Browse entries in the PDBbind-CN Database
HEADER RNA BINDING PROTEIN/RNA 24-JAN-11 3QGC TITLE CRYSTAL STRUCTURE OF FBF-2 R288Y MUTANT IN COMPLEX WITH GLD-1 FBEA A7U TITLE 2 MUTANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: FEM-3 MRNA-BINDING FACTOR 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PUM-HD DOMAIN, RSIDUES 164-575; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 5'-R(*UP*GP*UP*GP*CP*CP*UP*UP*A)-3'; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 3 ORGANISM_COMMON: NEMATODE; SOURCE 4 ORGANISM_TAXID: 6239; SOURCE 5 GENE: FBF-2, F21H12.5; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: SYNTHETIC RNA KEYWDS FBF, FEM-3 BINDING FACTOR, PUF, RNA-BINDING SPECIFICITY, BASE KEYWDS 2 STACKING, RNA BINDING PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR Y.WANG,C.QIU,Y.Y.KOH,L.OPPERMAN,L.GROSS,T.M.T.HALL,M.WICKENS REVDAT 2 30-MAR-11 3QGC 1 JRNL REVDAT 1 23-MAR-11 3QGC 0 JRNL AUTH Y.Y.KOH,Y.WANG,C.QIU,L.OPPERMAN,L.GROSS,T.M.TANAKA HALL, JRNL AUTH 2 M.WICKENS JRNL TITL STACKING INTERACTIONS IN PUF-RNA COMPLEXES. JRNL REF RNA V. 17 718 2011 JRNL REFN ISSN 1355-8382 JRNL PMID 21372189 JRNL DOI 10.1261/RNA.2540311 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX.REFINE REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.60 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 42132 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.210 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2114 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.01 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.45 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.76500 REMARK 3 B22 (A**2) : -0.00000 REMARK 3 B33 (A**2) : -0.00000 REMARK 3 B12 (A**2) : 1.76500 REMARK 3 B13 (A**2) : -3.52900 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : 9.480 NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3QGC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-11. REMARK 100 THE RCSB ID CODE IS RCSB063609. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42132 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 43.600 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 11.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.15500 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5 REMARK 200 DATA REDUNDANCY IN SHELL : 11.40 REMARK 200 R MERGE FOR SHELL (I) : 0.55000 REMARK 200 R SYM FOR SHELL (I) : 0.55000 REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3K5Y REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5, 10% POLYETHYLENE REMARK 280 GLYCOL 8000, AND 8% ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.79633 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.59267 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.69450 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 84.49083 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.89817 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 163 REMARK 465 SER A 164 REMARK 465 ASN A 165 REMARK 465 ASN A 166 REMARK 465 VAL A 167 REMARK 465 THR A 568 REMARK 465 HIS A 569 REMARK 465 PRO A 570 REMARK 465 ILE A 571 REMARK 465 TYR A 572 REMARK 465 GLU A 573 REMARK 465 LEU A 574 REMARK 465 GLN A 575 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 G B 2 P G B 2 O5' -0.134 REMARK 500 G B 2 C5 G B 2 N7 0.041 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 258 46.61 -85.60 REMARK 500 ASP A 312 -151.62 -109.60 REMARK 500 ARG A 441 -3.67 72.36 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3K5Y RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FBF-2/GLD-1 FBEA COMPLEX REMARK 900 RELATED ID: 3QG9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FBF-2 IN COMPLEX WITH GLD-1 FBEA A7U REMARK 900 MUTANT REMARK 900 RELATED ID: 3QGB RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FBF-2 R288Y MUTANT IN COMPLEX WITH GLD REMARK 900 -1 FBEA DBREF 3QGC A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 3QGC B 1 9 PDB 3QGC 3QGC 1 9 SEQADV 3QGC GLY A 163 UNP Q09312 EXPRESSION TAG SEQADV 3QGC TYR A 288 UNP Q09312 ARG 288 ENGINEERED MUTATION SEQRES 1 A 413 GLY SER ASN ASN VAL LEU PRO THR TRP SER LEU ASP SER SEQRES 2 A 413 ASN GLY GLU MET ARG SER ARG LEU SER LEU SER GLU VAL SEQRES 3 A 413 LEU ASP SER GLY ASP LEU MET LYS PHE ALA VAL ASP LYS SEQRES 4 A 413 THR GLY CYS GLN PHE LEU GLU LYS ALA VAL LYS GLY SER SEQRES 5 A 413 LEU THR SER TYR GLN LYS PHE GLN LEU PHE GLU GLN VAL SEQRES 6 A 413 ILE GLY ARG LYS ASP ASP PHE LEU LYS LEU SER THR ASN SEQRES 7 A 413 ILE PHE GLY ASN TYR LEU VAL GLN SER VAL ILE GLY ILE SEQRES 8 A 413 SER LEU ALA THR ASN ASP ASP GLY TYR THR LYS ARG GLN SEQRES 9 A 413 GLU LYS LEU LYS ASN PHE ILE SER SER GLN MET THR ASP SEQRES 10 A 413 MET CYS LEU ASP LYS PHE ALA CYS TYR VAL ILE GLN SER SEQRES 11 A 413 SER LEU GLN ASN MET ASP LEU SER LEU ALA CYS LYS LEU SEQRES 12 A 413 VAL GLN ALA LEU PRO ARG ASP ALA ARG LEU ILE ALA ILE SEQRES 13 A 413 CYS VAL ASP GLN ASN ALA ASN HIS VAL ILE GLN LYS VAL SEQRES 14 A 413 VAL ALA VAL ILE PRO LEU LYS ASN TRP GLU PHE ILE VAL SEQRES 15 A 413 ASP PHE VAL ALA THR PRO GLU HIS LEU ARG GLN ILE CYS SEQRES 16 A 413 SER ASP LYS TYR GLY CYS ARG VAL VAL GLN THR ILE ILE SEQRES 17 A 413 GLU LYS LEU THR ALA ASP SER MET ASN VAL ASP LEU THR SEQRES 18 A 413 SER ALA ALA GLN ASN LEU ARG GLU ARG ALA LEU GLN ARG SEQRES 19 A 413 LEU MET THR SER VAL THR ASN ARG CYS GLN GLU LEU ALA SEQRES 20 A 413 THR ASN GLU TYR ALA ASN TYR ILE ILE GLN HIS ILE VAL SEQRES 21 A 413 SER ASN ASP ASP LEU ALA VAL TYR ARG GLU CYS ILE ILE SEQRES 22 A 413 GLU LYS CYS LEU MET ARG ASN LEU LEU SER LEU SER GLN SEQRES 23 A 413 GLU LYS PHE ALA SER HIS VAL VAL GLU LYS ALA PHE LEU SEQRES 24 A 413 HIS ALA PRO LEU GLU LEU LEU ALA GLU MET MET ASP GLU SEQRES 25 A 413 ILE PHE ASP GLY TYR ILE PRO HIS PRO ASP THR GLY LYS SEQRES 26 A 413 ASP ALA LEU ASP ILE MET MET PHE HIS GLN PHE GLY ASN SEQRES 27 A 413 TYR VAL VAL GLN CYS MET LEU THR ILE CYS CYS ASP ALA SEQRES 28 A 413 VAL SER GLY ARG ARG GLN THR LYS GLU GLY GLY TYR ASP SEQRES 29 A 413 HIS ALA ILE SER PHE GLN ASP TRP LEU LYS LYS LEU HIS SEQRES 30 A 413 SER ARG VAL THR LYS GLU ARG HIS ARG LEU SER ARG PHE SEQRES 31 A 413 SER SER GLY LYS LYS MET ILE GLU THR LEU ALA ASN LEU SEQRES 32 A 413 ARG SER THR HIS PRO ILE TYR GLU LEU GLN SEQRES 1 B 9 U G U G C C U U A FORMUL 3 HOH *452(H2 O) HELIX 1 1 PRO A 169 LEU A 173 5 5 HELIX 2 2 SER A 184 GLY A 192 1 9 HELIX 3 3 ASP A 193 VAL A 199 1 7 HELIX 4 4 ASP A 200 LYS A 212 1 13 HELIX 5 5 THR A 216 ILE A 228 1 13 HELIX 6 6 ARG A 230 THR A 239 1 10 HELIX 7 7 PHE A 242 THR A 257 1 16 HELIX 8 8 GLY A 261 GLN A 276 1 16 HELIX 9 9 GLN A 276 ASP A 283 1 8 HELIX 10 10 PHE A 285 MET A 297 1 13 HELIX 11 11 ASP A 298 ALA A 308 1 11 HELIX 12 12 ASP A 312 VAL A 320 1 9 HELIX 13 13 ALA A 324 ILE A 335 1 12 HELIX 14 14 PRO A 336 ALA A 348 1 13 HELIX 15 15 THR A 349 SER A 358 1 10 HELIX 16 16 TYR A 361 LEU A 373 1 13 HELIX 17 17 ASP A 376 VAL A 380 5 5 HELIX 18 18 THR A 383 ARG A 404 1 22 HELIX 19 19 ARG A 404 THR A 410 1 7 HELIX 20 20 ALA A 414 ASN A 424 1 11 HELIX 21 21 LEU A 427 LEU A 439 1 13 HELIX 22 22 ASN A 442 GLN A 448 1 7 HELIX 23 23 PHE A 451 ALA A 463 1 13 HELIX 24 24 PRO A 464 GLY A 478 1 15 HELIX 25 25 ASP A 488 HIS A 496 1 9 HELIX 26 26 PHE A 498 SER A 515 1 18 HELIX 27 27 HIS A 527 GLU A 545 1 19 HELIX 28 28 GLU A 545 SER A 550 1 6 HELIX 29 29 PHE A 552 SER A 567 1 16 SHEET 1 A 2 LYS A 521 GLU A 522 0 SHEET 2 A 2 TYR A 525 ASP A 526 -1 O TYR A 525 N GLU A 522 SSBOND 1 CYS A 405 CYS A 438 1555 1555 2.04 CRYST1 96.577 96.577 101.389 90.00 90.00 120.00 P 61 6 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 0.010354 0.005978 0.000000 0.00000 SCALE2 0.000000 0.011956 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009863 0.00000 ATOM 1 N LEU A 168 -6.325 13.687 -22.103 1.00 49.36 N ANISOU 1 N LEU A 168 5972 5307 7475 -490 -1249 -2142 N ATOM 2 CA LEU A 168 -7.214 14.772 -22.509 1.00 55.89 C ANISOU 2 CA LEU A 168 6865 6218 8152 -531 -1320 -2037 C ATOM 3 C LEU A 168 -8.311 14.329 -23.487 1.00 50.49 C ANISOU 3 C LEU A 168 6222 5581 7381 -606 -1578 -2128 C ATOM 4 O LEU A 168 -8.158 13.331 -24.189 1.00 52.90 O ANISOU 4 O LEU A 168 6566 5873 7661 -630 -1670 -2324 O ATOM 5 CB LEU A 168 -6.410 15.954 -23.067 1.00 63.18 C ANISOU 5 CB LEU A 168 7933 7238 8835 -517 -1149 -2053 C ATOM 6 CG LEU A 168 -5.295 15.732 -24.092 1.00 62.85 C ANISOU 6 CG LEU A 168 8026 7249 8607 -505 -1057 -2273 C ATOM 7 CD1 LEU A 168 -4.652 17.063 -24.403 1.00 48.97 C ANISOU 7 CD1 LEU A 168 6398 5579 6631 -481 -868 -2229 C ATOM 8 CD2 LEU A 168 -4.226 14.734 -23.641 1.00 75.79 C ANISOU 8 CD2 LEU A 168 9579 8811 10405 -464 -953 -2371 C ATOM 9 N PRO A 169 -9.418 15.086 -23.531 1.00 46.60 N ANISOU 9 N PRO A 169 5710 5157 6838 -644 -1697 -1981 N ATOM 10 CA PRO A 169 -10.634 14.790 -24.295 1.00 45.47 C ANISOU 10 CA PRO A 169 5559 5092 6626 -715 -1961 -2011 C ATOM 11 C PRO A 169 -10.332 14.477 -25.746 1.00 44.51 C ANISOU 11 C PRO A 169 5594 5071 6248 -746 -2044 -2242 C ATOM 12 O PRO A 169 -9.518 15.150 -26.378 1.00 48.09 O ANISOU 12 O PRO A 169 6186 5606 6481 -693 -1890 -2280 O ATOM 13 CB PRO A 169 -11.429 16.093 -24.205 1.00 50.08 C ANISOU 13 CB PRO A 169 6121 5788 7120 -686 -1962 -1765 C ATOM 14 CG PRO A 169 -10.940 16.745 -22.979 1.00 45.87 C ANISOU 14 CG PRO A 169 5530 5165 6733 -648 -1760 -1615 C ATOM 15 CD PRO A 169 -9.497 16.395 -22.866 1.00 44.61 C ANISOU 15 CD PRO A 169 5441 4932 6576 -619 -1571 -1770 C ATOM 16 N THR A 170 -10.993 13.447 -26.257 1.00 46.97 N ANISOU 16 N THR A 170 5879 5378 6590 -807 -2252 -2361 N ATOM 17 CA THR A 170 -10.821 13.032 -27.635 1.00 54.78 C ANISOU 17 CA THR A 170 7011 6462 7342 -844 -2348 -2583 C ATOM 18 C THR A 170 -11.188 14.148 -28.615 1.00 55.26 C ANISOU 18 C THR A 170 7174 6724 7097 -793 -2352 -2469 C ATOM 19 O THR A 170 -10.579 14.265 -29.677 1.00 54.61 O ANISOU 19 O THR A 170 7252 6732 6765 -778 -2301 -2607 O ATOM 20 CB THR A 170 -11.652 11.775 -27.929 1.00 57.37 C ANISOU 20 CB THR A 170 7274 6751 7772 -922 -2579 -2694 C ATOM 21 OG1 THR A 170 -11.620 11.497 -29.334 1.00 65.67 O ANISOU 21 OG1 THR A 170 8472 7919 8559 -971 -2694 -2902 O ATOM 22 CG2 THR A 170 -13.094 11.985 -27.488 1.00 60.54 C ANISOU 22 CG2 THR A 170 7528 7191 8283 -962 -2764 -2496 C ATOM 23 N TRP A 171 -12.168 14.974 -28.257 1.00 52.13 N ANISOU 23 N TRP A 171 6689 6398 6719 -765 -2406 -2214 N ATOM 24 CA TRP A 171 -12.585 16.064 -29.137 1.00 51.79 C ANISOU 24 CA TRP A 171 6737 6543 6397 -707 -2416 -2080 C ATOM 25 C TRP A 171 -11.440 17.028 -29.424 1.00 52.32 C ANISOU 25 C TRP A 171 6959 6654 6268 -628 -2158 -2071 C ATOM 26 O TRP A 171 -11.436 17.720 -30.445 1.00 51.21 O ANISOU 26 O TRP A 171 6953 6663 5843 -589 -2146 -2048 O ATOM 27 CB TRP A 171 -13.784 16.825 -28.559 1.00 48.07 C ANISOU 27 CB TRP A 171 6131 6121 6012 -677 -2493 -1793 C ATOM 28 CG TRP A 171 -13.503 17.591 -27.287 1.00 43.47 C ANISOU 28 CG TRP A 171 5471 5444 5603 -621 -2295 -1598 C ATOM 29 CD1 TRP A 171 -13.807 17.203 -26.014 1.00 39.03 C ANISOU 29 CD1 TRP A 171 4744 4740 5347 -654 -2301 -1522 C ATOM 30 CD2 TRP A 171 -12.893 18.884 -27.176 1.00 43.85 C ANISOU 30 CD2 TRP A 171 5608 5532 5521 -531 -2062 -1454 C ATOM 31 NE1 TRP A 171 -13.412 18.164 -25.116 1.00 38.10 N ANISOU 31 NE1 TRP A 171 4607 4575 5294 -591 -2088 -1345 N ATOM 32 CE2 TRP A 171 -12.850 19.208 -25.805 1.00 41.68 C ANISOU 32 CE2 TRP A 171 5213 5136 5486 -516 -1938 -1302 C ATOM 33 CE3 TRP A 171 -12.375 19.796 -28.100 1.00 45.56 C ANISOU 33 CE3 TRP A 171 5998 5873 5439 -467 -1943 -1441 C ATOM 34 CZ2 TRP A 171 -12.307 20.404 -25.338 1.00 41.76 C ANISOU 34 CZ2 TRP A 171 5273 5146 5448 -443 -1700 -1144 C ATOM 35 CZ3 TRP A 171 -11.835 20.981 -27.634 1.00 43.54 C ANISOU 35 CZ3 TRP A 171 5792 5612 5141 -393 -1705 -1281 C ATOM 36 CH2 TRP A 171 -11.805 21.274 -26.266 1.00 39.04 C ANISOU 36 CH2 TRP A 171 5100 4920 4815 -384 -1586 -1137 C ATOM 37 N SER A 172 -10.463 17.062 -28.526 1.00 53.77 N ANISOU 37 N SER A 172 7123 6707 6601 -609 -1954 -2089 N ATOM 38 CA SER A 172 -9.360 18.004 -28.641 1.00 51.01 C ANISOU 38 CA SER A 172 6899 6387 6094 -542 -1694 -2069 C ATOM 39 C SER A 172 -8.150 17.380 -29.319 1.00 51.86 C ANISOU 39 C SER A 172 7137 6476 6092 -559 -1602 -2345 C ATOM 40 O SER A 172 -7.095 18.002 -29.395 1.00 49.37 O ANISOU 40 O SER A 172 6921 6174 5665 -515 -1377 -2367 O ATOM 41 CB SER A 172 -8.945 18.504 -27.261 1.00 46.03 C ANISOU 41 CB SER A 172 6173 5640 5677 -512 -1510 -1921 C ATOM 42 OG SER A 172 -8.008 17.618 -26.672 1.00 40.91 O ANISOU 42 OG SER A 172 5489 4848 5207 -544 -1432 -2097 O ATOM 43 N LEU A 173 -8.299 16.151 -29.803 1.00 54.63 N ANISOU 43 N LEU A 173 7485 6794 6477 -626 -1769 -2559 N ATOM 44 CA LEU A 173 -7.174 15.424 -30.394 1.00 61.01 C ANISOU 44 CA LEU A 173 8405 7566 7212 -644 -1687 -2837 C ATOM 45 C LEU A 173 -7.286 15.283 -31.911 1.00 62.21 C ANISOU 45 C LEU A 173 8715 7859 7061 -665 -1784 -2986 C ATOM 46 O LEU A 173 -8.385 15.187 -32.458 1.00 58.03 O ANISOU 46 O LEU A 173 8174 7422 6452 -699 -1997 -2938 O ATOM 47 CB LEU A 173 -7.028 14.036 -29.759 1.00 58.27 C ANISOU 47 CB LEU A 173 7953 7045 7143 -702 -1768 -3003 C ATOM 48 CG LEU A 173 -6.690 13.979 -28.268 1.00 55.22 C ANISOU 48 CG LEU A 173 7409 6508 7063 -670 -1643 -2874 C ATOM 49 CD1 LEU A 173 -6.666 12.540 -27.781 1.00 57.44 C ANISOU 49 CD1 LEU A 173 7566 6647 7611 -683 -1708 -2962 C ATOM 50 CD2 LEU A 173 -5.362 14.670 -27.971 1.00 47.77 C ANISOU 50 CD2 LEU A 173 6513 5560 6078 -598 -1354 -2853 C ATOM 51 N ASP A 174 -6.139 15.278 -32.584 1.00 65.13 N ANISOU 51 N ASP A 174 9232 8253 7263 -649 -1624 -3167 N ATOM 52 CA ASP A 174 -6.105 15.059 -34.026 1.00 71.90 C ANISOU 52 CA ASP A 174 10254 9235 7832 -675 -1696 -3339 C ATOM 53 C ASP A 174 -6.086 13.566 -34.335 1.00 83.49 C ANISOU 53 C ASP A 174 11712 10615 9396 -753 -1838 -3608 C ATOM 54 O ASP A 174 -6.297 12.739 -33.446 1.00 83.84 O ANISOU 54 O ASP A 174 11616 10510 9730 -786 -1912 -3632 O ATOM 55 CB ASP A 174 -4.901 15.762 -34.667 1.00 72.02 C ANISOU 55 CB ASP A 174 10439 9320 7605 -626 -1451 -3413 C ATOM 56 CG ASP A 174 -3.567 15.245 -34.147 1.00 78.36 C ANISOU 56 CG ASP A 174 11230 9988 8556 -615 -1253 -3588 C ATOM 57 OD1 ASP A 174 -2.549 15.947 -34.328 1.00 80.40 O ANISOU 57 OD1 ASP A 174 11583 10285 8681 -569 -1020 -3599 O ATOM 58 OD2 ASP A 174 -3.528 14.145 -33.558 1.00 79.55 O ANISOU 58 OD2 ASP A 174 11256 9998 8971 -642 -1317 -3676 O ATOM 59 N SER A 175 -5.825 13.231 -35.595 1.00 88.16 N ANISOU 59 N SER A 175 12462 11295 9741 -783 -1871 -3811 N ATOM 60 CA SER A 175 -5.807 11.843 -36.039 1.00 95.05 C ANISOU 60 CA SER A 175 13353 12093 10669 -860 -2002 -4083 C ATOM 61 C SER A 175 -4.728 11.020 -35.340 1.00 94.41 C ANISOU 61 C SER A 175 13189 11832 10851 -826 -1829 -4190 C ATOM 62 O SER A 175 -4.945 9.856 -35.005 1.00 90.80 O ANISOU 62 O SER A 175 12634 11249 10617 -862 -1930 -4279 O ATOM 63 CB SER A 175 -5.608 11.777 -37.554 1.00 99.59 C ANISOU 63 CB SER A 175 14127 12808 10904 -889 -2027 -4266 C ATOM 64 OG SER A 175 -6.531 12.618 -38.223 1.00102.85 O ANISOU 64 OG SER A 175 14591 13406 11081 -887 -2148 -4095 O ATOM 65 N ASN A 176 -3.567 11.630 -35.119 1.00 97.20 N ANISOU 65 N ASN A 176 13570 12180 11181 -749 -1565 -4160 N ATOM 66 CA ASN A 176 -2.434 10.928 -34.520 1.00100.91 C ANISOU 66 CA ASN A 176 13950 12512 11880 -703 -1387 -4239 C ATOM 67 C ASN A 176 -2.347 11.026 -32.993 1.00 96.71 C ANISOU 67 C ASN A 176 13222 11857 11664 -658 -1314 -4043 C ATOM 68 O ASN A 176 -1.275 10.849 -32.414 1.00 95.48 O ANISOU 68 O ASN A 176 12993 11629 11655 -603 -1126 -4051 O ATOM 69 CB ASN A 176 -1.113 11.366 -35.168 1.00106.74 C ANISOU 69 CB ASN A 176 14807 13316 12433 -656 -1141 -4339 C ATOM 70 CG ASN A 176 -1.119 12.826 -35.591 1.00111.13 C ANISOU 70 CG ASN A 176 15488 14025 12712 -632 -1046 -4206 C ATOM 71 OD1 ASN A 176 -1.844 13.219 -36.506 1.00113.00 O ANISOU 71 OD1 ASN A 176 15862 14391 12683 -669 -1177 -4222 O ATOM 72 ND2 ASN A 176 -0.293 13.634 -34.936 1.00112.33 N ANISOU 72 ND2 ASN A 176 15594 14168 12918 -571 -818 -4072 N ATOM 73 N GLY A 177 -3.476 11.304 -32.347 1.00 93.52 N ANISOU 73 N GLY A 177 12731 11442 11362 -683 -1467 -3866 N ATOM 74 CA GLY A 177 -3.552 11.286 -30.895 1.00 89.15 C ANISOU 74 CA GLY A 177 11990 10769 11113 -650 -1424 -3682 C ATOM 75 C GLY A 177 -2.848 12.437 -30.198 1.00 85.85 C ANISOU 75 C GLY A 177 11548 10375 10696 -584 -1198 -3507 C ATOM 76 O GLY A 177 -2.538 12.360 -29.008 1.00 82.43 O ANISOU 76 O GLY A 177 10966 9847 10508 -547 -1108 -3384 O ATOM 77 N GLU A 178 -2.594 13.510 -30.937 1.00 83.50 N ANISOU 77 N GLU A 178 11400 10209 10116 -571 -1102 -3494 N ATOM 78 CA GLU A 178 -1.969 14.692 -30.363 1.00 81.26 C ANISOU 78 CA GLU A 178 11112 9956 9805 -517 -882 -3328 C ATOM 79 C GLU A 178 -2.970 15.833 -30.243 1.00 74.03 C ANISOU 79 C GLU A 178 10238 9116 8774 -525 -955 -3138 C ATOM 80 O GLU A 178 -3.952 15.887 -30.980 1.00 75.80 O ANISOU 80 O GLU A 178 10537 9426 8840 -564 -1150 -3152 O ATOM 81 CB GLU A 178 -0.770 15.127 -31.206 1.00 88.38 C ANISOU 81 CB GLU A 178 12149 10945 10486 -487 -673 -3438 C ATOM 82 CG GLU A 178 0.387 14.144 -31.180 1.00 97.26 C ANISOU 82 CG GLU A 178 13213 11999 11743 -472 -563 -3603 C ATOM 83 CD GLU A 178 1.623 14.681 -31.873 1.00104.82 C ANISOU 83 CD GLU A 178 14277 13043 12509 -447 -335 -3681 C ATOM 84 OE1 GLU A 178 2.730 14.172 -31.595 1.00109.20 O ANISOU 84 OE1 GLU A 178 14751 13547 13193 -427 -198 -3759 O ATOM 85 OE2 GLU A 178 1.488 15.615 -32.691 1.00106.12 O ANISOU 85 OE2 GLU A 178 14601 13329 12393 -450 -295 -3657 O ATOM 86 N MET A 179 -2.722 16.744 -29.308 1.00 68.47 N ANISOU 86 N MET A 179 9475 8390 8151 -487 -799 -2946 N ATOM 87 CA MET A 179 -3.594 17.896 -29.136 1.00 60.03 C ANISOU 87 CA MET A 179 8427 7393 6990 -475 -830 -2726 C ATOM 88 C MET A 179 -3.596 18.755 -30.398 1.00 58.59 C ANISOU 88 C MET A 179 8424 7381 6456 -448 -786 -2710 C ATOM 89 O MET A 179 -2.537 19.105 -30.913 1.00 58.00 O ANISOU 89 O MET A 179 8473 7350 6213 -428 -598 -2816 O ATOM 90 CB MET A 179 -3.152 18.730 -27.929 1.00 55.15 C ANISOU 90 CB MET A 179 7732 6713 6510 -441 -633 -2546 C ATOM 91 CG MET A 179 -4.200 19.721 -27.461 1.00 50.89 C ANISOU 91 CG MET A 179 7137 6216 5981 -416 -670 -2254 C ATOM 92 SD MET A 179 -3.613 20.838 -26.177 1.00 46.36 S ANISOU 92 SD MET A 179 6510 5585 5521 -381 -411 -2052 S ATOM 93 CE MET A 179 -2.466 21.843 -27.120 1.00 44.76 C ANISOU 93 CE MET A 179 6510 5499 4996 -343 -161 -2112 C ATOM 94 N ARG A 180 -4.786 19.085 -30.895 1.00 60.18 N ANISOU 94 N ARG A 180 8637 7682 6548 -448 -962 -2576 N ATOM 95 CA ARG A 180 -4.930 19.918 -32.091 1.00 63.30 C ANISOU 95 CA ARG A 180 9200 8245 6606 -419 -946 -2534 C ATOM 96 C ARG A 180 -4.197 21.250 -31.946 1.00 65.27 C ANISOU 96 C ARG A 180 9539 8535 6725 -360 -679 -2399 C ATOM 97 O ARG A 180 -3.937 21.703 -30.831 1.00 60.60 O ANISOU 97 O ARG A 180 8855 7857 6311 -340 -544 -2270 O ATOM 98 CB ARG A 180 -6.408 20.171 -32.391 1.00 61.83 C ANISOU 98 CB ARG A 180 8974 8150 6367 -417 -1176 -2359 C ATOM 99 CG ARG A 180 -7.160 18.961 -32.916 1.00 67.43 C ANISOU 99 CG ARG A 180 9643 8867 7112 -485 -1449 -2510 C ATOM 100 CD ARG A 180 -8.650 19.079 -32.631 1.00 69.00 C ANISOU 100 CD ARG A 180 9712 9102 7400 -489 -1671 -2308 C ATOM 101 NE ARG A 180 -9.178 20.399 -32.967 1.00 71.38 N ANISOU 101 NE ARG A 180 10075 9536 7509 -420 -1641 -2067 N ATOM 102 CZ ARG A 180 -10.361 20.852 -32.565 1.00 74.61 C ANISOU 102 CZ ARG A 180 10370 9980 7998 -395 -1768 -1834 C ATOM 103 NH1 ARG A 180 -11.140 20.092 -31.806 1.00 73.38 N ANISOU 103 NH1 ARG A 180 10032 9739 8109 -443 -1933 -1813 N ATOM 104 NH2 ARG A 180 -10.766 22.066 -32.915 1.00 77.90 N ANISOU 104 NH2 ARG A 180 10854 10513 8230 -321 -1726 -1620 N ATOM 105 N SER A 181 -3.882 21.878 -33.077 1.00 72.88 N ANISOU 105 N SER A 181 10687 9630 7373 -338 -603 -2429 N ATOM 106 CA SER A 181 -3.070 23.096 -33.093 1.00 77.43 C ANISOU 106 CA SER A 181 11376 10248 7797 -292 -335 -2334 C ATOM 107 C SER A 181 -3.887 24.385 -33.115 1.00 73.20 C ANISOU 107 C SER A 181 10877 9795 7141 -236 -328 -2043 C ATOM 108 O SER A 181 -3.409 25.435 -32.687 1.00 75.86 O ANISOU 108 O SER A 181 11253 10123 7446 -199 -109 -1906 O ATOM 109 CB SER A 181 -2.108 23.086 -34.284 1.00 89.08 C ANISOU 109 CB SER A 181 13044 11809 8993 -302 -216 -2538 C ATOM 110 OG SER A 181 -1.006 22.230 -34.046 1.00 95.05 O ANISOU 110 OG SER A 181 13771 12474 9870 -334 -114 -2778 O ATOM 111 N ARG A 182 -5.114 24.309 -33.616 1.00 63.08 N ANISOU 111 N ARG A 182 9581 8594 5793 -230 -564 -1951 N ATOM 112 CA ARG A 182 -5.947 25.498 -33.740 1.00 60.58 C ANISOU 112 CA ARG A 182 9302 8365 5353 -165 -575 -1676 C ATOM 113 C ARG A 182 -7.000 25.587 -32.634 1.00 47.83 C ANISOU 113 C ARG A 182 7492 6679 4003 -148 -688 -1463 C ATOM 114 O ARG A 182 -8.076 26.151 -32.836 1.00 44.24 O ANISOU 114 O ARG A 182 7021 6302 3485 -104 -812 -1264 O ATOM 115 CB ARG A 182 -6.624 25.528 -35.110 1.00 73.16 C ANISOU 115 CB ARG A 182 11018 10117 6660 -158 -754 -1688 C ATOM 116 CG ARG A 182 -5.655 25.579 -36.284 1.00 84.55 C ANISOU 116 CG ARG A 182 12675 11645 7805 -172 -635 -1876 C ATOM 117 CD ARG A 182 -6.367 25.353 -37.615 1.00 92.57 C ANISOU 117 CD ARG A 182 13799 12815 8559 -182 -850 -1922 C ATOM 118 NE ARG A 182 -7.451 26.308 -37.839 1.00 97.28 N ANISOU 118 NE ARG A 182 14409 13513 9039 -115 -949 -1647 N ATOM 119 CZ ARG A 182 -8.733 26.056 -37.591 1.00100.37 C ANISOU 119 CZ ARG A 182 14655 13926 9554 -109 -1196 -1520 C ATOM 120 NH1 ARG A 182 -9.099 24.876 -37.109 1.00101.01 N ANISOU 120 NH1 ARG A 182 14573 13929 9876 -175 -1368 -1644 N ATOM 121 NH2 ARG A 182 -9.652 26.985 -37.823 1.00100.90 N ANISOU 121 NH2 ARG A 182 14739 14091 9507 -37 -1269 -1266 N ATOM 122 N LEU A 183 -6.686 25.037 -31.467 1.00 43.40 N ANISOU 122 N LEU A 183 6782 5973 3737 -181 -642 -1503 N ATOM 123 CA LEU A 183 -7.631 25.020 -30.357 1.00 38.27 C ANISOU 123 CA LEU A 183 5942 5245 3355 -175 -741 -1321 C ATOM 124 C LEU A 183 -7.800 26.423 -29.795 1.00 38.25 C ANISOU 124 C LEU A 183 5953 5245 3335 -106 -573 -1050 C ATOM 125 O LEU A 183 -6.841 27.187 -29.719 1.00 37.50 O ANISOU 125 O LEU A 183 5963 5140 3144 -86 -323 -1039 O ATOM 126 CB LEU A 183 -7.136 24.077 -29.262 1.00 44.53 C ANISOU 126 CB LEU A 183 6590 5879 4451 -230 -717 -1441 C ATOM 127 CG LEU A 183 -8.207 23.291 -28.509 1.00 51.27 C ANISOU 127 CG LEU A 183 7246 6658 5575 -265 -937 -1386 C ATOM 128 CD1 LEU A 183 -8.893 22.317 -29.456 1.00 53.81 C ANISOU 128 CD1 LEU A 183 7571 7049 5826 -309 -1204 -1529 C ATOM 129 CD2 LEU A 183 -7.592 22.552 -27.332 1.00 54.12 C ANISOU 129 CD2 LEU A 183 7483 6855 6226 -310 -867 -1475 C ATOM 130 N SER A 184 -9.018 26.761 -29.386 1.00 39.05 N ANISOU 130 N SER A 184 5945 5358 3536 -73 -703 -833 N ATOM 131 CA SER A 184 -9.275 28.077 -28.802 1.00 34.51 C ANISOU 131 CA SER A 184 5374 4773 2964 -4 -547 -568 C ATOM 132 C SER A 184 -9.516 27.976 -27.299 1.00 33.17 C ANISOU 132 C SER A 184 5021 4464 3120 -21 -509 -462 C ATOM 133 O SER A 184 -9.976 26.947 -26.799 1.00 34.23 O ANISOU 133 O SER A 184 5000 4533 3472 -74 -678 -531 O ATOM 134 CB SER A 184 -10.475 28.738 -29.480 1.00 40.42 C ANISOU 134 CB SER A 184 6149 5647 3561 66 -695 -370 C ATOM 135 OG SER A 184 -11.688 28.235 -28.952 1.00 39.15 O ANISOU 135 OG SER A 184 5798 5466 3613 56 -916 -277 O ATOM 136 N LEU A 185 -9.201 29.041 -26.570 1.00 29.15 N ANISOU 136 N LEU A 185 4532 3904 2640 17 -283 -297 N ATOM 137 CA LEU A 185 -9.420 29.035 -25.132 1.00 25.00 C ANISOU 137 CA LEU A 185 3843 3248 2406 -1 -231 -187 C ATOM 138 C LEU A 185 -10.893 28.807 -24.827 1.00 25.45 C ANISOU 138 C LEU A 185 3743 3314 2614 15 -458 -37 C ATOM 139 O LEU A 185 -11.235 28.036 -23.927 1.00 25.60 O ANISOU 139 O LEU A 185 3595 3237 2894 -36 -550 -56 O ATOM 140 CB LEU A 185 -8.956 30.349 -24.500 1.00 23.54 C ANISOU 140 CB LEU A 185 3724 3023 2198 39 47 -16 C ATOM 141 CG LEU A 185 -9.212 30.490 -22.996 1.00 24.34 C ANISOU 141 CG LEU A 185 3669 2996 2582 22 119 118 C ATOM 142 CD1 LEU A 185 -8.552 29.388 -22.188 1.00 27.53 C ANISOU 142 CD1 LEU A 185 3963 3291 3208 -62 111 -60 C ATOM 143 CD2 LEU A 185 -8.749 31.857 -22.492 1.00 22.74 C ANISOU 143 CD2 LEU A 185 3556 2763 2323 59 400 282 C ATOM 144 N SER A 186 -11.762 29.484 -25.575 1.00 27.03 N ANISOU 144 N SER A 186 3995 3629 2648 86 -546 116 N ATOM 145 CA SER A 186 -13.195 29.398 -25.307 1.00 31.31 C ANISOU 145 CA SER A 186 4381 4191 3323 110 -751 280 C ATOM 146 C SER A 186 -13.748 27.985 -25.498 1.00 29.84 C ANISOU 146 C SER A 186 4070 4012 3256 36 -1027 121 C ATOM 147 O SER A 186 -14.591 27.549 -24.723 1.00 28.04 O ANISOU 147 O SER A 186 3663 3727 3263 11 -1151 194 O ATOM 148 CB SER A 186 -13.974 30.430 -26.117 1.00 30.19 C ANISOU 148 CB SER A 186 4323 4180 2969 211 -790 478 C ATOM 149 OG SER A 186 -13.865 31.696 -25.490 1.00 28.46 O ANISOU 149 OG SER A 186 4145 3913 2757 278 -559 688 O ATOM 150 N GLU A 187 -13.254 27.268 -26.502 1.00 29.93 N ANISOU 150 N GLU A 187 4179 4086 3108 -4 -1113 -101 N ATOM 151 CA GLU A 187 -13.609 25.855 -26.676 1.00 31.65 C ANISOU 151 CA GLU A 187 4296 4291 3439 -87 -1352 -286 C ATOM 152 C GLU A 187 -13.301 25.052 -25.418 1.00 29.53 C ANISOU 152 C GLU A 187 3884 3855 3481 -157 -1317 -359 C ATOM 153 O GLU A 187 -14.127 24.279 -24.941 1.00 30.17 O ANISOU 153 O GLU A 187 3804 3892 3768 -205 -1498 -354 O ATOM 154 CB GLU A 187 -12.815 25.228 -27.818 1.00 35.15 C ANISOU 154 CB GLU A 187 4888 4796 3672 -125 -1382 -542 C ATOM 155 CG GLU A 187 -13.186 25.683 -29.201 1.00 48.29 C ANISOU 155 CG GLU A 187 6690 6633 5024 -80 -1478 -520 C ATOM 156 CD GLU A 187 -12.341 24.994 -30.253 1.00 64.40 C ANISOU 156 CD GLU A 187 8876 8721 6871 -128 -1494 -791 C ATOM 157 OE1 GLU A 187 -12.455 23.755 -30.390 1.00 69.56 O ANISOU 157 OE1 GLU A 187 9465 9345 7619 -207 -1663 -983 O ATOM 158 OE2 GLU A 187 -11.557 25.690 -30.931 1.00 69.89 O ANISOU 158 OE2 GLU A 187 9753 9478 7322 -89 -1329 -813 O ATOM 159 N VAL A 188 -12.098 25.231 -24.887 1.00 27.83 N ANISOU 159 N VAL A 188 3728 3549 3296 -165 -1085 -427 N ATOM 160 CA VAL A 188 -11.705 24.510 -23.688 1.00 25.32 C ANISOU 160 CA VAL A 188 3286 3076 3260 -227 -1040 -493 C ATOM 161 C VAL A 188 -12.570 24.929 -22.494 1.00 23.96 C ANISOU 161 C VAL A 188 2957 2834 3314 -214 -1035 -262 C ATOM 162 O VAL A 188 -13.056 24.086 -21.756 1.00 30.52 O ANISOU 162 O VAL A 188 3635 3577 4385 -272 -1157 -281 O ATOM 163 CB VAL A 188 -10.215 24.707 -23.359 1.00 32.60 C ANISOU 163 CB VAL A 188 4300 3930 4158 -233 -785 -600 C ATOM 164 CG1 VAL A 188 -9.855 23.960 -22.086 1.00 31.45 C ANISOU 164 CG1 VAL A 188 4018 3626 4305 -293 -752 -654 C ATOM 165 CG2 VAL A 188 -9.359 24.235 -24.517 1.00 30.73 C ANISOU 165 CG2 VAL A 188 4209 3757 3712 -248 -785 -839 C ATOM 166 N LEU A 189 -12.773 26.227 -22.318 1.00 23.52 N ANISOU 166 N LEU A 189 2944 2814 3179 -141 -892 -46 N ATOM 167 CA LEU A 189 -13.569 26.716 -21.200 1.00 27.25 C ANISOU 167 CA LEU A 189 3279 3222 3854 -124 -864 176 C ATOM 168 C LEU A 189 -15.013 26.224 -21.265 1.00 28.06 C ANISOU 168 C LEU A 189 3231 3364 4067 -132 -1127 256 C ATOM 169 O LEU A 189 -15.607 25.867 -20.247 1.00 23.74 O ANISOU 169 O LEU A 189 2521 2728 3771 -169 -1177 330 O ATOM 170 CB LEU A 189 -13.548 28.242 -21.173 1.00 22.62 C ANISOU 170 CB LEU A 189 2787 2675 3132 -35 -662 388 C ATOM 171 CG LEU A 189 -12.200 28.873 -20.802 1.00 21.06 C ANISOU 171 CG LEU A 189 2711 2419 2873 -37 -371 351 C ATOM 172 CD1 LEU A 189 -12.307 30.376 -20.910 1.00 20.27 C ANISOU 172 CD1 LEU A 189 2716 2364 2622 50 -192 563 C ATOM 173 CD2 LEU A 189 -11.802 28.463 -19.384 1.00 21.06 C ANISOU 173 CD2 LEU A 189 2590 2269 3142 -102 -279 336 C ATOM 174 N ASP A 190 -15.577 26.236 -22.469 1.00 28.93 N ANISOU 174 N ASP A 190 3396 3614 3981 -100 -1291 243 N ATOM 175 CA ASP A 190 -16.968 25.834 -22.682 1.00 31.22 C ANISOU 175 CA ASP A 190 3548 3971 4343 -106 -1551 319 C ATOM 176 C ASP A 190 -17.180 24.329 -22.443 1.00 35.26 C ANISOU 176 C ASP A 190 3936 4415 5047 -216 -1746 135 C ATOM 177 O ASP A 190 -18.275 23.888 -22.077 1.00 38.67 O ANISOU 177 O ASP A 190 4202 4842 5648 -247 -1921 207 O ATOM 178 CB ASP A 190 -17.399 26.194 -24.109 1.00 33.17 C ANISOU 178 CB ASP A 190 3901 4396 4306 -50 -1679 332 C ATOM 179 CG ASP A 190 -17.679 27.682 -24.290 1.00 36.86 C ANISOU 179 CG ASP A 190 4445 4937 4623 69 -1548 575 C ATOM 180 OD1 ASP A 190 -17.968 28.096 -25.435 1.00 37.30 O ANISOU 180 OD1 ASP A 190 4602 5137 4431 126 -1631 606 O ATOM 181 OD2 ASP A 190 -17.632 28.438 -23.301 1.00 34.91 O ANISOU 181 OD2 ASP A 190 4160 4603 4501 106 -1365 738 O ATOM 182 N SER A 191 -16.118 23.555 -22.643 1.00 29.27 N ANISOU 182 N SER A 191 3257 3600 4263 -273 -1705 -100 N ATOM 183 CA SER A 191 -16.192 22.092 -22.732 1.00 36.14 C ANISOU 183 CA SER A 191 4058 4419 5256 -372 -1893 -311 C ATOM 184 C SER A 191 -16.427 21.379 -21.404 1.00 36.63 C ANISOU 184 C SER A 191 3949 4323 5646 -441 -1911 -297 C ATOM 185 O SER A 191 -16.894 20.244 -21.384 1.00 37.47 O ANISOU 185 O SER A 191 3961 4389 5885 -521 -2101 -412 O ATOM 186 CB SER A 191 -14.894 21.552 -23.309 1.00 32.93 C ANISOU 186 CB SER A 191 3797 3989 4727 -400 -1813 -562 C ATOM 187 OG SER A 191 -13.873 21.644 -22.324 1.00 30.37 O ANISOU 187 OG SER A 191 3477 3532 4531 -405 -1594 -581 O ATOM 188 N GLY A 192 -16.073 22.032 -20.304 1.00 35.20 N ANISOU 188 N GLY A 192 3737 4049 5588 -414 -1708 -163 N ATOM 189 CA GLY A 192 -16.137 21.418 -18.991 1.00 35.70 C ANISOU 189 CA GLY A 192 3659 3957 5948 -478 -1694 -149 C ATOM 190 C GLY A 192 -14.924 20.538 -18.735 1.00 38.02 C ANISOU 190 C GLY A 192 4001 4137 6308 -533 -1621 -368 C ATOM 191 O GLY A 192 -14.854 19.841 -17.726 1.00 41.66 O ANISOU 191 O GLY A 192 4406 4447 6977 -529 -1574 -362 O ATOM 192 N ASP A 193 -13.961 20.582 -19.650 1.00 31.36 N ANISOU 192 N ASP A 193 3315 3349 5251 -509 -1552 -524 N ATOM 193 CA ASP A 193 -12.796 19.704 -19.588 1.00 30.68 C ANISOU 193 CA ASP A 193 3280 3171 5207 -552 -1496 -752 C ATOM 194 C ASP A 193 -11.510 20.403 -19.162 1.00 27.78 C ANISOU 194 C ASP A 193 3003 2766 4788 -514 -1223 -750 C ATOM 195 O ASP A 193 -10.431 19.819 -19.239 1.00 30.12 O ANISOU 195 O ASP A 193 3357 3012 5077 -522 -1147 -931 O ATOM 196 CB ASP A 193 -12.574 19.028 -20.940 1.00 30.89 C ANISOU 196 CB ASP A 193 3412 3276 5047 -568 -1623 -971 C ATOM 197 CG ASP A 193 -13.617 17.966 -21.235 1.00 41.87 C ANISOU 197 CG ASP A 193 4707 4668 6535 -637 -1897 -1041 C ATOM 198 OD1 ASP A 193 -14.043 17.849 -22.402 1.00 43.29 O ANISOU 198 OD1 ASP A 193 4950 4970 6528 -638 -2041 -1111 O ATOM 199 OD2 ASP A 193 -14.016 17.253 -20.293 1.00 43.90 O ANISOU 199 OD2 ASP A 193 4847 4797 7036 -647 -1924 -992 O ATOM 200 N LEU A 194 -11.615 21.652 -18.725 1.00 24.88 N ANISOU 200 N LEU A 194 2994 3084 3377 -118 -1033 247 N ATOM 201 CA LEU A 194 -10.419 22.398 -18.325 1.00 27.54 C ANISOU 201 CA LEU A 194 3310 3433 3721 -88 -932 213 C ATOM 202 C LEU A 194 -9.486 21.619 -17.387 1.00 29.77 C ANISOU 202 C LEU A 194 3579 3669 4062 -89 -959 173 C ATOM 203 O LEU A 194 -8.267 21.650 -17.548 1.00 26.28 O ANISOU 203 O LEU A 194 3142 3217 3625 -51 -913 107 O ATOM 204 CB LEU A 194 -10.801 23.734 -17.695 1.00 25.04 C ANISOU 204 CB LEU A 194 2948 3162 3403 -101 -848 281 C ATOM 205 CG LEU A 194 -9.631 24.565 -17.145 1.00 24.71 C ANISOU 205 CG LEU A 194 2883 3132 3374 -79 -750 257 C ATOM 206 CD1 LEU A 194 -9.917 26.055 -17.297 1.00 24.37 C ANISOU 206 CD1 LEU A 194 2825 3139 3297 -71 -657 302 C ATOM 207 CD2 LEU A 194 -9.348 24.235 -15.688 1.00 34.61 C ANISOU 207 CD2 LEU A 194 4105 4357 4689 -108 -768 273 C ATOM 208 N MET A 195 -10.052 20.932 -16.402 1.00 25.51 N ANISOU 208 N MET A 195 3023 3101 3568 -135 -1033 215 N ATOM 209 CA MET A 195 -9.235 20.207 -15.427 1.00 27.33 C ANISOU 209 CA MET A 195 3245 3284 3856 -143 -1067 185 C ATOM 210 C MET A 195 -8.342 19.152 -16.085 1.00 30.05 C ANISOU 210 C MET A 195 3629 3580 4209 -104 -1120 94 C ATOM 211 O MET A 195 -7.267 18.854 -15.582 1.00 28.22 O ANISOU 211 O MET A 195 3389 3316 4018 -85 -1115 47 O ATOM 212 CB MET A 195 -10.104 19.570 -14.338 1.00 27.55 C ANISOU 212 CB MET A 195 3256 3288 3923 -206 -1146 250 C ATOM 213 CG MET A 195 -10.783 20.582 -13.415 1.00 32.81 C ANISOU 213 CG MET A 195 3878 3997 4590 -240 -1084 333 C ATOM 214 SD MET A 195 -9.597 21.515 -12.420 1.00 30.25 S ANISOU 214 SD MET A 195 3528 3679 4286 -223 -985 319 S ATOM 215 CE MET A 195 -8.865 20.188 -11.464 1.00 28.57 C ANISOU 215 CE MET A 195 3328 3392 4135 -245 -1079 286 C ATOM 216 N LYS A 196 -8.776 18.586 -17.207 1.00 28.29 N ANISOU 216 N LYS A 196 3452 3349 3950 -90 -1173 68 N ATOM 217 CA LYS A 196 -7.937 17.616 -17.915 1.00 29.88 C ANISOU 217 CA LYS A 196 3696 3503 4152 -45 -1217 -25 C ATOM 218 C LYS A 196 -6.764 18.284 -18.638 1.00 32.32 C ANISOU 218 C LYS A 196 4006 3840 4433 18 -1110 -94 C ATOM 219 O LYS A 196 -5.668 17.734 -18.705 1.00 33.55 O ANISOU 219 O LYS A 196 4167 3962 4616 58 -1111 -170 O ATOM 220 CB LYS A 196 -8.768 16.799 -18.906 1.00 30.31 C ANISOU 220 CB LYS A 196 3809 3537 4171 -50 -1310 -34 C ATOM 221 CG LYS A 196 -9.851 15.946 -18.265 1.00 36.00 C ANISOU 221 CG LYS A 196 4530 4223 4925 -114 -1429 27 C ATOM 222 CD LYS A 196 -10.525 15.051 -19.305 1.00 40.93 C ANISOU 222 CD LYS A 196 5219 4817 5517 -115 -1530 8 C ATOM 223 CE LYS A 196 -11.792 14.407 -18.756 1.00 47.86 C ANISOU 223 CE LYS A 196 6088 5672 6423 -189 -1640 87 C ATOM 224 NZ LYS A 196 -12.851 15.417 -18.456 1.00 51.09 N ANISOU 224 NZ LYS A 196 6447 6145 6821 -230 -1592 183 N ATOM 225 N PHE A 197 -7.001 19.466 -19.192 1.00 24.25 N ANISOU 225 N PHE A 197 2978 2879 3359 25 -1019 -66 N ATOM 226 CA PHE A 197 -5.929 20.239 -19.822 1.00 25.81 C ANISOU 226 CA PHE A 197 3171 3109 3527 75 -908 -118 C ATOM 227 C PHE A 197 -4.923 20.756 -18.806 1.00 22.99 C ANISOU 227 C PHE A 197 2758 2754 3224 79 -844 -122 C ATOM 228 O PHE A 197 -3.723 20.734 -19.045 1.00 25.21 O ANISOU 228 O PHE A 197 3030 3030 3520 122 -794 -189 O ATOM 229 CB PHE A 197 -6.512 21.436 -20.572 1.00 22.13 C ANISOU 229 CB PHE A 197 2713 2704 2992 74 -834 -76 C ATOM 230 CG PHE A 197 -7.137 21.071 -21.894 1.00 29.95 C ANISOU 230 CG PHE A 197 3769 3697 3915 86 -875 -95 C ATOM 231 CD1 PHE A 197 -6.381 21.084 -23.057 1.00 33.90 C ANISOU 231 CD1 PHE A 197 4312 4208 4362 136 -825 -168 C ATOM 232 CD2 PHE A 197 -8.465 20.703 -21.969 1.00 28.88 C ANISOU 232 CD2 PHE A 197 3652 3552 3768 47 -964 -39 C ATOM 233 CE1 PHE A 197 -6.945 20.750 -24.279 1.00 36.12 C ANISOU 233 CE1 PHE A 197 4663 4489 4573 147 -865 -187 C ATOM 234 CE2 PHE A 197 -9.037 20.355 -23.195 1.00 33.26 C ANISOU 234 CE2 PHE A 197 4271 4104 4260 56 -1012 -56 C ATOM 235 CZ PHE A 197 -8.271 20.379 -24.346 1.00 28.80 C ANISOU 235 CZ PHE A 197 3758 3548 3637 107 -964 -131 C ATOM 236 N ALA A 198 -5.428 21.236 -17.674 1.00 25.33 N ANISOU 236 N ALA A 198 3017 3057 3551 34 -843 -48 N ATOM 237 CA ALA A 198 -4.587 21.899 -16.676 1.00 24.28 C ANISOU 237 CA ALA A 198 2836 2927 3461 31 -781 -40 C ATOM 238 C ALA A 198 -3.565 20.975 -16.016 1.00 26.32 C ANISOU 238 C ALA A 198 3082 3130 3790 44 -829 -94 C ATOM 239 O ALA A 198 -2.545 21.448 -15.524 1.00 26.30 O ANISOU 239 O ALA A 198 3044 3128 3822 57 -773 -113 O ATOM 240 CB ALA A 198 -5.447 22.556 -15.616 1.00 20.96 C ANISOU 240 CB ALA A 198 2388 2523 3050 -20 -775 49 C ATOM 241 N VAL A 199 -3.836 19.673 -15.985 1.00 25.78 N ANISOU 241 N VAL A 199 3041 3009 3745 38 -938 -117 N ATOM 242 CA VAL A 199 -2.894 18.740 -15.362 1.00 25.26 C ANISOU 242 CA VAL A 199 2967 2883 3749 52 -995 -169 C ATOM 243 C VAL A 199 -2.063 17.955 -16.378 1.00 26.93 C ANISOU 243 C VAL A 199 3203 3069 3960 114 -1008 -267 C ATOM 244 O VAL A 199 -1.352 17.009 -16.028 1.00 31.01 O ANISOU 244 O VAL A 199 3718 3528 4536 134 -1071 -319 O ATOM 245 CB VAL A 199 -3.582 17.764 -14.387 1.00 24.37 C ANISOU 245 CB VAL A 199 2866 2717 3677 0 -1115 -128 C ATOM 246 CG1 VAL A 199 -4.315 18.542 -13.302 1.00 25.91 C ANISOU 246 CG1 VAL A 199 3034 2939 3873 -59 -1091 -34 C ATOM 247 CG2 VAL A 199 -4.527 16.823 -15.133 1.00 28.77 C ANISOU 247 CG2 VAL A 199 3473 3254 4205 -9 -1206 -131 C ATOM 248 N ASP A 200 -2.132 18.376 -17.628 1.00 27.79 N ANISOU 248 N ASP A 200 3336 3220 4003 148 -947 -294 N ATOM 249 CA ASP A 200 -1.381 17.751 -18.705 1.00 30.42 C ANISOU 249 CA ASP A 200 3698 3539 4323 211 -941 -390 C ATOM 250 C ASP A 200 -0.333 18.761 -19.142 1.00 33.43 C ANISOU 250 C ASP A 200 4043 3970 4690 250 -808 -422 C ATOM 251 O ASP A 200 -0.623 19.953 -19.211 1.00 31.57 O ANISOU 251 O ASP A 200 3792 3790 4414 229 -726 -369 O ATOM 252 CB ASP A 200 -2.331 17.430 -19.861 1.00 34.04 C ANISOU 252 CB ASP A 200 4223 4007 4704 214 -977 -393 C ATOM 253 CG ASP A 200 -1.620 16.833 -21.066 1.00 39.87 C ANISOU 253 CG ASP A 200 5003 4733 5412 281 -964 -494 C ATOM 254 OD1 ASP A 200 -1.344 15.617 -21.059 1.00 38.75 O ANISOU 254 OD1 ASP A 200 4888 4529 5307 305 -1052 -551 O ATOM 255 OD2 ASP A 200 -1.363 17.581 -22.033 1.00 37.04 O ANISOU 255 OD2 ASP A 200 4656 4427 4990 310 -867 -514 O ATOM 256 N LYS A 201 0.880 18.305 -19.428 1.00 32.70 N ANISOU 256 N LYS A 201 3934 3858 4632 306 -786 -507 N ATOM 257 CA LYS A 201 1.955 19.238 -19.757 1.00 37.59 C ANISOU 257 CA LYS A 201 4508 4524 5249 338 -658 -535 C ATOM 258 C LYS A 201 1.587 20.098 -20.961 1.00 36.68 C ANISOU 258 C LYS A 201 4426 4474 5035 346 -569 -527 C ATOM 259 O LYS A 201 1.647 21.327 -20.903 1.00 37.56 O ANISOU 259 O LYS A 201 4511 4638 5124 327 -479 -480 O ATOM 260 CB LYS A 201 3.265 18.493 -20.021 1.00 41.89 C ANISOU 260 CB LYS A 201 5030 5038 5846 403 -650 -635 C ATOM 261 CG LYS A 201 4.428 19.407 -20.359 1.00 50.26 C ANISOU 261 CG LYS A 201 6035 6149 6912 435 -518 -664 C ATOM 262 CD LYS A 201 5.678 18.611 -20.679 1.00 56.92 C ANISOU 262 CD LYS A 201 6852 6965 7812 505 -509 -765 C ATOM 263 CE LYS A 201 6.726 19.479 -21.369 1.00 59.44 C ANISOU 263 CE LYS A 201 7125 7345 8115 540 -365 -799 C ATOM 264 NZ LYS A 201 7.055 20.698 -20.582 1.00 48.81 N ANISOU 264 NZ LYS A 201 5714 6032 6798 496 -300 -733 N ATOM 265 N THR A 202 1.191 19.444 -22.048 1.00 35.68 N ANISOU 265 N THR A 202 4366 4342 4849 374 -600 -571 N ATOM 266 CA THR A 202 0.869 20.136 -23.288 1.00 34.51 C ANISOU 266 CA THR A 202 4262 4250 4602 384 -525 -570 C ATOM 267 C THR A 202 -0.358 21.027 -23.140 1.00 31.76 C ANISOU 267 C THR A 202 3927 3935 4207 327 -526 -471 C ATOM 268 O THR A 202 -0.374 22.167 -23.612 1.00 34.26 O ANISOU 268 O THR A 202 4241 4307 4470 320 -433 -440 O ATOM 269 CB THR A 202 0.624 19.138 -24.435 1.00 41.45 C ANISOU 269 CB THR A 202 5220 5104 5424 423 -576 -637 C ATOM 270 OG1 THR A 202 1.769 18.287 -24.586 1.00 40.72 O ANISOU 270 OG1 THR A 202 5115 4979 5377 484 -573 -735 O ATOM 271 CG2 THR A 202 0.366 19.878 -25.737 1.00 51.05 C ANISOU 271 CG2 THR A 202 6488 6378 6531 433 -495 -638 C ATOM 272 N GLY A 203 -1.391 20.499 -22.497 1.00 31.22 N ANISOU 272 N GLY A 203 3871 3831 4160 285 -633 -420 N ATOM 273 CA GLY A 203 -2.606 21.257 -22.273 1.00 30.21 C ANISOU 273 CA GLY A 203 3747 3732 4000 233 -641 -327 C ATOM 274 C GLY A 203 -2.364 22.493 -21.419 1.00 33.13 C ANISOU 274 C GLY A 203 4056 4137 4396 207 -560 -268 C ATOM 275 O GLY A 203 -2.845 23.573 -21.751 1.00 32.52 O ANISOU 275 O GLY A 203 3982 4106 4267 192 -500 -217 O ATOM 276 N CYS A 204 -1.618 22.349 -20.323 1.00 33.71 N ANISOU 276 N CYS A 204 4076 4184 4547 204 -563 -275 N ATOM 277 CA CYS A 204 -1.398 23.480 -19.414 1.00 33.18 C ANISOU 277 CA CYS A 204 3957 4141 4507 176 -497 -219 C ATOM 278 C CYS A 204 -0.542 24.533 -20.099 1.00 35.15 C ANISOU 278 C CYS A 204 4192 4440 4722 202 -375 -240 C ATOM 279 O CYS A 204 -0.740 25.731 -19.902 1.00 35.06 O ANISOU 279 O CYS A 204 4165 4465 4690 180 -310 -183 O ATOM 280 CB CYS A 204 -0.747 23.035 -18.100 1.00 29.84 C ANISOU 280 CB CYS A 204 3490 3674 4174 165 -537 -224 C ATOM 281 SG CYS A 204 -1.097 24.132 -16.643 1.00 33.68 S ANISOU 281 SG CYS A 204 3934 4172 4690 110 -510 -131 S ATOM 282 N GLN A 205 0.403 24.073 -20.909 1.00 34.56 N ANISOU 282 N GLN A 205 4125 4365 4643 250 -343 -321 N ATOM 283 CA GLN A 205 1.232 24.957 -21.712 1.00 41.99 C ANISOU 283 CA GLN A 205 5054 5354 5544 275 -224 -346 C ATOM 284 C GLN A 205 0.368 25.809 -22.646 1.00 43.61 C ANISOU 284 C GLN A 205 5309 5608 5654 261 -182 -302 C ATOM 285 O GLN A 205 0.610 27.007 -22.810 1.00 35.99 O ANISOU 285 O GLN A 205 4330 4686 4661 250 -92 -269 O ATOM 286 CB GLN A 205 2.232 24.126 -22.515 1.00 50.97 C ANISOU 286 CB GLN A 205 6199 6483 6686 333 -206 -445 C ATOM 287 CG GLN A 205 3.081 24.904 -23.490 1.00 62.31 C ANISOU 287 CG GLN A 205 7628 7972 8073 360 -80 -477 C ATOM 288 CD GLN A 205 4.134 24.027 -24.145 1.00 76.12 C ANISOU 288 CD GLN A 205 9373 9711 9838 421 -58 -579 C ATOM 289 OE1 GLN A 205 4.824 23.260 -23.470 1.00 82.71 O ANISOU 289 OE1 GLN A 205 10165 10503 10760 443 -100 -621 O ATOM 290 NE2 GLN A 205 4.260 24.133 -25.464 1.00 74.29 N ANISOU 290 NE2 GLN A 205 9189 9516 9521 451 7 -619 N ATOM 291 N PHE A 206 -0.645 25.188 -23.248 1.00 35.94 N ANISOU 291 N PHE A 206 4397 4624 4633 259 -254 -299 N ATOM 292 CA PHE A 206 -1.582 25.907 -24.102 1.00 31.46 C ANISOU 292 CA PHE A 206 3880 4095 3979 244 -235 -253 C ATOM 293 C PHE A 206 -2.356 26.943 -23.289 1.00 32.84 C ANISOU 293 C PHE A 206 4026 4286 4164 198 -227 -159 C ATOM 294 O PHE A 206 -2.452 28.110 -23.679 1.00 29.14 O ANISOU 294 O PHE A 206 3563 3859 3650 189 -154 -120 O ATOM 295 CB PHE A 206 -2.550 24.934 -24.787 1.00 28.70 C ANISOU 295 CB PHE A 206 3597 3721 3588 246 -332 -266 C ATOM 296 CG PHE A 206 -3.795 25.591 -25.316 1.00 26.26 C ANISOU 296 CG PHE A 206 3328 3438 3212 218 -347 -197 C ATOM 297 CD1 PHE A 206 -3.750 26.385 -26.452 1.00 31.30 C ANISOU 297 CD1 PHE A 206 4010 4119 3764 228 -275 -198 C ATOM 298 CD2 PHE A 206 -5.011 25.418 -24.672 1.00 30.85 C ANISOU 298 CD2 PHE A 206 3902 4001 3817 179 -434 -130 C ATOM 299 CE1 PHE A 206 -4.895 26.999 -26.934 1.00 35.40 C ANISOU 299 CE1 PHE A 206 4566 4658 4226 203 -296 -133 C ATOM 300 CE2 PHE A 206 -6.161 26.026 -25.144 1.00 32.23 C ANISOU 300 CE2 PHE A 206 4106 4200 3940 155 -450 -67 C ATOM 301 CZ PHE A 206 -6.102 26.820 -26.279 1.00 35.78 C ANISOU 301 CZ PHE A 206 4600 4688 4307 168 -385 -68 C ATOM 302 N LEU A 207 -2.900 26.513 -22.153 1.00 29.43 N ANISOU 302 N LEU A 207 3566 3821 3794 170 -302 -122 N ATOM 303 CA LEU A 207 -3.683 27.402 -21.298 1.00 31.38 C ANISOU 303 CA LEU A 207 3787 4082 4055 131 -297 -36 C ATOM 304 C LEU A 207 -2.853 28.595 -20.839 1.00 29.75 C ANISOU 304 C LEU A 207 3540 3900 3864 128 -199 -20 C ATOM 305 O LEU A 207 -3.317 29.740 -20.866 1.00 30.74 O ANISOU 305 O LEU A 207 3666 4055 3957 112 -151 38 O ATOM 306 CB LEU A 207 -4.256 26.638 -20.104 1.00 29.59 C ANISOU 306 CB LEU A 207 3537 3815 3892 102 -388 -7 C ATOM 307 CG LEU A 207 -5.381 25.661 -20.450 1.00 32.29 C ANISOU 307 CG LEU A 207 3915 4135 4218 89 -493 4 C ATOM 308 CD1 LEU A 207 -5.835 24.891 -19.224 1.00 36.15 C ANISOU 308 CD1 LEU A 207 4379 4584 4772 55 -577 33 C ATOM 309 CD2 LEU A 207 -6.545 26.390 -21.075 1.00 31.44 C ANISOU 309 CD2 LEU A 207 3832 4063 4051 73 -487 64 C ATOM 310 N GLU A 208 -1.618 28.314 -20.441 1.00 33.71 N ANISOU 310 N GLU A 208 4007 4385 4417 145 -173 -70 N ATOM 311 CA GLU A 208 -0.684 29.324 -19.959 1.00 38.43 C ANISOU 311 CA GLU A 208 4562 4999 5041 141 -88 -61 C ATOM 312 C GLU A 208 -0.534 30.466 -20.954 1.00 39.74 C ANISOU 312 C GLU A 208 4748 5215 5138 147 6 -48 C ATOM 313 O GLU A 208 -0.663 31.639 -20.594 1.00 38.99 O ANISOU 313 O GLU A 208 4642 5139 5035 125 55 7 O ATOM 314 CB GLU A 208 0.681 28.683 -19.725 1.00 50.25 C ANISOU 314 CB GLU A 208 6021 6473 6600 167 -78 -131 C ATOM 315 CG GLU A 208 1.594 29.486 -18.834 1.00 64.60 C ANISOU 315 CG GLU A 208 7785 8289 8471 153 -24 -115 C ATOM 316 CD GLU A 208 1.131 29.469 -17.394 1.00 70.14 C ANISOU 316 CD GLU A 208 8469 8957 9225 117 -84 -64 C ATOM 317 OE1 GLU A 208 1.534 30.371 -16.620 1.00 61.05 O ANISOU 317 OE1 GLU A 208 7290 7807 8101 96 -44 -30 O ATOM 318 OE2 GLU A 208 0.356 28.549 -17.050 1.00 70.32 O ANISOU 318 OE2 GLU A 208 8509 8950 9259 109 -172 -58 O ATOM 319 N LYS A 209 -0.251 30.110 -22.203 1.00 30.39 N ANISOU 319 N LYS A 209 3598 4048 3900 176 30 -100 N ATOM 320 CA LYS A 209 -0.093 31.076 -23.285 1.00 39.26 C ANISOU 320 CA LYS A 209 4752 5218 4947 181 117 -92 C ATOM 321 C LYS A 209 -1.414 31.781 -23.592 1.00 33.59 C ANISOU 321 C LYS A 209 4076 4517 4169 158 98 -21 C ATOM 322 O LYS A 209 -1.461 32.999 -23.767 1.00 30.23 O ANISOU 322 O LYS A 209 3656 4120 3710 143 160 25 O ATOM 323 CB LYS A 209 0.416 30.373 -24.543 1.00 43.79 C ANISOU 323 CB LYS A 209 5363 5803 5471 219 138 -167 C ATOM 324 CG LYS A 209 1.252 31.247 -25.456 1.00 57.44 C ANISOU 324 CG LYS A 209 7099 7579 7147 228 252 -182 C ATOM 325 CD LYS A 209 2.551 31.654 -24.771 1.00 68.47 C ANISOU 325 CD LYS A 209 8422 8980 8615 227 320 -197 C ATOM 326 CE LYS A 209 3.622 32.047 -25.777 1.00 74.04 C ANISOU 326 CE LYS A 209 9126 9727 9279 246 429 -240 C ATOM 327 NZ LYS A 209 3.152 33.103 -26.715 1.00 78.93 N ANISOU 327 NZ LYS A 209 9801 10389 9801 226 486 -194 N ATOM 328 N ALA A 210 -2.489 31.009 -23.656 1.00 25.21 N ANISOU 328 N ALA A 210 3044 3436 3098 154 7 -10 N ATOM 329 CA ALA A 210 -3.802 31.579 -23.941 1.00 27.85 C ANISOU 329 CA ALA A 210 3413 3784 3386 134 -22 58 C ATOM 330 C ALA A 210 -4.255 32.587 -22.884 1.00 23.03 C ANISOU 330 C ALA A 210 2763 3176 2809 106 -7 132 C ATOM 331 O ALA A 210 -4.898 33.581 -23.214 1.00 29.70 O ANISOU 331 O ALA A 210 3629 4045 3613 96 18 186 O ATOM 332 CB ALA A 210 -4.830 30.476 -24.109 1.00 29.04 C ANISOU 332 CB ALA A 210 3592 3910 3533 131 -130 57 C ATOM 333 N VAL A 211 -3.918 32.355 -21.616 1.00 23.79 N ANISOU 333 N VAL A 211 2810 3247 2981 96 -22 135 N ATOM 334 CA VAL A 211 -4.401 33.259 -20.563 1.00 26.88 C ANISOU 334 CA VAL A 211 3173 3638 3402 71 -10 202 C ATOM 335 C VAL A 211 -3.562 34.531 -20.415 1.00 27.71 C ANISOU 335 C VAL A 211 3263 3761 3504 68 83 215 C ATOM 336 O VAL A 211 -3.950 35.454 -19.709 1.00 29.12 O ANISOU 336 O VAL A 211 3430 3941 3694 52 102 270 O ATOM 337 CB VAL A 211 -4.558 32.566 -19.179 1.00 31.66 C ANISOU 337 CB VAL A 211 3740 4207 4080 54 -70 211 C ATOM 338 CG1 VAL A 211 -5.499 31.370 -19.284 1.00 38.26 C ANISOU 338 CG1 VAL A 211 4591 5025 4920 49 -167 209 C ATOM 339 CG2 VAL A 211 -3.210 32.162 -18.612 1.00 35.98 C ANISOU 339 CG2 VAL A 211 4256 4733 4683 61 -52 159 C ATOM 340 N LYS A 212 -2.417 34.581 -21.086 1.00 24.84 N ANISOU 340 N LYS A 212 2901 3411 3126 84 142 165 N ATOM 341 CA LYS A 212 -1.583 35.779 -21.068 1.00 26.81 C ANISOU 341 CA LYS A 212 3137 3678 3370 76 230 179 C ATOM 342 C LYS A 212 -2.020 36.786 -22.129 1.00 29.46 C ANISOU 342 C LYS A 212 3520 4048 3626 74 276 214 C ATOM 343 O LYS A 212 -1.524 37.905 -22.176 1.00 36.67 O ANISOU 343 O LYS A 212 4431 4977 4527 63 344 238 O ATOM 344 CB LYS A 212 -0.116 35.406 -21.303 1.00 40.40 C ANISOU 344 CB LYS A 212 4831 5402 5118 91 277 113 C ATOM 345 CG LYS A 212 0.559 34.780 -20.095 1.00 51.92 C ANISOU 345 CG LYS A 212 6237 6825 6667 88 245 88 C ATOM 346 CD LYS A 212 2.046 34.558 -20.348 1.00 64.03 C ANISOU 346 CD LYS A 212 7733 8362 8232 105 298 27 C ATOM 347 CE LYS A 212 2.737 35.857 -20.744 1.00 70.53 C ANISOU 347 CE LYS A 212 8549 9218 9030 91 395 49 C ATOM 348 NZ LYS A 212 4.217 35.707 -20.797 1.00 73.04 N ANISOU 348 NZ LYS A 212 8816 9541 9395 102 448 -3 N ATOM 349 N GLY A 213 -2.935 36.377 -22.994 1.00 29.62 N ANISOU 349 N GLY A 213 3585 4078 3593 83 234 217 N ATOM 350 CA GLY A 213 -3.372 37.221 -24.094 1.00 28.98 C ANISOU 350 CA GLY A 213 3556 4025 3431 81 266 247 C ATOM 351 C GLY A 213 -4.552 38.092 -23.708 1.00 28.67 C ANISOU 351 C GLY A 213 3523 3983 3386 67 241 324 C ATOM 352 O GLY A 213 -4.876 38.240 -22.530 1.00 27.54 O ANISOU 352 O GLY A 213 3343 3822 3301 58 220 355 O ATOM 353 N SER A 214 -5.204 38.677 -24.700 1.00 25.61 N ANISOU 353 N SER A 214 3187 3614 2929 67 244 356 N ATOM 354 CA SER A 214 -6.403 39.439 -24.420 1.00 24.46 C ANISOU 354 CA SER A 214 3047 3465 2781 60 213 426 C ATOM 355 C SER A 214 -7.454 38.436 -24.006 1.00 30.45 C ANISOU 355 C SER A 214 3789 4208 3573 63 122 434 C ATOM 356 O SER A 214 -7.578 37.372 -24.610 1.00 30.50 O ANISOU 356 O SER A 214 3816 4212 3562 69 74 395 O ATOM 357 CB SER A 214 -6.860 40.207 -25.659 1.00 28.91 C ANISOU 357 CB SER A 214 3673 4049 3264 60 226 457 C ATOM 358 OG SER A 214 -5.807 41.013 -26.138 1.00 31.05 O ANISOU 358 OG SER A 214 3962 4336 3498 53 311 446 O ATOM 359 N LEU A 215 -8.186 38.759 -22.951 1.00 22.27 N ANISOU 359 N LEU A 215 2716 3160 2587 56 99 481 N ATOM 360 CA LEU A 215 -9.295 37.927 -22.515 1.00 19.67 C ANISOU 360 CA LEU A 215 2365 2819 2290 53 17 501 C ATOM 361 C LEU A 215 -10.541 38.793 -22.458 1.00 24.14 C ANISOU 361 C LEU A 215 2930 3393 2851 54 0 572 C ATOM 362 O LEU A 215 -10.482 39.927 -21.977 1.00 21.13 O ANISOU 362 O LEU A 215 2539 3012 2476 56 50 607 O ATOM 363 CB LEU A 215 -9.018 37.377 -21.117 1.00 19.19 C ANISOU 363 CB LEU A 215 2251 2737 2302 44 6 491 C ATOM 364 CG LEU A 215 -7.847 36.416 -20.903 1.00 20.16 C ANISOU 364 CG LEU A 215 2363 2845 2452 44 8 422 C ATOM 365 CD1 LEU A 215 -7.803 36.031 -19.440 1.00 19.99 C ANISOU 365 CD1 LEU A 215 2295 2799 2501 31 -12 429 C ATOM 366 CD2 LEU A 215 -8.031 35.174 -21.738 1.00 23.18 C ANISOU 366 CD2 LEU A 215 2772 3223 2814 51 -54 381 C ATOM 367 N THR A 216 -11.666 38.251 -22.926 1.00 19.90 N ANISOU 367 N THR A 216 2400 2857 2304 53 -75 594 N ATOM 368 CA THR A 216 -12.944 38.925 -22.785 1.00 26.42 C ANISOU 368 CA THR A 216 3211 3688 3140 56 -101 663 C ATOM 369 C THR A 216 -13.440 38.685 -21.377 1.00 23.99 C ANISOU 369 C THR A 216 2840 3372 2903 48 -115 688 C ATOM 370 O THR A 216 -12.956 37.782 -20.686 1.00 21.93 O ANISOU 370 O THR A 216 2556 3098 2678 37 -127 654 O ATOM 371 CB THR A 216 -13.996 38.341 -23.744 1.00 33.01 C ANISOU 371 CB THR A 216 4068 4526 3948 54 -185 680 C ATOM 372 OG1 THR A 216 -14.248 36.977 -23.385 1.00 28.11 O ANISOU 372 OG1 THR A 216 3423 3893 3363 40 -252 658 O ATOM 373 CG2 THR A 216 -13.510 38.405 -25.186 1.00 33.94 C ANISOU 373 CG2 THR A 216 4258 4650 3985 59 -179 649 C ATOM 374 N SER A 217 -14.402 39.495 -20.950 1.00 19.44 N ANISOU 374 N SER A 217 2238 2801 2346 56 -113 748 N ATOM 375 CA SER A 217 -14.988 39.362 -19.619 1.00 19.12 C ANISOU 375 CA SER A 217 2140 2757 2367 50 -118 778 C ATOM 376 C SER A 217 -15.476 37.950 -19.316 1.00 20.06 C ANISOU 376 C SER A 217 2229 2871 2520 29 -192 770 C ATOM 377 O SER A 217 -15.227 37.412 -18.230 1.00 19.89 O ANISOU 377 O SER A 217 2177 2840 2541 14 -189 760 O ATOM 378 CB SER A 217 -16.152 40.355 -19.445 1.00 21.29 C ANISOU 378 CB SER A 217 2391 3043 2654 68 -113 843 C ATOM 379 OG SER A 217 -16.744 40.169 -18.173 1.00 27.62 O ANISOU 379 OG SER A 217 3137 3845 3512 62 -113 870 O ATOM 380 N TYR A 218 -16.158 37.326 -20.271 1.00 22.80 N ANISOU 380 N TYR A 218 2590 3222 2849 24 -263 776 N ATOM 381 CA TYR A 218 -16.685 35.991 -19.994 1.00 19.72 C ANISOU 381 CA TYR A 218 2174 2824 2494 -1 -341 774 C ATOM 382 C TYR A 218 -15.558 34.955 -19.894 1.00 21.95 C ANISOU 382 C TYR A 218 2478 3086 2776 -12 -349 706 C ATOM 383 O TYR A 218 -15.626 34.045 -19.082 1.00 19.68 O ANISOU 383 O TYR A 218 2161 2784 2532 -33 -385 700 O ATOM 384 CB TYR A 218 -17.723 35.559 -21.027 1.00 23.47 C ANISOU 384 CB TYR A 218 2661 3304 2952 -6 -425 799 C ATOM 385 CG TYR A 218 -18.456 34.305 -20.601 1.00 23.52 C ANISOU 385 CG TYR A 218 2631 3302 3004 -37 -508 812 C ATOM 386 CD1 TYR A 218 -19.136 34.254 -19.390 1.00 27.03 C ANISOU 386 CD1 TYR A 218 3008 3753 3508 -52 -505 857 C ATOM 387 CD2 TYR A 218 -18.470 33.176 -21.410 1.00 28.41 C ANISOU 387 CD2 TYR A 218 3286 3904 3604 -51 -589 781 C ATOM 388 CE1 TYR A 218 -19.815 33.098 -18.993 1.00 29.32 C ANISOU 388 CE1 TYR A 218 3264 4036 3840 -86 -582 874 C ATOM 389 CE2 TYR A 218 -19.137 