 93 -431 C ATOM 274 CD GLU A 31 32.756 7.994 6.846 1.00 14.41 C ANISOU 274 CD GLU A 31 2170 2122 1184 -72 101 -491 C ATOM 275 OE1 GLU A 31 31.886 8.681 6.292 1.00 22.99 O ANISOU 275 OE1 GLU A 31 2680 4292 1763 1132 -623 -1170 O ATOM 276 OE2 GLU A 31 33.236 6.972 6.320 1.00 14.43 O ANISOU 276 OE2 GLU A 31 2368 2019 1098 -348 226 -422 O ATOM 277 N LYS A 32 34.842 11.076 10.534 1.00 7.25 N ANISOU 277 N LYS A 32 1074 840 842 164 2 61 N ATOM 278 CA LYS A 32 36.245 11.397 10.867 1.00 7.77 C ANISOU 278 CA LYS A 32 1158 851 943 155 -43 -136 C ATOM 279 C LYS A 32 36.513 11.174 12.335 1.00 6.55 C ANISOU 279 C LYS A 32 904 582 1002 188 14 43 C ATOM 280 O LYS A 32 37.622 10.691 12.701 1.00 7.67 O ANISOU 280 O LYS A 32 972 899 1042 169 44 94 O ATOM 281 CB LYS A 32 36.567 12.834 10.449 1.00 9.19 C ANISOU 281 CB LYS A 32 1357 1027 1110 -45 -43 291 C ATOM 282 CG LYS A 32 37.954 13.330 10.758 1.00 15.00 C ANISOU 282 CG LYS A 32 1198 1644 2857 -154 -113 930 C ATOM 283 CD LYS A 32 38.162 14.777 10.336 1.00 24.66 C ANISOU 283 CD LYS A 32 2548 1706 5115 -1037 -426 861 C ATOM 284 CE LYS A 32 39.541 15.308 10.730 1.00 33.49 C ANISOU 284 CE LYS A 32 2892 2718 7113 -1431 -988 772 C ATOM 285 NZ LYS A 32 40.002 16.280 9.695 1.00 58.62 N ANISOU 285 NZ LYS A 32 6562 4428 11283 -3489 2852 1363 N ATOM 286 N GLY A 33 35.581 11.482 13.231 1.00 6.52 N ANISOU 286 N GLY A 33 844 694 939 58 -49 58 N ATOM 287 CA GLY A 33 35.804 11.224 14.629 1.00 6.84 C ANISOU 287 CA GLY A 33 1016 584 999 -1 34 89 C ATOM 288 C GLY A 33 35.924 9.764 15.017 1.00 5.70 C ANISOU 288 C GLY A 33 763 615 788 101 180 54 C ATOM 289 O GLY A 33 36.676 9.413 15.931 1.00 6.63 O ANISOU 289 O GLY A 33 859 807 853 94 63 136 O ATOM 290 N VAL A 34 35.151 8.899 14.336 1.00 6.56 N ANISOU 290 N VAL A 34 985 604 905 5 64 8 N ATOM 291 CA VAL A 34 35.341 7.457 14.507 1.00 6.21 C ANISOU 291 CA VAL A 34 917 649 794 74 -132 77 C ATOM 292 C VAL A 34 36.780 7.088 14.087 1.00 6.77 C ANISOU 292 C VAL A 34 863 891 817 120 -106 -80 C ATOM 293 O VAL A 34 37.451 6.368 14.827 1.00 7.14 O ANISOU 293 O VAL A 34 973 808 930 42 -56 19 O ATOM 294 CB VAL A 34 34.283 6.619 13.748 1.00 6.65 C ANISOU 294 CB VAL A 34 890 755 884 -83 4 -74 C ATOM 295 CG1 VAL A 34 34.568 5.128 13.840 1.00 8.59 C ANISOU 295 CG1 VAL A 34 1252 788 1225 16 -162 -143 C ATOM 296 CG2 VAL A 34 32.874 6.936 14.261 1.00 7.98 C ANISOU 296 CG2 VAL A 34 987 920 1125 -124 128 -133 C ATOM 297 N SER A 35 37.233 7.565 12.930 1.00 6.48 N ANISOU 297 N SER A 35 838 704 921 40 -116 -5 N ATOM 298 CA SER A 35 38.603 7.325 12.480 1.00 7.66 C ANISOU 298 CA SER A 35 1008 908 994 41 99 -192 C ATOM 299 C SER A 35 39.583 7.795 13.549 1.00 6.28 C ANISOU 299 C SER A 35 784 648 956 -8 205 34 C ATOM 300 O SER A 35 40.566 7.093 13.868 1.00 7.90 O ANISOU 300 O SER A 35 864 810 1328 82 131 15 O ATOM 301 CB SER A 35 38.874 8.019 11.146 1.00 9.28 C ANISOU 301 CB SER A 35 1125 1406 995 228 109 -52 C ATOM 302 OG SER A 35 37.995 7.525 10.114 1.00 9.96 O ANISOU 302 OG SER A 35 1310 1518 957 181 73 -102 O ATOM 303 N GLU A 36 39.390 8.991 14.115 1.00 6.84 N ANISOU 303 N GLU A 36 961 723 913 110 29 -56 N ATOM 304 CA GLU A 36 40.313 9.517 15.104 1.00 6.97 C ANISOU 304 CA GLU A 36 943 738 968 22 56 48 C ATOM 305 C GLU A 36 40.360 8.633 16.345 1.00 6.59 C ANISOU 305 C GLU A 36 984 612 909 -16 19 -25 C ATOM 306 O GLU A 36 41.422 8.363 16.949 1.00 6.97 O ANISOU 306 O GLU A 36 959 641 1048 -52 -46 60 O ATOM 307 CB AGLU A 36 39.919 10.939 15.550 0.81 7.43 C ANISOU 307 CB AGLU A 36 968 600 1257 -73 -33 44 C ATOM 308 CG AGLU A 36 40.165 12.012 14.482 0.81 7.50 C ANISOU 308 CG AGLU A 36 1036 824 988 85 -58 71 C ATOM 309 CD AGLU A 36 39.767 13.415 14.918 0.81 7.51 C ANISOU 309 CD AGLU A 36 1031 776 1046 -27 137 146 C ATOM 310 OE1AGLU A 36 39.122 13.577 15.980 0.81 7.38 O ANISOU 310 OE1AGLU A 36 953 775 1074 -98 147 19 O ATOM 311 OE2AGLU A 36 40.075 14.354 14.171 0.81 10.92 O ANISOU 311 OE2AGLU A 36 2108 826 1213 -266 545 -39 O ATOM 312 CB BGLU A 36 39.915 10.947 15.499 0.19 7.07 C ANISOU 312 CB BGLU A 36 1059 628 998 -128 57 70 C ATOM 313 CG BGLU A 36 39.873 11.907 14.319 0.19 7.91 C ANISOU 313 CG BGLU A 36 1135 915 954 262 28 157 C ATOM 314 CD BGLU A 36 39.601 13.349 14.682 0.19 10.16 C ANISOU 314 CD BGLU A 36 1393 812 1656 239 -63 240 C ATOM 315 OE1BGLU A 36 39.087 13.648 15.780 0.19 13.74 O ANISOU 315 OE1BGLU A 36 1911 1061 2250 401 281 -411 O ATOM 316 OE2BGLU A 36 39.901 14.230 13.846 0.19 13.52 O ANISOU 316 OE2BGLU A 36 1395 1115 2629 -372 -452 751 O ATOM 317 N ALA A 37 39.183 8.169 16.820 1.00 6.57 N ANISOU 317 N ALA A 37 925 643 929 125 68 63 N ATOM 318 CA ALA A 37 39.122 7.331 18.008 1.00 6.34 C ANISOU 318 CA ALA A 37 870 623 914 58 76 19 C ATOM 319 C ALA A 37 39.875 6.003 17.797 1.00 6.39 C ANISOU 319 C ALA A 37 865 594 971 55 83 106 C ATOM 320 O ALA A 37 40.642 5.571 18.643 1.00 7.46 O ANISOU 320 O ALA A 37 971 689 1174 -38 -44 102 O ATOM 321 CB ALA A 37 37.681 7.039 18.392 1.00 7.24 C ANISOU 321 CB ALA A 37 863 624 1264 66 153 36 C ATOM 322 N LYS A 38 39.633 5.364 16.650 1.00 6.88 N ANISOU 322 N LYS A 38 855 573 1185 32 -12 -94 N ATOM 323 CA LYS A 38 40.341 4.110 16.347 1.00 6.66 C ANISOU 323 CA LYS A 38 928 709 896 194 135 139 C ATOM 324 C LYS A 38 41.841 4.363 16.244 1.00 7.14 C ANISOU 324 C LYS A 38 979 643 1089 148 212 21 C ATOM 325 O LYS A 38 42.655 3.545 16.721 1.00 7.99 O ANISOU 325 O LYS A 38 775 747 1514 87 70 60 O ATOM 326 CB LYS A 38 39.771 3.490 15.077 1.00 7.11 C ANISOU 326 CB LYS A 38 1084 617 1001 104 165 12 C ATOM 327 CG LYS A 38 38.359 2.977 15.245 1.00 8.22 C ANISOU 327 CG LYS A 38 1147 839 1139 17 73 40 C ATOM 328 CD LYS A 38 37.819 2.251 14.025 1.00 10.00 C ANISOU 328 CD LYS A 38 1396 1110 1295 -130 12 -157 C ATOM 329 CE ALYS A 38 36.451 1.645 14.348 0.50 10.80 C ANISOU 329 CE ALYS A 38 1017 1119 1968 146 -63 -260 C ATOM 330 NZ ALYS A 38 35.815 1.066 13.141 0.50 20.28 N ANISOU 330 NZ ALYS A 38 1880 2434 3391 -239 -631 -1477 N ATOM 331 CE BLYS A 38 36.345 1.875 14.165 0.50 11.41 C ANISOU 331 CE BLYS A 38 1498 1150 1688 -402 -181 262 C ATOM 332 NZ BLYS A 38 36.120 0.721 15.072 0.50 12.20 N ANISOU 332 NZ BLYS A 38 2002 1216 1419 -619 -579 247 N ATOM 333 N ALA A 39 42.248 5.465 15.613 1.00 7.81 N ANISOU 333 N ALA A 39 999 822 1146 -65 62 24 N ATOM 334 CA ALA A 39 43.681 5.751 15.479 1.00 7.83 C ANISOU 334 CA ALA A 39 972 760 1245 -45 85 -67 C ATOM 335 C ALA A 39 44.316 5.938 16.858 1.00 7.47 C ANISOU 335 C ALA A 39 999 630 1210 -90 76 19 C ATOM 336 O ALA A 39 45.466 5.515 17.093 1.00 8.83 O ANISOU 336 O ALA A 39 1047 944 1362 125 60 124 O ATOM 337 CB ALA A 39 43.911 6.961 14.617 1.00 8.84 C ANISOU 337 CB ALA A 39 1332 909 1117 -119 372 -51 C ATOM 338 N ALA A 40 43.625 6.594 17.783 1.00 7.74 N ANISOU 338 N ALA A 40 959 700 1280 -29 26 -4 N ATOM 339 CA ALA A 40 44.162 6.818 19.126 1.00 7.32 C ANISOU 339 CA ALA A 40 766 781 1233 -61 -25 -5 C ATOM 340 C ALA A 40 44.403 5.494 19.840 1.00 7.75 C ANISOU 340 C ALA A 40 967 719 1258 -29 61 18 C ATOM 341 O ALA A 40 45.411 5.304 20.520 1.00 7.96 O ANISOU 341 O ALA A 40 926 715 1383 -12 86 -9 O ATOM 342 CB ALA A 40 43.235 7.719 19.946 1.00 7.57 C ANISOU 342 CB ALA A 40 721 743 1412 -28 -185 -106 C ATOM 343 N GLY A 41 43.455 4.568 19.710 1.00 7.56 N ANISOU 343 N GLY A 41 765 636 1472 151 150 5 N ATOM 344 CA GLY A 41 43.624 3.243 20.310 1.00 7.34 C ANISOU 344 CA GLY A 41 710 705 1375 42 38 126 C ATOM 345 C GLY A 41 44.767 2.460 19.695 1.00 7.51 C ANISOU 345 C GLY A 41 787 537 1530 38 0 -4 C ATOM 346 O GLY A 41 45.535 1.823 20.440 1.00 7.99 O ANISOU 346 O GLY A 41 819 588 1629 100 98 78 O ATOM 347 N LYS A 42 44.896 2.482 18.381 1.00 7.74 N ANISOU 347 N LYS A 42 749 625 1568 -50 126 85 N ATOM 348 CA LYS A 42 45.965 1.776 17.713 1.00 8.21 C ANISOU 348 CA LYS A 42 669 877 1574 -17 91 106 C ATOM 349 C LYS A 42 47.313 2.345 18.172 1.00 7.80 C ANISOU 349 C LYS A 42 691 812 1461 53 116 14 C ATOM 350 O LYS A 42 48.291 1.634 18.396 1.00 9.45 O ANISOU 350 O LYS A 42 688 957 1946 168 68 40 O ATOM 351 CB ALYS A 42 45.763 1.879 16.208 0.35 9.44 C ANISOU 351 CB ALYS A 42 593 1401 1593 359 -5 -61 C ATOM 352 CG ALYS A 42 46.791 1.100 15.400 0.35 9.76 C ANISOU 352 CG ALYS A 42 810 1312 1584 688 -114 6 C ATOM 353 CD ALYS A 42 46.396 1.059 13.932 0.35 14.42 C ANISOU 353 CD ALYS A 42 1242 2537 1699 287 -298 -681 C ATOM 354 CE ALYS A 42 47.464 0.356 13.103 0.35 20.68 C ANISOU 354 CE ALYS A 42 2502 2917 2440 585 6 -1706 C ATOM 355 NZ ALYS A 42 47.058 -0.040 11.734 0.35 28.33 N ANISOU 355 NZ ALYS A 42 3121 5278 2366 1086 -205 -1834 N ATOM 356 CB BLYS A 42 45.807 1.892 16.208 0.65 10.46 C ANISOU 356 CB BLYS A 42 803 1620 1549 135 21 -42 C ATOM 357 CG BLYS A 42 44.789 1.036 15.505 0.65 14.01 C ANISOU 357 CG BLYS A 42 1431 2182 1712 -420 24 -172 C ATOM 358 CD BLYS A 42 44.770 1.264 14.004 0.65 20.61 C ANISOU 358 CD BLYS A 42 2709 3530 1591 -612 -106 -456 C ATOM 359 CE BLYS A 42 43.563 0.592 13.367 0.65 22.39 C ANISOU 359 CE BLYS A 42 2935 3847 1724 -977 -574 532 C ATOM 360 NZ BLYS A 42 42.307 1.280 13.718 0.65 26.73 N ANISOU 360 NZ BLYS A 42 2799 3414 3946 -906 -597 968 N ATOM 361 N LEU A 43 47.420 3.663 18.297 1.00 7.73 N ANISOU 361 N LEU A 43 821 848 1269 -33 192 33 N ATOM 362 CA LEU A 43 48.662 4.339 18.704 1.00 8.45 C ANISOU 362 CA LEU A 43 984 842 1385 -172 227 121 C ATOM 363 C LEU A 43 49.010 3.976 20.156 1.00 7.68 C ANISOU 363 C LEU A 43 714 800 1404 -14 141 56 C ATOM 364 O LEU A 43 50.142 3.704 20.490 1.00 9.47 O ANISOU 364 O LEU A 43 714 1039 1844 31 95 19 O ATOM 365 CB LEU A 43 48.491 5.835 18.571 1.00 8.59 C ANISOU 365 CB LEU A 43 982 798 1486 -103 198 143 C ATOM 366 CG LEU A 43 49.675 6.707 18.951 1.00 9.90 C ANISOU 366 CG LEU A 43 1404 987 1371 -372 137 219 C ATOM 367 CD1 LEU A 43 50.948 6.387 18.140 1.00 13.17 C ANISOU 367 CD1 LEU A 43 1119 1710 2173 -359 253 470 C ATOM 368 CD2 LEU A 43 49.306 8.201 18.826 1.00 10.93 C ANISOU 368 CD2 LEU A 43 1672 841 1640 -520 -174 481 C ATOM 369 N LEU A 44 48.021 3.975 21.051 1.00 7.54 N ANISOU 369 N LEU A 44 649 871 1343 -201 57 194 N ATOM 370 CA LEU A 44 48.250 3.602 22.440 1.00 8.04 C ANISOU 370 CA LEU A 44 1008 684 1364 19 184 132 C ATOM 371 C LEU A 44 48.792 2.165 22.488 1.00 7.88 C ANISOU 371 C LEU A 44 738 834 1423 16 106 41 C ATOM 372 O LEU A 44 49.740 1.888 23.250 1.00 8.75 O ANISOU 372 O LEU A 44 757 1138 1431 139 96 131 O ATOM 373 CB LEU A 44 47.001 3.755 23.283 1.00 6.95 C ANISOU 373 CB LEU A 44 818 560 1262 -26 58 103 C ATOM 374 CG LEU A 44 46.643 5.178 23.679 1.00 7.27 C ANISOU 374 CG LEU A 44 898 649 1217 116 88 159 C ATOM 375 CD1 LEU A 44 45.201 5.321 24.116 1.00 8.88 C ANISOU 375 CD1 LEU A 44 890 900 1583 95 115 -29 C ATOM 376 CD2 LEU A 44 47.571 5.675 24.794 1.00 8.62 C ANISOU 376 CD2 LEU A 44 1080 846 1351 87 -11 -63 C ATOM 377 N LYS A 45 48.217 1.258 21.702 1.00 8.37 N ANISOU 377 N LYS A 45 952 666 1560 -57 88 66 N ATOM 378 CA LYS A 45 48.735 -0.115 21.667 1.00 9.46 C ANISOU 378 CA LYS A 45 811 766 2019 41 84 -69 C ATOM 379 C LYS A 45 50.185 -0.133 21.200 1.00 10.35 C ANISOU 379 C LYS A 45 779 1209 1946 87 -16 93 C ATOM 380 O LYS A 45 51.080 -0.760 21.809 1.00 11.93 O ANISOU 380 O LYS A 45 987 1249 2296 405 86 118 O ATOM 381 CB ALYS A 45 47.885 -0.975 20.745 0.35 12.59 C ANISOU 381 CB ALYS A 45 1186 827 2770 -378 -35 -185 C ATOM 382 CG ALYS A 45 48.272 -2.452 20.733 0.35 16.38 C ANISOU 382 CG ALYS A 45 1840 1000 3384 42 -134 -637 C ATOM 383 CD ALYS A 45 48.978 -2.873 19.456 0.35 20.97 C ANISOU 383 CD ALYS A 45 2669 1450 3849 235 589 -443 C ATOM 384 CE ALYS A 45 50.469 -3.036 19.667 0.35 24.94 C ANISOU 384 CE ALYS A 45 2543 2079 4854 293 1020 -87 C ATOM 385 NZ ALYS A 45 51.268 -2.951 18.418 0.35 27.93 N ANISOU 385 NZ ALYS A 45 3288 2676 4647 -339 1387 -2937 N ATOM 386 CB BLYS A 45 47.882 -0.961 20.732 0.65 9.81 C ANISOU 386 CB BLYS A 45 902 556 2270 61 -134 82 C ATOM 387 CG BLYS A 45 48.382 -2.396 20.601 0.65 13.40 C ANISOU 387 CG BLYS A 45 1477 668 2946 199 53 -298 C ATOM 388 CD BLYS A 45 47.644 -3.254 19.585 0.65 17.38 C ANISOU 388 CD BLYS A 45 1626 952 4026 -506 -4 -638 C ATOM 389 CE BLYS A 45 48.180 -4.678 19.736 0.65 23.24 C ANISOU 389 CE BLYS A 45 1533 1308 5987 162 -612 -1568 C ATOM 390 NZ BLYS A 45 49.590 -4.908 19.312 0.65 38.12 N ANISOU 390 NZ BLYS A 45 2495 2808 9179 674 1483 196 N ATOM 391 N GLU A 46 50.472 0.531 20.085 1.00 11.00 N ANISOU 391 N GLU A 46 1034 1121 2024 314 289 13 N ATOM 392 CA GLU A 46 51.811 0.575 19.552 1.00 11.98 C ANISOU 392 CA GLU A 46 1019 1660 1873 514 291 -106 C ATOM 393 C GLU A 46 52.843 1.139 20.541 1.00 12.00 C ANISOU 393 C GLU A 46 976 1776 1808 330 295 271 C ATOM 394 O GLU A 46 54.018 0.700 20.546 1.00 13.60 O ANISOU 394 O GLU A 46 946 1871 2352 310 201 151 O ATOM 395 CB GLU A 46 51.807 1.401 18.236 1.00 15.59 C ANISOU 395 CB GLU A 46 1428 2792 1704 528 477 190 C ATOM 396 CG GLU A 46 51.212 0.549 17.082 1.00 20.33 C ANISOU 396 CG GLU A 46 1911 3982 1830 -34 431 5 C ATOM 397 CD GLU A 46 50.835 1.410 15.886 1.00 20.30 C ANISOU 397 CD GLU A 46 1934 3935 1845 905 175 -431 C ATOM 398 OE1 GLU A 46 50.942 2.680 16.014 1.00 27.73 O ANISOU 398 OE1 GLU A 46 2044 3685 4806 1318 -64 23 O ATOM 399 OE2 GLU A 46 50.419 0.775 14.914 1.00 30.67 O ANISOU 399 OE2 GLU A 46 3546 6501 1607 554 239 -1300 O ATOM 400 N GLU A 47 52.422 2.089 21.340 1.00 11.01 N ANISOU 400 N GLU A 47 843 1540 1801 -17 330 153 N ATOM 401 CA GLU A 47 53.281 2.747 22.333 1.00 12.20 C ANISOU 401 CA GLU A 47 706 1915 2015 -158 179 243 C ATOM 402 C GLU A 47 53.336 2.033 23.670 1.00 11.71 C ANISOU 402 C GLU A 47 657 1830 1963 -47 199 199 C ATOM 403 O GLU A 47 53.970 2.504 24.634 1.00 13.53 O ANISOU 403 O GLU A 47 1054 2049 2036 -18 30 169 O ATOM 404 CB GLU A 47 52.811 4.214 22.475 1.00 13.72 C ANISOU 404 CB GLU A 47 1663 1626 1925 -431 139 225 C ATOM 405 CG GLU A 47 53.026 4.996 21.181 1.00 15.20 C ANISOU 405 CG GLU A 47 1839 1997 1939 -662 36 347 C ATOM 406 CD GLU A 47 54.298 5.811 21.142 1.00 20.36 C ANISOU 406 CD GLU A 47 2228 3024 2485 -1341 447 233 C ATOM 407 OE1 GLU A 47 55.127 5.691 22.066 1.00 30.85 O ANISOU 407 OE1 GLU A 47 2897 3933 4891 -1978 -1188 934 O ATOM 408 OE2 GLU A 47 54.453 6.552 20.165 1.00 25.64 O ANISOU 408 OE2 GLU A 47 3553 2978 3209 -1177 1181 560 O ATOM 409 N GLY A 48 52.696 0.873 23.802 1.00 11.74 N ANISOU 409 N GLY A 48 942 1608 1909 204 143 160 N ATOM 410 CA GLY A 48 52.815 -0.018 24.928 1.00 12.24 C ANISOU 410 CA GLY A 48 1056 1594 1999 244 72 219 C ATOM 411 C GLY A 48 51.875 0.252 26.082 1.00 11.90 C ANISOU 411 C GLY A 48 1146 1523 1854 293 -3 206 C ATOM 412 O GLY A 48 52.112 -0.240 27.202 1.00 16.19 O ANISOU 412 O GLY A 48 1342 2677 2131 874 152 783 O ATOM 413 N TYR A 49 50.808 1.001 25.866 1.00 9.87 N ANISOU 413 N TYR A 49 857 1227 1665 10 81 391 N ATOM 414 CA TYR A 49 49.845 1.348 26.909 1.00 9.01 C ANISOU 414 CA TYR A 49 925 1283 1214 -118 -78 230 C ATOM 415 C TYR A 49 48.711 0.342 27.016 1.00 9.13 C ANISOU 415 C TYR A 49 834 1381 1253 -134 82 0 C ATOM 416 O TYR A 49 48.094 0.023 26.017 1.00 13.66 O ANISOU 416 O TYR A 49 1357 2347 1486 -737 -74 35 O ATOM 417 CB TYR A 49 49.275 2.777 26.646 1.00 10.38 C ANISOU 417 CB TYR A 49 921 1341 1683 21 56 169 C ATOM 418 CG TYR A 49 50.272 3.899 26.925 1.00 10.45 C ANISOU 418 CG TYR A 49 883 1305 1783 -59 44 217 C ATOM 419 CD1 TYR A 49 51.208 4.249 25.927 1.00 10.86 C ANISOU 419 CD1 TYR A 49 1341 1032 1754 -19 16 592 C ATOM 420 CD2 TYR A 49 50.361 4.579 28.112 1.00 11.47 C ANISOU 420 CD2 TYR A 49 1070 1222 2066 78 132 20 C ATOM 421 CE1 TYR A 49 52.149 5.246 26.139 1.00 11.06 C ANISOU 421 CE1 TYR A 49 1309 850 2044 40 368 380 C ATOM 422 CE2 TYR A 49 51.290 5.572 28.354 1.00 12.08 C ANISOU 422 CE2 TYR A 49 1310 1208 2072 -43 237 -27 C ATOM 423 CZ TYR A 49 52.173 5.909 27.351 1.00 11.51 C ANISOU 423 CZ TYR A 49 1405 702 2265 102 331 185 C ATOM 424 OH TYR A 49 53.096 6.884 27.629 1.00 13.63 O ANISOU 424 OH TYR A 49 1541 886 2750 -51 428 -42 O ATOM 425 N SER A 50 48.390 -0.103 28.213 1.00 8.53 N ANISOU 425 N SER A 50 746 1182 1313 -112 40 -8 N ATOM 426 CA SER A 50 47.128 -0.772 28.530 1.00 8.80 C ANISOU 426 CA SER A 50 955 990 1398 -108 211 7 C ATOM 427 C SER A 50 46.655 -0.238 29.857 1.00 7.97 C ANISOU 427 C SER A 50 782 853 1393 -60 50 10 C ATOM 428 O SER A 50 47.373 0.466 30.586 1.00 8.59 O ANISOU 428 O SER A 50 935 778 1552 -33 -34 -64 O ATOM 429 CB SER A 50 47.222 -2.307 28.518 1.00 11.64 C ANISOU 429 CB SER A 50 1496 1039 1889 0 491 -65 C ATOM 430 OG SER A 50 48.050 -2.761 29.501 1.00 15.33 O ANISOU 430 OG SER A 50 2302 945 2577 151 -165 219 O ATOM 431 N PHE A 51 45.412 -0.567 30.216 1.00 7.50 N ANISOU 431 N PHE A 51 804 809 1237 -10 55 62 N ATOM 432 CA PHE A 51 44.748 0.042 31.364 1.00 7.05 C ANISOU 432 CA PHE A 51 843 619 1216 109 -20 1 C ATOM 433 C PHE A 51 44.137 -1.004 32.315 1.00 6.13 C ANISOU 433 C PHE A 51 516 717 1097 -2 -175 -7 C ATOM 434 O PHE A 51 43.974 -2.186 31.961 1.00 6.95 O ANISOU 434 O PHE A 51 808 654 1178 44 -209 -52 O ATOM 435 CB PHE A 51 43.657 1.011 30.878 1.00 7.11 C ANISOU 435 CB PHE A 51 698 736 1266 -14 -126 86 C ATOM 436 CG PHE A 51 44.306 2.070 29.957 1.00 8.28 C ANISOU 436 CG PHE A 51 1148 634 1362 -78 -134 129 C ATOM 437 CD1 PHE A 51 45.022 3.108 30.517 1.00 7.17 C ANISOU 437 CD1 PHE A 51 842 638 1245 38 -197 135 C ATOM 438 CD2 PHE A 51 44.205 1.987 28.580 1.00 8.96 C ANISOU 438 CD2 PHE A 51 1423 676 1307 -121 -88 0 C ATOM 439 CE1 PHE A 51 45.686 4.033 29.716 1.00 8.23 C ANISOU 439 CE1 PHE A 51 1098 683 1344 2 92 96 C ATOM 440 CE2 PHE A 51 44.855 2.887 27.771 1.00 10.67 C ANISOU 440 CE2 PHE A 51 1880 904 1270 -327 124 -59 C ATOM 441 CZ PHE A 51 45.569 3.950 28.343 1.00 9.54 C ANISOU 441 CZ PHE A 51 1406 844 1372 -175 219 -10 C ATOM 442 N ASP A 52 43.786 -0.508 33.510 1.00 6.88 N ANISOU 442 N ASP A 52 879 584 1153 -86 -80 9 N ATOM 443 CA ASP A 52 43.015 -1.261 34.489 1.00 6.49 C ANISOU 443 CA ASP A 52 729 632 1104 -10 -122 141 C ATOM 444 C ASP A 52 41.601 -0.717 34.692 1.00 6.44 C ANISOU 444 C ASP A 52 711 581 1154 11 -277 101 C ATOM 445 O ASP A 52 40.712 -1.443 35.198 1.00 7.37 O ANISOU 445 O ASP A 52 827 678 1294 -13 -51 105 O ATOM 446 CB ASP A 52 43.716 -1.293 35.853 1.00 8.61 C ANISOU 446 CB ASP A 52 1139 886 1248 247 -439 56 C ATOM 447 CG ASP A 52 45.119 -1.874 35.702 1.00 8.78 C ANISOU 447 CG ASP A 52 1052 1041 1245 181 -408 165 C ATOM 448 OD1 ASP A 52 45.242 -3.045 35.218 1.00 11.05 O ANISOU 448 OD1 ASP A 52 1118 856 2224 263 -580 83 O ATOM 449 OD2 ASP A 52 46.103 -1.170 36.007 1.00 10.58 O ANISOU 449 OD2 ASP A 52 1209 1077 1733 128 -545 64 O ATOM 450 N PHE A 53 41.312 0.524 34.378 1.00 5.89 N ANISOU 450 N PHE A 53 672 611 954 30 -65 101 N ATOM 451 CA PHE A 53 40.013 1.151 34.647 1.00 5.68 C ANISOU 451 CA PHE A 53 720 576 862 43 -106 75 C ATOM 452 C PHE A 53 39.831 2.342 33.719 1.00 5.13 C ANISOU 452 C PHE A 53 594 479 875 125 -33 -29 C ATOM 453 O PHE A 53 40.825 3.072 33.466 1.00 6.88 O ANISOU 453 O PHE A 53 734 739 1142 -135 -205 200 O ATOM 454 CB PHE A 53 39.916 1.597 36.118 1.00 6.91 C ANISOU 454 CB PHE A 53 1005 765 856 -40 3 28 C ATOM 455 CG PHE A 53 38.508 1.817 36.621 1.00 6.66 C ANISOU 455 CG PHE A 53 1023 697 809 -53 -35 -178 C ATOM 456 CD1 PHE A 53 37.844 3.041 36.427 1.00 7.44 C ANISOU 456 CD1 PHE A 53 1042 873 912 24 -114 -134 C ATOM 457 CD2 PHE A 53 37.835 0.809 37.276 1.00 7.78 C ANISOU 457 CD2 PHE A 53 1013 853 1091 -178 119 -212 C ATOM 458 CE1 PHE A 53 36.572 3.228 36.857 1.00 7.96 C ANISOU 458 CE1 PHE A 53 1192 982 851 79 9 -256 C ATOM 459 CE2 PHE A 53 36.527 0.982 37.729 1.00 7.57 C ANISOU 459 CE2 PHE A 53 867 989 1020 -270 -91 -231 C ATOM 460 CZ PHE A 53 35.918 2.206 37.513 1.00 8.63 C ANISOU 460 CZ PHE A 53 974 1126 1180 -81 24 -237 C ATOM 461 N ALA A 54 38.602 2.597 33.264 1.00 5.17 N ANISOU 461 N ALA A 54 639 576 749 30 -160 52 N ATOM 462 CA ALA A 54 38.296 3.783 32.448 1.00 5.28 C ANISOU 462 CA ALA A 54 620 494 893 51 -80 80 C ATOM 463 C ALA A 54 37.184 4.640 33.056 1.00 4.78 C ANISOU 463 C ALA A 54 507 532 778 -48 -76 142 C ATOM 464 O ALA A 54 36.173 4.110 33.520 1.00 6.18 O ANISOU 464 O ALA A 54 619 626 1105 -30 55 79 O ATOM 465 CB ALA A 54 37.877 3.378 31.052 1.00 5.63 C ANISOU 465 CB ALA A 54 728 601 810 37 -138 134 C ATOM 466 N TYR A 55 37.348 5.966 32.972 1.00 5.20 N ANISOU 466 N TYR A 55 573 476 928 10 -78 66 N ATOM 467 CA TYR A 55 36.316 6.936 33.246 1.00 5.24 C ANISOU 467 CA TYR A 55 583 530 880 28 0 108 C ATOM 468 C TYR A 55 35.894 7.658 31.976 1.00 5.21 C ANISOU 468 C TYR A 55 673 435 874 1 -55 0 C ATOM 469 O TYR A 55 36.741 8.031 31.121 1.00 6.30 O ANISOU 469 O TYR A 55 680 803 911 6 1 201 O ATOM 470 CB TYR A 55 36.766 8.020 34.257 1.00 5.92 C ANISOU 470 CB TYR A 55 770 463 1016 -71 -148 1 C ATOM 471 CG TYR A 55 37.006 7.440 35.646 1.00 5.91 C ANISOU 471 CG TYR A 55 873 441 933 107 12 -64 C ATOM 472 CD1 TYR A 55 35.951 7.310 36.541 1.00 6.27 C ANISOU 472 CD1 TYR A 55 822 669 890 123 -90 -138 C ATOM 473 CD2 TYR A 55 38.251 6.957 36.040 1.00 6.23 C ANISOU 473 CD2 TYR A 55 849 609 910 117 -61 -89 C ATOM 474 CE1 TYR A 55 36.131 6.746 37.808 1.00 6.68 C ANISOU 474 CE1 TYR A 55 1112 640 784 -68 -120 -75 C ATOM 475 CE2 TYR A 55 38.453 6.417 37.285 1.00 7.57 C ANISOU 475 CE2 TYR A 55 1047 898 930 59 -229 -177 C ATOM 476 CZ TYR A 55 37.394 6.304 38.192 1.00 7.24 C ANISOU 476 CZ TYR A 55 1283 736 731 29 -186 -61 C ATOM 477 OH TYR A 55 37.629 5.709 39.411 1.00 8.30 O ANISOU 477 OH TYR A 55 1239 1041 873 -6 -222 20 O ATOM 478 N THR A 56 34.609 7.968 31.834 1.00 5.25 N ANISOU 478 N THR A 56 637 536 823 -57 -37 126 N ATOM 479 CA THR A 56 34.104 8.786 30.756 1.00 5.14 C ANISOU 479 CA THR A 56 553 563 837 -4 -44 76 C ATOM 480 C THR A 56 32.866 9.545 31.233 1.00 5.24 C ANISOU 480 C THR A 56 567 547 877 -38 39 60 C ATOM 481 O THR A 56 32.463 9.449 32.395 1.00 5.92 O ANISOU 481 O THR A 56 747 629 871 19 31 62 O ATOM 482 CB THR A 56 33.877 7.907 29.501 1.00 6.03 C ANISOU 482 CB THR A 56 990 509 793 21 -47 36 C ATOM 483 OG1 THR A 56 33.588 8.724 28.351 1.00 6.38 O ANISOU 483 OG1 THR A 56 989 618 819 113 -33 20 O ATOM 484 CG2 THR A 56 32.718 6.927 29.613 1.00 6.19 C ANISOU 484 CG2 THR A 56 847 496 1007 105 -31 -85 C ATOM 485 N SER A 57 32.281 10.366 30.348 1.00 5.22 N ANISOU 485 N SER A 57 581 594 807 86 22 6 N ATOM 486 CA SER A 57 31.083 11.113 30.640 1.00 5.13 C ANISOU 486 CA SER A 57 635 464 849 53 119 -5 C ATOM 487 C SER A 57 29.836 10.276 30.342 1.00 5.27 C ANISOU 487 C SER A 57 627 469 905 63 -19 117 C ATOM 488 O SER A 57 29.929 9.075 30.112 1.00 6.14 O ANISOU 488 O SER A 57 754 455 1123 42 -40 90 O ATOM 489 CB SER A 57 31.093 12.416 29.839 1.00 5.27 C ANISOU 489 CB SER A 57 569 467 968 25 -103 -10 C ATOM 490 OG SER A 57 30.849 12.090 28.461 1.00 5.73 O ANISOU 490 OG SER A 57 883 476 820 -7 -141 -6 O ATOM 491 N VAL A 58 28.665 10.919 30.327 1.00 5.12 N ANISOU 491 N VAL A 58 612 430 905 -32 76 -72 N ATOM 492 CA VAL A 58 27.435 10.284 29.866 1.00 5.22 C ANISOU 492 CA VAL A 58 640 500 843 -1 5 25 C ATOM 493 C VAL A 58 27.045 10.712 28.458 1.00 5.56 C ANISOU 493 C VAL A 58 705 587 822 -85 -39 95 C ATOM 494 O VAL A 58 25.930 10.452 27.978 1.00 7.44 O ANISOU 494 O VAL A 58 668 1009 1148 -119 -150 297 O ATOM 495 CB VAL A 58 26.258 10.443 30.865 1.00 5.64 C ANISOU 495 CB VAL A 58 576 730 836 -94 27 -103 C ATOM 496 CG1 VAL A 58 26.570 9.715 32.152 1.00 7.39 C ANISOU 496 CG1 VAL A 58 1052 940 815 -237 59 -16 C ATOM 497 CG2 VAL A 58 25.881 11.894 31.119 1.00 7.80 C ANISOU 497 CG2 VAL A 58 719 781 1464 -83 226 -323 C ATOM 498 N LEU A 59 27.986 11.358 27.724 1.00 5.17 N ANISOU 498 N LEU A 59 634 613 716 -49 -123 29 N ATOM 499 CA LEU A 59 27.747 11.829 26.360 1.00 4.82 C ANISOU 499 CA LEU A 59 550 501 782 47 -20 39 C ATOM 500 C LEU A 59 28.395 10.880 25.369 1.00 5.55 C ANISOU 500 C LEU A 59 876 513 719 178 -68 -3 C ATOM 501 O LEU A 59 29.594 10.496 25.468 1.00 5.59 O ANISOU 501 O LEU A 59 674 478 971 59 18 76 O ATOM 502 CB LEU A 59 28.244 13.255 26.248 1.00 5.72 C ANISOU 502 CB LEU A 59 869 486 819 -27 -70 14 C ATOM 503 CG LEU A 59 27.634 14.250 27.235 1.00 5.92 C ANISOU 503 CG LEU A 59 864 561 824 129 -51 -7 C ATOM 504 CD1 LEU A 59 28.313 15.593 27.148 1.00 6.85 C ANISOU 504 CD1 LEU A 59 1027 531 1045 88 -162 -79 C ATOM 505 CD2 LEU A 59 26.126 14.398 27.060 1.00 8.96 C ANISOU 505 CD2 LEU A 59 825 1215 1365 51 36 -172 C ATOM 506 N LYS A 60 27.636 10.437 24.367 1.00 5.27 N ANISOU 506 N LYS A 60 704 443 855 53 -70 29 N ATOM 507 CA LYS A 60 28.036 9.390 23.456 1.00 5.11 C ANISOU 507 CA LYS A 60 938 192 811 26 -49 