32.026 -21.024 1.00 26.54 C ANISOU 389 CE2 TYR A 218 3018 3655 3410 -83 -672 796 C ATOM 390 CZ TYR A 218 -19.807 31.993 -19.819 1.00 30.72 C ANISOU 390 CZ TYR A 218 3478 4194 4001 -103 -668 845 C ATOM 391 OH TYR A 218 -20.473 30.844 -19.447 1.00 36.99 O ANISOU 391 OH TYR A 218 4241 4976 4836 -141 -750 864 O ATOM 392 N GLN A 219 -14.511 35.093 -20.702 1.00 21.02 N ANISOU 392 N GLN A 219 2410 2965 2612 3 -315 654 N ATOM 393 CA GLN A 219 -13.397 34.156 -20.575 1.00 20.75 C ANISOU 393 CA GLN A 219 2389 2911 2585 -1 -317 587 C ATOM 394 C GLN A 219 -12.802 34.221 -19.180 1.00 19.34 C ANISOU 394 C GLN A 219 2171 2721 2457 -10 -277 583 C ATOM 395 O GLN A 219 -12.518 33.191 -18.566 1.00 18.96 O ANISOU 395 O GLN A 219 2108 2651 2446 -25 -316 557 O ATOM 396 CB GLN A 219 -12.329 34.416 -21.636 1.00 20.24 C ANISOU 396 CB GLN A 219 2376 2850 2462 18 -271 533 C ATOM 397 CG GLN A 219 -12.776 34.007 -23.034 1.00 23.30 C ANISOU 397 CG GLN A 219 2818 3243 2794 24 -324 522 C ATOM 398 CD GLN A 219 -11.810 34.470 -24.088 1.00 23.55 C ANISOU 398 CD GLN A 219 2904 3286 2759 42 -264 479 C ATOM 399 OE1 GLN A 219 -11.216 35.534 -23.966 1.00 21.04 O ANISOU 399 OE1 GLN A 219 2584 2982 2430 49 -183 487 O ATOM 400 NE2 GLN A 219 -11.633 33.667 -25.121 1.00 24.30 N ANISOU 400 NE2 GLN A 219 3050 3375 2809 49 -302 432 N ATOM 401 N LYS A 220 -12.629 35.436 -18.673 1.00 20.35 N ANISOU 401 N LYS A 220 2287 2859 2586 -1 -205 610 N ATOM 402 CA LYS A 220 -12.136 35.615 -17.309 1.00 18.31 C ANISOU 402 CA LYS A 220 1998 2588 2372 -11 -169 612 C ATOM 403 C LYS A 220 -13.097 34.989 -16.311 1.00 19.60 C ANISOU 403 C LYS A 220 2121 2746 2581 -33 -218 650 C ATOM 404 O LYS A 220 -12.690 34.298 -15.371 1.00 18.02 O ANISOU 404 O LYS A 220 1905 2525 2418 -52 -234 633 O ATOM 405 CB LYS A 220 -11.996 37.106 -16.994 1.00 18.10 C ANISOU 405 CB LYS A 220 1972 2571 2334 3 -90 642 C ATOM 406 CG LYS A 220 -10.874 37.804 -17.750 1.00 18.16 C ANISOU 406 CG LYS A 220 2015 2583 2303 18 -30 607 C ATOM 407 CD LYS A 220 -10.763 39.284 -17.336 1.00 24.58 C ANISOU 407 CD LYS A 220 2830 3398 3109 27 39 641 C ATOM 408 CE LYS A 220 -10.077 40.094 -18.428 1.00 37.31 C ANISOU 408 CE LYS A 220 4484 5022 4670 38 88 627 C ATOM 409 NZ LYS A 220 -10.107 41.547 -18.124 1.00 41.89 N ANISOU 409 NZ LYS A 220 5073 5601 5242 46 144 666 N ATOM 410 N PHE A 221 -14.379 35.245 -16.516 1.00 18.43 N ANISOU 410 N PHE A 221 1955 2617 2431 -33 -243 704 N ATOM 411 CA PHE A 221 -15.405 34.738 -15.614 1.00 19.17 C ANISOU 411 CA PHE A 221 2004 2713 2568 -56 -283 749 C ATOM 412 C PHE A 221 -15.322 33.216 -15.512 1.00 20.51 C ANISOU 412 C PHE A 221 2171 2861 2760 -85 -362 722 C ATOM 413 O PHE A 221 -15.368 32.643 -14.415 1.00 19.90 O ANISOU 413 O PHE A 221 2070 2771 2722 -111 -377 731 O ATOM 414 CB PHE A 221 -16.784 35.160 -16.120 1.00 18.79 C ANISOU 414 CB PHE A 221 1934 2690 2517 -49 -306 807 C ATOM 415 CG PHE A 221 -17.908 34.856 -15.162 1.00 21.24 C ANISOU 415 CG PHE A 221 2187 3011 2873 -71 -330 862 C ATOM 416 CD1 PHE A 221 -18.196 35.718 -14.123 1.00 21.97 C ANISOU 416 CD1 PHE A 221 2250 3115 2984 -62 -266 896 C ATOM 417 CD2 PHE A 221 -18.688 33.726 -15.322 1.00 25.55 C ANISOU 417 CD2 PHE A 221 2711 3556 3441 -100 -415 879 C ATOM 418 CE1 PHE A 221 -19.252 35.464 -13.258 1.00 26.81 C ANISOU 418 CE1 PHE A 221 2808 3743 3635 -80 -278 947 C ATOM 419 CE2 PHE A 221 -19.733 33.451 -14.446 1.00 31.00 C ANISOU 419 CE2 PHE A 221 3344 4261 4176 -124 -432 934 C ATOM 420 CZ PHE A 221 -20.019 34.328 -13.418 1.00 25.37 C ANISOU 420 CZ PHE A 221 2598 3564 3479 -113 -360 968 C ATOM 421 N GLN A 222 -15.199 32.556 -16.658 1.00 18.89 N ANISOU 421 N GLN A 222 1999 2649 2529 -81 -413 688 N ATOM 422 CA GLN A 222 -15.092 31.106 -16.683 1.00 19.86 C ANISOU 422 CA GLN A 222 2130 2746 2672 -104 -495 657 C ATOM 423 C GLN A 222 -13.830 30.617 -15.995 1.00 19.51 C ANISOU 423 C GLN A 222 2094 2672 2648 -107 -478 603 C ATOM 424 O GLN A 222 -13.859 29.641 -15.251 1.00 19.20 O ANISOU 424 O GLN A 222 2041 2608 2646 -135 -531 601 O ATOM 425 CB GLN A 222 -15.114 30.588 -18.123 1.00 19.54 C ANISOU 425 CB GLN A 222 2134 2700 2590 -93 -547 624 C ATOM 426 CG GLN A 222 -16.463 30.719 -18.830 1.00 21.08 C ANISOU 426 CG GLN A 222 2322 2914 2772 -99 -598 678 C ATOM 427 CD GLN A 222 -16.357 30.337 -20.290 1.00 24.58 C ANISOU 427 CD GLN A 222 2824 3350 3164 -86 -643 641 C ATOM 428 OE1 GLN A 222 -15.618 30.962 -21.040 1.00 21.14 O ANISOU 428 OE1 GLN A 222 2430 2923 2680 -58 -589 606 O ATOM 429 NE2 GLN A 222 -17.086 29.297 -20.698 1.00 22.08 N ANISOU 429 NE2 GLN A 222 2516 3018 2855 -108 -744 648 N ATOM 430 N LEU A 223 -12.709 31.268 -16.271 1.00 21.42 N ANISOU 430 N LEU A 223 2358 2914 2867 -81 -411 562 N ATOM 431 CA LEU A 223 -11.460 30.922 -15.602 1.00 18.38 C ANISOU 431 CA LEU A 223 1974 2502 2507 -81 -392 513 C ATOM 432 C LEU A 223 -11.568 31.104 -14.088 1.00 20.54 C ANISOU 432 C LEU A 223 2216 2767 2822 -105 -376 548 C ATOM 433 O LEU A 223 -11.082 30.268 -13.319 1.00 19.96 O ANISOU 433 O LEU A 223 2137 2662 2784 -124 -412 526 O ATOM 434 CB LEU A 223 -10.307 31.776 -16.142 1.00 20.74 C ANISOU 434 CB LEU A 223 2294 2809 2777 -51 -313 473 C ATOM 435 CG LEU A 223 -9.751 31.362 -17.500 1.00 23.56 C ANISOU 435 CG LEU A 223 2688 3167 3095 -28 -322 416 C ATOM 436 CD1 LEU A 223 -9.060 32.547 -18.168 1.00 26.14 C ANISOU 436 CD1 LEU A 223 3033 3518 3380 -4 -234 405 C ATOM 437 CD2 LEU A 223 -8.789 30.183 -17.334 1.00 20.78 C ANISOU 437 CD2 LEU A 223 2340 2780 2774 -26 -360 350 C ATOM 438 N PHE A 224 -12.202 32.189 -13.646 1.00 18.27 N ANISOU 438 N PHE A 224 1909 2503 2528 -103 -324 601 N ATOM 439 CA PHE A 224 -12.352 32.410 -12.207 1.00 18.54 C ANISOU 439 CA PHE A 224 1921 2531 2593 -124 -304 635 C ATOM 440 C PHE A 224 -13.172 31.281 -11.585 1.00 19.45 C ANISOU 440 C PHE A 224 2015 2636 2740 -162 -378 662 C ATOM 441 O PHE A 224 -12.833 30.748 -10.520 1.00 23.71 O ANISOU 441 O PHE A 224 2550 3149 3308 -188 -396 659 O ATOM 442 CB PHE A 224 -13.046 33.744 -11.908 1.00 19.56 C ANISOU 442 CB PHE A 224 2036 2688 2708 -111 -238 687 C ATOM 443 CG PHE A 224 -12.317 34.949 -12.411 1.00 18.25 C ANISOU 443 CG PHE A 224 1892 2529 2511 -80 -166 670 C ATOM 444 CD1 PHE A 224 -10.938 34.943 -12.551 1.00 17.75 C ANISOU 444 CD1 PHE A 224 1851 2447 2447 -73 -143 616 C ATOM 445 CD2 PHE A 224 -13.019 36.112 -12.716 1.00 21.37 C ANISOU 445 CD2 PHE A 224 2286 2951 2884 -58 -121 711 C ATOM 446 CE1 PHE A 224 -10.269 36.063 -13.002 1.00 19.96 C ANISOU 446 CE1 PHE A 224 2149 2734 2700 -50 -77 605 C ATOM 447 CE2 PHE A 224 -12.356 37.243 -13.162 1.00 17.28 C ANISOU 447 CE2 PHE A 224 1792 2436 2337 -34 -58 700 C ATOM 448 CZ PHE A 224 -10.981 37.218 -13.310 1.00 18.27 C ANISOU 448 CZ PHE A 224 1939 2543 2458 -33 -35 648 C ATOM 449 N GLU A 225 -14.255 30.908 -12.249 1.00 20.49 N ANISOU 449 N GLU A 225 2135 2785 2866 -168 -426 692 N ATOM 450 CA GLU A 225 -15.111 29.835 -11.736 1.00 20.77 C ANISOU 450 CA GLU A 225 2147 2813 2933 -209 -501 725 C ATOM 451 C GLU A 225 -14.425 28.467 -11.756 1.00 27.15 C ANISOU 451 C GLU A 225 2978 3578 3759 -229 -578 676 C ATOM 452 O GLU A 225 -14.572 27.667 -10.828 1.00 24.99 O ANISOU 452 O GLU A 225 2695 3283 3518 -267 -622 691 O ATOM 453 CB GLU A 225 -16.421 29.773 -12.526 1.00 31.40 C ANISOU 453 CB GLU A 225 3473 4187 4273 -213 -541 769 C ATOM 454 CG GLU A 225 -17.280 31.032 -12.416 1.00 46.45 C ANISOU 454 CG GLU A 225 5347 6133 6171 -194 -476 825 C ATOM 455 CD GLU A 225 -17.885 31.231 -11.031 1.00 64.49 C ANISOU 455 CD GLU A 225 7591 8430 8483 -218 -444 876 C ATOM 456 OE1 GLU A 225 -17.693 30.352 -10.163 1.00 67.86 O ANISOU 456 OE1 GLU A 225 8016 8834 8934 -255 -477 874 O ATOM 457 OE2 GLU A 225 -18.558 32.266 -10.813 1.00 66.61 O ANISOU 457 OE2 GLU A 225 7831 8728 8748 -198 -385 919 O ATOM 458 N GLN A 226 -13.676 28.187 -12.814 1.00 21.68 N ANISOU 458 N GLN A 226 2320 2872 3047 -202 -594 616 N ATOM 459 CA GLN A 226 -13.153 26.839 -12.992 1.00 19.86 C ANISOU 459 CA GLN A 226 2111 2599 2834 -213 -675 567 C ATOM 460 C GLN A 226 -11.791 26.605 -12.345 1.00 21.73 C ANISOU 460 C GLN A 226 2360 2800 3094 -207 -659 515 C ATOM 461 O GLN A 226 -11.449 25.469 -12.043 1.00 22.17 O ANISOU 461 O GLN A 226 2427 2815 3179 -224 -730 487 O ATOM 462 CB GLN A 226 -13.085 26.480 -14.479 1.00 22.26 C ANISOU 462 CB GLN A 226 2449 2902 3105 -187 -710 525 C ATOM 463 CG GLN A 226 -14.447 26.487 -15.166 1.00 23.82 C ANISOU 463 CG GLN A 226 2640 3124 3286 -199 -751 576 C ATOM 464 CD GLN A 226 -14.352 26.046 -16.605 1.00 24.91 C ANISOU 464 CD GLN A 226 2823 3255 3386 -176 -795 532 C ATOM 465 OE1 GLN A 226 -13.559 25.165 -16.936 1.00 27.23 O ANISOU 465 OE1 GLN A 226 3151 3513 3680 -166 -835 468 O ATOM 466 NE2 GLN A 226 -15.154 26.668 -17.477 1.00 25.51 N ANISOU 466 NE2 GLN A 226 2903 3361 3427 -166 -789 564 N ATOM 467 N VAL A 227 -11.018 27.668 -12.135 1.00 19.01 N ANISOU 467 N VAL A 227 2014 2469 2739 -182 -572 502 N ATOM 468 CA VAL A 227 -9.657 27.514 -11.579 1.00 20.89 C ANISOU 468 CA VAL A 227 2259 2674 3004 -174 -558 451 C ATOM 469 C VAL A 227 -9.558 27.920 -10.111 1.00 23.77 C ANISOU 469 C VAL A 227 2609 3029 3393 -201 -531 486 C ATOM 470 O VAL A 227 -8.892 27.252 -9.314 1.00 23.69 O ANISOU 470 O VAL A 227 2604 2979 3419 -218 -569 465 O ATOM 471 CB VAL A 227 -8.609 28.292 -12.423 1.00 21.94 C ANISOU 471 CB VAL A 227 2404 2820 3113 -131 -486 402 C ATOM 472 CG1 VAL A 227 -7.233 28.263 -11.748 1.00 21.51 C ANISOU 472 CG1 VAL A 227 2345 2734 3094 -125 -467 359 C ATOM 473 CG2 VAL A 227 -8.533 27.721 -13.824 1.00 21.06 C ANISOU 473 CG2 VAL A 227 2316 2711 2974 -105 -516 356 C ATOM 474 N ILE A 228 -10.231 29.003 -9.740 1.00 19.99 N ANISOU 474 N ILE A 228 2117 2583 2894 -203 -469 540 N ATOM 475 CA ILE A 228 -10.171 29.474 -8.361 1.00 19.34 C ANISOU 475 CA ILE A 228 2029 2493 2826 -226 -437 572 C ATOM 476 C ILE A 228 -11.549 29.630 -7.725 1.00 24.07 C ANISOU 476 C ILE A 228 2608 3118 3420 -253 -435 643 C ATOM 477 O ILE A 228 -11.709 30.348 -6.743 1.00 31.54 O ANISOU 477 O ILE A 228 3551 4070 4361 -262 -385 676 O ATOM 478 CB ILE A 228 -9.402 30.802 -8.251 1.00 27.21 C ANISOU 478 CB ILE A 228 3032 3498 3807 -199 -349 561 C ATOM 479 CG1 ILE A 228 -10.069 31.897 -9.095 1.00 22.73 C ANISOU 479 CG1 ILE A 228 2460 2976 3201 -171 -289 588 C ATOM 480 CG2 ILE A 228 -7.965 30.594 -8.690 1.00 20.83 C ANISOU 480 CG2 ILE A 228 2236 2665 3015 -178 -349 494 C ATOM 481 CD1 ILE A 228 -9.457 33.291 -8.856 1.00 21.59 C ANISOU 481 CD1 ILE A 228 2324 2838 3041 -150 -204 589 C ATOM 482 N GLY A 229 -12.531 28.933 -8.278 1.00 22.85 N ANISOU 482 N GLY A 229 2440 2977 3266 -267 -490 666 N ATOM 483 CA GLY A 229 -13.916 29.121 -7.887 1.00 23.74 C ANISOU 483 CA GLY A 229 2522 3122 3376 -288 -484 735 C ATOM 484 C GLY A 229 -14.435 28.049 -6.946 1.00 26.40 C ANISOU 484 C GLY A 229 2849 3441 3740 -342 -548 768 C ATOM 485 O GLY A 229 -15.340 28.305 -6.157 1.00 25.26 O ANISOU 485 O GLY A 229 2680 3320 3597 -366 -523 826 O ATOM 486 N ARG A 230 -13.880 26.844 -7.048 1.00 22.44 N ANISOU 486 N ARG A 230 2023 3190 3315 -124 -219 820 N ATOM 487 CA ARG A 230 -14.309 25.721 -6.216 1.00 26.99 C ANISOU 487 CA ARG A 230 2538 3809 3907 -229 -278 936 C ATOM 488 C ARG A 230 -13.126 25.184 -5.437 1.00 27.66 C ANISOU 488 C ARG A 230 2680 3832 3998 -263 -305 929 C ATOM 489 O ARG A 230 -12.070 24.915 -6.015 1.00 23.11 O ANISOU 489 O ARG A 230 2187 3135 3460 -242 -349 853 O ATOM 490 CB ARG A 230 -14.875 24.589 -7.074 1.00 37.20 C ANISOU 490 CB ARG A 230 3819 5038 5277 -301 -399 993 C ATOM 491 CG ARG A 230 -16.378 24.653 -7.334 1.00 53.74 C ANISOU 491 CG ARG A 230 5817 7240 7364 -326 -396 1070 C ATOM 492 CD ARG A 230 -16.731 25.603 -8.469 1.00 66.84 C ANISOU 492 CD ARG A 230 7490 8880 9024 -229 -347 984 C ATOM 493 NE ARG A 230 -16.191 25.221 -9.778 1.00 73.42 N ANISOU 493 NE ARG A 230 8406 9559 9932 -212 -420 918 N ATOM 494 CZ ARG A 230 -15.727 24.017 -10.107 1.00 74.29 C ANISOU 494 CZ ARG A 230 8560 9559 10109 -271 -540 940 C ATOM 495 NH1 ARG A 230 -15.729 23.023 -9.230 1.00 68.49 N ANISOU 495 NH1 ARG A 230 7806 8835 9383 -366 -613 1034 N ATOM 496 NH2 ARG A 230 -15.264 23.807 -11.332 1.00 75.61 N ANISOU 496 NH2 ARG A 230 8794 9608 10329 -232 -598 864 N ATOM 497 N LYS A 231 -13.310 24.995 -4.137 1.00 24.96 N ANISOU 497 N LYS A 231 2288 3582 3615 -317 -282 1007 N ATOM 498 CA LYS A 231 -12.204 24.605 -3.264 1.00 23.35 C ANISOU 498 CA LYS A 231 2139 3324 3409 -346 -297 998 C ATOM 499 C LYS A 231 -11.488 23.336 -3.701 1.00 28.38 C ANISOU 499 C LYS A 231 2845 3814 4123 -405 -436 992 C ATOM 500 O LYS A 231 -10.261 23.306 -3.743 1.00 26.15 O ANISOU 500 O LYS A 231 2642 3441 3852 -367 -446 908 O ATOM 501 CB LYS A 231 -12.673 24.428 -1.826 1.00 30.53 C ANISOU 501 CB LYS A 231 2975 4360 4265 -415 -269 1101 C ATOM 502 CG LYS A 231 -11.504 24.190 -0.863 1.00 34.79 C ANISOU 502 CG LYS A 231 3577 4844 4799 -434 -270 1084 C ATOM 503 CD LYS A 231 -11.967 23.554 0.433 1.00 44.23 C ANISOU 503 CD LYS A 231 4705 6138 5961 -547 -293 1208 C ATOM 504 CE LYS A 231 -12.913 24.461 1.201 1.00 52.35 C ANISOU 504 CE LYS A 231 5625 7371 6894 -512 -177 1251 C ATOM 505 NZ LYS A 231 -12.213 25.278 2.232 1.00 58.57 N ANISOU 505 NZ LYS A 231 6439 8194 7622 -443 -78 1206 N ATOM 506 N ASP A 232 -12.234 22.273 -3.995 1.00 30.48 N ANISOU 506 N ASP A 232 3082 4062 4436 -496 -555 1080 N ATOM 507 CA ASP A 232 -11.564 21.019 -4.344 1.00 33.81 C ANISOU 507 CA ASP A 232 3582 4337 4926 -543 -716 1070 C ATOM 508 C ASP A 232 -10.725 21.124 -5.624 1.00 29.56 C ANISOU 508 C ASP A 232 3121 3683 4427 -443 -743 934 C ATOM 509 O ASP A 232 -9.557 20.726 -5.631 1.00 26.64 O ANISOU 509 O ASP A 232 2825 3223 4073 -414 -797 856 O ATOM 510 CB ASP A 232 -12.509 19.803 -4.343 1.00 34.93 C ANISOU 510 CB ASP A 232 3694 4470 5107 -673 -868 1203 C ATOM 511 CG ASP A 232 -13.768 20.016 -5.161 1.00 41.64 C ANISOU 511 CG ASP A 232 4474 5383 5965 -678 -857 1252 C ATOM 512 OD1 ASP A 232 -13.898 21.050 -5.846 1.00 42.62 O ANISOU 512 OD1 ASP A 232 4582 5540 6074 -574 -745 1173 O ATOM 513 OD2 ASP A 232 -14.637 19.123 -5.112 1.00 41.91 O ANISOU 513 OD2 ASP A 232 4472 5432 6019 -794 -973 1377 O ATOM 514 N ASP A 233 -11.297 21.676 -6.693 1.00 23.76 N ANISOU 514 N ASP A 233 2364 2963 3700 -389 -704 902 N ATOM 515 CA ASP A 233 -10.516 21.877 -7.919 1.00 23.42 C ANISOU 515 CA ASP A 233 2382 2836 3679 -297 -719 775 C ATOM 516 C ASP A 233 -9.330 22.833 -7.729 1.00 25.77 C ANISOU 516 C ASP A 233 2720 3148 3925 -219 -611 669 C ATOM 517 O ASP A 233 -8.251 22.613 -8.291 1.00 22.27 O ANISOU 517 O ASP A 233 2334 2640 3489 -169 -654 570 O ATOM 518 CB ASP A 233 -11.400 22.343 -9.080 1.00 22.48 C ANISOU 518 CB ASP A 233 2233 2732 3576 -262 -696 766 C ATOM 519 CG ASP A 233 -12.223 21.206 -9.681 1.00 37.73 C ANISOU 519 CG ASP A 233 4156 4604 5575 -323 -842 840 C ATOM 520 OD1 ASP A 233 -12.023 20.038 -9.278 1.00 34.51 O ANISOU 520 OD1 ASP A 233 3779 4131 5202 -389 -979 889 O ATOM 521 OD2 ASP A 233 -13.069 21.477 -10.561 1.00 33.37 O ANISOU 521 OD2 ASP A 233 3574 4063 5042 -307 -833 849 O ATOM 522 N PHE A 234 -9.535 23.897 -6.952 1.00 21.69 N ANISOU 522 N PHE A 234 2171 2724 3347 -204 -480 688 N ATOM 523 CA PHE A 234 -8.460 24.839 -6.640 1.00 20.79 C ANISOU 523 CA PHE A 234 2100 2622 3176 -144 -387 606 C ATOM 524 C PHE A 234 -7.291 24.110 -5.968 1.00 21.26 C ANISOU 524 C PHE A 234 2208 2625 3244 -164 -440 581 C ATOM 525 O PHE A 234 -6.132 24.306 -6.314 1.00 20.83 O ANISOU 525 O PHE A 234 2204 2538 3173 -115 -435 486 O ATOM 526 CB PHE A 234 -8.976 25.956 -5.735 1.00 20.76 C ANISOU 526 CB PHE A 234 2060 2721 3107 -126 -265 645 C ATOM 527 CG PHE A 234 -7.892 26.814 -5.145 1.00 20.17 C ANISOU 527 CG PHE A 234 2037 2651 2975 -81 -188 586 C ATOM 528 CD1 PHE A 234 -7.277 27.796 -5.904 1.00 19.92 C ANISOU 528 CD1 PHE A 234 2056 2607 2907 -19 -145 499 C ATOM 529 CD2 PHE A 234 -7.496 26.640 -3.824 1.00 22.35 C ANISOU 529 CD2 PHE A 234 2316 2947 3230 -109 -166 624 C ATOM 530 CE1 PHE A 234 -6.281 28.599 -5.365 1.00 19.09 C ANISOU 530 CE1 PHE A 234 2003 2507 2744 12 -86 457 C ATOM 531 CE2 PHE A 234 -6.492 27.430 -3.267 1.00 20.31 C ANISOU 531 CE2 PHE A 234 2110 2688 2920 -68 -99 574 C ATOM 532 CZ PHE A 234 -5.886 28.415 -4.033 1.00 21.47 C ANISOU 532 CZ PHE A 234 2307 2820 3028 -9 -61 494 C ATOM 533 N LEU A 235 -7.604 23.253 -5.009 1.00 21.34 N ANISOU 533 N LEU A 235 2201 2632 3276 -241 -498 668 N ATOM 534 CA LEU A 235 -6.555 22.525 -4.301 1.00 21.37 C ANISOU 534 CA LEU A 235 2256 2573 3290 -264 -561 645 C ATOM 535 C LEU A 235 -5.866 21.510 -5.205 1.00 21.67 C ANISOU 535 C LEU A 235 2349 2506 3378 -241 -705 569 C ATOM 536 O LEU A 235 -4.653 21.300 -5.104 1.00 23.00 O ANISOU 536 O LEU A 235 2569 2632 3537 -202 -733 483 O ATOM 537 CB LEU A 235 -7.127 21.834 -3.069 1.00 22.10 C ANISOU 537 CB LEU A 235 2319 2688 3390 -367 -604 766 C ATOM 538 CG LEU A 235 -7.553 22.817 -1.972 1.00 38.54 C ANISOU 538 CG LEU A 235 4349 4890 5406 -371 -462 823 C ATOM 539 CD1 LEU A 235 -8.173 22.093 -0.770 1.00 45.71 C ANISOU 539 CD1 LEU A 235 5212 5846 6309 -486 -506 951 C ATOM 540 CD2 LEU A 235 -6.364 23.650 -1.532 1.00 38.79 C ANISOU 540 CD2 LEU A 235 4432 4913 5394 -302 -369 738 C ATOM 541 N LYS A 236 -6.655 20.879 -6.072 1.00 25.55 N ANISOU 541 N LYS A 236 2827 2963 3918 -259 -802 598 N ATOM 542 CA LYS A 236 -6.157 19.876 -7.002 1.00 26.49 C ANISOU 542 CA LYS A 236 2998 2983 4083 -224 -959 525 C ATOM 543 C LYS A 236 -5.195 20.505 -8.009 1.00 24.44 C ANISOU 543 C LYS A 236 2758 2738 3792 -115 -907 384 C ATOM 544 O LYS A 236 -4.157 19.931 -8.329 1.00 22.54 O ANISOU 544 O LYS A 236 2562 2452 3551 -60 -994 284 O ATOM 545 CB LYS A 236 -7.327 19.209 -7.722 1.00 27.46 C ANISOU 545 CB LYS A 236 3102 3071 4261 -267 -1065 598 C ATOM 546 CG LYS A 236 -6.947 18.383 -8.935 1.00 42.50 C ANISOU 546 CG LYS A 236 5058 4882 6208 -204 -1217 511 C ATOM 547 CD LYS A 236 -6.419 17.023 -8.545 1.00 59.51 C ANISOU 547 CD LYS A 236 7284 6929 8398 -228 -1416 504 C ATOM 548 CE LYS A 236 -6.600 16.032 -9.686 1.00 69.48 C ANISOU 548 CE LYS A 236 8593 8093 9713 -188 -1608 467 C ATOM 549 NZ LYS A 236 -8.025 15.948 -10.120 1.00 69.64 N ANISOU 549 NZ LYS A 236 8574 8115 9772 -258 -1629 587 N ATOM 550 N LEU A 237 -5.528 21.695 -8.499 1.00 20.99 N ANISOU 550 N LEU A 237 2285 2373 3318 -85 -772 373 N ATOM 551 CA LEU A 237 -4.623 22.396 -9.411 1.00 20.92 C ANISOU 551 CA LEU A 237 2290 2395 3262 -4 -719 254 C ATOM 552 C LEU A 237 -3.403 22.959 -8.670 1.00 21.61 C ANISOU 552 C LEU A 237 2401 2522 3288 16 -642 201 C ATOM 553 O LEU A 237 -2.270 22.890 -9.159 1.00 21.47 O ANISOU 553 O LEU A 237 2403 2517 3237 70 -666 96 O ATOM 554 CB LEU A 237 -5.359 23.512 -10.145 1.00 20.34 C ANISOU 554 CB LEU A 237 2186 2377 3167 10 -618 265 C ATOM 555 CG LEU A 237 -6.451 23.037 -11.106 1.00 21.72 C ANISOU 555 CG LEU A 237 2339 2515 3399 2 -690 298 C ATOM 556 CD1 LEU A 237 -6.856 24.194 -12.007 1.00 22.76 C ANISOU 556 CD1 LEU A 237 2454 2694 3499 32 -598 272 C ATOM 557 CD2 LEU A 237 -5.956 21.874 -11.943 1.00 24.68 C ANISOU 557 CD2 LEU A 237 2744 2820 3814 40 -842 230 C ATOM 558 N SER A 238 -3.641 23.509 -7.483 1.00 19.82 N ANISOU 558 N SER A 238 2166 2324 3040 -26 -553 274 N ATOM 559 CA SER A 238 -2.578 24.143 -6.723 1.00 19.63 C ANISOU 559 CA SER A 238 2168 2332 2958 -11 -475 237 C ATOM 560 C SER A 238 -1.485 23.141 -6.354 1.00 20.41 C ANISOU 560 C SER A 238 2303 2382 3070 -1 -570 178 C ATOM 561 O SER A 238 -0.313 23.498 -6.282 1.00 20.01 O ANISOU 561 O SER A 238 2274 2360 2969 35 -536 102 O ATOM 562 CB SER A 238 -3.131 24.817 -5.473 1.00 20.54 C ANISOU 562 CB SER A 238 2270 2483 3051 -50 -377 328 C ATOM 563 OG SER A 238 -3.873 25.976 -5.834 1.00 21.43 O ANISOU 563 OG SER A 238 2360 2653 3130 -32 -285 349 O ATOM 564 N THR A 239 -1.881 21.893 -6.127 1.00 20.21 N ANISOU 564 N THR A 239 2287 2282 3108 -36 -701 214 N ATOM 565 CA THR A 239 -0.944 20.855 -5.708 1.00 21.95 C ANISOU 565 CA THR A 239 2555 2439 3347 -25 -820 159 C ATOM 566 C THR A 239 -0.438 20.038 -6.895 1.00 29.57 C ANISOU 566 C THR A 239 3538 3370 4326 50 -957 48 C ATOM 567 O THR A 239 0.172 18.979 -6.723 1.00 29.81 O ANISOU 567 O THR A 239 3614 3334 4380 73 -1101 -7 O ATOM 568 CB THR A 239 -1.568 19.905 -4.656 1.00 24.69 C ANISOU 568 CB THR A 239 2919 2715 3746 -115 -914 264 C ATOM 569 OG1 THR A 239 -2.774 19.328 -5.174 1.00 26.85 O ANISOU 569 OG1 THR A 239 3173 2957 4071 -160 -1000 341 O ATOM 570 CG2 THR A 239 -1.893 20.656 -3.383 1.00 25.53 C ANISOU 570 CG2 THR A 239 3003 2873 3824 -176 -782 359 C ATOM 571 N ASN A 240 -0.689 20.533 -8.099 1.00 25.75 N ANISOU 571 N ASN A 240 3023 2934 3826 94 -922 9 N ATOM 572 CA ASN A 240 -0.292 19.817 -9.302 1.00 24.31 C ANISOU 572 CA ASN A 240 2850 2738 3651 175 -1047 -98 C ATOM 573 C ASN A 240 0.947 20.402 -9.952 1.00 25.74 C ANISOU 573 C ASN A 240 3012 3021 3748 256 -990 -228 C ATOM 574 O ASN A 240 1.133 21.618 -9.995 1.00 20.21 O ANISOU 574 O ASN A 240 2284 2406 2987 240 -840 -219 O ATOM 575 CB ASN A 240 -1.422 19.795 -10.326 1.00 22.05 C ANISOU 575 CB ASN A 240 2540 2434 3403 170 -1072 -57 C ATOM 576 CG ASN A 240 -1.054 19.008 -11.565 1.00 26.88 C ANISOU 576 CG ASN A 240 3164 3028 4023 262 -1213 -169 C ATOM 577 OD1 ASN A 240 -0.740 19.579 -12.609 1.00 22.93 O ANISOU 577 OD1 ASN A 240 2631 2607 3475 320 -1160 -245 O ATOM 578 ND2 ASN A 240 -1.052 17.692 -11.444 1.00 22.93 N ANISOU 578 ND2 ASN A 240 2713 2426 3574 278 -1404 -182 N ATOM 579 N ILE A 241 1.790 19.518 -10.466 1.00 22.11 N ANISOU 579 N ILE A 241 2567 2557 3276 342 -1123 -349 N ATOM 580 CA ILE A 241 3.063 19.912 -11.055 1.00 23.06 C ANISOU 580 CA ILE A 241 2657 2804 3303 421 -1087 -480 C ATOM 581 C ILE A 241 2.893 20.963 -12.154 1.00 23.68 C ANISOU 581 C ILE A 241 2682 2990 3324 423 -977 -490 C ATOM 582 O ILE A 241 3.678 21.911 -12.235 1.00 27.26 O ANISOU 582 O ILE A 241 3106 3563 3689 418 -866 -523 O ATOM 583 CB ILE A 241 3.828 18.673 -11.576 1.00 27.30 C ANISOU 583 CB ILE A 241 3210 3328 3834 535 -1274 -621 C ATOM 584 CG1 ILE A 241 5.156 19.078 -12.214 1.00 32.94 C ANISOU 584 CG1 ILE A 241 3871 4212 4433 620 -1234 -761 C ATOM 585 CG2 ILE A 241 2.960 17.881 -12.548 1.00 27.31 C ANISOU 585 CG2 ILE A 241 3225 3255 3896 572 -1412 -624 C ATOM 586 CD1 ILE A 241 6.112 17.902 -12.425 1.00 39.70 C ANISOU 586 CD1 ILE A 241 4741 5077 5266 748 -1414 -917 C ATOM 587 N PHE A 242 1.849 20.830 -12.971 1.00 22.24 N ANISOU 587 N PHE A 242 2493 2765 3192 419 -1011 -452 N ATOM 588 CA PHE A 242 1.603 21.814 -14.021 1.00 22.92 C ANISOU 588 CA PHE A 242 2538 2940 3231 412 -917 -456 C ATOM 589 C PHE A 242 0.554 22.825 -13.611 1.00 21.06 C ANISOU 589 C PHE A 242 2306 2676 3021 321 -792 -328 C ATOM 590 O PHE A 242 0.698 24.004 -13.879 1.00 24.13 O ANISOU 590 O PHE A 242 2679 3145 3345 293 -678 -319 O ATOM 591 CB PHE A 242 1.159 21.141 -15.318 1.00 24.61 C ANISOU 591 CB PHE A 242 2740 3135 3474 476 -1028 -510 C ATOM 592 CG PHE A 242 2.103 20.085 -15.776 1.00 25.49 C ANISOU 592 CG PHE A 242 2850 3276 3558 590 -1175 -649 C ATOM 593 CD1 PHE A 242 3.447 20.380 -15.943 1.00 26.57 C ANISOU 593 CD1 PHE A 242 2946 3563 3586 643 -1142 -761 C ATOM 594 CD2 PHE A 242 1.660 18.797 -16.017 1.00 27.54 C ANISOU 594 CD2 PHE A 242 3150 3420 3894 646 -1358 -670 C ATOM 595 CE1 PHE A 242 4.338 19.409 -16.349 1.00 32.17 C ANISOU 595 CE1 PHE A 242 3646 4320 4258 766 -1283 -904 C ATOM 596 CE2 PHE A 242 2.552 17.817 -16.428 1.00 37.14 C ANISOU 596 CE2 PHE A 242 4373 4661 5078 771 -1513 -814 C ATOM 597 CZ PHE A 242 3.893 18.130 -16.590 1.00 35.83 C ANISOU 597 CZ PHE A 242 4157 4659 4799 838 -1472 -937 C ATOM 598 N GLY A 243 -0.505 22.348 -12.964 1.00 21.98 N ANISOU 598 N GLY A 243 2444 2684 3224 276 -826 -229 N ATOM 599 CA GLY A 243 -1.630 23.204 -12.623 1.00 20.01 C ANISOU 599 CA GLY A 243 2187 2420 2995 207 -723 -115 C ATOM 600 C GLY A 243 -1.312 24.387 -11.727 1.00 20.41 C ANISOU 600 C GLY A 243 2243 2525 2987 168 -584 -77 C ATOM 601 O GLY A 243 -2.007 25.393 -11.770 1.00 19.01 O ANISOU 601 O GLY A 243 2060 2369 2795 138 -494 -22 O ATOM 602 N ASN A 244 -0.282 24.286 -10.891 1.00 20.02 N ANISOU 602 N ASN A 244 2210 2493 2902 172 -574 -108 N ATOM 603 CA ASN A 244 -0.025 25.380 -9.958 1.00 18.69 C ANISOU 603 CA ASN A 244 2057 2362 2682 135 -453 -63 C ATOM 604 C ASN A 244 0.306 26.675 -10.698 1.00 18.53 C ANISOU 604 C ASN A 244 2034 2426 2579 133 -370 -90 C ATOM 605 O ASN A 244 0.049 27.770 -10.188 1.00 18.27 O ANISOU 605 O ASN A 244 2023 2408 2512 102 -281 -35 O ATOM 606 CB ASN A 244 1.080 25.030 -8.956 1.00 19.02 C ANISOU 606 CB ASN A 244 2121 2404 2702 140 -461 -93 C ATOM 607 CG ASN A 244 2.466 25.146 -9.551 1.00 19.83 C ANISOU 607 CG ASN A 244 2215 2593 2725 183 -470 -204 C ATOM 608 OD1 ASN A 244 3.071 26.226 -9.562 1.00 22.43 O ANISOU 608 OD1 ASN A 244 2547 3001 2974 165 -382 -210 O ATOM 609 ND2 ASN A 244 2.986 24.034 -10.041 1.00 22.48 N ANISOU 609 ND2 ASN A 244 2540 2924 3076 241 -586 -292 N ATOM 610 N TYR A 245 0.896 26.546 -11.882 1.00 19.03 N ANISOU 610 N TYR A 245 2076 2550 2603 166 -410 -176 N ATOM 611 CA TYR A 245 1.195 27.705 -12.715 1.00 18.82 C ANISOU 611 CA TYR A 245 2047 2612 2492 147 -351 -197 C ATOM 612 C TYR A 245 -0.086 28.366 -13.213 1.00 19.32 C ANISOU 612 C TYR A 245 2118 2638 2586 123 -322 -137 C ATOM 613 O TYR A 245 -0.191 29.592 -13.260 1.00 19.29 O ANISOU 613 O TYR A 245 2141 2662 2525 87 -258 -106 O ATOM 614 CB TYR A 245 2.070 27.311 -13.912 1.00 21.02 C ANISOU 614 CB TYR A 245 2286 2988 2715 187 -408 -303 C ATOM 615 CG TYR A 245 3.492 26.952 -13.531 1.00 22.28 C ANISOU 615 CG TYR A 245 2429 3226 2810 214 -426 -378 C ATOM 616 CD1 TYR A 245 4.441 27.936 -13.312 1.00 23.10 C ANISOU 616 CD1 TYR A 245 2536 3431 2808 170 -356 -378 C ATOM 617 CD2 TYR A 245 3.882 25.624 -13.398 1.00 25.24 C ANISOU 617 CD2 TYR A 245 2791 3574 3226 283 -525 -447 C ATOM 618 CE1 TYR A 245 5.752 27.612 -12.972 1.00 24.32 C ANISOU 618 CE1 TYR A 245 2669 3672 2899 194 -370 -447 C ATOM 619 CE2 TYR A 245 5.188 25.290 -13.045 1.00 23.93 C ANISOU 619 CE2 TYR A 245 2610 3487 2998 319 -547 -527 C ATOM 620 CZ TYR A 245 6.111 26.290 -12.837 1.00 28.68 C ANISOU 620 CZ TYR A 245 3202 4201 3493 274 -462 -526 C ATOM 621 OH TYR A 245 7.403 25.957 -12.497 1.00 29.89 O ANISOU 621 OH TYR A 245 3333 4444 3582 309 -482 -605 O ATOM 622 N LEU A 246 -1.052 27.553 -13.616 1.00 19.69 N ANISOU 622 N LEU A 246 2146 2618 2717 144 -381 -121 N ATOM 623 CA LEU A 246 -2.318 28.099 -14.093 1.00 19.10 C ANISOU 623 CA LEU A 246 2073 2509 2675 127 -358 -68 C ATOM 624 C LEU A 246 -3.029 28.803 -12.950 1.00 19.06 C ANISOU 624 C LEU A 246 2088 2477 2677 100 -287 18 C ATOM 625 O LEU A 246 -3.613 29.864 -13.141 1.00 18.51 O ANISOU 625 O LEU A 246 2037 2415 2579 88 -239 45 O ATOM 626 CB LEU A 246 -3.219 26.996 -14.648 1.00 18.62 C ANISOU 626 CB LEU A 246 1987 2380 2707 149 -443 -58 C ATOM 627 CG LEU A 246 -4.543 27.532 -15.199 1.00 24.49 C ANISOU 627 CG LEU A 246 2726 3095 3485 134 -420 -6 C ATOM 628 CD1 LEU A 246 -4.282 28.514 -16.341 1.00 19.35 C ANISOU 628 CD1 LEU A 246 2086 2497 2768 130 -392 -57 C ATOM 629 CD2 LEU A 246 -5.422 26.387 -15.653 1.00 26.30 C ANISOU 629 CD2 LEU A 246 2933 3254 3807 147 -512 16 C ATOM 630 N VAL A 247 -2.958 28.229 -11.755 1.00 18.16 N ANISOU 630 N VAL A 247 1973 2335 2594 94 -288 56 N ATOM 631 CA VAL A 247 -3.587 28.855 -10.597 1.00 18.08 C ANISOU 631 CA VAL A 247 1972 2319 2579 77 -220 133 C ATOM 632 C VAL A 247 -2.968 30.224 -10.341 1.00 19.51 C ANISOU 632 C VAL A 247 2200 2544 2671 74 -150 121 C ATOM 633 O VAL A 247 -3.680 31.208 -10.135 1.00 18.40 O ANISOU 633 O VAL A 247 2079 2408 2506 79 -106 158 O ATOM 634 CB VAL A 247 -3.458 27.991 -9.338 1.00 19.40 C ANISOU 634 CB VAL A 247 2130 2458 2783 63 -237 175 C ATOM 635 CG1 VAL A 247 -3.900 28.786 -8.110 1.00 19.35 C ANISOU 635 CG1 VAL A 247 2131 2473 2747 54 -157 242 C ATOM 636 CG2 VAL A 247 -4.293 26.702 -9.476 1.00 19.75 C ANISOU 636 CG2 VAL A 247 2139 2452 2915 47 -325 214 C ATOM 637 N GLN A 248 -1.643 30.300 -10.379 1.00 17.71 N ANISOU 637 N GLN A 248 1991 2350 2387 68 -150 69 N ATOM 638 CA GLN A 248 -0.977 31.586 -10.167 1.00 18.11 C ANISOU 638 CA GLN A 248 2095 2441 2346 50 -100 68 C ATOM 639 C GLN A 248 -1.369 32.630 -11.215 1.00 18.30 C ANISOU 639 C GLN A 248 2145 2484 2324 36 -101 59 C ATOM 640 O GLN A 248 -1.613 33.798 -10.877 1.00 18.26 O ANISOU 640 O GLN A 248 2195 2473 2270 30 -74 91 O ATOM 641 CB GLN A 248 0.545 31.404 -10.129 1.00 17.26 C ANISOU 641 CB GLN A 248 1992 2387 2180 37 -108 14 C ATOM 642 CG GLN A 248 1.024 30.537 -8.980 1.00 18.05 C ANISOU 642 CG GLN A 248 2083 2458 2316 50 -110 19 C ATOM 643 CD GLN A 248 2.516 30.299 -9.050 1.00 23.92 C ANISOU 643 CD GLN A 248 2823 3264 3001 47 -125 -47 C ATOM 644 OE1 GLN A 248 3.310 31.237 -8.970 1.00 21.42 O ANISOU 644 OE1 GLN A 248 2538 3003 2598 17 -90 -47 O ATOM 645 NE2 GLN A 248 2.904 29.046 -9.225 1.00 18.26 N ANISOU 645 NE2 GLN A 248 2070 2544 2325 79 -190 -104 N ATOM 646 N SER A 249 -1.440 32.219 -12.482 1.00 18.09 N ANISOU 646 N SER A 249 2086 2475 2311 34 -143 16 N ATOM 647 CA SER A 249 -1.858 33.126 -13.551 1.00 19.23 C ANISOU 647 CA SER A 249 2256 2632 2418 13 -153 8 C ATOM 648 C SER A 249 -3.279 33.636 -13.359 1.00 17.60 C ANISOU 648 C SER A 249 2068 2366 2253 35 -140 56 C ATOM 649 O SER A 249 -3.539 34.828 -13.525 1.00 19.36 O ANISOU 649 O SER A 249 2350 2585 2423 23 -138 66 O ATOM 650 CB SER A 249 -1.728 32.458 -14.933 1.00 21.21 C ANISOU 650 CB SER A 249 2461 2914 2682 14 -202 -50 C ATOM 651 OG SER A 249 -0.367 32.253 -15.241 1.00 32.05 O ANISOU 651 OG SER A 249 3815 4378 3985 -2 -215 -105 O ATOM 652 N VAL A 250 -4.197 32.744 -13.009 1.00 17.61 N ANISOU 652 N VAL A 250 2020 2329 2343 67 -143 84 N ATOM 653 CA VAL A 250 -5.590 33.151 -12.793 1.00 17.76 C ANISOU 653 CA VAL A 250 2035 2318 2395 93 -129 128 C ATOM 654 C VAL A 250 -5.752 34.021 -11.549 1.00 18.16 C ANISOU 654 C VAL A 250 2123 2378 2400 115 -85 165 C ATOM 655 O VAL A 250 -6.533 34.960 -11.543 1.00 19.05 O ANISOU 655 O VAL A 250 2266 2485 2486 143 -81 174 O ATOM 656 CB VAL A 250 -6.541 31.950 -12.760 1.00 18.01 C ANISOU 656 CB VAL A 250 1997 2324 2522 105 -152 162 C ATOM 657 CG1 VAL A 250 -7.959 32.412 -12.413 1.00 18.81 C ANISOU 657 CG1 VAL A 250 2079 2427 2640 132 -130 211 C ATOM 658 CG2 VAL A 250 -6.503 31.239 -14.119 1.00 18.04 C ANISOU 658 CG2 VAL A 250 1978 2309 2567 98 -210 120 C ATOM 659 N ILE A 251 -5.000 33.738 -10.494 1.00 18.20 N ANISOU 659 N ILE A 251 2130 2394 2392 110 -59 180 N ATOM 660 CA ILE A 251 -5.023 34.648 -9.349 1.00 17.72 C ANISOU 660 CA ILE A 251 2114 2342 2277 137 -22 208 C ATOM 661 C ILE A 251 -4.625 36.060 -9.794 1.00 17.65 C ANISOU 661 C ILE A 251 2197 2329 2181 131 -41 183 C ATOM 662 O ILE A 251 -5.271 37.049 -9.424 1.00 19.65 O ANISOU 662 O ILE A 251 2497 2574 2396 175 -45 193 O ATOM 663 CB ILE A 251 -4.122 34.130 -8.217 1.00 18.55 C ANISOU 663 CB ILE A 251 2215 2454 2380 125 4 225 C ATOM 664 CG1 ILE A 251 -4.777 32.906 -7.564 1.00 17.82 C ANISOU 664 CG1 ILE A 251 2045 2361 2365 126 9 267 C ATOM 665 CG2 ILE A 251 -3.870 35.221 -7.184 1.00 21.00 C ANISOU 665 CG2 ILE A 251 2591 2769 2619 152 34 243 C ATOM 666 CD1 ILE A 251 -3.844 32.161 -6.589 1.00 17.71 C ANISOU 666 CD1 ILE A 251 2027 2339 2361 104 17 277 C ATOM 667 N GLY A 252 -3.572 36.165 -10.598 1.00 17.84 N ANISOU 667 N GLY A 252 2248 2365 2165 77 -66 150 N ATOM 668 CA GLY A 252 -3.138 37.461 -11.107 1.00 17.88 C ANISOU 668 CA GLY A 252 2344 2370 2080 44 -103 138 C ATOM 669 C GLY A 252 -4.211 38.165 -11.929 1.00 21.69 C ANISOU 669 C GLY A 252 2857 2822 2561 61 -143 128 C ATOM 670 O GLY A 252 -4.438 39.369 -11.794 1.00 20.07 O ANISOU 670 O GLY A 252 2741 2590 2294 75 -181 133 O ATOM 671 N ILE A 253 -4.885 37.413 -12.787 1.00 17.75 N ANISOU 671 N ILE A 253 2292 2320 2132 66 -146 112 N ATOM 672 CA ILE A 253 -5.960 37.983 -13.600 1.00 18.05 C ANISOU 672 CA ILE A 253 2352 2326 2179 85 -183 100 C ATOM 673 C ILE A 253 -7.117 38.416 -12.707 1.00 18.23 C ANISOU 673 C ILE A 253 2379 2333 2214 168 -170 119 C ATOM 674 O ILE A 253 -7.657 39.502 -12.879 1.00 18.88 O ANISOU 674 O ILE A 253 2533 2388 2251 198 -215 104 O ATOM 675 CB ILE A 253 -6.433 36.993 -14.697 1.00 18.43 C ANISOU 675 CB ILE A 253 2324 2372 2305 74 -190 81 C ATOM 676 CG1 ILE A 253 -5.258 36.624 -15.616 1.00 22.63 C ANISOU 676 CG1 ILE A 253 2847 2944 2807 7 -209 48 C ATOM 677 CG2 ILE A 253 -7.610 37.571 -15.502 1.00 18.09 C ANISOU 677 CG2 ILE A 253 2304 2291 2278 96 -226 69 C ATOM 678 CD1 ILE A 253 -5.534 35.469 -16.565 1.00 24.01 C ANISOU 678 CD1 ILE A 253 2946 3121 3057 11 -223 24 C ATOM 679 N SER A 254 -7.455 37.601 -11.712 1.00 18.27 N ANISOU 679 N SER A 254 2309 2364 2268 205 -119 151 N ATOM 680 CA SER A 254 -8.515 37.959 -10.775 1.00 20.04 C ANISOU 680 CA SER A 254 2517 2611 2488 286 -100 170 C ATOM 681 C SER A 254 -8.209 39.279 -10.072 1.00 22.11 C ANISOU 681 C SER A 254 2882 2863 2658 329 -125 158 C ATOM 682 O SER A 254 -9.081 40.137 -9.929 1.00 20.08 O ANISOU 682 O SER A 254 2660 2605 2365 405 -157 139 O ATOM 683 CB SER A 254 -8.711 36.862 -9.720 1.00 21.31 C ANISOU 683 CB SER A 254 2581 2816 2699 295 -44 217 C ATOM 684 OG SER A 254 -9.785 37.208 -8.857 1.00 19.63 O ANISOU 684 OG SER A 254 2334 2657 2469 372 -24 236 O ATOM 685 N LEU A 255 -6.965 39.438 -9.629 1.00 18.74 N ANISOU 685 N LEU A 255 2506 2425 2187 287 -120 167 N ATOM 686 CA LEU A 255 -6.556 40.654 -8.920 1.00 18.88 C ANISOU 686 CA LEU A 255 2635 2423 2117 320 -157 164 C ATOM 687 C LEU A 255 -6.560 41.881 -9.834 1.00 24.17 C ANISOU 687 C LEU A 255 3422 3040 2720 303 -253 134 C ATOM 688 O LEU A 255 -6.704 43.005 -9.364 1.00 24.53 O ANISOU 688 O LEU A 255 3568 3055 2695 360 -315 123 O ATOM 689 CB LEU A 255 -5.159 40.471 -8.328 1.00 19.28 C ANISOU 689 CB LEU A 255 2711 2475 2139 263 -133 187 C ATOM 690 CG LEU A 255 -5.065 39.518 -7.137 1.00 21.37 C ANISOU 690 CG LEU A 255 2895 2776 2449 286 -56 218 C ATOM 691 CD1 LEU A 255 -3.611 39.188 -6.787 1.00 23.76 C ANISOU 691 CD1 LEU A 255 3216 3076 2734 220 -37 230 C ATOM 692 CD2 LEU A 255 -5.761 40.118 -5.961 1.00 18.73 C ANISOU 692 CD2 LEU A 255 2578 2459 2081 386 -48 228 C ATOM 693 N ALA A 256 -6.402 41.665 -11.135 1.00 21.27 N ANISOU 693 N ALA A 256 3047 2662 2372 227 -277 120 N ATOM 694 CA ALA A 256 -6.352 42.767 -12.108 1.00 19.04 C ANISOU 694 CA ALA A 256 2876 2331 2026 185 -377 98 C ATOM 695 C ALA A 256 -7.740 43.180 -12.611 1.00 26.16 C ANISOU 695 C ALA A 256 3787 3202 2950 258 -421 62 C ATOM 696 O ALA A 256 -7.891 44.170 -13.331 1.00 28.24 O ANISOU 696 O ALA A 256 4155 3412 3161 238 -520 39 O ATOM 697 CB ALA A 256 -5.465 42.377 -13.279 1.00 23.69 C ANISOU 697 CB ALA A 256 3448 2942 2611 63 -383 99 C ATOM 698 N THR A 257 -8.759 42.422 -12.224 1.00 21.90 N ANISOU 698 N THR A 257 3138 2701 2483 336 -356 60 N ATOM 699 CA THR A 257 -10.094 42.602 -12.790 1.00 22.75 C ANISOU 699 CA THR A 257 3226 2798 2621 400 -384 27 C ATOM 700 C THR A 257 -11.050 43.154 -11.740 1.00 25.59 C ANISOU 700 C THR A 257 3585 3189 2948 537 -392 8 C ATOM 701 O THR A 257 -11.659 42.413 -10.965 1.00 24.15 O ANISOU 701 O THR A 257 3288 3084 2805 593 -316 29 O ATOM 702 CB THR A 257 -10.628 41.284 -13.392 1.00 26.18 C ANISOU 702 CB THR A 257 3526 3264 3158 373 -318 42 C ATOM 703 OG1 THR A 257 -9.676 40.775 -14.333 1.00 23.04 O ANISOU 703 OG1 THR A 257 3127 2849 2779 264 -318 48 O ATOM 704 CG2 THR A 257 -11.942 41.512 -14.104 1.00 27.19 C ANISOU 704 CG2 THR A 257 3639 3377 3315 426 -353 10 C ATOM 705 N ASN A 258 -11.186 44.473 -11.732 1.00 24.87 N ANISOU 705 N ASN A 258 3626 3046 2776 591 -498 -34 N ATOM 706 CA ASN A 258 -11.981 45.170 -10.727 1.00 26.43 C ANISOU 706 CA ASN A 258 3843 3278 2919 742 -530 -69 C ATOM 707 C ASN A 258 -13.464 45.277 -11.037 1.00 31.17 C ANISOU 707 C ASN A 258 4389 3917 3537 847 -548 -120 C ATOM 708 O ASN A 258 -14.055 46.351 -10.899 1.00 32.64 O ANISOU 708 O ASN A 258 4663 4083 3654 959 -650 -183 O ATOM 709 CB ASN A 258 -11.415 46.567 -10.529 1.00 31.98 C ANISOU 709 CB ASN A 258 4732 3900 3521 765 -662 -97 C ATOM 710 CG ASN A 258 -10.026 46.532 -9.965 1.00 39.42 C ANISOU 710 CG ASN A 258 5722 4824 4432 682 -642 -44 C ATOM 711 OD1 ASN A 258 -9.047 46.835 -10.654 1.00 47.13 O ANISOU 711 OD1 ASN A 258 6786 5739 5382 557 -695 -21 O ATOM 712 ND2 ASN A 258 -9.922 46.120 -8.711 1.00 37.76 N ANISOU 712 ND2 ASN A 258 5445 4679 4222 743 -562 -22 N ATOM 713 N ASP A 259 -14.073 44.175 -11.449 1.00 24.34 N ANISOU 713 N ASP A 259 3382 3107 2759 815 -463 -94 N ATOM 714 CA ASP A 259 -15.513 44.175 -11.646 1.00 22.53 C ANISOU 714 CA ASP A 259 3078 2937 2545 912 -469 -132 C ATOM 715 C ASP A 259 -16.213 43.933 -10.318 1.00 27.11 C ANISOU 715 C ASP A 259 3545 3661 3096 1026 -407 -124 C ATOM 716 O ASP A 259 -15.564 43.873 -9.280 1.00 27.84 O ANISOU 716 O ASP A 259 3637 3787 3155 1034 -369 -95 O ATOM 717 CB ASP A 259 -15.938 43.156 -12.707 1.00 25.81 C ANISOU 717 CB ASP A 259 3398 3348 3061 827 -421 -103 C ATOM 718 CG ASP A 259 -15.537 41.734 -12.365 1.00 34.06 C ANISOU 718 CG ASP A 259 4316 4446 4179 742 -313 -22 C ATOM 719 OD1 ASP A 259 -15.131 41.453 -11.215 1.00 35.67 O ANISOU 719 OD1 ASP A 259 4482 4711 4361 756 -260 13 O ATOM 720 OD2 ASP A 259 -15.632 40.883 -13.271 1.00 38.90 O ANISOU 720 OD2 ASP A 259 4875 5033 4872 663 -291 3 O ATOM 721 N ASP A 260 -17.538 43.810 -10.353 1.00 25.33 N ANISOU 721 N ASP A 260 3219 3532 2875 1113 -397 -149 N ATOM 722 CA ASP A 260 -18.321 43.652 -9.139 1.00 29.57 C ANISOU 722 CA ASP A 260 3633 4240 3363 1226 -344 -146 C ATOM 723 C ASP A 260 -18.014 42.360 -8.381 1.00 30.73 C ANISOU 723 C ASP A 260 3643 4476 3558 1139 -225 -46 C ATOM 724 O ASP A 260 -18.301 42.259 -7.195 1.00 34.73 O ANISOU 724 O ASP A 260 4066 5119 4012 1207 -180 -29 O ATOM 725 CB ASP A 260 -19.815 43.729 -9.446 1.00 32.60 C ANISOU 725 CB ASP A 260 3922 4728 3737 1324 -359 -190 C ATOM 726 CG ASP A 260 -20.637 43.968 -8.215 1.00 45.52 C ANISOU 726 CG ASP A 260 5454 6560 5280 1476 -337 -217 C ATOM 727 OD1 ASP A 260 -20.453 45.030 -7.578 1.00 47.36 O ANISOU 727 OD1 ASP A 260 5786 6791 5418 1604 -408 -289 O ATOM 728 OD2 ASP A 260 -21.459 43.091 -7.880 1.00 49.24 O ANISOU 728 OD2 ASP A 260 5746 7195 5769 1465 -256 -163 O ATOM 729 N GLY A 261 -17.427 41.381 -9.059 1.00 23.46 N ANISOU 729 N GLY A 261 2703 3480 2732 991 -186 17 N ATOM 730 CA GLY A 261 -17.128 40.107 -8.424 1.00 24.36 C ANISOU 730 CA GLY A 261 2702 3656 2897 901 -98 109 C ATOM 731 C GLY A 261 -15.801 40.056 -7.687 1.00 27.96 C ANISOU 731 C GLY A 261 3223 4064 3339 855 -75 134 C ATOM 732 O GLY A 261 -15.472 39.059 -7.048 1.00 26.60 O ANISOU 732 O GLY A 261 2971 3935 3201 787 -13 205 O ATOM 733 N TYR A 262 -15.038 41.138 -7.765 1.00 23.10 N ANISOU 733 N TYR A 262 2755 3354 2667 887 -135 80 N ATOM 734 CA TYR A 262 -13.672 41.146 -7.233 1.00 21.92 C ANISOU 734 CA TYR A 262 2680 3144 2505 831 -121 104 C ATOM 735 C TYR A 262 -13.610 40.773 -5.751 1.00 22.71 C ANISOU 735 C TYR A 262 2706 3346 2575 866 -55 146 C ATOM 736 O TYR A 262 -12.856 39.892 -5.354 1.00 27.04 O ANISOU 736 O TYR A 262 3220 3887 3167 777 -2 203 O ATOM 737 CB TYR A 262 -13.049 42.525 -7.468 1.00 21.99 C ANISOU 737 CB TYR A 262 2864 3053 2439 869 -216 45 C ATOM 738 CG TYR A 262 -11.655 42.726 -6.886 1.00 21.44 C ANISOU 738 CG TYR A 262 2882 2925 2339 817 -215 69 C ATOM 739 CD1 TYR A 262 -10.515 42.599 -7.682 1.00 24.47 C ANISOU 739 CD1 TYR A 262 3334 3217 2745 693 -232 85 C ATOM 740 CD2 TYR A 262 -11.484 43.070 -5.553 1.00 28.30 C ANISOU 740 CD2 TYR A 262 3762 3842 3148 896 -199 74 C ATOM 741 CE1 TYR A 262 -9.239 42.796 -7.156 1.00 24.64 C ANISOU 741 CE1 TYR A 262 3430 3200 2732 644 -232 108 C ATOM 742 CE2 TYR A 262 -10.216 43.274 -5.016 1.00 23.94 C ANISOU 742 CE2 TYR A 262 3295 3233 2569 849 -201 98 C ATOM 743 CZ TYR A 262 -9.101 43.140 -5.818 1.00 29.92 C ANISOU 743 CZ TYR A 262 4117 3902 3350 721 -218 116 C ATOM 744 OH TYR A 262 -7.852 43.349 -5.272 1.00 29.18 O ANISOU 744 OH TYR A 262 4099 3765 3223 673 -220 142 O ATOM 745 N THR A 263 -14.394 41.452 -4.923 1.00 24.83 N ANISOU 745 N THR A 263 2953 3717 2765 1001 -66 113 N ATOM 746 CA THR A 263 -14.313 41.214 -3.479 1.00 27.81 C ANISOU 746 CA THR A 263 3265 4201 3100 1041 -8 149 C ATOM 747 C THR A 263 -14.610 39.765 -3.121 1.00 27.58 C ANISOU 747 C THR A 263 3076 4267 3135 945 77 238 C ATOM 748 O THR A 263 -13.887 39.151 -2.347 1.00 28.98 O ANISOU 748 O THR A 263 3236 4446 3330 881 124 292 O ATOM 749 CB THR A 263 -15.240 42.160 -2.703 1.00 34.87 C ANISOU 749 CB THR A 263 4142 5219 3886 1219 -39 88 C ATOM 750 OG1 THR A 263 -14.816 43.511 -2.924 1.00 34.32 O ANISOU 750 OG1 THR A 263 4249 5038 3753 1305 -143 9 O ATOM 751 CG2 THR A 263 -15.178 41.858 -1.207 1.00 40.85 C ANISOU 751 CG2 THR A 263 4819 6106 4595 1257 27 129 C ATOM 752 N LYS A 264 -15.680 39.219 -3.688 1.00 28.20 N ANISOU 752 N LYS A 264 3046 4419 3250 929 86 256 N ATOM 753 CA LYS A 264 -16.054 37.842 -3.404 1.00 29.56 C ANISOU 753 CA LYS A 264 3074 4679 3479 826 141 351 C ATOM 754 C LYS A 264 -14.995 36.853 -3.858 1.00 30.17 C ANISOU 754 C LYS A 264 3189 4623 3653 680 146 400 C ATOM 755 O LYS A 264 -14.683 35.912 -3.132 1.00 28.89 O ANISOU 755 O LYS A 264 2966 4494 3516 602 180 471 O ATOM 756 CB LYS A 264 -17.418 37.501 -4.016 1.00 38.29 C ANISOU 756 CB LYS A 264 4064 5883 4601 831 135 366 C ATOM 757 CG LYS A 264 -18.585 38.149 -3.289 1.00 48.18 C ANISOU 757 CG LYS A 264 5223 7334 5748 969 145 335 C ATOM 758 CD LYS A 264 -19.921 37.707 -3.874 1.00 60.15 C ANISOU 758 CD LYS A 264 6610 8965 7280 960 143 360 C ATOM 759 CE LYS A 264 -21.085 38.445 -3.228 1.00 68.37 C ANISOU 759 CE LYS A 264 7553 10224 8201 1117 146 310 C ATOM 760 NZ LYS A 264 -22.393 38.046 -3.827 1.00 74.68 N ANISOU 760 NZ LYS A 264 8220 11145 9009 1107 143 334 N ATOM 761 N ARG A 265 -14.433 37.064 -5.049 1.00 24.35 N ANISOU 761 N ARG A 265 2549 3741 2961 647 104 357 N ATOM 762 CA ARG A 265 -13.387 36.172 -5.549 1.00 21.62 C ANISOU 762 CA ARG A 265 2237 3284 2694 529 100 384 C ATOM 763 C ARG A 265 -12.174 36.155 -4.627 1.00 22.03 C ANISOU 763 C ARG A 265 2344 3303 2725 507 124 395 C ATOM 764 O ARG A 265 -11.602 35.100 -4.340 1.00 23.31 O ANISOU 764 O ARG A 265 2474 3444 2938 422 138 443 O ATOM 765 CB ARG A 265 -12.928 36.578 -6.959 1.00 24.57 C ANISOU 765 CB ARG A 265 2706 3534 3095 508 50 327 C ATOM 766 CG ARG A 265 -13.913 36.253 -8.067 1.00 24.71 C ANISOU 766 CG ARG A 265 2673 3550 3165 495 24 325 C ATOM 767 CD ARG A 265 -13.257 36.345 -9.456 1.00 20.88 C ANISOU 767 CD ARG A 265 2271 2943 2718 446 -21 282 C ATOM 768 NE ARG A 265 -12.450 37.559 -9.619 1.00 21.65 N ANISOU 768 NE ARG A 265 2498 2980 2749 473 -50 222 N ATOM 769 CZ ARG A 265 -12.928 38.722 -10.061 1.00 22.43 C ANISOU 769 CZ ARG A 265 2667 3059 2797 538 -98 168 C ATOM 770 NH1 ARG A 265 -14.218 38.838 -10.361 1.00 21.23 N ANISOU 770 NH1 ARG A 265 2460 2952 2654 596 -109 156 N ATOM 771 NH2 ARG A 265 -12.120 39.773 -10.190 1.00 20.24 N ANISOU 771 NH2 ARG A 265 2517 2719 2455 543 -144 128 N ATOM 772 N GLN A 266 -11.769 37.329 -4.170 1.00 23.92 N ANISOU 772 N GLN A 266 2673 3529 2886 586 116 348 N ATOM 773 CA GLN A 266 -10.568 37.406 -3.349 1.00 20.70 C ANISOU 773 CA GLN A 266 2329 3080 2457 566 135 356 C ATOM 774 C GLN A 266 -10.812 36.852 -1.944 1.00 23.62 C ANISOU 774 C GLN A 266 2612 3553 2811 572 188 414 C ATOM 775 O GLN A 266 -9.927 36.222 -1.364 1.00 23.38 O ANISOU 775 O GLN A 266 2589 3489 2805 508 211 447 O ATOM 776 CB GLN A 266 -10.046 38.844 -3.288 1.00 34.85 C ANISOU 776 CB GLN A 266 4257 4816 4167 641 93 298 C ATOM 777 CG GLN A 266 -8.969 39.183 -4.330 1.00 47.12 C ANISOU 777 CG GLN A 266 5922 6250 5731 573 47 267 C ATOM 778 CD GLN A 266 -9.297 38.713 -5.744 1.00 51.05 C ANISOU 778 CD GLN A 266 6391 6715 6290 514 24 255 C ATOM 779 OE1 GLN A 266 -9.981 39.405 -6.519 1.00 37.71 O ANISOU 779 OE1 GLN A 266 4733 5012 4582 555 -23 216 O ATOM 780 NE2 GLN A 266 -8.775 37.544 -6.101 1.00 55.33 N ANISOU 780 NE2 GLN A 266 6882 7237 6904 423 46 282 N ATOM 781 N GLU A 267 -12.010 37.071 -1.413 1.00 25.31 N ANISOU 781 N GLU A 267 2738 3900 2977 648 205 423 N ATOM 782 CA GLU A 267 -12.367 36.528 -0.102 1.00 30.35 C ANISOU 782 CA GLU A 267 3275 4669 3589 646 255 485 C ATOM 783 C GLU A 267 -12.427 35.012 -0.176 1.00 28.13 C ANISOU 783 C GLU A 267 2902 4395 3390 508 265 569 C ATOM 784 O GLU A 267 -11.997 34.314 0.739 1.00 28.75 O ANISOU 784 O GLU A 267 2952 4494 3479 446 288 625 O ATOM 785 CB GLU A 267 -13.717 37.079 0.375 1.00 29.82 C ANISOU 785 CB GLU A 267 3113 4779 3439 760 266 473 C ATOM 786 CG GLU A 267 -14.228 36.455 1.680 1.00 40.26 C ANISOU 786 CG GLU A 267 4301 6276 4719 744 318 547 C ATOM 787 CD GLU A 267 -13.554 37.025 2.926 1.00 43.34 C ANISOU 787 CD GLU A 267 4743 6683 5040 811 343 533 C ATOM 788 OE1 GLU A 267 -12.698 37.929 2.795 1.00 46.43 O ANISOU 788 OE1 GLU A 267 5280 6946 5415 872 314 468 O ATOM 789 OE2 GLU A 267 -13.885 36.567 4.043 1.00 43.07 O ANISOU 789 OE2 GLU A 267 4606 6794 4964 797 387 591 O ATOM 790 N LYS A 268 -12.961 34.505 -1.280 1.00 24.87 N ANISOU 790 N LYS A 268 2455 3957 3039 459 234 576 N ATOM 791 CA LYS A 268 -13.039 33.071 -1.493 1.00 25.15 C ANISOU 791 CA LYS A 268 2422 3977 3156 331 214 653 C ATOM 792 C LYS A 268 -11.643 32.447 -1.565 1.00 27.72 C ANISOU 792 C LYS A 268 2830 4161 3539 255 194 648 C ATOM 793 O LYS A 268 -11.384 31.412 -0.955 1.00 29.28 O ANISOU 793 O LYS A 268 2993 4362 3772 169 183 712 O ATOM 794 CB LYS A 268 -13.852 32.773 -2.753 1.00 28.29 C ANISOU 794 CB LYS A 268 2784 4359 3604 310 174 652 C ATOM 795 CG LYS A 268 -13.792 31.354 -3.211 1.00 37.59 C ANISOU 795 CG LYS A 268 3927 5480 4874 185 125 717 C ATOM 796 CD LYS A 268 -14.478 31.196 -4.566 1.00 42.65 C ANISOU 796 CD LYS A 268 4556 6083 5567 178 82 703 C ATOM 797 CE LYS A 268 -15.987 31.285 -4.453 1.00 35.46 C ANISOU 797 CE LYS A 268 3527 5326 4621 199 94 749 C ATOM 798 NZ LYS A 268 -16.617 30.898 -5.758 1.00 34.49 N ANISOU 798 NZ LYS A 268 3391 5150 4565 171 43 752 N ATOM 799 N LEU A 269 -10.737 33.088 -2.292 1.00 27.43 N ANISOU 799 N LEU A 269 2904 4012 3507 285 181 573 N ATOM 800 CA LEU A 269 -9.358 32.609 -2.386 1.00 25.06 C ANISOU 800 CA LEU A 269 2675 3600 3245 228 163 555 C ATOM 801 C LEU A 269 -8.705 32.600 -1.000 1.00 24.41 C ANISOU 801 C LEU A 269 2608 3538 3128 225 200 580 C ATOM 802 O LEU A 269 -8.019 31.652 -0.622 1.00 25.07 O ANISOU 802 O LEU A 269 2692 3578 3255 154 184 608 O ATOM 803 CB LEU A 269 -8.570 33.500 -3.351 1.00 24.01 C ANISOU 803 CB LEU A 269 2647 3382 3094 261 147 475 C ATOM 804 CG LEU A 269 -7.136 33.135 -3.725 1.00 34.14 C ANISOU 804 CG LEU A 269 3996 4573 4400 210 126 440 C ATOM 805 CD1 LEU A 269 -7.076 31.811 -4.480 1.00 26.89 C ANISOU 805 CD1 LEU A 269 3036 3615 3565 143 76 448 C ATOM 806 CD2 LEU A 269 -6.550 34.258 -4.571 1.00 39.43 C ANISOU 806 CD2 LEU A 269 4758 5200 5023 239 113 376 C ATOM 807 N LYS A 270 -8.954 33.648 -0.226 1.00 22.47 N ANISOU 807 N LYS A 270 2377 3358 2804 311 240 569 N ATOM 808 CA LYS A 270 -8.403 33.731 1.128 1.00 22.98 C ANISOU 808 CA LYS A 270 2455 3446 2829 320 277 592 C ATOM 809 C LYS A 270 -8.927 32.591 1.994 1.00 24.39 C ANISOU 809 C LYS A 270 2528 3709 3032 245 286 679 C ATOM 810 O LYS A 270 -8.171 31.963 2.736 1.00 25.49 O ANISOU 810 O LYS A 270 2683 3811 3192 186 288 709 O ATOM 811 CB LYS A 270 -8.724 35.088 1.760 1.00 26.11 C ANISOU 811 CB LYS A 270 2885 3907 3130 444 303 559 C ATOM 812 CG LYS A 270 -8.231 35.252 3.199 1.00 26.92 C ANISOU 812 CG LYS A 270 3002 4042 3186 468 341 583 C ATOM 813 CD LYS A 270 -9.285 34.825 4.197 1.00 29.48 C ANISOU 813 CD LYS A 270 3196 4530 3474 474 376 645 C ATOM 814 CE LYS A 270 -10.479 35.758 4.186 1.00 40.46 C ANISOU 814 CE LYS A 270 4537 6051 4783 599 380 613 C ATOM 815 NZ LYS A 270 -11.479 35.390 5.234 1.00 37.75 N ANISOU 815 NZ LYS A 270 4052 5908 4384 609 419 673 N ATOM 816 N ASN A 271 -10.221 32.314 1.883 1.00 24.65 N ANISOU 816 N ASN A 271 2453 3855 3057 239 284 723 N ATOM 817 CA ASN A 271 -10.832 31.213 2.619 1.00 27.56 C ANISOU 817 CA ASN A 271 2713 4320 3439 145 278 822 C ATOM 818 C ASN A 271 -10.294 29.843 2.219 1.00 29.41 C ANISOU 818 C ASN A 271 2962 4443 3768 16 209 861 C ATOM 819 O ASN A 271 -9.996 29.013 3.086 1.00 25.87 O ANISOU 819 O ASN A 271 2496 3998 3333 -68 191 923 O ATOM 820 CB ASN A 271 -12.355 31.261 2.476 1.00 30.01 C ANISOU 820 CB ASN A 271 2898 4792 3711 162 284 864 C ATOM 821 CG ASN A 271 -12.973 32.368 3.302 1.00 35.71 C ANISOU 821 CG ASN A 271 3576 5671 4321 288 342 839 C ATOM 822 OD1 ASN A 271 -12.367 32.840 4.262 1.00 36.36 O ANISOU 822 OD1 ASN A 271 3701 5759 4355 336 377 822 O ATOM 823 ND2 ASN A 271 -14.172 32.795 2.931 1.00 35.59 N ANISOU 823 ND2 ASN A 271 3478 5784 4261 352 347 829 N ATOM 824 N PHE A 272 -10.157 29.605 0.915 1.00 22.11 N ANISOU 824 N PHE A 272 2076 3420 2906 5 160 821 N ATOM 825 CA PHE A 272 -9.656 28.320 0.446 1.00 23.95 C ANISOU 825 CA PHE A 272 2330 3545 3225 -94 76 842 C ATOM 826 C PHE A 272 -8.260 28.038 0.991 1.00 26.74 C ANISOU 826 C PHE A 272 2766 3800 3594 -114 66 810 C ATOM 827 O PHE A 272 -7.989 26.956 1.525 1.00 29.21 O ANISOU 827 O PHE A 272 3075 4080 3944 -202 8 861 O ATOM 828 CB PHE A 272 -9.594 28.269 -1.084 1.00 23.15 C ANISOU 828 CB PHE A 272 2265 3354 3175 -77 29 782 C ATOM 829 CG PHE A 272 -10.941 28.239 -1.758 1.00 22.30 C ANISOU 829 CG PHE A 272 2080 3317 3076 -79 14 819 C ATOM 830 CD1 PHE A 272 -12.097 28.060 -1.025 1.00 24.28 C ANISOU 830 CD1 PHE A 272 2223 3711 3290 -113 30 909 C ATOM 831 CD2 PHE A 272 -11.033 28.354 -3.142 1.00 27.92 C ANISOU 831 CD2 PHE A 272 2821 3959 3827 -53 -18 765 C ATOM 832 CE1 PHE A 272 -13.337 28.023 -1.656 1.00 27.79 C ANISOU 832 CE1 PHE A 272 2589 4231 3737 -116 16 944 C ATOM 833 CE2 PHE A 272 -12.263 28.313 -3.776 1.00 26.25 C ANISOU 833 CE2 PHE A 272 2541 3805 3627 -56 -34 798 C ATOM 834 CZ PHE A 272 -13.409 28.144 -3.033 1.00 26.70 C ANISOU 834 CZ PHE A 272 2492 4005 3649 -87 -17 888 C ATOM 835 N ILE A 273 -7.374 29.012 0.834 1.00 23.54 N ANISOU 835 N ILE A 273 2440 3346 3157 -36 113 728 N ATOM 836 CA ILE A 273 -5.987 28.869 1.283 1.00 25.59 C ANISOU 836 CA ILE A 273 2779 3519 3423 -46 110 690 C ATOM 837 C ILE A 273 -5.906 28.761 2.805 1.00 26.18 C ANISOU 837 C ILE A 273 2837 3642 3467 -70 145 747 C ATOM 838 O ILE A 273 -5.243 27.868 3.342 1.00 27.95 O ANISOU 838 O ILE A 273 3083 3809 3727 -136 102 766 O ATOM 839 CB ILE A 273 -5.117 30.037 0.778 1.00 23.91 C ANISOU 839 CB ILE A 273 2651 3264 3170 31 149 603 C ATOM 840 CG1 ILE A 273 -4.967 29.967 -0.746 1.00 21.23 C ANISOU 840 CG1 ILE A 273 2331 2872 2863 36 103 545 C ATOM 841 CG2 ILE A 273 -3.733 29.991 1.407 1.00 22.91 C ANISOU 841 CG2 ILE A 273 2595 3074 3036 23 156 573 C ATOM 842 CD1 ILE A 273 -4.267 31.165 -1.353 1.00 22.90 C ANISOU 842 CD1 ILE A 273 2617 3062 3021 91 131 475 C ATOM 843 N SER A 274 -6.597 29.654 3.506 1.00 22.65 N ANISOU 843 N SER A 274 2352 3305 2948 -11 214 772 N ATOM 844 CA SER A 274 -6.538 29.645 4.972 1.00 29.69 C ANISOU 844 CA SER A 274 3224 4259 3799 -23 254 823 C ATOM 845 C SER A 274 -6.939 28.296 5.536 1.00 32.39 C ANISOU 845 C SER A 274 3497 4630 4178 -148 200 916 C ATOM 846 O SER A 274 -6.279 27.766 6.432 1.00 27.37 O ANISOU 846 O SER A 274 2889 3956 3554 -203 187 942 O ATOM 847 CB SER A 274 -7.424 30.737 5.562 1.00 30.25 C ANISOU 847 CB SER A 274 3244 4470 3778 72 323 831 C ATOM 848 OG SER A 274 -6.900 32.012 5.258 1.00 35.46 O ANISOU 848 OG SER A 274 3994 5083 4396 181 352 750 O ATOM 849 N SER A 275 -8.029 27.747 5.008 1.00 27.44 N ANISOU 849 N SER A 275 2787 4069 3570 -199 159 970 N ATOM 850 CA SER A 275 -8.569 26.483 5.488 1.00 28.44 C ANISOU 850 CA SER A 275 2847 4236 3723 -335 87 1077 C ATOM 851 C SER A 275 -7.584 25.337 5.307 1.00 31.26 C ANISOU 851 C SER A 275 3285 4430 4163 -419 -18 1067 C ATOM 852 O SER A 275 -7.647 24.335 6.022 1.00 36.32 O ANISOU 852 O SER A 275 3909 5071 4821 -535 -88 1148 O ATOM 853 CB SER A 275 -9.873 26.148 4.753 1.00 32.85 C ANISOU 853 CB SER A 275 3312 4882 4288 -373 50 1133 C ATOM 854 OG SER A 275 -9.606 25.674 3.444 1.00 32.32 O ANISOU 854 OG SER A 275 3299 4681 4300 -381 -27 1087 O ATOM 855 N GLN A 276 -6.677 25.480 4.349 1.00 25.10 N ANISOU 855 N GLN A 276 2591 3519 3426 -361 -38 966 N ATOM 856 CA GLN A 276 -5.761 24.394 4.012 1.00 27.60 C ANISOU 856 CA GLN A 276 2979 3691 3815 -415 -151 934 C ATOM 857 C GLN A 276 -4.298 24.831 4.110 1.00 26.49 C ANISOU 857 C GLN A 276 2933 3459 3672 -349 -118 834 C ATOM 858 O GLN A 276 -3.419 24.255 3.476 1.00 28.24 O ANISOU 858 O GLN A 276 3215 3573 3940 -345 -194 764 O ATOM 859 CB GLN A 276 -6.069 23.902 2.603 1.00 33.13 C ANISOU 859 CB GLN A 276 3682 4336 4571 -415 -234 905 C ATOM 860 CG GLN A 276 -5.867 22.411 2.420 1.00 54.96 C ANISOU 860 CG GLN A 276 6479 6997 7405 -507 -397 930 C ATOM 861 CD GLN A 276 -6.909 21.576 3.152 1.00 59.84 C ANISOU 861 CD GLN A 276 7033 7681 8024 -640 -467 1073 C ATOM 862 OE1 GLN A 276 -6.893 21.471 4.376 1.00 56.14 O ANISOU 862 OE1 GLN A 276 6547 7261 7522 -701 -447 1138 O ATOM 863 NE2 GLN A 276 -7.811 20.965 2.398 1.00 66.55 N ANISOU 863 NE2 GLN A 276 7845 8535 8906 -692 -556 1127 N ATOM 864 N MET A 277 -4.039 25.842 4.921 1.00 27.82 N ANISOU 864 N MET A 277 2795 4319 3455 -10 -613 841 N ATOM 865 CA MET A 277 -2.724 26.484 4.940 1.00 25.83 C ANISOU 865 CA MET A 277 2590 4019 3207 46 -530 735 C ATOM 866 C MET A 277 -1.534 25.541 5.158 1.00 28.30 C ANISOU 866 C MET A 277 2953 4261 3538 18 -612 711 C ATOM 867 O MET A 277 -0.567 25.571 4.395 1.00 28.90 O ANISOU 867 O MET A 277 3097 4247 3636 74 -609 629 O ATOM 868 CB MET A 277 -2.706 27.603 5.979 1.00 25.62 C ANISOU 868 CB MET A 277 2496 4096 3142 55 -405 698 C ATOM 869 CG MET A 277 -1.434 28.435 5.962 1.00 26.84 C ANISOU 869 CG MET A 277 2696 4199 3301 119 -312 593 C ATOM 870 SD MET A 277 -1.285 29.377 4.427 1.00 32.59 S ANISOU 870 SD MET A 277 3497 4836 4049 213 -259 523 S ATOM 871 CE MET A 277 0.096 30.457 4.806 1.00 33.85 C ANISOU 871 CE MET A 277 3682 4979 4199 263 -148 421 C ATOM 872 N THR A 278 -1.580 24.722 6.205 1.00 28.82 N ANISOU 872 N THR A 278 2983 4374 3593 -73 -691 775 N ATOM 873 CA THR A 278 -0.424 23.879 6.514 1.00 32.92 C ANISOU 873 CA THR A 278 3552 4821 4136 -101 -779 739 C ATOM 874 C THR A 278 -0.153 22.897 5.385 1.00 30.37 C ANISOU 874 C THR A 278 3299 4382 3859 -75 -921 726 C ATOM 875 O THR A 278 0.974 22.782 4.908 1.00 35.94 O ANISOU 875 O THR A 278 4062 5006 4586 -22 -934 624 O ATOM 876 CB THR A 278 -0.601 23.096 7.814 1.00 32.04 C ANISOU 876 CB THR A 278 3397 4773 4005 -220 -866 823 C ATOM 877 OG1 THR A 278 -0.710 24.014 8.907 1.00 35.15 O ANISOU 877 OG1 THR A 278 3721 5284 4352 -235 -731 818 O ATOM 878 CG2 THR A 278 0.598 22.197 8.038 1.00 29.11 C ANISOU 878 CG2 THR A 278 3089 4304 3668 -244 -981 774 C ATOM 879 N ASP A 279 -1.201 22.207 4.956 1.00 28.58 N ANISOU 879 N ASP A 279 3061 4154 3646 -108 -1030 823 N ATOM 880 CA ASP A 279 -1.106 21.250 3.856 1.00 35.45 C ANISOU 880 CA ASP A 279 3988 4917 4563 -75 -1182 818 C ATOM 881 C ASP A 279 -0.558 21.879 2.576 1.00 35.73 C ANISOU 881 C ASP A 279 4074 4890 4610 39 -1103 708 C ATOM 882 O ASP A 279 0.240 21.271 1.867 1.00 35.74 O ANISOU 882 O ASP A 279 4126 4812 4641 84 -1194 634 O ATOM 883 CB ASP A 279 -2.469 20.616 3.584 1.00 41.91 C ANISOU 883 CB ASP A 279 4780 5752 5393 -121 -1288 949 C ATOM 884 CG ASP A 279 -2.908 19.673 4.697 1.00 59.17 C ANISOU 884 CG ASP A 279 6925 7989 7568 -253 -1423 1068 C ATOM 885 OD1 ASP A 279 -2.030 19.111 5.391 1.00 54.90 O ANISOU 885 OD1 ASP A 279 6404 7420 7034 -301 -1503 1043 O ATOM 886 OD2 ASP A 279 -4.132 19.493 4.875 1.00 66.52 O ANISOU 886 OD2 ASP A 279 7804 8989 8480 -315 -1454 1187 O ATOM 887 N MET A 280 -0.983 23.098 2.278 1.00 27.28 N ANISOU 887 N MET A 280 2988 3864 3514 84 -944 692 N ATOM 888 CA MET A 280 -0.500 23.775 1.080 1.00 18.60 C ANISOU 888 CA MET A 280 1937 2714 2416 174 -868 600 C ATOM 889 C MET A 280 0.969 24.196 1.225 1.00 25.21 C ANISOU 889 C MET A 280 2802 3538 3237 205 -797 479 C ATOM 890 O MET A 280 1.771 24.045 0.297 1.00 26.83 O ANISOU 890 O MET A 280 3053 3692 3448 259 -819 392 O ATOM 891 CB MET A 280 -1.384 24.976 0.766 1.00 19.73 C ANISOU 891 CB MET A 280 2060 2898 2539 202 -740 620 C ATOM 892 CG MET A 280 -2.753 24.580 0.213 1.00 22.05 C ANISOU 892 CG MET A 280 2342 3183 2854 194 -811 714 C ATOM 893 SD MET A 280 -3.716 26.010 -0.329 1.00 25.23 S ANISOU 893 SD MET A 280 2734 3611 3242 239 -679 708 S ATOM 894 CE MET A 280 -2.956 26.374 -1.910 1.00 25.51 C ANISOU 894 CE MET A 280 2858 3549 3285 319 -657 618 C ATOM 895 N CYS A 281 1.330 24.713 2.393 1.00 26.00 N ANISOU 895 N CYS A 281 2871 3692 3317 173 -714 470 N ATOM 896 CA CYS A 281 2.706 25.166 2.605 1.00 27.22 C ANISOU 896 CA CYS A 281 3050 3832 3458 202 -641 360 C ATOM 897 C CYS A 281 3.716 24.037 2.422 1.00 33.09 C ANISOU 897 C CYS A 281 3833 4512 4229 204 -771 290 C ATOM 898 O CYS A 281 4.785 24.233 1.841 1.00 31.48 O ANISOU 898 O CYS A 281 3662 4281 4016 254 -741 178 O ATOM 899 CB CYS A 281 2.866 25.796 3.987 1.00 24.01 C ANISOU 899 CB CYS A 281 2602 3489 3033 168 -547 370 C ATOM 900 SG CYS A 281 2.157 27.434 4.082 1.00 32.62 S ANISOU 900 SG CYS A 281 3653 4650 4091 203 -382 384 S ATOM 901 N LEU A 282 3.364 22.854 2.912 1.00 25.16 N ANISOU 901 N LEU A 282 2820 3487 3253 145 -928 354 N ATOM 902 CA LEU A 282 4.255 21.708 2.860 1.00 25.36 C ANISOU 902 CA LEU A 282 2880 3444 3312 143 -1087 286 C ATOM 903 C LEU A 282 4.264 21.027 1.491 1.00 36.40 C ANISOU 903 C LEU A 282 4308 4787 4733 204 -1205 243 C ATOM 904 O LEU A 282 5.136 20.204 1.213 1.00 41.94 O ANISOU 904 O LEU A 282 5037 5438 5461 229 -1333 148 O ATOM 905 CB LEU A 282 3.878 20.688 3.946 1.00 32.47 C ANISOU 905 CB LEU A 282 3764 4338 4235 45 -1237 378 C ATOM 906 CG LEU A 282 4.001 21.154 5.400 1.00 29.88 C ANISOU 906 CG LEU A 282 3404 4068 3883 -23 -1148 411 C ATOM 907 CD1 LEU A 282 3.413 20.119 6.346 1.00 32.55 C ANISOU 907 CD1 LEU A 282 3723 4414 4233 -139 -1308 527 C ATOM 908 CD2 LEU A 282 5.452 21.455 5.762 1.00 22.50 C ANISOU 908 CD2 LEU A 282 2499 3100 2950 11 -1089 276 C ATOM 909 N ASP A 283 3.295 21.363 0.639 1.00 30.42 N ANISOU 909 N ASP A 283 3546 4042 3970 231 -1170 305 N ATOM 910 CA ASP A 283 3.240 20.785 -0.699 1.00 27.59 C ANISOU 910 CA ASP A 283 3215 3636 3633 295 -1273 268 C ATOM 911 C ASP A 283 4.263 21.443 -1.604 1.00 32.60 C ANISOU 911 C ASP A 283 3871 4283 4234 369 -1173 129 C ATOM 912 O ASP A 283 4.400 22.670 -1.631 1.00 30.48 O ANISOU 912 O ASP A 283 3600 4058 3922 377 -994 113 O ATOM 913 CB ASP A 283 1.859 20.939 -1.328 1.00 27.96 C ANISOU 913 CB ASP A 283 3254 3684 3687 300 -1267 380 C ATOM 914 CG ASP A 283 1.743 20.189 -2.640 1.00 27.22 C ANISOU 914 CG ASP A 283 3187 3534 3622 366 -1398 352 C ATOM 915 OD1 ASP A 283 1.832 20.825 -3.709 1.00 24.77 O ANISOU 915 OD1 ASP A 283 2895 3230 3289 428 -1311 298 O ATOM 916 OD2 ASP A 283 1.597 18.954 -2.596 1.00 33.54 O ANISOU 916 OD2 ASP A 283 3996 4277 4471 350 -1587 377 O ATOM 917 N LYS A 284 4.943 20.605 -2.372 1.00 26.38 N ANISOU 917 N LYS A 284 3099 3462 3461 421 -1303 30 N ATOM 918 CA LYS A 284 6.030 21.012 -3.251 1.00 33.73 C ANISOU 918 CA LYS A 284 4040 4423 4352 485 -1237 -118 C ATOM 919 C LYS A 284 5.595 21.990 -4.340 1.00 30.03 C ANISOU 919 C LYS A 284 3580 3989 3840 517 -1105 -102 C ATOM 920 O LYS A 284 6.422 22.722 -4.877 1.00 34.15 O ANISOU 920 O LYS A 284 4106 4559 4308 541 -996 -196 O ATOM 921 CB LYS A 284 6.638 19.755 -3.883 1.00 44.03 C ANISOU 921 CB LYS A 284 5348 5695 5687 540 -1440 -226 C ATOM 922 CG LYS A 284 7.735 19.982 -4.900 1.00 53.96 C ANISOU 922 CG LYS A 284 6601 7007 6896 609 -1400 -392 C ATOM 923 CD LYS A 284 8.178 18.647 -5.478 1.00 65.23 C ANISOU 923 CD LYS A 284 8019 8405 8359 672 -1630 -502 C ATOM 924 CE LYS A 284 9.323 18.802 -6.464 1.00 72.10 C ANISOU 924 CE LYS A 284 8868 9356 9170 741 -1600 -687 C ATOM 925 NZ LYS A 284 9.769 17.477 -6.986 1.00 74.86 N ANISOU 925 NZ LYS A 284 9211 9671 9564 814 -1818 -816 N ATOM 926 N PHE A 285 4.311 21.992 -4.686 1.00 23.01 N ANISOU 926 N PHE A 285 2695 3075 2973 512 -1123 17 N ATOM 927 CA PHE A 285 3.837 22.901 -5.731 1.00 18.73 C ANISOU 927 CA PHE A 285 2170 2550 2397 537 -1014 34 C ATOM 928 C PHE A 285 2.916 23.982 -5.179 1.00 20.23 C ANISOU 928 C PHE A 285 2355 2751 2579 494 -880 140 C ATOM 929 O PHE A 285 2.974 25.129 -5.613 1.00 23.42 O ANISOU 929 O PHE A 285 2775 3182 2942 497 -748 125 O ATOM 930 CB PHE A 285 3.152 22.134 -6.880 1.00 21.68 C ANISOU 930 CB PHE A 285 2557 2881 2800 587 -1141 58 C ATOM 931 CG PHE A 285 4.005 21.044 -7.449 1.00 21.89 C ANISOU 931 CG PHE A 285 2578 2903 2837 644 -1294 -58 C ATOM 932 CD1 PHE A 285 5.139 21.353 -8.180 1.00 29.23 C ANISOU 932 CD1 PHE A 285 3503 3894 3708 683 -1241 -200 C ATOM 933 CD2 PHE A 285 3.711 19.713 -7.204 1.00 29.49 C ANISOU 933 CD2 PHE A 285 3533 3806 3865 655 -1502 -30 C ATOM 934 CE1 PHE A 285 5.961 20.342 -8.679 1.00 31.62 C ANISOU 934 CE1 PHE A 285 3789 4209 4017 744 -1391 -331 C ATOM 935 CE2 PHE A 285 4.517 18.708 -7.711 1.00 34.65 C ANISOU 935 CE2 PHE A 285 4182 4450 4535 715 -1659 -157 C ATOM 936 CZ PHE A 285 5.640 19.028 -8.447 1.00 33.75 C ANISOU 936 CZ PHE A 285 4054 4410 4361 767 -1608 -312 C ATOM 937 N ALA A 286 2.064 23.626 -4.227 1.00 19.11 N ANISOU 937 N ALA A 286 2190 2597 2473 449 -925 243 N ATOM 938 CA ALA A 286 1.116 24.615 -3.700 1.00 23.97 C ANISOU 938 CA ALA A 286 2788 3239 3080 416 -811 329 C ATOM 939 C ALA A 286 1.848 25.714 -2.912 1.00 18.11 C ANISOU 939 C ALA A 286 2034 2547 2299 398 -664 281 C ATOM 940 O ALA A 286 1.330 26.809 -2.731 1.00 18.78 O ANISOU 940 O ALA A 286 2110 2657 2367 391 -556 311 O ATOM 941 CB ALA A 286 0.056 23.947 -2.845 1.00 24.69 C ANISOU 941 CB ALA A 286 2842 3331 3206 366 -894 445 C ATOM 942 N CYS A 287 3.062 25.433 -2.449 1.00 17.85 N ANISOU 942 N CYS A 287 2002 2524 2257 396 -671 199 N ATOM 943 CA CYS A 287 3.833 26.469 -1.743 1.00 17.48 C ANISOU 943 CA CYS A 287 1948 2517 2177 386 -536 150 C ATOM 944 C CYS A 287 4.033 27.711 -2.634 1.00 17.01 C ANISOU 944 C CYS A 287 1916 2472 2076 412 -419 113 C ATOM 945 O CYS A 287 4.039 28.844 -2.148 1.00 18.58 O ANISOU 945 O CYS A 287 2107 2696 2256 403 -310 121 O ATOM 946 CB CYS A 287 5.189 25.916 -1.295 1.00 25.19 C ANISOU 946 CB CYS A 287 2929 3490 3152 387 -569 52 C ATOM 947 SG CYS A 287 6.113 25.206 -2.677 1.00 30.18 S ANISOU 947 SG CYS A 287 3589 4108 3769 439 -654 -68 S ATOM 948 N TYR A 288 4.164 27.505 -3.941 1.00 18.09 N ANISOU 948 N TYR A 288 2083 2593 2197 441 -455 76 N ATOM 949 CA TYR A 288 4.317 28.632 -4.862 1.00 17.14 C ANISOU 949 CA TYR A 288 1994 2488 2032 448 -362 52 C ATOM 950 C TYR A 288 3.054 29.455 -5.004 1.00 17.97 C ANISOU 950 C TYR A 288 2106 2573 2150 440 -323 139 C ATOM 951 O TYR A 288 3.115 30.665 -5.244 1.00 17.74 O ANISOU 951 O TYR A 288 2097 2552 2091 431 -239 134 O ATOM 952 CB TYR A 288 4.765 28.135 -6.242 1.00 17.73 C ANISOU 952 CB TYR A 288 2092 2565 2079 476 -416 -12 C ATOM 953 CG TYR A 288 6.133 27.499 -6.169 1.00 17.52 C ANISOU 953 CG TYR A 288 2052 2575 2030 489 -447 -127 C ATOM 954 CD1 TYR A 288 7.258 28.276 -5.975 1.00 25.46 C ANISOU 954 CD1 TYR A 288 3058 3630 2984 473 -348 -200 C ATOM 955 CD2 TYR A 288 6.290 26.123 -6.276 1.00 21.37 C ANISOU 955 CD2 TYR A 288 2526 3044 2551 520 -588 -168 C ATOM 956 CE1 TYR A 288 8.516 27.702 -5.880 1.00 23.56 C ANISOU 956 CE1 TYR A 288 2801 3427 2725 487 -376 -318 C ATOM 957 CE2 TYR A 288 7.540 25.539 -6.196 1.00 18.71 C ANISOU 957 CE2 TYR A 288 2174 2739 2197 538 -631 -292 C ATOM 958 CZ TYR A 288 8.647 26.337 -6.000 1.00 26.20 C ANISOU 958 CZ TYR A 288 3120 3744 3093 522 -519 -370 C ATOM 959 OH TYR A 288 9.895 25.765 -5.916 1.00 28.89 O ANISOU 959 OH TYR A 288 3441 4119 3415 543 -561 -506 O ATOM 960 N VAL A 289 1.912 28.787 -4.881 1.00 22.62 N ANISOU 960 N VAL A 289 2678 3132 2783 442 -399 216 N ATOM 961 CA VAL A 289 0.626 29.480 -4.872 1.00 19.77 C ANISOU 961 CA VAL A 289 2314 2758 2440 437 -372 290 C ATOM 962 C VAL A 289 0.507 30.355 -3.630 1.00 18.67 C ANISOU 962 C VAL A 289 2134 2661 2297 418 -292 303 C ATOM 963 O VAL A 289 0.058 31.494 -3.719 1.00 20.78 O ANISOU 963 O VAL A 289 2409 2930 2557 422 -234 308 O ATOM 964 CB VAL A 289 -0.550 28.493 -4.952 1.00 20.88 C ANISOU 964 CB VAL A 289 2439 2868 2628 439 -474 370 C ATOM 965 CG1 VAL A 289 -1.897 29.217 -4.731 1.00 21.95 C ANISOU 965 CG1 VAL A 289 2555 3004 2780 432 -443 435 C ATOM 966 CG2 VAL A 289 -0.544 27.775 -6.285 1.00 17.74 C ANISOU 966 CG2 VAL A 289 2082 2420 2238 472 -556 356 C ATOM 967 N ILE A 290 0.923 29.824 -2.479 1.00 20.98 N ANISOU 967 N ILE A 290 2387 2990 2597 399 -301 302 N ATOM 968 CA ILE A 290 0.963 30.616 -1.254 1.00 18.58 C ANISOU 968 CA ILE A 290 2040 2737 2285 387 -224 303 C ATOM 969 C ILE A 290 1.903 31.818 -1.384 1.00 18.58 C ANISOU 969 C ILE A 290 2067 2740 2254 403 -131 237 C ATOM 970 O ILE A 290 1.533 32.954 -1.069 1.00 18.67 O ANISOU 970 O ILE A 290 2065 2768 2261 413 -75 241 O ATOM 971 CB ILE A 290 1.433 29.791 -0.045 1.00 19.50 C ANISOU 971 CB ILE A 290 2116 2885 2409 358 -253 308 C ATOM 972 CG1 ILE A 290 0.567 28.546 0.128 1.00 23.71 C ANISOU 972 CG1 ILE A 290 2624 3416 2970 327 -366 385 C ATOM 973 CG2 ILE A 290 1.369 30.633 1.216 1.00 19.26 C ANISOU 973 CG2 ILE A 290 2034 2915 2368 351 -173 311 C ATOM 974 CD1 ILE A 290 -0.845 28.864 0.435 1.00 32.82 C ANISOU 974 CD1 ILE A 290 3729 4611 4129 313 -360 462 C ATOM 975 N GLN A 291 3.118 31.577 -1.847 1.00 16.68 N ANISOU 975 N GLN A 291 1861 2487 1990 405 -125 171 N ATOM 976 CA GLN A 291 4.079 32.669 -1.968 1.00 16.71 C ANISOU 976 CA GLN A 291 1889 2500 1958 409 -43 115 C ATOM 977 C GLN A 291 3.586 33.775 -2.907 1.00 19.98 C ANISOU 977 C GLN A 291 2341 2894 2355 409 -19 131 C ATOM 978 O GLN A 291 3.708 34.958 -2.606 1.00 18.58 O ANISOU 978 O GLN A 291 2168 2723 2169 410 33 125 O ATOM 979 CB GLN A 291 5.417 32.134 -2.461 1.00 16.85 C ANISOU 979 CB GLN A 291 1933 2524 1946 407 -48 36 C ATOM 980 CG GLN A 291 6.116 31.285 -1.412 1.00 18.17 C ANISOU 980 CG GLN A 291 2071 2700 2132 405 -69 1 C ATOM 981 CD GLN A 291 7.395 30.681 -1.928 1.00 29.94 C ANISOU 981 CD GLN A 291 3581 4199 3597 411 -91 -96 C ATOM 982 OE1 GLN A 291 7.660 29.505 -1.722 1.00 40.55 O ANISOU 982 OE1 GLN A 291 4914 5529 4963 415 -176 -127 O ATOM 983 NE2 GLN A 291 8.198 31.487 -2.601 1.00 30.76 N ANISOU 983 NE2 GLN A 291 3709 4328 3650 408 -25 -149 N ATOM 984 N SER A 292 3.030 33.402 -4.048 1.00 17.04 N ANISOU 984 N SER A 292 2000 2491 1982 409 -70 150 N ATOM 985 CA SER A 292 2.597 34.434 -4.989 1.00 19.41 C ANISOU 985 CA SER A 292 2347 2762 2267 400 -59 164 C ATOM 986 C SER A 292 1.392 35.184 -4.436 1.00 18.91 C ANISOU 986 C SER A 292 2260 2684 2239 413 -61 209 C ATOM 987 O SER A 292 1.270 36.393 -4.628 1.00 22.72 O ANISOU 987 O SER A 292 2769 3149 2715 408 -44 204 O ATOM 988 CB SER A 292 2.297 33.847 -6.376 1.00 30.22 C ANISOU 988 CB SER A 292 3757 4099 3625 398 -114 171 C ATOM 989 OG SER A 292 1.347 32.812 -6.301 1.00 38.93 O ANISOU 989 OG SER A 292 4838 5179 4775 420 -181 216 O ATOM 990 N SER A 293 0.529 34.481 -3.707 1.00 17.96 N ANISOU 990 N SER A 293 2088 2579 2156 426 -91 247 N ATOM 991 CA SER A 293 -0.621 35.125 -3.067 1.00 17.16 C ANISOU 991 CA SER A 293 1945 2492 2084 441 -93 275 C ATOM 992 C SER A 293 -0.208 36.126 -1.984 1.00 20.15 C ANISOU 992 C SER A 293 2287 2915 2456 454 -38 243 C ATOM 993 O SER A 293 -0.784 37.207 -1.882 1.00 20.13 O ANISOU 993 O SER A 293 2277 2908 2463 473 -41 232 O ATOM 994 CB SER A 293 -1.578 34.080 -2.481 1.00 24.42 C ANISOU 994 CB SER A 293 2806 3442 3032 439 -137 328 C ATOM 995 OG SER A 293 -2.123 33.275 -3.512 1.00 22.63 O ANISOU 995 OG SER A 293 2615 3164 2821 438 -200 362 O ATOM 996 N LEU A 294 0.789 35.764 -1.182 1.00 17.70 N ANISOU 996 N LEU A 294 1953 2641 2132 448 0 221 N ATOM 997 CA LEU A 294 1.261 36.637 -0.110 1.00 18.23 C ANISOU 997 CA LEU A 294 1985 2747 2197 467 51 190 C ATOM 998 C LEU A 294 1.749 37.965 -0.655 1.00 17.00 C ANISOU 998 C LEU A 294 1880 2554 2027 474 67 159 C ATOM 999 O LEU A 294 1.500 39.010 -0.064 1.00 19.23 O ANISOU 999 O LEU A 294 2136 2850 2321 503 71 142 O ATOM 1000 CB LEU A 294 2.397 35.964 0.667 1.00 17.12 C ANISOU 1000 CB LEU A 294 1828 2631 2045 457 85 168 C ATOM 1001 CG LEU A 294 1.952 34.821 1.575 1.00 16.51 C ANISOU 1001 CG LEU A 294 1692 2599 1983 440 59 203 C ATOM 1002 CD1 LEU A 294 3.166 34.027 2.037 1.00 16.25 C ANISOU 1002 CD1 LEU A 294 1668 2563 1944 423 68 173 C ATOM 1003 CD2 LEU A 294 1.150 35.377 2.776 1.00 17.18 C ANISOU 1003 CD2 LEU A 294 1694 2757 2075 458 78 218 C ATOM 1004 N GLN A 295 2.445 37.932 -1.788 1.00 17.15 N ANISOU 1004 N GLN A 295 1969 2532 2016 444 65 149 N ATOM 1005 CA GLN A 295 3.034 39.165 -2.304 1.00 19.64 C ANISOU 1005 CA GLN A 295 2336 2819 2308 430 73 130 C ATOM 1006 C GLN A 295 2.133 39.936 -3.267 1.00 22.58 C ANISOU 1006 C GLN A 295 2755 3138 2688 419 14 150 C ATOM 1007 O GLN A 295 2.341 41.124 -3.504 1.00 20.18 O ANISOU 1007 O GLN A 295 2487 2805 2375 407 -6 142 O ATOM 1008 CB GLN A 295 4.404 38.901 -2.931 1.00 23.81 C ANISOU 1008 CB GLN A 295 2907 3354 2785 392 107 102 C ATOM 1009 CG GLN A 295 4.379 38.142 -4.254 1.00 31.04 C ANISOU 1009 CG GLN A 295 3864 4257 3672 361 79 107 C ATOM 1010 CD GLN A 295 5.779 37.789 -4.730 1.00 35.23 C ANISOU 1010 CD GLN A 295 4415 4826 4146 330 113 60 C ATOM 1011 OE1 GLN A 295 5.969 37.302 -5.847 1.00 33.83 O ANISOU 1011 OE1 GLN A 295 4265 4656 3930 305 94 48 O ATOM 1012 NE2 GLN A 295 6.765 38.025 -3.875 1.00 24.14 N ANISOU 1012 NE2 GLN A 295 2989 3449 2733 335 163 25 N ATOM 1013 N ASN A 296 1.120 39.271 -3.801 1.00 19.22 N ANISOU 1013 N ASN A 296 2330 2692 2281 422 -24 177 N ATOM 1014 CA ASN A 296 0.276 39.895 -4.806 1.00 22.28 C ANISOU 1014 CA ASN A 296 2771 3015 2679 409 -84 192 C ATOM 1015 C ASN A 296 -1.117 40.316 -4.325 1.00 22.03 C ANISOU 1015 C ASN A 296 2698 2974 2697 451 -131 193 C ATOM 1016 O ASN A 296 -1.650 41.315 -4.797 1.00 20.92 O ANISOU 1016 O ASN A 296 2596 2779 2572 449 -189 182 O ATOM 1017 CB ASN A 296 0.163 38.995 -6.042 1.00 23.97 C ANISOU 1017 CB ASN A 296 3032 3199 2876 382 -104 216 C ATOM 1018 CG ASN A 296 1.463 38.914 -6.823 1.00 30.27 C ANISOU 1018 CG ASN A 296 3877 4013 3612 335 -75 199 C ATOM 1019 OD1 ASN A 296 2.117 39.923 -7.063 1.00 29.88 O ANISOU 1019 OD1 ASN A 296 3865 3959 3528 298 -69 188 O ATOM 1020 ND2 ASN A 296 1.837 37.710 -7.231 1.00 24.02 N ANISOU 1020 ND2 ASN A 296 3079 3245 2801 335 -67 192 N ATOM 1021 N MET A 297 -1.708 39.554 -3.404 1.00 18.78 N ANISOU 1021 N MET A 297 2207 2621 2309 482 -116 202 N ATOM 1022 CA MET A 297 -3.049 39.864 -2.922 1.00 20.64 C ANISOU 1022 CA MET A 297 2386 2875 2583 519 -156 194 C ATOM 1023 C MET A 297 -3.054 41.197 -2.217 1.00 23.29 C ANISOU 1023 C MET A 297 2693 3227 2929 555 -173 142 C ATOM 1024 O MET A 297 -2.007 41.668 -1.792 1.00 20.25 O ANISOU 1024 O MET A 297 2314 2854 2526 554 -140 125 O ATOM 1025 CB MET A 297 -3.528 38.801 -1.933 1.00 19.19 C ANISOU 1025 CB MET A 297 2111 2777 2405 529 -132 219 C ATOM 1026 CG MET A 297 -3.940 37.482 -2.557 1.00 28.68 C ANISOU 1026 CG MET A 297 3327 3958 3611 505 -152 274 C ATOM 1027 SD MET A 297 -4.606 36.411 -1.239 1.00 37.18 S ANISOU 1027 SD MET A 297 4289 5147 4691 500 -146 314 S ATOM 1028 CE MET A 297 -6.194 37.187 -0.949 1.00 74.76 C ANISOU 1028 CE MET A 297 8982 9948 9474 535 -183 290 C ATOM 1029 N ASP A 298 -4.231 41.808 -2.095 1.00 19.12 N ANISOU 1029 N ASP A 298 2132 2698 2434 591 -234 111 N ATOM 1030 CA ASP A 298 -4.366 43.001 -1.284 1.00 21.99 C ANISOU 1030 CA ASP A 298 2447 3093 2815 642 -269 47 C ATOM 1031 C ASP A 298 -3.771 42.683 0.082 1.00 21.48 C ANISOU 1031 C ASP A 298 2294 3136 2731 665 -196 40 C ATOM 1032 O ASP A 298 -3.994 41.613 0.634 1.00 20.50 O ANISOU 1032 O ASP A 298 2108 3086 2594 654 -148 72 O ATOM 1033 CB ASP A 298 -5.832 43.405 -1.131 1.00 21.41 C ANISOU 1033 CB ASP A 298 2317 3040 2776 688 -341 -1 C ATOM 1034 CG ASP A 298 -6.445 43.882 -2.441 1.00 26.85 C ANISOU 1034 CG ASP A 298 3102 3607 3494 670 -428 -6 C ATOM 1035 OD1 ASP A 298 -5.706 44.407 -3.292 1.00 23.89 O ANISOU 1035 OD1 ASP A 298 2830 3138 3111 630 -454 10 O ATOM 1036 OD2 ASP A 298 -7.664 43.734 -2.614 1.00 27.01 O ANISOU 1036 OD2 ASP A 298 3093 3627 3540 691 -472 -26 O ATOM 1037 N LEU A 299 -3.017 43.621 0.624 1.00 18.72 N ANISOU 1037 N LEU A 299 1941 2789 2382 693 -197 3 N ATOM 1038 CA LEU A 299 -2.285 43.339 1.855 1.00 19.37 C ANISOU 1038 CA LEU A 299 1954 2957 2448 713 -124 -2 C ATOM 1039 C LEU A 299 -3.199 42.864 2.989 1.00 19.36 C ANISOU 1039 C LEU A 299 1826 3084 2445 746 -107 -18 C ATOM 1040 O LEU A 299 -2.871 41.917 3.708 1.00 18.94 O ANISOU 1040 O LEU A 299 1726 3101 2369 723 -41 16 O ATOM 1041 CB LEU A 299 -1.473 44.560 2.269 1.00 21.72 C ANISOU 1041 CB LEU A 299 2266 3233 2756 751 -146 -44 C ATOM 1042 CG LEU A 299 -0.657 44.394 3.549 1.00 20.96 C ANISOU 1042 CG LEU A 299 2105 3212 2648 779 -73 -54 C ATOM 1043 CD1 LEU A 299 0.283 43.192 3.443 1.00 18.37 C ANISOU 1043 CD1 LEU A 299 1811 2879 2289 718 15 -2 C ATOM 1044 CD2 LEU A 299 0.134 45.665 3.805 1.00 24.20 C ANISOU 1044 CD2 LEU A 299 2539 3580 3074 819 -109 -91 C ATOM 1045 N SER A 300 -4.350 43.506 3.149 1.00 19.68 N ANISOU 1045 N SER A 300 1807 3164 2506 794 -174 -72 N ATOM 1046 CA SER A 300 -5.263 43.117 4.217 1.00 23.59 C ANISOU 1046 CA SER A 300 2168 3809 2987 820 -159 -94 C ATOM 1047 C SER A 300 -5.627 41.643 4.133 1.00 24.12 C ANISOU 1047 C SER A 300 2218 3916 3029 753 -113 -14 C ATOM 1048 O SER A 300 -5.731 40.967 5.152 1.00 27.16 O ANISOU 1048 O SER A 300 2511 4423 3384 737 -68 7 O ATOM 1049 CB SER A 300 -6.530 43.968 4.183 1.00 34.39 C ANISOU 1049 CB SER A 300 3478 5210 4379 880 -249 -177 C ATOM 1050 OG SER A 300 -6.256 45.268 4.670 1.00 42.89 O ANISOU 1050 OG SER A 300 4531 6288 5476 956 -305 -262 O ATOM 1051 N LEU A 301 -5.828 41.143 2.919 1.00 21.87 N ANISOU 1051 N LEU A 301 2023 3530 2757 711 -135 33 N ATOM 1052 CA LEU A 301 -6.141 39.725 2.740 1.00 19.54 C ANISOU 1052 CA LEU A 301 1722 3255 2446 651 -114 114 C ATOM 1053 C LEU A 301 -4.911 38.831 2.879 1.00 19.61 C ANISOU 1053 C LEU A 301 1773 3242 2436 604 -59 167 C ATOM 1054 O LEU A 301 -4.989 37.739 3.456 1.00 23.06 O ANISOU 1054 O LEU A 301 2161 3746 2854 562 -41 220 O ATOM 1055 CB LEU A 301 -6.836 39.480 1.402 1.00 25.66 C ANISOU 1055 CB LEU A 301 2574 3930 3247 633 -166 141 C ATOM 1056 CG LEU A 301 -8.295 39.956 1.308 1.00 31.52 C ANISOU 1056 CG LEU A 301 3262 4705 4010 668 -226 96 C ATOM 1057 CD1 LEU A 301 -8.954 39.336 0.107 1.00 36.24 C ANISOU 1057 CD1 LEU A 301 3929 5209 4630 640 -265 145 C ATOM 1058 CD2 LEU A 301 -9.081 39.599 2.566 1.00 39.11 C ANISOU 1058 CD2 LEU A 301 4074 5843 4942 672 -208 88 C ATOM 1059 N ALA A 302 -3.770 39.274 2.359 1.00 19.15 N ANISOU 1059 N ALA A 302 1803 3093 2382 606 -42 152 N ATOM 1060 CA ALA A 302 -2.541 38.504 2.568 1.00 19.47 C ANISOU 1060 CA ALA A 302 1875 3121 2404 571 7 180 C ATOM 1061 C ALA A 302 -2.243 38.320 4.047 1.00 23.98 C ANISOU 1061 C ALA A 302 2357 3796 2959 577 51 173 C ATOM 1062 O ALA A 302 -1.773 37.258 4.452 1.00 21.40 O ANISOU 1062 O ALA A 302 2023 3489 2620 534 70 211 O ATOM 1063 CB ALA A 302 -1.345 39.136 1.850 1.00 18.32 C ANISOU 1063 CB ALA A 302 1823 2883 2255 572 23 155 C ATOM 1064 N CYS A 303 -2.522 39.342 4.860 1.00 20.45 N ANISOU 1064 N CYS A 303 1842 3415 2514 630 56 119 N ATOM 1065 CA CYS A 303 -2.330 39.213 6.307 1.00 25.72 C ANISOU 1065 CA CYS A 303 2415 4196 3162 639 97 109 C ATOM 1066 C CYS A 303 -3.162 38.070 6.898 1.00 25.49 C ANISOU 1066 C CYS A 303 2305 4274 3107 584 91 165 C ATOM 1067 O CYS A 303 -2.727 37.384 7.832 1.00 24.92 O ANISOU 1067 O CYS A 303 2192 4263 3013 547 121 193 O ATOM 1068 CB CYS A 303 -2.645 40.534 7.023 1.00 21.21 C ANISOU 1068 CB CYS A 303 1772 3690 2598 718 86 32 C ATOM 1069 SG CYS A 303 -1.408 41.818 6.662 1.00 26.92 S ANISOU 1069 SG CYS A 303 2584 4295 3348 771 85 -18 S ATOM 1070 N LYS A 304 -4.354 37.855 6.353 1.00 23.99 N ANISOU 1070 N LYS A 304 2094 4103 2919 572 45 186 N ATOM 1071 CA LYS A 304 -5.206 36.764 6.839 1.00 25.03 C ANISOU 1071 CA LYS A 304 2148 4338 3022 509 29 251 C ATOM 1072 C LYS A 304 -4.603 35.381 6.570 1.00 26.33 C ANISOU 1072 C LYS A 304 2376 4442 3187 433 15 333 C ATOM 1073 O LYS A 304 -4.791 34.457 7.360 1.00 23.34 O ANISOU 1073 O LYS A 304 1939 4150 2781 368 4 391 O ATOM 1074 CB LYS A 304 -6.627 36.874 6.284 1.00 29.48 C ANISOU 1074 CB LYS A 304 2676 4933 3591 517 -20 252 C ATOM 1075 CG LYS A 304 -7.309 38.184 6.661 1.00 35.26 C ANISOU 1075 CG LYS A 304 3330 5742 4324 595 -29 154 C ATOM 1076 CD LYS A 304 -8.701 37.962 7.215 1.00 54.18 C ANISOU 1076 CD LYS A 304 5596 8302 6687 579 -51 152 C ATOM 1077 CE LYS A 304 -9.278 39.254 7.787 1.00 61.15 C ANISOU 1077 CE LYS A 304 6381 9289 7565 668 -67 31 C ATOM 1078 NZ LYS A 304 -9.514 40.283 6.728 1.00 63.13 N ANISOU 1078 NZ LYS A 304 6711 9406 7871 737 -125 -41 N ATOM 1079 N LEU A 305 -3.857 35.237 5.479 1.00 21.31 N ANISOU 1079 N LEU A 305 1855 3664 2579 438 6 334 N ATOM 1080 CA LEU A 305 -3.167 33.971 5.202 1.00 20.27 C ANISOU 1080 CA LEU A 305 1781 3470 2452 382 -22 387 C ATOM 1081 C LEU A 305 -2.134 33.671 6.274 1.00 23.75 C ANISOU 1081 C LEU A 305 2204 3942 2877 359 12 378 C ATOM 1082 O LEU A 305 -1.966 32.529 6.696 1.00 26.78 O ANISOU 1082 O LEU A 305 2580 4341 3254 295 -28 431 O ATOM 1083 CB LEU A 305 -2.461 34.011 3.835 1.00 20.43 C ANISOU 1083 CB LEU A 305 1916 3351 2494 402 -32 366 C ATOM 1084 CG LEU A 305 -3.324 34.321 2.616 1.00 27.78 C ANISOU 1084 CG LEU A 305 2887 4223 3444 424 -68 372 C ATOM 1085 CD1 LEU A 305 -2.498 34.144 1.335 1.00 30.73 C ANISOU 1085 CD1 LEU A 305 3369 4480 3828 428 -80 358 C ATOM 1086 CD2 LEU A 305 -4.565 33.453 2.581 1.00 27.84 C ANISOU 1086 CD2 LEU A 305 2850 4272 3457 389 -128 441 C ATOM 1087 N VAL A 306 -1.428 34.708 6.700 1.00 23.77 N ANISOU 1087 N VAL A 306 2207 3946 2880 411 74 312 N ATOM 1088 CA VAL A 306 -0.407 34.576 7.732 1.00 21.56 C ANISOU 1088 CA VAL A 306 1913 3686 2590 401 113 294 C ATOM 1089 C VAL A 306 -1.055 34.120 9.037 1.00 26.25 C ANISOU 1089 C VAL A 306 2401 4419 3154 355 108 335 C ATOM 1090 O VAL A 306 -0.526 33.268 9.753 1.00 24.23 O ANISOU 1090 O VAL A 306 2141 4177 2889 298 96 365 O ATOM 1091 CB VAL A 306 0.316 35.907 7.957 1.00 19.32 C ANISOU 1091 CB VAL A 306 1641 3383 2316 475 175 219 C ATOM 1092 CG1 VAL A 306 1.318 35.775 9.085 1.00 23.96 C ANISOU 1092 CG1 VAL A 306 2214 3991 2899 470 218 200 C ATOM 1093 CG2 VAL A 306 1.012 36.347 6.665 1.00 19.93 C ANISOU 1093 CG2 VAL A 306 1824 3337 2412 500 176 188 C ATOM 1094 N GLN A 307 -2.215 34.700 9.327 1.00 24.84 N ANISOU 1094 N GLN A 307 2132 4349 2955 376 111 330 N ATOM 1095 CA GLN A 307 -2.984 34.364 10.509 1.00 26.13 C ANISOU 1095 CA GLN A 307 2176 4679 3074 328 108 365 C ATOM 1096 C GLN A 307 -3.363 32.885 10.537 1.00 33.33 C ANISOU 1096 C GLN A 307 3086 5610 3969 218 39 467 C ATOM 1097 O GLN A 307 -3.586 32.319 11.601 1.00 34.16 O ANISOU 1097 O GLN A 307 3114 5832 4032 145 28 515 O ATOM 1098 CB GLN A 307 -4.237 35.243 10.565 1.00 30.24 C ANISOU 1098 CB GLN A 307 2601 5312 3576 377 110 327 C ATOM 1099 CG GLN A 307 -5.139 34.972 11.736 1.00 44.68 C ANISOU 1099 CG GLN A 307 4286 7346 5344 327 109 353 C ATOM 1100 CD GLN A 307 -6.186 36.054 11.910 1.00 56.54 C ANISOU 1100 CD GLN A 307 5684 8971 6829 401 115 275 C ATOM 1101 OE1 GLN A 307 -6.508 36.779 10.964 1.00 49.82 O ANISOU 1101 OE1 GLN A 307 4877 8036 6016 469 95 223 O ATOM 1102 NE2 GLN A 307 -6.719 36.175 13.125 1.00 60.36 N ANISOU 1102 NE2 GLN A 307 6023 9659 7252 386 134 258 N ATOM 1103 N ALA A 308 -3.423 32.258 9.367 1.00 25.53 N ANISOU 1103 N ALA A 308 2182 4506 3013 203 -17 503 N ATOM 1104 CA ALA A 308 -3.818 30.851 9.268 1.00 25.97 C ANISOU 1104 CA ALA A 308 2244 4561 3063 106 -108 602 C ATOM 1105 C ALA A 308 -2.645 29.889 9.448 1.00 25.90 C ANISOU 1105 C ALA A 308 2307 4463 3072 57 -152 620 C ATOM 1106 O ALA A 308 -2.829 28.673 9.458 1.00 26.83 O ANISOU 1106 O ALA A 308 2435 4568 3190 -26 -251 699 O ATOM 1107 CB ALA A 308 -4.498 30.591 7.933 1.00 27.51 C ANISOU 1107 CB ALA A 308 2490 4674 3287 121 -162 629 C ATOM 1108 N LEU A 309 -1.436 30.416 9.572 1.00 20.60 N ANISOU 1108 N LEU A 309 1686 3724 2419 109 -93 544 N ATOM 1109 CA LEU A 309 -0.306 29.546 9.879 1.00 21.38 C ANISOU 1109 CA LEU A 309 1843 3747 2534 66 -137 543 C ATOM 1110 C LEU A 309 -0.539 28.846 11.219 1.00 27.97 C ANISOU 1110 C LEU A 309 2607 4687 3332 -33 -176 609 C ATOM 1111 O LEU A 309 -1.154 29.414 12.109 1.00 28.32 O ANISOU 1111 O LEU A 309 2555 4872 3335 -41 -121 619 O ATOM 1112 CB LEU A 309 1.003 30.333 9.901 1.00 19.98 C ANISOU 1112 CB LEU A 309 1719 3496 2376 139 -55 445 C ATOM 1113 CG LEU A 309 1.513 30.721 8.514 1.00 23.70 C ANISOU 1113 CG LEU A 309 2277 3852 2876 206 -42 388 C ATOM 1114 CD1 LEU A 309 2.602 31.785 8.618 1.00 22.88 C ANISOU 1114 CD1 LEU A 309 2205 3710 2780 275 51 300 C ATOM 1115 CD2 LEU A 309 2.035 29.488 7.783 1.00 20.90 C ANISOU 1115 CD2 LEU A 309 1995 3400 2545 171 -141 396 C ATOM 1116 N PRO A 310 -0.050 27.606 11.355 1.00 28.57 N ANISOU 1116 N PRO A 310 2731 4701 3425 -111 -283 651 N ATOM 1117 CA PRO A 310 -0.200 26.848 12.601 1.00 33.96 C ANISOU 1117 CA PRO A 310 3360 5469 4073 -226 -342 725 C ATOM 1118 C PRO A 310 0.703 27.419 13.689 1.00 36.49 C ANISOU 1118 C PRO A 310 3668 5814 4384 -208 -257 663 C ATOM 1119 O PRO A 310 1.669 28.131 13.387 1.00 30.22 O ANISOU 1119 O PRO A 310 2928 4932 3622 -114 -181 566 O ATOM 1120 CB PRO A 310 0.262 25.443 12.202 1.00 30.65 C ANISOU 1120 CB PRO A 310 3023 4930 3692 -294 -501 763 C ATOM 1121 CG PRO A 310 1.199 25.685 11.061 1.00 28.98 C ANISOU 1121 CG PRO A 310 2907 4571 3533 -190 -481 663 C ATOM 1122 CD PRO A 310 0.550 26.786 10.290 1.00 25.86 C ANISOU 1122 CD PRO A 310 2487 4208 3129 -102 -376 636 C ATOM 1123 N ARG A 311 0.383 27.117 14.941 1.00 34.68 N ANISOU 1123 N ARG A 311 3363 5707 4106 -301 -272 723 N ATOM 1124 CA ARG A 311 1.127 27.649 16.075 1.00 36.71 C ANISOU 1124 CA ARG A 311 3597 6001 4350 -287 -193 672 C ATOM 1125 C ARG A 311 1.737 26.531 16.904 1.00 39.75 C ANISOU 1125 C ARG A 311 4018 6349 4737 -405 -297 718 C ATOM 1126 O ARG A 311 2.333 26.782 17.945 1.00 39.48 O ANISOU 1126 O ARG A 311 3968 6343 4692 -415 -249 690 O ATOM 1127 CB ARG A 311 0.207 28.481 16.964 1.00 41.29 C ANISOU 1127 CB ARG A 311 4040 6786 4862 -283 -106 685 C ATOM 1128 CG ARG A 311 -0.714 29.387 16.201 1.00 40.50 C ANISOU 1128 CG ARG A 311 3891 6744 4755 -194 -47 657 C ATOM 1129 CD ARG A 311 0.086 30.325 15.334 1.00 37.91 C ANISOU 1129 CD ARG A 311 3642 6275 4485 -56 24 552 C ATOM 1130 NE ARG A 311 -0.762 31.123 14.452 1.00 42.34 N ANISOU 1130 NE ARG A 311 4179 6860 5049 20 55 527 N ATOM 1131 CZ ARG A 311 -1.186 32.349 14.734 1.00 41.94 C ANISOU 1131 CZ ARG A 311 4052 6903 4980 105 131 465 C ATOM 1132 NH1 ARG A 311 -0.855 32.921 15.881 1.00 38.53 N ANISOU 1132 NH1 ARG A 311 3555 6559 4525 131 190 424 N ATOM 1133 NH2 ARG A 311 -1.942 33.002 13.867 1.00 42.77 N ANISOU 1133 NH2 ARG A 311 4147 7008 5095 168 137 438 N ATOM 1134 N ASP A 312 1.582 25.296 16.446 1.00 39.83 N ANISOU 1134 N ASP A 312 4079 6290 4766 -494 -450 788 N ATOM 1135 CA ASP A 312 2.078 24.156 17.200 1.00 42.90 C ANISOU 1135 CA ASP A 312 4506 6634 5159 -620 -585 838 C ATOM 1136 C ASP A 312 3.276 23.515 16.517 1.00 44.83 C ANISOU 1136 C ASP A 312 4880 6670 5484 -585 -678 762 C ATOM 1137 O ASP A 312 4.024 24.181 15.804 1.00 40.94 O ANISOU 1137 O ASP A 312 4437 6086 5031 -458 -591 651 O ATOM 1138 CB ASP A 312 0.966 23.128 17.416 1.00 46.89 C ANISOU 1138 CB ASP A 312 4963 7235 5619 -774 -728 987 C ATOM 1139 CG ASP A 312 0.225 22.782 16.135 1.00 49.45 C ANISOU 1139 CG ASP A 312 5305 7516 5966 -748 -796 1025 C ATOM 1140 OD1 ASP A 312 0.808 22.926 15.042 1.00 41.28 O ANISOU 1140 OD1 ASP A 312 4351 6338 4994 -638 -787 940 O ATOM 1141 OD2 ASP A 312 -0.942 22.350 16.225 1.00 49.41 O ANISOU 1141 OD2 ASP A 312 5232 7629 5914 -843 -860 1141 O ATOM 1142 N ALA A 313 3.448 22.217 16.736 1.00 41.31 N ANISOU 1142 N ALA A 313 4482 6158 5057 -701 -866 819 N ATOM 1143 CA ALA A 313 4.584 21.494 16.183 1.00 41.32 C ANISOU 1143 CA ALA A 313 4597 5969 5133 -673 -984 734 C ATOM 1144 C ALA A 313 4.640 21.596 14.661 1.00 34.36 C ANISOU 1144 C ALA A 313 3759 5002 4292 -559 -983 670 C ATOM 1145 O ALA A 313 5.710 21.475 14.062 1.00 35.84 O ANISOU 1145 O ALA A 313 4025 5060 4534 -484 -1006 553 O ATOM 1146 CB ALA A 313 4.550 20.038 16.626 1.00 46.45 C ANISOU 1146 CB ALA A 313 5285 6568 5797 -825 -1223 818 C ATOM 1147 N ARG A 314 3.492 21.825 14.034 1.00 32.63 N ANISOU 1147 N ARG A 314 3386 4055 4956 152 -758 1067 N ATOM 1148 CA ARG A 314 3.436 21.947 12.581 1.00 35.48 C ANISOU 1148 CA ARG A 314 3800 4322 5357 149 -813 967 C ATOM 1149 C ARG A 314 4.238 23.151 12.089 1.00 29.59 C ANISOU 1149 C ARG A 314 3142 3600 4501 197 -720 799 C ATOM 1150 O ARG A 314 4.725 23.153 10.954 1.00 35.33 O ANISOU 1150 O ARG A 314 3930 4254 5240 202 -767 681 O ATOM 1151 CB ARG A 314 1.982 22.031 12.094 1.00 29.92 C ANISOU 1151 CB ARG A 314 3039 3610 4719 128 -831 1075 C ATOM 1152 CG ARG A 314 1.160 20.771 12.383 1.00 35.69 C ANISOU 1152 CG ARG A 314 3682 4300 5581 70 -948 1247 C ATOM 1153 CD ARG A 314 -0.315 20.959 12.046 1.00 33.48 C ANISOU 1153 CD ARG A 314 3335 4030 5357 50 -951 1370 C ATOM 1154 NE ARG A 314 -0.947 21.961 12.901 1.00 34.21 N ANISOU 1154 NE ARG A 314 3380 4261 5357 84 -808 1444 N ATOM 1155 CZ ARG A 314 -2.135 22.512 12.665 1.00 39.51 C ANISOU 1155 CZ ARG A 314 4004 4971 6039 87 -767 1523 C ATOM 1156 NH1 ARG A 314 -2.834 22.163 11.592 1.00 37.09 N ANISOU 1156 NH1 ARG A 314 3692 4570 5833 52 -861 1543 N ATOM 1157 NH2 ARG A 314 -2.622 23.421 13.499 1.00 41.52 N ANISOU 1157 NH2 ARG A 314 4217 5358 6200 130 -637 1577 N ATOM 1158 N LEU A 315 4.368 24.176 12.927 1.00 27.97 N ANISOU 1158 N LEU A 315 2941 3498 4188 236 -593 791 N ATOM 1159 CA LEU A 315 5.116 25.367 12.518 1.00 28.14 C ANISOU 1159 CA LEU A 315 3041 3539 4112 277 -512 644 C ATOM 1160 C LEU A 315 6.604 25.044 12.425 1.00 25.04 C ANISOU 1160 C LEU A 315 2711 3110 3693 283 -542 523 C ATOM 1161 O LEU A 315 7.310 25.540 11.543 1.00 26.18 O ANISOU 1161 O LEU A 315 2921 3224 3804 298 -537 395 O ATOM 1162 CB LEU A 315 4.871 26.536 13.473 1.00 27.57 C ANISOU 1162 CB LEU A 315 2959 3579 3937 322 -383 663 C ATOM 1163 CG LEU A 315 5.492 27.877 13.048 1.00 26.13 C ANISOU 1163 CG LEU A 315 2853 3413 3664 362 -306 525 C ATOM 1164 CD1 LEU A 315 5.107 28.218 11.605 1.00 26.61 C ANISOU 1164 CD1 LEU A 315 2942 3408 3761 349 -337 471 C ATOM 1165 CD2 LEU A 315 5.071 29.000 13.984 1.00 27.05 C ANISOU 1165 CD2 LEU A 315 2956 3631 3691 411 -195 550 C ATOM 1166 N ILE A 316 7.087 24.204 13.336 1.00 23.61 N ANISOU 1166 N ILE A 316 2506 2937 3528 270 -574 569 N ATOM 1167 CA ILE A 316 8.464 23.736 13.249 1.00 22.80 C ANISOU 1167 CA ILE A 316 2455 2794 3415 273 -616 464 C ATOM 1168 C ILE A 316 8.653 22.988 11.937 1.00 25.87 C ANISOU 1168 C ILE A 316 2871 3077 3882 256 -730 398 C ATOM 1169 O ILE A 316 9.620 23.218 11.210 1.00 25.38 O ANISOU 1169 O ILE A 316 2870 2990 3784 276 -735 265 O ATOM 1170 CB ILE A 316 8.814 22.760 14.389 1.00 28.64 C ANISOU 1170 CB ILE A 316 3154 3546 4181 254 -655 543 C ATOM 1171 CG1 ILE A 316 8.525 23.391 15.749 1.00 30.26 C ANISOU 1171 CG1 ILE A 316 3323 3866 4307 275 -549 622 C ATOM 1172 CG2 ILE A 316 10.262 22.332 14.285 1.00 31.65 C ANISOU 1172 CG2 ILE A 316 3590 3886 4549 261 -696 428 C ATOM 1173 CD1 ILE A 316 8.975 22.535 16.917 1.00 35.04 C ANISOU 1173 CD1 ILE A 316 3892 4498 4923 259 -577 695 C ATOM 1174 N ALA A 317 7.723 22.085 11.639 1.00 26.58 N ANISOU 1174 N ALA A 317 2910 3108 4079 221 -826 494 N ATOM 1175 CA ALA A 317 7.781 21.309 10.400 1.00 27.02 C ANISOU 1175 CA ALA A 317 2991 3060 4217 211 -949 435 C ATOM 1176 C ALA A 317 7.832 22.225 9.177 1.00 24.70 C ANISOU 1176 C ALA A 317 2751 2760 3872 238 -911 322 C ATOM 1177 O ALA A 317 8.523 21.947 8.202 1.00 23.75 O ANISOU 1177 O ALA A 317 2679 2588 3756 255 -971 207 O ATOM 1178 CB ALA A 317 6.587 20.368 10.303 1.00 31.93 C ANISOU 1178 CB ALA A 317 3547 3622 4964 168 -1054 570 C ATOM 1179 N ILE A 318 7.091 23.319 9.228 1.00 21.61 N ANISOU 1179 N ILE A 318 2350 2429 3433 245 -813 356 N ATOM 1180 CA ILE A 318 7.092 24.259 8.112 1.00 23.11 C ANISOU 1180 CA ILE A 318 2587 2619 3576 266 -775 261 C ATOM 1181 C ILE A 318 8.458 24.951 7.978 1.00 21.49 C ANISOU 1181 C ILE A 318 2446 2448 3272 298 -714 125 C ATOM 1182 O ILE A 318 8.996 25.066 6.879 1.00 25.04 O ANISOU 1182 O ILE A 318 2939 2870 3704 313 -742 20 O ATOM 1183 CB ILE A 318 5.963 25.285 8.250 1.00 23.71 C ANISOU 1183 CB ILE A 318 2635 2748 3627 267 -688 333 C ATOM 1184 CG1 ILE A 318 4.628 24.625 7.894 1.00 26.61 C ANISOU 1184 CG1 ILE A 318 2945 3065 4099 234 -766 447 C ATOM 1185 CG2 ILE A 318 6.206 26.469 7.327 1.00 24.28 C ANISOU 1185 CG2 ILE A 318 2760 2835 3629 291 -628 228 C ATOM 1186 CD1 ILE A 318 3.430 25.499 8.195 1.00 28.08 C ANISOU 1186 CD1 ILE A 318 3088 3311 4270 235 -684 539 C ATOM 1187 N CYS A 319 9.018 25.388 9.100 1.00 23.07 N ANISOU 1187 N CYS A 319 2647 2712 3407 310 -636 131 N ATOM 1188 CA CYS A 319 10.300 26.090 9.085 1.00 22.38 C ANISOU 1188 CA CYS A 319 2615 2659 3230 337 -578 15 C ATOM 1189 C CYS A 319 11.474 25.233 8.616 1.00 25.32 C ANISOU 1189 C CYS A 319 3018 2987 3616 343 -655 -75 C ATOM 1190 O CYS A 319 12.440 25.764 8.066 1.00 30.64 O ANISOU 1190 O CYS A 319 3736 3678 4227 365 -629 -181 O ATOM 1191 CB CYS A 319 10.618 26.687 10.463 1.00 22.11 C ANISOU 1191 CB CYS A 319 2575 2698 3128 350 -489 45 C ATOM 1192 SG CYS A 319 9.525 28.028 10.949 1.00 28.98 S ANISOU 1192 SG CYS A 319 3425 3636 3947 367 -381 108 S ATOM 1193 N VAL A 320 11.407 23.918 8.825 1.00 21.79 N ANISOU 1193 N VAL A 320 2544 2486 3251 327 -754 -32 N ATOM 1194 CA VAL A 320 12.522 23.055 8.447 1.00 19.81 C ANISOU 1194 CA VAL A 320 2321 2192 3014 341 -833 -122 C ATOM 1195 C VAL A 320 12.274 22.286 7.159 1.00 24.54 C ANISOU 1195 C VAL A 320 2929 2715 3681 347 -947 -167 C ATOM 1196 O VAL A 320 13.096 21.466 6.759 1.00 24.78 O ANISOU 1196 O VAL A 320 2980 2705 3731 367 -1029 -243 O ATOM 1197 CB VAL A 320 12.917 22.060 9.569 1.00 25.05 C ANISOU 1197 CB VAL A 320 2957 2841 3719 326 -879 -68 C ATOM 1198 CG1 VAL A 320 13.249 22.817 10.844 1.00 27.57 C ANISOU 1198 CG1 VAL A 320 3273 3242 3962 328 -769 -34 C ATOM 1199 CG2 VAL A 320 11.805 21.017 9.805 1.00 21.76 C ANISOU 1199 CG2 VAL A 320 2483 2366 3417 290 -974 58 C ATOM 1200 N ASP A 321 11.149 22.568 6.501 1.00 26.01 N ANISOU 1200 N ASP A 321 3101 2883 3898 335 -955 -124 N ATOM 1201 CA ASP A 321 10.782 21.880 5.271 1.00 24.51 C ANISOU 1201 CA ASP A 321 2920 2619 3773 342 -1068 -162 C ATOM 1202 C ASP A 321 11.526 22.480 4.076 1.00 27.66 C ANISOU 1202 C ASP A 321 3370 3044 4095 382 -1046 -297 C ATOM 1203 O ASP A 321 11.599 23.703 3.949 1.00 22.39 O ANISOU 1203 O ASP A 321 2718 2442 3347 386 -939 -317 O ATOM 1204 CB ASP A 321 9.277 22.031 5.024 1.00 23.59 C ANISOU 1204 CB ASP A 321 2768 2479 3717 312 -1080 -60 C ATOM 1205 CG ASP A 321 8.793 21.163 3.897 1.00 26.35 C ANISOU 1205 CG ASP A 321 3123 2740 4151 315 -1216 -82 C ATOM 1206 OD1 ASP A 321 8.830 19.932 4.078 1.00 28.99 O ANISOU 1206 OD1 ASP A 321 3441 3001 4574 306 -1337 -58 O ATOM 1207 OD2 ASP A 321 8.384 21.696 2.837 1.00 28.14 O ANISOU 1207 OD2 ASP A 321 3370 2965 4358 327 -1211 -124 O ATOM 1208 N GLN A 322 12.043 21.633 3.182 1.00 21.73 N ANISOU 1208 N GLN A 322 2642 2244 3369 414 -1152 -387 N ATOM 1209 CA GLN A 322 12.801 22.123 2.029 1.00 22.78 C ANISOU 1209 CA GLN A 322 2816 2417 3422 458 -1134 -512 C ATOM 1210 C GLN A 322 11.973 23.039 1.132 1.00 24.20 C ANISOU 1210 C GLN A 322 3002 2618 3577 452 -1091 -504 C ATOM 1211 O GLN A 322 12.518 23.924 0.475 1.00 27.12 O ANISOU 1211 O GLN A 322 3396 3051 3858 474 -1025 -573 O ATOM 1212 CB GLN A 322 13.355 20.965 1.201 1.00 30.36 C ANISOU 1212 CB GLN A 322 3796 3322 4416 503 -1267 -608 C ATOM 1213 CG GLN A 322 12.289 20.029 0.669 1.00 40.79 C ANISOU 1213 CG GLN A 322 5105 4546 5848 495 -1401 -570 C ATOM 1214 CD GLN A 322 12.888 18.858 -0.094 1.00 50.34 C ANISOU 1214 CD GLN A 322 6339 5696 7091 550 -1545 -676 C ATOM 1215 OE1 GLN A 322 13.836 19.025 -0.866 1.00 46.40 O ANISOU 1215 OE1 GLN A 322 5871 5248 6510 608 -1534 -798 O ATOM 1216 NE2 GLN A 322 12.337 17.667 0.120 1.00 53.61 N ANISOU 1216 NE2 GLN A 322 6736 6006 7628 535 -1684 -628 N ATOM 1217 N ASN A 323 10.662 22.828 1.104 1.00 27.93 N ANISOU 1217 N ASN A 323 3447 3038 4128 421 -1132 -412 N ATOM 1218 CA ASN A 323 9.772 23.706 0.337 1.00 26.32 C ANISOU 1218 CA ASN A 323 3244 2850 3908 410 -1091 -392 C ATOM 1219 C ASN A 323 9.144 24.796 1.183 1.00 23.70 C ANISOU 1219 C ASN A 323 2888 2567 3550 377 -971 -299 C ATOM 1220 O ASN A 323 9.191 25.972 0.822 1.00 22.47 O ANISOU 1220 O ASN A 323 2748 2466 3322 381 -882 -324 O ATOM 1221 CB ASN A 323 8.678 22.890 -0.358 1.00 28.20 C ANISOU 1221 CB ASN A 323 3468 3001 4246 400 -1213 -353 C ATOM 1222 CG ASN A 323 9.248 21.874 -1.316 1.00 34.23 C ANISOU 1222 CG ASN A 323 4261 3714 5030 446 -1341 -459 C ATOM 1223 OD1 ASN A 323 10.091 22.201 -2.150 1.00 38.86 O ANISOU 1223 OD1 ASN A 323 4882 4349 5532 491 -1324 -572 O ATOM 1224 ND2 ASN A 323 8.815 20.627 -1.184 1.00 38.91 N ANISOU 1224 ND2 ASN A 323 4838 4212 5733 437 -1476 -423 N ATOM 1225 N ALA A 324 8.557 24.413 2.312 1.00 22.27 N ANISOU 1225 N ALA A 324 2667 2368 3427 347 -971 -191 N ATOM 1226 CA ALA A 324 7.782 25.362 3.102 1.00 21.55 C ANISOU 1226 CA ALA A 324 2547 2326 3317 324 -867 -98 C ATOM 1227 C ALA A 324 8.614 26.472 3.725 1.00 21.68 C ANISOU 1227 C ALA A 324 2585 2422 3230 339 -745 -139 C ATOM 1228 O ALA A 324 8.081 27.531 4.018 1.00 20.49 O ANISOU 1228 O ALA A 324 2427 2315 3043 335 -658 -100 O ATOM 1229 CB ALA A 324 6.947 24.646 4.179 1.00 22.57 C ANISOU 1229 CB ALA A 324 2618 2432 3526 293 -896 36 C ATOM 1230 N ASN A 325 9.914 26.255 3.938 1.00 18.24 N ANISOU 1230 N ASN A 325 2177 2004 2749 359 -744 -218 N ATOM 1231 CA ASN A 325 10.701 27.307 4.588 1.00 19.36 C ANISOU 1231 CA ASN A 325 2339 2217 2800 369 -636 -250 C ATOM 1232 C ASN A 325 10.641 28.593 3.770 1.00 15.35 C ANISOU 1232 C ASN A 325 1855 1745 2231 376 -573 -293 C ATOM 1233 O ASN A 325 10.715 29.697 4.314 1.00 16.90 O ANISOU 1233 O ASN A 325 2059 1989 2373 377 -484 -284 O ATOM 1234 CB ASN A 325 12.157 26.882 4.866 1.00 18.76 C ANISOU 1234 CB ASN A 325 2287 2154 2686 388 -649 -328 C ATOM 1235 CG ASN A 325 13.032 26.878 3.613 1.00 22.89 C ANISOU 1235 CG ASN A 325 2844 2682 3171 414 -681 -441 C ATOM 1236 OD1 ASN A 325 13.200 25.848 2.951 1.00 25.53 O ANISOU 1236 OD1 ASN A 325 3181 2972 3546 429 -777 -482 O ATOM 1237 ND2 ASN A 325 13.591 28.027 3.286 1.00 16.27 N ANISOU 1237 ND2 ASN A 325 2028 1901 2253 422 -605 -489 N ATOM 1238 N HIS A 326 10.514 28.448 2.457 1.00 17.18 N ANISOU 1238 N HIS A 326 2100 1953 2474 382 -625 -340 N ATOM 1239 CA HIS A 326 10.449 29.610 1.577 1.00 18.09 C ANISOU 1239 CA HIS A 326 2235 2103 2536 385 -575 -375 C ATOM 1240 C HIS A 326 9.137 30.380 1.727 1.00 18.20 C ANISOU 1240 C HIS A 326 2227 2114 2573 366 -530 -293 C ATOM 1241 O HIS A 326 9.063 31.565 1.413 1.00 17.99 O ANISOU 1241 O HIS A 326 2215 2122 2501 365 -468 -304 O ATOM 1242 CB HIS A 326 10.662 29.171 0.127 1.00 18.92 C ANISOU 1242 CB HIS A 326 2357 2192 2641 402 -647 -446 C ATOM 1243 CG HIS A 326 12.020 28.597 -0.110 1.00 18.03 C ANISOU 1243 CG HIS A 326 2263 2098 2488 432 -679 -537 C ATOM 1244 ND1 HIS A 326 13.151 29.379 -0.176 1.00 18.71 N ANISOU 1244 ND1 HIS A 326 2367 2251 2489 444 -617 -595 N ATOM 1245 CD2 HIS A 326 12.436 27.317 -0.253 1.00 19.67 C ANISOU 1245 CD2 HIS A 326 2473 2268 2732 454 -771 -578 C ATOM 1246 CE1 HIS A 326 14.207 28.605 -0.365 1.00 21.75 C ANISOU 1246 CE1 HIS A 326 2761 2646 2855 473 -662 -666 C ATOM 1247 NE2 HIS A 326 13.797 27.349 -0.422 1.00 22.54 N ANISOU 1247 NE2 HIS A 326 2854 2681 3027 483 -757 -662 N ATOM 1248 N VAL A 327 8.096 29.710 2.202 1.00 16.73 N ANISOU 1248 N VAL A 327 2005 1889 2461 351 -565 -205 N ATOM 1249 CA VAL A 327 6.851 30.417 2.511 1.00 16.49 C ANISOU 1249 CA VAL A 327 1947 1868 2451 338 -517 -119 C ATOM 1250 C VAL A 327 7.072 31.330 3.718 1.00 16.41 C ANISOU 1250 C VAL A 327 1936 1916 2385 349 -418 -98 C ATOM 1251 O VAL A 327 6.687 32.492 3.702 1.00 17.45 O ANISOU 1251 O VAL A 327 2073 2076 2482 355 -353 -92 O ATOM 1252 CB VAL A 327 5.686 29.439 2.800 1.00 18.21 C ANISOU 1252 CB VAL A 327 2116 2040 2765 318 -580 -15 C ATOM 1253 CG1 VAL A 327 4.469 30.205 3.364 1.00 19.89 C ANISOU 1253 CG1 VAL A 327 2290 2280 2986 312 -514 83 C ATOM 1254 CG2 VAL A 327 5.298 28.685 1.527 1.00 18.90 C ANISOU 1254 CG2 VAL A 327 2208 2061 2912 309 -684 -35 C ATOM 1255 N ILE A 328 7.712 30.810 4.764 1.00 15.58 N ANISOU 1255 N ILE A 328 1826 1826 2269 355 -412 -92 N ATOM 1256 CA ILE A 328 8.023 31.654 5.919 1.00 16.12 C ANISOU 1256 CA ILE A 328 1899 1951 2277 373 -326 -84 C ATOM 1257 C ILE A 328 8.913 32.826 5.516 1.00 17.40 C ANISOU 1257 C ILE A 328 2107 2140 2364 385 -276 -173 C ATOM 1258 O ILE A 328 8.685 33.946 5.943 1.00 14.71 O ANISOU 1258 O ILE A 328 1773 1832 1984 399 -211 -166 O ATOM 1259 CB ILE A 328 8.670 30.867 7.088 1.00 16.47 C ANISOU 1259 CB ILE A 328 1931 2008 2317 377 -332 -67 C ATOM 1260 CG1 ILE A 328 7.722 29.770 7.578 1.00 18.48 C ANISOU 1260 CG1 ILE A 328 2130 2241 2650 359 -382 41 C ATOM 1261 CG2 ILE A 328 8.999 31.798 8.246 1.00 20.10 C ANISOU 1261 CG2 ILE A 328 2402 2529 2707 401 -246 -68 C ATOM 1262 CD1 ILE A 328 6.323 30.280 7.899 1.00 19.63 C ANISOU 1262 CD1 ILE A 328 2232 2412 2813 361 -340 139 C ATOM 1263 N GLN A 329 9.924 32.575 4.685 1.00 17.13 N ANISOU 1263 N GLN A 329 2102 2096 2312 382 -312 -253 N ATOM 1264 CA GLN A 329 10.786 33.663 4.239 1.00 16.52 C ANISOU 1264 CA GLN A 329 2060 2048 2168 387 -272 -324 C ATOM 1265 C GLN A 329 10.031 34.716 3.417 1.00 18.18 C ANISOU 1265 C GLN A 329 2273 2259 2374 381 -249 -314 C ATOM 1266 O GLN A 329 10.319 35.903 3.511 1.00 15.62 O ANISOU 1266 O GLN A 329 1968 1960 2006 384 -199 -335 O ATOM 1267 CB GLN A 329 11.984 33.126 3.446 1.00 16.54 C ANISOU 1267 CB GLN A 329 2082 2053 2148 390 -316 -403 C ATOM 1268 CG GLN A 329 12.911 32.227 4.254 1.00 16.45 C ANISOU 1268 CG GLN A 329 2072 2043 2134 398 -336 -424 C ATOM 1269 CD GLN A 329 14.218 32.008 3.556 1.00 22.11 C ANISOU 1269 CD GLN A 329 2810 2780 2812 409 -361 -508 C ATOM 1270 OE1 GLN A 329 15.057 32.909 3.498 1.00 21.78 O ANISOU 1270 OE1 GLN A 329 2785 2778 2711 409 -318 -547 O ATOM 1271 NE2 GLN A 329 14.407 30.808 3.011 1.00 19.65 N ANISOU 1271 NE2 GLN A 329 2493 2441 2533 419 -437 -537 N ATOM 1272 N LYS A 330 9.053 34.281 2.625 1.00 14.92 N ANISOU 1272 N LYS A 330 1841 1813 2013 370 -291 -281 N ATOM 1273 CA LYS A 330 8.210 35.223 1.867 1.00 14.93 C ANISOU 1273 CA LYS A 330 1842 1812 2019 362 -272 -263 C ATOM 1274 C LYS A 330 7.368 36.089 2.814 1.00 14.41 C ANISOU 1274 C LYS A 330 1761 1760 1952 372 -210 -204 C ATOM 1275 O LYS A 330 7.261 37.310 2.640 1.00 15.90 O ANISOU 1275 O LYS A 330 1965 1963 2113 376 -170 -216 O ATOM 1276 CB LYS A 330 7.293 34.486 0.883 1.00 15.03 C ANISOU 1276 CB LYS A 330 1836 1783 2092 349 -337 -235 C ATOM 1277 CG LYS A 330 6.381 35.437 0.051 1.00 18.06 C ANISOU 1277 CG LYS A 330 2218 2162 2484 338 -321 -213 C ATOM 1278 CD LYS A 330 7.219 36.275 -0.920 1.00 19.35 C ANISOU 1278 CD LYS A 330 2411 2352 2588 335 -310 -282 C ATOM 1279 CE LYS A 330 7.835 35.415 -2.014 1.00 25.27 C ANISOU 1279 CE LYS A 330 3171 3100 3331 337 -377 -339 C ATOM 1280 NZ LYS A 330 8.654 36.255 -2.963 1.00 24.38 N ANISOU 1280 NZ LYS A 330 3077 3032 3154 334 -361 -393 N ATOM 1281 N VAL A 331 6.772 35.459 3.817 1.00 14.65 N ANISOU 1281 N VAL A 331 1760 1791 2014 381 -206 -140 N ATOM 1282 CA VAL A 331 6.008 36.203 4.821 1.00 14.74 C ANISOU 1282 CA VAL A 331 1753 1833 2014 404 -144 -86 C ATOM 1283 C VAL A 331 6.868 37.312 5.409 1.00 14.96 C ANISOU 1283 C VAL A 331 1818 1893 1972 426 -91 -143 C ATOM 1284 O VAL A 331 6.469 38.473 5.500 1.00 15.62 O ANISOU 1284 O VAL A 331 1910 1988 2035 444 -51 -144 O ATOM 1285 CB VAL A 331 5.537 35.271 5.963 1.00 15.45 C ANISOU 1285 CB VAL A 331 1800 1939 2132 412 -145 -9 C ATOM 1286 CG1 VAL A 331 4.964 36.084 7.133 1.00 18.79 C ANISOU 1286 CG1 VAL A 331 2205 2414 2519 451 -73 34 C ATOM 1287 CG2 VAL A 331 4.489 34.275 5.454 1.00 16.53 C ANISOU 1287 CG2 VAL A 331 1893 2037 2350 387 -205 67 C ATOM 1288 N VAL A 332 8.066 36.943 5.821 1.00 14.84 N ANISOU 1288 N VAL A 332 1825 1889 1926 427 -96 -190 N ATOM 1289 CA VAL A 332 8.962 37.906 6.434 1.00 15.06 C ANISOU 1289 CA VAL A 332 1887 1942 1893 445 -56 -242 C ATOM 1290 C VAL A 332 9.277 39.057 5.469 1.00 14.68 C ANISOU 1290 C VAL A 332 1869 1885 1826 433 -54 -290 C ATOM 1291 O VAL A 332 9.414 40.206 5.881 1.00 18.51 O ANISOU 1291 O VAL A 332 2376 2379 2280 451 -23 -310 O ATOM 1292 CB VAL A 332 10.242 37.200 6.901 1.00 17.70 C ANISOU 1292 CB VAL A 332 2237 2285 2203 442 -72 -283 C ATOM 1293 CG1 VAL A 332 11.273 38.208 7.335 1.00 22.08 C ANISOU 1293 CG1 VAL A 332 2830 2858 2700 454 -43 -341 C ATOM 1294 CG2 VAL A 332 9.891 36.254 8.032 1.00 16.80 C ANISOU 1294 CG2 VAL A 332 2092 2186 2104 456 -70 -227 C ATOM 1295 N ALA A 333 9.385 38.736 4.193 1.00 19.04 N ANISOU 1295 N ALA A 333 2421 2418 2397 404 -93 -306 N ATOM 1296 CA ALA A 333 9.706 39.732 3.173 1.00 20.31 C ANISOU 1296 CA ALA A 333 2600 2577 2538 387 -96 -341 C ATOM 1297 C ALA A 333 8.572 40.713 2.837 1.00 19.50 C ANISOU 1297 C ALA A 333 2492 2460 2457 388 -79 -306 C ATOM 1298 O ALA A 333 8.821 41.902 2.631 1.00 21.18 O ANISOU 1298 O ALA A 333 2724 2673 2649 385 -67 -327 O ATOM 1299 CB ALA A 333 10.204 39.052 1.914 1.00 22.40 C ANISOU 1299 CB ALA A 333 2864 2840 2806 363 -142 -370 C ATOM 1300 N VAL A 334 7.332 40.237 2.778 1.00 16.96 N ANISOU 1300 N VAL A 334 2140 2123 2181 392 -84 -250 N ATOM 1301 CA VAL A 334 6.268 41.078 2.208 1.00 19.58 C ANISOU 1301 CA VAL A 334 2463 2439 2538 390 -77 -219 C ATOM 1302 C VAL A 334 5.097 41.454 3.135 1.00 17.40 C ANISOU 1302 C VAL A 334 2164 2170 2279 425 -39 -165 C ATOM 1303 O VAL A 334 4.162 42.132 2.701 1.00 16.64 O ANISOU 1303 O VAL A 334 2056 2059 2205 427 -34 -137 O ATOM 1304 CB VAL A 334 5.709 40.456 0.907 1.00 19.62 C ANISOU 1304 CB VAL A 334 2451 2420 2583 361 -123 -201 C ATOM 1305 CG1 VAL A 334 6.868 40.150 -0.075 1.00 18.70 C ANISOU 1305 CG1 VAL A 334 2356 2313 2437 338 -158 -260 C ATOM 1306 CG2 VAL A 334 4.926 39.175 1.219 1.00 14.84 C ANISOU 1306 CG2 VAL A 334 1811 1800 2027 363 -147 -147 C ATOM 1307 N ILE A 335 5.156 41.033 4.393 1.00 16.10 N ANISOU 1307 N ILE A 335 1988 2031 2098 455 -14 -148 N ATOM 1308 CA ILE A 335 4.055 41.249 5.335 1.00 15.10 C ANISOU 1308 CA ILE A 335 1829 1929 1978 496 25 -90 C ATOM 1309 C ILE A 335 4.559 42.040 6.549 1.00 15.66 C ANISOU 1309 C ILE A 335 1924 2034 1991 544 66 -126 C ATOM 1310 O ILE A 335 5.631 41.739 7.064 1.00 16.78 O ANISOU 1310 O ILE A 335 2088 2186 2100 544 64 -165 O ATOM 1311 CB ILE A 335 3.505 39.912 5.834 1.00 15.37 C ANISOU 1311 CB ILE A 335 1817 1979 2046 494 15 -19 C ATOM 1312 CG1 ILE A 335 3.057 39.029 4.662 1.00 17.42 C ANISOU 1312 CG1 ILE A 335 2056 2195 2368 448 -42 12 C ATOM 1313 CG2 ILE A 335 2.359 40.145 6.825 1.00 17.70 C ANISOU 1313 CG2 ILE A 335 2068 2318 2340 540 60 53 C ATOM 1314 CD1 ILE A 335 1.890 39.593 3.884 1.00 16.04 C ANISOU 1314 CD1 ILE A 335 1863 2001 2231 442 -44 49 C ATOM 1315 N PRO A 336 3.799 43.055 7.017 1.00 17.73 N ANISOU 1315 N PRO A 336 2183 2313 2242 591 99 -117 N ATOM 1316 CA PRO A 336 4.336 43.791 8.171 1.00 15.56 C ANISOU 1316 CA PRO A 336 1937 2066 1909 645 127 -163 C ATOM 1317 C PRO A 336 4.533 42.910 9.405 1.00 19.10 C ANISOU 