105 C ATOM 508 C LYS A 60 29.266 9.733 22.646 1.00 5.22 C ANISOU 508 C LYS A 60 978 376 629 56 -40 -32 C ATOM 509 O LYS A 60 30.003 8.823 22.239 1.00 6.16 O ANISOU 509 O LYS A 60 934 595 812 65 -91 -23 O ATOM 510 CB LYS A 60 26.866 8.909 22.540 1.00 6.66 C ANISOU 510 CB LYS A 60 968 717 845 11 -72 18 C ATOM 511 CG LYS A 60 26.428 9.915 21.494 1.00 6.91 C ANISOU 511 CG LYS A 60 826 928 871 117 -107 138 C ATOM 512 CD LYS A 60 25.281 9.420 20.596 1.00 8.12 C ANISOU 512 CD LYS A 60 1055 1082 947 -188 -198 -30 C ATOM 513 CE LYS A 60 23.970 9.393 21.350 1.00 8.41 C ANISOU 513 CE LYS A 60 1025 954 1217 -270 -181 52 C ATOM 514 NZ LYS A 60 22.826 8.996 20.532 1.00 14.25 N ANISOU 514 NZ LYS A 60 1046 2647 1720 -420 -206 -632 N ATOM 515 N ARG A 61 29.551 10.981 22.344 1.00 5.25 N ANISOU 515 N ARG A 61 675 515 803 1 -29 51 N ATOM 516 CA ARG A 61 30.758 11.263 21.582 1.00 5.48 C ANISOU 516 CA ARG A 61 756 572 755 43 -1 -59 C ATOM 517 C ARG A 61 31.995 10.787 22.394 1.00 5.23 C ANISOU 517 C ARG A 61 675 524 789 -15 81 151 C ATOM 518 O ARG A 61 32.971 10.312 21.778 1.00 5.94 O ANISOU 518 O ARG A 61 722 744 791 43 47 36 O ATOM 519 CB ARG A 61 30.837 12.729 21.152 1.00 5.48 C ANISOU 519 CB ARG A 61 690 620 770 44 -21 127 C ATOM 520 CG ARG A 61 30.909 13.800 22.271 1.00 5.48 C ANISOU 520 CG ARG A 61 672 567 845 112 84 78 C ATOM 521 CD ARG A 61 30.639 15.157 21.786 1.00 5.64 C ANISOU 521 CD ARG A 61 584 621 937 45 -33 46 C ATOM 522 NE ARG A 61 30.567 16.274 22.626 1.00 6.03 N ANISOU 522 NE ARG A 61 769 652 869 47 -26 -81 N ATOM 523 CZ ARG A 61 29.523 16.870 23.167 1.00 5.97 C ANISOU 523 CZ ARG A 61 757 821 692 70 3 -26 C ATOM 524 NH1 ARG A 61 28.385 16.219 23.232 1.00 5.86 N ANISOU 524 NH1 ARG A 61 808 530 890 147 107 -14 N ATOM 525 NH2 ARG A 61 29.675 18.069 23.692 1.00 6.25 N ANISOU 525 NH2 ARG A 61 517 823 1037 43 39 -180 N ATOM 526 N ALA A 62 31.980 10.963 23.721 1.00 5.46 N ANISOU 526 N ALA A 62 713 571 791 123 -41 -60 N ATOM 527 CA ALA A 62 33.068 10.496 24.579 1.00 5.18 C ANISOU 527 CA ALA A 62 622 479 867 20 0 -5 C ATOM 528 C ALA A 62 32.994 8.970 24.799 1.00 4.98 C ANISOU 528 C ALA A 62 617 508 769 16 -118 -35 C ATOM 529 O ALA A 62 34.012 8.290 24.675 1.00 5.64 O ANISOU 529 O ALA A 62 741 519 883 85 61 -12 O ATOM 530 CB ALA A 62 33.085 11.244 25.899 1.00 6.15 C ANISOU 530 CB ALA A 62 813 618 906 -37 -149 -59 C ATOM 531 N ILE A 63 31.804 8.431 25.092 1.00 5.27 N ANISOU 531 N ILE A 63 684 424 895 20 -10 -16 N ATOM 532 CA ILE A 63 31.636 7.016 25.359 1.00 5.24 C ANISOU 532 CA ILE A 63 692 421 878 67 -11 46 C ATOM 533 C ILE A 63 32.082 6.217 24.113 1.00 5.48 C ANISOU 533 C ILE A 63 856 398 827 41 23 54 C ATOM 534 O ILE A 63 32.822 5.227 24.219 1.00 5.29 O ANISOU 534 O ILE A 63 671 498 842 10 41 51 O ATOM 535 CB ILE A 63 30.194 6.675 25.731 1.00 5.50 C ANISOU 535 CB ILE A 63 841 424 827 -25 52 73 C ATOM 536 CG1 ILE A 63 29.771 7.364 27.033 1.00 6.20 C ANISOU 536 CG1 ILE A 63 878 585 892 5 77 -65 C ATOM 537 CG2 ILE A 63 29.995 5.153 25.832 1.00 6.29 C ANISOU 537 CG2 ILE A 63 847 414 1128 -54 171 20 C ATOM 538 CD1 ILE A 63 28.254 7.435 27.184 1.00 6.63 C ANISOU 538 CD1 ILE A 63 862 846 810 -103 176 38 C ATOM 539 N HIS A 64 31.627 6.627 22.927 1.00 5.26 N ANISOU 539 N HIS A 64 606 541 852 47 0 27 N ATOM 540 CA HIS A 64 32.005 5.925 21.698 1.00 5.46 C ANISOU 540 CA HIS A 64 757 429 887 36 -60 -11 C ATOM 541 C HIS A 64 33.489 6.044 21.367 1.00 5.45 C ANISOU 541 C HIS A 64 747 468 856 50 58 129 C ATOM 542 O HIS A 64 34.104 5.117 20.801 1.00 5.93 O ANISOU 542 O HIS A 64 881 529 845 26 119 -75 O ATOM 543 CB HIS A 64 31.147 6.419 20.524 1.00 5.71 C ANISOU 543 CB HIS A 64 786 492 892 11 -84 0 C ATOM 544 CG HIS A 64 29.717 5.994 20.634 1.00 5.74 C ANISOU 544 CG HIS A 64 773 581 825 13 -79 27 C ATOM 545 ND1 HIS A 64 28.723 6.562 19.871 1.00 6.91 N ANISOU 545 ND1 HIS A 64 730 920 976 -7 -121 91 N ATOM 546 CD2 HIS A 64 29.120 5.016 21.364 1.00 6.60 C ANISOU 546 CD2 HIS A 64 888 596 1025 -100 -110 33 C ATOM 547 CE1 HIS A 64 27.569 5.948 20.128 1.00 6.61 C ANISOU 547 CE1 HIS A 64 715 777 1021 -3 -47 -128 C ATOM 548 NE2 HIS A 64 27.807 5.024 21.042 1.00 7.13 N ANISOU 548 NE2 HIS A 64 860 784 1065 -128 -111 -64 N ATOM 549 N THR A 65 34.087 7.197 21.752 1.00 5.35 N ANISOU 549 N THR A 65 752 448 832 48 -27 5 N ATOM 550 CA THR A 65 35.553 7.272 21.618 1.00 5.34 C ANISOU 550 CA THR A 65 745 475 810 -30 52 2 C ATOM 551 C THR A 65 36.213 6.202 22.491 1.00 5.44 C ANISOU 551 C THR A 65 674 542 852 -17 10 4 C ATOM 552 O THR A 65 37.097 5.476 22.010 1.00 6.27 O ANISOU 552 O THR A 65 788 549 1045 37 147 81 O ATOM 553 CB THR A 65 36.058 8.655 21.994 1.00 5.12 C ANISOU 553 CB THR A 65 762 488 696 23 17 -33 C ATOM 554 OG1 THR A 65 35.565 9.638 21.042 1.00 6.47 O ANISOU 554 OG1 THR A 65 859 702 898 105 26 108 O ATOM 555 CG2 THR A 65 37.571 8.772 21.923 1.00 6.13 C ANISOU 555 CG2 THR A 65 771 666 891 -149 -70 82 C ATOM 556 N LEU A 66 35.793 6.086 23.742 1.00 5.25 N ANISOU 556 N LEU A 66 728 458 809 19 57 -27 N ATOM 557 CA LEU A 66 36.319 5.060 24.629 1.00 5.27 C ANISOU 557 CA LEU A 66 669 459 873 62 114 34 C ATOM 558 C LEU A 66 36.102 3.639 24.097 1.00 5.61 C ANISOU 558 C LEU A 66 754 498 879 -39 171 -42 C ATOM 559 O LEU A 66 37.045 2.823 24.095 1.00 5.86 O ANISOU 559 O LEU A 66 811 568 846 78 126 -10 O ATOM 560 CB LEU A 66 35.684 5.202 26.045 1.00 5.63 C ANISOU 560 CB LEU A 66 771 615 753 209 -12 6 C ATOM 561 CG LEU A 66 36.169 4.186 27.058 1.00 5.85 C ANISOU 561 CG LEU A 66 859 563 801 93 35 -5 C ATOM 562 CD1 LEU A 66 37.666 4.302 27.320 1.00 6.52 C ANISOU 562 CD1 LEU A 66 895 745 839 193 -182 30 C ATOM 563 CD2 LEU A 66 35.342 4.287 28.357 1.00 7.36 C ANISOU 563 CD2 LEU A 66 1011 1079 708 278 -8 115 C ATOM 564 N TRP A 67 34.891 3.310 23.639 1.00 5.95 N ANISOU 564 N TRP A 67 772 587 902 -41 97 -43 N ATOM 565 CA TRP A 67 34.632 1.960 23.114 1.00 5.60 C ANISOU 565 CA TRP A 67 804 493 830 -122 73 129 C ATOM 566 C TRP A 67 35.580 1.625 21.966 1.00 5.12 C ANISOU 566 C TRP A 67 690 382 873 -44 -53 0 C ATOM 567 O TRP A 67 36.136 0.543 21.900 1.00 6.36 O ANISOU 567 O TRP A 67 838 548 1029 143 19 40 O ATOM 568 CB TRP A 67 33.164 1.828 22.742 1.00 5.95 C ANISOU 568 CB TRP A 67 824 466 970 -115 90 0 C ATOM 569 CG TRP A 67 32.183 1.783 23.877 1.00 5.60 C ANISOU 569 CG TRP A 67 772 343 1014 1 42 -75 C ATOM 570 CD1 TRP A 67 32.469 1.712 25.205 1.00 6.32 C ANISOU 570 CD1 TRP A 67 858 580 963 42 129 40 C ATOM 571 CD2 TRP A 67 30.756 1.786 23.780 1.00 6.04 C ANISOU 571 CD2 TRP A 67 741 277 1276 47 102 56 C ATOM 572 NE1 TRP A 67 31.306 1.689 25.960 1.00 6.91 N ANISOU 572 NE1 TRP A 67 1024 485 1117 -66 243 -210 N ATOM 573 CE2 TRP A 67 30.238 1.718 25.078 1.00 7.09 C ANISOU 573 CE2 TRP A 67 875 520 1298 108 224 -269 C ATOM 574 CE3 TRP A 67 29.858 1.828 22.685 1.00 6.59 C ANISOU 574 CE3 TRP A 67 702 452 1350 132 84 149 C ATOM 575 CZ2 TRP A 67 28.862 1.690 25.349 1.00 7.75 C ANISOU 575 CZ2 TRP A 67 939 431 1576 2 323 -153 C ATOM 576 CZ3 TRP A 67 28.513 1.808 22.936 1.00 7.62 C ANISOU 576 CZ3 TRP A 67 739 561 1595 36 8 40 C ATOM 577 CH2 TRP A 67 28.035 1.738 24.252 1.00 8.48 C ANISOU 577 CH2 TRP A 67 773 671 1776 -30 278 -160 C ATOM 578 N ASN A 68 35.784 2.566 21.035 1.00 5.35 N ANISOU 578 N ASN A 68 672 558 804 26 70 95 N ATOM 579 CA ASN A 68 36.673 2.340 19.918 1.00 5.65 C ANISOU 579 CA ASN A 68 792 437 918 9 47 -105 C ATOM 580 C ASN A 68 38.111 2.155 20.388 1.00 5.94 C ANISOU 580 C ASN A 68 717 646 894 -32 100 -46 C ATOM 581 O ASN A 68 38.830 1.267 19.889 1.00 6.55 O ANISOU 581 O ASN A 68 711 663 1116 4 34 -57 O ATOM 582 CB ASN A 68 36.572 3.504 18.924 1.00 7.01 C ANISOU 582 CB ASN A 68 888 787 990 32 184 160 C ATOM 583 CG ASN A 68 35.399 3.451 18.010 1.00 7.70 C ANISOU 583 CG ASN A 68 1189 928 808 11 47 30 C ATOM 584 OD1 ASN A 68 35.138 2.463 17.321 1.00 13.87 O ANISOU 584 OD1 ASN A 68 2509 910 1852 29 -851 -87 O ATOM 585 ND2 ASN A 68 34.655 4.551 17.896 1.00 11.03 N ANISOU 585 ND2 ASN A 68 1592 1400 1199 520 -490 -352 N ATOM 586 N VAL A 69 38.588 2.959 21.343 1.00 5.66 N ANISOU 586 N VAL A 69 669 568 913 -73 41 74 N ATOM 587 CA VAL A 69 39.923 2.798 21.909 1.00 5.71 C ANISOU 587 CA VAL A 69 561 541 1067 -135 129 26 C ATOM 588 C VAL A 69 40.080 1.425 22.565 1.00 5.68 C ANISOU 588 C VAL A 69 570 594 993 -45 -40 -19 C ATOM 589 O VAL A 69 41.085 0.733 22.318 1.00 6.45 O ANISOU 589 O VAL A 69 730 691 1030 74 176 26 O ATOM 590 CB VAL A 69 40.210 3.963 22.895 1.00 5.90 C ANISOU 590 CB VAL A 69 651 668 921 -62 69 7 C ATOM 591 CG1 VAL A 69 41.432 3.668 23.777 1.00 7.70 C ANISOU 591 CG1 VAL A 69 767 925 1232 2 -123 -48 C ATOM 592 CG2 VAL A 69 40.412 5.264 22.137 1.00 7.03 C ANISOU 592 CG2 VAL A 69 1112 457 1100 -78 -5 -26 C ATOM 593 N LEU A 70 39.101 1.050 23.390 1.00 5.82 N ANISOU 593 N LEU A 70 763 475 972 139 165 36 N ATOM 594 CA LEU A 70 39.175 -0.243 24.076 1.00 5.42 C ANISOU 594 CA LEU A 70 747 467 844 92 -17 7 C ATOM 595 C LEU A 70 39.244 -1.385 23.074 1.00 6.08 C ANISOU 595 C LEU A 70 815 492 1003 33 58 -72 C ATOM 596 O LEU A 70 39.987 -2.360 23.281 1.00 6.38 O ANISOU 596 O LEU A 70 877 474 1072 119 -17 -5 O ATOM 597 CB LEU A 70 37.998 -0.437 25.060 1.00 7.33 C ANISOU 597 CB LEU A 70 983 766 1035 32 209 52 C ATOM 598 CG LEU A 70 37.976 0.538 26.257 1.00 7.91 C ANISOU 598 CG LEU A 70 1203 820 981 258 221 59 C ATOM 599 CD1 LEU A 70 36.746 0.272 27.116 1.00 9.94 C ANISOU 599 CD1 LEU A 70 1378 947 1450 153 521 209 C ATOM 600 CD2 LEU A 70 39.240 0.462 27.090 1.00 9.13 C ANISOU 600 CD2 LEU A 70 1442 974 1053 153 -81 -44 C ATOM 601 N ASP A 71 38.468 -1.314 21.992 1.00 6.23 N ANISOU 601 N ASP A 71 695 482 1191 21 -96 -94 N ATOM 602 CA ASP A 71 38.551 -2.416 21.001 1.00 5.82 C ANISOU 602 CA ASP A 71 793 489 929 -85 97 37 C ATOM 603 C ASP A 71 39.932 -2.489 20.388 1.00 6.54 C ANISOU 603 C ASP A 71 851 595 1039 33 151 48 C ATOM 604 O ASP A 71 40.491 -3.604 20.208 1.00 8.06 O ANISOU 604 O ASP A 71 891 584 1588 84 93 -75 O ATOM 605 CB ASP A 71 37.471 -2.227 19.958 1.00 6.98 C ANISOU 605 CB ASP A 71 844 724 1085 -124 23 -41 C ATOM 606 CG ASP A 71 36.074 -2.613 20.404 1.00 7.39 C ANISOU 606 CG ASP A 71 836 882 1089 -128 24 -186 C ATOM 607 OD1 ASP A 71 35.937 -3.422 21.337 1.00 8.38 O ANISOU 607 OD1 ASP A 71 930 922 1332 -171 236 -98 O ATOM 608 OD2 ASP A 71 35.111 -2.170 19.718 1.00 9.29 O ANISOU 608 OD2 ASP A 71 825 1324 1379 -108 -97 -112 O ATOM 609 N GLU A 72 40.577 -1.374 20.052 1.00 6.62 N ANISOU 609 N GLU A 72 720 647 1146 -9 198 51 N ATOM 610 CA GLU A 72 41.934 -1.426 19.489 1.00 6.69 C ANISOU 610 CA GLU A 72 809 686 1047 -85 199 -178 C ATOM 611 C GLU A 72 42.923 -2.020 20.461 1.00 7.18 C ANISOU 611 C GLU A 72 802 699 1226 -66 250 60 C ATOM 612 O GLU A 72 43.921 -2.644 20.052 1.00 9.07 O ANISOU 612 O GLU A 72 969 1156 1320 228 266 89 O ATOM 613 CB GLU A 72 42.374 -0.044 19.052 1.00 7.92 C ANISOU 613 CB GLU A 72 990 842 1178 -150 283 121 C ATOM 614 CG GLU A 72 41.509 0.531 17.929 1.00 8.50 C ANISOU 614 CG GLU A 72 831 1078 1319 -92 257 197 C ATOM 615 CD GLU A 72 41.517 -0.229 16.627 1.00 9.98 C ANISOU 615 CD GLU A 72 1370 1234 1186 374 161 176 C ATOM 616 OE1 GLU A 72 42.497 -0.916 16.305 1.00 15.77 O ANISOU 616 OE1 GLU A 72 1787 2762 1444 1088 371 45 O ATOM 617 OE2 GLU A 72 40.529 -0.110 15.868 1.00 13.74 O ANISOU 617 OE2 GLU A 72 1642 1925 1653 491 -231 -210 O ATOM 618 N LEU A 73 42.690 -1.865 21.757 1.00 7.00 N ANISOU 618 N LEU A 73 695 834 1131 -7 191 62 N ATOM 619 CA LEU A 73 43.549 -2.402 22.808 1.00 7.23 C ANISOU 619 CA LEU A 73 554 872 1319 32 56 4 C ATOM 620 C LEU A 73 43.213 -3.841 23.198 1.00 7.00 C ANISOU 620 C LEU A 73 523 723 1413 179 100 -73 C ATOM 621 O LEU A 73 43.879 -4.462 24.023 1.00 8.58 O ANISOU 621 O LEU A 73 964 777 1520 302 -111 -105 O ATOM 622 CB LEU A 73 43.440 -1.514 24.063 1.00 8.37 C ANISOU 622 CB LEU A 73 1131 757 1291 -85 27 39 C ATOM 623 CG LEU A 73 43.936 -0.084 23.941 1.00 9.12 C ANISOU 623 CG LEU A 73 1256 736 1474 -30 -94 189 C ATOM 624 CD1 LEU A 73 43.556 0.722 25.181 1.00 12.89 C ANISOU 624 CD1 LEU A 73 1957 1209 1733 -400 -313 -399 C ATOM 625 CD2 LEU A 73 45.415 -0.016 23.637 1.00 14.66 C ANISOU 625 CD2 LEU A 73 1295 1310 2966 -513 0 -81 C ATOM 626 N ASP A 74 42.131 -4.383 22.641 1.00 6.92 N ANISOU 626 N ASP A 74 747 702 1180 58 88 -11 N ATOM 627 CA ASP A 74 41.590 -5.675 23.070 1.00 7.44 C ANISOU 627 CA ASP A 74 993 562 1272 20 122 -143 C ATOM 628 C ASP A 74 41.280 -5.665 24.566 1.00 7.03 C ANISOU 628 C ASP A 74 941 463 1269 61 70 -54 C ATOM 629 O ASP A 74 41.524 -6.636 25.291 1.00 7.70 O ANISOU 629 O ASP A 74 1069 580 1278 222 4 -3 O ATOM 630 CB ASP A 74 42.444 -6.904 22.656 1.00 7.78 C ANISOU 630 CB ASP A 74 1114 680 1164 178 22 -176 C ATOM 631 CG ASP A 74 41.670 -8.189 22.715 1.00 8.66 C ANISOU 631 CG ASP A 74 1091 624 1573 180 246 -296 C ATOM 632 OD1 ASP A 74 40.419 -8.197 22.651 1.00 9.86 O ANISOU 632 OD1 ASP A 74 1125 963 1659 63 42 -280 O ATOM 633 OD2 ASP A 74 42.331 -9.234 22.849 1.00 12.98 O ANISOU 633 OD2 ASP A 74 1360 651 2920 187 -6 -110 O ATOM 634 N GLN A 75 40.694 -4.553 25.020 1.00 6.30 N ANISOU 634 N GLN A 75 859 485 1051 123 -1 47 N ATOM 635 CA GLN A 75 40.282 -4.377 26.400 1.00 6.87 C ANISOU 635 CA GLN A 75 803 789 1019 9 0 -17 C ATOM 636 C GLN A 75 38.796 -3.950 26.502 1.00 5.72 C ANISOU 636 C GLN A 75 797 497 880 -13 18 84 C ATOM 637 O GLN A 75 38.426 -3.152 27.380 1.00 6.59 O ANISOU 637 O GLN A 75 973 518 1012 -96 46 -30 O ATOM 638 CB GLN A 75 41.181 -3.386 27.138 1.00 6.86 C ANISOU 638 CB GLN A 75 780 727 1099 22 -40 80 C ATOM 639 CG GLN A 75 42.631 -3.872 27.321 1.00 6.93 C ANISOU 639 CG GLN A 75 788 647 1200 -35 -4 87 C ATOM 640 CD GLN A 75 43.343 -3.078 28.380 1.00 7.27 C ANISOU 640 CD GLN A 75 673 774 1317 4 -108 75 C ATOM 641 OE1 GLN A 75 43.728 -1.903 28.200 1.00 8.18 O ANISOU 641 OE1 GLN A 75 861 894 1355 -183 -180 46 O ATOM 642 NE2 GLN A 75 43.482 -3.652 29.558 1.00 8.38 N ANISOU 642 NE2 GLN A 75 975 806 1403 83 -250 74 N ATOM 643 N ALA A 76 37.924 -4.525 25.661 1.00 6.29 N ANISOU 643 N ALA A 76 759 640 991 -70 22 -20 N ATOM 644 CA ALA A 76 36.499 -4.257 25.749 1.00 5.99 C ANISOU 644 CA ALA A 76 785 471 1021 -61 68 17 C ATOM 645 C ALA A 76 35.917 -4.671 27.089 1.00 5.36 C ANISOU 645 C ALA A 76 701 370 967 -113 -15 17 C ATOM 646 O ALA A 76 34.867 -4.185 27.508 1.00 6.55 O ANISOU 646 O ALA A 76 855 666 967 98 -2 26 O ATOM 647 CB ALA A 76 35.706 -4.870 24.593 1.00 8.28 C ANISOU 647 CB ALA A 76 948 1143 1056 -111 -133 33 C ATOM 648 N TRP A 77 36.613 -5.592 27.784 1.00 5.65 N ANISOU 648 N TRP A 77 682 497 968 -18 13 1 N ATOM 649 CA TRP A 77 36.252 -6.087 29.093 1.00 6.39 C ANISOU 649 CA TRP A 77 1005 478 944 -31 -211 43 C ATOM 650 C TRP A 77 36.566 -5.155 30.240 1.00 6.07 C ANISOU 650 C TRP A 77 847 496 962 -24 -214 49 C ATOM 651 O TRP A 77 36.196 -5.445 31.393 1.00 7.41 O ANISOU 651 O TRP A 77 1156 660 998 -46 -87 -104 O ATOM 652 CB TRP A 77 36.951 -7.451 29.365 1.00 6.82 C ANISOU 652 CB TRP A 77 1152 452 988 -45 -203 -28 C ATOM 653 CG TRP A 77 38.445 -7.411 29.119 1.00 7.11 C ANISOU 653 CG TRP A 77 1124 492 1086 51 -183 55 C ATOM 654 CD1 TRP A 77 39.072 -7.745 27.929 1.00 8.16 C ANISOU 654 CD1 TRP A 77 1180 526 1396 73 -46 -104 C ATOM 655 CD2 TRP A 77 39.511 -7.046 29.999 1.00 7.96 C ANISOU 655 CD2 TRP A 77 1172 556 1297 -35 -312 199 C ATOM 656 NE1 TRP A 77 40.419 -7.606 28.047 1.00 9.52 N ANISOU 656 NE1 TRP A 77 1175 732 1710 -3 74 135 N ATOM 657 CE2 TRP A 77 40.735 -7.187 29.286 1.00 9.25 C ANISOU 657 CE2 TRP A 77 1114 531 1869 40 -227 145 C ATOM 658 CE3 TRP A 77 39.528 -6.626 31.325 1.00 10.50 C ANISOU 658 CE3 TRP A 77 1617 928 1446 213 -611 -86 C ATOM 659 CZ2 TRP A 77 41.992 -6.905 29.871 1.00 10.69 C ANISOU 659 CZ2 TRP A 77 1154 764 2144 80 -320 172 C ATOM 660 CZ3 TRP A 77 40.769 -6.351 31.928 1.00 11.53 C ANISOU 660 CZ3 TRP A 77 1775 943 1664 -32 -647 -194 C ATOM 661 CH2 TRP A 77 41.955 -6.503 31.167 1.00 13.11 C ANISOU 661 CH2 TRP A 77 1585 1216 2180 305 -659 29 C ATOM 662 N LEU A 78 37.223 -4.042 30.005 1.00 6.18 N ANISOU 662 N LEU A 78 892 409 1048 72 -173 -99 N ATOM 663 CA LEU A 78 37.710 -3.154 31.063 1.00 6.29 C ANISOU 663 CA LEU A 78 610 764 1017 -53 -103 -125 C ATOM 664 C LEU A 78 36.554 -2.612 31.879 1.00 5.41 C ANISOU 664 C LEU A 78 527 507 1022 -127 -219 -226 C ATOM 665 O LEU A 78 35.541 -2.193 31.301 1.00 6.04 O ANISOU 665 O LEU A 78 636 651 1008 13 -190 -143 O ATOM 666 CB LEU A 78 38.457 -1.952 30.452 1.00 6.90 C ANISOU 666 CB LEU A 78 715 638 1267 -33 38 -144 C ATOM 667 CG LEU A 78 39.442 -1.263 31.370 1.00 7.85 C ANISOU 667 CG LEU A 78 824 894 1264 -135 7 -226 C ATOM 668 CD1 LEU A 78 40.649 -2.136 31.685 1.00 11.04 C ANISOU 668 CD1 LEU A 78 832 1449 1915 137 -274 -540 C ATOM 669 CD2 LEU A 78 39.853 0.046 30.726 1.00 9.11 C ANISOU 669 CD2 LEU A 78 988 1080 1391 -433 210 -246 C ATOM 670 N PRO A 79 36.674 -2.505 33.201 1.00 6.18 N ANISOU 670 N PRO A 79 837 575 936 97 -138 -63 N ATOM 671 CA PRO A 79 35.671 -1.755 33.957 1.00 5.93 C ANISOU 671 CA PRO A 79 692 565 998 26 -100 40 C ATOM 672 C PRO A 79 35.614 -0.296 33.520 1.00 5.56 C ANISOU 672 C PRO A 79 611 544 958 25 -110 -16 C ATOM 673 O PRO A 79 36.639 0.369 33.343 1.00 6.19 O ANISOU 673 O PRO A 79 648 561 1141 -49 -119 -18 O ATOM 674 CB PRO A 79 36.164 -1.858 35.429 1.00 8.22 C ANISOU 674 CB PRO A 79 1521 715 889 80 -104 -44 C ATOM 675 CG PRO A 79 37.081 -3.045 35.442 1.00 10.28 C ANISOU 675 CG PRO A 79 1330 1427 1148 429 -201 228 C ATOM 676 CD PRO A 79 37.714 -3.071 34.098 1.00 7.30 C ANISOU 676 CD PRO A 79 842 735 1195 156 -213 139 C ATOM 677 N VAL A 80 34.379 0.208 33.352 1.00 5.53 N ANISOU 677 N VAL A 80 664 439 998 -51 -89 27 N ATOM 678 CA VAL A 80 34.105 1.597 32.916 1.00 5.01 C ANISOU 678 CA VAL A 80 590 343 973 -3 -139 -64 C ATOM 679 C VAL A 80 33.124 2.251 33.866 1.00 5.40 C ANISOU 679 C VAL A 80 819 466 765 -104 -39 16 C ATOM 680 O VAL A 80 32.115 1.621 34.243 1.00 6.84 O ANISOU 680 O VAL A 80 944 570 1084 -91 80 109 O ATOM 681 CB VAL A 80 33.497 1.580 31.481 1.00 5.47 C ANISOU 681 CB VAL A 80 695 599 783 -110 -59 6 C ATOM 682 CG1 VAL A 80 33.091 3.001 31.056 1.00 7.35 C ANISOU 682 CG1 VAL A 80 1120 800 872 132 43 165 C ATOM 683 CG2 VAL A 80 34.439 0.950 30.484 1.00 6.64 C ANISOU 683 CG2 VAL A 80 1005 627 890 -43 -23 -54 C ATOM 684 N GLU A 81 33.393 3.494 34.266 1.00 5.66 N ANISOU 684 N GLU A 81 836 487 828 29 60 -61 N ATOM 685 CA GLU A 81 32.480 4.318 35.025 1.00 5.39 C ANISOU 685 CA GLU A 81 515 662 871 49 108 56 C ATOM 686 C GLU A 81 32.142 5.554 34.176 1.00 5.99 C ANISOU 686 C GLU A 81 743 578 956 26 86 -5 C ATOM 687 O GLU A 81 33.056 6.246 33.725 1.00 6.44 O ANISOU 687 O GLU A 81 746 595 1107 15 110 93 O ATOM 688 CB GLU A 81 33.082 4.719 36.378 1.00 6.81 C ANISOU 688 CB GLU A 81 982 616 989 -111 41 -123 C ATOM 689 CG GLU A 81 32.170 5.553 37.255 1.00 7.83 C ANISOU 689 CG GLU A 81 1096 934 946 -34 135 -81 C ATOM 690 CD GLU A 81 32.663 5.686 38.685 1.00 9.27 C ANISOU 690 CD GLU A 81 1590 946 988 55 -35 -160 C ATOM 691 OE1 GLU A 81 33.176 4.663 39.254 1.00 10.11 O ANISOU 691 OE1 GLU A 81 1418 1106 1318 156 -189 30 O ATOM 692 OE2 GLU A 81 32.494 6.789 39.269 1.00 10.15 O ANISOU 692 OE2 GLU A 81 1671 887 1297 -36 -47 -183 O ATOM 693 N LYS A 82 30.847 5.790 33.988 1.00 6.11 N ANISOU 693 N LYS A 82 710 510 1101 36 73 110 N ATOM 694 CA LYS A 82 30.318 6.866 33.170 1.00 6.07 C ANISOU 694 CA LYS A 82 704 404 1196 1 65 139 C ATOM 695 C LYS A 82 29.692 7.916 34.093 1.00 7.82 C ANISOU 695 C LYS A 82 1031 526 1413 181 232 155 C ATOM 696 O LYS A 82 28.762 7.610 34.847 1.00 13.06 O ANISOU 696 O LYS A 82 1452 805 2704 0 1173 -58 O ATOM 697 CB LYS A 82 29.275 6.346 32.187 1.00 7.97 C ANISOU 697 CB LYS A 82 820 524 1684 -38 -260 235 C ATOM 698 CG LYS A 82 29.801 5.179 31.342 1.00 7.00 C ANISOU 698 CG LYS A 82 759 579 1324 -158 -313 198 C ATOM 699 CD LYS A 82 28.878 4.658 30.299 1.00 11.64 C ANISOU 699 CD LYS A 82 1357 932 2135 -225 -991 36 C ATOM 700 CE LYS A 82 29.374 3.473 29.512 1.00 11.39 C ANISOU 700 CE LYS A 82 1407 564 2357 -399 -1089 -11 C ATOM 701 NZ LYS A 82 29.148 2.162 30.177 1.00 15.35 N ANISOU 701 NZ LYS A 82 2568 998 2265 -588 -559 352 N ATOM 702 N SER A 83 30.213 9.152 34.127 1.00 6.92 N ANISOU 702 N SER A 83 902 610 1118 50 120 -65 N ATOM 703 CA SER A 83 29.730 10.151 35.078 1.00 7.31 C ANISOU 703 CA SER A 83 1131 558 1090 40 134 1 C ATOM 704 C SER A 83 29.415 11.468 34.393 1.00 5.90 C ANISOU 704 C SER A 83 808 513 921 -40 160 -187 C ATOM 705 O SER A 83 30.251 12.022 33.656 1.00 6.25 O ANISOU 705 O SER A 83 768 739 868 25 66 32 O ATOM 706 CB SER A 83 30.776 10.386 36.151 1.00 9.13 C ANISOU 706 CB SER A 83 1628 704 1138 165 -112 -110 C ATOM 707 OG SER A 83 30.466 11.420 37.036 1.00 10.51 O ANISOU 707 OG SER A 83 2136 751 1106 208 -207 32 O ATOM 708 N TRP A 84 28.249 12.046 34.721 1.00 6.30 N ANISOU 708 N TRP A 84 712 761 922 68 106 -20 N ATOM 709 CA TRP A 84 27.907 13.391 34.271 1.00 5.90 C ANISOU 709 CA TRP A 84 803 730 708 58 -3 -50 C ATOM 710 C TRP A 84 28.903 14.430 34.709 1.00 6.09 C ANISOU 710 C TRP A 84 899 853 563 31 19 -70 C ATOM 711 O TRP A 84 29.013 15.499 34.107 1.00 6.76 O ANISOU 711 O TRP A 84 979 685 905 29 58 -24 O ATOM 712 CB TRP A 84 26.543 13.751 34.796 1.00 7.47 C ANISOU 712 CB TRP A 84 835 991 1013 215 7 -41 C ATOM 713 CG TRP A 84 26.437 14.024 36.280 1.00 7.97 C ANISOU 713 CG TRP A 84 718 1357 955 268 150 23 C ATOM 714 CD1 TRP A 84 26.225 13.178 37.300 1.00 10.11 C ANISOU 714 CD1 TRP A 84 1099 1589 1153 402 147 237 C ATOM 715 CD2 TRP A 84 26.522 15.335 36.902 1.00 8.76 C ANISOU 715 CD2 TRP A 84 862 1512 954 297 136 -184 C ATOM 716 NE1 TRP A 84 26.191 13.835 38.498 1.00 11.96 N ANISOU 716 NE1 TRP A 84 1387 2171 987 839 399 274 N ATOM 717 CE2 TRP A 84 26.359 15.169 38.286 1.00 10.65 C ANISOU 717 CE2 TRP A 84 1089 2005 952 784 95 -165 C ATOM 718 CE3 TRP A 84 26.720 16.629 36.421 1.00 9.73 C ANISOU 718 CE3 TRP A 84 1103 1454 1138 83 -17 -326 C ATOM 719 CZ2 TRP A 84 26.392 16.270 39.141 1.00 14.52 C ANISOU 719 CZ2 TRP A 84 1547 2732 1236 855 17 -755 C ATOM 720 CZ3 TRP A 84 26.749 17.721 37.266 1.00 14.26 C ANISOU 720 CZ3 TRP A 84 1661 1611 2147 278 153 -780 C ATOM 721 CH2 TRP A 84 26.589 17.514 38.642 1.00 14.71 C ANISOU 721 CH2 TRP A 84 1367 2342 1880 510 -167 -1272 C ATOM 722 N LYS A 85 29.605 14.215 35.759 1.00 6.52 N ANISOU 722 N LYS A 85 910 747 819 -59 -10 -116 N ATOM 723 CA LYS A 85 30.631 15.110 36.329 1.00 5.90 C ANISOU 723 CA LYS A 85 683 584 974 85 -52 -122 C ATOM 724 C LYS A 85 31.768 15.377 35.332 1.00 6.26 C ANISOU 724 C LYS A 85 807 613 957 38 -64 -75 C ATOM 725 O LYS A 85 32.472 16.392 35.446 1.00 6.51 O ANISOU 725 O LYS A 85 876 595 1002 24 -75 57 O ATOM 726 CB LYS A 85 31.109 14.647 37.690 1.00 7.10 C ANISOU 726 CB LYS A 85 801 863 1032 -10 -137 -42 C ATOM 727 CG LYS A 85 29.973 14.586 38.726 1.00 8.68 C ANISOU 727 CG LYS A 85 990 1294 1012 73 -28 102 C ATOM 728 CD LYS A 85 30.369 13.975 40.049 1.00 10.93 C ANISOU 728 CD LYS A 85 1637 1463 1053 -58 -106 171 C ATOM 729 CE LYS A 85 29.176 13.939 41.005 1.00 12.02 C ANISOU 729 CE LYS A 85 1798 1587 1183 -358 117 227 C ATOM 730 NZ LYS A 85 29.448 13.463 42.360 1.00 16.94 N ANISOU 730 NZ LYS A 85 2556 2493 1389 -575 -117 696 N ATOM 731 N LEU A 86 31.997 14.489 34.354 1.00 6.11 N ANISOU 731 N LEU A 86 912 633 778 53 20 44 N ATOM 732 CA LEU A 86 32.957 14.679 33.286 1.00 5.82 C ANISOU 732 CA LEU A 86 800 581 831 -18 -88 -65 C ATOM 733 C LEU A 86 32.343 15.252 31.991 1.00 5.00 C ANISOU 733 C LEU A 86 684 422 793 -14 -19 -6 C ATOM 734 O LEU A 86 33.052 15.374 30.988 1.00 5.61 O ANISOU 734 O LEU A 86 630 579 922 19 -20 34 O ATOM 735 CB LEU A 86 33.718 13.356 32.963 1.00 5.88 C ANISOU 735 CB LEU A 86 746 492 995 70 -29 91 C ATOM 736 CG LEU A 86 34.654 12.902 34.083 1.00 6.71 C ANISOU 736 CG LEU A 86 819 682 1048 -28 -99 135 C ATOM 737 CD1 LEU A 86 35.195 11.485 33.752 1.00 6.98 C ANISOU 737 CD1 LEU A 86 829 644 1181 58 -113 113 C ATOM 738 CD2 LEU A 86 35.796 13.838 34.331 1.00 9.93 C ANISOU 738 CD2 LEU A 86 1029 677 2068 -88 -590 180 C ATOM 739 N ASN A 87 31.077 15.617 32.002 1.00 5.87 N ANISOU 739 N ASN A 87 651 574 1004 136 10 -32 N ATOM 740 CA ASN A 87 30.420 16.198 30.834 1.00 5.56 C ANISOU 740 CA ASN A 87 647 654 810 -13 20 -69 C ATOM 741 C ASN A 87 31.135 17.480 30.375 1.00 5.70 C ANISOU 741 C ASN A 87 734 579 852 -65 65 -91 C ATOM 742 O ASN A 87 31.750 18.222 31.161 1.00 6.44 O ANISOU 742 O ASN A 87 1003 481 962 41 -155 -25 O ATOM 743 CB ASN A 87 28.937 16.515 31.099 1.00 5.53 C ANISOU 743 CB ASN A 87 647 608 846 52 -77 -1 C ATOM 744 CG ASN A 87 28.003 15.349 30.920 1.00 5.56 C ANISOU 744 CG ASN A 87 648 509 953 95 -56 77 C ATOM 745 OD1 ASN A 87 28.416 14.209 30.725 1.00 6.06 O ANISOU 745 OD1 ASN A 87 728 602 971 126 -74 -33 O ATOM 746 ND2 ASN A 87 26.699 15.642 30.976 1.00 6.74 N ANISOU 746 ND2 ASN A 87 630 596 1335 40 -80 -78 N ATOM 747 N GLU A 88 31.002 17.772 29.081 1.00 5.82 N ANISOU 747 N GLU A 88 723 537 949 48 -12 -37 N ATOM 748 CA GLU A 88 31.317 19.090 28.495 1.00 5.50 C ANISOU 748 CA GLU A 88 670 589 832 15 45 -7 C ATOM 749 C GLU A 88 30.642 20.180 29.298 1.00 5.54 C ANISOU 749 C GLU A 88 800 512 793 114 -24 37 C ATOM 750 O GLU A 88 29.601 19.994 29.934 1.00 5.99 O ANISOU 750 O GLU A 88 836 535 904 198 20 29 O ATOM 751 CB GLU A 88 30.849 19.119 27.035 1.00 5.43 C ANISOU 751 CB GLU A 88 692 446 926 21 -24 -144 C ATOM 752 CG GLU A 88 31.245 20.322 26.262 1.00 5.93 C ANISOU 752 CG GLU A 88 826 418 1009 87 -139 -11 C ATOM 753 CD GLU A 88 32.746 20.546 26.255 1.00 6.16 C ANISOU 753 CD GLU A 88 871 436 1033 -17 -61 73 C ATOM 754 OE1 GLU A 88 33.293 21.137 27.210 1.00 7.51 O ANISOU 754 OE1 GLU A 88 736 1077 1042 -37 -22 -37 O ATOM 755 OE2 GLU A 88 33.381 20.033 25.294 1.00 7.45 O ANISOU 755 OE2 GLU A 88 823 939 1070 21 -10 10 O ATOM 756 N ARG A 89 31.250 21.384 29.284 1.00 6.61 N ANISOU 756 N ARG A 89 755 641 1116 46 -126 -124 N ATOM 757 CA ARG A 89 30.569 22.586 29.797 1.00 6.87 C ANISOU 757 CA ARG A 89 893 557 1161 101 -210 -83 C ATOM 758 C ARG A 89 29.233 22.775 29.101 1.00 6.39 C ANISOU 758 C ARG A 89 905 601 923 78 -106 -93 C ATOM 759 O ARG A 89 29.179 22.790 27.866 1.00 7.30 O ANISOU 759 O ARG A 89 881 938 956 175 14 -40 O ATOM 760 CB AARG A 89 31.520 23.771 29.579 0.62 8.37 C ANISOU 760 CB AARG A 89 979 756 1445 -84 111 -215 C ATOM 761 CG AARG A 89 30.940 25.128 29.862 0.62 9.64 C ANISOU 761 CG AARG A 89 981 589 2094 23 -220 147 C ATOM 762 CD AARG A 89 30.314 25.815 28.638 0.62 16.20 C ANISOU 762 CD AARG A 89 1984 1405 2765 -342 -348 1193 C ATOM 763 NE AARG A 89 31.324 26.174 27.734 0.62 15.23 N ANISOU 763 NE AARG A 89 1894 1124 2768 313 -42 952 N ATOM 764 CZ AARG A 89 31.963 27.287 27.491 0.62 12.22 C ANISOU 764 CZ AARG A 89 1562 1419 1660 -178 -276 454 C ATOM 765 NH1AARG A 89 31.740 28.408 28.165 0.62 12.70 N ANISOU 765 NH1AARG A 89 1282 1993 1550 -435 -553 -125 N ATOM 766 NH2AARG A 89 32.873 27.193 26.511 0.62 15.27 N ANISOU 766 NH2AARG A 89 2017 1488 2297 245 216 537 N ATOM 767 CB BARG A 89 31.496 23.787 29.610 0.38 6.85 C ANISOU 767 CB BARG A 89 949 527 1127 123 -430 364 C ATOM 768 CG BARG A 89 30.930 25.110 30.069 0.38 7.43 C ANISOU 768 CG BARG A 89 1093 526 1204 -4 -130 282 C ATOM 769 CD BARG A 89 31.828 26.290 29.694 0.38 6.44 C ANISOU 769 CD BARG A 89 1103 555 788 -48 -113 104 C ATOM 770 NE BARG A 89 31.586 26.652 28.333 0.38 9.37 N ANISOU 770 NE BARG A 89 1315 1132 1114 -722 -726 511 N ATOM 771 CZ BARG A 89 31.273 27.673 27.608 0.38 6.93 C ANISOU 771 CZ BARG A 89 492 836 1304 -276 -735 272 C ATOM 772 NH1BARG A 89 31.142 28.906 28.099 0.38 17.15 N ANISOU 772 NH1BARG A 89 3163 1471 1881 897 1260 -147 N ATOM 773 NH2BARG A 89 31.099 27.530 26.306 0.38 7.61 N ANISOU 773 NH2BARG A 89 932 626 1333 -346 -781 555 N ATOM 774 N HIS A 90 28.192 23.023 29.885 1.00 5.88 N ANISOU 774 N HIS A 90 848 519 868 16 -114 12 N ATOM 775 CA HIS A 90 26.890 23.306 29.321 1.00 6.42 C ANISOU 775 CA HIS A 90 853 598 987 -3 -178 -39 C ATOM 776 C HIS A 90 26.868 24.666 28.599 1.00 6.07 C ANISOU 776 C HIS A 90 796 567 942 132 -35 -3 C ATOM 777 O HIS A 90 27.362 25.668 29.147 1.00 7.60 O ANISOU 777 O HIS A 90 1059 633 1195 94 -162 -89 O ATOM 778 CB HIS A 90 25.816 23.275 30.461 1.00 6.56 C ANISOU 778 CB HIS A 90 965 632 897 174 -85 123 C ATOM 779 CG HIS A 90 24.420 23.106 29.965 1.00 6.72 C ANISOU 779 CG HIS A 90 912 654 986 177 -10 181 C ATOM 780 ND1 HIS A 90 23.667 24.146 29.497 1.00 8.08 N ANISOU 780 ND1 HIS A 90 1006 681 1383 205 -106 -102 N ATOM 781 CD2 HIS A 90 23.620 22.036 29.809 1.00 7.36 C ANISOU 781 CD2 HIS A 90 834 682 1280 204 47 -133 C ATOM 782 CE1 HIS A 90 22.523 23.732 29.024 1.00 7.54 C ANISOU 782 CE1 HIS A 90 972 720 1173 212 -184 5 C ATOM 783 NE2 HIS A 90 22.456 22.413 29.244 1.00 7.22 N ANISOU 783 NE2 HIS A 90 832 612 1298 275 68 95 N ATOM 784 N TYR A 91 26.290 24.726 27.406 1.00 6.55 N ANISOU 784 N TYR A 91 918 545 1028 143 -81 -8 N ATOM 785 CA TYR A 91 26.331 25.928 26.570 1.00 6.64 C ANISOU 785 CA TYR A 91 903 632 987 163 -92 65 C ATOM 786 C TYR A 91 25.074 26.762 26.625 1.00 7.46 C ANISOU 786 C TYR A 91 1072 750 1014 310 301 74 C ATOM 787 O TYR A 91 24.859 27.698 25.842 1.00 8.20 O ANISOU 787 O TYR A 91 1139 575 1401 216 151 188 O ATOM 788 CB TYR A 91 26.620 25.564 25.089 1.00 8.64 C ANISOU 788 CB TYR A 91 1406 761 1116 418 238 -103 C ATOM 789 CG TYR A 91 27.918 26.034 24.528 1.00 9.93 C ANISOU 789 CG TYR A 91 1534 968 1270 561 332 310 C ATOM 790 CD1 TYR A 91 28.203 27.382 24.481 1.00 13.15 C ANISOU 790 CD1 TYR A 91 1621 948 2427 546 543 789 C ATOM 791 CD2 TYR A 91 28.897 25.167 24.021 1.00 10.65 C ANISOU 791 CD2 TYR A 91 1752 1195 1099 644 502 236 C ATOM 792 CE1 TYR A 91 29.377 27.872 23.951 1.00 15.47 C ANISOU 792 CE1 TYR A 91 1903 1189 2785 676 960 1101 C ATOM 793 CE2 TYR A 91 30.079 25.628 23.497 1.00 12.28 C ANISOU 793 CE2 TYR A 91 1674 1499 1492 835 454 596 C ATOM 794 CZ TYR A 91 30.327 26.995 23.465 1.00 17.17 C ANISOU 794 CZ TYR A 91 2107 1481 2937 917 1228 1495 C ATOM 795 OH TYR A 91 31.512 27.462 22.959 1.00 19.63 O ANISOU 795 OH TYR A 91 2179 2315 2966 831 1381 1743 O ATOM 796 N GLY A 92 24.200 26.531 27.524 1.00 7.50 N ANISOU 796 N GLY A 92 1034 651 1165 320 67 56 N ATOM 797 CA GLY A 92 22.950 27.284 27.753 1.00 7.10 C ANISOU 797 CA GLY A 92 892 687 1119 149 149 -81 C ATOM 798 C GLY A 92 22.105 27.305 26.502 1.00 7.03 C ANISOU 798 C GLY A 92 868 666 1137 86 142 45 C ATOM 799 O GLY A 92 21.983 26.327 25.774 1.00 7.58 O ANISOU 799 O GLY A 92 1033 768 1079 204 77 -60 O ATOM 800 N ALA A 93 21.505 28.470 26.254 1.00 7.88 N ANISOU 800 N ALA A 93 1149 664 1183 132 -2 16 N ATOM 801 CA ALA A 93 20.660 28.733 25.091 1.00 8.74 C ANISOU 801 CA ALA A 93 1161 990 1169 272 43 43 C ATOM 802 C ALA A 93 21.459 28.692 23.784 1.00 8.76 C ANISOU 802 C ALA A 93 1246 908 1176 570 78 211 C ATOM 803 O ALA A 93 20.860 28.697 22.712 1.00 10.05 O ANISOU 803 O ALA A 93 1397 1255 1167 376 62 283 O ATOM 804 CB ALA A 93 19.969 30.071 25.234 1.00 9.44 C ANISOU 804 CB ALA A 93 1067 1121 1399 398 180 68 C ATOM 805 N LEU A 94 22.798 28.642 23.810 1.00 8.66 N ANISOU 805 N LEU A 94 1301 818 1172 241 173 144 N ATOM 806 CA LEU A 94 23.554 28.521 22.573 1.00 8.75 C ANISOU 806 CA LEU A 94 1291 783 1251 271 207 97 C ATOM 807 C LEU A 94 23.543 27.096 22.030 1.00 8.47 C ANISOU 807 C LEU A 94 1363 804 1050 325 -65 151 C ATOM 808 O LEU A 94 23.945 26.882 20.881 1.00 9.21 O ANISOU 808 O LEU A 94 1494 814 1190 271 -26 36 O ATOM 809 CB LEU A 94 24.994 28.998 22.750 1.00 8.94 C ANISOU 809 CB LEU A 94 1289 793 1315 329 127 298 C ATOM 810 CG LEU A 94 25.140 30.427 23.278 1.00 9.45 C ANISOU 810 CG LEU A 94 1338 656 1596 202 163 344 C ATOM 811 CD1 LEU A 94 26.607 30.813 23.325 1.00 10.24 C ANISOU 811 CD1 LEU A 94 1347 884 1659 230 168 339 C ATOM 812 CD2 LEU A 94 24.314 31.441 22.490 1.00 11.74 C ANISOU 812 CD2 LEU A 94 1546 803 2112 225 -38 550 C ATOM 813 N GLN A 95 23.130 26.069 22.785 1.00 8.63 N ANISOU 813 N GLN A 95 1297 775 1206 406 30 127 N ATOM 814 CA GLN A 95 23.219 24.676 22.290 1.00 8.09 C ANISOU 814 CA GLN A 95 1185 818 1072 242 -46 182 C ATOM 815 C GLN A 95 22.379 24.519 21.028 1.00 7.90 C ANISOU 815 C GLN A 95 994 835 1174 117 46 213 C ATOM 816 O GLN A 95 21.172 24.791 20.999 1.00 9.80 O ANISOU 816 O GLN A 95 1118 1459 1145 356 -4 206 O ATOM 817 CB GLN A 95 22.804 23.684 23.385 1.00 8.24 C ANISOU 817 CB GLN A 95 1133 863 1134 193 93 144 C ATOM 818 CG GLN A 95 23.772 23.640 24.552 1.00 7.72 C ANISOU 818 CG GLN A 95 1181 692 1059 174 65 122 C ATOM 819 CD GLN A 95 23.568 22.604 25.629 1.00 7.63 C ANISOU 819 CD GLN A 95 1131 762 1005 139 104 6 C ATOM 820 OE1 GLN A 95 24.460 22.530 26.531 1.00 7.36 O ANISOU 820 OE1 GLN A 95 1199 653 946 227 -60 20 O ATOM 821 NE2 GLN A 95 22.493 21.819 25.590 1.00 7.57 N ANISOU 821 NE2 GLN A 95 1018 639 1219 178 139 129 N ATOM 822 N GLY A 96 23.037 24.062 19.962 1.00 8.45 N ANISOU 822 N GLY A 96 1208 925 1077 214 25 136 N ATOM 823 CA GLY A 96 22.459 23.851 18.651 1.00 8.00 C ANISOU 823 CA GLY A 96 995 898 1145 219 -44 271 C ATOM 824 C GLY A 96 22.699 24.977 17.665 1.00 8.67 C ANISOU 824 C GLY A 96 1152 926 1216 121 -79 353 C ATOM 825 O GLY A 96 22.496 24.767 16.478 1.00 10.70 O ANISOU 825 O GLY A 96 1689 1108 1269 180 -224 385 O ATOM 826 N LEU A 97 23.099 26.142 18.124 1.00 9.16 N ANISOU 826 N LEU A 97 1340 842 1298 217 113 284 N ATOM 827 CA LEU A 97 23.296 27.292 17.220 1.00 8.77 C ANISOU 827 CA LEU A 97 1242 887 1203 189 -45 272 C ATOM 828 C LEU A 97 24.612 27.165 16.463 1.00 8.84 C ANISOU 828 C LEU A 97 1350 697 1311 233 86 249 C ATOM 829 O LEU A 97 25.616 26.665 16.983 1.00 9.81 O ANISOU 829 O LEU A 97 1434 944 1348 382 90 293 O ATOM 830 CB LEU A 97 23.213 28.613 17.999 1.00 10.06 C ANISOU 830 CB LEU A 97 1743 900 1181 338 162 279 C ATOM 831 CG LEU A 97 21.909 28.958 18.715 1.00 14.13 C ANISOU 831 CG LEU A 97 1884 1318 2165 724 307 126 C ATOM 832 CD1 LEU A 97 22.021 30.344 19.349 1.00 14.09 C ANISOU 832 CD1 LEU A 97 1904 1227 2224 527 657 219 C ATOM 833 CD2 LEU A 97 20.678 28.883 17.821 1.00 17.54 C ANISOU 833 CD2 LEU A 97 1691 2120 2854 211 281 95 C ATOM 834 N ASN A 98 24.658 27.682 15.243 1.00 8.89 N ANISOU 834 N ASN A 98 1224 804 1350 317 65 268 N ATOM 835 CA ASN A 98 25.861 27.750 14.444 1.00 9.46 C ANISOU 835 CA ASN A 98 1272 878 1445 131 102 366 C ATOM 836 C ASN A 98 26.751 28.885 14.957 1.00 8.37 C ANISOU 836 C ASN A 98 1306 607 1269 285 83 361 C ATOM 837 O ASN A 98 26.274 29.997 15.200 1.00 10.09 O ANISOU 837 O ASN A 98 1372 827 1635 346 300 315 O ATOM 838 CB ASN A 98 25.501 27.938 12.958 1.00 10.60 C ANISOU 838 CB ASN A 98 1339 1279 1409 5 11 299 C ATOM 839 CG ASN A 98 26.708 28.114 12.067 1.00 10.69 C ANISOU 839 CG ASN A 98 1499 1086 1475 281 143 396 C ATOM 840 OD1 ASN A 98 27.299 29.202 12.042 1.00 11.16 O ANISOU 840 OD1 ASN A 98 1471 1154 1616 180 229 516 O ATOM 841 ND2 ASN A 98 27.096 27.069 11.307 1.00 14.21 N ANISOU 841 ND2 ASN A 98 2258 1639 1504 31 224 -163 N ATOM 842 N LYS A 99 28.037 28.614 15.165 1.00 8.72 N ANISOU 842 N LYS A 99 1304 816 1193 283 41 151 N ATOM 843 CA LYS A 99 28.952 29.555 15.761 1.00 9.01 C ANISOU 843 CA LYS A 99 1269 867 1287 160 166 233 C ATOM 844 C LYS A 99 29.188 30.799 14.902 1.00 9.55 C ANISOU 844 C LYS A 99 1443 712 1476 427 253 299 C ATOM 845 O LYS A 99 29.290 31.910 15.419 1.00 9.97 O ANISOU 845 O LYS A 99 1192 794 1804 372 243 165 O ATOM 846 CB LYS A 99 30.280 28.888 16.151 1.00 8.25 C ANISOU 846 CB LYS A 99 1149 523 1464 181 289 172 C ATOM 847 CG LYS A 99 30.096 27.597 16.961 1.00 9.35 C ANISOU 847 CG LYS A 99 1548 747 1260 32 -45 177 C ATOM 848 CD LYS A 99 31.425 27.056 17.507 1.00 10.60 C ANISOU 848 CD LYS A 99 1621 952 1456 10 -232 338 C ATOM 849 CE LYS A 99 31.310 25.549 17.704 1.00 9.70 C ANISOU 849 CE LYS A 99 1291 846 1547 -101 -315 147 C ATOM 850 NZ LYS A 99 32.569 24.924 18.273 1.00 10.60 N ANISOU 850 NZ LYS A 99 1438 1077 1513 37 -277 278 N ATOM 851 N ALA A 100 29.263 30.626 13.588 1.00 9.58 N ANISOU 851 N ALA A 100 1496 618 1525 243 269 336 N ATOM 852 CA ALA A 100 29.466 31.729 12.673 1.00 10.93 C ANISOU 852 CA ALA A 100 1609 920 1626 511 431 606 C ATOM 853 C ALA A 100 28.236 32.634 12.640 1.00 10.50 C ANISOU 853 C ALA A 100 1602 946 1442 516 55 239 C ATOM 854 O ALA A 100 28.342 33.881 12.690 1.00 11.43 O ANISOU 854 O ALA A 100 1484 967 1893 513 292 446 O ATOM 855 CB ALA A 100 29.809 31.253 11.252 1.00 12.75 C ANISOU 855 CB ALA A 100 1885 1121 1839 445 876 588 C ATOM 856 N GLU A 101 27.049 32.047 12.549 1.00 11.50 N ANISOU 856 N GLU A 101 1622 949 1800 471 192 476 N ATOM 857 CA GLU A 101 25.789 32.779 12.518 1.00 11.19 C ANISOU 857 CA GLU A 101 1591 936 1724 407 71 518 C ATOM 858 C GLU A 101 25.594 33.564 13.807 1.00 10.70 C ANISOU 858 C GLU A 101 1496 777 1793 301 460 607 C ATOM 859 O GLU A 101 25.105 34.699 13.798 1.00 11.18 O ANISOU 859 O GLU A 101 1318 793 2136 276 149 336 O ATOM 860 CB GLU A 101 24.624 31.846 12.245 1.00 12.57 C ANISOU 860 CB GLU A 101 1650 1154 1972 224 340 409 C ATOM 861 CG GLU A 101 24.647 31.167 10.897 1.00 14.74 C ANISOU 861 CG GLU A 101 2281 1386 1934 306 -185 363 C ATOM 862 CD GLU A 101 23.589 30.093 10.762 1.00 16.70 C ANISOU 862 CD GLU A 101 2067 1894 2382 196 -150 49 C ATOM 863 OE1 GLU A 101 22.597 30.135 11.540 1.00 20.16 O ANISOU 863 OE1 GLU A 101 2059 3162 2440 36 -85 284 O ATOM 864 OE2 GLU A 101 23.815 29.214 9.890 1.00 23.25 O ANISOU 864 OE2 GLU A 101 2556 2814 3464 -161 -63 -1031 O ATOM 865 N THR A 102 26.001 32.935 14.929 1.00 10.03 N ANISOU 865 N THR A 102 1237 907 1666 220 339 360 N ATOM 866 CA THR A 102 25.853 33.564 16.229 1.00 9.45 C ANISOU 866 CA THR A 102 1106 704 1780 229 351 272 C ATOM 867 C THR A 102 26.818 34.753 16.348 1.00 8.91 C ANISOU 867 C THR A 102 855 682 1849 387 194 445 C ATOM 868 O THR A 102 26.448 35.840 16.845 1.00 10.09 O ANISOU 868 O THR A 102 1011 621 2201 292 264 313 O ATOM 869 CB THR A 102 26.057 32.550 17.369 1.00 10.08 C ANISOU 869 CB THR A 102 1280 862 1687 208 553 324 C ATOM 870 OG1 THR A 102 25.106 31.472 17.199 1.00 11.65 O ANISOU 870 OG1 THR A 102 1738 814 1875 39 642 196 O ATOM 871 CG2 THR A 102 25.854 33.152 18.745 1.00 11.28 C ANISOU 871 CG2 THR A 102 1534 959 1794 286 595 106 C ATOM 872 N ALA A 103 28.063 34.586 15.867 1.00 10.41 N ANISOU 872 N ALA A 103 975 845 2136 341 346 411 N ATOM 873 CA ALA A 103 29.026 35.682 15.888 1.00 9.98 C ANISOU 873 CA ALA A 103 910 923 1959 284 137 418 C ATOM 874 C ALA A 103 28.554 36.838 15.004 1.00 11.59 C ANISOU 874 C ALA A 103 1498 886 2018 416 146 435 C ATOM 875 O ALA A 103 28.772 38.020 15.319 1.00 11.39 O ANISOU 875 O ALA A 103 1172 852 2305 375 188 433 O ATOM 876 CB ALA A 103 30.370 35.189 15.410 1.00 11.46 C ANISOU 876 CB ALA A 103 1040 1242 2071 370 430 519 C ATOM 877 N GLU A 104 27.897 36.562 13.870 1.00 10.14 N ANISOU 877 N GLU A 104 1107 948 1799 423 417 450 N ATOM 878 CA GLU A 104 27.372 37.640 13.047 1.00 10.69 C ANISOU 878 CA GLU A 104 1041 1064 1956 337 288 494 C ATOM 879 C GLU A 104 26.262 38.380 13.795 1.00 10.24 C ANISOU 879 C GLU A 104 926 902 2064 309 174 419 C ATOM 880 O GLU A 104 26.190 39.629 13.788 1.00 11.33 O ANISOU 880 O GLU A 104 1450 875 1979 233 133 380 O ATOM 881 CB GLU A 104 26.839 37.087 11.749 1.00 11.25 C ANISOU 881 CB GLU A 104 1087 1098 2088 349 155 364 C ATOM 882 CG AGLU A 104 26.414 38.180 10.794 0.60 10.84 C ANISOU 882 CG AGLU A 104 758 1358 2003 437 406 510 C ATOM 883 CD AGLU A 104 25.984 37.721 9.428 0.60 11.50 C ANISOU 883 CD AGLU A 104 1096 1382 1892 674 525 537 C ATOM 884 OE1AGLU A 104 26.790 37.086 8.727 0.60 16.40 O ANISOU 884 OE1AGLU A 104 1333 2468 2428 1041 468 -104 O ATOM 885 OE2AGLU A 104 24.842 38.007 9.036 0.60 11.50 O ANISOU 885 OE2AGLU A 104 1104 1347 1918 670 362 -151 O ATOM 886 CG BGLU A 104 25.984 37.965 10.881 0.40 9.81 C ANISOU 886 CG BGLU A 104 872 1133 1722 390 533 462 C ATOM 887 CD BGLU A 104 25.485 37.329 9.604 0.40 10.98 C ANISOU 887 CD BGLU A 104 990 1329 1853 620 394 308 C ATOM 888 OE1BGLU A 104 25.291 36.100 9.542 0.40 16.04 O ANISOU 888 OE1BGLU A 104 2799 1405 1891 337 386 76 O ATOM 889 OE2BGLU A 104 25.286 38.077 8.624 0.40 15.74 O ANISOU 889 OE2BGLU A 104 1923 1786 2272 370 -491 580 O ATOM 890 N LYS A 105 25.333 37.660 14.442 1.00 9.40 N ANISOU 890 N LYS A 105 1024 961 1588 247 170 274 N ATOM 891 CA LYS A 105 24.147 38.281 15.022 1.00 9.37 C ANISOU 891 CA LYS A 105 986 927 1646 206 93 254 C ATOM 892 C LYS A 105 24.436 39.081 16.285 1.00 8.51 C ANISOU 892 C LYS A 105 717 852 1665 307 -5 254 C ATOM 893 O LYS A 105 23.776 40.074 16.541 1.00 9.59 O ANISOU 893 O LYS A 105 906 887 1852 348 19 188 O ATOM 894 CB ALYS A 105 23.092 37.222 15.321 0.68 12.28 C ANISOU 894 CB ALYS A 105 1203 1258 2205 -134 472 -319 C ATOM 895 CG ALYS A 105 22.368 36.744 14.082 0.68 17.05 C ANISOU 895 CG ALYS A 105 1506 1889 3083 63 -25 -1077 C ATOM 896 CD ALYS A 105 21.133 35.953 14.553 0.68 21.87 C ANISOU 896 CD ALYS A 105 1408 2205 4697 -211 -1046 313 C ATOM 897 CE ALYS A 105 20.181 36.011 13.367 0.68 28.32 C ANISOU 897 CE ALYS A 105 1950 4238 4573 -676 -1207 790 C ATOM 898 NZ ALYS A 105 20.902 35.497 12.180 0.68 34.11 N ANISOU 898 NZ ALYS A 105 2150 6428 4381 -950 -889 864 N ATOM 899 CB BLYS A 105 23.073 37.216 15.280 0.32 13.61 C ANISOU 899 CB BLYS A 105 1082 1382 2705 -179 348 -284 C ATOM 900 CG BLYS A 105 22.086 37.076 14.128 0.32 16.48 C ANISOU 900 CG BLYS A 105 1173 1764 3324 -58 -58 -393 C ATOM 901 CD BLYS A 105 22.545 36.035 13.136 0.32 21.31 C ANISOU 901 CD BLYS A 105 2224 2355 3517 -60 -316 -1040 C ATOM 902 CE BLYS A 105 21.781 34.725 13.222 0.32 24.39 C ANISOU 902 CE BLYS A 105 2862 3065 3339 -910 676 -1950 C ATOM 903 NZ BLYS A 105 22.391 33.790 14.194 0.32 23.86 N ANISOU 903 NZ BLYS A 105 2133 2162 4771 -1178 1375 -1129 N ATOM 904 N TYR A 106 25.410 38.613 17.097 1.00 9.46 N ANISOU 904 N TYR A 106 860 915 1817 343 -117 217 N ATOM 905 CA TYR A 106 25.724 39.157 18.402 1.00 10.66 C ANISOU 905 CA TYR A 106 1128 963 1958 448 -338 216 C ATOM 906 C TYR A 106 27.136 39.763 18.525 1.00 11.52 C ANISOU 906 C TYR A 106 1106 1139 2133 418 -506 142 C ATOM 907 O TYR A 106 27.436 40.354 19.562 1.00 15.39 O ANISOU 907 O TYR A 106 2041 1322 2485 291 -845 -224 O ATOM 908 CB TYR A 106 25.558 38.051 19.465 1.00 10.72 C ANISOU 908 CB TYR A 106 1117 1192 1763 633 -114 218 C ATOM 909 CG TYR A 106 24.137 37.546 19.586 1.00 11.23 C ANISOU 909 CG TYR A 106 1156 1316 1794 443 -10 75 C ATOM 910 CD1 TYR A 106 23.116 38.303 20.198 1.00 11.62 C ANISOU 910 CD1 TYR A 106 1092 1528 1797 381 -98 -198 C ATOM 911 CD2 TYR A 106 23.765 36.327 19.092 1.00 11.80 C ANISOU 911 CD2 TYR A 106 1292 1012 2181 494 362 298 C ATOM 912 CE1 TYR A 106 21.828 37.808 20.290 1.00 10.86 C ANISOU 912 CE1 TYR A 106 1170 1321 1636 326 71 -307 C ATOM 913 CE2 TYR A 106 22.490 35.820 19.174 1.00 11.07 C ANISOU 913 CE2 TYR A 106 1434 779 1994 361 437 137 C ATOM 914 CZ TYR A 106 21.498 36.562 19.772 1.00 9.70 C ANISOU 914 CZ TYR A 106 1155 985 1545 470 69 124 C ATOM 915 OH TYR A 106 20.207 36.131 19.894 1.00 10.93 O ANISOU 915 OH TYR A 106 1226 1218 1710 310 107 -29 O ATOM 916 N GLY A 107 27.974 39.607 17.502 1.00 12.59 N ANISOU 916 N GLY A 107 1278 1194 2312 -76 -271 273 N ATOM 917 CA GLY A 107 29.347 40.100 17.546 1.00 12.67 C ANISOU 917 CA GLY A 107 1397 1000 2418 -211 -347 366 C ATOM 918 C GLY A 107 30.394 39.059 17.811 1.00 14.08 C ANISOU 918 C GLY A 107 1234 1708 2408 -51 -222 1010 C ATOM 919 O GLY A 107 30.219 38.136 18.652 1.00 14.92 O ANISOU 919 O GLY A 107 926 1985 2756 -55 -116 1276 O ATOM 920 N ASP A 108 31.534 39.129 17.157 1.00 13.25 N ANISOU 920 N ASP A 108 1427 1486 2122 -132 -173 905 N ATOM 921 CA ASP A 108 32.602 38.113 17.251 1.00 13.07 C ANISOU 921 CA ASP A 108 917 1829 2221 -354 -134 726 C ATOM 922 C ASP A 108 33.170 38.107 18.649 1.00 14.14 C ANISOU 922 C ASP A 108 1231 1730 2413 -177 -338 855 C ATOM 923 O ASP A 108 33.414 37.072 19.227 1.00 16.20 O ANISOU 923 O ASP A 108 1640 2057 2459 -64 29 1261 O ATOM 924 CB AASP A 108 33.667 38.382 16.179 0.51 17.78 C ANISOU 924 CB AASP A 108 1586 2539 2629 -734 479 271 C ATOM 925 CG AASP A 108 33.793 37.635 14.880 0.51 15.58 C ANISOU 925 CG AASP A 108 1107 2143 2671 -449 176 303 C ATOM 926 OD1AASP A 108 33.324 36.484 14.699 0.51 14.28 O ANISOU 926 OD1AASP A 108 829 1989 2607 -267 -348 672 O ATOM 927 OD2AASP A 108 34.433 38.161 13.909 0.51 16.33 O ANISOU 927 OD2AASP A 108 2447 1206 2551 -143 375 314 O ATOM 928 CB BASP A 108 33.676 38.416 16.200 0.49 18.14 C ANISOU 928 CB BASP A 108 1691 2539 2664 -699 572 350 C ATOM 929 CG BASP A 108 34.510 37.202 15.846 0.49 18.62 C ANISOU 929 CG BASP A 108 1435 3014 2627 -402 460 424 C ATOM 930 OD1BASP A 108 33.959 36.168 15.404 0.49 21.36 O ANISOU 930 OD1BASP A 108 1856 2517 3744 -224 561 288 O ATOM 931 OD2BASP A 108 35.745 37.290 16.004 0.49 32.82 O ANISOU 931 OD2BASP A 108 1563 5634 5273 35 -350 -1284 O ATOM 932 N GLU A 109 33.376 39.298 19.250 1.00 14.15 N ANISOU 932 N GLU A 109 1237 2053 2087 -72 -133 558 N ATOM 933 CA GLU A 109 33.978 39.350 20.599 1.00 16.74 C ANISOU 933 CA GLU A 109 1154 2804 2403 -464 -431 707 C ATOM 934 C GLU A 109 33.015 38.761 21.619 1.00 13.75 C ANISOU 934 C GLU A 109 1138 2246 1842 20 -380 379 C ATOM 935 O GLU A 109 33.435 37.982 22.517 1.00 17.53 O ANISOU 935 O GLU A 109 998 3207 2456 45 -445 1095 O ATOM 936 CB GLU A 109 34.421 40.781 20.960 1.00 23.75 C ANISOU 936 CB GLU A 109 2474 3443 3108 -1516 -781 428 C ATOM 937 CG GLU A 109 35.058 40.819 22.356 1.00 27.64 C ANISOU 937 CG GLU A 109 3450 3470 3581 -1588 -1531 786 C ATOM 938 CD GLU A 109 36.312 39.951 22.463 1.00 33.39 C ANISOU 938 CD GLU A 109 3158 4421 5106 -1604 -1344 2325 C ATOM 939 OE1 GLU A 109 37.019 39.749 21.438 1.00 39.94 O ANISOU 939 OE1 GLU A 109 2498 7179 5501 -865 -1837 595 O ATOM 940 OE2 GLU A 109 36.621 39.454 23.585 1.00 41.98 O ANISOU 940 OE2 GLU A 109 4894 5081 5977 -1576 -2281 3004 O ATOM 941 N GLN A 110 31.724 39.082 21.537 1.00 15.90 N ANISOU 941 N GLN A 110 1236 2487 2317 191 -183 1132 N ATOM 942 CA GLN A 110 30.720 38.458 22.402 1.00 16.62 C ANISOU 942 CA GLN A 110 1278 2740 2296 429 38 1250 C ATOM 943 C GLN A 110 30.747 36.938 22.294 1.00 16.01 C ANISOU 943 C GLN A 110 913 2697 2471 552 154 1505 C ATOM 944 O GLN A 110 30.672 36.190 23.277 1.00 17.58 O ANISOU 944 O GLN A 110 1303 2931 2446 350 191 1553 O ATOM 945 CB GLN A 110 29.320 39.013 22.086 1.00 16.10 C ANISOU 945 CB GLN A 110 1279 2176 2664 274 -107 1361 C ATOM 946 CG GLN A 110 28.242 38.368 22.971 1.00 16.43 C ANISOU 946 CG GLN A 110 1262 2397 2583 340 -28 1305 C ATOM 947 CD GLN A 110 28.437 38.742 24.438 1.00 18.58 C ANISOU 947 CD GLN A 110 1455 3003 2601 526 -69 1288 C ATOM 948 OE1 GLN A 110 28.105 39.863 24.862 1.00 21.08 O ANISOU 948 OE1 GLN A 110 2218 3244 2548 707 79 1032 O ATOM 949 NE2 GLN A 110 28.973 37.843 25.264 1.00 19.70 N ANISOU 949 NE2 GLN A 110 1380 3281 2825 328 -571 1320 N ATOM 950 N VAL A 111 30.881 36.413 21.068 1.00 15.85 N ANISOU 950 N VAL A 111 1082 2459 2481 215 78 1444 N ATOM 951 CA VAL A 111 30.930 34.938 20.959 1.00 15.74 C ANISOU 951 CA VAL A 111 1001 2387 2593 353 1 1686 C ATOM 952 C VAL A 111 32.209 34.427 21.612 1.00 18.02 C ANISOU 952 C VAL A 111 967 2845 3036 63 -226 2184 C ATOM 953 O VAL A 111 32.188 33.376 22.238 1.00 21.34 O ANISOU 953 O VAL A 111 1280 3197 3629 99 -359 2667 O ATOM 954 CB VAL A 111 30.674 34.470 19.518 1.00 15.53 C ANISOU 954 CB VAL A 111 1222 1979 2701 -73 -156 1725 C ATOM 955 CG1 VAL A 111 31.027 33.000 19.291 1.00 16.88 C ANISOU 955 CG1 VAL A 111 1495 1878 3039 -216 -197 1745 C ATOM 956 CG2 VAL A 111 29.200 34.634 19.115 1.00 16.93 C ANISOU 956 CG2 VAL A 111 1071 2555 2805 -97 8 1489 C ATOM 957 N LYS A 112 33.328 35.136 21.484 1.00 18.34 N ANISOU 957 N LYS A 112 914 2801 3253 119 106 1701 N ATOM 958 CA LYS A 112 34.591 34.639 22.048 1.00 17.90 C ANISOU 958 CA LYS A 112 987 2555 3261 -67 -120 1582 C ATOM 959 C LYS A 112 34.455 34.533 23.546 1.00 19.46 C ANISOU 959 C LYS A 112 1341 2712 3342 166 -159 1713 C ATOM 960 O LYS A 112 34.965 33.594 24.193 1.00 20.86 O ANISOU 960 O LYS A 112 1404 3085 3435 491 100 1962 O ATOM 961 CB LYS A 112 35.716 35.564 21.587 1.00 18.33 C ANISOU 961 CB LYS A 112 1006 2390 3567 -95 21 1245 C ATOM 962 CG LYS A 112 36.290 35.161 20.250 1.00 31.48 C ANISOU 962 CG LYS A 112 2691 5378 3891 109 1202 1473 C ATOM 963 CD LYS A 112 36.221 36.116 19.110 1.00 41.99 C ANISOU 963 CD LYS A 112 5056 6386 4514 1091 2340 2268 C ATOM 964 CE LYS A 112 37.210 35.790 17.990 1.00 43.76 C ANISOU 964 CE LYS A 112 4948 6580 5098 1414 2745 2858 C ATOM 965 NZ LYS A 112 38.439 36.633 18.085 1.00 51.37 N ANISOU 965 NZ LYS A 112 5632 7492 6395 636 3181 2345 N ATOM 966 N GLN A 113 33.749 35.516 24.116 1.00 17.37 N ANISOU 966 N GLN A 113 992 2751 2858 141 -327 1866 N ATOM 967 CA GLN A 113 33.531 35.507 25.560 1.00 20.86 C ANISOU 967 CA GLN A 113 1700 3335 2892 4 -51 1977 C ATOM 968 C GLN A 113 32.615 34.372 25.977 1.00 20.07 C ANISOU 968 C GLN A 113 1642 3178 2804 126 -52 1883 C ATOM 969 O GLN A 113 32.828 33.670 26.981 1.00 19.22 O ANISOU 969 O GLN A 113 