1317 C PRO A 336 2364 2566 2326 673 151 -137 C ATOM 1318 O PRO A 336 3.781 41.965 9.623 1.00 16.64 O ANISOU 1318 O PRO A 336 2001 2281 2039 670 159 -61 O ATOM 1319 CB PRO A 336 3.276 44.867 8.446 1.00 17.43 C ANISOU 1319 CB PRO A 336 2165 2316 2144 700 153 -152 C ATOM 1320 CG PRO A 336 2.580 45.058 7.122 1.00 17.65 C ANISOU 1320 CG PRO A 336 2179 2300 2227 658 129 -126 C ATOM 1321 CD PRO A 336 2.594 43.695 6.458 1.00 15.99 C ANISOU 1321 CD PRO A 336 1941 2079 2056 600 104 -82 C ATOM 1322 N LEU A 337 5.528 43.261 10.213 1.00 18.57 N ANISOU 1322 N LEU A 337 2335 2514 2207 698 159 -194 N ATOM 1323 CA LEU A 337 5.946 42.459 11.366 1.00 15.92 C ANISOU 1323 CA LEU A 337 1988 2226 1836 720 177 -179 C ATOM 1324 C LEU A 337 4.816 42.110 12.338 1.00 16.87 C ANISOU 1324 C LEU A 337 2051 2415 1942 773 219 -101 C ATOM 1325 O LEU A 337 4.792 41.008 12.899 1.00 22.11 O ANISOU 1325 O LEU A 337 2677 3114 2607 765 223 -44 O ATOM 1326 CB LEU A 337 7.072 43.170 12.121 1.00 17.62 C ANISOU 1326 CB LEU A 337 2257 2445 1994 750 178 -258 C ATOM 1327 CG LEU A 337 7.376 42.594 13.515 1.00 19.62 C ANISOU 1327 CG LEU A 337 2500 2759 2196 791 204 -245 C ATOM 1328 CD1 LEU A 337 7.855 41.147 13.430 1.00 19.02 C ANISOU 1328 CD1 LEU A 337 2399 2681 2145 738 186 -207 C ATOM 1329 CD2 LEU A 337 8.412 43.470 14.226 1.00 18.86 C ANISOU 1329 CD2 LEU A 337 2463 2659 2045 827 199 -329 C ATOM 1330 N LYS A 338 3.889 43.031 12.568 1.00 17.21 N ANISOU 1330 N LYS A 338 2085 2485 1971 830 247 -94 N ATOM 1331 CA LYS A 338 2.867 42.759 13.583 1.00 17.94 C ANISOU 1331 CA LYS A 338 2118 2663 2036 891 293 -19 C ATOM 1332 C LYS A 338 2.147 41.433 13.293 1.00 22.10 C ANISOU 1332 C LYS A 338 2575 3202 2621 843 285 92 C ATOM 1333 O LYS A 338 1.815 40.671 14.205 1.00 20.14 O ANISOU 1333 O LYS A 338 2275 3024 2354 864 309 166 O ATOM 1334 CB LYS A 338 1.860 43.909 13.695 1.00 18.60 C ANISOU 1334 CB LYS A 338 2194 2771 2103 961 321 -25 C ATOM 1335 CG LYS A 338 0.781 43.698 14.762 1.00 26.55 C ANISOU 1335 CG LYS A 338 3132 3885 3072 1037 374 55 C ATOM 1336 CD LYS A 338 1.379 43.444 16.141 1.00 22.93 C ANISOU 1336 CD LYS A 338 2677 3503 2534 1090 401 43 C ATOM 1337 CE LYS A 338 0.286 43.243 17.196 1.00 23.23 C ANISOU 1337 CE LYS A 338 2637 3665 2523 1170 458 131 C ATOM 1338 NZ LYS A 338 0.822 42.701 18.467 1.00 20.60 N ANISOU 1338 NZ LYS A 338 2293 3414 2119 1207 482 145 N ATOM 1339 N ASN A 339 1.920 41.161 12.014 1.00 19.10 N ANISOU 1339 N ASN A 339 2193 2754 2311 778 246 105 N ATOM 1340 CA ASN A 339 1.247 39.942 11.600 1.00 21.44 C ANISOU 1340 CA ASN A 339 2428 3043 2673 728 221 203 C ATOM 1341 C ASN A 339 2.013 38.642 11.870 1.00 19.01 C ANISOU 1341 C ASN A 339 2113 2728 2380 685 189 224 C ATOM 1342 O ASN A 339 1.398 37.606 12.095 1.00 22.43 O ANISOU 1342 O ASN A 339 2485 3183 2855 665 174 323 O ATOM 1343 CB ASN A 339 0.878 40.038 10.122 1.00 19.70 C ANISOU 1343 CB ASN A 339 2218 2748 2520 675 180 197 C ATOM 1344 CG ASN A 339 0.043 41.265 9.818 1.00 18.75 C ANISOU 1344 CG ASN A 339 2099 2630 2396 713 206 186 C ATOM 1345 OD1 ASN A 339 0.558 42.270 9.316 1.00 25.84 O ANISOU 1345 OD1 ASN A 339 3054 3488 3277 715 199 102 O ATOM 1346 ND2 ASN A 339 -1.237 41.202 10.131 1.00 17.77 N ANISOU 1346 ND2 ASN A 339 1910 2552 2288 743 232 275 N ATOM 1347 N TRP A 340 3.342 38.677 11.818 1.00 17.26 N ANISOU 1347 N TRP A 340 1950 2475 2131 669 170 136 N ATOM 1348 CA TRP A 340 4.114 37.458 12.039 1.00 19.85 C ANISOU 1348 CA TRP A 340 2274 2793 2476 631 135 148 C ATOM 1349 C TRP A 340 4.978 37.530 13.293 1.00 20.68 C ANISOU 1349 C TRP A 340 2399 2948 2510 669 164 116 C ATOM 1350 O TRP A 340 5.890 36.726 13.485 1.00 19.18 O ANISOU 1350 O TRP A 340 2220 2743 2323 640 135 101 O ATOM 1351 CB TRP A 340 4.961 37.071 10.810 1.00 18.53 C ANISOU 1351 CB TRP A 340 2146 2546 2347 572 75 85 C ATOM 1352 CG TRP A 340 5.799 38.160 10.242 1.00 18.22 C ANISOU 1352 CG TRP A 340 2172 2478 2273 574 80 -18 C ATOM 1353 CD1 TRP A 340 5.413 39.087 9.306 1.00 19.97 C ANISOU 1353 CD1 TRP A 340 2412 2670 2506 569 80 -45 C ATOM 1354 CD2 TRP A 340 7.180 38.423 10.530 1.00 18.90 C ANISOU 1354 CD2 TRP A 340 2308 2561 2311 575 79 -100 C ATOM 1355 NE1 TRP A 340 6.470 39.915 9.005 1.00 19.33 N ANISOU 1355 NE1 TRP A 340 2386 2569 2388 565 78 -133 N ATOM 1356 CE2 TRP A 340 7.559 39.536 9.747 1.00 17.82 C ANISOU 1356 CE2 TRP A 340 2215 2394 2161 570 77 -168 C ATOM 1357 CE3 TRP A 340 8.134 37.824 11.365 1.00 19.51 C ANISOU 1357 CE3 TRP A 340 2396 2657 2360 578 77 -117 C ATOM 1358 CZ2 TRP A 340 8.846 40.062 9.775 1.00 16.08 C ANISOU 1358 CZ2 TRP A 340 2045 2164 1903 565 72 -246 C ATOM 1359 CZ3 TRP A 340 9.422 38.357 11.402 1.00 19.33 C ANISOU 1359 CZ3 TRP A 340 2426 2623 2296 577 74 -202 C ATOM 1360 CH2 TRP A 340 9.766 39.460 10.610 1.00 19.92 C ANISOU 1360 CH2 TRP A 340 2540 2669 2361 570 71 -263 C ATOM 1361 N GLU A 341 4.679 38.484 14.168 1.00 20.98 N ANISOU 1361 N GLU A 341 2441 3046 2484 737 218 105 N ATOM 1362 CA GLU A 341 5.424 38.585 15.405 1.00 26.10 C ANISOU 1362 CA GLU A 341 3108 3748 3060 781 245 75 C ATOM 1363 C GLU A 341 5.351 37.269 16.181 1.00 20.91 C ANISOU 1363 C GLU A 341 2395 3137 2413 765 239 166 C ATOM 1364 O GLU A 341 6.324 36.861 16.828 1.00 24.76 O ANISOU 1364 O GLU A 341 2904 3635 2871 763 232 139 O ATOM 1365 CB GLU A 341 4.908 39.756 16.257 1.00 23.11 C ANISOU 1365 CB GLU A 341 2734 3436 2610 870 299 55 C ATOM 1366 CG GLU A 341 5.830 40.107 17.405 1.00 31.53 C ANISOU 1366 CG GLU A 341 3841 4544 3597 920 317 -6 C ATOM 1367 CD GLU A 341 5.309 41.275 18.227 1.00 42.08 C ANISOU 1367 CD GLU A 341 5186 5944 4859 1020 360 -38 C ATOM 1368 OE1 GLU A 341 4.109 41.595 18.101 1.00 42.28 O ANISOU 1368 OE1 GLU A 341 5168 6003 4892 1054 387 12 O ATOM 1369 OE2 GLU A 341 6.106 41.862 18.990 1.00 45.42 O ANISOU 1369 OE2 GLU A 341 5660 6381 5218 1066 363 -114 O ATOM 1370 N PHE A 342 4.215 36.585 16.099 1.00 20.34 N ANISOU 1370 N PHE A 342 2249 3089 2389 751 237 279 N ATOM 1371 CA PHE A 342 4.069 35.293 16.764 1.00 24.82 C ANISOU 1371 CA PHE A 342 2755 3695 2981 727 220 383 C ATOM 1372 C PHE A 342 5.135 34.280 16.333 1.00 26.73 C ANISOU 1372 C PHE A 342 3023 3862 3271 661 153 353 C ATOM 1373 O PHE A 342 5.531 33.418 17.108 1.00 24.31 O ANISOU 1373 O PHE A 342 2692 3583 2961 651 140 397 O ATOM 1374 CB PHE A 342 2.659 34.723 16.586 1.00 26.87 C ANISOU 1374 CB PHE A 342 2927 3980 3301 712 214 518 C ATOM 1375 CG PHE A 342 2.400 34.123 15.227 1.00 26.50 C ANISOU 1375 CG PHE A 342 2878 3834 3357 639 145 532 C ATOM 1376 CD1 PHE A 342 2.616 32.774 14.992 1.00 22.50 C ANISOU 1376 CD1 PHE A 342 2345 3279 2924 577 73 586 C ATOM 1377 CD2 PHE A 342 1.919 34.901 14.198 1.00 25.44 C ANISOU 1377 CD2 PHE A 342 2767 3654 3244 638 146 490 C ATOM 1378 CE1 PHE A 342 2.375 32.220 13.742 1.00 22.45 C ANISOU 1378 CE1 PHE A 342 2341 3181 3009 519 0 589 C ATOM 1379 CE2 PHE A 342 1.662 34.355 12.949 1.00 26.71 C ANISOU 1379 CE2 PHE A 342 2926 3729 3492 577 80 500 C ATOM 1380 CZ PHE A 342 1.901 33.014 12.718 1.00 27.39 C ANISOU 1380 CZ PHE A 342 2991 3768 3648 520 6 546 C ATOM 1381 N ILE A 343 5.608 34.387 15.100 1.00 21.22 N ANISOU 1381 N ILE A 343 2373 3074 2614 620 111 277 N ATOM 1382 CA ILE A 343 6.640 33.468 14.622 1.00 19.13 C ANISOU 1382 CA ILE A 343 2135 2744 2390 568 47 236 C ATOM 1383 C ILE A 343 7.968 33.747 15.303 1.00 21.02 C ANISOU 1383 C ILE A 343 2427 2998 2563 588 63 153 C ATOM 1384 O ILE A 343 8.708 32.824 15.667 1.00 20.70 O ANISOU 1384 O ILE A 343 2384 2947 2534 564 29 158 O ATOM 1385 CB ILE A 343 6.821 33.566 13.099 1.00 17.45 C ANISOU 1385 CB ILE A 343 1957 2446 2225 529 1 172 C ATOM 1386 CG1 ILE A 343 5.513 33.234 12.391 1.00 22.25 C ANISOU 1386 CG1 ILE A 343 2516 3032 2905 507 -25 255 C ATOM 1387 CG2 ILE A 343 7.925 32.623 12.647 1.00 20.27 C ANISOU 1387 CG2 ILE A 343 2340 2747 2613 489 -65 123 C ATOM 1388 CD1 ILE A 343 5.589 33.340 10.878 1.00 23.67 C ANISOU 1388 CD1 ILE A 343 2729 3138 3129 474 -72 195 C ATOM 1389 N VAL A 344 8.261 35.024 15.507 1.00 20.10 N ANISOU 1389 N VAL A 344 2355 2902 2379 631 111 79 N ATOM 1390 CA VAL A 344 9.474 35.404 16.217 1.00 22.34 C ANISOU 1390 CA VAL A 344 2689 3200 2598 653 125 2 C ATOM 1391 C VAL A 344 9.450 34.826 17.630 1.00 26.99 C ANISOU 1391 C VAL A 344 3243 3864 3150 681 146 66 C ATOM 1392 O VAL A 344 10.435 34.248 18.090 1.00 23.88 O ANISOU 1392 O VAL A 344 2864 3464 2744 666 125 44 O ATOM 1393 CB VAL A 344 9.623 36.925 16.292 1.00 24.83 C ANISOU 1393 CB VAL A 344 3055 3525 2854 700 163 -77 C ATOM 1394 CG1 VAL A 344 10.811 37.303 17.176 1.00 28.89 C ANISOU 1394 CG1 VAL A 344 3617 4056 3303 726 172 -146 C ATOM 1395 CG2 VAL A 344 9.753 37.516 14.891 1.00 23.07 C ANISOU 1395 CG2 VAL A 344 2865 3232 2667 666 138 -135 C ATOM 1396 N ASP A 345 8.317 34.975 18.313 1.00 25.43 N ANISOU 1396 N ASP A 345 2992 3740 2930 723 189 148 N ATOM 1397 CA ASP A 345 8.176 34.456 19.665 1.00 29.39 C ANISOU 1397 CA ASP A 345 3449 4330 3387 754 215 223 C ATOM 1398 C ASP A 345 8.203 32.933 19.710 1.00 28.15 C ANISOU 1398 C ASP A 345 3240 4157 3299 695 163 314 C ATOM 1399 O ASP A 345 8.790 32.353 20.617 1.00 26.41 O ANISOU 1399 O ASP A 345 3010 3972 3052 696 158 336 O ATOM 1400 CB ASP A 345 6.915 35.014 20.330 1.00 33.79 C ANISOU 1400 CB ASP A 345 3955 4985 3899 821 275 293 C ATOM 1401 CG ASP A 345 7.045 36.496 20.645 1.00 42.34 C ANISOU 1401 CG ASP A 345 5094 6094 4899 897 320 195 C ATOM 1402 OD1 ASP A 345 6.028 37.210 20.618 1.00 44.52 O ANISOU 1402 OD1 ASP A 345 5347 6411 5158 946 357 216 O ATOM 1403 OD2 ASP A 345 8.177 36.947 20.921 1.00 45.49 O ANISOU 1403 OD2 ASP A 345 5559 6469 5255 909 313 97 O ATOM 1404 N PHE A 346 7.579 32.295 18.724 1.00 22.15 N ANISOU 1404 N PHE A 346 2447 3339 2629 643 116 365 N ATOM 1405 CA PHE A 346 7.613 30.840 18.598 1.00 24.35 C ANISOU 1405 CA PHE A 346 2682 3580 2990 582 46 443 C ATOM 1406 C PHE A 346 9.048 30.331 18.452 1.00 27.70 C ANISOU 1406 C PHE A 346 3160 3943 3423 552 -2 358 C ATOM 1407 O PHE A 346 9.476 29.400 19.141 1.00 26.14 O ANISOU 1407 O PHE A 346 2938 3757 3238 533 -33 404 O ATOM 1408 CB PHE A 346 6.792 30.406 17.382 1.00 25.84 C ANISOU 1408 CB PHE A 346 2844 3699 3275 536 -7 484 C ATOM 1409 CG PHE A 346 6.707 28.913 17.204 1.00 29.56 C ANISOU 1409 CG PHE A 346 3269 4121 3843 476 -95 567 C ATOM 1410 CD1 PHE A 346 5.640 28.199 17.726 1.00 28.66 C ANISOU 1410 CD1 PHE A 346 3066 4051 3775 461 -109 722 C ATOM 1411 CD2 PHE A 346 7.682 28.229 16.494 1.00 26.37 C ANISOU 1411 CD2 PHE A 346 2908 3626 3487 437 -170 493 C ATOM 1412 CE1 PHE A 346 5.557 26.824 17.551 1.00 28.87 C ANISOU 1412 CE1 PHE A 346 3049 4020 3901 402 -206 802 C ATOM 1413 CE2 PHE A 346 7.608 26.859 16.326 1.00 27.71 C ANISOU 1413 CE2 PHE A 346 3038 3739 3751 388 -264 561 C ATOM 1414 CZ PHE A 346 6.540 26.158 16.848 1.00 30.27 C ANISOU 1414 CZ PHE A 346 3276 4097 4129 367 -287 717 C ATOM 1415 N VAL A 347 9.786 30.931 17.528 1.00 23.84 N ANISOU 1415 N VAL A 347 2739 3391 2928 546 -11 238 N ATOM 1416 CA VAL A 347 11.159 30.509 17.257 1.00 23.35 C ANISOU 1416 CA VAL A 347 2725 3274 2872 521 -55 152 C ATOM 1417 C VAL A 347 12.033 30.761 18.477 1.00 21.95 C ANISOU 1417 C VAL A 347 2570 3151 2618 552 -19 123 C ATOM 1418 O VAL A 347 12.963 30.008 18.744 1.00 28.00 O ANISOU 1418 O VAL A 347 3346 3895 3396 531 -58 106 O ATOM 1419 CB VAL A 347 11.734 31.233 16.012 1.00 23.81 C ANISOU 1419 CB VAL A 347 2843 3273 2929 513 -63 38 C ATOM 1420 CG1 VAL A 347 13.237 31.118 15.970 1.00 31.64 C ANISOU 1420 CG1 VAL A 347 3884 4238 3898 504 -85 -55 C ATOM 1421 CG2 VAL A 347 11.098 30.678 14.726 1.00 25.10 C ANISOU 1421 CG2 VAL A 347 2988 3373 3176 476 -120 58 C ATOM 1422 N ALA A 348 11.705 31.798 19.244 1.00 24.10 N ANISOU 1422 N ALA A 348 2851 3494 2813 607 50 120 N ATOM 1423 CA ALA A 348 12.504 32.167 20.413 1.00 21.82 C ANISOU 1423 CA ALA A 348 2590 3258 2444 646 83 84 C ATOM 1424 C ALA A 348 12.335 31.233 21.607 1.00 27.32 C ANISOU 1424 C ALA A 348 3231 4020 3130 649 83 184 C ATOM 1425 O ALA A 348 13.086 31.328 22.564 1.00 29.14 O ANISOU 1425 O ALA A 348 3483 4290 3300 674 99 158 O ATOM 1426 CB ALA A 348 12.221 33.609 20.841 1.00 24.67 C ANISOU 1426 CB ALA A 348 2981 3669 2722 713 147 36 C ATOM 1427 N THR A 349 11.348 30.346 21.569 1.00 25.43 N ANISOU 1427 N THR A 349 2918 3794 2950 623 61 304 N ATOM 1428 CA THR A 349 11.169 29.394 22.669 1.00 29.58 C ANISOU 1428 CA THR A 349 3381 4384 3475 617 52 417 C ATOM 1429 C THR A 349 12.374 28.459 22.640 1.00 35.32 C ANISOU 1429 C THR A 349 4132 5047 4243 571 -13 382 C ATOM 1430 O THR A 349 12.713 27.932 21.585 1.00 34.14 O ANISOU 1430 O THR A 349 4000 4802 4171 524 -77 343 O ATOM 1431 CB THR A 349 9.885 28.578 22.482 1.00 37.86 C ANISOU 1431 CB THR A 349 4341 5446 4599 585 26 562 C ATOM 1432 OG1 THR A 349 8.756 29.463 22.440 1.00 44.11 O ANISOU 1432 OG1 THR A 349 5108 6297 5355 630 88 593 O ATOM 1433 CG2 THR A 349 9.707 27.588 23.617 1.00 43.60 C ANISOU 1433 CG2 THR A 349 4995 6243 5329 573 12 693 C ATOM 1434 N PRO A 350 13.032 28.259 23.792 1.00 34.71 N ANISOU 1434 N PRO A 350 4325 5111 3753 886 -386 884 N ATOM 1435 CA PRO A 350 14.305 27.524 23.851 1.00 35.28 C ANISOU 1435 CA PRO A 350 4406 5114 3885 886 -485 840 C ATOM 1436 C PRO A 350 14.336 26.243 23.021 1.00 35.79 C ANISOU 1436 C PRO A 350 4433 5039 4126 811 -540 908 C ATOM 1437 O PRO A 350 15.276 26.034 22.250 1.00 33.79 O ANISOU 1437 O PRO A 350 4182 4685 3970 784 -602 789 O ATOM 1438 CB PRO A 350 14.434 27.186 25.335 1.00 40.50 C ANISOU 1438 CB PRO A 350 5081 5896 4413 968 -501 950 C ATOM 1439 CG PRO A 350 13.738 28.296 26.022 1.00 40.47 C ANISOU 1439 CG PRO A 350 5098 6036 4243 1036 -420 938 C ATOM 1440 CD PRO A 350 12.615 28.744 25.121 1.00 37.81 C ANISOU 1440 CD PRO A 350 4734 5668 3962 978 -338 948 C ATOM 1441 N GLU A 351 13.327 25.395 23.177 1.00 35.38 N ANISOU 1441 N GLU A 351 4342 4980 4119 783 -523 1096 N ATOM 1442 CA GLU A 351 13.309 24.119 22.474 1.00 37.80 C ANISOU 1442 CA GLU A 351 4612 5145 4606 718 -594 1165 C ATOM 1443 C GLU A 351 13.094 24.304 20.974 1.00 32.55 C ANISOU 1443 C GLU A 351 3938 4367 4061 653 -592 1054 C ATOM 1444 O GLU A 351 13.689 23.590 20.168 1.00 31.18 O ANISOU 1444 O GLU A 351 3757 4072 4018 621 -670 992 O ATOM 1445 CB GLU A 351 12.247 23.187 23.054 1.00 47.24 C ANISOU 1445 CB GLU A 351 5757 6355 5836 700 -583 1409 C ATOM 1446 CG GLU A 351 12.170 21.832 22.362 1.00 59.07 C ANISOU 1446 CG GLU A 351 7212 7690 7542 633 -675 1485 C ATOM 1447 CD GLU A 351 13.488 21.067 22.392 1.00 66.10 C ANISOU 1447 CD GLU A 351 8118 8498 8499 648 -788 1419 C ATOM 1448 OE1 GLU A 351 14.294 21.289 23.323 1.00 71.41 O ANISOU 1448 OE1 GLU A 351 8823 9256 9055 711 -799 1399 O ATOM 1449 OE2 GLU A 351 13.716 20.238 21.482 1.00 59.47 O ANISOU 1449 OE2 GLU A 351 7258 7507 7829 604 -872 1382 O ATOM 1450 N HIS A 352 12.249 25.260 20.598 1.00 24.77 N ANISOU 1450 N HIS A 352 2955 3428 3028 640 -506 1025 N ATOM 1451 CA HIS A 352 12.054 25.559 19.179 1.00 26.92 C ANISOU 1451 CA HIS A 352 3225 3609 3393 587 -501 915 C ATOM 1452 C HIS A 352 13.323 26.119 18.557 1.00 29.55 C ANISOU 1452 C HIS A 352 3591 3911 3724 598 -528 716 C ATOM 1453 O HIS A 352 13.721 25.716 17.466 1.00 26.29 O ANISOU 1453 O HIS A 352 3172 3397 3418 565 -573 635 O ATOM 1454 CB HIS A 352 10.889 26.527 18.964 1.00 25.53 C ANISOU 1454 CB HIS A 352 3044 3493 3161 576 -405 931 C ATOM 1455 CG HIS A 352 9.579 26.013 19.470 1.00 27.16 C ANISOU 1455 CG HIS A 352 3204 3733 3383 561 -369 1131 C ATOM 1456 ND1 HIS A 352 8.522 26.843 19.780 1.00 31.98 N ANISOU 1456 ND1 HIS A 352 3802 4440 3908 576 -273 1183 N ATOM 1457 CD2 HIS A 352 9.159 24.755 19.737 1.00 32.81 C ANISOU 1457 CD2 HIS A 352 3873 4397 4198 533 -416 1300 C ATOM 1458 CE1 HIS A 352 7.504 26.116 20.204 1.00 35.53 C ANISOU 1458 CE1 HIS A 352 4196 4904 4400 557 -255 1379 C ATOM 1459 NE2 HIS A 352 7.865 24.846 20.189 1.00 34.21 N ANISOU 1459 NE2 HIS A 352 4005 4643 4349 527 -343 1459 N ATOM 1460 N LEU A 353 13.958 27.051 19.250 1.00 28.32 N ANISOU 1460 N LEU A 353 3466 3845 3448 649 -503 637 N ATOM 1461 CA LEU A 353 15.171 27.657 18.726 1.00 26.11 C ANISOU 1461 CA LEU A 353 3205 3540 3176 657 -526 461 C ATOM 1462 C LEU A 353 16.201 26.574 18.430 1.00 25.14 C ANISOU 1462 C LEU A 353 3069 3329 3154 653 -617 432 C ATOM 1463 O LEU A 353 16.850 26.586 17.377 1.00 24.89 O ANISOU 1463 O LEU A 353 3031 3230 3197 632 -637 316 O ATOM 1464 CB LEU A 353 15.749 28.669 19.713 1.00 23.98 C ANISOU 1464 CB LEU A 353 2965 3370 2777 718 -511 394 C ATOM 1465 CG LEU A 353 16.924 29.469 19.148 1.00 24.55 C ANISOU 1465 CG LEU A 353 3044 3415 2871 718 -529 220 C ATOM 1466 CD1 LEU A 353 16.421 30.514 18.159 1.00 29.76 C ANISOU 1466 CD1 LEU A 353 3703 4062 3541 681 -463 149 C ATOM 1467 CD2 LEU A 353 17.720 30.118 20.258 1.00 29.12 C ANISOU 1467 CD2 LEU A 353 3645 4067 3352 783 -558 159 C ATOM 1468 N ARG A 354 16.318 25.620 19.347 1.00 25.57 N ANISOU 1468 N ARG A 354 3117 3389 3211 677 -671 543 N ATOM 1469 CA ARG A 354 17.288 24.532 19.211 1.00 29.60 C ANISOU 1469 CA ARG A 354 3613 3813 3820 681 -769 524 C ATOM 1470 C ARG A 354 17.025 23.695 17.965 1.00 27.98 C ANISOU 1470 C ARG A 354 3383 3485 3764 633 -807 512 C ATOM 1471 O ARG A 354 17.932 23.443 17.175 1.00 30.16 O ANISOU 1471 O ARG A 354 3652 3695 4113 636 -853 392 O ATOM 1472 CB ARG A 354 17.259 23.629 20.447 1.00 30.82 C ANISOU 1472 CB ARG A 354 3762 3993 3954 711 -820 676 C ATOM 1473 CG ARG A 354 18.267 22.484 20.405 1.00 41.84 C ANISOU 1473 CG ARG A 354 5142 5296 5457 721 -931 663 C ATOM 1474 CD ARG A 354 17.998 21.452 21.497 1.00 43.88 C ANISOU 1474 CD ARG A 354 5389 5563 5721 738 -983 852 C ATOM 1475 NE ARG A 354 16.804 20.652 21.220 1.00 57.07 N ANISOU 1475 NE ARG A 354 7025 7171 7487 687 -984 1008 N ATOM 1476 CZ ARG A 354 16.762 19.637 20.357 1.00 65.52 C ANISOU 1476 CZ ARG A 354 8066 8097 8731 648 -1062 1010 C ATOM 1477 NH1 ARG A 354 17.847 19.293 19.673 1.00 71.19 N ANISOU 1477 NH1 ARG A 354 8786 8730 9532 661 -1135 862 N ATOM 1478 NH2 ARG A 354 15.632 18.966 20.172 1.00 65.91 N ANISOU 1478 NH2 ARG A 354 8079 8087 8875 600 -1070 1156 N ATOM 1479 N GLN A 355 15.785 23.264 17.787 1.00 26.66 N ANISOU 1479 N GLN A 355 3197 3288 3642 596 -791 634 N ATOM 1480 CA GLN A 355 15.431 22.444 16.631 1.00 24.69 C ANISOU 1480 CA GLN A 355 2926 2916 3539 555 -843 622 C ATOM 1481 C GLN A 355 15.588 23.207 15.321 1.00 27.37 C ANISOU 1481 C GLN A 355 3278 3240 3881 542 -803 462 C ATOM 1482 O GLN A 355 16.156 22.705 14.360 1.00 30.16 O ANISOU 1482 O GLN A 355 3625 3515 4320 545 -859 363 O ATOM 1483 CB GLN A 355 13.986 21.974 16.728 1.00 30.51 C ANISOU 1483 CB GLN A 355 3635 3629 4328 514 -833 789 C ATOM 1484 CG GLN A 355 13.687 21.060 17.888 1.00 41.64 C ANISOU 1484 CG GLN A 355 5018 5043 5760 518 -873 981 C ATOM 1485 CD GLN A 355 12.276 20.529 17.807 1.00 49.01 C ANISOU 1485 CD GLN A 355 5907 5934 6780 468 -869 1148 C ATOM 1486 OE1 GLN A 355 11.818 20.139 16.733 1.00 43.55 O ANISOU 1486 OE1 GLN A 355 5198 5135 6213 428 -912 1112 O ATOM 1487 NE2 GLN A 355 11.570 20.531 18.932 1.00 55.45 N ANISOU 1487 NE2 GLN A 355 6700 6839 7529 474 -818 1331 N ATOM 1488 N ILE A 356 15.048 24.415 15.274 1.00 21.12 N ANISOU 1488 N ILE A 356 2503 2529 2993 533 -708 443 N ATOM 1489 CA ILE A 356 15.031 25.165 14.025 1.00 21.28 C ANISOU 1489 CA ILE A 356 2532 2538 3015 515 -665 320 C ATOM 1490 C ILE A 356 16.428 25.623 13.589 1.00 25.88 C ANISOU 1490 C ILE A 356 3122 3131 3581 542 -668 164 C ATOM 1491 O ILE A 356 16.778 25.500 12.413 1.00 27.41 O ANISOU 1491 O ILE A 356 3309 3278 3826 539 -681 68 O ATOM 1492 CB ILE A 356 14.047 26.342 14.096 1.00 21.44 C ANISOU 1492 CB ILE A 356 2565 2633 2950 497 -568 348 C ATOM 1493 CG1 ILE A 356 12.626 25.802 14.277 1.00 24.01 C ANISOU 1493 CG1 ILE A 356 2868 2937 3317 466 -565 500 C ATOM 1494 CG2 ILE A 356 14.109 27.184 12.829 1.00 19.68 C ANISOU 1494 CG2 ILE A 356 2352 2402 2723 480 -525 227 C ATOM 1495 CD1 ILE A 356 11.624 26.863 14.658 1.00 24.20 C ANISOU 1495 CD1 ILE A 356 2897 3049 3250 462 -471 551 C ATOM 1496 N CYS A 357 17.221 26.143 14.524 1.00 23.26 N ANISOU 1496 N CYS A 357 2798 2865 3177 573 -659 142 N ATOM 1497 CA CYS A 357 18.561 26.646 14.187 1.00 26.09 C ANISOU 1497 CA CYS A 357 3150 3234 3529 595 -662 5 C ATOM 1498 C CYS A 357 19.531 25.542 13.794 1.00 24.82 C ANISOU 1498 C CYS A 357 2967 3003 3462 617 -744 -47 C ATOM 1499 O CYS A 357 20.484 25.782 13.057 1.00 25.94 O ANISOU 1499 O CYS A 357 3090 3139 3626 630 -741 -163 O ATOM 1500 CB CYS A 357 19.162 27.459 15.341 1.00 23.43 C ANISOU 1500 CB CYS A 357 2824 2975 3103 626 -649 -11 C ATOM 1501 SG CYS A 357 18.356 29.040 15.631 1.00 25.82 S ANISOU 1501 SG CYS A 357 3150 3361 3299 616 -556 -11 S ATOM 1502 N SER A 358 19.301 24.342 14.316 1.00 22.63 N ANISOU 1502 N SER A 358 2685 2673 3242 624 -819 45 N ATOM 1503 CA SER A 358 20.156 23.194 14.050 1.00 27.52 C ANISOU 1503 CA SER A 358 3282 3214 3960 651 -912 3 C ATOM 1504 C SER A 358 19.742 22.417 12.803 1.00 23.35 C ANISOU 1504 C SER A 358 2743 2596 3532 641 -951 -32 C ATOM 1505 O SER A 358 20.130 21.264 12.615 1.00 27.21 O ANISOU 1505 O SER A 358 3216 3000 4121 665 -1046 -44 O ATOM 1506 CB SER A 358 20.168 22.280 15.275 1.00 30.04 C ANISOU 1506 CB SER A 358 3600 3514 4301 667 -987 124 C ATOM 1507 OG SER A 358 20.619 23.021 16.400 1.00 35.28 O ANISOU 1507 OG SER A 358 4278 4269 4858 690 -959 137 O ATOM 1508 N ASP A 359 18.967 23.074 11.951 1.00 24.00 N ANISOU 1508 N ASP A 359 2838 2696 3587 612 -885 -54 N ATOM 1509 CA ASP A 359 18.466 22.479 10.719 1.00 24.45 C ANISOU 1509 CA ASP A 359 2891 2678 3720 608 -920 -95 C ATOM 1510 C ASP A 359 18.954 23.268 9.504 1.00 21.92 C ANISOU 1510 C ASP A 359 2572 2401 3357 622 -857 -232 C ATOM 1511 O ASP A 359 19.071 24.480 9.554 1.00 21.18 O ANISOU 1511 O ASP A 359 2484 2388 3176 607 -767 -252 O ATOM 1512 CB ASP A 359 16.940 22.476 10.720 1.00 24.24 C ANISOU 1512 CB ASP A 359 2874 2631 3705 560 -904 19 C ATOM 1513 CG ASP A 359 16.371 21.868 9.461 1.00 22.16 C ANISOU 1513 CG ASP A 359 2610 2285 3526 558 -956 -28 C ATOM 1514 OD1 ASP A 359 16.292 20.624 9.389 1.00 29.58 O ANISOU 1514 OD1 ASP A 359 3533 3121 4583 569 -1067 -6 O ATOM 1515 OD2 ASP A 359 16.027 22.627 8.536 1.00 22.40 O ANISOU 1515 OD2 ASP A 359 2653 2349 3507 550 -896 -91 O ATOM 1516 N LYS A 360 19.230 22.565 8.414 1.00 24.03 N ANISOU 1516 N LYS A 360 2830 2613 3687 656 -910 -324 N ATOM 1517 CA LYS A 360 19.766 23.158 7.194 1.00 21.59 C ANISOU 1517 CA LYS A 360 2516 2353 3334 683 -854 -449 C ATOM 1518 C LYS A 360 18.886 24.281 6.642 1.00 22.86 C ANISOU 1518 C LYS A 360 2698 2569 3419 642 -760 -430 C ATOM 1519 O LYS A 360 19.374 25.333 6.212 1.00 25.91 O ANISOU 1519 O LYS A 360 3077 3033 3734 642 -674 -483 O ATOM 1520 CB LYS A 360 19.894 22.034 6.158 1.00 32.19 C ANISOU 1520 CB LYS A 360 3853 3622 4755 735 -943 -537 C ATOM 1521 CG LYS A 360 20.380 22.435 4.802 1.00 44.47 C ANISOU 1521 CG LYS A 360 5403 5233 6261 780 -894 -664 C ATOM 1522 CD LYS A 360 19.936 21.395 3.768 1.00 52.73 C ANISOU 1522 CD LYS A 360 6462 6203 7372 827 -989 -734 C ATOM 1523 CE LYS A 360 20.072 19.975 4.289 1.00 60.42 C ANISOU 1523 CE LYS A 360 7424 7057 8474 854 -1130 -725 C ATOM 1524 NZ LYS A 360 19.584 18.986 3.284 1.00 66.93 N ANISOU 1524 NZ LYS A 360 8261 7793 9376 902 -1240 -801 N ATOM 1525 N TYR A 361 17.579 24.056 6.640 1.00 20.02 N ANISOU 1525 N TYR A 361 2358 2165 3084 607 -781 -349 N ATOM 1526 CA TYR A 361 16.655 25.089 6.178 1.00 17.35 C ANISOU 1526 CA TYR A 361 2038 1871 2680 568 -700 -323 C ATOM 1527 C TYR A 361 16.268 26.054 7.285 1.00 19.24 C ANISOU 1527 C TYR A 361 2285 2170 2858 527 -629 -232 C ATOM 1528 O TYR A 361 16.163 27.254 7.046 1.00 18.78 O ANISOU 1528 O TYR A 361 2233 2174 2727 509 -544 -247 O ATOM 1529 CB TYR A 361 15.420 24.455 5.554 1.00 23.75 C ANISOU 1529 CB TYR A 361 2862 2610 3552 553 -758 -289 C ATOM 1530 CG TYR A 361 15.794 23.519 4.428 1.00 23.70 C ANISOU 1530 CG TYR A 361 2855 2546 3603 608 -841 -400 C ATOM 1531 CD1 TYR A 361 16.365 24.006 3.255 1.00 20.28 C ANISOU 1531 CD1 TYR A 361 2428 2174 3105 650 -795 -516 C ATOM 1532 CD2 TYR A 361 15.608 22.149 4.550 1.00 26.14 C ANISOU 1532 CD2 TYR A 361 3155 2745 4032 625 -968 -387 C ATOM 1533 CE1 TYR A 361 16.723 23.146 2.226 1.00 25.16 C ANISOU 1533 CE1 TYR A 361 3047 2755 3758 717 -870 -629 C ATOM 1534 CE2 TYR A 361 15.955 21.287 3.533 1.00 29.93 C ANISOU 1534 CE2 TYR A 361 3636 3169 4565 687 -1056 -504 C ATOM 1535 CZ TYR A 361 16.507 21.786 2.372 1.00 33.82 C ANISOU 1535 CZ TYR A 361 4139 3735 4975 739 -1006 -631 C ATOM 1536 OH TYR A 361 16.850 20.917 1.366 1.00 33.13 O ANISOU 1536 OH TYR A 361 4055 3605 4927 817 -1094 -757 O ATOM 1537 N GLY A 362 16.045 25.529 8.487 1.00 18.34 N ANISOU 1537 N GLY A 362 2166 2034 2770 518 -667 -136 N ATOM 1538 CA GLY A 362 15.651 26.354 9.608 1.00 18.60 C ANISOU 1538 CA GLY A 362 2206 2131 2732 495 -606 -52 C ATOM 1539 C GLY A 362 16.645 27.460 9.926 1.00 19.72 C ANISOU 1539 C GLY A 362 2348 2348 2797 509 -546 -121 C ATOM 1540 O GLY A 362 16.239 28.564 10.286 1.00 20.81 O ANISOU 1540 O GLY A 362 2496 2544 2865 492 -478 -100 O ATOM 1541 N CYS A 363 17.945 27.175 9.812 1.00 21.64 N ANISOU 1541 N CYS A 363 2573 2587 3061 542 -577 -204 N ATOM 1542 CA CYS A 363 18.943 28.191 10.136 1.00 18.16 C ANISOU 1542 CA CYS A 363 2121 2208 2570 551 -532 -265 C ATOM 1543 C CYS A 363 18.877 29.362 9.165 1.00 20.55 C ANISOU 1543 C CYS A 363 2421 2549 2837 531 -452 -319 C ATOM 1544 O CYS A 363 19.125 30.498 9.551 1.00 20.99 O ANISOU 1544 O CYS A 363 2474 2652 2849 520 -405 -332 O ATOM 1545 CB CYS A 363 20.370 27.621 10.208 1.00 21.68 C ANISOU 1545 CB CYS A 363 2537 2642 3059 590 -583 -338 C ATOM 1546 SG CYS A 363 21.052 26.998 8.657 1.00 29.35 S ANISOU 1546 SG CYS A 363 3481 3584 4087 621 -598 -445 S ATOM 1547 N ARG A 364 18.532 29.089 7.914 1.00 16.80 N ANISOU 1547 N ARG A 364 1948 2053 2384 529 -445 -349 N ATOM 1548 CA ARG A 364 18.320 30.163 6.932 1.00 18.31 C ANISOU 1548 CA ARG A 364 2140 2283 2536 509 -369 -380 C ATOM 1549 C ARG A 364 17.074 30.976 7.279 1.00 20.22 C ANISOU 1549 C ARG A 364 2409 2538 2737 470 -326 -307 C ATOM 1550 O ARG A 364 17.080 32.207 7.180 1.00 17.92 O ANISOU 1550 O ARG A 364 2115 2285 2407 451 -265 -317 O ATOM 1551 CB ARG A 364 18.224 29.594 5.510 1.00 17.45 C ANISOU 1551 CB ARG A 364 2031 2156 2445 529 -379 -432 C ATOM 1552 CG ARG A 364 17.951 30.644 4.402 1.00 21.93 C ANISOU 1552 CG ARG A 364 2600 2768 2963 513 -302 -451 C ATOM 1553 CD ARG A 364 18.876 31.884 4.501 1.00 21.97 C ANISOU 1553 CD ARG A 364 2573 2833 2943 499 -232 -472 C ATOM 1554 NE ARG A 364 20.274 31.550 4.199 1.00 25.92 N ANISOU 1554 NE ARG A 364 3028 3356 3465 538 -236 -541 N ATOM 1555 CZ ARG A 364 21.278 32.427 4.150 1.00 31.78 C ANISOU 1555 CZ ARG A 364 3724 4144 4209 531 -185 -563 C ATOM 1556 NH1 ARG A 364 21.063 33.718 4.368 1.00 26.36 N ANISOU 1556 NH1 ARG A 364 3034 3476 3507 487 -134 -528 N ATOM 1557 NH2 ARG A 364 22.507 32.009 3.867 1.00 32.30 N ANISOU 1557 NH2 ARG A 364 3740 4232 4302 570 -190 -621 N ATOM 1558 N VAL A 365 16.000 30.297 7.681 1.00 16.59 N ANISOU 1558 N VAL A 365 1968 2043 2294 461 -361 -231 N ATOM 1559 CA VAL A 365 14.798 31.012 8.121 1.00 16.72 C ANISOU 1559 CA VAL A 365 2001 2078 2272 432 -319 -156 C ATOM 1560 C VAL A 365 15.099 31.989 9.260 1.00 15.81 C ANISOU 1560 C VAL A 365 1887 2018 2101 436 -284 -148 C ATOM 1561 O VAL A 365 14.624 33.148 9.269 1.00 15.85 O ANISOU 1561 O VAL A 365 1900 2055 2065 421 -229 -145 O ATOM 1562 CB VAL A 365 13.691 30.042 8.589 1.00 14.82 C ANISOU 1562 CB VAL A 365 1765 1797 2069 422 -363 -56 C ATOM 1563 CG1 VAL A 365 12.515 30.825 9.178 1.00 15.98 C ANISOU 1563 CG1 VAL A 365 1919 1981 2171 402 -310 25 C ATOM 1564 CG2 VAL A 365 13.221 29.188 7.423 1.00 18.26 C ANISOU 1564 CG2 VAL A 365 2201 2168 2571 417 -411 -70 C ATOM 1565 N VAL A 366 15.874 31.524 10.235 1.00 15.08 N ANISOU 1565 N VAL A 366 1788 1932 2009 463 -324 -148 N ATOM 1566 CA VAL A 366 16.182 32.353 11.395 1.00 14.55 C ANISOU 1566 CA VAL A 366 1727 1917 1885 480 -309 -150 C ATOM 1567 C VAL A 366 17.062 33.509 10.960 1.00 17.80 C ANISOU 1567 C VAL A 366 2124 2347 2294 474 -278 -240 C ATOM 1568 O VAL A 366 16.856 34.632 11.406 1.00 17.05 O ANISOU 1568 O VAL A 366 2037 2283 2159 473 -248 -249 O ATOM 1569 CB VAL A 366 16.835 31.549 12.525 1.00 17.57 C ANISOU 1569 CB VAL A 366 2107 2305 2264 514 -370 -128 C ATOM 1570 CG1 VAL A 366 17.316 32.491 13.623 1.00 20.38 C ANISOU 1570 CG1 VAL A 366 2471 2718 2556 543 -365 -158 C ATOM 1571 CG2 VAL A 366 15.830 30.565 13.111 1.00 20.35 C ANISOU 1571 CG2 VAL A 366 2467 2647 2618 516 -393 -10 C ATOM 1572 N GLN A 367 18.017 33.264 10.059 1.00 16.79 N ANISOU 1572 N GLN A 367 1969 2198 2212 472 -285 -303 N ATOM 1573 CA GLN A 367 18.829 34.394 9.591 1.00 18.38 C ANISOU 1573 CA GLN A 367 2143 2417 2423 459 -249 -367 C ATOM 1574 C GLN A 367 17.985 35.420 8.841 1.00 20.34 C ANISOU 1574 C GLN A 367 2401 2673 2654 426 -187 -351 C ATOM 1575 O GLN A 367 18.170 36.626 8.991 1.00 16.19 O ANISOU 1575 O GLN A 367 1866 2160 2126 413 -162 -372 O ATOM 1576 CB GLN A 367 19.997 33.963 8.694 1.00 19.27 C ANISOU 1576 CB GLN A 367 2213 2523 2585 468 -253 -427 C ATOM 1577 CG GLN A 367 20.859 35.168 8.295 1.00 23.97 C ANISOU 1577 CG GLN A 367 2766 3139 3202 450 -212 -471 C ATOM 1578 CD GLN A 367 22.128 34.781 7.581 1.00 27.37 C ANISOU 1578 CD GLN A 367 3140 3579 3679 466 -210 -523 C ATOM 1579 OE1 GLN A 367 22.649 33.686 7.774 1.00 30.37 O ANISOU 1579 OE1 GLN A 367 3512 3946 4079 500 -258 -546 O ATOM 1580 NE2 GLN A 367 22.640 35.687 6.752 1.00 28.35 N ANISOU 1580 NE2 GLN A 367 3221 3727 3825 444 -155 -537 N ATOM 1581 N THR A 368 17.050 34.953 8.028 1.00 13.48 N ANISOU 1581 N THR A 368 1551 1790 1782 414 -172 -316 N ATOM 1582 CA THR A 368 16.170 35.883 7.325 1.00 15.35 C ANISOU 1582 CA THR A 368 1800 2032 2001 385 -120 -295 C ATOM 1583 C THR A 368 15.339 36.735 8.277 1.00 18.55 C ANISOU 1583 C THR A 368 2226 2452 2372 381 -105 -260 C ATOM 1584 O THR A 368 15.153 37.935 8.054 1.00 15.84 O ANISOU 1584 O THR A 368 1880 2115 2025 363 -70 -269 O ATOM 1585 CB THR A 368 15.255 35.128 6.361 1.00 15.43 C ANISOU 1585 CB THR A 368 1827 2020 2015 379 -122 -265 C ATOM 1586 OG1 THR A 368 16.074 34.534 5.352 1.00 20.87 O ANISOU 1586 OG1 THR A 368 2497 2707 2724 395 -131 -317 O ATOM 1587 CG2 THR A 368 14.225 36.081 5.707 1.00 16.72 C ANISOU 1587 CG2 THR A 368 2006 2189 2158 350 -75 -236 C ATOM 1588 N ILE A 369 14.828 36.114 9.329 1.00 16.05 N ANISOU 1588 N ILE A 369 1926 2143 2031 402 -133 -215 N ATOM 1589 CA ILE A 369 14.068 36.835 10.351 1.00 13.26 C ANISOU 1589 CA ILE A 369 1590 1820 1629 417 -118 -184 C ATOM 1590 C ILE A 369 14.937 37.900 11.033 1.00 14.04 C ANISOU 1590 C ILE A 369 1682 1938 1716 435 -127 -251 C ATOM 1591 O ILE A 369 14.526 39.058 11.195 1.00 15.59 O ANISOU 1591 O ILE A 369 1884 2143 1897 435 -105 -267 O ATOM 1592 CB ILE A 369 13.532 35.859 11.411 1.00 13.98 C ANISOU 1592 CB ILE A 369 1692 1931 1688 445 -144 -113 C ATOM 1593 CG1 ILE A 369 12.407 35.000 10.828 1.00 16.39 C ANISOU 1593 CG1 ILE A 369 1998 2209 2022 422 -140 -34 C ATOM 1594 CG2 ILE A 369 13.052 36.630 12.709 1.00 16.42 C ANISOU 1594 CG2 ILE A 369 2016 2299 1923 484 -129 -97 C ATOM 1595 CD1 ILE A 369 11.900 33.938 11.797 1.00 19.01 C ANISOU 1595 CD1 ILE A 369 2327 2552 2344 440 -167 59 C ATOM 1596 N ILE A 370 16.143 37.516 11.434 1.00 14.71 N ANISOU 1596 N ILE A 370 1750 2020 1818 452 -169 -295 N ATOM 1597 CA ILE A 370 17.066 38.468 12.064 1.00 18.59 C ANISOU 1597 CA ILE A 370 2227 2518 2316 468 -195 -365 C ATOM 1598 C ILE A 370 17.344 39.655 11.144 1.00 17.04 C ANISOU 1598 C ILE A 370 2006 2295 2174 430 -164 -402 C ATOM 1599 O ILE A 370 17.317 40.808 11.584 1.00 17.27 O ANISOU 1599 O ILE A 370 2034 2320 2206 436 -173 -437 O ATOM 1600 CB ILE A 370 18.395 37.797 12.437 1.00 15.57 C ANISOU 1600 CB ILE A 370 1821 2130 1963 487 -248 -405 C ATOM 1601 CG1 ILE A 370 18.197 36.807 13.579 1.00 18.79 C ANISOU 1601 CG1 ILE A 370 2256 2567 2316 531 -289 -364 C ATOM 1602 CG2 ILE A 370 19.428 38.833 12.838 1.00 20.03 C ANISOU 1602 CG2 ILE A 370 2360 2687 2564 493 -281 -482 C ATOM 1603 CD1 ILE A 370 19.396 35.881 13.789 1.00 19.20 C ANISOU 1603 CD1 ILE A 370 2285 2605 2405 548 -345 -390 C ATOM 1604 N GLU A 371 17.589 39.369 9.865 1.00 19.37 N ANISOU 1604 N GLU A 371 2277 2573 2510 395 -132 -392 N ATOM 1605 CA GLU A 371 17.843 40.416 8.871 1.00 18.66 C ANISOU 1605 CA GLU A 371 2157 2465 2468 356 -94 -404 C ATOM 1606 C GLU A 371 16.682 41.412 8.765 1.00 21.57 C ANISOU 1606 C GLU A 371 2550 2826 2819 342 -65 -377 C ATOM 1607 O GLU A 371 16.890 42.631 8.724 1.00 16.86 O ANISOU 1607 O GLU A 371 1934 2207 2263 325 -65 -399 O ATOM 1608 CB GLU A 371 18.170 39.785 7.510 1.00 20.05 C ANISOU 1608 CB GLU A 371 2310 2645 2664 336 -59 -390 C ATOM 1609 CG GLU A 371 19.562 39.136 7.496 1.00 20.01 C ANISOU 1609 CG GLU A 371 2262 2646 2696 351 -83 -431 C ATOM 1610 CD GLU A 371 19.817 38.270 6.279 1.00 30.13 C ANISOU 1610 CD GLU A 371 3527 3942 3977 355 -55 -428 C ATOM 1611 OE1 GLU A 371 20.995 37.966 6.013 1.00 29.35 O ANISOU 1611 OE1 GLU A 371 3380 3857 3915 367 -58 -462 O ATOM 1612 OE2 GLU A 371 18.846 37.876 5.607 1.00 29.32 O ANISOU 1612 OE2 GLU A 371 3460 3842 3840 354 -36 -397 O ATOM 1613 N LYS A 372 15.460 40.895 8.760 1.00 17.61 N ANISOU 1613 N LYS A 372 2086 2338 2268 349 -48 -329 N ATOM 1614 CA LYS A 372 14.285 41.760 8.680 1.00 16.15 C ANISOU 1614 CA LYS A 372 1921 2148 2066 342 -21 -302 C ATOM 1615 C LYS A 372 14.101 42.575 9.975 1.00 19.05 C ANISOU 1615 C LYS A 372 2302 2527 2410 380 -49 -336 C ATOM 1616 O LYS A 372 13.550 43.670 9.948 1.00 22.52 O ANISOU 1616 O LYS A 372 2746 2951 2860 378 -39 -345 O ATOM 1617 CB LYS A 372 13.032 40.927 8.386 1.00 17.08 C ANISOU 1617 CB LYS A 372 2066 2277 2148 342 -1 -237 C ATOM 1618 CG LYS A 372 11.748 41.745 8.250 1.00 20.98 C ANISOU 1618 CG LYS A 372 2575 2768 2629 336 29 -205 C ATOM 1619 CD LYS A 372 11.860 42.811 7.155 1.00 25.45 C ANISOU 1619 CD LYS A 372 3127 3305 3238 299 53 -213 C ATOM 1620 CE LYS A 372 12.223 42.213 5.792 1.00 26.86 C ANISOU 1620 CE LYS A 372 3296 3478 3432 270 71 -197 C ATOM 1621 NZ LYS A 372 12.132 43.233 4.678 1.00 26.90 N ANISOU 1621 NZ LYS A 372 3290 3468 3465 236 102 -181 N ATOM 1622 N LEU A 373 14.583 42.046 11.097 1.00 15.26 N ANISOU 1622 N LEU A 373 1829 2073 1895 422 -89 -360 N ATOM 1623 CA LEU A 373 14.463 42.718 12.399 1.00 17.59 C ANISOU 1623 CA LEU A 373 2142 2394 2148 477 -123 -403 C ATOM 1624 C LEU A 373 15.630 43.674 12.696 1.00 18.07 C ANISOU 1624 C LEU A 373 2179 2420 2268 481 -177 -490 C ATOM 1625 O LEU A 373 15.699 44.283 13.761 1.00 20.25 O ANISOU 1625 O LEU A 373 2468 2710 2515 533 -224 -548 O ATOM 1626 CB LEU A 373 14.332 41.687 13.530 1.00 16.47 C ANISOU 1626 CB LEU A 373 2023 2309 1927 530 -143 -377 C ATOM 1627 CG LEU A 373 13.076 40.812 13.506 1.00 20.22 C ANISOU 1627 CG LEU A 373 2513 2816 2352 533 -100 -280 C ATOM 1628 CD1 LEU A 373 13.078 39.802 14.656 1.00 20.45 C ANISOU 1628 CD1 LEU A 373 2556 2901 2312 582 -122 -238 C ATOM 1629 CD2 LEU A 373 11.805 41.668 13.541 1.00 20.54 C ANISOU 1629 CD2 LEU A 373 2566 2875 2364 546 -60 -261 C ATOM 1630 N THR A 374 16.528 43.827 11.735 1.00 16.82 N ANISOU 1630 N THR A 374 1979 2219 2195 428 -172 -498 N ATOM 1631 CA THR A 374 17.696 44.667 11.917 1.00 20.51 C ANISOU 1631 CA THR A 374 2405 2644 2743 419 -225 -564 C ATOM 1632 C THR A 374 17.418 46.103 11.452 1.00 21.00 C ANISOU 1632 C THR A 374 2450 2653 2875 390 -223 -576 C ATOM 1633 O THR A 374 16.844 46.314 10.385 1.00 21.91 O ANISOU 1633 O THR A 374 2560 2756 3008 347 -166 -520 O ATOM 1634 CB THR A 374 18.893 44.092 11.145 1.00 18.28 C ANISOU 1634 CB THR A 374 2071 2348 2525 380 -217 -556 C ATOM 1635 OG1 THR A 374 19.220 42.801 11.680 1.00 18.71 O ANISOU 1635 OG1 THR A 374 2141 2440 2527 413 -235 -555 O ATOM 1636 CG2 THR A 374 20.096 45.004 11.273 1.00 22.84 C ANISOU 1636 CG2 THR A 374 2592 2878 3209 362 -269 -611 C ATOM 1637 N ALA A 375 17.829 47.083 12.251 1.00 20.71 N ANISOU 1637 N ALA A 375 2404 2581 2883 417 -296 -652 N ATOM 1638 CA ALA A 375 17.639 48.489 11.889 1.00 24.78 C ANISOU 1638 CA ALA A 375 2898 3029 3487 391 -314 -668 C ATOM 1639 C ALA A 375 18.719 48.931 10.905 1.00 24.40 C ANISOU 1639 C ALA A 375 2776 2924 3573 317 -311 -642 C ATOM 1640 O ALA A 375 19.615 49.711 11.247 1.00 27.27 O ANISOU 1640 O ALA A 375 3093 3227 4041 309 -384 -694 O ATOM 1641 CB ALA A 375 17.654 49.375 13.140 1.00 26.15 C ANISOU 1641 CB ALA A 375 3090 3180 3667 457 -408 -771 C ATOM 1642 N ASP A 376 18.649 48.421 9.683 1.00 20.95 N ANISOU 1642 N ASP A 376 2321 2508 3132 267 -229 -558 N ATOM 1643 CA ASP A 376 19.660 48.748 8.687 1.00 20.59 C ANISOU 1643 CA ASP A 376 2197 2431 3194 203 -207 -516 C ATOM 1644 C ASP A 376 19.078 49.664 7.610 1.00 22.02 C ANISOU 1644 C ASP A 376 2363 2579 3426 153 -162 -445 C ATOM 1645 O ASP A 376 17.939 50.118 7.726 1.00 25.41 O ANISOU 1645 O ASP A 376 2840 2997 3819 169 -160 -444 O ATOM 1646 CB ASP A 376 20.252 47.471 8.072 1.00 23.97 C ANISOU 1646 CB ASP A 376 2608 2919 3580 195 -153 -481 C ATOM 1647 CG ASP A 376 19.194 46.564 7.484 1.00 34.59 C ANISOU 1647 CG ASP A 376 4010 4319 4815 206 -85 -432 C ATOM 1648 OD1 ASP A 376 18.101 47.067 7.146 1.00 28.90 O ANISOU 1648 OD1 ASP A 376 3322 3589 4070 198 -60 -400 O ATOM 1649 OD2 ASP A 376 19.457 45.351 7.357 1.00 41.96 O ANISOU 1649 OD2 ASP A 376 4951 5298 5695 224 -66 -429 O ATOM 1650 N SER A 377 19.851 49.934 6.562 1.00 23.81 N ANISOU 1650 N SER A 377 2519 2795 3734 96 -123 -380 N ATOM 1651 CA SER A 377 19.425 50.898 5.552 1.00 26.85 C ANISOU 1651 CA SER A 377 2880 3145 4177 46 -86 -300 C ATOM 1652 C SER A 377 18.141 50.447 4.850 1.00 27.10 C ANISOU 1652 C SER A 377 2977 3227 4095 56 -18 -251 C ATOM 1653 O SER A 377 17.380 51.271 4.340 1.00 30.05 O ANISOU 1653 O SER A 377 3359 3566 4492 34 -7 -205 O ATOM 1654 CB SER A 377 20.542 51.158 4.534 1.00 34.35 C ANISOU 1654 CB SER A 377 3734 4097 5221 -12 -44 -221 C ATOM 1655 OG SER A 377 20.858 49.983 3.813 1.00 39.50 O ANISOU 1655 OG SER A 377 4383 4840 5786 -2 32 -189 O ATOM 1656 N MET A 378 17.877 49.144 4.863 1.00 24.10 N ANISOU 1656 N MET A 378 2640 2916 3601 90 15 -263 N ATOM 1657 CA MET A 378 16.683 48.616 4.203 1.00 27.78 C ANISOU 1657 CA MET A 378 3162 3422 3969 99 67 -221 C ATOM 1658 C MET A 378 15.384 48.853 4.972 1.00 29.19 C ANISOU 1658 C MET A 378 3403 3584 4104 133 39 -249 C ATOM 1659 O MET A 378 14.298 48.697 4.410 1.00 30.29 O ANISOU 1659 O MET A 378 3579 3739 4189 133 74 -208 O ATOM 1660 CB MET A 378 16.850 47.126 3.889 1.00 30.39 C ANISOU 1660 CB MET A 378 3511 3822 4214 123 101 -222 C ATOM 1661 CG MET A 378 17.950 46.852 2.867 1.00 46.81 C ANISOU 1661 CG MET A 378 5531 5939 6317 102 147 -186 C ATOM 1662 SD MET A 378 17.714 45.300 1.991 1.00106.11 S ANISOU 1662 SD MET A 378 13074 13525 13717 135 192 -178 S ATOM 1663 CE MET A 378 16.283 45.710 0.994 1.00 91.31 C ANISOU 1663 CE MET A 378 11247 11654 11792 122 227 -115 C ATOM 1664 N ASN A 379 15.489 49.226 6.247 1.00 21.58 N ANISOU 1664 N ASN A 379 2448 2592 3159 166 -24 -322 N ATOM 1665 CA ASN A 379 14.306 49.495 7.069 1.00 18.30 C ANISOU 1665 CA ASN A 379 2084 2174 2694 212 -47 -354 C ATOM 1666 C ASN A 379 14.059 50.980 7.361 1.00 19.46 C ANISOU 1666 C ASN A 379 2220 2249 2925 212 -96 -384 C ATOM 1667 O ASN A 379 13.229 51.315 8.196 1.00 18.10 O ANISOU 1667 O ASN A 379 2084 2077 2717 265 -124 -430 O ATOM 1668 CB ASN A 379 14.383 48.742 8.403 1.00 21.19 C ANISOU 1668 CB ASN A 379 2481 2582 2989 274 -82 -417 C ATOM 1669 CG ASN A 379 13.902 47.312 8.295 1.00 30.20 C ANISOU 1669 CG ASN A 379 3653 3787 4034 288 -38 -378 C ATOM 1670 OD1 ASN A 379 14.439 46.412 8.949 1.00 30.64 O ANISOU 1670 OD1 ASN A 379 3715 3876 4052 314 -57 -402 O ATOM 1671 ND2 ASN A 379 12.880 47.091 7.475 1.00 20.18 N ANISOU 1671 ND2 ASN A 379 2403 2529 2734 270 10 -316 N ATOM 1672 N VAL A 380 14.740 51.877 6.661 1.00 16.74 N ANISOU 1672 N VAL A 380 1822 1844 2695 158 -107 -353 N ATOM 1673 CA VAL A 380 14.549 53.297 6.949 1.00 16.81 C ANISOU 1673 CA VAL A 380 1815 1765 2806 158 -171 -384 C ATOM 1674 C VAL A 380 13.134 53.795 6.655 1.00 17.08 C ANISOU 1674 C VAL A 380 1888 1789 2813 171 -151 -357 C ATOM 1675 O VAL A 380 12.746 54.865 7.129 1.00 24.46 O ANISOU 1675 O VAL A 380 2825 2659 3811 195 -212 -404 O ATOM 1676 CB VAL A 380 15.571 54.178 6.209 1.00 25.85 C ANISOU 1676 CB VAL A 380 2883 2838 4102 87 -189 -334 C ATOM 1677 CG1 VAL A 380 16.973 53.872 6.714 1.00 30.11 C ANISOU 1677 CG1 VAL A 380 3374 3373 4693 82 -229 -378 C ATOM 1678 CG2 VAL A 380 15.465 53.966 4.695 1.00 26.68 C ANISOU 1678 CG2 VAL A 380 2967 2976 4194 29 -99 -210 C ATOM 1679 N ASP A 381 12.357 53.023 5.895 1.00 19.91 N ANISOU 1679 N ASP A 381 2275 2207 3081 161 -76 -288 N ATOM 1680 CA ASP A 381 10.978 53.418 5.583 1.00 21.41 C ANISOU 1680 CA ASP A 381 2497 2390 3246 174 -58 -259 C ATOM 1681 C ASP A 381 9.962 53.095 6.688 1.00 22.44 C ANISOU 1681 C ASP A 381 2675 2563 3289 250 -68 -319 C ATOM 1682 O ASP A 381 8.794 53.479 6.595 1.00 21.12 O ANISOU 1682 O ASP A 381 2527 2390 3106 271 -58 -305 O ATOM 1683 CB ASP A 381 10.519 52.755 4.290 1.00 17.27 C ANISOU 1683 CB ASP A 381 1983 1910 2669 136 15 -163 C ATOM 1684 CG ASP A 381 10.467 51.260 4.419 1.00 26.36 C ANISOU 1684 CG ASP A 381 3161 3142 3713 157 52 -165 C ATOM 1685 OD1 ASP A 381 11.507 50.678 4.792 1.00 22.05 O ANISOU 1685 OD1 ASP A 381 2599 2617 3162 158 45 -196 O ATOM 1686 OD2 ASP A 381 9.397 50.670 4.172 1.00 24.77 O ANISOU 1686 OD2 ASP A 381 2993 2976 3444 171 82 -135 O ATOM 1687 N LEU A 382 10.385 52.386 7.733 1.00 23.95 N ANISOU 1687 N LEU A 382 2880 2802 3419 296 -84 -379 N ATOM 1688 CA LEU A 382 9.474 52.106 8.849 1.00 19.28 C ANISOU 1688 CA LEU A 382 2325 2264 2736 375 -87 -425 C ATOM 1689 C LEU A 382 9.120 53.372 9.635 1.00 22.58 C ANISOU 1689 C LEU A 382 2747 2637 3197 433 -151 -508 C ATOM 1690 O LEU A 382 9.968 54.245 9.821 1.00 21.93 O ANISOU 1690 O LEU A 382 2640 2482 3210 425 -220 -566 O ATOM 1691 CB LEU A 382 10.102 51.086 9.815 1.00 18.10 C ANISOU 1691 CB LEU A 382 2188 2179 2510 414 -95 -463 C ATOM 1692 CG LEU A 382 10.343 49.679 9.280 1.00 19.95 C ANISOU 1692 CG LEU A 382 2425 2463 2692 379 -44 -396 C ATOM 1693 CD1 LEU A 382 10.979 48.836 10.381 1.00 21.86 C ANISOU 1693 CD1 LEU A 382 2677 2757 2871 424 -68 -438 C ATOM 1694 CD2 LEU A 382 9.049 49.052 8.824 1.00 25.72 C ANISOU 1694 CD2 LEU A 382 3175 3232 3365 377 13 -323 C ATOM 1695 N THR A 383 7.880 53.458 10.121 1.00 21.67 N ANISOU 1695 N THR A 383 2655 2562 3015 495 -132 -518 N ATOM 1696 CA THR A 383 7.510 54.511 11.067 1.00 20.94 C ANISOU 1696 CA THR A 383 2572 2449 2936 577 -194 -618 C ATOM 1697 C THR A 383 8.277 54.283 12.363 1.00 23.63 C ANISOU 1697 C THR A 383 2926 2830 3221 647 -245 -714 C ATOM 1698 O THR A 383 8.751 53.179 12.615 1.00 20.90 O ANISOU 1698 O THR A 383 2588 2549 2804 641 -216 -687 O ATOM 1699 CB THR A 383 6.004 54.495 11.436 1.00 26.39 C ANISOU 1699 CB THR A 383 3280 3202 3545 646 -150 -608 C ATOM 1700 OG1 THR A 383 5.640 53.210 11.968 1.00 21.97 O ANISOU 1700 OG1 THR A 383 2736 2755 2858 676 -88 -565 O ATOM 1701 CG2 THR A 383 5.133 54.825 10.240 1.00 21.08 C ANISOU 1701 CG2 THR A 383 2595 2485 2929 589 -113 -524 C ATOM 1702 N SER A 384 8.382 55.306 13.210 1.00 24.63 N ANISOU 1702 N SER A 384 3057 2921 3379 721 -330 -831 N ATOM 1703 CA SER A 384 9.073 55.104 14.479 1.00 29.21 C ANISOU 1703 CA SER A 384 3656 3548 3895 801 -389 -931 C ATOM 1704 C SER A 384 8.324 54.086 15.345 1.00 24.71 C ANISOU 1704 C SER A 384 3118 3124 3146 881 -322 -909 C ATOM 1705 O SER A 384 8.933 53.337 16.107 1.00 25.03 O ANISOU 1705 O SER A 384 3173 3230 3106 915 -333 -929 O ATOM 1706 CB SER A 384 9.288 56.429 15.226 1.00 36.03 C ANISOU 1706 CB SER A 384 4521 4341 4826 877 -508 -1076 C ATOM 1707 OG SER A 384 8.065 56.912 15.731 1.00 43.40 O ANISOU 1707 OG SER A 384 5477 5320 5692 974 -497 -1121 O ATOM 1708 N ALA A 385 7.001 54.051 15.219 1.00 25.49 N ANISOU 1708 N ALA A 385 3222 3273 3190 909 -254 -859 N ATOM 1709 CA ALA A 385 6.218 53.081 15.971 1.00 25.24 C ANISOU 1709 CA ALA A 385 3207 3381 3004 977 -182 -811 C ATOM 1710 C ALA A 385 6.587 51.666 15.534 1.00 22.71 C ANISOU 1710 C ALA A 385 2881 3096 2653 899 -123 -699 C ATOM 1711 O ALA A 385 6.759 50.776 16.369 1.00 22.67 O ANISOU 1711 O ALA A 385 2889 3183 2543 945 -107 -683 O ATOM 1712 CB ALA A 385 4.728 53.338 15.785 1.00 27.48 C ANISOU 1712 CB ALA A 385 3481 3701 3260 1009 -119 -766 C ATOM 1713 N ALA A 386 6.722 51.469 14.224 1.00 19.50 N ANISOU 1713 N ALA A 386 2456 2616 2337 788 -97 -622 N ATOM 1714 CA ALA A 386 7.129 50.178 13.671 1.00 17.73 C ANISOU 1714 CA ALA A 386 2225 2409 2100 716 -54 -530 C ATOM 1715 C ALA A 386 8.568 49.811 14.027 1.00 20.30 C ANISOU 1715 C ALA A 386 2553 2724 2437 705 -105 -577 C ATOM 1716 O ALA A 386 8.900 48.629 14.160 1.00 17.04 O ANISOU 1716 O ALA A 386 2143 2357 1974 691 -81 -526 O ATOM 1717 CB ALA A 386 6.920 50.158 12.138 1.00 22.43 C ANISOU 1717 CB ALA A 386 2804 2936 2783 615 -20 -452 C ATOM 1718 N GLN A 387 9.432 50.815 14.167 1.00 19.91 N ANISOU 1718 N GLN A 387 2496 2603 2465 709 -182 -671 N ATOM 1719 CA GLN A 387 10.814 50.562 14.596 1.00 21.16 C ANISOU 1719 CA GLN A 387 2649 2748 2644 705 -241 -724 C ATOM 1720 C GLN A 387 10.817 50.088 16.041 1.00 19.93 C ANISOU 1720 C GLN A 387 2524 2689 2360 809 -265 -774 C ATOM 1721 O GLN A 387 11.599 49.222 16.430 1.00 19.26 O ANISOU 1721 O GLN A 387 2442 2638 2239 809 -278 -766 O ATOM 1722 CB GLN A 387 11.664 51.829 14.466 1.00 26.93 C ANISOU 1722 CB GLN A 387 3356 3373 3505 688 -330 -812 C ATOM 1723 CG GLN A 387 11.935 52.257 13.040 1.00 26.91 C ANISOU 1723 CG GLN A 387 3313 3278 3632 581 -309 -749 C ATOM 1724 CD GLN A 387 13.076 51.479 12.397 1.00 24.63 C ANISOU 1724 CD GLN A 387 2993 2980 3385 507 -292 -700 C ATOM 1725 OE1 GLN A 387 13.561 50.495 12.946 1.00 24.58 O ANISOU 1725 OE1 GLN A 387 2998 3032 3310 529 -291 -705 O ATOM 1726 NE2 GLN A 387 13.519 51.937 11.228 1.00 23.47 N ANISOU 1726 NE2 GLN A 387 2804 2763 3350 423 -279 -649 N ATOM 1727 N ASN A 388 9.946 50.666 16.853 1.00 21.10 N ANISOU 1727 N ASN A 388 2693 2888 2435 904 -271 -824 N ATOM 1728 CA ASN A 388 9.875 50.227 18.232 1.00 26.04 C ANISOU 1728 CA ASN A 388 3350 3627 2918 1014 -284 -861 C ATOM 1729 C ASN A 388 9.426 48.783 18.316 1.00 24.60 C ANISOU 1729 C ASN A 388 3170 3538 2639 1002 -199 -733 C ATOM 1730 O ASN A 388 9.979 47.995 19.089 1.00 26.15 O ANISOU 1730 O ASN A 388 3380 3798 2759 1038 -216 -727 O ATOM 1731 CB ASN A 388 8.958 51.116 19.066 1.00 32.61 C ANISOU 1731 CB ASN A 388 4201 4513 3676 1133 -297 -939 C ATOM 1732 CG ASN A 388 9.296 51.047 20.540 1.00 55.10 C ANISOU 1732 CG ASN A 388 7083 7460 6393 1263 -351 -1027 C ATOM 1733 OD1 ASN A 388 8.575 50.435 21.328 1.00 61.31 O ANISOU 1733 OD1 ASN A 388 7884 8382 7029 1344 -292 -978 O ATOM 1734 ND2 ASN A 388 10.429 51.638 20.912 1.00 61.96 N ANISOU 1734 ND2 ASN A 388 7959 8263 7320 1282 -467 -1151 N ATOM 1735 N LEU A 389 8.420 48.441 17.519 1.00 19.17 N ANISOU 1735 N LEU A 389 2466 2853 1966 950 -117 -628 N ATOM 1736 CA LEU A 389 7.941 47.066 17.448 1.00 20.30 C ANISOU 1736 CA LEU A 389 2601 3060 2051 924 -47 -498 C ATOM 1737 C LEU A 389 9.049 46.109 17.014 1.00 21.44 C ANISOU 1737 C LEU A 389 2741 3164 2242 851 -67 -467 C ATOM 1738 O LEU A 389 9.229 45.033 17.604 1.00 21.25 O ANISOU 1738 O LEU A 389 2722 3203 2151 871 -59 -411 O ATOM 1739 CB LEU A 389 6.762 46.969 16.483 1.00 21.51 C ANISOU 1739 CB LEU A 389 2734 3195 2246 869 24 -404 C ATOM 1740 CG LEU A 389 6.096 45.600 16.407 1.00 20.68 C ANISOU 1740 CG LEU A 389 2612 3145 2101 843 88 -265 C ATOM 1741 CD1 LEU A 389 5.206 45.382 17.627 1.00 23.79 C ANISOU 1741 CD1 LEU A 389 3002 3667 2368 943 131 -222 C ATOM 1742 CD2 LEU A 389 5.278 45.461 15.149 1.00 24.30 C ANISOU 1742 CD2 LEU A 389 3048 3546 2638 763 130 -189 C ATOM 1743 N ARG A 390 9.784 46.504 15.982 1.00 17.92 N ANISOU 1743 N ARG A 390 2280 2617 1913 771 -94 -497 N ATOM 1744 CA ARG A 390 10.920 45.719 15.484 1.00 15.88 C ANISOU 1744 CA ARG A 390 2009 2318 1707 708 -114 -482 C ATOM 1745 C ARG A 390 11.986 45.569 16.566 1.00 20.61 C ANISOU 1745 C ARG A 390 2620 2946 2267 763 -182 -553 C ATOM 1746 O ARG A 390 12.551 44.489 16.758 1.00 25.21 O ANISOU 1746 O ARG A 390 3201 3551 2826 754 -188 -515 O ATOM 1747 CB ARG A 390 11.547 46.408 14.271 1.00 15.34 C ANISOU 1747 CB ARG A 390 1915 2149 1764 628 -127 -508 C ATOM 1748 CG ARG A 390 12.726 45.629 13.650 1.00 16.58 C ANISOU 1748 CG ARG A 390 2050 2273 1976 568 -138 -493 C ATOM 1749 CD ARG A 390 13.645 46.524 12.789 1.00 20.53 C ANISOU 1749 CD ARG A 390 2515 2691 2595 509 -164 -535 C ATOM 1750 NE ARG A 390 13.960 47.750 13.518 1.00 20.91 N ANISOU 1750 NE ARG A 390 2562 2707 2677 550 -232 -628 N ATOM 1751 CZ ARG A 390 14.756 47.815 14.580 1.00 22.86 C ANISOU 1751 CZ ARG A 390 2813 2966 2908 603 -304 -707 C ATOM 1752 NH1 ARG A 390 15.371 46.724 15.031 1.00 22.21 N ANISOU 1752 NH1 ARG A 390 2734 2927 2776 617 -313 -695 N ATOM 1753 NH2 ARG A 390 14.939 48.978 15.195 1.00 24.38 N ANISOU 1753 NH2 ARG A 390 3005 3120 3137 645 -377 -802 N ATOM 1754 N GLU A 391 12.274 46.666 17.256 1.00 21.27 N ANISOU 1754 N GLU A 391 2713 3020 2348 823 -244 -661 N ATOM 1755 CA GLU A 391 13.350 46.678 18.250 1.00 22.84 C ANISOU 1755 CA GLU A 391 2922 3234 2521 879 -328 -747 C ATOM 1756 C GLU A 391 13.067 45.679 19.357 1.00 27.23 C ANISOU 1756 C GLU A 391 3506 3907 2932 955 -313 -702 C ATOM 1757 O GLU A 391 13.961 44.940 19.789 1.00 27.15 O ANISOU 1757 O GLU A 391 3499 3912 2905 962 -353 -703 O ATOM 1758 CB GLU A 391 13.528 48.081 18.839 1.00 27.12 C ANISOU 1758 CB GLU A 391 3473 3745 3086 943 -409 -880 C ATOM 1759 CG GLU A 391 14.928 48.342 19.383 1.00 37.55 C ANISOU 1759 CG GLU A 391 4786 5024 4456 961 -519 -983 C ATOM 1760 CD GLU A 391 15.963 48.451 18.271 1.00 43.00 C ANISOU 1760 CD GLU A 391 5425 5605 5310 849 -535 -972 C ATOM 1761 OE1 GLU A 391 16.561 47.421 17.914 1.00 33.33 O ANISOU 1761 OE1 GLU A 391 4183 4388 4094 800 -509 -910 O ATOM 1762 OE2 GLU A 391 16.165 49.562 17.732 1.00 43.70 O ANISOU 1762 OE2 GLU A 391 5485 5600 5521 811 -571 -1018 O ATOM 1763 N ARG A 392 11.818 45.652 19.812 1.00 24.46 N ANISOU 1763 N ARG A 392 3172 3641 2481 1013 -255 -652 N ATOM 1764 CA ARG A 392 11.420 44.737 20.880 1.00 35.56 C ANISOU 1764 CA ARG A 392 4598 5172 3743 1089 -228 -584 C ATOM 1765 C ARG A 392 11.458 43.282 20.434 1.00 30.44 C ANISOU 1765 C ARG A 392 3932 4524 3112 1019 -184 -451 C ATOM 1766 O ARG A 392 11.906 42.410 21.183 1.00 24.63 O ANISOU 1766 O ARG A 392 3206 3844 2310 1053 -205 -414 O ATOM 1767 CB ARG A 392 10.032 45.082 21.423 1.00 36.33 C ANISOU 1767 CB ARG A 392 4702 5366 3734 1169 -164 -551 C ATOM 1768 CG ARG A 392 9.936 46.461 22.046 1.00 47.77 C ANISOU 1768 CG ARG A 392 6173 6829 5148 1265 -217 -695 C ATOM 1769 CD ARG A 392 8.804 46.543 23.060 1.00 58.03 C ANISOU 1769 CD ARG A 392 7485 8277 6287 1389 -162 -669 C ATOM 1770 NE ARG A 392 7.480 46.540 22.443 1.00 69.19 N ANISOU 1770 NE ARG A 392 8869 9703 7718 1357 -65 -572 N ATOM 1771 CZ ARG A 392 6.690 45.474 22.369 1.00 63.83 C ANISOU 1771 CZ ARG A 392 8164 9089 7000 1329 24 -409 C ATOM 1772 NH1 ARG A 392 7.092 44.312 22.869 1.00 69.42 N ANISOU 1772 NH1 ARG A 392 8874 9854 7650 1328 29 -321 N ATOM 1773 NH2 ARG A 392 5.497 45.573 21.796 1.00 42.38 N ANISOU 1773 NH2 ARG A 392 5415 6374 4313 1302 100 -333 N ATOM 1774 N ALA A 393 10.980 43.014 19.225 1.00 23.50 N ANISOU 1774 N ALA A 393 3028 3580 2322 926 -131 -380 N ATOM 1775 CA ALA A 393 11.061 41.664 18.686 1.00 23.57 C ANISOU 1775 CA ALA A 393 3019 3569 2367 859 -107 -272 C ATOM 1776 C ALA A 393 12.519 41.223 18.540 1.00 23.53 C ANISOU 1776 C ALA A 393 3011 3510 2420 828 -173 -322 C ATOM 1777 O ALA A 393 