1113 3280 2909 280 42 2020 O ATOM 970 CB GLN A 113 32.904 36.820 26.035 1.00 20.66 C ANISOU 970 CB GLN A 113 1825 3315 2709 -347 -394 1411 C ATOM 971 CG GLN A 113 33.947 37.951 26.040 1.00 23.98 C ANISOU 971 CG GLN A 113 2566 4119 2424 -1128 -637 1053 C ATOM 972 CD GLN A 113 35.066 37.633 27.020 1.00 26.98 C ANISOU 972 CD GLN A 113 2167 4078 4007 64 -1004 68 C ATOM 973 OE1 GLN A 113 36.222 37.456 26.628 1.00 49.84 O ANISOU 973 OE1 GLN A 113 1531 8499 8905 -1136 -709 -1842 O ATOM 974 NE2 GLN A 113 34.765 37.531 28.307 1.00 36.44 N ANISOU 974 NE2 GLN A 113 4090 6118 3637 -1603 -2226 2216 N ATOM 975 N TRP A 114 31.547 34.156 25.194 1.00 21.56 N ANISOU 975 N TRP A 114 1274 3207 3711 342 -361 2481 N ATOM 976 CA TRP A 114 30.673 33.038 25.524 1.00 20.91 C ANISOU 976 CA TRP A 114 1087 2951 3905 548 -113 2233 C ATOM 977 C TRP A 114 31.422 31.696 25.358 1.00 22.50 C ANISOU 977 C TRP A 114 1313 3195 4041 879 387 2663 C ATOM 978 O TRP A 114 31.048 30.724 26.053 1.00 28.35 O ANISOU 978 O TRP A 114 1787 3607 5378 1337 1086 3427 O ATOM 979 CB TRP A 114 29.470 33.075 24.626 1.00 18.05 C ANISOU 979 CB TRP A 114 1140 2578 3141 597 116 1800 C ATOM 980 CG TRP A 114 28.401 34.070 24.964 1.00 15.29 C ANISOU 980 CG TRP A 114 1171 1767 2872 292 -239 1286 C ATOM 981 CD1 TRP A 114 28.177 34.628 26.191 1.00 17.37 C ANISOU 981 CD1 TRP A 114 969 3029 2603 240 -373 1245 C ATOM 982 CD2 TRP A 114 27.407 34.613 24.101 1.00 12.96 C ANISOU 982 CD2 TRP A 114 774 1902 2250 194 118 1051 C ATOM 983 NE1 TRP A 114 27.109 35.490 26.132 1.00 15.92 N ANISOU 983 NE1 TRP A 114 1228 2927 1894 399 -53 1161 N ATOM 984 CE2 TRP A 114 26.610 35.501 24.856 1.00 12.62 C ANISOU 984 CE2 TRP A 114 1039 1859 1897 222 -92 903 C ATOM 985 CE3 TRP A 114 27.104 34.429 22.746 1.00 12.13 C ANISOU 985 CE3 TRP A 114 1041 1303 2264 488 171 798 C ATOM 986 CZ2 TRP A 114 25.551 36.196 24.283 1.00 13.20 C ANISOU 986 CZ2 TRP A 114 1246 1863 1908 426 -92 801 C ATOM 987 CZ3 TRP A 114 26.036 35.136 22.197 1.00 11.08 C ANISOU 987 CZ3 TRP A 114 991 956 2262 253 1 698 C ATOM 988 CH2 TRP A 114 25.279 35.986 22.960 1.00 10.56 C ANISOU 988 CH2 TRP A 114 1027 938 2049 318 -259 603 C ATOM 989 N ARG A 115 32.390 31.601 24.472 1.00 22.86 N ANISOU 989 N ARG A 115 997 3647 4044 776 241 2545 N ATOM 990 CA ARG A 115 33.132 30.334 24.279 1.00 19.16 C ANISOU 990 CA ARG A 115 738 3337 3206 404 -127 2174 C ATOM 991 C ARG A 115 34.134 30.095 25.383 1.00 19.32 C ANISOU 991 C ARG A 115 1080 3181 3078 458 -178 2017 C ATOM 992 O ARG A 115 34.372 28.982 25.842 1.00 20.57 O ANISOU 992 O ARG A 115 1261 3384 3172 573 52 2402 O ATOM 993 CB ARG A 115 33.868 30.329 22.913 1.00 19.37 C ANISOU 993 CB ARG A 115 1097 3316 2947 -422 -261 1577 C ATOM 994 CG ARG A 115 33.019 30.104 21.672 1.00 20.52 C ANISOU 994 CG ARG A 115 991 3370 3438 -214 -679 1491 C ATOM 995 CD ARG A 115 33.770 30.135 20.367 1.00 18.52 C ANISOU 995 CD ARG A 115 1343 2558 3135 -299 -882 455 C ATOM 996 NE ARG A 115 34.869 29.168 20.146 1.00 24.71 N ANISOU 996 NE ARG A 115 3426 2619 3343 1049 -173 1353 N ATOM 997 CZ ARG A 115 35.721 29.180 19.098 1.00 23.40 C ANISOU 997 CZ ARG A 115 4364 972 3553 339 431 0 C ATOM 998 NH1 ARG A 115 35.702 30.056 18.073 1.00 20.84 N ANISOU 998 NH1 ARG A 115 2288 2385 3247 -2 -49 431 N ATOM 999 NH2 ARG A 115 36.713 28.278 18.968 1.00 23.75 N ANISOU 999 NH2 ARG A 115 4502 1819 2704 777 -380 -547 N ATOM 1000 N ARG A 116 34.839 31.127 25.805 1.00 19.39 N ANISOU 1000 N ARG A 116 1102 3236 3029 673 -134 1472 N ATOM 1001 CA ARG A 116 36.091 31.021 26.522 1.00 18.50 C ANISOU 1001 CA ARG A 116 1096 3210 2726 717 -20 1374 C ATOM 1002 C ARG A 116 36.246 31.880 27.755 1.00 20.31 C ANISOU 1002 C ARG A 116 1088 4019 2608 935 87 1146 C ATOM 1003 O ARG A 116 37.235 31.659 28.470 1.00 23.84 O ANISOU 1003 O ARG A 116 1442 5456 2158 1333 23 1335 O ATOM 1004 CB ARG A 116 37.220 31.494 25.586 1.00 16.08 C ANISOU 1004 CB ARG A 116 1252 2316 2542 130 -57 419 C ATOM 1005 CG ARG A 116 37.668 30.520 24.533 1.00 20.30 C ANISOU 1005 CG ARG A 116 2019 1872 3821 114 802 272 C ATOM 1006 CD ARG A 116 38.642 29.664 25.422 1.00 27.51 C ANISOU 1006 CD ARG A 116 3593 2516 4343 1184 -300 -579 C ATOM 1007 NE ARG A 116 38.531 28.364 24.878 1.00 22.38 N ANISOU 1007 NE ARG A 116 3244 2956 2305 1617 -1010 -679 N ATOM 1008 CZ ARG A 116 39.465 27.481 24.631 1.00 14.08 C ANISOU 1008 CZ ARG A 116 2080 2061 1210 470 -306 -108 C ATOM 1009 NH1 ARG A 116 40.746 27.699 24.891 1.00 14.62 N ANISOU 1009 NH1 ARG A 116 2326 1224 2006 -151 -332 188 N ATOM 1010 NH2 ARG A 116 39.070 26.344 24.128 1.00 13.96 N ANISOU 1010 NH2 ARG A 116 1664 1832 1809 -7 -158 267 N ATOM 1011 N GLY A 117 35.405 32.871 27.997 1.00 20.78 N ANISOU 1011 N GLY A 117 1697 3817 2383 1063 390 1387 N ATOM 1012 CA GLY A 117 35.634 33.707 29.167 1.00 20.21 C ANISOU 1012 CA GLY A 117 1910 3355 2413 826 213 1581 C ATOM 1013 C GLY A 117 35.587 32.894 30.446 1.00 17.71 C ANISOU 1013 C GLY A 117 1776 2467 2484 530 -150 1335 C ATOM 1014 O GLY A 117 34.647 32.134 30.670 1.00 17.89 O ANISOU 1014 O GLY A 117 1833 2595 2368 407 -132 1153 O ATOM 1015 N PHE A 118 36.548 32.986 31.352 1.00 13.59 N ANISOU 1015 N PHE A 118 1810 1584 1770 612 276 609 N ATOM 1016 CA PHE A 118 36.800 32.014 32.397 1.00 12.00 C ANISOU 1016 CA PHE A 118 1456 1473 1630 158 -44 531 C ATOM 1017 C PHE A 118 35.559 31.756 33.261 1.00 10.78 C ANISOU 1017 C PHE A 118 1419 1090 1588 214 -90 373 C ATOM 1018 O PHE A 118 35.144 30.613 33.470 1.00 10.04 O ANISOU 1018 O PHE A 118 1113 1121 1578 78 -322 166 O ATOM 1019 CB PHE A 118 37.987 32.426 33.296 1.00 13.95 C ANISOU 1019 CB PHE A 118 1572 1117 2611 -34 -351 485 C ATOM 1020 CG PHE A 118 38.292 31.391 34.396 1.00 12.32 C ANISOU 1020 CG PHE A 118 1438 1040 2202 -70 -659 121 C ATOM 1021 CD1 PHE A 118 38.937 30.196 34.047 1.00 11.64 C ANISOU 1021 CD1 PHE A 118 1482 864 2076 -199 -663 17 C ATOM 1022 CD2 PHE A 118 37.921 31.585 35.703 1.00 11.96 C ANISOU 1022 CD2 PHE A 118 1430 797 2319 8 -587 -5 C ATOM 1023 CE1 PHE A 118 39.196 29.251 35.020 1.00 12.24 C ANISOU 1023 CE1 PHE A 118 1509 1163 1978 -1 -761 36 C ATOM 1024 CE2 PHE A 118 38.187 30.643 36.679 1.00 12.10 C ANISOU 1024 CE2 PHE A 118 1285 1037 2277 -65 -379 158 C ATOM 1025 CZ PHE A 118 38.795 29.428 36.332 1.00 11.19 C ANISOU 1025 CZ PHE A 118 1418 756 2077 -249 -718 16 C ATOM 1026 N ALA A 119 34.987 32.850 33.793 1.00 11.59 N ANISOU 1026 N ALA A 119 1613 1167 1622 102 -307 -129 N ATOM 1027 CA ALA A 119 33.805 32.784 34.652 1.00 12.46 C ANISOU 1027 CA ALA A 119 1556 1479 1699 238 -349 -253 C ATOM 1028 C ALA A 119 32.544 33.272 33.925 1.00 11.86 C ANISOU 1028 C ALA A 119 1658 1040 1807 211 -407 -153 C ATOM 1029 O ALA A 119 31.508 33.395 34.583 1.00 15.15 O ANISOU 1029 O ALA A 119 1729 2023 2005 609 -332 -227 O ATOM 1030 CB ALA A 119 33.976 33.530 35.983 1.00 14.25 C ANISOU 1030 CB ALA A 119 1513 2162 1739 292 -344 -441 C ATOM 1031 N VAL A 120 32.616 33.522 32.626 1.00 14.55 N ANISOU 1031 N VAL A 120 1418 2077 2033 436 -409 324 N ATOM 1032 CA VAL A 120 31.500 33.975 31.806 1.00 14.01 C ANISOU 1032 CA VAL A 120 1155 2114 2053 308 -131 696 C ATOM 1033 C VAL A 120 30.572 32.789 31.505 1.00 13.88 C ANISOU 1033 C VAL A 120 1378 2131 1766 437 -376 337 C ATOM 1034 O VAL A 120 31.006 31.723 31.100 1.00 14.28 O ANISOU 1034 O VAL A 120 1567 2365 1494 423 34 269 O ATOM 1035 CB VAL A 120 31.994 34.616 30.511 1.00 17.45 C ANISOU 1035 CB VAL A 120 1220 3255 2154 539 110 1047 C ATOM 1036 CG1 VAL A 120 30.831 34.972 29.586 1.00 20.56 C ANISOU 1036 CG1 VAL A 120 1749 3822 2242 1315 -11 1095 C ATOM 1037 CG2 VAL A 120 32.832 35.859 30.833 1.00 22.78 C ANISOU 1037 CG2 VAL A 120 1449 3804 3403 -255 753 1414 C ATOM 1038 N THR A 121 29.272 33.002 31.715 1.00 14.10 N ANISOU 1038 N THR A 121 1279 2019 2060 337 -333 319 N ATOM 1039 CA THR A 121 28.300 31.992 31.364 1.00 12.67 C ANISOU 1039 CA THR A 121 1363 1944 1508 438 -146 197 C ATOM 1040 C THR A 121 27.566 32.343 30.076 1.00 11.53 C ANISOU 1040 C THR A 121 1472 1359 1550 451 -189 182 C ATOM 1041 O THR A 121 27.118 33.463 29.889 1.00 12.16 O ANISOU 1041 O THR A 121 1575 1301 1743 306 -393 24 O ATOM 1042 CB THR A 121 27.258 31.794 32.484 1.00 12.99 C ANISOU 1042 CB THR A 121 1273 2101 1562 506 -116 81 C ATOM 1043 OG1 THR A 121 26.737 33.086 32.894 1.00 15.81 O ANISOU 1043 OG1 THR A 121 1496 2235 2277 801 67 13 O ATOM 1044 CG2 THR A 121 27.895 31.083 33.668 1.00 14.64 C ANISOU 1044 CG2 THR A 121 2163 1764 1636 196 -303 282 C ATOM 1045 N PRO A 122 27.382 31.388 29.163 1.00 10.22 N ANISOU 1045 N PRO A 122 1318 1212 1352 447 28 291 N ATOM 1046 CA PRO A 122 26.464 31.617 28.034 1.00 9.71 C ANISOU 1046 CA PRO A 122 1160 864 1666 35 -106 218 C ATOM 1047 C PRO A 122 25.084 31.976 28.515 1.00 9.61 C ANISOU 1047 C PRO A 122 1321 760 1571 249 -94 233 C ATOM 1048 O PRO A 122 24.744 31.669 29.666 1.00 10.62 O ANISOU 1048 O PRO A 122 1463 872 1698 353 60 261 O ATOM 1049 CB PRO A 122 26.503 30.252 27.327 1.00 11.38 C ANISOU 1049 CB PRO A 122 1591 1170 1561 369 42 38 C ATOM 1050 CG PRO A 122 27.863 29.701 27.643 1.00 11.13 C ANISOU 1050 CG PRO A 122 1341 851 2038 85 93 121 C ATOM 1051 CD PRO A 122 28.051 30.056 29.106 1.00 10.82 C ANISOU 1051 CD PRO A 122 1256 947 1908 122 16 468 C ATOM 1052 N PRO A 123 24.263 32.619 27.703 1.00 10.10 N ANISOU 1052 N PRO A 123 1428 868 1541 292 -171 51 N ATOM 1053 CA PRO A 123 22.874 32.938 28.067 1.00 10.28 C ANISOU 1053 CA PRO A 123 1300 907 1700 206 -245 -3 C ATOM 1054 C PRO A 123 22.150 31.677 28.549 1.00 10.38 C ANISOU 1054 C PRO A 123 1249 841 1855 278 -202 -28 C ATOM 1055 O PRO A 123 22.326 30.576 27.989 1.00 10.48 O ANISOU 1055 O PRO A 123 1502 825 1652 326 -181 88 O ATOM 1056 CB PRO A 123 22.275 33.536 26.789 1.00 11.77 C ANISOU 1056 CB PRO A 123 1608 1021 1841 269 -479 10 C ATOM 1057 CG PRO A 123 23.515 34.065 26.071 1.00 14.99 C ANISOU 1057 CG PRO A 123 1772 1796 2128 554 -225 631 C ATOM 1058 CD PRO A 123 24.601 33.058 26.332 1.00 12.13 C ANISOU 1058 CD PRO A 123 1887 1084 1639 497 0 402 C ATOM 1059 N GLU A 124 21.319 31.812 29.573 1.00 9.57 N ANISOU 1059 N GLU A 124 1173 574 1889 121 -293 -53 N ATOM 1060 CA GLU A 124 20.698 30.700 30.284 1.00 10.33 C ANISOU 1060 CA GLU A 124 1217 735 1974 66 -344 186 C ATOM 1061 C GLU A 124 19.460 30.150 29.599 1.00 9.07 C ANISOU 1061 C GLU A 124 1070 832 1546 104 -106 150 C ATOM 1062 O GLU A 124 18.643 30.902 29.001 1.00 11.09 O ANISOU 1062 O GLU A 124 1271 1070 1871 310 -362 51 O ATOM 1063 CB GLU A 124 20.253 31.124 31.684 1.00 14.93 C ANISOU 1063 CB GLU A 124 1906 2021 1746 -609 -371 50 C ATOM 1064 CG GLU A 124 21.164 31.534 32.770 1.00 16.96 C ANISOU 1064 CG GLU A 124 2252 1833 2358 -237 -898 -150 C ATOM 1065 CD GLU A 124 20.550 31.708 34.150 1.00 22.87 C ANISOU 1065 CD GLU A 124 3118 3074 2498 46 -783 -1327 C ATOM 1066 OE1 GLU A 124 19.348 31.974 34.351 1.00 21.68 O ANISOU 1066 OE1 GLU A 124 3311 2324 2603 352 -535 -678 O ATOM 1067 OE2 GLU A 124 21.337 31.565 35.120 1.00 29.04 O ANISOU 1067 OE2 GLU A 124 3736 4900 2396 1053 -661 -166 O ATOM 1068 N LEU A 125 19.242 28.843 29.685 1.00 8.46 N ANISOU 1068 N LEU A 125 998 812 1405 125 6 23 N ATOM 1069 CA LEU A 125 17.975 28.188 29.486 1.00 8.29 C ANISOU 1069 CA LEU A 125 985 726 1440 220 -56 90 C ATOM 1070 C LEU A 125 16.999 28.543 30.616 1.00 9.17 C ANISOU 1070 C LEU A 125 957 1016 1511 216 -32 -89 C ATOM 1071 O LEU A 125 17.421 28.941 31.709 1.00 10.05 O ANISOU 1071 O LEU A 125 1157 1217 1443 381 -133 -105 O ATOM 1072 CB LEU A 125 18.119 26.653 29.517 1.00 8.23 C ANISOU 1072 CB LEU A 125 1113 768 1246 82 -38 -45 C ATOM 1073 CG LEU A 125 19.016 25.982 28.471 1.00 8.57 C ANISOU 1073 CG LEU A 125 1169 804 1285 256 122 143 C ATOM 1074 CD1 LEU A 125 18.974 24.468 28.685 1.00 8.99 C ANISOU 1074 CD1 LEU A 125 1176 769 1469 260 292 137 C ATOM 1075 CD2 LEU A 125 18.571 26.328 27.059 1.00 8.99 C ANISOU 1075 CD2 LEU A 125 969 1140 1306 322 105 190 C ATOM 1076 N THR A 126 15.720 28.322 30.367 1.00 8.98 N ANISOU 1076 N THR A 126 1056 1035 1321 167 51 67 N ATOM 1077 CA THR A 126 14.707 28.162 31.391 1.00 8.98 C ANISOU 1077 CA THR A 126 1104 910 1398 261 172 118 C ATOM 1078 C THR A 126 14.345 26.667 31.505 1.00 9.05 C ANISOU 1078 C THR A 126 1185 970 1284 100 -25 41 C ATOM 1079 O THR A 126 14.619 25.862 30.592 1.00 10.40 O ANISOU 1079 O THR A 126 1364 1069 1518 161 72 -77 O ATOM 1080 CB ATHR A 126 13.435 29.020 31.216 0.81 9.78 C ANISOU 1080 CB ATHR A 126 1283 1174 1259 434 85 -141 C ATOM 1081 OG1ATHR A 126 12.880 28.602 29.957 0.81 10.04 O ANISOU 1081 OG1ATHR A 126 1379 1144 1290 405 4 24 O ATOM 1082 CG2ATHR A 126 13.771 30.495 31.198 0.81 12.69 C ANISOU 1082 CG2ATHR A 126 1963 1049 1809 601 181 -358 C ATOM 1083 CB BTHR A 126 13.513 29.061 31.029 0.19 10.56 C ANISOU 1083 CB BTHR A 126 1330 1135 1547 580 -123 -443 C ATOM 1084 OG1BTHR A 126 13.989 30.420 31.013 0.19 15.29 O ANISOU 1084 OG1BTHR A 126 1581 1141 3088 578 -23 377 O ATOM 1085 CG2BTHR A 126 12.391 29.013 32.040 0.19 15.83 C ANISOU 1085 CG2BTHR A 126 1272 1549 3193 226 579 -787 C ATOM 1086 N LYS A 127 13.736 26.247 32.623 1.00 9.68 N ANISOU 1086 N LYS A 127 1256 987 1434 75 49 86 N ATOM 1087 CA LYS A 127 13.465 24.842 32.906 1.00 8.96 C ANISOU 1087 CA LYS A 127 1071 952 1382 270 228 59 C ATOM 1088 C LYS A 127 12.431 24.221 31.972 1.00 9.07 C ANISOU 1088 C LYS A 127 948 1030 1467 300 232 -59 C ATOM 1089 O LYS A 127 12.376 22.978 31.838 1.00 10.77 O ANISOU 1089 O LYS A 127 1309 1054 1731 269 -38 3 O ATOM 1090 CB LYS A 127 13.080 24.728 34.370 1.00 10.02 C ANISOU 1090 CB LYS A 127 1414 994 1401 175 265 4 C ATOM 1091 CG LYS A 127 14.195 25.024 35.348 1.00 11.45 C ANISOU 1091 CG LYS A 127 1658 1263 1429 473 -51 -21 C ATOM 1092 CD LYS A 127 13.915 24.683 36.797 1.00 15.03 C ANISOU 1092 CD LYS A 127 2450 1868 1393 271 158 -245 C ATOM 1093 CE LYS A 127 12.886 25.667 37.310 1.00 17.24 C ANISOU 1093 CE LYS A 127 2706 2263 1583 533 381 -48 C ATOM 1094 NZ LYS A 127 12.675 25.443 38.787 1.00 18.85 N ANISOU 1094 NZ LYS A 127 3402 2119 1642 -71 860 -320 N ATOM 1095 N ASP A 128 11.597 25.035 31.321 1.00 8.78 N ANISOU 1095 N ASP A 128 1055 857 1423 197 195 -51 N ATOM 1096 CA ASP A 128 10.618 24.539 30.369 1.00 8.79 C ANISOU 1096 CA ASP A 128 990 932 1417 142 200 59 C ATOM 1097 C ASP A 128 11.230 24.236 28.997 1.00 9.06 C ANISOU 1097 C ASP A 128 1023 1104 1315 159 140 54 C ATOM 1098 O ASP A 128 10.636 23.515 28.189 1.00 10.28 O ANISOU 1098 O ASP A 128 1097 1422 1389 84 -6 1 O ATOM 1099 CB ASP A 128 9.437 25.521 30.150 1.00 10.72 C ANISOU 1099 CB ASP A 128 1158 1280 1634 433 163 -57 C ATOM 1100 CG ASP A 128 9.959 26.779 29.511 1.00 10.26 C ANISOU 1100 CG ASP A 128 1095 1235 1568 509 -62 19 C ATOM 1101 OD1 ASP A 128 10.564 27.572 30.287 1.00 11.45 O ANISOU 1101 OD1 ASP A 128 1131 1469 1748 328 -123 -85 O ATOM 1102 OD2 ASP A 128 9.764 26.965 28.276 1.00 11.07 O ANISOU 1102 OD2 ASP A 128 1150 1383 1672 212 -147 34 O ATOM 1103 N ASP A 129 12.415 24.741 28.707 1.00 8.34 N ANISOU 1103 N ASP A 129 973 909 1285 205 101 36 N ATOM 1104 CA ASP A 129 13.063 24.531 27.405 1.00 8.23 C ANISOU 1104 CA ASP A 129 1107 801 1220 175 128 89 C ATOM 1105 C ASP A 129 13.208 23.037 27.164 1.00 7.93 C ANISOU 1105 C ASP A 129 886 871 1257 294 -17 27 C ATOM 1106 O ASP A 129 13.568 22.291 28.066 1.00 8.64 O ANISOU 1106 O ASP A 129 1007 937 1340 255 -70 28 O ATOM 1107 CB ASP A 129 14.388 25.253 27.348 1.00 8.43 C ANISOU 1107 CB ASP A 129 1082 899 1223 148 11 137 C ATOM 1108 CG ASP A 129 15.002 25.424 25.982 1.00 8.24 C ANISOU 1108 CG ASP A 129 891 885 1354 126 77 37 C ATOM 1109 OD1 ASP A 129 15.281 24.410 25.311 1.00 9.14 O ANISOU 1109 OD1 ASP A 129 1188 840 1447 311 110 121 O ATOM 1110 OD2 ASP A 129 15.254 26.611 25.590 1.00 8.66 O ANISOU 1110 OD2 ASP A 129 1114 847 1327 161 161 107 O ATOM 1111 N GLU A 130 12.976 22.572 25.924 1.00 7.71 N ANISOU 1111 N GLU A 130 790 833 1307 268 -95 19 N ATOM 1112 CA GLU A 130 13.167 21.214 25.552 1.00 9.41 C ANISOU 1112 CA GLU A 130 931 865 1778 326 -115 -131 C ATOM 1113 C GLU A 130 14.580 20.703 25.901 1.00 9.53 C ANISOU 1113 C GLU A 130 911 863 1848 352 9 -136 C ATOM 1114 O GLU A 130 14.749 19.503 26.122 1.00 9.68 O ANISOU 1114 O GLU A 130 1221 814 1644 273 -196 -67 O ATOM 1115 CB GLU A 130 12.901 21.007 24.063 1.00 19.04 C ANISOU 1115 CB GLU A 130 2968 1861 2405 961 -1307 -1065 C ATOM 1116 CG GLU A 130 11.501 21.110 23.515 1.00 32.68 C ANISOU 1116 CG GLU A 130 3282 5729 3406 950 -1944 -1306 C ATOM 1117 CD GLU A 130 11.416 20.763 22.032 1.00 38.65 C ANISOU 1117 CD GLU A 130 4108 6931 3645 797 -2260 -2005 C ATOM 1118 OE1 GLU A 130 12.476 20.441 21.443 1.00 41.56 O ANISOU 1118 OE1 GLU A 130 5616 4844 5331 267 -659 -3391 O ATOM 1119 OE2 GLU A 130 10.275 20.829 21.531 1.00 54.52 O ANISOU 1119 OE2 GLU A 130 5058 10273 5384 16 -3669 -2353 O ATOM 1120 N ARG A 131 15.553 21.626 25.914 1.00 8.31 N ANISOU 1120 N ARG A 131 942 979 1236 230 -54 -165 N ATOM 1121 CA ARG A 131 16.953 21.274 26.141 1.00 8.05 C ANISOU 1121 CA ARG A 131 912 995 1150 309 0 -4 C ATOM 1122 C ARG A 131 17.326 21.175 27.610 1.00 7.47 C ANISOU 1122 C ARG A 131 976 728 1134 257 38 87 C ATOM 1123 O ARG A 131 18.444 20.785 27.959 1.00 8.69 O ANISOU 1123 O ARG A 131 886 1146 1268 252 -9 123 O ATOM 1124 CB ARG A 131 17.846 22.313 25.435 1.00 8.67 C ANISOU 1124 CB ARG A 131 912 1179 1201 458 140 200 C ATOM 1125 CG ARG A 131 17.650 22.415 23.942 1.00 8.71 C ANISOU 1125 CG ARG A 131 1254 886 1169 406 203 14 C ATOM 1126 CD ARG A 131 18.380 23.565 23.305 1.00 9.31 C ANISOU 1126 CD ARG A 131 1313 993 1231 490 110 209 C ATOM 1127 NE ARG A 131 17.753 24.832 23.698 1.00 8.41 N ANISOU 1127 NE ARG A 131 1014 959 1221 391 15 248 N ATOM 1128 CZ ARG A 131 18.152 26.036 23.380 1.00 8.73 C ANISOU 1128 CZ ARG A 131 1048 948 1319 327 183 323 C ATOM 1129 NH1 ARG A 131 19.236 26.165 22.637 1.00 9.75 N ANISOU 1129 NH1 ARG A 131 1084 1260 1359 292 149 246 N ATOM 1130 NH2 ARG A 131 17.463 27.095 23.782 1.00 9.07 N ANISOU 1130 NH2 ARG A 131 1084 964 1400 243 78 156 N ATOM 1131 N TYR A 132 16.436 21.536 28.536 1.00 7.48 N ANISOU 1131 N TYR A 132 997 645 1201 314 22 82 N ATOM 1132 CA TYR A 132 16.778 21.531 29.973 1.00 7.47 C ANISOU 1132 CA TYR A 132 955 726 1156 230 135 109 C ATOM 1133 C TYR A 132 17.202 20.123 30.403 1.00 6.50 C ANISOU 1133 C TYR A 132 643 661 1167 145 125 4 C ATOM 1134 O TYR A 132 16.413 19.176 30.166 1.00 8.05 O ANISOU 1134 O TYR A 132 949 707 1404 27 -119 109 O ATOM 1135 CB TYR A 132 15.634 21.990 30.834 1.00 8.19 C ANISOU 1135 CB TYR A 132 874 923 1314 292 68 -42 C ATOM 1136 CG TYR A 132 15.897 22.005 32.310 1.00 8.41 C ANISOU 1136 CG TYR A 132 969 953 1274 322 211 -7 C ATOM 1137 CD1 TYR A 132 16.984 22.664 32.866 1.00 9.09 C ANISOU 1137 CD1 TYR A 132 1180 872 1403 303 -92 -24 C ATOM 1138 CD2 TYR A 132 15.035 21.370 33.201 1.00 8.92 C ANISOU 1138 CD2 TYR A 132 1017 1119 1254 354 274 -137 C ATOM 1139 CE1 TYR A 132 17.205 22.671 34.213 1.00 9.87 C ANISOU 1139 CE1 TYR A 132 1528 720 1502 441 -186 64 C ATOM 1140 CE2 TYR A 132 15.255 21.407 34.567 1.00 10.31 C ANISOU 1140 CE2 TYR A 132 1446 1293 1178 379 363 -290 C ATOM 1141 CZ TYR A 132 16.344 22.048 35.087 1.00 9.98 C ANISOU 1141 CZ TYR A 132 1832 671 1288 439 -117 -51 C ATOM 1142 OH TYR A 132 16.568 22.125 36.457 1.00 12.67 O ANISOU 1142 OH TYR A 132 2300 1255 1259 868 -285 -112 O ATOM 1143 N PRO A 133 18.367 19.913 31.019 1.00 6.96 N ANISOU 1143 N PRO A 133 768 673 1203 180 -40 -33 N ATOM 1144 CA PRO A 133 18.774 18.559 31.397 1.00 6.99 C ANISOU 1144 CA PRO A 133 850 681 1126 118 -64 11 C ATOM 1145 C PRO A 133 17.777 17.816 32.308 1.00 7.57 C ANISOU 1145 C PRO A 133 715 802 1359 282 -19 137 C ATOM 1146 O PRO A 133 17.790 16.562 32.271 1.00 8.53 O ANISOU 1146 O PRO A 133 1012 739 1489 203 163 163 O ATOM 1147 CB PRO A 133 20.147 18.756 32.072 1.00 8.08 C ANISOU 1147 CB PRO A 133 756 1046 1269 177 -31 166 C ATOM 1148 CG PRO A 133 20.702 19.945 31.360 1.00 8.16 C ANISOU 1148 CG PRO A 133 757 942 1403 40 -52 52 C ATOM 1149 CD PRO A 133 19.490 20.842 31.217 1.00 7.62 C ANISOU 1149 CD PRO A 133 804 798 1296 61 -17 -45 C ATOM 1150 N GLY A 134 16.952 18.490 33.067 1.00 7.80 N ANISOU 1150 N GLY A 134 931 821 1213 289 46 101 N ATOM 1151 CA GLY A 134 16.017 17.792 33.925 1.00 8.65 C ANISOU 1151 CA GLY A 134 986 988 1314 230 65 151 C ATOM 1152 C GLY A 134 15.036 16.883 33.208 1.00 8.72 C ANISOU 1152 C GLY A 134 981 836 1497 225 94 237 C ATOM 1153 O GLY A 134 14.535 15.963 33.848 1.00 10.14 O ANISOU 1153 O GLY A 134 1107 1071 1674 99 156 416 O ATOM 1154 N HIS A 135 14.755 17.123 31.941 1.00 9.29 N ANISOU 1154 N HIS A 135 1230 835 1465 -170 -30 200 N ATOM 1155 CA HIS A 135 13.848 16.260 31.206 1.00 9.05 C ANISOU 1155 CA HIS A 135 781 801 1857 88 -23 123 C ATOM 1156 C HIS A 135 14.442 14.906 30.819 1.00 8.53 C ANISOU 1156 C HIS A 135 847 825 1568 96 -106 1 C ATOM 1157 O HIS A 135 13.730 13.986 30.425 1.00 11.47 O ANISOU 1157 O HIS A 135 985 984 2389 -81 -86 -211 O ATOM 1158 CB HIS A 135 13.371 16.932 29.903 1.00 10.80 C ANISOU 1158 CB HIS A 135 1141 1146 1818 315 -231 36 C ATOM 1159 CG HIS A 135 12.799 18.291 30.089 1.00 10.30 C ANISOU 1159 CG HIS A 135 1109 1097 1706 225 -167 105 C ATOM 1160 ND1 HIS A 135 11.789 18.583 30.948 1.00 14.18 N ANISOU 1160 ND1 HIS A 135 1351 1276 2762 482 360 280 N ATOM 1161 CD2 HIS A 135 13.097 19.428 29.435 1.00 11.56 C ANISOU 1161 CD2 HIS A 135 1299 1063 2029 173 -170 146 C ATOM 1162 CE1 HIS A 135 11.492 19.843 30.868 1.00 16.26 C ANISOU 1162 CE1 HIS A 135 1622 1443 3112 822 461 548 C ATOM 1163 NE2 HIS A 135 12.269 20.404 29.969 1.00 13.83 N ANISOU 1163 NE2 HIS A 135 1168 1311 2775 348 -92 245 N ATOM 1164 N ASP A 136 15.749 14.764 30.866 1.00 8.97 N ANISOU 1164 N ASP A 136 859 915 1633 199 -68 57 N ATOM 1165 CA ASP A 136 16.470 13.614 30.290 1.00 8.29 C ANISOU 1165 CA ASP A 136 672 1037 1440 25 -60 -46 C ATOM 1166 C ASP A 136 16.688 12.561 31.331 1.00 8.23 C ANISOU 1166 C ASP A 136 684 811 1632 171 -28 -83 C ATOM 1167 O ASP A 136 17.207 12.843 32.436 1.00 8.61 O ANISOU 1167 O ASP A 136 980 896 1398 112 112 90 O ATOM 1168 CB AASP A 136 17.794 13.911 29.576 0.53 8.80 C ANISOU 1168 CB AASP A 136 833 1475 1037 -88 -50 -338 C ATOM 1169 CG AASP A 136 18.481 12.722 28.933 0.53 11.59 C ANISOU 1169 CG AASP A 136 1084 1400 1921 52 292 -296 C ATOM 1170 OD1AASP A 136 18.769 11.740 29.672 0.53 11.82 O ANISOU 1170 OD1AASP A 136 1017 2149 1326 737 -382 -526 O ATOM 1171 OD2AASP A 136 18.761 12.680 27.707 0.53 10.25 O ANISOU 1171 OD2AASP A 136 1496 602 1796 516 1 -391 O ATOM 1172 CB BASP A 136 17.772 14.287 29.827 0.47 10.76 C ANISOU 1172 CB BASP A 136 1057 1890 1142 -181 326 -13 C ATOM 1173 CG BASP A 136 18.489 13.469 28.794 0.47 9.12 C ANISOU 1173 CG BASP A 136 1006 1627 832 -292 49 35 C ATOM 1174 OD1BASP A 136 18.732 12.294 29.097 0.47 13.95 O ANISOU 1174 OD1BASP A 136 2422 2162 715 769 255 363 O ATOM 1175 OD2BASP A 136 18.792 13.957 27.704 0.47 9.43 O ANISOU 1175 OD2BASP A 136 926 1581 1075 -85 352 220 O ATOM 1176 N PRO A 137 16.356 11.303 31.029 1.00 12.73 N ANISOU 1176 N PRO A 137 1684 962 2189 -42 -614 -10 N ATOM 1177 CA PRO A 137 16.533 10.232 32.014 1.00 16.91 C ANISOU 1177 CA PRO A 137 1952 1123 3351 -476 -1081 576 C ATOM 1178 C PRO A 137 17.937 10.021 32.482 1.00 17.92 C ANISOU 1178 C PRO A 137 1947 848 4013 -16 -1075 542 C ATOM 1179 O PRO A 137 18.151 9.436 33.539 1.00 20.90 O ANISOU 1179 O PRO A 137 2277 958 4704 -579 -1600 1093 O ATOM 1180 CB PRO A 137 16.019 8.992 31.248 1.00 22.91 C ANISOU 1180 CB PRO A 137 2683 855 5168 -90 -1807 225 C ATOM 1181 CG PRO A 137 16.168 9.332 29.800 1.00 23.66 C ANISOU 1181 CG PRO A 137 3069 1328 4594 711 -1966 -898 C ATOM 1182 CD PRO A 137 15.817 10.812 29.736 1.00 16.65 C ANISOU 1182 CD PRO A 137 1996 1157 3175 186 -1500 -475 C ATOM 1183 N ARG A 138 18.969 10.450 31.793 1.00 15.15 N ANISOU 1183 N ARG A 138 1864 1260 2634 546 -606 -1044 N ATOM 1184 CA ARG A 138 20.175 10.051 32.533 1.00 13.32 C ANISOU 1184 CA ARG A 138 1749 1281 2031 77 -202 -213 C ATOM 1185 C ARG A 138 20.576 11.004 33.625 1.00 12.35 C ANISOU 1185 C ARG A 138 1688 940 2065 605 -492 -104 C ATOM 1186 O ARG A 138 21.584 10.744 34.292 1.00 12.48 O ANISOU 1186 O ARG A 138 1485 1055 2202 539 -433 -165 O ATOM 1187 CB ARG A 138 21.276 10.006 31.523 1.00 12.39 C ANISOU 1187 CB ARG A 138 1604 1478 1623 -377 -462 59 C ATOM 1188 CG ARG A 138 21.692 11.373 31.136 1.00 9.22 C ANISOU 1188 CG ARG A 138 1402 836 1264 260 -206 -318 C ATOM 1189 CD ARG A 138 22.555 11.412 29.873 1.00 13.09 C ANISOU 1189 CD ARG A 138 1758 2014 1203 575 12 21 C ATOM 1190 NE ARG A 138 21.639 11.257 28.765 1.00 15.43 N ANISOU 1190 NE ARG A 138 2054 2341 1466 1253 -376 -994 N ATOM 1191 CZ ARG A 138 21.902 11.113 27.460 1.00 9.82 C ANISOU 1191 CZ ARG A 138 1837 553 1341 370 -370 261 C ATOM 1192 NH1 ARG A 138 23.141 11.094 27.062 1.00 14.02 N ANISOU 1192 NH1 ARG A 138 2279 1369 1677 -47 129 -166 N ATOM 1193 NH2 ARG A 138 20.884 10.949 26.614 1.00 13.01 N ANISOU 1193 NH2 ARG A 138 2632 1044 1267 160 -736 35 N ATOM 1194 N TYR A 139 19.834 12.081 33.850 1.00 8.21 N ANISOU 1194 N TYR A 139 984 804 1332 99 40 201 N ATOM 1195 CA TYR A 139 20.054 12.983 34.968 1.00 8.38 C ANISOU 1195 CA TYR A 139 1031 914 1239 164 236 156 C ATOM 1196 C TYR A 139 18.982 12.852 36.040 1.00 9.69 C ANISOU 1196 C TYR A 139 1188 1036 1459 362 428 405 C ATOM 1197 O TYR A 139 18.833 13.773 36.875 1.00 10.99 O ANISOU 1197 O TYR A 139 1480 1225 1469 420 581 284 O ATOM 1198 CB TYR A 139 20.185 14.477 34.485 1.00 7.70 C ANISOU 1198 CB TYR A 139 1008 728 1189 208 201 39 C ATOM 1199 CG TYR A 139 21.165 14.554 33.350 1.00 6.65 C ANISOU 1199 CG TYR A 139 1032 499 996 98 103 -71 C ATOM 1200 CD1 TYR A 139 22.518 14.259 33.534 1.00 7.16 C ANISOU 1200 CD1 TYR A 139 1052 672 995 165 74 -172 C ATOM 1201 CD2 TYR A 139 20.784 14.927 32.051 1.00 6.66 C ANISOU 1201 CD2 TYR A 139 856 649 1025 61 117 -82 C ATOM 1202 CE1 TYR A 139 23.422 14.313 32.492 1.00 6.50 C ANISOU 1202 CE1 TYR A 139 856 562 1051 122 -2 4 C ATOM 1203 CE2 TYR A 139 21.693 14.985 31.008 1.00 6.52 C ANISOU 1203 CE2 TYR A 139 819 663 994 11 22 124 C ATOM 1204 CZ TYR A 139 23.011 14.684 31.218 1.00 6.33 C ANISOU 1204 CZ TYR A 139 739 632 1034 -9 97 59 C ATOM 1205 OH TYR A 139 23.963 14.707 30.203 1.00 6.69 O ANISOU 1205 OH TYR A 139 766 682 1093 84 66 92 O ATOM 1206 N ALA A 140 18.273 11.709 36.069 1.00 11.86 N ANISOU 1206 N ALA A 140 1383 1235 1889 142 548 560 N ATOM 1207 CA ALA A 140 17.158 11.527 36.982 1.00 15.15 C ANISOU 1207 CA ALA A 140 1635 1846 2276 -159 813 404 C ATOM 1208 C ALA A 140 17.596 11.689 38.448 1.00 15.23 C ANISOU 1208 C ALA A 140 2037 1689 2061 507 958 521 C ATOM 1209 O ALA A 140 16.755 12.041 39.300 1.00 19.93 O ANISOU 1209 O ALA A 140 2722 2522 2330 1182 1503 978 O ATOM 1210 CB ALA A 140 16.537 10.141 36.811 1.00 19.81 C ANISOU 1210 CB ALA A 140 2089 2222 3214 -744 493 758 C ATOM 1211 N LYS A 141 18.863 11.408 38.783 1.00 14.38 N ANISOU 1211 N LYS A 141 2144 1564 1756 476 887 587 N ATOM 1212 CA LYS A 141 19.323 11.464 40.181 1.00 16.69 C ANISOU 1212 CA LYS A 141 2513 2025 1803 531 852 537 C ATOM 1213 C LYS A 141 19.864 12.833 40.557 1.00 18.02 C ANISOU 1213 C LYS A 141 3473 2026 1347 596 595 441 C ATOM 1214 O LYS A 141 20.177 13.106 41.730 1.00 20.54 O ANISOU 1214 O LYS A 141 3572 2753 1479 531 48 555 O ATOM 1215 CB LYS A 141 20.298 10.313 40.486 1.00 19.97 C ANISOU 1215 CB LYS A 141 3491 2049 2048 765 394 816 C ATOM 1216 CG LYS A 141 19.686 8.923 40.363 1.00 22.73 C ANISOU 1216 CG LYS A 141 4457 2050 2131 487 447 1119 C ATOM 1217 CD LYS A 141 20.801 7.909 40.629 1.00 28.65 C ANISOU 1217 CD LYS A 141 5082 1957 3846 556 -542 1233 C ATOM 1218 CE LYS A 141 20.323 6.528 40.255 1.00 37.98 C ANISOU 1218 CE LYS A 141 6853 1831 5747 424 -754 1126 C ATOM 1219 NZ LYS A 141 21.421 5.519 40.335 1.00 49.16 N ANISOU 1219 NZ LYS A 141 9048 2447 7182 1756 -4071 -348 N ATOM 1220 N LEU A 142 19.936 13.793 39.618 1.00 13.68 N ANISOU 1220 N LEU A 142 2302 1624 1273 821 536 261 N ATOM 1221 CA LEU A 142 20.483 15.109 39.928 1.00 13.65 C ANISOU 1221 CA LEU A 142 2488 1738 962 763 347 9 C ATOM 1222 C LEU A 142 19.465 16.003 40.598 1.00 15.92 C ANISOU 1222 C LEU A 142 2765 2053 1232 870 672 -22 C ATOM 1223 O LEU A 142 18.270 15.923 40.273 1.00 18.67 O ANISOU 1223 O LEU A 142 2591 2357 2144 731 946 -353 O ATOM 1224 CB LEU A 142 21.019 15.814 38.657 1.00 11.78 C ANISOU 1224 CB LEU A 142 1834 1442 1201 846 244 188 C ATOM 1225 CG LEU A 142 22.447 15.478 38.223 1.00 12.03 C ANISOU 1225 CG LEU A 142 1821 1580 1171 940 49 -134 C ATOM 1226 CD1 LEU A 142 22.572 14.011 37.842 1.00 10.90 C ANISOU 1226 CD1 LEU A 142 1431 1450 1260 509 102 -89 C ATOM 1227 CD2 LEU A 142 22.887 16.377 37.058 1.00 11.32 C ANISOU 1227 CD2 LEU A 142 1326 1512 1464 267 -95 -195 C ATOM 1228 N SER A 143 19.930 16.889 41.504 1.00 18.13 N ANISOU 1228 N SER A 143 2941 2203 1743 983 781 -431 N ATOM 1229 CA SER A 143 19.115 17.961 42.061 1.00 20.87 C ANISOU 1229 CA SER A 143 3405 2940 1585 1649 549 -641 C ATOM 1230 C SER A 143 18.971 19.201 41.143 1.00 20.51 C ANISOU 1230 C SER A 143 2856 2888 2050 1656 554 -506 C ATOM 1231 O SER A 143 19.725 19.312 40.196 1.00 15.05 O ANISOU 1231 O SER A 143 1897 1982 1838 853 -12 -980 O ATOM 1232 CB SER A 143 19.721 18.435 43.399 1.00 24.89 C ANISOU 1232 CB SER A 143 3961 3759 1735 1856 324 -1002 C ATOM 1233 OG SER A 143 20.947 19.104 43.084 1.00 24.63 O ANISOU 1233 OG SER A 143 3904 3304 2153 1818 -6 -1155 O ATOM 1234 N GLU A 144 18.041 20.163 41.433 1.00 19.78 N ANISOU 1234 N GLU A 144 2923 3054 1539 1675 541 -497 N ATOM 1235 CA GLU A 144 17.899 21.386 40.652 1.00 21.62 C ANISOU 1235 CA GLU A 144 2919 2924 2373 1566 -182 -469 C ATOM 1236 C GLU A 144 19.225 22.120 40.590 1.00 18.91 C ANISOU 1236 C GLU A 144 3301 2059 1826 1486 -178 -1237 C ATOM 1237 O GLU A 144 19.607 22.640 39.531 1.00 19.94 O ANISOU 1237 O GLU A 144 2942 2471 2165 1480 -186 -906 O ATOM 1238 CB GLU A 144 16.856 22.357 41.229 1.00 19.35 C ANISOU 1238 CB GLU A 144 3390 2445 1518 1278 121 -377 C ATOM 1239 CG GLU A 144 16.771 23.655 40.442 1.00 19.25 C ANISOU 1239 CG GLU A 144 2658 2552 2105 1094 1008 17 C ATOM 1240 CD GLU A 144 15.646 24.589 40.800 1.00 18.65 C ANISOU 1240 CD GLU A 144 2918 2073 2096 948 980 -138 C ATOM 1241 OE1 GLU A 144 14.930 24.327 41.799 1.00 15.96 O ANISOU 1241 OE1 GLU A 144 2205 2171 1687 707 595 -555 O ATOM 1242 OE2 GLU A 144 15.391 25.632 40.111 1.00 18.69 O ANISOU 1242 OE2 GLU A 144 2552 1999 2551 595 550 21 O ATOM 1243 N LYS A 145 19.884 22.165 41.767 1.00 22.64 N ANISOU 1243 N LYS A 145 3730 2713 2161 1820 -715 -1326 N ATOM 1244 CA LYS A 145 21.155 22.863 41.779 1.00 26.91 C ANISOU 1244 CA LYS A 145 4266 2964 2996 1263 -923 -1971 C ATOM 1245 C LYS A 145 22.208 22.137 40.940 1.00 21.89 C ANISOU 1245 C LYS A 145 3512 2133 2670 846 -889 -1293 C ATOM 1246 O LYS A 145 23.091 22.849 40.444 1.00 28.68 O ANISOU 1246 O LYS A 145 4833 2133 3932 71 -208 -1527 O ATOM 1247 CB LYS A 145 21.764 23.119 43.174 1.00 35.58 C ANISOU 1247 CB LYS A 145 5341 4732 3448 936 -1245 -2895 C ATOM 1248 CG LYS A 145 23.015 23.965 43.167 1.00 46.15 C ANISOU 1248 CG LYS A 145 6094 5764 5677 29 -2403 -2625 C ATOM 1249 CD LYS A 145 23.163 25.198 42.307 1.00 53.13 C ANISOU 1249 CD LYS A 145 6661 4764 8760 -314 -2284 -2248 C ATOM 1250 CE LYS A 145 22.931 26.501 43.057 1.00 59.90 C ANISOU 1250 CE LYS A 145 7178 5606 9977 -414 -1677 -3223 C ATOM 1251 NZ LYS A 145 23.224 27.689 42.197 1.00 71.88 N ANISOU 1251 NZ LYS A 145 9942 4671 12696 43 -1487 -2580 N ATOM 1252 N GLU A 146 22.139 20.815 40.803 1.00 17.62 N ANISOU 1252 N GLU A 146 2601 2170 1923 657 -786 -1134 N ATOM 1253 CA GLU A 146 23.123 20.145 39.917 1.00 15.45 C ANISOU 1253 CA GLU A 146 2248 1601 2022 547 -851 -851 C ATOM 1254 C GLU A 146 22.770 20.313 38.457 1.00 12.23 C ANISOU 1254 C GLU A 146 1599 1141 1906 449 -381 -389 C ATOM 1255 O GLU A 146 23.663 20.276 37.599 1.00 14.78 O ANISOU 1255 O GLU A 146 1306 1829 2480 179 -243 -339 O ATOM 1256 CB GLU A 146 23.217 18.686 40.328 1.00 12.78 C ANISOU 1256 CB GLU A 146 1513 1935 1410 452 -272 -250 C ATOM 1257 CG GLU A 146 23.997 18.440 41.655 1.00 16.62 C ANISOU 1257 CG GLU A 146 1893 2860 1562 665 -561 -435 C ATOM 1258 CD GLU A 146 23.846 17.019 42.146 1.00 16.92 C ANISOU 1258 CD GLU A 146 1987 3267 1174 754 -275 122 C ATOM 1259 OE1 GLU A 146 22.765 16.382 42.065 1.00 18.64 O ANISOU 1259 OE1 GLU A 146 2262 2905 1916 687 -588 206 O ATOM 1260 OE2 GLU A 146 24.848 16.480 42.646 1.00 23.81 O ANISOU 1260 OE2 GLU A 146 2173 4206 2668 457 -574 1418 O ATOM 1261 N LEU A 147 21.494 20.390 38.082 1.00 10.79 N ANISOU 1261 N LEU A 147 1435 1009 1657 241 -204 -233 N ATOM 1262 CA LEU A 147 21.031 20.463 36.724 1.00 9.56 C ANISOU 1262 CA LEU A 147 1320 791 1519 121 -79 -314 C ATOM 1263 C LEU A 147 21.355 21.849 36.165 1.00 10.28 C ANISOU 1263 C LEU A 147 1330 743 1833 255 -127 -196 C ATOM 1264 O LEU A 147 20.817 22.858 36.648 1.00 12.81 O ANISOU 1264 O LEU A 147 1989 859 2021 429 165 -210 O ATOM 1265 CB LEU A 147 19.504 20.242 36.653 1.00 10.38 C ANISOU 1265 CB LEU A 147 1395 1024 1523 127 -96 75 C ATOM 1266 CG LEU A 147 19.032 18.827 36.969 1.00 9.65 C ANISOU 1266 CG LEU A 147 1456 962 1248 46 129 -120 C ATOM 1267 CD1 LEU A 147 17.527 18.788 37.235 1.00 10.14 C ANISOU 1267 CD1 LEU A 147 1420 893 1541 189 111 -69 C ATOM 1268 CD2 LEU A 147 19.378 17.835 35.865 1.00 9.82 C ANISOU 1268 CD2 LEU A 147 1209 1264 1259 152 -18 -194 C ATOM 1269 N PRO A 148 22.232 22.005 35.185 1.00 10.26 N ANISOU 1269 N PRO A 148 1407 760 1734 455 -232 29 N ATOM 1270 CA PRO A 148 22.592 23.343 34.733 1.00 10.01 C ANISOU 1270 CA PRO A 148 1418 826 1561 193 -340 -46 C ATOM 1271 C PRO A 148 21.617 23.994 33.765 1.00 8.85 C ANISOU 1271 C PRO A 148 1339 633 1392 55 -159 1 C ATOM 1272 O PRO A 148 21.051 23.333 32.894 1.00 10.40 O ANISOU 1272 O PRO A 148 1396 914 1642 170 -374 -286 O ATOM 1273 CB PRO A 148 23.950 23.112 34.021 1.00 12.24 C ANISOU 1273 CB PRO A 148 1516 1047 2088 366 -164 7 C ATOM 1274 CG PRO A 148 23.799 21.708 33.496 1.00 14.26 C ANISOU 1274 CG PRO A 148 1807 849 2761 520 361 90 C ATOM 1275 CD PRO A 148 23.015 20.932 34.529 1.00 11.06 C ANISOU 1275 CD PRO A 148 1308 923 1971 382 -202 -224 C ATOM 1276 N LEU A 149 21.496 25.314 33.879 1.00 8.77 N ANISOU 1276 N LEU A 149 1299 676 1356 216 -56 -60 N ATOM 1277 CA LEU A 149 20.911 26.175 32.867 1.00 8.66 C ANISOU 1277 CA LEU A 149 1127 763 1400 243 59 -2 C ATOM 1278 C LEU A 149 21.935 26.749 31.863 1.00 8.44 C ANISOU 1278 C LEU A 149 1103 818 1286 258 -21 -1 C ATOM 1279 O LEU A 149 21.523 27.221 30.789 1.00 9.11 O ANISOU 1279 O LEU A 149 1376 878 1207 406 -45 -104 O ATOM 1280 CB LEU A 149 20.159 27.338 33.546 1.00 9.65 C ANISOU 1280 CB LEU A 149 1665 808 1194 479 144 -19 C ATOM 1281 CG LEU A 149 19.038 26.957 34.504 1.00 11.19 C ANISOU 1281 CG LEU A 149 1727 1221 1304 502 238 20 C ATOM 1282 CD1 LEU A 149 18.503 28.241 35.180 1.00 13.57 C ANISOU 1282 CD1 LEU A 149 1994 1426 1736 473 444 -294 C ATOM 1283 CD2 LEU A 149 17.923 26.203 33.802 1.00 13.10 C ANISOU 1283 CD2 LEU A 149 1933 1038 2007 138 310 129 C ATOM 1284 N THR A 150 23.204 26.694 32.276 1.00 8.26 N ANISOU 1284 N THR A 150 1071 806 1261 284 60 -47 N ATOM 1285 CA THR A 150 24.379 27.227 31.605 1.00 7.52 C ANISOU 1285 CA THR A 150 1028 815 1013 337 -38 -107 C ATOM 1286 C THR A 150 25.599 26.885 32.471 1.00 8.14 C ANISOU 1286 C THR A 150 1069 961 1061 508 -107 -167 C ATOM 1287 O THR A 150 25.390 26.602 33.667 1.00 9.62 O ANISOU 1287 O THR A 150 1268 1325 1063 476 -105 -23 O ATOM 1288 CB THR A 150 24.258 28.730 31.407 1.00 8.62 C ANISOU 1288 CB THR A 150 1159 897 1219 376 63 197 C ATOM 1289 OG1 THR A 150 25.372 29.115 30.602 1.00 9.59 O ANISOU 1289 OG1 THR A 150 1248 1011 1386 245 105 119 O ATOM 1290 CG2 THR A 150 24.290 29.533 32.708 1.00 12.94 C ANISOU 1290 CG2 THR A 150 2287 948 1681 520 373 -204 C ATOM 1291 N GLU A 151 26.790 26.904 31.955 1.00 7.03 N ANISOU 1291 N GLU A 151 1041 617 1012 171 -221 -220 N ATOM 1292 CA GLU A 151 28.015 26.734 32.717 1.00 7.93 C ANISOU 1292 CA GLU A 151 1090 717 1207 205 -367 -191 C ATOM 1293 C GLU A 151 29.119 27.597 32.106 1.00 8.35 C ANISOU 1293 C GLU A 151 987 726 1459 186 -421 -211 C ATOM 1294 O GLU A 151 29.168 27.862 30.910 1.00 11.32 O ANISOU 1294 O GLU A 151 1724 957 1621 -317 -732 371 O ATOM 1295 CB GLU A 151 28.470 25.249 32.825 1.00 8.22 C ANISOU 1295 CB GLU A 151 1319 722 1081 302 -298 -142 C ATOM 1296 CG GLU A 151 27.581 24.360 33.688 1.00 9.31 C ANISOU 1296 CG GLU A 151 1802 785 952 368 -214 -22 C ATOM 1297 CD GLU A 151 28.121 22.928 33.732 1.00 8.11 C ANISOU 1297 CD GLU A 151 1349 741 992 364 70 -77 C ATOM 1298 OE1 GLU A 151 28.452 22.417 32.652 1.00 7.76 O ANISOU 1298 OE1 GLU A 151 1310 735 902 245 -116 -31 O ATOM 1299 OE2 GLU A 151 28.199 22.338 34.860 1.00 9.89 O ANISOU 1299 OE2 GLU A 151 1717 1109 933 630 147 -18 O ATOM 1300 N SER A 152 30.084 27.934 32.950 1.00 9.93 N ANISOU 1300 N SER A 152 964 1333 1477 170 -372 -469 N ATOM 1301 CA SER A 152 31.356 28.518 32.599 1.00 9.18 C ANISOU 1301 CA SER A 152 987 929 1573 183 -539 -213 C ATOM 1302 C SER A 152 32.455 27.470 32.826 1.00 8.26 C ANISOU 1302 C SER A 152 936 909 1295 142 -442 -248 C ATOM 1303 O SER A 152 32.222 26.427 33.486 1.00 8.90 O ANISOU 1303 O SER A 152 1079 954 1351 205 -324 -204 O ATOM 1304 CB SER A 152 31.644 29.703 33.504 1.00 9.49 C ANISOU 1304 CB SER A 152 984 1111 1508 213 -362 -326 C ATOM 1305 OG SER A 152 31.693 29.271 34.850 1.00 10.02 O ANISOU 1305 OG SER A 152 1220 1049 1536 33 -303 -274 O ATOM 1306 N LEU A 153 33.686 27.745 32.393 1.00 9.01 N ANISOU 1306 N LEU A 153 1062 771 1588 161 -360 -282 N ATOM 1307 CA LEU A 153 34.820 26.872 32.764 1.00 8.82 C ANISOU 1307 CA LEU A 153 1006 909 1436 204 -267 -179 C ATOM 1308 C LEU A 153 34.960 26.882 34.285 1.00 8.15 C ANISOU 1308 C LEU A 153 1014 665 1419 -94 -196 -114 C ATOM 1309 O LEU A 153 35.249 25.833 34.868 1.00 8.80 O ANISOU 1309 O LEU A 153 1172 753 1419 103 -164 -144 O ATOM 1310 CB LEU A 153 36.125 27.314 32.113 1.00 9.45 C ANISOU 1310 CB LEU A 153 1174 890 1525 100 -56 -42 C ATOM 1311 CG LEU A 153 37.388 26.492 32.438 1.00 8.16 C ANISOU 1311 CG LEU A 153 1061 847 1191 8 -99 -29 C ATOM 1312 CD1 LEU A 153 37.213 24.985 32.106 1.00 10.63 C ANISOU 1312 CD1 LEU A 153 1498 912 1627 113 -293 -252 C ATOM 1313 CD2 LEU A 153 38.604 27.074 31.726 1.00 11.00 C ANISOU 1313 CD2 LEU A 153 1197 1306 1675 26 181 -33 C ATOM 1314 N ALA A 154 34.779 28.009 34.964 1.00 9.05 N ANISOU 1314 N ALA A 154 1151 806 1482 20 -342 -252 N ATOM 1315 CA ALA A 154 34.900 28.066 36.435 1.00 9.80 C ANISOU 1315 CA ALA A 154 1477 780 1468 -3 -316 -177 C ATOM 1316 C ALA A 154 33.931 27.061 37.076 1.00 9.29 C ANISOU 1316 C ALA A 154 1371 710 1449 42 -274 -250 C ATOM 1317 O ALA A 154 34.311 26.291 37.971 1.00 9.50 O ANISOU 1317 O ALA A 154 1325 930 1355 15 -375 -219 O ATOM 1318 CB ALA A 154 34.650 29.443 36.978 1.00 10.00 C ANISOU 1318 CB ALA A 154 1550 816 1432 34 -158 -156 C ATOM 1319 N LEU A 155 32.654 27.030 36.598 1.00 8.85 N ANISOU 1319 N LEU A 155 1380 758 1224 111 -146 -65 N ATOM 1320 CA LEU A 155 31.682 26.084 37.143 1.00 9.38 C ANISOU 1320 CA LEU A 155 1324 870 1371 0 -9 -367 C ATOM 1321 C LEU A 155 31.981 24.620 36.769 1.00 9.05 C ANISOU 1321 C LEU A 155 1316 719 1403 -79 93 -308 C ATOM 1322 O LEU A 155 31.688 23.697 37.551 1.00 10.00 O ANISOU 1322 O LEU A 155 1519 1026 1256 -217 -20 -138 O ATOM 1323 CB LEU A 155 30.258 26.476 36.728 1.00 10.30 C ANISOU 1323 CB LEU A 155 1461 945 1507 61 -303 -371 C ATOM 1324 CG LEU A 155 29.712 27.745 37.367 1.00 11.68 C ANISOU 1324 CG LEU A 155 1268 1539 1631 187 -20 -725 C ATOM 1325 CD1 LEU A 155 28.416 28.245 36.738 1.00 12.81 C ANISOU 1325 CD1 LEU A 155 1665 1225 1977 311 -213 -356 C ATOM 1326 CD2 LEU A 155 29.482 27.566 38.901 1.00 15.76 C ANISOU 1326 CD2 LEU A 155 1865 2477 1648 764 -86 -593 C ATOM 1327 N THR A 156 32.605 24.424 35.598 1.00 8.65 N ANISOU 1327 N THR A 156 1285 776 1226 -30 20 -169 N ATOM 1328 CA THR A 156 33.044 23.080 35.165 1.00 7.82 C ANISOU 1328 CA THR A 156 1085 783 1104 -44 -24 -136 C ATOM 1329 C THR A 156 34.130 22.570 36.100 1.00 7.92 C ANISOU 1329 C THR A 156 931 921 1155 -180 30 -66 C ATOM 1330 O THR A 156 34.058 21.419 36.590 1.00 8.09 O ANISOU 1330 O THR A 156 1299 780 995 -223 -116 -118 O ATOM 1331 CB THR A 156 33.501 23.125 33.702 1.00 7.24 C ANISOU 1331 CB THR A 156 698 866 1186 -103 -65 -143 C ATOM 1332 OG1 THR A 156 32.434 23.599 32.874 1.00 9.43 O ANISOU 1332 OG1 THR A 156 1358 992 1232 148 -298 -164 O ATOM 1333 CG2 THR A 156 33.852 21.727 33.224 1.00 8.64 C ANISOU 1333 CG2 THR A 156 1326 852 1103 43 -64 -81 C ATOM 1334 N ILE A 157 35.109 23.408 36.464 1.00 8.34 N ANISOU 1334 N ILE A 157 1094 726 1349 -71 -198 -99 N ATOM 1335 CA ILE A 157 36.127 23.064 37.454 1.00 8.25 C ANISOU 1335 CA ILE A 157 1270 760 1104 -2 -237 -186 C ATOM 1336 C ILE A 157 35.488 22.634 38.755 1.00 9.00 C ANISOU 1336 C ILE A 157 1343 877 1201 -24 -70 -170 C ATOM 1337 O ILE A 157 35.914 21.671 39.407 1.00 8.65 O ANISOU 1337 O ILE A 157 1264 797 1226 -81 -203 -164 O ATOM 1338 CB ILE A 157 37.105 24.246 37.636 1.00 8.61 C ANISOU 1338 CB ILE A 157 1340 671 1259 -53 -310 -140 C ATOM 1339 CG1 ILE A 157 37.969 24.448 36.386 1.00 8.69 C ANISOU 1339 CG1 ILE A 157 1137 783 1383 20 -328 -64 C ATOM 1340 CG2 ILE A 157 37.938 24.113 38.855 1.00 10.72 C ANISOU 1340 CG2 ILE A 157 1615 1056 1401 -379 -492 -90 C ATOM 1341 CD1 ILE A 157 38.650 25.783 36.234 1.00 8.96 C ANISOU 1341 CD1 ILE A 157 1311 819 1273 -91 -209 -211 C ATOM 1342 N ASP A 158 34.461 23.376 39.181 1.00 9.27 N ANISOU 1342 N ASP A 158 1327 1009 1185 101 -189 -189 N ATOM 1343 CA ASP A 158 33.813 23.121 40.468 1.00 9.29 C ANISOU 1343 CA ASP A 158 1313 1068 1151 92 -191 -266 C ATOM 1344 C ASP A 158 33.160 21.747 40.530 1.00 9.88 C ANISOU 1344 C ASP A 158 1663 1069 1022 -19 3 -379 C ATOM 1345 O ASP A 158 32.957 21.268 41.642 1.00 11.99 O ANISOU 1345 O ASP A 158 2418 1103 1036 63 -1 -322 O ATOM 1346 CB ASP A 158 32.768 24.185 40.803 1.00 9.81 C ANISOU 1346 CB ASP A 158 1405 1065 1256 26 -19 -207 C ATOM 1347 CG ASP A 158 33.345 25.546 41.148 1.00 12.60 C ANISOU 1347 CG ASP A 158 1756 1215 1817 14 -51 -619 C ATOM 1348 OD1 ASP A 158 34.537 25.610 41.499 1.00 14.75 O ANISOU 1348 OD1 ASP A 158 1966 1574 2065 -250 -327 -890 O ATOM 1349 OD2 ASP A 158 32.582 26.538 41.093 1.00 18.05 O ANISOU 1349 OD2 ASP A 158 2595 1256 3008 408 -344 -744 O ATOM 1350 N ARG A 159 32.839 21.088 39.405 1.00 9.37 N ANISOU 1350 N ARG A 159 1598 935 1025 -91 -112 -246 N ATOM 1351 CA ARG A 159 32.387 19.675 39.460 1.00 8.78 C ANISOU 1351 CA ARG A 159 1179 1037 1122 -151 54 -357 C ATOM 1352 C ARG A 159 33.443 18.643 39.094 1.00 8.51 C ANISOU 1352 C ARG A 159 1334 938 962 -85 136 -263 C ATOM 1353 O ARG A 159 33.478 17.544 39.656 1.00 9.77 O ANISOU 1353 O ARG A 159 1461 1002 1247 -171 178 -155 O ATOM 1354 CB ARG A 159 31.105 19.450 38.655 1.00 9.91 C ANISOU 1354 CB ARG A 159 1484 1210 1070 -19 -248 -148 C ATOM 1355 CG ARG A 159 31.164 19.876 37.244 1.00 10.04 C ANISOU 1355 CG ARG A 159 889 1436 1491 383 -156 577 C ATOM 1356 CD ARG A 159 29.922 19.406 36.443 1.00 8.94 C ANISOU 1356 CD ARG A 159 1196 1188 1015 514 -66 -28 C ATOM 1357 NE ARG A 159 29.770 20.028 35.128 1.00 7.06 N ANISOU 1357 NE ARG A 159 1067 643 971 129 -13 -6 N ATOM 1358 CZ ARG A 159 30.350 19.571 34.012 1.00 6.68 C ANISOU 1358 CZ ARG A 159 1002 536 999 39 -118 -63 C ATOM 1359 NH1 ARG A 159 31.160 18.525 34.016 1.00 6.38 N ANISOU 1359 NH1 ARG A 159 909 690 824 67 -154 12 N ATOM 1360 NH2 ARG A 159 30.129 20.183 32.872 1.00 7.91 N ANISOU 1360 NH2 ARG A 159 1350 702 955 231 -3 -8 N ATOM 1361 N VAL A 160 34.358 18.983 38.174 1.00 8.49 N ANISOU 1361 N VAL A 160 1436 913 878 -106 150 -365 N ATOM 1362 CA VAL A 160 35.387 18.028 37.779 1.00 7.95 C ANISOU 1362 CA VAL A 160 1197 775 1050 -206 144 -181 C ATOM 1363 C VAL A 160 36.437 17.768 38.852 1.00 8.31 C ANISOU 1363 C VAL A 160 1484 687 985 -185 35 -171 C ATOM 1364 O VAL A 160 36.827 16.609 39.091 1.00 9.16 O ANISOU 1364 O VAL A 160 1527 732 1220 -223 11 -121 O ATOM 1365 CB VAL A 160 36.085 18.489 36.463 1.00 7.27 C ANISOU 1365 CB VAL A 160 1141 660 962 -202 58 -196 C ATOM 1366 CG1 VAL A 160 37.272 17.613 36.128 1.00 8.46 C ANISOU 1366 CG1 VAL A 160 1170 914 1131 -84 118 -73 C ATOM 1367 CG2 VAL A 160 35.121 18.528 35.293 1.00 8.60 C ANISOU 1367 CG2 VAL A 160 1423 599 1246 -148 -251 -88 C ATOM 1368 N ILE A 161 36.933 18.818 39.493 1.00 7.90 N ANISOU 1368 N ILE A 161 1243 681 1077 -49 -51 -128 N ATOM 1369 CA ILE A 161 38.026 18.658 40.446 1.00 8.66 C ANISOU 1369 CA ILE A 161 1381 728 1179 -43 -210 -71 C ATOM 1370 C ILE A 161 37.546 17.862 41.660 1.00 8.37 C ANISOU 1370 C ILE A 161 1456 557 1166 -75 -152 -187 C ATOM 1371 O ILE A 161 38.346 16.967 42.120 1.00 8.90 O ANISOU 1371 O ILE A 161 1436 758 1187 -73 -190 -70 O ATOM 1372 CB ILE A 161 38.671 20.029 40.760 1.00 9.01 C ANISOU 1372 CB ILE A 161 1303 857 1262 -169 -220 -19 C ATOM 1373 CG2 ILE A 161 39.444 19.898 42.082 1.00 16.80 C ANISOU 1373 CG2 ILE A 161 2558 1444 2380 -801 -1585 507 C ATOM 1374 CG1AILE A 161 39.561 20.562 39.662 0.50 11.86 C ANISOU 1374 CG1AILE A 161 1587 763 2158 31 610 -195 C ATOM 1375 CD1AILE A 161 39.031 20.713 38.270 0.50 19.24 C ANISOU 1375 CD1AILE A 161 3940 1537 1832 -543 674 584 C ATOM 1376 CG1BILE A 161 39.498 20.610 39.631 0.50 14.13 C ANISOU 1376 CG1BILE A 161 1825 1277 2267 -243 573 155 C ATOM 1377 CD1BILE A 161 40.038 19.727 38.533 0.50 12.19 C ANISOU 1377 CD1BILE A 161 2060 1480 1092 -1398 81 -67 C ATOM 1378 N PRO A 162 36.373 18.072 42.260 1.00 9.10 N ANISOU 1378 N PRO A 162 1626 812 1019 125 -102 -89 N ATOM 1379 CA PRO A 162 35.952 17.147 43.349 1.00 9.46 C ANISOU 1379 CA PRO A 162 1688 914 993 12 -27 -184 C ATOM 1380 C PRO A 162 35.880 15.698 42.915 1.00 8.39 C ANISOU 1380 C PRO A 162 1308 889 991 56 -58 -81 C ATOM 1381 O PRO A 162 36.217 14.815 43.682 1.00 9.09 O ANISOU 1381 O PRO A 162 1435 952 1068 6 -74 44 O ATOM 1382 CB PRO A 162 34.567 17.713 43.790 1.00 10.18 C ANISOU 1382 CB PRO A 162 1864 1068 935 299 35 12 C ATOM 1383 CG PRO A 162 34.734 19.174 43.484 1.00 10.37 C ANISOU 1383 CG PRO A 162 1703 1148 1088 179 114 81 C ATOM 1384 CD PRO A 162 35.420 19.174 42.112 1.00 10.46 C ANISOU 1384 CD PRO A 162 1769 1064 1143 261 203 -43 C ATOM 1385 N TYR A 163 35.415 15.421 41.695 1.00 8.88 N ANISOU 1385 N TYR A 163 1405 866 1103 0 -75 -181 N ATOM 1386 CA TYR A 163 35.345 14.031 41.196 1.00 8.01 C ANISOU 1386 CA TYR A 163 1315 781 947 141 -119 -58 C ATOM 1387 C TYR A 163 36.727 13.410 41.072 1.00 7.77 C ANISOU 1387 C TYR A 163 1366 872 715 114 81 18 C ATOM 1388 O TYR A 163 36.984 12.254 41.443 1.00 7.71 O ANISOU 1388 O TYR A 163 1262 654 1013 5 -167 -22 O ATOM 1389 CB TYR A 163 34.562 13.998 39.891 1.00 8.79 C ANISOU 1389 CB TYR A 163 1560 788 991 -119 -197 12 C ATOM 1390 CG TYR A 163 34.248 12.640 39.337 1.00 7.44 C ANISOU 1390 CG TYR A 163 1098 643 1087 125 -134 -53 C ATOM 1391 CD1 TYR A 163 33.551 11.686 40.074 1.00 8.22 C ANISOU 1391 CD1 TYR A 163 1302 900 922 -191 -207 -167 C ATOM 1392 CD2 TYR A 163 34.607 12.258 38.056 1.00 8.33 C ANISOU 1392 CD2 TYR A 163 976 948 1241 -162 54 -195 C ATOM 1393 CE1 TYR A 163 33.247 10.439 39.600 1.00 7.31 C ANISOU 1393 CE1 TYR A 163 983 708 1087 7 0 -38 C ATOM 1394 CE2 TYR A 163 34.302 11.017 37.554 1.00 8.49 C ANISOU 1394 CE2 TYR A 163 1116 1014 1096 -284 65 -205 C ATOM 1395 CZ TYR A 163 33.620 10.077 38.320 1.00 7.42 C ANISOU 1395 CZ TYR A 163 1102 713 1005 42 -71 -67 C ATOM 1396 OH TYR A 163 33.326 8.860 37.761 1.00 8.66 O ANISOU 1396 OH TYR A 163 1279 782 1229 -37 12 -94 O ATOM 1397 N TRP A 164 37.661 14.217 40.555 1.00 8.57 N ANISOU 1397 N TRP A 164 1413 747 1098 45 38 85 N ATOM 1398 CA TRP A 164 39.087 13.875 40.542 1.00 8.12 C ANISOU 1398 CA TRP A 164 1386 596 1105 4 149 -69 C ATOM 1399 C TRP A 164 39.598 13.477 41.936 1.00 8.17 C ANISOU 1399 C TRP A 164 1253 690 1160 -82 13 -149 C ATOM 1400 O TRP A 164 40.164 12.383 42.138 1.00 8.76 O ANISOU 1400 O TRP A 164 1249 815 1265 -148 -135 -108 O ATOM 1401 CB TRP A 164 39.925 14.965 39.924 1.00 8.41 C ANISOU 1401 CB TRP A 164 1254 610 1331 24 27 -97 C ATOM 1402 CG TRP A 164 41.414 14.831 40.070 1.00 9.20 C ANISOU 1402 CG TRP A 164 1241 936 1319 -112 -47 -82 C ATOM 1403 CD1 TRP A 164 42.195 15.589 40.953 1.00 10.37 C ANISOU 1403 CD1 TRP A 164 1517 1148 1273 -333 -21 -185 C ATOM 1404 CD2 TRP A 164 42.298 13.974 39.358 1.00 8.33 C ANISOU 1404 CD2 TRP A 164 1162 855 1148 31 -134 66 C ATOM 1405 NE1 TRP A 164 43.518 15.219 40.801 1.00 10.55 N ANISOU 1405 NE1 TRP A 164 1505 1265 1240 -242 -220 -16 N ATOM 1406 CE2 TRP A 164 43.593 14.242 39.845 1.00 9.90 C ANISOU 1406 CE2 TRP A 164 1255 1106 1399 -39 -232 51 C ATOM 1407 CE3 TRP A 164 42.126 13.023 38.342 1.00 8.93 C ANISOU 1407 CE3 TRP A 164 1081 964 1347 -204 176 -69 C ATOM 1408 CZ2 TRP A 164 44.713 13.557 39.356 1.00 10.80 C ANISOU 1408 CZ2 TRP A 164 1113 1405 1587 -17 -255 79 C ATOM 1409 CZ3 TRP A 164 43.243 12.353 37.879 1.00 