12.872 40.091 18.881 1.00 22.68 O ANISOU 1777 O ALA A 393 2902 3423 2292 830 -186 -261 O ATOM 1778 CB ALA A 393 10.324 41.571 17.347 1.00 20.37 C ANISOU 1778 CB ALA A 393 2592 3099 2049 774 -54 -212 C ATOM 1779 N LEU A 394 13.370 42.113 18.040 1.00 19.27 N ANISOU 1779 N LEU A 394 2464 2898 1962 800 -215 -425 N ATOM 1780 CA LEU A 394 14.776 41.759 17.893 1.00 24.92 C ANISOU 1780 CA LEU A 394 3163 3564 2740 772 -274 -472 C ATOM 1781 C LEU A 394 15.363 41.434 19.256 1.00 28.08 C ANISOU 1781 C LEU A 394 3586 4029 3054 854 -336 -503 C ATOM 1782 O LEU A 394 16.078 40.445 19.416 1.00 22.18 O ANISOU 1782 O LEU A 394 2833 3282 2314 846 -364 -475 O ATOM 1783 CB LEU A 394 15.573 42.888 17.233 1.00 22.44 C ANISOU 1783 CB LEU A 394 2825 3167 2533 733 -309 -569 C ATOM 1784 CG LEU A 394 17.078 42.641 17.112 1.00 19.95 C ANISOU 1784 CG LEU A 394 2480 2805 2293 707 -370 -620 C ATOM 1785 CD1 LEU A 394 17.416 41.481 16.145 1.00 18.24 C ANISOU 1785 CD1 LEU A 394 2239 2564 2128 644 -335 -551 C ATOM 1786 CD2 LEU A 394 17.786 43.931 16.672 1.00 22.36 C ANISOU 1786 CD2 LEU A 394 2752 3035 2707 677 -410 -707 C ATOM 1787 N GLN A 395 15.036 42.257 20.247 1.00 20.78 N ANISOU 1787 N GLN A 395 2688 3163 2043 940 -360 -564 N ATOM 1788 CA GLN A 395 15.586 42.073 21.583 1.00 24.39 C ANISOU 1788 CA GLN A 395 3172 3692 2401 1032 -427 -607 C ATOM 1789 C GLN A 395 15.148 40.737 22.165 1.00 28.07 C ANISOU 1789 C GLN A 395 3650 4243 2772 1059 -391 -477 C ATOM 1790 O GLN A 395 15.953 40.026 22.772 1.00 31.43 O ANISOU 1790 O GLN A 395 4082 4689 3169 1085 -445 -472 O ATOM 1791 CB GLN A 395 15.184 43.243 22.499 1.00 22.22 C ANISOU 1791 CB GLN A 395 2928 3473 2040 1134 -460 -705 C ATOM 1792 CG GLN A 395 15.801 43.169 23.892 1.00 46.93 C ANISOU 1792 CG GLN A 395 6092 6683 5057 1245 -542 -769 C ATOM 1793 CD GLN A 395 15.424 44.360 24.745 1.00 66.50 C ANISOU 1793 CD GLN A 395 8603 9215 7450 1358 -585 -887 C ATOM 1794 OE1 GLN A 395 14.512 45.119 24.402 1.00 70.42 O ANISOU 1794 OE1 GLN A 395 9098 9706 7954 1361 -538 -899 O ATOM 1795 NE2 GLN A 395 16.122 44.535 25.864 1.00 74.57 N ANISOU 1795 NE2 GLN A 395 9656 10288 8390 1458 -683 -982 N ATOM 1796 N ARG A 396 13.887 40.373 21.954 1.00 26.16 N ANISOU 1796 N ARG A 396 3404 4043 2492 1047 -303 -365 N ATOM 1797 CA ARG A 396 13.380 39.104 22.464 1.00 28.33 C ANISOU 1797 CA ARG A 396 3677 4390 2695 1063 -267 -220 C ATOM 1798 C ARG A 396 14.062 37.901 21.814 1.00 30.02 C ANISOU 1798 C ARG A 396 3868 4529 3008 985 -289 -160 C ATOM 1799 O ARG A 396 14.396 36.933 22.488 1.00 27.94 O ANISOU 1799 O ARG A 396 3609 4304 2702 1012 -317 -93 O ATOM 1800 CB ARG A 396 11.863 39.018 22.314 1.00 30.71 C ANISOU 1800 CB ARG A 396 3964 4743 2960 1061 -172 -108 C ATOM 1801 CG ARG A 396 11.118 40.093 23.118 1.00 36.28 C ANISOU 1801 CG ARG A 396 4690 5547 3548 1161 -146 -159 C ATOM 1802 CD ARG A 396 9.637 39.779 23.293 1.00 37.48 C ANISOU 1802 CD ARG A 396 4819 5784 3636 1180 -49 -21 C ATOM 1803 NE ARG A 396 8.969 39.512 22.028 1.00 40.34 N ANISOU 1803 NE ARG A 396 5147 6058 4123 1074 0 48 N ATOM 1804 CZ ARG A 396 8.465 40.456 21.239 1.00 40.84 C ANISOU 1804 CZ ARG A 396 5204 6068 4246 1044 24 -11 C ATOM 1805 NH1 ARG A 396 8.559 41.736 21.585 1.00 36.55 N ANISOU 1805 NH1 ARG A 396 4684 5542 3663 1109 1 -142 N ATOM 1806 NH2 ARG A 396 7.876 40.119 20.106 1.00 30.15 N ANISOU 1806 NH2 ARG A 396 3821 4639 2996 953 62 57 N ATOM 1807 N LEU A 397 14.268 37.961 20.503 1.00 22.27 N ANISOU 1807 N LEU A 397 2863 3443 2155 894 -278 -184 N ATOM 1808 CA LEU A 397 14.959 36.883 19.790 1.00 22.05 C ANISOU 1808 CA LEU A 397 2813 3341 2223 829 -302 -150 C ATOM 1809 C LEU A 397 16.433 36.792 20.188 1.00 23.85 C ANISOU 1809 C LEU A 397 3041 3548 2472 850 -386 -236 C ATOM 1810 O LEU A 397 16.945 35.696 20.417 1.00 24.66 O ANISOU 1810 O LEU A 397 3137 3643 2587 850 -423 -186 O ATOM 1811 CB LEU A 397 14.819 37.051 18.268 1.00 21.26 C ANISOU 1811 CB LEU A 397 2689 3151 2238 742 -268 -165 C ATOM 1812 CG LEU A 397 15.465 35.974 17.378 1.00 22.38 C ANISOU 1812 CG LEU A 397 2807 3219 2477 685 -290 -145 C ATOM 1813 CD1 LEU A 397 14.890 34.599 17.719 1.00 22.39 C ANISOU 1813 CD1 LEU A 397 2806 3236 2466 687 -291 -17 C ATOM 1814 CD2 LEU A 397 15.246 36.291 15.887 1.00 20.60 C ANISOU 1814 CD2 LEU A 397 2563 2926 2337 616 -251 -167 C ATOM 1815 N MET A 398 17.114 37.933 20.268 1.00 22.63 N ANISOU 1815 N MET A 398 2889 3377 2334 867 -424 -361 N ATOM 1816 CA MET A 398 18.538 37.940 20.619 1.00 24.04 C ANISOU 1816 CA MET A 398 3057 3528 2548 884 -511 -448 C ATOM 1817 C MET A 398 18.786 37.413 22.036 1.00 27.41 C ANISOU 1817 C MET A 398 3515 4037 2863 971 -567 -428 C ATOM 1818 O MET A 398 19.832 36.826 22.316 1.00 23.67 O ANISOU 1818 O MET A 398 3031 3544 2418 979 -635 -449 O ATOM 1819 CB MET A 398 19.137 39.339 20.476 1.00 22.52 C ANISOU 1819 CB MET A 398 2854 3294 2409 884 -549 -580 C ATOM 1820 CG MET A 398 19.263 39.842 19.032 1.00 22.19 C ANISOU 1820 CG MET A 398 2772 3165 2495 794 -507 -600 C ATOM 1821 SD MET A 398 20.407 38.843 18.039 1.00 27.84 S ANISOU 1821 SD MET A 398 3437 3815 3327 727 -516 -586 S ATOM 1822 CE MET A 398 19.268 37.960 16.983 1.00 20.77 C ANISOU 1822 CE MET A 398 2546 2913 2434 674 -426 -473 C ATOM 1823 N THR A 399 17.832 37.635 22.933 1.00 25.39 N ANISOU 1823 N THR A 399 3294 3879 2475 1042 -538 -386 N ATOM 1824 CA THR A 399 17.965 37.118 24.295 1.00 28.88 C ANISOU 1824 CA THR A 399 3766 4419 2787 1134 -582 -350 C ATOM 1825 C THR A 399 18.013 35.594 24.271 1.00 27.07 C ANISOU 1825 C THR A 399 3523 4184 2577 1104 -577 -214 C ATOM 1826 O THR A 399 18.811 34.964 24.971 1.00 29.12 O ANISOU 1826 O THR A 399 3790 4463 2810 1143 -647 -207 O ATOM 1827 CB THR A 399 16.803 37.580 25.190 1.00 30.28 C ANISOU 1827 CB THR A 399 3977 4721 2808 1222 -532 -311 C ATOM 1828 OG1 THR A 399 16.825 39.009 25.297 1.00 31.49 O ANISOU 1828 OG1 THR A 399 4145 4872 2947 1263 -556 -454 O ATOM 1829 CG2 THR A 399 16.917 36.971 26.579 1.00 35.76 C ANISOU 1829 CG2 THR A 399 4701 5534 3351 1323 -568 -253 C ATOM 1830 N SER A 400 17.164 34.999 23.445 1.00 24.18 N ANISOU 1830 N SER A 400 3135 3784 2269 1035 -505 -108 N ATOM 1831 CA SER A 400 17.099 33.554 23.355 1.00 28.45 C ANISOU 1831 CA SER A 400 3657 4302 2849 1003 -508 24 C ATOM 1832 C SER A 400 18.353 33.001 22.678 1.00 28.67 C ANISOU 1832 C SER A 400 3662 4227 3005 954 -574 -38 C ATOM 1833 O SER A 400 18.938 32.017 23.139 1.00 28.22 O ANISOU 1833 O SER A 400 3602 4165 2955 971 -632 11 O ATOM 1834 CB SER A 400 15.836 33.140 22.609 1.00 36.52 C ANISOU 1834 CB SER A 400 4658 5304 3914 944 -427 139 C ATOM 1835 OG SER A 400 15.675 31.741 22.657 1.00 45.05 O ANISOU 1835 OG SER A 400 5719 6361 5037 919 -441 276 O ATOM 1836 N VAL A 401 18.775 33.650 21.597 1.00 20.46 N ANISOU 1836 N VAL A 401 2601 3110 2063 899 -565 -141 N ATOM 1837 CA VAL A 401 20.000 33.255 20.897 1.00 24.12 C ANISOU 1837 CA VAL A 401 3033 3488 2644 860 -617 -209 C ATOM 1838 C VAL A 401 21.200 33.359 21.820 1.00 24.24 C ANISOU 1838 C VAL A 401 3052 3522 2634 917 -707 -283 C ATOM 1839 O VAL A 401 22.036 32.462 21.862 1.00 25.78 O ANISOU 1839 O VAL A 401 3230 3683 2883 917 -765 -276 O ATOM 1840 CB VAL A 401 20.241 34.113 19.632 1.00 21.39 C ANISOU 1840 CB VAL A 401 2660 3077 2392 799 -581 -301 C ATOM 1841 CG1 VAL A 401 21.665 33.899 19.086 1.00 25.05 C ANISOU 1841 CG1 VAL A 401 3082 3476 2961 777 -633 -383 C ATOM 1842 CG2 VAL A 401 19.205 33.779 18.581 1.00 20.60 C ANISOU 1842 CG2 VAL A 401 2553 2945 2330 742 -508 -230 C ATOM 1843 N THR A 402 21.267 34.447 22.583 1.00 25.82 N ANISOU 1843 N THR A 402 3277 3777 2756 971 -728 -359 N ATOM 1844 CA THR A 402 22.400 34.662 23.483 1.00 30.83 C ANISOU 1844 CA THR A 402 3918 4429 3369 1031 -828 -445 C ATOM 1845 C THR A 402 22.426 33.641 24.622 1.00 27.70 C ANISOU 1845 C THR A 402 3549 4100 2874 1097 -875 -354 C ATOM 1846 O THR A 402 23.493 33.167 25.026 1.00 29.60 O ANISOU 1846 O THR A 402 3781 4323 3143 1121 -961 -386 O ATOM 1847 CB THR A 402 22.410 36.090 24.043 1.00 35.38 C ANISOU 1847 CB THR A 402 4516 5041 3887 1083 -855 -558 C ATOM 1848 OG1 THR A 402 22.682 37.008 22.974 1.00 33.59 O ANISOU 1848 OG1 THR A 402 4250 4732 3780 1015 -833 -641 O ATOM 1849 CG2 THR A 402 23.486 36.223 25.089 1.00 48.82 C ANISOU 1849 CG2 THR A 402 6228 6766 5554 1156 -972 -642 C ATOM 1850 N ASN A 403 21.249 33.295 25.127 1.00 26.45 N ANISOU 1850 N ASN A 403 3421 4022 2607 1126 -816 -232 N ATOM 1851 CA ASN A 403 21.123 32.265 26.159 1.00 35.16 C ANISOU 1851 CA ASN A 403 4545 5197 3618 1183 -846 -110 C ATOM 1852 C ASN A 403 21.600 30.884 25.713 1.00 34.43 C ANISOU 1852 C ASN A 403 4421 5025 3636 1132 -879 -30 C ATOM 1853 O ASN A 403 22.016 30.070 26.535 1.00 34.74 O ANISOU 1853 O ASN A 403 4470 5094 3636 1178 -942 35 O ATOM 1854 CB ASN A 403 19.676 32.171 26.640 1.00 34.01 C ANISOU 1854 CB ASN A 403 4420 5152 3351 1213 -759 26 C ATOM 1855 CG ASN A 403 19.267 33.357 27.493 1.00 45.47 C ANISOU 1855 CG ASN A 403 5910 6715 4650 1304 -746 -45 C ATOM 1856 OD1 ASN A 403 20.088 34.209 27.842 1.00 48.00 O ANISOU 1856 OD1 ASN A 403 6248 7035 4953 1351 -818 -195 O ATOM 1857 ND2 ASN A 403 17.988 33.419 27.829 1.00 43.31 N ANISOU 1857 ND2 ASN A 403 5646 6536 4274 1334 -658 60 N ATOM 1858 N ARG A 404 21.523 30.610 24.417 1.00 28.18 N ANISOU 1858 N ARG A 404 3593 4133 2982 1045 -841 -35 N ATOM 1859 CA ARG A 404 22.001 29.334 23.883 1.00 36.69 C ANISOU 1859 CA ARG A 404 4639 5123 4177 1004 -881 16 C ATOM 1860 C ARG A 404 23.221 29.475 22.967 1.00 28.70 C ANISOU 1860 C ARG A 404 3588 4019 3296 967 -921 -119 C ATOM 1861 O ARG A 404 23.501 28.580 22.179 1.00 30.46 O ANISOU 1861 O ARG A 404 3780 4162 3631 926 -936 -102 O ATOM 1862 CB ARG A 404 20.881 28.616 23.122 1.00 40.52 C ANISOU 1862 CB ARG A 404 5110 5569 4719 943 -817 135 C ATOM 1863 CG ARG A 404 19.884 27.890 24.016 1.00 61.18 C ANISOU 1863 CG ARG A 404 7740 8253 7254 971 -798 316 C ATOM 1864 CD ARG A 404 19.387 26.609 23.354 1.00 71.71 C ANISOU 1864 CD ARG A 404 9041 9497 8708 911 -803 435 C ATOM 1865 NE ARG A 404 18.559 25.806 24.253 1.00 78.40 N ANISOU 1865 NE ARG A 404 9888 10399 9500 932 -797 630 N ATOM 1866 CZ ARG A 404 18.309 24.511 24.086 1.00 78.10 C ANISOU 1866 CZ ARG A 404 9820 10286 9567 897 -837 760 C ATOM 1867 NH1 ARG A 404 18.828 23.859 23.057 1.00 75.82 N ANISOU 1867 NH1 ARG A 404 9507 9865 9435 849 -891 698 N ATOM 1868 NH2 ARG A 404 17.541 23.865 24.953 1.00 83.01 N ANISOU 1868 NH2 ARG A 404 10434 10966 10140 914 -826 953 N ATOM 1869 N CYS A 405 23.930 30.596 23.081 1.00 24.48 N ANISOU 1869 N CYS A 405 2460 3960 2882 366 -214 -9 N ATOM 1870 CA CYS A 405 25.073 30.932 22.233 1.00 22.09 C ANISOU 1870 CA CYS A 405 2223 3574 2597 393 -246 -83 C ATOM 1871 C CYS A 405 26.102 29.795 22.062 1.00 25.34 C ANISOU 1871 C CYS A 405 2664 3941 3023 403 -293 -2 C ATOM 1872 O CYS A 405 26.521 29.483 20.951 1.00 23.77 O ANISOU 1872 O CYS A 405 2516 3617 2899 417 -339 -21 O ATOM 1873 CB CYS A 405 25.774 32.197 22.801 1.00 30.15 C ANISOU 1873 CB CYS A 405 3227 4701 3527 410 -213 -200 C ATOM 1874 SG CYS A 405 27.380 32.545 22.058 1.00120.36 S ANISOU 1874 SG CYS A 405 14718 16062 14951 436 -241 -278 S ATOM 1875 N GLN A 406 26.517 29.197 23.175 1.00 26.08 N ANISOU 1875 N GLN A 406 2721 4146 3043 400 -286 85 N ATOM 1876 CA GLN A 406 27.502 28.115 23.177 1.00 29.08 C ANISOU 1876 CA GLN A 406 3122 4493 3433 413 -337 163 C ATOM 1877 C GLN A 406 27.066 26.977 22.254 1.00 29.01 C ANISOU 1877 C GLN A 406 3132 4327 3564 404 -396 240 C ATOM 1878 O GLN A 406 27.809 26.553 21.371 1.00 26.17 O ANISOU 1878 O GLN A 406 2812 3867 3264 424 -453 212 O ATOM 1879 CB GLN A 406 27.648 27.571 24.603 1.00 37.77 C ANISOU 1879 CB GLN A 406 4168 5743 4440 407 -319 275 C ATOM 1880 CG GLN A 406 28.966 26.864 24.903 1.00 52.98 C ANISOU 1880 CG GLN A 406 6114 7686 6330 433 -364 316 C ATOM 1881 CD GLN A 406 29.204 25.641 24.041 1.00 67.48 C ANISOU 1881 CD GLN A 406 7986 9361 8293 433 -444 386 C ATOM 1882 OE1 GLN A 406 28.276 24.896 23.726 1.00 74.64 O ANISOU 1882 OE1 GLN A 406 8876 10180 9304 408 -463 476 O ATOM 1883 NE2 GLN A 406 30.458 25.422 23.661 1.00 70.05 N ANISOU 1883 NE2 GLN A 406 8350 9649 8616 462 -495 333 N ATOM 1884 N GLU A 407 25.852 26.484 22.474 1.00 25.90 N ANISOU 1884 N GLU A 407 2697 3919 3223 376 -382 329 N ATOM 1885 CA GLU A 407 25.303 25.394 21.675 1.00 27.75 C ANISOU 1885 CA GLU A 407 2931 4005 3606 369 -435 398 C ATOM 1886 C GLU A 407 25.180 25.763 20.189 1.00 26.62 C ANISOU 1886 C GLU A 407 2832 3730 3552 393 -464 283 C ATOM 1887 O GLU A 407 25.463 24.961 19.309 1.00 25.67 O ANISOU 1887 O GLU A 407 2724 3494 3535 411 -531 288 O ATOM 1888 CB GLU A 407 23.933 24.995 22.227 1.00 33.33 C ANISOU 1888 CB GLU A 407 3581 4733 4349 329 -399 499 C ATOM 1889 CG GLU A 407 23.232 23.898 21.438 1.00 51.06 C ANISOU 1889 CG GLU A 407 5812 6822 6766 322 -450 562 C ATOM 1890 CD GLU A 407 21.939 23.436 22.096 1.00 60.82 C ANISOU 1890 CD GLU A 407 6984 8085 8038 275 -410 673 C ATOM 1891 OE1 GLU A 407 21.557 24.006 23.143 1.00 56.40 O ANISOU 1891 OE1 GLU A 407 6390 7680 7358 249 -344 696 O ATOM 1892 OE2 GLU A 407 21.305 22.501 21.561 1.00 66.98 O ANISOU 1892 OE2 GLU A 407 7740 8739 8969 266 -448 731 O ATOM 1893 N LEU A 408 24.764 26.986 19.906 1.00 21.56 N ANISOU 1893 N LEU A 408 2207 3112 2870 396 -419 175 N ATOM 1894 CA LEU A 408 24.536 27.382 18.518 1.00 20.24 C ANISOU 1894 CA LEU A 408 2079 2832 2778 419 -443 79 C ATOM 1895 C LEU A 408 25.849 27.591 17.772 1.00 20.76 C ANISOU 1895 C LEU A 408 2193 2869 2826 448 -481 7 C ATOM 1896 O LEU A 408 25.978 27.221 16.611 1.00 19.28 O ANISOU 1896 O LEU A 408 2023 2583 2717 471 -532 -27 O ATOM 1897 CB LEU A 408 23.701 28.652 18.467 1.00 19.84 C ANISOU 1897 CB LEU A 408 2032 2811 2695 414 -390 -7 C ATOM 1898 CG LEU A 408 22.304 28.516 19.079 1.00 21.99 C ANISOU 1898 CG LEU A 408 2252 3114 2987 386 -353 41 C ATOM 1899 CD1 LEU A 408 21.601 29.867 19.162 1.00 25.60 C ANISOU 1899 CD1 LEU A 408 2707 3618 3401 384 -308 -63 C ATOM 1900 CD2 LEU A 408 21.472 27.541 18.267 1.00 24.11 C ANISOU 1900 CD2 LEU A 408 2509 3257 3394 391 -391 82 C ATOM 1901 N ALA A 409 26.815 28.205 18.442 1.00 18.90 N ANISOU 1901 N ALA A 409 1970 2729 2483 447 -456 -26 N ATOM 1902 CA ALA A 409 28.109 28.490 17.831 1.00 19.27 C ANISOU 1902 CA ALA A 409 2057 2763 2500 467 -483 -102 C ATOM 1903 C ALA A 409 28.830 27.231 17.386 1.00 19.71 C ANISOU 1903 C ALA A 409 2115 2759 2616 484 -559 -61 C ATOM 1904 O ALA A 409 29.583 27.259 16.418 1.00 18.37 O ANISOU 1904 O ALA A 409 1972 2545 2462 504 -598 -131 O ATOM 1905 CB ALA A 409 29.004 29.274 18.806 1.00 19.48 C ANISOU 1905 CB ALA A 409 2084 2910 2407 465 -440 -143 C ATOM 1906 N THR A 410 28.630 26.135 18.109 1.00 19.34 N ANISOU 1906 N THR A 410 2032 2716 2601 475 -584 50 N ATOM 1907 CA THR A 410 29.374 24.916 17.819 1.00 19.83 C ANISOU 1907 CA THR A 410 2087 2720 2728 492 -668 87 C ATOM 1908 C THR A 410 28.631 23.994 16.859 1.00 19.36 C ANISOU 1908 C THR A 410 2001 2533 2822 503 -728 111 C ATOM 1909 O THR A 410 29.170 22.978 16.428 1.00 22.45 O ANISOU 1909 O THR A 410 2376 2861 3295 523 -811 121 O ATOM 1910 CB THR A 410 29.732 24.125 19.098 1.00 20.19 C ANISOU 1910 CB THR A 410 2105 2828 2737 481 -678 204 C ATOM 1911 OG1 THR A 410 28.550 23.889 19.865 1.00 25.31 O ANISOU 1911 OG1 THR A 410 2714 3500 3403 451 -637 314 O ATOM 1912 CG2 THR A 410 30.734 24.892 19.945 1.00 21.05 C ANISOU 1912 CG2 THR A 410 2234 3066 2699 487 -637 158 C ATOM 1913 N ASN A 411 27.396 24.354 16.534 1.00 19.26 N ANISOU 1913 N ASN A 411 1978 2485 2854 495 -691 107 N ATOM 1914 CA ASN A 411 26.552 23.518 15.686 1.00 20.04 C ANISOU 1914 CA ASN A 411 2042 2469 3105 509 -741 122 C ATOM 1915 C ASN A 411 26.831 23.663 14.192 1.00 19.92 C ANISOU 1915 C ASN A 411 2040 2391 3138 552 -788 6 C ATOM 1916 O ASN A 411 27.123 24.752 13.720 1.00 19.85 O ANISOU 1916 O ASN A 411 2074 2420 3047 559 -753 -81 O ATOM 1917 CB ASN A 411 25.080 23.826 15.959 1.00 19.59 C ANISOU 1917 CB ASN A 411 1964 2406 3074 486 -681 156 C ATOM 1918 CG ASN A 411 24.154 22.959 15.141 1.00 24.47 C ANISOU 1918 CG ASN A 411 2538 2905 3856 504 -729 165 C ATOM 1919 OD1 ASN A 411 23.948 21.771 15.437 1.00 28.30 O ANISOU 1919 OD1 ASN A 411 2972 3332 4448 494 -773 258 O ATOM 1920 ND2 ASN A 411 23.597 23.537 14.106 1.00 19.18 N ANISOU 1920 ND2 ASN A 411 1880 2193 3212 532 -722 67 N ATOM 1921 N GLU A 412 26.682 22.563 13.451 1.00 19.25 N ANISOU 1921 N GLU A 412 1910 2213 3193 580 -869 6 N ATOM 1922 CA GLU A 412 26.991 22.511 12.024 1.00 22.55 C ANISOU 1922 CA GLU A 412 2320 2588 3660 628 -928 -105 C ATOM 1923 C GLU A 412 26.224 23.527 11.180 1.00 18.20 C ANISOU 1923 C GLU A 412 1794 2037 3084 645 -880 -181 C ATOM 1924 O GLU A 412 26.719 23.965 10.139 1.00 19.37 O ANISOU 1924 O GLU A 412 1958 2199 3201 677 -900 -273 O ATOM 1925 CB GLU A 412 26.716 21.108 11.470 1.00 25.43 C ANISOU 1925 CB GLU A 412 2609 2851 4201 660 -1025 -95 C ATOM 1926 CG GLU A 412 25.248 20.743 11.471 1.00 24.47 C ANISOU 1926 CG GLU A 412 2444 2655 4198 657 -1007 -49 C ATOM 1927 CD GLU A 412 25.013 19.273 11.153 1.00 34.84 C ANISOU 1927 CD GLU A 412 3671 3860 5708 682 -1105 -24 C ATOM 1928 OE1 GLU A 412 25.700 18.749 10.252 1.00 31.16 O ANISOU 1928 OE1 GLU A 412 3169 3369 5303 730 -1194 -110 O ATOM 1929 OE2 GLU A 412 24.143 18.653 11.807 1.00 31.33 O ANISOU 1929 OE2 GLU A 412 3187 3359 5359 652 -1093 78 O ATOM 1930 N TYR A 413 25.037 23.926 11.642 1.00 18.09 N ANISOU 1930 N TYR A 413 1782 2014 3076 623 -818 -141 N ATOM 1931 CA TYR A 413 24.230 24.902 10.920 1.00 18.24 C ANISOU 1931 CA TYR A 413 1826 2028 3077 640 -777 -210 C ATOM 1932 C TYR A 413 24.080 26.227 11.649 1.00 21.88 C ANISOU 1932 C TYR A 413 2338 2561 3415 604 -691 -210 C ATOM 1933 O TYR A 413 24.152 27.279 11.037 1.00 19.62 O ANISOU 1933 O TYR A 413 2093 2291 3071 617 -667 -280 O ATOM 1934 CB TYR A 413 22.826 24.355 10.609 1.00 19.24 C ANISOU 1934 CB TYR A 413 1904 2076 3331 657 -785 -201 C ATOM 1935 CG TYR A 413 22.869 23.153 9.721 1.00 19.93 C ANISOU 1935 CG TYR A 413 1927 2086 3560 705 -875 -228 C ATOM 1936 CD1 TYR A 413 23.418 23.234 8.445 1.00 21.84 C ANISOU 1936 CD1 TYR A 413 2165 2331 3803 760 -927 -328 C ATOM 1937 CD2 TYR A 413 22.361 21.933 10.144 1.00 23.76 C ANISOU 1937 CD2 TYR A 413 2345 2500 4183 696 -912 -157 C ATOM 1938 CE1 TYR A 413 23.471 22.123 7.622 1.00 23.62 C ANISOU 1938 CE1 TYR A 413 2315 2498 4163 812 -1018 -372 C ATOM 1939 CE2 TYR A 413 22.417 20.811 9.329 1.00 29.36 C ANISOU 1939 CE2 TYR A 413 2981 3131 5043 744 -1005 -195 C ATOM 1940 CZ TYR A 413 22.967 20.919 8.068 1.00 27.64 C ANISOU 1940 CZ TYR A 413 2754 2925 4822 805 -1059 -311 C ATOM 1941 OH TYR A 413 23.022 19.819 7.256 1.00 30.67 O ANISOU 1941 OH TYR A 413 3066 3243 5343 838 -1149 -374 O ATOM 1942 N ALA A 414 23.856 26.189 12.954 1.00 18.06 N ANISOU 1942 N ALA A 414 1845 2124 2894 561 -647 -134 N ATOM 1943 CA ALA A 414 23.549 27.434 13.654 1.00 17.69 C ANISOU 1943 CA ALA A 414 1826 2148 2745 532 -572 -152 C ATOM 1944 C ALA A 414 24.791 28.329 13.744 1.00 20.24 C ANISOU 1944 C ALA A 414 2194 2537 2958 528 -555 -201 C ATOM 1945 O ALA A 414 24.677 29.517 14.009 1.00 18.73 O ANISOU 1945 O ALA A 414 2027 2391 2698 516 -505 -246 O ATOM 1946 CB ALA A 414 22.963 27.156 15.020 1.00 18.35 C ANISOU 1946 CB ALA A 414 1873 2288 2809 491 -530 -65 C ATOM 1947 N ASN A 415 25.977 27.771 13.503 1.00 18.88 N ANISOU 1947 N ASN A 415 2028 2368 2777 540 -601 -202 N ATOM 1948 CA ASN A 415 27.168 28.622 13.521 1.00 17.52 C ANISOU 1948 CA ASN A 415 1895 2255 2506 535 -583 -258 C ATOM 1949 C ASN A 415 27.055 29.764 12.498 1.00 17.40 C ANISOU 1949 C ASN A 415 1918 2219 2476 548 -565 -338 C ATOM 1950 O ASN A 415 27.635 30.819 12.681 1.00 16.27 O ANISOU 1950 O ASN A 415 1803 2119 2258 534 -527 -381 O ATOM 1951 CB ASN A 415 28.453 27.811 13.305 1.00 17.85 C ANISOU 1951 CB ASN A 415 1934 2303 2545 548 -642 -261 C ATOM 1952 CG ASN A 415 28.674 27.450 11.859 1.00 21.14 C ANISOU 1952 CG ASN A 415 2348 2662 3021 584 -702 -317 C ATOM 1953 OD1 ASN A 415 29.180 28.259 11.090 1.00 18.75 O ANISOU 1953 OD1 ASN A 415 2077 2378 2671 591 -692 -385 O ATOM 1954 ND2 ASN A 415 28.300 26.221 11.477 1.00 18.83 N ANISOU 1954 ND2 ASN A 415 2010 2307 2837 608 -768 -290 N ATOM 1955 N TYR A 416 26.277 29.568 11.436 1.00 16.99 N ANISOU 1955 N TYR A 416 1860 2098 2497 578 -592 -357 N ATOM 1956 CA TYR A 416 26.104 30.625 10.447 1.00 16.30 C ANISOU 1956 CA TYR A 416 1808 1992 2394 593 -579 -418 C ATOM 1957 C TYR A 416 25.300 31.788 11.007 1.00 19.06 C ANISOU 1957 C TYR A 416 2174 2351 2718 573 -520 -431 C ATOM 1958 O TYR A 416 25.509 32.943 10.629 1.00 16.81 O ANISOU 1958 O TYR A 416 1924 2068 2396 569 -497 -474 O ATOM 1959 CB TYR A 416 25.423 30.087 9.194 1.00 16.56 C ANISOU 1959 CB TYR A 416 1822 1961 2508 640 -626 -439 C ATOM 1960 CG TYR A 416 26.338 29.206 8.393 1.00 16.12 C ANISOU 1960 CG TYR A 416 1744 1909 2472 669 -691 -459 C ATOM 1961 CD1 TYR A 416 27.301 29.765 7.574 1.00 17.60 C ANISOU 1961 CD1 TYR A 416 1957 2135 2597 676 -699 -505 C ATOM 1962 CD2 TYR A 416 26.264 27.828 8.486 1.00 19.58 C ANISOU 1962 CD2 TYR A 416 2129 2315 2995 686 -748 -433 C ATOM 1963 CE1 TYR A 416 28.157 28.981 6.843 1.00 20.42 C ANISOU 1963 CE1 TYR A 416 2283 2512 2963 702 -761 -538 C ATOM 1964 CE2 TYR A 416 27.120 27.025 7.759 1.00 23.95 C ANISOU 1964 CE2 TYR A 416 2651 2876 3574 715 -818 -469 C ATOM 1965 CZ TYR A 416 28.069 27.615 6.939 1.00 24.48 C ANISOU 1965 CZ TYR A 416 2740 2996 3565 724 -824 -527 C ATOM 1966 OH TYR A 416 28.934 26.832 6.220 1.00 23.33 O ANISOU 1966 OH TYR A 416 2554 2875 3437 754 -898 -575 O ATOM 1967 N ILE A 417 24.380 31.480 11.909 1.00 16.31 N ANISOU 1967 N ILE A 417 1795 2009 2393 557 -499 -395 N ATOM 1968 CA ILE A 417 23.565 32.530 12.505 1.00 16.43 C ANISOU 1968 CA ILE A 417 1812 2045 2386 540 -451 -421 C ATOM 1969 C ILE A 417 24.443 33.371 13.419 1.00 19.33 C ANISOU 1969 C ILE A 417 2186 2492 2668 511 -413 -442 C ATOM 1970 O ILE A 417 24.404 34.601 13.393 1.00 16.49 O ANISOU 1970 O ILE A 417 1843 2135 2287 505 -389 -498 O ATOM 1971 CB ILE A 417 22.395 31.937 13.297 1.00 17.42 C ANISOU 1971 CB ILE A 417 1892 2179 2549 526 -436 -380 C ATOM 1972 CG1 ILE A 417 21.437 31.219 12.355 1.00 22.21 C ANISOU 1972 CG1 ILE A 417 2486 2699 3254 559 -471 -379 C ATOM 1973 CG2 ILE A 417 21.665 33.028 14.096 1.00 19.00 C ANISOU 1973 CG2 ILE A 417 2079 2428 2710 505 -389 -421 C ATOM 1974 CD1 ILE A 417 20.395 30.416 13.086 1.00 33.23 C ANISOU 1974 CD1 ILE A 417 3829 4096 4701 540 -459 -326 C ATOM 1975 N ILE A 418 25.229 32.692 14.247 1.00 18.59 N ANISOU 1975 N ILE A 418 2072 2459 2533 496 -412 -399 N ATOM 1976 CA ILE A 418 26.078 33.390 15.192 1.00 16.85 C ANISOU 1976 CA ILE A 418 1846 2325 2231 477 -377 -426 C ATOM 1977 C ILE A 418 27.080 34.250 14.424 1.00 17.31 C ANISOU 1977 C ILE A 418 1946 2362 2269 481 -380 -488 C ATOM 1978 O ILE A 418 27.324 35.400 14.793 1.00 18.46 O ANISOU 1978 O ILE A 418 2092 2538 2385 469 -347 -544 O ATOM 1979 CB ILE A 418 26.817 32.410 16.106 1.00 18.45 C ANISOU 1979 CB ILE A 418 2024 2596 2391 469 -384 -365 C ATOM 1980 CG1 ILE A 418 25.807 31.574 16.902 1.00 18.01 C ANISOU 1980 CG1 ILE A 418 1921 2565 2356 458 -378 -284 C ATOM 1981 CG2 ILE A 418 27.782 33.173 17.048 1.00 17.32 C ANISOU 1981 CG2 ILE A 418 1871 2552 2158 460 -349 -411 C ATOM 1982 CD1 ILE A 418 24.778 32.433 17.671 1.00 23.39 C ANISOU 1982 CD1 ILE A 418 2569 3308 3013 442 -329 -313 C ATOM 1983 N GLN A 419 27.633 33.709 13.340 1.00 16.95 N ANISOU 1983 N GLN A 419 1927 2267 2246 497 -420 -481 N ATOM 1984 CA GLN A 419 28.518 34.494 12.485 1.00 16.14 C ANISOU 1984 CA GLN A 419 1861 2149 2124 497 -420 -529 C ATOM 1985 C GLN A 419 27.826 35.699 11.892 1.00 15.90 C ANISOU 1985 C GLN A 419 1852 2068 2121 497 -402 -563 C ATOM 1986 O GLN A 419 28.412 36.772 11.820 1.00 21.76 O ANISOU 1986 O GLN A 419 2610 2814 2843 481 -379 -602 O ATOM 1987 CB GLN A 419 29.096 33.662 11.341 1.00 15.70 C ANISOU 1987 CB GLN A 419 1817 2065 2084 518 -472 -521 C ATOM 1988 CG GLN A 419 30.183 32.696 11.745 1.00 17.47 C ANISOU 1988 CG GLN A 419 2025 2334 2277 517 -500 -511 C ATOM 1989 CD GLN A 419 30.711 31.967 10.528 1.00 22.43 C ANISOU 1989 CD GLN A 419 2654 2941 2928 541 -558 -525 C ATOM 1990 OE1 GLN A 419 31.429 32.539 9.713 1.00 22.81 O ANISOU 1990 OE1 GLN A 419 2722 3002 2944 538 -557 -567 O ATOM 1991 NE2 GLN A 419 30.324 30.719 10.379 1.00 16.74 N ANISOU 1991 NE2 GLN A 419 1902 2192 2268 565 -611 -493 N ATOM 1992 N HIS A 420 26.584 35.530 11.454 1.00 15.89 N ANISOU 1992 N HIS A 420 1849 2015 2174 517 -416 -549 N ATOM 1993 CA HIS A 420 25.873 36.667 10.902 1.00 16.64 C ANISOU 1993 CA HIS A 420 1966 2058 2299 522 -407 -581 C ATOM 1994 C HIS A 420 25.757 37.783 11.938 1.00 19.69 C ANISOU 1994 C HIS A 420 2335 2474 2671 497 -369 -625 C ATOM 1995 O HIS A 420 25.963 38.950 11.635 1.00 18.66 O ANISOU 1995 O HIS A 420 2223 2315 2553 488 -360 -660 O ATOM 1996 CB HIS A 420 24.476 36.281 10.440 1.00 19.98 C ANISOU 1996 CB HIS A 420 2383 2428 2781 552 -427 -572 C ATOM 1997 CG HIS A 420 23.699 37.445 9.907 1.00 20.30 C ANISOU 1997 CG HIS A 420 2447 2412 2853 563 -425 -608 C ATOM 1998 ND1 HIS A 420 22.753 38.118 10.653 1.00 23.93 N ANISOU 1998 ND1 HIS A 420 2888 2871 3335 554 -408 -646 N ATOM 1999 CD2 HIS A 420 23.782 38.094 8.726 1.00 17.82 C ANISOU 1999 CD2 HIS A 420 2171 2049 2551 581 -442 -613 C ATOM 2000 CE1 HIS A 420 22.256 39.108 9.931 1.00 20.28 C ANISOU 2000 CE1 HIS A 420 2453 2345 2906 569 -420 -675 C ATOM 2001 NE2 HIS A 420 22.859 39.116 8.758 1.00 28.48 N ANISOU 2001 NE2 HIS A 420 3530 3354 3939 586 -439 -648 N ATOM 2002 N ILE A 421 25.415 37.416 13.163 1.00 16.50 N ANISOU 2002 N ILE A 421 1887 2134 2247 486 -350 -622 N ATOM 2003 CA ILE A 421 25.217 38.419 14.198 1.00 18.47 C ANISOU 2003 CA ILE A 421 2101 2434 2484 470 -319 -679 C ATOM 2004 C ILE A 421 26.538 39.101 14.518 1.00 19.27 C ANISOU 2004 C ILE A 421 2201 2573 2549 454 -300 -718 C ATOM 2005 O ILE A 421 26.618 40.328 14.554 1.00 21.70 O ANISOU 2005 O ILE A 421 2503 2860 2883 447 -291 -779 O ATOM 2006 CB ILE A 421 24.571 37.812 15.452 1.00 17.08 C ANISOU 2006 CB ILE A 421 1867 2344 2278 463 -301 -663 C ATOM 2007 CG1 ILE A 421 23.156 37.319 15.112 1.00 18.51 C ANISOU 2007 CG1 ILE A 421 2044 2479 2511 474 -316 -639 C ATOM 2008 CG2 ILE A 421 24.557 38.844 16.608 1.00 17.99 C ANISOU 2008 CG2 ILE A 421 1926 2543 2365 452 -272 -739 C ATOM 2009 CD1 ILE A 421 22.574 36.321 16.130 1.00 20.48 C ANISOU 2009 CD1 ILE A 421 2240 2805 2736 461 -301 -586 C ATOM 2010 N VAL A 422 27.584 38.307 14.717 1.00 19.39 N ANISOU 2010 N VAL A 422 2219 2634 2513 451 -300 -688 N ATOM 2011 CA VAL A 422 28.885 38.860 15.062 1.00 18.47 C ANISOU 2011 CA VAL A 422 2098 2561 2360 438 -280 -733 C ATOM 2012 C VAL A 422 29.420 39.779 13.957 1.00 18.98 C ANISOU 2012 C VAL A 422 2204 2548 2460 428 -284 -757 C ATOM 2013 O VAL A 422 30.031 40.805 14.234 1.00 20.16 O ANISOU 2013 O VAL A 422 2339 2704 2618 413 -263 -815 O ATOM 2014 CB VAL A 422 29.891 37.740 15.441 1.00 21.13 C ANISOU 2014 CB VAL A 422 2433 2962 2636 441 -287 -700 C ATOM 2015 CG1 VAL A 422 31.300 38.299 15.592 1.00 19.10 C ANISOU 2015 CG1 VAL A 422 2176 2738 2342 431 -269 -758 C ATOM 2016 CG2 VAL A 422 29.459 37.087 16.760 1.00 19.84 C ANISOU 2016 CG2 VAL A 422 2219 2891 2431 447 -275 -673 C ATOM 2017 N SER A 423 29.151 39.428 12.703 1.00 16.39 N ANISOU 2017 N SER A 423 1919 2151 2156 437 -312 -711 N ATOM 2018 CA SER A 423 29.722 40.147 11.585 1.00 17.12 C ANISOU 2018 CA SER A 423 2049 2188 2267 427 -316 -711 C ATOM 2019 C SER A 423 28.984 41.437 11.239 1.00 20.50 C ANISOU 2019 C SER A 423 2486 2542 2761 422 -314 -730 C ATOM 2020 O SER A 423 29.504 42.267 10.507 1.00 28.68 O ANISOU 2020 O SER A 423 3545 3534 3818 405 -310 -727 O ATOM 2021 CB SER A 423 29.769 39.236 10.348 1.00 26.78 C ANISOU 2021 CB SER A 423 3304 3389 3481 445 -351 -659 C ATOM 2022 OG SER A 423 30.649 38.145 10.591 1.00 29.01 O ANISOU 2022 OG SER A 423 3576 3732 3714 447 -363 -653 O ATOM 2023 N ASN A 424 27.772 41.604 11.749 1.00 20.06 N ANISOU 2023 N ASN A 424 2408 2473 2739 436 -319 -749 N ATOM 2024 CA ASN A 424 26.945 42.738 11.331 1.00 19.89 C ANISOU 2024 CA ASN A 424 2397 2372 2789 440 -331 -770 C ATOM 2025 C ASN A 424 27.048 43.938 12.291 1.00 19.27 C ANISOU 2025 C ASN A 424 2271 2301 2752 422 -315 -850 C ATOM 2026 O ASN A 424 26.646 43.863 13.452 1.00 20.48 O ANISOU 2026 O ASN A 424 2368 2521 2892 427 -305 -902 O ATOM 2027 CB ASN A 424 25.489 42.292 11.170 1.00 25.20 C ANISOU 2027 CB ASN A 424 3071 3018 3486 470 -354 -760 C ATOM 2028 CG ASN A 424 24.621 43.350 10.518 1.00 33.37 C ANISOU 2028 CG ASN A 424 4126 3960 4593 482 -379 -777 C ATOM 2029 OD1 ASN A 424 25.027 44.501 10.361 1.00 30.77 O ANISOU 2029 OD1 ASN A 424 3800 3584 4306 464 -380 -797 O ATOM 2030 ND2 ASN A 424 23.420 42.963 10.137 1.00 32.67 N ANISOU 2030 ND2 ASN A 424 4046 3840 4525 513 -402 -771 N ATOM 2031 N ASP A 425 27.578 45.049 11.794 1.00 21.87 N ANISOU 2031 N ASP A 425 2612 2564 3133 403 -316 -861 N ATOM 2032 CA ASP A 425 27.740 46.248 12.605 1.00 23.05 C ANISOU 2032 CA ASP A 425 2706 2706 3346 389 -310 -946 C ATOM 2033 C ASP A 425 26.397 46.761 13.126 1.00 19.26 C ANISOU 2033 C ASP A 425 2186 2207 2923 409 -337 -1008 C ATOM 2034 O ASP A 425 26.330 47.356 14.194 1.00 20.86 O ANISOU 2034 O ASP A 425 2316 2456 3155 410 -333 -1102 O ATOM 2035 CB ASP A 425 28.457 47.338 11.805 1.00 25.00 C ANISOU 2035 CB ASP A 425 2976 2861 3661 362 -312 -929 C ATOM 2036 CG ASP A 425 29.950 47.085 11.685 1.00 26.22 C ANISOU 2036 CG ASP A 425 3139 3058 3765 334 -279 -912 C ATOM 2037 OD1 ASP A 425 30.487 46.261 12.460 1.00 26.11 O ANISOU 2037 OD1 ASP A 425 3101 3144 3675 339 -256 -938 O ATOM 2038 OD2 ASP A 425 30.589 47.722 10.827 1.00 28.70 O ANISOU 2038 OD2 ASP A 425 3481 3308 4115 306 -275 -871 O ATOM 2039 N ASP A 426 25.320 46.522 12.377 1.00 18.53 N ANISOU 2039 N ASP A 426 2135 2058 2847 430 -365 -967 N ATOM 2040 CA ASP A 426 23.999 46.950 12.850 1.00 22.49 C ANISOU 2040 CA ASP A 426 2598 2547 3399 450 -393 -1035 C ATOM 2041 C ASP A 426 23.457 46.096 14.002 1.00 22.95 C ANISOU 2041 C ASP A 426 2601 2727 3393 459 -375 -1072 C ATOM 2042 O ASP A 426 22.383 46.367 14.547 1.00 21.98 O ANISOU 2042 O ASP A 426 2431 2623 3297 472 -393 -1139 O ATOM 2043 CB ASP A 426 22.995 47.019 11.696 1.00 22.72 C ANISOU 2043 CB ASP A 426 2686 2477 3469 474 -431 -991 C ATOM 2044 CG ASP A 426 23.311 48.143 10.722 1.00 25.55 C ANISOU 2044 CG ASP A 426 3085 2717 3906 466 -457 -961 C ATOM 2045 OD1 ASP A 426 23.287 47.919 9.499 1.00 25.43 O ANISOU 2045 OD1 ASP A 426 3135 2647 3878 478 -469 -876 O ATOM 2046 OD2 ASP A 426 23.604 49.255 11.181 1.00 22.37 O ANISOU 2046 OD2 ASP A 426 2640 2280 3581 449 -468 -1022 O ATOM 2047 N LEU A 427 24.201 45.061 14.369 1.00 19.03 N ANISOU 2047 N LEU A 427 2105 2316 2811 451 -341 -1025 N ATOM 2048 CA LEU A 427 23.849 44.244 15.520 1.00 19.14 C ANISOU 2048 CA LEU A 427 2062 2453 2757 455 -320 -1040 C ATOM 2049 C LEU A 427 24.965 44.292 16.560 1.00 21.45 C ANISOU 2049 C LEU A 427 2301 2851 2997 444 -288 -1077 C ATOM 2050 O LEU A 427 25.112 43.375 17.366 1.00 21.00 O ANISOU 2050 O LEU A 427 2214 2903 2861 445 -265 -1052 O ATOM 2051 CB LEU A 427 23.605 42.794 15.080 1.00 18.15 C ANISOU 2051 CB LEU A 427 1980 2336 2582 462 -316 -943 C ATOM 2052 CG LEU A 427 22.434 42.594 14.115 1.00 17.68 C ANISOU 2052 CG LEU A 427 1961 2188 2569 482 -345 -917 C ATOM 2053 CD1 LEU A 427 22.377 41.148 13.592 1.00 20.68 C ANISOU 2053 CD1 LEU A 427 2373 2567 2916 492 -346 -828 C ATOM 2054 CD2 LEU A 427 21.143 42.942 14.832 1.00 18.04 C ANISOU 2054 CD2 LEU A 427 1950 2264 2638 488 -353 -987 C ATOM 2055 N ALA A 428 25.734 45.375 16.535 1.00 24.65 N ANISOU 2055 N ALA A 428 2692 3221 3453 436 -289 -1136 N ATOM 2056 CA ALA A 428 26.898 45.542 17.407 1.00 24.20 C ANISOU 2056 CA ALA A 428 2583 3252 3358 431 -260 -1188 C ATOM 2057 C ALA A 428 26.651 45.204 18.883 1.00 24.07 C ANISOU 2057 C ALA A 428 2475 3398 3272 447 -241 -1244 C ATOM 2058 O ALA A 428 27.457 44.505 19.500 1.00 23.12 O ANISOU 2058 O ALA A 428 2340 3376 3067 450 -213 -1224 O ATOM 2059 CB ALA A 428 27.473 46.942 17.269 1.00 29.02 C ANISOU 2059 CB ALA A 428 3169 3793 4065 422 -269 -1267 C ATOM 2060 N VAL A 429 25.549 45.684 19.456 1.00 22.21 N ANISOU 2060 N VAL A 429 2175 3200 3065 459 -257 -1315 N ATOM 2061 CA VAL A 429 25.299 45.412 20.865 1.00 25.95 C ANISOU 2061 CA VAL A 429 2547 3850 3460 474 -238 -1370 C ATOM 2062 C VAL A 429 25.150 43.906 21.142 1.00 29.63 C ANISOU 2062 C VAL A 429 3039 4400 3820 469 -213 -1253 C ATOM 2063 O VAL A 429 25.593 43.403 22.177 1.00 23.67 O ANISOU 2063 O VAL A 429 2229 3792 2973 478 -185 -1251 O ATOM 2064 CB VAL A 429 24.107 46.218 21.420 1.00 33.25 C ANISOU 2064 CB VAL A 429 3385 4814 4433 486 -264 -1481 C ATOM 2065 CG1 VAL A 429 22.787 45.625 20.953 1.00 30.46 C ANISOU 2065 CG1 VAL A 429 3072 4422 4080 479 -278 -1419 C ATOM 2066 CG2 VAL A 429 24.176 46.252 22.924 1.00 37.52 C ANISOU 2066 CG2 VAL A 429 3799 5560 4896 506 -244 -1568 C ATOM 2067 N TYR A 430 24.580 43.185 20.185 1.00 24.76 N ANISOU 2067 N TYR A 430 2503 3684 3219 458 -225 -1154 N ATOM 2068 CA TYR A 430 24.400 41.739 20.299 1.00 25.66 C ANISOU 2068 CA TYR A 430 2642 3844 3263 452 -210 -1038 C ATOM 2069 C TYR A 430 25.687 40.977 19.982 1.00 26.86 C ANISOU 2069 C TYR A 430 2849 3983 3373 450 -202 -964 C ATOM 2070 O TYR A 430 25.962 39.928 20.565 1.00 26.91 O ANISOU 2070 O TYR A 430 2844 4073 3307 450 -188 -894 O ATOM 2071 CB TYR A 430 23.216 41.282 19.438 1.00 27.28 C ANISOU 2071 CB TYR A 430 2896 3953 3517 448 -231 -983 C ATOM 2072 CG TYR A 430 21.963 42.024 19.847 1.00 26.51 C ANISOU 2072 CG TYR A 430 2737 3882 3454 452 -242 -1071 C ATOM 2073 CD1 TYR A 430 21.339 41.740 21.057 1.00 27.45 C ANISOU 2073 CD1 TYR A 430 2766 4155 3509 447 -221 -1091 C ATOM 2074 CD2 TYR A 430 21.444 43.047 19.065 1.00 27.15 C ANISOU 2074 CD2 TYR A 430 2842 3845 3628 460 -276 -1138 C ATOM 2075 CE1 TYR A 430 20.211 42.429 21.464 1.00 26.34 C ANISOU 2075 CE1 TYR A 430 2558 4056 3395 451 -235 -1188 C ATOM 2076 CE2 TYR A 430 20.312 43.754 19.465 1.00 27.57 C ANISOU 2076 CE2 TYR A 430 2834 3925 3718 466 -296 -1236 C ATOM 2077 CZ TYR A 430 19.701 43.437 20.668 1.00 33.56 C ANISOU 2077 CZ TYR A 430 3498 4843 4409 461 -275 -1267 C ATOM 2078 OH TYR A 430 18.586 44.129 21.086 1.00 33.65 O ANISOU 2078 OH TYR A 430 3439 4896 4452 467 -297 -1378 O ATOM 2079 N ARG A 431 26.477 41.517 19.067 1.00 22.59 N ANISOU 2079 N ARG A 431 2364 3339 2879 446 -213 -980 N ATOM 2080 CA ARG A 431 27.819 41.003 18.837 1.00 24.38 C ANISOU 2080 CA ARG A 431 2630 3568 3067 444 -206 -943 C ATOM 2081 C ARG A 431 28.616 40.956 20.149 1.00 27.05 C ANISOU 2081 C ARG A 431 2900 4052 3327 455 -179 -988 C ATOM 2082 O ARG A 431 29.289 39.971 20.457 1.00 23.91 O ANISOU 2082 O ARG A 431 2512 3711 2860 460 -174 -930 O ATOM 2083 CB ARG A 431 28.537 41.894 17.844 1.00 20.49 C ANISOU 2083 CB ARG A 431 2183 2969 2635 434 -214 -977 C ATOM 2084 CG ARG A 431 30.046 41.734 17.848 1.00 19.59 C ANISOU 2084 CG ARG A 431 2083 2881 2479 429 -200 -985 C ATOM 2085 CD ARG A 431 30.613 42.209 16.539 1.00 36.03 C ANISOU 2085 CD ARG A 431 4227 4848 4613 411 -211 -972 C ATOM 2086 NE ARG A 431 30.566 43.649 16.438 1.00 36.31 N ANISOU 2086 NE ARG A 431 4240 4827 4729 401 -208 -1045 N ATOM 2087 CZ ARG A 431 30.389 44.330 15.312 1.00 26.88 C ANISOU 2087 CZ ARG A 431 3091 3516 3606 385 -224 -1022 C ATOM 2088 NH1 ARG A 431 30.208 43.715 14.145 1.00 22.46 N ANISOU 2088 NH1 ARG A 431 2600 2896 3038 383 -242 -935 N ATOM 2089 NH2 ARG A 431 30.381 45.651 15.369 1.00 23.25 N ANISOU 2089 NH2 ARG A 431 2600 3002 3232 375 -225 -1088 N ATOM 2090 N GLU A 432 28.545 42.033 20.921 1.00 27.16 N ANISOU 2090 N GLU A 432 2837 4127 3354 465 -167 -1099 N ATOM 2091 CA GLU A 432 29.329 42.109 22.148 1.00 24.81 C ANISOU 2091 CA GLU A 432 2463 3979 2983 486 -143 -1161 C ATOM 2092 C GLU A 432 28.851 41.128 23.216 1.00 26.26 C ANISOU 2092 C GLU A 432 2597 4313 3067 498 -129 -1102 C ATOM 2093 O GLU A 432 29.666 40.509 23.915 1.00 26.26 O ANISOU 2093 O GLU A 432 2579 4418 2982 514 -114 -1079 O ATOM 2094 CB GLU A 432 29.357 43.544 22.668 1.00 34.33 C ANISOU 2094 CB GLU A 432 3585 5215 4246 500 -140 -1311 C ATOM 2095 CG GLU A 432 29.912 44.498 21.625 1.00 34.54 C ANISOU 2095 CG GLU A 432 3659 5085 4378 483 -153 -1351 C ATOM 2096 CD GLU A 432 30.114 45.904 22.133 1.00 38.37 C ANISOU 2096 CD GLU A 432 4054 5583 4942 496 -157 -1501 C ATOM 2097 OE1 GLU A 432 29.821 46.169 23.319 1.00 37.72 O ANISOU 2097 OE1 GLU A 432 3864 5643 4826 526 -151 -1593 O ATOM 2098 OE2 GLU A 432 30.577 46.742 21.333 1.00 37.58 O ANISOU 2098 OE2 GLU A 432 3986 5353 4941 477 -167 -1528 O ATOM 2099 N CYS A 433 27.535 40.966 23.319 1.00 23.95 N ANISOU 2099 N CYS A 433 2284 4032 2785 489 -134 -1072 N ATOM 2100 CA CYS A 433 26.957 40.021 24.263 1.00 26.72 C ANISOU 2100 CA CYS A 433 2585 4520 3046 490 -118 -996 C ATOM 2101 C CYS A 433 27.442 38.612 23.959 1.00 27.80 C ANISOU 2101 C CYS A 433 2791 4626 3147 481 -124 -854 C ATOM 2102 O CYS A 433 27.819 37.863 24.853 1.00 24.73 O ANISOU 2102 O CYS A 433 2368 4362 2668 491 -110 -796 O ATOM 2103 CB CYS A 433 25.436 40.031 24.160 1.00 31.81 C ANISOU 2103 CB CYS A 433 3211 5150 3727 473 -125 -982 C ATOM 2104 SG CYS A 433 24.578 39.205 25.520 1.00 85.38 S ANISOU 2104 SG CYS A 433 9900 12139 10402 468 -97 -915 S ATOM 2105 N ILE A 434 27.410 38.250 22.684 1.00 25.81 N ANISOU 2105 N ILE A 434 2629 4210 2966 465 -150 -799 N ATOM 2106 CA ILE A 434 27.744 36.894 22.283 1.00 25.74 C ANISOU 2106 CA ILE A 434 2678 4156 2947 459 -168 -675 C ATOM 2107 C ILE A 434 29.202 36.604 22.595 1.00 27.80 C ANISOU 2107 C ILE A 434 2948 4465 3148 475 -169 -680 C ATOM 2108 O ILE A 434 29.537 35.561 23.153 1.00 27.97 O ANISOU 2108 O ILE A 434 2964 4552 3114 481 -174 -596 O ATOM 2109 CB ILE A 434 27.471 36.666 20.778 1.00 27.61 C ANISOU 2109 CB ILE A 434 2996 4218 3275 449 -201 -641 C ATOM 2110 CG1 ILE A 434 25.971 36.539 20.539 1.00 31.50 C ANISOU 2110 CG1 ILE A 434 3480 4670 3819 438 -205 -612 C ATOM 2111 CG2 ILE A 434 28.198 35.411 20.289 1.00 29.82 C ANISOU 2111 CG2 ILE A 434 3325 4451 3553 450 -231 -552 C ATOM 2112 CD1 ILE A 434 25.583 36.487 19.087 1.00 30.68 C ANISOU 2112 CD1 ILE A 434 3444 4409 3803 438 -235 -600 C ATOM 2113 N ILE A 435 30.070 37.545 22.256 1.00 21.83 N ANISOU 2113 N ILE A 435 2206 3678 2411 482 -164 -781 N ATOM 2114 CA ILE A 435 31.482 37.337 22.494 1.00 27.70 C ANISOU 2114 CA ILE A 435 2958 4463 3102 498 -164 -805 C ATOM 2115 C ILE A 435 31.727 37.131 23.999 1.00 33.35 C ANISOU 2115 C ILE A 435 3595 5360 3715 525 -141 -813 C ATOM 2116 O ILE A 435 32.503 36.263 24.400 1.00 35.25 O ANISOU 2116 O ILE A 435 3845 5656 3893 540 -151 -762 O ATOM 2117 CB ILE A 435 32.317 38.511 21.956 1.00 24.67 C ANISOU 2117 CB ILE A 435 2589 4023 2763 497 -155 -921 C ATOM 2118 CG1 ILE A 435 32.218 38.579 20.428 1.00 28.83 C ANISOU 2118 CG1 ILE A 435 3197 4387 3372 472 -180 -892 C ATOM 2119 CG2 ILE A 435 33.770 38.361 22.361 1.00 35.05 C ANISOU 2119 CG2 ILE A 435 3899 5400 4018 516 -150 -968 C ATOM 2120 CD1 ILE A 435 32.826 39.838 19.835 1.00 27.39 C ANISOU 2120 CD1 ILE A 435 3024 4137 3245 461 -169 -986 C ATOM 2121 N GLU A 436 31.043 37.912 24.828 1.00 34.40 N ANISOU 2121 N GLU A 436 3645 5595 3830 534 -114 -879 N ATOM 2122 CA GLU A 436 31.210 37.801 26.281 1.00 34.51 C ANISOU 2122 CA GLU A 436 3568 5810 3735 566 -90 -895 C ATOM 2123 C GLU A 436 30.618 36.520 26.857 1.00 37.33 C ANISOU 2123 C GLU A 436 3915 6243 4026 558 -92 -742 C ATOM 2124 O GLU A 436 31.192 35.906 27.755 1.00 42.66 O ANISOU 2124 O GLU A 436 4557 7046 4604 583 -86 -697 O ATOM 2125 CB GLU A 436 30.622 39.026 26.984 1.00 41.13 C ANISOU 2125 CB GLU A 436 4304 6748 4575 581 -67 -1025 C ATOM 2126 CG GLU A 436 31.354 40.316 26.655 1.00 55.79 C ANISOU 2126 CG GLU A 436 6149 8548 6502 594 -66 -1182 C ATOM 2127 CD GLU A 436 31.062 41.431 27.638 1.00 75.63 C ANISOU 2127 CD GLU A 436 8532 11197 9006 625 -51 -1331 C ATOM 2128 OE1 GLU A 436 29.872 41.707 27.915 1.00 81.62 O ANISOU 2128 OE1 GLU A 436 9237 12000 9776 617 -53 -1343 O ATOM 2129 OE2 GLU A 436 32.032 42.044 28.134 1.00 78.22 O ANISOU 2129 OE2 GLU A 436 8805 11592 9321 661 -40 -1449 O ATOM 2130 N LYS A 437 29.477 36.117 26.320 1.00 34.42 N ANISOU 2130 N LYS A 437 3573 5791 3714 524 -102 -659 N ATOM 2131 CA LYS A 437 28.681 35.055 26.913 1.00 35.08 C ANISOU 2131 CA LYS A 437 3629 5947 3753 508 -98 -518 C ATOM 2132 C LYS A 437 29.228 33.683 26.588 1.00 36.49 C ANISOU 2132 C LYS A 437 3871 6055 3937 502 -131 -380 C ATOM 2133 O LYS A 437 29.155 32.771 27.411 1.00 34.69 O ANISOU 2133 O LYS A 437 3611 5926 3644 503 -129 -264 O ATOM 2134 CB LYS A 437 27.229 35.160 26.446 1.00 40.06 C ANISOU 2134 CB LYS A 437 4257 6509 4454 475 -96 -496 C ATOM 2135 CG LYS A 437 26.387 33.920 26.698 1.00 47.83 C ANISOU 2135 CG LYS A 437 5233 7509 5432 447 -98 -334 C ATOM 2136 CD LYS A 437 25.916 33.861 28.142 1.00 52.69 C ANISOU 2136 CD LYS A 437 5740 8347 5931 448 -60 -301 C ATOM 2137 CE LYS A 437 25.062 32.631 28.383 1.00 57.79 C ANISOU 2137 CE LYS A 437 6376 9004 6580 411 -58 -125 C ATOM 2138 NZ LYS A 437 24.815 32.402 29.831 1.00 62.48 N ANISOU 2138 NZ LYS A 437 6865 9834 7040 411 -20 -62 N ATOM 2139 N CYS A 438 29.774 33.512 25.388 1.00 27.46 N ANISOU 2139 N CYS A 438 2813 4745 2875 497 -167 -391 N ATOM 2140 CA CYS A 438 30.245 32.181 25.025 1.00 29.85 C ANISOU 2140 CA CYS A 438 3167 4974 3200 494 -211 -274 C ATOM 2141 C CYS A 438 31.667 32.099 24.489 1.00 28.94 C ANISOU 2141 C CYS A 438 3106 4803 3086 515 -243 -328 C ATOM 2142 O CYS A 438 32.271 31.025 24.556 1.00 35.41 O ANISOU 2142 O CYS A 438 3947 5610 3898 524 -283 -249 O ATOM 2143 CB CYS A 438 29.252 31.457 24.095 1.00 32.61 C ANISOU 2143 CB CYS A 438 3553 5181 3657 465 -240 -185 C ATOM 2144 SG CYS A 438 29.294 31.921 22.367 1.00 40.68 S ANISOU 2144 SG CYS A 438 4651 6013 4791 460 -269 -266 S ATOM 2145 N LEU A 439 32.214 33.202 23.971 1.00 24.85 N ANISOU 2145 N LEU A 439 2607 4251 2584 522 -229 -462 N ATOM 2146 CA LEU A 439 33.559 33.130 23.362 1.00 22.16 C ANISOU 2146 CA LEU A 439 2316 3856 2248 534 -256 -519 C ATOM 2147 C LEU A 439 34.696 33.419 24.356 1.00 19.92 C ANISOU 2147 C LEU A 439 1997 3705 1868 569 -238 -592 C ATOM 2148 O LEU A 439 35.651 32.644 24.449 1.00 23.53 O ANISOU 2148 O LEU A 439 2475 4172 2292 587 -271 -570 O ATOM 2149 CB LEU A 439 33.672 34.026 22.116 1.00 21.47 C ANISOU 2149 CB LEU A 439 2273 3648 2235 518 -256 -607 C ATOM 2150 CG LEU A 439 32.612 33.816 21.030 1.00 25.07 C ANISOU 2150 CG LEU A 439 2767 3977 2784 494 -276 -553 C ATOM 2151 CD1 LEU A 439 32.928 34.683 19.817 1.00 25.72 C ANISOU 2151 CD1 LEU A 439 2893 3957 2921 483 -278 -632 C ATOM 2152 CD2 LEU A 439 32.548 32.344 20.640 1.00 24.06 C ANISOU 2152 CD2 LEU A 439 2664 3790 2688 494 -330 -443 C ATOM 2153 N MET A 440 34.611 34.527 25.086 1.00 22.20 N ANISOU 2153 N MET A 440 2224 4096 2117 583 -190 -690 N ATOM 2154 CA MET A 440 35.679 34.874 26.042 1.00 21.05 C ANISOU 2154 CA MET A 440 2031 4085 1884 626 -171 -780 C ATOM 2155 C MET A 440 35.931 33.732 27.009 1.00 24.91 C ANISOU 2155 C MET A 440 2499 4687 2280 653 -188 -676 C ATOM 2156 O MET A 440 34.990 33.087 27.473 1.00 26.60 O ANISOU 2156 O MET A 440 2688 4944 2474 641 -188 -552 O ATOM 2157 CB MET A 440 35.340 36.133 26.835 1.00 28.78 C ANISOU 2157 CB MET A 440 2921 5176 2838 644 -123 -896 C ATOM 2158 CG MET A 440 35.158 37.366 25.994 1.00 34.77 C ANISOU 2158 CG MET A 440 3691 5824 3697 621 -111 -1003 C ATOM 2159 SD MET A 440 36.465 37.544 24.772 1.00 46.59 S ANISOU 2159 SD MET A 440 5272 7178 5253 606 -129 -1063 S ATOM 2160 CE MET A 440 37.902 37.840 25.761 1.00 20.07 C ANISOU 2160 CE MET A 440 1857 3956 1812 657 -110 -1189 C ATOM 2161 N ARG A 441 37.206 33.497 27.298 1.00 21.18 N ANISOU 2161 N ARG A 441 2035 4261 1753 688 -203 -726 N ATOM 2162 CA ARG A 441 37.656 32.416 28.179 1.00 24.45 C ANISOU 2162 CA ARG A 441 2436 4777 2078 722 -229 -634 C ATOM 2163 C ARG A 441 37.517 31.038 27.532 1.00 27.82 C ANISOU 2163 C ARG A 441 2929 5081 2562 696 -293 -484 C ATOM 2164 O ARG A 441 37.919 30.044 28.118 1.00 22.93 O ANISOU 2164 O ARG A 441 2309 4513 1892 720 -329 -394 O ATOM 2165 CB ARG A 441 36.954 32.470 29.543 1.00 28.87 C ANISOU 2165 CB ARG A 441 2904 5527 2539 745 -191 -581 C ATOM 2166 CG ARG A 441 37.248 33.743 30.324 1.00 32.20 C ANISOU 2166 CG ARG A 441 3239 6097 2900 786 -139 -749 C ATOM 2167 CD ARG A 441 36.328 33.895 31.539 1.00 41.90 C ANISOU 2167 CD ARG A 441 4363 7522 4037 803 -102 -707 C ATOM 2168 NE ARG A 441 34.920 33.818 31.161 1.00 50.36 N ANISOU 2168 NE ARG A 441 5436 8528 5170 748 -94 -615 N ATOM 2169 CZ ARG A 441 34.210 34.851 30.719 1.00 51.57 C ANISOU 2169 CZ ARG A 441 5569 8628 5396 724 -72 -711 C ATOM 2170 NH1 ARG A 441 34.778 36.044 30.602 1.00 49.13 N ANISOU 2170 NH1 ARG A 441 5233 8318 5117 747 -56 -892 N ATOM 2171 NH2 ARG A 441 32.934 34.689 30.390 1.00 52.35 N ANISOU 2171 NH2 ARG A 441 5673 8672 5547 678 -69 -627 N ATOM 2172 N ASN A 442 36.954 30.983 26.325 1.00 23.41 N ANISOU 2172 N ASN A 442 2474 4205 2217 -260 -85 -446 N ATOM 2173 CA ASN A 442 36.829 29.720 25.604 1.00 20.56 C ANISOU 2173 CA ASN A 442 2120 3764 1928 -288 -85 -337 C ATOM 2174 C ASN A 442 37.520 29.741 24.262 1.00 18.79 C ANISOU 2174 C ASN A 442 1935 3379 1826 -243 -120 -334 C ATOM 2175 O ASN A 442 37.320 28.834 23.451 1.00 21.38 O ANISOU 2175 O ASN A 442 2263 3633 2229 -255 -119 -276 O ATOM 2176 CB ASN A 442 35.350 29.374 25.380 1.00 22.92 C ANISOU 2176 CB ASN A 442 2371 4103 2234 -303 -32 -358 C ATOM 2177 CG ASN A 442 34.596 29.239 26.677 1.00 30.51 C ANISOU 2177 CG ASN A 442 3290 5226 3078 -355 17 -352 C ATOM 2178 OD1 ASN A 442 33.612 29.932 26.916 1.00 35.44 O ANISOU 2178 OD1 ASN A 442 3874 5926 3666 -341 57 -454 O ATOM 2179 ND2 ASN A 442 35.070 28.355 27.534 1.00 23.35 N ANISOU 2179 ND2 ASN A 442 2391 4373 2109 -412 14 -231 N ATOM 2180 N LEU A 443 38.346 30.757 24.027 1.00 18.21 N ANISOU 2180 N LEU A 443 1890 3253 1776 -194 -147 -399 N ATOM 2181 CA LEU A 443 38.885 30.962 22.675 1.00 18.03 C ANISOU 2181 CA LEU A 443 1904 3084 1863 -144 -167 -408 C ATOM 2182 C LEU A 443 39.764 29.800 22.222 1.00 19.94 C ANISOU 2182 C LEU A 443 2172 3236 2168 -174 -195 -298 C ATOM 2183 O LEU A 443 39.696 29.382 21.067 1.00 16.73 O ANISOU 2183 O LEU A 443 1778 2737 1843 -156 -196 -284 O ATOM 2184 CB LEU A 443 39.636 32.291 22.551 1.00 17.05 C ANISOU 2184 CB LEU A 443 1802 2913 1764 -88 -181 -492 C ATOM 2185 CG LEU A 443 38.792 33.554 22.721 1.00 18.45 C ANISOU 2185 CG LEU A 443 1949 3144 1919 -44 -154 -613 C ATOM 2186 CD1 LEU A 443 39.643 34.805 22.576 1.00 18.88 C ANISOU 2186 CD1 LEU A 443 2019 3131 2024 8 -166 -687 C ATOM 2187 CD2 LEU A 443 37.616 33.610 21.722 1.00 19.45 C ANISOU 2187 CD2 LEU A 443 2061 3244 2086 -8 -131 -641 C ATOM 2188 N LEU A 444 40.576 29.258 23.121 1.00 17.30 N ANISOU 2188 N LEU A 444 1843 2932 1799 -218 -221 -225 N ATOM 2189 CA LEU A 444 41.478 28.169 22.735 1.00 20.24 C ANISOU 2189 CA LEU A 444 2233 3210 2247 -246 -252 -123 C ATOM 2190 C LEU A 444 40.677 26.924 22.375 1.00 19.04 C ANISOU 2190 C LEU A 444 2053 3047 2132 -285 -230 -52 C ATOM 2191 O LEU A 444 40.940 26.289 21.365 1.00 17.47 O ANISOU 2191 O LEU A 444 1862 2743 2034 -281 -238 -26 O ATOM 2192 CB LEU A 444 42.498 27.861 23.848 1.00 19.87 C ANISOU 2192 CB LEU A 444 2192 3203 2153 -281 -292 -54 C ATOM 2193 CG LEU A 444 43.412 26.651 23.595 1.00 20.43 C ANISOU 2193 CG LEU A 444 2273 3181 2310 -314 -327 60 C ATOM 2194 CD1 LEU A 444 44.249 26.824 22.303 1.00 20.04 C ANISOU 2194 CD1 LEU A 444 2253 2978 2385 -275 -341 28 C ATOM 2195 CD2 LEU A 444 44.321 26.413 24.793 1.00 21.57 C ANISOU 2195 CD2 LEU A 444 2418 3382 2395 -343 -374 129 C ATOM 2196 N SER A 445 39.673 26.588 23.180 1.00 18.41 N ANISOU 2196 N SER A 445 1936 3079 1980 -324 -197 -30 N ATOM 2197 CA SER A 445 38.899 25.398 22.887 1.00 18.09 C ANISOU 2197 CA SER A 445 1859 3023 1991 -366 -171 34 C ATOM 2198 C SER A 445 38.085 25.571 21.606 1.00 22.73 C ANISOU 2198 C SER A 445 2434 3553 2648 -325 -153 -48 C ATOM 2199 O SER A 445 38.048 24.672 20.780 1.00 21.61 O ANISOU 2199 O SER A 445 2280 3329 2603 -336 -156 -17 O ATOM 2200 CB SER A 445 37.961 25.034 24.047 1.00 29.38 C ANISOU 2200 CB SER A 445 3248 4586 3329 -418 -129 77 C ATOM 2201 OG SER A 445 37.057 26.084 24.322 1.00 39.99 O ANISOU 2201 OG SER A 445 4576 6025 4594 -391 -96 -33 O ATOM 2202 N LEU A 446 37.444 26.726 21.444 1.00 19.51 N ANISOU 2202 N LEU A 446 2027 3191 2196 -276 -137 -157 N ATOM 2203 CA LEU A 446 36.547 26.941 20.302 1.00 20.09 C ANISOU 2203 CA LEU A 446 2084 3228 2320 -231 -124 -234 C ATOM 2204 C LEU A 446 37.322 27.062 19.002 1.00 19.44 C ANISOU 2204 C LEU A 446 2043 3025 2318 -183 -155 -249 C ATOM 2205 O LEU A 446 36.825 26.722 17.933 1.00 19.99 O ANISOU 2205 O LEU A 446 2100 3049 2445 -159 -155 -277 O ATOM 2206 CB LEU A 446 35.669 28.177 20.516 1.00 17.48 C ANISOU 2206 CB LEU A 446 1739 2975 1927 -188 -103 -340 C ATOM 2207 CG LEU A 446 34.621 28.041 21.626 1.00 20.58 C ANISOU 2207 CG LEU A 446 2079 3495 2245 -234 -59 -347 C ATOM 2208 CD1 LEU A 446 33.911 29.365 21.827 1.00 28.54 C ANISOU 2208 CD1 LEU A 446 3071 4569 3205 -187 -41 -465 C ATOM 2209 CD2 LEU A 446 33.629 26.928 21.342 1.00 25.56 C ANISOU 2209 CD2 LEU A 446 2657 4129 2926 -273 -31 -317 C ATOM 2210 N SER A 447 38.550 27.548 19.087 1.00 17.75 N ANISOU 2210 N SER A 447 1876 2763 2106 -166 -180 -235 N ATOM 2211 CA SER A 447 39.355 27.670 17.884 1.00 17.66 C ANISOU 2211 CA SER A 447 1904 2638 2167 -124 -200 -245 C ATOM 2212 C SER A 447 39.764 26.283 17.375 1.00 20.82 C ANISOU 2212 C SER A 447 2294 2966 2651 -164 -212 -176 C ATOM 2213 O SER A 447 40.179 26.126 16.227 1.00 16.88 O ANISOU 2213 O SER A 447 1814 2382 2216 -135 -220 -191 O ATOM 2214 CB SER A 447 40.572 28.571 18.164 1.00 18.92 C ANISOU 2214 CB SER A 447 2108 2760 2320 -99 -217 -254 C ATOM 2215 OG SER A 447 41.611 27.816 18.746 1.00 45.09 O ANISOU 2215 OG SER A 447 5429 6047 5657 -148 -241 -175 O ATOM 2216 N GLN A 448 39.622 25.263 18.216 1.00 16.08 N ANISOU 2216 N GLN A 448 1659 2400 2053 -231 -209 -99 N ATOM 2217 CA GLN A 448 39.937 23.901 17.780 1.00 17.44 C ANISOU 2217 CA GLN A 448 1807 2495 2324 -273 -218 -34 C ATOM 2218 C GLN A 448 38.712 23.114 17.328 1.00 19.44 C ANISOU 2218 C GLN A 448 2003 2763 2620 -291 -194 -53 C ATOM 2219 O GLN A 448 38.800 21.917 17.093 1.00 20.38 O ANISOU 2219 O GLN A 448 2086 2826 2832 -332 -195 -4 O ATOM 2220 CB GLN A 448 40.626 23.127 18.896 1.00 18.49 C ANISOU 2220 CB GLN A 448 1930 2633 2460 -335 -233 78 C ATOM 2221 CG GLN A 448 42.000 23.652 19.230 1.00 17.33 C ANISOU 2221 CG GLN A 448 1831 2452 2302 -322 -268 97 C ATOM 2222 CD GLN A 448 42.567 22.993 20.461 1.00 26.44 C ANISOU 2222 CD GLN A 448 2973 3637 3435 -377 -290 208 C ATOM 2223 OE1 GLN A 448 43.048 21.869 20.401 1.00 25.15 O ANISOU 2223 OE1 GLN A 448 2789 3403 3362 -415 -307 292 O ATOM 2224 NE2 GLN A 448 42.509 23.691 21.592 1.00 23.78 N ANISOU 2224 NE2 GLN A 448 2646 3408 2981 -379 -293 207 N ATOM 2225 N GLU A 449 37.573 23.784 17.228 1.00 18.58 N ANISOU 2225 N GLU A 449 1878 2727 2455 -259 -172 -129 N ATOM 2226 CA GLU A 449 36.357 23.133 16.761 1.00 22.06 C ANISOU 2226 CA GLU A 449 2257 3184 2940 -270 -151 -165 C ATOM 2227 C GLU A 449 36.088 23.412 15.290 1.00 23.42 C ANISOU 2227 C GLU A 449 2435 3314 3148 -205 -167 -257 C ATOM 2228 O GLU A 449 36.307 24.522 14.810 1.00 18.91 O ANISOU 2228 O GLU A 449 1913 2743 2530 -140 -180 -309 O ATOM 2229 CB GLU A 449 35.168 23.608 17.594 1.00 26.39 C ANISOU 2229 CB GLU A 449 2771 3845 3410 -279 -117 -196 C ATOM 2230 CG GLU A 449 35.315 23.274 19.045 1.00 29.05 C ANISOU 2230 CG GLU A 449 3098 4246 3695 -344 -96 -105 C