11.00 C ANISOU 1409 CZ3 TRP A 164 1209 1265 1706 54 -102 -377 C ATOM 1410 CH2 TRP A 164 44.498 12.639 38.391 1.00 11.19 C ANISOU 1410 CH2 TRP A 164 1148 1227 1877 5 -65 0 C ATOM 1411 N ASN A 165 39.405 14.378 42.923 1.00 8.78 N ANISOU 1411 N ASN A 165 1502 832 1003 -66 -65 -74 N ATOM 1412 CA ASN A 165 39.942 14.132 44.266 1.00 8.35 C ANISOU 1412 CA ASN A 165 1147 882 1142 -86 -163 -21 C ATOM 1413 C ASN A 165 39.210 13.036 45.036 1.00 8.70 C ANISOU 1413 C ASN A 165 1487 867 952 -221 -115 -129 C ATOM 1414 O ASN A 165 39.854 12.313 45.813 1.00 10.68 O ANISOU 1414 O ASN A 165 1702 1042 1314 -72 -176 90 O ATOM 1415 CB ASN A 165 39.935 15.455 45.052 1.00 10.30 C ANISOU 1415 CB ASN A 165 1880 878 1154 -23 -488 -53 C ATOM 1416 CG ASN A 165 41.082 16.368 44.697 1.00 13.29 C ANISOU 1416 CG ASN A 165 2541 922 1586 -429 -281 -412 C ATOM 1417 OD1 ASN A 165 42.183 15.875 44.470 1.00 15.10 O ANISOU 1417 OD1 ASN A 165 2328 1580 1829 -711 67 -241 O ATOM 1418 ND2 ASN A 165 40.792 17.657 44.640 1.00 17.35 N ANISOU 1418 ND2 ASN A 165 3593 906 2091 -479 -1113 175 N ATOM 1419 N GLU A 166 37.902 12.875 44.833 1.00 8.67 N ANISOU 1419 N GLU A 166 1468 943 882 -271 0 -213 N ATOM 1420 CA GLU A 166 37.121 11.884 45.604 1.00 8.00 C ANISOU 1420 CA GLU A 166 1277 878 883 -38 28 -124 C ATOM 1421 C GLU A 166 37.231 10.489 45.038 1.00 7.82 C ANISOU 1421 C GLU A 166 1320 812 839 106 11 -53 C ATOM 1422 O GLU A 166 37.184 9.516 45.799 1.00 9.36 O ANISOU 1422 O GLU A 166 1668 920 969 -42 -74 -26 O ATOM 1423 CB GLU A 166 35.635 12.293 45.582 1.00 8.98 C ANISOU 1423 CB GLU A 166 1341 1084 987 204 97 17 C ATOM 1424 CG GLU A 166 35.300 13.575 46.302 1.00 9.33 C ANISOU 1424 CG GLU A 166 1424 1347 776 140 77 -245 C ATOM 1425 CD GLU A 166 34.001 14.211 45.850 1.00 10.44 C ANISOU 1425 CD GLU A 166 1699 1035 1233 248 -51 -81 C ATOM 1426 OE1 GLU A 166 33.281 13.679 44.999 1.00 13.20 O ANISOU 1426 OE1 GLU A 166 1830 1518 1668 470 -442 -353 O ATOM 1427 OE2 GLU A 166 33.671 15.269 46.428 1.00 12.08 O ANISOU 1427 OE2 GLU A 166 1840 1477 1272 444 129 -201 O ATOM 1428 N THR A 167 37.367 10.388 43.723 1.00 8.15 N ANISOU 1428 N THR A 167 1325 869 903 -221 212 -124 N ATOM 1429 CA THR A 167 37.146 9.122 42.991 1.00 7.55 C ANISOU 1429 CA THR A 167 1344 767 760 -84 30 33 C ATOM 1430 C THR A 167 38.315 8.726 42.125 1.00 7.32 C ANISOU 1430 C THR A 167 1270 819 691 -5 -36 -13 C ATOM 1431 O THR A 167 38.885 7.602 42.249 1.00 8.17 O ANISOU 1431 O THR A 167 1308 821 975 -3 -137 91 O ATOM 1432 CB THR A 167 35.831 9.236 42.172 1.00 7.75 C ANISOU 1432 CB THR A 167 1257 796 893 39 50 30 C ATOM 1433 OG1 THR A 167 34.779 9.435 43.108 1.00 9.21 O ANISOU 1433 OG1 THR A 167 1318 1022 1160 -151 197 -223 O ATOM 1434 CG2 THR A 167 35.615 8.022 41.280 1.00 8.71 C ANISOU 1434 CG2 THR A 167 1446 1018 845 -123 76 -93 C ATOM 1435 N ILE A 168 38.756 9.553 41.188 1.00 7.08 N ANISOU 1435 N ILE A 168 1068 803 817 4 -88 53 N ATOM 1436 CA ILE A 168 39.722 9.131 40.161 1.00 6.35 C ANISOU 1436 CA ILE A 168 934 578 900 -46 -89 -70 C ATOM 1437 C ILE A 168 41.115 8.986 40.749 1.00 6.95 C ANISOU 1437 C ILE A 168 1057 651 933 -97 -223 17 C ATOM 1438 O ILE A 168 41.809 7.957 40.587 1.00 7.62 O ANISOU 1438 O ILE A 168 1083 777 1037 28 -220 -37 O ATOM 1439 CB ILE A 168 39.690 10.038 38.935 1.00 6.66 C ANISOU 1439 CB ILE A 168 807 799 925 -84 -63 26 C ATOM 1440 CG1 ILE A 168 38.292 10.142 38.321 1.00 7.32 C ANISOU 1440 CG1 ILE A 168 975 880 927 -88 -194 -47 C ATOM 1441 CG2 ILE A 168 40.715 9.536 37.922 1.00 7.56 C ANISOU 1441 CG2 ILE A 168 1064 863 945 -69 6 -71 C ATOM 1442 CD1 ILE A 168 38.166 11.084 37.112 1.00 8.51 C ANISOU 1442 CD1 ILE A 168 879 1264 1091 106 -156 200 C ATOM 1443 N LEU A 169 41.611 10.049 41.407 1.00 7.19 N ANISOU 1443 N LEU A 169 951 704 1075 -93 -218 -79 N ATOM 1444 CA LEU A 169 42.976 10.044 41.949 1.00 8.35 C ANISOU 1444 CA LEU A 169 1148 885 1139 -159 -376 9 C ATOM 1445 C LEU A 169 43.118 8.928 42.949 1.00 9.00 C ANISOU 1445 C LEU A 169 1421 856 1143 -53 -392 59 C ATOM 1446 O LEU A 169 44.147 8.230 42.948 1.00 9.87 O ANISOU 1446 O LEU A 169 1341 992 1416 -43 -479 -73 O ATOM 1447 CB LEU A 169 43.335 11.447 42.496 1.00 10.35 C ANISOU 1447 CB LEU A 169 1524 804 1604 -146 -690 -21 C ATOM 1448 CG LEU A 169 44.719 11.539 43.164 1.00 11.73 C ANISOU 1448 CG LEU A 169 1689 1013 1756 -372 -784 -58 C ATOM 1449 CD1 LEU A 169 45.818 11.150 42.187 1.00 14.44 C ANISOU 1449 CD1 LEU A 169 1519 1320 2647 -107 -568 116 C ATOM 1450 CD2 LEU A 169 44.868 12.956 43.731 1.00 14.70 C ANISOU 1450 CD2 LEU A 169 1951 934 2698 -208 -1284 -162 C ATOM 1451 N PRO A 170 42.195 8.665 43.884 1.00 9.09 N ANISOU 1451 N PRO A 170 1501 906 1045 -16 -399 51 N ATOM 1452 CA PRO A 170 42.384 7.514 44.788 1.00 10.12 C ANISOU 1452 CA PRO A 170 1696 883 1265 -148 -357 134 C ATOM 1453 C PRO A 170 42.538 6.185 44.060 1.00 9.84 C ANISOU 1453 C PRO A 170 1689 805 1244 -289 -228 192 C ATOM 1454 O PRO A 170 43.271 5.289 44.501 1.00 11.69 O ANISOU 1454 O PRO A 170 2049 974 1418 -58 -527 155 O ATOM 1455 CB PRO A 170 41.105 7.537 45.621 1.00 11.92 C ANISOU 1455 CB PRO A 170 2000 1261 1267 -221 -133 87 C ATOM 1456 CG PRO A 170 40.790 9.043 45.718 1.00 11.13 C ANISOU 1456 CG PRO A 170 1634 1355 1240 -93 -282 -58 C ATOM 1457 CD PRO A 170 41.059 9.490 44.303 1.00 9.85 C ANISOU 1457 CD PRO A 170 1458 1106 1180 -16 -391 -63 C ATOM 1458 N ARG A 171 41.803 6.012 42.950 1.00 9.97 N ANISOU 1458 N ARG A 171 1711 812 1265 23 -246 59 N ATOM 1459 CA ARG A 171 41.968 4.758 42.199 1.00 9.69 C ANISOU 1459 CA ARG A 171 1617 716 1348 -170 -266 132 C ATOM 1460 C ARG A 171 43.379 4.659 41.643 1.00 9.21 C ANISOU 1460 C ARG A 171 1496 738 1267 -34 -427 -6 C ATOM 1461 O ARG A 171 44.003 3.616 41.697 1.00 11.17 O ANISOU 1461 O ARG A 171 1856 757 1632 115 -474 -116 O ATOM 1462 CB ARG A 171 40.927 4.646 41.103 1.00 10.29 C ANISOU 1462 CB ARG A 171 1298 1140 1472 -158 -115 -151 C ATOM 1463 CG ARG A 171 41.064 3.294 40.409 1.00 10.59 C ANISOU 1463 CG ARG A 171 1247 1155 1623 -29 -223 -268 C ATOM 1464 CD ARG A 171 39.927 3.086 39.409 1.00 10.56 C ANISOU 1464 CD ARG A 171 1165 1246 1604 182 -161 -397 C ATOM 1465 NE ARG A 171 38.607 2.945 39.980 1.00 9.10 N ANISOU 1465 NE ARG A 171 1190 824 1444 103 -198 -320 N ATOM 1466 CZ ARG A 171 38.074 1.870 40.587 1.00 9.60 C ANISOU 1466 CZ ARG A 171 1481 981 1186 147 -278 -140 C ATOM 1467 NH1 ARG A 171 38.699 0.743 40.736 1.00 11.41 N ANISOU 1467 NH1 ARG A 171 1552 888 1897 145 -341 -189 N ATOM 1468 NH2 ARG A 171 36.824 1.922 41.059 1.00 10.25 N ANISOU 1468 NH2 ARG A 171 1608 1043 1243 158 -5 -99 N ATOM 1469 N MET A 172 43.889 5.768 41.087 1.00 8.95 N ANISOU 1469 N MET A 172 1145 872 1386 64 -357 97 N ATOM 1470 CA MET A 172 45.258 5.784 40.629 1.00 9.87 C ANISOU 1470 CA MET A 172 1152 980 1619 44 -320 -168 C ATOM 1471 C MET A 172 46.225 5.446 41.756 1.00 11.03 C ANISOU 1471 C MET A 172 1234 1033 1926 -73 -621 -127 C ATOM 1472 O MET A 172 47.145 4.672 41.561 1.00 13.53 O ANISOU 1472 O MET A 172 1744 1405 1992 393 -623 -12 O ATOM 1473 CB MET A 172 45.638 7.123 40.032 1.00 10.72 C ANISOU 1473 CB MET A 172 1389 1104 1581 -53 -113 -61 C ATOM 1474 CG MET A 172 44.794 7.492 38.849 1.00 10.78 C ANISOU 1474 CG MET A 172 1298 1257 1541 -28 -39 37 C ATOM 1475 SD MET A 172 44.992 9.219 38.401 1.00 12.60 S ANISOU 1475 SD MET A 172 1775 1349 1664 -94 -231 182 S ATOM 1476 CE MET A 172 46.846 9.220 38.266 1.00 10.04 C ANISOU 1476 CE MET A 172 1885 897 1034 -229 15 118 C ATOM 1477 N LYS A 173 46.004 5.978 42.927 1.00 11.54 N ANISOU 1477 N LYS A 173 1599 1013 1772 18 -670 29 N ATOM 1478 CA LYS A 173 46.931 5.783 44.040 1.00 15.13 C ANISOU 1478 CA LYS A 173 2360 1316 2071 118 -1190 -95 C ATOM 1479 C LYS A 173 46.942 4.328 44.504 1.00 17.73 C ANISOU 1479 C LYS A 173 2966 1369 2401 204 -1760 64 C ATOM 1480 O LYS A 173 47.962 3.881 45.057 1.00 19.29 O ANISOU 1480 O LYS A 173 2971 1698 2661 532 -1707 -163 O ATOM 1481 CB LYS A 173 46.676 6.743 45.196 1.00 14.25 C ANISOU 1481 CB LYS A 173 2133 1489 1792 148 -969 45 C ATOM 1482 CG LYS A 173 47.084 8.200 44.909 1.00 14.41 C ANISOU 1482 CG LYS A 173 2266 1445 1764 69 -984 -55 C ATOM 1483 CD LYS A 173 46.776 9.157 46.012 1.00 18.87 C ANISOU 1483 CD LYS A 173 3691 1705 1775 98 -809 -176 C ATOM 1484 CE LYS A 173 47.412 10.519 45.827 1.00 19.08 C ANISOU 1484 CE LYS A 173 3707 1590 1953 163 -1114 -275 C ATOM 1485 NZ LYS A 173 46.906 11.431 46.889 1.00 23.78 N ANISOU 1485 NZ LYS A 173 4731 1978 2326 -550 -192 -583 N ATOM 1486 N SER A 174 45.838 3.604 44.278 1.00 15.71 N ANISOU 1486 N SER A 174 2786 1115 2069 322 -1363 203 N ATOM 1487 CA SER A 174 45.744 2.179 44.596 1.00 17.40 C ANISOU 1487 CA SER A 174 3197 1231 2182 335 -765 378 C ATOM 1488 C SER A 174 46.510 1.278 43.619 1.00 18.31 C ANISOU 1488 C SER A 174 3141 1298 2518 126 -1041 -258 C ATOM 1489 O SER A 174 46.606 0.079 43.884 1.00 21.91 O ANISOU 1489 O SER A 174 3817 1442 3067 575 -1150 -75 O ATOM 1490 CB SER A 174 44.283 1.741 44.650 1.00 19.35 C ANISOU 1490 CB SER A 174 3453 1644 2257 -65 -478 449 C ATOM 1491 OG SER A 174 43.710 1.534 43.367 1.00 19.57 O ANISOU 1491 OG SER A 174 3637 1048 2753 -262 -955 239 O ATOM 1492 N GLY A 175 47.114 1.826 42.582 1.00 17.94 N ANISOU 1492 N GLY A 175 2593 1882 2340 722 -1011 -129 N ATOM 1493 CA GLY A 175 48.024 1.184 41.638 1.00 17.27 C ANISOU 1493 CA GLY A 175 2115 1481 2966 602 -1188 -492 C ATOM 1494 C GLY A 175 47.375 0.869 40.321 1.00 15.11 C ANISOU 1494 C GLY A 175 1843 1541 2356 532 -694 -74 C ATOM 1495 O GLY A 175 47.898 0.126 39.482 1.00 24.26 O ANISOU 1495 O GLY A 175 2415 3535 3266 1694 -1266 -1318 O ATOM 1496 N GLU A 176 46.195 1.359 40.022 1.00 12.60 N ANISOU 1496 N GLU A 176 1849 1494 1443 544 -357 282 N ATOM 1497 CA GLU A 176 45.495 1.113 38.773 1.00 12.64 C ANISOU 1497 CA GLU A 176 1819 1679 1306 514 -255 153 C ATOM 1498 C GLU A 176 45.822 2.130 37.689 1.00 12.09 C ANISOU 1498 C GLU A 176 1977 1272 1345 437 -450 99 C ATOM 1499 O GLU A 176 45.961 3.341 37.966 1.00 15.42 O ANISOU 1499 O GLU A 176 2948 1260 1650 788 -480 -140 O ATOM 1500 CB GLU A 176 43.964 1.073 38.987 1.00 11.79 C ANISOU 1500 CB GLU A 176 1788 1512 1181 734 -256 -54 C ATOM 1501 CG GLU A 176 43.616 -0.051 39.972 1.00 15.41 C ANISOU 1501 CG GLU A 176 2054 2016 1784 354 -151 344 C ATOM 1502 CD GLU A 176 42.138 -0.294 40.110 1.00 15.51 C ANISOU 1502 CD GLU A 176 2182 1888 1822 -47 -285 -244 C ATOM 1503 OE1 GLU A 176 41.381 0.066 39.207 1.00 16.70 O ANISOU 1503 OE1 GLU A 176 2099 1820 2426 119 -452 -114 O ATOM 1504 OE2 GLU A 176 41.694 -0.807 41.147 1.00 24.73 O ANISOU 1504 OE2 GLU A 176 2415 4761 2219 -449 8 537 O ATOM 1505 N ARG A 177 45.982 1.632 36.469 1.00 9.33 N ANISOU 1505 N ARG A 177 1235 951 1358 124 -552 105 N ATOM 1506 CA ARG A 177 46.282 2.450 35.287 1.00 8.19 C ANISOU 1506 CA ARG A 177 1189 661 1263 138 -571 -70 C ATOM 1507 C ARG A 177 44.965 2.963 34.726 1.00 6.71 C ANISOU 1507 C ARG A 177 926 581 1041 -64 -297 -40 C ATOM 1508 O ARG A 177 44.164 2.156 34.259 1.00 7.23 O ANISOU 1508 O ARG A 177 751 594 1401 18 -158 -77 O ATOM 1509 CB ARG A 177 47.054 1.649 34.265 1.00 8.87 C ANISOU 1509 CB ARG A 177 916 779 1675 127 -278 57 C ATOM 1510 CG ARG A 177 48.442 1.193 34.662 1.00 10.70 C ANISOU 1510 CG ARG A 177 998 695 2373 121 -494 137 C ATOM 1511 CD ARG A 177 48.988 0.125 33.704 1.00 12.65 C ANISOU 1511 CD ARG A 177 845 1184 2779 320 -29 126 C ATOM 1512 NE ARG A 177 48.220 -1.111 33.871 1.00 13.36 N ANISOU 1512 NE ARG A 177 1257 1034 2784 192 -552 -246 N ATOM 1513 CZ ARG A 177 48.454 -2.239 33.206 1.00 16.42 C ANISOU 1513 CZ ARG A 177 1470 1472 3296 26 -138 -642 C ATOM 1514 NH1 ARG A 177 49.447 -2.297 32.331 1.00 21.27 N ANISOU 1514 NH1 ARG A 177 1849 1891 4340 -212 469 -1269 N ATOM 1515 NH2 ARG A 177 47.688 -3.279 33.472 1.00 20.34 N ANISOU 1515 NH2 ARG A 177 2368 1445 3917 -406 454 -1241 N ATOM 1516 N VAL A 178 44.723 4.262 34.759 1.00 6.69 N ANISOU 1516 N VAL A 178 794 634 1115 -5 -247 40 N ATOM 1517 CA VAL A 178 43.468 4.908 34.369 1.00 6.01 C ANISOU 1517 CA VAL A 178 645 739 899 -111 -184 32 C ATOM 1518 C VAL A 178 43.599 5.596 33.003 1.00 5.79 C ANISOU 1518 C VAL A 178 586 493 1122 1 -157 112 C ATOM 1519 O VAL A 178 44.643 6.199 32.671 1.00 6.41 O ANISOU 1519 O VAL A 178 580 767 1089 -85 -164 67 O ATOM 1520 CB VAL A 178 43.037 5.905 35.468 1.00 6.55 C ANISOU 1520 CB VAL A 178 689 753 1045 -54 -123 30 C ATOM 1521 CG1 VAL A 178 41.889 6.767 34.997 1.00 7.99 C ANISOU 1521 CG1 VAL A 178 993 854 1187 125 -279 -82 C ATOM 1522 CG2 VAL A 178 42.698 5.170 36.773 1.00 7.86 C ANISOU 1522 CG2 VAL A 178 1106 941 940 -52 -15 5 C ATOM 1523 N ILE A 179 42.525 5.499 32.226 1.00 5.83 N ANISOU 1523 N ILE A 179 614 570 1033 -112 -211 168 N ATOM 1524 CA ILE A 179 42.249 6.337 31.046 1.00 6.23 C ANISOU 1524 CA ILE A 179 680 755 933 23 -31 149 C ATOM 1525 C ILE A 179 40.977 7.128 31.314 1.00 5.99 C ANISOU 1525 C ILE A 179 457 662 1158 -83 -274 120 C ATOM 1526 O ILE A 179 40.009 6.579 31.879 1.00 6.19 O ANISOU 1526 O ILE A 179 653 606 1092 -70 -74 100 O ATOM 1527 CB ILE A 179 42.162 5.519 29.755 1.00 6.54 C ANISOU 1527 CB ILE A 179 726 679 1080 -17 -210 106 C ATOM 1528 CG1 ILE A 179 41.936 6.415 28.517 1.00 6.76 C ANISOU 1528 CG1 ILE A 179 842 780 945 58 21 142 C ATOM 1529 CG2 ILE A 179 41.094 4.421 29.783 1.00 7.10 C ANISOU 1529 CG2 ILE A 179 903 791 1002 -156 76 79 C ATOM 1530 CD1 ILE A 179 42.149 5.776 27.188 1.00 8.72 C ANISOU 1530 CD1 ILE A 179 1311 955 1045 7 -39 20 C ATOM 1531 N ILE A 180 40.977 8.416 30.920 1.00 5.68 N ANISOU 1531 N ILE A 180 591 651 914 -48 -106 150 N ATOM 1532 CA ILE A 180 39.805 9.289 30.966 1.00 5.67 C ANISOU 1532 CA ILE A 180 592 572 989 -85 -128 66 C ATOM 1533 C ILE A 180 39.514 9.744 29.535 1.00 5.88 C ANISOU 1533 C ILE A 180 590 655 991 -10 -48 149 C ATOM 1534 O ILE A 180 40.355 10.398 28.909 1.00 6.93 O ANISOU 1534 O ILE A 180 691 801 1139 -100 -13 241 O ATOM 1535 CB ILE A 180 39.994 10.522 31.847 1.00 6.24 C ANISOU 1535 CB ILE A 180 796 613 961 -16 -62 149 C ATOM 1536 CG1 ILE A 180 40.460 10.121 33.270 1.00 6.75 C ANISOU 1536 CG1 ILE A 180 872 942 751 -16 28 45 C ATOM 1537 CG2 ILE A 180 38.743 11.375 31.879 1.00 7.08 C ANISOU 1537 CG2 ILE A 180 726 848 1116 59 -65 -43 C ATOM 1538 CD1 ILE A 180 40.818 11.317 34.131 1.00 7.92 C ANISOU 1538 CD1 ILE A 180 1170 800 1038 -18 -40 21 C ATOM 1539 N ALA A 181 38.315 9.398 29.007 1.00 5.72 N ANISOU 1539 N ALA A 181 766 547 860 -102 -73 144 N ATOM 1540 CA ALA A 181 37.835 9.841 27.694 1.00 5.22 C ANISOU 1540 CA ALA A 181 680 462 842 -74 -76 66 C ATOM 1541 C ALA A 181 36.738 10.869 27.970 1.00 5.46 C ANISOU 1541 C ALA A 181 848 567 661 39 42 30 C ATOM 1542 O ALA A 181 35.690 10.553 28.511 1.00 6.19 O ANISOU 1542 O ALA A 181 750 651 950 41 -48 87 O ATOM 1543 CB ALA A 181 37.311 8.699 26.889 1.00 6.56 C ANISOU 1543 CB ALA A 181 964 589 941 73 -132 -133 C ATOM 1544 N ALA A 182 36.997 12.135 27.584 1.00 6.07 N ANISOU 1544 N ALA A 182 780 520 1008 76 -101 -19 N ATOM 1545 CA ALA A 182 36.040 13.197 27.992 1.00 6.85 C ANISOU 1545 CA ALA A 182 1096 464 1043 87 71 33 C ATOM 1546 C ALA A 182 35.996 14.329 26.964 1.00 6.18 C ANISOU 1546 C ALA A 182 819 539 991 4 59 37 C ATOM 1547 O ALA A 182 35.964 14.031 25.737 1.00 7.10 O ANISOU 1547 O ALA A 182 1046 667 985 28 106 53 O ATOM 1548 CB ALA A 182 36.265 13.630 29.432 1.00 6.84 C ANISOU 1548 CB ALA A 182 1019 489 1090 95 -66 36 C ATOM 1549 N HIS A 183 35.945 15.565 27.384 1.00 5.91 N ANISOU 1549 N HIS A 183 740 573 931 82 -145 129 N ATOM 1550 CA HIS A 183 35.549 16.713 26.578 1.00 5.65 C ANISOU 1550 CA HIS A 183 633 552 962 -15 5 145 C ATOM 1551 C HIS A 183 36.523 17.864 26.710 1.00 6.46 C ANISOU 1551 C HIS A 183 750 521 1183 58 -146 58 C ATOM 1552 O HIS A 183 37.301 17.939 27.670 1.00 7.25 O ANISOU 1552 O HIS A 183 815 638 1302 -61 -186 86 O ATOM 1553 CB HIS A 183 34.140 17.194 26.993 1.00 5.79 C ANISOU 1553 CB HIS A 183 772 473 957 90 -121 -52 C ATOM 1554 CG HIS A 183 33.092 16.127 26.822 1.00 5.11 C ANISOU 1554 CG HIS A 183 516 445 980 112 -14 -93 C ATOM 1555 ND1 HIS A 183 32.414 15.938 25.637 1.00 5.79 N ANISOU 1555 ND1 HIS A 183 770 470 959 -18 -58 72 N ATOM 1556 CD2 HIS A 183 32.667 15.143 27.650 1.00 6.10 C ANISOU 1556 CD2 HIS A 183 743 734 842 -9 -131 -39 C ATOM 1557 CE1 HIS A 183 31.602 14.885 25.813 1.00 5.55 C ANISOU 1557 CE1 HIS A 183 676 536 897 -25 -181 53 C ATOM 1558 NE2 HIS A 183 31.724 14.349 27.006 1.00 5.60 N ANISOU 1558 NE2 HIS A 183 728 543 857 -5 -71 -18 N ATOM 1559 N GLY A 184 36.485 18.812 25.787 1.00 8.21 N ANISOU 1559 N GLY A 184 848 720 1552 -132 -150 338 N ATOM 1560 CA GLY A 184 37.304 19.985 25.824 1.00 8.87 C ANISOU 1560 CA GLY A 184 847 882 1640 -195 -116 322 C ATOM 1561 C GLY A 184 37.374 20.719 27.156 1.00 8.88 C ANISOU 1561 C GLY A 184 980 698 1696 -130 -246 324 C ATOM 1562 O GLY A 184 38.458 20.886 27.722 1.00 9.33 O ANISOU 1562 O GLY A 184 882 741 1923 -203 -279 278 O ATOM 1563 N ASN A 185 36.225 21.152 27.692 1.00 8.29 N ANISOU 1563 N ASN A 185 911 703 1535 -163 -322 264 N ATOM 1564 CA ASN A 185 36.294 21.953 28.906 1.00 8.48 C ANISOU 1564 CA ASN A 185 777 527 1917 -162 -471 45 C ATOM 1565 C ASN A 185 36.440 21.119 30.165 1.00 7.67 C ANISOU 1565 C ASN A 185 652 694 1568 -88 -185 -46 C ATOM 1566 O ASN A 185 37.020 21.625 31.132 1.00 8.75 O ANISOU 1566 O ASN A 185 1109 647 1570 -148 -126 -118 O ATOM 1567 CB AASN A 185 35.136 22.973 28.805 0.49 12.01 C ANISOU 1567 CB AASN A 185 1109 472 2981 82 -185 265 C ATOM 1568 CG AASN A 185 35.258 23.808 27.522 0.49 11.05 C ANISOU 1568 CG AASN A 185 1300 347 2550 -153 -881 -32 C ATOM 1569 OD1AASN A 185 36.269 24.489 27.298 0.49 13.55 O ANISOU 1569 OD1AASN A 185 1775 858 2515 -433 -367 172 O ATOM 1570 ND2AASN A 185 34.188 23.789 26.750 0.49 15.62 N ANISOU 1570 ND2AASN A 185 1851 948 3137 530 -1475 -983 N ATOM 1571 CB BASN A 185 35.004 22.766 29.168 0.51 8.36 C ANISOU 1571 CB BASN A 185 689 750 1739 -149 -566 17 C ATOM 1572 CG BASN A 185 34.975 24.087 28.420 0.51 8.61 C ANISOU 1572 CG BASN A 185 848 685 1739 -169 -805 -61 C ATOM 1573 OD1BASN A 185 35.531 25.106 28.826 0.51 7.52 O ANISOU 1573 OD1BASN A 185 1073 541 1244 -81 -650 -77 O ATOM 1574 ND2BASN A 185 34.333 24.019 27.249 0.51 9.08 N ANISOU 1574 ND2BASN A 185 1289 176 1986 -281 -1124 -30 N ATOM 1575 N SER A 186 35.981 19.877 30.193 1.00 7.20 N ANISOU 1575 N SER A 186 852 644 1240 -4 -103 -60 N ATOM 1576 CA SER A 186 36.227 19.050 31.384 1.00 6.73 C ANISOU 1576 CA SER A 186 837 543 1176 6 -12 -138 C ATOM 1577 C SER A 186 37.679 18.647 31.497 1.00 6.51 C ANISOU 1577 C SER A 186 801 502 1171 -45 -53 1 C ATOM 1578 O SER A 186 38.243 18.608 32.594 1.00 7.46 O ANISOU 1578 O SER A 186 974 651 1208 -48 -85 -161 O ATOM 1579 CB SER A 186 35.233 17.910 31.469 1.00 7.54 C ANISOU 1579 CB SER A 186 924 838 1101 -215 -49 -170 C ATOM 1580 OG SER A 186 35.203 17.098 30.315 1.00 7.10 O ANISOU 1580 OG SER A 186 970 747 982 -179 -81 -67 O ATOM 1581 N LEU A 187 38.341 18.376 30.357 1.00 6.87 N ANISOU 1581 N LEU A 187 700 705 1206 -45 -107 -128 N ATOM 1582 CA LEU A 187 39.765 18.102 30.353 1.00 7.29 C ANISOU 1582 CA LEU A 187 719 817 1235 -43 -151 -214 C ATOM 1583 C LEU A 187 40.605 19.365 30.570 1.00 7.95 C ANISOU 1583 C LEU A 187 675 934 1410 -91 9 -417 C ATOM 1584 O LEU A 187 41.599 19.329 31.293 1.00 9.12 O ANISOU 1584 O LEU A 187 856 1119 1491 -106 -147 -375 O ATOM 1585 CB LEU A 187 40.235 17.331 29.125 1.00 7.48 C ANISOU 1585 CB LEU A 187 820 821 1201 -15 -133 -187 C ATOM 1586 CG LEU A 187 39.668 15.915 28.968 1.00 7.57 C ANISOU 1586 CG LEU A 187 933 617 1325 66 74 -54 C ATOM 1587 CD1 LEU A 187 40.070 15.335 27.611 1.00 8.84 C ANISOU 1587 CD1 LEU A 187 1330 663 1366 172 -85 -236 C ATOM 1588 CD2 LEU A 187 40.083 15.025 30.112 1.00 8.39 C ANISOU 1588 CD2 LEU A 187 982 831 1373 159 -345 -161 C ATOM 1589 N ARG A 188 40.181 20.513 30.028 1.00 8.01 N ANISOU 1589 N ARG A 188 659 990 1397 -126 17 -288 N ATOM 1590 CA ARG A 188 40.860 21.774 30.333 1.00 9.22 C ANISOU 1590 CA ARG A 188 1000 1079 1424 -301 16 -214 C ATOM 1591 C ARG A 188 40.775 22.081 31.830 1.00 7.93 C ANISOU 1591 C ARG A 188 845 779 1389 -217 -139 -110 C ATOM 1592 O ARG A 188 41.745 22.569 32.415 1.00 8.96 O ANISOU 1592 O ARG A 188 980 863 1561 -283 -189 -184 O ATOM 1593 CB ARG A 188 40.368 22.920 29.434 1.00 9.79 C ANISOU 1593 CB ARG A 188 1272 1180 1268 -591 -72 -99 C ATOM 1594 CG ARG A 188 40.872 22.878 28.014 1.00 13.88 C ANISOU 1594 CG ARG A 188 1594 2445 1236 -1242 139 -176 C ATOM 1595 CD ARG A 188 40.193 23.810 27.007 1.00 16.51 C ANISOU 1595 CD ARG A 188 1568 3506 1198 -1319 -179 149 C ATOM 1596 NE ARG A 188 40.429 25.196 27.416 1.00 15.80 N ANISOU 1596 NE ARG A 188 1519 3074 1410 -735 -344 451 N ATOM 1597 CZ ARG A 188 39.581 26.127 27.841 1.00 16.14 C ANISOU 1597 CZ ARG A 188 1191 3320 1621 -555 -272 933 C ATOM 1598 NH1 ARG A 188 38.272 25.864 27.938 1.00 20.50 N ANISOU 1598 NH1 ARG A 188 1142 4672 1973 -746 -638 1231 N ATOM 1599 NH2 ARG A 188 40.026 27.344 28.190 1.00 16.29 N ANISOU 1599 NH2 ARG A 188 1235 3450 1503 -223 -161 243 N ATOM 1600 N ALA A 189 39.630 21.801 32.467 1.00 7.96 N ANISOU 1600 N ALA A 189 974 831 1220 -250 -106 -171 N ATOM 1601 CA ALA A 189 39.498 21.978 33.903 1.00 8.40 C ANISOU 1601 CA ALA A 189 1179 699 1313 -243 -113 -133 C ATOM 1602 C ALA A 189 40.546 21.155 34.657 1.00 8.34 C ANISOU 1602 C ALA A 189 1169 657 1342 -209 -179 -162 C ATOM 1603 O ALA A 189 41.246 21.669 35.541 1.00 9.44 O ANISOU 1603 O ALA A 189 1218 847 1522 -196 -235 -283 O ATOM 1604 CB ALA A 189 38.099 21.579 34.340 1.00 8.61 C ANISOU 1604 CB ALA A 189 1102 846 1324 -149 -16 -295 C ATOM 1605 N LEU A 190 40.646 19.855 34.298 1.00 8.74 N ANISOU 1605 N LEU A 190 1306 647 1368 -199 -186 -109 N ATOM 1606 CA LEU A 190 41.617 18.993 34.979 1.00 8.80 C ANISOU 1606 CA LEU A 190 1370 638 1337 -103 -22 -31 C ATOM 1607 C LEU A 190 43.036 19.457 34.705 1.00 8.40 C ANISOU 1607 C LEU A 190 1326 483 1382 -93 -200 -64 C ATOM 1608 O LEU A 190 43.854 19.492 35.641 1.00 10.66 O ANISOU 1608 O LEU A 190 1596 878 1577 -231 -368 -41 O ATOM 1609 CB LEU A 190 41.374 17.537 34.565 1.00 9.27 C ANISOU 1609 CB LEU A 190 1152 717 1652 -145 31 -82 C ATOM 1610 CG LEU A 190 42.308 16.507 35.238 1.00 9.75 C ANISOU 1610 CG LEU A 190 1369 687 1650 -95 -190 -125 C ATOM 1611 CD1 LEU A 190 42.210 16.527 36.765 1.00 11.93 C ANISOU 1611 CD1 LEU A 190 2167 759 1606 -51 -215 -206 C ATOM 1612 CD2 LEU A 190 42.056 15.129 34.695 1.00 11.07 C ANISOU 1612 CD2 LEU A 190 1569 767 1871 -189 -334 -332 C ATOM 1613 N VAL A 191 43.388 19.788 33.462 1.00 8.73 N ANISOU 1613 N VAL A 191 1070 742 1506 -202 -197 -31 N ATOM 1614 CA VAL A 191 44.750 20.242 33.118 1.00 9.38 C ANISOU 1614 CA VAL A 191 1099 752 1713 -335 -272 -106 C ATOM 1615 C VAL A 191 45.115 21.526 33.847 1.00 9.57 C ANISOU 1615 C VAL A 191 1016 871 1751 -243 -175 -286 C ATOM 1616 O VAL A 191 46.232 21.663 34.345 1.00 10.88 O ANISOU 1616 O VAL A 191 915 1022 2195 -419 -134 -252 O ATOM 1617 CB VAL A 191 44.948 20.379 31.595 1.00 11.21 C ANISOU 1617 CB VAL A 191 1375 1258 1626 -471 -59 -273 C ATOM 1618 CG1 VAL A 191 46.224 21.085 31.210 1.00 12.84 C ANISOU 1618 CG1 VAL A 191 1582 1417 1879 -552 27 -94 C ATOM 1619 CG2 VAL A 191 44.953 18.985 30.952 1.00 11.39 C ANISOU 1619 CG2 VAL A 191 1247 1267 1811 -227 -156 -316 C ATOM 1620 N LYS A 192 44.173 22.482 33.975 1.00 9.70 N ANISOU 1620 N LYS A 192 1155 802 1728 -257 -169 -231 N ATOM 1621 CA LYS A 192 44.482 23.699 34.714 1.00 9.86 C ANISOU 1621 CA LYS A 192 1259 670 1819 -360 -160 -184 C ATOM 1622 C LYS A 192 44.922 23.349 36.131 1.00 10.74 C ANISOU 1622 C LYS A 192 1469 639 1971 -194 -505 -202 C ATOM 1623 O LYS A 192 45.833 23.973 36.669 1.00 11.46 O ANISOU 1623 O LYS A 192 1342 916 2096 -229 -405 -308 O ATOM 1624 CB LYS A 192 43.250 24.602 34.792 1.00 9.93 C ANISOU 1624 CB LYS A 192 1412 872 1489 -191 -313 -156 C ATOM 1625 CG LYS A 192 43.506 25.953 35.385 1.00 11.23 C ANISOU 1625 CG LYS A 192 1532 917 1816 -225 -41 -381 C ATOM 1626 CD LYS A 192 42.269 26.790 35.630 1.00 11.27 C ANISOU 1626 CD LYS A 192 1416 1050 1817 -84 -330 -237 C ATOM 1627 CE ALYS A 192 42.622 28.150 36.238 0.69 12.61 C ANISOU 1627 CE ALYS A 192 1496 1118 2178 16 -242 -488 C ATOM 1628 NZ ALYS A 192 43.135 28.051 37.621 0.69 11.79 N ANISOU 1628 NZ ALYS A 192 1571 694 2217 -57 -290 -495 N ATOM 1629 CE BLYS A 192 42.602 28.245 35.924 0.31 12.18 C ANISOU 1629 CE BLYS A 192 1416 984 2228 85 -542 -206 C ATOM 1630 NZ BLYS A 192 43.415 28.436 37.150 0.31 12.84 N ANISOU 1630 NZ BLYS A 192 1332 1504 2044 -178 -265 -511 N ATOM 1631 N TYR A 193 44.207 22.401 36.746 1.00 9.76 N ANISOU 1631 N TYR A 193 1093 1014 1600 -134 -413 -210 N ATOM 1632 CA TYR A 193 44.458 22.025 38.121 1.00 11.08 C ANISOU 1632 CA TYR A 193 1427 1098 1685 -211 -441 -187 C ATOM 1633 C TYR A 193 45.802 21.293 38.249 1.00 11.59 C ANISOU 1633 C TYR A 193 1612 1272 1521 69 -464 -74 C ATOM 1634 O TYR A 193 46.629 21.568 39.124 1.00 14.21 O ANISOU 1634 O TYR A 193 1694 1469 2235 -51 -795 -397 O ATOM 1635 CB TYR A 193 43.333 21.159 38.629 1.00 11.97 C ANISOU 1635 CB TYR A 193 1709 1134 1703 -201 -202 -106 C ATOM 1636 CG TYR A 193 43.355 20.736 40.058 1.00 12.62 C ANISOU 1636 CG TYR A 193 1965 1120 1712 -674 -501 -41 C ATOM 1637 CD1 TYR A 193 43.090 21.689 41.076 1.00 13.58 C ANISOU 1637 CD1 TYR A 193 1872 1571 1718 -602 -486 -221 C ATOM 1638 CD2 TYR A 193 43.617 19.422 40.425 1.00 15.23 C ANISOU 1638 CD2 TYR A 193 2188 1299 2297 -429 -1107 86 C ATOM 1639 CE1 TYR A 193 43.112 21.318 42.409 1.00 15.28 C ANISOU 1639 CE1 TYR A 193 2538 1523 1743 -870 -234 -167 C ATOM 1640 CE2 TYR A 193 43.617 19.047 41.771 1.00 17.41 C ANISOU 1640 CE2 TYR A 193 2938 1270 2409 -375 -1206 274 C ATOM 1641 CZ TYR A 193 43.368 19.998 42.751 1.00 19.08 C ANISOU 1641 CZ TYR A 193 3352 1717 2181 -903 -1176 65 C ATOM 1642 OH TYR A 193 43.362 19.573 44.069 1.00 23.93 O ANISOU 1642 OH TYR A 193 5051 1821 2221 -1263 -1690 189 O ATOM 1643 N LEU A 194 46.022 20.337 37.340 1.00 11.46 N ANISOU 1643 N LEU A 194 1459 1069 1827 -85 -587 -87 N ATOM 1644 CA LEU A 194 47.279 19.586 37.421 1.00 12.46 C ANISOU 1644 CA LEU A 194 1488 974 2272 -130 -92 -18 C ATOM 1645 C LEU A 194 48.501 20.420 37.071 1.00 13.85 C ANISOU 1645 C LEU A 194 1489 1590 2184 -620 -588 50 C ATOM 1646 O LEU A 194 49.578 20.189 37.656 1.00 17.15 O ANISOU 1646 O LEU A 194 1710 1420 3384 -242 -944 -188 O ATOM 1647 CB LEU A 194 47.168 18.386 36.511 1.00 11.44 C ANISOU 1647 CB LEU A 194 1309 898 2140 -37 -395 55 C ATOM 1648 CG LEU A 194 46.149 17.304 36.860 1.00 11.70 C ANISOU 1648 CG LEU A 194 1620 1097 1727 -216 -252 52 C ATOM 1649 CD1 LEU A 194 46.182 16.163 35.860 1.00 11.81 C ANISOU 1649 CD1 LEU A 194 1355 944 2189 -99 -214 -30 C ATOM 1650 CD2 LEU A 194 46.479 16.668 38.205 1.00 15.56 C ANISOU 1650 CD2 LEU A 194 2576 1309 2028 -202 -514 321 C ATOM 1651 N ASP A 195 48.393 21.345 36.108 1.00 13.66 N ANISOU 1651 N ASP A 195 1742 809 2639 -197 -56 -45 N ATOM 1652 CA ASP A 195 49.501 22.161 35.615 1.00 11.99 C ANISOU 1652 CA ASP A 195 1306 990 2258 -160 -237 -247 C ATOM 1653 C ASP A 195 49.659 23.456 36.392 1.00 12.53 C ANISOU 1653 C ASP A 195 1394 1066 2302 -249 -220 -205 C ATOM 1654 O ASP A 195 50.541 24.262 36.079 1.00 14.26 O ANISOU 1654 O ASP A 195 1079 1289 3051 -333 -176 -450 O ATOM 1655 CB ASP A 195 49.328 22.442 34.095 1.00 13.26 C ANISOU 1655 CB ASP A 195 1401 1378 2258 -79 -182 -197 C ATOM 1656 CG ASP A 195 49.548 21.268 33.188 1.00 12.67 C ANISOU 1656 CG ASP A 195 1043 1511 2262 -331 155 -251 C ATOM 1657 OD1 ASP A 195 49.516 20.141 33.689 1.00 15.00 O ANISOU 1657 OD1 ASP A 195 1834 1368 2496 -332 -63 -378 O ATOM 1658 OD2 ASP A 195 49.700 21.487 31.969 1.00 16.71 O ANISOU 1658 OD2 ASP A 195 2137 1881 2331 -477 426 -313 O ATOM 1659 N ASN A 196 48.847 23.747 37.405 1.00 13.48 N ANISOU 1659 N ASN A 196 1869 1189 2065 -371 -115 -324 N ATOM 1660 CA ASN A 196 48.947 25.011 38.139 1.00 14.40 C ANISOU 1660 CA ASN A 196 2159 1449 1865 -356 -495 -383 C ATOM 1661 C ASN A 196 48.843 26.207 37.220 1.00 14.30 C ANISOU 1661 C ASN A 196 2029 1185 2221 -370 -656 -455 C ATOM 1662 O ASN A 196 49.522 27.200 37.404 1.00 15.06 O ANISOU 1662 O ASN A 196 1801 1366 2553 -345 -815 -349 O ATOM 1663 CB ASN A 196 50.248 25.092 38.973 1.00 16.05 C ANISOU 1663 CB ASN A 196 2304 1857 1939 -381 -611 -314 C ATOM 1664 CG ASN A 196 50.458 23.832 39.770 1.00 18.32 C ANISOU 1664 CG ASN A 196 2380 2275 2303 -3 -442 42 C ATOM 1665 OD1 ASN A 196 51.491 23.144 39.730 1.00 26.63 O ANISOU 1665 OD1 ASN A 196 3104 2917 4096 781 -789 -173 O ATOM 1666 ND2 ASN A 196 49.423 23.534 40.529 1.00 22.85 N ANISOU 1666 ND2 ASN A 196 3146 3494 2043 -667 -280 381 N ATOM 1667 N MET A 197 47.927 26.152 36.255 1.00 12.77 N ANISOU 1667 N MET A 197 1672 938 2240 -262 -519 -404 N ATOM 1668 CA MET A 197 47.788 27.257 35.318 1.00 11.91 C ANISOU 1668 CA MET A 197 1354 1012 2160 -394 -166 -325 C ATOM 1669 C MET A 197 46.915 28.411 35.812 1.00 11.65 C ANISOU 1669 C MET A 197 1104 892 2430 -393 -351 -443 C ATOM 1670 O MET A 197 45.946 28.227 36.585 1.00 11.89 O ANISOU 1670 O MET A 197 1377 1051 2091 -165 -320 -228 O ATOM 1671 CB MET A 197 47.169 26.760 34.010 1.00 11.94 C ANISOU 1671 CB MET A 197 1502 1004 2032 -311 -121 -259 C ATOM 1672 CG MET A 197 48.119 25.963 33.125 1.00 14.46 C ANISOU 1672 CG MET A 197 1712 1555 2228 32 -271 -507 C ATOM 1673 SD MET A 197 47.277 25.290 31.694 1.00 19.21 S ANISOU 1673 SD MET A 197 1692 2894 2712 -486 -211 -1209 S ATOM 1674 CE MET A 197 48.628 24.457 30.903 1.00 21.51 C ANISOU 1674 CE MET A 197 3193 2285 2696 752 -271 -962 C ATOM 1675 N SER A 198 47.261 29.613 35.352 1.00 11.79 N ANISOU 1675 N SER A 198 1373 1068 2037 -249 -174 -404 N ATOM 1676 CA SER A 198 46.477 30.821 35.620 1.00 13.24 C ANISOU 1676 CA SER A 198 1714 872 2444 -233 -664 -393 C ATOM 1677 C SER A 198 45.217 30.828 34.739 1.00 11.88 C ANISOU 1677 C SER A 198 1327 1362 1827 -215 -188 -304 C ATOM 1678 O SER A 198 45.103 30.055 33.772 1.00 12.86 O ANISOU 1678 O SER A 198 1473 1318 2095 -221 -347 -390 O ATOM 1679 CB SER A 198 47.300 32.100 35.379 1.00 13.19 C ANISOU 1679 CB SER A 198 1809 1144 2058 -411 -519 -249 C ATOM 1680 OG SER A 198 47.619 32.127 33.998 1.00 15.49 O ANISOU 1680 OG SER A 198 2001 1706 2178 -301 -399 -371 O ATOM 1681 N GLU A 199 44.300 31.771 35.026 1.00 13.53 N ANISOU 1681 N GLU A 199 1829 1133 2180 25 -240 -173 N ATOM 1682 CA GLU A 199 43.220 31.929 34.061 1.00 13.66 C ANISOU 1682 CA GLU A 199 1617 1027 2548 -68 -211 74 C ATOM 1683 C GLU A 199 43.744 32.278 32.661 1.00 14.60 C ANISOU 1683 C GLU A 199 1706 1403 2438 70 -305 219 C ATOM 1684 O GLU A 199 43.226 31.776 31.669 1.00 16.32 O ANISOU 1684 O GLU A 199 1530 2124 2548 -36 -165 6 O ATOM 1685 CB GLU A 199 42.247 33.016 34.531 1.00 14.88 C ANISOU 1685 CB GLU A 199 1767 1040 2844 -122 -198 -211 C ATOM 1686 CG GLU A 199 41.480 32.702 35.760 1.00 15.51 C ANISOU 1686 CG GLU A 199 2053 1481 2359 140 -323 -358 C ATOM 1687 CD GLU A 199 40.504 33.768 36.190 1.00 15.25 C ANISOU 1687 CD GLU A 199 1796 1075 2923 -187 -145 -288 C ATOM 1688 OE1 GLU A 199 40.043 34.594 35.388 1.00 19.09 O ANISOU 1688 OE1 GLU A 199 2374 1304 3574 153 -169 43 O ATOM 1689 OE2 GLU A 199 40.140 33.751 37.374 1.00 18.23 O ANISOU 1689 OE2 GLU A 199 2344 1650 2931 176 -1 -580 O ATOM 1690 N GLU A 200 44.724 33.199 32.581 1.00 14.72 N ANISOU 1690 N GLU A 200 1995 1271 2326 27 -163 303 N ATOM 1691 CA GLU A 200 45.275 33.590 31.256 1.00 17.64 C ANISOU 1691 CA GLU A 200 2005 2127 2571 96 118 404 C ATOM 1692 C GLU A 200 45.849 32.394 30.523 1.00 17.75 C ANISOU 1692 C GLU A 200 1659 2311 2775 -83 250 114 C ATOM 1693 O GLU A 200 45.713 32.172 29.300 1.00 21.05 O ANISOU 1693 O GLU A 200 2751 2780 2468 782 712 498 O ATOM 1694 CB GLU A 200 46.206 34.766 31.588 1.00 24.93 C ANISOU 1694 CB GLU A 200 4142 1733 3598 -796 451 700 C ATOM 1695 CG GLU A 200 45.546 35.915 32.354 1.00 34.39 C ANISOU 1695 CG GLU A 200 5348 3250 4471 -552 126 -999 C ATOM 1696 CD GLU A 200 45.055 35.929 33.776 1.00 34.89 C ANISOU 1696 CD GLU A 200 5353 3024 4878 1333 727 243 C ATOM 1697 OE1 GLU A 200 45.466 35.074 34.629 1.00 27.44 O ANISOU 1697 OE1 GLU A 200 3748 1549 5130 -784 -883 -295 O ATOM 1698 OE2 GLU A 200 44.210 36.833 34.076 1.00 35.72 O ANISOU 1698 OE2 GLU A 200 4749 2100 6723 464 1635 525 O ATOM 1699 N GLU A 201 46.554 31.481 31.207 1.00 15.28 N ANISOU 1699 N GLU A 201 1881 1530 2392 -525 152 -156 N ATOM 1700 CA GLU A 201 47.177 30.307 30.573 1.00 14.94 C ANISOU 1700 CA GLU A 201 1411 1921 2344 -452 168 -335 C ATOM 1701 C GLU A 201 46.134 29.332 30.115 1.00 14.42 C ANISOU 1701 C GLU A 201 1234 1924 2323 -272 63 -554 C ATOM 1702 O GLU A 201 46.251 28.865 29.003 1.00 17.40 O ANISOU 1702 O GLU A 201 1661 2666 2285 -524 169 -584 O ATOM 1703 CB GLU A 201 48.183 29.652 31.532 1.00 16.69 C ANISOU 1703 CB GLU A 201 1638 1762 2941 -556 -419 -620 C ATOM 1704 CG GLU A 201 49.480 30.464 31.700 1.00 16.77 C ANISOU 1704 CG GLU A 201 1205 2773 2394 -766 305 -12 C ATOM 1705 CD GLU A 201 50.348 30.000 32.834 1.00 17.84 C ANISOU 1705 CD GLU A 201 1625 2559 2594 -889 -187 -204 C ATOM 1706 OE1 GLU A 201 49.849 29.427 33.837 1.00 15.09 O ANISOU 1706 OE1 GLU A 201 1128 1877 2729 -220 -142 -125 O ATOM 1707 OE2 GLU A 201 51.575 30.299 32.732 1.00 21.72 O ANISOU 1707 OE2 GLU A 201 1770 4015 2466 -1169 -339 392 O ATOM 1708 N ILE A 202 45.101 29.065 30.922 1.00 14.12 N ANISOU 1708 N ILE A 202 1269 1890 2206 -356 -32 -239 N ATOM 1709 CA ILE A 202 44.166 28.045 30.470 1.00 12.59 C ANISOU 1709 CA ILE A 202 1129 1863 1791 -199 -37 -113 C ATOM 1710 C ILE A 202 43.339 28.511 29.279 1.00 12.90 C ANISOU 1710 C ILE A 202 1345 2064 1494 28 124 -94 C ATOM 1711 O ILE A 202 42.900 27.716 28.433 1.00 12.80 O ANISOU 1711 O ILE A 202 1136 2136 1591 34 -9 -57 O ATOM 1712 CB ILE A 202 43.237 27.562 31.620 1.00 11.80 C ANISOU 1712 CB ILE A 202 1121 1816 1547 -170 -258 -9 C ATOM 1713 CG1 ILE A 202 42.607 26.224 31.270 1.00 11.30 C ANISOU 1713 CG1 ILE A 202 1234 1709 1351 -117 -135 -34 C ATOM 1714 CG2 ILE A 202 42.232 28.635 31.988 1.00 13.77 C ANISOU 1714 CG2 ILE A 202 1370 1887 1975 -235 131 -423 C ATOM 1715 CD1 ILE A 202 43.537 25.071 30.943 1.00 13.14 C ANISOU 1715 CD1 ILE A 202 1268 2013 1710 39 110 -206 C ATOM 1716 N LEU A 203 43.093 29.812 29.165 1.00 13.75 N ANISOU 1716 N LEU A 203 1431 2075 1718 -24 -236 -161 N ATOM 1717 CA LEU A 203 42.339 30.370 28.034 1.00 16.64 C ANISOU 1717 CA LEU A 203 2200 2269 1854 -416 -315 518 C ATOM 1718 C LEU A 203 43.076 30.097 26.734 1.00 14.82 C ANISOU 1718 C LEU A 203 2254 1618 1758 -955 -490 262 C ATOM 1719 O LEU A 203 42.461 29.991 25.683 1.00 17.89 O ANISOU 1719 O LEU A 203 2822 2143 1831 -754 -791 509 O ATOM 1720 CB LEU A 203 41.999 31.835 28.199 1.00 23.81 C ANISOU 1720 CB LEU A 203 4640 2679 1727 743 -557 400 C ATOM 1721 CG LEU A 203 42.983 32.861 28.703 1.00 35.60 C ANISOU 1721 CG LEU A 203 7599 2198 3729 -704 -184 36 C ATOM 1722 CD1 LEU A 203 43.890 33.486 27.648 1.00 48.04 C ANISOU 1722 CD1 LEU A 203 8127 6878 3248 -3433 -139 -1062 C ATOM 1723 CD2 LEU A 203 42.203 34.013 29.360 1.00 46.98 C ANISOU 1723 CD2 LEU A 203 9226 3177 5449 -173 358 -946 C ATOM 1724 N GLU A 204 44.382 29.948 26.745 1.00 15.61 N ANISOU 1724 N GLU A 204 2228 1927 1775 -1075 -241 -187 N ATOM 1725 CA GLU A 204 45.133 29.696 25.510 1.00 18.36 C ANISOU 1725 CA GLU A 204 2952 2139 1884 -1622 203 -316 C ATOM 1726 C GLU A 204 45.124 28.248 25.100 1.00 17.20 C ANISOU 1726 C GLU A 204 2866 2045 1623 -1452 255 -142 C ATOM 1727 O GLU A 204 45.485 27.930 23.966 1.00 17.39 O ANISOU 1727 O GLU A 204 2783 2065 1760 -1052 381 29 O ATOM 1728 CB GLU A 204 46.594 30.147 25.692 1.00 25.13 C ANISOU 1728 CB GLU A 204 3129 3453 2967 -2216 985 -1517 C ATOM 1729 CG GLU A 204 46.734 31.663 25.591 1.00 39.80 C ANISOU 1729 CG GLU A 204 4900 3791 6430 -3439 1614 -981 C ATOM 1730 CD GLU A 204 46.662 32.088 24.116 1.00 48.40 C ANISOU 1730 CD GLU A 204 6717 4092 7581 -2275 850 774 C ATOM 1731 OE1 GLU A 204 47.202 31.334 23.263 1.00 58.89 O ANISOU 1731 OE1 GLU A 204 6963 9256 6156 -1066 2830 1667 O ATOM 1732 OE2 GLU A 204 46.060 33.133 23.803 1.00 79.20 O ANISOU 1732 OE2 GLU A 204 9740 7214 13139 379 -1068 2003 O ATOM 1733 N LEU A 205 44.830 27.322 26.005 1.00 13.46 N ANISOU 1733 N LEU A 205 1593 2004 1516 -844 9 -30 N ATOM 1734 CA LEU A 205 44.983 25.909 25.730 1.00 12.77 C ANISOU 1734 CA LEU A 205 1313 2058 1480 -240 -81 64 C ATOM 1735 C LEU A 205 43.785 25.354 24.968 1.00 9.64 C ANISOU 1735 C LEU A 205 1271 1222 1170 -177 61 266 C ATOM 1736 O LEU A 205 42.637 25.476 25.407 1.00 11.18 O ANISOU 1736 O LEU A 205 1248 1449 1551 -140 128 155 O ATOM 1737 CB LEU A 205 45.164 25.061 26.998 1.00 14.18 C ANISOU 1737 CB LEU A 205 1616 2316 1458 -366 -267 175 C ATOM 1738 CG LEU A 205 45.156 23.525 26.792 1.00 16.38 C ANISOU 1738 CG LEU A 205 2009 2282 1934 252 87 221 C ATOM 1739 CD1 LEU A 205 46.331 23.035 25.970 1.00 20.56 C ANISOU 1739 CD1 LEU A 205 1882 3354 2575 857 -47 198 C ATOM 1740 CD2 LEU A 205 45.113 22.830 28.175 1.00 17.66 C ANISOU 1740 CD2 LEU A 205 2615 2031 2066 78 -393 215 C ATOM 1741 N ASN A 206 44.063 24.664 23.877 1.00 10.03 N ANISOU 1741 N ASN A 206 1026 1377 1406 -151 9 152 N ATOM 1742 CA ASN A 206 43.082 23.837 23.181 1.00 11.15 C ANISOU 1742 CA ASN A 206 1418 1341 1477 -272 -68 117 C ATOM 1743 C ASN A 206 43.616 22.422 23.136 1.00 11.01 C ANISOU 1743 C ASN A 206 1224 1239 1720 -303 245 247 C ATOM 1744 O ASN A 206 44.699 22.139 22.616 1.00 15.42 O ANISOU 1744 O ASN A 206 1276 1478 3104 -217 549 663 O ATOM 1745 CB ASN A 206 42.818 24.363 21.784 1.00 13.47 C ANISOU 1745 CB ASN A 206 1368 1948 1802 -318 -526 477 C ATOM 1746 CG ASN A 206 42.427 25.817 21.757 1.00 17.32 C ANISOU 1746 CG ASN A 206 3042 2387 1153 731 -303 319 C ATOM 1747 OD1 ASN A 206 41.375 26.170 22.215 1.00 26.10 O ANISOU 1747 OD1 ASN A 206 3437 4461 2018 1969 -350 189 O ATOM 1748 ND2 ASN A 206 43.300 26.610 21.131 1.00 21.41 N ANISOU 1748 ND2 ASN A 206 4584 1655 1895 113 -389 576 N ATOM 1749 N ILE A 207 42.849 21.500 23.686 1.00 11.15 N ANISOU 1749 N ILE A 207 1459 1282 1496 -580 370 -195 N ATOM 1750 CA ILE A 207 43.231 20.074 23.606 1.00 12.21 C ANISOU 1750 CA ILE A 207 1842 1282 1515 -727 61 26 C ATOM 1751 C ILE A 207 42.628 19.469 22.344 1.00 10.20 C ANISOU 1751 C ILE A 207 1256 986 1633 -552 215 -86 C ATOM 1752 O ILE A 207 41.393 19.519 22.205 1.00 11.84 O ANISOU 1752 O ILE A 207 1212 1554 1734 -504 264 -363 O ATOM 1753 CB ILE A 207 42.797 19.314 24.871 1.00 13.92 C ANISOU 1753 CB ILE A 207 2250 1468 1571 -917 325 -26 C ATOM 1754 CG1 ILE A 207 43.429 19.923 26.128 1.00 16.81 C ANISOU 1754 CG1 ILE A 207 3167 1806 1412 -861 271 -254 C ATOM 1755 CG2 ILE A 207 43.125 17.847 24.722 1.00 14.40 C ANISOU 1755 CG2 ILE A 207 2560 1389 1524 -879 34 17 C ATOM 1756 CD1 ILE A 207 42.908 19.304 27.419 1.00 15.94 C ANISOU 1756 CD1 ILE A 207 2114 2330 1612 -1157 418 -357 C ATOM 1757 N PRO A 208 43.391 18.977 21.383 1.00 9.39 N ANISOU 1757 N PRO A 208 1101 988 1479 -155 -15 172 N ATOM 1758 CA PRO A 208 42.773 18.528 20.130 1.00 9.01 C ANISOU 1758 CA PRO A 208 1142 935 1346 -194 59 199 C ATOM 1759 C PRO A 208 42.004 17.223 20.287 1.00 7.16 C ANISOU 1759 C PRO A 208 826 809 1086 24 171 138 C ATOM 1760 O PRO A 208 42.271 16.376 21.116 1.00 8.55 O ANISOU 1760 O PRO A 208 1132 937 1179 -84 -79 251 O ATOM 1761 CB PRO A 208 43.917 18.334 19.163 1.00 10.81 C ANISOU 1761 CB PRO A 208 1237 1270 1600 -400 337 288 C ATOM 1762 CG PRO A 208 45.119 18.840 19.854 1.00 18.41 C ANISOU 1762 CG PRO A 208 1154 3287 2552 -69 302 -1397 C ATOM 1763 CD PRO A 208 44.857 18.975 21.354 1.00 10.87 C ANISOU 1763 CD PRO A 208 1049 1017 2065 -66 -119 88 C ATOM 1764 N THR A 209 40.999 17.044 19.413 1.00 7.98 N ANISOU 1764 N THR A 209 1207 735 1090 -108 -45 190 N ATOM 1765 CA THR A 209 40.184 15.831 19.437 1.00 7.21 C ANISOU 1765 CA THR A 209 1138 665 937 -33 161 39 C ATOM 1766 C THR A 209 41.035 14.589 19.141 1.00 7.19 C ANISOU 1766 C THR A 209 960 703 1070 -168 126 -43 C ATOM 1767 O THR A 209 41.864 14.535 18.220 1.00 8.46 O ANISOU 1767 O THR A 209 1077 987 1150 36 242 180 O ATOM 1768 CB THR A 209 39.004 15.908 18.459 1.00 8.28 C ANISOU 1768 CB THR A 209 1196 867 1085 -44 18 0 C ATOM 1769 OG1 THR A 209 39.464 16.092 17.084 1.00 8.86 O ANISOU 1769 OG1 THR A 209 1344 838 1184 -12 -27 372 O ATOM 1770 CG2 THR A 209 38.008 17.020 18.777 1.00 9.22 C ANISOU 1770 CG2 THR A 209 1220 946 1338 83 -63 197 C ATOM 1771 N GLY A 210 40.807 13.519 19.890 1.00 6.87 N ANISOU 1771 N GLY A 210 872 747 991 90 128 35 N ATOM 1772 CA GLY A 210 41.415 12.236 19.606 1.00 7.33 C ANISOU 1772 CA GLY A 210 922 813 1050 204 0 85 C ATOM 1773 C GLY A 210 42.900 12.080 19.806 1.00 6.78 C ANISOU 1773 C GLY A 210 908 586 1083 75 108 110 C ATOM 1774 O GLY A 210 43.470 11.098 19.309 1.00 10.01 O ANISOU 1774 O GLY A 210 894 1073 1836 263 -174 -377 O ATOM 1775 N VAL A 211 43.538 12.960 20.543 1.00 7.36 N ANISOU 1775 N VAL A 211 910 758 1126 -8 82 66 N ATOM 1776 CA VAL A 211 44.989 12.905 20.709 1.00 7.39 C ANISOU 1776 CA VAL A 211 881 757 1168 7 195 140 C ATOM 1777 C VAL A 211 45.359 12.473 22.136 1.00 7.34 C ANISOU 1777 C VAL A 211 988 628 1175 -142 -50 19 C ATOM 1778 O VAL A 211 45.058 13.216 23.097 1.00 7.80 O ANISOU 1778 O VAL A 211 865 878 1219 22 4 11 O ATOM 1779 CB VAL A 211 45.694 14.247 20.402 1.00 8.74 C ANISOU 1779 CB VAL A 211 994 800 1527 -68 -91 271 C ATOM 1780 CG1 VAL A 211 47.211 14.149 20.660 1.00 9.99 C ANISOU 1780 CG1 VAL A 211 976 1052 1767 -252 117 182 C ATOM 1781 CG2 VAL A 211 45.428 14.682 18.956 1.00 9.73 C ANISOU 1781 CG2 VAL A 211 1306 1070 1322 -28 321 329 C ATOM 1782 N PRO A 212 45.982 11.313 22.358 1.00 6.92 N ANISOU 1782 N PRO A 212 845 681 1104 -133 -14 38 N ATOM 1783 CA PRO A 212 46.335 10.951 23.752 1.00 7.46 C ANISOU 1783 CA PRO A 212 943 707 1184 -141 10 129 C ATOM 1784 C PRO A 212 47.280 11.950 24.412 1.00 6.77 C ANISOU 1784 C PRO A 212 710 802 1060 -85 34 100 C ATOM 1785 O PRO A 212 48.265 12.328 23.804 1.00 7.91 O ANISOU 1785 O PRO A 212 874 865 1267 -150 129 96 O ATOM 1786 CB PRO A 212 46.965 9.564 23.614 1.00 7.89 C ANISOU 1786 CB PRO A 212 956 767 1275 -72 54 141 C ATOM 1787 CG PRO A 212 46.417 9.043 22.313 1.00 8.77 C ANISOU 1787 CG PRO A 212 1355 701 1275 -76 -22 97 C ATOM 1788 CD PRO A 212 46.369 10.241 21.420 1.00 8.39 C ANISOU 1788 CD PRO A 212 1248 727 1213 -65 221 66 C ATOM 1789 N LEU A 213 46.950 12.352 25.636 1.00 7.09 N ANISOU 1789 N LEU A 213 677 878 1140 -97 -71 36 N ATOM 1790 CA LEU A 213 47.728 13.249 26.494 1.00 6.58 C ANISOU 1790 CA LEU A 213 570 758 1173 -165 -19 98 C ATOM 1791 C LEU A 213 48.108 12.452 27.728 1.00 6.54 C ANISOU 1791 C LEU A 213 647 671 1168 -232 -31 102 C ATOM 1792 O LEU A 213 47.248 12.051 28.522 1.00 7.87 O ANISOU 1792 O LEU A 213 678 1095 1219 -251 5 140 O ATOM 1793 CB LEU A 213 46.919 14.519 26.823 1.00 8.40 C ANISOU 1793 CB LEU A 213 1050 658 1484 -117 46 201 C ATOM 1794 CG LEU A 213 47.552 15.486 27.826 1.00 8.72 C ANISOU 1794 CG LEU A 213 1221 654 1437 -122 39 138 C ATOM 1795 CD1 LEU A 213 48.939 15.897 27.421 1.00 10.11 C ANISOU 1795 CD1 LEU A 213 1221 964 1658 -275 15 -51 C ATOM 1796 CD2 LEU A 213 46.645 16.686 28.019 1.00 11.16 C ANISOU 1796 CD2 LEU A 213 1651 803 1787 87 257 56 C ATOM 1797 N VAL A 214 49.395 12.151 27.872 1.00 7.48 N ANISOU 1797 N VAL A 214 607 954 1280 -160 6 201 N ATOM 1798 CA VAL A 214 49.916 11.339 28.950 1.00 7.50 C ANISOU 1798 CA VAL A 214 642 872 1334 -267 -49 222 C ATOM 1799 C VAL A 214 50.502 12.197 30.065 1.00 8.27 C ANISOU 1799 C VAL A 214 580 1107 1456 -208 -59 37 C ATOM 1800 O VAL A 214 51.349 13.081 29.802 1.00 9.86 O ANISOU 1800 O VAL A 214 1052 984 1708 -421 -195 148 O ATOM 1801 CB VAL A 214 51.020 10.370 28.426 1.00 8.39 C ANISOU 1801 CB VAL A 214 950 574 1664 -215 65 230 C ATOM 1802 CG1 VAL A 214 51.574 9.493 29.533 1.00 9.93 C ANISOU 1802 CG1 VAL A 214 828 1188 1758 7 -20 308 C ATOM 1803 CG2 VAL A 214 50.539 9.552 27.245 1.00 10.19 C ANISOU 1803 CG2 VAL A 214 1295 872 1704 -169 -1 90 C ATOM 1804 N TYR A 215 50.119 11.925 31.299 1.00 8.04 N ANISOU 1804 N TYR A 215 689 1004 1363 -66 -164 51 N ATOM 1805 CA TYR A 215 50.708 12.470 32.489 1.00 8.44 C ANISOU 1805 CA TYR A 215 851 915 1440 -198 -264 197 C ATOM 1806 C TYR A 215 51.522 11.419 33.233 1.00 9.16 C ANISOU 1806 C TYR A 215 1068 802 1611 -270 -510 80 C ATOM 1807 O TYR A 215 51.070 10.297 33.414 1.00 10.65 O ANISOU 1807 O TYR A 215 1399 761 1888 -267 -461 313 O ATOM 1808 CB TYR A 215 49.638 13.026 33.472 1.00 9.95 C ANISOU 1808 CB TYR A 215 1312 1032 1436 -106 -168 -57 C ATOM 1809 CG TYR A 215 49.223 14.434 33.171 1.00 8.89 C ANISOU 1809 CG TYR A 215 948 976 1452 -240 -121 63 C ATOM 1810 CD1 TYR A 215 48.335 14.742 32.139 1.00 9.86 C ANISOU 1810 CD1 TYR A 215 731 1204 1812 -39 -287 -177 C ATOM 1811 CD2 TYR A 215 49.728 15.504 33.918 1.00 9.44 C ANISOU 1811 CD2 TYR A 215 1177 1061 1349 -157 -187 -129 C ATOM 1812 CE1 TYR A 215 47.977 16.042 31.885 1.00 10.35 C ANISOU 1812 CE1 TYR A 215 1125 1099 1707 -181 -222 66 C ATOM 1813 CE2 TYR A 215 49.361 16.824 33.634 1.00 10.19 C ANISOU 1813 CE2 TYR A 215 1010 1051 1809 -87 -163 -203 C ATOM 1814 CZ TYR A 215 48.474 17.081 32.605 1.00 9.66 C ANISOU 1814 CZ TYR A 215 779 1138 1752 -130 -12 -13 C ATOM 1815 OH TYR A 215 48.078 18.365 32.290 1.00 12.89 O ANISOU 1815 OH TYR A 215 1486 1138 2275 158 -395 -264 O ATOM 1816 N GLU A 216 52.715 11.811 33.686 1.00 9.53 N ANISOU 1816 N GLU A 216 927 999 1697 -167 -464 138 N ATOM 1817 CA GLU A 216 53.550 11.084 34.643 1.00 10.24 C ANISOU 1817 CA GLU A 216 1034 955 1902 -137 -612 67 C ATOM 1818 C GLU A 216 53.460 11.706 36.012 1.00 10.82 C ANISOU 1818 C GLU A 216 1145 1125 1841 -176 -663 34 C ATOM 1819 O GLU A 216 53.604 12.931 36.128 1.00 12.72 O ANISOU 1819 O GLU A 216 1520 1123 2188 -263 -402 -119 O ATOM 1820 CB GLU A 216 55.009 11.077 34.151 1.00 11.67 C ANISOU 1820 CB GLU A 216 1014 1481 1937 -125 -544 318 C ATOM 1821 CG GLU A 216 55.163 10.327 32.846 1.00 13.55 C ANISOU 1821 CG GLU A 216 1334 1742 2072 -169 -294 165 C ATOM 1822 CD GLU A 216 56.610 10.097 32.423 1.00 14.33 C ANISOU 1822 CD GLU A 216 1321 1721 2401 46 -357 74 C ATOM 1823 OE1 GLU A 216 57.517 10.424 33.184 1.00 20.27 O ANISOU 1823 OE1 GLU A 216 1398 3403 2901 16 -483 -483 O ATOM 1824 OE2 GLU A 216 56.816 9.554 31.312 1.00 15.57 O ANISOU 1824 OE2 GLU A 216 1743 1737 2435 515 -344 130 O ATOM 1825 N PHE A 217 53.224 10.876 37.011 1.00 12.11 N ANISOU 1825 N PHE A 217 1217 1462 1922 -21 -443 107 N ATOM 1826 CA PHE A 217 53.137 11.279 38.406 1.00 13.64 C ANISOU 1826 CA PHE A 217 1329 2017 1836 27 -438 161 C ATOM 1827 C PHE A 217 54.250 10.602 39.215 1.00 14.68 C ANISOU 1827 C PHE A 217 1572 1935 2072 149 -657 15 C ATOM 1828 O PHE A 217 54.506 9.376 39.025 1.00 13.79 O ANISOU 1828 O PHE A 217 1535 1822 1884 -32 -636 133 O ATOM 1829 CB PHE A 217 51.772 10.840 38.952 1.00 12.20 C ANISOU 1829 CB PHE A 217 1509 1402 1722 -70 -478 471 C ATOM 1830 CG PHE A 217 50.590 11.657 38.495 1.00 10.27 C ANISOU 1830 CG PHE A 217 1280 1134 1489 -219 -503 261 C ATOM 1831 CD1 PHE A 217 49.924 11.338 37.319 1.00 10.36 C ANISOU 1831 CD1 PHE A 217 1239 1097 1601 -461 -474 160 C ATOM 1832 CD2 PHE A 217 50.141 12.757 39.227 1.00 12.48 C ANISOU 1832 CD2 PHE A 217 1508 1657 1578 -92 -493 -122 C ATOM 1833 CE1 PHE A 217 48.854 12.095 36.880 1.00 10.17 C ANISOU 1833 CE1 PHE A 217 1253 1413 1199 -425 -418 252 C ATOM 1834 CE2 PHE A 217 49.044 13.521 38.809 1.00 11.74 C ANISOU 1834 CE2 PHE A 217 1586 1261 1616 -111 -399 -82 C ATOM 1835 CZ PHE A 217 48.406 13.145 37.643 1.00 11.70 C ANISOU 1835 CZ PHE A 217 1502 1154 1792 -336 -557 170 C ATOM 1836 N ASP A 218 54.858 11.357 40.143 1.00 15.44 N ANISOU 1836 N ASP A 218 1980 1658 2228 -10 -941 295 N ATOM 1837 CA ASP A 218 55.878 10.764 41.018 1.00 18.09 C ANISOU 1837 CA ASP A 218 2030 2095 2750 -66 -1237 405 C ATOM 1838 C ASP A 218 55.227 9.981 42.155 1.00 18.62 C ANISOU 1838 C ASP A 218 2308 1946 2823 73 -1523 707 C ATOM 1839 O ASP A 218 54.018 9.740 42.148 1.00 19.08 O ANISOU 1839 O ASP A 218 2386 2362 2502 -169 -1169 747 O ATOM 1840 CB ASP A 218 56.838 11.841 41.528 1.00 19.46 C ANISOU 1840 CB ASP A 218 1988 2529 2878 -190 -1055 72 C ATOM 1841 CG ASP A 218 56.240 12.825 42.514 1.00 20.74 C ANISOU 1841 CG ASP A 218 1739 3087 3055 38 -1548 -396 C ATOM 1842 OD1 ASP A 218 55.166 12.584 43.114 1.00 19.77 O ANISOU 1842 OD1 ASP A 218 2369 2763 2378 79 -1232 -48 O ATOM 1843 OD2 ASP A 218 56.869 13.888 42.745 1.00 25.07 O ANISOU 1843 OD2 ASP A 218 2535 3428 3562 -455 -1070 -923 O ATOM 1844 N GLU A 219 56.030 9.613 43.154 1.00 24.77 N ANISOU 1844 N GLU A 219 2964 3736 2711 437 -1754 712 N ATOM 1845 CA GLU A 219 55.589 8.685 44.164 1.00 26.14 C ANISOU 1845 CA GLU A 219 4046 3140 2747 983 -1814 824 C ATOM 1846 C GLU A 219 54.645 9.379 45.138 1.00 25.62 C ANISOU 1846 C GLU A 219 4106 3223 2405 492 -1600 891 C ATOM 1847 O GLU A 219 53.931 8.673 45.847 1.00 30.14 O ANISOU 1847 O GLU A 219 4447 4258 2747 -303 -1611 929 O ATOM 1848 CB GLU A 219 56.729 8.021 44.964 1.00 35.50 