ATOM 2231 CD GLU A 449 34.044 22.758 19.649 1.00 41.87 C ANISOU 2231 CD GLU A 449 4653 5945 5310 -390 -47 -98 C ATOM 2232 OE1 GLU A 449 33.967 22.692 20.894 1.00 47.96 O ANISOU 2232 OE1 GLU A 449 5416 6797 6008 -437 -20 -34 O ATOM 2233 OE2 GLU A 449 33.125 22.416 18.876 1.00 41.99 O ANISOU 2233 OE2 GLU A 449 4620 5943 5392 -380 -36 -159 O ATOM 2234 N LYS A 450 35.589 22.409 14.575 1.00 18.15 N ANISOU 2234 N LYS A 450 1715 2613 2568 -221 -167 -277 N ATOM 2235 CA LYS A 450 35.355 22.552 13.148 1.00 18.62 C ANISOU 2235 CA LYS A 450 1777 2643 2654 -160 -187 -365 C ATOM 2236 C LYS A 450 34.426 23.729 12.851 1.00 19.31 C ANISOU 2236 C LYS A 450 1874 2802 2662 -90 -189 -449 C ATOM 2237 O LYS A 450 34.712 24.546 11.981 1.00 17.41 O ANISOU 2237 O LYS A 450 1681 2545 2387 -19 -209 -491 O ATOM 2238 CB LYS A 450 34.753 21.270 12.583 1.00 17.87 C ANISOU 2238 CB LYS A 450 1604 2520 2666 -193 -185 -392 C ATOM 2239 CG LYS A 450 34.526 21.302 11.066 1.00 20.82 C ANISOU 2239 CG LYS A 450 1973 2876 3060 -129 -212 -491 C ATOM 2240 CD LYS A 450 33.781 20.046 10.622 1.00 23.51 C ANISOU 2240 CD LYS A 450 2219 3200 3512 -165 -209 -538 C ATOM 2241 CE LYS A 450 33.497 20.073 9.131 1.00 31.01 C ANISOU 2241 CE LYS A 450 3159 4153 4470 -98 -241 -649 C ATOM 2242 NZ LYS A 450 34.763 20.151 8.348 1.00 37.09 N ANISOU 2242 NZ LYS A 450 3992 4863 5239 -72 -258 -639 N ATOM 2243 N PHE A 451 33.301 23.812 13.560 1.00 17.98 N ANISOU 2243 N PHE A 451 1655 2710 2468 -109 -166 -470 N ATOM 2244 CA PHE A 451 32.322 24.862 13.241 1.00 17.05 C ANISOU 2244 CA PHE A 451 1531 2654 2292 -42 -171 -558 C ATOM 2245 C PHE A 451 32.591 26.157 14.002 1.00 20.57 C ANISOU 2245 C PHE A 451 2025 3138 2652 -16 -162 -552 C ATOM 2246 O PHE A 451 32.578 27.241 13.420 1.00 19.75 O ANISOU 2246 O PHE A 451 1959 3033 2514 60 -180 -600 O ATOM 2247 CB PHE A 451 30.883 24.364 13.461 1.00 17.40 C ANISOU 2247 CB PHE A 451 1486 2758 2366 -67 -151 -609 C ATOM 2248 CG PHE A 451 30.595 23.089 12.723 1.00 20.29 C ANISOU 2248 CG PHE A 451 1792 3083 2834 -93 -159 -629 C ATOM 2249 CD1 PHE A 451 30.572 23.079 11.337 1.00 21.16 C ANISOU 2249 CD1 PHE A 451 1907 3167 2967 -30 -200 -700 C ATOM 2250 CD2 PHE A 451 30.413 21.896 13.406 1.00 22.34 C ANISOU 2250 CD2 PHE A 451 1991 3328 3170 -180 -125 -575 C ATOM 2251 CE1 PHE A 451 30.336 21.900 10.638 1.00 25.73 C ANISOU 2251 CE1 PHE A 451 2422 3709 3645 -54 -209 -736 C ATOM 2252 CE2 PHE A 451 30.176 20.709 12.712 1.00 25.42 C ANISOU 2252 CE2 PHE A 451 2316 3668 3676 -205 -131 -602 C ATOM 2253 CZ PHE A 451 30.144 20.717 11.332 1.00 25.88 C ANISOU 2253 CZ PHE A 451 2373 3704 3758 -143 -175 -691 C ATOM 2254 N ALA A 452 32.867 26.053 15.296 1.00 17.27 N ANISOU 2254 N ALA A 452 1606 2753 2204 -76 -136 -493 N ATOM 2255 CA ALA A 452 33.017 27.266 16.089 1.00 16.50 C ANISOU 2255 CA ALA A 452 1539 2704 2027 -55 -126 -508 C ATOM 2256 C ALA A 452 34.267 28.063 15.712 1.00 18.19 C ANISOU 2256 C ALA A 452 1828 2853 2231 -9 -150 -494 C ATOM 2257 O ALA A 452 34.336 29.266 15.953 1.00 15.99 O ANISOU 2257 O ALA A 452 1573 2593 1910 34 -149 -534 O ATOM 2258 CB ALA A 452 33.011 26.936 17.588 1.00 17.87 C ANISOU 2258 CB ALA A 452 1690 2946 2154 -130 -93 -452 C ATOM 2259 N SER A 453 35.264 27.413 15.121 1.00 17.84 N ANISOU 2259 N SER A 453 1816 2726 2236 -20 -168 -443 N ATOM 2260 CA SER A 453 36.458 28.153 14.726 1.00 16.92 C ANISOU 2260 CA SER A 453 1766 2542 2121 21 -184 -432 C ATOM 2261 C SER A 453 36.131 29.296 13.761 1.00 15.24 C ANISOU 2261 C SER A 453 1580 2317 1895 111 -191 -498 C ATOM 2262 O SER A 453 36.785 30.342 13.787 1.00 16.10 O ANISOU 2262 O SER A 453 1732 2395 1990 150 -189 -504 O ATOM 2263 CB SER A 453 37.541 27.226 14.149 1.00 18.56 C ANISOU 2263 CB SER A 453 1997 2661 2394 -4 -198 -375 C ATOM 2264 OG SER A 453 37.052 26.472 13.051 1.00 19.10 O ANISOU 2264 OG SER A 453 2039 2706 2510 8 -206 -402 O ATOM 2265 N HIS A 454 35.121 29.103 12.925 1.00 15.29 N ANISOU 2265 N HIS A 454 1556 2346 1909 145 -199 -546 N ATOM 2266 CA HIS A 454 34.680 30.159 12.031 1.00 15.82 C ANISOU 2266 CA HIS A 454 1643 2411 1958 236 -211 -599 C ATOM 2267 C HIS A 454 34.060 31.332 12.790 1.00 19.90 C ANISOU 2267 C HIS A 454 2143 2979 2438 263 -199 -644 C ATOM 2268 O HIS A 454 34.161 32.474 12.350 1.00 16.25 O ANISOU 2268 O HIS A 454 1712 2491 1971 333 -203 -666 O ATOM 2269 CB HIS A 454 33.654 29.620 11.047 1.00 15.30 C ANISOU 2269 CB HIS A 454 1537 2372 1905 266 -232 -647 C ATOM 2270 CG HIS A 454 34.197 28.570 10.149 1.00 15.40 C ANISOU 2270 CG HIS A 454 1558 2337 1957 251 -245 -626 C ATOM 2271 ND1 HIS A 454 34.966 28.861 9.038 1.00 16.31 N ANISOU 2271 ND1 HIS A 454 1729 2398 2068 304 -257 -615 N ATOM 2272 CD2 HIS A 454 34.113 27.217 10.197 1.00 17.84 C ANISOU 2272 CD2 HIS A 454 1821 2641 2318 186 -245 -616 C ATOM 2273 CE1 HIS A 454 35.323 27.741 8.449 1.00 20.46 C ANISOU 2273 CE1 HIS A 454 2243 2895 2637 274 -264 -610 C ATOM 2274 NE2 HIS A 454 34.814 26.728 9.129 1.00 19.16 N ANISOU 2274 NE2 HIS A 454 2013 2752 2513 203 -259 -612 N ATOM 2275 N VAL A 455 33.407 31.040 13.911 1.00 17.57 N ANISOU 2275 N VAL A 455 1797 2756 2123 207 -180 -658 N ATOM 2276 CA VAL A 455 32.809 32.084 14.744 1.00 16.06 C ANISOU 2276 CA VAL A 455 1580 2624 1898 223 -162 -714 C ATOM 2277 C VAL A 455 33.896 32.876 15.423 1.00 16.54 C ANISOU 2277 C VAL A 455 1682 2657 1945 220 -154 -696 C ATOM 2278 O VAL A 455 33.793 34.091 15.541 1.00 16.76 O ANISOU 2278 O VAL A 455 1712 2683 1972 270 -149 -746 O ATOM 2279 CB VAL A 455 31.866 31.488 15.799 1.00 16.60 C ANISOU 2279 CB VAL A 455 1580 2786 1942 156 -135 -732 C ATOM 2280 CG1 VAL A 455 31.374 32.566 16.774 1.00 17.06 C ANISOU 2280 CG1 VAL A 455 1610 2911 1960 166 -111 -797 C ATOM 2281 CG2 VAL A 455 30.686 30.803 15.115 1.00 17.95 C ANISOU 2281 CG2 VAL A 455 1696 2979 2143 164 -142 -769 C ATOM 2282 N VAL A 456 34.935 32.174 15.878 1.00 15.82 N ANISOU 2282 N VAL A 456 1617 2541 1853 162 -153 -628 N ATOM 2283 CA VAL A 456 36.065 32.815 16.538 1.00 17.48 C ANISOU 2283 CA VAL A 456 1862 2725 2056 155 -151 -614 C ATOM 2284 C VAL A 456 36.735 33.787 15.562 1.00 15.14 C ANISOU 2284 C VAL A 456 1615 2334 1804 230 -159 -624 C ATOM 2285 O VAL A 456 37.066 34.912 15.927 1.00 15.67 O ANISOU 2285 O VAL A 456 1689 2386 1878 261 -151 -663 O ATOM 2286 CB VAL A 456 37.068 31.770 17.105 1.00 17.65 C ANISOU 2286 CB VAL A 456 1898 2731 2075 82 -159 -532 C ATOM 2287 CG1 VAL A 456 38.386 32.442 17.569 1.00 15.84 C ANISOU 2287 CG1 VAL A 456 1707 2458 1853 86 -167 -523 C ATOM 2288 CG2 VAL A 456 36.424 31.005 18.272 1.00 18.20 C ANISOU 2288 CG2 VAL A 456 1920 2904 2092 10 -143 -511 C ATOM 2289 N GLU A 457 36.902 33.369 14.311 1.00 14.81 N ANISOU 2289 N GLU A 457 1603 2230 1795 260 -171 -593 N ATOM 2290 CA GLU A 457 37.461 34.255 13.303 1.00 14.61 C ANISOU 2290 CA GLU A 457 1626 2121 1804 333 -171 -591 C ATOM 2291 C GLU A 457 36.637 35.526 13.148 1.00 16.51 C ANISOU 2291 C GLU A 457 1850 2377 2046 405 -166 -651 C ATOM 2292 O GLU A 457 37.178 36.635 13.184 1.00 17.82 O ANISOU 2292 O GLU A 457 2037 2489 2245 445 -153 -662 O ATOM 2293 CB GLU A 457 37.555 33.529 11.954 1.00 15.62 C ANISOU 2293 CB GLU A 457 1780 2208 1947 356 -183 -557 C ATOM 2294 CG GLU A 457 38.675 32.511 11.898 1.00 16.85 C ANISOU 2294 CG GLU A 457 1959 2312 2130 300 -184 -500 C ATOM 2295 CD GLU A 457 38.795 31.947 10.496 1.00 26.00 C ANISOU 2295 CD GLU A 457 3142 3432 3304 330 -192 -484 C ATOM 2296 OE1 GLU A 457 39.089 32.737 9.577 1.00 25.07 O ANISOU 2296 OE1 GLU A 457 3067 3270 3189 397 -183 -481 O ATOM 2297 OE2 GLU A 457 38.568 30.740 10.318 1.00 19.41 O ANISOU 2297 OE2 GLU A 457 2280 2615 2481 287 -204 -477 O ATOM 2298 N LYS A 458 35.327 35.373 12.984 1.00 17.12 N ANISOU 2298 N LYS A 458 1884 2521 2100 423 -176 -691 N ATOM 2299 CA LYS A 458 34.450 36.543 12.868 1.00 20.60 C ANISOU 2299 CA LYS A 458 2299 2977 2551 492 -177 -751 C ATOM 2300 C LYS A 458 34.562 37.472 14.081 1.00 19.73 C ANISOU 2300 C LYS A 458 2161 2885 2449 478 -154 -803 C ATOM 2301 O LYS A 458 34.542 38.690 13.930 1.00 18.20 O ANISOU 2301 O LYS A 458 1968 2650 2298 540 -148 -836 O ATOM 2302 CB LYS A 458 32.987 36.126 12.664 1.00 18.56 C ANISOU 2302 CB LYS A 458 1984 2795 2272 503 -193 -798 C ATOM 2303 CG LYS A 458 32.700 35.423 11.340 1.00 20.63 C ANISOU 2303 CG LYS A 458 2262 3046 2529 537 -223 -773 C ATOM 2304 CD LYS A 458 33.261 36.196 10.141 1.00 24.06 C ANISOU 2304 CD LYS A 458 2757 3405 2978 623 -233 -735 C ATOM 2305 CE LYS A 458 32.630 35.736 8.817 1.00 34.30 C ANISOU 2305 CE LYS A 458 4056 4722 4253 678 -270 -735 C ATOM 2306 NZ LYS A 458 33.145 34.402 8.405 1.00 39.39 N ANISOU 2306 NZ LYS A 458 4715 5365 4887 625 -274 -705 N ATOM 2307 N ALA A 459 34.671 36.898 15.277 1.00 16.11 N ANISOU 2307 N ALA A 459 1677 2493 1953 398 -143 -812 N ATOM 2308 CA ALA A 459 34.822 37.712 16.491 1.00 18.77 C ANISOU 2308 CA ALA A 459 1983 2866 2283 380 -123 -872 C ATOM 2309 C ALA A 459 36.105 38.550 16.454 1.00 18.05 C ANISOU 2309 C ALA A 459 1933 2682 2243 405 -119 -862 C ATOM 2310 O ALA A 459 36.073 39.751 16.727 1.00 18.77 O ANISOU 2310 O ALA A 459 2002 2752 2377 445 -106 -926 O ATOM 2311 CB ALA A 459 34.771 36.843 17.747 1.00 17.80 C ANISOU 2311 CB ALA A 459 1830 2841 2090 290 -113 -867 C ATOM 2312 N PHE A 460 37.231 37.932 16.101 1.00 16.61 N ANISOU 2312 N PHE A 460 1802 2439 2071 380 -126 -787 N ATOM 2313 CA PHE A 460 38.470 38.680 15.955 1.00 20.43 C ANISOU 2313 CA PHE A 460 2321 2824 2617 404 -118 -777 C ATOM 2314 C PHE A 460 38.318 39.802 14.910 1.00 23.61 C ANISOU 2314 C PHE A 460 2740 3140 3089 495 -107 -784 C ATOM 2315 O PHE A 460 38.737 40.936 15.146 1.00 17.73 O ANISOU 2315 O PHE A 460 1987 2341 2410 527 -89 -825 O ATOM 2316 CB PHE A 460 39.642 37.761 15.582 1.00 19.12 C ANISOU 2316 CB PHE A 460 2205 2600 2460 367 -127 -695 C ATOM 2317 CG PHE A 460 40.337 37.154 16.772 1.00 17.14 C ANISOU 2317 CG PHE A 460 1941 2395 2175 291 -139 -687 C ATOM 2318 CD1 PHE A 460 40.205 35.802 17.060 1.00 20.13 C ANISOU 2318 CD1 PHE A 460 2315 2829 2502 228 -154 -633 C ATOM 2319 CD2 PHE A 460 41.116 37.938 17.607 1.00 16.79 C ANISOU 2319 CD2 PHE A 460 1885 2339 2155 286 -136 -734 C ATOM 2320 CE1 PHE A 460 40.843 35.247 18.171 1.00 23.44 C ANISOU 2320 CE1 PHE A 460 2725 3295 2887 163 -169 -612 C ATOM 2321 CE2 PHE A 460 41.751 37.388 18.713 1.00 20.58 C ANISOU 2321 CE2 PHE A 460 2353 2873 2592 222 -155 -726 C ATOM 2322 CZ PHE A 460 41.614 36.046 18.990 1.00 20.25 C ANISOU 2322 CZ PHE A 460 2314 2890 2492 162 -172 -658 C ATOM 2323 N LEU A 461 37.683 39.490 13.780 1.00 19.31 N ANISOU 2323 N LEU A 461 2215 2587 2533 537 -117 -746 N ATOM 2324 CA LEU A 461 37.551 40.453 12.682 1.00 16.38 C ANISOU 2324 CA LEU A 461 1868 2139 2216 628 -110 -729 C ATOM 2325 C LEU A 461 36.657 41.641 13.013 1.00 22.20 C ANISOU 2325 C LEU A 461 2554 2888 2993 680 -105 -803 C ATOM 2326 O LEU A 461 36.846 42.726 12.462 1.00 23.22 O ANISOU 2326 O LEU A 461 2696 2932 3196 750 -90 -793 O ATOM 2327 CB LEU A 461 37.005 39.774 11.432 1.00 18.17 C ANISOU 2327 CB LEU A 461 2123 2377 2403 663 -131 -678 C ATOM 2328 CG LEU A 461 37.956 38.784 10.747 1.00 18.79 C ANISOU 2328 CG LEU A 461 2256 2418 2466 632 -130 -606 C ATOM 2329 CD1 LEU A 461 37.184 37.878 9.819 1.00 24.57 C ANISOU 2329 CD1 LEU A 461 2990 3201 3144 647 -157 -590 C ATOM 2330 CD2 LEU A 461 39.036 39.551 9.982 1.00 22.44 C ANISOU 2330 CD2 LEU A 461 2774 2767 2986 680 -100 -553 C ATOM 2331 N HIS A 462 35.677 41.437 13.891 1.00 18.60 N ANISOU 2331 N HIS A 462 2038 2534 2496 648 -113 -874 N ATOM 2332 CA HIS A 462 34.642 42.450 14.108 1.00 21.73 C ANISOU 2332 CA HIS A 462 2376 2950 2931 699 -112 -953 C ATOM 2333 C HIS A 462 34.483 42.969 15.530 1.00 27.38 C ANISOU 2333 C HIS A 462 3026 3722 3653 659 -93 -1056 C ATOM 2334 O HIS A 462 33.650 43.837 15.784 1.00 26.75 O ANISOU 2334 O HIS A 462 2889 3658 3618 699 -88 -1135 O ATOM 2335 CB HIS A 462 33.293 41.927 13.610 1.00 19.95 C ANISOU 2335 CB HIS A 462 2123 2797 2662 721 -139 -962 C ATOM 2336 CG HIS A 462 33.267 41.662 12.142 1.00 20.76 C ANISOU 2336 CG HIS A 462 2278 2853 2759 781 -163 -883 C ATOM 2337 ND1 HIS A 462 33.125 42.666 11.203 1.00 23.30 N ANISOU 2337 ND1 HIS A 462 2616 3102 3136 878 -170 -856 N ATOM 2338 CD2 HIS A 462 33.346 40.504 11.441 1.00 21.08 C ANISOU 2338 CD2 HIS A 462 2352 2915 2741 760 -182 -826 C ATOM 2339 CE1 HIS A 462 33.137 42.137 9.993 1.00 26.03 C ANISOU 2339 CE1 HIS A 462 3010 3439 3443 914 -193 -784 C ATOM 2340 NE2 HIS A 462 33.271 40.827 10.108 1.00 22.21 N ANISOU 2340 NE2 HIS A 462 2535 3010 2893 844 -200 -773 N ATOM 2341 N ALA A 463 35.252 42.432 16.465 1.00 20.33 N ANISOU 2341 N ALA A 463 2138 2869 2716 583 -85 -1060 N ATOM 2342 CA ALA A 463 35.143 42.870 17.849 1.00 22.62 C ANISOU 2342 CA ALA A 463 2368 3234 2993 543 -69 -1162 C ATOM 2343 C ALA A 463 35.538 44.332 17.984 1.00 24.50 C ANISOU 2343 C ALA A 463 2579 3390 3342 595 -52 -1232 C ATOM 2344 O ALA A 463 36.439 44.801 17.297 1.00 27.01 O ANISOU 2344 O ALA A 463 2938 3587 3736 632 -47 -1182 O ATOM 2345 CB ALA A 463 36.022 42.010 18.746 1.00 25.18 C ANISOU 2345 CB ALA A 463 2709 3614 3244 458 -71 -1137 C ATOM 2346 N PRO A 464 34.850 45.060 18.874 1.00 24.65 N ANISOU 2346 N PRO A 464 2520 3470 3376 596 -37 -1353 N ATOM 2347 CA PRO A 464 35.252 46.415 19.267 1.00 27.02 C ANISOU 2347 CA PRO A 464 2776 3703 3789 631 -18 -1446 C ATOM 2348 C PRO A 464 36.657 46.337 19.837 1.00 28.64 C ANISOU 2348 C PRO A 464 3004 3884 3993 587 -16 -1444 C ATOM 2349 O PRO A 464 36.985 45.318 20.446 1.00 27.87 O ANISOU 2349 O PRO A 464 2927 3877 3783 517 -29 -1415 O ATOM 2350 CB PRO A 464 34.287 46.765 20.405 1.00 29.64 C ANISOU 2350 CB PRO A 464 3017 4156 4091 608 -4 -1586 C ATOM 2351 CG PRO A 464 33.212 45.787 20.357 1.00 35.58 C ANISOU 2351 CG PRO A 464 3766 5014 4740 580 -12 -1558 C ATOM 2352 CD PRO A 464 33.671 44.579 19.605 1.00 25.18 C ANISOU 2352 CD PRO A 464 2532 3678 3358 556 -33 -1415 C ATOM 2353 N LEU A 465 37.459 47.382 19.670 1.00 29.99 N ANISOU 2353 N LEU A 465 3167 3935 4293 627 -1 -1473 N ATOM 2354 CA LEU A 465 38.876 47.309 20.029 1.00 36.53 C ANISOU 2354 CA LEU A 465 4019 4720 5140 592 -3 -1464 C ATOM 2355 C LEU A 465 39.143 46.908 21.481 1.00 32.89 C ANISOU 2355 C LEU A 465 3520 4398 4579 518 -16 -1550 C ATOM 2356 O LEU A 465 40.081 46.162 21.761 1.00 29.53 O ANISOU 2356 O LEU A 465 3133 3990 4097 469 -35 -1499 O ATOM 2357 CB LEU A 465 39.608 48.605 19.670 1.00 42.27 C ANISOU 2357 CB LEU A 465 4727 5291 6045 648 23 -1500 C ATOM 2358 CG LEU A 465 39.671 48.851 18.161 1.00 52.67 C ANISOU 2358 CG LEU A 465 6103 6464 7444 717 38 -1376 C ATOM 2359 CD1 LEU A 465 40.780 49.830 17.810 1.00 54.94 C ANISOU 2359 CD1 LEU A 465 6389 6588 7896 752 70 -1375 C ATOM 2360 CD2 LEU A 465 39.869 47.537 17.410 1.00 58.60 C ANISOU 2360 CD2 LEU A 465 6941 7238 8085 691 18 -1238 C ATOM 2361 N GLU A 466 38.314 47.378 22.405 1.00 30.79 N ANISOU 2361 N GLU A 466 3177 4236 4287 510 -6 -1678 N ATOM 2362 CA GLU A 466 38.480 47.010 23.805 1.00 32.22 C ANISOU 2362 CA GLU A 466 3320 4571 4352 442 -16 -1759 C ATOM 2363 C GLU A 466 38.370 45.498 23.989 1.00 30.94 C ANISOU 2363 C GLU A 466 3212 4519 4027 378 -37 -1648 C ATOM 2364 O GLU A 466 39.154 44.884 24.713 1.00 28.19 O ANISOU 2364 O GLU A 466 2879 4237 3596 324 -59 -1629 O ATOM 2365 CB GLU A 466 37.427 47.722 24.655 1.00 41.61 C ANISOU 2365 CB GLU A 466 4416 5863 5531 446 6 -1914 C ATOM 2366 CG GLU A 466 37.392 47.301 26.109 1.00 57.01 C ANISOU 2366 CG GLU A 466 6326 8004 7332 376 1 -1997 C ATOM 2367 CD GLU A 466 36.345 48.070 26.908 1.00 73.33 C ANISOU 2367 CD GLU A 466 8294 10172 9396 382 32 -2165 C ATOM 2368 OE1 GLU A 466 36.282 49.312 26.776 1.00 75.33 O ANISOU 2368 OE1 GLU A 466 8486 10335 9802 435 48 -2278 O ATOM 2369 OE2 GLU A 466 35.585 47.432 27.669 1.00 77.85 O ANISOU 2369 OE2 GLU A 466 8846 10912 9822 332 44 -2183 O ATOM 2370 N LEU A 467 37.395 44.897 23.320 1.00 25.55 N ANISOU 2370 N LEU A 467 2552 3850 3308 385 -31 -1574 N ATOM 2371 CA LEU A 467 37.166 43.465 23.437 1.00 26.15 C ANISOU 2371 CA LEU A 467 2667 4017 3252 325 -44 -1472 C ATOM 2372 C LEU A 467 38.209 42.688 22.639 1.00 24.45 C ANISOU 2372 C LEU A 467 2532 3704 3053 317 -68 -1336 C ATOM 2373 O LEU A 467 38.617 41.585 23.020 1.00 26.36 O ANISOU 2373 O LEU A 467 2804 4006 3206 259 -87 -1260 O ATOM 2374 CB LEU A 467 35.771 43.141 22.915 1.00 23.82 C ANISOU 2374 CB LEU A 467 2359 3756 2937 340 -30 -1454 C ATOM 2375 CG LEU A 467 34.954 42.077 23.638 1.00 43.01 C ANISOU 2375 CG LEU A 467 4771 6339 5233 273 -20 -1435 C ATOM 2376 CD1 LEU A 467 34.935 42.340 25.136 1.00 41.07 C ANISOU 2376 CD1 LEU A 467 4468 6237 4900 227 -4 -1538 C ATOM 2377 CD2 LEU A 467 33.532 42.066 23.079 1.00 40.72 C ANISOU 2377 CD2 LEU A 467 4448 6064 4961 302 -4 -1452 C ATOM 2378 N LEU A 468 38.616 43.248 21.510 1.00 23.02 N ANISOU 2378 N LEU A 468 2384 3373 2989 378 -65 -1301 N ATOM 2379 CA LEU A 468 39.664 42.628 20.708 1.00 23.43 C ANISOU 2379 CA LEU A 468 2507 3326 3068 374 -80 -1187 C ATOM 2380 C LEU A 468 40.941 42.511 21.526 1.00 24.52 C ANISOU 2380 C LEU A 468 2648 3470 3198 331 -98 -1200 C ATOM 2381 O LEU A 468 41.652 41.509 21.449 1.00 20.59 O ANISOU 2381 O LEU A 468 2193 2967 2661 290 -120 -1110 O ATOM 2382 CB LEU A 468 39.931 43.443 19.445 1.00 23.47 C ANISOU 2382 CB LEU A 468 2542 3175 3202 449 -64 -1158 C ATOM 2383 CG LEU A 468 41.079 42.960 18.562 1.00 22.15 C ANISOU 2383 CG LEU A 468 2444 2897 3075 450 -68 -1052 C ATOM 2384 CD1 LEU A 468 40.820 41.553 18.079 1.00 18.72 C ANISOU 2384 CD1 LEU A 468 2053 2505 2554 414 -87 -952 C ATOM 2385 CD2 LEU A 468 41.269 43.903 17.395 1.00 29.70 C ANISOU 2385 CD2 LEU A 468 3424 3711 4150 527 -41 -1026 C ATOM 2386 N ALA A 469 41.237 43.540 22.310 1.00 22.39 N ANISOU 2386 N ALA A 469 2325 3211 2973 341 -92 -1319 N ATOM 2387 CA ALA A 469 42.438 43.525 23.125 1.00 23.54 C ANISOU 2387 CA ALA A 469 2462 3368 3113 307 -116 -1351 C ATOM 2388 C ALA A 469 42.371 42.399 24.145 1.00 22.90 C ANISOU 2388 C ALA A 469 2382 3445 2875 235 -146 -1318 C ATOM 2389 O ALA A 469 43.376 41.745 24.415 1.00 22.40 O ANISOU 2389 O ALA A 469 2346 3379 2787 200 -178 -1263 O ATOM 2390 CB ALA A 469 42.641 44.872 23.823 1.00 28.78 C ANISOU 2390 CB ALA A 469 3054 4026 3856 333 -105 -1508 C ATOM 2391 N GLU A 470 41.189 42.185 24.720 1.00 25.08 N ANISOU 2391 N GLU A 470 2625 3855 3050 215 -132 -1351 N ATOM 2392 CA GLU A 470 40.989 41.095 25.676 1.00 24.36 C ANISOU 2392 CA GLU A 470 2533 3918 2803 147 -150 -1304 C ATOM 2393 C GLU A 470 41.149 39.746 25.000 1.00 21.35 C ANISOU 2393 C GLU A 470 2215 3498 2398 117 -165 -1144 C ATOM 2394 O GLU A 470 41.717 38.818 25.583 1.00 23.14 O ANISOU 2394 O GLU A 470 2459 3783 2549 66 -194 -1072 O ATOM 2395 CB GLU A 470 39.606 41.172 26.333 1.00 28.65 C ANISOU 2395 CB GLU A 470 3025 4605 3255 131 -118 -1370 C ATOM 2396 CG GLU A 470 39.487 42.238 27.401 1.00 32.36 C ANISOU 2396 CG GLU A 470 3421 5168 3705 138 -107 -1536 C ATOM 2397 CD GLU A 470 38.085 42.333 27.981 1.00 48.24 C ANISOU 2397 CD GLU A 470 5377 7316 5635 123 -68 -1608 C ATOM 2398 OE1 GLU A 470 37.696 43.437 28.424 1.00 53.82 O ANISOU 2398 OE1 GLU A 470 6016 8054 6379 150 -46 -1762 O ATOM 2399 OE2 GLU A 470 37.370 41.307 27.993 1.00 46.85 O ANISOU 2399 OE2 GLU A 470 5219 7212 5369 84 -55 -1517 O ATOM 2400 N MET A 471 40.628 39.629 23.781 1.00 18.71 N ANISOU 2400 N MET A 471 1909 3071 2129 151 -147 -1092 N ATOM 2401 CA MET A 471 40.786 38.396 23.009 1.00 18.02 C ANISOU 2401 CA MET A 471 1874 2934 2038 128 -159 -957 C ATOM 2402 C MET A 471 42.242 38.100 22.696 1.00 20.81 C ANISOU 2402 C MET A 471 2270 3186 2450 122 -188 -896 C ATOM 2403 O MET A 471 42.698 36.968 22.848 1.00 18.83 O ANISOU 2403 O MET A 471 2044 2951 2162 75 -213 -802 O ATOM 2404 CB MET A 471 39.986 38.470 21.697 1.00 18.04 C ANISOU 2404 CB MET A 471 1894 2858 2101 176 -139 -933 C ATOM 2405 CG MET A 471 38.485 38.526 21.895 1.00 20.80 C ANISOU 2405 CG MET A 471 2200 3304 2400 178 -115 -980 C ATOM 2406 SD MET A 471 37.636 38.722 20.311 1.00 24.68 S ANISOU 2406 SD MET A 471 2708 3701 2967 247 -105 -960 S ATOM 2407 CE MET A 471 37.906 37.120 19.562 1.00 23.36 C ANISOU 2407 CE MET A 471 2590 3503 2782 208 -123 -828 C ATOM 2408 N MET A 472 42.975 39.109 22.238 1.00 21.52 N ANISOU 2408 N MET A 472 2366 3165 2645 170 -182 -946 N ATOM 2409 CA MET A 472 44.397 38.921 21.958 1.00 20.89 C ANISOU 2409 CA MET A 472 2319 2983 2635 165 -204 -902 C ATOM 2410 C MET A 472 45.139 38.495 23.220 1.00 19.99 C ANISOU 2410 C MET A 472 2186 2957 2452 113 -246 -909 C ATOM 2411 O MET A 472 45.968 37.577 23.186 1.00 21.84 O ANISOU 2411 O MET A 472 2447 3162 2687 80 -277 -823 O ATOM 2412 CB MET A 472 45.019 40.207 21.416 1.00 22.09 C ANISOU 2412 CB MET A 472 2468 3008 2919 222 -181 -968 C ATOM 2413 CG MET A 472 44.542 40.582 20.029 1.00 18.23 C ANISOU 2413 CG MET A 472 2010 2414 2502 279 -145 -933 C ATOM 2414 SD MET A 472 45.352 39.598 18.746 1.00 25.23 S ANISOU 2414 SD MET A 472 2968 3186 3434 274 -145 -803 S ATOM 2415 CE MET A 472 44.543 40.239 17.284 1.00 25.20 C ANISOU 2415 CE MET A 472 2991 3104 3482 350 -104 -782 C ATOM 2416 N ASP A 473 44.851 39.188 24.318 1.00 22.41 N ANISOU 2416 N ASP A 473 2441 3372 2703 110 -249 -1014 N ATOM 2417 CA ASP A 473 45.497 38.909 25.595 1.00 22.62 C ANISOU 2417 CA ASP A 473 2443 3506 2645 68 -292 -1035 C ATOM 2418 C ASP A 473 45.204 37.493 26.047 1.00 26.27 C ANISOU 2418 C ASP A 473 2925 4069 2987 10 -314 -916 C ATOM 2419 O ASP A 473 46.047 36.854 26.662 1.00 23.30 O ANISOU 2419 O ASP A 473 2555 3727 2571 -23 -361 -864 O ATOM 2420 CB ASP A 473 45.041 39.895 26.671 1.00 25.19 C ANISOU 2420 CB ASP A 473 2704 3952 2914 76 -285 -1182 C ATOM 2421 CG ASP A 473 45.605 41.291 26.462 1.00 40.30 C ANISOU 2421 CG ASP A 473 4584 5763 4964 127 -273 -1309 C ATOM 2422 OD1 ASP A 473 45.175 42.206 27.189 1.00 38.42 O ANISOU 2422 OD1 ASP A 473 4286 5603 4710 140 -260 -1446 O ATOM 2423 OD2 ASP A 473 46.465 41.473 25.569 1.00 43.40 O ANISOU 2423 OD2 ASP A 473 5007 5996 5487 153 -271 -1275 O ATOM 2424 N GLU A 474 44.003 37.005 25.742 1.00 22.77 N ANISOU 2424 N GLU A 474 2486 3669 2495 0 -281 -871 N ATOM 2425 CA GLU A 474 43.649 35.643 26.109 1.00 21.09 C ANISOU 2425 CA GLU A 474 2286 3538 2189 -57 -291 -753 C ATOM 2426 C GLU A 474 44.497 34.627 25.347 1.00 22.13 C ANISOU 2426 C GLU A 474 2463 3552 2393 -72 -319 -629 C ATOM 2427 O GLU A 474 44.937 33.635 25.914 1.00 20.04 O ANISOU 2427 O GLU A 474 2205 3332 2079 -117 -353 -537 O ATOM 2428 CB GLU A 474 42.158 35.360 25.864 1.00 23.14 C ANISOU 2428 CB GLU A 474 2532 3854 2405 -64 -245 -742 C ATOM 2429 CG GLU A 474 41.803 33.899 26.075 1.00 26.72 C ANISOU 2429 CG GLU A 474 2996 4362 2795 -123 -247 -610 C ATOM 2430 CD GLU A 474 40.300 33.637 26.120 1.00 26.51 C ANISOU 2430 CD GLU A 474 2940 4419 2715 -139 -198 -615 C ATOM 2431 OE1 GLU A 474 39.519 34.583 26.370 1.00 25.18 O ANISOU 2431 OE1 GLU A 474 2735 4311 2521 -114 -167 -728 O ATOM 2432 OE2 GLU A 474 39.910 32.470 25.930 1.00 22.31 O ANISOU 2432 OE2 GLU A 474 2413 3888 2175 -178 -190 -510 O ATOM 2433 N ILE A 475 44.713 34.858 24.055 1.00 17.28 N ANISOU 2433 N ILE A 475 1877 2791 1897 -33 -302 -625 N ATOM 2434 CA ILE A 475 45.561 33.943 23.282 1.00 19.38 C ANISOU 2434 CA ILE A 475 2181 2943 2239 -46 -323 -525 C ATOM 2435 C ILE A 475 47.024 34.030 23.743 1.00 23.34 C ANISOU 2435 C ILE A 475 2685 3403 2780 -53 -369 -527 C ATOM 2436 O ILE A 475 47.656 33.015 24.026 1.00 21.02 O ANISOU 2436 O ILE A 475 2399 3107 2481 -91 -408 -437 O ATOM 2437 CB ILE A 475 45.444 34.196 21.779 1.00 17.66 C ANISOU 2437 CB ILE A 475 1994 2593 2124 -1 -290 -526 C ATOM 2438 CG1 ILE A 475 43.988 34.009 21.336 1.00 20.40 C ANISOU 2438 CG1 ILE A 475 2333 2988 2431 7 -256 -524 C ATOM 2439 CG2 ILE A 475 46.368 33.260 20.995 1.00 15.90 C ANISOU 2439 CG2 ILE A 475 1804 2258 1981 -16 -307 -437 C ATOM 2440 CD1 ILE A 475 43.408 32.658 21.699 1.00 18.69 C ANISOU 2440 CD1 ILE A 475 2105 2845 2153 -51 -264 -437 C ATOM 2441 N PHE A 476 47.548 35.247 23.856 1.00 18.23 N ANISOU 2441 N PHE A 476 2024 2722 2181 -15 -366 -632 N ATOM 2442 CA PHE A 476 48.954 35.432 24.202 1.00 18.87 C ANISOU 2442 CA PHE A 476 2099 2750 2320 -15 -409 -652 C ATOM 2443 C PHE A 476 49.290 35.089 25.666 1.00 20.82 C ANISOU 2443 C PHE A 476 2317 3137 2457 -53 -466 -651 C ATOM 2444 O PHE A 476 50.406 34.660 25.967 1.00 23.46 O ANISOU 2444 O PHE A 476 2652 3442 2822 -68 -518 -616 O ATOM 2445 CB PHE A 476 49.399 36.877 23.881 1.00 22.72 C ANISOU 2445 CB PHE A 476 2571 3151 2910 37 -383 -772 C ATOM 2446 CG PHE A 476 49.392 37.206 22.401 1.00 19.24 C ANISOU 2446 CG PHE A 476 2166 2557 2587 77 -332 -753 C ATOM 2447 CD1 PHE A 476 50.086 36.417 21.500 1.00 18.69 C ANISOU 2447 CD1 PHE A 476 2135 2378 2589 68 -333 -664 C ATOM 2448 CD2 PHE A 476 48.715 38.315 21.925 1.00 22.73 C ANISOU 2448 CD2 PHE A 476 2600 2969 3069 126 -284 -825 C ATOM 2449 CE1 PHE A 476 50.080 36.711 20.135 1.00 19.27 C ANISOU 2449 CE1 PHE A 476 2242 2327 2752 106 -284 -645 C ATOM 2450 CE2 PHE A 476 48.715 38.621 20.569 1.00 18.07 C ANISOU 2450 CE2 PHE A 476 2045 2248 2573 167 -238 -795 C ATOM 2451 CZ PHE A 476 49.394 37.826 19.680 1.00 22.20 C ANISOU 2451 CZ PHE A 476 2610 2676 3148 157 -237 -706 C ATOM 2452 N ASP A 477 48.331 35.272 26.571 1.00 22.82 N ANISOU 2452 N ASP A 477 2543 3547 2581 -66 -457 -690 N ATOM 2453 CA ASP A 477 48.633 35.239 28.006 1.00 24.90 C ANISOU 2453 CA ASP A 477 2774 3963 2725 -90 -507 -717 C ATOM 2454 C ASP A 477 47.589 34.521 28.863 1.00 28.42 C ANISOU 2454 C ASP A 477 3211 4582 3006 -133 -498 -655 C ATOM 2455 O ASP A 477 47.770 34.383 30.068 1.00 31.61 O ANISOU 2455 O ASP A 477 3592 5131 3286 -155 -537 -659 O ATOM 2456 CB ASP A 477 48.788 36.670 28.547 1.00 26.39 C ANISOU 2456 CB ASP A 477 2916 4190 2922 -55 -504 -891 C ATOM 2457 CG ASP A 477 50.027 37.369 28.024 1.00 49.78 C ANISOU 2457 CG ASP A 477 5873 6999 6041 -21 -521 -955 C ATOM 2458 OD1 ASP A 477 51.143 36.870 28.277 1.00 58.68 O ANISOU 2458 OD1 ASP A 477 7005 8100 7193 -35 -579 -913 O ATOM 2459 OD2 ASP A 477 49.885 38.431 27.373 1.00 54.52 O ANISOU 2459 OD2 ASP A 477 6463 7505 6749 21 -474 -1047 O ATOM 2460 N GLY A 478 46.502 34.069 28.251 1.00 26.53 N ANISOU 2460 N GLY A 478 2987 4331 2762 -143 -447 -600 N ATOM 2461 CA GLY A 478 45.381 33.547 29.016 1.00 26.50 C ANISOU 2461 CA GLY A 478 2966 4486 2617 -181 -421 -559 C ATOM 2462 C GLY A 478 45.492 32.115 29.513 1.00 30.95 C ANISOU 2462 C GLY A 478 3544 5105 3110 -236 -449 -396 C ATOM 2463 O GLY A 478 44.697 31.693 30.348 1.00 33.60 O ANISOU 2463 O GLY A 478 3862 5587 3316 -271 -428 -355 O ATOM 2464 N TYR A 479 46.467 31.360 29.012 1.00 25.52 N ANISOU 2464 N TYR A 479 2883 4298 2514 -242 -491 -300 N ATOM 2465 CA TYR A 479 46.539 29.930 29.313 1.00 28.91 C ANISOU 2465 CA TYR A 479 3323 4749 2914 -292 -513 -133 C ATOM 2466 C TYR A 479 47.896 29.518 29.838 1.00 31.32 C ANISOU 2466 C TYR A 479 3633 5040 3228 -298 -594 -72 C ATOM 2467 O TYR A 479 48.922 30.056 29.424 1.00 27.67 O ANISOU 2467 O TYR A 479 3176 4474 2864 -266 -628 -136 O ATOM 2468 CB TYR A 479 46.209 29.095 28.072 1.00 26.85 C ANISOU 2468 CB TYR A 479 3081 4347 2775 -301 -482 -53 C ATOM 2469 CG TYR A 479 44.834 29.364 27.523 1.00 19.70 C ANISOU 2469 CG TYR A 479 2166 3455 1863 -294 -411 -103 C ATOM 2470 CD1 TYR A 479 43.738 28.619 27.940 1.00 22.61 C ANISOU 2470 CD1 TYR A 479 2515 3918 2156 -336 -372 -33 C ATOM 2471 CD2 TYR A 479 44.627 30.372 26.589 1.00 19.75 C ANISOU 2471 CD2 TYR A 479 2179 3380 1945 -243 -382 -218 C ATOM 2472 CE1 TYR A 479 42.473 28.873 27.440 1.00 27.80 C ANISOU 2472 CE1 TYR A 479 3157 4588 2817 -328 -311 -88 C ATOM 2473 CE2 TYR A 479 43.367 30.632 26.086 1.00 21.57 C ANISOU 2473 CE2 TYR A 479 2398 3627 2172 -231 -326 -265 C ATOM 2474 CZ TYR A 479 42.296 29.881 26.513 1.00 23.25 C ANISOU 2474 CZ TYR A 479 2587 3933 2312 -273 -293 -206 C ATOM 2475 OH TYR A 479 41.037 30.143 26.012 1.00 21.04 O ANISOU 2475 OH TYR A 479 2289 3668 2038 -260 -241 -261 O ATOM 2476 N ILE A 480 47.898 28.547 30.744 1.00 29.50 N ANISOU 2476 N ILE A 480 3398 4911 2900 -340 -623 57 N ATOM 2477 CA ILE A 480 49.153 28.045 31.298 1.00 27.40 C ANISOU 2477 CA ILE A 480 3132 4639 2638 -345 -710 133 C ATOM 2478 C ILE A 480 49.726 27.020 30.321 1.00 26.17 C ANISOU 2478 C ILE A 480 2993 4301 2649 -357 -725 243 C ATOM 2479 O ILE A 480 49.024 26.103 29.888 1.00 24.72 O ANISOU 2479 O ILE A 480 2813 4079 2500 -388 -684 343 O ATOM 2480 CB ILE A 480 48.964 27.417 32.704 1.00 46.01 C ANISOU 2480 CB ILE A 480 5478 7185 4817 -380 -740 241 C ATOM 2481 CG1 ILE A 480 48.667 28.496 33.750 1.00 50.37 C ANISOU 2481 CG1 ILE A 480 6010 7929 5202 -364 -739 110 C ATOM 2482 CG2 ILE A 480 50.215 26.659 33.125 1.00 41.29 C ANISOU 2482 CG2 ILE A 480 4883 6559 4245 -385 -835 354 C ATOM 2483 CD1 ILE A 480 47.285 29.098 33.668 1.00 59.74 C ANISOU 2483 CD1 ILE A 480 7184 9188 6326 -367 -647 20 C ATOM 2484 N PRO A 481 50.993 27.199 29.936 1.00 26.17 N ANISOU 2484 N PRO A 481 2997 4182 2764 -332 -779 212 N ATOM 2485 CA PRO A 481 51.638 26.274 28.995 1.00 25.30 C ANISOU 2485 CA PRO A 481 2896 3896 2821 -342 -794 299 C ATOM 2486 C PRO A 481 51.713 24.859 29.559 1.00 29.49 C ANISOU 2486 C PRO A 481 3418 4452 3334 -385 -832 482 C ATOM 2487 O PRO A 481 51.629 24.679 30.776 1.00 27.44 O ANISOU 2487 O PRO A 481 3149 4346 2931 -400 -868 545 O ATOM 2488 CB PRO A 481 53.061 26.845 28.856 1.00 22.00 C ANISOU 2488 CB PRO A 481 2473 3389 2497 -309 -853 222 C ATOM 2489 CG PRO A 481 52.973 28.254 29.339 1.00 31.38 C ANISOU 2489 CG PRO A 481 3652 4669 3602 -275 -846 65 C ATOM 2490 CD PRO A 481 51.919 28.244 30.405 1.00 26.65 C ANISOU 2490 CD PRO A 481 3045 4271 2812 -295 -830 88 C ATOM 2491 N HIS A 482 51.877 23.867 28.689 1.00 26.50 N ANISOU 2491 N HIS A 482 3038 3926 3103 -404 -824 568 N ATOM 2492 CA HIS A 482 51.995 22.484 29.147 1.00 28.01 C ANISOU 2492 CA HIS A 482 3214 4114 3314 -445 -859 748 C ATOM 2493 C HIS A 482 53.107 22.335 30.168 1.00 27.81 C ANISOU 2493 C HIS A 482 3178 4142 3244 -438 -958 807 C ATOM 2494 O HIS A 482 54.209 22.821 29.959 1.00 27.21 O ANISOU 2494 O HIS A 482 3100 3993 3244 -408 -1009 731 O ATOM 2495 CB HIS A 482 52.240 21.524 27.975 1.00 33.35 C ANISOU 2495 CB HIS A 482 3880 4600 4190 -461 -843 801 C ATOM 2496 CG HIS A 482 52.182 20.082 28.368 1.00 36.85 C ANISOU 2496 CG HIS A 482 4299 5026 4677 -505 -865 985 C ATOM 2497 ND1 HIS A 482 51.038 19.319 28.234 1.00 46.40 N ANISOU 2497 ND1 HIS A 482 5494 6248 5888 -543 -802 1063 N ATOM 2498 CD2 HIS A 482 53.112 19.268 28.919 1.00 38.66 C ANISOU 2498 CD2 HIS A 482 4510 5223 4957 -516 -944 1109 C ATOM 2499 CE1 HIS A 482 51.275 18.096 28.668 1.00 45.87 C ANISOU 2499 CE1 HIS A 482 5400 6149 5879 -577 -835 1231 C ATOM 2500 NE2 HIS A 482 52.526 18.036 29.091 1.00 49.38 N ANISOU 2500 NE2 HIS A 482 5842 6567 6351 -560 -923 1267 N ATOM 2501 N PRO A 483 52.815 21.651 31.284 1.00 26.88 N ANISOU 2501 N PRO A 483 3052 4156 3005 -466 -985 949 N ATOM 2502 CA PRO A 483 53.748 21.536 32.406 1.00 28.42 C ANISOU 2502 CA PRO A 483 3238 4442 3119 -455 -1086 1014 C ATOM 2503 C PRO A 483 55.052 20.835 32.033 1.00 33.28 C ANISOU 2503 C PRO A 483 3836 4896 3912 -448 -1165 1077 C ATOM 2504 O PRO A 483 56.078 21.094 32.662 1.00 33.28 O ANISOU 2504 O PRO A 483 3826 4933 3886 -422 -1257 1063 O ATOM 2505 CB PRO A 483 52.980 20.667 33.413 1.00 34.56 C ANISOU 2505 CB PRO A 483 4012 5362 3758 -495 -1077 1192 C ATOM 2506 CG PRO A 483 51.553 20.784 33.035 1.00 38.21 C ANISOU 2506 CG PRO A 483 4481 5858 4180 -519 -964 1161 C ATOM 2507 CD PRO A 483 51.530 20.978 31.550 1.00 31.22 C ANISOU 2507 CD PRO A 483 3599 4784 3481 -508 -917 1054 C ATOM 2508 N ASP A 484 55.008 19.954 31.038 1.00 29.86 N ANISOU 2508 N ASP A 484 3394 4291 3661 -471 -1132 1139 N ATOM 2509 CA ASP A 484 56.192 19.191 30.650 1.00 31.84 C ANISOU 2509 CA ASP A 484 3620 4380 4097 -468 -1200 1201 C ATOM 2510 C ASP A 484 56.906 19.808 29.451 1.00 25.50 C ANISOU 2510 C ASP A 484 2819 3415 3455 -441 -1184 1044 C ATOM 2511 O ASP A 484 58.119 19.973 29.468 1.00 32.61 O ANISOU 2511 O ASP A 484 3704 4249 4438 -417 -1255 1007 O ATOM 2512 CB ASP A 484 55.824 17.741 30.328 1.00 41.45 C ANISOU 2512 CB ASP A 484 4813 5498 5437 -511 -1178 1368 C ATOM 2513 CG ASP A 484 55.203 17.015 31.508 1.00 52.02 C ANISOU 2513 CG ASP A 484 6147 6980 6638 -541 -1190 1551 C ATOM 2514 OD1 ASP A 484 55.564 17.323 32.668 1.00 54.49 O ANISOU 2514 OD1 ASP A 484 6467 7444 6791 -524 -1259 1590 O ATOM 2515 OD2 ASP A 484 54.355 16.129 31.266 1.00 53.04 O ANISOU 2515 OD2 ASP A 484 6261 7071 6820 -581 -1129 1655 O ATOM 2516 N THR A 485 56.153 20.140 28.411 1.00 28.12 N ANISOU 2516 N THR A 485 3166 3686 3830 -444 -1090 955 N ATOM 2517 CA THR A 485 56.771 20.555 27.150 1.00 29.35 C ANISOU 2517 CA THR A 485 3325 3679 4147 -422 -1063 831 C ATOM 2518 C THR A 485 56.910 22.064 26.996 1.00 30.84 C ANISOU 2518 C THR A 485 3538 3905 4276 -382 -1040 658 C ATOM 2519 O THR A 485 57.703 22.528 26.189 1.00 26.43 O ANISOU 2519 O THR A 485 2979 3223 3839 -359 -1033 562 O ATOM 2520 CB THR A 485 55.979 20.042 25.944 1.00 28.56 C ANISOU 2520 CB THR A 485 3227 3478 4145 -443 -977 827 C ATOM 2521 OG1 THR A 485 54.685 20.651 25.952 1.00 24.16 O ANISOU 2521 OG1 THR A 485 2694 3031 3454 -442 -906 777 O ATOM 2522 CG2 THR A 485 55.812 18.521 26.020 1.00 37.47 C ANISOU 2522 CG2 THR A 485 4321 4551 5365 -486 -991 989 C ATOM 2523 N GLY A 486 56.130 22.828 27.751 1.00 27.83 N ANISOU 2523 N GLY A 486 3172 3688 3715 -373 -1023 617 N ATOM 2524 CA GLY A 486 56.137 24.270 27.591 1.00 23.42 C ANISOU 2524 CA GLY A 486 2628 3159 3112 -335 -994 450 C ATOM 2525 C GLY A 486 55.347 24.753 26.379 1.00 22.87 C ANISOU 2525 C GLY A 486 2583 3018 3091 -325 -896 367 C ATOM 2526 O GLY A 486 55.339 25.940 26.065 1.00 21.03 O ANISOU 2526 O GLY A 486 2360 2780 2848 -291 -862 235 O ATOM 2527 N LYS A 487 54.664 23.846 25.686 1.00 21.66 N ANISOU 2527 N LYS A 487 2431 2807 2990 -352 -851 442 N ATOM 2528 CA LYS A 487 53.841 24.287 24.557 1.00 22.84 C ANISOU 2528 CA LYS A 487 2602 2909 3168 -338 -765 364 C ATOM 2529 C LYS A 487 52.706 25.173 25.061 1.00 25.68 C ANISOU 2529 C LYS A 487 2973 3414 3371 -326 -725 302 C ATOM 2530 O LYS A 487 52.055 24.829 26.035 1.00 26.55 O ANISOU 2530 O LYS A 487 3073 3655 3360 -351 -735 369 O ATOM 2531 CB LYS A 487 53.285 23.084 23.792 1.00 26.64 C ANISOU 2531 CB LYS A 487 3074 3315 3734 -370 -732 448 C ATOM 2532 CG LYS A 487 54.372 22.230 23.145 1.00 45.57 C ANISOU 2532 CG LYS A 487 5453 5554 6306 -381 -762 490 C ATOM 2533 CD LYS A 487 53.791 21.032 22.407 1.00 56.94 C ANISOU 2533 CD LYS A 487 6872 6922 7839 -413 -729 558 C ATOM 2534 CE LYS A 487 52.600 21.431 21.569 1.00 63.57 C ANISOU 2534 CE LYS A 487 7730 7785 8639 -401 -651 485 C ATOM 2535 NZ LYS A 487 52.891 22.668 20.798 1.00 74.02 N ANISOU 2535 NZ LYS A 487 9087 9072 9963 -352 -618 355 N ATOM 2536 N ASP A 488 52.485 26.325 24.428 1.00 18.57 N ANISOU 2536 N ASP A 488 1986 2508 2561 -370 -420 354 N ATOM 2537 CA ASP A 488 51.412 27.223 24.866 1.00 20.27 C ANISOU 2537 CA ASP A 488 2200 2820 2683 -408 -382 328 C ATOM 2538 C ASP A 488 50.245 27.298 23.878 1.00 23.61 C ANISOU 2538 C ASP A 488 2644 3230 3098 -391 -346 273 C ATOM 2539 O ASP A 488 50.208 26.574 22.877 1.00 20.93 O ANISOU 2539 O ASP A 488 2321 2808 2821 -356 -351 261 O ATOM 2540 CB ASP A 488 51.946 28.628 25.197 1.00 21.31 C ANISOU 2540 CB ASP A 488 2316 3010 2773 -392 -348 278 C ATOM 2541 CG ASP A 488 52.574 29.321 23.999 1.00 26.77 C ANISOU 2541 CG ASP A 488 3021 3643 3508 -330 -304 213 C ATOM 2542 OD1 ASP A 488 52.292 28.913 22.847 1.00 23.52 O ANISOU 2542 OD1 ASP A 488 2633 3170 3131 -295 -287 189 O ATOM 2543 OD2 ASP A 488 53.349 30.282 24.212 1.00 23.95 O ANISOU 2543 OD2 ASP A 488 2650 3305 3145 -321 -287 185 O ATOM 2544 N ALA A 489 49.287 28.171 24.156 1.00 20.79 N ANISOU 2544 N ALA A 489 2280 2957 2664 -409 -315 229 N ATOM 2545 CA ALA A 489 48.083 28.219 23.332 1.00 22.34 C ANISOU 2545 CA ALA A 489 2491 3152 2848 -393 -292 173 C ATOM 2546 C ALA A 489 48.432 28.549 21.891 1.00 21.28 C ANISOU 2546 C ALA A 489 2391 2937 2759 -314 -264 115 C ATOM 2547 O ALA A 489 47.887 27.965 20.960 1.00 17.13 O ANISOU 2547 O ALA A 489 1881 2363 2263 -288 -264 91 O ATOM 2548 CB ALA A 489 47.103 29.225 23.882 1.00 20.35 C ANISOU 2548 CB ALA A 489 2217 3007 2508 -411 -271 115 C ATOM 2549 N LEU A 490 49.345 29.490 21.703 1.00 21.62 N ANISOU 2549 N LEU A 490 2442 2970 2802 -281 -241 93 N ATOM 2550 CA LEU A 490 49.726 29.889 20.360 1.00 22.24 C ANISOU 2550 CA LEU A 490 2554 2989 2907 -219 -209 48 C ATOM 2551 C LEU A 490 50.390 28.717 19.623 1.00 24.51 C ANISOU 2551 C LEU A 490 2840 3206 3268 -192 -221 67 C ATOM 2552 O LEU A 490 50.109 28.490 18.452 1.00 24.49 O ANISOU 2552 O LEU A 490 2860 3166 3280 -146 -205 28 O ATOM 2553 CB LEU A 490 50.622 31.126 20.422 1.00 24.18 C ANISOU 2553 CB LEU A 490 2805 3241 3141 -209 -184 33 C ATOM 2554 CG LEU A 490 50.975 31.884 19.153 1.00 28.39 C ANISOU 2554 CG LEU A 490 3379 3731 3677 -165 -144 -3 C ATOM 2555 CD1 LEU A 490 49.706 32.336 18.415 1.00 28.56 C ANISOU 2555 CD1 LEU A 490 3445 3752 3656 -132 -140 -52 C ATOM 2556 CD2 LEU A 490 51.853 33.078 19.533 1.00 22.29 C ANISOU 2556 CD2 LEU A 490 2605 2966 2900 -181 -129 -4 C ATOM 2557 N ASP A 491 51.230 27.948 20.316 1.00 20.18 N ANISOU 2557 N ASP A 491 2262 2640 2765 -214 -256 120 N ATOM 2558 CA ASP A 491 51.797 26.725 19.747 1.00 19.66 C ANISOU 2558 CA ASP A 491 2187 2503 2780 -183 -288 129 C ATOM 2559 C ASP A 491 50.723 25.733 19.298 1.00 24.90 C ANISOU 2559 C ASP A 491 2863 3129 3468 -183 -316 123 C ATOM 2560 O ASP A 491 50.798 25.164 18.204 1.00 25.17 O ANISOU 2560 O ASP A 491 2903 3110 3550 -130 -318 79 O ATOM 2561 CB ASP A 491 52.690 26.005 20.758 1.00 20.99 C ANISOU 2561 CB ASP A 491 2326 2654 2994 -209 -345 192 C ATOM 2562 CG ASP A 491 54.015 26.705 20.994 1.00 31.90 C ANISOU 2562 CG ASP A 491 3682 4057 4382 -195 -327 183 C ATOM 2563 OD1 ASP A 491 54.683 27.099 20.017 1.00 29.48 O ANISOU 2563 OD1 ASP A 491 3370 3739 4094 -150 -284 129 O ATOM 2564 OD2 ASP A 491 54.402 26.826 22.177 1.00 28.10 O ANISOU 2564 OD2 ASP A 491 3182 3610 3885 -232 -358 229 O ATOM 2565 N ILE A 492 49.745 25.495 20.163 1.00 19.64 N ANISOU 2565 N ILE A 492 2195 2497 2769 -246 -339 165 N ATOM 2566 CA ILE A 492 48.675 24.553 19.840 1.00 17.15 C ANISOU 2566 CA ILE A 492 1885 2149 2481 -264 -367 163 C ATOM 2567 C ILE A 492 47.919 25.025 18.607 1.00 21.04 C ANISOU 2567 C ILE A 492 2397 2644 2951 -208 -326 75 C ATOM 2568 O ILE A 492 47.726 24.274 17.655 1.00 21.51 O ANISOU 2568 O ILE A 492 2463 2645 3066 -167 -343 37 O ATOM 2569 CB ILE A 492 47.691 24.411 21.012 1.00 15.81 C ANISOU 2569 CB ILE A 492 1702 2045 2259 -356 -382 219 C ATOM 2570 CG1 ILE A 492 48.375 23.671 22.163 1.00 23.10 C ANISOU 2570 CG1 ILE A 492 2616 2954 3208 -414 -439 323 C ATOM 2571 CG2 ILE A 492 46.465 23.632 20.583 1.00 20.74 C ANISOU 2571 CG2 ILE A 492 2325 2648 2906 -381 -399 203 C ATOM 2572 CD1 ILE A 492 47.513 23.572 23.407 1.00 35.45 C ANISOU 2572 CD1 ILE A 492 4163 4606 4699 -518 -449 391 C ATOM 2573 N MET A 493 47.506 26.280 18.622 1.00 17.97 N ANISOU 2573 N MET A 493 2020 2324 2485 -202 -281 37 N ATOM 2574 CA MET A 493 46.639 26.805 17.571 1.00 20.98 C ANISOU 2574 CA MET A 493 2425 2713 2833 -151 -254 -41 C ATOM 2575 C MET A 493 47.335 26.873 16.219 1.00 20.42 C ANISOU 2575 C MET A 493 2380 2592 2785 -73 -232 -84 C ATOM 2576 O MET A 493 46.736 26.555 15.196 1.00 18.19 O ANISOU 2576 O MET A 493 2112 2289 2509 -28 -234 -139 O ATOM 2577 CB MET A 493 46.121 28.182 17.975 1.00 18.15 C ANISOU 2577 CB MET A 493 2075 2428 2393 -157 -227 -72 C ATOM 2578 CG MET A 493 45.116 28.119 19.124 1.00 17.90 C ANISOU 2578 CG MET A 493 2006 2473 2320 -226 -242 -60 C ATOM 2579 SD MET A 493 44.813 29.766 19.758 1.00 24.37 S ANISOU 2579 SD MET A 493 2823 3379 3056 -221 -224 -109 S ATOM 2580 CE MET A 493 43.865 30.529 18.428 1.00 19.65 C ANISOU 2580 CE MET A 493 2267 2764 2435 -138 -217 -210 C ATOM 2581 N MET A 494 48.600 27.286 16.215 1.00 17.78 N ANISOU 2581 N MET A 494 2046 2251 2459 -61 -211 -64 N ATOM 2582 CA MET A 494 49.351 27.421 14.971 1.00 18.53 C ANISOU 2582 CA MET A 494 2156 2323 2561 1 -179 -103 C ATOM 2583 C MET A 494 49.415 26.138 14.175 1.00 21.27 C ANISOU 2583 C MET A 494 2486 2621 2973 44 -208 -137 C ATOM 2584 O MET A 494 49.417 26.160 12.949 1.00 24.90 O ANISOU 2584 O MET A 494 2961 3081 3418 102 -185 -194 O ATOM 2585 CB MET A 494 50.790 27.894 15.239 1.00 17.57 C ANISOU 2585 CB MET A 494 2018 2209 2450 -8 -154 -75 C ATOM 2586 CG MET A 494 50.911 29.358 15.501 1.00 26.82 C ANISOU 2586 CG MET A 494 3215 3416 3559 -29 -117 -66 C ATOM 2587 SD MET A 494 52.646 29.819 15.488 1.00 24.33 S ANISOU 2587 SD MET A 494 2872 3107 3265 -38 -80 -48 S ATOM 2588 CE MET A 494 53.390 28.556 16.497 1.00 30.93 C ANISOU 2588 CE MET A 494 3645 3924 4182 -55 -134 -15 C ATOM 2589 N PHE A 495 49.493 25.014 14.870 1.00 18.48 N ANISOU 2589 N PHE A 495 2102 2227 2692 14 -263 -102 N ATOM 2590 CA PHE A 495 49.626 23.736 14.192 1.00 22.53 C ANISOU 2590 CA PHE A 495 2596 2677 3288 57 -308 -139 C ATOM 2591 C PHE A 495 48.352 22.903 14.216 1.00 25.25 C ANISOU 2591 C PHE A 495 2943 2987 3665 36 -355 -147 C ATOM 2592 O PHE A 495 48.350 21.759 13.766 1.00 25.17 O ANISOU 2592 O PHE A 495 2916 2909 3737 64 -408 -177 O ATOM 2593 CB PHE A 495 50.797 22.965 14.794 1.00 22.65 C ANISOU 2593 CB PHE A 495 2576 2647 3384 52 -355 -102 C ATOM 2594 CG PHE A 495 52.115 23.627 14.550 1.00 17.15 C ANISOU 2594 CG PHE A 495 1860 1986 2670 82 -309 -119 C ATOM 2595 CD1 PHE A 495 52.784 23.437 13.345 1.00 24.04 C ANISOU 2595 CD1 PHE A 495 2712 2865 3558 154 -286 -198 C ATOM 2596 CD2 PHE A 495 52.685 24.445 15.514 1.00 18.20 C ANISOU 2596 CD2 PHE A 495 1989 2157 2767 35 -288 -62 C ATOM 2597 CE1 PHE A 495 54.010 24.061 13.107 1.00 20.57 C ANISOU 2597 CE1 PHE A 495 2246 2474 3098 169 -236 -214 C ATOM 2598 CE2 PHE A 495 53.909 25.055 15.287 1.00 20.81 C ANISOU 2598 CE2 PHE A 495 2296 2522 3090 53 -245 -80 C ATOM 2599 CZ PHE A 495 54.564 24.872 14.079 1.00 21.68 C ANISOU 2599 CZ PHE A 495 2382 2642 3212 115 -215 -153 C ATOM 2600 N HIS A 496 47.263 23.475 14.720 1.00 16.24 N ANISOU 2600 N HIS A 496 1816 1892 2462 -13 -339 -130 N ATOM 2601 CA HIS A 496 45.994 22.731 14.768 1.00 16.18 C ANISOU 2601 CA HIS A 496 1800 1866 2481 -46 -377 -142 C ATOM 2602 C HIS A 496 45.240 22.806 13.448 1.00 17.16 C ANISOU 2602 C HIS A 496 1938 1994 2589 24 -364 -241 C ATOM 2603 O HIS A 496 45.288 23.832 12.777 1.00 16.85 O ANISOU 2603 O HIS A 496 1926 2001 2476 75 -316 -283 O ATOM 2604 CB HIS A 496 45.086 23.276 15.875 1.00 15.54 C ANISOU 2604 CB HIS A 496 1713 1856 2336 -129 -364 -98 C ATOM 2605 CG HIS A 496 43.901 22.403 16.157 1.00 17.07 C ANISOU 2605 CG HIS A 496 1884 2039 2562 -191 -402 -93 C ATOM 2606 ND1 HIS A 496 42.675 22.588 15.561 1.00 17.49 N ANISOU 2606 ND1 HIS A 496 1933 2127 2588 -175 -391 -169 N ATOM 2607 CD2 HIS A 496 43.771 21.320 16.966 1.00 17.88 C ANISOU 2607 CD2 HIS A 496 1969 2100 2725 -275 -454 -15 C ATOM 2608 CE1 HIS A 496 41.828 21.668 16.001 1.00 20.63 C ANISOU 2608 CE1 HIS A 496 2300 2510 3027 -252 -427 -146 C ATOM 2609 NE2 HIS A 496 42.475 20.885 16.840 1.00 18.26 N ANISOU 2609 NE2 HIS A 496 1997 2160 2781 -317 -466 -46 N ATOM 2610 N GLN A 497 44.519 21.734 13.102 1.00 16.48 N ANISOU 2610 N GLN A 497 1834 1856 2571 22 -414 -275 N ATOM 2611 CA GLN A 497 43.826 21.641 11.812 1.00 16.23 C ANISOU 2611 CA GLN A 497 1809 1824 2533 96 -415 -379 C ATOM 2612 C GLN A 497 42.792 22.749 11.602 1.00 18.81 C ANISOU 2612 C GLN A 497 2156 2230 2760 106 -375 -421 C ATOM 2613 O GLN A 497 42.493 23.126 10.456 1.00 16.69 O ANISOU 2613 O GLN A 497 1910 1982 2450 187 -362 -501 O ATOM 2614 CB GLN A 497 43.174 20.264 11.628 1.00 17.30 C ANISOU 2614 CB GLN A 497 1916 1885 2773 79 -484 -408 C ATOM 2615 CG GLN A 497 42.014 20.001 12.566 1.00 19.72 C ANISOU 2615 CG GLN A 497 2201 2205 3086 -26 -503 -365 C ATOM 2616 CD GLN A 497 41.424 18.610 12.404 1.00 34.43 C ANISOU 2616 CD GLN A 497 4036 3980 5065 -58 -577 -383 C ATOM 2617 OE1 GLN A 497 41.241 18.125 11.288 1.00 30.26 O ANISOU 2617 OE1 GLN A 497 3502 3411 4584 19 -605 -481 O ATOM 2618 NE2 GLN A 497 41.111 17.968 13.523 1.00 33.33 N ANISOU 2618 NE2 GLN A 497 3881 3813 4971 -176 -611 -288 N ATOM 2619 N PHE A 498 42.229 23.263 12.694 1.00 15.63 N ANISOU 2619 N PHE A 498 1744 1880 2316 31 -363 -373 N ATOM 2620 CA PHE A 498 41.290 24.375 12.575 1.00 15.29 C ANISOU 2620 CA PHE A 498 1714 1912 2184 49 -336 -424 C ATOM 2621 C PHE A 498 41.860 25.644 13.189 1.00 15.23 C ANISOU 2621 C PHE A 498 1731 1953 2104 40 -296 -381 C ATOM 2622 O PHE A 498 41.628 26.760 12.709 1.00 15.27 O ANISOU 2622 O PHE A 498 1772 1991 2040 93 -277 -424 O ATOM 2623 CB PHE A 498 39.938 24.033 13.217 1.00 16.52 C ANISOU 2623 CB PHE A 498 1824 2109 2344 -21 -356 -441 C ATOM 2624 CG PHE A 498 39.348 22.743 12.733 1.00 17.94 C ANISOU 2624 CG PHE A 498 1974 2232 2608 -31 -401 -478 C ATOM 2625 CD1 PHE A 498 39.265 22.469 11.374 1.00 20.97 C ANISOU 2625 CD1 PHE A 498 2375 2578 3015 65 -418 -565 C ATOM 2626 CD2 PHE A 498 38.861 21.807 13.631 1.00 17.14 C ANISOU 2626 CD2 PHE A 498 1829 2121 2564 -140 -429 -424 C ATOM 2627 CE1 PHE A 498 38.728 21.269 10.914 1.00 23.41 C ANISOU 2627 CE1 PHE A 498 2653 2829 3413 59 -468 -612 C ATOM 2628 CE2 PHE A 498 38.311 20.607 13.179 1.00 17.54 C ANISOU 2628 CE2 PHE A 498 1853 2104 2707 -156 -479 -457 C ATOM 2629 CZ PHE A 498 38.251 20.342 11.809 1.00 22.45 C ANISOU 2629 CZ PHE A 498 2488 2680 3362 -52 -501 -558 C ATOM 2630 N GLY A 499 42.599 25.474 14.279 1.00 15.40 N ANISOU 2630 N GLY A 499 1734 1972 2145 -27 -294 -296 N ATOM 2631 CA GLY A 499 43.163 26.617 14.971 1.00 17.62 C ANISOU 2631 CA GLY A 499 2030 2298 2368 -41 -263 -260 C ATOM 2632 C GLY A 499 44.088 27.455 14.116 1.00 18.78 C ANISOU 2632 C GLY A 499 2223 2424 2487 28 -232 -273 C ATOM 2633 O GLY A 499 44.189 28.662 14.323 1.00 17.19 O ANISOU 2633 O GLY A 499 2047 2255 2230 35 -211 -274 O ATOM 2634 N ASN A 500 44.767 26.831 13.154 1.00 14.51 N ANISOU 2634 N ASN A 500 1692 1834 1987 75 -231 -285 N ATOM 2635 CA ASN A 500 45.732 27.559 12.341 1.00 14.89 C ANISOU 2635 CA ASN A 500 1778 1879 2003 125 -193 -289 C ATOM 2636 C ASN A 500 45.090 28.741 11.593 1.00 16.27 C ANISOU 2636 C ASN A 500 2007 2080 2096 173 -177 -333 C ATOM 2637 O ASN A 500 45.718 29.778 11.385 1.00 14.78 O ANISOU 2637 O ASN A 500 1857 1898 1862 181 -147 -311 O ATOM 2638 CB ASN A 500 46.457 26.615 11.373 1.00 16.83 C ANISOU 2638 CB ASN A 500 2010 2087 2296 173 -194 -315 C ATOM 2639 CG ASN A 500 45.616 26.266 10.141 1.00 17.41 C ANISOU 2639 CG ASN A 500 2101 2160 2356 240 -208 -397 C ATOM 2640 OD1 ASN A 500 45.644 26.979 9.148 1.00 16.82 O ANISOU 2640 OD1 ASN A 500 2068 2110 2212 293 -180 -428 O ATOM 2641 ND2 ASN A 500 44.890 25.150 10.200 1.00 16.92 N ANISOU 2641 ND2 ASN A 500 2005 2065 2358 235 -255 -427 N ATOM 2642 N TYR A 501 43.823 28.589 11.219 1.00 14.27 N ANISOU 2642 N TYR A 501 1757 1838 1827 201 -204 -394 N ATOM 2643 CA TYR A 501 43.126 29.645 10.506 1.00 14.76 C ANISOU 2643 CA TYR A 501 1874 1919 1817 256 -208 -440 C ATOM 2644 C TYR A 501 42.827 30.821 11.427 1.00 14.78 C ANISOU 2644 C TYR A 501 1887 1946 1782 227 -213 -427 C ATOM 2645 O TYR A 501 42.714 31.968 10.976 1.00 15.35 O ANISOU 2645 O TYR A 501 2017 2015 1800 266 -217 -440 O ATOM 2646 CB TYR A 501 41.820 29.139 9.916 1.00 15.06 C ANISOU 2646 CB TYR A 501 1902 1966 1854 298 -245 -523 C ATOM 2647 CG TYR A 501 42.002 28.096 8.843 1.00 14.72 C ANISOU 2647 CG TYR A 501 1853 1899 1843 345 -250 -559 C ATOM 2648 CD1 TYR A 501 42.317 28.466 7.539 1.00 19.06 C ANISOU 2648 CD1 TYR A 501 2455 2452 2335 419 -236 -585 C ATOM 2649 CD2 TYR A 501 41.872 26.744 9.136 1.00 15.67 C ANISOU 2649 CD2 TYR A 501 1913 1992 2047 314 -273 -568 C ATOM 2650 CE1 TYR A 501 42.480 27.512 6.542 1.00 17.68 C ANISOU 2650 CE1 TYR A 501 2265 2269 2182 469 -242 -636 C ATOM 2651 CE2 TYR A 501 42.033 25.782 8.138 1.00 16.54 C ANISOU 2651 CE2 TYR A 501 2013 2076 2197 366 -289 -619 C ATOM 2652 CZ TYR A 501 42.330 26.184 6.849 1.00 18.82 C ANISOU 2652 CZ TYR A 501 2346 2383 2422 447 -272 -660 C ATOM 2653 OH TYR A 501 42.489 25.244 5.862 1.00 18.14 O ANISOU 2653 OH TYR A 501 2240 2285 2366 505 -288 -725 O ATOM 2654 N VAL A 502 42.668 30.542 12.718 1.00 15.29 N ANISOU 2654 N VAL A 502 1896 2039 1874 159 -219 -404 N ATOM 2655 CA VAL A 502 42.380 31.623 13.653 1.00 13.80 C ANISOU 2655 CA VAL A 502 1704 1889 1649 136 -227 -409 C ATOM 2656 C VAL A 502 43.629 32.464 13.834 1.00 15.97 C ANISOU 2656 C VAL A 502 2012 2138 1917 123 -202 -351 C ATOM 2657 O VAL A 502 43.559 33.687 13.849 1.00 16.19 O ANISOU 2657 O VAL A 502 2080 2162 1911 143 -213 -366 O ATOM 2658 CB VAL A 502 41.898 31.091 15.013 1.00 16.10 C ANISOU 2658 CB VAL A 502 1921 2239 1956 60 -236 -399 C ATOM 2659 CG1 VAL A 502 41.860 32.207 16.040 1.00 17.63 C ANISOU 2659 CG1 VAL A 502 2103 2484 2111 38 -242 -407 C ATOM 2660 CG2 VAL A 502 40.501 30.452 14.866 1.00 18.34 C ANISOU 2660 CG2 VAL A 502 2167 2561 2241 62 -260 -467 C ATOM 2661 N VAL A 503 44.770 31.806 14.004 1.00 14.00 N ANISOU 2661 N VAL A 503 1743 1868 1709 88 -175 -289 N ATOM 2662 CA VAL A 503 46.039 32.532 14.108 1.00 13.86 C ANISOU 2662 CA VAL A 503 1746 1830 1691 72 -147 -239 C ATOM 2663 C VAL A 503 46.314 33.343 12.834 1.00 13.94 C ANISOU 2663 C VAL A 503 1828 1806 1662 120 -130 -245 C ATOM 2664 O VAL A 503 46.814 34.462 12.911 1.00 15.38 O ANISOU 2664 O VAL A 503 2046 1972 1825 109 -122 -221 O ATOM 2665 CB VAL A 503 47.219 31.601 14.394 1.00 14.13 C ANISOU 2665 CB VAL A 503 1738 1851 1779 38 -127 -186 C ATOM 2666 CG1 VAL A 503 48.504 32.440 14.610 1.00 19.51 C ANISOU 2666 CG1 VAL A 503 2428 2523 2461 13 -98 -144 C ATOM 2667 CG2 VAL A 503 46.921 30.745 15.615 1.00 18.19 C ANISOU 2667 CG2 VAL A 503 2194 2391 2326 -15 -154 -163 C ATOM 2668 N GLN A 504 45.986 32.794 11.664 1.00 15.45 N ANISOU 2668 N GLN A 504 2042 1989 1840 171 -126 -274 N ATOM 2669 CA GLN A 504 46.176 33.542 10.405 1.00 14.49 C ANISOU 2669 CA GLN A 504 1994 1849 1661 215 -111 -272 C ATOM 2670 C GLN A 504 45.320 34.807 10.421 1.00 17.82 C ANISOU 2670 C GLN A 504 2477 2256 2039 240 -152 -295 C ATOM 2671 O GLN A 504 45.744 35.873 9.981 1.00 17.92 O ANISOU 2671 O GLN A 504 2554 2237 2016 241 -148 -261 O ATOM 2672 CB GLN A 504 45.813 32.684 9.174 1.00 15.18 C ANISOU 2672 CB GLN A 504 2090 1945 1732 274 -110 -315 C ATOM 2673 CG GLN A 504 46.810 31.568 8.881 1.00 27.07 C ANISOU 2673 CG GLN A 504 3546 3460 3280 266 -75 -305 C ATOM 2674 CD GLN A 504 46.400 30.709 7.679 1.00 26.25 C ANISOU 2674 CD GLN A 504 3442 3368 3162 332 -82 -366 C ATOM 2675 OE1 GLN A 504 46.486 31.145 6.539 1.00 31.75 O ANISOU 2675 OE1 GLN A 504 4191 4084 3789 374 -64 -376 O ATOM 2676 NE2 GLN A 504 45.944 29.493 7.942 1.00 16.17 N ANISOU 2676 NE2 GLN A 504 2110 2082 1952 339 -113 -407 N ATOM 2677 N CYS A 505 44.101 34.662 10.919 1.00 19.49 N ANISOU 2677 N CYS A 505 2661 2488 2255 259 -197 -357 N ATOM 2678 CA CYS A 505 43.171 35.771 11.037 1.00 18.93 C ANISOU 2678 CA CYS A 505 2631 2409 2152 296 -251 -403 C ATOM 2679 C CYS A 505 43.770 36.858 11.941 1.00 16.41 C ANISOU 2679 C CYS A 505 2320 2071 1845 254 -257 -371 C ATOM 2680 O CYS A 505 43.782 38.043 11.585 1.00 17.16 O ANISOU 2680 O CYS A 505 2486 2117 1916 277 -288 -365 O ATOM 2681 CB CYS A 505 41.851 35.246 11.605 1.00 22.41 C ANISOU 2681 CB CYS A 505 3010 2901 2603 309 -287 -485 C ATOM 2682 SG CYS A 505 40.571 36.489 11.806 1.00 24.45 S ANISOU 2682 SG CYS A 505 3293 3168 2830 369 -365 -578 S ATOM 2683 N MET A 506 44.273 36.449 13.102 1.00 15.05 N ANISOU 2683 N MET A 506 2076 1932 1711 191 -234 -349 N ATOM 2684 CA MET A 506 44.909 37.382 14.044 1.00 15.17 C ANISOU 2684 CA MET A 506 2085 1938 1742 150 -240 -326 C ATOM 2685 C MET A 506 46.025 38.158 13.363 1.00 17.62 C ANISOU 2685 C MET A 506 2461 2183 2050 135 -216 -260 C ATOM 2686 O MET A 506 46.136 39.372 13.508 1.00 17.35 O ANISOU 2686 O MET A 506 2472 2104 2016 134 -249 -259 O ATOM 2687 CB MET A 506 45.490 36.601 15.230 1.00 15.89 C ANISOU 2687 CB MET A 506 2092 2078 1867 85 -213 -297 C ATOM 2688 CG MET A 506 44.434 36.003 16.167 1.00 18.67 C ANISOU 2688 CG MET A 506 2373 2507 2213 73 -236 -348 C ATOM 2689 SD MET A 506 45.165 34.891 17.388 1.00 21.16 S ANISOU 2689 SD MET A 506 2607 2872 2560 -8 -208 -286 S ATOM 2690 CE MET A 506 46.271 36.015 18.249 1.00 19.11 C ANISOU 2690 CE MET A 506 2346 2607 2310 -40 -209 -261 C ATOM 2691 N LEU A 507 46.880 37.440 12.639 1.00 15.04 N ANISOU 2691 N LEU A 507 2135 1854 1724 119 -160 -209 N ATOM 2692 CA LEU A 507 48.027 38.059 11.970 1.00 16.33 C ANISOU 2692 CA LEU A 507 2347 1979 1879 90 -122 -143 C ATOM 2693 C LEU A 507 47.598 39.047 10.895 1.00 20.12 C ANISOU 2693 C LEU A 507 2931 2407 2307 127 -151 -134 C ATOM 2694 O LEU A 507 48.131 40.155 10.812 1.00 20.29 O ANISOU 2694 O LEU A 507 3007 2376 2327 95 -158 -89 O ATOM 2695 CB LEU A 507 48.924 36.969 11.356 1.00 15.95 C ANISOU 2695 CB LEU A 507 2262 1961 1836 76 -58 -112 C ATOM 2696 CG LEU A 507 50.146 37.468 10.579 1.00 22.70 C ANISOU 2696 CG LEU A 507 3149 2805 2671 37 -3 -51 C ATOM 2697 CD1 LEU A 507 51.060 38.281 11.508 1.00 20.20 C ANISOU 2697 CD1 LEU A 507 2812 2467 2398 -32 4 -14 C ATOM 2698 CD2 LEU A 507 50.896 36.281 9.973 1.00 24.65 C ANISOU 2698 CD2 LEU A 507 3343 3101 2923 40 53 -51 C ATOM 2699 N THR A 508 46.634 38.642 10.070 1.00 18.79 N ANISOU 2699 N THR A 508 2793 2250 2097 194 -173 -174 N ATOM 2700 CA THR A 508 46.139 39.501 8.993 1.00 18.73 C ANISOU 2700 CA THR A 508 2891 2195 2030 240 -212 -164 C ATOM 2701 C THR A 508 45.528 40.772 9.559 1.00 24.26 C ANISOU 2701 C THR A 508 3637 2835 2746 257 -294 -191 C ATOM 2702 O THR A 508 45.675 41.856 8.983 1.00 21.65 O ANISOU 2702 O THR A 508 3402 2432 2390 258 -328 -145 O ATOM 2703 CB THR A 508 45.105 38.766 8.119 1.00 26.99 C ANISOU 2703 CB THR A 508 3949 3273 3034 319 -233 -222 C ATOM 2704 OG1 THR A 508 45.755 37.670 7.473 1.00 23.63 O ANISOU 2704 OG1 THR A 508 3486 2895 2595 309 -165 -204 O ATOM 2705 CG2 THR A 508 44.523 39.704 7.053 1.00 26.67 C ANISOU 2705 CG2 THR A 508 4024 3184 2926 375 -289 -214 C ATOM 2706 N ILE A 509 44.853 40.635 10.696 1.00 19.70 N ANISOU 2706 N ILE A 509 2989 2287 2208 269 -329 -266 N ATOM 2707 CA ILE A 509 44.230 41.784 11.336 1.00 16.82 C ANISOU 2707 CA ILE A 509 2648 1880 1864 296 -413 -319 C ATOM 2708 C ILE A 509 45.320 42.774 11.748 1.00 20.70 C ANISOU 2708 C ILE A 509 3167 2307 2391 231 -410 -255 C ATOM 2709 O ILE A 509 45.222 43.962 11.465 1.00 19.34 O ANISOU 2709 O ILE A 509 3079 2047 2222 247 -475 -244 O ATOM 2710 CB ILE A 509 43.402 41.373 12.562 1.00 16.85 C ANISOU 2710 CB ILE A 509 2550 1960 1894 308 -436 -416 C ATOM 2711 CG1 ILE A 509 42.079 40.757 12.101 1.00 21.62 C ANISOU 2711 CG1 ILE A 509 3139 2609 2466 379 -466 -497 C ATOM 2712 CG2 ILE A 509 43.163 42.582 13.484 1.00 22.85 C ANISOU 2712 CG2 ILE A 509 3308 2689 2685 318 -510 -472 C ATOM 2713 CD1 ILE A 509 41.368 39.974 13.174 1.00 24.87 C ANISOU 2713 CD1 ILE A 509 3436 3120 2893 365 -459 -572 C ATOM 2714 N CYS A 510 46.370 42.279 12.395 1.00 17.65 N ANISOU 2714 N CYS A 510 2711 1958 2036 157 -341 -213 N ATOM 2715 CA CYS A 510 47.466 43.140 12.821 1.00 21.47 C ANISOU 2715 CA CYS A 510 3207 2390 2561 89 -333 -159 C ATOM 2716 C CYS A 510 48.214 43.760 11.646 1.00 22.38 C ANISOU 2716 C CYS A 510 3419 2433 2650 54 -310 -62 C ATOM 2717 O CYS A 510 48.544 44.948 11.672 1.00 23.66 O ANISOU 2717 O CYS A 510 3643 2509 2839 24 -354 -29 O ATOM 2718 CB CYS A 510 48.438 42.386 13.735 1.00 19.22 C ANISOU 2718 CB CYS A 510 2821 2170 2313 24 -267 -141 C ATOM 2719 SG CYS A 510 47.709 41.841 15.309 1.00 22.77 S ANISOU 2719 SG CYS A 510 3161 2709 2783 40 -296 -233 S ATOM 2720 N CYS A 511 48.490 42.971 10.615 1.00 20.11 N ANISOU 2720 N CYS A 511 3144 2185 2310 53 -245 -17 N ATOM 2721 CA CYS A 511 49.154 43.527 9.445 1.00 19.38 C ANISOU 2721 CA CYS A 511 3142 2050 2173 14 -216 78 C ATOM 2722 C CYS A 511 48.275 44.592 8.769 1.00 25.83 C ANISOU 2722 C CYS A 511 4084 2776 2956 65 -310 86 C ATOM 2723 O CYS A 511 48.779 45.632 8.333 1.00 29.71 O ANISOU 2723 O CYS A 511 4662 3184 3442 14 -329 167 O ATOM 2724 CB CYS A 511 49.577 42.425 8.465 1.00 23.38 C ANISOU 2724 CB CYS A 511 3626 2638 2620 12 -129 106 C ATOM 2725 SG CYS A 511 50.886 41.366 9.134 1.00 27.25 S ANISOU 2725 SG CYS A 511 3982 3210 3160 -54 -32 110 S ATOM 2726 N ASP A 512 46.965 44.358 8.707 1.00 22.68 N ANISOU 2726 N ASP A 512 3693 2386 2538 162 -375 2 N ATOM 2727 CA ASP A 512 46.062 45.369 8.144 1.00 25.76 C ANISOU 2727 CA ASP A 512 4197 2685 2903 226 -483 -6 C ATOM 2728 C ASP A 512 46.126 46.664 8.963 1.00 26.95 C ANISOU 2728 C ASP A 512 4379 2733 3129 208 -568 -17 C ATOM 2729 O ASP A 512 46.131 47.763 8.409 1.00 33.70 O ANISOU 2729 O ASP A 512 5350 3475 3979 204 -639 41 O ATOM 2730 CB ASP A 512 44.610 44.875 8.091 1.00 24.38 C ANISOU 2730 CB ASP A 512 4003 2551 2709 338 -544 -120 C ATOM 2731 CG ASP A 512 44.353 43.884 6.954 1.00 34.81 C ANISOU 2731 CG ASP A 512 5335 3940 3951 376 -496 -111 C ATOM 2732 OD1 ASP A 512 45.257 43.648 6.126 1.00 28.36 O ANISOU 2732 OD1 ASP A 512 4549 3143 3085 324 -420 -18 O ATOM 2733 OD2 ASP A 512 43.232 43.338 6.893 1.00 37.94 O ANISOU 2733 OD2 ASP A 512 5701 4379 4335 459 -534 -206 O ATOM 2734 N ALA A 513 46.166 46.539 10.284 1.00 28.33 N ANISOU 2734 N ALA A 513 4450 2943 3370 197 -569 -91 N ATOM 2735 CA ALA A 513 46.176 47.719 11.147 1.00 29.09 C ANISOU 2735 CA ALA A 513 4559 2953 3542 190 -656 -128 C ATOM 2736 C ALA A 513 47.440 48.554 10.984 1.00 30.36 C ANISOU 2736 C ALA A 513 4776 3024 3737 87 -636 -15 C ATOM 2737 O ALA A 513 47.369 49.770 10.846 1.00 30.06 O ANISOU 2737 O ALA A 513 4829 2857 3735 87 -731 6 O ATOM 2738 CB ALA A 513 45.987 47.324 12.610 1.00 27.43 C ANISOU 2738 CB ALA A 513 4216 2827 3380 197 -652 -235 C ATOM 2739 N VAL A 514 48.599 47.909 10.991 1.00 27.42 N ANISOU 2739 N VAL A 514 4346 2716 3358 -3 -519 55 N ATOM 2740 CA VAL A 514 49.854 48.657 10.940 1.00 34.62 C ANISOU 2740 CA VAL A 514 5286 3559 4307 -114 -490 151 C ATOM 2741 C VAL A 514 50.152 49.147 9.521 1.00 37.28 C ANISOU 2741 C VAL A 514 5752 3831 4582 -157 -480 278 C ATOM 2742 O VAL A 514 50.993 50.023 9.314 1.00 35.08 O ANISOU 2742 O VAL A 514 5529 3468 4330 -251 -480 370 O ATOM 2743 CB VAL A 514 51.042 47.841 11.503 1.00 34.55 C ANISOU 2743 CB VAL A 514 5159 3648 4319 -194 -374 169 C ATOM 2744 CG1 VAL A 514 50.720 47.322 12.901 1.00 33.66 C ANISOU 2744 CG1 VAL A 514 4928 3606 4254 -154 -389 57 C ATOM 2745 CG2 VAL A 514 51.388 46.701 10.574 1.00 38.89 C ANISOU 2745 CG2 VAL A 514 5689 4297 4791 -204 -267 218 C ATOM 2746 N SER A 515 49.434 48.589 8.554 1.00 34.51 N ANISOU 2746 N SER A 515 5448 3522 4142 -90 -474 283 N ATOM 2747 CA SER A 515 49.620 48.922 7.147 1.00 37.92 C ANISOU 2747 CA SER A 515 6000 3919 4487 -121 -461 402 C ATOM 2748 C SER A 515 48.675 50.035 6.689 1.00 44.13 C ANISOU 2748 C SER A 515 6930 4568 5270 -58 -606 414 C ATOM 2749 O SER A 515 48.783 50.524 5.565 1.00 43.87 O ANISOU 2749 O SER A 515 7020 4482 5165 -88 -620 526 O ATOM 2750 CB SER A 515 49.380 47.671 6.295 1.00 43.55 C ANISOU 2750 CB SER A 515 6683 4762 5101 -75 -380 393 C ATOM 2751 OG SER A 515 50.067 47.739 5.060 1.00 64.30 O ANISOU 2751 OG SER A 515 9381 7413 7636 -144 -313 514 O ATOM 2752 N GLY A 516 47.739 50.415 7.552 1.00 42.74 N ANISOU 2752 N GLY A 516 6736 4339 5165 31 -718 294 N ATOM 2753 CA GLY A 516 46.785 51.465 7.239 1.00 41.74 C ANISOU 2753 CA GLY A 516 6732 4076 5051 110 -875 277 C ATOM 2754 C GLY A 516 45.521 50.990 6.551 1.00 43.05 C ANISOU 2754 C GLY A 516 6932 4283 5142 239 -927 213 C ATOM 2755 O GLY A 516 44.668 51.792 6.175 1.00 46.84 O ANISOU 2755 O GLY A 516 7518 4656 5624 319 -1065 194 O ATOM 2756 N ARG A 517 45.384 49.683 6.384 1.00 36.97 N ANISOU 2756 N ARG A 517 6072 3662 4312 262 -825 173 N ATOM 2757 CA ARG A 517 44.220 49.140 5.707 1.00 39.27 C ANISOU 2757 CA ARG A 517 6384 4002 4535 379 -865 105 C ATOM 2758 C ARG A 517 43.053 48.983 6.669 1.00 45.20 C ANISOU 2758 C ARG A 517 7048 4781 5346 484 -943 -69 C ATOM 2759 O ARG A 517 41.922 48.726 6.253 1.00 51.60 O ANISOU 2759 O ARG A 517 7870 5616 6118 591 -1005 -151 O ATOM 2760 CB ARG A 517 44.563 47.801 5.063 1.00 35.77 C ANISOU 2760 CB ARG A 517 5881 3702 4009 359 -731 130 C ATOM 2761 CG ARG A 517 45.641 47.905 3.995 1.00 45.29 C ANISOU 2761 CG ARG A 517 7163 4911 5134 263 -650 288 C ATOM 2762 CD ARG A 517 45.796 46.600 3.231 1.00 48.55 C ANISOU 2762 CD ARG A 517 7519 5467 5459 273 -540 285 C ATOM 2763 NE ARG A 517 46.332 45.545 4.083 1.00 52.31 N ANISOU 2763 NE ARG A 517 7843 6042 5990 237 -440 227 N ATOM 2764 CZ ARG A 517 47.625 45.266 4.188 1.00 53.50 C ANISOU 2764 CZ ARG A 517 7939 6240 6148 133 -331 293 C ATOM 2765 NH1 ARG A 517 48.507 45.963 3.487 1.00 56.78 N ANISOU 2765 NH1 ARG A 517 8434 6626 6515 43 -297 420 N ATOM 2766 NH2 ARG A 517 48.034 44.290 4.987 1.00 49.50 N ANISOU 2766 NH2 ARG A 517 7299 5814 5696 115 -259 235 N ATOM 2767 N ARG A 518 43.337 49.137 7.957 1.00 42.02 N ANISOU 2767 N ARG A 518 6551 4384 5030 450 -937 -130 N ATOM 2768 CA ARG A 518 42.326 48.995 8.997 1.00 34.18 C ANISOU 2768 CA ARG A 518 5458 3443 4086 532 -996 -297 C ATOM 2769 C ARG A 518 42.428 50.128 10.019 1.00 33.63 C ANISOU 2769 C ARG A 518 5382 3284 4112 527 -1088 -351 C ATOM 2770 O ARG A 518 43.499 50.389 10.573 1.00 38.01 O ANISOU 2770 O ARG A 518 5914 3816 4714 431 -1039 -291 O ATOM 2771 CB ARG A 518 42.468 47.636 9.695 1.00 41.06 C ANISOU 2771 CB ARG A 518 6178 4470 4950 499 -876 -344 C ATOM 2772 CG ARG A 518 41.609 47.493 10.927 1.00 42.74 C ANISOU 2772 CG ARG A 518 6274 4756 5208 550 -917 -499 C ATOM 2773 CD ARG A 518 41.827 46.158 11.622 1.00 47.08 C ANISOU 2773 CD ARG A 518 6689 5449 5749 501 -802 -518 C ATOM 2774 NE ARG A 518 41.053 46.117 12.855 1.00 47.91 N ANISOU 2774 NE ARG A 518 6684 5635 5885 533 -839 -656 N ATOM 2775 CZ ARG A 518 40.048 45.285 13.093 1.00 43.36 C ANISOU 2775 CZ ARG A 518 6024 5169 5283 575 -830 -752 C ATOM 2776 NH1 ARG A 518 39.685 44.373 12.191 1.00 40.20 N ANISOU 2776 NH1 ARG A 518 5635 4803 4836 596 -790 -731 N ATOM 2777 NH2 ARG A 518 39.413 45.365 14.248 1.00 43.26 N ANISOU 2777 NH2 ARG A 518 5909 5240 5290 593 -861 -873 N ATOM 2778 N GLN A 519 41.304 50.792 10.268 1.00 33.28 N ANISOU 2778 N GLN A 519 5350 3195 4098 637 -1227 -478 N ATOM 2779 CA GLN A 519 41.254 51.936 11.176 1.00 34.95 C ANISOU 2779 CA GLN A 519 5559 3317 4406 657 -1340 -557 C ATOM 2780 C GLN A 519 41.580 51.524 12.614 1.00 38.19 C ANISOU 2780 C GLN A 519 5811 3841 4858 613 -1273 -641 C ATOM 2781 O GLN A 519 41.011 50.566 13.138 1.00 38.93 O ANISOU 2781 O GLN A 519 5785 4087 4918 638 -1215 -731 O ATOM 2782 CB GLN A 519 39.871 52.590 11.105 1.00 43.50 C ANISOU 2782 CB GLN A 519 6670 4350 5508 804 -1505 -703 C ATOM 2783 CG GLN A 519 39.651 53.693 12.106 1.00 49.15 C ANISOU 2783 CG GLN A 519 7359 4991 6325 849 -1635 -827 C ATOM 2784 CD GLN A 519 40.576 54.866 11.881 1.00 52.62 C ANISOU 2784 CD GLN A 519 7923 5235 6833 784 -1703 -709 C ATOM 2785 OE1 GLN A 519 41.509 55.094 12.652 1.00 51.41 O ANISOU 2785 OE1 GLN A 519 7724 5072 6737 694 -1658 -683 O ATOM 2786 NE2 GLN A 519 40.334 55.613 10.809 1.00 52.72 N ANISOU 2786 NE2 GLN A 519 8099 5090 6841 824 -1815 -632 N ATOM 2787 N THR A 520 42.493 52.257 13.245 1.00 36.01 N ANISOU 2787 N THR A 520 5537 3492 4654 543 -1285 -607 N ATOM 2788 CA THR A 520 42.968 51.923 14.587 1.00 34.52 C ANISOU 2788 CA THR A 520 5209 3408 4499 492 -1222 -670 C ATOM 2789 C THR A 520 42.383 52.836 15.665 1.00 34.67 C ANISOU 2789 C THR A 520 5173 3409 4592 564 -1350 -839 C ATOM 2790 O THR A 520 42.533 52.570 16.855 1.00 40.33 O ANISOU 2790 O THR A 520 5763 4239 5323 543 -1313 -922 O ATOM 2791 CB THR A 520 44.509 51.970 14.664 1.00 35.06 C ANISOU 2791 CB THR A 520 5288 3437 4596 358 -1132 -531 C ATOM 2792 OG1 THR A 520 44.982 53.184 14.068 1.00 37.03 O ANISOU 2792 OG1 THR A 520 5671 3500 4900 328 -1217 -447 O ATOM 2793 CG2 THR A 520 45.117 50.790 13.919 1.00 33.32 C ANISOU 2793 CG2 THR A 520 5064 3296 4299 289 -984 -405 C ATOM 2794 N LYS A 521 41.722 53.910 15.239 1.00 39.82 N ANISOU 2794 N LYS A 521 5920 3923 5288 651 -1505 -893 N ATOM 2795 CA LYS A 521 41.064 54.835 16.159 1.00 44.06 C ANISOU 2795 CA LYS A 521 6406 4435 5900 741 -1647 -1077 C ATOM 2796 C LYS A 521 39.670 54.344 16.537 1.00 39.98 C ANISOU 2796 C LYS A 521 5784 4070 5337 855 -1677 -1260 C ATOM 2797 O LYS A 521 38.841 54.059 15.680 1.00 46.77 O ANISOU 2797 O LYS A 521 6691 4931 6148 925 -1702 -1267 O ATOM 2798 CB LYS A 521 40.974 56.241 15.553 1.00 46.79 C ANISOU 2798 CB LYS A 521 6902 4548 6329 791 -1821 -1062 C ATOM 2799 CG LYS A 521 42.316 56.916 15.312 1.00 51.92 C ANISOU 2799 CG LYS A 521 7649 5038 7041 669 -1811 -898 C ATOM 2800 CD LYS A 521 42.126 58.343 14.810 1.00 64.76 C ANISOU 2800 CD LYS A 521 9424 6423 8760 718 -2004 -891 C ATOM 2801 CE LYS A 521 43.454 59.057 14.612 1.00 70.45 C ANISOU 2801 CE LYS A 521 10236 6982 9550 581 -1997 -727 C ATOM 2802 NZ LYS A 521 43.273 60.402 13.989 1.00 75.31 N ANISOU 2802 NZ LYS A 521 11019 7343 10254 615 -2189 -688 N ATOM 2803 N GLU A 522 39.424 54.249 17.834 1.00 54.05 N ANISOU 2803 N GLU A 522 7418 5991 7129 870 -1671 -1410 N ATOM 2804 CA GLU A 522 38.135 53.819 18.350 1.00 56.54 C ANISOU 2804 CA GLU A 522 7609 6476 7398 963 -1691 -1596 C ATOM 2805 C GLU A 522 38.146 54.091 19.848 1.00 53.19 C ANISOU 2805 C GLU A 522 7039 6171 6998 965 -1707 -1750 C ATOM 2806 O GLU A 522 39.194 53.991 20.493 1.00 47.16 O ANISOU 2806 O GLU A 522 6243 5426 6248 868 -1634 -1679 O ATOM 2807 CB GLU A 522 37.920 52.328 18.073 1.00 58.64 C ANISOU 2807 CB GLU A 522 7817 6900 7562 913 -1539 -1530 C ATOM 2808 CG GLU A 522 36.546 51.793 18.450 1.00 65.18 C ANISOU 2808 CG GLU A 522 8522 7905 8337 993 -1549 -1704 C ATOM 2809 CD GLU A 522 36.347 50.338 18.031 1.00 72.21 C ANISOU 2809 CD GLU A 522 9374 8918 9142 938 -1411 -1623 C ATOM 2810 OE1 GLU A 522 36.768 49.970 16.912 1.00 77.72 O ANISOU 2810 OE1 GLU A 522 10183 9524 9824 908 -1368 -1472 O ATOM 2811 OE2 GLU A 522 35.762 49.564 18.817 1.00 70.69 O ANISOU 2811 OE2 GLU A 522 9041 8918 8900 922 -1349 -1714 O ATOM 2812 N GLY A 523 36.993 54.454 20.397 1.00 50.24 N ANISOU 2812 N GLY A 523 6574 5887 6627 1079 -1805 -1968 N ATOM 2813 CA GLY A 523 36.885 54.739 21.818 1.00 60.61 C ANISOU 2813 CA GLY A 523 7739 7340 7949 1093 -1826 -2139 C ATOM 2814 C GLY A 523 37.614 55.997 22.266 1.00 66.58 C ANISOU 2814 C GLY A 523 8537 7943 8816 1102 -1939 -2174 C ATOM 2815 O GLY A 523 37.940 56.145 23.448 1.00 66.81 O ANISOU 2815 O GLY A 523 8453 8079 8851 1079 -1928 -2267 O ATOM 2816 N GLY A 524 37.868 56.905 21.327 1.00 66.71 N ANISOU 2816 N GLY A 524 8717 7710 8921 1133 -2053 -2098 N ATOM 2817 CA GLY A 524 38.521 58.166 21.638 1.00 66.17 C ANISOU 2817 CA GLY A 524 8704 7462 8977 1140 -2180 -2125 C ATOM 2818 C GLY A 524 40.030 58.051 21.743 1.00 65.51 C ANISOU 2818 C GLY A 524 8661 7313 8917 989 -2077 -1937 C ATOM 2819 O GLY A 524 40.686 58.878 22.381 1.00 62.58 O ANISOU 2819 O GLY A 524 8281 6859 8636 970 -2145 -1979 O ATOM 2820 N TYR A 525 40.590 57.023 21.111 1.00 65.44 N ANISOU 2820 N TYR A 525 8690 7342 8830 885 -1916 -1740 N ATOM 2821 CA TYR A 525 42.031 56.818 21.140 1.00 67.99 C ANISOU 2821 CA TYR A 525 9043 7619 9170 743 -1810 -1564 C ATOM 2822 C TYR A 525 42.498 55.971 19.956 1.00 57.18 C ANISOU 2822 C TYR A 525 7769 6221 7736 660 -1684 -1345 C ATOM 2823 O TYR A 525 41.738 55.163 19.429 1.00 57.03 O ANISOU 2823 O TYR A 525 7745 6292 7634 698 -1634 -1340 O ATOM 2824 CB TYR A 525 42.447 56.176 22.468 1.00 81.30 C ANISOU 2824 CB TYR A 525 10566 9510 10813 689 -1709 -1625 C ATOM 2825 CG TYR A 525 43.942 56.131 22.693 1.00 92.83 C ANISOU 2825 CG TYR A 525 12037 10924 12309 559 -1627 -1486 C ATOM 2826 CD1 TYR A 525 44.671 57.297 22.896 1.00 96.23 C ANISOU 2826 CD1 TYR A 525 12515 11187 12859 537 -1725 -1494 C ATOM 2827 CD2 TYR A 525 44.623 54.921 22.712 1.00 96.50 C ANISOU 2827 CD2 TYR A 525 12461 11509 12697 460 -1459 -1354 C ATOM 2828 CE1 TYR A 525 46.038 57.258 23.102 1.00 97.08 C ANISOU 2828 CE1 TYR A 525 12623 11260 13004 415 -1650 -1376 C ATOM 2829 CE2 TYR A 525 45.990 54.873 22.919 1.00 96.44 C ANISOU 2829 CE2 TYR A 525 12453 11467 12724 349 -1389 -1240 C ATOM 2830 CZ TYR A 525 46.691 56.044 23.113 1.00 96.04 C ANISOU 2830 CZ TYR A 525 12443 11261 12788 325 -1481 -1253 C ATOM 2831 OH TYR A 525 48.050 55.999 23.320 1.00 93.97 O ANISOU 2831 OH TYR A 525 12171 10971 12563 211 -1410 -1150 O ATOM 2832 N ASP A 526 43.744 56.186 19.537 1.00 45.18 N ANISOU 2832 N ASP A 526 6330 4580 6256 548 -1636 -1176 N ATOM 2833 CA ASP A 526 44.358 55.426 18.452 1.00 42.68 C ANISOU 2833 CA ASP A 526 6092 4247 5877 460 -1511 -973 C ATOM 2834 C ASP A 526 45.062 54.219 19.072 1.00 39.76 C ANISOU 2834 C ASP A 526 5605 4055 5447 374 -1344 -926 C ATOM 2835 O ASP A 526 45.972 54.373 19.889 1.00 42.08 O ANISOU 2835 O ASP A 526 5837 4366 5784 306 -1315 -925 O ATOM 2836 CB ASP A 526 45.354 56.313 17.698 1.00 42.98 C ANISOU 2836 CB ASP A 526 6268 4076 5986 376 -1544 -821 C ATOM 2837 CG ASP A 526 45.930 55.643 16.464 1.00 48.84 C ANISOU 2837 CG ASP A 526 7096 4805 6655 292 -1425 -621 C ATOM 2838 OD1 ASP A 526 45.650 54.450 16.239 1.00 45.80 O ANISOU 2838 OD1 ASP A 526 6659 4568 6175 300 -1315 -604 O ATOM 2839 OD2 ASP A 526 46.674 56.313 15.718 1.00 52.29 O ANISOU 2839 OD2 ASP A 526 7650 5087 7129 214 -1443 -483 O ATOM 2840 N HIS A 527 44.629 53.022 18.695 1.00 31.25 N ANISOU 2840 N HIS A 527 4496 3104 4274 381 -1245 -893 N ATOM 2841 CA HIS A 527 45.111 51.796 19.321 1.00 27.70 C ANISOU 2841 CA HIS A 527 3933 2823 3767 315 -1107 -863 C ATOM 2842 C HIS A 527 46.253 51.187 18.553 1.00 31.50 C ANISOU 2842 C HIS A 527 4463 3276 4231 213 -989 -682 C ATOM 2843 O HIS A 527 46.569 50.012 18.750 1.00 31.80 O ANISOU 2843 O HIS A 527 4430 3438 4216 170 -877 -639 O ATOM 2844 CB HIS A 527 43.995 50.756 19.391 1.00 33.51 C ANISOU 2844 CB HIS A 527 4598 3715 4418 373 -1068 -932 C ATOM 2845 CG HIS A 527 42.886 51.115 20.324 1.00 46.88 C ANISOU 2845 CG HIS A 527 6203 5499 6111 463 -1155 -1125 C ATOM 2846 ND1 HIS A 527 42.017 52.157 20.082 1.00 49.99 N ANISOU 2846 ND1 HIS A 527 6645 5801 6546 566 -1297 -1239 N ATOM 2847 CD2 HIS A 527 42.488 50.556 21.493 1.00 53.50 C ANISOU 2847 CD2 HIS A 527 6901 6522 6905 465 -1121 -1229 C ATOM 2848 CE1 HIS A 527 41.138 52.231 21.065 1.00 51.90 C ANISOU 2848 CE1 HIS A 527 6771 6176 6772 632 -1344 -1419 C ATOM 2849 NE2 HIS A 527 41.402 51.271 21.933 1.00 61.49 N ANISOU 2849 NE2 HIS A 527 7871 7566 7929 567 -1234 -1411 N ATOM 2850 N ALA A 528 46.862 51.969 17.670 1.00 28.54 N ANISOU 2850 N ALA A 528 4207 2741 3897 172 -1017 -579 N ATOM 2851 CA ALA A 528 47.904 51.434 16.805 1.00 35.38 C ANISOU 2851 CA ALA A 528 5118 3592 4735 76 -904 -414 C ATOM 2852 C ALA A 528 49.002 50.764 17.623 1.00 30.65 C ANISOU 2852 C ALA A 528 4411 3091 4145 -9 -801 -387 C ATOM 2853 O ALA A 528 49.542 49.743 17.214 1.00 27.74 O ANISOU 2853 O ALA A 528 4018 2795 3727 -56 -689 -304 O ATOM 2854 CB ALA A 528 48.477 52.524 15.912 1.00 34.33 C ANISOU 2854 CB ALA A 528 5118 3278 4646 24 -954 -308 C ATOM 2855 N ILE A 529 49.314 51.341 18.784 1.00 27.97 N ANISOU 2855 N ILE A 529 4004 2756 3870 -19 -849 -468 N ATOM 2856 CA ILE A 529 50.340 50.807 19.674 1.00 24.14 C ANISOU 2856 CA ILE A 529 3414 2362 3397 -90 -772 -456 C ATOM 2857 C ILE A 529 50.018 49.375 20.087 1.00 21.63 C ANISOU 2857 C ILE A 529 3003 2214 3000 -73 -689 -472 C ATOM 2858 O ILE A 529 50.912 48.538 20.211 1.00 24.77 O ANISOU 2858 O ILE A 529 3349 2677 3384 -135 -596 -404 O ATOM 2859 CB ILE A 529 50.482 51.677 20.946 1.00 30.97 C ANISOU 2859 CB ILE A 529 4214 3220 4333 -81 -857 -572 C ATOM 2860 CG1 ILE A 529 50.778 53.124 20.560 1.00 49.82 C ANISOU 2860 CG1 ILE A 529 6696 5416 6815 -100 -956 -560 C ATOM 2861 CG2 ILE A 529 51.599 51.161 21.819 1.00 33.10 C ANISOU 2861 CG2 ILE A 529 4382 3581 4614 -153 -784 -555 C ATOM 2862 CD1 ILE A 529 50.715 54.113 21.725 1.00 56.04 C ANISOU 2862 CD1 ILE A 529 7430 6178 7686 -68 -1069 -702 C ATOM 2863 N SER A 530 48.737 49.086 20.280 1.00 25.29 N ANISOU 2863 N SER A 530 3446 2748 3417 11 -726 -562 N ATOM 2864 CA SER A 530 48.313 47.734 20.625 1.00 27.13 C ANISOU 2864 CA SER A 530 3599 3131 3577 20 -655 -570 C ATOM 2865 C SER A 530 48.526 46.747 19.481 1.00 26.58 C ANISOU 2865 C SER A 530 3574 3059 3466 -4 -568 -458 C ATOM 2866 O SER A 530 49.048 45.659 19.692 1.00 20.92 O ANISOU 2866 O SER A 530 2800 2424 2727 -45 -488 -408 O ATOM 2867 CB SER A 530 46.854 47.724 21.073 1.00 26.89 C ANISOU 2867 CB SER A 530 3529 3181 3507 105 -716 -700 C ATOM 2868 OG SER A 530 46.718 48.469 22.272 1.00 29.62 O ANISOU 2868 OG SER A 530 3807 3568 3879 126 -786 -819 O ATOM 2869 N PHE A 531 48.102 47.117 18.279 1.00 20.04 N ANISOU 2869 N PHE A 531 2849 2139 2628 29 -592 -424 N ATOM 2870 CA PHE A 531 48.301 46.265 17.121 1.00 23.04 C ANISOU 2870 CA PHE A 531 3271 2519 2962 13 -516 -329 C ATOM 2871 C PHE A 531 49.787 46.005 16.862 1.00 24.67 C ANISOU 2871 C PHE A 531 3472 2712 3189 -78 -431 -222 C ATOM 2872 O PHE A 531 50.175 44.911 16.450 1.00 23.52 O ANISOU 2872 O PHE A 531 3299 2626 3012 -99 -350 -170 O ATOM 2873 CB PHE A 531 47.635 46.879 15.880 1.00 22.48 C ANISOU 2873 CB PHE A 531 3321 2350 2871 64 -569 -310 C ATOM 2874 CG PHE A 531 46.127 46.821 15.905 1.00 20.65 C ANISOU 2874 CG PHE A 531 3086 2152 2608 163 -638 -417 C ATOM 2875 CD1 PHE A 531 45.462 45.653 15.593 1.00 22.99 C ANISOU 2875 CD1 PHE A 531 3345 2540 2849 194 -591 -432 C ATOM 2876 CD2 PHE A 531 45.380 47.943 16.240 1.00 27.99 C ANISOU 2876 CD2 PHE A 531 4042 3021 3571 227 -755 -513 C ATOM 2877 CE1 PHE A 531 44.079 45.592 15.613 1.00 22.07 C ANISOU 2877 CE1 PHE A 531 3215 2464 2707 279 -652 -537 C ATOM 2878 CE2 PHE A 531 43.994 47.899 16.253 1.00 26.61 C ANISOU 2878 CE2 PHE A 531 3853 2889 3370 322 -821 -626 C ATOM 2879 CZ PHE A 531 43.341 46.722 15.937 1.00 29.39 C ANISOU 2879 CZ PHE A 531 4164 3341 3662 345 -765 -637 C ATOM 2880 N GLN A 532 50.617 47.014 17.097 1.00 24.32 N ANISOU 2880 N GLN A 532 3447 2589 3203 -131 -455 -199 N ATOM 2881 CA GLN A 532 52.055 46.867 16.889 1.00 24.03 C ANISOU 2881 CA GLN A 532 3393 2546 3190 -223 -377 -110 C ATOM 2882 C GLN A 532 52.629 45.879 17.894 1.00 18.20 C ANISOU 2882 C GLN A 532 2535 1921 2458 -246 -324 -131 C ATOM 2883 O GLN A 532 53.518 45.085 17.576 1.00 20.78 O ANISOU 2883 O GLN A 532 2827 2291 2778 -290 -242 -71 O ATOM 2884 CB GLN A 532 52.758 48.223 16.994 1.00 27.35 C ANISOU 2884 CB GLN A 532 3856 2853 3682 -282 -424 -88 C ATOM 2885 CG GLN A 532 52.406 49.154 15.839 1.00 37.50 C ANISOU 2885 CG GLN A 532 5278 4011 4961 -280 -473 -31 C ATOM 2886 CD GLN A 532 52.982 50.546 16.001 1.00 52.60 C ANISOU 2886 CD GLN A 532 7240 5790 6956 -340 -539 -10 C ATOM 2887 OE1 GLN A 532 52.807 51.407 15.133 1.00 58.18 O ANISOU 2887 OE1 GLN A 532 8064 6374 7666 -352 -591 51 O ATOM 2888 NE2 GLN A 532 53.667 50.780 17.118 1.00 52.20 N ANISOU 2888 NE2 GLN A 532 7102 5758 6973 -378 -546 -60 N ATOM 2889 N ASP A 533 52.099 45.926 19.105 1.00 20.55 N ANISOU 2889 N ASP A 533 2769 2273 2765 -212 -375 -220 N ATOM 2890 CA ASP A 533 52.498 45.013 20.158 1.00 21.07 C ANISOU 2890 CA ASP A 533 2730 2451 2826 -228 -341 -238 C ATOM 2891 C ASP A 533 52.107 43.586 19.766 1.00 23.10 C ANISOU 2891 C ASP A 533 2966 2782 3028 -207 -285 -208 C ATOM 2892 O ASP A 533 52.921 42.659 19.837 1.00 20.78 O ANISOU 2892 O ASP A 533 2624 2534 2738 -240 -227 -161 O ATOM 2893 CB ASP A 533 51.785 45.411 21.461 1.00 24.34 C ANISOU 2893 CB ASP A 533 3087 2923 3238 -191 -413 -346 C ATOM 2894 CG ASP A 533 52.383 44.756 22.684 1.00 41.39 C ANISOU 2894 CG ASP A 533 5144 5189 5394 -221 -392 -357 C ATOM 2895 OD1 ASP A 533 53.542 44.325 22.609 1.00 52.23 O ANISOU 2895 OD1 ASP A 533 6491 6561 6792 -273 -340 -293 O ATOM 2896 OD2 ASP A 533 51.706 44.687 23.730 1.00 46.80 O ANISOU 2896 OD2 ASP A 533 5770 5965 6045 -193 -431 -435 O ATOM 2897 N TRP A 534 50.852 43.402 19.371 1.00 18.80 N ANISOU 2897 N TRP A 534 2456 2247 2440 -147 -311 -244 N ATOM 2898 CA TRP A 534 50.414 42.062 18.981 1.00 15.77 C ANISOU 2898 CA TRP A 534 2053 1924 2015 -128 -266 -222 C ATOM 2899 C TRP A 534 51.191 41.542 17.781 1.00 16.72 C ANISOU 2899 C TRP A 534 2210 2009 2135 -150 -200 -141 C ATOM 2900 O TRP A 534 51.531 40.358 17.714 1.00 18.45 O ANISOU 2900 O TRP A 534 2385 2276 2350 -158 -154 -112 O ATOM 2901 CB TRP A 534 48.908 42.013 18.726 1.00 18.36 C ANISOU 2901 CB TRP A 534 2405 2269 2300 -62 -308 -285 C ATOM 2902 CG TRP A 534 48.115 42.525 19.881 1.00 16.61 C ANISOU 2902 CG TRP A 534 2135 2104 2071 -38 -369 -381 C ATOM 2903 CD1 TRP A 534 48.399 42.371 21.213 1.00 20.54 C ANISOU 2903 CD1 TRP A 534 2548 2686 2569 -69 -373 -408 C ATOM 2904 CD2 TRP A 534 46.908 43.283 19.810 1.00 17.07 C ANISOU 2904 CD2 TRP A 534 2219 2152 2115 28 -440 -473 C ATOM 2905 NE1 TRP A 534 47.438 42.999 21.971 1.00 21.20 N ANISOU 2905 NE1 TRP A 534 2599 2822 2633 -30 -436 -515 N ATOM 2906 CE2 TRP A 534 46.508 43.558 21.132 1.00 20.36 C ANISOU 2906 CE2 TRP A 534 2556 2657 2522 32 -480 -562 C ATOM 2907 CE3 TRP A 534 46.120 43.751 18.753 1.00 22.95 C ANISOU 2907 CE3 TRP A 534 3045 2826 2849 88 -480 -494 C ATOM 2908 CZ2 TRP A 534 45.366 44.293 21.425 1.00 25.95 C ANISOU 2908 CZ2 TRP A 534 3254 3389 3218 97 -555 -683 C ATOM 2909 CZ3 TRP A 534 44.980 44.475 19.046 1.00 25.17 C ANISOU 2909 CZ3 TRP A 534 3322 3117 3122 155 -563 -609 C ATOM 2910 CH2 TRP A 534 44.616 44.739 20.368 1.00 27.02 C ANISOU 2910 CH2 TRP A 534 3468 3445 3355 160 -598 -708 C ATOM 2911 N LEU A 535 51.472 42.426 16.834 1.00 16.09 N ANISOU 2911 N LEU A 535 2209 1846 2059 -159 -200 -106 N ATOM 2912 CA LEU A 535 52.183 42.031 15.637 1.00 16.46 C ANISOU 2912 CA LEU A 535 2288 1877 2088 -183 -133 -36 C ATOM 2913 C LEU A 535 53.567 41.553 15.998 1.00 16.80 C ANISOU 2913 C LEU A 535 2258 1957 2168 -244 -75 -1 C ATOM 2914 O LEU A 535 54.049 40.551 15.470 1.00 20.40 O ANISOU 2914 O LEU A 535 2683 2455 2614 -245 -19 24 O ATOM 2915 CB LEU A 535 52.287 43.211 14.673 1.00 17.32 C ANISOU 2915 CB LEU A 535 2498 1895 2188 -199 -148 8 C ATOM 2916 CG LEU A 535 53.052 42.933 13.378 1.00 22.44 C ANISOU 2916 CG LEU A 535 3181 2545 2800 -235 -72 84 C ATOM 2917 CD1 LEU A 535 52.540 41.678 12.693 1.00 27.59 C ANISOU 2917 CD1 LEU A 535 3820 3261 3402 -179 -38 70 C ATOM 2918 CD2 LEU A 535 52.899 44.135 12.458 1.00 27.10 C ANISOU 2918 CD2 LEU A 535 3888 3044 3366 -250 -102 136 C ATOM 2919 N LYS A 536 54.219 42.306 16.874 1.00 17.09 N ANISOU 2919 N LYS A 536 2264 1977 2253 -288 -96 -9 N ATOM 2920 CA LYS A 536 55.559 41.968 17.339 1.00 19.49 C ANISOU 2920 CA LYS A 536 2490 2316 2599 -344 -52 12 C ATOM 2921 C LYS A 536 55.603 40.591 17.991 1.00 22.11 C ANISOU 2921 C LYS A 536 2741 2729 2930 -320 -41 -5 C ATOM 2922 O LYS A 536 56.558 39.848 17.803 1.00 19.61 O ANISOU 2922 O LYS A 536 2374 2446 2633 -340 5 18 O ATOM 2923 CB LYS A 536 56.048 43.023 18.328 1.00 28.98 C ANISOU 2923 CB LYS A 536 3667 3488 3854 -385 -94 -13 C ATOM 2924 CG LYS A 536 57.528 42.955 18.651 1.00 42.43 C ANISOU 2924 CG LYS A 536 5299 5215 5608 -451 -52 6 C ATOM 2925 CD LYS A 536 58.060 44.338 19.022 1.00 57.71 C ANISOU 2925 CD LYS A 536 7246 7083 7600 -508 -85 -2 C ATOM 2926 CE LYS A 536 57.574 45.396 18.038 1.00 65.88 C ANISOU 2926 CE LYS A 536 8392 8015 8624 -521 -105 34 C ATOM 2927 NZ LYS A 536 57.957 45.077 16.634 1.00 72.13 N ANISOU 2927 NZ LYS A 536 9226 8806 9374 -552 -27 110 N ATOM 2928 N LYS A 537 54.575 40.245 18.760 1.00 17.67 N ANISOU 2928 N LYS A 537 2166 2202 2347 -279 -88 -45 N ATOM 2929 CA LYS A 537 54.535 38.922 19.384 1.00 16.90 C ANISOU 2929 CA LYS A 537 2003 2171 2246 -266 -86 -44 C ATOM 2930 C LYS A 537 54.419 37.830 18.327 1.00 19.78 C ANISOU 2930 C LYS A 537 2381 2536 2597 -238 -48 -20 C ATOM 2931 O LYS A 537 55.128 36.834 18.354 1.00 17.33 O ANISOU 2931 O LYS A 537 2022 2251 2313 -242 -27 -2 O ATOM 2932 CB LYS A 537 53.348 38.816 20.331 1.00 16.29 C ANISOU 2932 CB LYS A 537 1913 2141 2137 -241 -137 -87 C ATOM 2933 CG LYS A 537 53.458 39.670 21.600 1.00 23.21 C ANISOU 2933 CG LYS A 537 2753 3046 3022 -260 -182 -128 C ATOM 2934 CD LYS A 537 52.233 39.391 22.492 1.00 23.00 C ANISOU 2934 CD LYS A 537 2698 3096 2944 -237 -222 -175 C ATOM 2935 CE LYS A 537 52.152 40.329 23.681 1.00 24.63 C ANISOU 2935 CE LYS A 537 2867 3347 3145 -244 -271 -239 C ATOM 2936 NZ LYS A 537 53.062 39.916 24.758 1.00 28.43 N ANISOU 2936 NZ LYS A 537 3279 3889 3634 -280 -274 -218 N ATOM 2937 N LEU A 538 53.485 38.008 17.409 1.00 18.73 N ANISOU 2937 N LEU A 538 2314 2376 2426 -202 -48 -29 N ATOM 2938 CA LEU A 538 53.320 37.050 16.325 1.00 19.09 C ANISOU 2938 CA LEU A 538 2374 2425 2455 -170 -16 -19 C ATOM 2939 C LEU A 538 54.587 36.947 15.480 1.00 20.95 C ANISOU 2939 C LEU A 538 2598 2657 2704 -194 43 11 C ATOM 2940 O LEU A 538 55.001 35.853 15.132 1.00 19.88 O ANISOU 2940 O LEU A 538 2421 2548 2584 -177 66 9 O ATOM 2941 CB LEU A 538 52.116 37.425 15.462 1.00 16.72 C ANISOU 2941 CB LEU A 538 2150 2098 2106 -124 -33 -40 C ATOM 2942 CG LEU A 538 50.770 37.302 16.179 1.00 21.83 C ANISOU 2942 CG LEU A 538 2790 2768 2735 -94 -86 -87 C ATOM 2943 CD1 LEU A 538 49.654 37.945 15.347 1.00 23.29 C ANISOU 2943 CD1 LEU A 538 3050 2921 2878 -44 -114 -120 C ATOM 2944 CD2 LEU A 538 50.439 35.853 16.471 1.00 21.24 C ANISOU 2944 CD2 LEU A 538 2663 2736 2672 -86 -87 -91 C ATOM 2945 N HIS A 539 55.207 38.081 15.167 1.00 19.32 N ANISOU 2945 N HIS A 539 2422 2422 2495 -236 65 34 N ATOM 2946 CA HIS A 539 56.414 38.075 14.331 1.00 20.20 C ANISOU 2946 CA HIS A 539 2515 2549 2610 -273 131 62 C ATOM 2947 C HIS A 539 57.528 37.318 15.032 1.00 26.48 C ANISOU 2947 C HIS A 539 3211 3389 3463 -292 145 50 C ATOM 2948 O HIS A 539 58.287 36.568 14.414 1.00 23.11 O ANISOU 2948 O HIS A 539 2737 3001 3043 -286 189 42 O ATOM 2949 CB HIS A 539 56.887 39.490 14.069 1.00 22.11 C ANISOU 2949 CB HIS A 539 2805 2748 2848 -335 146 98 C ATOM 2950 CG HIS A 539 58.149 39.566 13.267 1.00 33.97 C ANISOU 2950 CG HIS A 539 4279 4281 4346 -392 222 129 C ATOM 2951 ND1 HIS A 539 59.400 39.450 13.833 1.00 36.01 N ANISOU 2951 ND1 HIS A 539 4447 4576 4660 -441 250 121 N ATOM 2952 CD2 HIS A 539 58.352 39.758 11.941 1.00 39.53 C ANISOU 2952 CD2 HIS A 539 5028 5001 4991 -411 278 165 C ATOM 2953 CE1 HIS A 539 60.320 39.563 12.891 1.00 40.68 C ANISOU 2953 CE1 HIS A 539 5020 5206 5228 -491 324 144 C ATOM 2954 NE2 HIS A 539 59.712 39.753 11.734 1.00 38.48 N ANISOU 2954 NE2 HIS A 539 4825 4921 4876 -477 345 175 N ATOM 2955 N SER A 540 57.632 37.528 16.333 1.00 18.00 N ANISOU 2955 N SER A 540 2100 2314 2427 -309 102 41 N ATOM 2956 CA SER A 540 58.653 36.839 17.094 1.00 19.87 C ANISOU 2956 CA SER A 540 2246 2589 2717 -320 99 30 C ATOM 2957 C SER A 540 58.426 35.333 17.135 1.00 18.10 C ANISOU 2957 C SER A 540 1986 2387 2504 -267 79 18 C ATOM 2958 O SER A 540 59.384 34.553 17.007 1.00 20.65 O ANISOU 2958 O SER A 540 2244 2737 2866 -259 93 4 O ATOM 2959 CB SER A 540 58.729 37.407 18.510 1.00 26.55 C ANISOU 2959 CB SER A 540 3063 3435 3588 -346 49 21 C ATOM 2960 OG SER A 540 59.704 36.705 19.246 1.00 32.31 O ANISOU 2960 OG SER A 540 3709 4202 4365 -350 37 13 O ATOM 2961 N ARG A 541 57.175 34.916 17.320 1.00 17.41 N ANISOU 2961 N ARG A 541 1936 2288 2390 -232 41 17 N ATOM 2962 CA ARG A 541 56.870 33.480 17.358 1.00 19.03 C ANISOU 2962 CA ARG A 541 2116 2499 2614 -191 13 12 C ATOM 2963 C ARG A 541 57.142 32.854 16.006 1.00 19.63 C ANISOU 2963 C ARG A 541 2192 2576 2691 -155 53 -9 C ATOM 2964 O ARG A 541 57.755 31.789 15.918 1.00 16.78 O ANISOU 2964 O ARG A 541 1777 2222 2376 -129 42 -27 O ATOM 2965 CB ARG A 541 55.420 33.205 17.780 1.00 17.48 C ANISOU 2965 CB ARG A 541 1956 2298 2388 -175 -30 14 C ATOM 2966 CG ARG A 541 55.096 31.700 17.898 1.00 15.29 C ANISOU 2966 CG ARG A 541 1655 2015 2142 -148 -67 19 C ATOM 2967 CD ARG A 541 55.965 31.009 18.975 1.00 21.45 C ANISOU 2967 CD ARG A 541 2374 2805 2973 -165 -109 45 C ATOM 2968 NE ARG A 541 55.644 31.592 20.274 1.00 23.21 N ANISOU 2968 NE ARG A 541 2592 3060 3165 -205 -138 67 N ATOM 2969 CZ ARG A 541 54.792 31.065 21.148 1.00 25.28 C ANISOU 2969 CZ ARG A 541 2854 3343 3406 -222 -182 93 C ATOM 2970 NH1 ARG A 541 54.215 29.892 20.901 1.00 21.39 N ANISOU 2970 NH1 ARG A 541 2369 2825 2933 -209 -209 111 N ATOM 2971 NH2 ARG A 541 54.530 31.705 22.281 1.00 22.38 N ANISOU 2971 NH2 ARG A 541 2477 3029 2999 -257 -201 101 N ATOM 2972 N VAL A 542 56.687 33.515 14.941 1.00 17.44 N ANISOU 2972 N VAL A 542 1975 2292 2360 -150 92 -12 N ATOM 2973 CA VAL A 542 56.866 32.961 13.602 1.00 16.90 C ANISOU 2973 CA VAL A 542 1907 2241 2272 -113 132 -38 C ATOM 2974 C VAL A 542 58.349 32.860 13.250 1.00 20.07 C ANISOU 2974 C VAL A 542 2240 2687 2700 -133 181 -53 C ATOM 2975 O VAL A 542 58.780 31.890 12.629 1.00 18.44 O ANISOU 2975 O VAL A 542 1985 2509 2513 -91 190 -97 O ATOM 2976 CB VAL A 542 56.120 33.775 12.551 1.00 19.32 C ANISOU 2976 CB VAL A 542 2299 2540 2504 -106 161 -29 C ATOM 2977 CG1 VAL A 542 56.521 33.335 11.148 1.00 23.83 C ANISOU 2977 CG1 VAL A 542 2863 3153 3039 -77 212 -56 C ATOM 2978 CG2 VAL A 542 54.609 33.629 12.766 1.00 19.05 C ANISOU 2978 CG2 VAL A 542 2314 2474 2448 -70 108 -39 C ATOM 2979 N THR A 543 59.126 33.853 13.675 1.00 18.83 N ANISOU 2979 N THR A 543 2069 2538 2549 -195 206 -29 N ATOM 2980 CA THR A 543 60.566 33.840 13.459 1.00 24.45 C ANISOU 2980 CA THR A 543 2701 3300 3289 -225 254 -49 C ATOM 2981 C THR A 543 61.222 32.650 14.158 1.00 20.64 C ANISOU 2981 C THR A 543 2128 2830 2883 -186 209 -89 C ATOM 2982 O THR A 543 61.994 31.904 13.551 1.00 21.46 O ANISOU 2982 O THR A 543 2164 2980 3010 -155 230 -141 O ATOM 2983 CB THR A 543 61.223 35.151 13.959 1.00 30.66 C ANISOU 2983 CB THR A 543 3486 4081 4081 -307 278 -16 C ATOM 2984 OG1 THR A 543 60.751 36.245 13.168 1.00 28.85 O ANISOU 2984 OG1 THR A 543 3345 3831 3787 -345 315 26 O ATOM 2985 CG2 THR A 543 62.745 35.076 13.855 1.00 35.63 C ANISOU 2985 CG2 THR A 543 4016 4774 4749 -343 326 -46 C ATOM 2986 N LYS A 544 60.922 32.483 15.436 1.00 21.01 N ANISOU 2986 N LYS A 544 2173 2842 2968 -186 141 -68 N ATOM 2987 CA LYS A 544 61.481 31.390 16.229 1.00 20.76 C ANISOU 2987 CA LYS A 544 2070 2808 3007 -152 79 -90 C ATOM 2988 C LYS A 544 61.100 30.013 15.697 1.00 18.61 C ANISOU 2988 C LYS A 544 1792 2518 2762 -81 43 -121 C ATOM 2989 O LYS A 544 61.907 29.090 15.719 1.00 19.80 O ANISOU 2989 O LYS A 544 1872 2676 2976 -41 11 -165 O ATOM 2990 CB LYS A 544 60.992 31.499 17.670 1.00 19.83 C ANISOU 2990 CB LYS A 544 1971 2663 2900 -171 12 -47 C ATOM 2991 CG LYS A 544 61.619 32.645 18.465 1.00 24.62 C ANISOU 2991 CG LYS A 544 2558 3290 3508 -230 23 -35 C ATOM 2992 CD LYS A 544 60.924 32.742 19.818 1.00 25.01 C ANISOU 2992 CD LYS A 544 2629 3328 3546 -241 -43 -1 C ATOM 2993 CE LYS A 544 61.459 33.879 20.646 1.00 34.30 C ANISOU 2993 CE LYS A 544 3784 4524 4725 -291 -43 -3 C ATOM 2994 NZ LYS A 544 60.723 33.964 21.940 1.00 30.48 N ANISOU 2994 NZ LYS A 544 3316 4051 4214 -298 -105 19 N ATOM 2995 N GLU A 545 59.859 29.877 15.246 1.00 18.11 N ANISOU 2995 N GLU A 545 1798 2425 2657 -62 38 -107 N ATOM 2996 CA GLU A 545 59.338 28.585 14.805 1.00 18.80 C ANISOU 2996 CA GLU A 545 1885 2482 2777 0 -7 -137 C ATOM 2997 C GLU A 545 59.284 28.414 13.284 1.00 17.45 C ANISOU 2997 C GLU A 545 1717 2342 2571 42 46 -194 C ATOM 2998 O GLU A 545 58.549 27.569 12.776 1.00 17.83 O ANISOU 2998 O GLU A 545 1783 2361 2629 92 14 -222 O ATOM 2999 CB GLU A 545 57.970 28.346 15.443 1.00 18.28 C ANISOU 2999 CB GLU A 545 1879 2368 2699 -7 -59 -91 C ATOM 3000 CG GLU A 545 58.082 27.726 16.853 1.00 21.93 C ANISOU 3000 CG GLU A 545 2317 2800 3213 -24 -139 -47 C ATOM 3001 CD GLU A 545 58.625 26.298 16.805 1.00 27.13 C ANISOU 3001 CD GLU A 545 2928 3419 3961 27 -207 -75 C ATOM 3002 OE1 GLU A 545 59.863 26.118 16.739 1.00 26.95 O ANISOU 3002 OE1 GLU A 545 2840 3415 3985 51 -209 -115 O ATOM 3003 OE2 GLU A 545 57.814 25.343 16.813 1.00 27.03 O ANISOU 3003 OE2 GLU A 545 2940 3353 3978 46 -263 -63 O ATOM 3004 N ARG A 546 60.073 29.203 12.564 1.00 20.29 N ANISOU 3004 N ARG A 546 2297 2978 2434 -382 -17 159 N ATOM 3005 CA ARG A 546 59.991 29.216 11.108 1.00 20.92 C ANISOU 3005 CA ARG A 546 2461 3061 2425 -346 49 147 C ATOM 3006 C ARG A 546 60.235 27.853 10.469 1.00 21.13 C ANISOU 3006 C ARG A 546 2410 3146 2472 -225 73 97 C ATOM 3007 O ARG A 546 59.594 27.512 9.484 1.00 21.09 O ANISOU 3007 O ARG A 546 2492 3104 2416 -143 78 72 O ATOM 3008 CB ARG A 546 60.933 30.262 10.513 1.00 22.09 C ANISOU 3008 CB ARG A 546 2629 3263 2503 -466 149 185 C ATOM 3009 CG ARG A 546 62.405 30.005 10.780 1.00 24.17 C ANISOU 3009 CG ARG A 546 2724 3653 2808 -519 218 184 C ATOM 3010 CD ARG A 546 63.252 31.135 10.200 1.00 33.92 C ANISOU 3010 CD ARG A 546 3989 4931 3970 -648 320 221 C ATOM 3011 NE ARG A 546 64.676 30.957 10.477 1.00 41.93 N ANISOU 3011 NE ARG A 546 4837 6065 5028 -706 388 215 N ATOM 3012 CZ ARG A 546 65.249 31.205 11.653 1.00 49.10 C ANISOU 3012 CZ ARG A 546 5641 7006 6010 -775 360 229 C ATOM 3013 NH1 ARG A 546 64.521 31.636 12.677 1.00 39.81 N ANISOU 3013 NH1 ARG A 546 4507 5750 4868 -796 269 253 N ATOM 3014 NH2 ARG A 546 66.555 31.017 11.808 1.00 56.24 N ANISOU 3014 NH2 ARG A 546 6395 8021 6954 -821 424 216 N ATOM 3015 N HIS A 547 61.158 27.071 11.015 1.00 21.39 N ANISOU 3015 N HIS A 547 2279 3268 2579 -211 84 81 N ATOM 3016 CA HIS A 547 61.439 25.768 10.411 1.00 21.64 C ANISOU 3016 CA HIS A 547 2231 3358 2634 -97 105 31 C ATOM 3017 C HIS A 547 60.257 24.820 10.501 1.00 20.59 C ANISOU 3017 C HIS A 547 2140 3148 2536 34 20 -6 C ATOM 3018 O HIS A 547 59.876 24.203 9.497 1.00 20.68 O ANISOU 3018 O HIS A 547 2194 3151 2513 128 37 -41 O ATOM 3019 CB HIS A 547 62.705 25.143 11.000 1.00 22.20 C ANISOU 3019 CB HIS A 547 2115 3539 2779 -109 130 18 C ATOM 3020 CG HIS A 547 63.958 25.849 10.574 1.00 24.43 C ANISOU 3020 CG HIS A 547 2344 3915 3023 -217 235 36 C ATOM 3021 ND1 HIS A 547 64.652 26.702 11.406 1.00 33.28 N ANISOU 3021 ND1 HIS A 547 3413 5065 4167 -339 245 72 N ATOM 3022 CD2 HIS A 547 64.611 25.859 9.391 1.00 29.63 C ANISOU 3022 CD2 HIS A 547 2998 4640 3618 -224 337 21 C ATOM 3023 CE1 HIS A 547 65.693 27.192 10.758 1.00 32.46 C ANISOU 3023 CE1 HIS A 547 3271 5043 4020 -417 350 78 C ATOM 3024 NE2 HIS A 547 65.695 26.697 9.534 1.00 35.35 N ANISOU 3024 NE2 HIS A 547 3665 5433 4332 -352 409 48 N ATOM 3025 N ARG A 548 59.657 24.704 11.679 1.00 19.62 N ANISOU 3025 N ARG A 548 2008 2966 2480 40 -71 0 N ATOM 3026 CA ARG A 548 58.451 23.880 11.780 1.00 20.03 C ANISOU 3026 CA ARG A 548 2111 2935 2565 156 -150 -37 C ATOM 3027 C ARG A 548 57.295 24.477 10.986 1.00 20.62 C ANISOU 3027 C ARG A 548 2359 2912 2565 175 -164 -39 C ATOM 3028 O ARG A 548 56.550 23.753 10.325 1.00 18.17 O ANISOU 3028 O ARG A 548 2096 2561 2246 285 -184 -81 O ATOM 3029 CB ARG A 548 58.043 23.648 13.237 1.00 18.92 C ANISOU 3029 CB ARG A 548 1929 2750 2510 152 -241 -31 C ATOM 3030 CG ARG A 548 58.629 22.359 13.833 1.00 21.89 C ANISOU 3030 CG ARG A 548 2155 3188 2974 221 -264 -57 C ATOM 3031 CD ARG A 548 58.261 22.197 15.309 1.00 23.56 C ANISOU 3031 CD ARG A 548 2334 3355 3262 207 -351 -46 C ATOM 3032 NE ARG A 548 59.145 22.992 16.146 1.00 22.71 N ANISOU 3032 NE ARG A 548 2164 3297 3169 89 -339 -4 N ATOM 3033 CZ ARG A 548 60.313 22.568 16.624 1.00 25.38 C ANISOU 3033 CZ ARG A 548 2359 3727 3556 72 -322 -3 C ATOM 3034 NH1 ARG A 548 60.747 21.325 16.374 1.00 20.66 N ANISOU 3034 NH1 ARG A 548 1666 3183 3001 169 -319 -41 N ATOM 3035 NH2 ARG A 548 61.050 23.390 17.367 1.00 18.88 N ANISOU 3035 NH2 ARG A 548 1489 2942 2743 -40 -313 34 N ATOM 3036 N LEU A 549 57.127 25.792 11.054 1.00 18.67 N ANISOU 3036 N LEU A 549 2206 2623 2265 71 -156 2 N ATOM 3037 CA LEU A 549 56.016 26.421 10.342 1.00 18.04 C ANISOU 3037 CA LEU A 549 2296 2445 2115 87 -178 -1 C ATOM 3038 C LEU A 549 56.114 26.228 8.832 1.00 18.79 C ANISOU 3038 C LEU A 549 2449 2562 2127 142 -111 -21 C ATOM 3039 O LEU A 549 55.102 26.069 8.144 1.00 20.42 O ANISOU 3039 O LEU A 549 2765 2694 2298 222 -143 -51 O ATOM 3040 CB LEU A 549 55.934 27.909 10.687 1.00 18.11 C ANISOU 3040 CB LEU A 549 2390 2409 2080 -41 -180 50 C ATOM 3041 CG LEU A 549 55.394 28.203 12.086 1.00 17.89 C ANISOU 3041 CG LEU A 549 2353 2323 2122 -81 -265 61 C ATOM 3042 CD1 LEU A 549 55.669 29.678 12.446 1.00 18.47 C ANISOU 3042 CD1 LEU A 549 2479 2380 2157 -223 -250 115 C ATOM 3043 CD2 LEU A 549 53.914 27.859 12.137 1.00 20.35 C ANISOU 3043 CD2 LEU A 549 2759 2523 2451 10 -350 21 C ATOM 3044 N SER A 550 57.334 26.226 8.310 1.00 19.85 N ANISOU 3044 N SER A 550 2509 2802 2233 100 -18 -8 N ATOM 3045 CA SER A 550 57.521 26.125 6.860 1.00 20.76 C ANISOU 3045 CA SER A 550 2681 2946 2261 139 56 -24 C ATOM 3046 C SER A 550 57.135 24.741 6.317 1.00 23.48 C ANISOU 3046 C SER A 550 2990 3297 2632 289 38 -85 C ATOM 3047 O SER A 550 57.065 24.535 5.102 1.00 20.96 O ANISOU 3047 O SER A 550 2732 2989 2245 343 84 -108 O ATOM 3048 CB SER A 550 58.955 26.503 6.481 1.00 25.09 C ANISOU 3048 CB SER A 550 3153 3608 2773 47 167 1 C ATOM 3049 OG SER A 550 59.884 25.550 6.968 1.00 32.91 O ANISOU 3049 OG SER A 550 3964 4695 3844 72 184 -21 O ATOM 3050 N ARG A 551 56.868 23.794 7.215 1.00 19.63 N ANISOU 3050 N ARG A 551 2411 2801 2245 356 -31 -113 N ATOM 3051 CA ARG A 551 56.402 22.473 6.786 1.00 19.30 C ANISOU 3051 CA ARG A 551 2340 2753 2238 500 -58 -172 C ATOM 3052 C ARG A 551 54.947 22.514 6.317 1.00 22.74 C ANISOU 3052 C ARG A 551 2925 3073 2643 577 -121 -199 C ATOM 3053 O ARG A 551 54.477 21.586 5.669 1.00 20.36 O ANISOU 3053 O ARG A 551 2631 2758 2346 695 -134 -250 O ATOM 3054 CB ARG A 551 56.518 21.463 7.955 1.00 20.07 C ANISOU 3054 CB ARG A 551 2303 2868 2453 545 -118 -190 C ATOM 3055 CG ARG A 551 57.934 21.148 8.364 1.00 20.12 C ANISOU 3055 CG ARG A 551 2148 2993 2503 501 -67 -179 C ATOM 3056 CD ARG A 551 57.964 20.276 9.628 1.00 20.15 C ANISOU 3056 CD ARG A 551 2038 2999 2619 537 -139 -190 C ATOM 3057 NE ARG A 551 57.070 19.133 9.513 1.00 23.55 N ANISOU 3057 NE ARG A 551 2480 3376 3093 672 -198 -241 N ATOM 3058 CZ ARG A 551 56.658 18.403 10.542 1.00 26.11 C ANISOU 3058 CZ ARG A 551 2754 3664 3505 717 -275 -254 C ATOM 3059 NH1 ARG A 551 57.070 18.701 11.769 1.00 18.78 N ANISOU 3059 NH1 ARG A 551 1762 2748 2627 640 -306 -219 N ATOM 3060 NH2 ARG A 551 55.832 17.384 10.338 1.00 25.12 N ANISOU 3060 NH2 ARG A 551 2644 3487 3413 837 -322 -301 N ATOM 3061 N PHE A 552 54.231 23.578 6.665 1.00 18.13 N ANISOU 3061 N PHE A 552 2455 2403 2031 511 -162 -171 N ATOM 3062 CA PHE A 552 52.778 23.616 6.471 1.00 19.17 C ANISOU 3062 CA PHE A 552 2715 2415 2154 582 -239 -203 C ATOM 3063 C PHE A 552 52.345 24.786 5.612 1.00 18.73 C ANISOU 3063 C PHE A 552 2824 2301 1991 536 -222 -182 C ATOM 3064 O PHE A 552 52.924 25.866 5.699 1.00 18.23 O ANISOU 3064 O PHE A 552 2789 2258 1881 418 -181 -129 O ATOM 3065 CB PHE A 552 52.073 23.717 7.825 1.00 18.41 C ANISOU 3065 CB PHE A 552 2608 2247 2138 560 -327 -200 C ATOM 3066 CG PHE A 552 52.356 22.565 8.726 1.00 20.72 C ANISOU 3066 CG PHE A 552 2757 2580 2535 609 -355 -221 C ATOM 3067 CD1 PHE A 552 51.614 21.397 8.627 1.00 28.13 C ANISOU 3067 CD1 PHE A 552 3681 3482 3525 736 -403 -279 C ATOM 3068 CD2 PHE A 552 53.379 22.632 9.653 1.00 18.66 C ANISOU 3068 CD2 PHE A 552 2376 2393 2320 529 -336 -183 C ATOM 3069 CE1 PHE A 552 51.887 20.313 9.452 1.00 31.63 C ANISOU 3069 CE1 PHE A 552 3997 3958 4062 781 -429 -296 C ATOM 3070 CE2 PHE A 552 53.668 21.558 10.476 1.00 18.35 C ANISOU 3070 CE2 PHE A 552 2209 2390 2374 576 -365 -201 C ATOM 3071 CZ PHE A 552 52.912 20.388 10.373 1.00 24.21 C ANISOU 3071 CZ PHE A 552 2944 3092 3165 702 -412 -256 C ATOM 3072 N SER A 553 51.302 24.583 4.808 1.00 17.44 N ANISOU 3072 N SER A 553 2773 2061 1792 631 -260 -225 N ATOM 3073 CA SER A 553 50.739 25.669 4.034 1.00 17.73 C ANISOU 3073 CA SER A 553 2980 2027 1730 599 -262 -210 C ATOM 3074 C SER A 553 50.408 26.896 4.887 1.00 17.41 C ANISOU 3074 C SER A 553 3002 1921 1692 489 -305 -167 C ATOM 3075 O SER A 553 50.690 28.023 4.481 1.00 18.63 O ANISOU 3075 O SER A 553 3246 2068 1764 399 -268 -122 O ATOM 3076 CB SER A 553 49.476 25.201 3.282 1.00 19.68 C ANISOU 3076 CB SER A 553 3333 2185 1961 728 -322 -273 C ATOM 3077 OG SER A 553 49.808 24.225 2.309 1.00 20.21 O ANISOU 3077 OG SER A 553 3362 2312 2007 823 -274 -309 O ATOM 3078 N SER A 554 49.791 26.681 6.047 1.00 17.01 N ANISOU 3078 N SER A 554 2909 1820 1732 496 -383 -183 N ATOM 3079 CA SER A 554 49.412 27.794 6.924 1.00 16.76 C ANISOU 3079 CA SER A 554 2934 1725 1712 397 -430 -150 C ATOM 3080 C SER A 554 50.645 28.548 7.424 1.00 17.72 C ANISOU 3080 C SER A 554 2988 1925 1820 260 -367 -82 C ATOM 3081 O SER A 554 50.622 29.778 7.548 1.00 16.75 O ANISOU 3081 O SER A 554 2947 1764 1652 161 -368 -40 O ATOM 3082 CB SER A 554 48.624 27.286 8.129 1.00 15.83 C ANISOU 3082 CB SER A 554 2764 1552 1699 431 -517 -182 C ATOM 3083 OG SER A 554 49.384 26.340 8.868 1.00 17.76 O ANISOU 3083 OG SER A 554 2847 1879 2022 440 -498 -180 O ATOM 3084 N GLY A 555 51.710 27.807 7.724 1.00 17.10 N ANISOU 3084 N GLY A 555 2758 1953 1785 256 -315 -73 N ATOM 3085 CA GLY A 555 52.957 28.416 8.165 1.00 17.94 C ANISOU 3085 CA GLY A 555 2786 2144 1888 133 -250 -17 C ATOM 3086 C GLY A 555 53.606 29.236 7.068 1.00 19.23 C ANISOU 3086 C GLY A 555 3023 2343 1942 68 -163 18 C ATOM 3087 O GLY A 555 54.060 30.361 7.289 1.00 19.11 O ANISOU 3087 O GLY A 555 3040 2331 1891 -53 -134 69 O ATOM 3088 N LYS A 556 53.663 28.672 5.869 1.00 19.22 N ANISOU 3088 N LYS A 556 3050 2366 1885 148 -118 -10 N ATOM 3089 CA LYS A 556 54.188 29.432 4.739 1.00 21.16 C ANISOU 3089 CA LYS A 556 3384 2637 2018 91 -33 20 C ATOM 3090 C LYS A 556 53.378 30.706 4.483 1.00 22.64 C ANISOU 3090 C LYS A 556 3752 2718 2132 38 -71 47 C ATOM 3091 O LYS A 556 53.949 31.749 4.153 1.00 22.50 O ANISOU 3091 O LYS A 556 3793 2713 2041 -69 -12 97 O ATOM 3092 CB LYS A 556 54.290 28.549 3.491 1.00 20.89 C ANISOU 3092 CB LYS A 556 3356 2644 1936 195 15 -20 C ATOM 3093 CG LYS A 556 55.516 27.622 3.552 1.00 23.52 C ANISOU 3093 CG LYS A 556 3512 3108 2315 205 88 -31 C ATOM 3094 CD LYS A 556 55.556 26.641 2.385 1.00 35.58 C ANISOU 3094 CD LYS A 556 5037 4676 3807 318 129 -79 C ATOM 3095 CE LYS A 556 54.450 25.614 2.507 1.00 45.29 C ANISOU 3095 CE LYS A 556 6269 5840 5098 460 38 -138 C ATOM 3096 NZ LYS A 556 54.570 24.543 1.475 1.00 52.36 N ANISOU 3096 NZ LYS A 556 7137 6783 5973 574 75 -188 N ATOM 3097 N LYS A 557 52.059 30.636 4.658 1.00 19.36 N ANISOU 3097 N LYS A 557 3422 2193 1739 111 -170 12 N ATOM 3098 CA LYS A 557 51.220 31.818 4.457 1.00 19.80 C ANISOU 3098 CA LYS A 557 3649 2140 1734 70 -218 29 C ATOM 3099 C LYS A 557 51.538 32.914 5.474 1.00 19.45 C ANISOU 3099 C LYS A 557 3594 2085 1711 -68 -227 83 C ATOM 3100 O LYS A 557 51.535 34.094 5.132 1.00 24.52 O ANISOU 3100 O LYS A 557 4353 2685 2278 -151 -214 123 O ATOM 3101 CB LYS A 557 49.726 31.478 4.546 1.00 27.13 C ANISOU 3101 CB LYS A 557 4656 2955 2697 177 -327 -29 C ATOM 3102 CG LYS A 557 49.135 30.659 3.395 1.00 41.76 C ANISOU 3102 CG LYS A 557 6569 4786 4511 314 -334 -85 C ATOM 3103 CD LYS A 557 47.647 30.413 3.666 1.00 49.21 C ANISOU 3103 CD LYS A 557 7580 5613 5504 407 -448 -146 C ATOM 3104 CE LYS A 557 47.017 29.468 2.654 1.00 64.33 C ANISOU 3104 CE LYS A 557 9536 7506 7399 552 -464 -211 C ATOM 3105 NZ LYS A 557 45.557 29.255 2.920 1.00 67.26 N ANISOU 3105 NZ LYS A 557 9970 7762 7822 640 -574 -276 N ATOM 3106 N MET A 558 51.810 32.539 6.720 1.00 19.53 N ANISOU 3106 N MET A 558 3467 2130 1822 -92 -253 83 N ATOM 3107 CA MET A 558 52.108 33.543 7.748 1.00 18.45 C ANISOU 3107 CA MET A 558 3313 1985 1712 -220 -266 131 C ATOM 3108 C MET A 558 53.455 34.170 7.482 1.00 21.73 C ANISOU 3108 C MET A 558 3689 2491 2076 -336 -162 187 C ATOM 3109 O MET A 558 53.641 35.378 7.619 1.00 20.05 O ANISOU 3109 O MET A 558 3544 2252 1823 -447 -150 233 O ATOM 3110 CB MET A 558 52.095 32.923 9.157 1.00 17.55 C ANISOU 3110 CB MET A 558 3061 1890 1716 -214 -318 116 C ATOM 3111 CG MET A 558 50.706 32.512 9.591 1.00 19.58 C ANISOU 3111 CG MET A 558 3366 2047 2028 -125 -423 63 C ATOM 3112 SD MET A 558 50.599 32.285 11.379 1.00 23.89 S ANISOU 3112 SD MET A 558 3792 2591 2694 -161 -490 62 S ATOM 3113 CE MET A 558 51.677 30.878 11.606 1.00 21.01 C ANISOU 3113 CE MET A 558 3239 2352 2391 -111 -437 53 C ATOM 3114 N ILE A 559 54.409 33.336 7.102 1.00 21.26 N ANISOU 3114 N ILE A 559 3516 2538 2022 -309 -85 179 N ATOM 3115 CA ILE A 559 55.730 33.827 6.748 1.00 24.97 C ANISOU 3115 CA ILE A 559 3940 3102 2445 -412 24 223 C ATOM 3116 C ILE A 559 55.634 34.821 5.595 1.00 29.22 C ANISOU 3116 C ILE A 559 4646 3598 2859 -459 71 252 C ATOM 3117 O ILE A 559 56.268 35.878 5.630 1.00 29.68 O ANISOU 3117 O ILE A 559 4733 3671 2875 -586 122 303 O ATOM 3118 CB ILE A 559 56.669 32.653 6.405 1.00 23.56 C ANISOU 3118 CB ILE A 559 3617 3041 2293 -357 95 196 C ATOM 3119 CG1 ILE A 559 56.950 31.857 7.682 1.00 24.55 C ANISOU 3119 CG1 ILE A 559 3574 3212 2541 -337 51 179 C ATOM 3120 CG2 ILE A 559 57.952 33.151 5.758 1.00 28.53 C ANISOU 3120 CG2 ILE A 559 4220 3764 2858 -454 217 231 C ATOM 3121 CD1 ILE A 559 57.555 30.505 7.453 1.00 28.41 C ANISOU 3121 CD1 ILE A 559 3927 3794 3074 -249 87 139 C ATOM 3122 N GLU A 560 54.811 34.492 4.595 1.00 23.90 N ANISOU 3122 N GLU A 560 4087 2867 2127 -358 49 220 N ATOM 3123 CA GLU A 560 54.600 35.368 3.435 1.00 25.51 C ANISOU 3123 CA GLU A 560 4468 3019 2205 -387 83 244 C ATOM 3124 C GLU A 560 53.894 36.674 3.814 1.00 26.61 C ANISOU 3124 C GLU A 560 4743 3049 2319 -462 18 277 C ATOM 3125 O GLU A 560 54.244 37.747 3.318 1.00 29.96 O ANISOU 3125 O GLU A 560 5269 3458 2657 -560 67 326 O ATOM 3126 CB GLU A 560 53.772 34.654 2.369 1.00 27.43 C ANISOU 3126 CB GLU A 560 4802 3218 2401 -248 57 194 C ATOM 3127 CG GLU A 560 53.238 35.590 1.287 1.00 47.70 C ANISOU 3127 CG GLU A 560 7579 5702 4843 -262 58 214 C ATOM 3128 CD GLU A 560 52.233 34.915 0.358 1.00 63.95 C ANISOU 3128 CD GLU A 560 9734 7699 6864 -116 9 158 C ATOM 3129 OE1 GLU A 560 52.128 35.347 -0.811 1.00 68.34 O ANISOU 3129 OE1 GLU A 560 10435 8226 7304 -110 42 169 O ATOM 3130 OE2 GLU A 560 51.548 33.959 0.796 1.00 64.43 O ANISOU 3130 OE2 GLU A 560 9730 7740 7009 -8 -63 102 O ATOM 3131 N THR A 561 52.872 36.566 4.652 1.00 22.63 N ANISOU 3131 N THR A 561 4246 2465 1888 -415 -93 248 N ATOM 3132 CA THR A 561 52.171 37.735 5.174 1.00 26.37 C ANISOU 3132 CA THR A 561 4828 2835 2356 -482 -165 271 C ATOM 3133 C THR A 561 53.144 38.711 5.841 1.00 27.28 C ANISOU 3133 C THR A 561 4894 2995 2476 -639 -114 334 C ATOM 3134 O THR A 561 53.118 39.917 5.571 1.00 28.49 O ANISOU 3134 O THR A 561 5169 3095 2560 -728 -106 376 O ATOM 3135 CB THR A 561 51.069 37.322 6.173 1.00 30.42 C ANISOU 3135 CB THR A 561 5314 3277 2969 -413 -283 224 C ATOM 3136 OG1 THR A 561 50.072 36.547 5.491 1.00 31.03 O ANISOU 3136 OG1 THR A 561 5455 3297 3036 -272 -335 164 O ATOM 3137 CG2 THR A 561 50.416 38.553 6.793 1.00 34.62 C ANISOU 3137 CG2 THR A 561 5943 3709 3501 -490 -355 245 C ATOM 3138 N LEU A 562 54.007 38.195 6.710 1.00 25.36 N ANISOU 3138 N LEU A 562 4473 2849 2315 -672 -81 339 N ATOM 3139 CA LEU A 562 55.008 39.042 7.362 1.00 24.30 C ANISOU 3139 CA LEU A 562 4275 2767 2193 -818 -30 393 C ATOM 3140 C LEU A 562 56.034 39.613 6.384 1.00 32.70 C ANISOU 3140 C LEU A 562 5376 3889 3159 -903 90 435 C ATOM 3141 O LEU A 562 56.397 40.789 6.475 1.00 32.34 O ANISOU 3141 O LEU A 562 5388 3825 3074 -1026 119 485 O ATOM 3142 CB LEU A 562 55.692 38.282 8.506 1.00 23.00 C ANISOU 3142 CB LEU A 562 3908 2691 2139 -824 -28 382 C ATOM 3143 CG LEU A 562 54.796 38.117 9.738 1.00 20.30 C ANISOU 3143 CG LEU A 562 3538 2285 1891 -791 -142 357 C ATOM 3144 CD1 LEU A 562 55.295 36.986 10.653 1.00 23.10 C ANISOU 3144 CD1 LEU A 562 3704 2722 2349 -750 -148 332 C ATOM 3145 CD2 LEU A 562 54.722 39.436 10.508 1.00 21.64 C ANISOU 3145 CD2 LEU A 562 3756 2403 2065 -914 -174 399 C ATOM 3146 N ALA A 563 56.492 38.789 5.444 1.00 28.59 N ANISOU 3146 N ALA A 563 4825 3438 2601 -839 162 415 N ATOM 3147 CA ALA A 563 57.406 39.253 4.399 1.00 32.83 C ANISOU 3147 CA ALA A 563 5406 4029 3038 -912 282 449 C ATOM 3148 C ALA A 563 56.804 40.386 3.563 1.00 36.90 C ANISOU 3148 C ALA A 563 6139 4442 3438 -951 274 481 C ATOM 3149 O ALA A 563 57.485 41.362 3.253 1.00 44.71 O ANISOU 3149 O ALA A 563 7181 5444 4361 -1073 348 532 O ATOM 3150 CB ALA A 563 57.818 38.096 3.499 1.00 33.98 C ANISOU 3150 CB ALA A 563 5493 4257 3163 -819 348 410 C ATOM 3151 N ASN A 564 55.531 40.256 3.198 1.00 31.04 N ANISOU 3151 N ASN A 564 5525 3596 2673 -849 183 451 N ATOM 3152 CA ASN A 564 54.861 41.266 2.376 1.00 38.60 C ANISOU 3152 CA ASN A 564 6698 4446 3522 -869 160 476 C ATOM 3153 C ASN A 564 54.716 42.597 3.100 1.00 43.42 C ANISOU 3153 C ASN A 564 7373 4987 4138 -988 119 522 C ATOM 3154 O ASN A 564 54.706 43.659 2.472 1.00 39.83 O ANISOU 3154 O ASN A 564 7071 4477 3586 -1061 142 564 O ATOM 3155 CB ASN A 564 53.476 40.789 1.935 1.00 45.04 C ANISOU 3155 CB ASN A 564 7622 5163 4327 -725 58 423 C ATOM 3156 CG ASN A 564 53.540 39.693 0.902 1.00 51.77 C ANISOU 3156 CG ASN A 564 8465 6066 5141 -612 102 383 C ATOM 3157 OD1 ASN A 564 54.596 39.437 0.319 1.00 51.41 O ANISOU 3157 OD1 ASN A 564 8362 6119 5052 -647 216 399 O ATOM 3158 ND2 ASN A 564 52.408 39.032 0.668 1.00 51.41 N ANISOU 3158 ND2 ASN A 564 8470 5952 5112 -474 13 325 N ATOM 3159 N LEU A 565 54.591 42.532 4.420 1.00 39.33 N ANISOU 3159 N LEU A 565 6742 4471 3731 -1007 57 512 N ATOM 3160 CA LEU A 565 54.443 43.736 5.223 1.00 43.83 C ANISOU 3160 CA LEU A 565 7357 4978 4318 -1116 12 550 C ATOM 3161 C LEU A 565 55.727 44.565 5.222 1.00 53.49 C ANISOU 3161 C LEU A 565 8546 6271 5506 -1270 120 612 C ATOM 3162 O LEU A 565 55.680 45.783 5.043 1.00 48.71 O ANISOU 3162 O LEU A 565 8067 5602 4840 -1365 122 657 O ATOM 3163 CB LEU A 565 54.026 43.384 6.653 1.00 37.67 C ANISOU 3163 CB LEU A 565 6456 4190 3666 -1095 -77 522 C ATOM 3164 CG LEU A 565 53.681 44.574 7.546 1.00 36.41 C ANISOU 3164 CG LEU A 565 6346 3955 3533 -1193 -142 550 C ATOM 3165 CD1 LEU A 565 52.563 45.392 6.939 1.00 38.53 C ANISOU 3165 CD1 LEU A 565 6823 4088 3730 -1171 -215 548 C ATOM 3166 CD2 LEU A 565 53.306 44.107 8.938 1.00 36.73 C ANISOU 3166 CD2 LEU A 565 6260 3997 3697 -1167 -222 518 C ATOM 3167 N ARG A 566 56.866 43.900 5.412 1.00 67.62 N ANISOU 3167 N ARG A 566 10166 8189 7336 -1294 209 611 N ATOM 3168 CA ARG A 566 58.170 44.567 5.394 1.00 85.09 C ANISOU 3168 CA ARG A 566 12326 10481 9524 -1437 321 660 C ATOM 3169 C ARG A 566 58.294 45.502 4.196 1.00 89.04 C ANISOU 3169 C ARG A 566 13004 10937 9888 -1503 388 703 C ATOM 3170 O ARG A 566 58.483 46.709 4.350 1.00 94.56 O ANISOU 3170 O ARG A 566 13781 11594 10554 -1623 400 752 O ATOM 3171 CB ARG A 566 59.305 43.544 5.330 1.00 96.61 C ANISOU 3171 CB ARG A 566 13602 12083 11022 -1422 417 639 C ATOM 3172 CG ARG A 566 59.032 42.238 6.046 1.00106.64 C ANISOU 3172 CG ARG A 566 14726 13392 12400 -1305 354 584 C ATOM 3173 CD ARG A 566 59.485 42.272 7.492 1.00113.71 C ANISOU 3173 CD ARG A 566 15465 14331 13409 -1364 323 589 C ATOM 3174 NE ARG A 566 59.342 40.961 8.118 1.00116.46 N ANISOU 3174 NE ARG A 566 15671 14724 13853 -1255 275 538 N ATOM 3175 CZ ARG A 566 60.107 39.912 7.831 1.00117.10 C ANISOU 3175 CZ ARG A 566 15623 14911 13958 -1204 339 510 C ATOM 3176 NH1 ARG A 566 61.069 40.020 6.923 1.00118.61 N ANISOU 3176 NH1 ARG A 566 15806 15177 14084 -1255 458 524 N ATOM 3177 NH2 ARG A 566 59.908 38.754 8.446 1.00115.64 N ANISOU 3177 NH2 ARG A 566 15320 14756 13863 -1104 285 466 N ATOM 3178 N SER A 567 58.188 44.932 3.001 1.00 85.69 N ANISOU 3178 N SER A 567 12650 10524 9385 -1423 431 685 N ATOM 3179 CA SER A 567 58.287 45.709 1.772 1.00 85.93 C ANISOU 3179 CA SER A 567 12859 10514 9276 -1474 497 723 C ATOM 3180 C SER A 567 56.997 46.473 1.490 1.00 89.72 C ANISOU 3180 C SER A 567 13549 10841 9699 -1441 389 732 C ATOM 3181 O SER A 567 56.786 46.959 0.379 1.00 96.91 O ANISOU 3181 O SER A 567 14635 11697 10489 -1445 417 753 O ATOM 3182 CB SER A 567 58.630 44.802 0.589 1.00 83.88 C ANISOU 3182 CB SER A 567 12599 10322 8950 -1398 580 697 C ATOM 3183 OG SER A 567 57.540 43.961 0.255 1.00 79.32 O ANISOU 3183 OG SER A 567 12070 9691 8377 -1239 492 646 O TER 3184 SER A 567 ATOM 3185 O5' U B 1 45.946 20.986 1.455 1.00 28.81 O ANISOU 3185 O5' U B 1 3117 4174 3655 60 -141 -765 O ATOM 3186 C5' U B 1 44.767 21.634 1.818 1.00 24.01 C ANISOU 3186 C5' U B 1 2494 3581 3047 91 -188 -799 C ATOM 3187 C4' U B 1 44.491 21.288 3.276 1.00 21.10 C ANISOU 3187 C4' U B 1 2116 3112 2788 53 -134 -781 C ATOM 3188 O4' U B 1 45.580 21.790 4.128 1.00 20.31 O ANISOU 3188 O4' U B 1 2094 2938 2683 33 -110 -637 O ATOM 3189 C3' U B 1 43.248 21.979 3.778 1.00 21.45 C ANISOU 3189 C3' U B 1 2153 3163 2835 88 -184 -802 C ATOM 3190 O3' U B 1 42.168 21.197 3.454 1.00 21.75 O ANISOU 3190 O3' U B 1 2104 3236 2922 88 -179 -936 O ATOM 3191 C2' U B 1 43.502 22.052 5.298 1.00 20.39 C ANISOU 3191 C2' U B 1 2047 2921 2780 62 -142 -718 C ATOM 3192 O2' U B 1 43.217 20.824 5.969 1.00 20.30 O ANISOU 3192 O2' U B 1 1959 2855 2899 24 -66 -784 O ATOM 3193 C1' U B 1 44.999 22.328 5.350 1.00 19.89 C ANISOU 3193 C1' U B 1 2056 2825 2675 39 -117 -597 C ATOM 3194 N1 U B 1 45.280 23.770 5.392 1.00 21.66 N ANISOU 3194 N1 U B 1 2368 3059 2802 75 -185 -489 N ATOM 3195 C2 U B 1 45.265 24.393 6.606 1.00 19.07 C ANISOU 3195 C2 U B 1 2085 2660 2500 72 -184 -408 C ATOM 3196 O2 U B 1 45.020 23.782 7.626 1.00 18.74 O ANISOU 3196 O2 U B 1 2007 2555 2560 45 -130 -421 O ATOM 3197 N3 U B 1 45.537 25.748 6.606 1.00 19.24 N ANISOU 3197 N3 U B 1 2190 2689 2430 105 -244 -310 N ATOM 3198 C4 U B 1 45.815 26.527 5.489 1.00 22.56 C ANISOU 3198 C4 U B 1 2646 3185 2741 145 -304 -285 C ATOM 3199 O4 U B 1 46.047 27.734 5.627 1.00 22.89 O ANISOU 3199 O4 U B 1 2757 3223 2715 173 -351 -193 O ATOM 3200 C5 U B 1 45.805 25.794 4.241 1.00 20.66 C ANISOU 3200 C5 U B 1 2348 3022 2481 152 -303 -374 C ATOM 3201 C6 U B 1 45.545 24.481 4.253 1.00 21.39 C ANISOU 3201 C6 U B 1 2366 3103 2657 115 -246 -471 C ATOM 3202 P G B 2 40.730 21.806 3.169 1.00 22.26 P ANISOU 3202 P G B 2 2145 3371 2944 135 -247 -996 P ATOM 3203 OP1 G B 2 39.883 20.716 2.579 1.00 22.90 O ANISOU 3203 OP1 G B 2 2129 3498 3074 122 -231 -1145 O ATOM 3204 OP2 G B 2 40.985 23.077 2.280 1.00 22.36 O ANISOU 3204 OP2 G B 2 2215 3468 2814 185 -316 -934 O ATOM 3205 O5' G B 2 40.201 22.237 4.459 1.00 23.34 O ANISOU 3205 O5' G B 2 2305 3434 3131 143 -250 -939 O ATOM 3206 C5' G B 2 39.803 21.201 5.479 1.00 21.45 C ANISOU 3206 C5' G B 2 2003 3113 3033 112 -191 -982 C ATOM 3207 C4' G B 2 38.923 21.741 6.603 1.00 21.76 C ANISOU 3207 C4' G B 2 2055 3104 3108 142 -217 -939 C ATOM 3208 O4' G B 2 39.562 22.852 7.237 1.00 20.46 O ANISOU 3208 O4' G B 2 1983 2897 2893 155 -237 -807 O ATOM 3209 C3' G B 2 37.592 22.291 6.123 1.00 21.54 C ANISOU 3209 C3' G B 2 2016 3151 3016 188 -285 -986 C ATOM 3210 O3' G B 2 36.682 21.181 5.891 1.00 22.02 O ANISOU 3210 O3' G B 2 1979 3233 3155 178 -267 -1112 O ATOM 3211 C2' G B 2 37.215 23.139 7.325 1.00 22.50 C ANISOU 3211 C2' G B 2 2192 3209 3149 218 -310 -888 C ATOM 3212 O2' G B 2 36.628 22.400 8.327 1.00 23.06 O ANISOU 3212 O2' G B 2 2206 3212 3343 216 -280 -912 O ATOM 3213 C1' G B 2 38.579 23.715 7.704 1.00 20.37 C ANISOU 3213 C1' G B 2 2000 2889 2851 200 -291 -775 C ATOM 3214 N9 G B 2 38.831 25.063 7.133 1.00 20.63 N ANISOU 3214 N9 G B 2 2116 2975 2748 231 -348 -702 N ATOM 3215 C8 G B 2 39.172 25.341 5.809 1.00 23.71 C ANISOU 3215 C8 G B 2 2512 3458 3040 241 -373 -725 C ATOM 3216 N7 G B 2 39.320 26.636 5.579 1.00 20.85 N ANISOU 3216 N7 G B 2 2222 3128 2574 277 -420 -642 N ATOM 3217 C5 G B 2 39.044 27.206 6.860 1.00 20.29 C ANISOU 3217 C5 G B 2 2200 2974 2535 286 -425 -564 C ATOM 3218 C6 G B 2 39.036 28.570 7.259 1.00 23.94 C ANISOU 3218 C6 G B 2 2749 3424 2925 319 -464 -459 C ATOM 3219 O6 G B 2 39.272 29.583 6.563 1.00 20.14 O ANISOU 3219 O6 G B 2 2313 3001 2338 349 -499 -411 O ATOM 3220 N1 G B 2 38.722 28.746 8.607 1.00 19.45 N ANISOU 3220 N1 G B 2 2209 2765 2418 321 -458 -406 N ATOM 3221 C2 G B 2 38.437 27.676 9.459 1.00 19.22 C ANISOU 3221 C2 G B 2 2119 2670 2512 298 -418 -450 C ATOM 3222 N2 G B 2 38.149 27.992 10.707 1.00 19.64 N ANISOU 3222 N2 G B 2 2202 2646 2614 312 -419 -388 N ATOM 3223 N3 G B 2 38.437 26.391 9.082 1.00 19.49 N ANISOU 3223 N3 G B 2 2068 2718 2621 268 -377 -548 N ATOM 3224 C4 G B 2 38.743 26.269 7.791 1.00 24.50 C ANISOU 3224 C4 G B 2 2685 3434 3188 262 -385 -598 C ATOM 3225 P U B 3 35.521 21.342 4.841 1.00 24.43 P ANISOU 3225 P U B 3 2249 3653 3382 206 -321 -1199 P ATOM 3226 OP1 U B 3 34.766 20.070 4.815 1.00 26.72 O ANISOU 3226 OP1 U B 3 2439 3939 3775 185 -292 -1320 O ATOM 3227 OP2 U B 3 36.050 21.842 3.550 1.00 23.97 O ANISOU 3227 OP2 U B 3 2215 3692 3202 214 -346 -1207 O ATOM 3228 O5' U B 3 34.617 22.493 5.496 1.00 22.52 O ANISOU 3228 O5' U B 3 2060 3407 3088 257 -377 -1116 O ATOM 3229 C5' U B 3 33.514 23.028 4.761 1.00 22.99 C ANISOU 3229 C5' U B 3 2112 3571 3054 293 -428 -1149 C ATOM 3230 C4' U B 3 32.243 22.887 5.581 1.00 22.84 C ANISOU 3230 C4' U B 3 2068 3520 3092 318 -446 -1152 C ATOM 3231 O4' U B 3 32.470 23.539 6.848 1.00 23.96 O ANISOU 3231 O4' U B 3 2277 3564 3263 338 -450 -1033 O ATOM 3232 C3' U B 3 30.992 23.527 5.024 1.00 23.25 C ANISOU 3232 C3' U B 3 2120 3672 3041 358 -497 -1160 C ATOM 3233 O3' U B 3 30.477 22.584 4.086 1.00 29.22 O ANISOU 3233 O3' U B 3 2787 4506 3810 336 -489 -1293 O ATOM 3234 C2' U B 3 30.179 23.667 6.309 1.00 23.58 C ANISOU 3234 C2' U B 3 2180 3633 3147 388 -513 -1096 C ATOM 3235 O2' U B 3 29.577 22.446 6.683 1.00 28.71 O ANISOU 3235 O2' U B 3 2744 4244 3923 375 -494 -1177 O ATOM 3236 C1' U B 3 31.248 24.035 7.346 1.00 24.02 C ANISOU 3236 C1' U B 3 2300 3577 3251 383 -492 -995 C ATOM 3237 N1 U B 3 31.364 25.507 7.546 1.00 23.96 N ANISOU 3237 N1 U B 3 2394 3576 3133 419 -526 -875 N ATOM 3238 C2 U B 3 30.535 26.073 8.479 1.00 24.19 C ANISOU 3238 C2 U B 3 2464 3563 3165 462 -555 -798 C ATOM 3239 O2 U B 3 29.748 25.400 9.121 1.00 22.27 O ANISOU 3239 O2 U B 3 2172 3279 3011 475 -558 -822 O ATOM 3240 N3 U B 3 30.671 27.434 8.629 1.00 21.83 N ANISOU 3240 N3 U B 3 2262 3270 2762 491 -582 -689 N ATOM 3241 C4 U B 3 31.529 28.264 7.930 1.00 23.83 C ANISOU 3241 C4 U B 3 2567 3569 2917 485 -582 -652 C ATOM 3242 O4 U B 3 31.541 29.482 8.162 1.00 21.46 O ANISOU 3242 O4 U B 3 2351 3268 2534 515 -603 -553 O ATOM 3243 C5 U B 3 32.358 27.589 6.961 1.00 22.98 C ANISOU 3243 C5 U B 3 2409 3507 2816 445 -556 -735 C ATOM 3244 C6 U B 3 32.240 26.263 6.800 1.00 21.88 C ANISOU 3244 C6 U B 3 2182 3362 2770 413 -529 -841 C ATOM 3245 P G B 4 29.677 23.095 2.809 1.00 30.49 P ANISOU 3245 P G B 4 2928 4823 3832 358 -524 -1338 P ATOM 3246 OP1 G B 4 29.577 21.938 1.903 1.00 26.12 O ANISOU 3246 OP1 G B 4 2281 4328 3315 321 -503 -1483 O ATOM 3247 OP2 G B 4 30.253 24.364 2.326 1.00 27.83 O ANISOU 3247 OP2 G B 4 2661 4543 3369 385 -542 -1253 O ATOM 3248 O5' G B 4 28.248 23.462 3.451 1.00 28.81 O ANISOU 3248 O5' G B 4 2724 4613 3608 396 -558 -1295 O ATOM 3249 C5' G B 4 27.444 22.438 3.998 1.00 34.01 C ANISOU 3249 C5' G B 4 3319 5223 4380 386 -553 -1355 C ATOM 3250 C4' G B 4 26.062 22.961 4.334 1.00 29.49 C ANISOU 3250 C4' G B 4 2762 4683 3757 430 -594 -1302 C ATOM 3251 O4' G B 4 26.202 24.074 5.242 1.00 28.91 O ANISOU 3251 O4' G B 4 2786 4548 3649 470 -612 -1158 O ATOM 3252 C3' G B 4 25.260 23.545 3.184 1.00 32.33 C ANISOU 3252 C3' G B 4 3114 5203 3969 445 -616 -1323 C ATOM 3253 O3' G B 4 24.627 22.488 2.491 1.00 36.27 O ANISOU 3253 O3' G B 4 3516 5766 4500 417 -611 -1455 O ATOM 3254 C2' G B 4 24.248 24.354 3.972 1.00 28.96 C ANISOU 3254 C2' G B 4 2746 4760 3498 496 -649 -1207 C ATOM 3255 O2' G B 4 23.325 23.501 4.610 1.00 29.01 O ANISOU 3255 O2' G B 4 2704 4716 3604 501 -662 -1237 O ATOM 3256 C1' G B 4 25.141 24.977 5.039 1.00 34.08 C ANISOU 3256 C1' G B 4 3479 5285 4186 511 -645 -1096 C ATOM 3257 N9 G B 4 25.705 26.259 4.657 1.00 28.95 N ANISOU 3257 N9 G B 4 2906 4682 3410 529 -647 -1013 N ATOM 3258 C8 G B 4 26.849 26.511 3.937 1.00 31.01 C ANISOU 3258 C8 G B 4 3175 4975 3631 509 -628 -1031 C ATOM 3259 N7 G B 4 27.068 27.787 3.763 1.00 31.61 N ANISOU 3259 N7 G B 4 3323 5092 3596 540 -637 -936 N ATOM 3260 C5 G B 4 26.000 28.409 4.403 1.00 26.33 C ANISOU 3260 C5 G B 4 2700 4417 2888 579 -658 -851 C ATOM 3261 C6 G B 4 25.674 29.776 4.568 1.00 30.64 C ANISOU 3261 C6 G B 4 3329 4992 3322 623 -668 -728 C ATOM 3262 O6 G B 4 26.287 30.769 4.169 1.00 34.49 O ANISOU 3262 O6 G B 4 3863 5517 3723 637 -661 -670 O ATOM 3263 N1 G B 4 24.504 29.952 5.300 1.00 26.39 N ANISOU 3263 N1 G B 4 2818 4431 2777 656 -689 -666 N ATOM 3264 C2 G B 4 23.738 28.939 5.814 1.00 26.63 C ANISOU 3264 C2 G B 4 2798 4417 2903 652 -703 -713 C ATOM 3265 N2 G B 4 22.625 29.293 6.487 1.00 28.43 N ANISOU 3265 N2 G B 4 3065 4630 3107 694 -727 -629 N ATOM 3266 N3 G B 4 24.021 27.659 5.659 1.00 29.47 N ANISOU 3266 N3 G B 4 3073 4750 3374 612 -693 -831 N ATOM 3267 C4 G B 4 25.162 27.475 4.959 1.00 24.20 C ANISOU 3267 C4 G B 4 2383 4102 2709 575 -668 -894 C ATOM 3268 P C B 5 24.124 22.688 0.992 1.00 40.03 P ANISOU 3268 P C B 5 3947 6424 4841 412 -618 -1529 P ATOM 3269 OP1 C B 5 23.677 21.353 0.530 1.00 38.70 O ANISOU 3269 OP1 C B 5 3676 6279 4748 371 -607 -1675 O ATOM 3270 OP2 C B 5 25.109 23.470 0.216 1.00 37.51 O ANISOU 3270 OP2 C B 5 3660 6168 4425 418 -607 -1505 O ATOM 3271 O5' C B 5 22.869 23.638 1.188 1.00 28.35 O ANISOU 3271 O5' C B 5 2509 5010 3255 459 -648 -1431 O ATOM 3272 C5' C B 5 21.720 23.071 1.757 1.00 32.57 C ANISOU 3272 C5' C B 5 3014 5516 3846 466 -668 -1438 C ATOM 3273 C4' C B 5 20.656 24.140 1.905 1.00 37.02 C ANISOU 3273 C4' C B 5 3634 6145 4285 514 -693 -1321 C ATOM 3274 O4' C B 5 21.061 25.171 2.841 1.00 30.79 O ANISOU 3274 O4' C B 5 2949 5268 3480 553 -700 -1176 O ATOM 3275 C3' C B 5 20.389 24.890 0.618 1.00 41.92 C ANISOU 3275 C3' C B 5 4243 6948 4737 520 -682 -1329 C ATOM 3276 O3' C B 5 19.501 24.114 -0.166 1.00 37.51 O ANISOU 3276 O3' C B 5 3594 6496 4161 495 -684 -1437 O ATOM 3277 C2' C B 5 19.745 26.170 1.147 1.00 31.24 C ANISOU 3277 C2' C B 5 2981 5609 3280 573 -694 -1168 C ATOM 3278 O2' C B 5 18.400 25.945 1.506 1.00 34.49 O ANISOU 3278 O2' C B 5 3384 6037 3682 590 -717 -1138 O ATOM 3279 C1' C B 5 20.586 26.427 2.394 1.00 32.39 C ANISOU 3279 C1' C B 5 3206 5581 3520 588 -701 -1083 C ATOM 3280 N1 C B 5 21.742 27.335 2.124 1.00 35.22 N ANISOU 3280 N1 C B 5 3618 5944 3822 594 -683 -1036 N ATOM 3281 C2 C B 5 21.587 28.697 2.356 1.00 33.32 C ANISOU 3281 C2 C B 5 3464 5724 3472 638 -683 -899 C ATOM 3282 O2 C B 5 20.503 29.084 2.791 1.00 36.02 O ANISOU 3282 O2 C B 5 3840 6079 3765 669 -696 -819 O ATOM 3283 N3 C B 5 22.614 29.543 2.097 1.00 34.56 N ANISOU 3283 N3 C B 5 3666 5885 3579 645 -667 -854 N ATOM 3284 C4 C B 5 23.769 29.063 1.636 1.00 33.69 C ANISOU 3284 C4 C B 5 3520 5759 3522 613 -655 -934 C ATOM 3285 N4 C B 5 24.761 29.926 1.400 1.00 28.36 N ANISOU 3285 N4 C B 5 2892 5088 2797 626 -644 -879 N ATOM 3286 C5 C B 5 23.946 27.670 1.385 1.00 35.00 C ANISOU 3286 C5 C B 5 3601 5904 3792 568 -652 -1071 C ATOM 3287 C6 C B 5 22.917 26.849 1.634 1.00 34.53 C ANISOU 3287 C6 C B 5 3495 5841 3786 559 -664 -1121 C ATOM 3288 P C B 6 19.468 24.350 -1.739 1.00 42.91 P ANISOU 3288 P C B 6 4216 7377 4712 482 -663 -1516 P ATOM 3289 OP1 C B 6 18.493 23.405 -2.337 1.00 43.39 O ANISOU 3289 OP1 C B 6 4184 7525 4778 451 -668 -1630 O ATOM 3290 OP2 C B 6 20.857 24.334 -2.249 1.00 40.20 O ANISOU 3290 OP2 C B 6 3865 7021 4388 466 -644 -1566 O ATOM 3291 O5' C B 6 18.926 25.855 -1.811 1.00 33.91 O ANISOU 3291 O5' C B 6 3145 6330 3410 534 -658 -1368 O ATOM 3292 C5' C B 6 17.556 26.156 -1.635 1.00 38.99 C ANISOU 3292 C5' C B 6 3799 7037 3977 556 -668 -1299 C ATOM 3293 C4' C B 6 17.313 27.612 -2.005 1.00 37.64 C ANISOU 3293 C4' C B 6 3680 6981 3639 600 -644 -1175 C ATOM 3294 O4' C B 6 18.136 28.454 -1.171 1.00 37.15 O ANISOU 3294 O4' C B 6 3718 6799 3598 630 -646 -1062 O ATOM 3295 C3' C B 6 17.718 28.005 -3.420 1.00 40.52 C ANISOU 3295 C3' C B 6 3980 7521 3894 598 -609 -1235 C ATOM 3296 O3' C B 6 16.655 27.735 -4.305 1.00 38.87 O ANISOU 3296 O3' C B 6 3691 7482 3597 586 -596 -1292 O ATOM 3297 C2' C B 6 17.899 29.507 -3.275 1.00 40.27 C ANISOU 3297 C2' C B 6 4029 7517 3754 649 -586 -1082 C ATOM 3298 O2' C B 6 16.654 30.173 -3.296 1.00 42.85 O ANISOU 3298 O2' C B 6 4376 7947 3958 677 -569 -984 O ATOM 3299 C1' C B 6 18.536 29.602 -1.894 1.00 39.00 C ANISOU 3299 C1' C B 6 3969 7144 3706 658 -613 -1005 C ATOM 3300 N1 C B 6 20.029 29.645 -1.938 1.00 46.62 N ANISOU 3300 N1 C B 6 4947 8032 4735 649 -611 -1035 N ATOM 3301 C2 C B 6 20.662 30.861 -2.194 1.00 51.76 C ANISOU 3301 C2 C B 6 5643 8721 5301 685 -588 -946 C ATOM 3302 O2 C B 6 19.957 31.860 -2.376 1.00 57.12 O ANISOU 3302 O2 C B 6 6349 9499 5856 722 -565 -848 O ATOM 3303 N3 C B 6 22.019 30.907 -2.233 1.00 51.92 N ANISOU 3303 N3 C B 6 5678 8672 5376 679 -590 -964 N ATOM 3304 C4 C B 6 22.734 29.797 -2.031 1.00 48.87 C ANISOU 3304 C4 C B 6 5264 8185 5119 638 -607 -1063 C ATOM 3305 N4 C B 6 24.068 29.889 -2.082 1.00 45.32 N ANISOU 3305 N4 C B 6 4833 7673 4711 633 -606 -1066 N ATOM 3306 C5 C B 6 22.107 28.543 -1.772 1.00 47.34 C ANISOU 3306 C5 C B 6 5019 7951 5016 600 -623 -1158 C ATOM 3307 C6 C B 6 20.766 28.515 -1.737 1.00 49.71 C ANISOU 3307 C6 C B 6 5304 8318 5265 608 -627 -1141 C ATOM 3308 P U B 7 16.939 27.435 -5.843 1.00 49.72 P ANISOU 3308 P U B 7 4949 9034 4908 566 -570 -1427 P ATOM 3309 OP1 U B 7 18.393 27.188 -6.006 1.00 41.61 O ANISOU 3309 OP1 U B 7 3917 7929 3964 557 -574 -1491 O ATOM 3310 OP2 U B 7 16.254 28.478 -6.642 1.00 54.52 O ANISOU 3310 OP2 U B 7 5535 9842 5339 602 -528 -1354 O ATOM 3311 O5' U B 7 16.158 26.065 -6.043 1.00 44.92 O ANISOU 3311 O5' U B 7 4259 8443 4365 515 -590 -1562 O ATOM 3312 C5' U B 7 16.568 24.901 -5.349 1.00 47.15 C ANISOU 3312 C5' U B 7 4540 8556 4819 478 -620 -1644 C ATOM 3313 C4' U B 7 15.346 24.194 -4.802 1.00 43.53 C ANISOU 3313 C4' U B 7 4069 8068 4404 461 -645 -1650 C ATOM 3314 O4' U B 7 14.865 24.938 -3.661 1.00 38.86 O ANISOU 3314 O4' U B 7 3580 7386 3801 504 -661 -1483 O ATOM 3315 C3' U B 7 14.142 24.164 -5.738 1.00 45.13 C ANISOU 3315 C3' U B 7 4199 8468 4479 450 -632 -1685 C ATOM 3316 O3' U B 7 14.246 23.096 -6.656 1.00 43.61 O ANISOU 3316 O3' U B 7 3899 8345 4326 400 -629 -1864 O ATOM 3317 C2' U B 7 13.036 23.878 -4.735 1.00 45.74 C ANISOU 3317 C2' U B 7 4317 8464 4599 456 -665 -1609 C ATOM 3318 O2' U B 7 12.986 22.504 -4.392 1.00 47.74 O ANISOU 3318 O2' U B 7 4519 8611 5010 416 -693 -1727 O ATOM 3319 C1' U B 7 13.470 24.735 -3.544 1.00 40.90 C ANISOU 3319 C1' U B 7 3823 7702 4014 505 -675 -1451 C ATOM 3320 N1 U B 7 12.768 26.053 -3.509 1.00 35.86 N ANISOU 3320 N1 U B 7 3252 7159 3214 552 -656 -1287 N ATOM 3321 C2 U B 7 11.454 26.056 -3.101 1.00 34.90 C ANISOU 3321 C2 U B 7 3152 7063 3047 566 -672 -1204 C ATOM 3322 O2 U B 7 10.872 25.037 -2.775 1.00 37.84 O ANISOU 3322 O2 U B 7 3487 7382 3511 544 -707 -1263 O ATOM 3323 N3 U B 7 10.851 27.292 -3.091 1.00 35.02 N ANISOU 3323 N3 U B 7 3232 7168 2907 609 -645 -1046 N ATOM 3324 C4 U B 7 11.425 28.498 -3.441 1.00 35.36 C ANISOU 3324 C4 U B 7 3315 7276 2845 639 -601 -969 C ATOM 3325 O4 U B 7 10.744 29.516 -3.386 1.00 34.10 O ANISOU 3325 O4 U B 7 3210 7196 2551 676 -571 -825 O ATOM 3326 C5 U B 7 12.808 28.416 -3.861 1.00 32.60 C ANISOU 3326 C5 U B 7 2935 6894 2559 625 -591 -1066 C ATOM 3327 C6 U B 7 13.413 27.218 -3.883 1.00 31.55 C ANISOU 3327 C6 U B 7 2744 6674 2568 583 -619 -1215 C ATOM 3328 P U B 8 14.116 23.366 -8.223 1.00 48.80 P ANISOU 3328 P U B 8 4462 9242 4837 393 -593 -1942 P ATOM 3329 OP1 U B 8 14.185 22.063 -8.925 1.00 45.47 O ANISOU 3329 OP1 U B 8 3938 8850 4487 337 -600 -2134 O ATOM 3330 OP2 U B 8 15.007 24.470 -8.620 1.00 42.48 O ANISOU 3330 OP2 U B 8 3690 8494 3957 437 -565 -1874 O ATOM 3331 O5' U B 8 12.624 23.924 -8.338 1.00 39.90 O ANISOU 3331 O5' U B 8 3334 8258 3567 408 -581 -1848 O ATOM 3332 C5' U B 8 12.137 24.237 -9.637 1.00 37.97 C ANISOU 3332 C5' U B 8 3001 8253 3172 406 -542 -1891 C ATOM 3333 C4' U B 8 10.819 23.529 -9.859 1.00 40.17 C ANISOU 3333 C4' U B 8 3223 8621 3421 367 -552 -1941 C ATOM 3334 O4' U B 8 9.837 24.051 -8.933 1.00 35.97 O ANISOU 3334 O4' U B 8 2775 8046 2846 394 -562 -1776 O ATOM 3335 C3' U B 8 10.209 23.726 -11.236 1.00 39.74 C ANISOU 3335 C3' U B 8 3062 8831 3209 357 -508 -1998 C ATOM 3336 O3' U B 8 10.809 22.821 -12.161 1.00 41.85 O ANISOU 3336 O3' U B 8 3226 9146 3528 318 -510 -2191 O ATOM 3337 C2' U B 8 8.757 23.373 -10.946 1.00 44.32 C ANISOU 3337 C2' U B 8 3639 9452 3749 333 -522 -1960 C ATOM 3338 O2' U B 8 8.550 21.978 -10.930 1.00 46.17 O ANISOU 3338 O2' U B 8 3817 9620 4106 275 -561 -2111 O ATOM 3339 C1' U B 8 8.564 23.934 -9.537 1.00 33.66 C ANISOU 3339 C1' U B 8 2423 7929 2439 374 -546 -1780 C ATOM 3340 N1 U B 8 7.877 25.258 -9.536 1.00 37.78 N ANISOU 3340 N1 U B 8 2997 8572 2786 421 -503 -1596 N ATOM 3341 C2 U B 8 6.511 25.251 -9.713 1.00 38.29 C ANISOU 3341 C2 U B 8 3042 8765 2741 409 -492 -1541 C ATOM 3342 O2 U B 8 5.881 24.225 -9.879 1.00 38.61 O ANISOU 3342 O2 U B 8 3023 8822 2825 362 -521 -1641 O ATOM 3343 N3 U B 8 5.922 26.489 -9.715 1.00 35.74 N ANISOU 3343 N3 U B 8 2769 8555 2255 453 -442 -1364 N ATOM 3344 C4 U B 8 6.546 27.716 -9.544 1.00 39.46 C ANISOU 3344 C4 U B 8 3307 9019 2669 507 -402 -1243 C ATOM 3345 O4 U B 8 5.878 28.752 -9.567 1.00 31.81 O ANISOU 3345 O4 U B 8 2377 8160 1549 542 -351 -1085 O ATOM 3346 C5 U B 8 7.981 27.639 -9.361 1.00 34.57 C ANISOU 3346 C5 U B 8 2702 8257 2175 516 -424 -1315 C ATOM 3347 C6 U B 8 8.582 26.438 -9.359 1.00 36.93 C ANISOU 3347 C6 U B 8 2955 8449 2628 473 -472 -1482 C ATOM 3348 P A B 9 11.044 23.274 -13.682 1.00 54.75 P ANISOU 3348 P A B 9 4751 11027 5025 332 -461 -2259 P ATOM 3349 OP1 A B 9 12.103 22.415 -14.253 1.00 58.28 O ANISOU 3349 OP1 A B 9 5136 11434 5572 307 -476 -2429 O ATOM 3350 OP2 A B 9 11.177 24.752 -13.715 1.00 50.62 O ANISOU 3350 OP2 A B 9 4273 10584 4378 399 -417 -2095 O ATOM 3351 O5' A B 9 9.660 22.869 -14.370 1.00 55.99 O ANISOU 3351 O5' A B 9 4819 11376 5079 293 -445 -2312 O ATOM 3352 C5' A B 9 9.312 21.491 -14.496 1.00 64.51 C ANISOU 3352 C5' A B 9 5839 12419 6252 226 -479 -2472 C ATOM 3353 C4' A B 9 8.150 21.337 -15.455 1.00 67.60 C ANISOU 3353 C4' A B 9 6128 13047 6509 196 -451 -2523 C ATOM 3354 O4' A B 9 7.152 22.314 -15.088 1.00 65.26 O ANISOU 3354 O4' A B 9 5885 12831 6079 227 -423 -2337 O ATOM 3355 C3' A B 9 8.465 21.656 -16.908 1.00 74.44 C ANISOU 3355 C3' A B 9 6876 14150 7257 209 -403 -2609 C ATOM 3356 O3' A B 9 8.913 20.488 -17.578 1.00 73.46 O ANISOU 3356 O3' A B 9 6666 14027 7221 160 -424 -2818 O ATOM 3357 C2' A B 9 7.115 22.107 -17.453 1.00 79.21 C ANISOU 3357 C2' A B 9 7425 14987 7685 203 -358 -2547 C ATOM 3358 O2' A B 9 6.362 21.027 -17.965 1.00 85.68 O ANISOU 3358 O2' A B 9 8157 15886 8511 134 -373 -2691 O ATOM 3359 C1' A B 9 6.404 22.676 -16.228 1.00 67.39 C ANISOU 3359 C1' A B 9 6053 13376 6175 223 -368 -2350 C ATOM 3360 N9 A B 9 6.231 24.125 -16.264 1.00 60.45 N ANISOU 3360 N9 A B 9 5211 12610 5146 286 -309 -2167 N ATOM 3361 C8 A B 9 7.158 25.092 -15.991 1.00 58.18 C ANISOU 3361 C8 A B 9 4985 12260 4861 348 -290 -2070 C ATOM 3362 N7 A B 9 6.692 26.314 -16.112 1.00 60.22 N ANISOU 3362 N7 A B 9 5260 12654 4966 395 -227 -1908 N ATOM 3363 C5 A B 9 5.370 26.133 -16.491 1.00 61.74 C ANISOU 3363 C5 A B 9 5401 13015 5044 361 -200 -1895 C ATOM 3364 C6 A B 9 4.322 27.032 -16.778 1.00 63.77 C ANISOU 3364 C6 A B 9 5645 13472 5113 382 -127 -1748 C ATOM 3365 N6 A B 9 4.452 28.362 -16.729 1.00 60.06 N ANISOU 3365 N6 A B 9 5215 13067 4540 445 -61 -1585 N ATOM 3366 N1 A B 9 3.125 26.511 -17.123 1.00 73.95 N ANISOU 3366 N1 A B 9 6879 14895 6323 332 -118 -1773 N ATOM 3367 C2 A B 9 2.985 25.181 -17.175 1.00 76.98 C ANISOU 3367 C2 A B 9 7221 15213 6815 268 -181 -1938 C ATOM 3368 N3 A B 9 3.894 24.240 -16.926 1.00 70.85 N ANISOU 3368 N3 A B 9 6449 14250 6220 244 -249 -2088 N ATOM 3369 C4 A B 9 5.073 24.788 -16.588 1.00 64.33 C ANISOU 3369 C4 A B 9 5681 13299 5464 293 -253 -2054 C TER 3370 A B 9 HETATM 3371 O HOH A 1 21.036 41.440 9.978 1.00 22.23 O HETATM 3372 O HOH A 2 8.242 42.424 6.837 1.00 22.50 O HETATM 3373 O HOH A 3 39.597 27.640 25.991 1.00 20.26 O HETATM 3374 O HOH A 4 12.877 36.752 2.573 1.00 23.56 O HETATM 3375 O HOH A 5 54.911 30.693 26.470 1.00 25.13 O HETATM 3376 O HOH A 6 42.365 32.476 8.324 1.00 22.24 O HETATM 3377 O HOH A 7 40.967 19.156 8.732 1.00 28.85 O HETATM 3378 O HOH A 8 42.074 21.652 8.337 1.00 23.73 O HETATM 3379 O HOH A 9 48.075 24.015 9.363 1.00 26.95 O HETATM 3380 O HOH A 10 -6.671 40.372 -2.694 1.00 23.85 O HETATM 3381 O HOH A 11 13.012 39.226 3.911 1.00 27.19 O HETATM 3382 O HOH A 12 16.377 51.077 9.991 1.00 26.32 O HETATM 3383 O HOH A 13 32.067 23.314 16.500 1.00 23.88 O HETATM 3384 O HOH A 15 39.883 32.065 7.252 1.00 26.53 O HETATM 3385 O HOH A 16 62.674 27.212 13.606 1.00 25.96 O HETATM 3386 O HOH A 17 6.767 55.531 6.891 1.00 23.91 O HETATM 3387 O HOH A 18 19.411 46.575 14.494 1.00 24.60 O HETATM 3388 O HOH A 19 48.425 24.096 6.567 1.00 18.90 O HETATM 3389 O HOH A 20 -4.426 38.007 -19.794 1.00 25.35 O HETATM 3390 O HOH A 21 -5.112 45.955 1.718 1.00 24.96 O HETATM 3391 O HOH A 22 -2.725 46.381 -0.636 1.00 28.66 O HETATM 3392 O HOH A 23 50.280 27.769 10.923 1.00 20.55 O HETATM 3393 O HOH A 24 26.772 20.001 14.791 1.00 27.00 O HETATM 3394 O HOH A 25 16.676 30.517 1.102 1.00 21.96 O HETATM 3395 O HOH A 26 33.052 45.341 11.837 1.00 31.35 O HETATM 3396 O HOH A 27 13.179 32.182 -0.127 1.00 33.57 O HETATM 3397 O HOH A 28 48.486 29.851 11.470 1.00 23.87 O HETATM 3398 O HOH A 29 -12.843 20.463 -15.916 1.00 30.61 O HETATM 3399 O HOH A 30 -0.519 35.292 -8.755 1.00 28.30 O HETATM 3400 O HOH A 32 55.534 25.280 18.169 1.00 26.28 O HETATM 3401 O HOH A 33 26.635 33.636 8.221 1.00 26.69 O HETATM 3402 O HOH A 34 12.601 54.330 10.224 1.00 29.80 O HETATM 3403 O HOH A 35 4.015 43.195 -2.498 1.00 23.50 O HETATM 3404 O HOH A 36 -6.412 45.709 -9.385 1.00 34.27 O HETATM 3405 O HOH A 37 -11.172 31.627 -27.419 1.00 26.33 O HETATM 3406 O HOH A 38 50.111 31.423 23.870 1.00 21.18 O HETATM 3407 O HOH A 39 6.163 46.898 10.361 1.00 35.28 O HETATM 3408 O HOH A 40 -1.664 36.640 -14.464 1.00 28.64 O HETATM 3409 O HOH A 41 30.387 27.901 4.268 1.00 32.25 O HETATM 3410 O HOH A 42 -12.038 33.067 -6.084 1.00 33.54 O HETATM 3411 O HOH A 43 3.920 45.792 11.720 1.00 23.86 O HETATM 3412 O HOH A 44 22.465 19.937 13.558 1.00 24.81 O HETATM 3413 O HOH A 45 -0.646 40.281 -9.343 1.00 26.20 O HETATM 3414 O HOH A 46 -13.769 23.546 -19.129 1.00 25.49 O HETATM 3415 O HOH A 47 7.910 48.626 5.443 1.00 27.65 O HETATM 3416 O HOH A 48 -6.137 40.918 -16.752 1.00 31.85 O HETATM 3417 O HOH A 49 48.090 35.404 7.595 1.00 40.01 O HETATM 3418 O HOH A 50 13.226 41.576 2.429 1.00 34.10 O HETATM 3419 O HOH A 51 48.164 21.589 17.701 1.00 30.68 O HETATM 3420 O HOH A 52 -2.560 41.182 -11.072 1.00 22.85 O HETATM 3421 O HOH A 53 -4.004 29.062 12.740 1.00 43.35 O HETATM 3422 O HOH A 54 48.373 21.853 2.521 1.00 26.45 O HETATM 3423 O HOH A 55 -12.981 23.341 -12.555 1.00 30.72 O HETATM 3424 O HOH A 56 2.173 31.382 -13.843 1.00 30.65 O HETATM 3425 O HOH A 57 10.701 33.111 -0.358 1.00 29.21 O HETATM 3426 O HOH A 58 19.054 19.692 8.486 1.00 28.17 O HETATM 3427 O HOH A 59 61.032 31.299 23.139 1.00 33.19 O HETATM 3428 O HOH A 60 15.007 39.508 5.750 1.00 23.19 O HETATM 3429 O HOH A 62 9.396 44.174 4.760 1.00 30.28 O HETATM 3430 O HOH A 63 22.911 45.430 8.345 1.00 35.05 O HETATM 3431 O HOH A 64 33.269 39.100 8.023 1.00 29.92 O HETATM 3432 O HOH A 65 39.823 36.107 28.583 1.00 29.76 O HETATM 3433 O HOH A 67 -12.862 42.541 -17.641 1.00 42.92 O HETATM 3434 O HOH A 68 55.847 24.874 31.153 1.00 26.81 O HETATM 3435 O HOH A 69 41.521 38.208 28.304 1.00 29.27 O HETATM 3436 O HOH A 70 45.024 19.218 14.417 1.00 23.94 O HETATM 3437 O HOH A 71 12.187 18.861 3.822 1.00 35.11 O HETATM 3438 O HOH A 72 48.381 26.278 27.088 1.00 35.48 O HETATM 3439 O HOH A 73 -8.831 18.469 -4.208 1.00 33.00 O HETATM 3440 O HOH A 74 35.177 19.784 15.840 1.00 26.24 O HETATM 3441 O HOH A 75 28.273 45.203 8.805 1.00 32.05 O HETATM 3442 O HOH A 76 52.492 37.221 25.762 1.00 33.18 O HETATM 3443 O HOH A 77 14.820 19.630 7.405 1.00 27.78 O HETATM 3444 O HOH A 78 41.692 23.486 24.805 1.00 45.23 O HETATM 3445 O HOH A 79 55.634 19.398 4.470 1.00 32.85 O HETATM 3446 O HOH A 80 50.258 42.867 24.794 1.00 39.55 O HETATM 3447 O HOH A 81 -16.400 34.140 -11.785 1.00 35.13 O HETATM 3448 O HOH A 82 -15.866 31.742 -23.625 1.00 30.06 O HETATM 3449 O HOH A 83 18.899 47.647 17.082 1.00 30.28 O HETATM 3450 O HOH A 84 -7.702 30.979 -27.864 1.00 35.82 O HETATM 3451 O HOH A 85 38.300 43.719 15.553 1.00 27.05 O HETATM 3452 O HOH A 86 1.625 16.795 -9.555 1.00 33.06 O HETATM 3453 O HOH A 87 -16.509 34.855 -1.297 1.00 39.68 O HETATM 3454 O HOH A 88 1.668 17.626 -4.966 1.00 34.41 O HETATM 3455 O HOH A 89 56.976 18.284 6.801 1.00 27.86 O HETATM 3456 O HOH A 90 18.884 35.208 5.071 1.00 26.86 O HETATM 3457 O HOH A 91 1.783 38.269 15.537 1.00 28.15 O HETATM 3458 O HOH A 93 -18.013 24.680 -18.871 1.00 41.56 O HETATM 3459 O HOH A 94 -7.233 46.588 -4.482 1.00 35.14 O HETATM 3460 O HOH A 95 -16.411 36.981 -10.918 1.00 32.11 O HETATM 3461 O HOH A 96 -1.372 36.790 12.197 1.00 33.19 O HETATM 3462 O HOH A 97 -16.009 25.296 -2.751 1.00 30.55 O HETATM 3463 O HOH A 98 54.368 22.735 18.242 1.00 31.73 O HETATM 3464 O HOH A 99 56.533 27.375 30.133 1.00 28.69 O HETATM 3465 O HOH A 100 42.085 25.704 3.211 1.00 28.73 O HETATM 3466 O HOH A 102 29.629 49.446 8.968 1.00 39.67 O HETATM 3467 O HOH A 105 48.037 46.890 24.589 1.00 52.76 O HETATM 3468 O HOH A 106 14.634 17.369 3.451 1.00 41.13 O HETATM 3469 O HOH A 107 8.346 44.390 8.843 1.00 32.31 O HETATM 3470 O HOH A 108 -6.577 39.396 -18.818 1.00 30.65 O HETATM 3471 O HOH A 110 -13.871 22.993 -15.154 1.00 35.73 O HETATM 3472 O HOH A 111 3.911 44.798 3.723 1.00 30.48 O HETATM 3473 O HOH A 114 24.877 50.675 9.242 1.00 42.32 O HETATM 3474 O HOH A 115 -3.612 40.274 -15.927 1.00 35.25 O HETATM 3475 O HOH A 116 16.725 45.655 19.739 1.00 34.83 O HETATM 3476 O HOH A 117 56.409 27.474 23.559 1.00 35.83 O HETATM 3477 O HOH A 118 26.868 19.818 7.938 1.00 37.75 O HETATM 3478 O HOH A 119 7.221 57.789 13.570 1.00 46.58 O HETATM 3479 O HOH A 120 36.692 24.382 10.159 1.00 27.29 O HETATM 3480 O HOH A 121 52.809 48.342 23.591 1.00 39.61 O HETATM 3481 O HOH A 122 4.341 43.501 20.300 1.00 27.10 O HETATM 3482 O HOH A 123 52.591 19.122 25.111 1.00 46.97 O HETATM 3483 O HOH A 124 16.489 44.619 6.909 1.00 31.88 O HETATM 3484 O HOH A 125 -17.538 28.091 -16.384 1.00 29.92 O HETATM 3485 O HOH A 126 34.540 54.922 19.294 1.00 46.58 O HETATM 3486 O HOH A 127 -16.262 38.362 -13.471 1.00 34.89 O HETATM 3487 O HOH A 128 23.834 47.619 18.456 1.00 31.22 O HETATM 3488 O HOH A 129 56.072 28.299 27.252 1.00 31.34 O HETATM 3489 O HOH A 130 -8.977 44.792 -16.254 1.00 46.56 O HETATM 3490 O HOH A 131 33.954 48.382 23.792 1.00 53.10 O HETATM 3491 O HOH A 132 -17.762 40.966 -4.774 1.00 29.61 O HETATM 3492 O HOH A 133 24.114 42.170 24.829 1.00 48.18 O HETATM 3493 O HOH A 135 49.523 21.906 5.232 1.00 35.88 O HETATM 3494 O HOH A 136 17.108 38.875 3.904 1.00 43.12 O HETATM 3495 O HOH A 137 51.743 33.849 -3.066 1.00 38.18 O HETATM 3496 O HOH A 138 3.820 32.306 19.067 1.00 39.15 O HETATM 3497 O HOH A 139 40.056 30.299 29.959 1.00 34.27 O HETATM 3498 O HOH A 141 23.936 34.814 4.198 1.00 37.51 O HETATM 3499 O HOH A 142 53.125 48.988 4.825 1.00 43.19 O HETATM 3500 O HOH A 143 52.934 21.559 2.715 1.00 50.46 O HETATM 3501 O HOH A 144 24.644 32.507 6.394 1.00 37.20 O HETATM 3502 O HOH A 145 32.913 38.058 29.427 1.00 49.31 O HETATM 3503 O HOH A 146 45.334 27.311 31.494 1.00 36.45 O HETATM 3504 O HOH A 147 21.911 31.156 8.459 1.00 40.83 O HETATM 3505 O HOH A 149 21.820 21.820 18.664 1.00 47.20 O HETATM 3506 O HOH A 150 14.059 45.171 5.459 1.00 33.41 O HETATM 3507 O HOH A 152 13.343 17.389 8.251 1.00 42.76 O HETATM 3508 O HOH A 153 5.525 31.714 -6.245 1.00 34.58 O HETATM 3509 O HOH A 154 50.283 32.446 31.203 1.00 29.42 O HETATM 3510 O HOH A 155 -12.109 46.457 -7.076 1.00 41.99 O HETATM 3511 O HOH A 156 4.148 41.771 22.274 1.00 51.15 O HETATM 3512 O HOH A 157 -8.428 49.287 -7.420 1.00 51.32 O HETATM 3513 O HOH A 159 9.367 27.766 -12.926 1.00 35.73 O HETATM 3514 O HOH A 160 37.989 22.018 21.405 1.00 37.42 O HETATM 3515 O HOH A 161 58.702 36.480 6.714 1.00 36.74 O HETATM 3516 O HOH A 162 53.638 48.958 20.511 1.00 33.22 O HETATM 3517 O HOH A 576 -2.309 39.467 -18.608 1.00 46.65 O HETATM 3518 O HOH A 577 6.344 21.969 -12.444 1.00 33.71 O HETATM 3519 O HOH A 578 22.805 49.259 7.075 1.00 35.31 O HETATM 3520 O HOH A 579 -0.286 15.933 -13.773 1.00 32.75 O HETATM 3521 O HOH A 580 26.212 22.283 19.441 1.00 38.98 O HETATM 3522 O HOH A 581 -12.307 25.933 -9.165 1.00 34.90 O HETATM 3523 O HOH A 582 62.733 29.143 7.146 1.00 50.16 O HETATM 3524 O HOH A 583 -16.055 43.888 -5.754 1.00 30.46 O HETATM 3525 O HOH A 584 -1.769 39.428 -13.985 1.00 44.16 O HETATM 3526 O HOH A 585 36.230 34.541 8.585 1.00 38.72 O HETATM 3527 O HOH A 586 -15.748 25.863 0.274 1.00 54.65 O HETATM 3528 O HOH A 587 11.155 35.771 -0.084 1.00 41.37 O HETATM 3529 O HOH A 588 37.637 37.262 30.089 1.00 40.47 O HETATM 3530 O HOH A 589 31.303 18.793 16.010 1.00 47.05 O HETATM 3531 O HOH A 590 -5.185 15.030 -18.256 1.00 43.63 O HETATM 3532 O HOH A 591 1.969 38.461 18.133 1.00 50.97 O HETATM 3533 O HOH A 592 21.529 18.361 16.132 1.00 55.44 O HETATM 3534 O HOH A 593 -7.316 40.926 -21.174 1.00 35.51 O HETATM 3535 O HOH A 594 -6.423 34.681 -25.370 1.00 47.46 O HETATM 3536 O HOH A 595 49.498 29.135 26.981 1.00 26.18 O HETATM 3537 O HOH A 596 58.732 29.266 3.890 1.00 46.79 O HETATM 3538 O HOH A 597 48.524 54.275 19.285 1.00 41.58 O HETATM 3539 O HOH A 598 7.916 46.624 12.439 1.00 25.44 O HETATM 3540 O HOH A 599 -16.052 32.698 -8.014 1.00 44.31 O HETATM 3541 O HOH A 600 15.920 18.958 11.641 1.00 46.99 O HETATM 3542 O HOH A 601 -6.194 46.113 -13.515 1.00 33.29 O HETATM 3543 O HOH A 602 36.514 17.957 9.222 1.00 49.67 O HETATM 3544 O HOH A 603 -18.544 37.865 -17.635 1.00 27.06 O HETATM 3545 O HOH A 604 64.343 29.731 17.043 1.00 37.24 O HETATM 3546 O HOH A 605 12.853 35.681 24.490 1.00 41.68 O HETATM 3547 O HOH A 606 51.330 22.052 18.449 1.00 34.30 O HETATM 3548 O HOH A 607 9.755 17.623 10.014 1.00 47.36 O HETATM 3549 O HOH A 608 40.628 39.340 6.824 1.00 51.16 O HETATM 3550 O HOH A 609 -1.743 34.783 -26.230 1.00 51.39 O HETATM 3551 O HOH A 610 2.113 20.383 18.750 1.00 48.78 O HETATM 3552 O HOH A 611 9.323 32.998 23.237 1.00 36.37 O HETATM 3553 O HOH A 612 35.776 31.512 8.042 1.00 35.74 O HETATM 3554 O HOH A 613 -12.200 44.322 -2.003 1.00 46.70 O HETATM 3555 O HOH A 614 14.839 24.862 -0.188 1.00 32.07 O HETATM 3556 O HOH A 615 -0.450 16.055 -26.959 1.00 49.67 O HETATM 3557 O HOH A 616 -17.249 31.688 -27.647 1.00 44.45 O HETATM 3558 O HOH A 617 -9.066 43.013 -20.376 1.00 45.54 O HETATM 3559 O HOH A 618 -14.876 38.964 -15.802 1.00 52.49 O HETATM 3560 O HOH A 619 48.884 40.528 24.528 1.00 51.38 O HETATM 3561 O HOH A 620 2.929 29.014 -22.452 1.00 42.10 O HETATM 3562 O HOH A 621 37.067 26.405 27.211 1.00 46.91 O HETATM 3563 O HOH A 622 -3.727 24.064 -29.508 1.00 49.53 O HETATM 3564 O HOH A 623 17.007 33.818 1.803 1.00 51.37 O HETATM 3565 O HOH A 624 48.025 31.752 26.701 1.00 25.44 O HETATM 3566 O HOH A 625 -7.835 46.464 -7.082 1.00 35.65 O HETATM 3567 O HOH A 626 56.397 31.543 2.696 1.00 31.47 O HETATM 3568 O HOH A 627 30.894 46.185 18.420 1.00 31.89 O HETATM 3569 O HOH A 628 4.114 47.565 3.674 1.00 43.66 O HETATM 3570 O HOH A 629 -13.443 32.881 -8.469 1.00 37.50 O HETATM 3571 O HOH A 630 43.032 35.175 7.509 1.00 36.32 O HETATM 3572 O HOH A 631 -16.760 22.585 -15.185 1.00 48.30 O HETATM 3573 O HOH A 632 59.137 40.856 16.913 1.00 37.38 O HETATM 3574 O HOH A 633 -3.558 24.555 8.386 1.00 40.44 O HETATM 3575 O HOH A 634 2.981 34.169 -9.454 1.00 33.32 O HETATM 3576 O HOH A 635 10.134 44.836 10.955 1.00 35.51 O HETATM 3577 O HOH A 636 -16.605 20.325 -26.713 1.00 51.36 O HETATM 3578 O HOH A 637 11.745 27.318 -7.302 1.00 34.99 O HETATM 3579 O HOH A 638 1.546 15.425 -18.940 1.00 41.74 O HETATM 3580 O HOH A 639 1.233 18.792 1.758 1.00 35.92 O HETATM 3581 O HOH A 640 5.188 31.166 21.301 1.00 51.06 O HETATM 3582 O HOH A 641 41.055 25.295 26.769 1.00 34.74 O HETATM 3583 O HOH A 642 32.094 33.107 27.632 1.00 35.54 O HETATM 3584 O HOH A 643 61.547 27.549 17.921 1.00 40.19 O HETATM 3585 O HOH A 644 41.303 34.709 30.383 1.00 41.51 O HETATM 3586 O HOH A 645 -5.404 47.677 -10.986 1.00 40.23 O HETATM 3587 O HOH A 646 -14.796 45.971 -7.387 1.00 42.13 O HETATM 3588 O HOH A 647 -2.513 38.876 10.775 1.00 49.40 O HETATM 3589 O HOH A 648 9.131 19.324 7.648 1.00 37.57 O HETATM 3590 O HOH A 649 -6.340 41.940 7.622 1.00 37.32 O HETATM 3591 O HOH A 650 -10.013 18.469 -1.652 1.00 45.87 O HETATM 3592 O HOH A 651 5.011 17.745 -1.747 1.00 38.04 O HETATM 3593 O HOH A 652 61.219 22.662 7.590 1.00 40.64 O HETATM 3594 O HOH A 653 10.506 31.925 25.475 1.00 43.31 O HETATM 3595 O HOH A 654 6.164 34.304 -5.458 1.00 42.96 O HETATM 3596 O HOH A 655 23.409 20.591 4.659 1.00 38.88 O HETATM 3597 O HOH A 656 56.538 44.941 21.789 1.00 47.47 O HETATM 3598 O HOH A 657 40.462 43.549 9.616 1.00 44.95 O HETATM 3599 O HOH A 658 42.003 32.360 29.347 1.00 37.16 O HETATM 3600 O HOH A 659 10.909 37.967 -1.670 1.00 49.05 O HETATM 3601 O HOH A 660 50.849 41.542 4.542 1.00 42.50 O HETATM 3602 O HOH A 661 11.378 25.498 25.419 1.00 42.29 O HETATM 3603 O HOH A 662 -10.333 46.274 -14.097 1.00 48.07 O HETATM 3604 O HOH A 663 -11.635 41.050 -0.890 1.00 39.67 O HETATM 3605 O HOH A 664 31.637 30.746 29.161 1.00 41.68 O HETATM 3606 O HOH A 665 -18.279 31.020 -24.914 1.00 53.39 O HETATM 3607 O HOH A 666 3.631 18.461 9.688 1.00 46.69 O HETATM 3608 O HOH A 667 -19.000 27.646 -18.856 1.00 36.96 O HETATM 3609 O HOH A 668 24.789 20.591 17.903 1.00 41.76 O HETATM 3610 O HOH A 669 36.258 49.565 21.984 1.00 41.69 O HETATM 3611 O HOH A 670 33.630 46.441 15.164 1.00 37.47 O HETATM 3612 O HOH A 671 56.074 24.214 33.685 1.00 38.53 O HETATM 3613 O HOH A 672 6.892 47.581 3.140 1.00 34.04 O HETATM 3614 O HOH A 673 30.590 43.898 8.550 1.00 46.86 O HETATM 3615 O HOH A 674 31.838 49.072 21.999 1.00 39.51 O HETATM 3616 O HOH A 675 28.712 20.136 16.672 1.00 40.25 O HETATM 3617 O HOH A 676 -16.839 23.157 -25.963 1.00 46.81 O HETATM 3618 O HOH A 677 -16.717 34.814 -6.018 1.00 42.17 O HETATM 3619 O HOH A 678 16.523 53.736 10.681 1.00 34.99 O HETATM 3620 O HOH A 679 -13.575 33.974 7.622 1.00 55.10 O HETATM 3621 O HOH A 680 1.786 34.055 -12.493 1.00 46.85 O HETATM 3622 O HOH A 681 4.279 36.740 -8.257 1.00 42.17 O HETATM 3623 O HOH A 682 -2.992 17.374 -7.459 1.00 47.23 O HETATM 3624 O HOH A 683 -17.785 36.511 0.538 1.00 46.41 O HETATM 3625 O HOH A 684 22.666 40.084 5.366 1.00 37.78 O HETATM 3626 O HOH A 685 65.476 30.047 8.292 1.00 47.87 O HETATM 3627 O HOH A 686 56.948 43.634 11.416 1.00 48.01 O HETATM 3628 O HOH A 687 19.117 35.728 2.250 1.00 53.15 O HETATM 3629 O HOH A 688 -7.120 33.270 8.253 1.00 44.89 O HETATM 3630 O HOH A 689 6.041 44.819 5.505 1.00 43.22 O HETATM 3631 O HOH A 690 -17.399 19.735 -16.026 1.00 48.16 O HETATM 3632 O HOH A 691 43.743 31.366 5.400 1.00 50.14 O HETATM 3633 O HOH A 692 0.160 37.759 -10.167 1.00 46.43 O HETATM 3634 O HOH A 693 43.304 17.602 15.967 1.00 51.93 O HETATM 3635 O HOH A 694 56.903 49.652 11.543 1.00 47.10 O HETATM 3636 O HOH A 695 24.252 26.771 24.999 1.00 45.02 O HETATM 3637 O HOH A 696 60.175 18.655 30.857 1.00 42.04 O HETATM 3638 O HOH A 697 14.849 55.814 9.725 1.00 35.05 O HETATM 3639 O HOH A 698 10.225 39.033 26.799 1.00 43.10 O HETATM 3640 O HOH A 699 41.054 36.909 8.204 1.00 40.41 O HETATM 3641 O HOH A 700 51.933 31.243 -2.103 1.00 41.51 O HETATM 3642 O HOH A 701 24.252 51.325 5.889 1.00 45.52 O HETATM 3643 O HOH A 702 6.909 18.475 2.950 1.00 38.10 O HETATM 3644 O HOH A 703 13.884 40.284 26.456 1.00 51.00 O HETATM 3645 O HOH A 704 25.985 24.548 25.918 1.00 50.95 O HETATM 3646 O HOH A 705 17.006 29.945 24.311 1.00 41.24 O HETATM 3647 O HOH A 706 -17.053 39.169 0.092 1.00 45.94 O HETATM 3648 O HOH A 707 31.546 28.158 24.931 1.00 40.96 O HETATM 3649 O HOH A 708 52.165 31.253 0.734 1.00 45.73 O HETATM 3650 O HOH A 709 21.714 46.408 17.324 1.00 48.71 O HETATM 3651 O HOH A 710 32.290 48.516 16.922 1.00 43.49 O HETATM 3652 O HOH A 711 57.334 34.351 1.942 1.00 53.49 O HETATM 3653 O HOH A 712 -2.692 35.730 14.395 1.00 51.30 O HETATM 3654 O HOH A 713 9.821 18.448 16.998 1.00 54.19 O HETATM 3655 O HOH A 714 55.204 34.932 -1.256 1.00 50.53 O HETATM 3656 O HOH A 715 12.799 37.687 26.478 1.00 49.16 O HETATM 3657 O HOH A 716 25.523 29.507 25.988 1.00 49.01 O HETATM 3658 O HOH A 717 9.761 18.848 12.666 1.00 49.45 O HETATM 3659 O HOH A 718 -0.557 36.704 16.145 1.00 43.87 O HETATM 3660 O HOH A 719 39.292 33.885 5.151 1.00 42.84 O HETATM 3661 O HOH A 720 -15.246 22.339 -3.658 1.00 43.18 O HETATM 3662 O HOH A 721 21.236 16.451 5.728 1.00 49.79 O HETATM 3663 O HOH A 722 47.204 34.672 3.323 1.00 37.80 O HETATM 3664 O HOH A 723 7.456 44.980 3.176 1.00 38.41 O HETATM 3665 O HOH A 724 36.753 47.038 15.418 1.00 53.15 O HETATM 3666 O HOH A 725 6.556 49.948 23.070 1.00 44.96 O HETATM 3667 O HOH A 726 -2.030 25.774 15.713 1.00 45.08 O HETATM 3668 O HOH A 727 -18.901 30.390 -15.872 1.00 52.27 O HETATM 3669 O HOH A 728 16.910 20.142 14.076 1.00 42.53 O HETATM 3670 O HOH A 729 34.516 28.865 30.344 1.00 49.26 O HETATM 3671 O HOH A 730 21.359 39.933 24.001 1.00 52.39 O HETATM 3672 O HOH A 731 47.251 38.462 4.965 1.00 50.90 O HETATM 3673 O HOH A 732 -18.907 36.230 -9.417 1.00 51.73 O HETATM 3674 O HOH A 733 9.430 22.992 -5.336 1.00 51.09 O HETATM 3675 O HOH A 734 40.990 52.433 6.907 1.00 49.14 O HETATM 3676 O HOH A 735 3.047 35.116 20.549 1.00 44.94 O HETATM 3677 O HOH A 736 55.770 47.150 19.942 1.00 46.14 O HETATM 3678 O HOH A 737 -0.961 15.866 -8.899 1.00 49.61 O HETATM 3679 O HOH A 738 -3.817 22.284 6.428 1.00 45.72 O HETATM 3680 O HOH A 739 32.363 17.357 12.919 1.00 50.02 O HETATM 3681 O HOH A 740 23.835 54.638 5.842 1.00 44.41 O HETATM 3682 O HOH A 741 26.820 38.310 27.622 1.00 41.45 O HETATM 3683 O HOH A 742 -15.416 40.056 2.073 1.00 47.93 O HETATM 3684 O HOH A 743 44.070 37.069 29.526 1.00 41.83 O HETATM 3685 O HOH A 744 44.299 25.684 1.519 1.00 41.81 O HETATM 3686 O HOH A 745 -16.637 26.743 -27.743 1.00 52.22 O HETATM 3687 O HOH A 746 40.678 45.897 26.910 1.00 43.60 O HETATM 3688 O HOH A 747 26.281 47.313 8.572 1.00 48.77 O HETATM 3689 O HOH A 748 -12.692 40.532 1.768 1.00 41.48 O HETATM 3690 O HOH A 749 -17.560 29.281 -1.411 1.00 49.51 O HETATM 3691 O HOH A 750 18.357 40.837 24.051 1.00 41.54 O HETATM 3692 O HOH A 751 8.395 59.905 15.465 1.00 47.21 O HETATM 3693 O HOH A 752 27.690 29.129 28.148 1.00 55.23 O HETATM 3694 O HOH A 753 19.720 19.588 0.326 1.00 53.75 O HETATM 3695 O HOH A 754 16.058 36.506 2.406 1.00 46.78 O HETATM 3696 O HOH A 755 -6.107 17.647 -4.380 1.00 51.95 O HETATM 3697 O HOH A 756 5.802 28.492 21.471 1.00 45.70 O HETATM 3698 O HOH A 757 49.266 23.719 26.121 1.00 54.64 O HETATM 3699 O HOH A 758 -20.515 28.698 -22.084 1.00 51.80 O HETATM 3700 O HOH A 759 49.943 35.128 2.950 1.00 45.41 O HETATM 3701 O HOH A 760 63.875 23.575 7.779 1.00 48.31 O HETATM 3702 O HOH A 761 28.988 36.045 8.622 1.00 47.45 O HETATM 3703 O HOH A 762 39.884 49.531 25.598 1.00 49.29 O HETATM 3704 O HOH A 763 49.961 20.780 25.146 1.00 47.18 O HETATM 3705 O HOH A 764 26.675 44.713 24.424 1.00 49.96 O HETATM 3706 O HOH A 765 8.322 17.593 -1.021 1.00 54.04 O HETATM 3707 O HOH A 766 61.671 32.884 6.978 1.00 48.24 O HETATM 3708 O HOH A 767 26.358 39.933 8.904 1.00 36.93 O HETATM 3709 O HOH A 768 27.851 37.378 29.973 1.00 50.35 O HETATM 3710 O HOH A 769 -11.641 46.794 -4.116 1.00 54.50 O HETATM 3711 O HOH A 770 33.017 50.486 19.548 1.00 51.18 O HETATM 3712 O HOH A 771 -12.250 17.297 -15.973 1.00 49.72 O HETATM 3713 O HOH A 772 58.511 20.238 3.591 1.00 52.21 O HETATM 3714 O HOH A 773 -11.244 20.894 -0.761 1.00 47.40 O HETATM 3715 O HOH A 774 40.033 18.642 16.102 1.00 49.60 O HETATM 3716 O HOH A 775 33.174 48.579 11.213 1.00 48.31 O HETATM 3717 O HOH A 776 49.984 55.921 17.146 1.00 50.60 O HETATM 3718 O HOH A 777 30.496 37.750 31.353 1.00 49.95 O HETATM 3719 O HOH A 778 -23.131 43.008 -5.720 1.00 51.44 O HETATM 3720 O HOH A 779 -9.464 34.024 -27.306 1.00 52.93 O HETATM 3721 O HOH A 780 59.550 46.814 12.038 1.00 52.40 O HETATM 3722 O HOH A 781 6.616 17.596 7.537 1.00 49.97 O HETATM 3723 O HOH A 782 -7.007 48.723 -0.526 1.00 46.70 O HETATM 3724 O HOH A 783 29.975 32.905 6.985 1.00 50.08 O HETATM 3725 O HOH A 784 38.622 41.233 6.125 1.00 50.27 O HETATM 3726 O HOH A 785 53.614 25.743 32.910 1.00 39.70 O HETATM 3727 O HOH A 786 -6.743 44.868 -19.056 1.00 50.99 O HETATM 3728 O HOH A 787 -17.590 37.220 -7.128 1.00 45.10 O HETATM 3729 O HOH A 788 -10.523 15.638 -14.449 1.00 51.92 O HETATM 3730 O HOH A 789 0.876 23.454 -25.855 1.00 46.74 O HETATM 3731 O HOH A 790 42.052 41.518 4.922 1.00 48.03 O HETATM 3732 O HOH A 791 2.185 14.179 -13.657 1.00 50.91 O HETATM 3733 O HOH A 792 49.303 32.108 33.873 1.00 49.78 O HETATM 3734 O HOH A 793 42.840 41.492 29.242 1.00 53.23 O HETATM 3735 O HOH A 794 39.086 19.604 20.224 1.00 50.98 O HETATM 3736 O HOH A 795 6.486 32.415 23.866 1.00 48.95 O HETATM 3737 O HOH A 796 7.491 19.279 14.169 1.00 49.27 O HETATM 3738 O HOH A 797 59.973 22.628 4.966 1.00 44.20 O HETATM 3739 O HOH A 798 36.576 52.188 9.555 1.00 51.91 O HETATM 3740 O HOH A 799 54.958 31.264 0.292 1.00 51.23 O HETATM 3741 O HOH A 800 15.873 42.171 5.194 1.00 43.54 O HETATM 3742 O HOH A 801 -16.181 21.031 -7.468 1.00 46.66 O HETATM 3743 O HOH A 802 21.693 36.921 3.464 1.00 49.47 O HETATM 3744 O HOH A 803 27.277 37.755 7.318 1.00 49.58 O HETATM 3745 O HOH A 804 5.720 23.318 19.266 1.00 54.93 O HETATM 3746 O HOH A 805 7.743 43.844 19.530 1.00 36.92 O HETATM 3747 O HOH A 806 3.844 37.653 19.755 1.00 45.82 O HETATM 3748 O HOH A 807 46.701 33.745 5.702 1.00 37.04 O HETATM 3749 O HOH A 808 -12.919 27.745 2.838 1.00 45.56 O HETATM 3750 O HOH A 809 3.917 42.610 24.754 1.00 51.80 O HETATM 3751 O HOH A 810 -6.788 14.301 -16.106 1.00 48.12 O HETATM 3752 O HOH A 811 12.596 47.166 22.865 1.00 47.81 O HETATM 3753 O HOH A 812 41.363 18.878 18.589 1.00 51.31 O HETATM 3754 O HOH A 813 55.084 42.746 21.610 1.00 37.57 O HETATM 3755 O HOH A 814 -11.338 18.003 -7.268 1.00 38.96 O HETATM 3756 O HOH A 815 57.061 30.013 24.148 1.00 47.47 O HETATM 3757 O HOH A 816 21.061 43.092 7.902 1.00 51.25 O HETATM 3758 O HOH A 817 -1.319 36.170 -17.302 1.00 48.08 O HETATM 3759 O HOH A 818 -7.790 16.469 -13.920 1.00 50.57 O HETATM 3760 O HOH A 819 22.153 17.222 10.839 1.00 45.68 O HETATM 3761 O HOH A 820 9.688 40.364 -2.452 1.00 53.21 O HETATM 3762 O HOH A 821 -7.478 50.422 -9.881 1.00 50.40 O HETATM 3763 O HOH A 822 -5.198 39.339 10.177 1.00 47.68 O HETATM 3764 O HOH A 823 12.334 19.126 13.872 1.00 51.15 O HETATM 3765 O HOH A 824 26.799 22.523 23.734 1.00 50.79 O HETATM 3766 O HOH A 825 0.870 17.619 4.395 1.00 52.85 O HETATM 3767 O HOH A 826 17.601 35.496 29.817 1.00 49.22 O HETATM 3768 O HOH A 827 52.638 51.665 10.739 1.00 49.76 O HETATM 3769 O HOH A 828 -14.694 21.169 -1.198 1.00 52.86 O HETATM 3770 O HOH A 829 -7.872 46.002 1.331 1.00 42.36 O HETATM 3771 O HOH A 830 48.414 23.641 31.207 1.00 44.52 O HETATM 3772 O HOH A 831 54.725 26.110 -1.189 1.00 46.91 O HETATM 3773 O HOH A 832 -9.373 44.842 -0.941 1.00 48.85 O HETATM 3774 O HOH A 833 -17.127 27.506 -4.029 1.00 46.26 O HETATM 3775 O HOH A 834 13.134 39.664 -0.785 1.00 54.01 O HETATM 3776 O HOH A 835 -13.901 18.677 -13.962 1.00 54.16 O HETATM 3777 O HOH A 836 38.515 49.764 9.288 1.00 49.67 O HETATM 3778 O HOH A 837 4.248 14.586 -18.116 1.00 52.03 O HETATM 3779 O HOH A 838 -8.337 29.390 -32.861 1.00 47.56 O HETATM 3780 O HOH A 839 23.762 33.329 1.530 1.00 50.79 O HETATM 3781 O HOH A 840 45.284 25.481 29.480 1.00 53.22 O HETATM 3782 O HOH A 841 35.679 17.693 13.377 1.00 46.38 O HETATM 3783 O HOH A 842 -13.258 28.819 5.542 1.00 53.44 O HETATM 3784 O HOH B 14 27.294 22.884 7.764 1.00 26.85 O HETATM 3785 O HOH B 31 46.283 21.959 9.366 1.00 25.55 O HETATM 3786 O HOH B 61 22.142 25.536 6.050 1.00 28.25 O HETATM 3787 O HOH B 66 36.473 24.541 3.272 1.00 29.06 O HETATM 3788 O HOH B 92 26.503 25.796 0.106 1.00 39.25 O HETATM 3789 O HOH B 101 35.507 26.201 5.358 1.00 29.38 O HETATM 3790 O HOH B 103 40.187 27.501 3.027 1.00 29.91 O HETATM 3791 O HOH B 109 8.553 26.943 -1.733 1.00 27.52 O HETATM 3792 O HOH B 112 6.732 31.053 -8.586 1.00 33.79 O HETATM 3793 O HOH B 134 34.306 23.929 8.619 1.00 45.09 O HETATM 3794 O HOH B 148 38.953 24.660 1.900 1.00 34.02 O HETATM 3795 O HOH B 151 41.515 30.021 4.192 1.00 47.28 O HETATM 3796 O HOH B 173 16.353 27.575 2.027 1.00 29.25 O HETATM 3797 O HOH B 176 14.378 26.919 -8.355 1.00 39.53 O HETATM 3798 O HOH B 184 32.998 31.644 7.137 1.00 49.09 O HETATM 3799 O HOH B 198 16.090 20.014 -8.294 1.00 48.48 O HETATM 3800 O HOH B 218 27.272 28.924 0.243 1.00 42.70 O HETATM 3801 O HOH B 224 29.019 28.268 2.102 1.00 44.37 O HETATM 3802 O HOH B 226 20.595 33.466 0.599 1.00 53.01 O HETATM 3803 O HOH B 237 17.742 23.435 -8.835 1.00 54.81 O HETATM 3804 O HOH B 249 28.852 30.923 3.016 1.00 46.72 O HETATM 3805 O HOH B 260 45.075 19.630 8.515 1.00 32.55 O HETATM 3806 O HOH B 303 16.144 22.451 -1.160 1.00 35.12 O HETATM 3807 O HOH B 307 35.388 28.939 4.807 1.00 51.83 O HETATM 3808 O HOH B 313 15.698 31.832 -1.540 1.00 49.52 O HETATM 3809 O HOH B 325 23.488 25.033 -1.582 1.00 47.95 O HETATM 3810 O HOH B 337 21.318 25.603 -4.609 1.00 49.82 O HETATM 3811 O HOH B 347 19.465 31.027 1.041 1.00 35.53 O HETATM 3812 O HOH B 351 33.769 22.014 0.860 1.00 54.53 O HETATM 3813 O HOH B 365 45.172 21.870 -1.314 1.00 36.69 O HETATM 3814 O HOH B 380 32.681 18.810 6.058 1.00 36.89 O HETATM 3815 O HOH B 389 29.985 19.744 5.817 1.00 48.25 O HETATM 3816 O HOH B 397 8.186 18.360 -18.803 1.00 48.95 O HETATM 3817 O HOH B 406 18.548 22.020 -4.819 1.00 49.38 O HETATM 3818 O HOH B 428 11.414 32.216 -3.165 1.00 50.79 O HETATM 3819 O HOH B 439 7.382 16.556 -15.795 1.00 52.79 O HETATM 3820 O HOH B 441 37.929 28.983 1.913 1.00 48.89 O HETATM 3821 O HOH B 513 25.825 19.596 0.278 1.00 50.78 O HETATM 3822 O HOH B 542 39.179 31.769 0.726 1.00 51.65 O CONECT 1874 2144 CONECT 2144 1874 MASTER 262 0 0 29 2 0 0 6 3820 2 2 33 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3qg9
RCSB PDB
PDBbind
RNA (5-UGUGCCUUA-3)
Entry Information
PDB ID
3qgc
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
RNA-binding domain of FBF-2 (amino acids 164-575) R288Y mutant
Ligand Name
RNA (5-UGUGCCUUA-3)
EC.Number
E.C.-.-.-.-
Resolution
1.9(Å)
Affinity (Kd/Ki/IC50)
Kd=8.8nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) Rna Vol. 17: pp. 718-727
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q09312
Entrez Gene ID
No matched NCBI Entrez Gene ID found!
ASD
Information of known allosteric effects of PDB entries
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