C ANISOU 1848 CB GLU A 219 4083 5572 3832 1368 -2021 1695 C ATOM 1849 CG GLU A 219 58.049 7.790 44.256 1.00 47.14 C ANISOU 1849 CG GLU A 219 3736 7827 6346 1437 -2123 -1097 C ATOM 1850 CD GLU A 219 58.014 6.653 43.270 1.00 46.86 C ANISOU 1850 CD GLU A 219 2874 7911 7019 1866 -3127 -1426 C ATOM 1851 OE1 GLU A 219 57.038 5.861 43.283 1.00 59.98 O ANISOU 1851 OE1 GLU A 219 3765 8107 10917 1204 -3492 -1592 O ATOM 1852 OE2 GLU A 219 58.964 6.506 42.457 1.00 60.08 O ANISOU 1852 OE2 GLU A 219 6073 7322 9434 2141 -384 -1919 O ATOM 1853 N ASN A 220 54.707 10.712 45.111 1.00 25.69 N ANISOU 1853 N ASN A 220 4279 3139 2343 350 -2116 111 N ATOM 1854 CA ASN A 220 53.805 11.505 45.913 1.00 27.03 C ANISOU 1854 CA ASN A 220 4297 3589 2383 -106 -1797 -270 C ATOM 1855 C ASN A 220 52.612 11.974 45.089 1.00 21.99 C ANISOU 1855 C ASN A 220 3460 3126 1767 -304 -872 234 C ATOM 1856 O ASN A 220 51.859 12.818 45.577 1.00 21.27 O ANISOU 1856 O ASN A 220 3135 3217 1731 -828 -357 -9 O ATOM 1857 CB ASN A 220 54.481 12.759 46.501 1.00 32.14 C ANISOU 1857 CB ASN A 220 4994 4370 2847 -345 -1854 -1075 C ATOM 1858 CG ASN A 220 55.441 12.422 47.615 1.00 34.14 C ANISOU 1858 CG ASN A 220 5089 4693 3192 -890 -2129 -602 C ATOM 1859 OD1 ASN A 220 55.018 11.803 48.591 1.00 37.25 O ANISOU 1859 OD1 ASN A 220 4668 5232 4255 -828 -2302 511 O ATOM 1860 ND2 ASN A 220 56.693 12.811 47.451 1.00 37.41 N ANISOU 1860 ND2 ASN A 220 4989 5787 3440 -631 -1964 475 N ATOM 1861 N PHE A 221 52.480 11.458 43.893 1.00 16.65 N ANISOU 1861 N PHE A 221 2285 2137 1905 -361 -845 326 N ATOM 1862 CA PHE A 221 51.444 11.888 42.939 1.00 16.24 C ANISOU 1862 CA PHE A 221 1952 2224 1995 -272 -693 221 C ATOM 1863 C PHE A 221 51.473 13.378 42.650 1.00 18.87 C ANISOU 1863 C PHE A 221 3019 2302 1849 -359 -1211 384 C ATOM 1864 O PHE A 221 50.450 14.007 42.375 1.00 19.37 O ANISOU 1864 O PHE A 221 3252 1788 2320 -235 -1393 -314 O ATOM 1865 CB PHE A 221 50.046 11.410 43.387 1.00 18.45 C ANISOU 1865 CB PHE A 221 2079 2981 1948 -402 -241 -273 C ATOM 1866 CG PHE A 221 49.972 9.903 43.162 1.00 21.85 C ANISOU 1866 CG PHE A 221 2393 3021 2888 -961 200 -248 C ATOM 1867 CD1 PHE A 221 50.411 9.038 44.144 1.00 25.53 C ANISOU 1867 CD1 PHE A 221 2965 2798 3939 -603 -543 -230 C ATOM 1868 CD2 PHE A 221 49.486 9.424 41.948 1.00 21.91 C ANISOU 1868 CD2 PHE A 221 2382 2936 3006 -1367 486 -471 C ATOM 1869 CE1 PHE A 221 50.391 7.680 43.970 1.00 24.80 C ANISOU 1869 CE1 PHE A 221 2831 2836 3754 -1100 399 -194 C ATOM 1870 CE2 PHE A 221 49.449 8.054 41.788 1.00 23.95 C ANISOU 1870 CE2 PHE A 221 2679 2934 3485 -1397 641 -379 C ATOM 1871 CZ PHE A 221 49.897 7.193 42.770 1.00 25.67 C ANISOU 1871 CZ PHE A 221 3067 3018 3668 -664 601 -548 C ATOM 1872 N LYS A 222 52.667 13.963 42.627 1.00 17.06 N ANISOU 1872 N LYS A 222 3125 1718 1638 -285 -728 -119 N ATOM 1873 CA LYS A 222 52.896 15.286 42.019 1.00 17.51 C ANISOU 1873 CA LYS A 222 3214 1510 1930 -185 -882 -262 C ATOM 1874 C LYS A 222 53.161 15.050 40.534 1.00 14.80 C ANISOU 1874 C LYS A 222 2450 1250 1922 -68 -665 37 C ATOM 1875 O LYS A 222 53.962 14.182 40.157 1.00 14.87 O ANISOU 1875 O LYS A 222 2175 1400 2075 -15 -803 62 O ATOM 1876 CB LYS A 222 54.024 16.045 42.692 1.00 22.58 C ANISOU 1876 CB LYS A 222 3813 2353 2414 -901 -1246 -31 C ATOM 1877 CG LYS A 222 54.387 17.420 42.139 1.00 22.94 C ANISOU 1877 CG LYS A 222 2891 2149 3678 -630 -1046 -85 C ATOM 1878 CD LYS A 222 55.599 18.083 42.781 1.00 27.05 C ANISOU 1878 CD LYS A 222 3313 2401 4565 -678 -1419 -693 C ATOM 1879 CE LYS A 222 55.910 19.375 42.030 1.00 29.09 C ANISOU 1879 CE LYS A 222 3814 2976 4261 -1579 -1906 -572 C ATOM 1880 NZ LYS A 222 56.231 19.240 40.577 1.00 56.88 N ANISOU 1880 NZ LYS A 222 8710 8303 4598 -2287 -137 111 N ATOM 1881 N PRO A 223 52.470 15.785 39.645 1.00 14.39 N ANISOU 1881 N PRO A 223 2070 1396 2000 26 -822 -293 N ATOM 1882 CA PRO A 223 52.807 15.649 38.217 1.00 13.87 C ANISOU 1882 CA PRO A 223 2016 1366 1890 -116 -881 -25 C ATOM 1883 C PRO A 223 54.280 15.936 37.945 1.00 14.69 C ANISOU 1883 C PRO A 223 2141 1500 1941 -488 -850 -119 C ATOM 1884 O PRO A 223 54.830 16.963 38.413 1.00 18.31 O ANISOU 1884 O PRO A 223 2612 1704 2640 -687 -660 -461 O ATOM 1885 CB PRO A 223 51.890 16.670 37.552 1.00 17.79 C ANISOU 1885 CB PRO A 223 2619 1551 2591 171 -788 410 C ATOM 1886 CG PRO A 223 50.786 16.889 38.528 1.00 18.84 C ANISOU 1886 CG PRO A 223 1949 2018 3189 149 -914 184 C ATOM 1887 CD PRO A 223 51.317 16.668 39.897 1.00 17.54 C ANISOU 1887 CD PRO A 223 2344 1598 2724 235 -528 -198 C ATOM 1888 N LEU A 224 54.912 15.055 37.182 1.00 13.80 N ANISOU 1888 N LEU A 224 1899 1468 1875 -618 -768 -7 N ATOM 1889 CA LEU A 224 56.313 15.189 36.742 1.00 15.29 C ANISOU 1889 CA LEU A 224 1898 1896 2016 -576 -815 -30 C ATOM 1890 C LEU A 224 56.441 15.739 35.325 1.00 14.28 C ANISOU 1890 C LEU A 224 1513 1639 2275 -471 -749 217 C ATOM 1891 O LEU A 224 57.330 16.557 35.021 1.00 16.34 O ANISOU 1891 O LEU A 224 1568 2298 2340 -739 -598 14 O ATOM 1892 CB LEU A 224 56.994 13.828 36.789 1.00 19.14 C ANISOU 1892 CB LEU A 224 1847 2354 3071 -213 -847 804 C ATOM 1893 CG LEU A 224 57.456 13.105 38.025 1.00 24.21 C ANISOU 1893 CG LEU A 224 2547 3296 3354 -171 -1073 1195 C ATOM 1894 CD1 LEU A 224 57.783 11.652 37.678 1.00 27.06 C ANISOU 1894 CD1 LEU A 224 2897 3347 4038 575 -563 1745 C ATOM 1895 CD2 LEU A 224 58.652 13.807 38.629 1.00 27.28 C ANISOU 1895 CD2 LEU A 224 2389 5495 2480 -684 -765 960 C ATOM 1896 N LYS A 225 55.584 15.305 34.416 1.00 12.86 N ANISOU 1896 N LYS A 225 1517 1342 2026 -315 -696 274 N ATOM 1897 CA LYS A 225 55.672 15.647 33.003 1.00 13.60 C ANISOU 1897 CA LYS A 225 958 2177 2032 -447 -359 275 C ATOM 1898 C LYS A 225 54.346 15.321 32.322 1.00 9.34 C ANISOU 1898 C LYS A 225 775 1261 1513 -240 -26 114 C ATOM 1899 O LYS A 225 53.599 14.481 32.850 1.00 10.43 O ANISOU 1899 O LYS A 225 1249 1109 1604 -447 -195 116 O ATOM 1900 CB LYS A 225 56.746 14.823 32.314 1.00 20.44 C ANISOU 1900 CB LYS A 225 787 4440 2539 173 -855 -661 C ATOM 1901 CG LYS A 225 56.965 15.045 30.850 1.00 29.07 C ANISOU 1901 CG LYS A 225 3273 4497 3276 -1240 1356 -522 C ATOM 1902 CD LYS A 225 57.943 13.984 30.344 1.00 33.83 C ANISOU 1902 CD LYS A 225 5251 3874 3730 -1016 1403 -1284 C ATOM 1903 CE LYS A 225 58.968 13.612 31.412 1.00 33.44 C ANISOU 1903 CE LYS A 225 5465 3362 3880 99 1880 -584 C ATOM 1904 NZ LYS A 225 60.068 12.760 30.813 1.00 42.99 N ANISOU 1904 NZ LYS A 225 3047 7179 6107 -1178 2502 -2660 N ATOM 1905 N ARG A 226 54.094 15.966 31.195 1.00 10.38 N ANISOU 1905 N ARG A 226 1132 1338 1475 -486 -157 113 N ATOM 1906 CA ARG A 226 52.935 15.637 30.377 1.00 9.50 C ANISOU 1906 CA ARG A 226 1076 957 1576 -339 -219 64 C ATOM 1907 C ARG A 226 53.322 15.784 28.911 1.00 9.16 C ANISOU 1907 C ARG A 226 849 1056 1575 -385 -215 159 C ATOM 1908 O ARG A 226 54.108 16.684 28.579 1.00 10.41 O ANISOU 1908 O ARG A 226 1124 1079 1752 -480 -175 101 O ATOM 1909 CB ARG A 226 51.655 16.377 30.754 1.00 10.57 C ANISOU 1909 CB ARG A 226 1237 1099 1681 -246 -130 -209 C ATOM 1910 CG ARG A 226 51.498 17.802 30.329 1.00 12.12 C ANISOU 1910 CG ARG A 226 1431 1190 1982 -17 -283 -63 C ATOM 1911 CD ARG A 226 52.375 18.804 31.037 1.00 12.78 C ANISOU 1911 CD ARG A 226 1627 1109 2119 -58 -172 -227 C ATOM 1912 NE ARG A 226 51.994 18.993 32.431 1.00 14.39 N ANISOU 1912 NE ARG A 226 1973 1489 2006 -291 -185 -91 N ATOM 1913 CZ ARG A 226 52.743 19.024 33.519 1.00 13.17 C ANISOU 1913 CZ ARG A 226 1659 1225 2119 -499 -148 -185 C ATOM 1914 NH1 ARG A 226 54.059 18.843 33.470 1.00 16.34 N ANISOU 1914 NH1 ARG A 226 1714 2192 2304 -323 -12 -14 N ATOM 1915 NH2 ARG A 226 52.135 19.224 34.699 1.00 14.05 N ANISOU 1915 NH2 ARG A 226 1584 1767 1987 -272 -283 -100 N ATOM 1916 N TYR A 227 52.785 14.956 28.036 1.00 8.72 N ANISOU 1916 N TYR A 227 697 1102 1515 -332 -122 148 N ATOM 1917 CA TYR A 227 53.159 14.945 26.630 1.00 9.21 C ANISOU 1917 CA TYR A 227 805 1202 1492 -171 -103 225 C ATOM 1918 C TYR A 227 52.073 14.276 25.779 1.00 8.32 C ANISOU 1918 C TYR A 227 900 780 1482 -162 -124 361 C ATOM 1919 O TYR A 227 51.336 13.400 26.217 1.00 9.17 O ANISOU 1919 O TYR A 227 986 975 1524 -268 149 251 O ATOM 1920 CB TYR A 227 54.487 14.262 26.434 1.00 9.23 C ANISOU 1920 CB TYR A 227 857 1017 1632 -234 -149 19 C ATOM 1921 CG TYR A 227 54.655 12.940 27.121 1.00 9.80 C ANISOU 1921 CG TYR A 227 850 1052 1821 -170 62 155 C ATOM 1922 CD1 TYR A 227 54.292 11.728 26.564 1.00 10.60 C ANISOU 1922 CD1 TYR A 227 709 1015 2304 -138 -246 170 C ATOM 1923 CD2 TYR A 227 55.221 12.892 28.399 1.00 11.93 C ANISOU 1923 CD2 TYR A 227 1501 1037 1994 -299 -248 338 C ATOM 1924 CE1 TYR A 227 54.489 10.541 27.257 1.00 11.87 C ANISOU 1924 CE1 TYR A 227 993 1122 2395 -233 -202 355 C ATOM 1925 CE2 TYR A 227 55.412 11.700 29.085 1.00 12.24 C ANISOU 1925 CE2 TYR A 227 1278 1138 2236 -271 -254 451 C ATOM 1926 CZ TYR A 227 55.049 10.513 28.531 1.00 10.54 C ANISOU 1926 CZ TYR A 227 636 1019 2350 -52 -42 322 C ATOM 1927 OH TYR A 227 55.192 9.268 29.122 1.00 12.67 O ANISOU 1927 OH TYR A 227 1329 1047 2439 144 -12 281 O ATOM 1928 N TYR A 228 52.002 14.730 24.541 1.00 8.64 N ANISOU 1928 N TYR A 228 1080 843 1360 -311 3 215 N ATOM 1929 CA TYR A 228 51.074 14.135 23.580 1.00 8.62 C ANISOU 1929 CA TYR A 228 934 808 1532 -194 -65 86 C ATOM 1930 C TYR A 228 51.726 12.963 22.860 1.00 8.64 C ANISOU 1930 C TYR A 228 756 919 1608 -196 121 126 C ATOM 1931 O TYR A 228 52.934 12.938 22.676 1.00 12.23 O ANISOU 1931 O TYR A 228 711 1492 2443 -301 178 -341 O ATOM 1932 CB TYR A 228 50.620 15.149 22.538 1.00 8.90 C ANISOU 1932 CB TYR A 228 1085 908 1388 -57 53 73 C ATOM 1933 CG TYR A 228 49.723 16.279 22.950 1.00 9.04 C ANISOU 1933 CG TYR A 228 1095 786 1554 -103 196 69 C ATOM 1934 CD1 TYR A 228 48.483 16.051 23.523 1.00 9.19 C ANISOU 1934 CD1 TYR A 228 917 1109 1468 -46 -35 110 C ATOM 1935 CD2 TYR A 228 50.056 17.601 22.709 1.00 12.00 C ANISOU 1935 CD2 TYR A 228 1419 788 2352 -184 -12 127 C ATOM 1936 CE1 TYR A 228 47.632 17.071 23.875 1.00 10.50 C ANISOU 1936 CE1 TYR A 228 1263 1478 1247 181 95 -33 C ATOM 1937 CE2 TYR A 228 49.209 18.648 23.065 1.00 13.70 C ANISOU 1937 CE2 TYR A 228 1284 890 3033 -48 -415 -71 C ATOM 1938 CZ TYR A 228 47.993 18.381 23.647 1.00 12.29 C ANISOU 1938 CZ TYR A 228 1499 1255 1915 93 -304 -393 C ATOM 1939 OH TYR A 228 47.081 19.348 24.040 1.00 16.29 O ANISOU 1939 OH TYR A 228 1612 1607 2970 357 -536 -743 O ATOM 1940 N LEU A 229 50.917 11.965 22.487 1.00 8.82 N ANISOU 1940 N LEU A 229 879 910 1563 -279 273 33 N ATOM 1941 CA LEU A 229 51.315 10.887 21.627 1.00 9.07 C ANISOU 1941 CA LEU A 229 1083 677 1688 39 58 158 C ATOM 1942 C LEU A 229 50.844 11.118 20.192 1.00 8.27 C ANISOU 1942 C LEU A 229 974 603 1567 -128 190 133 C ATOM 1943 O LEU A 229 49.682 11.485 19.956 1.00 9.12 O ANISOU 1943 O LEU A 229 1025 1040 1400 -67 179 136 O ATOM 1944 CB LEU A 229 50.781 9.530 22.090 1.00 9.17 C ANISOU 1944 CB LEU A 229 999 914 1571 -143 145 229 C ATOM 1945 CG LEU A 229 51.131 9.124 23.513 1.00 10.41 C ANISOU 1945 CG LEU A 229 1247 1004 1703 26 72 376 C ATOM 1946 CD1 LEU A 229 50.491 7.770 23.848 1.00 10.41 C ANISOU 1946 CD1 LEU A 229 1379 973 1602 49 2 367 C ATOM 1947 CD2 LEU A 229 52.631 9.093 23.726 1.00 12.25 C ANISOU 1947 CD2 LEU A 229 1331 1638 1686 -99 -131 468 C ATOM 1948 N GLY A 230 51.717 10.918 19.232 1.00 9.19 N ANISOU 1948 N GLY A 230 1003 743 1745 -160 292 278 N ATOM 1949 CA GLY A 230 51.415 10.990 17.814 1.00 11.11 C ANISOU 1949 CA GLY A 230 1711 881 1630 -420 396 104 C ATOM 1950 C GLY A 230 52.347 11.917 17.052 1.00 9.44 C ANISOU 1950 C GLY A 230 1140 823 1624 -96 321 218 C ATOM 1951 O GLY A 230 53.453 12.196 17.470 1.00 11.44 O ANISOU 1951 O GLY A 230 1194 1372 1779 -106 195 277 O ATOM 1952 N ASN A 231 51.882 12.361 15.895 1.00 9.98 N ANISOU 1952 N ASN A 231 1317 774 1702 -64 209 215 N ATOM 1953 CA ASN A 231 52.663 13.161 14.965 1.00 9.99 C ANISOU 1953 CA ASN A 231 1114 1052 1629 -161 264 274 C ATOM 1954 C ASN A 231 52.694 14.623 15.426 1.00 10.12 C ANISOU 1954 C ASN A 231 1193 997 1656 -164 252 265 C ATOM 1955 O ASN A 231 51.641 15.317 15.457 1.00 9.99 O ANISOU 1955 O ASN A 231 1163 1173 1460 -72 93 216 O ATOM 1956 CB ASN A 231 52.105 13.012 13.559 1.00 12.59 C ANISOU 1956 CB ASN A 231 1823 1263 1698 -314 130 148 C ATOM 1957 CG ASN A 231 52.919 13.817 12.541 1.00 12.90 C ANISOU 1957 CG ASN A 231 2054 1473 1376 -438 260 -55 C ATOM 1958 OD1 ASN A 231 52.845 15.047 12.457 1.00 14.00 O ANISOU 1958 OD1 ASN A 231 1702 1508 2110 -319 320 319 O ATOM 1959 ND2 ASN A 231 53.704 13.072 11.776 1.00 17.46 N ANISOU 1959 ND2 ASN A 231 2693 1882 2059 -51 669 -121 N ATOM 1960 N ALA A 232 53.878 15.113 15.804 1.00 10.51 N ANISOU 1960 N ALA A 232 1085 1126 1783 -174 387 239 N ATOM 1961 CA ALA A 232 53.992 16.409 16.445 1.00 10.07 C ANISOU 1961 CA ALA A 232 1128 1160 1539 -190 -21 352 C ATOM 1962 C ALA A 232 53.483 17.549 15.545 1.00 10.22 C ANISOU 1962 C ALA A 232 1071 1181 1631 -140 126 350 C ATOM 1963 O ALA A 232 52.764 18.473 16.023 1.00 10.59 O ANISOU 1963 O ALA A 232 1072 1229 1722 -99 164 283 O ATOM 1964 CB ALA A 232 55.413 16.668 16.900 1.00 13.05 C ANISOU 1964 CB ALA A 232 1152 1517 2289 -275 -149 455 C ATOM 1965 N ASP A 233 53.846 17.521 14.257 1.00 10.68 N ANISOU 1965 N ASP A 233 1181 1306 1569 -171 218 431 N ATOM 1966 CA ASP A 233 53.416 18.609 13.367 1.00 11.26 C ANISOU 1966 CA ASP A 233 1484 1159 1634 -248 95 327 C ATOM 1967 C ASP A 233 51.900 18.647 13.256 1.00 10.30 C ANISOU 1967 C ASP A 233 1518 949 1447 -148 4 327 C ATOM 1968 O ASP A 233 51.293 19.709 13.317 1.00 13.25 O ANISOU 1968 O ASP A 233 1729 977 2330 -109 39 467 O ATOM 1969 CB ASP A 233 54.015 18.410 11.997 1.00 13.94 C ANISOU 1969 CB ASP A 233 1605 2162 1529 -525 137 660 C ATOM 1970 CG ASP A 233 55.449 18.858 11.837 1.00 17.02 C ANISOU 1970 CG ASP A 233 1234 2800 2434 116 279 1045 C ATOM 1971 OD1 ASP A 233 56.170 18.984 12.822 1.00 29.13 O ANISOU 1971 OD1 ASP A 233 1412 6927 2728 -1216 274 304 O ATOM 1972 OD2 ASP A 233 55.829 19.073 10.667 1.00 19.66 O ANISOU 1972 OD2 ASP A 233 2435 2475 2561 -673 1069 271 O ATOM 1973 N GLU A 234 51.253 17.501 13.121 1.00 10.71 N ANISOU 1973 N GLU A 234 1371 1044 1655 -190 324 141 N ATOM 1974 CA GLU A 234 49.813 17.406 13.004 1.00 10.34 C ANISOU 1974 CA GLU A 234 1410 972 1546 -51 17 221 C ATOM 1975 C GLU A 234 49.107 17.861 14.284 1.00 10.16 C ANISOU 1975 C GLU A 234 1168 1096 1597 -155 55 168 C ATOM 1976 O GLU A 234 48.159 18.633 14.232 1.00 10.63 O ANISOU 1976 O GLU A 234 1356 998 1687 0 -46 200 O ATOM 1977 CB GLU A 234 49.368 15.997 12.582 1.00 13.16 C ANISOU 1977 CB GLU A 234 1860 1128 2011 -383 119 -24 C ATOM 1978 CG GLU A 234 49.709 15.702 11.150 1.00 19.82 C ANISOU 1978 CG GLU A 234 3273 2237 2019 314 -201 -490 C ATOM 1979 CD GLU A 234 49.501 14.228 10.770 1.00 26.50 C ANISOU 1979 CD GLU A 234 5098 2446 2525 348 -1174 -919 C ATOM 1980 OE1 GLU A 234 48.921 13.463 11.587 1.00 30.44 O ANISOU 1980 OE1 GLU A 234 6485 1837 3245 -24 -1460 -434 O ATOM 1981 OE2 GLU A 234 49.920 13.893 9.645 1.00 37.85 O ANISOU 1981 OE2 GLU A 234 7613 3585 3182 -85 -464 -1897 O ATOM 1982 N ILE A 235 49.594 17.408 15.423 1.00 9.56 N ANISOU 1982 N ILE A 235 1076 1007 1549 -165 5 137 N ATOM 1983 CA ILE A 235 48.981 17.738 16.718 1.00 8.93 C ANISOU 1983 CA ILE A 235 909 873 1611 -163 100 261 C ATOM 1984 C ILE A 235 49.097 19.229 17.018 1.00 8.06 C ANISOU 1984 C ILE A 235 914 875 1275 -157 18 356 C ATOM 1985 O ILE A 235 48.116 19.893 17.367 1.00 9.74 O ANISOU 1985 O ILE A 235 1047 1039 1616 -42 -18 113 O ATOM 1986 CB ILE A 235 49.619 16.884 17.819 1.00 8.42 C ANISOU 1986 CB ILE A 235 794 767 1637 -216 89 215 C ATOM 1987 CG1 ILE A 235 49.381 15.386 17.621 1.00 8.79 C ANISOU 1987 CG1 ILE A 235 1037 809 1492 -251 335 175 C ATOM 1988 CG2 ILE A 235 49.107 17.390 19.159 1.00 9.34 C ANISOU 1988 CG2 ILE A 235 1261 707 1581 -204 41 176 C ATOM 1989 CD1 ILE A 235 50.281 14.470 18.411 1.00 10.62 C ANISOU 1989 CD1 ILE A 235 1761 761 1512 111 304 122 C ATOM 1990 N ALA A 236 50.323 19.770 16.837 1.00 8.96 N ANISOU 1990 N ALA A 236 1075 715 1616 -188 73 309 N ATOM 1991 CA ALA A 236 50.490 21.217 17.162 1.00 9.32 C ANISOU 1991 CA ALA A 236 1143 723 1676 -224 -78 286 C ATOM 1992 C ALA A 236 49.640 22.064 16.263 1.00 9.30 C ANISOU 1992 C ALA A 236 1234 790 1508 -66 111 255 C ATOM 1993 O ALA A 236 49.054 23.058 16.695 1.00 10.59 O ANISOU 1993 O ALA A 236 1530 880 1615 103 4 254 O ATOM 1994 CB ALA A 236 51.972 21.531 17.106 1.00 11.24 C ANISOU 1994 CB ALA A 236 1219 895 2156 -349 -121 331 C ATOM 1995 N ALA A 237 49.506 21.700 14.947 1.00 10.02 N ANISOU 1995 N ALA A 237 1332 939 1537 -162 -9 203 N ATOM 1996 CA ALA A 237 48.619 22.481 14.079 1.00 11.02 C ANISOU 1996 CA ALA A 237 1465 1188 1532 -165 -20 311 C ATOM 1997 C ALA A 237 47.175 22.433 14.552 1.00 10.19 C ANISOU 1997 C ALA A 237 1442 1161 1270 17 -115 325 C ATOM 1998 O ALA A 237 46.437 23.417 14.499 1.00 12.22 O ANISOU 1998 O ALA A 237 1523 1024 2096 -35 -93 416 O ATOM 1999 CB ALA A 237 48.792 22.036 12.639 1.00 11.53 C ANISOU 1999 CB ALA A 237 1517 1308 1555 153 81 231 C ATOM 2000 N LYS A 238 46.749 21.238 14.984 1.00 10.61 N ANISOU 2000 N LYS A 238 1358 999 1675 -78 -29 154 N ATOM 2001 CA LYS A 238 45.395 21.000 15.454 1.00 12.23 C ANISOU 2001 CA LYS A 238 1225 1351 2071 -360 -253 -74 C ATOM 2002 C LYS A 238 45.072 21.652 16.798 1.00 11.60 C ANISOU 2002 C LYS A 238 1173 1418 1816 -229 -62 213 C ATOM 2003 O LYS A 238 43.877 21.852 17.111 1.00 13.87 O ANISOU 2003 O LYS A 238 1158 1799 2312 -395 -81 -34 O ATOM 2004 CB LYS A 238 45.207 19.478 15.612 1.00 14.11 C ANISOU 2004 CB LYS A 238 1612 1421 2326 -520 -193 101 C ATOM 2005 CG LYS A 238 43.812 18.964 15.308 1.00 14.85 C ANISOU 2005 CG LYS A 238 1688 1699 2255 -675 -372 96 C ATOM 2006 CD LYS A 238 43.735 17.439 15.427 1.00 17.64 C ANISOU 2006 CD LYS A 238 2361 1767 2573 -888 -14 -113 C ATOM 2007 CE LYS A 238 42.312 16.934 15.268 1.00 17.39 C ANISOU 2007 CE LYS A 238 2281 1719 2606 -924 535 -59 C ATOM 2008 NZ LYS A 238 42.167 15.530 15.623 1.00 18.03 N ANISOU 2008 NZ LYS A 238 2979 1745 2127 -1023 262 -103 N ATOM 2009 N ALA A 239 46.068 21.980 17.576 1.00 10.68 N ANISOU 2009 N ALA A 239 1126 1159 1773 -115 -46 214 N ATOM 2010 CA ALA A 239 45.886 22.611 18.884 1.00 10.37 C ANISOU 2010 CA ALA A 239 1207 1167 1567 -102 40 384 C ATOM 2011 C ALA A 239 45.769 24.138 18.817 1.00 9.75 C ANISOU 2011 C ALA A 239 920 1204 1583 15 410 412 C ATOM 2012 O ALA A 239 45.532 24.761 19.893 1.00 12.03 O ANISOU 2012 O ALA A 239 1395 1434 1742 -170 337 88 O ATOM 2013 CB ALA A 239 47.018 22.215 19.828 1.00 13.40 C ANISOU 2013 CB ALA A 239 1786 1396 1910 70 -380 420 C ATOM 2014 N ALA A 240 45.877 24.736 17.656 1.00 10.39 N ANISOU 2014 N ALA A 240 1150 1157 1641 -173 154 438 N ATOM 2015 CA ALA A 240 45.647 26.185 17.463 1.00 9.72 C ANISOU 2015 CA ALA A 240 1120 922 1650 -350 0 224 C ATOM 2016 C ALA A 240 44.159 26.511 17.564 1.00 11.08 C ANISOU 2016 C ALA A 240 1169 957 2082 -280 -117 294 C ATOM 2017 O ALA A 240 43.297 25.714 17.131 1.00 10.91 O ANISOU 2017 O ALA A 240 971 1070 2106 -211 123 217 O ATOM 2018 CB ALA A 240 46.111 26.643 16.096 1.00 10.78 C ANISOU 2018 CB ALA A 240 1653 980 1465 -255 -61 226 C ATOM 2019 N ALA A 241 43.802 27.681 18.088 1.00 9.99 N ANISOU 2019 N ALA A 241 971 1092 1733 -280 -24 343 N ATOM 2020 CA ALA A 241 42.409 28.129 18.142 1.00 10.70 C ANISOU 2020 CA ALA A 241 1034 1392 1640 -214 -44 294 C ATOM 2021 C ALA A 241 41.835 28.412 16.757 1.00 10.58 C ANISOU 2021 C ALA A 241 1001 1409 1610 -201 6 396 C ATOM 2022 O ALA A 241 42.520 29.013 15.899 1.00 11.79 O ANISOU 2022 O ALA A 241 1339 1530 1610 -342 88 312 O ATOM 2023 CB ALA A 241 42.310 29.400 18.976 1.00 12.21 C ANISOU 2023 CB ALA A 241 1054 1657 1929 -163 102 0 C ATOM 2024 N VAL A 242 40.595 27.991 16.537 1.00 10.17 N ANISOU 2024 N VAL A 242 1011 1315 1538 -9 -31 242 N ATOM 2025 CA VAL A 242 39.886 28.184 15.293 1.00 9.83 C ANISOU 2025 CA VAL A 242 1000 1173 1562 -60 -74 411 C ATOM 2026 C VAL A 242 38.893 29.327 15.396 1.00 9.60 C ANISOU 2026 C VAL A 242 868 1114 1664 -164 74 394 C ATOM 2027 O VAL A 242 38.210 29.452 16.403 1.00 11.27 O ANISOU 2027 O VAL A 242 1320 1401 1561 56 116 501 O ATOM 2028 CB VAL A 242 39.145 26.899 14.881 1.00 10.73 C ANISOU 2028 CB VAL A 242 1204 1250 1621 -78 25 212 C ATOM 2029 CG1 VAL A 242 38.327 27.101 13.618 1.00 12.25 C ANISOU 2029 CG1 VAL A 242 1085 1787 1784 -234 -106 142 C ATOM 2030 CG2 VAL A 242 40.161 25.754 14.712 1.00 13.31 C ANISOU 2030 CG2 VAL A 242 1493 1274 2292 64 -99 91 C ATOM 2031 N ALA A 243 38.817 30.173 14.377 1.00 10.09 N ANISOU 2031 N ALA A 243 1186 1177 1472 24 199 336 N ATOM 2032 CA ALA A 243 37.922 31.330 14.399 1.00 11.63 C ANISOU 2032 CA ALA A 243 1229 1242 1947 75 294 544 C ATOM 2033 C ALA A 243 36.467 30.899 14.542 1.00 10.70 C ANISOU 2033 C ALA A 243 1207 1183 1677 89 67 145 C ATOM 2034 O ALA A 243 36.090 29.786 14.171 1.00 11.29 O ANISOU 2034 O ALA A 243 1213 1249 1827 154 -149 81 O ATOM 2035 CB ALA A 243 38.161 32.109 13.108 1.00 14.37 C ANISOU 2035 CB ALA A 243 1960 1375 2124 186 368 711 C ATOM 2036 N ASN A 244 35.582 31.802 14.964 1.00 11.71 N ANISOU 2036 N ASN A 244 1302 1059 2086 79 481 430 N ATOM 2037 CA ASN A 244 34.157 31.526 15.033 1.00 12.07 C ANISOU 2037 CA ASN A 244 1277 1360 1949 189 332 401 C ATOM 2038 C ASN A 244 33.591 31.158 13.676 1.00 12.67 C ANISOU 2038 C ASN A 244 1612 1336 1866 23 266 586 C ATOM 2039 O ASN A 244 32.592 30.422 13.624 1.00 14.10 O ANISOU 2039 O ASN A 244 1386 1826 2144 -4 38 723 O ATOM 2040 CB ASN A 244 33.322 32.717 15.557 1.00 12.65 C ANISOU 2040 CB ASN A 244 1349 1446 2013 527 -36 414 C ATOM 2041 CG ASN A 244 33.665 33.145 16.951 1.00 13.79 C ANISOU 2041 CG ASN A 244 1572 1491 2178 338 -38 156 C ATOM 2042 OD1 ASN A 244 33.982 32.285 17.796 1.00 14.97 O ANISOU 2042 OD1 ASN A 244 1764 2171 1751 679 94 305 O ATOM 2043 ND2 ASN A 244 33.618 34.456 17.249 1.00 16.52 N ANISOU 2043 ND2 ASN A 244 1667 1533 3076 -77 416 -153 N ATOM 2044 N GLN A 245 34.220 31.632 12.608 1.00 14.19 N ANISOU 2044 N GLN A 245 1315 2126 1951 323 126 1062 N ATOM 2045 CA GLN A 245 33.716 31.383 11.242 1.00 18.76 C ANISOU 2045 CA GLN A 245 2084 3118 1928 260 0 1126 C ATOM 2046 C GLN A 245 34.083 29.975 10.766 1.00 17.71 C ANISOU 2046 C GLN A 245 1356 3158 2216 -412 -434 487 C ATOM 2047 O GLN A 245 33.603 29.593 9.691 1.00 22.00 O ANISOU 2047 O GLN A 245 1662 4415 2283 -529 -608 318 O ATOM 2048 CB GLN A 245 34.259 32.413 10.259 1.00 22.11 C ANISOU 2048 CB GLN A 245 2757 3388 2257 1087 844 1587 C ATOM 2049 CG GLN A 245 33.675 33.827 10.399 1.00 22.13 C ANISOU 2049 CG GLN A 245 2280 3188 2939 677 814 1432 C ATOM 2050 CD GLN A 245 34.123 34.478 11.709 1.00 21.23 C ANISOU 2050 CD GLN A 245 1822 3306 2939 953 767 1401 C ATOM 2051 OE1 GLN A 245 35.277 34.348 12.117 1.00 20.55 O ANISOU 2051 OE1 GLN A 245 1644 2647 3516 601 785 1668 O ATOM 2052 NE2 GLN A 245 33.241 35.172 12.449 1.00 20.60 N ANISOU 2052 NE2 GLN A 245 1834 2553 3441 774 811 1300 N ATOM 2053 N GLY A 246 34.899 29.220 11.522 1.00 16.95 N ANISOU 2053 N GLY A 246 1538 2844 2060 210 -325 -232 N ATOM 2054 CA GLY A 246 35.414 27.907 11.173 1.00 17.17 C ANISOU 2054 CA GLY A 246 1575 2725 2222 -252 -146 -797 C ATOM 2055 C GLY A 246 36.799 27.933 10.539 1.00 15.29 C ANISOU 2055 C GLY A 246 1357 1778 2674 -279 -281 -446 C ATOM 2056 O GLY A 246 37.385 28.970 10.231 1.00 15.67 O ANISOU 2056 O GLY A 246 1674 1650 2628 -191 -461 -227 O ATOM 2057 N LYS A 247 37.399 26.755 10.283 1.00 15.16 N ANISOU 2057 N LYS A 247 2005 1681 2076 -402 168 -537 N ATOM 2058 CA LYS A 247 38.634 26.484 9.627 1.00 16.94 C ANISOU 2058 CA LYS A 247 1675 1425 3336 -298 104 -477 C ATOM 2059 C LYS A 247 38.457 26.159 8.114 1.00 27.24 C ANISOU 2059 C LYS A 247 3456 4383 2511 -142 1696 318 C ATOM 2060 O LYS A 247 37.603 26.745 7.468 1.00 35.62 O ANISOU 2060 O LYS A 247 3652 6453 3428 -2113 -208 1713 O ATOM 2061 CB LYS A 247 39.169 25.131 10.143 1.00 19.83 C ANISOU 2061 CB LYS A 247 3264 995 3278 -91 480 -751 C ATOM 2062 CG LYS A 247 40.607 24.840 9.825 1.00 29.35 C ANISOU 2062 CG LYS A 247 3362 3074 4715 1397 -380 -856 C ATOM 2063 CD LYS A 247 41.243 23.930 10.862 1.00 32.99 C ANISOU 2063 CD LYS A 247 3539 4080 4917 61 -618 438 C ATOM 2064 CE LYS A 247 40.321 22.798 11.254 1.00 39.17 C ANISOU 2064 CE LYS A 247 5580 4309 4994 -1294 -808 -356 C ATOM 2065 NZ LYS A 247 39.945 22.032 10.027 1.00 50.61 N ANISOU 2065 NZ LYS A 247 8331 5868 5029 -1966 -414 -1091 N TER 2066 LYS A 247 END